data_9JGB
# 
_entry.id   9JGB 
# 
_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   9JGB         pdb_00009jgb 10.2210/pdb9jgb/pdb 
WWPDB D_1300051274 ?            ?                   
# 
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                        9JGB 
_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 'SULFATE ION'                                        96.063    1  ?       ? ? ? 
3 non-polymer syn 'SULFITE ION'                                        80.063    1  ?       ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                       62.068    1  ?       ? ? ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                              106.120   1  ?       ? ? ? 
6 water       nat water                                                18.015    18 ?       ? ? ? 
# 
_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 'SULFATE ION'           SO4 
3 'SULFITE ION'           SO3 
4 1,2-ETHANEDIOL          EDO 
5 'DI(HYDROXYETHYL)ETHER' PEG 
6 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 
ALA 'L-peptide linking' y ALANINE                 ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE              ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'         ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                ?                 'C3 H7 N O2 S'   121.158 
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  
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                 'C4 H10 O3'      106.120 
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 
SO3 non-polymer         . 'SULFITE ION'           ?                 'O3 S -2'        80.063  
SO4 non-polymer         . 'SULFATE ION'           ?                 'O4 S -2'        96.063  
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 
# 
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 SO4 1  301 1  SO4 SO4 A . 
C 3 SO3 1  302 2  SO3 SO3 A . 
D 4 EDO 1  303 3  EDO EDO A . 
E 5 PEG 1  304 4  PEG PEG A . 
F 6 HOH 1  401 5  HOH HOH A . 
F 6 HOH 2  402 17 HOH HOH A . 
F 6 HOH 3  403 9  HOH HOH A . 
F 6 HOH 4  404 4  HOH HOH A . 
F 6 HOH 5  405 7  HOH HOH A . 
F 6 HOH 6  406 6  HOH HOH A . 
F 6 HOH 7  407 10 HOH HOH A . 
F 6 HOH 8  408 3  HOH HOH A . 
F 6 HOH 9  409 1  HOH HOH A . 
F 6 HOH 10 410 11 HOH HOH A . 
F 6 HOH 11 411 13 HOH HOH A . 
F 6 HOH 12 412 8  HOH HOH A . 
F 6 HOH 13 413 14 HOH HOH A . 
F 6 HOH 14 414 16 HOH HOH A . 
F 6 HOH 15 415 2  HOH HOH A . 
F 6 HOH 16 416 18 HOH HOH A . 
F 6 HOH 17 417 12 HOH HOH A . 
F 6 HOH 18 418 15 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                     9JGB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     113.810 
_cell.length_a_esd                 ? 
_cell.length_b                     113.810 
_cell.length_b_esd                 ? 
_cell.length_c                     102.400 
_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                         9JGB 
_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                   9JGB 
_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          MICROBATCH 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_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 ammonium sulfate, 0.1M Tris-Base pH 8.0, 20% (v/v) PEG smear broad' 
_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         2023-04-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   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                                       9JGB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.10 
_reflns.d_resolution_low                               71.01 
_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                                     4773 
_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                                13.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.89 
_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                                0.139 
_reflns.pdbx_Rpim_I_all                                0.038 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       62217 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.134 
_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                                    3.10 
_reflns_shell.d_res_low                                     3.31 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           11144 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             847 
_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                               13.2 
_reflns_shell.pdbx_chi_squared                              0.68 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     5.4 
_reflns_shell.pdbx_Rrim_I_all                               0.445 
_reflns_shell.pdbx_Rpim_I_all                               0.122 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.955 
_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                                  0.427 
_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]                            -2.31 
_refine.aniso_B[1][2]                            -1.15 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -2.31 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            7.49 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               58.147 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.953 
_refine.correlation_coeff_Fo_to_Fc_free          0.886 
_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                                 9JGB 
_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                            3.10 
_refine.ls_d_res_low                             71.01 
_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                     4521 
_refine.ls_number_reflns_R_free                  251 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.98 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16830 
_refine.ls_R_factor_R_free                       0.24511 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16391 
_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                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.503 
_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                             36.492 
_refine.overall_SU_ML                            0.331 
_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                       3.10 
_refine_hist.d_res_low                        71.01 
_refine_hist.number_atoms_solvent             18 
_refine_hist.number_atoms_total               1909 
_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         20 
_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' ? 0.005  0.012  1927 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1912 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.183  1.667  2595 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.394  1.582  4415 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.041  5.000  225  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.829  5.000  16   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.659 10.000 371  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.051  0.200  288  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  2185 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  415  ? 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' ? 1.917  2.849  903  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.916  2.849  903  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.283  5.109  1127 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.282  5.111  1128 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.285  3.211  1024 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.284  3.213  1025 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.762  5.749  1469 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.173  27.18  2140 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.173  27.19  2141 ? 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                       3.100 
_refine_ls_shell.d_res_low                        3.181 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             15 
_refine_ls_shell.number_reflns_R_work             331 
_refine_ls_shell.percent_reflns_obs               100.00 
_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                  0.128 
_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                  0.273 
# 
_struct.entry_id                     9JGB 
_struct.title                        'Crystal structure of Nep1 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        9JGB 
_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 6 ? 
# 
_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              9JGB 
_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)' 5110  ? 
1 MORE         -35   ? 
1 'SSA (A^2)'  19330 ? 
# 
_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 
# 
_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' 11_444 x-y-1/3,-y-2/3,-z-2/3 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 
-1.0000000000 0.0000000000 -65.7082341365 0.0000000000 0.0000000000 -1.0000000000 -68.2666666667 
# 
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 ARG A 65  ? ASP A 78  ? ARG A 65  ASP A 78  1 ? 14 
HELX_P HELX_P7  AA7 SER A 79  ? GLU A 84  ? SER A 79  GLU A 84  1 ? 6  
HELX_P HELX_P8  AA8 ASN A 110 ? GLY A 125 ? ASN A 110 GLY A 125 1 ? 16 
HELX_P HELX_P9  AA9 THR A 140 ? ASN A 149 ? THR A 140 ASN A 149 1 ? 10 
HELX_P HELX_P10 AB1 ILE A 164 ? ASP A 173 ? ILE A 164 ASP A 173 1 ? 10 
HELX_P HELX_P11 AB2 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       -12.11 
# 
_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 TYR A 90  ? O TYR A 90  N LEU A 9   ? N LEU A 9   
AA1 5 6 N ALA A 12  ? N ALA A 12  O VAL A 182 ? O VAL A 182 
AA1 6 7 O THR A 179 ? O THR A 179 N VAL A 152 ? N VAL A 152 
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                   9JGB 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 59  ? ? 52.28   16.30  
2 1 LYS A 139 ? ? -172.33 126.25 
3 1 LYS A 177 ? ? -145.19 53.33  
4 1 ARG A 203 ? ? -89.89  -70.20 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     109 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.104 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_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         -2.4610 
_pdbx_refine_tls.origin_y         -20.5534 
_pdbx_refine_tls.origin_z         -32.4500 
_pdbx_refine_tls.T[1][1]          0.2515 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0204 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0339 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2089 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0412 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0311 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          3.2408 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0995 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.4647 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          4.2978 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0144 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.0984 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.1716 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.1224 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.1766 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.1022 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.2317 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.1796 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1838 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0823 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0602 
_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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
PEG C1   C N N 260 
PEG O1   O N N 261 
PEG C2   C N N 262 
PEG O2   O N N 263 
PEG C3   C N N 264 
PEG C4   C N N 265 
PEG O4   O N N 266 
PEG H11  H N N 267 
PEG H12  H N N 268 
PEG HO1  H N N 269 
PEG H21  H N N 270 
PEG H22  H N N 271 
PEG H31  H N N 272 
PEG H32  H N N 273 
PEG H41  H N N 274 
PEG H42  H N N 275 
PEG HO4  H N N 276 
PHE N    N N N 277 
PHE CA   C N S 278 
PHE C    C N N 279 
PHE O    O N N 280 
PHE CB   C N N 281 
PHE CG   C Y N 282 
PHE CD1  C Y N 283 
PHE CD2  C Y N 284 
PHE CE1  C Y N 285 
PHE CE2  C Y N 286 
PHE CZ   C Y N 287 
PHE OXT  O N N 288 
PHE H    H N N 289 
PHE H2   H N N 290 
PHE HA   H N N 291 
PHE HB2  H N N 292 
PHE HB3  H N N 293 
PHE HD1  H N N 294 
PHE HD2  H N N 295 
PHE HE1  H N N 296 
PHE HE2  H N N 297 
PHE HZ   H N N 298 
PHE HXT  H N N 299 
PRO N    N N N 300 
PRO CA   C N S 301 
PRO C    C N N 302 
PRO O    O N N 303 
PRO CB   C N N 304 
PRO CG   C N N 305 
PRO CD   C N N 306 
PRO OXT  O N N 307 
PRO H    H N N 308 
PRO HA   H N N 309 
PRO HB2  H N N 310 
PRO HB3  H N N 311 
PRO HG2  H N N 312 
PRO HG3  H N N 313 
PRO HD2  H N N 314 
PRO HD3  H N N 315 
PRO HXT  H N N 316 
SER N    N N N 317 
SER CA   C N S 318 
SER C    C N N 319 
SER O    O N N 320 
SER CB   C N N 321 
SER OG   O N N 322 
SER OXT  O N N 323 
SER H    H N N 324 
SER H2   H N N 325 
SER HA   H N N 326 
SER HB2  H N N 327 
SER HB3  H N N 328 
SER HG   H N N 329 
SER HXT  H N N 330 
SO3 S    S N N 331 
SO3 O1   O N N 332 
SO3 O2   O N N 333 
SO3 O3   O N N 334 
SO4 S    S N N 335 
SO4 O1   O N N 336 
SO4 O2   O N N 337 
SO4 O3   O N N 338 
SO4 O4   O N N 339 
THR N    N N N 340 
THR CA   C N S 341 
THR C    C N N 342 
THR O    O N N 343 
THR CB   C N R 344 
THR OG1  O N N 345 
THR CG2  C N N 346 
THR OXT  O N N 347 
THR H    H N N 348 
THR H2   H N N 349 
THR HA   H N N 350 
THR HB   H N N 351 
THR HG1  H N N 352 
THR HG21 H N N 353 
THR HG22 H N N 354 
THR HG23 H N N 355 
THR HXT  H N N 356 
TRP N    N N N 357 
TRP CA   C N S 358 
TRP C    C N N 359 
TRP O    O N N 360 
TRP CB   C N N 361 
TRP CG   C Y N 362 
TRP CD1  C Y N 363 
TRP CD2  C Y N 364 
TRP NE1  N Y N 365 
TRP CE2  C Y N 366 
TRP CE3  C Y N 367 
TRP CZ2  C Y N 368 
TRP CZ3  C Y N 369 
TRP CH2  C Y N 370 
TRP OXT  O N N 371 
TRP H    H N N 372 
TRP H2   H N N 373 
TRP HA   H N N 374 
TRP HB2  H N N 375 
TRP HB3  H N N 376 
TRP HD1  H N N 377 
TRP HE1  H N N 378 
TRP HE3  H N N 379 
TRP HZ2  H N N 380 
TRP HZ3  H N N 381 
TRP HH2  H N N 382 
TRP HXT  H N N 383 
TYR N    N N N 384 
TYR CA   C N S 385 
TYR C    C N N 386 
TYR O    O N N 387 
TYR CB   C N N 388 
TYR CG   C Y N 389 
TYR CD1  C Y N 390 
TYR CD2  C Y N 391 
TYR CE1  C Y N 392 
TYR CE2  C Y N 393 
TYR CZ   C Y N 394 
TYR OH   O N N 395 
TYR OXT  O N N 396 
TYR H    H N N 397 
TYR H2   H N N 398 
TYR HA   H N N 399 
TYR HB2  H N N 400 
TYR HB3  H N N 401 
TYR HD1  H N N 402 
TYR HD2  H N N 403 
TYR HE1  H N N 404 
TYR HE2  H N N 405 
TYR HH   H N N 406 
TYR HXT  H N N 407 
VAL N    N N N 408 
VAL CA   C N S 409 
VAL C    C N N 410 
VAL O    O N N 411 
VAL CB   C N N 412 
VAL CG1  C N N 413 
VAL CG2  C N N 414 
VAL OXT  O N N 415 
VAL H    H N N 416 
VAL H2   H N N 417 
VAL HA   H N N 418 
VAL HB   H N N 419 
VAL HG11 H N N 420 
VAL HG12 H N N 421 
VAL HG13 H N N 422 
VAL HG21 H N N 423 
VAL HG22 H N N 424 
VAL HG23 H N N 425 
VAL HXT  H N N 426 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PEG C1  O1   sing N N 246 
PEG C1  C2   sing N N 247 
PEG C1  H11  sing N N 248 
PEG C1  H12  sing N N 249 
PEG O1  HO1  sing N N 250 
PEG C2  O2   sing N N 251 
PEG C2  H21  sing N N 252 
PEG C2  H22  sing N N 253 
PEG O2  C3   sing N N 254 
PEG C3  C4   sing N N 255 
PEG C3  H31  sing N N 256 
PEG C3  H32  sing N N 257 
PEG C4  O4   sing N N 258 
PEG C4  H41  sing N N 259 
PEG C4  H42  sing N N 260 
PEG O4  HO4  sing N N 261 
PHE N   CA   sing N N 262 
PHE N   H    sing N N 263 
PHE N   H2   sing N N 264 
PHE CA  C    sing N N 265 
PHE CA  CB   sing N N 266 
PHE CA  HA   sing N N 267 
PHE C   O    doub N N 268 
PHE C   OXT  sing N N 269 
PHE CB  CG   sing N N 270 
PHE CB  HB2  sing N N 271 
PHE CB  HB3  sing N N 272 
PHE CG  CD1  doub Y N 273 
PHE CG  CD2  sing Y N 274 
PHE CD1 CE1  sing Y N 275 
PHE CD1 HD1  sing N N 276 
PHE CD2 CE2  doub Y N 277 
PHE CD2 HD2  sing N N 278 
PHE CE1 CZ   doub Y N 279 
PHE CE1 HE1  sing N N 280 
PHE CE2 CZ   sing Y N 281 
PHE CE2 HE2  sing N N 282 
PHE CZ  HZ   sing N N 283 
PHE OXT HXT  sing N N 284 
PRO N   CA   sing N N 285 
PRO N   CD   sing N N 286 
PRO N   H    sing N N 287 
PRO CA  C    sing N N 288 
PRO CA  CB   sing N N 289 
PRO CA  HA   sing N N 290 
PRO C   O    doub N N 291 
PRO C   OXT  sing N N 292 
PRO CB  CG   sing N N 293 
PRO CB  HB2  sing N N 294 
PRO CB  HB3  sing N N 295 
PRO CG  CD   sing N N 296 
PRO CG  HG2  sing N N 297 
PRO CG  HG3  sing N N 298 
PRO CD  HD2  sing N N 299 
PRO CD  HD3  sing N N 300 
PRO OXT HXT  sing N N 301 
SER N   CA   sing N N 302 
SER N   H    sing N N 303 
SER N   H2   sing N N 304 
SER CA  C    sing N N 305 
SER CA  CB   sing N N 306 
SER CA  HA   sing N N 307 
SER C   O    doub N N 308 
SER C   OXT  sing N N 309 
SER CB  OG   sing N N 310 
SER CB  HB2  sing N N 311 
SER CB  HB3  sing N N 312 
SER OG  HG   sing N N 313 
SER OXT HXT  sing N N 314 
SO3 S   O1   doub N N 315 
SO3 S   O2   sing N N 316 
SO3 S   O3   sing N N 317 
SO4 S   O1   doub N N 318 
SO4 S   O2   doub N N 319 
SO4 S   O3   sing N N 320 
SO4 S   O4   sing N N 321 
THR N   CA   sing N N 322 
THR N   H    sing N N 323 
THR N   H2   sing N N 324 
THR CA  C    sing N N 325 
THR CA  CB   sing N N 326 
THR CA  HA   sing N N 327 
THR C   O    doub N N 328 
THR C   OXT  sing N N 329 
THR CB  OG1  sing N N 330 
THR CB  CG2  sing N N 331 
THR CB  HB   sing N N 332 
THR OG1 HG1  sing N N 333 
THR CG2 HG21 sing N N 334 
THR CG2 HG22 sing N N 335 
THR CG2 HG23 sing N N 336 
THR OXT HXT  sing N N 337 
TRP N   CA   sing N N 338 
TRP N   H    sing N N 339 
TRP N   H2   sing N N 340 
TRP CA  C    sing N N 341 
TRP CA  CB   sing N N 342 
TRP CA  HA   sing N N 343 
TRP C   O    doub N N 344 
TRP C   OXT  sing N N 345 
TRP CB  CG   sing N N 346 
TRP CB  HB2  sing N N 347 
TRP CB  HB3  sing N N 348 
TRP CG  CD1  doub Y N 349 
TRP CG  CD2  sing Y N 350 
TRP CD1 NE1  sing Y N 351 
TRP CD1 HD1  sing N N 352 
TRP CD2 CE2  doub Y N 353 
TRP CD2 CE3  sing Y N 354 
TRP NE1 CE2  sing Y N 355 
TRP NE1 HE1  sing N N 356 
TRP CE2 CZ2  sing Y N 357 
TRP CE3 CZ3  doub Y N 358 
TRP CE3 HE3  sing N N 359 
TRP CZ2 CH2  doub Y N 360 
TRP CZ2 HZ2  sing N N 361 
TRP CZ3 CH2  sing Y N 362 
TRP CZ3 HZ3  sing N N 363 
TRP CH2 HH2  sing N N 364 
TRP OXT HXT  sing N N 365 
TYR N   CA   sing N N 366 
TYR N   H    sing N N 367 
TYR N   H2   sing N N 368 
TYR CA  C    sing N N 369 
TYR CA  CB   sing N N 370 
TYR CA  HA   sing N N 371 
TYR C   O    doub N N 372 
TYR C   OXT  sing N N 373 
TYR CB  CG   sing N N 374 
TYR CB  HB2  sing N N 375 
TYR CB  HB3  sing N N 376 
TYR CG  CD1  doub Y N 377 
TYR CG  CD2  sing Y N 378 
TYR CD1 CE1  sing Y N 379 
TYR CD1 HD1  sing N N 380 
TYR CD2 CE2  doub Y N 381 
TYR CD2 HD2  sing N N 382 
TYR CE1 CZ   doub Y N 383 
TYR CE1 HE1  sing N N 384 
TYR CE2 CZ   sing Y N 385 
TYR CE2 HE2  sing N N 386 
TYR CZ  OH   sing N N 387 
TYR OH  HH   sing N N 388 
TYR OXT HXT  sing N N 389 
VAL N   CA   sing N N 390 
VAL N   H    sing N N 391 
VAL N   H2   sing N N 392 
VAL CA  C    sing N N 393 
VAL CA  CB   sing N N 394 
VAL CA  HA   sing N N 395 
VAL C   O    doub N N 396 
VAL C   OXT  sing N N 397 
VAL CB  CG1  sing N N 398 
VAL CB  CG2  sing N N 399 
VAL CB  HB   sing N N 400 
VAL CG1 HG11 sing N N 401 
VAL CG1 HG12 sing N N 402 
VAL CG1 HG13 sing N N 403 
VAL CG2 HG21 sing N N 404 
VAL CG2 HG22 sing N N 405 
VAL CG2 HG23 sing N N 406 
VAL OXT HXT  sing N N 407 
# 
_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             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-O50087-F1 
_pdbx_initial_refinement_model.details          O50087 
# 
_atom_sites.entry_id                    9JGB 
_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]   0.008787 
_atom_sites.fract_transf_matrix[1][2]   0.005073 
_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]   0.010146 
_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]   0.009766 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU A 1 2   ? 11.355  -17.279 -14.200 1.00 95.66  ? 2   GLU A N   1 
ATOM   2    C CA  . GLU A 1 2   ? 11.032  -16.656 -15.515 1.00 94.36  ? 2   GLU A CA  1 
ATOM   3    C C   . GLU A 1 2   ? 12.238  -15.869 -16.036 1.00 96.64  ? 2   GLU A C   1 
ATOM   4    O O   . GLU A 1 2   ? 12.109  -14.737 -16.507 1.00 95.21  ? 2   GLU A O   1 
ATOM   5    C CB  . GLU A 1 2   ? 9.763   -15.810 -15.390 1.00 95.63  ? 2   GLU A CB  1 
ATOM   6    C CG  . GLU A 1 2   ? 8.504   -16.658 -15.282 1.00 95.33  ? 2   GLU A CG  1 
ATOM   7    C CD  . GLU A 1 2   ? 7.228   -15.989 -15.761 1.00 96.57  ? 2   GLU A CD  1 
ATOM   8    O OE1 . GLU A 1 2   ? 7.184   -14.737 -15.790 1.00 97.84  ? 2   GLU A OE1 1 
ATOM   9    O OE2 . GLU A 1 2   ? 6.295   -16.731 -16.147 1.00 96.38  ? 2   GLU A OE2 1 
ATOM   10   N N   . GLU A 1 3   ? 13.416  -16.499 -15.953 1.00 97.95  ? 3   GLU A N   1 
ATOM   11   C CA  . GLU A 1 3   ? 14.659  -15.927 -16.450 1.00 96.52  ? 3   GLU A CA  1 
ATOM   12   C C   . GLU A 1 3   ? 15.352  -16.929 -17.374 1.00 92.94  ? 3   GLU A C   1 
ATOM   13   O O   . GLU A 1 3   ? 16.352  -16.599 -18.006 1.00 95.88  ? 3   GLU A O   1 
ATOM   14   C CB  . GLU A 1 3   ? 15.544  -15.519 -15.266 1.00 98.52  ? 3   GLU A CB  1 
ATOM   15   C CG  . GLU A 1 3   ? 16.961  -15.137 -15.656 1.00 97.87  ? 3   GLU A CG  1 
ATOM   16   C CD  . GLU A 1 3   ? 17.770  -14.452 -14.572 1.00 100.66 ? 3   GLU A CD  1 
ATOM   17   O OE1 . GLU A 1 3   ? 18.992  -14.313 -14.761 1.00 102.85 ? 3   GLU A OE1 1 
ATOM   18   O OE2 . GLU A 1 3   ? 17.181  -14.060 -13.550 1.00 100.99 ? 3   GLU A OE2 1 
ATOM   19   N N   . LYS A 1 4   ? 14.816  -18.152 -17.461 1.00 87.34  ? 4   LYS A N   1 
ATOM   20   C CA  . LYS A 1 4   ? 15.425  -19.191 -18.274 1.00 82.87  ? 4   LYS A CA  1 
ATOM   21   C C   . LYS A 1 4   ? 14.997  -18.995 -19.728 1.00 75.36  ? 4   LYS A C   1 
ATOM   22   O O   . LYS A 1 4   ? 13.994  -18.344 -20.005 1.00 73.25  ? 4   LYS A O   1 
ATOM   23   C CB  . LYS A 1 4   ? 15.025  -20.568 -17.740 1.00 81.81  ? 4   LYS A CB  1 
ATOM   24   C CG  . LYS A 1 4   ? 13.555  -20.908 -17.917 1.00 79.64  ? 4   LYS A CG  1 
ATOM   25   C CD  . LYS A 1 4   ? 13.210  -22.323 -17.544 1.00 80.76  ? 4   LYS A CD  1 
ATOM   26   C CE  . LYS A 1 4   ? 13.297  -22.604 -16.060 1.00 83.23  ? 4   LYS A CE  1 
ATOM   27   N NZ  . LYS A 1 4   ? 12.490  -23.795 -15.704 1.00 82.57  ? 4   LYS A NZ  1 
ATOM   28   N N   . LYS A 1 5   ? 15.763  -19.579 -20.649 1.00 70.60  ? 5   LYS A N   1 
ATOM   29   C CA  . LYS A 1 5   ? 15.432  -19.526 -22.057 1.00 66.83  ? 5   LYS A CA  1 
ATOM   30   C C   . LYS A 1 5   ? 14.124  -20.268 -22.298 1.00 62.61  ? 5   LYS A C   1 
ATOM   31   O O   . LYS A 1 5   ? 14.050  -21.458 -22.021 1.00 61.85  ? 5   LYS A O   1 
ATOM   32   C CB  . LYS A 1 5   ? 16.535  -20.188 -22.882 1.00 67.80  ? 5   LYS A CB  1 
ATOM   33   C CG  . LYS A 1 5   ? 17.860  -19.452 -22.882 1.00 70.86  ? 5   LYS A CG  1 
ATOM   34   C CD  . LYS A 1 5   ? 18.915  -20.163 -23.675 1.00 72.05  ? 5   LYS A CD  1 
ATOM   35   C CE  . LYS A 1 5   ? 20.132  -19.299 -23.903 1.00 75.34  ? 5   LYS A CE  1 
ATOM   36   N NZ  . LYS A 1 5   ? 21.308  -20.125 -24.250 1.00 78.88  ? 5   LYS A NZ  1 
ATOM   37   N N   . ARG A 1 6   ? 13.113  -19.562 -22.818 1.00 59.54  ? 6   ARG A N   1 
ATOM   38   C CA  . ARG A 1 6   ? 11.888  -20.197 -23.282 1.00 56.63  ? 6   ARG A CA  1 
ATOM   39   C C   . ARG A 1 6   ? 11.566  -19.728 -24.697 1.00 54.53  ? 6   ARG A C   1 
ATOM   40   O O   . ARG A 1 6   ? 11.988  -18.648 -25.109 1.00 58.57  ? 6   ARG A O   1 
ATOM   41   C CB  . ARG A 1 6   ? 10.706  -19.856 -22.372 1.00 55.66  ? 6   ARG A CB  1 
ATOM   42   C CG  . ARG A 1 6   ? 10.932  -20.186 -20.908 1.00 58.01  ? 6   ARG A CG  1 
ATOM   43   C CD  . ARG A 1 6   ? 9.589   -20.286 -20.219 1.00 58.01  ? 6   ARG A CD  1 
ATOM   44   N NE  . ARG A 1 6   ? 9.689   -20.583 -18.800 1.00 61.22  ? 6   ARG A NE  1 
ATOM   45   C CZ  . ARG A 1 6   ? 10.142  -19.741 -17.882 1.00 64.62  ? 6   ARG A CZ  1 
ATOM   46   N NH1 . ARG A 1 6   ? 10.501  -18.520 -18.226 1.00 66.81  ? 6   ARG A NH1 1 
ATOM   47   N NH2 . ARG A 1 6   ? 10.243  -20.124 -16.624 1.00 67.34  ? 6   ARG A NH2 1 
ATOM   48   N N   . LEU A 1 7   ? 10.795  -20.537 -25.423 1.00 49.73  ? 7   LEU A N   1 
ATOM   49   C CA  . LEU A 1 7   ? 10.279  -20.132 -26.713 1.00 47.95  ? 7   LEU A CA  1 
ATOM   50   C C   . LEU A 1 7   ? 8.881   -19.537 -26.531 1.00 47.86  ? 7   LEU A C   1 
ATOM   51   O O   . LEU A 1 7   ? 7.973   -20.183 -26.001 1.00 45.37  ? 7   LEU A O   1 
ATOM   52   C CB  . LEU A 1 7   ? 10.276  -21.343 -27.648 1.00 46.64  ? 7   LEU A CB  1 
ATOM   53   C CG  . LEU A 1 7   ? 9.506   -21.178 -28.960 1.00 45.26  ? 7   LEU A CG  1 
ATOM   54   C CD1 . LEU A 1 7   ? 10.137  -20.149 -29.881 1.00 44.86  ? 7   LEU A CD1 1 
ATOM   55   C CD2 . LEU A 1 7   ? 9.384   -22.519 -29.671 1.00 44.99  ? 7   LEU A CD2 1 
ATOM   56   N N   . HIS A 1 8   ? 8.721   -18.279 -26.964 1.00 49.74  ? 8   HIS A N   1 
ATOM   57   C CA  . HIS A 1 8   ? 7.408   -17.662 -27.030 1.00 50.03  ? 8   HIS A CA  1 
ATOM   58   C C   . HIS A 1 8   ? 6.841   -17.860 -28.432 1.00 48.57  ? 8   HIS A C   1 
ATOM   59   O O   . HIS A 1 8   ? 7.335   -17.276 -29.397 1.00 47.93  ? 8   HIS A O   1 
ATOM   60   C CB  . HIS A 1 8   ? 7.469   -16.212 -26.558 1.00 52.38  ? 8   HIS A CB  1 
ATOM   61   C CG  . HIS A 1 8   ? 7.831   -16.120 -25.113 1.00 55.91  ? 8   HIS A CG  1 
ATOM   62   N ND1 . HIS A 1 8   ? 6.952   -15.678 -24.145 1.00 56.40  ? 8   HIS A ND1 1 
ATOM   63   C CD2 . HIS A 1 8   ? 8.978   -16.435 -24.472 1.00 57.19  ? 8   HIS A CD2 1 
ATOM   64   C CE1 . HIS A 1 8   ? 7.566   -15.707 -22.966 1.00 58.82  ? 8   HIS A CE1 1 
ATOM   65   N NE2 . HIS A 1 8   ? 8.796   -16.163 -23.138 1.00 58.50  ? 8   HIS A NE2 1 
ATOM   66   N N   . LEU A 1 9   ? 5.792   -18.690 -28.502 1.00 46.89  ? 9   LEU A N   1 
ATOM   67   C CA  . LEU A 1 9   ? 5.250   -19.167 -29.754 1.00 46.73  ? 9   LEU A CA  1 
ATOM   68   C C   . LEU A 1 9   ? 3.827   -18.650 -29.928 1.00 47.67  ? 9   LEU A C   1 
ATOM   69   O O   . LEU A 1 9   ? 2.933   -19.096 -29.217 1.00 47.67  ? 9   LEU A O   1 
ATOM   70   C CB  . LEU A 1 9   ? 5.261   -20.694 -29.747 1.00 46.78  ? 9   LEU A CB  1 
ATOM   71   C CG  . LEU A 1 9   ? 4.534   -21.340 -30.926 1.00 47.85  ? 9   LEU A CG  1 
ATOM   72   C CD1 . LEU A 1 9   ? 5.198   -20.967 -32.249 1.00 48.89  ? 9   LEU A CD1 1 
ATOM   73   C CD2 . LEU A 1 9   ? 4.474   -22.856 -30.774 1.00 48.01  ? 9   LEU A CD2 1 
ATOM   74   N N   . ILE A 1 10  ? 3.635   -17.770 -30.925 1.00 45.22  ? 10  ILE A N   1 
ATOM   75   C CA  . ILE A 1 10  ? 2.357   -17.156 -31.217 1.00 41.71  ? 10  ILE A CA  1 
ATOM   76   C C   . ILE A 1 10  ? 1.764   -17.800 -32.462 1.00 39.14  ? 10  ILE A C   1 
ATOM   77   O O   . ILE A 1 10  ? 2.354   -17.736 -33.523 1.00 36.33  ? 10  ILE A O   1 
ATOM   78   C CB  . ILE A 1 10  ? 2.562   -15.651 -31.442 1.00 44.79  ? 10  ILE A CB  1 
ATOM   79   C CG1 . ILE A 1 10  ? 3.356   -15.015 -30.297 1.00 45.69  ? 10  ILE A CG1 1 
ATOM   80   C CG2 . ILE A 1 10  ? 1.235   -14.931 -31.705 1.00 44.07  ? 10  ILE A CG2 1 
ATOM   81   C CD1 . ILE A 1 10  ? 4.060   -13.743 -30.705 1.00 46.17  ? 10  ILE A CD1 1 
ATOM   82   N N   . ILE A 1 11  ? 0.574   -18.387 -32.320 1.00 40.70  ? 11  ILE A N   1 
ATOM   83   C CA  . ILE A 1 11  ? -0.239  -18.829 -33.441 1.00 39.99  ? 11  ILE A CA  1 
ATOM   84   C C   . ILE A 1 11  ? -1.039  -17.622 -33.914 1.00 40.13  ? 11  ILE A C   1 
ATOM   85   O O   . ILE A 1 11  ? -2.002  -17.236 -33.241 1.00 39.55  ? 11  ILE A O   1 
ATOM   86   C CB  . ILE A 1 11  ? -1.184  -19.973 -33.013 1.00 39.85  ? 11  ILE A CB  1 
ATOM   87   C CG1 . ILE A 1 11  ? -0.439  -21.089 -32.284 1.00 38.19  ? 11  ILE A CG1 1 
ATOM   88   C CG2 . ILE A 1 11  ? -1.988  -20.488 -34.206 1.00 40.02  ? 11  ILE A CG2 1 
ATOM   89   C CD1 . ILE A 1 11  ? 0.606   -21.738 -33.127 1.00 40.51  ? 11  ILE A CD1 1 
ATOM   90   N N   . ALA A 1 12  ? -0.635  -17.032 -35.054 1.00 40.06  ? 12  ALA A N   1 
ATOM   91   C CA  . ALA A 1 12  ? -1.083  -15.687 -35.391 1.00 39.70  ? 12  ALA A CA  1 
ATOM   92   C C   . ALA A 1 12  ? -2.197  -15.750 -36.420 1.00 40.64  ? 12  ALA A C   1 
ATOM   93   O O   . ALA A 1 12  ? -2.330  -16.752 -37.122 1.00 40.67  ? 12  ALA A O   1 
ATOM   94   C CB  . ALA A 1 12  ? 0.058   -14.839 -35.878 1.00 39.09  ? 12  ALA A CB  1 
ATOM   95   N N   . ASP A 1 13  ? -2.994  -14.670 -36.444 1.00 41.44  ? 13  ASP A N   1 
ATOM   96   C CA  . ASP A 1 13  ? -3.964  -14.403 -37.491 1.00 41.91  ? 13  ASP A CA  1 
ATOM   97   C C   . ASP A 1 13  ? -4.852  -15.626 -37.642 1.00 42.24  ? 13  ASP A C   1 
ATOM   98   O O   . ASP A 1 13  ? -5.249  -15.971 -38.762 1.00 49.46  ? 13  ASP A O   1 
ATOM   99   C CB  . ASP A 1 13  ? -3.279  -14.044 -38.816 1.00 41.90  ? 13  ASP A CB  1 
ATOM   100  C CG  . ASP A 1 13  ? -2.784  -12.612 -38.905 1.00 43.54  ? 13  ASP A CG  1 
ATOM   101  O OD1 . ASP A 1 13  ? -3.297  -11.730 -38.170 1.00 43.21  ? 13  ASP A OD1 1 
ATOM   102  O OD2 . ASP A 1 13  ? -1.893  -12.379 -39.727 1.00 45.73  ? 13  ASP A OD2 1 
ATOM   103  N N   . ALA A 1 14  ? -5.135  -16.257 -36.501 1.00 38.73  ? 14  ALA A N   1 
ATOM   104  C CA  . ALA A 1 14  ? -5.835  -17.527 -36.457 1.00 38.51  ? 14  ALA A CA  1 
ATOM   105  C C   . ALA A 1 14  ? -7.278  -17.375 -36.940 1.00 41.45  ? 14  ALA A C   1 
ATOM   106  O O   . ALA A 1 14  ? -7.969  -16.396 -36.620 1.00 40.78  ? 14  ALA A O   1 
ATOM   107  C CB  . ALA A 1 14  ? -5.796  -18.056 -35.044 1.00 37.70  ? 14  ALA A CB  1 
ATOM   108  N N   . GLU A 1 15  ? -7.745  -18.385 -37.686 1.00 43.76  ? 15  GLU A N   1 
ATOM   109  C CA  . GLU A 1 15  ? -9.122  -18.413 -38.157 1.00 44.99  ? 15  GLU A CA  1 
ATOM   110  C C   . GLU A 1 15  ? -10.000 -18.990 -37.050 1.00 44.07  ? 15  GLU A C   1 
ATOM   111  O O   . GLU A 1 15  ? -10.745 -19.957 -37.259 1.00 43.75  ? 15  GLU A O   1 
ATOM   112  C CB  . GLU A 1 15  ? -9.195  -19.177 -39.479 1.00 46.76  ? 15  GLU A CB  1 
ATOM   113  C CG  . GLU A 1 15  ? -8.358  -18.529 -40.576 1.00 48.63  ? 15  GLU A CG  1 
ATOM   114  C CD  . GLU A 1 15  ? -8.766  -17.106 -40.908 1.00 48.70  ? 15  GLU A CD  1 
ATOM   115  O OE1 . GLU A 1 15  ? -7.941  -16.361 -41.493 1.00 50.27  ? 15  GLU A OE1 1 
ATOM   116  O OE2 . GLU A 1 15  ? -9.907  -16.747 -40.553 1.00 49.63  ? 15  GLU A OE2 1 
ATOM   117  N N   . LEU A 1 16  ? -9.893  -18.354 -35.872 1.00 41.00  ? 16  LEU A N   1 
ATOM   118  C CA  . LEU A 1 16  ? -10.710 -18.694 -34.727 1.00 40.39  ? 16  LEU A CA  1 
ATOM   119  C C   . LEU A 1 16  ? -11.538 -17.473 -34.352 1.00 40.92  ? 16  LEU A C   1 
ATOM   120  O O   . LEU A 1 16  ? -11.000 -16.475 -33.867 1.00 40.95  ? 16  LEU A O   1 
ATOM   121  C CB  . LEU A 1 16  ? -9.812  -19.140 -33.572 1.00 40.57  ? 16  LEU A CB  1 
ATOM   122  C CG  . LEU A 1 16  ? -10.518 -19.475 -32.253 1.00 40.25  ? 16  LEU A CG  1 
ATOM   123  C CD1 . LEU A 1 16  ? -11.372 -20.723 -32.368 1.00 38.76  ? 16  LEU A CD1 1 
ATOM   124  C CD2 . LEU A 1 16  ? -9.503  -19.646 -31.137 1.00 40.24  ? 16  LEU A CD2 1 
ATOM   125  N N   . GLU A 1 17  ? -12.848 -17.580 -34.600 1.00 40.70  ? 17  GLU A N   1 
ATOM   126  C CA  . GLU A 1 17  ? -13.778 -16.497 -34.345 1.00 41.52  ? 17  GLU A CA  1 
ATOM   127  C C   . GLU A 1 17  ? -15.159 -17.096 -34.156 1.00 41.29  ? 17  GLU A C   1 
ATOM   128  O O   . GLU A 1 17  ? -15.403 -18.237 -34.550 1.00 40.61  ? 17  GLU A O   1 
ATOM   129  C CB  . GLU A 1 17  ? -13.809 -15.510 -35.510 1.00 43.30  ? 17  GLU A CB  1 
ATOM   130  C CG  . GLU A 1 17  ? -14.198 -16.148 -36.826 1.00 45.19  ? 17  GLU A CG  1 
ATOM   131  C CD  . GLU A 1 17  ? -14.035 -15.248 -38.038 1.00 48.84  ? 17  GLU A CD  1 
ATOM   132  O OE1 . GLU A 1 17  ? -13.377 -15.694 -39.014 1.00 53.90  ? 17  GLU A OE1 1 
ATOM   133  O OE2 . GLU A 1 17  ? -14.551 -14.104 -38.002 1.00 48.07  ? 17  GLU A OE2 1 
ATOM   134  N N   . THR A 1 18  ? -16.051 -16.309 -33.548 1.00 41.38  ? 18  THR A N   1 
ATOM   135  C CA  . THR A 1 18  ? -17.444 -16.695 -33.493 1.00 40.44  ? 18  THR A CA  1 
ATOM   136  C C   . THR A 1 18  ? -18.074 -16.249 -34.793 1.00 40.10  ? 18  THR A C   1 
ATOM   137  O O   . THR A 1 18  ? -17.448 -15.569 -35.589 1.00 39.53  ? 18  THR A O   1 
ATOM   138  C CB  . THR A 1 18  ? -18.182 -16.149 -32.266 1.00 41.63  ? 18  THR A CB  1 
ATOM   139  O OG1 . THR A 1 18  ? -18.521 -14.769 -32.446 1.00 42.63  ? 18  THR A OG1 1 
ATOM   140  C CG2 . THR A 1 18  ? -17.395 -16.383 -30.996 1.00 40.84  ? 18  THR A CG2 1 
ATOM   141  N N   . VAL A 1 19  ? -19.315 -16.658 -35.006 1.00 42.08  ? 19  VAL A N   1 
ATOM   142  C CA  . VAL A 1 19  ? -19.909 -16.414 -36.297 1.00 43.82  ? 19  VAL A CA  1 
ATOM   143  C C   . VAL A 1 19  ? -19.810 -14.913 -36.548 1.00 45.87  ? 19  VAL A C   1 
ATOM   144  O O   . VAL A 1 19  ? -20.049 -14.113 -35.644 1.00 50.74  ? 19  VAL A O   1 
ATOM   145  C CB  . VAL A 1 19  ? -21.335 -16.959 -36.385 1.00 44.15  ? 19  VAL A CB  1 
ATOM   146  C CG1 . VAL A 1 19  ? -21.966 -16.613 -37.716 1.00 45.06  ? 19  VAL A CG1 1 
ATOM   147  C CG2 . VAL A 1 19  ? -21.326 -18.462 -36.173 1.00 43.97  ? 19  VAL A CG2 1 
ATOM   148  N N   . PRO A 1 20  ? -19.343 -14.489 -37.738 1.00 43.39  ? 20  PRO A N   1 
ATOM   149  C CA  . PRO A 1 20  ? -19.370 -13.078 -38.111 1.00 44.52  ? 20  PRO A CA  1 
ATOM   150  C C   . PRO A 1 20  ? -20.776 -12.475 -38.174 1.00 46.65  ? 20  PRO A C   1 
ATOM   151  O O   . PRO A 1 20  ? -21.724 -13.118 -38.638 1.00 46.93  ? 20  PRO A O   1 
ATOM   152  C CB  . PRO A 1 20  ? -18.711 -13.086 -39.493 1.00 44.24  ? 20  PRO A CB  1 
ATOM   153  C CG  . PRO A 1 20  ? -17.869 -14.324 -39.463 1.00 42.27  ? 20  PRO A CG  1 
ATOM   154  C CD  . PRO A 1 20  ? -18.731 -15.338 -38.758 1.00 41.78  ? 20  PRO A CD  1 
ATOM   155  N N   . PRO A 1 21  ? -20.944 -11.221 -37.687 1.00 49.03  ? 21  PRO A N   1 
ATOM   156  C CA  . PRO A 1 21  ? -22.233 -10.526 -37.691 1.00 53.00  ? 21  PRO A CA  1 
ATOM   157  C C   . PRO A 1 21  ? -22.955 -10.568 -39.029 1.00 55.98  ? 21  PRO A C   1 
ATOM   158  O O   . PRO A 1 21  ? -24.179 -10.725 -39.071 1.00 57.52  ? 21  PRO A O   1 
ATOM   159  C CB  . PRO A 1 21  ? -21.864 -9.070  -37.383 1.00 53.09  ? 21  PRO A CB  1 
ATOM   160  C CG  . PRO A 1 21  ? -20.635 -9.190  -36.531 1.00 51.02  ? 21  PRO A CG  1 
ATOM   161  C CD  . PRO A 1 21  ? -19.901 -10.409 -37.049 1.00 48.65  ? 21  PRO A CD  1 
ATOM   162  N N   . GLU A 1 22  ? -22.165 -10.437 -40.103 1.00 56.76  ? 22  GLU A N   1 
ATOM   163  C CA  . GLU A 1 22  ? -22.683 -10.393 -41.459 1.00 59.33  ? 22  GLU A CA  1 
ATOM   164  C C   . GLU A 1 22  ? -23.621 -11.565 -41.731 1.00 60.29  ? 22  GLU A C   1 
ATOM   165  O O   . GLU A 1 22  ? -24.650 -11.346 -42.357 1.00 63.17  ? 22  GLU A O   1 
ATOM   166  C CB  . GLU A 1 22  ? -21.542 -10.419 -42.474 1.00 59.19  ? 22  GLU A CB  1 
ATOM   167  C CG  . GLU A 1 22  ? -20.602 -9.239  -42.351 1.00 59.73  ? 22  GLU A CG  1 
ATOM   168  C CD  . GLU A 1 22  ? -19.423 -9.493  -41.428 1.00 58.27  ? 22  GLU A CD  1 
ATOM   169  O OE1 . GLU A 1 22  ? -18.302 -9.042  -41.747 1.00 55.91  ? 22  GLU A OE1 1 
ATOM   170  O OE2 . GLU A 1 22  ? -19.629 -10.170 -40.396 1.00 60.50  ? 22  GLU A OE2 1 
ATOM   171  N N   . ILE A 1 23  ? -23.270 -12.780 -41.264 1.00 58.70  ? 23  ILE A N   1 
ATOM   172  C CA  . ILE A 1 23  ? -23.956 -13.990 -41.694 1.00 59.59  ? 23  ILE A CA  1 
ATOM   173  C C   . ILE A 1 23  ? -24.709 -14.670 -40.544 1.00 61.57  ? 23  ILE A C   1 
ATOM   174  O O   . ILE A 1 23  ? -24.923 -15.889 -40.596 1.00 61.65  ? 23  ILE A O   1 
ATOM   175  C CB  . ILE A 1 23  ? -22.951 -14.948 -42.366 1.00 57.17  ? 23  ILE A CB  1 
ATOM   176  C CG1 . ILE A 1 23  ? -21.810 -15.356 -41.432 1.00 53.24  ? 23  ILE A CG1 1 
ATOM   177  C CG2 . ILE A 1 23  ? -22.424 -14.336 -43.650 1.00 58.40  ? 23  ILE A CG2 1 
ATOM   178  C CD1 . ILE A 1 23  ? -21.044 -16.566 -41.904 1.00 50.73  ? 23  ILE A CD1 1 
ATOM   179  N N   . LEU A 1 24  ? -25.168 -13.906 -39.536 1.00 62.88  ? 24  LEU A N   1 
ATOM   180  C CA  . LEU A 1 24  ? -25.901 -14.501 -38.427 1.00 62.53  ? 24  LEU A CA  1 
ATOM   181  C C   . LEU A 1 24  ? -27.285 -14.942 -38.902 1.00 67.41  ? 24  LEU A C   1 
ATOM   182  O O   . LEU A 1 24  ? -27.935 -15.773 -38.266 1.00 68.27  ? 24  LEU A O   1 
ATOM   183  C CB  . LEU A 1 24  ? -26.002 -13.510 -37.268 1.00 62.23  ? 24  LEU A CB  1 
ATOM   184  C CG  . LEU A 1 24  ? -24.693 -13.143 -36.568 1.00 61.34  ? 24  LEU A CG  1 
ATOM   185  C CD1 . LEU A 1 24  ? -24.913 -12.063 -35.517 1.00 62.79  ? 24  LEU A CD1 1 
ATOM   186  C CD2 . LEU A 1 24  ? -24.058 -14.350 -35.909 1.00 60.39  ? 24  LEU A CD2 1 
ATOM   187  N N   . ASP A 1 25  ? -27.720 -14.424 -40.051 1.00 69.91  ? 25  ASP A N   1 
ATOM   188  C CA  . ASP A 1 25  ? -29.045 -14.742 -40.548 1.00 75.12  ? 25  ASP A CA  1 
ATOM   189  C C   . ASP A 1 25  ? -28.937 -15.425 -41.906 1.00 75.24  ? 25  ASP A C   1 
ATOM   190  O O   . ASP A 1 25  ? -29.823 -15.268 -42.743 1.00 79.37  ? 25  ASP A O   1 
ATOM   191  C CB  . ASP A 1 25  ? -29.912 -13.481 -40.619 1.00 80.01  ? 25  ASP A CB  1 
ATOM   192  C CG  . ASP A 1 25  ? -29.260 -12.339 -41.384 1.00 84.52  ? 25  ASP A CG  1 
ATOM   193  O OD1 . ASP A 1 25  ? -28.171 -12.575 -41.979 1.00 87.75  ? 25  ASP A OD1 1 
ATOM   194  O OD2 . ASP A 1 25  ? -29.819 -11.214 -41.360 1.00 84.48  ? 25  ASP A OD2 1 
ATOM   195  N N   . HIS A 1 26  ? -27.849 -16.167 -42.128 1.00 70.54  ? 26  HIS A N   1 
ATOM   196  C CA  . HIS A 1 26  ? -27.766 -17.018 -43.301 1.00 71.00  ? 26  HIS A CA  1 
ATOM   197  C C   . HIS A 1 26  ? -28.444 -18.322 -42.898 1.00 72.59  ? 26  HIS A C   1 
ATOM   198  O O   . HIS A 1 26  ? -28.269 -18.782 -41.769 1.00 74.32  ? 26  HIS A O   1 
ATOM   199  C CB  . HIS A 1 26  ? -26.316 -17.135 -43.783 1.00 69.14  ? 26  HIS A CB  1 
ATOM   200  C CG  . HIS A 1 26  ? -26.144 -17.951 -45.022 1.00 71.18  ? 26  HIS A CG  1 
ATOM   201  N ND1 . HIS A 1 26  ? -26.324 -19.319 -45.058 1.00 70.41  ? 26  HIS A ND1 1 
ATOM   202  C CD2 . HIS A 1 26  ? -25.793 -17.590 -46.269 1.00 72.66  ? 26  HIS A CD2 1 
ATOM   203  C CE1 . HIS A 1 26  ? -26.097 -19.758 -46.291 1.00 70.73  ? 26  HIS A CE1 1 
ATOM   204  N NE2 . HIS A 1 26  ? -25.769 -18.726 -47.043 1.00 72.41  ? 26  HIS A NE2 1 
ATOM   205  N N   . PRO A 1 27  ? -29.237 -18.967 -43.787 1.00 71.78  ? 27  PRO A N   1 
ATOM   206  C CA  . PRO A 1 27  ? -29.964 -20.179 -43.420 1.00 70.54  ? 27  PRO A CA  1 
ATOM   207  C C   . PRO A 1 27  ? -29.127 -21.186 -42.640 1.00 68.02  ? 27  PRO A C   1 
ATOM   208  O O   . PRO A 1 27  ? -29.553 -21.651 -41.581 1.00 67.33  ? 27  PRO A O   1 
ATOM   209  C CB  . PRO A 1 27  ? -30.283 -20.759 -44.802 1.00 71.85  ? 27  PRO A CB  1 
ATOM   210  C CG  . PRO A 1 27  ? -30.573 -19.539 -45.638 1.00 74.45  ? 27  PRO A CG  1 
ATOM   211  C CD  . PRO A 1 27  ? -29.628 -18.475 -45.122 1.00 72.93  ? 27  PRO A CD  1 
ATOM   212  N N   . ALA A 1 28  ? -27.917 -21.448 -43.163 1.00 65.72  ? 28  ALA A N   1 
ATOM   213  C CA  . ALA A 1 28  ? -27.068 -22.550 -42.739 1.00 61.37  ? 28  ALA A CA  1 
ATOM   214  C C   . ALA A 1 28  ? -26.631 -22.276 -41.306 1.00 59.75  ? 28  ALA A C   1 
ATOM   215  O O   . ALA A 1 28  ? -26.446 -23.210 -40.528 1.00 56.58  ? 28  ALA A O   1 
ATOM   216  C CB  . ALA A 1 28  ? -25.878 -22.695 -43.660 1.00 59.30  ? 28  ALA A CB  1 
ATOM   217  N N   . ILE A 1 29  ? -26.501 -20.984 -40.970 1.00 59.65  ? 29  ILE A N   1 
ATOM   218  C CA  . ILE A 1 29  ? -26.098 -20.572 -39.637 1.00 57.73  ? 29  ILE A CA  1 
ATOM   219  C C   . ILE A 1 29  ? -27.260 -20.745 -38.654 1.00 61.41  ? 29  ILE A C   1 
ATOM   220  O O   . ILE A 1 29  ? -27.015 -21.097 -37.500 1.00 59.83  ? 29  ILE A O   1 
ATOM   221  C CB  . ILE A 1 29  ? -25.561 -19.129 -39.683 1.00 57.25  ? 29  ILE A CB  1 
ATOM   222  C CG1 . ILE A 1 29  ? -24.336 -19.009 -40.600 1.00 56.15  ? 29  ILE A CG1 1 
ATOM   223  C CG2 . ILE A 1 29  ? -25.278 -18.595 -38.286 1.00 56.45  ? 29  ILE A CG2 1 
ATOM   224  C CD1 . ILE A 1 29  ? -23.093 -19.772 -40.144 1.00 53.17  ? 29  ILE A CD1 1 
ATOM   225  N N   . VAL A 1 30  ? -28.507 -20.522 -39.118 1.00 65.83  ? 30  VAL A N   1 
ATOM   226  C CA  . VAL A 1 30  ? -29.688 -20.583 -38.267 1.00 70.20  ? 30  VAL A CA  1 
ATOM   227  C C   . VAL A 1 30  ? -30.048 -22.044 -38.002 1.00 74.32  ? 30  VAL A C   1 
ATOM   228  O O   . VAL A 1 30  ? -30.381 -22.422 -36.878 1.00 79.97  ? 30  VAL A O   1 
ATOM   229  C CB  . VAL A 1 30  ? -30.886 -19.843 -38.894 1.00 75.04  ? 30  VAL A CB  1 
ATOM   230  C CG1 . VAL A 1 30  ? -32.087 -19.835 -37.958 1.00 78.12  ? 30  VAL A CG1 1 
ATOM   231  C CG2 . VAL A 1 30  ? -30.554 -18.420 -39.322 1.00 75.58  ? 30  VAL A CG2 1 
ATOM   232  N N   . ASN A 1 31  ? -30.015 -22.848 -39.067 1.00 74.79  ? 31  ASN A N   1 
ATOM   233  C CA  . ASN A 1 31  ? -30.374 -24.252 -38.999 1.00 76.29  ? 31  ASN A CA  1 
ATOM   234  C C   . ASN A 1 31  ? -29.399 -25.014 -38.114 1.00 74.76  ? 31  ASN A C   1 
ATOM   235  O O   . ASN A 1 31  ? -29.763 -26.025 -37.510 1.00 73.64  ? 31  ASN A O   1 
ATOM   236  C CB  . ASN A 1 31  ? -30.338 -24.909 -40.378 1.00 77.68  ? 31  ASN A CB  1 
ATOM   237  C CG  . ASN A 1 31  ? -31.310 -24.270 -41.339 1.00 78.76  ? 31  ASN A CG  1 
ATOM   238  O OD1 . ASN A 1 31  ? -32.472 -24.052 -40.980 1.00 80.64  ? 31  ASN A OD1 1 
ATOM   239  N ND2 . ASN A 1 31  ? -30.847 -23.973 -42.544 1.00 78.31  ? 31  ASN A ND2 1 
ATOM   240  N N   . TYR A 1 32  ? -28.142 -24.555 -38.127 1.00 73.07  ? 32  TYR A N   1 
ATOM   241  C CA  . TYR A 1 32  ? -27.096 -25.149 -37.318 1.00 69.81  ? 32  TYR A CA  1 
ATOM   242  C C   . TYR A 1 32  ? -27.295 -24.687 -35.878 1.00 72.01  ? 32  TYR A C   1 
ATOM   243  O O   . TYR A 1 32  ? -27.198 -25.488 -34.946 1.00 71.93  ? 32  TYR A O   1 
ATOM   244  C CB  . TYR A 1 32  ? -25.743 -24.761 -37.916 1.00 66.06  ? 32  TYR A CB  1 
ATOM   245  C CG  . TYR A 1 32  ? -24.555 -25.272 -37.119 1.00 63.89  ? 32  TYR A CG  1 
ATOM   246  C CD1 . TYR A 1 32  ? -24.189 -24.680 -35.916 1.00 63.73  ? 32  TYR A CD1 1 
ATOM   247  C CD2 . TYR A 1 32  ? -23.814 -26.362 -37.561 1.00 62.99  ? 32  TYR A CD2 1 
ATOM   248  C CE1 . TYR A 1 32  ? -23.123 -25.160 -35.173 1.00 61.99  ? 32  TYR A CE1 1 
ATOM   249  C CE2 . TYR A 1 32  ? -22.745 -26.849 -36.830 1.00 60.09  ? 32  TYR A CE2 1 
ATOM   250  C CZ  . TYR A 1 32  ? -22.411 -26.252 -35.632 1.00 59.85  ? 32  TYR A CZ  1 
ATOM   251  O OH  . TYR A 1 32  ? -21.366 -26.719 -34.915 1.00 62.49  ? 32  TYR A OH  1 
ATOM   252  N N   . ALA A 1 33  ? -27.593 -23.389 -35.726 1.00 72.58  ? 33  ALA A N   1 
ATOM   253  C CA  . ALA A 1 33  ? -27.728 -22.777 -34.416 1.00 74.34  ? 33  ALA A CA  1 
ATOM   254  C C   . ALA A 1 33  ? -28.952 -23.344 -33.721 1.00 76.42  ? 33  ALA A C   1 
ATOM   255  O O   . ALA A 1 33  ? -28.931 -23.517 -32.503 1.00 76.21  ? 33  ALA A O   1 
ATOM   256  C CB  . ALA A 1 33  ? -27.822 -21.279 -34.544 1.00 76.85  ? 33  ALA A CB  1 
ATOM   257  N N   . LYS A 1 34  ? -29.989 -23.619 -34.527 1.00 80.13  ? 34  LYS A N   1 
ATOM   258  C CA  . LYS A 1 34  ? -31.225 -24.218 -34.056 1.00 84.29  ? 34  LYS A CA  1 
ATOM   259  C C   . LYS A 1 34  ? -30.938 -25.628 -33.547 1.00 81.06  ? 34  LYS A C   1 
ATOM   260  O O   . LYS A 1 34  ? -31.178 -25.908 -32.376 1.00 79.82  ? 34  LYS A O   1 
ATOM   261  C CB  . LYS A 1 34  ? -32.280 -24.188 -35.165 1.00 90.82  ? 34  LYS A CB  1 
ATOM   262  C CG  . LYS A 1 34  ? -33.696 -24.546 -34.723 1.00 98.98  ? 34  LYS A CG  1 
ATOM   263  C CD  . LYS A 1 34  ? -34.790 -24.109 -35.695 1.00 103.72 ? 34  LYS A CD  1 
ATOM   264  C CE  . LYS A 1 34  ? -34.652 -24.705 -37.082 1.00 106.18 ? 34  LYS A CE  1 
ATOM   265  N NZ  . LYS A 1 34  ? -34.692 -26.187 -37.058 1.00 110.06 ? 34  LYS A NZ  1 
ATOM   266  N N   . ARG A 1 35  ? -30.374 -26.488 -34.406 1.00 80.41  ? 35  ARG A N   1 
ATOM   267  C CA  . ARG A 1 35  ? -30.097 -27.866 -34.020 1.00 84.00  ? 35  ARG A CA  1 
ATOM   268  C C   . ARG A 1 35  ? -29.254 -27.882 -32.747 1.00 80.24  ? 35  ARG A C   1 
ATOM   269  O O   . ARG A 1 35  ? -29.552 -28.636 -31.831 1.00 80.50  ? 35  ARG A O   1 
ATOM   270  C CB  . ARG A 1 35  ? -29.426 -28.677 -35.139 1.00 87.51  ? 35  ARG A CB  1 
ATOM   271  C CG  . ARG A 1 35  ? -30.383 -29.180 -36.218 1.00 95.32  ? 35  ARG A CG  1 
ATOM   272  C CD  . ARG A 1 35  ? -29.823 -30.249 -37.148 1.00 100.50 ? 35  ARG A CD  1 
ATOM   273  N NE  . ARG A 1 35  ? -28.404 -30.060 -37.448 1.00 107.49 ? 35  ARG A NE  1 
ATOM   274  C CZ  . ARG A 1 35  ? -27.909 -29.478 -38.543 1.00 111.29 ? 35  ARG A CZ  1 
ATOM   275  N NH1 . ARG A 1 35  ? -26.599 -29.397 -38.715 1.00 106.17 ? 35  ARG A NH1 1 
ATOM   276  N NH2 . ARG A 1 35  ? -28.717 -28.972 -39.460 1.00 116.96 ? 35  ARG A NH2 1 
ATOM   277  N N   . ARG A 1 36  ? -28.233 -27.023 -32.670 1.00 80.20  ? 36  ARG A N   1 
ATOM   278  C CA  . ARG A 1 36  ? -27.336 -27.012 -31.523 1.00 76.95  ? 36  ARG A CA  1 
ATOM   279  C C   . ARG A 1 36  ? -27.888 -26.172 -30.379 1.00 75.95  ? 36  ARG A C   1 
ATOM   280  O O   . ARG A 1 36  ? -27.177 -25.970 -29.397 1.00 72.25  ? 36  ARG A O   1 
ATOM   281  C CB  . ARG A 1 36  ? -25.949 -26.505 -31.913 1.00 75.84  ? 36  ARG A CB  1 
ATOM   282  C CG  . ARG A 1 36  ? -25.085 -27.597 -32.527 1.00 79.50  ? 36  ARG A CG  1 
ATOM   283  C CD  . ARG A 1 36  ? -23.606 -27.398 -32.260 1.00 81.45  ? 36  ARG A CD  1 
ATOM   284  N NE  . ARG A 1 36  ? -23.371 -27.010 -30.873 1.00 81.94  ? 36  ARG A NE  1 
ATOM   285  C CZ  . ARG A 1 36  ? -22.540 -26.050 -30.475 1.00 80.28  ? 36  ARG A CZ  1 
ATOM   286  N NH1 . ARG A 1 36  ? -21.692 -25.492 -31.327 1.00 73.49  ? 36  ARG A NH1 1 
ATOM   287  N NH2 . ARG A 1 36  ? -22.529 -25.692 -29.202 1.00 83.57  ? 36  ARG A NH2 1 
ATOM   288  N N   . LYS A 1 37  ? -29.144 -25.717 -30.507 1.00 77.14  ? 37  LYS A N   1 
ATOM   289  C CA  . LYS A 1 37  ? -29.826 -25.004 -29.442 1.00 77.85  ? 37  LYS A CA  1 
ATOM   290  C C   . LYS A 1 37  ? -28.884 -23.953 -28.859 1.00 71.88  ? 37  LYS A C   1 
ATOM   291  O O   . LYS A 1 37  ? -28.646 -23.937 -27.652 1.00 69.32  ? 37  LYS A O   1 
ATOM   292  C CB  . LYS A 1 37  ? -30.289 -25.993 -28.366 1.00 81.49  ? 37  LYS A CB  1 
ATOM   293  C CG  . LYS A 1 37  ? -31.227 -27.095 -28.847 1.00 86.31  ? 37  LYS A CG  1 
ATOM   294  C CD  . LYS A 1 37  ? -31.899 -27.872 -27.721 1.00 91.85  ? 37  LYS A CD  1 
ATOM   295  C CE  . LYS A 1 37  ? -30.915 -28.563 -26.795 1.00 92.40  ? 37  LYS A CE  1 
ATOM   296  N NZ  . LYS A 1 37  ? -31.594 -29.264 -25.676 1.00 95.11  ? 37  LYS A NZ  1 
ATOM   297  N N   . LYS A 1 38  ? -28.324 -23.102 -29.729 1.00 67.98  ? 38  LYS A N   1 
ATOM   298  C CA  . LYS A 1 38  ? -27.381 -22.095 -29.273 1.00 68.60  ? 38  LYS A CA  1 
ATOM   299  C C   . LYS A 1 38  ? -27.507 -20.831 -30.125 1.00 69.21  ? 38  LYS A C   1 
ATOM   300  O O   . LYS A 1 38  ? -27.676 -20.908 -31.345 1.00 69.56  ? 38  LYS A O   1 
ATOM   301  C CB  . LYS A 1 38  ? -25.960 -22.659 -29.311 1.00 67.16  ? 38  LYS A CB  1 
ATOM   302  C CG  . LYS A 1 38  ? -25.138 -22.392 -28.060 1.00 67.91  ? 38  LYS A CG  1 
ATOM   303  C CD  . LYS A 1 38  ? -23.655 -22.606 -28.262 1.00 66.74  ? 38  LYS A CD  1 
ATOM   304  C CE  . LYS A 1 38  ? -22.849 -22.414 -26.994 1.00 67.57  ? 38  LYS A CE  1 
ATOM   305  N NZ  . LYS A 1 38  ? -23.111 -21.088 -26.383 1.00 68.86  ? 38  LYS A NZ  1 
ATOM   306  N N   . ARG A 1 39  ? -27.423 -19.671 -29.455 1.00 68.47  ? 39  ARG A N   1 
ATOM   307  C CA  . ARG A 1 39  ? -27.498 -18.381 -30.118 1.00 68.08  ? 39  ARG A CA  1 
ATOM   308  C C   . ARG A 1 39  ? -26.356 -18.242 -31.127 1.00 65.33  ? 39  ARG A C   1 
ATOM   309  O O   . ARG A 1 39  ? -25.184 -18.288 -30.743 1.00 62.07  ? 39  ARG A O   1 
ATOM   310  C CB  . ARG A 1 39  ? -27.392 -17.260 -29.086 1.00 69.46  ? 39  ARG A CB  1 
ATOM   311  C CG  . ARG A 1 39  ? -28.658 -17.010 -28.287 1.00 73.87  ? 39  ARG A CG  1 
ATOM   312  C CD  . ARG A 1 39  ? -28.322 -16.285 -26.999 1.00 76.18  ? 39  ARG A CD  1 
ATOM   313  N NE  . ARG A 1 39  ? -29.289 -15.255 -26.651 1.00 79.36  ? 39  ARG A NE  1 
ATOM   314  C CZ  . ARG A 1 39  ? -30.317 -15.429 -25.832 1.00 84.16  ? 39  ARG A CZ  1 
ATOM   315  N NH1 . ARG A 1 39  ? -30.955 -14.381 -25.342 1.00 88.81  ? 39  ARG A NH1 1 
ATOM   316  N NH2 . ARG A 1 39  ? -30.669 -16.647 -25.457 1.00 84.26  ? 39  ARG A NH2 1 
ATOM   317  N N   . PRO A 1 40  ? -26.658 -17.986 -32.426 1.00 64.74  ? 40  PRO A N   1 
ATOM   318  C CA  . PRO A 1 40  ? -25.660 -18.060 -33.495 1.00 62.21  ? 40  PRO A CA  1 
ATOM   319  C C   . PRO A 1 40  ? -24.380 -17.279 -33.236 1.00 58.60  ? 40  PRO A C   1 
ATOM   320  O O   . PRO A 1 40  ? -23.307 -17.732 -33.620 1.00 56.38  ? 40  PRO A O   1 
ATOM   321  C CB  . PRO A 1 40  ? -26.342 -17.415 -34.707 1.00 63.91  ? 40  PRO A CB  1 
ATOM   322  C CG  . PRO A 1 40  ? -27.816 -17.579 -34.439 1.00 65.64  ? 40  PRO A CG  1 
ATOM   323  C CD  . PRO A 1 40  ? -27.967 -17.551 -32.932 1.00 66.49  ? 40  PRO A CD  1 
ATOM   324  N N   . GLU A 1 41  ? -24.518 -16.126 -32.569 1.00 59.12  ? 41  GLU A N   1 
ATOM   325  C CA  . GLU A 1 41  ? -23.406 -15.211 -32.344 1.00 58.22  ? 41  GLU A CA  1 
ATOM   326  C C   . GLU A 1 41  ? -22.450 -15.743 -31.272 1.00 58.14  ? 41  GLU A C   1 
ATOM   327  O O   . GLU A 1 41  ? -21.363 -15.190 -31.112 1.00 57.48  ? 41  GLU A O   1 
ATOM   328  C CB  . GLU A 1 41  ? -23.909 -13.817 -31.956 1.00 58.73  ? 41  GLU A CB  1 
ATOM   329  C CG  . GLU A 1 41  ? -24.826 -13.785 -30.734 1.00 59.30  ? 41  GLU A CG  1 
ATOM   330  C CD  . GLU A 1 41  ? -26.308 -14.055 -30.974 1.00 59.66  ? 41  GLU A CD  1 
ATOM   331  O OE1 . GLU A 1 41  ? -27.109 -13.792 -30.050 1.00 60.31  ? 41  GLU A OE1 1 
ATOM   332  O OE2 . GLU A 1 41  ? -26.664 -14.525 -32.080 1.00 58.00  ? 41  GLU A OE2 1 
ATOM   333  N N   . LYS A 1 42  ? -22.856 -16.804 -30.551 1.00 59.47  ? 42  LYS A N   1 
ATOM   334  C CA  . LYS A 1 42  ? -22.027 -17.437 -29.535 1.00 58.43  ? 42  LYS A CA  1 
ATOM   335  C C   . LYS A 1 42  ? -21.201 -18.580 -30.121 1.00 54.97  ? 42  LYS A C   1 
ATOM   336  O O   . LYS A 1 42  ? -20.277 -19.065 -29.465 1.00 52.14  ? 42  LYS A O   1 
ATOM   337  C CB  . LYS A 1 42  ? -22.886 -18.091 -28.451 1.00 61.67  ? 42  LYS A CB  1 
ATOM   338  C CG  . LYS A 1 42  ? -23.977 -17.231 -27.836 1.00 65.41  ? 42  LYS A CG  1 
ATOM   339  C CD  . LYS A 1 42  ? -23.509 -16.333 -26.728 1.00 66.48  ? 42  LYS A CD  1 
ATOM   340  C CE  . LYS A 1 42  ? -24.603 -16.118 -25.704 1.00 70.96  ? 42  LYS A CE  1 
ATOM   341  N NZ  . LYS A 1 42  ? -24.357 -14.896 -24.901 1.00 75.41  ? 42  LYS A NZ  1 
ATOM   342  N N   . ILE A 1 43  ? -21.587 -19.045 -31.319 1.00 53.85  ? 43  ILE A N   1 
ATOM   343  C CA  . ILE A 1 43  ? -21.052 -20.278 -31.884 1.00 51.99  ? 43  ILE A CA  1 
ATOM   344  C C   . ILE A 1 43  ? -19.692 -19.991 -32.520 1.00 47.39  ? 43  ILE A C   1 
ATOM   345  O O   . ILE A 1 43  ? -19.526 -18.949 -33.135 1.00 47.54  ? 43  ILE A O   1 
ATOM   346  C CB  . ILE A 1 43  ? -22.057 -20.873 -32.894 1.00 51.77  ? 43  ILE A CB  1 
ATOM   347  C CG1 . ILE A 1 43  ? -23.330 -21.336 -32.182 1.00 54.53  ? 43  ILE A CG1 1 
ATOM   348  C CG2 . ILE A 1 43  ? -21.423 -21.989 -33.715 1.00 49.82  ? 43  ILE A CG2 1 
ATOM   349  C CD1 . ILE A 1 43  ? -24.377 -21.970 -33.085 1.00 56.53  ? 43  ILE A CD1 1 
ATOM   350  N N   . ILE A 1 44  ? -18.740 -20.921 -32.394 1.00 43.84  ? 44  ILE A N   1 
ATOM   351  C CA  . ILE A 1 44  ? -17.469 -20.795 -33.099 1.00 42.67  ? 44  ILE A CA  1 
ATOM   352  C C   . ILE A 1 44  ? -17.676 -21.154 -34.567 1.00 43.34  ? 44  ILE A C   1 
ATOM   353  O O   . ILE A 1 44  ? -18.206 -22.217 -34.883 1.00 43.06  ? 44  ILE A O   1 
ATOM   354  C CB  . ILE A 1 44  ? -16.359 -21.669 -32.473 1.00 39.85  ? 44  ILE A CB  1 
ATOM   355  C CG1 . ILE A 1 44  ? -16.015 -21.230 -31.045 1.00 38.48  ? 44  ILE A CG1 1 
ATOM   356  C CG2 . ILE A 1 44  ? -15.128 -21.698 -33.363 1.00 37.30  ? 44  ILE A CG2 1 
ATOM   357  C CD1 . ILE A 1 44  ? -15.257 -19.948 -30.956 1.00 37.59  ? 44  ILE A CD1 1 
ATOM   358  N N   . LEU A 1 45  ? -17.200 -20.267 -35.447 1.00 46.11  ? 45  LEU A N   1 
ATOM   359  C CA  . LEU A 1 45  ? -17.298 -20.446 -36.886 1.00 47.27  ? 45  LEU A CA  1 
ATOM   360  C C   . LEU A 1 45  ? -16.397 -21.597 -37.312 1.00 45.02  ? 45  LEU A C   1 
ATOM   361  O O   . LEU A 1 45  ? -15.182 -21.540 -37.100 1.00 40.65  ? 45  LEU A O   1 
ATOM   362  C CB  . LEU A 1 45  ? -16.870 -19.156 -37.597 1.00 49.27  ? 45  LEU A CB  1 
ATOM   363  C CG  . LEU A 1 45  ? -16.892 -19.208 -39.127 1.00 49.11  ? 45  LEU A CG  1 
ATOM   364  C CD1 . LEU A 1 45  ? -18.304 -19.009 -39.657 1.00 50.96  ? 45  LEU A CD1 1 
ATOM   365  C CD2 . LEU A 1 45  ? -15.948 -18.176 -39.715 1.00 48.32  ? 45  LEU A CD2 1 
ATOM   366  N N   . ASP A 1 46  ? -17.039 -22.580 -37.959 1.00 46.70  ? 46  ASP A N   1 
ATOM   367  C CA  . ASP A 1 46  ? -16.436 -23.823 -38.414 1.00 46.61  ? 46  ASP A CA  1 
ATOM   368  C C   . ASP A 1 46  ? -16.916 -24.068 -39.845 1.00 45.64  ? 46  ASP A C   1 
ATOM   369  O O   . ASP A 1 46  ? -18.058 -24.474 -40.050 1.00 45.35  ? 46  ASP A O   1 
ATOM   370  C CB  . ASP A 1 46  ? -16.808 -24.967 -37.462 1.00 48.46  ? 46  ASP A CB  1 
ATOM   371  C CG  . ASP A 1 46  ? -16.343 -26.358 -37.868 1.00 52.00  ? 46  ASP A CG  1 
ATOM   372  O OD1 . ASP A 1 46  ? -15.896 -26.520 -39.026 1.00 53.21  ? 46  ASP A OD1 1 
ATOM   373  O OD2 . ASP A 1 46  ? -16.438 -27.286 -37.015 1.00 55.13  ? 46  ASP A OD2 1 
ATOM   374  N N   . SER A 1 47  ? -16.027 -23.808 -40.815 1.00 44.49  ? 47  SER A N   1 
ATOM   375  C CA  . SER A 1 47  ? -16.330 -23.906 -42.239 1.00 45.28  ? 47  SER A CA  1 
ATOM   376  C C   . SER A 1 47  ? -16.885 -25.281 -42.624 1.00 46.17  ? 47  SER A C   1 
ATOM   377  O O   . SER A 1 47  ? -17.716 -25.363 -43.525 1.00 46.74  ? 47  SER A O   1 
ATOM   378  C CB  . SER A 1 47  ? -15.108 -23.575 -43.065 1.00 43.73  ? 47  SER A CB  1 
ATOM   379  O OG  . SER A 1 47  ? -14.088 -24.534 -42.860 1.00 41.44  ? 47  SER A OG  1 
ATOM   380  N N   . THR A 1 48  ? -16.438 -26.357 -41.956 1.00 45.51  ? 48  THR A N   1 
ATOM   381  C CA  . THR A 1 48  ? -16.902 -27.698 -42.288 1.00 48.52  ? 48  THR A CA  1 
ATOM   382  C C   . THR A 1 48  ? -18.426 -27.775 -42.214 1.00 51.94  ? 48  THR A C   1 
ATOM   383  O O   . THR A 1 48  ? -19.029 -28.479 -43.012 1.00 54.51  ? 48  THR A O   1 
ATOM   384  C CB  . THR A 1 48  ? -16.264 -28.784 -41.411 1.00 47.06  ? 48  THR A CB  1 
ATOM   385  O OG1 . THR A 1 48  ? -14.855 -28.816 -41.653 1.00 46.87  ? 48  THR A OG1 1 
ATOM   386  C CG2 . THR A 1 48  ? -16.800 -30.170 -41.690 1.00 47.73  ? 48  THR A CG2 1 
ATOM   387  N N   . TYR A 1 49  ? -19.041 -27.057 -41.267 1.00 54.42  ? 49  TYR A N   1 
ATOM   388  C CA  . TYR A 1 49  ? -20.493 -26.988 -41.168 1.00 57.50  ? 49  TYR A CA  1 
ATOM   389  C C   . TYR A 1 49  ? -21.038 -25.737 -41.865 1.00 55.73  ? 49  TYR A C   1 
ATOM   390  O O   . TYR A 1 49  ? -22.121 -25.777 -42.433 1.00 57.24  ? 49  TYR A O   1 
ATOM   391  C CB  . TYR A 1 49  ? -20.920 -27.054 -39.698 1.00 61.46  ? 49  TYR A CB  1 
ATOM   392  C CG  . TYR A 1 49  ? -20.728 -28.424 -39.053 1.00 67.44  ? 49  TYR A CG  1 
ATOM   393  C CD1 . TYR A 1 49  ? -21.364 -29.562 -39.547 1.00 70.45  ? 49  TYR A CD1 1 
ATOM   394  C CD2 . TYR A 1 49  ? -19.920 -28.579 -37.931 1.00 70.88  ? 49  TYR A CD2 1 
ATOM   395  C CE1 . TYR A 1 49  ? -21.193 -30.806 -38.955 1.00 72.49  ? 49  TYR A CE1 1 
ATOM   396  C CE2 . TYR A 1 49  ? -19.744 -29.815 -37.328 1.00 72.01  ? 49  TYR A CE2 1 
ATOM   397  C CZ  . TYR A 1 49  ? -20.379 -30.934 -37.839 1.00 73.05  ? 49  TYR A CZ  1 
ATOM   398  O OH  . TYR A 1 49  ? -20.180 -32.139 -37.218 1.00 74.88  ? 49  TYR A OH  1 
ATOM   399  N N   . HIS A 1 50  ? -20.285 -24.634 -41.853 1.00 53.00  ? 50  HIS A N   1 
ATOM   400  C CA  . HIS A 1 50  ? -20.834 -23.339 -42.216 1.00 52.89  ? 50  HIS A CA  1 
ATOM   401  C C   . HIS A 1 50  ? -20.387 -22.871 -43.605 1.00 55.17  ? 50  HIS A C   1 
ATOM   402  O O   . HIS A 1 50  ? -20.461 -21.685 -43.902 1.00 55.75  ? 50  HIS A O   1 
ATOM   403  C CB  . HIS A 1 50  ? -20.430 -22.321 -41.148 1.00 50.43  ? 50  HIS A CB  1 
ATOM   404  C CG  . HIS A 1 50  ? -20.807 -22.710 -39.755 1.00 49.03  ? 50  HIS A CG  1 
ATOM   405  N ND1 . HIS A 1 50  ? -19.962 -22.573 -38.675 1.00 45.90  ? 50  HIS A ND1 1 
ATOM   406  C CD2 . HIS A 1 50  ? -21.961 -23.183 -39.266 1.00 49.29  ? 50  HIS A CD2 1 
ATOM   407  C CE1 . HIS A 1 50  ? -20.598 -22.962 -37.582 1.00 46.24  ? 50  HIS A CE1 1 
ATOM   408  N NE2 . HIS A 1 50  ? -21.814 -23.337 -37.918 1.00 47.27  ? 50  HIS A NE2 1 
ATOM   409  N N   . HIS A 1 51  ? -19.951 -23.791 -44.470 1.00 58.01  ? 51  HIS A N   1 
ATOM   410  C CA  . HIS A 1 51  ? -19.361 -23.417 -45.751 1.00 58.85  ? 51  HIS A CA  1 
ATOM   411  C C   . HIS A 1 51  ? -20.371 -22.612 -46.561 1.00 59.08  ? 51  HIS A C   1 
ATOM   412  O O   . HIS A 1 51  ? -20.041 -21.553 -47.096 1.00 57.91  ? 51  HIS A O   1 
ATOM   413  C CB  . HIS A 1 51  ? -18.879 -24.646 -46.540 1.00 60.46  ? 51  HIS A CB  1 
ATOM   414  C CG  . HIS A 1 51  ? -19.901 -25.732 -46.650 1.00 64.13  ? 51  HIS A CG  1 
ATOM   415  N ND1 . HIS A 1 51  ? -20.854 -25.744 -47.648 1.00 68.74  ? 51  HIS A ND1 1 
ATOM   416  C CD2 . HIS A 1 51  ? -20.183 -26.779 -45.856 1.00 64.36  ? 51  HIS A CD2 1 
ATOM   417  C CE1 . HIS A 1 51  ? -21.658 -26.788 -47.475 1.00 69.21  ? 51  HIS A CE1 1 
ATOM   418  N NE2 . HIS A 1 51  ? -21.262 -27.440 -46.399 1.00 66.55  ? 51  HIS A NE2 1 
ATOM   419  N N   . ALA A 1 52  ? -21.616 -23.104 -46.596 1.00 60.29  ? 52  ALA A N   1 
ATOM   420  C CA  . ALA A 1 52  ? -22.652 -22.546 -47.453 1.00 63.38  ? 52  ALA A CA  1 
ATOM   421  C C   . ALA A 1 52  ? -22.930 -21.080 -47.097 1.00 64.47  ? 52  ALA A C   1 
ATOM   422  O O   . ALA A 1 52  ? -23.573 -20.365 -47.862 1.00 63.78  ? 52  ALA A O   1 
ATOM   423  C CB  . ALA A 1 52  ? -23.898 -23.394 -47.357 1.00 64.34  ? 52  ALA A CB  1 
ATOM   424  N N   . ALA A 1 53  ? -22.428 -20.641 -45.933 1.00 64.15  ? 53  ALA A N   1 
ATOM   425  C CA  . ALA A 1 53  ? -22.644 -19.300 -45.427 1.00 63.97  ? 53  ALA A CA  1 
ATOM   426  C C   . ALA A 1 53  ? -21.405 -18.434 -45.631 1.00 65.84  ? 53  ALA A C   1 
ATOM   427  O O   . ALA A 1 53  ? -21.441 -17.241 -45.338 1.00 70.44  ? 53  ALA A O   1 
ATOM   428  C CB  . ALA A 1 53  ? -23.014 -19.383 -43.969 1.00 61.43  ? 53  ALA A CB  1 
ATOM   429  N N   . LEU A 1 54  ? -20.313 -19.027 -46.126 1.00 65.54  ? 54  LEU A N   1 
ATOM   430  C CA  . LEU A 1 54  ? -19.056 -18.308 -46.252 1.00 65.90  ? 54  LEU A CA  1 
ATOM   431  C C   . LEU A 1 54  ? -18.833 -17.879 -47.696 1.00 71.48  ? 54  LEU A C   1 
ATOM   432  O O   . LEU A 1 54  ? -17.967 -17.042 -47.932 1.00 70.14  ? 54  LEU A O   1 
ATOM   433  C CB  . LEU A 1 54  ? -17.908 -19.198 -45.767 1.00 64.41  ? 54  LEU A CB  1 
ATOM   434  C CG  . LEU A 1 54  ? -17.888 -19.508 -44.266 1.00 62.26  ? 54  LEU A CG  1 
ATOM   435  C CD1 . LEU A 1 54  ? -16.621 -20.252 -43.874 1.00 58.59  ? 54  LEU A CD1 1 
ATOM   436  C CD2 . LEU A 1 54  ? -18.025 -18.242 -43.434 1.00 62.91  ? 54  LEU A CD2 1 
ATOM   437  N N   . ARG A 1 55  ? -19.635 -18.427 -48.628 1.00 78.20  ? 55  ARG A N   1 
ATOM   438  C CA  . ARG A 1 55  ? -19.467 -18.232 -50.065 1.00 83.45  ? 55  ARG A CA  1 
ATOM   439  C C   . ARG A 1 55  ? -19.270 -16.759 -50.404 1.00 87.01  ? 55  ARG A C   1 
ATOM   440  O O   . ARG A 1 55  ? -18.530 -16.431 -51.330 1.00 90.93  ? 55  ARG A O   1 
ATOM   441  C CB  . ARG A 1 55  ? -20.699 -18.667 -50.876 1.00 89.73  ? 55  ARG A CB  1 
ATOM   442  C CG  . ARG A 1 55  ? -21.055 -20.147 -50.834 1.00 90.85  ? 55  ARG A CG  1 
ATOM   443  C CD  . ARG A 1 55  ? -22.323 -20.438 -51.629 1.00 94.33  ? 55  ARG A CD  1 
ATOM   444  N NE  . ARG A 1 55  ? -23.002 -21.671 -51.227 1.00 99.15  ? 55  ARG A NE  1 
ATOM   445  C CZ  . ARG A 1 55  ? -22.461 -22.895 -51.228 1.00 100.48 ? 55  ARG A CZ  1 
ATOM   446  N NH1 . ARG A 1 55  ? -21.269 -23.102 -51.763 1.00 97.59  ? 55  ARG A NH1 1 
ATOM   447  N NH2 . ARG A 1 55  ? -23.122 -23.919 -50.705 1.00 99.13  ? 55  ARG A NH2 1 
ATOM   448  N N   . GLN A 1 56  ? -19.987 -15.883 -49.690 1.00 89.87  ? 56  GLN A N   1 
ATOM   449  C CA  . GLN A 1 56  ? -20.083 -14.480 -50.071 1.00 92.75  ? 56  GLN A CA  1 
ATOM   450  C C   . GLN A 1 56  ? -19.375 -13.600 -49.040 1.00 87.20  ? 56  GLN A C   1 
ATOM   451  O O   . GLN A 1 56  ? -19.288 -12.393 -49.235 1.00 91.51  ? 56  GLN A O   1 
ATOM   452  C CB  . GLN A 1 56  ? -21.541 -14.065 -50.344 1.00 98.00  ? 56  GLN A CB  1 
ATOM   453  C CG  . GLN A 1 56  ? -22.623 -15.008 -49.809 1.00 100.00 ? 56  GLN A CG  1 
ATOM   454  C CD  . GLN A 1 56  ? -22.875 -14.887 -48.323 1.00 96.22  ? 56  GLN A CD  1 
ATOM   455  O OE1 . GLN A 1 56  ? -23.614 -14.014 -47.873 1.00 96.59  ? 56  GLN A OE1 1 
ATOM   456  N NE2 . GLN A 1 56  ? -22.301 -15.797 -47.551 1.00 90.23  ? 56  GLN A NE2 1 
ATOM   457  N N   . LEU A 1 57  ? -18.810 -14.209 -47.989 1.00 80.56  ? 57  LEU A N   1 
ATOM   458  C CA  . LEU A 1 57  ? -18.119 -13.470 -46.943 1.00 73.57  ? 57  LEU A CA  1 
ATOM   459  C C   . LEU A 1 57  ? -16.690 -13.184 -47.386 1.00 71.39  ? 57  LEU A C   1 
ATOM   460  O O   . LEU A 1 57  ? -16.071 -14.019 -48.039 1.00 70.72  ? 57  LEU A O   1 
ATOM   461  C CB  . LEU A 1 57  ? -18.085 -14.316 -45.669 1.00 69.39  ? 57  LEU A CB  1 
ATOM   462  C CG  . LEU A 1 57  ? -18.596 -13.650 -44.396 1.00 66.32  ? 57  LEU A CG  1 
ATOM   463  C CD1 . LEU A 1 57  ? -18.043 -14.362 -43.175 1.00 62.89  ? 57  LEU A CD1 1 
ATOM   464  C CD2 . LEU A 1 57  ? -18.259 -12.171 -44.351 1.00 67.24  ? 57  LEU A CD2 1 
ATOM   465  N N   . GLU A 1 58  ? -16.159 -12.027 -46.971 1.00 70.12  ? 58  GLU A N   1 
ATOM   466  C CA  . GLU A 1 58  ? -14.774 -11.674 -47.240 1.00 67.75  ? 58  GLU A CA  1 
ATOM   467  C C   . GLU A 1 58  ? -13.849 -12.729 -46.635 1.00 59.33  ? 58  GLU A C   1 
ATOM   468  O O   . GLU A 1 58  ? -14.086 -13.217 -45.538 1.00 55.13  ? 58  GLU A O   1 
ATOM   469  C CB  . GLU A 1 58  ? -14.471 -10.274 -46.703 1.00 71.47  ? 58  GLU A CB  1 
ATOM   470  C CG  . GLU A 1 58  ? -13.068 -9.798  -47.039 1.00 76.09  ? 58  GLU A CG  1 
ATOM   471  C CD  . GLU A 1 58  ? -12.854 -8.294  -46.963 1.00 82.27  ? 58  GLU A CD  1 
ATOM   472  O OE1 . GLU A 1 58  ? -11.976 -7.868  -46.187 1.00 87.92  ? 58  GLU A OE1 1 
ATOM   473  O OE2 . GLU A 1 58  ? -13.555 -7.549  -47.683 1.00 83.22  ? 58  GLU A OE2 1 
ATOM   474  N N   . ASP A 1 59  ? -12.804 -13.091 -47.382 1.00 58.12  ? 59  ASP A N   1 
ATOM   475  C CA  . ASP A 1 59  ? -11.856 -14.123 -46.987 1.00 56.04  ? 59  ASP A CA  1 
ATOM   476  C C   . ASP A 1 59  ? -12.572 -15.422 -46.606 1.00 53.10  ? 59  ASP A C   1 
ATOM   477  O O   . ASP A 1 59  ? -11.940 -16.303 -46.024 1.00 49.73  ? 59  ASP A O   1 
ATOM   478  C CB  . ASP A 1 59  ? -10.961 -13.669 -45.826 1.00 55.68  ? 59  ASP A CB  1 
ATOM   479  C CG  . ASP A 1 59  ? -9.868  -12.680 -46.193 1.00 57.43  ? 59  ASP A CG  1 
ATOM   480  O OD1 . ASP A 1 59  ? -9.969  -12.097 -47.274 1.00 61.23  ? 59  ASP A OD1 1 
ATOM   481  O OD2 . ASP A 1 59  ? -8.915  -12.513 -45.385 1.00 57.99  ? 59  ASP A OD2 1 
ATOM   482  N N   . GLY A 1 60  ? -13.853 -15.564 -46.990 1.00 53.52  ? 60  GLY A N   1 
ATOM   483  C CA  . GLY A 1 60  ? -14.723 -16.634 -46.512 1.00 53.76  ? 60  GLY A CA  1 
ATOM   484  C C   . GLY A 1 60  ? -14.144 -18.045 -46.670 1.00 54.42  ? 60  GLY A C   1 
ATOM   485  O O   . GLY A 1 60  ? -14.518 -18.966 -45.939 1.00 51.36  ? 60  GLY A O   1 
ATOM   486  N N   . GLU A 1 61  ? -13.232 -18.210 -47.636 1.00 58.40  ? 61  GLU A N   1 
ATOM   487  C CA  . GLU A 1 61  ? -12.747 -19.519 -48.042 1.00 59.71  ? 61  GLU A CA  1 
ATOM   488  C C   . GLU A 1 61  ? -11.627 -19.999 -47.126 1.00 55.51  ? 61  GLU A C   1 
ATOM   489  O O   . GLU A 1 61  ? -11.260 -21.169 -47.201 1.00 56.30  ? 61  GLU A O   1 
ATOM   490  C CB  . GLU A 1 61  ? -12.221 -19.485 -49.480 1.00 63.95  ? 61  GLU A CB  1 
ATOM   491  C CG  . GLU A 1 61  ? -10.787 -18.967 -49.581 1.00 66.34  ? 61  GLU A CG  1 
ATOM   492  C CD  . GLU A 1 61  ? -10.612 -17.452 -49.625 1.00 69.19  ? 61  GLU A CD  1 
ATOM   493  O OE1 . GLU A 1 61  ? -9.607  -16.963 -49.052 1.00 69.41  ? 61  GLU A OE1 1 
ATOM   494  O OE2 . GLU A 1 61  ? -11.480 -16.752 -50.226 1.00 68.77  ? 61  GLU A OE2 1 
ATOM   495  N N   . ARG A 1 62  ? -11.039 -19.098 -46.329 1.00 53.48  ? 62  ARG A N   1 
ATOM   496  C CA  . ARG A 1 62  ? -9.977  -19.491 -45.412 1.00 53.27  ? 62  ARG A CA  1 
ATOM   497  C C   . ARG A 1 62  ? -10.447 -19.392 -43.960 1.00 48.25  ? 62  ARG A C   1 
ATOM   498  O O   . ARG A 1 62  ? -9.712  -19.760 -43.043 1.00 43.64  ? 62  ARG A O   1 
ATOM   499  C CB  . ARG A 1 62  ? -8.712  -18.651 -45.625 1.00 55.31  ? 62  ARG A CB  1 
ATOM   500  C CG  . ARG A 1 62  ? -8.882  -17.178 -45.292 1.00 58.86  ? 62  ARG A CG  1 
ATOM   501  C CD  . ARG A 1 62  ? -7.627  -16.397 -45.597 1.00 63.38  ? 62  ARG A CD  1 
ATOM   502  N NE  . ARG A 1 62  ? -6.676  -16.407 -44.501 1.00 65.14  ? 62  ARG A NE  1 
ATOM   503  C CZ  . ARG A 1 62  ? -5.451  -15.887 -44.564 1.00 70.88  ? 62  ARG A CZ  1 
ATOM   504  N NH1 . ARG A 1 62  ? -4.906  -15.563 -45.726 1.00 70.07  ? 62  ARG A NH1 1 
ATOM   505  N NH2 . ARG A 1 62  ? -4.753  -15.724 -43.454 1.00 75.23  ? 62  ARG A NH2 1 
ATOM   506  N N   . ARG A 1 63  ? -11.679 -18.923 -43.753 1.00 47.71  ? 63  ARG A N   1 
ATOM   507  C CA  . ARG A 1 63  ? -12.129 -18.577 -42.415 1.00 47.74  ? 63  ARG A CA  1 
ATOM   508  C C   . ARG A 1 63  ? -12.835 -19.758 -41.758 1.00 46.15  ? 63  ARG A C   1 
ATOM   509  O O   . ARG A 1 63  ? -13.311 -20.666 -42.436 1.00 49.37  ? 63  ARG A O   1 
ATOM   510  C CB  . ARG A 1 63  ? -13.023 -17.341 -42.476 1.00 47.90  ? 63  ARG A CB  1 
ATOM   511  C CG  . ARG A 1 63  ? -12.245 -16.088 -42.835 1.00 47.70  ? 63  ARG A CG  1 
ATOM   512  C CD  . ARG A 1 63  ? -13.157 -14.924 -43.111 1.00 49.47  ? 63  ARG A CD  1 
ATOM   513  N NE  . ARG A 1 63  ? -13.704 -14.390 -41.882 1.00 48.65  ? 63  ARG A NE  1 
ATOM   514  C CZ  . ARG A 1 63  ? -14.401 -13.266 -41.814 1.00 49.76  ? 63  ARG A CZ  1 
ATOM   515  N NH1 . ARG A 1 63  ? -14.754 -12.622 -42.915 1.00 50.63  ? 63  ARG A NH1 1 
ATOM   516  N NH2 . ARG A 1 63  ? -14.758 -12.804 -40.632 1.00 50.17  ? 63  ARG A NH2 1 
ATOM   517  N N   . GLY A 1 64  ? -12.849 -19.743 -40.426 1.00 42.81  ? 64  GLY A N   1 
ATOM   518  C CA  . GLY A 1 64  ? -13.551 -20.761 -39.672 1.00 43.31  ? 64  GLY A CA  1 
ATOM   519  C C   . GLY A 1 64  ? -12.866 -22.121 -39.754 1.00 41.22  ? 64  GLY A C   1 
ATOM   520  O O   . GLY A 1 64  ? -13.489 -23.121 -40.120 1.00 39.27  ? 64  GLY A O   1 
ATOM   521  N N   . ARG A 1 65  ? -11.588 -22.129 -39.373 1.00 40.73  ? 65  ARG A N   1 
ATOM   522  C CA  . ARG A 1 65  ? -10.780 -23.335 -39.335 1.00 41.46  ? 65  ARG A CA  1 
ATOM   523  C C   . ARG A 1 65  ? -10.104 -23.424 -37.970 1.00 41.40  ? 65  ARG A C   1 
ATOM   524  O O   . ARG A 1 65  ? -8.871  -23.463 -37.892 1.00 43.46  ? 65  ARG A O   1 
ATOM   525  C CB  . ARG A 1 65  ? -9.726  -23.312 -40.449 1.00 42.57  ? 65  ARG A CB  1 
ATOM   526  C CG  . ARG A 1 65  ? -10.291 -23.314 -41.862 1.00 46.80  ? 65  ARG A CG  1 
ATOM   527  C CD  . ARG A 1 65  ? -11.004 -24.600 -42.259 1.00 51.21  ? 65  ARG A CD  1 
ATOM   528  N NE  . ARG A 1 65  ? -10.181 -25.796 -42.085 1.00 56.73  ? 65  ARG A NE  1 
ATOM   529  C CZ  . ARG A 1 65  ? -9.066  -26.086 -42.771 1.00 63.74  ? 65  ARG A CZ  1 
ATOM   530  N NH1 . ARG A 1 65  ? -8.775  -25.467 -43.911 1.00 68.12  ? 65  ARG A NH1 1 
ATOM   531  N NH2 . ARG A 1 65  ? -8.265  -27.046 -42.332 1.00 59.61  ? 65  ARG A NH2 1 
ATOM   532  N N   . PRO A 1 66  ? -10.881 -23.451 -36.860 1.00 39.81  ? 66  PRO A N   1 
ATOM   533  C CA  . PRO A 1 66  ? -10.320 -23.606 -35.513 1.00 39.21  ? 66  PRO A CA  1 
ATOM   534  C C   . PRO A 1 66  ? -9.549  -24.908 -35.284 1.00 39.58  ? 66  PRO A C   1 
ATOM   535  O O   . PRO A 1 66  ? -8.692  -24.976 -34.406 1.00 38.05  ? 66  PRO A O   1 
ATOM   536  C CB  . PRO A 1 66  ? -11.569 -23.586 -34.617 1.00 40.00  ? 66  PRO A CB  1 
ATOM   537  C CG  . PRO A 1 66  ? -12.689 -24.035 -35.524 1.00 40.06  ? 66  PRO A CG  1 
ATOM   538  C CD  . PRO A 1 66  ? -12.349 -23.393 -36.849 1.00 40.47  ? 66  PRO A CD  1 
ATOM   539  N N   . ASP A 1 67  ? -9.885  -25.940 -36.072 1.00 40.79  ? 67  ASP A N   1 
ATOM   540  C CA  . ASP A 1 67  ? -9.120  -27.175 -36.142 1.00 39.25  ? 67  ASP A CA  1 
ATOM   541  C C   . ASP A 1 67  ? -7.624  -26.900 -36.187 1.00 36.98  ? 67  ASP A C   1 
ATOM   542  O O   . ASP A 1 67  ? -6.892  -27.556 -35.455 1.00 39.35  ? 67  ASP A O   1 
ATOM   543  C CB  . ASP A 1 67  ? -9.485  -28.043 -37.350 1.00 39.32  ? 67  ASP A CB  1 
ATOM   544  C CG  . ASP A 1 67  ? -9.626  -27.259 -38.638 1.00 38.40  ? 67  ASP A CG  1 
ATOM   545  O OD1 . ASP A 1 67  ? -10.600 -26.504 -38.736 1.00 37.99  ? 67  ASP A OD1 1 
ATOM   546  O OD2 . ASP A 1 67  ? -8.759  -27.405 -39.514 1.00 38.63  ? 67  ASP A OD2 1 
ATOM   547  N N   . ILE A 1 68  ? -7.173  -25.971 -37.039 1.00 35.38  ? 68  ILE A N   1 
ATOM   548  C CA  . ILE A 1 68  ? -5.738  -25.732 -37.191 1.00 34.76  ? 68  ILE A CA  1 
ATOM   549  C C   . ILE A 1 68  ? -5.132  -25.383 -35.833 1.00 32.37  ? 68  ILE A C   1 
ATOM   550  O O   . ILE A 1 68  ? -4.085  -25.908 -35.472 1.00 30.63  ? 68  ILE A O   1 
ATOM   551  C CB  . ILE A 1 68  ? -5.436  -24.673 -38.277 1.00 35.39  ? 68  ILE A CB  1 
ATOM   552  C CG1 . ILE A 1 68  ? -5.572  -25.285 -39.678 1.00 36.58  ? 68  ILE A CG1 1 
ATOM   553  C CG2 . ILE A 1 68  ? -4.061  -24.041 -38.077 1.00 35.10  ? 68  ILE A CG2 1 
ATOM   554  C CD1 . ILE A 1 68  ? -5.682  -24.259 -40.800 1.00 37.87  ? 68  ILE A CD1 1 
ATOM   555  N N   . VAL A 1 69  ? -5.839  -24.547 -35.068 1.00 32.60  ? 69  VAL A N   1 
ATOM   556  C CA  . VAL A 1 69  ? -5.412  -24.144 -33.737 1.00 33.16  ? 69  VAL A CA  1 
ATOM   557  C C   . VAL A 1 69  ? -5.375  -25.350 -32.800 1.00 34.04  ? 69  VAL A C   1 
ATOM   558  O O   . VAL A 1 69  ? -4.367  -25.607 -32.151 1.00 33.65  ? 69  VAL A O   1 
ATOM   559  C CB  . VAL A 1 69  ? -6.330  -23.035 -33.206 1.00 33.17  ? 69  VAL A CB  1 
ATOM   560  C CG1 . VAL A 1 69  ? -5.993  -22.655 -31.784 1.00 33.46  ? 69  VAL A CG1 1 
ATOM   561  C CG2 . VAL A 1 69  ? -6.267  -21.811 -34.112 1.00 35.34  ? 69  VAL A CG2 1 
ATOM   562  N N   . HIS A 1 70  ? -6.477  -26.096 -32.748 1.00 35.24  ? 70  HIS A N   1 
ATOM   563  C CA  . HIS A 1 70  ? -6.573  -27.268 -31.902 1.00 36.92  ? 70  HIS A CA  1 
ATOM   564  C C   . HIS A 1 70  ? -5.315  -28.140 -32.014 1.00 39.11  ? 70  HIS A C   1 
ATOM   565  O O   . HIS A 1 70  ? -4.668  -28.466 -31.019 1.00 41.22  ? 70  HIS A O   1 
ATOM   566  C CB  . HIS A 1 70  ? -7.848  -28.023 -32.268 1.00 36.94  ? 70  HIS A CB  1 
ATOM   567  C CG  . HIS A 1 70  ? -8.114  -29.157 -31.359 1.00 37.99  ? 70  HIS A CG  1 
ATOM   568  N ND1 . HIS A 1 70  ? -8.586  -30.360 -31.823 1.00 39.68  ? 70  HIS A ND1 1 
ATOM   569  C CD2 . HIS A 1 70  ? -8.015  -29.275 -30.038 1.00 39.27  ? 70  HIS A CD2 1 
ATOM   570  C CE1 . HIS A 1 70  ? -8.750  -31.181 -30.797 1.00 41.67  ? 70  HIS A CE1 1 
ATOM   571  N NE2 . HIS A 1 70  ? -8.408  -30.539 -29.704 1.00 41.72  ? 70  HIS A NE2 1 
ATOM   572  N N   . ILE A 1 71  ? -4.964  -28.503 -33.247 1.00 39.53  ? 71  ILE A N   1 
ATOM   573  C CA  . ILE A 1 71  ? -3.888  -29.435 -33.536 1.00 40.08  ? 71  ILE A CA  1 
ATOM   574  C C   . ILE A 1 71  ? -2.528  -28.828 -33.191 1.00 40.46  ? 71  ILE A C   1 
ATOM   575  O O   . ILE A 1 71  ? -1.600  -29.546 -32.820 1.00 42.80  ? 71  ILE A O   1 
ATOM   576  C CB  . ILE A 1 71  ? -3.971  -29.825 -35.020 1.00 42.98  ? 71  ILE A CB  1 
ATOM   577  C CG1 . ILE A 1 71  ? -5.278  -30.570 -35.314 1.00 47.42  ? 71  ILE A CG1 1 
ATOM   578  C CG2 . ILE A 1 71  ? -2.750  -30.622 -35.440 1.00 43.94  ? 71  ILE A CG2 1 
ATOM   579  C CD1 . ILE A 1 71  ? -5.856  -30.313 -36.714 1.00 49.97  ? 71  ILE A CD1 1 
ATOM   580  N N   . CYS A 1 72  ? -2.396  -27.509 -33.366 1.00 37.23  ? 72  CYS A N   1 
ATOM   581  C CA  . CYS A 1 72  ? -1.182  -26.801 -33.019 1.00 34.37  ? 72  CYS A CA  1 
ATOM   582  C C   . CYS A 1 72  ? -0.995  -26.723 -31.511 1.00 33.18  ? 72  CYS A C   1 
ATOM   583  O O   . CYS A 1 72  ? 0.125   -26.671 -31.025 1.00 31.97  ? 72  CYS A O   1 
ATOM   584  C CB  . CYS A 1 72  ? -1.243  -25.384 -33.549 1.00 35.85  ? 72  CYS A CB  1 
ATOM   585  S SG  . CYS A 1 72  ? -0.856  -25.295 -35.308 1.00 39.62  ? 72  CYS A SG  1 
ATOM   586  N N   . LEU A 1 73  ? -2.099  -26.652 -30.770 1.00 34.03  ? 73  LEU A N   1 
ATOM   587  C CA  . LEU A 1 73  ? -2.013  -26.505 -29.327 1.00 35.57  ? 73  LEU A CA  1 
ATOM   588  C C   . LEU A 1 73  ? -1.752  -27.879 -28.720 1.00 38.49  ? 73  LEU A C   1 
ATOM   589  O O   . LEU A 1 73  ? -0.841  -28.020 -27.916 1.00 41.95  ? 73  LEU A O   1 
ATOM   590  C CB  . LEU A 1 73  ? -3.282  -25.833 -28.777 1.00 34.98  ? 73  LEU A CB  1 
ATOM   591  C CG  . LEU A 1 73  ? -3.487  -24.353 -29.157 1.00 34.62  ? 73  LEU A CG  1 
ATOM   592  C CD1 . LEU A 1 73  ? -4.748  -23.785 -28.505 1.00 34.70  ? 73  LEU A CD1 1 
ATOM   593  C CD2 . LEU A 1 73  ? -2.292  -23.466 -28.809 1.00 33.49  ? 73  LEU A CD2 1 
ATOM   594  N N   . LEU A 1 74  ? -2.479  -28.912 -29.161 1.00 38.48  ? 74  LEU A N   1 
ATOM   595  C CA  . LEU A 1 74  ? -2.206  -30.260 -28.691 1.00 39.51  ? 74  LEU A CA  1 
ATOM   596  C C   . LEU A 1 74  ? -0.748  -30.615 -28.960 1.00 41.19  ? 74  LEU A C   1 
ATOM   597  O O   . LEU A 1 74  ? -0.156  -31.439 -28.259 1.00 45.31  ? 74  LEU A O   1 
ATOM   598  C CB  . LEU A 1 74  ? -3.102  -31.260 -29.424 1.00 38.80  ? 74  LEU A CB  1 
ATOM   599  C CG  . LEU A 1 74  ? -4.584  -31.251 -29.078 1.00 37.53  ? 74  LEU A CG  1 
ATOM   600  C CD1 . LEU A 1 74  ? -5.328  -32.181 -30.021 1.00 37.06  ? 74  LEU A CD1 1 
ATOM   601  C CD2 . LEU A 1 74  ? -4.808  -31.677 -27.639 1.00 38.73  ? 74  LEU A CD2 1 
ATOM   602  N N   . ASN A 1 75  ? -0.201  -30.059 -30.039 1.00 40.13  ? 75  ASN A N   1 
ATOM   603  C CA  . ASN A 1 75  ? 1.182   -30.320 -30.376 1.00 41.75  ? 75  ASN A CA  1 
ATOM   604  C C   . ASN A 1 75  ? 2.081   -29.589 -29.397 1.00 43.02  ? 75  ASN A C   1 
ATOM   605  O O   . ASN A 1 75  ? 2.973   -30.189 -28.806 1.00 47.35  ? 75  ASN A O   1 
ATOM   606  C CB  . ASN A 1 75  ? 1.497   -29.957 -31.823 1.00 40.81  ? 75  ASN A CB  1 
ATOM   607  C CG  . ASN A 1 75  ? 1.268   -31.129 -32.751 1.00 41.55  ? 75  ASN A CG  1 
ATOM   608  O OD1 . ASN A 1 75  ? 1.253   -32.293 -32.331 1.00 38.58  ? 75  ASN A OD1 1 
ATOM   609  N ND2 . ASN A 1 75  ? 1.117   -30.819 -34.026 1.00 43.32  ? 75  ASN A ND2 1 
ATOM   610  N N   . ALA A 1 76  ? 1.817   -28.297 -29.227 1.00 42.12  ? 76  ALA A N   1 
ATOM   611  C CA  . ALA A 1 76  ? 2.669   -27.455 -28.408 1.00 42.21  ? 76  ALA A CA  1 
ATOM   612  C C   . ALA A 1 76  ? 2.628   -27.883 -26.938 1.00 41.23  ? 76  ALA A C   1 
ATOM   613  O O   . ALA A 1 76  ? 3.672   -28.108 -26.335 1.00 41.87  ? 76  ALA A O   1 
ATOM   614  C CB  . ALA A 1 76  ? 2.247   -26.025 -28.578 1.00 42.04  ? 76  ALA A CB  1 
ATOM   615  N N   . LEU A 1 77  ? 1.418   -28.028 -26.387 1.00 39.31  ? 77  LEU A N   1 
ATOM   616  C CA  . LEU A 1 77  ? 1.205   -28.116 -24.951 1.00 38.90  ? 77  LEU A CA  1 
ATOM   617  C C   . LEU A 1 77  ? 1.618   -29.474 -24.418 1.00 40.07  ? 77  LEU A C   1 
ATOM   618  O O   . LEU A 1 77  ? 2.027   -29.567 -23.270 1.00 44.24  ? 77  LEU A O   1 
ATOM   619  C CB  . LEU A 1 77  ? -0.274  -27.893 -24.639 1.00 38.23  ? 77  LEU A CB  1 
ATOM   620  C CG  . LEU A 1 77  ? -0.782  -26.469 -24.833 1.00 37.04  ? 77  LEU A CG  1 
ATOM   621  C CD1 . LEU A 1 77  ? -2.289  -26.421 -24.727 1.00 37.31  ? 77  LEU A CD1 1 
ATOM   622  C CD2 . LEU A 1 77  ? -0.175  -25.552 -23.806 1.00 38.94  ? 77  LEU A CD2 1 
ATOM   623  N N   . ASP A 1 78  ? 1.475   -30.524 -25.220 1.00 38.84  ? 78  ASP A N   1 
ATOM   624  C CA  . ASP A 1 78  ? 1.921   -31.833 -24.790 1.00 40.60  ? 78  ASP A CA  1 
ATOM   625  C C   . ASP A 1 78  ? 3.379   -32.053 -25.170 1.00 41.21  ? 78  ASP A C   1 
ATOM   626  O O   . ASP A 1 78  ? 3.927   -33.128 -24.937 1.00 43.76  ? 78  ASP A O   1 
ATOM   627  C CB  . ASP A 1 78  ? 1.003   -32.912 -25.347 1.00 41.36  ? 78  ASP A CB  1 
ATOM   628  C CG  . ASP A 1 78  ? -0.349  -32.854 -24.672 1.00 43.70  ? 78  ASP A CG  1 
ATOM   629  O OD1 . ASP A 1 78  ? -0.452  -33.391 -23.515 1.00 45.35  ? 78  ASP A OD1 1 
ATOM   630  O OD2 . ASP A 1 78  ? -1.264  -32.218 -25.277 1.00 42.99  ? 78  ASP A OD2 1 
ATOM   631  N N   . SER A 1 79  ? 4.020   -31.040 -25.750 1.00 41.28  ? 79  SER A N   1 
ATOM   632  C CA  . SER A 1 79  ? 5.418   -31.179 -26.124 1.00 42.44  ? 79  SER A CA  1 
ATOM   633  C C   . SER A 1 79  ? 6.249   -31.458 -24.876 1.00 43.90  ? 79  SER A C   1 
ATOM   634  O O   . SER A 1 79  ? 5.871   -31.078 -23.771 1.00 44.42  ? 79  SER A O   1 
ATOM   635  C CB  . SER A 1 79  ? 5.913   -29.959 -26.850 1.00 41.25  ? 79  SER A CB  1 
ATOM   636  O OG  . SER A 1 79  ? 5.867   -28.834 -25.998 1.00 41.82  ? 79  SER A OG  1 
ATOM   637  N N   . ILE A 1 80  ? 7.381   -32.126 -25.067 1.00 44.11  ? 80  ILE A N   1 
ATOM   638  C CA  . ILE A 1 80  ? 8.348   -32.244 -23.996 1.00 47.51  ? 80  ILE A CA  1 
ATOM   639  C C   . ILE A 1 80  ? 8.809   -30.846 -23.572 1.00 49.67  ? 80  ILE A C   1 
ATOM   640  O O   . ILE A 1 80  ? 9.054   -30.596 -22.385 1.00 52.18  ? 80  ILE A O   1 
ATOM   641  C CB  . ILE A 1 80  ? 9.537   -33.115 -24.438 1.00 48.78  ? 80  ILE A CB  1 
ATOM   642  C CG1 . ILE A 1 80  ? 9.100   -34.557 -24.713 1.00 49.03  ? 80  ILE A CG1 1 
ATOM   643  C CG2 . ILE A 1 80  ? 10.655  -33.037 -23.410 1.00 50.92  ? 80  ILE A CG2 1 
ATOM   644  C CD1 . ILE A 1 80  ? 10.196  -35.453 -25.247 1.00 50.47  ? 80  ILE A CD1 1 
ATOM   645  N N   . LEU A 1 81  ? 8.944   -29.945 -24.556 1.00 48.90  ? 81  LEU A N   1 
ATOM   646  C CA  . LEU A 1 81  ? 9.466   -28.605 -24.340 1.00 48.81  ? 81  LEU A CA  1 
ATOM   647  C C   . LEU A 1 81  ? 8.630   -27.881 -23.291 1.00 49.84  ? 81  LEU A C   1 
ATOM   648  O O   . LEU A 1 81  ? 9.178   -27.124 -22.483 1.00 50.91  ? 81  LEU A O   1 
ATOM   649  C CB  . LEU A 1 81  ? 9.430   -27.843 -25.665 1.00 47.09  ? 81  LEU A CB  1 
ATOM   650  C CG  . LEU A 1 81  ? 10.211  -26.531 -25.691 1.00 48.53  ? 81  LEU A CG  1 
ATOM   651  C CD1 . LEU A 1 81  ? 11.712  -26.765 -25.828 1.00 49.55  ? 81  LEU A CD1 1 
ATOM   652  C CD2 . LEU A 1 81  ? 9.721   -25.637 -26.821 1.00 48.10  ? 81  LEU A CD2 1 
ATOM   653  N N   . ASN A 1 82  ? 7.306   -28.116 -23.340 1.00 48.21  ? 82  ASN A N   1 
ATOM   654  C CA  . ASN A 1 82  ? 6.372   -27.465 -22.440 1.00 48.08  ? 82  ASN A CA  1 
ATOM   655  C C   . ASN A 1 82  ? 6.497   -28.094 -21.060 1.00 52.19  ? 82  ASN A C   1 
ATOM   656  O O   . ASN A 1 82  ? 6.442   -27.409 -20.040 1.00 58.04  ? 82  ASN A O   1 
ATOM   657  C CB  . ASN A 1 82  ? 4.929   -27.563 -22.933 1.00 44.55  ? 82  ASN A CB  1 
ATOM   658  C CG  . ASN A 1 82  ? 3.985   -26.694 -22.133 1.00 43.13  ? 82  ASN A CG  1 
ATOM   659  O OD1 . ASN A 1 82  ? 4.263   -25.523 -21.905 1.00 46.33  ? 82  ASN A OD1 1 
ATOM   660  N ND2 . ASN A 1 82  ? 2.868   -27.240 -21.703 1.00 41.22  ? 82  ASN A ND2 1 
ATOM   661  N N   . LYS A 1 83  ? 6.686   -29.410 -21.047 1.00 52.13  ? 83  LYS A N   1 
ATOM   662  C CA  . LYS A 1 83  ? 6.766   -30.151 -19.806 1.00 53.64  ? 83  LYS A CA  1 
ATOM   663  C C   . LYS A 1 83  ? 7.983   -29.658 -19.028 1.00 56.88  ? 83  LYS A C   1 
ATOM   664  O O   . LYS A 1 83  ? 7.917   -29.557 -17.807 1.00 61.11  ? 83  LYS A O   1 
ATOM   665  C CB  . LYS A 1 83  ? 6.762   -31.656 -20.111 1.00 53.10  ? 83  LYS A CB  1 
ATOM   666  C CG  . LYS A 1 83  ? 5.523   -32.164 -20.850 1.00 50.11  ? 83  LYS A CG  1 
ATOM   667  C CD  . LYS A 1 83  ? 5.311   -33.666 -20.745 1.00 51.03  ? 83  LYS A CD  1 
ATOM   668  C CE  . LYS A 1 83  ? 4.106   -34.215 -21.488 1.00 48.54  ? 83  LYS A CE  1 
ATOM   669  N NZ  . LYS A 1 83  ? 2.876   -33.423 -21.246 1.00 47.25  ? 83  LYS A NZ  1 
ATOM   670  N N   . GLU A 1 84  ? 9.056   -29.283 -19.745 1.00 57.17  ? 84  GLU A N   1 
ATOM   671  C CA  . GLU A 1 84  ? 10.302  -28.803 -19.147 1.00 59.11  ? 84  GLU A CA  1 
ATOM   672  C C   . GLU A 1 84  ? 10.252  -27.314 -18.798 1.00 57.33  ? 84  GLU A C   1 
ATOM   673  O O   . GLU A 1 84  ? 11.263  -26.738 -18.414 1.00 58.90  ? 84  GLU A O   1 
ATOM   674  C CB  . GLU A 1 84  ? 11.464  -28.955 -20.132 1.00 60.70  ? 84  GLU A CB  1 
ATOM   675  C CG  . GLU A 1 84  ? 11.766  -30.380 -20.531 1.00 61.95  ? 84  GLU A CG  1 
ATOM   676  C CD  . GLU A 1 84  ? 12.581  -31.144 -19.509 1.00 66.43  ? 84  GLU A CD  1 
ATOM   677  O OE1 . GLU A 1 84  ? 12.068  -32.183 -19.017 1.00 67.50  ? 84  GLU A OE1 1 
ATOM   678  O OE2 . GLU A 1 84  ? 13.730  -30.706 -19.221 1.00 69.14  ? 84  GLU A OE2 1 
ATOM   679  N N   . ASP A 1 85  ? 9.100   -26.674 -18.979 1.00 55.21  ? 85  ASP A N   1 
ATOM   680  C CA  . ASP A 1 85  ? 8.972   -25.251 -18.721 1.00 56.71  ? 85  ASP A CA  1 
ATOM   681  C C   . ASP A 1 85  ? 9.945   -24.470 -19.609 1.00 57.69  ? 85  ASP A C   1 
ATOM   682  O O   . ASP A 1 85  ? 10.819  -23.761 -19.111 1.00 59.00  ? 85  ASP A O   1 
ATOM   683  C CB  . ASP A 1 85  ? 9.155   -24.953 -17.229 1.00 59.17  ? 85  ASP A CB  1 
ATOM   684  C CG  . ASP A 1 85  ? 9.062   -23.477 -16.877 1.00 59.65  ? 85  ASP A CG  1 
ATOM   685  O OD1 . ASP A 1 85  ? 8.156   -22.806 -17.417 1.00 57.27  ? 85  ASP A OD1 1 
ATOM   686  O OD2 . ASP A 1 85  ? 9.900   -23.008 -16.068 1.00 61.33  ? 85  ASP A OD2 1 
ATOM   687  N N   . ARG A 1 86  ? 9.784   -24.613 -20.934 1.00 56.47  ? 86  ARG A N   1 
ATOM   688  C CA  . ARG A 1 86  ? 10.612  -23.908 -21.901 1.00 56.01  ? 86  ARG A CA  1 
ATOM   689  C C   . ARG A 1 86  ? 9.752   -23.431 -23.062 1.00 53.66  ? 86  ARG A C   1 
ATOM   690  O O   . ARG A 1 86  ? 10.238  -23.369 -24.183 1.00 54.10  ? 86  ARG A O   1 
ATOM   691  C CB  . ARG A 1 86  ? 11.690  -24.813 -22.509 1.00 57.83  ? 86  ARG A CB  1 
ATOM   692  C CG  . ARG A 1 86  ? 12.716  -25.360 -21.530 1.00 61.52  ? 86  ARG A CG  1 
ATOM   693  C CD  . ARG A 1 86  ? 13.743  -24.324 -21.139 1.00 64.66  ? 86  ARG A CD  1 
ATOM   694  N NE  . ARG A 1 86  ? 14.944  -24.954 -20.616 1.00 69.89  ? 86  ARG A NE  1 
ATOM   695  C CZ  . ARG A 1 86  ? 16.026  -24.305 -20.199 1.00 75.00  ? 86  ARG A CZ  1 
ATOM   696  N NH1 . ARG A 1 86  ? 16.045  -22.983 -20.163 1.00 77.66  ? 86  ARG A NH1 1 
ATOM   697  N NH2 . ARG A 1 86  ? 17.094  -24.984 -19.816 1.00 78.11  ? 86  ARG A NH2 1 
ATOM   698  N N   . LEU A 1 87  ? 8.479   -23.118 -22.799 1.00 53.30  ? 87  LEU A N   1 
ATOM   699  C CA  . LEU A 1 87  ? 7.568   -22.704 -23.851 1.00 50.87  ? 87  LEU A CA  1 
ATOM   700  C C   . LEU A 1 87  ? 6.404   -21.929 -23.252 1.00 50.72  ? 87  LEU A C   1 
ATOM   701  O O   . LEU A 1 87  ? 5.656   -22.463 -22.428 1.00 51.66  ? 87  LEU A O   1 
ATOM   702  C CB  . LEU A 1 87  ? 7.044   -23.935 -24.597 1.00 51.34  ? 87  LEU A CB  1 
ATOM   703  C CG  . LEU A 1 87  ? 5.929   -23.668 -25.616 1.00 50.69  ? 87  LEU A CG  1 
ATOM   704  C CD1 . LEU A 1 87  ? 6.490   -23.197 -26.956 1.00 49.22  ? 87  LEU A CD1 1 
ATOM   705  C CD2 . LEU A 1 87  ? 5.068   -24.909 -25.808 1.00 50.79  ? 87  LEU A CD2 1 
ATOM   706  N N   . ARG A 1 88  ? 6.237   -20.689 -23.733 1.00 49.31  ? 88  ARG A N   1 
ATOM   707  C CA  . ARG A 1 88  ? 4.962   -19.996 -23.642 1.00 46.30  ? 88  ARG A CA  1 
ATOM   708  C C   . ARG A 1 88  ? 4.319   -19.996 -25.028 1.00 43.04  ? 88  ARG A C   1 
ATOM   709  O O   . ARG A 1 88  ? 4.975   -19.658 -26.003 1.00 44.28  ? 88  ARG A O   1 
ATOM   710  C CB  . ARG A 1 88  ? 5.170   -18.598 -23.054 1.00 46.69  ? 88  ARG A CB  1 
ATOM   711  C CG  . ARG A 1 88  ? 5.738   -18.603 -21.640 1.00 48.35  ? 88  ARG A CG  1 
ATOM   712  C CD  . ARG A 1 88  ? 4.959   -19.447 -20.647 1.00 48.04  ? 88  ARG A CD  1 
ATOM   713  N NE  . ARG A 1 88  ? 5.573   -19.473 -19.331 1.00 49.95  ? 88  ARG A NE  1 
ATOM   714  C CZ  . ARG A 1 88  ? 6.299   -20.477 -18.855 1.00 51.07  ? 88  ARG A CZ  1 
ATOM   715  N NH1 . ARG A 1 88  ? 6.635   -21.492 -19.631 1.00 50.41  ? 88  ARG A NH1 1 
ATOM   716  N NH2 . ARG A 1 88  ? 6.725   -20.445 -17.607 1.00 53.39  ? 88  ARG A NH2 1 
ATOM   717  N N   . VAL A 1 89  ? 3.047   -20.396 -25.106 1.00 40.71  ? 89  VAL A N   1 
ATOM   718  C CA  . VAL A 1 89  ? 2.311   -20.450 -26.361 1.00 39.62  ? 89  VAL A CA  1 
ATOM   719  C C   . VAL A 1 89  ? 1.154   -19.453 -26.297 1.00 39.69  ? 89  VAL A C   1 
ATOM   720  O O   . VAL A 1 89  ? 0.493   -19.326 -25.280 1.00 40.59  ? 89  VAL A O   1 
ATOM   721  C CB  . VAL A 1 89  ? 1.812   -21.880 -26.673 1.00 39.57  ? 89  VAL A CB  1 
ATOM   722  C CG1 . VAL A 1 89  ? 0.909   -22.436 -25.584 1.00 40.17  ? 89  VAL A CG1 1 
ATOM   723  C CG2 . VAL A 1 89  ? 1.104   -21.986 -28.021 1.00 37.90  ? 89  VAL A CG2 1 
ATOM   724  N N   . TYR A 1 90  ? 0.911   -18.747 -27.404 1.00 41.10  ? 90  TYR A N   1 
ATOM   725  C CA  . TYR A 1 90  ? -0.121  -17.722 -27.468 1.00 41.84  ? 90  TYR A CA  1 
ATOM   726  C C   . TYR A 1 90  ? -0.944  -17.912 -28.746 1.00 41.49  ? 90  TYR A C   1 
ATOM   727  O O   . TYR A 1 90  ? -0.481  -18.522 -29.713 1.00 43.02  ? 90  TYR A O   1 
ATOM   728  C CB  . TYR A 1 90  ? 0.482   -16.316 -27.467 1.00 41.99  ? 90  TYR A CB  1 
ATOM   729  C CG  . TYR A 1 90  ? 1.545   -15.988 -26.424 1.00 44.62  ? 90  TYR A CG  1 
ATOM   730  C CD1 . TYR A 1 90  ? 2.856   -16.463 -26.539 1.00 45.27  ? 90  TYR A CD1 1 
ATOM   731  C CD2 . TYR A 1 90  ? 1.266   -15.119 -25.373 1.00 45.97  ? 90  TYR A CD2 1 
ATOM   732  C CE1 . TYR A 1 90  ? 3.835   -16.124 -25.617 1.00 45.78  ? 90  TYR A CE1 1 
ATOM   733  C CE2 . TYR A 1 90  ? 2.236   -14.776 -24.442 1.00 46.97  ? 90  TYR A CE2 1 
ATOM   734  C CZ  . TYR A 1 90  ? 3.517   -15.287 -24.559 1.00 47.55  ? 90  TYR A CZ  1 
ATOM   735  O OH  . TYR A 1 90  ? 4.468   -14.947 -23.642 1.00 50.60  ? 90  TYR A OH  1 
ATOM   736  N N   . VAL A 1 91  ? -2.171  -17.384 -28.749 1.00 39.24  ? 91  VAL A N   1 
ATOM   737  C CA  . VAL A 1 91  ? -2.985  -17.389 -29.946 1.00 38.64  ? 91  VAL A CA  1 
ATOM   738  C C   . VAL A 1 91  ? -3.441  -15.952 -30.179 1.00 41.26  ? 91  VAL A C   1 
ATOM   739  O O   . VAL A 1 91  ? -4.019  -15.346 -29.283 1.00 44.47  ? 91  VAL A O   1 
ATOM   740  C CB  . VAL A 1 91  ? -4.167  -18.373 -29.815 1.00 38.55  ? 91  VAL A CB  1 
ATOM   741  C CG1 . VAL A 1 91  ? -5.255  -18.109 -30.851 1.00 38.41  ? 91  VAL A CG1 1 
ATOM   742  C CG2 . VAL A 1 91  ? -3.714  -19.834 -29.865 1.00 35.94  ? 91  VAL A CG2 1 
ATOM   743  N N   . HIS A 1 92  ? -3.108  -15.399 -31.358 1.00 40.88  ? 92  HIS A N   1 
ATOM   744  C CA  . HIS A 1 92  ? -3.614  -14.115 -31.821 1.00 38.30  ? 92  HIS A CA  1 
ATOM   745  C C   . HIS A 1 92  ? -4.523  -14.420 -32.999 1.00 35.34  ? 92  HIS A C   1 
ATOM   746  O O   . HIS A 1 92  ? -4.048  -15.088 -33.918 1.00 33.92  ? 92  HIS A O   1 
ATOM   747  C CB  . HIS A 1 92  ? -2.468  -13.193 -32.265 1.00 39.58  ? 92  HIS A CB  1 
ATOM   748  C CG  . HIS A 1 92  ? -2.907  -12.061 -33.149 1.00 40.49  ? 92  HIS A CG  1 
ATOM   749  N ND1 . HIS A 1 92  ? -2.871  -12.130 -34.527 1.00 40.40  ? 92  HIS A ND1 1 
ATOM   750  C CD2 . HIS A 1 92  ? -3.465  -10.886 -32.865 1.00 41.11  ? 92  HIS A CD2 1 
ATOM   751  C CE1 . HIS A 1 92  ? -3.365  -11.022 -35.044 1.00 40.29  ? 92  HIS A CE1 1 
ATOM   752  N NE2 . HIS A 1 92  ? -3.733  -10.254 -34.052 1.00 41.54  ? 92  HIS A NE2 1 
ATOM   753  N N   . THR A 1 93  ? -5.784  -13.933 -32.945 1.00 34.23  ? 93  THR A N   1 
ATOM   754  C CA  . THR A 1 93  ? -6.809  -14.262 -33.928 1.00 33.35  ? 93  THR A CA  1 
ATOM   755  C C   . THR A 1 93  ? -6.833  -13.254 -35.071 1.00 36.11  ? 93  THR A C   1 
ATOM   756  O O   . THR A 1 93  ? -6.260  -12.158 -34.957 1.00 36.97  ? 93  THR A O   1 
ATOM   757  C CB  . THR A 1 93  ? -8.212  -14.347 -33.321 1.00 32.95  ? 93  THR A CB  1 
ATOM   758  O OG1 . THR A 1 93  ? -8.787  -13.060 -33.038 1.00 33.36  ? 93  THR A OG1 1 
ATOM   759  C CG2 . THR A 1 93  ? -8.220  -15.241 -32.097 1.00 32.75  ? 93  THR A CG2 1 
ATOM   760  N N   . ARG A 1 94  ? -7.544  -13.643 -36.148 1.00 37.02  ? 94  ARG A N   1 
ATOM   761  C CA  . ARG A 1 94  ? -7.785  -12.782 -37.302 1.00 39.53  ? 94  ARG A CA  1 
ATOM   762  C C   . ARG A 1 94  ? -8.665  -11.580 -36.948 1.00 41.21  ? 94  ARG A C   1 
ATOM   763  O O   . ARG A 1 94  ? -8.983  -10.798 -37.837 1.00 43.20  ? 94  ARG A O   1 
ATOM   764  C CB  . ARG A 1 94  ? -8.500  -13.532 -38.434 1.00 39.86  ? 94  ARG A CB  1 
ATOM   765  C CG  . ARG A 1 94  ? -10.009 -13.689 -38.249 1.00 40.04  ? 94  ARG A CG  1 
ATOM   766  C CD  . ARG A 1 94  ? -10.790 -13.321 -39.509 1.00 40.92  ? 94  ARG A CD  1 
ATOM   767  N NE  . ARG A 1 94  ? -10.291 -14.016 -40.696 1.00 40.48  ? 94  ARG A NE  1 
ATOM   768  C CZ  . ARG A 1 94  ? -10.098 -13.468 -41.893 1.00 42.16  ? 94  ARG A CZ  1 
ATOM   769  N NH1 . ARG A 1 94  ? -9.416  -14.118 -42.820 1.00 41.39  ? 94  ARG A NH1 1 
ATOM   770  N NH2 . ARG A 1 94  ? -10.530 -12.242 -42.145 1.00 45.08  ? 94  ARG A NH2 1 
ATOM   771  N N   . ASN A 1 95  ? -9.115  -11.470 -35.689 1.00 41.74  ? 95  ASN A N   1 
ATOM   772  C CA  . ASN A 1 95  ? -9.888  -10.322 -35.248 1.00 44.85  ? 95  ASN A CA  1 
ATOM   773  C C   . ASN A 1 95  ? -9.191  -9.628  -34.086 1.00 45.51  ? 95  ASN A C   1 
ATOM   774  O O   . ASN A 1 95  ? -9.851  -8.943  -33.310 1.00 48.34  ? 95  ASN A O   1 
ATOM   775  C CB  . ASN A 1 95  ? -11.319 -10.698 -34.859 1.00 46.64  ? 95  ASN A CB  1 
ATOM   776  C CG  . ASN A 1 95  ? -12.123 -11.135 -36.059 1.00 48.27  ? 95  ASN A CG  1 
ATOM   777  O OD1 . ASN A 1 95  ? -11.915 -10.619 -37.152 1.00 53.41  ? 95  ASN A OD1 1 
ATOM   778  N ND2 . ASN A 1 95  ? -13.007 -12.102 -35.883 1.00 48.79  ? 95  ASN A ND2 1 
ATOM   779  N N   . ASP A 1 96  ? -7.863  -9.761  -34.007 1.00 43.54  ? 96  ASP A N   1 
ATOM   780  C CA  . ASP A 1 96  ? -7.091  -9.006  -33.037 1.00 44.22  ? 96  ASP A CA  1 
ATOM   781  C C   . ASP A 1 96  ? -7.642  -9.253  -31.629 1.00 43.36  ? 96  ASP A C   1 
ATOM   782  O O   . ASP A 1 96  ? -7.940  -8.317  -30.883 1.00 42.26  ? 96  ASP A O   1 
ATOM   783  C CB  . ASP A 1 96  ? -7.041  -7.532  -33.441 1.00 46.40  ? 96  ASP A CB  1 
ATOM   784  C CG  . ASP A 1 96  ? -5.928  -7.179  -34.421 1.00 48.54  ? 96  ASP A CG  1 
ATOM   785  O OD1 . ASP A 1 96  ? -4.951  -7.956  -34.534 1.00 47.22  ? 96  ASP A OD1 1 
ATOM   786  O OD2 . ASP A 1 96  ? -6.025  -6.095  -35.056 1.00 54.86  ? 96  ASP A OD2 1 
ATOM   787  N N   . TYR A 1 97  ? -7.789  -10.541 -31.292 1.00 42.04  ? 97  TYR A N   1 
ATOM   788  C CA  . TYR A 1 97  ? -7.926  -10.988 -29.917 1.00 43.16  ? 97  TYR A CA  1 
ATOM   789  C C   . TYR A 1 97  ? -6.776  -11.950 -29.606 1.00 42.94  ? 97  TYR A C   1 
ATOM   790  O O   . TYR A 1 97  ? -6.383  -12.795 -30.419 1.00 39.52  ? 97  TYR A O   1 
ATOM   791  C CB  . TYR A 1 97  ? -9.270  -11.675 -29.644 1.00 43.93  ? 97  TYR A CB  1 
ATOM   792  C CG  . TYR A 1 97  ? -10.510 -10.797 -29.742 1.00 45.91  ? 97  TYR A CG  1 
ATOM   793  C CD1 . TYR A 1 97  ? -10.858 -9.924  -28.720 1.00 49.11  ? 97  TYR A CD1 1 
ATOM   794  C CD2 . TYR A 1 97  ? -11.329 -10.840 -30.860 1.00 45.74  ? 97  TYR A CD2 1 
ATOM   795  C CE1 . TYR A 1 97  ? -11.969 -9.100  -28.819 1.00 51.14  ? 97  TYR A CE1 1 
ATOM   796  C CE2 . TYR A 1 97  ? -12.459 -10.047 -30.957 1.00 48.28  ? 97  TYR A CE2 1 
ATOM   797  C CZ  . TYR A 1 97  ? -12.779 -9.163  -29.939 1.00 50.12  ? 97  TYR A CZ  1 
ATOM   798  O OH  . TYR A 1 97  ? -13.897 -8.378  -30.033 1.00 49.30  ? 97  TYR A OH  1 
ATOM   799  N N   . VAL A 1 98  ? -6.258  -11.842 -28.383 1.00 44.50  ? 98  VAL A N   1 
ATOM   800  C CA  . VAL A 1 98  ? -5.165  -12.694 -27.967 1.00 43.13  ? 98  VAL A CA  1 
ATOM   801  C C   . VAL A 1 98  ? -5.652  -13.636 -26.878 1.00 41.39  ? 98  VAL A C   1 
ATOM   802  O O   . VAL A 1 98  ? -6.504  -13.277 -26.076 1.00 41.80  ? 98  VAL A O   1 
ATOM   803  C CB  . VAL A 1 98  ? -3.972  -11.838 -27.517 1.00 46.33  ? 98  VAL A CB  1 
ATOM   804  C CG1 . VAL A 1 98  ? -3.060  -12.574 -26.543 1.00 46.88  ? 98  VAL A CG1 1 
ATOM   805  C CG2 . VAL A 1 98  ? -3.198  -11.346 -28.731 1.00 47.17  ? 98  VAL A CG2 1 
ATOM   806  N N   . ILE A 1 99  ? -5.113  -14.854 -26.901 1.00 41.08  ? 99  ILE A N   1 
ATOM   807  C CA  . ILE A 1 99  ? -5.414  -15.863 -25.903 1.00 41.54  ? 99  ILE A CA  1 
ATOM   808  C C   . ILE A 1 99  ? -4.101  -16.274 -25.261 1.00 41.82  ? 99  ILE A C   1 
ATOM   809  O O   . ILE A 1 99  ? -3.212  -16.813 -25.932 1.00 39.62  ? 99  ILE A O   1 
ATOM   810  C CB  . ILE A 1 99  ? -6.151  -17.086 -26.478 1.00 41.25  ? 99  ILE A CB  1 
ATOM   811  C CG1 . ILE A 1 99  ? -7.481  -16.692 -27.134 1.00 41.91  ? 99  ILE A CG1 1 
ATOM   812  C CG2 . ILE A 1 99  ? -6.323  -18.117 -25.371 1.00 42.11  ? 99  ILE A CG2 1 
ATOM   813  C CD1 . ILE A 1 99  ? -8.174  -17.801 -27.913 1.00 41.18  ? 99  ILE A CD1 1 
ATOM   814  N N   . TYR A 1 100 ? -4.035  -15.984 -23.958 1.00 44.80  ? 100 TYR A N   1 
ATOM   815  C CA  . TYR A 1 100 ? -2.958  -16.383 -23.070 1.00 46.91  ? 100 TYR A CA  1 
ATOM   816  C C   . TYR A 1 100 ? -3.255  -17.780 -22.525 1.00 49.08  ? 100 TYR A C   1 
ATOM   817  O O   . TYR A 1 100 ? -4.392  -18.066 -22.129 1.00 52.02  ? 100 TYR A O   1 
ATOM   818  C CB  . TYR A 1 100 ? -2.930  -15.309 -21.980 1.00 48.24  ? 100 TYR A CB  1 
ATOM   819  C CG  . TYR A 1 100 ? -2.640  -13.900 -22.477 1.00 46.49  ? 100 TYR A CG  1 
ATOM   820  C CD1 . TYR A 1 100 ? -1.357  -13.525 -22.842 1.00 45.60  ? 100 TYR A CD1 1 
ATOM   821  C CD2 . TYR A 1 100 ? -3.654  -12.953 -22.588 1.00 45.93  ? 100 TYR A CD2 1 
ATOM   822  C CE1 . TYR A 1 100 ? -1.090  -12.241 -23.287 1.00 46.68  ? 100 TYR A CE1 1 
ATOM   823  C CE2 . TYR A 1 100 ? -3.397  -11.663 -23.023 1.00 45.91  ? 100 TYR A CE2 1 
ATOM   824  C CZ  . TYR A 1 100 ? -2.109  -11.308 -23.374 1.00 46.32  ? 100 TYR A CZ  1 
ATOM   825  O OH  . TYR A 1 100 ? -1.833  -10.059 -23.836 1.00 46.60  ? 100 TYR A OH  1 
ATOM   826  N N   . ILE A 1 101 ? -2.236  -18.646 -22.503 1.00 47.24  ? 101 ILE A N   1 
ATOM   827  C CA  . ILE A 1 101 ? -2.462  -20.050 -22.211 1.00 46.99  ? 101 ILE A CA  1 
ATOM   828  C C   . ILE A 1 101 ? -1.473  -20.493 -21.144 1.00 47.98  ? 101 ILE A C   1 
ATOM   829  O O   . ILE A 1 101 ? -0.282  -20.618 -21.435 1.00 47.76  ? 101 ILE A O   1 
ATOM   830  C CB  . ILE A 1 101 ? -2.333  -20.887 -23.498 1.00 46.98  ? 101 ILE A CB  1 
ATOM   831  C CG1 . ILE A 1 101 ? -3.317  -20.397 -24.569 1.00 46.25  ? 101 ILE A CG1 1 
ATOM   832  C CG2 . ILE A 1 101 ? -2.475  -22.379 -23.196 1.00 46.45  ? 101 ILE A CG2 1 
ATOM   833  C CD1 . ILE A 1 101 ? -3.451  -21.316 -25.752 1.00 45.13  ? 101 ILE A CD1 1 
ATOM   834  N N   . LYS A 1 102 ? -1.989  -20.724 -19.928 1.00 48.74  ? 102 LYS A N   1 
ATOM   835  C CA  . LYS A 1 102 ? -1.181  -21.157 -18.804 1.00 49.99  ? 102 LYS A CA  1 
ATOM   836  C C   . LYS A 1 102 ? -0.611  -22.540 -19.103 1.00 48.38  ? 102 LYS A C   1 
ATOM   837  O O   . LYS A 1 102 ? -1.371  -23.447 -19.428 1.00 47.46  ? 102 LYS A O   1 
ATOM   838  C CB  . LYS A 1 102 ? -2.025  -21.173 -17.531 1.00 53.92  ? 102 LYS A CB  1 
ATOM   839  C CG  . LYS A 1 102 ? -2.446  -19.797 -17.038 1.00 57.69  ? 102 LYS A CG  1 
ATOM   840  C CD  . LYS A 1 102 ? -2.982  -19.787 -15.619 1.00 62.91  ? 102 LYS A CD  1 
ATOM   841  C CE  . LYS A 1 102 ? -3.160  -18.389 -15.061 1.00 66.56  ? 102 LYS A CE  1 
ATOM   842  N NZ  . LYS A 1 102 ? -3.848  -18.412 -13.746 1.00 70.70  ? 102 LYS A NZ  1 
ATOM   843  N N   . PRO A 1 103 ? 0.727   -22.741 -19.003 1.00 48.22  ? 103 PRO A N   1 
ATOM   844  C CA  . PRO A 1 103 ? 1.381   -23.951 -19.507 1.00 48.16  ? 103 PRO A CA  1 
ATOM   845  C C   . PRO A 1 103 ? 0.698   -25.261 -19.127 1.00 50.63  ? 103 PRO A C   1 
ATOM   846  O O   . PRO A 1 103 ? 0.505   -26.135 -19.972 1.00 51.70  ? 103 PRO A O   1 
ATOM   847  C CB  . PRO A 1 103 ? 2.762   -23.891 -18.846 1.00 49.10  ? 103 PRO A CB  1 
ATOM   848  C CG  . PRO A 1 103 ? 3.045   -22.418 -18.735 1.00 49.11  ? 103 PRO A CG  1 
ATOM   849  C CD  . PRO A 1 103 ? 1.698   -21.796 -18.428 1.00 49.41  ? 103 PRO A CD  1 
ATOM   850  N N   . GLU A 1 104 ? 0.299   -25.349 -17.857 1.00 53.13  ? 104 GLU A N   1 
ATOM   851  C CA  . GLU A 1 104 ? -0.300  -26.539 -17.274 1.00 54.17  ? 104 GLU A CA  1 
ATOM   852  C C   . GLU A 1 104 ? -1.638  -26.907 -17.924 1.00 52.04  ? 104 GLU A C   1 
ATOM   853  O O   . GLU A 1 104 ? -2.155  -27.993 -17.674 1.00 51.80  ? 104 GLU A O   1 
ATOM   854  C CB  . GLU A 1 104 ? -0.463  -26.343 -15.764 1.00 58.90  ? 104 GLU A CB  1 
ATOM   855  C CG  . GLU A 1 104 ? -1.217  -25.076 -15.356 1.00 61.62  ? 104 GLU A CG  1 
ATOM   856  C CD  . GLU A 1 104 ? -0.446  -23.752 -15.294 1.00 63.64  ? 104 GLU A CD  1 
ATOM   857  O OE1 . GLU A 1 104 ? -1.038  -22.765 -14.823 1.00 67.55  ? 104 GLU A OE1 1 
ATOM   858  O OE2 . GLU A 1 104 ? 0.733   -23.679 -15.722 1.00 61.24  ? 104 GLU A OE2 1 
ATOM   859  N N   . THR A 1 105 ? -2.192  -26.037 -18.775 1.00 50.78  ? 105 THR A N   1 
ATOM   860  C CA  . THR A 1 105 ? -3.475  -26.297 -19.419 1.00 50.38  ? 105 THR A CA  1 
ATOM   861  C C   . THR A 1 105 ? -3.495  -27.610 -20.219 1.00 49.78  ? 105 THR A C   1 
ATOM   862  O O   . THR A 1 105 ? -2.641  -27.867 -21.066 1.00 47.56  ? 105 THR A O   1 
ATOM   863  C CB  . THR A 1 105 ? -3.879  -25.123 -20.316 1.00 48.49  ? 105 THR A CB  1 
ATOM   864  O OG1 . THR A 1 105 ? -3.731  -23.927 -19.545 1.00 50.28  ? 105 THR A OG1 1 
ATOM   865  C CG2 . THR A 1 105 ? -5.293  -25.252 -20.838 1.00 47.33  ? 105 THR A CG2 1 
ATOM   866  N N   . ARG A 1 106 ? -4.506  -28.443 -19.926 1.00 52.15  ? 106 ARG A N   1 
ATOM   867  C CA  . ARG A 1 106 ? -4.822  -29.643 -20.686 1.00 50.51  ? 106 ARG A CA  1 
ATOM   868  C C   . ARG A 1 106 ? -5.979  -29.308 -21.630 1.00 48.77  ? 106 ARG A C   1 
ATOM   869  O O   . ARG A 1 106 ? -7.126  -29.137 -21.194 1.00 48.55  ? 106 ARG A O   1 
ATOM   870  C CB  . ARG A 1 106 ? -5.161  -30.812 -19.751 1.00 51.41  ? 106 ARG A CB  1 
ATOM   871  C CG  . ARG A 1 106 ? -5.361  -32.143 -20.460 1.00 51.79  ? 106 ARG A CG  1 
ATOM   872  C CD  . ARG A 1 106 ? -5.633  -33.280 -19.496 1.00 57.12  ? 106 ARG A CD  1 
ATOM   873  N NE  . ARG A 1 106 ? -5.891  -34.572 -20.132 1.00 59.27  ? 106 ARG A NE  1 
ATOM   874  C CZ  . ARG A 1 106 ? -7.032  -34.939 -20.719 1.00 60.39  ? 106 ARG A CZ  1 
ATOM   875  N NH1 . ARG A 1 106 ? -8.047  -34.092 -20.824 1.00 61.48  ? 106 ARG A NH1 1 
ATOM   876  N NH2 . ARG A 1 106 ? -7.153  -36.165 -21.205 1.00 59.76  ? 106 ARG A NH2 1 
ATOM   877  N N   . LEU A 1 107 ? -5.661  -29.174 -22.928 1.00 45.95  ? 107 LEU A N   1 
ATOM   878  C CA  . LEU A 1 107 ? -6.689  -28.941 -23.926 1.00 42.60  ? 107 LEU A CA  1 
ATOM   879  C C   . LEU A 1 107 ? -7.446  -30.232 -24.133 1.00 41.31  ? 107 LEU A C   1 
ATOM   880  O O   . LEU A 1 107 ? -6.850  -31.302 -24.042 1.00 41.58  ? 107 LEU A O   1 
ATOM   881  C CB  . LEU A 1 107 ? -6.083  -28.505 -25.259 1.00 42.04  ? 107 LEU A CB  1 
ATOM   882  C CG  . LEU A 1 107 ? -6.105  -27.009 -25.566 1.00 42.92  ? 107 LEU A CG  1 
ATOM   883  C CD1 . LEU A 1 107 ? -6.335  -26.805 -27.059 1.00 42.73  ? 107 LEU A CD1 1 
ATOM   884  C CD2 . LEU A 1 107 ? -7.151  -26.252 -24.760 1.00 42.63  ? 107 LEU A CD2 1 
ATOM   885  N N   . PRO A 1 108 ? -8.768  -30.155 -24.401 1.00 39.71  ? 108 PRO A N   1 
ATOM   886  C CA  . PRO A 1 108 ? -9.530  -31.312 -24.847 1.00 39.24  ? 108 PRO A CA  1 
ATOM   887  C C   . PRO A 1 108 ? -8.863  -31.980 -26.049 1.00 37.95  ? 108 PRO A C   1 
ATOM   888  O O   . PRO A 1 108 ? -8.529  -31.344 -27.044 1.00 33.54  ? 108 PRO A O   1 
ATOM   889  C CB  . PRO A 1 108 ? -10.911 -30.745 -25.205 1.00 38.59  ? 108 PRO A CB  1 
ATOM   890  C CG  . PRO A 1 108 ? -11.021 -29.490 -24.400 1.00 39.39  ? 108 PRO A CG  1 
ATOM   891  C CD  . PRO A 1 108 ? -9.611  -28.964 -24.245 1.00 39.34  ? 108 PRO A CD  1 
ATOM   892  N N   . ARG A 1 109 ? -8.671  -33.290 -25.934 1.00 40.85  ? 109 ARG A N   1 
ATOM   893  C CA  . ARG A 1 109 ? -8.193  -34.073 -27.055 1.00 42.03  ? 109 ARG A CA  1 
ATOM   894  C C   . ARG A 1 109 ? -9.279  -34.171 -28.134 1.00 42.27  ? 109 ARG A C   1 
ATOM   895  O O   . ARG A 1 109 ? -8.958  -34.152 -29.326 1.00 45.11  ? 109 ARG A O   1 
ATOM   896  C CB  . ARG A 1 109 ? -7.738  -35.453 -26.579 1.00 43.18  ? 109 ARG A CB  1 
ATOM   897  C CG  . ARG A 1 109 ? -6.410  -35.476 -25.827 1.00 42.97  ? 109 ARG A CG  1 
ATOM   898  C CD  . ARG A 1 109 ? -6.479  -35.216 -24.331 1.00 44.76  ? 109 ARG A CD  1 
ATOM   899  N NE  . ARG A 1 109 ? -5.846  -33.959 -23.973 1.00 45.17  ? 109 ARG A NE  1 
ATOM   900  C CZ  . ARG A 1 109 ? -4.531  -33.763 -23.896 1.00 45.35  ? 109 ARG A CZ  1 
ATOM   901  N NH1 . ARG A 1 109 ? -4.058  -32.536 -24.006 1.00 44.54  ? 109 ARG A NH1 1 
ATOM   902  N NH2 . ARG A 1 109 ? -3.686  -34.782 -23.826 1.00 45.26  ? 109 ARG A NH2 1 
ATOM   903  N N   . ASN A 1 110 ? -10.556 -34.244 -27.734 1.00 41.20  ? 110 ASN A N   1 
ATOM   904  C CA  . ASN A 1 110 ? -11.635 -34.340 -28.708 1.00 40.76  ? 110 ASN A CA  1 
ATOM   905  C C   . ASN A 1 110 ? -11.976 -32.961 -29.277 1.00 38.74  ? 110 ASN A C   1 
ATOM   906  O O   . ASN A 1 110 ? -12.244 -32.024 -28.534 1.00 38.63  ? 110 ASN A O   1 
ATOM   907  C CB  . ASN A 1 110 ? -12.870 -35.000 -28.102 1.00 42.24  ? 110 ASN A CB  1 
ATOM   908  C CG  . ASN A 1 110 ? -14.025 -35.037 -29.073 1.00 41.64  ? 110 ASN A CG  1 
ATOM   909  O OD1 . ASN A 1 110 ? -14.560 -33.993 -29.415 1.00 40.22  ? 110 ASN A OD1 1 
ATOM   910  N ND2 . ASN A 1 110 ? -14.421 -36.220 -29.514 1.00 43.41  ? 110 ASN A ND2 1 
ATOM   911  N N   . TYR A 1 111 ? -12.017 -32.853 -30.606 1.00 37.31  ? 111 TYR A N   1 
ATOM   912  C CA  . TYR A 1 111 ? -12.221 -31.577 -31.280 1.00 36.96  ? 111 TYR A CA  1 
ATOM   913  C C   . TYR A 1 111 ? -13.467 -30.836 -30.775 1.00 38.10  ? 111 TYR A C   1 
ATOM   914  O O   . TYR A 1 111 ? -13.428 -29.626 -30.603 1.00 37.96  ? 111 TYR A O   1 
ATOM   915  C CB  . TYR A 1 111 ? -12.323 -31.811 -32.793 1.00 36.68  ? 111 TYR A CB  1 
ATOM   916  C CG  . TYR A 1 111 ? -12.754 -30.594 -33.609 1.00 36.13  ? 111 TYR A CG  1 
ATOM   917  C CD1 . TYR A 1 111 ? -11.920 -29.495 -33.759 1.00 35.19  ? 111 TYR A CD1 1 
ATOM   918  C CD2 . TYR A 1 111 ? -14.002 -30.541 -34.220 1.00 36.31  ? 111 TYR A CD2 1 
ATOM   919  C CE1 . TYR A 1 111 ? -12.305 -28.391 -34.502 1.00 35.06  ? 111 TYR A CE1 1 
ATOM   920  C CE2 . TYR A 1 111 ? -14.404 -29.440 -34.955 1.00 35.83  ? 111 TYR A CE2 1 
ATOM   921  C CZ  . TYR A 1 111 ? -13.557 -28.358 -35.092 1.00 35.56  ? 111 TYR A CZ  1 
ATOM   922  O OH  . TYR A 1 111 ? -13.953 -27.266 -35.816 1.00 36.79  ? 111 TYR A OH  1 
ATOM   923  N N   . ASN A 1 112 ? -14.585 -31.538 -30.588 1.00 39.84  ? 112 ASN A N   1 
ATOM   924  C CA  . ASN A 1 112 ? -15.869 -30.902 -30.340 1.00 41.56  ? 112 ASN A CA  1 
ATOM   925  C C   . ASN A 1 112 ? -15.984 -30.417 -28.896 1.00 42.46  ? 112 ASN A C   1 
ATOM   926  O O   . ASN A 1 112 ? -16.785 -29.531 -28.631 1.00 43.07  ? 112 ASN A O   1 
ATOM   927  C CB  . ASN A 1 112 ? -17.031 -31.845 -30.662 1.00 44.90  ? 112 ASN A CB  1 
ATOM   928  C CG  . ASN A 1 112 ? -17.096 -32.191 -32.135 1.00 45.36  ? 112 ASN A CG  1 
ATOM   929  O OD1 . ASN A 1 112 ? -17.169 -31.294 -32.974 1.00 46.00  ? 112 ASN A OD1 1 
ATOM   930  N ND2 . ASN A 1 112 ? -17.047 -33.477 -32.454 1.00 45.26  ? 112 ASN A ND2 1 
ATOM   931  N N   . ARG A 1 113 ? -15.239 -31.029 -27.962 1.00 44.23  ? 113 ARG A N   1 
ATOM   932  C CA  . ARG A 1 113 ? -15.093 -30.504 -26.608 1.00 46.53  ? 113 ARG A CA  1 
ATOM   933  C C   . ARG A 1 113 ? -14.239 -29.240 -26.653 1.00 44.59  ? 113 ARG A C   1 
ATOM   934  O O   . ARG A 1 113 ? -14.503 -28.262 -25.966 1.00 43.99  ? 113 ARG A O   1 
ATOM   935  C CB  . ARG A 1 113 ? -14.403 -31.490 -25.659 1.00 49.85  ? 113 ARG A CB  1 
ATOM   936  C CG  . ARG A 1 113 ? -15.333 -32.423 -24.894 1.00 55.07  ? 113 ARG A CG  1 
ATOM   937  C CD  . ARG A 1 113 ? -14.606 -33.050 -23.700 1.00 60.17  ? 113 ARG A CD  1 
ATOM   938  N NE  . ARG A 1 113 ? -15.281 -34.233 -23.149 1.00 65.63  ? 113 ARG A NE  1 
ATOM   939  C CZ  . ARG A 1 113 ? -14.882 -35.508 -23.287 1.00 66.20  ? 113 ARG A CZ  1 
ATOM   940  N NH1 . ARG A 1 113 ? -13.732 -35.805 -23.879 1.00 63.05  ? 113 ARG A NH1 1 
ATOM   941  N NH2 . ARG A 1 113 ? -15.645 -36.492 -22.824 1.00 65.98  ? 113 ARG A NH2 1 
ATOM   942  N N   . PHE A 1 114 ? -13.190 -29.282 -27.474 1.00 43.50  ? 114 PHE A N   1 
ATOM   943  C CA  . PHE A 1 114 ? -12.316 -28.139 -27.657 1.00 41.37  ? 114 PHE A CA  1 
ATOM   944  C C   . PHE A 1 114 ? -13.099 -26.949 -28.194 1.00 38.92  ? 114 PHE A C   1 
ATOM   945  O O   . PHE A 1 114 ? -12.747 -25.818 -27.879 1.00 38.33  ? 114 PHE A O   1 
ATOM   946  C CB  . PHE A 1 114 ? -11.177 -28.474 -28.619 1.00 40.71  ? 114 PHE A CB  1 
ATOM   947  C CG  . PHE A 1 114 ? -10.494 -27.256 -29.177 1.00 40.92  ? 114 PHE A CG  1 
ATOM   948  C CD1 . PHE A 1 114 ? -9.548  -26.584 -28.421 1.00 41.09  ? 114 PHE A CD1 1 
ATOM   949  C CD2 . PHE A 1 114 ? -10.849 -26.748 -30.422 1.00 40.51  ? 114 PHE A CD2 1 
ATOM   950  C CE1 . PHE A 1 114 ? -8.928  -25.451 -28.921 1.00 41.60  ? 114 PHE A CE1 1 
ATOM   951  C CE2 . PHE A 1 114 ? -10.232 -25.609 -30.919 1.00 40.38  ? 114 PHE A CE2 1 
ATOM   952  C CZ  . PHE A 1 114 ? -9.272  -24.963 -30.167 1.00 40.75  ? 114 PHE A CZ  1 
ATOM   953  N N   . ILE A 1 115 ? -14.104 -27.220 -29.039 1.00 37.84  ? 115 ILE A N   1 
ATOM   954  C CA  . ILE A 1 115 ? -14.951 -26.180 -29.605 1.00 37.49  ? 115 ILE A CA  1 
ATOM   955  C C   . ILE A 1 115 ? -15.861 -25.654 -28.512 1.00 38.61  ? 115 ILE A C   1 
ATOM   956  O O   . ILE A 1 115 ? -16.096 -24.454 -28.411 1.00 40.94  ? 115 ILE A O   1 
ATOM   957  C CB  . ILE A 1 115 ? -15.798 -26.662 -30.799 1.00 36.89  ? 115 ILE A CB  1 
ATOM   958  C CG1 . ILE A 1 115 ? -14.948 -27.016 -32.019 1.00 34.99  ? 115 ILE A CG1 1 
ATOM   959  C CG2 . ILE A 1 115 ? -16.829 -25.600 -31.147 1.00 37.66  ? 115 ILE A CG2 1 
ATOM   960  C CD1 . ILE A 1 115 ? -14.410 -25.812 -32.734 1.00 34.57  ? 115 ILE A CD1 1 
ATOM   961  N N   . GLY A 1 116 ? -16.390 -26.571 -27.715 1.00 39.28  ? 116 GLY A N   1 
ATOM   962  C CA  . GLY A 1 116 ? -17.205 -26.175 -26.581 1.00 41.64  ? 116 GLY A CA  1 
ATOM   963  C C   . GLY A 1 116 ? -16.464 -25.202 -25.671 1.00 40.96  ? 116 GLY A C   1 
ATOM   964  O O   . GLY A 1 116 ? -17.040 -24.218 -25.217 1.00 42.17  ? 116 GLY A O   1 
ATOM   965  N N   . LEU A 1 117 ? -15.184 -25.498 -25.437 1.00 39.69  ? 117 LEU A N   1 
ATOM   966  C CA  . LEU A 1 117 ? -14.313 -24.686 -24.604 1.00 40.59  ? 117 LEU A CA  1 
ATOM   967  C C   . LEU A 1 117 ? -14.105 -23.304 -25.220 1.00 41.68  ? 117 LEU A C   1 
ATOM   968  O O   . LEU A 1 117 ? -14.095 -22.303 -24.508 1.00 44.17  ? 117 LEU A O   1 
ATOM   969  C CB  . LEU A 1 117 ? -12.974 -25.412 -24.467 1.00 38.82  ? 117 LEU A CB  1 
ATOM   970  C CG  . LEU A 1 117 ? -11.921 -24.705 -23.629 1.00 38.52  ? 117 LEU A CG  1 
ATOM   971  C CD1 . LEU A 1 117 ? -12.471 -24.408 -22.244 1.00 41.71  ? 117 LEU A CD1 1 
ATOM   972  C CD2 . LEU A 1 117 ? -10.665 -25.561 -23.538 1.00 37.51  ? 117 LEU A CD2 1 
ATOM   973  N N   . MET A 1 118 ? -13.945 -23.257 -26.546 1.00 41.29  ? 118 MET A N   1 
ATOM   974  C CA  . MET A 1 118 ? -13.723 -22.000 -27.234 1.00 41.90  ? 118 MET A CA  1 
ATOM   975  C C   . MET A 1 118 ? -14.979 -21.135 -27.132 1.00 43.13  ? 118 MET A C   1 
ATOM   976  O O   . MET A 1 118 ? -14.903 -19.917 -27.004 1.00 42.15  ? 118 MET A O   1 
ATOM   977  C CB  . MET A 1 118 ? -13.375 -22.248 -28.703 1.00 41.44  ? 118 MET A CB  1 
ATOM   978  C CG  . MET A 1 118 ? -11.984 -22.827 -28.906 1.00 42.27  ? 118 MET A CG  1 
ATOM   979  S SD  . MET A 1 118 ? -10.623 -21.857 -28.193 1.00 42.38  ? 118 MET A SD  1 
ATOM   980  C CE  . MET A 1 118 ? -10.360 -22.773 -26.678 1.00 43.44  ? 118 MET A CE  1 
ATOM   981  N N   . GLU A 1 119 ? -16.147 -21.763 -27.204 1.00 45.18  ? 119 GLU A N   1 
ATOM   982  C CA  . GLU A 1 119 ? -17.369 -20.989 -27.143 1.00 49.80  ? 119 GLU A CA  1 
ATOM   983  C C   . GLU A 1 119 ? -17.450 -20.345 -25.763 1.00 53.72  ? 119 GLU A C   1 
ATOM   984  O O   . GLU A 1 119 ? -17.760 -19.156 -25.640 1.00 53.84  ? 119 GLU A O   1 
ATOM   985  C CB  . GLU A 1 119 ? -18.560 -21.882 -27.467 1.00 51.46  ? 119 GLU A CB  1 
ATOM   986  C CG  . GLU A 1 119 ? -18.575 -22.331 -28.910 1.00 51.89  ? 119 GLU A CG  1 
ATOM   987  C CD  . GLU A 1 119 ? -19.660 -23.351 -29.229 1.00 55.60  ? 119 GLU A CD  1 
ATOM   988  O OE1 . GLU A 1 119 ? -19.870 -23.641 -30.450 1.00 53.69  ? 119 GLU A OE1 1 
ATOM   989  O OE2 . GLU A 1 119 ? -20.304 -23.850 -28.256 1.00 55.43  ? 119 GLU A OE2 1 
ATOM   990  N N   . ASN A 1 120 ? -17.126 -21.153 -24.744 1.00 55.67  ? 120 ASN A N   1 
ATOM   991  C CA  . ASN A 1 120 ? -17.029 -20.677 -23.379 1.00 58.85  ? 120 ASN A CA  1 
ATOM   992  C C   . ASN A 1 120 ? -16.078 -19.492 -23.338 1.00 55.92  ? 120 ASN A C   1 
ATOM   993  O O   . ASN A 1 120 ? -16.496 -18.394 -22.998 1.00 58.91  ? 120 ASN A O   1 
ATOM   994  C CB  . ASN A 1 120 ? -16.554 -21.762 -22.415 1.00 62.67  ? 120 ASN A CB  1 
ATOM   995  C CG  . ASN A 1 120 ? -17.606 -22.812 -22.142 1.00 64.52  ? 120 ASN A CG  1 
ATOM   996  O OD1 . ASN A 1 120 ? -18.784 -22.582 -22.399 1.00 67.27  ? 120 ASN A OD1 1 
ATOM   997  N ND2 . ASN A 1 120 ? -17.190 -23.949 -21.606 1.00 63.85  ? 120 ASN A ND2 1 
ATOM   998  N N   . LEU A 1 121 ? -14.819 -19.719 -23.719 1.00 50.33  ? 121 LEU A N   1 
ATOM   999  C CA  . LEU A 1 121 ? -13.784 -18.707 -23.554 1.00 48.96  ? 121 LEU A CA  1 
ATOM   1000 C C   . LEU A 1 121 ? -14.223 -17.360 -24.134 1.00 49.47  ? 121 LEU A C   1 
ATOM   1001 O O   . LEU A 1 121 ? -14.054 -16.339 -23.476 1.00 51.22  ? 121 LEU A O   1 
ATOM   1002 C CB  . LEU A 1 121 ? -12.472 -19.200 -24.173 1.00 44.70  ? 121 LEU A CB  1 
ATOM   1003 C CG  . LEU A 1 121 ? -11.332 -18.184 -24.229 1.00 44.03  ? 121 LEU A CG  1 
ATOM   1004 C CD1 . LEU A 1 121 ? -11.044 -17.560 -22.871 1.00 46.67  ? 121 LEU A CD1 1 
ATOM   1005 C CD2 . LEU A 1 121 ? -10.066 -18.835 -24.758 1.00 42.44  ? 121 LEU A CD2 1 
ATOM   1006 N N   . PHE A 1 122 ? -14.815 -17.353 -25.335 1.00 50.58  ? 122 PHE A N   1 
ATOM   1007 C CA  . PHE A 1 122 ? -15.276 -16.115 -25.961 1.00 52.62  ? 122 PHE A CA  1 
ATOM   1008 C C   . PHE A 1 122 ? -16.449 -15.498 -25.197 1.00 53.67  ? 122 PHE A C   1 
ATOM   1009 O O   . PHE A 1 122 ? -16.638 -14.293 -25.232 1.00 54.36  ? 122 PHE A O   1 
ATOM   1010 C CB  . PHE A 1 122 ? -15.680 -16.321 -27.424 1.00 52.47  ? 122 PHE A CB  1 
ATOM   1011 C CG  . PHE A 1 122 ? -14.547 -16.297 -28.418 1.00 54.26  ? 122 PHE A CG  1 
ATOM   1012 C CD1 . PHE A 1 122 ? -13.518 -17.220 -28.356 1.00 55.67  ? 122 PHE A CD1 1 
ATOM   1013 C CD2 . PHE A 1 122 ? -14.511 -15.348 -29.431 1.00 58.17  ? 122 PHE A CD2 1 
ATOM   1014 C CE1 . PHE A 1 122 ? -12.489 -17.192 -29.285 1.00 56.04  ? 122 PHE A CE1 1 
ATOM   1015 C CE2 . PHE A 1 122 ? -13.480 -15.319 -30.360 1.00 56.33  ? 122 PHE A CE2 1 
ATOM   1016 C CZ  . PHE A 1 122 ? -12.474 -16.246 -30.287 1.00 55.41  ? 122 PHE A CZ  1 
ATOM   1017 N N   . GLU A 1 123 ? -17.253 -16.328 -24.538 1.00 55.25  ? 123 GLU A N   1 
ATOM   1018 C CA  . GLU A 1 123 ? -18.413 -15.862 -23.795 1.00 59.67  ? 123 GLU A CA  1 
ATOM   1019 C C   . GLU A 1 123 ? -17.983 -15.197 -22.484 1.00 59.65  ? 123 GLU A C   1 
ATOM   1020 O O   . GLU A 1 123 ? -18.345 -14.066 -22.200 1.00 59.89  ? 123 GLU A O   1 
ATOM   1021 C CB  . GLU A 1 123 ? -19.350 -17.055 -23.556 1.00 62.80  ? 123 GLU A CB  1 
ATOM   1022 C CG  . GLU A 1 123 ? -20.591 -16.765 -22.732 1.00 67.10  ? 123 GLU A CG  1 
ATOM   1023 C CD  . GLU A 1 123 ? -21.471 -15.643 -23.258 1.00 73.61  ? 123 GLU A CD  1 
ATOM   1024 O OE1 . GLU A 1 123 ? -21.023 -14.923 -24.190 1.00 73.06  ? 123 GLU A OE1 1 
ATOM   1025 O OE2 . GLU A 1 123 ? -22.612 -15.479 -22.730 1.00 81.21  ? 123 GLU A OE2 1 
ATOM   1026 N N   . LYS A 1 124 ? -17.226 -15.926 -21.671 1.00 59.32  ? 124 LYS A N   1 
ATOM   1027 C CA  . LYS A 1 124 ? -16.896 -15.502 -20.328 1.00 61.19  ? 124 LYS A CA  1 
ATOM   1028 C C   . LYS A 1 124 ? -15.600 -14.701 -20.329 1.00 60.03  ? 124 LYS A C   1 
ATOM   1029 O O   . LYS A 1 124 ? -15.390 -13.898 -19.426 1.00 61.95  ? 124 LYS A O   1 
ATOM   1030 C CB  . LYS A 1 124 ? -16.798 -16.742 -19.441 1.00 63.85  ? 124 LYS A CB  1 
ATOM   1031 C CG  . LYS A 1 124 ? -18.130 -17.443 -19.239 1.00 68.32  ? 124 LYS A CG  1 
ATOM   1032 C CD  . LYS A 1 124 ? -18.002 -18.883 -18.834 1.00 72.51  ? 124 LYS A CD  1 
ATOM   1033 C CE  . LYS A 1 124 ? -19.251 -19.682 -19.150 1.00 76.85  ? 124 LYS A CE  1 
ATOM   1034 N NZ  . LYS A 1 124 ? -18.943 -21.120 -19.326 1.00 77.94  ? 124 LYS A NZ  1 
ATOM   1035 N N   . GLY A 1 125 ? -14.717 -14.950 -21.307 1.00 56.95  ? 125 GLY A N   1 
ATOM   1036 C CA  . GLY A 1 125 ? -13.493 -14.177 -21.438 1.00 55.81  ? 125 GLY A CA  1 
ATOM   1037 C C   . GLY A 1 125 ? -12.292 -14.806 -20.733 1.00 55.44  ? 125 GLY A C   1 
ATOM   1038 O O   . GLY A 1 125 ? -11.161 -14.434 -21.029 1.00 53.93  ? 125 GLY A O   1 
ATOM   1039 N N   . ALA A 1 126 ? -12.534 -15.731 -19.793 1.00 57.57  ? 126 ALA A N   1 
ATOM   1040 C CA  . ALA A 1 126 ? -11.469 -16.510 -19.176 1.00 57.10  ? 126 ALA A CA  1 
ATOM   1041 C C   . ALA A 1 126 ? -12.052 -17.782 -18.563 1.00 58.78  ? 126 ALA A C   1 
ATOM   1042 O O   . ALA A 1 126 ? -13.105 -17.733 -17.920 1.00 59.87  ? 126 ALA A O   1 
ATOM   1043 C CB  . ALA A 1 126 ? -10.754 -15.673 -18.148 1.00 57.81  ? 126 ALA A CB  1 
ATOM   1044 N N   . VAL A 1 127 ? -11.383 -18.923 -18.783 1.00 58.10  ? 127 VAL A N   1 
ATOM   1045 C CA  . VAL A 1 127 ? -11.961 -20.188 -18.348 1.00 60.64  ? 127 VAL A CA  1 
ATOM   1046 C C   . VAL A 1 127 ? -10.878 -21.113 -17.801 1.00 63.30  ? 127 VAL A C   1 
ATOM   1047 O O   . VAL A 1 127 ? -9.758  -21.140 -18.310 1.00 59.65  ? 127 VAL A O   1 
ATOM   1048 C CB  . VAL A 1 127 ? -12.732 -20.888 -19.483 1.00 58.16  ? 127 VAL A CB  1 
ATOM   1049 C CG1 . VAL A 1 127 ? -13.940 -20.089 -19.932 1.00 59.18  ? 127 VAL A CG1 1 
ATOM   1050 C CG2 . VAL A 1 127 ? -11.844 -21.199 -20.672 1.00 54.92  ? 127 VAL A CG2 1 
ATOM   1051 N N   . PRO A 1 128 ? -11.177 -21.902 -16.740 1.00 71.83  ? 128 PRO A N   1 
ATOM   1052 C CA  . PRO A 1 128 ? -12.393 -21.723 -15.940 1.00 77.36  ? 128 PRO A CA  1 
ATOM   1053 C C   . PRO A 1 128 ? -12.279 -20.556 -14.954 1.00 83.11  ? 128 PRO A C   1 
ATOM   1054 O O   . PRO A 1 128 ? -11.295 -19.818 -14.955 1.00 80.56  ? 128 PRO A O   1 
ATOM   1055 C CB  . PRO A 1 128 ? -12.554 -23.090 -15.256 1.00 78.12  ? 128 PRO A CB  1 
ATOM   1056 C CG  . PRO A 1 128 ? -11.136 -23.604 -15.104 1.00 77.34  ? 128 PRO A CG  1 
ATOM   1057 C CD  . PRO A 1 128 ? -10.374 -23.053 -16.290 1.00 73.50  ? 128 PRO A CD  1 
ATOM   1058 N N   . GLU A 1 129 ? -13.278 -20.433 -14.074 1.00 91.71  ? 129 GLU A N   1 
ATOM   1059 C CA  . GLU A 1 129 ? -13.683 -19.148 -13.524 1.00 98.84  ? 129 GLU A CA  1 
ATOM   1060 C C   . GLU A 1 129 ? -12.632 -18.643 -12.532 1.00 103.58 ? 129 GLU A C   1 
ATOM   1061 O O   . GLU A 1 129 ? -12.324 -17.455 -12.511 1.00 108.22 ? 129 GLU A O   1 
ATOM   1062 C CB  . GLU A 1 129 ? -15.062 -19.238 -12.856 1.00 103.21 ? 129 GLU A CB  1 
ATOM   1063 C CG  . GLU A 1 129 ? -15.991 -20.341 -13.379 1.00 103.64 ? 129 GLU A CG  1 
ATOM   1064 C CD  . GLU A 1 129 ? -15.880 -20.787 -14.834 1.00 101.30 ? 129 GLU A CD  1 
ATOM   1065 O OE1 . GLU A 1 129 ? -15.724 -22.009 -15.062 1.00 96.24  ? 129 GLU A OE1 1 
ATOM   1066 O OE2 . GLU A 1 129 ? -15.950 -19.932 -15.741 1.00 101.48 ? 129 GLU A OE2 1 
ATOM   1067 N N   . ASP A 1 130 ? -12.094 -19.551 -11.711 1.00 102.83 ? 130 ASP A N   1 
ATOM   1068 C CA  . ASP A 1 130 ? -11.043 -19.216 -10.763 1.00 104.01 ? 130 ASP A CA  1 
ATOM   1069 C C   . ASP A 1 130 ? -9.681  -19.283 -11.454 1.00 100.56 ? 130 ASP A C   1 
ATOM   1070 O O   . ASP A 1 130 ? -8.874  -18.366 -11.310 1.00 99.91  ? 130 ASP A O   1 
ATOM   1071 C CB  . ASP A 1 130 ? -11.085 -20.145 -9.546  1.00 109.46 ? 130 ASP A CB  1 
ATOM   1072 C CG  . ASP A 1 130 ? -11.011 -21.625 -9.895  1.00 107.94 ? 130 ASP A CG  1 
ATOM   1073 O OD1 . ASP A 1 130 ? -10.964 -21.944 -11.105 1.00 100.41 ? 130 ASP A OD1 1 
ATOM   1074 O OD2 . ASP A 1 130 ? -11.014 -22.447 -8.955  1.00 110.86 ? 130 ASP A OD2 1 
ATOM   1075 N N   . LEU A 1 131 ? -9.452  -20.365 -12.217 1.00 96.77  ? 131 LEU A N   1 
ATOM   1076 C CA  . LEU A 1 131 ? -8.128  -20.732 -12.703 1.00 90.10  ? 131 LEU A CA  1 
ATOM   1077 C C   . LEU A 1 131 ? -7.681  -19.818 -13.838 1.00 82.41  ? 131 LEU A C   1 
ATOM   1078 O O   . LEU A 1 131 ? -6.521  -19.419 -13.882 1.00 80.29  ? 131 LEU A O   1 
ATOM   1079 C CB  . LEU A 1 131 ? -8.134  -22.188 -13.186 1.00 87.47  ? 131 LEU A CB  1 
ATOM   1080 C CG  . LEU A 1 131 ? -7.936  -23.265 -12.118 1.00 88.70  ? 131 LEU A CG  1 
ATOM   1081 C CD1 . LEU A 1 131 ? -7.986  -24.644 -12.752 1.00 87.74  ? 131 LEU A CD1 1 
ATOM   1082 C CD2 . LEU A 1 131 ? -6.620  -23.090 -11.374 1.00 88.11  ? 131 LEU A CD2 1 
ATOM   1083 N N   . GLU A 1 132 ? -8.594  -19.539 -14.772 1.00 78.54  ? 132 GLU A N   1 
ATOM   1084 C CA  . GLU A 1 132 ? -8.258  -18.782 -15.968 1.00 74.77  ? 132 GLU A CA  1 
ATOM   1085 C C   . GLU A 1 132 ? -7.010  -19.371 -16.616 1.00 69.93  ? 132 GLU A C   1 
ATOM   1086 O O   . GLU A 1 132 ? -6.021  -18.668 -16.828 1.00 69.67  ? 132 GLU A O   1 
ATOM   1087 C CB  . GLU A 1 132 ? -8.006  -17.310 -15.645 1.00 75.43  ? 132 GLU A CB  1 
ATOM   1088 C CG  . GLU A 1 132 ? -9.157  -16.647 -14.926 1.00 78.34  ? 132 GLU A CG  1 
ATOM   1089 C CD  . GLU A 1 132 ? -8.995  -15.143 -14.801 1.00 80.17  ? 132 GLU A CD  1 
ATOM   1090 O OE1 . GLU A 1 132 ? -9.850  -14.529 -14.147 1.00 81.74  ? 132 GLU A OE1 1 
ATOM   1091 O OE2 . GLU A 1 132 ? -8.021  -14.590 -15.374 1.00 81.34  ? 132 GLU A OE2 1 
ATOM   1092 N N   . LEU A 1 133 ? -7.071  -20.673 -16.915 1.00 63.86  ? 133 LEU A N   1 
ATOM   1093 C CA  . LEU A 1 133 ? -6.024  -21.329 -17.676 1.00 58.62  ? 133 LEU A CA  1 
ATOM   1094 C C   . LEU A 1 133 ? -5.978  -20.744 -19.080 1.00 53.42  ? 133 LEU A C   1 
ATOM   1095 O O   . LEU A 1 133 ? -4.930  -20.810 -19.716 1.00 50.87  ? 133 LEU A O   1 
ATOM   1096 C CB  . LEU A 1 133 ? -6.308  -22.829 -17.749 1.00 57.73  ? 133 LEU A CB  1 
ATOM   1097 C CG  . LEU A 1 133 ? -6.370  -23.576 -16.420 1.00 57.45  ? 133 LEU A CG  1 
ATOM   1098 C CD1 . LEU A 1 133 ? -6.697  -25.038 -16.680 1.00 55.75  ? 133 LEU A CD1 1 
ATOM   1099 C CD2 . LEU A 1 133 ? -5.068  -23.429 -15.645 1.00 57.97  ? 133 LEU A CD2 1 
ATOM   1100 N N   . LEU A 1 134 ? -7.141  -20.250 -19.545 1.00 52.69  ? 134 LEU A N   1 
ATOM   1101 C CA  . LEU A 1 134 ? -7.287  -19.514 -20.796 1.00 49.36  ? 134 LEU A CA  1 
ATOM   1102 C C   . LEU A 1 134 ? -7.954  -18.172 -20.520 1.00 51.87  ? 134 LEU A C   1 
ATOM   1103 O O   . LEU A 1 134 ? -9.009  -18.115 -19.880 1.00 54.55  ? 134 LEU A O   1 
ATOM   1104 C CB  . LEU A 1 134 ? -8.158  -20.302 -21.776 1.00 45.89  ? 134 LEU A CB  1 
ATOM   1105 C CG  . LEU A 1 134 ? -7.727  -21.735 -22.072 1.00 45.39  ? 134 LEU A CG  1 
ATOM   1106 C CD1 . LEU A 1 134 ? -8.754  -22.422 -22.959 1.00 44.42  ? 134 LEU A CD1 1 
ATOM   1107 C CD2 . LEU A 1 134 ? -6.344  -21.790 -22.717 1.00 43.80  ? 134 LEU A CD2 1 
ATOM   1108 N N   . ARG A 1 135 ? -7.361  -17.123 -21.094 1.00 51.59  ? 135 ARG A N   1 
ATOM   1109 C CA  . ARG A 1 135 ? -7.767  -15.749 -20.878 1.00 53.31  ? 135 ARG A CA  1 
ATOM   1110 C C   . ARG A 1 135 ? -7.652  -15.023 -22.215 1.00 51.92  ? 135 ARG A C   1 
ATOM   1111 O O   . ARG A 1 135 ? -6.687  -15.230 -22.935 1.00 53.11  ? 135 ARG A O   1 
ATOM   1112 C CB  . ARG A 1 135 ? -6.857  -15.178 -19.790 1.00 57.40  ? 135 ARG A CB  1 
ATOM   1113 C CG  . ARG A 1 135 ? -7.015  -13.692 -19.512 1.00 61.25  ? 135 ARG A CG  1 
ATOM   1114 C CD  . ARG A 1 135 ? -6.043  -13.235 -18.434 1.00 64.73  ? 135 ARG A CD  1 
ATOM   1115 N NE  . ARG A 1 135 ? -4.636  -13.257 -18.843 1.00 63.42  ? 135 ARG A NE  1 
ATOM   1116 C CZ  . ARG A 1 135 ? -3.908  -12.180 -19.154 1.00 62.24  ? 135 ARG A CZ  1 
ATOM   1117 N NH1 . ARG A 1 135 ? -4.496  -11.017 -19.376 1.00 62.00  ? 135 ARG A NH1 1 
ATOM   1118 N NH2 . ARG A 1 135 ? -2.594  -12.280 -19.297 1.00 61.07  ? 135 ARG A NH2 1 
ATOM   1119 N N   . MET A 1 136 ? -8.631  -14.182 -22.550 1.00 53.31  ? 136 MET A N   1 
ATOM   1120 C CA  . MET A 1 136 ? -8.713  -13.594 -23.876 1.00 52.64  ? 136 MET A CA  1 
ATOM   1121 C C   . MET A 1 136 ? -9.055  -12.114 -23.778 1.00 52.75  ? 136 MET A C   1 
ATOM   1122 O O   . MET A 1 136 ? -9.898  -11.724 -22.981 1.00 56.27  ? 136 MET A O   1 
ATOM   1123 C CB  . MET A 1 136 ? -9.816  -14.288 -24.675 1.00 55.57  ? 136 MET A CB  1 
ATOM   1124 C CG  . MET A 1 136 ? -10.014 -13.730 -26.074 1.00 57.17  ? 136 MET A CG  1 
ATOM   1125 S SD  . MET A 1 136 ? -11.319 -14.632 -26.937 1.00 58.73  ? 136 MET A SD  1 
ATOM   1126 C CE  . MET A 1 136 ? -12.707 -13.921 -26.051 1.00 62.87  ? 136 MET A CE  1 
ATOM   1127 N N   . GLU A 1 137 ? -8.435  -11.294 -24.625 1.00 51.26  ? 137 GLU A N   1 
ATOM   1128 C CA  . GLU A 1 137 ? -8.732  -9.873  -24.647 1.00 51.53  ? 137 GLU A CA  1 
ATOM   1129 C C   . GLU A 1 137 ? -8.315  -9.284  -25.995 1.00 49.58  ? 137 GLU A C   1 
ATOM   1130 O O   . GLU A 1 137 ? -7.561  -9.902  -26.753 1.00 45.47  ? 137 GLU A O   1 
ATOM   1131 C CB  . GLU A 1 137 ? -8.066  -9.175  -23.461 1.00 53.71  ? 137 GLU A CB  1 
ATOM   1132 C CG  . GLU A 1 137 ? -6.561  -9.357  -23.409 1.00 54.94  ? 137 GLU A CG  1 
ATOM   1133 C CD  . GLU A 1 137 ? -5.882  -8.746  -22.190 1.00 59.46  ? 137 GLU A CD  1 
ATOM   1134 O OE1 . GLU A 1 137 ? -6.344  -9.011  -21.066 1.00 64.57  ? 137 GLU A OE1 1 
ATOM   1135 O OE2 . GLU A 1 137 ? -4.880  -8.020  -22.359 1.00 61.09  ? 137 GLU A OE2 1 
ATOM   1136 N N   . LYS A 1 138 ? -8.881  -8.104  -26.285 1.00 49.70  ? 138 LYS A N   1 
ATOM   1137 C CA  . LYS A 1 138 ? -8.601  -7.354  -27.494 1.00 49.15  ? 138 LYS A CA  1 
ATOM   1138 C C   . LYS A 1 138 ? -7.109  -7.015  -27.498 1.00 49.70  ? 138 LYS A C   1 
ATOM   1139 O O   . LYS A 1 138 ? -6.579  -6.496  -26.514 1.00 51.36  ? 138 LYS A O   1 
ATOM   1140 C CB  . LYS A 1 138 ? -9.497  -6.108  -27.527 1.00 51.92  ? 138 LYS A CB  1 
ATOM   1141 C CG  . LYS A 1 138 ? -9.564  -5.350  -28.849 1.00 53.52  ? 138 LYS A CG  1 
ATOM   1142 C CD  . LYS A 1 138 ? -10.294 -6.094  -29.971 1.00 53.58  ? 138 LYS A CD  1 
ATOM   1143 C CE  . LYS A 1 138 ? -10.114 -5.454  -31.332 1.00 53.60  ? 138 LYS A CE  1 
ATOM   1144 N NZ  . LYS A 1 138 ? -10.779 -6.251  -32.385 1.00 54.62  ? 138 LYS A NZ  1 
ATOM   1145 N N   . LYS A 1 139 ? -6.427  -7.341  -28.602 1.00 47.62  ? 139 LYS A N   1 
ATOM   1146 C CA  . LYS A 1 139 ? -4.993  -7.142  -28.686 1.00 48.04  ? 139 LYS A CA  1 
ATOM   1147 C C   . LYS A 1 139 ? -4.474  -7.410  -30.099 1.00 47.63  ? 139 LYS A C   1 
ATOM   1148 O O   . LYS A 1 139 ? -4.674  -8.486  -30.649 1.00 48.03  ? 139 LYS A O   1 
ATOM   1149 C CB  . LYS A 1 139 ? -4.285  -8.064  -27.691 1.00 48.18  ? 139 LYS A CB  1 
ATOM   1150 C CG  . LYS A 1 139 ? -2.768  -7.919  -27.662 1.00 48.84  ? 139 LYS A CG  1 
ATOM   1151 C CD  . LYS A 1 139 ? -2.194  -8.002  -26.264 1.00 49.36  ? 139 LYS A CD  1 
ATOM   1152 C CE  . LYS A 1 139 ? -2.404  -6.724  -25.491 1.00 51.40  ? 139 LYS A CE  1 
ATOM   1153 N NZ  . LYS A 1 139 ? -2.737  -7.013  -24.083 1.00 52.87  ? 139 LYS A NZ  1 
ATOM   1154 N N   . THR A 1 140 ? -3.756  -6.432  -30.663 1.00 48.73  ? 140 THR A N   1 
ATOM   1155 C CA  . THR A 1 140 ? -3.019  -6.625  -31.899 1.00 46.64  ? 140 THR A CA  1 
ATOM   1156 C C   . THR A 1 140 ? -1.767  -7.438  -31.603 1.00 44.62  ? 140 THR A C   1 
ATOM   1157 O O   . THR A 1 140 ? -1.425  -7.647  -30.440 1.00 44.08  ? 140 THR A O   1 
ATOM   1158 C CB  . THR A 1 140 ? -2.596  -5.304  -32.570 1.00 48.05  ? 140 THR A CB  1 
ATOM   1159 O OG1 . THR A 1 140 ? -1.580  -4.657  -31.794 1.00 48.75  ? 140 THR A OG1 1 
ATOM   1160 C CG2 . THR A 1 140 ? -3.769  -4.380  -32.826 1.00 48.48  ? 140 THR A CG2 1 
ATOM   1161 N N   . LEU A 1 141 ? -1.070  -7.822  -32.679 1.00 43.80  ? 141 LEU A N   1 
ATOM   1162 C CA  . LEU A 1 141 ? 0.077   -8.704  -32.599 1.00 43.39  ? 141 LEU A CA  1 
ATOM   1163 C C   . LEU A 1 141 ? 1.311   -7.933  -32.130 1.00 47.23  ? 141 LEU A C   1 
ATOM   1164 O O   . LEU A 1 141 ? 2.098   -8.444  -31.338 1.00 51.49  ? 141 LEU A O   1 
ATOM   1165 C CB  . LEU A 1 141 ? 0.264   -9.351  -33.971 1.00 41.33  ? 141 LEU A CB  1 
ATOM   1166 C CG  . LEU A 1 141 ? 1.372   -10.396 -34.072 1.00 40.32  ? 141 LEU A CG  1 
ATOM   1167 C CD1 . LEU A 1 141 ? 1.275   -11.420 -32.952 1.00 39.13  ? 141 LEU A CD1 1 
ATOM   1168 C CD2 . LEU A 1 141 ? 1.329   -11.077 -35.440 1.00 39.21  ? 141 LEU A CD2 1 
ATOM   1169 N N   . ASN A 1 142 ? 1.462   -6.686  -32.571 1.00 49.87  ? 142 ASN A N   1 
ATOM   1170 C CA  . ASN A 1 142 ? 2.553   -5.852  -32.095 1.00 52.24  ? 142 ASN A CA  1 
ATOM   1171 C C   . ASN A 1 142 ? 2.373   -5.500  -30.623 1.00 53.44  ? 142 ASN A C   1 
ATOM   1172 O O   . ASN A 1 142 ? 3.355   -5.433  -29.885 1.00 57.48  ? 142 ASN A O   1 
ATOM   1173 C CB  . ASN A 1 142 ? 2.688   -4.547  -32.878 1.00 54.25  ? 142 ASN A CB  1 
ATOM   1174 C CG  . ASN A 1 142 ? 3.581   -4.654  -34.095 1.00 55.25  ? 142 ASN A CG  1 
ATOM   1175 O OD1 . ASN A 1 142 ? 4.742   -5.108  -34.023 1.00 56.37  ? 142 ASN A OD1 1 
ATOM   1176 N ND2 . ASN A 1 142 ? 3.054   -4.205  -35.222 1.00 55.98  ? 142 ASN A ND2 1 
ATOM   1177 N N   . GLU A 1 143 ? 1.137   -5.191  -30.227 1.00 53.55  ? 143 GLU A N   1 
ATOM   1178 C CA  . GLU A 1 143 ? 0.812   -4.977  -28.826 1.00 56.37  ? 143 GLU A CA  1 
ATOM   1179 C C   . GLU A 1 143 ? 1.223   -6.212  -28.015 1.00 55.71  ? 143 GLU A C   1 
ATOM   1180 O O   . GLU A 1 143 ? 1.772   -6.089  -26.918 1.00 56.79  ? 143 GLU A O   1 
ATOM   1181 C CB  . GLU A 1 143 ? -0.670  -4.604  -28.709 1.00 58.29  ? 143 GLU A CB  1 
ATOM   1182 C CG  . GLU A 1 143 ? -0.947  -3.177  -29.171 1.00 63.61  ? 143 GLU A CG  1 
ATOM   1183 C CD  . GLU A 1 143 ? -2.398  -2.746  -29.371 1.00 64.75  ? 143 GLU A CD  1 
ATOM   1184 O OE1 . GLU A 1 143 ? -2.606  -1.547  -29.714 1.00 66.14  ? 143 GLU A OE1 1 
ATOM   1185 O OE2 . GLU A 1 143 ? -3.316  -3.598  -29.207 1.00 58.21  ? 143 GLU A OE2 1 
ATOM   1186 N N   . LEU A 1 144 ? 0.998   -7.403  -28.584 1.00 52.35  ? 144 LEU A N   1 
ATOM   1187 C CA  . LEU A 1 144 ? 1.329   -8.652  -27.919 1.00 51.40  ? 144 LEU A CA  1 
ATOM   1188 C C   . LEU A 1 144 ? 2.842   -8.860  -27.857 1.00 51.08  ? 144 LEU A C   1 
ATOM   1189 O O   . LEU A 1 144 ? 3.365   -9.341  -26.842 1.00 51.37  ? 144 LEU A O   1 
ATOM   1190 C CB  . LEU A 1 144 ? 0.661   -9.815  -28.663 1.00 49.16  ? 144 LEU A CB  1 
ATOM   1191 C CG  . LEU A 1 144 ? 1.311   -11.176 -28.409 1.00 49.91  ? 144 LEU A CG  1 
ATOM   1192 C CD1 . LEU A 1 144 ? 1.269   -11.558 -26.927 1.00 50.84  ? 144 LEU A CD1 1 
ATOM   1193 C CD2 . LEU A 1 144 ? 0.661   -12.256 -29.251 1.00 48.66  ? 144 LEU A CD2 1 
ATOM   1194 N N   . ILE A 1 145 ? 3.508   -8.582  -28.986 1.00 49.12  ? 145 ILE A N   1 
ATOM   1195 C CA  . ILE A 1 145 ? 4.950   -8.702  -29.093 1.00 49.51  ? 145 ILE A CA  1 
ATOM   1196 C C   . ILE A 1 145 ? 5.620   -7.735  -28.126 1.00 51.47  ? 145 ILE A C   1 
ATOM   1197 O O   . ILE A 1 145 ? 6.691   -8.021  -27.600 1.00 51.41  ? 145 ILE A O   1 
ATOM   1198 C CB  . ILE A 1 145 ? 5.410   -8.453  -30.537 1.00 48.24  ? 145 ILE A CB  1 
ATOM   1199 C CG1 . ILE A 1 145 ? 4.939   -9.582  -31.452 1.00 47.16  ? 145 ILE A CG1 1 
ATOM   1200 C CG2 . ILE A 1 145 ? 6.914   -8.281  -30.599 1.00 49.19  ? 145 ILE A CG2 1 
ATOM   1201 C CD1 . ILE A 1 145 ? 4.792   -9.162  -32.893 1.00 48.02  ? 145 ILE A CD1 1 
ATOM   1202 N N   . GLU A 1 146 ? 4.985   -6.587  -27.926 1.00 53.12  ? 146 GLU A N   1 
ATOM   1203 C CA  . GLU A 1 146 ? 5.482   -5.611  -26.982 1.00 58.19  ? 146 GLU A CA  1 
ATOM   1204 C C   . GLU A 1 146 ? 5.513   -6.238  -25.594 1.00 57.37  ? 146 GLU A C   1 
ATOM   1205 O O   . GLU A 1 146 ? 6.526   -6.184  -24.910 1.00 59.26  ? 146 GLU A O   1 
ATOM   1206 C CB  . GLU A 1 146 ? 4.597   -4.365  -26.994 1.00 62.32  ? 146 GLU A CB  1 
ATOM   1207 C CG  . GLU A 1 146 ? 5.238   -3.191  -26.285 1.00 67.45  ? 146 GLU A CG  1 
ATOM   1208 C CD  . GLU A 1 146 ? 4.384   -1.941  -26.194 1.00 70.93  ? 146 GLU A CD  1 
ATOM   1209 O OE1 . GLU A 1 146 ? 3.214   -1.963  -26.680 1.00 71.95  ? 146 GLU A OE1 1 
ATOM   1210 O OE2 . GLU A 1 146 ? 4.896   -0.946  -25.629 1.00 72.80  ? 146 GLU A OE2 1 
ATOM   1211 N N   . GLU A 1 147 ? 4.389   -6.828  -25.194 1.00 56.14  ? 147 GLU A N   1 
ATOM   1212 C CA  . GLU A 1 147 ? 4.255   -7.412  -23.875 1.00 56.74  ? 147 GLU A CA  1 
ATOM   1213 C C   . GLU A 1 147 ? 5.341   -8.446  -23.640 1.00 54.91  ? 147 GLU A C   1 
ATOM   1214 O O   . GLU A 1 147 ? 5.950   -8.465  -22.573 1.00 57.53  ? 147 GLU A O   1 
ATOM   1215 C CB  . GLU A 1 147 ? 2.914   -8.115  -23.727 1.00 57.96  ? 147 GLU A CB  1 
ATOM   1216 C CG  . GLU A 1 147 ? 1.751   -7.161  -23.597 1.00 60.40  ? 147 GLU A CG  1 
ATOM   1217 C CD  . GLU A 1 147 ? 0.469   -7.863  -23.196 1.00 62.15  ? 147 GLU A CD  1 
ATOM   1218 O OE1 . GLU A 1 147 ? 0.495   -9.110  -23.006 1.00 64.40  ? 147 GLU A OE1 1 
ATOM   1219 O OE2 . GLU A 1 147 ? -0.547  -7.167  -23.067 1.00 64.78  ? 147 GLU A OE2 1 
ATOM   1220 N N   . ILE A 1 148 ? 5.564   -9.309  -24.636 1.00 51.56  ? 148 ILE A N   1 
ATOM   1221 C CA  . ILE A 1 148 ? 6.594   -10.330 -24.526 1.00 49.94  ? 148 ILE A CA  1 
ATOM   1222 C C   . ILE A 1 148 ? 7.965   -9.691  -24.315 1.00 51.17  ? 148 ILE A C   1 
ATOM   1223 O O   . ILE A 1 148 ? 8.765   -10.215 -23.550 1.00 51.51  ? 148 ILE A O   1 
ATOM   1224 C CB  . ILE A 1 148 ? 6.597   -11.240 -25.761 1.00 47.32  ? 148 ILE A CB  1 
ATOM   1225 C CG1 . ILE A 1 148 ? 5.318   -12.073 -25.831 1.00 45.53  ? 148 ILE A CG1 1 
ATOM   1226 C CG2 . ILE A 1 148 ? 7.846   -12.107 -25.770 1.00 47.85  ? 148 ILE A CG2 1 
ATOM   1227 C CD1 . ILE A 1 148 ? 5.071   -12.734 -27.173 1.00 43.73  ? 148 ILE A CD1 1 
ATOM   1228 N N   . ASN A 1 149 ? 8.225   -8.586  -25.028 1.00 51.66  ? 149 ASN A N   1 
ATOM   1229 C CA  . ASN A 1 149 ? 9.512   -7.915  -25.022 1.00 53.00  ? 149 ASN A CA  1 
ATOM   1230 C C   . ASN A 1 149 ? 10.609  -8.926  -25.354 1.00 53.18  ? 149 ASN A C   1 
ATOM   1231 O O   . ASN A 1 149 ? 11.477  -9.216  -24.531 1.00 54.46  ? 149 ASN A O   1 
ATOM   1232 C CB  . ASN A 1 149 ? 9.738   -7.207  -23.691 1.00 55.34  ? 149 ASN A CB  1 
ATOM   1233 C CG  . ASN A 1 149 ? 10.996  -6.374  -23.688 1.00 58.23  ? 149 ASN A CG  1 
ATOM   1234 O OD1 . ASN A 1 149 ? 11.751  -6.375  -24.653 1.00 59.01  ? 149 ASN A OD1 1 
ATOM   1235 N ND2 . ASN A 1 149 ? 11.238  -5.658  -22.608 1.00 61.08  ? 149 ASN A ND2 1 
ATOM   1236 N N   . PRO A 1 150 ? 10.589  -9.519  -26.565 1.00 52.88  ? 150 PRO A N   1 
ATOM   1237 C CA  . PRO A 1 150 ? 11.542  -10.553 -26.944 1.00 53.51  ? 150 PRO A CA  1 
ATOM   1238 C C   . PRO A 1 150 ? 12.787  -9.936  -27.552 1.00 56.75  ? 150 PRO A C   1 
ATOM   1239 O O   . PRO A 1 150 ? 12.745  -8.783  -27.990 1.00 59.38  ? 150 PRO A O   1 
ATOM   1240 C CB  . PRO A 1 150 ? 10.785  -11.319 -28.029 1.00 51.44  ? 150 PRO A CB  1 
ATOM   1241 C CG  . PRO A 1 150 ? 10.010  -10.233 -28.741 1.00 51.40  ? 150 PRO A CG  1 
ATOM   1242 C CD  . PRO A 1 150 ? 9.642   -9.235  -27.655 1.00 52.58  ? 150 PRO A CD  1 
ATOM   1243 N N   . ASP A 1 151 ? 13.870  -10.724 -27.582 1.00 56.82  ? 151 ASP A N   1 
ATOM   1244 C CA  . ASP A 1 151 ? 15.141  -10.258 -28.109 1.00 58.59  ? 151 ASP A CA  1 
ATOM   1245 C C   . ASP A 1 151 ? 15.286  -10.672 -29.579 1.00 57.44  ? 151 ASP A C   1 
ATOM   1246 O O   . ASP A 1 151 ? 16.255  -10.279 -30.230 1.00 61.17  ? 151 ASP A O   1 
ATOM   1247 C CB  . ASP A 1 151 ? 16.305  -10.706 -27.220 1.00 60.66  ? 151 ASP A CB  1 
ATOM   1248 C CG  . ASP A 1 151 ? 16.431  -12.205 -27.010 1.00 59.84  ? 151 ASP A CG  1 
ATOM   1249 O OD1 . ASP A 1 151 ? 15.599  -12.939 -27.562 1.00 58.26  ? 151 ASP A OD1 1 
ATOM   1250 O OD2 . ASP A 1 151 ? 17.365  -12.631 -26.292 1.00 61.34  ? 151 ASP A OD2 1 
ATOM   1251 N N   . VAL A 1 152 ? 14.325  -11.435 -30.121 1.00 52.78  ? 152 VAL A N   1 
ATOM   1252 C CA  . VAL A 1 152 ? 14.300  -11.703 -31.552 1.00 50.98  ? 152 VAL A CA  1 
ATOM   1253 C C   . VAL A 1 152 ? 12.919  -12.205 -31.924 1.00 47.79  ? 152 VAL A C   1 
ATOM   1254 O O   . VAL A 1 152 ? 12.264  -12.873 -31.128 1.00 47.00  ? 152 VAL A O   1 
ATOM   1255 C CB  . VAL A 1 152 ? 15.360  -12.733 -32.000 1.00 51.78  ? 152 VAL A CB  1 
ATOM   1256 C CG1 . VAL A 1 152 ? 15.134  -14.115 -31.380 1.00 50.37  ? 152 VAL A CG1 1 
ATOM   1257 C CG2 . VAL A 1 152 ? 15.427  -12.837 -33.522 1.00 51.10  ? 152 VAL A CG2 1 
ATOM   1258 N N   . VAL A 1 153 ? 12.519  -11.917 -33.162 1.00 47.10  ? 153 VAL A N   1 
ATOM   1259 C CA  . VAL A 1 153 ? 11.220  -12.333 -33.657 1.00 45.10  ? 153 VAL A CA  1 
ATOM   1260 C C   . VAL A 1 153 ? 11.424  -13.108 -34.956 1.00 45.14  ? 153 VAL A C   1 
ATOM   1261 O O   . VAL A 1 153 ? 12.124  -12.651 -35.854 1.00 46.70  ? 153 VAL A O   1 
ATOM   1262 C CB  . VAL A 1 153 ? 10.279  -11.123 -33.818 1.00 44.31  ? 153 VAL A CB  1 
ATOM   1263 C CG1 . VAL A 1 153 ? 9.026   -11.474 -34.611 1.00 42.76  ? 153 VAL A CG1 1 
ATOM   1264 C CG2 . VAL A 1 153 ? 9.903   -10.534 -32.462 1.00 43.84  ? 153 VAL A CG2 1 
ATOM   1265 N N   . PHE A 1 154 ? 10.847  -14.307 -35.023 1.00 43.74  ? 154 PHE A N   1 
ATOM   1266 C CA  . PHE A 1 154 ? 10.949  -15.106 -36.224 1.00 44.68  ? 154 PHE A CA  1 
ATOM   1267 C C   . PHE A 1 154 ? 9.548   -15.316 -36.773 1.00 43.90  ? 154 PHE A C   1 
ATOM   1268 O O   . PHE A 1 154 ? 8.627   -15.600 -36.007 1.00 43.65  ? 154 PHE A O   1 
ATOM   1269 C CB  . PHE A 1 154 ? 11.628  -16.441 -35.933 1.00 44.64  ? 154 PHE A CB  1 
ATOM   1270 C CG  . PHE A 1 154 ? 13.106  -16.347 -35.679 1.00 46.45  ? 154 PHE A CG  1 
ATOM   1271 C CD1 . PHE A 1 154 ? 13.988  -16.095 -36.716 1.00 48.88  ? 154 PHE A CD1 1 
ATOM   1272 C CD2 . PHE A 1 154 ? 13.618  -16.501 -34.401 1.00 46.76  ? 154 PHE A CD2 1 
ATOM   1273 C CE1 . PHE A 1 154 ? 15.359  -16.024 -36.481 1.00 51.58  ? 154 PHE A CE1 1 
ATOM   1274 C CE2 . PHE A 1 154 ? 14.983  -16.414 -34.167 1.00 49.08  ? 154 PHE A CE2 1 
ATOM   1275 C CZ  . PHE A 1 154 ? 15.854  -16.180 -35.205 1.00 51.14  ? 154 PHE A CZ  1 
ATOM   1276 N N   . ILE A 1 155 ? 9.421   -15.177 -38.099 1.00 44.64  ? 155 ILE A N   1 
ATOM   1277 C CA  . ILE A 1 155 ? 8.140   -15.301 -38.763 1.00 43.87  ? 155 ILE A CA  1 
ATOM   1278 C C   . ILE A 1 155 ? 8.233   -16.472 -39.731 1.00 44.37  ? 155 ILE A C   1 
ATOM   1279 O O   . ILE A 1 155 ? 8.867   -16.389 -40.775 1.00 45.85  ? 155 ILE A O   1 
ATOM   1280 C CB  . ILE A 1 155 ? 7.738   -13.975 -39.441 1.00 44.86  ? 155 ILE A CB  1 
ATOM   1281 C CG1 . ILE A 1 155 ? 7.740   -12.834 -38.420 1.00 45.64  ? 155 ILE A CG1 1 
ATOM   1282 C CG2 . ILE A 1 155 ? 6.389   -14.098 -40.137 1.00 43.85  ? 155 ILE A CG2 1 
ATOM   1283 C CD1 . ILE A 1 155 ? 7.562   -11.456 -39.005 1.00 47.21  ? 155 ILE A CD1 1 
ATOM   1284 N N   . MET A 1 156 ? 7.580   -17.573 -39.369 1.00 43.92  ? 156 MET A N   1 
ATOM   1285 C CA  . MET A 1 156 ? 7.630   -18.769 -40.187 1.00 44.68  ? 156 MET A CA  1 
ATOM   1286 C C   . MET A 1 156 ? 6.783   -18.504 -41.434 1.00 48.55  ? 156 MET A C   1 
ATOM   1287 O O   . MET A 1 156 ? 5.578   -18.241 -41.349 1.00 46.91  ? 156 MET A O   1 
ATOM   1288 C CB  . MET A 1 156 ? 7.135   -19.980 -39.392 1.00 40.61  ? 156 MET A CB  1 
ATOM   1289 C CG  . MET A 1 156 ? 7.802   -20.108 -38.020 1.00 39.40  ? 156 MET A CG  1 
ATOM   1290 S SD  . MET A 1 156 ? 9.626   -19.980 -38.005 1.00 40.94  ? 156 MET A SD  1 
ATOM   1291 C CE  . MET A 1 156 ? 10.101  -21.174 -39.252 1.00 41.95  ? 156 MET A CE  1 
ATOM   1292 N N   . HIS A 1 157 ? 7.462   -18.524 -42.587 1.00 54.38  ? 157 HIS A N   1 
ATOM   1293 C CA  . HIS A 1 157 ? 6.936   -17.990 -43.830 1.00 59.01  ? 157 HIS A CA  1 
ATOM   1294 C C   . HIS A 1 157 ? 7.612   -18.716 -44.985 1.00 62.41  ? 157 HIS A C   1 
ATOM   1295 O O   . HIS A 1 157 ? 8.833   -18.872 -44.993 1.00 61.84  ? 157 HIS A O   1 
ATOM   1296 C CB  . HIS A 1 157 ? 7.266   -16.498 -43.927 1.00 64.20  ? 157 HIS A CB  1 
ATOM   1297 C CG  . HIS A 1 157 ? 6.454   -15.732 -44.910 1.00 68.47  ? 157 HIS A CG  1 
ATOM   1298 N ND1 . HIS A 1 157 ? 6.228   -16.147 -46.203 1.00 75.00  ? 157 HIS A ND1 1 
ATOM   1299 C CD2 . HIS A 1 157 ? 5.815   -14.561 -44.773 1.00 68.71  ? 157 HIS A CD2 1 
ATOM   1300 C CE1 . HIS A 1 157 ? 5.477   -15.244 -46.821 1.00 75.89  ? 157 HIS A CE1 1 
ATOM   1301 N NE2 . HIS A 1 157 ? 5.199   -14.282 -45.962 1.00 71.97  ? 157 HIS A NE2 1 
ATOM   1302 N N   . GLU A 1 158 ? 6.813   -19.112 -45.977 1.00 66.58  ? 158 GLU A N   1 
ATOM   1303 C CA  . GLU A 1 158 ? 7.290   -19.933 -47.074 1.00 72.28  ? 158 GLU A CA  1 
ATOM   1304 C C   . GLU A 1 158 ? 8.361   -19.206 -47.888 1.00 74.77  ? 158 GLU A C   1 
ATOM   1305 O O   . GLU A 1 158 ? 9.169   -19.848 -48.560 1.00 77.16  ? 158 GLU A O   1 
ATOM   1306 C CB  . GLU A 1 158 ? 6.114   -20.307 -47.968 1.00 78.34  ? 158 GLU A CB  1 
ATOM   1307 C CG  . GLU A 1 158 ? 6.521   -21.140 -49.163 1.00 90.03  ? 158 GLU A CG  1 
ATOM   1308 C CD  . GLU A 1 158 ? 5.345   -21.662 -49.967 1.00 97.59  ? 158 GLU A CD  1 
ATOM   1309 O OE1 . GLU A 1 158 ? 5.604   -22.347 -50.984 1.00 104.68 ? 158 GLU A OE1 1 
ATOM   1310 O OE2 . GLU A 1 158 ? 4.177   -21.370 -49.577 1.00 90.57  ? 158 GLU A OE2 1 
ATOM   1311 N N   . GLU A 1 159 ? 8.368   -17.871 -47.810 1.00 72.41  ? 159 GLU A N   1 
ATOM   1312 C CA  . GLU A 1 159 ? 9.186   -17.051 -48.680 1.00 74.27  ? 159 GLU A CA  1 
ATOM   1313 C C   . GLU A 1 159 ? 10.389  -16.502 -47.922 1.00 71.66  ? 159 GLU A C   1 
ATOM   1314 O O   . GLU A 1 159 ? 11.035  -15.560 -48.375 1.00 73.80  ? 159 GLU A O   1 
ATOM   1315 C CB  . GLU A 1 159 ? 8.311   -15.930 -49.222 1.00 78.78  ? 159 GLU A CB  1 
ATOM   1316 C CG  . GLU A 1 159 ? 7.031   -16.450 -49.836 1.00 81.62  ? 159 GLU A CG  1 
ATOM   1317 C CD  . GLU A 1 159 ? 6.167   -15.380 -50.479 1.00 85.95  ? 159 GLU A CD  1 
ATOM   1318 O OE1 . GLU A 1 159 ? 4.979   -15.282 -50.079 1.00 86.61  ? 159 GLU A OE1 1 
ATOM   1319 O OE2 . GLU A 1 159 ? 6.683   -14.648 -51.376 1.00 83.24  ? 159 GLU A OE2 1 
ATOM   1320 N N   . GLY A 1 160 ? 10.694  -17.103 -46.774 1.00 67.45  ? 160 GLY A N   1 
ATOM   1321 C CA  . GLY A 1 160 ? 11.789  -16.642 -45.943 1.00 67.65  ? 160 GLY A CA  1 
ATOM   1322 C C   . GLY A 1 160 ? 13.099  -17.355 -46.260 1.00 68.80  ? 160 GLY A C   1 
ATOM   1323 O O   . GLY A 1 160 ? 13.126  -18.243 -47.108 1.00 67.16  ? 160 GLY A O   1 
ATOM   1324 N N   . GLU A 1 161 ? 14.162  -16.912 -45.563 1.00 71.99  ? 161 GLU A N   1 
ATOM   1325 C CA  . GLU A 1 161 ? 15.507  -17.480 -45.576 1.00 75.63  ? 161 GLU A CA  1 
ATOM   1326 C C   . GLU A 1 161 ? 15.442  -18.954 -45.199 1.00 77.39  ? 161 GLU A C   1 
ATOM   1327 O O   . GLU A 1 161 ? 14.938  -19.277 -44.118 1.00 77.21  ? 161 GLU A O   1 
ATOM   1328 C CB  . GLU A 1 161 ? 16.364  -16.725 -44.551 1.00 76.04  ? 161 GLU A CB  1 
ATOM   1329 C CG  . GLU A 1 161 ? 17.696  -17.372 -44.208 1.00 77.10  ? 161 GLU A CG  1 
ATOM   1330 C CD  . GLU A 1 161 ? 18.808  -17.092 -45.199 1.00 80.94  ? 161 GLU A CD  1 
ATOM   1331 O OE1 . GLU A 1 161 ? 19.083  -15.904 -45.435 1.00 80.69  ? 161 GLU A OE1 1 
ATOM   1332 O OE2 . GLU A 1 161 ? 19.393  -18.067 -45.729 1.00 84.36  ? 161 GLU A OE2 1 
ATOM   1333 N N   . LEU A 1 162 ? 15.944  -19.845 -46.070 1.00 79.11  ? 162 LEU A N   1 
ATOM   1334 C CA  . LEU A 1 162 ? 15.702  -21.262 -45.840 1.00 77.49  ? 162 LEU A CA  1 
ATOM   1335 C C   . LEU A 1 162 ? 16.653  -21.788 -44.782 1.00 76.04  ? 162 LEU A C   1 
ATOM   1336 O O   . LEU A 1 162 ? 17.840  -21.495 -44.800 1.00 76.94  ? 162 LEU A O   1 
ATOM   1337 C CB  . LEU A 1 162 ? 15.886  -22.094 -47.102 1.00 78.82  ? 162 LEU A CB  1 
ATOM   1338 C CG  . LEU A 1 162 ? 15.544  -23.577 -46.930 1.00 78.18  ? 162 LEU A CG  1 
ATOM   1339 C CD1 . LEU A 1 162 ? 14.060  -23.818 -47.163 1.00 76.87  ? 162 LEU A CD1 1 
ATOM   1340 C CD2 . LEU A 1 162 ? 16.385  -24.489 -47.814 1.00 80.32  ? 162 LEU A CD2 1 
ATOM   1341 N N   . MET A 1 163 ? 16.111  -22.630 -43.909 1.00 75.16  ? 163 MET A N   1 
ATOM   1342 C CA  . MET A 1 163 ? 16.943  -23.301 -42.934 1.00 76.85  ? 163 MET A CA  1 
ATOM   1343 C C   . MET A 1 163 ? 16.539  -24.771 -42.814 1.00 75.92  ? 163 MET A C   1 
ATOM   1344 O O   . MET A 1 163 ? 15.373  -25.137 -42.954 1.00 71.51  ? 163 MET A O   1 
ATOM   1345 C CB  . MET A 1 163 ? 16.832  -22.595 -41.582 1.00 74.08  ? 163 MET A CB  1 
ATOM   1346 C CG  . MET A 1 163 ? 17.649  -21.333 -41.530 1.00 73.60  ? 163 MET A CG  1 
ATOM   1347 S SD  . MET A 1 163 ? 17.576  -20.619 -39.893 1.00 72.26  ? 163 MET A SD  1 
ATOM   1348 C CE  . MET A 1 163 ? 18.889  -21.534 -39.085 1.00 75.36  ? 163 MET A CE  1 
ATOM   1349 N N   . ILE A 1 164 ? 17.561  -25.606 -42.619 1.00 77.85  ? 164 ILE A N   1 
ATOM   1350 C CA  . ILE A 1 164 ? 17.389  -26.903 -41.999 1.00 75.49  ? 164 ILE A CA  1 
ATOM   1351 C C   . ILE A 1 164 ? 16.799  -26.663 -40.615 1.00 70.31  ? 164 ILE A C   1 
ATOM   1352 O O   . ILE A 1 164 ? 17.285  -25.821 -39.855 1.00 68.36  ? 164 ILE A O   1 
ATOM   1353 C CB  . ILE A 1 164 ? 18.725  -27.663 -41.912 1.00 80.72  ? 164 ILE A CB  1 
ATOM   1354 C CG1 . ILE A 1 164 ? 19.439  -27.760 -43.267 1.00 85.32  ? 164 ILE A CG1 1 
ATOM   1355 C CG2 . ILE A 1 164 ? 18.513  -29.019 -41.262 1.00 80.57  ? 164 ILE A CG2 1 
ATOM   1356 C CD1 . ILE A 1 164 ? 18.545  -28.129 -44.435 1.00 86.20  ? 164 ILE A CD1 1 
ATOM   1357 N N   . PRO A 1 165 ? 15.714  -27.383 -40.270 1.00 66.58  ? 165 PRO A N   1 
ATOM   1358 C CA  . PRO A 1 165 ? 15.085  -27.268 -38.955 1.00 63.13  ? 165 PRO A CA  1 
ATOM   1359 C C   . PRO A 1 165 ? 16.071  -27.438 -37.804 1.00 64.58  ? 165 PRO A C   1 
ATOM   1360 O O   . PRO A 1 165 ? 16.013  -26.671 -36.842 1.00 63.96  ? 165 PRO A O   1 
ATOM   1361 C CB  . PRO A 1 165 ? 14.083  -28.428 -38.943 1.00 61.99  ? 165 PRO A CB  1 
ATOM   1362 C CG  . PRO A 1 165 ? 13.751  -28.658 -40.403 1.00 62.72  ? 165 PRO A CG  1 
ATOM   1363 C CD  . PRO A 1 165 ? 15.030  -28.347 -41.144 1.00 66.60  ? 165 PRO A CD  1 
ATOM   1364 N N   . LYS A 1 166 ? 16.949  -28.453 -37.937 1.00 64.91  ? 166 LYS A N   1 
ATOM   1365 C CA  . LYS A 1 166 ? 17.992  -28.753 -36.968 1.00 63.23  ? 166 LYS A CA  1 
ATOM   1366 C C   . LYS A 1 166 ? 18.634  -27.430 -36.581 1.00 60.17  ? 166 LYS A C   1 
ATOM   1367 O O   . LYS A 1 166 ? 18.731  -27.097 -35.405 1.00 58.94  ? 166 LYS A O   1 
ATOM   1368 C CB  . LYS A 1 166 ? 19.009  -29.760 -37.543 1.00 68.13  ? 166 LYS A CB  1 
ATOM   1369 C CG  . LYS A 1 166 ? 20.047  -30.291 -36.553 1.00 70.08  ? 166 LYS A CG  1 
ATOM   1370 C CD  . LYS A 1 166 ? 20.935  -31.451 -37.021 1.00 72.95  ? 166 LYS A CD  1 
ATOM   1371 C CE  . LYS A 1 166 ? 22.171  -31.581 -36.139 1.00 75.74  ? 166 LYS A CE  1 
ATOM   1372 N NZ  . LYS A 1 166 ? 22.932  -32.838 -36.331 1.00 76.71  ? 166 LYS A NZ  1 
ATOM   1373 N N   . ASN A 1 167 ? 18.969  -26.656 -37.615 1.00 59.53  ? 167 ASN A N   1 
ATOM   1374 C CA  . ASN A 1 167 ? 19.821  -25.488 -37.498 1.00 60.08  ? 167 ASN A CA  1 
ATOM   1375 C C   . ASN A 1 167 ? 19.062  -24.335 -36.876 1.00 58.67  ? 167 ASN A C   1 
ATOM   1376 O O   . ASN A 1 167 ? 19.649  -23.554 -36.128 1.00 61.30  ? 167 ASN A O   1 
ATOM   1377 C CB  . ASN A 1 167 ? 20.340  -25.008 -38.852 1.00 60.88  ? 167 ASN A CB  1 
ATOM   1378 C CG  . ASN A 1 167 ? 21.356  -25.945 -39.477 1.00 62.43  ? 167 ASN A CG  1 
ATOM   1379 O OD1 . ASN A 1 167 ? 21.970  -26.756 -38.792 1.00 62.04  ? 167 ASN A OD1 1 
ATOM   1380 N ND2 . ASN A 1 167 ? 21.551  -25.834 -40.780 1.00 63.63  ? 167 ASN A ND2 1 
ATOM   1381 N N   . PHE A 1 168 ? 17.784  -24.203 -37.243 1.00 56.33  ? 168 PHE A N   1 
ATOM   1382 C CA  . PHE A 1 168 ? 16.961  -23.148 -36.679 1.00 53.61  ? 168 PHE A CA  1 
ATOM   1383 C C   . PHE A 1 168 ? 16.998  -23.265 -35.155 1.00 53.57  ? 168 PHE A C   1 
ATOM   1384 O O   . PHE A 1 168 ? 17.269  -22.272 -34.463 1.00 53.71  ? 168 PHE A O   1 
ATOM   1385 C CB  . PHE A 1 168 ? 15.548  -23.213 -37.256 1.00 50.49  ? 168 PHE A CB  1 
ATOM   1386 C CG  . PHE A 1 168 ? 14.667  -22.055 -36.871 1.00 48.64  ? 168 PHE A CG  1 
ATOM   1387 C CD1 . PHE A 1 168 ? 15.155  -20.757 -36.866 1.00 50.59  ? 168 PHE A CD1 1 
ATOM   1388 C CD2 . PHE A 1 168 ? 13.335  -22.248 -36.567 1.00 46.07  ? 168 PHE A CD2 1 
ATOM   1389 C CE1 . PHE A 1 168 ? 14.340  -19.686 -36.533 1.00 49.10  ? 168 PHE A CE1 1 
ATOM   1390 C CE2 . PHE A 1 168 ? 12.517  -21.174 -36.243 1.00 45.57  ? 168 PHE A CE2 1 
ATOM   1391 C CZ  . PHE A 1 168 ? 13.018  -19.894 -36.226 1.00 46.23  ? 168 PHE A CZ  1 
ATOM   1392 N N   . GLY A 1 169 ? 16.792  -24.501 -34.661 1.00 52.10  ? 169 GLY A N   1 
ATOM   1393 C CA  . GLY A 1 169 ? 16.898  -24.819 -33.248 1.00 52.47  ? 169 GLY A CA  1 
ATOM   1394 C C   . GLY A 1 169 ? 18.192  -24.303 -32.617 1.00 56.82  ? 169 GLY A C   1 
ATOM   1395 O O   . GLY A 1 169 ? 18.176  -23.732 -31.525 1.00 57.41  ? 169 GLY A O   1 
ATOM   1396 N N   . LYS A 1 170 ? 19.321  -24.516 -33.301 1.00 60.11  ? 170 LYS A N   1 
ATOM   1397 C CA  . LYS A 1 170 ? 20.603  -24.057 -32.793 1.00 63.84  ? 170 LYS A CA  1 
ATOM   1398 C C   . LYS A 1 170 ? 20.626  -22.534 -32.759 1.00 64.91  ? 170 LYS A C   1 
ATOM   1399 O O   . LYS A 1 170 ? 21.433  -21.933 -32.048 1.00 66.91  ? 170 LYS A O   1 
ATOM   1400 C CB  . LYS A 1 170 ? 21.763  -24.529 -33.673 1.00 67.43  ? 170 LYS A CB  1 
ATOM   1401 C CG  . LYS A 1 170 ? 21.736  -26.001 -34.043 1.00 68.16  ? 170 LYS A CG  1 
ATOM   1402 C CD  . LYS A 1 170 ? 23.087  -26.524 -34.413 1.00 72.54  ? 170 LYS A CD  1 
ATOM   1403 C CE  . LYS A 1 170 ? 23.125  -28.035 -34.476 1.00 73.50  ? 170 LYS A CE  1 
ATOM   1404 N NZ  . LYS A 1 170 ? 24.496  -28.512 -34.776 1.00 76.47  ? 170 LYS A NZ  1 
ATOM   1405 N N   . LEU A 1 171 ? 19.758  -21.934 -33.577 1.00 63.54  ? 171 LEU A N   1 
ATOM   1406 C CA  . LEU A 1 171 ? 19.710  -20.495 -33.743 1.00 63.50  ? 171 LEU A CA  1 
ATOM   1407 C C   . LEU A 1 171 ? 18.905  -19.911 -32.592 1.00 61.23  ? 171 LEU A C   1 
ATOM   1408 O O   . LEU A 1 171 ? 19.378  -19.017 -31.895 1.00 60.75  ? 171 LEU A O   1 
ATOM   1409 C CB  . LEU A 1 171 ? 19.097  -20.188 -35.118 1.00 61.51  ? 171 LEU A CB  1 
ATOM   1410 C CG  . LEU A 1 171 ? 19.036  -18.718 -35.524 1.00 60.38  ? 171 LEU A CG  1 
ATOM   1411 C CD1 . LEU A 1 171 ? 20.407  -18.073 -35.456 1.00 64.21  ? 171 LEU A CD1 1 
ATOM   1412 C CD2 . LEU A 1 171 ? 18.460  -18.577 -36.921 1.00 58.99  ? 171 LEU A CD2 1 
ATOM   1413 N N   . LEU A 1 172 ? 17.709  -20.472 -32.398 1.00 59.03  ? 172 LEU A N   1 
ATOM   1414 C CA  . LEU A 1 172 ? 16.818  -20.105 -31.309 1.00 59.23  ? 172 LEU A CA  1 
ATOM   1415 C C   . LEU A 1 172 ? 17.523  -20.205 -29.954 1.00 61.26  ? 172 LEU A C   1 
ATOM   1416 O O   . LEU A 1 172 ? 17.164  -19.497 -29.008 1.00 60.69  ? 172 LEU A O   1 
ATOM   1417 C CB  . LEU A 1 172 ? 15.607  -21.047 -31.331 1.00 57.68  ? 172 LEU A CB  1 
ATOM   1418 C CG  . LEU A 1 172 ? 14.571  -20.798 -32.426 1.00 56.94  ? 172 LEU A CG  1 
ATOM   1419 C CD1 . LEU A 1 172 ? 13.588  -21.956 -32.522 1.00 54.84  ? 172 LEU A CD1 1 
ATOM   1420 C CD2 . LEU A 1 172 ? 13.817  -19.498 -32.173 1.00 56.67  ? 172 LEU A CD2 1 
ATOM   1421 N N   . ASP A 1 173 ? 18.490  -21.122 -29.830 1.00 62.93  ? 173 ASP A N   1 
ATOM   1422 C CA  . ASP A 1 173 ? 19.111  -21.327 -28.530 1.00 65.30  ? 173 ASP A CA  1 
ATOM   1423 C C   . ASP A 1 173 ? 20.030  -20.151 -28.212 1.00 67.01  ? 173 ASP A C   1 
ATOM   1424 O O   . ASP A 1 173 ? 20.324  -19.899 -27.044 1.00 68.29  ? 173 ASP A O   1 
ATOM   1425 C CB  . ASP A 1 173 ? 19.861  -22.656 -28.424 1.00 66.34  ? 173 ASP A CB  1 
ATOM   1426 C CG  . ASP A 1 173 ? 20.290  -22.953 -26.998 1.00 66.61  ? 173 ASP A CG  1 
ATOM   1427 O OD1 . ASP A 1 173 ? 19.415  -22.955 -26.123 1.00 66.56  ? 173 ASP A OD1 1 
ATOM   1428 O OD2 . ASP A 1 173 ? 21.485  -23.155 -26.773 1.00 68.35  ? 173 ASP A OD2 1 
ATOM   1429 N N   . LYS A 1 174 ? 20.435  -19.411 -29.254 1.00 67.28  ? 174 LYS A N   1 
ATOM   1430 C CA  . LYS A 1 174 ? 21.373  -18.309 -29.104 1.00 67.88  ? 174 LYS A CA  1 
ATOM   1431 C C   . LYS A 1 174 ? 20.676  -17.074 -28.537 1.00 66.76  ? 174 LYS A C   1 
ATOM   1432 O O   . LYS A 1 174 ? 21.333  -16.053 -28.359 1.00 69.73  ? 174 LYS A O   1 
ATOM   1433 C CB  . LYS A 1 174 ? 22.007  -17.908 -30.441 1.00 67.62  ? 174 LYS A CB  1 
ATOM   1434 C CG  . LYS A 1 174 ? 22.781  -18.981 -31.198 1.00 67.80  ? 174 LYS A CG  1 
ATOM   1435 C CD  . LYS A 1 174 ? 23.197  -18.498 -32.577 1.00 68.71  ? 174 LYS A CD  1 
ATOM   1436 C CE  . LYS A 1 174 ? 23.642  -19.573 -33.546 1.00 69.68  ? 174 LYS A CE  1 
ATOM   1437 N NZ  . LYS A 1 174 ? 25.092  -19.878 -33.434 1.00 73.28  ? 174 LYS A NZ  1 
ATOM   1438 N N   . PHE A 1 175 ? 19.365  -17.150 -28.269 1.00 63.51  ? 175 PHE A N   1 
ATOM   1439 C CA  . PHE A 1 175 ? 18.660  -16.034 -27.656 1.00 62.70  ? 175 PHE A CA  1 
ATOM   1440 C C   . PHE A 1 175 ? 18.024  -16.447 -26.329 1.00 63.98  ? 175 PHE A C   1 
ATOM   1441 O O   . PHE A 1 175 ? 17.904  -17.630 -26.018 1.00 65.69  ? 175 PHE A O   1 
ATOM   1442 C CB  . PHE A 1 175 ? 17.601  -15.476 -28.600 1.00 58.62  ? 175 PHE A CB  1 
ATOM   1443 C CG  . PHE A 1 175 ? 18.105  -15.090 -29.963 1.00 57.92  ? 175 PHE A CG  1 
ATOM   1444 C CD1 . PHE A 1 175 ? 18.233  -16.028 -30.974 1.00 56.92  ? 175 PHE A CD1 1 
ATOM   1445 C CD2 . PHE A 1 175 ? 18.440  -13.779 -30.239 1.00 59.18  ? 175 PHE A CD2 1 
ATOM   1446 C CE1 . PHE A 1 175 ? 18.683  -15.657 -32.233 1.00 57.57  ? 175 PHE A CE1 1 
ATOM   1447 C CE2 . PHE A 1 175 ? 18.902  -13.413 -31.493 1.00 59.77  ? 175 PHE A CE2 1 
ATOM   1448 C CZ  . PHE A 1 175 ? 19.019  -14.350 -32.490 1.00 58.85  ? 175 PHE A CZ  1 
ATOM   1449 N N   . LYS A 1 176 ? 17.610  -15.434 -25.561 1.00 64.70  ? 176 LYS A N   1 
ATOM   1450 C CA  . LYS A 1 176 ? 17.083  -15.621 -24.223 1.00 64.60  ? 176 LYS A CA  1 
ATOM   1451 C C   . LYS A 1 176 ? 15.568  -15.755 -24.277 1.00 60.74  ? 176 LYS A C   1 
ATOM   1452 O O   . LYS A 1 176 ? 14.989  -16.475 -23.473 1.00 60.41  ? 176 LYS A O   1 
ATOM   1453 C CB  . LYS A 1 176 ? 17.399  -14.419 -23.333 1.00 68.27  ? 176 LYS A CB  1 
ATOM   1454 C CG  . LYS A 1 176 ? 18.832  -13.913 -23.373 1.00 72.48  ? 176 LYS A CG  1 
ATOM   1455 C CD  . LYS A 1 176 ? 18.908  -12.463 -22.944 1.00 75.79  ? 176 LYS A CD  1 
ATOM   1456 C CE  . LYS A 1 176 ? 20.267  -11.838 -23.162 1.00 79.18  ? 176 LYS A CE  1 
ATOM   1457 N NZ  . LYS A 1 176 ? 21.309  -12.523 -22.360 1.00 82.39  ? 176 LYS A NZ  1 
ATOM   1458 N N   . LYS A 1 177 ? 14.934  -15.033 -25.209 1.00 58.74  ? 177 LYS A N   1 
ATOM   1459 C CA  . LYS A 1 177 ? 13.482  -14.955 -25.243 1.00 56.03  ? 177 LYS A CA  1 
ATOM   1460 C C   . LYS A 1 177 ? 12.990  -14.877 -26.688 1.00 53.35  ? 177 LYS A C   1 
ATOM   1461 O O   . LYS A 1 177 ? 12.173  -14.028 -27.029 1.00 52.47  ? 177 LYS A O   1 
ATOM   1462 C CB  . LYS A 1 177 ? 13.003  -13.771 -24.393 1.00 56.47  ? 177 LYS A CB  1 
ATOM   1463 C CG  . LYS A 1 177 ? 11.540  -13.860 -23.976 1.00 55.67  ? 177 LYS A CG  1 
ATOM   1464 C CD  . LYS A 1 177 ? 11.098  -12.844 -22.921 1.00 57.80  ? 177 LYS A CD  1 
ATOM   1465 C CE  . LYS A 1 177 ? 9.721   -13.144 -22.349 1.00 55.66  ? 177 LYS A CE  1 
ATOM   1466 N NZ  . LYS A 1 177 ? 9.213   -12.037 -21.502 1.00 56.51  ? 177 LYS A NZ  1 
ATOM   1467 N N   . PRO A 1 178 ? 13.392  -15.812 -27.573 1.00 52.27  ? 178 PRO A N   1 
ATOM   1468 C CA  . PRO A 1 178 ? 12.978  -15.760 -28.973 1.00 51.10  ? 178 PRO A CA  1 
ATOM   1469 C C   . PRO A 1 178 ? 11.481  -15.983 -29.186 1.00 48.42  ? 178 PRO A C   1 
ATOM   1470 O O   . PRO A 1 178 ? 10.910  -16.975 -28.739 1.00 46.27  ? 178 PRO A O   1 
ATOM   1471 C CB  . PRO A 1 178 ? 13.752  -16.932 -29.596 1.00 51.15  ? 178 PRO A CB  1 
ATOM   1472 C CG  . PRO A 1 178 ? 13.870  -17.910 -28.452 1.00 51.15  ? 178 PRO A CG  1 
ATOM   1473 C CD  . PRO A 1 178 ? 14.183  -17.014 -27.271 1.00 53.08  ? 178 PRO A CD  1 
ATOM   1474 N N   . THR A 1 179 ? 10.852  -15.080 -29.931 1.00 48.08  ? 179 THR A N   1 
ATOM   1475 C CA  . THR A 1 179 ? 9.497   -15.346 -30.374 1.00 47.23  ? 179 THR A CA  1 
ATOM   1476 C C   . THR A 1 179 ? 9.486   -15.973 -31.770 1.00 46.68  ? 179 THR A C   1 
ATOM   1477 O O   . THR A 1 179 ? 10.273  -15.608 -32.650 1.00 48.55  ? 179 THR A O   1 
ATOM   1478 C CB  . THR A 1 179 ? 8.649   -14.079 -30.294 1.00 46.90  ? 179 THR A CB  1 
ATOM   1479 O OG1 . THR A 1 179 ? 8.579   -13.740 -28.907 1.00 46.90  ? 179 THR A OG1 1 
ATOM   1480 C CG2 . THR A 1 179 ? 7.266   -14.286 -30.865 1.00 45.39  ? 179 THR A CG2 1 
ATOM   1481 N N   . VAL A 1 180 ? 8.565   -16.923 -31.961 1.00 43.46  ? 180 VAL A N   1 
ATOM   1482 C CA  . VAL A 1 180 ? 8.326   -17.509 -33.265 1.00 41.81  ? 180 VAL A CA  1 
ATOM   1483 C C   . VAL A 1 180 ? 6.833   -17.419 -33.559 1.00 38.06  ? 180 VAL A C   1 
ATOM   1484 O O   . VAL A 1 180 ? 6.023   -17.746 -32.703 1.00 34.90  ? 180 VAL A O   1 
ATOM   1485 C CB  . VAL A 1 180 ? 8.824   -18.962 -33.341 1.00 42.39  ? 180 VAL A CB  1 
ATOM   1486 C CG1 . VAL A 1 180 ? 8.504   -19.581 -34.691 1.00 42.40  ? 180 VAL A CG1 1 
ATOM   1487 C CG2 . VAL A 1 180 ? 10.310  -19.059 -33.061 1.00 44.77  ? 180 VAL A CG2 1 
ATOM   1488 N N   . ILE A 1 181 ? 6.510   -16.999 -34.787 1.00 37.47  ? 181 ILE A N   1 
ATOM   1489 C CA  . ILE A 1 181 ? 5.149   -16.704 -35.184 1.00 37.53  ? 181 ILE A CA  1 
ATOM   1490 C C   . ILE A 1 181 ? 4.771   -17.616 -36.347 1.00 35.99  ? 181 ILE A C   1 
ATOM   1491 O O   . ILE A 1 181 ? 5.344   -17.526 -37.429 1.00 35.99  ? 181 ILE A O   1 
ATOM   1492 C CB  . ILE A 1 181 ? 4.961   -15.211 -35.547 1.00 40.10  ? 181 ILE A CB  1 
ATOM   1493 C CG1 . ILE A 1 181 ? 5.116   -14.285 -34.336 1.00 41.46  ? 181 ILE A CG1 1 
ATOM   1494 C CG2 . ILE A 1 181 ? 3.611   -14.983 -36.229 1.00 39.26  ? 181 ILE A CG2 1 
ATOM   1495 C CD1 . ILE A 1 181 ? 5.247   -12.804 -34.694 1.00 43.89  ? 181 ILE A CD1 1 
ATOM   1496 N N   . VAL A 1 182 ? 3.748   -18.438 -36.100 1.00 35.50  ? 182 VAL A N   1 
ATOM   1497 C CA  . VAL A 1 182 ? 3.214   -19.393 -37.051 1.00 36.12  ? 182 VAL A CA  1 
ATOM   1498 C C   . VAL A 1 182 ? 1.794   -18.947 -37.378 1.00 37.32  ? 182 VAL A C   1 
ATOM   1499 O O   . VAL A 1 182 ? 1.018   -18.620 -36.474 1.00 38.62  ? 182 VAL A O   1 
ATOM   1500 C CB  . VAL A 1 182 ? 3.234   -20.823 -36.479 1.00 35.03  ? 182 VAL A CB  1 
ATOM   1501 C CG1 . VAL A 1 182 ? 2.710   -21.843 -37.474 1.00 35.06  ? 182 VAL A CG1 1 
ATOM   1502 C CG2 . VAL A 1 182 ? 4.617   -21.227 -36.003 1.00 35.79  ? 182 VAL A CG2 1 
ATOM   1503 N N   . GLY A 1 183 ? 1.486   -18.913 -38.679 1.00 38.44  ? 183 GLY A N   1 
ATOM   1504 C CA  . GLY A 1 183 ? 0.177   -18.503 -39.150 1.00 38.69  ? 183 GLY A CA  1 
ATOM   1505 C C   . GLY A 1 183 ? -0.859  -19.569 -38.829 1.00 37.52  ? 183 GLY A C   1 
ATOM   1506 O O   . GLY A 1 183 ? -0.610  -20.750 -39.029 1.00 36.28  ? 183 GLY A O   1 
ATOM   1507 N N   . GLY A 1 184 ? -2.005  -19.139 -38.302 1.00 38.24  ? 184 GLY A N   1 
ATOM   1508 C CA  . GLY A 1 184 ? -3.003  -20.074 -37.812 1.00 37.44  ? 184 GLY A CA  1 
ATOM   1509 C C   . GLY A 1 184 ? -4.080  -20.320 -38.855 1.00 37.83  ? 184 GLY A C   1 
ATOM   1510 O O   . GLY A 1 184 ? -5.245  -20.535 -38.513 1.00 37.90  ? 184 GLY A O   1 
ATOM   1511 N N   . PHE A 1 185 ? -3.679  -20.259 -40.127 1.00 39.48  ? 185 PHE A N   1 
ATOM   1512 C CA  . PHE A 1 185 ? -4.648  -20.175 -41.202 1.00 40.85  ? 185 PHE A CA  1 
ATOM   1513 C C   . PHE A 1 185 ? -4.232  -21.151 -42.290 1.00 42.98  ? 185 PHE A C   1 
ATOM   1514 O O   . PHE A 1 185 ? -3.039  -21.379 -42.480 1.00 42.33  ? 185 PHE A O   1 
ATOM   1515 C CB  . PHE A 1 185 ? -4.766  -18.727 -41.683 1.00 42.05  ? 185 PHE A CB  1 
ATOM   1516 C CG  . PHE A 1 185 ? -3.447  -18.054 -41.967 1.00 42.63  ? 185 PHE A CG  1 
ATOM   1517 C CD1 . PHE A 1 185 ? -2.775  -18.259 -43.168 1.00 43.76  ? 185 PHE A CD1 1 
ATOM   1518 C CD2 . PHE A 1 185 ? -2.869  -17.229 -41.021 1.00 42.29  ? 185 PHE A CD2 1 
ATOM   1519 C CE1 . PHE A 1 185 ? -1.565  -17.637 -43.423 1.00 43.86  ? 185 PHE A CE1 1 
ATOM   1520 C CE2 . PHE A 1 185 ? -1.662  -16.598 -41.283 1.00 44.33  ? 185 PHE A CE2 1 
ATOM   1521 C CZ  . PHE A 1 185 ? -1.012  -16.807 -42.482 1.00 44.42  ? 185 PHE A CZ  1 
ATOM   1522 N N   . PRO A 1 186 ? -5.210  -21.725 -43.034 1.00 45.79  ? 186 PRO A N   1 
ATOM   1523 C CA  . PRO A 1 186 ? -4.939  -22.812 -43.981 1.00 47.64  ? 186 PRO A CA  1 
ATOM   1524 C C   . PRO A 1 186 ? -4.015  -22.413 -45.131 1.00 49.11  ? 186 PRO A C   1 
ATOM   1525 O O   . PRO A 1 186 ? -3.138  -23.183 -45.513 1.00 49.74  ? 186 PRO A O   1 
ATOM   1526 C CB  . PRO A 1 186 ? -6.334  -23.187 -44.504 1.00 47.58  ? 186 PRO A CB  1 
ATOM   1527 C CG  . PRO A 1 186 ? -7.164  -21.928 -44.308 1.00 46.30  ? 186 PRO A CG  1 
ATOM   1528 C CD  . PRO A 1 186 ? -6.627  -21.322 -43.030 1.00 44.67  ? 186 PRO A CD  1 
ATOM   1529 N N   . HIS A 1 187 ? -4.210  -21.203 -45.661 1.00 50.98  ? 187 HIS A N   1 
ATOM   1530 C CA  . HIS A 1 187 ? -3.478  -20.755 -46.835 1.00 56.48  ? 187 HIS A CA  1 
ATOM   1531 C C   . HIS A 1 187 ? -3.575  -19.231 -46.957 1.00 60.64  ? 187 HIS A C   1 
ATOM   1532 O O   . HIS A 1 187 ? -4.346  -18.580 -46.240 1.00 60.66  ? 187 HIS A O   1 
ATOM   1533 C CB  . HIS A 1 187 ? -3.998  -21.475 -48.085 1.00 56.38  ? 187 HIS A CB  1 
ATOM   1534 C CG  . HIS A 1 187 ? -5.485  -21.329 -48.305 1.00 57.81  ? 187 HIS A CG  1 
ATOM   1535 N ND1 . HIS A 1 187 ? -6.141  -20.116 -48.448 1.00 58.08  ? 187 HIS A ND1 1 
ATOM   1536 C CD2 . HIS A 1 187 ? -6.436  -22.278 -48.430 1.00 55.61  ? 187 HIS A CD2 1 
ATOM   1537 C CE1 . HIS A 1 187 ? -7.433  -20.333 -48.662 1.00 57.25  ? 187 HIS A CE1 1 
ATOM   1538 N NE2 . HIS A 1 187 ? -7.633  -21.642 -48.651 1.00 56.41  ? 187 HIS A NE2 1 
ATOM   1539 N N   . GLY A 1 188 ? -2.782  -18.677 -47.885 1.00 61.70  ? 188 GLY A N   1 
ATOM   1540 C CA  . GLY A 1 188 ? -2.684  -17.238 -48.078 1.00 63.06  ? 188 GLY A CA  1 
ATOM   1541 C C   . GLY A 1 188 ? -1.550  -16.645 -47.246 1.00 61.17  ? 188 GLY A C   1 
ATOM   1542 O O   . GLY A 1 188 ? -0.846  -17.385 -46.560 1.00 55.04  ? 188 GLY A O   1 
ATOM   1543 N N   . ASP A 1 189 ? -1.400  -15.314 -47.318 1.00 62.18  ? 189 ASP A N   1 
ATOM   1544 C CA  . ASP A 1 189 ? -0.357  -14.609 -46.593 1.00 61.95  ? 189 ASP A CA  1 
ATOM   1545 C C   . ASP A 1 189 ? -0.911  -14.192 -45.233 1.00 57.80  ? 189 ASP A C   1 
ATOM   1546 O O   . ASP A 1 189 ? -2.115  -14.253 -45.007 1.00 55.43  ? 189 ASP A O   1 
ATOM   1547 C CB  . ASP A 1 189 ? 0.147   -13.422 -47.420 1.00 69.16  ? 189 ASP A CB  1 
ATOM   1548 C CG  . ASP A 1 189 ? 1.495   -12.853 -46.988 1.00 74.07  ? 189 ASP A CG  1 
ATOM   1549 O OD1 . ASP A 1 189 ? 2.203   -13.501 -46.162 1.00 70.16  ? 189 ASP A OD1 1 
ATOM   1550 O OD2 . ASP A 1 189 ? 1.830   -11.748 -47.477 1.00 79.01  ? 189 ASP A OD2 1 
ATOM   1551 N N   . PHE A 1 190 ? -0.013  -13.803 -44.320 1.00 58.47  ? 190 PHE A N   1 
ATOM   1552 C CA  . PHE A 1 190 ? -0.397  -13.177 -43.063 1.00 57.86  ? 190 PHE A CA  1 
ATOM   1553 C C   . PHE A 1 190 ? -1.221  -11.916 -43.338 1.00 59.43  ? 190 PHE A C   1 
ATOM   1554 O O   . PHE A 1 190 ? -1.099  -11.302 -44.405 1.00 58.40  ? 190 PHE A O   1 
ATOM   1555 C CB  . PHE A 1 190 ? 0.835   -12.802 -42.228 1.00 57.47  ? 190 PHE A CB  1 
ATOM   1556 C CG  . PHE A 1 190 ? 1.510   -13.938 -41.501 1.00 54.88  ? 190 PHE A CG  1 
ATOM   1557 C CD1 . PHE A 1 190 ? 1.038   -14.378 -40.270 1.00 51.35  ? 190 PHE A CD1 1 
ATOM   1558 C CD2 . PHE A 1 190 ? 2.632   -14.555 -42.044 1.00 55.49  ? 190 PHE A CD2 1 
ATOM   1559 C CE1 . PHE A 1 190 ? 1.665   -15.421 -39.608 1.00 50.96  ? 190 PHE A CE1 1 
ATOM   1560 C CE2 . PHE A 1 190 ? 3.262   -15.595 -41.375 1.00 55.81  ? 190 PHE A CE2 1 
ATOM   1561 C CZ  . PHE A 1 190 ? 2.768   -16.035 -40.164 1.00 53.96  ? 190 PHE A CZ  1 
ATOM   1562 N N   . LYS A 1 191 ? -2.058  -11.548 -42.354 1.00 58.26  ? 191 LYS A N   1 
ATOM   1563 C CA  . LYS A 1 191 ? -2.801  -10.301 -42.393 1.00 59.89  ? 191 LYS A CA  1 
ATOM   1564 C C   . LYS A 1 191 ? -2.032  -9.232  -41.631 1.00 62.69  ? 191 LYS A C   1 
ATOM   1565 O O   . LYS A 1 191 ? -1.835  -8.147  -42.161 1.00 66.61  ? 191 LYS A O   1 
ATOM   1566 C CB  . LYS A 1 191 ? -4.184  -10.445 -41.768 1.00 57.37  ? 191 LYS A CB  1 
ATOM   1567 C CG  . LYS A 1 191 ? -5.034  -11.577 -42.318 1.00 57.34  ? 191 LYS A CG  1 
ATOM   1568 C CD  . LYS A 1 191 ? -6.511  -11.263 -42.212 1.00 57.40  ? 191 LYS A CD  1 
ATOM   1569 C CE  . LYS A 1 191 ? -6.921  -10.823 -40.820 1.00 55.67  ? 191 LYS A CE  1 
ATOM   1570 N NZ  . LYS A 1 191 ? -7.636  -9.527  -40.853 1.00 56.90  ? 191 LYS A NZ  1 
ATOM   1571 N N   . SER A 1 192 ? -1.630  -9.549  -40.391 1.00 63.57  ? 192 SER A N   1 
ATOM   1572 C CA  . SER A 1 192 ? -0.794  -8.670  -39.589 1.00 66.01  ? 192 SER A CA  1 
ATOM   1573 C C   . SER A 1 192 ? 0.617   -8.653  -40.172 1.00 71.77  ? 192 SER A C   1 
ATOM   1574 O O   . SER A 1 192 ? 1.234   -9.704  -40.310 1.00 80.56  ? 192 SER A O   1 
ATOM   1575 C CB  . SER A 1 192 ? -0.767  -9.093  -38.134 1.00 63.90  ? 192 SER A CB  1 
ATOM   1576 O OG  . SER A 1 192 ? -1.975  -8.754  -37.470 1.00 64.82  ? 192 SER A OG  1 
ATOM   1577 N N   . LYS A 1 193 ? 1.112   -7.466  -40.530 1.00 73.78  ? 193 LYS A N   1 
ATOM   1578 C CA  . LYS A 1 193 ? 2.505   -7.309  -40.899 1.00 76.60  ? 193 LYS A CA  1 
ATOM   1579 C C   . LYS A 1 193 ? 3.238   -6.706  -39.713 1.00 74.63  ? 193 LYS A C   1 
ATOM   1580 O O   . LYS A 1 193 ? 2.873   -5.627  -39.251 1.00 75.58  ? 193 LYS A O   1 
ATOM   1581 C CB  . LYS A 1 193 ? 2.652   -6.434  -42.146 1.00 85.58  ? 193 LYS A CB  1 
ATOM   1582 C CG  . LYS A 1 193 ? 2.150   -7.061  -43.442 1.00 89.29  ? 193 LYS A CG  1 
ATOM   1583 C CD  . LYS A 1 193 ? 2.597   -8.500  -43.667 1.00 87.22  ? 193 LYS A CD  1 
ATOM   1584 C CE  . LYS A 1 193 ? 2.350   -8.974  -45.084 1.00 87.70  ? 193 LYS A CE  1 
ATOM   1585 N NZ  . LYS A 1 193 ? 0.950   -8.734  -45.509 1.00 84.18  ? 193 LYS A NZ  1 
ATOM   1586 N N   . VAL A 1 194 ? 4.250   -7.438  -39.235 1.00 70.85  ? 194 VAL A N   1 
ATOM   1587 C CA  . VAL A 1 194 ? 5.071   -7.015  -38.116 1.00 71.78  ? 194 VAL A CA  1 
ATOM   1588 C C   . VAL A 1 194 ? 6.528   -7.209  -38.517 1.00 73.71  ? 194 VAL A C   1 
ATOM   1589 O O   . VAL A 1 194 ? 6.809   -7.866  -39.516 1.00 70.19  ? 194 VAL A O   1 
ATOM   1590 C CB  . VAL A 1 194 ? 4.747   -7.803  -36.830 1.00 68.46  ? 194 VAL A CB  1 
ATOM   1591 C CG1 . VAL A 1 194 ? 3.331   -7.551  -36.329 1.00 65.57  ? 194 VAL A CG1 1 
ATOM   1592 C CG2 . VAL A 1 194 ? 4.990   -9.292  -37.022 1.00 67.65  ? 194 VAL A CG2 1 
ATOM   1593 N N   . ASP A 1 195 ? 7.431   -6.613  -37.724 1.00 79.86  ? 195 ASP A N   1 
ATOM   1594 C CA  . ASP A 1 195 ? 8.866   -6.814  -37.856 1.00 79.52  ? 195 ASP A CA  1 
ATOM   1595 C C   . ASP A 1 195 ? 9.188   -8.245  -37.447 1.00 74.51  ? 195 ASP A C   1 
ATOM   1596 O O   . ASP A 1 195 ? 8.525   -8.792  -36.570 1.00 77.26  ? 195 ASP A O   1 
ATOM   1597 C CB  . ASP A 1 195 ? 9.682   -5.836  -36.997 1.00 82.22  ? 195 ASP A CB  1 
ATOM   1598 C CG  . ASP A 1 195 ? 10.174  -4.602  -37.736 1.00 83.91  ? 195 ASP A CG  1 
ATOM   1599 O OD1 . ASP A 1 195 ? 9.906   -4.498  -38.951 1.00 84.57  ? 195 ASP A OD1 1 
ATOM   1600 O OD2 . ASP A 1 195 ? 10.840  -3.770  -37.093 1.00 85.44  ? 195 ASP A OD2 1 
ATOM   1601 N N   . GLY A 1 196 ? 10.201  -8.824  -38.101 1.00 68.42  ? 196 GLY A N   1 
ATOM   1602 C CA  . GLY A 1 196 ? 10.633  -10.178 -37.820 1.00 62.57  ? 196 GLY A CA  1 
ATOM   1603 C C   . GLY A 1 196 ? 11.393  -10.793 -38.994 1.00 61.12  ? 196 GLY A C   1 
ATOM   1604 O O   . GLY A 1 196 ? 11.253  -10.365 -40.144 1.00 60.54  ? 196 GLY A O   1 
ATOM   1605 N N   . VAL A 1 197 ? 12.167  -11.834 -38.666 1.00 57.88  ? 197 VAL A N   1 
ATOM   1606 C CA  . VAL A 1 197 ? 13.007  -12.540 -39.608 1.00 57.41  ? 197 VAL A CA  1 
ATOM   1607 C C   . VAL A 1 197 ? 12.180  -13.655 -40.229 1.00 54.43  ? 197 VAL A C   1 
ATOM   1608 O O   . VAL A 1 197 ? 11.601  -14.458 -39.512 1.00 50.98  ? 197 VAL A O   1 
ATOM   1609 C CB  . VAL A 1 197 ? 14.245  -13.104 -38.891 1.00 58.75  ? 197 VAL A CB  1 
ATOM   1610 C CG1 . VAL A 1 197 ? 15.256  -13.651 -39.879 1.00 60.78  ? 197 VAL A CG1 1 
ATOM   1611 C CG2 . VAL A 1 197 ? 14.891  -12.076 -37.973 1.00 59.99  ? 197 VAL A CG2 1 
ATOM   1612 N N   . LYS A 1 198 ? 12.144  -13.705 -41.561 1.00 57.42  ? 198 LYS A N   1 
ATOM   1613 C CA  . LYS A 1 198 ? 11.290  -14.649 -42.266 1.00 58.41  ? 198 LYS A CA  1 
ATOM   1614 C C   . LYS A 1 198 ? 12.078  -15.916 -42.573 1.00 58.24  ? 198 LYS A C   1 
ATOM   1615 O O   . LYS A 1 198 ? 13.127  -15.872 -43.207 1.00 60.17  ? 198 LYS A O   1 
ATOM   1616 C CB  . LYS A 1 198 ? 10.667  -13.982 -43.497 1.00 61.98  ? 198 LYS A CB  1 
ATOM   1617 C CG  . LYS A 1 198 ? 9.677   -12.896 -43.107 1.00 64.33  ? 198 LYS A CG  1 
ATOM   1618 C CD  . LYS A 1 198 ? 9.034   -12.120 -44.219 1.00 68.86  ? 198 LYS A CD  1 
ATOM   1619 C CE  . LYS A 1 198 ? 7.885   -11.280 -43.687 1.00 69.82  ? 198 LYS A CE  1 
ATOM   1620 N NZ  . LYS A 1 198 ? 7.437   -10.259 -44.662 1.00 73.87  ? 198 LYS A NZ  1 
ATOM   1621 N N   . ILE A 1 199 ? 11.555  -17.043 -42.089 1.00 57.08  ? 199 ILE A N   1 
ATOM   1622 C CA  . ILE A 1 199 ? 12.270  -18.306 -42.103 1.00 58.43  ? 199 ILE A CA  1 
ATOM   1623 C C   . ILE A 1 199 ? 11.383  -19.334 -42.788 1.00 58.79  ? 199 ILE A C   1 
ATOM   1624 O O   . ILE A 1 199 ? 10.223  -19.483 -42.418 1.00 56.53  ? 199 ILE A O   1 
ATOM   1625 C CB  . ILE A 1 199 ? 12.637  -18.766 -40.676 1.00 56.55  ? 199 ILE A CB  1 
ATOM   1626 C CG1 . ILE A 1 199 ? 13.298  -17.655 -39.860 1.00 57.69  ? 199 ILE A CG1 1 
ATOM   1627 C CG2 . ILE A 1 199 ? 13.509  -20.010 -40.712 1.00 56.94  ? 199 ILE A CG2 1 
ATOM   1628 C CD1 . ILE A 1 199 ? 14.692  -17.312 -40.312 1.00 60.58  ? 199 ILE A CD1 1 
ATOM   1629 N N   . SER A 1 200 ? 11.951  -20.019 -43.785 1.00 62.70  ? 200 SER A N   1 
ATOM   1630 C CA  . SER A 1 200 ? 11.337  -21.199 -44.362 1.00 64.77  ? 200 SER A CA  1 
ATOM   1631 C C   . SER A 1 200 ? 12.127  -22.432 -43.920 1.00 67.88  ? 200 SER A C   1 
ATOM   1632 O O   . SER A 1 200 ? 13.361  -22.434 -43.989 1.00 71.93  ? 200 SER A O   1 
ATOM   1633 C CB  . SER A 1 200 ? 11.284  -21.072 -45.858 1.00 67.40  ? 200 SER A CB  1 
ATOM   1634 O OG  . SER A 1 200 ? 10.540  -22.144 -46.418 1.00 68.59  ? 200 SER A OG  1 
ATOM   1635 N N   . LEU A 1 201 ? 11.417  -23.470 -43.455 1.00 64.93  ? 201 LEU A N   1 
ATOM   1636 C CA  . LEU A 1 201 ? 12.055  -24.684 -42.954 1.00 66.21  ? 201 LEU A CA  1 
ATOM   1637 C C   . LEU A 1 201 ? 12.111  -25.774 -44.023 1.00 68.27  ? 201 LEU A C   1 
ATOM   1638 O O   . LEU A 1 201 ? 12.789  -26.785 -43.856 1.00 70.74  ? 201 LEU A O   1 
ATOM   1639 C CB  . LEU A 1 201 ? 11.287  -25.183 -41.726 1.00 64.01  ? 201 LEU A CB  1 
ATOM   1640 C CG  . LEU A 1 201 ? 11.533  -24.411 -40.433 1.00 64.49  ? 201 LEU A CG  1 
ATOM   1641 C CD1 . LEU A 1 201 ? 10.972  -25.161 -39.241 1.00 62.91  ? 201 LEU A CD1 1 
ATOM   1642 C CD2 . LEU A 1 201 ? 13.017  -24.150 -40.232 1.00 69.32  ? 201 LEU A CD2 1 
ATOM   1643 N N   . TYR A 1 202 ? 11.371  -25.565 -45.109 1.00 69.70  ? 202 TYR A N   1 
ATOM   1644 C CA  . TYR A 1 202 ? 11.297  -26.503 -46.211 1.00 73.28  ? 202 TYR A CA  1 
ATOM   1645 C C   . TYR A 1 202 ? 10.996  -25.672 -47.449 1.00 84.46  ? 202 TYR A C   1 
ATOM   1646 O O   . TYR A 1 202 ? 10.837  -24.454 -47.350 1.00 86.06  ? 202 TYR A O   1 
ATOM   1647 C CB  . TYR A 1 202 ? 10.227  -27.541 -45.876 1.00 65.93  ? 202 TYR A CB  1 
ATOM   1648 C CG  . TYR A 1 202 ? 10.096  -28.750 -46.793 1.00 65.08  ? 202 TYR A CG  1 
ATOM   1649 C CD1 . TYR A 1 202 ? 11.175  -29.587 -47.036 1.00 67.07  ? 202 TYR A CD1 1 
ATOM   1650 C CD2 . TYR A 1 202 ? 8.872   -29.103 -47.353 1.00 63.17  ? 202 TYR A CD2 1 
ATOM   1651 C CE1 . TYR A 1 202 ? 11.047  -30.716 -47.827 1.00 68.18  ? 202 TYR A CE1 1 
ATOM   1652 C CE2 . TYR A 1 202 ? 8.731   -30.230 -48.145 1.00 63.67  ? 202 TYR A CE2 1 
ATOM   1653 C CZ  . TYR A 1 202 ? 9.824   -31.044 -48.379 1.00 66.59  ? 202 TYR A CZ  1 
ATOM   1654 O OH  . TYR A 1 202 ? 9.741   -32.161 -49.164 1.00 68.91  ? 202 TYR A OH  1 
ATOM   1655 N N   . ARG A 1 203 ? 10.928  -26.315 -48.613 1.00 95.54  ? 203 ARG A N   1 
ATOM   1656 C CA  . ARG A 1 203 ? 10.613  -25.545 -49.792 1.00 105.60 ? 203 ARG A CA  1 
ATOM   1657 C C   . ARG A 1 203 ? 9.107   -25.505 -50.003 1.00 100.27 ? 203 ARG A C   1 
ATOM   1658 O O   . ARG A 1 203 ? 8.496   -24.447 -49.847 1.00 101.17 ? 203 ARG A O   1 
ATOM   1659 C CB  . ARG A 1 203 ? 11.307  -26.081 -51.033 1.00 125.14 ? 203 ARG A CB  1 
ATOM   1660 C CG  . ARG A 1 203 ? 11.044  -25.175 -52.220 1.00 147.49 ? 203 ARG A CG  1 
ATOM   1661 C CD  . ARG A 1 203 ? 11.656  -23.785 -52.067 1.00 161.80 ? 203 ARG A CD  1 
ATOM   1662 N NE  . ARG A 1 203 ? 10.817  -22.841 -51.326 1.00 166.30 ? 203 ARG A NE  1 
ATOM   1663 C CZ  . ARG A 1 203 ? 10.251  -21.742 -51.824 1.00 169.64 ? 203 ARG A CZ  1 
ATOM   1664 N NH1 . ARG A 1 203 ? 9.443   -21.026 -51.060 1.00 169.00 ? 203 ARG A NH1 1 
ATOM   1665 N NH2 . ARG A 1 203 ? 10.472  -21.363 -53.073 1.00 169.83 ? 203 ARG A NH2 1 
ATOM   1666 N N   . GLU A 1 204 ? 8.533   -26.656 -50.381 1.00 95.82  ? 204 GLU A N   1 
ATOM   1667 C CA  . GLU A 1 204 ? 7.092   -26.783 -50.522 1.00 90.90  ? 204 GLU A CA  1 
ATOM   1668 C C   . GLU A 1 204 ? 6.438   -26.316 -49.224 1.00 82.93  ? 204 GLU A C   1 
ATOM   1669 O O   . GLU A 1 204 ? 7.015   -26.468 -48.150 1.00 76.97  ? 204 GLU A O   1 
ATOM   1670 C CB  . GLU A 1 204 ? 6.695   -28.220 -50.873 1.00 91.78  ? 204 GLU A CB  1 
ATOM   1671 C CG  . GLU A 1 204 ? 6.555   -28.481 -52.368 1.00 98.57  ? 204 GLU A CG  1 
ATOM   1672 C CD  . GLU A 1 204 ? 7.615   -27.885 -53.288 1.00 104.19 ? 204 GLU A CD  1 
ATOM   1673 O OE1 . GLU A 1 204 ? 7.308   -27.655 -54.488 1.00 103.53 ? 204 GLU A OE1 1 
ATOM   1674 O OE2 . GLU A 1 204 ? 8.747   -27.650 -52.816 1.00 108.12 ? 204 GLU A OE2 1 
ATOM   1675 N N   . PRO A 1 205 ? 5.230   -25.710 -49.295 1.00 78.76  ? 205 PRO A N   1 
ATOM   1676 C CA  . PRO A 1 205 ? 4.538   -25.202 -48.109 1.00 73.07  ? 205 PRO A CA  1 
ATOM   1677 C C   . PRO A 1 205 ? 4.116   -26.310 -47.143 1.00 64.72  ? 205 PRO A C   1 
ATOM   1678 O O   . PRO A 1 205 ? 3.784   -27.418 -47.562 1.00 62.11  ? 205 PRO A O   1 
ATOM   1679 C CB  . PRO A 1 205 ? 3.298   -24.507 -48.696 1.00 75.86  ? 205 PRO A CB  1 
ATOM   1680 C CG  . PRO A 1 205 ? 3.053   -25.228 -50.007 1.00 77.90  ? 205 PRO A CG  1 
ATOM   1681 C CD  . PRO A 1 205 ? 4.443   -25.523 -50.524 1.00 81.38  ? 205 PRO A CD  1 
ATOM   1682 N N   . LEU A 1 206 ? 4.129   -25.985 -45.845 1.00 59.93  ? 206 LEU A N   1 
ATOM   1683 C CA  . LEU A 1 206 ? 3.772   -26.923 -44.789 1.00 54.99  ? 206 LEU A CA  1 
ATOM   1684 C C   . LEU A 1 206 ? 2.590   -26.364 -44.013 1.00 51.04  ? 206 LEU A C   1 
ATOM   1685 O O   . LEU A 1 206 ? 2.301   -25.170 -44.073 1.00 51.23  ? 206 LEU A O   1 
ATOM   1686 C CB  . LEU A 1 206 ? 4.975   -27.108 -43.862 1.00 53.50  ? 206 LEU A CB  1 
ATOM   1687 C CG  . LEU A 1 206 ? 6.229   -27.694 -44.510 1.00 56.68  ? 206 LEU A CG  1 
ATOM   1688 C CD1 . LEU A 1 206 ? 7.414   -27.631 -43.566 1.00 56.50  ? 206 LEU A CD1 1 
ATOM   1689 C CD2 . LEU A 1 206 ? 5.994   -29.133 -44.956 1.00 58.12  ? 206 LEU A CD2 1 
ATOM   1690 N N   . MET A 1 207 ? 1.920   -27.242 -43.278 1.00 48.14  ? 207 MET A N   1 
ATOM   1691 C CA  . MET A 1 207 ? 0.811   -26.827 -42.439 1.00 45.46  ? 207 MET A CA  1 
ATOM   1692 C C   . MET A 1 207 ? 1.366   -26.283 -41.127 1.00 41.24  ? 207 MET A C   1 
ATOM   1693 O O   . MET A 1 207 ? 2.478   -26.597 -40.729 1.00 37.37  ? 207 MET A O   1 
ATOM   1694 C CB  . MET A 1 207 ? -0.116  -28.012 -42.169 1.00 47.54  ? 207 MET A CB  1 
ATOM   1695 C CG  . MET A 1 207 ? -0.642  -28.641 -43.448 1.00 52.47  ? 207 MET A CG  1 
ATOM   1696 S SD  . MET A 1 207 ? -2.190  -27.909 -44.029 1.00 58.59  ? 207 MET A SD  1 
ATOM   1697 C CE  . MET A 1 207 ? -1.596  -26.461 -44.900 1.00 61.31  ? 207 MET A CE  1 
ATOM   1698 N N   . ALA A 1 208 ? 0.574   -25.440 -40.466 1.00 41.60  ? 208 ALA A N   1 
ATOM   1699 C CA  . ALA A 1 208 ? 0.938   -24.854 -39.184 1.00 39.39  ? 208 ALA A CA  1 
ATOM   1700 C C   . ALA A 1 208 ? 1.549   -25.905 -38.250 1.00 38.73  ? 208 ALA A C   1 
ATOM   1701 O O   . ALA A 1 208 ? 2.669   -25.719 -37.799 1.00 39.37  ? 208 ALA A O   1 
ATOM   1702 C CB  . ALA A 1 208 ? -0.271  -24.173 -38.580 1.00 37.51  ? 208 ALA A CB  1 
ATOM   1703 N N   . TRP A 1 209 ? 0.848   -27.017 -37.976 1.00 38.54  ? 209 TRP A N   1 
ATOM   1704 C CA  . TRP A 1 209 ? 1.303   -27.965 -36.958 1.00 39.44  ? 209 TRP A CA  1 
ATOM   1705 C C   . TRP A 1 209 ? 2.665   -28.573 -37.287 1.00 39.60  ? 209 TRP A C   1 
ATOM   1706 O O   . TRP A 1 209 ? 3.467   -28.797 -36.381 1.00 40.86  ? 209 TRP A O   1 
ATOM   1707 C CB  . TRP A 1 209 ? 0.287   -29.087 -36.692 1.00 40.25  ? 209 TRP A CB  1 
ATOM   1708 C CG  . TRP A 1 209 ? -0.162  -29.887 -37.883 1.00 40.67  ? 209 TRP A CG  1 
ATOM   1709 C CD1 . TRP A 1 209 ? 0.449   -30.956 -38.465 1.00 43.41  ? 209 TRP A CD1 1 
ATOM   1710 C CD2 . TRP A 1 209 ? -1.372  -29.668 -38.633 1.00 41.45  ? 209 TRP A CD2 1 
ATOM   1711 N NE1 . TRP A 1 209 ? -0.283  -31.410 -39.535 1.00 44.32  ? 209 TRP A NE1 1 
ATOM   1712 C CE2 . TRP A 1 209 ? -1.405  -30.635 -39.663 1.00 43.47  ? 209 TRP A CE2 1 
ATOM   1713 C CE3 . TRP A 1 209 ? -2.415  -28.748 -38.529 1.00 41.18  ? 209 TRP A CE3 1 
ATOM   1714 C CZ2 . TRP A 1 209 ? -2.439  -30.701 -40.589 1.00 43.51  ? 209 TRP A CZ2 1 
ATOM   1715 C CZ3 . TRP A 1 209 ? -3.435  -28.814 -39.445 1.00 42.36  ? 209 TRP A CZ3 1 
ATOM   1716 C CH2 . TRP A 1 209 ? -3.438  -29.769 -40.464 1.00 42.96  ? 209 TRP A CH2 1 
ATOM   1717 N N   . THR A 1 210 ? 2.888   -28.886 -38.569 1.00 38.62  ? 210 THR A N   1 
ATOM   1718 C CA  . THR A 1 210 ? 4.165   -29.384 -39.038 1.00 37.54  ? 210 THR A CA  1 
ATOM   1719 C C   . THR A 1 210 ? 5.248   -28.385 -38.648 1.00 39.18  ? 210 THR A C   1 
ATOM   1720 O O   . THR A 1 210 ? 6.277   -28.759 -38.081 1.00 40.76  ? 210 THR A O   1 
ATOM   1721 C CB  . THR A 1 210 ? 4.134   -29.570 -40.554 1.00 36.86  ? 210 THR A CB  1 
ATOM   1722 O OG1 . THR A 1 210 ? 3.011   -30.383 -40.877 1.00 34.18  ? 210 THR A OG1 1 
ATOM   1723 C CG2 . THR A 1 210 ? 5.415   -30.171 -41.086 1.00 39.36  ? 210 THR A CG2 1 
ATOM   1724 N N   . ILE A 1 211 ? 4.983   -27.113 -38.964 1.00 38.88  ? 211 ILE A N   1 
ATOM   1725 C CA  . ILE A 1 211 ? 5.897   -26.035 -38.647 1.00 40.35  ? 211 ILE A CA  1 
ATOM   1726 C C   . ILE A 1 211 ? 6.128   -26.052 -37.134 1.00 39.38  ? 211 ILE A C   1 
ATOM   1727 O O   . ILE A 1 211 ? 7.276   -26.084 -36.683 1.00 42.28  ? 211 ILE A O   1 
ATOM   1728 C CB  . ILE A 1 211 ? 5.369   -24.681 -39.193 1.00 41.50  ? 211 ILE A CB  1 
ATOM   1729 C CG1 . ILE A 1 211 ? 5.116   -24.721 -40.700 1.00 43.21  ? 211 ILE A CG1 1 
ATOM   1730 C CG2 . ILE A 1 211 ? 6.303   -23.531 -38.849 1.00 42.27  ? 211 ILE A CG2 1 
ATOM   1731 C CD1 . ILE A 1 211 ? 6.243   -25.402 -41.450 1.00 47.76  ? 211 ILE A CD1 1 
ATOM   1732 N N   . VAL A 1 212 ? 5.038   -26.088 -36.356 1.00 36.35  ? 212 VAL A N   1 
ATOM   1733 C CA  . VAL A 1 212 ? 5.128   -26.084 -34.900 1.00 36.66  ? 212 VAL A CA  1 
ATOM   1734 C C   . VAL A 1 212 ? 6.034   -27.221 -34.402 1.00 38.38  ? 212 VAL A C   1 
ATOM   1735 O O   . VAL A 1 212 ? 6.912   -26.998 -33.561 1.00 39.47  ? 212 VAL A O   1 
ATOM   1736 C CB  . VAL A 1 212 ? 3.722   -26.147 -34.269 1.00 35.49  ? 212 VAL A CB  1 
ATOM   1737 C CG1 . VAL A 1 212 ? 3.743   -26.623 -32.825 1.00 34.64  ? 212 VAL A CG1 1 
ATOM   1738 C CG2 . VAL A 1 212 ? 3.013   -24.798 -34.380 1.00 36.29  ? 212 VAL A CG2 1 
ATOM   1739 N N   . ASN A 1 213 ? 5.831   -28.434 -34.938 1.00 37.90  ? 213 ASN A N   1 
ATOM   1740 C CA  . ASN A 1 213 ? 6.526   -29.625 -34.475 1.00 38.30  ? 213 ASN A CA  1 
ATOM   1741 C C   . ASN A 1 213 ? 8.000   -29.591 -34.860 1.00 38.93  ? 213 ASN A C   1 
ATOM   1742 O O   . ASN A 1 213 ? 8.828   -30.041 -34.080 1.00 38.73  ? 213 ASN A O   1 
ATOM   1743 C CB  . ASN A 1 213 ? 5.890   -30.910 -35.015 1.00 39.41  ? 213 ASN A CB  1 
ATOM   1744 C CG  . ASN A 1 213 ? 4.443   -31.023 -34.604 1.00 39.13  ? 213 ASN A CG  1 
ATOM   1745 O OD1 . ASN A 1 213 ? 4.070   -30.588 -33.514 1.00 38.53  ? 213 ASN A OD1 1 
ATOM   1746 N ND2 . ASN A 1 213 ? 3.612   -31.544 -35.492 1.00 40.03  ? 213 ASN A ND2 1 
ATOM   1747 N N   . GLU A 1 214 ? 8.306   -29.109 -36.072 1.00 39.64  ? 214 GLU A N   1 
ATOM   1748 C CA  . GLU A 1 214 ? 9.683   -28.889 -36.492 1.00 42.45  ? 214 GLU A CA  1 
ATOM   1749 C C   . GLU A 1 214 ? 10.372  -27.904 -35.548 1.00 43.00  ? 214 GLU A C   1 
ATOM   1750 O O   . GLU A 1 214 ? 11.450  -28.183 -35.034 1.00 43.80  ? 214 GLU A O   1 
ATOM   1751 C CB  . GLU A 1 214 ? 9.720   -28.343 -37.919 1.00 43.37  ? 214 GLU A CB  1 
ATOM   1752 C CG  . GLU A 1 214 ? 9.352   -29.368 -38.976 1.00 43.65  ? 214 GLU A CG  1 
ATOM   1753 C CD  . GLU A 1 214 ? 10.426  -30.405 -39.256 1.00 45.79  ? 214 GLU A CD  1 
ATOM   1754 O OE1 . GLU A 1 214 ? 10.082  -31.462 -39.849 1.00 45.84  ? 214 GLU A OE1 1 
ATOM   1755 O OE2 . GLU A 1 214 ? 11.594  -30.168 -38.868 1.00 46.97  ? 214 GLU A OE2 1 
ATOM   1756 N N   . VAL A 1 215 ? 9.707   -26.775 -35.297 1.00 42.80  ? 215 VAL A N   1 
ATOM   1757 C CA  . VAL A 1 215 ? 10.285  -25.697 -34.514 1.00 45.50  ? 215 VAL A CA  1 
ATOM   1758 C C   . VAL A 1 215 ? 10.535  -26.134 -33.069 1.00 46.99  ? 215 VAL A C   1 
ATOM   1759 O O   . VAL A 1 215 ? 11.558  -25.772 -32.476 1.00 49.34  ? 215 VAL A O   1 
ATOM   1760 C CB  . VAL A 1 215 ? 9.391   -24.444 -34.539 1.00 43.64  ? 215 VAL A CB  1 
ATOM   1761 C CG1 . VAL A 1 215 ? 9.857   -23.435 -33.500 1.00 44.32  ? 215 VAL A CG1 1 
ATOM   1762 C CG2 . VAL A 1 215 ? 9.340   -23.815 -35.926 1.00 43.50  ? 215 VAL A CG2 1 
ATOM   1763 N N   . ILE A 1 216 ? 9.570   -26.844 -32.482 1.00 44.88  ? 216 ILE A N   1 
ATOM   1764 C CA  . ILE A 1 216 ? 9.628   -27.125 -31.058 1.00 44.51  ? 216 ILE A CA  1 
ATOM   1765 C C   . ILE A 1 216 ? 10.709  -28.171 -30.798 1.00 46.67  ? 216 ILE A C   1 
ATOM   1766 O O   . ILE A 1 216 ? 11.486  -28.027 -29.860 1.00 49.72  ? 216 ILE A O   1 
ATOM   1767 C CB  . ILE A 1 216 ? 8.247   -27.545 -30.518 1.00 41.41  ? 216 ILE A CB  1 
ATOM   1768 C CG1 . ILE A 1 216 ? 7.309   -26.340 -30.442 1.00 38.41  ? 216 ILE A CG1 1 
ATOM   1769 C CG2 . ILE A 1 216 ? 8.380   -28.255 -29.171 1.00 42.88  ? 216 ILE A CG2 1 
ATOM   1770 C CD1 . ILE A 1 216 ? 5.935   -26.631 -29.900 1.00 36.78  ? 216 ILE A CD1 1 
ATOM   1771 N N   . VAL A 1 217 ? 10.742  -29.215 -31.628 1.00 45.85  ? 217 VAL A N   1 
ATOM   1772 C CA  . VAL A 1 217 ? 11.641  -30.333 -31.411 1.00 47.98  ? 217 VAL A CA  1 
ATOM   1773 C C   . VAL A 1 217 ? 13.087  -29.867 -31.615 1.00 50.50  ? 217 VAL A C   1 
ATOM   1774 O O   . VAL A 1 217 ? 13.982  -30.259 -30.858 1.00 51.62  ? 217 VAL A O   1 
ATOM   1775 C CB  . VAL A 1 217 ? 11.263  -31.515 -32.330 1.00 47.42  ? 217 VAL A CB  1 
ATOM   1776 C CG1 . VAL A 1 217 ? 12.343  -32.566 -32.385 1.00 50.44  ? 217 VAL A CG1 1 
ATOM   1777 C CG2 . VAL A 1 217 ? 9.961   -32.169 -31.918 1.00 44.92  ? 217 VAL A CG2 1 
ATOM   1778 N N   . SER A 1 218 ? 13.311  -29.025 -32.637 1.00 50.52  ? 218 SER A N   1 
ATOM   1779 C CA  . SER A 1 218 ? 14.647  -28.539 -32.946 1.00 52.62  ? 218 SER A CA  1 
ATOM   1780 C C   . SER A 1 218 ? 15.193  -27.698 -31.793 1.00 54.36  ? 218 SER A C   1 
ATOM   1781 O O   . SER A 1 218 ? 16.388  -27.750 -31.506 1.00 59.68  ? 218 SER A O   1 
ATOM   1782 C CB  . SER A 1 218 ? 14.705  -27.807 -34.284 1.00 52.40  ? 218 SER A CB  1 
ATOM   1783 O OG  . SER A 1 218 ? 13.868  -26.667 -34.316 1.00 51.85  ? 218 SER A OG  1 
ATOM   1784 N N   . TYR A 1 219 ? 14.326  -26.935 -31.123 1.00 52.57  ? 219 TYR A N   1 
ATOM   1785 C CA  . TYR A 1 219 ? 14.737  -26.184 -29.951 1.00 54.07  ? 219 TYR A CA  1 
ATOM   1786 C C   . TYR A 1 219 ? 14.953  -27.166 -28.803 1.00 56.52  ? 219 TYR A C   1 
ATOM   1787 O O   . TYR A 1 219 ? 15.987  -27.117 -28.153 1.00 60.74  ? 219 TYR A O   1 
ATOM   1788 C CB  . TYR A 1 219 ? 13.677  -25.109 -29.693 1.00 52.03  ? 219 TYR A CB  1 
ATOM   1789 C CG  . TYR A 1 219 ? 13.936  -24.079 -28.596 1.00 51.59  ? 219 TYR A CG  1 
ATOM   1790 C CD1 . TYR A 1 219 ? 15.004  -23.194 -28.650 1.00 54.23  ? 219 TYR A CD1 1 
ATOM   1791 C CD2 . TYR A 1 219 ? 13.074  -23.963 -27.517 1.00 50.04  ? 219 TYR A CD2 1 
ATOM   1792 C CE1 . TYR A 1 219 ? 15.210  -22.241 -27.661 1.00 55.21  ? 219 TYR A CE1 1 
ATOM   1793 C CE2 . TYR A 1 219 ? 13.270  -23.024 -26.520 1.00 51.02  ? 219 TYR A CE2 1 
ATOM   1794 C CZ  . TYR A 1 219 ? 14.332  -22.146 -26.596 1.00 53.11  ? 219 TYR A CZ  1 
ATOM   1795 O OH  . TYR A 1 219 ? 14.497  -21.215 -25.610 1.00 53.10  ? 219 TYR A OH  1 
ATOM   1796 N N   . GLU A 1 220 ? 14.001  -28.082 -28.592 1.00 57.45  ? 220 GLU A N   1 
ATOM   1797 C CA  . GLU A 1 220 ? 14.078  -29.070 -27.524 1.00 59.99  ? 220 GLU A CA  1 
ATOM   1798 C C   . GLU A 1 220 ? 15.487  -29.646 -27.398 1.00 63.13  ? 220 GLU A C   1 
ATOM   1799 O O   . GLU A 1 220 ? 16.027  -29.709 -26.300 1.00 63.55  ? 220 GLU A O   1 
ATOM   1800 C CB  . GLU A 1 220 ? 13.139  -30.250 -27.774 1.00 59.75  ? 220 GLU A CB  1 
ATOM   1801 C CG  . GLU A 1 220 ? 11.708  -30.048 -27.324 1.00 58.19  ? 220 GLU A CG  1 
ATOM   1802 C CD  . GLU A 1 220 ? 10.863  -31.290 -27.538 1.00 59.18  ? 220 GLU A CD  1 
ATOM   1803 O OE1 . GLU A 1 220 ? 9.633   -31.223 -27.364 1.00 61.45  ? 220 GLU A OE1 1 
ATOM   1804 O OE2 . GLU A 1 220 ? 11.447  -32.332 -27.873 1.00 61.57  ? 220 GLU A OE2 1 
ATOM   1805 N N   . TRP A 1 221 ? 16.081  -30.078 -28.514 1.00 66.49  ? 221 TRP A N   1 
ATOM   1806 C CA  . TRP A 1 221 ? 17.334  -30.814 -28.457 1.00 75.38  ? 221 TRP A CA  1 
ATOM   1807 C C   . TRP A 1 221 ? 18.510  -29.869 -28.263 1.00 76.80  ? 221 TRP A C   1 
ATOM   1808 O O   . TRP A 1 221 ? 19.626  -30.302 -27.967 1.00 78.87  ? 221 TRP A O   1 
ATOM   1809 C CB  . TRP A 1 221 ? 17.504  -31.655 -29.720 1.00 83.72  ? 221 TRP A CB  1 
ATOM   1810 C CG  . TRP A 1 221 ? 16.324  -32.558 -29.936 1.00 95.86  ? 221 TRP A CG  1 
ATOM   1811 C CD1 . TRP A 1 221 ? 15.302  -32.825 -29.067 1.00 99.08  ? 221 TRP A CD1 1 
ATOM   1812 C CD2 . TRP A 1 221 ? 16.015  -33.260 -31.151 1.00 101.42 ? 221 TRP A CD2 1 
ATOM   1813 N NE1 . TRP A 1 221 ? 14.385  -33.658 -29.643 1.00 97.42  ? 221 TRP A NE1 1 
ATOM   1814 C CE2 . TRP A 1 221 ? 14.797  -33.939 -30.920 1.00 103.06 ? 221 TRP A CE2 1 
ATOM   1815 C CE3 . TRP A 1 221 ? 16.653  -33.379 -32.391 1.00 101.69 ? 221 TRP A CE3 1 
ATOM   1816 C CZ2 . TRP A 1 221 ? 14.209  -34.734 -31.898 1.00 107.76 ? 221 TRP A CZ2 1 
ATOM   1817 C CZ3 . TRP A 1 221 ? 16.061  -34.157 -33.357 1.00 103.95 ? 221 TRP A CZ3 1 
ATOM   1818 C CH2 . TRP A 1 221 ? 14.853  -34.807 -33.110 1.00 107.67 ? 221 TRP A CH2 1 
ATOM   1819 N N   . GLU A 1 222 ? 18.234  -28.576 -28.431 1.00 72.16  ? 222 GLU A N   1 
ATOM   1820 C CA  . GLU A 1 222 ? 19.230  -27.555 -28.198 1.00 71.13  ? 222 GLU A CA  1 
ATOM   1821 C C   . GLU A 1 222 ? 19.092  -26.988 -26.791 1.00 72.58  ? 222 GLU A C   1 
ATOM   1822 O O   . GLU A 1 222 ? 20.101  -26.713 -26.158 1.00 80.30  ? 222 GLU A O   1 
ATOM   1823 C CB  . GLU A 1 222 ? 19.102  -26.468 -29.261 1.00 67.78  ? 222 GLU A CB  1 
ATOM   1824 C CG  . GLU A 1 222 ? 19.503  -26.939 -30.642 1.00 66.84  ? 222 GLU A CG  1 
ATOM   1825 C CD  . GLU A 1 222 ? 20.967  -27.323 -30.796 1.00 68.93  ? 222 GLU A CD  1 
ATOM   1826 O OE1 . GLU A 1 222 ? 21.841  -26.570 -30.310 1.00 69.65  ? 222 GLU A OE1 1 
ATOM   1827 O OE2 . GLU A 1 222 ? 21.235  -28.354 -31.440 1.00 68.09  ? 222 GLU A OE2 1 
ATOM   1828 N N   . VAL A 1 223 ? 17.866  -26.773 -26.310 1.00 70.97  ? 223 VAL A N   1 
ATOM   1829 C CA  . VAL A 1 223 ? 17.680  -25.960 -25.117 1.00 74.09  ? 223 VAL A CA  1 
ATOM   1830 C C   . VAL A 1 223 ? 17.607  -26.868 -23.896 1.00 77.88  ? 223 VAL A C   1 
ATOM   1831 O O   . VAL A 1 223 ? 18.036  -26.482 -22.808 1.00 78.82  ? 223 VAL A O   1 
ATOM   1832 C CB  . VAL A 1 223 ? 16.446  -25.035 -25.213 1.00 72.52  ? 223 VAL A CB  1 
ATOM   1833 C CG1 . VAL A 1 223 ? 15.137  -25.813 -25.220 1.00 71.68  ? 223 VAL A CG1 1 
ATOM   1834 C CG2 . VAL A 1 223 ? 16.430  -23.983 -24.106 1.00 72.28  ? 223 VAL A CG2 1 
ATOM   1835 N N   . ILE A 1 224 ? 17.045  -28.066 -24.080 1.00 80.28  ? 224 ILE A N   1 
ATOM   1836 C CA  . ILE A 1 224 ? 16.961  -29.017 -22.990 1.00 83.67  ? 224 ILE A CA  1 
ATOM   1837 C C   . ILE A 1 224 ? 18.343  -29.637 -22.844 1.00 88.85  ? 224 ILE A C   1 
ATOM   1838 O O   . ILE A 1 224 ? 18.816  -30.330 -23.744 1.00 87.33  ? 224 ILE A O   1 
ATOM   1839 C CB  . ILE A 1 224 ? 15.844  -30.049 -23.232 1.00 82.54  ? 224 ILE A CB  1 
ATOM   1840 C CG1 . ILE A 1 224 ? 14.495  -29.353 -23.423 1.00 78.58  ? 224 ILE A CG1 1 
ATOM   1841 C CG2 . ILE A 1 224 ? 15.796  -31.068 -22.104 1.00 87.38  ? 224 ILE A CG2 1 
ATOM   1842 C CD1 . ILE A 1 224 ? 13.406  -30.256 -23.939 1.00 78.83  ? 224 ILE A CD1 1 
ATOM   1843 N N   . LYS A 1 225 ? 18.978  -29.328 -21.708 1.00 97.52  ? 225 LYS A N   1 
ATOM   1844 C CA  . LYS A 1 225 ? 20.381  -29.625 -21.468 1.00 105.44 ? 225 LYS A CA  1 
ATOM   1845 C C   . LYS A 1 225 ? 20.601  -31.133 -21.500 1.00 108.24 ? 225 LYS A C   1 
ATOM   1846 O O   . LYS A 1 225 ? 21.555  -31.619 -22.104 1.00 108.52 ? 225 LYS A O   1 
ATOM   1847 C CB  . LYS A 1 225 ? 20.798  -29.064 -20.106 1.00 109.74 ? 225 LYS A CB  1 
ATOM   1848 C CG  . LYS A 1 225 ? 20.769  -27.546 -19.997 1.00 109.56 ? 225 LYS A CG  1 
ATOM   1849 C CD  . LYS A 1 225 ? 20.977  -27.056 -18.588 1.00 114.19 ? 225 LYS A CD  1 
ATOM   1850 C CE  . LYS A 1 225 ? 21.135  -25.554 -18.515 1.00 116.67 ? 225 LYS A CE  1 
ATOM   1851 N NZ  . LYS A 1 225 ? 21.441  -25.105 -17.137 1.00 121.30 ? 225 LYS A NZ  1 
ATOM   1852 N N   . LYS A 1 226 ? 19.678  -31.844 -20.845 1.00 108.18 ? 226 LYS A N   1 
ATOM   1853 C CA  . LYS A 1 226 ? 19.675  -33.295 -20.766 1.00 108.51 ? 226 LYS A CA  1 
ATOM   1854 C C   . LYS A 1 226 ? 19.834  -33.911 -22.156 1.00 102.47 ? 226 LYS A C   1 
ATOM   1855 O O   . LYS A 1 226 ? 20.272  -35.056 -22.268 1.00 102.66 ? 226 LYS A O   1 
ATOM   1856 C CB  . LYS A 1 226 ? 18.364  -33.786 -20.144 1.00 111.79 ? 226 LYS A CB  1 
ATOM   1857 C CG  . LYS A 1 226 ? 17.765  -32.896 -19.060 1.00 116.01 ? 226 LYS A CG  1 
ATOM   1858 C CD  . LYS A 1 226 ? 16.500  -33.449 -18.453 1.00 116.75 ? 226 LYS A CD  1 
ATOM   1859 C CE  . LYS A 1 226 ? 15.553  -34.021 -19.485 1.00 116.13 ? 226 LYS A CE  1 
ATOM   1860 N NZ  . LYS A 1 226 ? 14.264  -34.427 -18.879 1.00 118.84 ? 226 LYS A NZ  1 
ATOM   1861 N N   . PHE A 1 227 ? 19.447  -33.162 -23.201 1.00 95.57  ? 227 PHE A N   1 
ATOM   1862 C CA  . PHE A 1 227 ? 19.499  -33.642 -24.572 1.00 95.14  ? 227 PHE A CA  1 
ATOM   1863 C C   . PHE A 1 227 ? 20.808  -33.211 -25.239 1.00 97.85  ? 227 PHE A C   1 
ATOM   1864 O O   . PHE A 1 227 ? 21.816  -33.087 -24.514 1.00 102.19 ? 227 PHE A O   1 
ATOM   1865 C CB  . PHE A 1 227 ? 18.317  -33.104 -25.378 1.00 93.65  ? 227 PHE A CB  1 
ATOM   1866 C CG  . PHE A 1 227 ? 16.952  -33.595 -24.960 1.00 96.06  ? 227 PHE A CG  1 
ATOM   1867 C CD1 . PHE A 1 227 ? 16.763  -34.399 -23.844 1.00 101.96 ? 227 PHE A CD1 1 
ATOM   1868 C CD2 . PHE A 1 227 ? 15.842  -33.253 -25.712 1.00 97.05  ? 227 PHE A CD2 1 
ATOM   1869 C CE1 . PHE A 1 227 ? 15.496  -34.840 -23.491 1.00 106.16 ? 227 PHE A CE1 1 
ATOM   1870 C CE2 . PHE A 1 227 ? 14.574  -33.692 -25.362 1.00 99.19  ? 227 PHE A CE2 1 
ATOM   1871 C CZ  . PHE A 1 227 ? 14.402  -34.484 -24.250 1.00 104.41 ? 227 PHE A CZ  1 
HETATM 1872 S S   . SO4 B 2 .   ? 19.070  -21.506 -18.945 1.00 90.46  ? 301 SO4 A S   1 
HETATM 1873 O O1  . SO4 B 2 .   ? 19.258  -22.752 -19.645 1.00 82.07  ? 301 SO4 A O1  1 
HETATM 1874 O O2  . SO4 B 2 .   ? 18.031  -20.739 -19.575 1.00 87.76  ? 301 SO4 A O2  1 
HETATM 1875 O O3  . SO4 B 2 .   ? 18.690  -21.762 -17.576 1.00 93.27  ? 301 SO4 A O3  1 
HETATM 1876 O O4  . SO4 B 2 .   ? 20.299  -20.763 -18.985 1.00 84.48  ? 301 SO4 A O4  1 
HETATM 1877 S S   . SO3 C 3 .   ? -11.046 -34.832 -23.598 1.00 74.09  ? 302 SO3 A S   1 
HETATM 1878 O O1  . SO3 C 3 .   ? -9.729  -34.126 -23.580 1.00 63.39  ? 302 SO3 A O1  1 
HETATM 1879 O O2  . SO3 C 3 .   ? -11.763 -34.297 -24.824 1.00 63.64  ? 302 SO3 A O2  1 
HETATM 1880 O O3  . SO3 C 3 .   ? -10.662 -36.244 -23.930 1.00 63.32  ? 302 SO3 A O3  1 
HETATM 1881 C C1  . EDO D 4 .   ? 4.797   -26.605 -16.220 1.00 63.11  ? 303 EDO A C1  1 
HETATM 1882 O O1  . EDO D 4 .   ? 5.391   -27.449 -15.242 1.00 64.00  ? 303 EDO A O1  1 
HETATM 1883 C C2  . EDO D 4 .   ? 4.568   -27.292 -17.522 1.00 63.28  ? 303 EDO A C2  1 
HETATM 1884 O O2  . EDO D 4 .   ? 3.200   -27.590 -17.790 1.00 63.29  ? 303 EDO A O2  1 
HETATM 1885 C C1  . PEG E 5 .   ? -20.522 -12.238 -28.453 1.00 63.33  ? 304 PEG A C1  1 
HETATM 1886 O O1  . PEG E 5 .   ? -20.893 -12.089 -27.092 1.00 58.24  ? 304 PEG A O1  1 
HETATM 1887 C C2  . PEG E 5 .   ? -19.554 -13.384 -28.675 1.00 66.81  ? 304 PEG A C2  1 
HETATM 1888 O O2  . PEG E 5 .   ? -18.196 -12.960 -28.533 1.00 66.45  ? 304 PEG A O2  1 
HETATM 1889 C C3  . PEG E 5 .   ? -17.718 -12.129 -29.591 1.00 55.83  ? 304 PEG A C3  1 
HETATM 1890 C C4  . PEG E 5 .   ? -16.215 -12.241 -29.723 1.00 55.77  ? 304 PEG A C4  1 
HETATM 1891 O O4  . PEG E 5 .   ? -15.506 -12.115 -28.482 1.00 54.08  ? 304 PEG A O4  1 
HETATM 1892 O O   . HOH F 6 .   ? 20.193  -24.488 -42.393 1.00 29.97  ? 401 HOH A O   1 
HETATM 1893 O O   . HOH F 6 .   ? 26.875  -18.618 -32.063 1.00 21.83  ? 402 HOH A O   1 
HETATM 1894 O O   . HOH F 6 .   ? -6.307  -12.118 -45.363 1.00 67.85  ? 403 HOH A O   1 
HETATM 1895 O O   . HOH F 6 .   ? -6.047  -38.021 -22.825 1.00 29.59  ? 404 HOH A O   1 
HETATM 1896 O O   . HOH F 6 .   ? 17.794  -28.133 -19.418 1.00 39.41  ? 405 HOH A O   1 
HETATM 1897 O O   . HOH F 6 .   ? 2.562   -21.355 -22.358 1.00 39.88  ? 406 HOH A O   1 
HETATM 1898 O O   . HOH F 6 .   ? 22.793  -31.005 -26.395 1.00 47.94  ? 407 HOH A O   1 
HETATM 1899 O O   . HOH F 6 .   ? -0.378  -2.652  -33.770 1.00 23.67  ? 408 HOH A O   1 
HETATM 1900 O O   . HOH F 6 .   ? -13.973 -12.832 -33.066 1.00 30.69  ? 409 HOH A O   1 
HETATM 1901 O O   . HOH F 6 .   ? -4.337  -4.501  -37.167 1.00 38.25  ? 410 HOH A O   1 
HETATM 1902 O O   . HOH F 6 .   ? -5.529  -15.504 -48.876 1.00 46.21  ? 411 HOH A O   1 
HETATM 1903 O O   . HOH F 6 .   ? 5.364   -8.214  -46.163 1.00 36.57  ? 412 HOH A O   1 
HETATM 1904 O O   . HOH F 6 .   ? -8.108  -24.842 -47.999 1.00 30.07  ? 413 HOH A O   1 
HETATM 1905 O O   . HOH F 6 .   ? -21.279 -34.261 -34.765 1.00 38.47  ? 414 HOH A O   1 
HETATM 1906 O O   . HOH F 6 .   ? -26.236 -19.527 -25.551 1.00 35.20  ? 415 HOH A O   1 
HETATM 1907 O O   . HOH F 6 .   ? 1.436   -17.491 -20.954 1.00 40.63  ? 416 HOH A O   1 
HETATM 1908 O O   . HOH F 6 .   ? -9.882  -27.039 -19.835 1.00 21.66  ? 417 HOH A O   1 
HETATM 1909 O O   . HOH F 6 .   ? -19.090 -31.978 -26.779 1.00 44.45  ? 418 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   ? 1.3815 1.2526 1.0004 -0.2135 -0.3712 0.0026  2   GLU A N   
2    C CA  . GLU A 2   ? 1.3433 1.2258 1.0163 -0.2044 -0.3347 -0.0022 2   GLU A CA  
3    C C   . GLU A 2   ? 1.3424 1.2341 1.0954 -0.2091 -0.3510 -0.0043 2   GLU A C   
4    O O   . GLU A 2   ? 1.3187 1.2048 1.0942 -0.2096 -0.3365 -0.0196 2   GLU A O   
5    C CB  . GLU A 2   ? 1.3828 1.2473 1.0034 -0.2024 -0.3057 -0.0252 2   GLU A CB  
6    C CG  . GLU A 2   ? 1.3977 1.2613 0.9633 -0.1949 -0.2783 -0.0190 2   GLU A CG  
7    C CD  . GLU A 2   ? 1.4208 1.2781 0.9703 -0.1873 -0.2390 -0.0351 2   GLU A CD  
8    O OE1 . GLU A 2   ? 1.4383 1.2836 0.9954 -0.1897 -0.2362 -0.0567 2   GLU A OE1 
9    O OE2 . GLU A 2   ? 1.4204 1.2853 0.9563 -0.1785 -0.2123 -0.0254 2   GLU A OE2 
10   N N   . GLU A 3   ? 1.3383 1.2446 1.1387 -0.2124 -0.3812 0.0125  3   GLU A N   
11   C CA  . GLU A 3   ? 1.2868 1.2066 1.1739 -0.2172 -0.3968 0.0144  3   GLU A CA  
12   C C   . GLU A 3   ? 1.2075 1.1565 1.1671 -0.2084 -0.3896 0.0397  3   GLU A C   
13   O O   . GLU A 3   ? 1.2119 1.1778 1.2533 -0.2100 -0.3932 0.0449  3   GLU A O   
14   C CB  . GLU A 3   ? 1.3190 1.2260 1.1985 -0.2320 -0.4479 0.0046  3   GLU A CB  
15   C CG  . GLU A 3   ? 1.2721 1.1964 1.2503 -0.2381 -0.4708 0.0101  3   GLU A CG  
16   C CD  . GLU A 3   ? 1.3131 1.2223 1.2894 -0.2539 -0.5213 -0.0049 3   GLU A CD  
17   O OE1 . GLU A 3   ? 1.3074 1.2326 1.3680 -0.2597 -0.5461 0.0021  3   GLU A OE1 
18   O OE2 . GLU A 3   ? 1.3546 1.2360 1.2466 -0.2603 -0.5355 -0.0244 3   GLU A OE2 
19   N N   . LYS A 4   ? 1.1439 1.0987 1.0759 -0.1992 -0.3778 0.0548  4   LYS A N   
20   C CA  . LYS A 4   ? 1.0574 1.0375 1.0539 -0.1899 -0.3713 0.0764  4   LYS A CA  
21   C C   . LYS A 4   ? 0.9466 0.9395 0.9771 -0.1784 -0.3245 0.0773  4   LYS A C   
22   O O   . LYS A 4   ? 0.9372 0.9179 0.9280 -0.1760 -0.2980 0.0650  4   LYS A O   
23   C CB  . LYS A 4   ? 1.0589 1.0369 1.0127 -0.1854 -0.3802 0.0916  4   LYS A CB  
24   C CG  . LYS A 4   ? 1.0568 1.0246 0.9447 -0.1778 -0.3458 0.0890  4   LYS A CG  
25   C CD  . LYS A 4   ? 1.0806 1.0481 0.9398 -0.1732 -0.3514 0.1070  4   LYS A CD  
26   C CE  . LYS A 4   ? 1.1383 1.0875 0.9366 -0.1843 -0.3895 0.1107  4   LYS A CE  
27   N NZ  . LYS A 4   ? 1.1485 1.0911 0.8978 -0.1804 -0.3827 0.1260  4   LYS A NZ  
28   N N   . LYS A 5   ? 0.8540 0.8710 0.9576 -0.1709 -0.3150 0.0918  5   LYS A N   
29   C CA  . LYS A 5   ? 0.7929 0.8218 0.9247 -0.1595 -0.2718 0.0944  5   LYS A CA  
30   C C   . LYS A 5   ? 0.7617 0.7833 0.8340 -0.1490 -0.2473 0.0955  5   LYS A C   
31   O O   . LYS A 5   ? 0.7543 0.7794 0.8163 -0.1444 -0.2559 0.1063  5   LYS A O   
32   C CB  . LYS A 5   ? 0.7678 0.8240 0.9845 -0.1530 -0.2671 0.1092  5   LYS A CB  
33   C CG  . LYS A 5   ? 0.7769 0.8457 1.0697 -0.1624 -0.2845 0.1097  5   LYS A CG  
34   C CD  . LYS A 5   ? 0.7537 0.8511 1.1329 -0.1551 -0.2764 0.1237  5   LYS A CD  
35   C CE  . LYS A 5   ? 0.7625 0.8750 1.2250 -0.1642 -0.2833 0.1243  5   LYS A CE  
36   N NZ  . LYS A 5   ? 0.7686 0.9095 1.3190 -0.1591 -0.2884 0.1375  5   LYS A NZ  
37   N N   . ARG A 6   ? 0.7375 0.7487 0.7760 -0.1455 -0.2183 0.0850  6   ARG A N   
38   C CA  . ARG A 6   ? 0.7161 0.7235 0.7122 -0.1347 -0.1919 0.0859  6   ARG A CA  
39   C C   . ARG A 6   ? 0.6801 0.6935 0.6984 -0.1255 -0.1560 0.0848  6   ARG A C   
40   O O   . ARG A 6   ? 0.7216 0.7349 0.7687 -0.1296 -0.1500 0.0805  6   ARG A O   
41   C CB  . ARG A 6   ? 0.7366 0.7221 0.6564 -0.1392 -0.1934 0.0734  6   ARG A CB  
42   C CG  . ARG A 6   ? 0.7821 0.7572 0.6647 -0.1495 -0.2277 0.0735  6   ARG A CG  
43   C CD  . ARG A 6   ? 0.8136 0.7713 0.6192 -0.1500 -0.2183 0.0654  6   ARG A CD  
44   N NE  . ARG A 6   ? 0.8750 0.8196 0.6314 -0.1603 -0.2478 0.0658  6   ARG A NE  
45   C CZ  . ARG A 6   ? 0.9291 0.8605 0.6656 -0.1719 -0.2727 0.0534  6   ARG A CZ  
46   N NH1 . ARG A 6   ? 0.9477 0.8771 0.7137 -0.1751 -0.2708 0.0391  6   ARG A NH1 
47   N NH2 . ARG A 6   ? 0.9846 0.9034 0.6705 -0.1807 -0.3005 0.0557  6   ARG A NH2 
48   N N   . LEU A 7   ? 0.6232 0.6401 0.6263 -0.1136 -0.1337 0.0890  7   LEU A N   
49   C CA  . LEU A 7   ? 0.5985 0.6168 0.6066 -0.1044 -0.1016 0.0874  7   LEU A CA  
50   C C   . LEU A 7   ? 0.6222 0.6223 0.5741 -0.1037 -0.0907 0.0757  7   LEU A C   
51   O O   . LEU A 7   ? 0.6068 0.6003 0.5167 -0.1017 -0.0922 0.0734  7   LEU A O   
52   C CB  . LEU A 7   ? 0.5716 0.6034 0.5973 -0.0915 -0.0857 0.0964  7   LEU A CB  
53   C CG  . LEU A 7   ? 0.5583 0.5886 0.5729 -0.0804 -0.0544 0.0945  7   LEU A CG  
54   C CD1 . LEU A 7   ? 0.5406 0.5752 0.5888 -0.0811 -0.0382 0.0966  7   LEU A CD1 
55   C CD2 . LEU A 7   ? 0.5493 0.5891 0.5712 -0.0682 -0.0437 0.0997  7   LEU A CD2 
56   N N   . HIS A 8   ? 0.6474 0.6393 0.6032 -0.1055 -0.0794 0.0690  8   HIS A N   
57   C CA  . HIS A 8   ? 0.6701 0.6464 0.5844 -0.1023 -0.0657 0.0584  8   HIS A CA  
58   C C   . HIS A 8   ? 0.6488 0.6293 0.5672 -0.0896 -0.0396 0.0641  8   HIS A C   
59   O O   . HIS A 8   ? 0.6298 0.6136 0.5777 -0.0875 -0.0270 0.0698  8   HIS A O   
60   C CB  . HIS A 8   ? 0.7051 0.6665 0.6184 -0.1116 -0.0721 0.0465  8   HIS A CB  
61   C CG  . HIS A 8   ? 0.7583 0.7124 0.6537 -0.1234 -0.0993 0.0377  8   HIS A CG  
62   N ND1 . HIS A 8   ? 0.7866 0.7233 0.6331 -0.1274 -0.1037 0.0217  8   HIS A ND1 
63   C CD2 . HIS A 8   ? 0.7644 0.7259 0.6827 -0.1318 -0.1242 0.0425  8   HIS A CD2 
64   C CE1 . HIS A 8   ? 0.8229 0.7550 0.6569 -0.1383 -0.1305 0.0166  8   HIS A CE1 
65   N NE2 . HIS A 8   ? 0.7993 0.7461 0.6774 -0.1413 -0.1453 0.0297  8   HIS A NE2 
66   N N   . LEU A 9   ? 0.6385 0.6179 0.5254 -0.0818 -0.0324 0.0627  9   LEU A N   
67   C CA  . LEU A 9   ? 0.6350 0.6186 0.5220 -0.0693 -0.0129 0.0674  9   LEU A CA  
68   C C   . LEU A 9   ? 0.6620 0.6326 0.5167 -0.0645 -0.0026 0.0587  9   LEU A C   
69   O O   . LEU A 9   ? 0.6726 0.6392 0.4995 -0.0648 -0.0060 0.0525  9   LEU A O   
70   C CB  . LEU A 9   ? 0.6322 0.6262 0.5191 -0.0638 -0.0160 0.0731  9   LEU A CB  
71   C CG  . LEU A 9   ? 0.6474 0.6434 0.5273 -0.0508 0.0010  0.0743  9   LEU A CG  
72   C CD1 . LEU A 9   ? 0.6508 0.6521 0.5548 -0.0447 0.0167  0.0799  9   LEU A CD1 
73   C CD2 . LEU A 9   ? 0.6465 0.6499 0.5279 -0.0464 -0.0044 0.0780  9   LEU A CD2 
74   N N   . ILE A 10  ? 0.6307 0.5953 0.4921 -0.0598 0.0106  0.0599  10  ILE A N   
75   C CA  . ILE A 10  ? 0.5977 0.5498 0.4373 -0.0543 0.0188  0.0529  10  ILE A CA  
76   C C   . ILE A 10  ? 0.5662 0.5216 0.3993 -0.0417 0.0308  0.0585  10  ILE A C   
77   O O   . ILE A 10  ? 0.5253 0.4838 0.3713 -0.0374 0.0398  0.0677  10  ILE A O   
78   C CB  . ILE A 10  ? 0.6366 0.5763 0.4888 -0.0582 0.0215  0.0519  10  ILE A CB  
79   C CG1 . ILE A 10  ? 0.6454 0.5816 0.5088 -0.0713 0.0073  0.0454  10  ILE A CG1 
80   C CG2 . ILE A 10  ? 0.6379 0.5634 0.4731 -0.0519 0.0280  0.0446  10  ILE A CG2 
81   C CD1 . ILE A 10  ? 0.6447 0.5729 0.5366 -0.0766 0.0091  0.0492  10  ILE A CD1 
82   N N   . ILE A 11  ? 0.5935 0.5472 0.4058 -0.0363 0.0311  0.0523  11  ILE A N   
83   C CA  . ILE A 11  ? 0.5877 0.5407 0.3912 -0.0246 0.0388  0.0540  11  ILE A CA  
84   C C   . ILE A 11  ? 0.5958 0.5351 0.3939 -0.0209 0.0430  0.0514  11  ILE A C   
85   O O   . ILE A 11  ? 0.5929 0.5260 0.3839 -0.0220 0.0409  0.0417  11  ILE A O   
86   C CB  . ILE A 11  ? 0.5885 0.5460 0.3798 -0.0217 0.0354  0.0486  11  ILE A CB  
87   C CG1 . ILE A 11  ? 0.5619 0.5298 0.3593 -0.0269 0.0282  0.0521  11  ILE A CG1 
88   C CG2 . ILE A 11  ? 0.5930 0.5495 0.3781 -0.0098 0.0398  0.0490  11  ILE A CG2 
89   C CD1 . ILE A 11  ? 0.5827 0.5592 0.3971 -0.0225 0.0308  0.0600  11  ILE A CD1 
90   N N   . ALA A 12  ? 0.5950 0.5293 0.3976 -0.0167 0.0499  0.0608  12  ALA A N   
91   C CA  . ALA A 12  ? 0.5953 0.5143 0.3989 -0.0157 0.0517  0.0618  12  ALA A CA  
92   C C   . ALA A 12  ? 0.6146 0.5265 0.4030 -0.0038 0.0527  0.0635  12  ALA A C   
93   O O   . ALA A 12  ? 0.6168 0.5350 0.3936 0.0033  0.0539  0.0657  12  ALA A O   
94   C CB  . ALA A 12  ? 0.5836 0.4988 0.4029 -0.0205 0.0574  0.0735  12  ALA A CB  
95   N N   . ASP A 13  ? 0.6285 0.5264 0.4196 -0.0018 0.0504  0.0610  13  ASP A N   
96   C CA  . ASP A 13  ? 0.6411 0.5287 0.4224 0.0090  0.0481  0.0655  13  ASP A CA  
97   C C   . ASP A 13  ? 0.6460 0.5426 0.4164 0.0163  0.0435  0.0584  13  ASP A C   
98   O O   . ASP A 13  ? 0.7435 0.6365 0.4992 0.0254  0.0406  0.0639  13  ASP A O   
99   C CB  . ASP A 13  ? 0.6470 0.5270 0.4180 0.0124  0.0539  0.0831  13  ASP A CB  
100  C CG  . ASP A 13  ? 0.6680 0.5334 0.4530 0.0070  0.0569  0.0928  13  ASP A CG  
101  O OD1 . ASP A 13  ? 0.6614 0.5176 0.4628 0.0042  0.0516  0.0846  13  ASP A OD1 
102  O OD2 . ASP A 13  ? 0.6980 0.5608 0.4789 0.0057  0.0658  0.1083  13  ASP A OD2 
103  N N   . ALA A 14  ? 0.5960 0.5030 0.3727 0.0115  0.0423  0.0467  14  ALA A N   
104  C CA  . ALA A 14  ? 0.5912 0.5083 0.3636 0.0156  0.0390  0.0408  14  ALA A CA  
105  C C   . ALA A 14  ? 0.6291 0.5408 0.4051 0.0247  0.0325  0.0362  14  ALA A C   
106  O O   . ALA A 14  ? 0.6190 0.5231 0.4074 0.0254  0.0317  0.0315  14  ALA A O   
107  C CB  . ALA A 14  ? 0.5760 0.5029 0.3536 0.0067  0.0404  0.0323  14  ALA A CB  
108  N N   . GLU A 15  ? 0.6594 0.5751 0.4284 0.0318  0.0267  0.0361  15  GLU A N   
109  C CA  . GLU A 15  ? 0.6734 0.5859 0.4503 0.0403  0.0170  0.0313  15  GLU A CA  
110  C C   . GLU A 15  ? 0.6511 0.5751 0.4484 0.0364  0.0188  0.0199  15  GLU A C   
111  O O   . GLU A 15  ? 0.6423 0.5728 0.4471 0.0399  0.0126  0.0156  15  GLU A O   
112  C CB  . GLU A 15  ? 0.7029 0.6123 0.4614 0.0491  0.0081  0.0351  15  GLU A CB  
113  C CG  . GLU A 15  ? 0.7391 0.6362 0.4726 0.0527  0.0100  0.0477  15  GLU A CG  
114  C CD  . GLU A 15  ? 0.7438 0.6260 0.4804 0.0556  0.0059  0.0549  15  GLU A CD  
115  O OE1 . GLU A 15  ? 0.7723 0.6442 0.4935 0.0549  0.0116  0.0677  15  GLU A OE1 
116  O OE2 . GLU A 15  ? 0.7487 0.6298 0.5071 0.0584  -0.0021 0.0481  15  GLU A OE2 
117  N N   . LEU A 16  ? 0.6090 0.5343 0.4147 0.0285  0.0279  0.0148  16  LEU A N   
118  C CA  . LEU A 16  ? 0.5930 0.5277 0.4139 0.0239  0.0341  0.0045  16  LEU A CA  
119  C C   . LEU A 16  ? 0.5955 0.5240 0.4352 0.0262  0.0378  -0.0038 16  LEU A C   
120  O O   . LEU A 16  ? 0.5999 0.5203 0.4357 0.0219  0.0430  -0.0058 16  LEU A O   
121  C CB  . LEU A 16  ? 0.5974 0.5385 0.4056 0.0123  0.0421  0.0043  16  LEU A CB  
122  C CG  . LEU A 16  ? 0.5886 0.5378 0.4029 0.0054  0.0516  -0.0045 16  LEU A CG  
123  C CD1 . LEU A 16  ? 0.5619 0.5216 0.3893 0.0073  0.0502  -0.0042 16  LEU A CD1 
124  C CD2 . LEU A 16  ? 0.5947 0.5454 0.3888 -0.0061 0.0561  -0.0032 16  LEU A CD2 
125  N N   . GLU A 17  ? 0.5833 0.5155 0.4475 0.0332  0.0341  -0.0093 17  GLU A N   
126  C CA  . GLU A 17  ? 0.5864 0.5140 0.4772 0.0377  0.0371  -0.0181 17  GLU A CA  
127  C C   . GLU A 17  ? 0.5685 0.5089 0.4914 0.0412  0.0382  -0.0261 17  GLU A C   
128  O O   . GLU A 17  ? 0.5566 0.5056 0.4808 0.0419  0.0315  -0.0226 17  GLU A O   
129  C CB  . GLU A 17  ? 0.6130 0.5249 0.5074 0.0471  0.0238  -0.0103 17  GLU A CB  
130  C CG  . GLU A 17  ? 0.6382 0.5493 0.5297 0.0559  0.0063  -0.0019 17  GLU A CG  
131  C CD  . GLU A 17  ? 0.6936 0.5865 0.5755 0.0641  -0.0074 0.0101  17  GLU A CD  
132  O OE1 . GLU A 17  ? 0.7697 0.6574 0.6210 0.0661  -0.0150 0.0211  17  GLU A OE1 
133  O OE2 . GLU A 17  ? 0.6796 0.5627 0.5842 0.0686  -0.0098 0.0086  17  GLU A OE2 
134  N N   . THR A 18  ? 0.5593 0.5008 0.5120 0.0435  0.0474  -0.0376 18  THR A N   
135  C CA  . THR A 18  ? 0.5294 0.4836 0.5234 0.0483  0.0485  -0.0449 18  THR A CA  
136  C C   . THR A 18  ? 0.5201 0.4665 0.5371 0.0610  0.0263  -0.0398 18  THR A C   
137  O O   . THR A 18  ? 0.5248 0.4551 0.5221 0.0653  0.0143  -0.0308 18  THR A O   
138  C CB  . THR A 18  ? 0.5337 0.4948 0.5533 0.0457  0.0707  -0.0606 18  THR A CB  
139  O OG1 . THR A 18  ? 0.5426 0.4919 0.5852 0.0539  0.0687  -0.0673 18  THR A OG1 
140  C CG2 . THR A 18  ? 0.5349 0.4980 0.5190 0.0328  0.0900  -0.0647 18  THR A CG2 
141  N N   . VAL A 19  ? 0.5273 0.4851 0.5865 0.0666  0.0204  -0.0445 19  VAL A N   
142  C CA  . VAL A 19  ? 0.5458 0.4960 0.6233 0.0785  -0.0060 -0.0385 19  VAL A CA  
143  C C   . VAL A 19  ? 0.5758 0.5086 0.6584 0.0853  -0.0101 -0.0368 19  VAL A C   
144  O O   . VAL A 19  ? 0.6299 0.5635 0.7344 0.0842  0.0073  -0.0477 19  VAL A O   
145  C CB  . VAL A 19  ? 0.5261 0.4922 0.6591 0.0832  -0.0129 -0.0455 19  VAL A CB  
146  C CG1 . VAL A 19  ? 0.5347 0.4910 0.6862 0.0960  -0.0448 -0.0393 19  VAL A CG1 
147  C CG2 . VAL A 19  ? 0.5211 0.5014 0.6481 0.0753  -0.0097 -0.0452 19  VAL A CG2 
148  N N   . PRO A 20  ? 0.5587 0.4735 0.6163 0.0915  -0.0311 -0.0228 20  PRO A N   
149  C CA  . PRO A 20  ? 0.5759 0.4719 0.6439 0.0987  -0.0387 -0.0179 20  PRO A CA  
150  C C   . PRO A 20  ? 0.5811 0.4798 0.7117 0.1095  -0.0483 -0.0253 20  PRO A C   
151  O O   . PRO A 20  ? 0.5716 0.4808 0.7307 0.1150  -0.0638 -0.0266 20  PRO A O   
152  C CB  . PRO A 20  ? 0.5924 0.4711 0.6174 0.1027  -0.0604 0.0012  20  PRO A CB  
153  C CG  . PRO A 20  ? 0.5783 0.4661 0.5619 0.0944  -0.0532 0.0028  20  PRO A CG  
154  C CD  . PRO A 20  ? 0.5538 0.4639 0.5697 0.0917  -0.0467 -0.0110 20  PRO A CD  
155  N N   . PRO A 21  ? 0.6051 0.4944 0.7634 0.1127  -0.0399 -0.0315 21  PRO A N   
156  C CA  . PRO A 21  ? 0.6327 0.5237 0.8575 0.1240  -0.0473 -0.0396 21  PRO A CA  
157  C C   . PRO A 21  ? 0.6668 0.5511 0.9089 0.1358  -0.0830 -0.0261 21  PRO A C   
158  O O   . PRO A 21  ? 0.6626 0.5600 0.9627 0.1433  -0.0923 -0.0337 21  PRO A O   
159  C CB  . PRO A 21  ? 0.6379 0.5088 0.8706 0.1263  -0.0404 -0.0413 21  PRO A CB  
160  C CG  . PRO A 21  ? 0.6281 0.4980 0.8124 0.1127  -0.0165 -0.0457 21  PRO A CG  
161  C CD  . PRO A 21  ? 0.6133 0.4897 0.7454 0.1056  -0.0226 -0.0330 21  PRO A CD  
162  N N   . GLU A 22  ? 0.7007 0.5647 0.8914 0.1368  -0.1024 -0.0061 22  GLU A N   
163  C CA  . GLU A 22  ? 0.7375 0.5890 0.9280 0.1474  -0.1388 0.0092  22  GLU A CA  
164  C C   . GLU A 22  ? 0.7350 0.6061 0.9497 0.1500  -0.1537 0.0022  22  GLU A C   
165  O O   . GLU A 22  ? 0.7581 0.6275 1.0146 0.1607  -0.1810 0.0047  22  GLU A O   
166  C CB  . GLU A 22  ? 0.7674 0.5979 0.8835 0.1449  -0.1498 0.0303  22  GLU A CB  
167  C CG  . GLU A 22  ? 0.7881 0.5977 0.8839 0.1419  -0.1383 0.0407  22  GLU A CG  
168  C CD  . GLU A 22  ? 0.7777 0.5945 0.8417 0.1283  -0.1067 0.0337  22  GLU A CD  
169  O OE1 . GLU A 22  ? 0.7670 0.5676 0.7895 0.1232  -0.1019 0.0478  22  GLU A OE1 
170  O OE2 . GLU A 22  ? 0.7929 0.6316 0.8742 0.1223  -0.0875 0.0151  22  GLU A OE2 
171  N N   . ILE A 23  ? 0.7164 0.6051 0.9089 0.1401  -0.1377 -0.0059 23  ILE A N   
172  C CA  . ILE A 23  ? 0.7186 0.6215 0.9240 0.1411  -0.1547 -0.0099 23  ILE A CA  
173  C C   . ILE A 23  ? 0.7159 0.6475 0.9758 0.1353  -0.1323 -0.0280 23  ILE A C   
174  O O   . ILE A 23  ? 0.7122 0.6575 0.9728 0.1308  -0.1357 -0.0321 23  ILE A O   
175  C CB  . ILE A 23  ? 0.7144 0.6103 0.8474 0.1355  -0.1602 -0.0017 23  ILE A CB  
176  C CG1 . ILE A 23  ? 0.6744 0.5771 0.7712 0.1228  -0.1265 -0.0053 23  ILE A CG1 
177  C CG2 . ILE A 23  ? 0.7560 0.6243 0.8385 0.1424  -0.1841 0.0169  23  ILE A CG2 
178  C CD1 . ILE A 23  ? 0.6596 0.5627 0.7050 0.1175  -0.1293 -0.0023 23  ILE A CD1 
179  N N   . LEU A 24  ? 0.7138 0.6539 1.0215 0.1358  -0.1095 -0.0391 24  LEU A N   
180  C CA  . LEU A 24  ? 0.6839 0.6510 1.0410 0.1300  -0.0841 -0.0553 24  LEU A CA  
181  C C   . LEU A 24  ? 0.7175 0.6996 1.1440 0.1375  -0.1065 -0.0592 24  LEU A C   
182  O O   . LEU A 24  ? 0.7071 0.7129 1.1739 0.1318  -0.0917 -0.0690 24  LEU A O   
183  C CB  . LEU A 24  ? 0.6699 0.6400 1.0546 0.1294  -0.0526 -0.0679 24  LEU A CB  
184  C CG  . LEU A 24  ? 0.6829 0.6413 1.0063 0.1199  -0.0284 -0.0678 24  LEU A CG  
185  C CD1 . LEU A 24  ? 0.6914 0.6494 1.0450 0.1211  -0.0019 -0.0833 24  LEU A CD1 
186  C CD2 . LEU A 24  ? 0.6802 0.6513 0.9632 0.1061  -0.0092 -0.0690 24  LEU A CD2 
187  N N   . ASP A 25  ? 0.7495 0.7172 1.1895 0.1496  -0.1441 -0.0501 25  ASP A N   
188  C CA  . ASP A 25  ? 0.7876 0.7683 1.2983 0.1575  -0.1707 -0.0537 25  ASP A CA  
189  C C   . ASP A 25  ? 0.8066 0.7740 1.2782 0.1607  -0.2128 -0.0423 25  ASP A C   
190  O O   . ASP A 25  ? 0.8466 0.8110 1.3580 0.1709  -0.2497 -0.0393 25  ASP A O   
191  C CB  . ASP A 25  ? 0.8283 0.8056 1.4062 0.1707  -0.1810 -0.0555 25  ASP A CB  
192  C CG  . ASP A 25  ? 0.9108 0.8558 1.4447 0.1786  -0.2005 -0.0400 25  ASP A CG  
193  O OD1 . ASP A 25  ? 0.9859 0.9122 1.4361 0.1739  -0.2078 -0.0269 25  ASP A OD1 
194  O OD2 . ASP A 25  ? 0.8954 0.8339 1.4805 0.1890  -0.2063 -0.0406 25  ASP A OD2 
195  N N   . HIS A 26  ? 0.7759 0.7345 1.1699 0.1524  -0.2081 -0.0369 26  HIS A N   
196  C CA  . HIS A 26  ? 0.7976 0.7461 1.1538 0.1542  -0.2429 -0.0311 26  HIS A CA  
197  C C   . HIS A 26  ? 0.7947 0.7678 1.1956 0.1473  -0.2397 -0.0437 26  HIS A C   
198  O O   . HIS A 26  ? 0.8064 0.7973 1.2200 0.1368  -0.2034 -0.0512 26  HIS A O   
199  C CB  . HIS A 26  ? 0.8137 0.7409 1.0724 0.1501  -0.2385 -0.0203 26  HIS A CB  
200  C CG  . HIS A 26  ? 0.8600 0.7737 1.0706 0.1528  -0.2714 -0.0161 26  HIS A CG  
201  N ND1 . HIS A 26  ? 0.8449 0.7705 1.0596 0.1473  -0.2763 -0.0263 26  HIS A ND1 
202  C CD2 . HIS A 26  ? 0.9063 0.7940 1.0604 0.1604  -0.3003 -0.0034 26  HIS A CD2 
203  C CE1 . HIS A 26  ? 0.8726 0.7796 1.0353 0.1521  -0.3078 -0.0226 26  HIS A CE1 
204  N NE2 . HIS A 26  ? 0.9151 0.7991 1.0371 0.1600  -0.3220 -0.0083 26  HIS A NE2 
205  N N   . PRO A 27  ? 0.7758 0.7496 1.2020 0.1521  -0.2782 -0.0459 27  PRO A N   
206  C CA  . PRO A 27  ? 0.7345 0.7316 1.2141 0.1450  -0.2771 -0.0575 27  PRO A CA  
207  C C   . PRO A 27  ? 0.7120 0.7171 1.1552 0.1311  -0.2434 -0.0608 27  PRO A C   
208  O O   . PRO A 27  ? 0.6788 0.7073 1.1722 0.1224  -0.2149 -0.0677 27  PRO A O   
209  C CB  . PRO A 27  ? 0.7616 0.7443 1.2243 0.1514  -0.3280 -0.0567 27  PRO A CB  
210  C CG  . PRO A 27  ? 0.8018 0.7657 1.2612 0.1652  -0.3587 -0.0466 27  PRO A CG  
211  C CD  . PRO A 27  ? 0.8006 0.7538 1.2166 0.1648  -0.3262 -0.0374 27  PRO A CD  
212  N N   . ALA A 28  ? 0.7188 0.7037 1.0746 0.1294  -0.2456 -0.0544 28  ALA A N   
213  C CA  . ALA A 28  ? 0.6758 0.6638 0.9923 0.1182  -0.2250 -0.0565 28  ALA A CA  
214  C C   . ALA A 28  ? 0.6490 0.6506 0.9708 0.1087  -0.1786 -0.0562 28  ALA A C   
215  O O   . ALA A 28  ? 0.6026 0.6169 0.9300 0.0978  -0.1569 -0.0592 28  ALA A O   
216  C CB  . ALA A 28  ? 0.6876 0.6509 0.9145 0.1207  -0.2367 -0.0500 28  ALA A CB  
217  N N   . ILE A 29  ? 0.6497 0.6467 0.9702 0.1131  -0.1654 -0.0526 29  ILE A N   
218  C CA  . ILE A 29  ? 0.6219 0.6287 0.9428 0.1051  -0.1238 -0.0544 29  ILE A CA  
219  C C   . ILE A 29  ? 0.6333 0.6661 1.0341 0.1012  -0.1042 -0.0641 29  ILE A C   
220  O O   . ILE A 29  ? 0.6097 0.6548 1.0089 0.0904  -0.0698 -0.0669 29  ILE A O   
221  C CB  . ILE A 29  ? 0.6305 0.6209 0.9240 0.1113  -0.1189 -0.0490 29  ILE A CB  
222  C CG1 . ILE A 29  ? 0.6510 0.6173 0.8652 0.1132  -0.1328 -0.0375 29  ILE A CG1 
223  C CG2 . ILE A 29  ? 0.6155 0.6148 0.9145 0.1039  -0.0787 -0.0545 29  ILE A CG2 
224  C CD1 . ILE A 29  ? 0.6319 0.5978 0.7906 0.1023  -0.1118 -0.0353 29  ILE A CD1 
225  N N   . VAL A 30  ? 0.6633 0.7045 1.1334 0.1097  -0.1261 -0.0686 30  VAL A N   
226  C CA  . VAL A 30  ? 0.6813 0.7489 1.2371 0.1074  -0.1067 -0.0780 30  VAL A CA  
227  C C   . VAL A 30  ? 0.7192 0.8037 1.3011 0.0965  -0.1028 -0.0801 30  VAL A C   
228  O O   . VAL A 30  ? 0.7730 0.8775 1.3879 0.0867  -0.0679 -0.0839 30  VAL A O   
229  C CB  . VAL A 30  ? 0.7169 0.7884 1.3460 0.1208  -0.1339 -0.0816 30  VAL A CB  
230  C CG1 . VAL A 30  ? 0.7142 0.8155 1.4385 0.1187  -0.1085 -0.0923 30  VAL A CG1 
231  C CG2 . VAL A 30  ? 0.7386 0.7893 1.3439 0.1324  -0.1444 -0.0769 30  VAL A CG2 
232  N N   . ASN A 31  ? 0.7331 0.8081 1.3006 0.0983  -0.1394 -0.0777 31  ASN A N   
233  C CA  . ASN A 31  ? 0.7386 0.8257 1.3343 0.0889  -0.1430 -0.0801 31  ASN A CA  
234  C C   . ASN A 31  ? 0.7357 0.8232 1.2817 0.0754  -0.1102 -0.0755 31  ASN A C   
235  O O   . ASN A 31  ? 0.7048 0.8076 1.2857 0.0644  -0.0958 -0.0759 31  ASN A O   
236  C CB  . ASN A 31  ? 0.7687 0.8395 1.3433 0.0944  -0.1904 -0.0807 31  ASN A CB  
237  C CG  . ASN A 31  ? 0.7680 0.8362 1.3884 0.1076  -0.2302 -0.0838 31  ASN A CG  
238  O OD1 . ASN A 31  ? 0.7554 0.8447 1.4640 0.1089  -0.2281 -0.0887 31  ASN A OD1 
239  N ND2 . ASN A 31  ? 0.7902 0.8329 1.3522 0.1172  -0.2658 -0.0802 31  ASN A ND2 
240  N N   . TYR A 32  ? 0.7472 0.8164 1.2128 0.0762  -0.1023 -0.0699 32  TYR A N   
241  C CA  . TYR A 32  ? 0.7236 0.7909 1.1379 0.0646  -0.0747 -0.0646 32  TYR A CA  
242  C C   . TYR A 32  ? 0.7396 0.8226 1.1738 0.0570  -0.0321 -0.0655 32  TYR A C   
243  O O   . TYR A 32  ? 0.7345 0.8279 1.1707 0.0446  -0.0071 -0.0623 32  TYR A O   
244  C CB  . TYR A 32  ? 0.7119 0.7555 1.0424 0.0689  -0.0836 -0.0589 32  TYR A CB  
245  C CG  . TYR A 32  ? 0.7030 0.7438 0.9809 0.0581  -0.0583 -0.0529 32  TYR A CG  
246  C CD1 . TYR A 32  ? 0.7035 0.7497 0.9684 0.0516  -0.0247 -0.0512 32  TYR A CD1 
247  C CD2 . TYR A 32  ? 0.7062 0.7381 0.9491 0.0548  -0.0695 -0.0499 32  TYR A CD2 
248  C CE1 . TYR A 32  ? 0.6979 0.7411 0.9163 0.0416  -0.0055 -0.0449 32  TYR A CE1 
249  C CE2 . TYR A 32  ? 0.6840 0.7137 0.8855 0.0455  -0.0490 -0.0434 32  TYR A CE2 
250  C CZ  . TYR A 32  ? 0.6830 0.7186 0.8726 0.0387  -0.0183 -0.0401 32  TYR A CZ  
251  O OH  . TYR A 32  ? 0.7308 0.7636 0.8801 0.0296  -0.0021 -0.0330 32  TYR A OH  
252  N N   . ALA A 33  ? 0.7421 0.8251 1.1904 0.0649  -0.0248 -0.0700 33  ALA A N   
253  C CA  . ALA A 33  ? 0.7569 0.8513 1.2163 0.0596  0.0155  -0.0744 33  ALA A CA  
254  C C   . ALA A 33  ? 0.7491 0.8696 1.2851 0.0534  0.0350  -0.0790 33  ALA A C   
255  O O   . ALA A 33  ? 0.7437 0.8752 1.2766 0.0429  0.0728  -0.0792 33  ALA A O   
256  C CB  . ALA A 33  ? 0.7900 0.8763 1.2538 0.0709  0.0148  -0.0801 33  ALA A CB  
257  N N   . LYS A 34  ? 0.7708 0.9002 1.3735 0.0597  0.0079  -0.0820 34  LYS A N   
258  C CA  . LYS A 34  ? 0.7863 0.9420 1.4745 0.0541  0.0214  -0.0857 34  LYS A CA  
259  C C   . LYS A 34  ? 0.7482 0.9092 1.4227 0.0385  0.0345  -0.0773 34  LYS A C   
260  O O   . LYS A 34  ? 0.7223 0.8986 1.4120 0.0274  0.0739  -0.0754 34  LYS A O   
261  C CB  . LYS A 34  ? 0.8433 1.0043 1.6032 0.0649  -0.0186 -0.0904 34  LYS A CB  
262  C CG  . LYS A 34  ? 0.9012 1.0923 1.7675 0.0612  -0.0054 -0.0958 34  LYS A CG  
263  C CD  . LYS A 34  ? 0.9326 1.1302 1.8779 0.0746  -0.0435 -0.1024 34  LYS A CD  
264  C CE  . LYS A 34  ? 0.9756 1.1559 1.9028 0.0794  -0.0987 -0.0997 34  LYS A CE  
265  N NZ  . LYS A 34  ? 1.0194 1.2054 1.9570 0.0664  -0.1025 -0.0967 34  LYS A NZ  
266  N N   . ARG A 35  ? 0.7560 0.9022 1.3971 0.0378  0.0029  -0.0721 35  ARG A N   
267  C CA  . ARG A 35  ? 0.8034 0.9518 1.4366 0.0239  0.0108  -0.0639 35  ARG A CA  
268  C C   . ARG A 35  ? 0.7747 0.9219 1.3521 0.0128  0.0513  -0.0560 35  ARG A C   
269  O O   . ARG A 35  ? 0.7665 0.9266 1.3657 -0.0003 0.0781  -0.0492 35  ARG A O   
270  C CB  . ARG A 35  ? 0.8672 0.9959 1.4618 0.0266  -0.0280 -0.0621 35  ARG A CB  
271  C CG  . ARG A 35  ? 0.9445 1.0763 1.6011 0.0321  -0.0675 -0.0692 35  ARG A CG  
272  C CD  . ARG A 35  ? 1.0268 1.1405 1.6510 0.0319  -0.1005 -0.0698 35  ARG A CD  
273  N NE  . ARG A 35  ? 1.1543 1.2453 1.6844 0.0357  -0.1027 -0.0663 35  ARG A NE  
274  C CZ  . ARG A 35  ? 1.2249 1.2968 1.7069 0.0482  -0.1306 -0.0703 35  ARG A CZ  
275  N NH1 . ARG A 35  ? 1.1923 1.2465 1.5951 0.0497  -0.1270 -0.0660 35  ARG A NH1 
276  N NH2 . ARG A 35  ? 1.2865 1.3571 1.8002 0.0590  -0.1619 -0.0774 35  ARG A NH2 
277  N N   . ARG A 36  ? 0.8029 0.9343 1.3101 0.0175  0.0554  -0.0561 36  ARG A N   
278  C CA  . ARG A 36  ? 0.7827 0.9100 1.2311 0.0074  0.0876  -0.0493 36  ARG A CA  
279  C C   . ARG A 36  ? 0.7593 0.9003 1.2262 0.0048  0.1266  -0.0554 36  ARG A C   
280  O O   . ARG A 36  ? 0.7318 0.8679 1.1454 -0.0026 0.1526  -0.0522 36  ARG A O   
281  C CB  . ARG A 36  ? 0.8029 0.9075 1.1713 0.0124  0.0746  -0.0473 36  ARG A CB  
282  C CG  . ARG A 36  ? 0.8654 0.9571 1.1980 0.0096  0.0522  -0.0389 36  ARG A CG  
283  C CD  . ARG A 36  ? 0.9212 0.9970 1.1764 0.0073  0.0569  -0.0328 36  ARG A CD  
284  N NE  . ARG A 36  ? 0.9334 1.0140 1.1660 -0.0020 0.0913  -0.0301 36  ARG A NE  
285  C CZ  . ARG A 36  ? 0.9319 1.0029 1.1156 -0.0008 0.1006  -0.0321 36  ARG A CZ  
286  N NH1 . ARG A 36  ? 0.8625 0.9184 1.0114 0.0078  0.0801  -0.0330 36  ARG A NH1 
287  N NH2 . ARG A 36  ? 0.9772 1.0531 1.1450 -0.0090 0.1311  -0.0327 36  ARG A NH2 
288  N N   . LYS A 37  ? 0.7435 0.9014 1.2863 0.0111  0.1298  -0.0650 37  LYS A N   
289  C CA  . LYS A 37  ? 0.7373 0.9110 1.3097 0.0093  0.1697  -0.0733 37  LYS A CA  
290  C C   . LYS A 37  ? 0.6905 0.8487 1.1917 0.0114  0.1858  -0.0784 37  LYS A C   
291  O O   . LYS A 37  ? 0.6681 0.8289 1.1367 0.0015  0.2217  -0.0780 37  LYS A O   
292  C CB  . LYS A 37  ? 0.7705 0.9615 1.3643 -0.0069 0.2047  -0.0650 37  LYS A CB  
293  C CG  . LYS A 37  ? 0.8007 1.0074 1.4714 -0.0112 0.1909  -0.0593 37  LYS A CG  
294  C CD  . LYS A 37  ? 0.8520 1.0791 1.5589 -0.0270 0.2319  -0.0511 37  LYS A CD  
295  C CE  . LYS A 37  ? 0.8889 1.1042 1.5177 -0.0418 0.2526  -0.0355 37  LYS A CE  
296  N NZ  . LYS A 37  ? 0.9068 1.1404 1.5665 -0.0576 0.2946  -0.0250 37  LYS A NZ  
297  N N   . LYS A 38  ? 0.6560 0.7965 1.1306 0.0235  0.1578  -0.0824 38  LYS A N   
298  C CA  . LYS A 38  ? 0.6904 0.8144 1.1018 0.0252  0.1687  -0.0871 38  LYS A CA  
299  C C   . LYS A 38  ? 0.6960 0.8095 1.1241 0.0411  0.1470  -0.0959 38  LYS A C   
300  O O   . LYS A 38  ? 0.6956 0.8038 1.1435 0.0500  0.1112  -0.0919 38  LYS A O   
301  C CB  . LYS A 38  ? 0.7046 0.8112 1.0361 0.0178  0.1578  -0.0748 38  LYS A CB  
302  C CG  . LYS A 38  ? 0.7369 0.8368 1.0067 0.0080  0.1868  -0.0753 38  LYS A CG  
303  C CD  . LYS A 38  ? 0.7525 0.8335 0.9500 0.0044  0.1701  -0.0653 38  LYS A CD  
304  C CE  . LYS A 38  ? 0.7851 0.8594 0.9230 -0.0063 0.1945  -0.0653 38  LYS A CE  
305  N NZ  . LYS A 38  ? 0.8021 0.8740 0.9403 -0.0019 0.2146  -0.0825 38  LYS A NZ  
306  N N   . ARG A 39  ? 0.6916 0.8002 1.1096 0.0445  0.1685  -0.1078 39  ARG A N   
307  C CA  . ARG A 39  ? 0.6857 0.7818 1.1194 0.0589  0.1512  -0.1154 39  ARG A CA  
308  C C   . ARG A 39  ? 0.6777 0.7503 1.0543 0.0623  0.1174  -0.1038 39  ARG A C   
309  O O   . ARG A 39  ? 0.6631 0.7231 0.9723 0.0547  0.1234  -0.0992 39  ARG A O   
310  C CB  . ARG A 39  ? 0.7086 0.8002 1.1302 0.0595  0.1825  -0.1310 39  ARG A CB  
311  C CG  . ARG A 39  ? 0.7347 0.8479 1.2240 0.0614  0.2155  -0.1467 39  ARG A CG  
312  C CD  . ARG A 39  ? 0.7780 0.8858 1.2304 0.0568  0.2534  -0.1623 39  ARG A CD  
313  N NE  . ARG A 39  ? 0.7950 0.9103 1.3099 0.0674  0.2739  -0.1830 39  ARG A NE  
314  C CZ  . ARG A 39  ? 0.8315 0.9699 1.3962 0.0654  0.3108  -0.1947 39  ARG A CZ  
315  N NH1 . ARG A 39  ? 0.8755 1.0168 1.4822 0.0747  0.3348  -0.2170 39  ARG A NH1 
316  N NH2 . ARG A 39  ? 0.8242 0.9819 1.3956 0.0536  0.3263  -0.1844 39  ARG A NH2 
317  N N   . PRO A 40  ? 0.6643 0.7296 1.0660 0.0742  0.0815  -0.0991 40  PRO A N   
318  C CA  . PRO A 40  ? 0.6570 0.7018 1.0050 0.0769  0.0505  -0.0863 40  PRO A CA  
319  C C   . PRO A 40  ? 0.6393 0.6642 0.9229 0.0744  0.0574  -0.0842 40  PRO A C   
320  O O   . PRO A 40  ? 0.6333 0.6472 0.8615 0.0699  0.0468  -0.0737 40  PRO A O   
321  C CB  . PRO A 40  ? 0.6675 0.7051 1.0555 0.0917  0.0172  -0.0847 40  PRO A CB  
322  C CG  . PRO A 40  ? 0.6533 0.7139 1.1270 0.0952  0.0234  -0.0943 40  PRO A CG  
323  C CD  . PRO A 40  ? 0.6560 0.7316 1.1386 0.0860  0.0690  -0.1056 40  PRO A CD  
324  N N   . GLU A 41  ? 0.6430 0.6640 0.9392 0.0774  0.0756  -0.0956 41  GLU A N   
325  C CA  . GLU A 41  ? 0.6550 0.6559 0.9013 0.0759  0.0797  -0.0956 41  GLU A CA  
326  C C   . GLU A 41  ? 0.6720 0.6741 0.8631 0.0613  0.1025  -0.0962 41  GLU A C   
327  O O   . GLU A 41  ? 0.6842 0.6704 0.8296 0.0579  0.1027  -0.0944 41  GLU A O   
328  C CB  . GLU A 41  ? 0.6516 0.6462 0.9336 0.0840  0.0906  -0.1101 41  GLU A CB  
329  C CG  . GLU A 41  ? 0.6394 0.6524 0.9611 0.0816  0.1250  -0.1287 41  GLU A CG  
330  C CD  . GLU A 41  ? 0.6104 0.6442 1.0123 0.0894  0.1242  -0.1337 41  GLU A CD  
331  O OE1 . GLU A 41  ? 0.6003 0.6483 1.0430 0.0897  0.1542  -0.1503 41  GLU A OE1 
332  O OE2 . GLU A 41  ? 0.5812 0.6170 1.0055 0.0951  0.0936  -0.1218 41  GLU A OE2 
333  N N   . LYS A 42  ? 0.6805 0.7009 0.8782 0.0526  0.1202  -0.0974 42  LYS A N   
334  C CA  . LYS A 42  ? 0.6842 0.7058 0.8302 0.0385  0.1390  -0.0951 42  LYS A CA  
335  C C   . LYS A 42  ? 0.6528 0.6722 0.7636 0.0332  0.1204  -0.0783 42  LYS A C   
336  O O   . LYS A 42  ? 0.6336 0.6501 0.6975 0.0226  0.1285  -0.0731 42  LYS A O   
337  C CB  . LYS A 42  ? 0.7110 0.7524 0.8800 0.0308  0.1687  -0.1016 42  LYS A CB  
338  C CG  . LYS A 42  ? 0.7393 0.7894 0.9566 0.0364  0.1928  -0.1200 42  LYS A CG  
339  C CD  . LYS A 42  ? 0.7685 0.8084 0.9490 0.0324  0.2172  -0.1347 42  LYS A CD  
340  C CE  . LYS A 42  ? 0.8079 0.8633 1.0248 0.0318  0.2541  -0.1520 42  LYS A CE  
341  N NZ  . LYS A 42  ? 0.8757 0.9178 1.0716 0.0336  0.2729  -0.1725 42  LYS A NZ  
342  N N   . ILE A 43  ? 0.6297 0.6507 0.7655 0.0406  0.0953  -0.0710 43  ILE A N   
343  C CA  . ILE A 43  ? 0.6136 0.6348 0.7270 0.0365  0.0796  -0.0586 43  ILE A CA  
344  C C   . ILE A 43  ? 0.5788 0.5820 0.6400 0.0378  0.0643  -0.0502 43  ILE A C   
345  O O   . ILE A 43  ? 0.5857 0.5764 0.6443 0.0459  0.0538  -0.0508 43  ILE A O   
346  C CB  . ILE A 43  ? 0.5925 0.6213 0.7531 0.0440  0.0583  -0.0573 43  ILE A CB  
347  C CG1 . ILE A 43  ? 0.6016 0.6513 0.8191 0.0403  0.0761  -0.0638 43  ILE A CG1 
348  C CG2 . ILE A 43  ? 0.5784 0.6020 0.7124 0.0426  0.0374  -0.0472 43  ILE A CG2 
349  C CD1 . ILE A 43  ? 0.6055 0.6645 0.8780 0.0462  0.0539  -0.0636 43  ILE A CD1 
350  N N   . ILE A 44  ? 0.5465 0.5484 0.5706 0.0299  0.0632  -0.0414 44  ILE A N   
351  C CA  . ILE A 44  ? 0.5505 0.5384 0.5326 0.0315  0.0495  -0.0331 44  ILE A CA  
352  C C   . ILE A 44  ? 0.5584 0.5412 0.5472 0.0413  0.0244  -0.0285 44  ILE A C   
353  O O   . ILE A 44  ? 0.5461 0.5366 0.5532 0.0414  0.0161  -0.0282 44  ILE A O   
354  C CB  . ILE A 44  ? 0.5266 0.5153 0.4722 0.0208  0.0561  -0.0258 44  ILE A CB  
355  C CG1 . ILE A 44  ? 0.5149 0.5048 0.4424 0.0108  0.0772  -0.0299 44  ILE A CG1 
356  C CG2 . ILE A 44  ? 0.5090 0.4864 0.4217 0.0236  0.0419  -0.0174 44  ILE A CG2 
357  C CD1 . ILE A 44  ? 0.5150 0.4922 0.4211 0.0118  0.0782  -0.0332 44  ILE A CD1 
358  N N   . LEU A 45  ? 0.6042 0.5726 0.5750 0.0488  0.0123  -0.0246 45  LEU A N   
359  C CA  . LEU A 45  ? 0.6238 0.5835 0.5888 0.0584  -0.0117 -0.0197 45  LEU A CA  
360  C C   . LEU A 45  ? 0.6064 0.5649 0.5394 0.0555  -0.0167 -0.0143 45  LEU A C   
361  O O   . LEU A 45  ? 0.5634 0.5175 0.4636 0.0506  -0.0081 -0.0088 45  LEU A O   
362  C CB  . LEU A 45  ? 0.6609 0.6035 0.6077 0.0653  -0.0192 -0.0137 45  LEU A CB  
363  C CG  . LEU A 45  ? 0.6690 0.5989 0.5981 0.0753  -0.0436 -0.0065 45  LEU A CG  
364  C CD1 . LEU A 45  ? 0.6787 0.6097 0.6479 0.0845  -0.0625 -0.0107 45  LEU A CD1 
365  C CD2 . LEU A 45  ? 0.6762 0.5886 0.5711 0.0777  -0.0444 0.0045  45  LEU A CD2 
366  N N   . ASP A 46  ? 0.6216 0.5835 0.5694 0.0592  -0.0320 -0.0171 46  ASP A N   
367  C CA  . ASP A 46  ? 0.6275 0.5884 0.5551 0.0579  -0.0387 -0.0157 46  ASP A CA  
368  C C   . ASP A 46  ? 0.6198 0.5711 0.5432 0.0686  -0.0647 -0.0183 46  ASP A C   
369  O O   . ASP A 46  ? 0.6023 0.5591 0.5617 0.0713  -0.0783 -0.0247 46  ASP A O   
370  C CB  . ASP A 46  ? 0.6373 0.6123 0.5916 0.0487  -0.0293 -0.0186 46  ASP A CB  
371  C CG  . ASP A 46  ? 0.6859 0.6595 0.6305 0.0475  -0.0376 -0.0186 46  ASP A CG  
372  O OD1 . ASP A 46  ? 0.7135 0.6758 0.6323 0.0554  -0.0523 -0.0197 46  ASP A OD1 
373  O OD2 . ASP A 46  ? 0.7164 0.6993 0.6789 0.0388  -0.0286 -0.0175 46  ASP A OD2 
374  N N   . SER A 47  ? 0.6247 0.5618 0.5037 0.0741  -0.0711 -0.0132 47  SER A N   
375  C CA  . SER A 47  ? 0.6457 0.5694 0.5053 0.0846  -0.0953 -0.0147 47  SER A CA  
376  C C   . SER A 47  ? 0.6510 0.5778 0.5254 0.0858  -0.1112 -0.0251 47  SER A C   
377  O O   . SER A 47  ? 0.6586 0.5785 0.5385 0.0934  -0.1360 -0.0302 47  SER A O   
378  C CB  . SER A 47  ? 0.6491 0.5586 0.4539 0.0882  -0.0921 -0.0069 47  SER A CB  
379  O OG  . SER A 47  ? 0.6244 0.5377 0.4123 0.0835  -0.0797 -0.0087 47  SER A OG  
380  N N   . THR A 48  ? 0.6371 0.5727 0.5194 0.0782  -0.0993 -0.0281 48  THR A N   
381  C CA  . THR A 48  ? 0.6690 0.6057 0.5689 0.0786  -0.1140 -0.0382 48  THR A CA  
382  C C   . THR A 48  ? 0.6921 0.6367 0.6448 0.0791  -0.1299 -0.0443 48  THR A C   
383  O O   . THR A 48  ? 0.7231 0.6624 0.6856 0.0838  -0.1537 -0.0537 48  THR A O   
384  C CB  . THR A 48  ? 0.6446 0.5897 0.5539 0.0693  -0.0982 -0.0377 48  THR A CB  
385  O OG1 . THR A 48  ? 0.6589 0.5969 0.5250 0.0704  -0.0874 -0.0337 48  THR A OG1 
386  C CG2 . THR A 48  ? 0.6444 0.5894 0.5797 0.0689  -0.1135 -0.0479 48  THR A CG2 
387  N N   . TYR A 49  ? 0.7074 0.6646 0.6958 0.0745  -0.1167 -0.0403 49  TYR A N   
388  C CA  . TYR A 49  ? 0.7239 0.6910 0.7698 0.0756  -0.1286 -0.0457 49  TYR A CA  
389  C C   . TYR A 49  ? 0.7040 0.6635 0.7500 0.0857  -0.1444 -0.0441 49  TYR A C   
390  O O   . TYR A 49  ? 0.7112 0.6716 0.7921 0.0913  -0.1687 -0.0497 49  TYR A O   
391  C CB  . TYR A 49  ? 0.7532 0.7396 0.8426 0.0647  -0.1023 -0.0436 49  TYR A CB  
392  C CG  . TYR A 49  ? 0.8219 0.8159 0.9245 0.0544  -0.0926 -0.0435 49  TYR A CG  
393  C CD1 . TYR A 49  ? 0.8495 0.8441 0.9832 0.0543  -0.1121 -0.0505 49  TYR A CD1 
394  C CD2 . TYR A 49  ? 0.8696 0.8686 0.9550 0.0446  -0.0658 -0.0357 49  TYR A CD2 
395  C CE1 . TYR A 49  ? 0.8684 0.8679 1.0179 0.0446  -0.1038 -0.0488 49  TYR A CE1 
396  C CE2 . TYR A 49  ? 0.8782 0.8820 0.9757 0.0352  -0.0584 -0.0327 49  TYR A CE2 
397  C CZ  . TYR A 49  ? 0.8802 0.8841 1.0112 0.0351  -0.0766 -0.0387 49  TYR A CZ  
398  O OH  . TYR A 49  ? 0.8976 0.9045 1.0430 0.0255  -0.0691 -0.0339 49  TYR A OH  
399  N N   . HIS A 50  ? 0.6845 0.6354 0.6939 0.0880  -0.1331 -0.0358 50  HIS A N   
400  C CA  . HIS A 50  ? 0.6819 0.6266 0.7011 0.0959  -0.1431 -0.0320 50  HIS A CA  
401  C C   . HIS A 50  ? 0.7358 0.6580 0.7024 0.1058  -0.1653 -0.0258 50  HIS A C   
402  O O   . HIS A 50  ? 0.7486 0.6610 0.7087 0.1115  -0.1699 -0.0179 50  HIS A O   
403  C CB  . HIS A 50  ? 0.6481 0.5976 0.6705 0.0909  -0.1147 -0.0271 50  HIS A CB  
404  C CG  . HIS A 50  ? 0.6103 0.5797 0.6730 0.0809  -0.0901 -0.0325 50  HIS A CG  
405  N ND1 . HIS A 50  ? 0.5756 0.5492 0.6191 0.0717  -0.0620 -0.0299 50  HIS A ND1 
406  C CD2 . HIS A 50  ? 0.5887 0.5746 0.7095 0.0785  -0.0893 -0.0396 50  HIS A CD2 
407  C CE1 . HIS A 50  ? 0.5614 0.5520 0.6437 0.0641  -0.0445 -0.0349 50  HIS A CE1 
408  N NE2 . HIS A 50  ? 0.5551 0.5542 0.6867 0.0679  -0.0588 -0.0404 50  HIS A NE2 
409  N N   . HIS A 51  ? 0.7876 0.7002 0.7163 0.1081  -0.1788 -0.0293 51  HIS A N   
410  C CA  . HIS A 51  ? 0.8263 0.7166 0.6931 0.1164  -0.1939 -0.0230 51  HIS A CA  
411  C C   . HIS A 51  ? 0.8290 0.7087 0.7072 0.1262  -0.2243 -0.0194 51  HIS A C   
412  O O   . HIS A 51  ? 0.8303 0.6945 0.6757 0.1313  -0.2275 -0.0066 51  HIS A O   
413  C CB  . HIS A 51  ? 0.8622 0.7445 0.6906 0.1180  -0.2038 -0.0319 51  HIS A CB  
414  C CG  . HIS A 51  ? 0.8928 0.7817 0.7619 0.1181  -0.2259 -0.0465 51  HIS A CG  
415  N ND1 . HIS A 51  ? 0.9534 0.8319 0.8262 0.1265  -0.2627 -0.0520 51  HIS A ND1 
416  C CD2 . HIS A 51  ? 0.8758 0.7805 0.7889 0.1102  -0.2181 -0.0554 51  HIS A CD2 
417  C CE1 . HIS A 51  ? 0.9403 0.8288 0.8606 0.1235  -0.2766 -0.0654 51  HIS A CE1 
418  N NE2 . HIS A 51  ? 0.8931 0.7972 0.8383 0.1135  -0.2488 -0.0670 51  HIS A NE2 
419  N N   . ALA A 52  ? 0.8239 0.7124 0.7545 0.1282  -0.2469 -0.0294 52  ALA A N   
420  C CA  . ALA A 52  ? 0.8610 0.7397 0.8075 0.1381  -0.2830 -0.0276 52  ALA A CA  
421  C C   . ALA A 52  ? 0.8670 0.7448 0.8379 0.1414  -0.2770 -0.0157 52  ALA A C   
422  O O   . ALA A 52  ? 0.8611 0.7262 0.8360 0.1507  -0.3059 -0.0091 52  ALA A O   
423  C CB  . ALA A 52  ? 0.8466 0.7395 0.8583 0.1377  -0.3046 -0.0415 52  ALA A CB  
424  N N   . ALA A 53  ? 0.8537 0.7435 0.8401 0.1339  -0.2408 -0.0133 53  ALA A N   
425  C CA  . ALA A 53  ? 0.8422 0.7317 0.8565 0.1361  -0.2307 -0.0057 53  ALA A CA  
426  C C   . ALA A 53  ? 0.8917 0.7635 0.8465 0.1354  -0.2154 0.0087  53  ALA A C   
427  O O   . ALA A 53  ? 0.9465 0.8128 0.9170 0.1375  -0.2088 0.0162  53  ALA A O   
428  C CB  . ALA A 53  ? 0.7824 0.6962 0.8555 0.1281  -0.2017 -0.0153 53  ALA A CB  
429  N N   . LEU A 54  ? 0.9119 0.7749 0.8033 0.1325  -0.2091 0.0119  54  LEU A N   
430  C CA  . LEU A 54  ? 0.9379 0.7875 0.7786 0.1301  -0.1905 0.0254  54  LEU A CA  
431  C C   . LEU A 54  ? 1.0359 0.8598 0.8202 0.1385  -0.2131 0.0395  54  LEU A C   
432  O O   . LEU A 54  ? 1.0354 0.8456 0.7840 0.1376  -0.2010 0.0546  54  LEU A O   
433  C CB  . LEU A 54  ? 0.9254 0.7841 0.7378 0.1209  -0.1644 0.0207  54  LEU A CB  
434  C CG  . LEU A 54  ? 0.8767 0.7573 0.7318 0.1110  -0.1388 0.0112  54  LEU A CG  
435  C CD1 . LEU A 54  ? 0.8389 0.7249 0.6623 0.1027  -0.1164 0.0104  54  LEU A CD1 
436  C CD2 . LEU A 54  ? 0.8743 0.7562 0.7596 0.1091  -0.1249 0.0149  54  LEU A CD2 
437  N N   . ARG A 55  ? 1.1256 0.9426 0.9031 0.1461  -0.2462 0.0349  55  ARG A N   
438  C CA  . ARG A 55  ? 1.2221 1.0133 0.9353 0.1541  -0.2704 0.0465  55  ARG A CA  
439  C C   . ARG A 55  ? 1.2787 1.0507 0.9765 0.1577  -0.2719 0.0689  55  ARG A C   
440  O O   . ARG A 55  ? 1.3577 1.1085 0.9886 0.1598  -0.2725 0.0842  55  ARG A O   
441  C CB  . ARG A 55  ? 1.2995 1.0848 1.0251 0.1629  -0.3138 0.0392  55  ARG A CB  
442  C CG  . ARG A 55  ? 1.3048 1.1031 1.0439 0.1608  -0.3223 0.0174  55  ARG A CG  
443  C CD  . ARG A 55  ? 1.3446 1.1364 1.1031 0.1691  -0.3691 0.0105  55  ARG A CD  
444  N NE  . ARG A 55  ? 1.3827 1.1933 1.1912 0.1656  -0.3772 -0.0108 55  ARG A NE  
445  C CZ  . ARG A 55  ? 1.4062 1.2204 1.1911 0.1608  -0.3670 -0.0250 55  ARG A CZ  
446  N NH1 . ARG A 55  ? 1.4001 1.1999 1.1079 0.1608  -0.3517 -0.0220 55  ARG A NH1 
447  N NH2 . ARG A 55  ? 1.3640 1.1962 1.2063 0.1562  -0.3718 -0.0419 55  ARG A NH2 
448  N N   . GLN A 56  ? 1.2915 1.0700 1.0531 0.1588  -0.2732 0.0708  56  GLN A N   
449  C CA  . GLN A 56  ? 1.3352 1.0934 1.0953 0.1640  -0.2831 0.0913  56  GLN A CA  
450  C C   . GLN A 56  ? 1.2558 1.0188 1.0387 0.1566  -0.2486 0.0958  56  GLN A C   
451  O O   . GLN A 56  ? 1.3157 1.0611 1.1000 0.1593  -0.2516 0.1129  56  GLN A O   
452  C CB  . GLN A 56  ? 1.3849 1.1402 1.1984 0.1742  -0.3204 0.0911  56  GLN A CB  
453  C CG  . GLN A 56  ? 1.3806 1.1610 1.2580 0.1747  -0.3309 0.0682  56  GLN A CG  
454  C CD  . GLN A 56  ? 1.3000 1.1062 1.2497 0.1684  -0.3009 0.0544  56  GLN A CD  
455  O OE1 . GLN A 56  ? 1.2835 1.0929 1.2937 0.1729  -0.3041 0.0549  56  GLN A OE1 
456  N NE2 . GLN A 56  ? 1.2198 1.0443 1.1643 0.1585  -0.2722 0.0414  56  GLN A NE2 
457  N N   . LEU A 57  ? 1.1601 0.9443 0.9565 0.1469  -0.2176 0.0814  57  LEU A N   
458  C CA  . LEU A 57  ? 1.0634 0.8526 0.8793 0.1389  -0.1868 0.0824  57  LEU A CA  
459  C C   . LEU A 57  ? 1.0605 0.8358 0.8162 0.1335  -0.1693 0.0984  57  LEU A C   
460  O O   . LEU A 57  ? 1.0694 0.8433 0.7743 0.1325  -0.1675 0.0995  57  LEU A O   
461  C CB  . LEU A 57  ? 0.9906 0.8069 0.8392 0.1304  -0.1635 0.0618  57  LEU A CB  
462  C CG  . LEU A 57  ? 0.9271 0.7553 0.8375 0.1276  -0.1485 0.0514  57  LEU A CG  
463  C CD1 . LEU A 57  ? 0.8748 0.7236 0.7910 0.1163  -0.1193 0.0375  57  LEU A CD1 
464  C CD2 . LEU A 57  ? 0.9431 0.7533 0.8584 0.1287  -0.1440 0.0638  57  LEU A CD2 
465  N N   . GLU A 58  ? 1.0438 0.8101 0.8103 0.1295  -0.1545 0.1089  58  GLU A N   
466  C CA  . GLU A 58  ? 1.0321 0.7880 0.7541 0.1226  -0.1345 0.1241  58  GLU A CA  
467  C C   . GLU A 58  ? 0.9237 0.6996 0.6312 0.1135  -0.1100 0.1115  58  GLU A C   
468  O O   . GLU A 58  ? 0.8518 0.6476 0.5954 0.1089  -0.1002 0.0934  58  GLU A O   
469  C CB  . GLU A 58  ? 1.0734 0.8180 0.8240 0.1188  -0.1241 0.1337  58  GLU A CB  
470  C CG  . GLU A 58  ? 1.1488 0.8816 0.8609 0.1111  -0.1048 0.1521  58  GLU A CG  
471  C CD  . GLU A 58  ? 1.2268 0.9393 0.9599 0.1092  -0.1029 0.1685  58  GLU A CD  
472  O OE1 . GLU A 58  ? 1.2921 1.0083 1.0402 0.0992  -0.0811 0.1665  58  GLU A OE1 
473  O OE2 . GLU A 58  ? 1.2448 0.9365 0.9806 0.1177  -0.1251 0.1836  58  GLU A OE2 
474  N N   . ASP A 59  ? 0.9279 0.6979 0.5823 0.1111  -0.1001 0.1219  59  ASP A N   
475  C CA  . ASP A 59  ? 0.9009 0.6880 0.5406 0.1040  -0.0790 0.1119  59  ASP A CA  
476  C C   . ASP A 59  ? 0.8520 0.6571 0.5086 0.1059  -0.0873 0.0906  59  ASP A C   
477  O O   . ASP A 59  ? 0.8036 0.6247 0.4613 0.0997  -0.0713 0.0804  59  ASP A O   
478  C CB  . ASP A 59  ? 0.8840 0.6811 0.5503 0.0928  -0.0542 0.1102  59  ASP A CB  
479  C CG  . ASP A 59  ? 0.9171 0.7000 0.5649 0.0877  -0.0401 0.1304  59  ASP A CG  
480  O OD1 . ASP A 59  ? 0.9816 0.7443 0.6004 0.0932  -0.0497 0.1485  59  ASP A OD1 
481  O OD2 . ASP A 59  ? 0.9161 0.7081 0.5793 0.0777  -0.0202 0.1287  59  ASP A OD2 
482  N N   . GLY A 60  ? 0.8535 0.6554 0.5245 0.1144  -0.1133 0.0853  60  GLY A N   
483  C CA  . GLY A 60  ? 0.8403 0.6596 0.5426 0.1153  -0.1223 0.0659  60  GLY A CA  
484  C C   . GLY A 60  ? 0.8543 0.6832 0.5303 0.1129  -0.1154 0.0556  60  GLY A C   
485  O O   . GLY A 60  ? 0.7997 0.6457 0.5062 0.1095  -0.1132 0.0407  60  GLY A O   
486  N N   . GLU A 61  ? 0.9273 0.7441 0.5477 0.1148  -0.1108 0.0641  61  GLU A N   
487  C CA  . GLU A 61  ? 0.9518 0.7732 0.5437 0.1155  -0.1075 0.0535  61  GLU A CA  
488  C C   . GLU A 61  ? 0.8895 0.7272 0.4923 0.1061  -0.0791 0.0496  61  GLU A C   
489  O O   . GLU A 61  ? 0.9002 0.7449 0.4939 0.1060  -0.0750 0.0385  61  GLU A O   
490  C CB  . GLU A 61  ? 1.0344 0.8358 0.5595 0.1221  -0.1116 0.0628  61  GLU A CB  
491  C CG  . GLU A 61  ? 1.0751 0.8736 0.5720 0.1169  -0.0824 0.0772  61  GLU A CG  
492  C CD  . GLU A 61  ? 1.1153 0.9012 0.6125 0.1148  -0.0781 0.0989  61  GLU A CD  
493  O OE1 . GLU A 61  ? 1.1122 0.9042 0.6207 0.1065  -0.0534 0.1069  61  GLU A OE1 
494  O OE2 . GLU A 61  ? 1.1182 0.8874 0.6074 0.1212  -0.1010 0.1083  61  GLU A OE2 
495  N N   . ARG A 62  ? 0.8564 0.6980 0.4775 0.0987  -0.0613 0.0586  62  ARG A N   
496  C CA  . ARG A 62  ? 0.8447 0.7012 0.4782 0.0895  -0.0382 0.0558  62  ARG A CA  
497  C C   . ARG A 62  ? 0.7602 0.6312 0.4419 0.0822  -0.0345 0.0479  62  ARG A C   
498  O O   . ARG A 62  ? 0.6934 0.5768 0.3877 0.0740  -0.0193 0.0448  62  ARG A O   
499  C CB  . ARG A 62  ? 0.8792 0.7295 0.4929 0.0852  -0.0191 0.0713  62  ARG A CB  
500  C CG  . ARG A 62  ? 0.9214 0.7628 0.5521 0.0822  -0.0188 0.0829  62  ARG A CG  
501  C CD  . ARG A 62  ? 0.9866 0.8210 0.6004 0.0773  -0.0007 0.0994  62  ARG A CD  
502  N NE  . ARG A 62  ? 0.9954 0.8442 0.6355 0.0666  0.0167  0.0963  62  ARG A NE  
503  C CZ  . ARG A 62  ? 1.0694 0.9174 0.7064 0.0601  0.0340  0.1082  62  ARG A CZ  
504  N NH1 . ARG A 62  ? 1.0741 0.9103 0.6780 0.0632  0.0415  0.1236  62  ARG A NH1 
505  N NH2 . ARG A 62  ? 1.1107 0.9701 0.7777 0.0501  0.0439  0.1048  62  ARG A NH2 
506  N N   . ARG A 63  ? 0.7451 0.6143 0.4533 0.0854  -0.0485 0.0444  63  ARG A N   
507  C CA  . ARG A 63  ? 0.7278 0.6082 0.4777 0.0789  -0.0411 0.0377  63  ARG A CA  
508  C C   . ARG A 63  ? 0.6937 0.5902 0.4696 0.0768  -0.0436 0.0239  63  ARG A C   
509  O O   . ARG A 63  ? 0.7362 0.6327 0.5069 0.0821  -0.0575 0.0188  63  ARG A O   
510  C CB  . ARG A 63  ? 0.7260 0.5967 0.4973 0.0837  -0.0508 0.0411  63  ARG A CB  
511  C CG  . ARG A 63  ? 0.7347 0.5895 0.4883 0.0829  -0.0449 0.0561  63  ARG A CG  
512  C CD  . ARG A 63  ? 0.7548 0.5961 0.5287 0.0896  -0.0585 0.0612  63  ARG A CD  
513  N NE  . ARG A 63  ? 0.7268 0.5761 0.5455 0.0859  -0.0508 0.0501  63  ARG A NE  
514  C CZ  . ARG A 63  ? 0.7346 0.5738 0.5821 0.0906  -0.0576 0.0515  63  ARG A CZ  
515  N NH1 . ARG A 63  ? 0.7547 0.5756 0.5933 0.0994  -0.0762 0.0653  63  ARG A NH1 
516  N NH2 . ARG A 63  ? 0.7251 0.5716 0.6095 0.0868  -0.0460 0.0387  63  ARG A NH2 
517  N N   . GLY A 64  ? 0.6388 0.5474 0.4404 0.0682  -0.0298 0.0184  64  GLY A N   
518  C CA  . GLY A 64  ? 0.6312 0.5547 0.4597 0.0645  -0.0289 0.0081  64  GLY A CA  
519  C C   . GLY A 64  ? 0.6079 0.5371 0.4213 0.0615  -0.0271 0.0069  64  GLY A C   
520  O O   . GLY A 64  ? 0.5786 0.5112 0.4021 0.0646  -0.0383 0.0007  64  GLY A O   
521  N N   . ARG A 65  ? 0.6076 0.5378 0.4022 0.0554  -0.0139 0.0122  65  ARG A N   
522  C CA  . ARG A 65  ? 0.6182 0.5539 0.4033 0.0525  -0.0105 0.0118  65  ARG A CA  
523  C C   . ARG A 65  ? 0.6117 0.5568 0.4045 0.0413  0.0034  0.0139  65  ARG A C   
524  O O   . ARG A 65  ? 0.6422 0.5876 0.4213 0.0379  0.0104  0.0194  65  ARG A O   
525  C CB  . ARG A 65  ? 0.6460 0.5728 0.3986 0.0579  -0.0098 0.0173  65  ARG A CB  
526  C CG  . ARG A 65  ? 0.7101 0.6249 0.4431 0.0690  -0.0247 0.0156  65  ARG A CG  
527  C CD  . ARG A 65  ? 0.7629 0.6794 0.5035 0.0734  -0.0387 0.0045  65  ARG A CD  
528  N NE  . ARG A 65  ? 0.8313 0.7536 0.5706 0.0708  -0.0319 0.0006  65  ARG A NE  
529  C CZ  . ARG A 65  ? 0.9305 0.8484 0.6428 0.0743  -0.0244 0.0019  65  ARG A CZ  
530  N NH1 . ARG A 65  ? 1.0019 0.9076 0.6786 0.0815  -0.0248 0.0057  65  ARG A NH1 
531  N NH2 . ARG A 65  ? 0.8725 0.7979 0.5946 0.0709  -0.0163 -0.0005 65  ARG A NH2 
532  N N   . PRO A 66  ? 0.5816 0.5345 0.3963 0.0350  0.0078  0.0097  66  PRO A N   
533  C CA  . PRO A 66  ? 0.5714 0.5315 0.3867 0.0239  0.0191  0.0117  66  PRO A CA  
534  C C   . PRO A 66  ? 0.5755 0.5407 0.3877 0.0198  0.0185  0.0157  66  PRO A C   
535  O O   . PRO A 66  ? 0.5573 0.5256 0.3629 0.0117  0.0242  0.0205  66  PRO A O   
536  C CB  . PRO A 66  ? 0.5718 0.5386 0.4096 0.0201  0.0242  0.0056  66  PRO A CB  
537  C CG  . PRO A 66  ? 0.5657 0.5330 0.4235 0.0285  0.0126  0.0010  66  PRO A CG  
538  C CD  . PRO A 66  ? 0.5805 0.5362 0.4209 0.0383  0.0022  0.0030  66  PRO A CD  
539  N N   . ASP A 67  ? 0.5885 0.5537 0.4075 0.0257  0.0095  0.0130  67  ASP A N   
540  C CA  . ASP A 67  ? 0.5683 0.5355 0.3874 0.0249  0.0070  0.0155  67  ASP A CA  
541  C C   . ASP A 67  ? 0.5451 0.5115 0.3484 0.0236  0.0124  0.0217  67  ASP A C   
542  O O   . ASP A 67  ? 0.5718 0.5430 0.3803 0.0174  0.0140  0.0268  67  ASP A O   
543  C CB  . ASP A 67  ? 0.5700 0.5324 0.3918 0.0344  -0.0044 0.0086  67  ASP A CB  
544  C CG  . ASP A 67  ? 0.5678 0.5209 0.3702 0.0446  -0.0099 0.0051  67  ASP A CG  
545  O OD1 . ASP A 67  ? 0.5614 0.5126 0.3694 0.0466  -0.0141 0.0030  67  ASP A OD1 
546  O OD2 . ASP A 67  ? 0.5793 0.5269 0.3614 0.0505  -0.0093 0.0050  67  ASP A OD2 
547  N N   . ILE A 68  ? 0.5323 0.4926 0.3194 0.0292  0.0146  0.0225  68  ILE A N   
548  C CA  . ILE A 68  ? 0.5270 0.4881 0.3056 0.0281  0.0212  0.0288  68  ILE A CA  
549  C C   . ILE A 68  ? 0.4926 0.4594 0.2777 0.0166  0.0253  0.0343  68  ILE A C   
550  O O   . ILE A 68  ? 0.4668 0.4388 0.2581 0.0129  0.0259  0.0391  68  ILE A O   
551  C CB  . ILE A 68  ? 0.5439 0.4967 0.3043 0.0344  0.0251  0.0313  68  ILE A CB  
552  C CG1 . ILE A 68  ? 0.5659 0.5125 0.3113 0.0457  0.0214  0.0267  68  ILE A CG1 
553  C CG2 . ILE A 68  ? 0.5394 0.4948 0.2996 0.0293  0.0347  0.0395  68  ILE A CG2 
554  C CD1 . ILE A 68  ? 0.5943 0.5295 0.3153 0.0524  0.0224  0.0304  68  ILE A CD1 
555  N N   . VAL A 69  ? 0.4963 0.4617 0.2808 0.0114  0.0269  0.0324  69  VAL A N   
556  C CA  . VAL A 69  ? 0.5027 0.4708 0.2864 0.0004  0.0296  0.0348  69  VAL A CA  
557  C C   . VAL A 69  ? 0.5100 0.4844 0.2989 -0.0061 0.0264  0.0380  69  VAL A C   
558  O O   . VAL A 69  ? 0.5042 0.4815 0.2927 -0.0126 0.0237  0.0442  69  VAL A O   
559  C CB  . VAL A 69  ? 0.5052 0.4688 0.2862 -0.0021 0.0337  0.0287  69  VAL A CB  
560  C CG1 . VAL A 69  ? 0.5111 0.4755 0.2849 -0.0134 0.0365  0.0280  69  VAL A CG1 
561  C CG2 . VAL A 69  ? 0.5366 0.4916 0.3147 0.0040  0.0350  0.0284  69  VAL A CG2 
562  N N   . HIS A 70  ? 0.5221 0.4981 0.3187 -0.0047 0.0255  0.0350  70  HIS A N   
563  C CA  . HIS A 70  ? 0.5399 0.5200 0.3429 -0.0112 0.0230  0.0403  70  HIS A CA  
564  C C   . HIS A 70  ? 0.5651 0.5470 0.3738 -0.0111 0.0163  0.0478  70  HIS A C   
565  O O   . HIS A 70  ? 0.5922 0.5758 0.3982 -0.0195 0.0130  0.0560  70  HIS A O   
566  C CB  . HIS A 70  ? 0.5344 0.5157 0.3534 -0.0073 0.0219  0.0360  70  HIS A CB  
567  C CG  . HIS A 70  ? 0.5437 0.5281 0.3717 -0.0153 0.0214  0.0432  70  HIS A CG  
568  N ND1 . HIS A 70  ? 0.5581 0.5425 0.4072 -0.0121 0.0153  0.0433  70  HIS A ND1 
569  C CD2 . HIS A 70  ? 0.5629 0.5486 0.3806 -0.0265 0.0256  0.0512  70  HIS A CD2 
570  C CE1 . HIS A 70  ? 0.5808 0.5668 0.4355 -0.0216 0.0167  0.0531  70  HIS A CE1 
571  N NE2 . HIS A 70  ? 0.5886 0.5754 0.4213 -0.0304 0.0232  0.0586  70  HIS A NE2 
572  N N   . ILE A 71  ? 0.5682 0.5491 0.3845 -0.0011 0.0141  0.0445  71  ILE A N   
573  C CA  . ILE A 71  ? 0.5703 0.5534 0.3990 0.0017  0.0097  0.0486  71  ILE A CA  
574  C C   . ILE A 71  ? 0.5742 0.5609 0.4021 -0.0024 0.0107  0.0548  71  ILE A C   
575  O O   . ILE A 71  ? 0.5976 0.5882 0.4403 -0.0046 0.0051  0.0615  71  ILE A O   
576  C CB  . ILE A 71  ? 0.6073 0.5871 0.4388 0.0144  0.0102  0.0398  71  ILE A CB  
577  C CG1 . ILE A 71  ? 0.6625 0.6384 0.5008 0.0176  0.0047  0.0330  71  ILE A CG1 
578  C CG2 . ILE A 71  ? 0.6138 0.5961 0.4595 0.0191  0.0097  0.0412  71  ILE A CG2 
579  C CD1 . ILE A 71  ? 0.7004 0.6700 0.5282 0.0288  0.0033  0.0219  71  ILE A CD1 
580  N N   . CYS A 72  ? 0.5380 0.5232 0.3536 -0.0031 0.0166  0.0529  72  CYS A N   
581  C CA  . CYS A 72  ? 0.4996 0.4879 0.3185 -0.0084 0.0168  0.0581  72  CYS A CA  
582  C C   . CYS A 72  ? 0.4858 0.4749 0.2998 -0.0207 0.0089  0.0634  72  CYS A C   
583  O O   . CYS A 72  ? 0.4660 0.4590 0.2897 -0.0259 0.0025  0.0695  72  CYS A O   
584  C CB  . CYS A 72  ? 0.5233 0.5071 0.3317 -0.0070 0.0244  0.0550  72  CYS A CB  
585  S SG  . CYS A 72  ? 0.5713 0.5539 0.3803 0.0056  0.0340  0.0537  72  CYS A SG  
586  N N   . LEU A 73  ? 0.5032 0.4884 0.3014 -0.0254 0.0097  0.0607  73  LEU A N   
587  C CA  . LEU A 73  ? 0.5281 0.5117 0.3115 -0.0373 0.0043  0.0646  73  LEU A CA  
588  C C   . LEU A 73  ? 0.5622 0.5480 0.3524 -0.0409 -0.0052 0.0753  73  LEU A C   
589  O O   . LEU A 73  ? 0.6062 0.5926 0.3950 -0.0481 -0.0163 0.0834  73  LEU A O   
590  C CB  . LEU A 73  ? 0.5289 0.5077 0.2926 -0.0407 0.0130  0.0566  73  LEU A CB  
591  C CG  . LEU A 73  ? 0.5275 0.5016 0.2862 -0.0382 0.0200  0.0467  73  LEU A CG  
592  C CD1 . LEU A 73  ? 0.5345 0.5046 0.2793 -0.0410 0.0293  0.0376  73  LEU A CD1 
593  C CD2 . LEU A 73  ? 0.5147 0.4865 0.2713 -0.0441 0.0142  0.0475  73  LEU A CD2 
594  N N   . LEU A 74  ? 0.5583 0.5445 0.3594 -0.0358 -0.0033 0.0760  74  LEU A N   
595  C CA  . LEU A 74  ? 0.5672 0.5536 0.3803 -0.0385 -0.0129 0.0873  74  LEU A CA  
596  C C   . LEU A 74  ? 0.5798 0.5704 0.4150 -0.0356 -0.0230 0.0931  74  LEU A C   
597  O O   . LEU A 74  ? 0.6291 0.6193 0.4734 -0.0402 -0.0354 0.1050  74  LEU A O   
598  C CB  . LEU A 74  ? 0.5529 0.5384 0.3830 -0.0314 -0.0099 0.0844  74  LEU A CB  
599  C CG  . LEU A 74  ? 0.5404 0.5240 0.3614 -0.0350 -0.0015 0.0814  74  LEU A CG  
600  C CD1 . LEU A 74  ? 0.5268 0.5096 0.3717 -0.0270 -0.0019 0.0763  74  LEU A CD1 
601  C CD2 . LEU A 74  ? 0.5614 0.5425 0.3675 -0.0478 -0.0029 0.0943  74  LEU A CD2 
602  N N   . ASN A 75  ? 0.5613 0.5557 0.4080 -0.0272 -0.0169 0.0853  75  ASN A N   
603  C CA  . ASN A 75  ? 0.5707 0.5715 0.4442 -0.0237 -0.0223 0.0894  75  ASN A CA  
604  C C   . ASN A 75  ? 0.5873 0.5903 0.4571 -0.0339 -0.0321 0.0960  75  ASN A C   
605  O O   . ASN A 75  ? 0.6351 0.6411 0.5229 -0.0374 -0.0463 0.1060  75  ASN A O   
606  C CB  . ASN A 75  ? 0.5540 0.5583 0.4384 -0.0124 -0.0095 0.0801  75  ASN A CB  
607  C CG  . ASN A 75  ? 0.5584 0.5617 0.4586 -0.0014 -0.0068 0.0749  75  ASN A CG  
608  O OD1 . ASN A 75  ? 0.5159 0.5178 0.4320 -0.0019 -0.0162 0.0800  75  ASN A OD1 
609  N ND2 . ASN A 75  ? 0.5829 0.5853 0.4778 0.0084  0.0053  0.0648  75  ASN A ND2 
610  N N   . ALA A 76  ? 0.5840 0.5842 0.4321 -0.0384 -0.0263 0.0899  76  ALA A N   
611  C CA  . ALA A 76  ? 0.5860 0.5867 0.4311 -0.0479 -0.0362 0.0927  76  ALA A CA  
612  C C   . ALA A 76  ? 0.5820 0.5776 0.4068 -0.0590 -0.0524 0.1011  76  ALA A C   
613  O O   . ALA A 76  ? 0.5849 0.5831 0.4229 -0.0643 -0.0697 0.1098  76  ALA A O   
614  C CB  . ALA A 76  ? 0.5915 0.5875 0.4185 -0.0497 -0.0261 0.0827  76  ALA A CB  
615  N N   . LEU A 77  ? 0.5706 0.5589 0.3642 -0.0625 -0.0468 0.0995  77  LEU A N   
616  C CA  . LEU A 77  ? 0.5791 0.5598 0.3393 -0.0744 -0.0568 0.1058  77  LEU A CA  
617  C C   . LEU A 77  ? 0.5909 0.5711 0.3604 -0.0770 -0.0724 0.1228  77  LEU A C   
618  O O   . LEU A 77  ? 0.6528 0.6274 0.4008 -0.0870 -0.0885 0.1321  77  LEU A O   
619  C CB  . LEU A 77  ? 0.5828 0.5577 0.3121 -0.0764 -0.0406 0.0988  77  LEU A CB  
620  C CG  . LEU A 77  ? 0.5733 0.5454 0.2886 -0.0757 -0.0276 0.0824  77  LEU A CG  
621  C CD1 . LEU A 77  ? 0.5832 0.5527 0.2819 -0.0748 -0.0100 0.0754  77  LEU A CD1 
622  C CD2 . LEU A 77  ? 0.6080 0.5735 0.2980 -0.0859 -0.0378 0.0785  77  LEU A CD2 
623  N N   . ASP A 78  ? 0.5640 0.5482 0.3635 -0.0681 -0.0689 0.1267  78  ASP A N   
624  C CA  . ASP A 78  ? 0.5813 0.5638 0.3975 -0.0695 -0.0847 0.1432  78  ASP A CA  
625  C C   . ASP A 78  ? 0.5725 0.5629 0.4305 -0.0647 -0.0989 0.1474  78  ASP A C   
626  O O   . ASP A 78  ? 0.5967 0.5866 0.4794 -0.0637 -0.1139 0.1606  78  ASP A O   
627  C CB  . ASP A 78  ? 0.5869 0.5675 0.4171 -0.0633 -0.0753 0.1447  78  ASP A CB  
628  C CG  . ASP A 78  ? 0.6308 0.6045 0.4251 -0.0709 -0.0641 0.1455  78  ASP A CG  
629  O OD1 . ASP A 78  ? 0.6615 0.6277 0.4339 -0.0812 -0.0731 0.1614  78  ASP A OD1 
630  O OD2 . ASP A 78  ? 0.6233 0.5992 0.4111 -0.0667 -0.0465 0.1310  78  ASP A OD2 
631  N N   . SER A 79  ? 0.5667 0.5646 0.4372 -0.0617 -0.0939 0.1368  79  SER A N   
632  C CA  . SER A 79  ? 0.5627 0.5708 0.4789 -0.0574 -0.1043 0.1403  79  SER A CA  
633  C C   . SER A 79  ? 0.5819 0.5874 0.4987 -0.0674 -0.1327 0.1553  79  SER A C   
634  O O   . SER A 79  ? 0.6065 0.6021 0.4791 -0.0787 -0.1421 0.1590  79  SER A O   
635  C CB  . SER A 79  ? 0.5414 0.5572 0.4687 -0.0550 -0.0927 0.1287  79  SER A CB  
636  O OG  . SER A 79  ? 0.5611 0.5713 0.4567 -0.0662 -0.0993 0.1257  79  SER A OG  
637  N N   . ILE A 80  ? 0.5651 0.5789 0.5320 -0.0626 -0.1465 0.1633  80  ILE A N   
638  C CA  . ILE A 80  ? 0.6056 0.6186 0.5811 -0.0713 -0.1771 0.1771  80  ILE A CA  
639  C C   . ILE A 80  ? 0.6376 0.6522 0.5972 -0.0803 -0.1833 0.1695  80  ILE A C   
640  O O   . ILE A 80  ? 0.6817 0.6880 0.6130 -0.0919 -0.2073 0.1766  80  ILE A O   
641  C CB  . ILE A 80  ? 0.5946 0.6193 0.6396 -0.0626 -0.1889 0.1848  80  ILE A CB  
642  C CG1 . ILE A 80  ? 0.5940 0.6134 0.6554 -0.0544 -0.1871 0.1923  80  ILE A CG1 
643  C CG2 . ILE A 80  ? 0.6157 0.6418 0.6773 -0.0713 -0.2235 0.1979  80  ILE A CG2 
644  C CD1 . ILE A 80  ? 0.5844 0.6147 0.7186 -0.0436 -0.1951 0.1966  80  ILE A CD1 
645  N N   . LEU A 81  ? 0.6189 0.6427 0.5963 -0.0752 -0.1625 0.1552  81  LEU A N   
646  C CA  . LEU A 81  ? 0.6178 0.6436 0.5930 -0.0829 -0.1667 0.1473  81  LEU A CA  
647  C C   . LEU A 81  ? 0.6584 0.6679 0.5673 -0.0943 -0.1718 0.1424  81  LEU A C   
648  O O   . LEU A 81  ? 0.6768 0.6823 0.5750 -0.1046 -0.1912 0.1406  81  LEU A O   
649  C CB  . LEU A 81  ? 0.5862 0.6207 0.5823 -0.0749 -0.1378 0.1348  81  LEU A CB  
650  C CG  . LEU A 81  ? 0.5968 0.6361 0.6112 -0.0814 -0.1403 0.1288  81  LEU A CG  
651  C CD1 . LEU A 81  ? 0.5815 0.6374 0.6637 -0.0808 -0.1542 0.1364  81  LEU A CD1 
652  C CD2 . LEU A 81  ? 0.5924 0.6325 0.6028 -0.0758 -0.1099 0.1177  81  LEU A CD2 
653  N N   . ASN A 82  ? 0.6545 0.6552 0.5222 -0.0922 -0.1538 0.1389  82  ASN A N   
654  C CA  . ASN A 82  ? 0.6780 0.6644 0.4842 -0.1013 -0.1516 0.1321  82  ASN A CA  
655  C C   . ASN A 82  ? 0.7448 0.7208 0.5175 -0.1115 -0.1770 0.1458  82  ASN A C   
656  O O   . ASN A 82  ? 0.8373 0.8022 0.5659 -0.1223 -0.1884 0.1413  82  ASN A O   
657  C CB  . ASN A 82  ? 0.6429 0.6254 0.4242 -0.0956 -0.1240 0.1249  82  ASN A CB  
658  C CG  . ASN A 82  ? 0.6474 0.6176 0.3736 -0.1035 -0.1164 0.1141  82  ASN A CG  
659  O OD1 . ASN A 82  ? 0.6923 0.6589 0.4090 -0.1084 -0.1189 0.1025  82  ASN A OD1 
660  N ND2 . ASN A 82  ? 0.6365 0.6002 0.3295 -0.1050 -0.1059 0.1170  82  ASN A ND2 
661  N N   . LYS A 83  ? 0.7366 0.7146 0.5296 -0.1080 -0.1865 0.1626  83  LYS A N   
662  C CA  . LYS A 83  ? 0.7700 0.7365 0.5314 -0.1171 -0.2107 0.1802  83  LYS A CA  
663  C C   . LYS A 83  ? 0.8102 0.7755 0.5755 -0.1256 -0.2439 0.1834  83  LYS A C   
664  O O   . LYS A 83  ? 0.8862 0.8372 0.5986 -0.1371 -0.2629 0.1892  83  LYS A O   
665  C CB  . LYS A 83  ? 0.7518 0.7204 0.5455 -0.1101 -0.2139 0.1977  83  LYS A CB  
666  C CG  . LYS A 83  ? 0.7148 0.6833 0.5057 -0.1027 -0.1841 0.1933  83  LYS A CG  
667  C CD  . LYS A 83  ? 0.7228 0.6864 0.5295 -0.1003 -0.1907 0.2123  83  LYS A CD  
668  C CE  . LYS A 83  ? 0.6903 0.6535 0.5004 -0.0935 -0.1643 0.2072  83  LYS A CE  
669  N NZ  . LYS A 83  ? 0.6921 0.6508 0.4524 -0.0989 -0.1422 0.1957  83  LYS A NZ  
670  N N   . GLU A 84  ? 0.7888 0.7687 0.6146 -0.1205 -0.2496 0.1785  84  GLU A N   
671  C CA  . GLU A 84  ? 0.8060 0.7881 0.6517 -0.1281 -0.2823 0.1807  84  GLU A CA  
672  C C   . GLU A 84  ? 0.7962 0.7720 0.6103 -0.1368 -0.2816 0.1618  84  GLU A C   
673  O O   . GLU A 84  ? 0.8083 0.7862 0.6435 -0.1434 -0.3072 0.1598  84  GLU A O   
674  C CB  . GLU A 84  ? 0.7903 0.7933 0.7229 -0.1191 -0.2841 0.1821  84  GLU A CB  
675  C CG  . GLU A 84  ? 0.7885 0.7988 0.7667 -0.1092 -0.2878 0.1980  84  GLU A CG  
676  C CD  . GLU A 84  ? 0.8431 0.8487 0.8321 -0.1149 -0.3297 0.2182  84  GLU A CD  
677  O OE1 . GLU A 84  ? 0.8693 0.8631 0.8322 -0.1150 -0.3369 0.2340  84  GLU A OE1 
678  O OE2 . GLU A 84  ? 0.8623 0.8758 0.8889 -0.1192 -0.3560 0.2193  84  GLU A OE2 
679  N N   . ASP A 85  ? 0.7861 0.7544 0.5571 -0.1363 -0.2529 0.1472  85  ASP A N   
680  C CA  . ASP A 85  ? 0.8163 0.7771 0.5613 -0.1431 -0.2495 0.1274  85  ASP A CA  
681  C C   . ASP A 85  ? 0.8021 0.7771 0.6128 -0.1401 -0.2486 0.1201  85  ASP A C   
682  O O   . ASP A 85  ? 0.8152 0.7885 0.6381 -0.1487 -0.2727 0.1154  85  ASP A O   
683  C CB  . ASP A 85  ? 0.8724 0.8156 0.5601 -0.1571 -0.2796 0.1265  85  ASP A CB  
684  C CG  . ASP A 85  ? 0.8911 0.8236 0.5517 -0.1645 -0.2788 0.1032  85  ASP A CG  
685  O OD1 . ASP A 85  ? 0.8654 0.7961 0.5147 -0.1600 -0.2473 0.0882  85  ASP A OD1 
686  O OD2 . ASP A 85  ? 0.9172 0.8424 0.5705 -0.1746 -0.3116 0.0998  85  ASP A OD2 
687  N N   . ARG A 86  ? 0.7683 0.7566 0.6206 -0.1283 -0.2205 0.1195  86  ARG A N   
688  C CA  . ARG A 86  ? 0.7378 0.7400 0.6503 -0.1249 -0.2124 0.1146  86  ARG A CA  
689  C C   . ARG A 86  ? 0.7083 0.7119 0.6188 -0.1158 -0.1752 0.1052  86  ARG A C   
690  O O   . ARG A 86  ? 0.6930 0.7102 0.6523 -0.1082 -0.1596 0.1068  86  ARG A O   
691  C CB  . ARG A 86  ? 0.7313 0.7526 0.7132 -0.1179 -0.2191 0.1284  86  ARG A CB  
692  C CG  . ARG A 86  ? 0.7709 0.7941 0.7724 -0.1250 -0.2589 0.1406  86  ARG A CG  
693  C CD  . ARG A 86  ? 0.8001 0.8259 0.8308 -0.1352 -0.2813 0.1348  86  ARG A CD  
694  N NE  . ARG A 86  ? 0.8476 0.8826 0.9253 -0.1383 -0.3171 0.1483  86  ARG A NE  
695  C CZ  . ARG A 86  ? 0.8977 0.9377 1.0143 -0.1474 -0.3450 0.1466  86  ARG A CZ  
696  N NH1 . ARG A 86  ? 0.9357 0.9699 1.0451 -0.1555 -0.3420 0.1313  86  ARG A NH1 
697  N NH2 . ARG A 86  ? 0.9167 0.9672 1.0842 -0.1484 -0.3775 0.1602  86  ARG A NH2 
698  N N   . LEU A 87  ? 0.7268 0.7166 0.5817 -0.1162 -0.1609 0.0958  87  LEU A N   
699  C CA  . LEU A 87  ? 0.6972 0.6870 0.5486 -0.1073 -0.1293 0.0878  87  LEU A CA  
700  C C   . LEU A 87  ? 0.7191 0.6925 0.5158 -0.1115 -0.1209 0.0738  87  LEU A C   
701  O O   . LEU A 87  ? 0.7481 0.7134 0.5012 -0.1144 -0.1234 0.0746  87  LEU A O   
702  C CB  . LEU A 87  ? 0.6983 0.6954 0.5570 -0.0959 -0.1145 0.0962  87  LEU A CB  
703  C CG  . LEU A 87  ? 0.6945 0.6896 0.5418 -0.0864 -0.0857 0.0883  87  LEU A CG  
704  C CD1 . LEU A 87  ? 0.6591 0.6638 0.5471 -0.0788 -0.0703 0.0876  87  LEU A CD1 
705  C CD2 . LEU A 87  ? 0.6998 0.6955 0.5346 -0.0793 -0.0780 0.0936  87  LEU A CD2 
706  N N   . ARG A 88  ? 0.7006 0.6694 0.5033 -0.1112 -0.1085 0.0619  88  ARG A N   
707  C CA  . ARG A 88  ? 0.6793 0.6355 0.4444 -0.1098 -0.0913 0.0482  88  ARG A CA  
708  C C   . ARG A 88  ? 0.6300 0.5918 0.4135 -0.0973 -0.0662 0.0495  88  ARG A C   
709  O O   . ARG A 88  ? 0.6309 0.5998 0.4520 -0.0934 -0.0605 0.0538  88  ARG A O   
710  C CB  . ARG A 88  ? 0.6918 0.6348 0.4476 -0.1186 -0.0992 0.0328  88  ARG A CB  
711  C CG  . ARG A 88  ? 0.7245 0.6593 0.4532 -0.1311 -0.1267 0.0293  88  ARG A CG  
712  C CD  . ARG A 88  ? 0.7410 0.6694 0.4148 -0.1336 -0.1286 0.0309  88  ARG A CD  
713  N NE  . ARG A 88  ? 0.7788 0.6977 0.4212 -0.1457 -0.1571 0.0295  88  ARG A NE  
714  C CZ  . ARG A 88  ? 0.7906 0.7147 0.4350 -0.1495 -0.1801 0.0461  88  ARG A CZ  
715  N NH1 . ARG A 88  ? 0.7633 0.7033 0.4486 -0.1418 -0.1775 0.0639  88  ARG A NH1 
716  N NH2 . ARG A 88  ? 0.8367 0.7490 0.4429 -0.1607 -0.2073 0.0443  88  ARG A NH2 
717  N N   . VAL A 89  ? 0.6103 0.5691 0.3673 -0.0916 -0.0516 0.0464  89  VAL A N   
718  C CA  . VAL A 89  ? 0.5914 0.5536 0.3605 -0.0798 -0.0315 0.0468  89  VAL A CA  
719  C C   . VAL A 89  ? 0.6031 0.5537 0.3513 -0.0783 -0.0188 0.0328  89  VAL A C   
720  O O   . VAL A 89  ? 0.6274 0.5704 0.3446 -0.0835 -0.0191 0.0240  89  VAL A O   
721  C CB  . VAL A 89  ? 0.5886 0.5586 0.3564 -0.0730 -0.0272 0.0554  89  VAL A CB  
722  C CG1 . VAL A 89  ? 0.6097 0.5745 0.3422 -0.0779 -0.0285 0.0537  89  VAL A CG1 
723  C CG2 . VAL A 89  ? 0.5628 0.5355 0.3418 -0.0607 -0.0103 0.0547  89  VAL A CG2 
724  N N   . TYR A 90  ? 0.6157 0.5646 0.3814 -0.0708 -0.0069 0.0313  90  TYR A N   
725  C CA  . TYR A 90  ? 0.6323 0.5697 0.3877 -0.0680 0.0037  0.0191  90  TYR A CA  
726  C C   . TYR A 90  ? 0.6239 0.5639 0.3886 -0.0555 0.0167  0.0229  90  TYR A C   
727  O O   . TYR A 90  ? 0.6356 0.5836 0.4152 -0.0497 0.0182  0.0337  90  TYR A O   
728  C CB  . TYR A 90  ? 0.6331 0.5602 0.4022 -0.0729 0.0002  0.0131  90  TYR A CB  
729  C CG  . TYR A 90  ? 0.6677 0.5917 0.4360 -0.0854 -0.0169 0.0094  90  TYR A CG  
730  C CD1 . TYR A 90  ? 0.6646 0.5991 0.4565 -0.0897 -0.0288 0.0214  90  TYR A CD1 
731  C CD2 . TYR A 90  ? 0.6965 0.6063 0.4439 -0.0927 -0.0218 -0.0076 90  TYR A CD2 
732  C CE1 . TYR A 90  ? 0.6707 0.6024 0.4665 -0.1013 -0.0482 0.0180  90  TYR A CE1 
733  C CE2 . TYR A 90  ? 0.7118 0.6166 0.4563 -0.1044 -0.0408 -0.0127 90  TYR A CE2 
734  C CZ  . TYR A 90  ? 0.7071 0.6231 0.4765 -0.1090 -0.0555 0.0008  90  TYR A CZ  
735  O OH  . TYR A 90  ? 0.7470 0.6583 0.5171 -0.1208 -0.0779 -0.0042 90  TYR A OH  
736  N N   . VAL A 91  ? 0.6007 0.5333 0.3569 -0.0510 0.0255  0.0131  91  VAL A N   
737  C CA  . VAL A 91  ? 0.5901 0.5226 0.3555 -0.0394 0.0337  0.0160  91  VAL A CA  
738  C C   . VAL A 91  ? 0.6253 0.5443 0.3982 -0.0370 0.0377  0.0084  91  VAL A C   
739  O O   . VAL A 91  ? 0.6707 0.5825 0.4363 -0.0405 0.0400  -0.0052 91  VAL A O   
740  C CB  . VAL A 91  ? 0.5896 0.5284 0.3467 -0.0348 0.0383  0.0134  91  VAL A CB  
741  C CG1 . VAL A 91  ? 0.5855 0.5214 0.3524 -0.0235 0.0437  0.0118  91  VAL A CG1 
742  C CG2 . VAL A 91  ? 0.5531 0.5033 0.3092 -0.0353 0.0336  0.0232  91  VAL A CG2 
743  N N   . HIS A 92  ? 0.6173 0.5316 0.4042 -0.0315 0.0390  0.0175  92  HIS A N   
744  C CA  . HIS A 92  ? 0.5860 0.4859 0.3833 -0.0273 0.0417  0.0146  92  HIS A CA  
745  C C   . HIS A 92  ? 0.5484 0.4485 0.3459 -0.0150 0.0443  0.0208  92  HIS A C   
746  O O   . HIS A 92  ? 0.5295 0.4357 0.3235 -0.0111 0.0444  0.0327  92  HIS A O   
747  C CB  . HIS A 92  ? 0.5997 0.4919 0.4121 -0.0320 0.0400  0.0235  92  HIS A CB  
748  C CG  . HIS A 92  ? 0.6125 0.4893 0.4365 -0.0258 0.0426  0.0283  92  HIS A CG  
749  N ND1 . HIS A 92  ? 0.6121 0.4874 0.4354 -0.0180 0.0458  0.0443  92  HIS A ND1 
750  C CD2 . HIS A 92  ? 0.6219 0.4830 0.4569 -0.0255 0.0418  0.0193  92  HIS A CD2 
751  C CE1 . HIS A 92  ? 0.6132 0.4719 0.4459 -0.0137 0.0455  0.0475  92  HIS A CE1 
752  N NE2 . HIS A 92  ? 0.6283 0.4784 0.4717 -0.0179 0.0430  0.0321  92  HIS A NE2 
753  N N   . THR A 93  ? 0.5347 0.4282 0.3376 -0.0089 0.0457  0.0118  93  THR A N   
754  C CA  . THR A 93  ? 0.5226 0.4166 0.3280 0.0027  0.0441  0.0156  93  THR A CA  
755  C C   . THR A 93  ? 0.5601 0.4393 0.3724 0.0094  0.0408  0.0260  93  THR A C   
756  O O   . THR A 93  ? 0.5722 0.4394 0.3932 0.0049  0.0416  0.0281  93  THR A O   
757  C CB  . THR A 93  ? 0.5135 0.4104 0.3282 0.0064  0.0466  0.0016  93  THR A CB  
758  O OG1 . THR A 93  ? 0.5172 0.4014 0.3488 0.0085  0.0484  -0.0076 93  THR A OG1 
759  C CG2 . THR A 93  ? 0.5102 0.4194 0.3147 -0.0016 0.0520  -0.0070 93  THR A CG2 
760  N N   . ARG A 94  ? 0.5733 0.4519 0.3815 0.0198  0.0357  0.0327  94  ARG A N   
761  C CA  . ARG A 94  ? 0.6099 0.4727 0.4193 0.0276  0.0300  0.0445  94  ARG A CA  
762  C C   . ARG A 94  ? 0.6273 0.4773 0.4613 0.0307  0.0271  0.0369  94  ARG A C   
763  O O   . ARG A 94  ? 0.6560 0.4909 0.4946 0.0376  0.0200  0.0475  94  ARG A O   
764  C CB  . ARG A 94  ? 0.6178 0.4822 0.4144 0.0383  0.0213  0.0503  94  ARG A CB  
765  C CG  . ARG A 94  ? 0.6129 0.4802 0.4282 0.0456  0.0135  0.0390  94  ARG A CG  
766  C CD  . ARG A 94  ? 0.6288 0.4835 0.4425 0.0573  -0.0012 0.0484  94  ARG A CD  
767  N NE  . ARG A 94  ? 0.6350 0.4878 0.4151 0.0611  -0.0060 0.0604  94  ARG A NE  
768  C CZ  . ARG A 94  ? 0.6689 0.5053 0.4276 0.0666  -0.0129 0.0766  94  ARG A CZ  
769  N NH1 . ARG A 94  ? 0.6713 0.5068 0.3944 0.0682  -0.0112 0.0855  94  ARG A NH1 
770  N NH2 . ARG A 94  ? 0.7070 0.5266 0.4791 0.0703  -0.0201 0.0844  94  ARG A NH2 
771  N N   . ASN A 95  ? 0.6273 0.4825 0.4759 0.0265  0.0325  0.0188  95  ASN A N   
772  C CA  . ASN A 95  ? 0.6620 0.5052 0.5370 0.0297  0.0326  0.0080  95  ASN A CA  
773  C C   . ASN A 95  ? 0.6709 0.5088 0.5494 0.0191  0.0401  -0.0040 95  ASN A C   
774  O O   . ASN A 95  ? 0.7025 0.5347 0.5996 0.0200  0.0443  -0.0209 95  ASN A O   
775  C CB  . ASN A 95  ? 0.6752 0.5279 0.5690 0.0366  0.0336  -0.0062 95  ASN A CB  
776  C CG  . ASN A 95  ? 0.6941 0.5480 0.5919 0.0479  0.0211  0.0043  95  ASN A CG  
777  O OD1 . ASN A 95  ? 0.7656 0.6056 0.6580 0.0531  0.0108  0.0201  95  ASN A OD1 
778  N ND2 . ASN A 95  ? 0.6929 0.5623 0.5984 0.0510  0.0211  -0.0034 95  ASN A ND2 
779  N N   . ASP A 96  ? 0.6508 0.4898 0.5138 0.0095  0.0411  0.0039  96  ASP A N   
780  C CA  . ASP A 96  ? 0.6604 0.4916 0.5280 -0.0011 0.0436  -0.0061 96  ASP A CA  
781  C C   . ASP A 96  ? 0.6490 0.4869 0.5115 -0.0049 0.0501  -0.0296 96  ASP A C   
782  O O   . ASP A 96  ? 0.6351 0.4611 0.5097 -0.0064 0.0529  -0.0465 96  ASP A O   
783  C CB  . ASP A 96  ? 0.6876 0.4962 0.5791 0.0007  0.0399  -0.0026 96  ASP A CB  
784  C CG  . ASP A 96  ? 0.7173 0.5183 0.6088 -0.0029 0.0370  0.0207  96  ASP A CG  
785  O OD1 . ASP A 96  ? 0.7014 0.5153 0.5773 -0.0092 0.0392  0.0296  96  ASP A OD1 
786  O OD2 . ASP A 96  ? 0.7976 0.5794 0.7075 0.0004  0.0334  0.0303  96  ASP A OD2 
787  N N   . TYR A 97  ? 0.6326 0.4886 0.4763 -0.0064 0.0532  -0.0302 97  TYR A N   
788  C CA  . TYR A 97  ? 0.6496 0.5132 0.4773 -0.0138 0.0600  -0.0468 97  TYR A CA  
789  C C   . TYR A 97  ? 0.6508 0.5251 0.4555 -0.0233 0.0556  -0.0378 97  TYR A C   
790  O O   . TYR A 97  ? 0.6053 0.4892 0.4071 -0.0210 0.0519  -0.0218 97  TYR A O   
791  C CB  . TYR A 97  ? 0.6546 0.5297 0.4850 -0.0076 0.0689  -0.0550 97  TYR A CB  
792  C CG  . TYR A 97  ? 0.6725 0.5399 0.5318 0.0020  0.0743  -0.0671 97  TYR A CG  
793  C CD1 . TYR A 97  ? 0.7144 0.5727 0.5790 -0.0001 0.0837  -0.0888 97  TYR A CD1 
794  C CD2 . TYR A 97  ? 0.6622 0.5310 0.5447 0.0138  0.0688  -0.0578 97  TYR A CD2 
795  C CE1 . TYR A 97  ? 0.7313 0.5827 0.6291 0.0099  0.0892  -0.1008 97  TYR A CE1 
796  C CE2 . TYR A 97  ? 0.6855 0.5480 0.6009 0.0233  0.0714  -0.0680 97  TYR A CE2 
797  C CZ  . TYR A 97  ? 0.7079 0.5621 0.6342 0.0217  0.0825  -0.0896 97  TYR A CZ  
798  O OH  . TYR A 97  ? 0.6865 0.5350 0.6517 0.0322  0.0859  -0.1007 97  TYR A OH  
799  N N   . VAL A 98  ? 0.6768 0.5490 0.4649 -0.0338 0.0553  -0.0495 98  VAL A N   
800  C CA  . VAL A 98  ? 0.6625 0.5439 0.4323 -0.0431 0.0481  -0.0414 98  VAL A CA  
801  C C   . VAL A 98  ? 0.6461 0.5367 0.3897 -0.0475 0.0532  -0.0488 98  VAL A C   
802  O O   . VAL A 98  ? 0.6559 0.5418 0.3905 -0.0477 0.0628  -0.0654 98  VAL A O   
803  C CB  . VAL A 98  ? 0.7059 0.5765 0.4781 -0.0531 0.0383  -0.0449 98  VAL A CB  
804  C CG1 . VAL A 98  ? 0.7180 0.5956 0.4678 -0.0643 0.0290  -0.0444 98  VAL A CG1 
805  C CG2 . VAL A 98  ? 0.7089 0.5762 0.5070 -0.0508 0.0341  -0.0285 98  VAL A CG2 
806  N N   . ILE A 99  ? 0.6416 0.5447 0.3746 -0.0506 0.0479  -0.0354 99  ILE A N   
807  C CA  . ILE A 99  ? 0.6534 0.5643 0.3607 -0.0562 0.0508  -0.0369 99  ILE A CA  
808  C C   . ILE A 99  ? 0.6619 0.5740 0.3530 -0.0668 0.0364  -0.0302 99  ILE A C   
809  O O   . ILE A 99  ? 0.6270 0.5462 0.3323 -0.0662 0.0272  -0.0153 99  ILE A O   
810  C CB  . ILE A 99  ? 0.6430 0.5672 0.3572 -0.0495 0.0562  -0.0264 99  ILE A CB  
811  C CG1 . ILE A 99  ? 0.6443 0.5683 0.3796 -0.0388 0.0671  -0.0329 99  ILE A CG1 
812  C CG2 . ILE A 99  ? 0.6605 0.5909 0.3485 -0.0574 0.0588  -0.0247 99  ILE A CG2 
813  C CD1 . ILE A 99  ? 0.6268 0.5625 0.3755 -0.0317 0.0684  -0.0232 99  ILE A CD1 
814  N N   . TYR A 100 ? 0.7121 0.6164 0.3736 -0.0760 0.0347  -0.0425 100 TYR A N   
815  C CA  . TYR A 100 ? 0.7467 0.6502 0.3857 -0.0873 0.0183  -0.0382 100 TYR A CA  
816  C C   . TYR A 100 ? 0.7788 0.6916 0.3946 -0.0901 0.0196  -0.0271 100 TYR A C   
817  O O   . TYR A 100 ? 0.8208 0.7348 0.4209 -0.0885 0.0358  -0.0324 100 TYR A O   
818  C CB  . TYR A 100 ? 0.7774 0.6647 0.3908 -0.0949 0.0163  -0.0594 100 TYR A CB  
819  C CG  . TYR A 100 ? 0.7500 0.6255 0.3906 -0.0928 0.0140  -0.0704 100 TYR A CG  
820  C CD1 . TYR A 100 ? 0.7317 0.6057 0.3953 -0.0975 -0.0033 -0.0631 100 TYR A CD1 
821  C CD2 . TYR A 100 ? 0.7436 0.6096 0.3921 -0.0863 0.0293  -0.0871 100 TYR A CD2 
822  C CE1 . TYR A 100 ? 0.7402 0.6022 0.4312 -0.0968 -0.0050 -0.0710 100 TYR A CE1 
823  C CE2 . TYR A 100 ? 0.7387 0.5915 0.4141 -0.0846 0.0262  -0.0958 100 TYR A CE2 
824  C CZ  . TYR A 100 ? 0.7380 0.5883 0.4338 -0.0904 0.0091  -0.0870 100 TYR A CZ  
825  O OH  . TYR A 100 ? 0.7361 0.5727 0.4619 -0.0898 0.0063  -0.0927 100 TYR A OH  
826  N N   . ILE A 101 ? 0.7525 0.6718 0.3706 -0.0943 0.0032  -0.0110 101 ILE A N   
827  C CA  . ILE A 101 ? 0.7506 0.6782 0.3565 -0.0956 0.0029  0.0035  101 ILE A CA  
828  C C   . ILE A 101 ? 0.7733 0.6971 0.3527 -0.1070 -0.0178 0.0109  101 ILE A C   
829  O O   . ILE A 101 ? 0.7619 0.6895 0.3633 -0.1085 -0.0361 0.0199  101 ILE A O   
830  C CB  . ILE A 101 ? 0.7338 0.6738 0.3775 -0.0862 0.0034  0.0180  101 ILE A CB  
831  C CG1 . ILE A 101 ? 0.7167 0.6583 0.3824 -0.0750 0.0199  0.0108  101 ILE A CG1 
832  C CG2 . ILE A 101 ? 0.7271 0.6739 0.3640 -0.0879 0.0006  0.0332  101 ILE A CG2 
833  C CD1 . ILE A 101 ? 0.6902 0.6419 0.3827 -0.0656 0.0216  0.0221  101 ILE A CD1 
834  N N   . LYS A 102 ? 0.8008 0.7174 0.3337 -0.1148 -0.0143 0.0077  102 LYS A N   
835  C CA  . LYS A 102 ? 0.8306 0.7406 0.3282 -0.1262 -0.0355 0.0155  102 LYS A CA  
836  C C   . LYS A 102 ? 0.8000 0.7201 0.3179 -0.1252 -0.0488 0.0401  102 LYS A C   
837  O O   . LYS A 102 ? 0.7835 0.7105 0.3091 -0.1208 -0.0354 0.0500  102 LYS A O   
838  C CB  . LYS A 102 ? 0.9037 0.8032 0.3420 -0.1339 -0.0237 0.0081  102 LYS A CB  
839  C CG  . LYS A 102 ? 0.9637 0.8505 0.3777 -0.1356 -0.0130 -0.0193 102 LYS A CG  
840  C CD  . LYS A 102 ? 1.0567 0.9309 0.4028 -0.1450 -0.0047 -0.0280 102 LYS A CD  
841  C CE  . LYS A 102 ? 1.1164 0.9752 0.4373 -0.1471 0.0012  -0.0583 102 LYS A CE  
842  N NZ  . LYS A 102 ? 1.1958 1.0428 0.4475 -0.1547 0.0164  -0.0688 102 LYS A NZ  
843  N N   . PRO A 103 ? 0.7929 0.7142 0.3249 -0.1293 -0.0759 0.0500  103 PRO A N   
844  C CA  . PRO A 103 ? 0.7772 0.7092 0.3435 -0.1257 -0.0883 0.0712  103 PRO A CA  
845  C C   . PRO A 103 ? 0.8143 0.7467 0.3628 -0.1266 -0.0829 0.0873  103 PRO A C   
846  O O   . PRO A 103 ? 0.8130 0.7548 0.3965 -0.1186 -0.0764 0.0973  103 PRO A O   
847  C CB  . PRO A 103 ? 0.7902 0.7189 0.3562 -0.1340 -0.1206 0.0774  103 PRO A CB  
848  C CG  . PRO A 103 ? 0.7942 0.7159 0.3560 -0.1375 -0.1227 0.0569  103 PRO A CG  
849  C CD  . PRO A 103 ? 0.8142 0.7267 0.3365 -0.1371 -0.0970 0.0400  103 PRO A CD  
850  N N   . GLU A 104 ? 0.8685 0.7892 0.3610 -0.1368 -0.0843 0.0889  104 GLU A N   
851  C CA  . GLU A 104 ? 0.8906 0.8086 0.3590 -0.1409 -0.0800 0.1070  104 GLU A CA  
852  C C   . GLU A 104 ? 0.8557 0.7810 0.3407 -0.1338 -0.0496 0.1049  104 GLU A C   
853  O O   . GLU A 104 ? 0.8541 0.7795 0.3344 -0.1361 -0.0445 0.1215  104 GLU A O   
854  C CB  . GLU A 104 ? 0.9797 0.8820 0.3762 -0.1540 -0.0846 0.1070  104 GLU A CB  
855  C CG  . GLU A 104 ? 1.0288 0.9237 0.3888 -0.1560 -0.0638 0.0807  104 GLU A CG  
856  C CD  . GLU A 104 ? 1.0569 0.9456 0.4153 -0.1574 -0.0781 0.0597  104 GLU A CD  
857  O OE1 . GLU A 104 ? 1.1206 1.0002 0.4457 -0.1596 -0.0629 0.0376  104 GLU A OE1 
858  O OE2 . GLU A 104 ? 1.0133 0.9062 0.4076 -0.1562 -0.1033 0.0644  104 GLU A OE2 
859  N N   . THR A 105 ? 0.8301 0.7611 0.3383 -0.1254 -0.0315 0.0861  105 THR A N   
860  C CA  . THR A 105 ? 0.8161 0.7543 0.3438 -0.1184 -0.0059 0.0825  105 THR A CA  
861  C C   . THR A 105 ? 0.7922 0.7388 0.3603 -0.1123 -0.0094 0.0992  105 THR A C   
862  O O   . THR A 105 ? 0.7502 0.7023 0.3544 -0.1056 -0.0231 0.1031  105 THR A O   
863  C CB  . THR A 105 ? 0.7831 0.7250 0.3343 -0.1093 0.0074  0.0615  105 THR A CB  
864  O OG1 . THR A 105 ? 0.8204 0.7523 0.3378 -0.1150 0.0077  0.0452  105 THR A OG1 
865  C CG2 . THR A 105 ? 0.7604 0.7087 0.3291 -0.1027 0.0317  0.0557  105 THR A CG2 
866  N N   . ARG A 106 ? 0.8237 0.7711 0.3867 -0.1149 0.0047  0.1081  106 ARG A N   
867  C CA  . ARG A 106 ? 0.7875 0.7413 0.3904 -0.1092 0.0051  0.1201  106 ARG A CA  
868  C C   . ARG A 106 ? 0.7532 0.7151 0.3846 -0.1001 0.0255  0.1053  106 ARG A C   
869  O O   . ARG A 106 ? 0.7540 0.7168 0.3737 -0.1035 0.0458  0.1004  106 ARG A O   
870  C CB  . ARG A 106 ? 0.8070 0.7553 0.3912 -0.1191 0.0051  0.1417  106 ARG A CB  
871  C CG  . ARG A 106 ? 0.7956 0.7477 0.4244 -0.1143 0.0014  0.1551  106 ARG A CG  
872  C CD  . ARG A 106 ? 0.8713 0.8157 0.4833 -0.1252 0.0003  0.1795  106 ARG A CD  
873  N NE  . ARG A 106 ? 0.8827 0.8286 0.5409 -0.1213 -0.0034 0.1917  106 ARG A NE  
874  C CZ  . ARG A 106 ? 0.8843 0.8363 0.5738 -0.1179 0.0134  0.1867  106 ARG A CZ  
875  N NH1 . ARG A 106 ? 0.8977 0.8567 0.5817 -0.1168 0.0357  0.1698  106 ARG A NH1 
876  N NH2 . ARG A 106 ? 0.8632 0.8137 0.5936 -0.1155 0.0062  0.1980  106 ARG A NH2 
877  N N   . LEU A 107 ? 0.7032 0.6707 0.3718 -0.0885 0.0200  0.0979  107 LEU A N   
878  C CA  . LEU A 107 ? 0.6496 0.6233 0.3458 -0.0791 0.0336  0.0857  107 LEU A CA  
879  C C   . LEU A 107 ? 0.6241 0.6009 0.3447 -0.0789 0.0367  0.0958  107 LEU A C   
880  O O   . LEU A 107 ? 0.6254 0.5998 0.3547 -0.0809 0.0239  0.1106  107 LEU A O   
881  C CB  . LEU A 107 ? 0.6330 0.6095 0.3547 -0.0674 0.0259  0.0773  107 LEU A CB  
882  C CG  . LEU A 107 ? 0.6470 0.6222 0.3616 -0.0636 0.0320  0.0616  107 LEU A CG  
883  C CD1 . LEU A 107 ? 0.6340 0.6124 0.3770 -0.0508 0.0326  0.0542  107 LEU A CD1 
884  C CD2 . LEU A 107 ? 0.6506 0.6238 0.3453 -0.0684 0.0485  0.0516  107 LEU A CD2 
885  N N   . PRO A 108 ? 0.5967 0.5786 0.3336 -0.0764 0.0526  0.0879  108 PRO A N   
886  C CA  . PRO A 108 ? 0.5783 0.5636 0.3491 -0.0748 0.0536  0.0944  108 PRO A CA  
887  C C   . PRO A 108 ? 0.5526 0.5372 0.3522 -0.0648 0.0363  0.0944  108 PRO A C   
888  O O   . PRO A 108 ? 0.4941 0.4798 0.3005 -0.0547 0.0318  0.0824  108 PRO A O   
889  C CB  . PRO A 108 ? 0.5613 0.5538 0.3513 -0.0708 0.0700  0.0805  108 PRO A CB  
890  C CG  . PRO A 108 ? 0.5826 0.5742 0.3400 -0.0748 0.0836  0.0713  108 PRO A CG  
891  C CD  . PRO A 108 ? 0.5940 0.5784 0.3224 -0.0753 0.0695  0.0721  108 PRO A CD  
892  N N   . ARG A 109 ? 0.5849 0.5665 0.4008 -0.0677 0.0276  0.1084  109 ARG A N   
893  C CA  . ARG A 109 ? 0.5900 0.5701 0.4367 -0.0578 0.0137  0.1061  109 ARG A CA  
894  C C   . ARG A 109 ? 0.5821 0.5656 0.4583 -0.0494 0.0170  0.0923  109 ARG A C   
895  O O   . ARG A 109 ? 0.6143 0.5970 0.5029 -0.0380 0.0087  0.0812  109 ARG A O   
896  C CB  . ARG A 109 ? 0.6023 0.5762 0.4623 -0.0633 0.0028  0.1245  109 ARG A CB  
897  C CG  . ARG A 109 ? 0.6080 0.5776 0.4469 -0.0681 -0.0089 0.1376  109 ARG A CG  
898  C CD  . ARG A 109 ? 0.6449 0.6110 0.4446 -0.0823 -0.0040 0.1518  109 ARG A CD  
899  N NE  . ARG A 109 ? 0.6610 0.6283 0.4270 -0.0835 -0.0038 0.1442  109 ARG A NE  
900  C CZ  . ARG A 109 ? 0.6656 0.6314 0.4261 -0.0824 -0.0197 0.1474  109 ARG A CZ  
901  N NH1 . ARG A 109 ? 0.6600 0.6284 0.4041 -0.0804 -0.0187 0.1348  109 ARG A NH1 
902  N NH2 . ARG A 109 ? 0.6595 0.6215 0.4388 -0.0822 -0.0371 0.1621  109 ARG A NH2 
903  N N   . ASN A 110 ? 0.5636 0.5511 0.4507 -0.0550 0.0289  0.0927  110 ASN A N   
904  C CA  . ASN A 110 ? 0.5458 0.5372 0.4658 -0.0477 0.0288  0.0798  110 ASN A CA  
905  C C   . ASN A 110 ? 0.5221 0.5177 0.4321 -0.0399 0.0339  0.0637  110 ASN A C   
906  O O   . ASN A 110 ? 0.5259 0.5250 0.4170 -0.0446 0.0474  0.0624  110 ASN A O   
907  C CB  . ASN A 110 ? 0.5543 0.5501 0.5004 -0.0568 0.0392  0.0871  110 ASN A CB  
908  C CG  . ASN A 110 ? 0.5320 0.5330 0.5172 -0.0498 0.0365  0.0730  110 ASN A CG  
909  O OD1 . ASN A 110 ? 0.5126 0.5193 0.4962 -0.0443 0.0418  0.0604  110 ASN A OD1 
910  N ND2 . ASN A 110 ? 0.5429 0.5410 0.5654 -0.0498 0.0262  0.0749  110 ASN A ND2 
911  N N   . TYR A 111 ? 0.5004 0.4942 0.4231 -0.0278 0.0227  0.0512  111 TYR A N   
912  C CA  . TYR A 111 ? 0.4989 0.4937 0.4115 -0.0194 0.0240  0.0386  111 TYR A CA  
913  C C   . TYR A 111 ? 0.5071 0.5093 0.4312 -0.0226 0.0374  0.0339  111 TYR A C   
914  O O   . TYR A 111 ? 0.5109 0.5135 0.4180 -0.0210 0.0448  0.0285  111 TYR A O   
915  C CB  . TYR A 111 ? 0.4927 0.4830 0.4178 -0.0068 0.0089  0.0276  111 TYR A CB  
916  C CG  . TYR A 111 ? 0.4884 0.4778 0.4067 0.0023  0.0073  0.0168  111 TYR A CG  
917  C CD1 . TYR A 111 ? 0.4872 0.4731 0.3765 0.0054  0.0107  0.0165  111 TYR A CD1 
918  C CD2 . TYR A 111 ? 0.4811 0.4727 0.4257 0.0074  0.0008  0.0081  111 TYR A CD2 
919  C CE1 . TYR A 111 ? 0.4883 0.4712 0.3724 0.0133  0.0083  0.0093  111 TYR A CE1 
920  C CE2 . TYR A 111 ? 0.4775 0.4668 0.4172 0.0159  -0.0034 0.0004  111 TYR A CE2 
921  C CZ  . TYR A 111 ? 0.4863 0.4705 0.3945 0.0189  0.0008  0.0017  111 TYR A CZ  
922  O OH  . TYR A 111 ? 0.5046 0.4844 0.4089 0.0270  -0.0041 -0.0034 111 TYR A OH  
923  N N   . ASN A 112 ? 0.5158 0.5241 0.4739 -0.0265 0.0408  0.0349  112 ASN A N   
924  C CA  . ASN A 112 ? 0.5267 0.5441 0.5081 -0.0272 0.0529  0.0280  112 ASN A CA  
925  C C   . ASN A 112 ? 0.5429 0.5651 0.5055 -0.0381 0.0764  0.0337  112 ASN A C   
926  O O   . ASN A 112 ? 0.5451 0.5738 0.5175 -0.0370 0.0898  0.0251  112 ASN A O   
927  C CB  . ASN A 112 ? 0.5502 0.5740 0.5817 -0.0281 0.0485  0.0271  112 ASN A CB  
928  C CG  . ASN A 112 ? 0.5526 0.5704 0.6006 -0.0165 0.0239  0.0172  112 ASN A CG  
929  O OD1 . ASN A 112 ? 0.5640 0.5792 0.6046 -0.0061 0.0153  0.0069  112 ASN A OD1 
930  N ND2 . ASN A 112 ? 0.5461 0.5598 0.6137 -0.0181 0.0119  0.0202  112 ASN A ND2 
931  N N   . ARG A 113 ? 0.5752 0.5936 0.5118 -0.0483 0.0810  0.0476  113 ARG A N   
932  C CA  . ARG A 113 ? 0.6155 0.6342 0.5183 -0.0584 0.1002  0.0523  113 ARG A CA  
933  C C   . ARG A 113 ? 0.6047 0.6173 0.4721 -0.0536 0.0975  0.0434  113 ARG A C   
934  O O   . ARG A 113 ? 0.6025 0.6161 0.4529 -0.0561 0.1128  0.0358  113 ARG A O   
935  C CB  . ARG A 113 ? 0.6673 0.6805 0.5464 -0.0702 0.1002  0.0715  113 ARG A CB  
936  C CG  . ARG A 113 ? 0.7249 0.7435 0.6239 -0.0812 0.1154  0.0842  113 ARG A CG  
937  C CD  . ARG A 113 ? 0.8052 0.8156 0.6652 -0.0941 0.1182  0.1046  113 ARG A CD  
938  N NE  . ARG A 113 ? 0.8666 0.8786 0.7484 -0.1049 0.1275  0.1225  113 ARG A NE  
939  C CZ  . ARG A 113 ? 0.8707 0.8756 0.7690 -0.1082 0.1123  0.1391  113 ARG A CZ  
940  N NH1 . ARG A 113 ? 0.8356 0.8317 0.7282 -0.1013 0.0878  0.1398  113 ARG A NH1 
941  N NH2 . ARG A 113 ? 0.8586 0.8651 0.7832 -0.1184 0.1227  0.1550  113 ARG A NH2 
942  N N   . PHE A 114 ? 0.5960 0.6019 0.4548 -0.0469 0.0787  0.0439  114 PHE A N   
943  C CA  . PHE A 114 ? 0.5797 0.5798 0.4122 -0.0427 0.0746  0.0370  114 PHE A CA  
944  C C   . PHE A 114 ? 0.5436 0.5454 0.3897 -0.0344 0.0801  0.0222  114 PHE A C   
945  O O   . PHE A 114 ? 0.5444 0.5418 0.3703 -0.0344 0.0848  0.0155  114 PHE A O   
946  C CB  . PHE A 114 ? 0.5740 0.5688 0.4040 -0.0360 0.0563  0.0403  114 PHE A CB  
947  C CG  . PHE A 114 ? 0.5830 0.5730 0.3986 -0.0296 0.0526  0.0327  114 PHE A CG  
948  C CD1 . PHE A 114 ? 0.5959 0.5818 0.3837 -0.0357 0.0539  0.0345  114 PHE A CD1 
949  C CD2 . PHE A 114 ? 0.5736 0.5621 0.4034 -0.0182 0.0471  0.0244  114 PHE A CD2 
950  C CE1 . PHE A 114 ? 0.6066 0.5876 0.3863 -0.0310 0.0509  0.0285  114 PHE A CE1 
951  C CE2 . PHE A 114 ? 0.5782 0.5610 0.3951 -0.0134 0.0450  0.0203  114 PHE A CE2 
952  C CZ  . PHE A 114 ? 0.5914 0.5708 0.3860 -0.0200 0.0477  0.0224  114 PHE A CZ  
953  N N   . ILE A 115 ? 0.5162 0.5231 0.3986 -0.0272 0.0764  0.0173  115 ILE A N   
954  C CA  . ILE A 115 ? 0.5045 0.5130 0.4069 -0.0185 0.0782  0.0048  115 ILE A CA  
955  C C   . ILE A 115 ? 0.5138 0.5293 0.4241 -0.0242 0.1006  -0.0012 115 ILE A C   
956  O O   . ILE A 115 ? 0.5443 0.5577 0.4536 -0.0203 0.1077  -0.0118 115 ILE A O   
957  C CB  . ILE A 115 ? 0.4832 0.4950 0.4235 -0.0093 0.0642  0.0013  115 ILE A CB  
958  C CG1 . ILE A 115 ? 0.4663 0.4693 0.3940 -0.0015 0.0437  0.0034  115 ILE A CG1 
959  C CG2 . ILE A 115 ? 0.4833 0.4980 0.4497 -0.0016 0.0667  -0.0099 115 ILE A CG2 
960  C CD1 . ILE A 115 ? 0.4704 0.4646 0.3785 0.0067  0.0378  -0.0007 115 ILE A CD1 
961  N N   . GLY A 116 ? 0.5164 0.5398 0.4363 -0.0335 0.1129  0.0056  116 GLY A N   
962  C CA  . GLY A 116 ? 0.5431 0.5736 0.4656 -0.0402 0.1390  0.0007  116 GLY A CA  
963  C C   . GLY A 116 ? 0.5530 0.5750 0.4283 -0.0446 0.1491  -0.0045 116 GLY A C   
964  O O   . GLY A 116 ? 0.5668 0.5903 0.4451 -0.0430 0.1657  -0.0179 116 GLY A O   
965  N N   . LEU A 117 ? 0.5534 0.5660 0.3888 -0.0497 0.1376  0.0051  117 LEU A N   
966  C CA  . LEU A 117 ? 0.5832 0.5862 0.3728 -0.0549 0.1410  0.0010  117 LEU A CA  
967  C C   . LEU A 117 ? 0.5980 0.5944 0.3914 -0.0455 0.1353  -0.0135 117 LEU A C   
968  O O   . LEU A 117 ? 0.6378 0.6286 0.4118 -0.0476 0.1466  -0.0256 117 LEU A O   
969  C CB  . LEU A 117 ? 0.5731 0.5691 0.3328 -0.0608 0.1238  0.0159  117 LEU A CB  
970  C CG  . LEU A 117 ? 0.5881 0.5736 0.3018 -0.0672 0.1209  0.0135  117 LEU A CG  
971  C CD1 . LEU A 117 ? 0.6392 0.6233 0.3224 -0.0767 0.1429  0.0077  117 LEU A CD1 
972  C CD2 . LEU A 117 ? 0.5829 0.5640 0.2782 -0.0724 0.1019  0.0300  117 LEU A CD2 
973  N N   . MET A 118 ? 0.5855 0.5809 0.4025 -0.0352 0.1180  -0.0122 118 MET A N   
974  C CA  . MET A 118 ? 0.5943 0.5819 0.4158 -0.0265 0.1113  -0.0217 118 MET A CA  
975  C C   . MET A 118 ? 0.5993 0.5902 0.4494 -0.0209 0.1255  -0.0363 118 MET A C   
976  O O   . MET A 118 ? 0.5907 0.5734 0.4373 -0.0178 0.1290  -0.0476 118 MET A O   
977  C CB  . MET A 118 ? 0.5842 0.5697 0.4207 -0.0170 0.0913  -0.0152 118 MET A CB  
978  C CG  . MET A 118 ? 0.6043 0.5855 0.4164 -0.0204 0.0787  -0.0038 118 MET A CG  
979  S SD  . MET A 118 ? 0.6206 0.5916 0.3980 -0.0274 0.0777  -0.0051 118 MET A SD  
980  C CE  . MET A 118 ? 0.6420 0.6163 0.3922 -0.0414 0.0843  0.0014  118 MET A CE  
981  N N   . GLU A 119 ? 0.6097 0.6128 0.4942 -0.0193 0.1332  -0.0365 119 GLU A N   
982  C CA  . GLU A 119 ? 0.6541 0.6629 0.5753 -0.0130 0.1465  -0.0503 119 GLU A CA  
983  C C   . GLU A 119 ? 0.7123 0.7191 0.6098 -0.0202 0.1713  -0.0621 119 GLU A C   
984  O O   . GLU A 119 ? 0.7122 0.7138 0.6196 -0.0146 0.1789  -0.0773 119 GLU A O   
985  C CB  . GLU A 119 ? 0.6545 0.6785 0.6223 -0.0111 0.1491  -0.0473 119 GLU A CB  
986  C CG  . GLU A 119 ? 0.6529 0.6757 0.6431 -0.0022 0.1223  -0.0406 119 GLU A CG  
987  C CD  . GLU A 119 ? 0.6797 0.7165 0.7164 -0.0018 0.1204  -0.0376 119 GLU A CD  
988  O OE1 . GLU A 119 ? 0.6487 0.6840 0.7072 0.0067  0.0970  -0.0357 119 GLU A OE1 
989  O OE2 . GLU A 119 ? 0.6689 0.7174 0.7197 -0.0104 0.1424  -0.0373 119 GLU A OE2 
990  N N   . ASN A 120 ? 0.7474 0.7567 0.6112 -0.0326 0.1825  -0.0545 120 ASN A N   
991  C CA  . ASN A 120 ? 0.8018 0.8064 0.6277 -0.0412 0.2042  -0.0643 120 ASN A CA  
992  C C   . ASN A 120 ? 0.7798 0.7678 0.5770 -0.0392 0.1942  -0.0747 120 ASN A C   
993  O O   . ASN A 120 ? 0.8173 0.8005 0.6206 -0.0353 0.2070  -0.0934 120 ASN A O   
994  C CB  . ASN A 120 ? 0.8641 0.8693 0.6479 -0.0552 0.2099  -0.0497 120 ASN A CB  
995  C CG  . ASN A 120 ? 0.8734 0.8939 0.6841 -0.0598 0.2273  -0.0408 120 ASN A CG  
996  O OD1 . ASN A 120 ? 0.8883 0.9204 0.7473 -0.0536 0.2413  -0.0499 120 ASN A OD1 
997  N ND2 . ASN A 120 ? 0.8740 0.8943 0.6577 -0.0708 0.2262  -0.0224 120 ASN A ND2 
998  N N   . LEU A 121 ? 0.7202 0.6998 0.4922 -0.0417 0.1715  -0.0630 121 LEU A N   
999  C CA  . LEU A 121 ? 0.7172 0.6814 0.4615 -0.0429 0.1616  -0.0706 121 LEU A CA  
1000 C C   . LEU A 121 ? 0.7157 0.6732 0.4908 -0.0320 0.1623  -0.0863 121 LEU A C   
1001 O O   . LEU A 121 ? 0.7468 0.6931 0.5061 -0.0336 0.1693  -0.1025 121 LEU A O   
1002 C CB  . LEU A 121 ? 0.6692 0.6294 0.3998 -0.0448 0.1369  -0.0541 121 LEU A CB  
1003 C CG  . LEU A 121 ? 0.6711 0.6171 0.3848 -0.0458 0.1237  -0.0592 121 LEU A CG  
1004 C CD1 . LEU A 121 ? 0.7208 0.6567 0.3957 -0.0551 0.1321  -0.0732 121 LEU A CD1 
1005 C CD2 . LEU A 121 ? 0.6538 0.5997 0.3589 -0.0484 0.1032  -0.0418 121 LEU A CD2 
1006 N N   . PHE A 122 ? 0.7134 0.6763 0.5322 -0.0209 0.1540  -0.0819 122 PHE A N   
1007 C CA  . PHE A 122 ? 0.7309 0.6861 0.5823 -0.0099 0.1517  -0.0933 122 PHE A CA  
1008 C C   . PHE A 122 ? 0.7357 0.6946 0.6090 -0.0070 0.1760  -0.1134 122 PHE A C   
1009 O O   . PHE A 122 ? 0.7424 0.6908 0.6321 -0.0007 0.1781  -0.1278 122 PHE A O   
1010 C CB  . PHE A 122 ? 0.7153 0.6744 0.6040 0.0012  0.1348  -0.0824 122 PHE A CB  
1011 C CG  . PHE A 122 ? 0.7462 0.6959 0.6196 0.0028  0.1126  -0.0682 122 PHE A CG  
1012 C CD1 . PHE A 122 ? 0.7735 0.7254 0.6161 -0.0050 0.1052  -0.0555 122 PHE A CD1 
1013 C CD2 . PHE A 122 ? 0.7932 0.7318 0.6850 0.0123  0.1000  -0.0667 122 PHE A CD2 
1014 C CE1 . PHE A 122 ? 0.7838 0.7288 0.6165 -0.0030 0.0885  -0.0435 122 PHE A CE1 
1015 C CE2 . PHE A 122 ? 0.7778 0.7081 0.6543 0.0133  0.0835  -0.0528 122 PHE A CE2 
1016 C CZ  . PHE A 122 ? 0.7743 0.7089 0.6223 0.0058  0.0792  -0.0421 122 PHE A CZ  
1017 N N   . GLU A 123 ? 0.7492 0.7231 0.6270 -0.0115 0.1951  -0.1139 123 GLU A N   
1018 C CA  . GLU A 123 ? 0.7948 0.7755 0.6967 -0.0090 0.2229  -0.1327 123 GLU A CA  
1019 C C   . GLU A 123 ? 0.8142 0.7830 0.6692 -0.0168 0.2405  -0.1502 123 GLU A C   
1020 O O   . GLU A 123 ? 0.8153 0.7759 0.6842 -0.0109 0.2515  -0.1714 123 GLU A O   
1021 C CB  . GLU A 123 ? 0.8206 0.8220 0.7434 -0.0127 0.2386  -0.1246 123 GLU A CB  
1022 C CG  . GLU A 123 ? 0.8620 0.8748 0.8128 -0.0115 0.2726  -0.1421 123 GLU A CG  
1023 C CD  . GLU A 123 ? 0.9243 0.9376 0.9350 0.0031  0.2749  -0.1591 123 GLU A CD  
1024 O OE1 . GLU A 123 ? 0.9180 0.9183 0.9396 0.0117  0.2493  -0.1577 123 GLU A OE1 
1025 O OE2 . GLU A 123 ? 1.0034 1.0300 1.0521 0.0060  0.3031  -0.1731 123 GLU A OE2 
1026 N N   . LYS A 124 ? 0.8293 0.7961 0.6286 -0.0299 0.2420  -0.1418 124 LYS A N   
1027 C CA  . LYS A 124 ? 0.8740 0.8301 0.6207 -0.0388 0.2585  -0.1575 124 LYS A CA  
1028 C C   . LYS A 124 ? 0.8772 0.8125 0.5910 -0.0414 0.2362  -0.1621 124 LYS A C   
1029 O O   . LYS A 124 ? 0.9167 0.8384 0.5988 -0.0450 0.2455  -0.1826 124 LYS A O   
1030 C CB  . LYS A 124 ? 0.9198 0.8834 0.6229 -0.0521 0.2695  -0.1433 124 LYS A CB  
1031 C CG  . LYS A 124 ? 0.9588 0.9422 0.6948 -0.0517 0.2972  -0.1408 124 LYS A CG  
1032 C CD  . LYS A 124 ? 1.0177 1.0096 0.7279 -0.0634 0.2994  -0.1171 124 LYS A CD  
1033 C CE  . LYS A 124 ? 1.0469 1.0603 0.8126 -0.0612 0.3164  -0.1087 124 LYS A CE  
1034 N NZ  . LYS A 124 ? 1.0609 1.0803 0.8202 -0.0694 0.3040  -0.0811 124 LYS A NZ  
1035 N N   . GLY A 125 ? 0.8366 0.7697 0.5575 -0.0401 0.2077  -0.1437 125 GLY A N   
1036 C CA  . GLY A 125 ? 0.8345 0.7502 0.5360 -0.0424 0.1866  -0.1461 125 GLY A CA  
1037 C C   . GLY A 125 ? 0.8495 0.7604 0.4966 -0.0558 0.1738  -0.1357 125 GLY A C   
1038 O O   . GLY A 125 ? 0.8364 0.7371 0.4758 -0.0584 0.1522  -0.1313 125 GLY A O   
1039 N N   . ALA A 126 ? 0.8860 0.8037 0.4979 -0.0646 0.1868  -0.1309 126 ALA A N   
1040 C CA  . ALA A 126 ? 0.8972 0.8114 0.4609 -0.0768 0.1719  -0.1164 126 ALA A CA  
1041 C C   . ALA A 126 ? 0.9211 0.8471 0.4652 -0.0835 0.1872  -0.1026 126 ALA A C   
1042 O O   . ALA A 126 ? 0.9349 0.8653 0.4745 -0.0838 0.2153  -0.1137 126 ALA A O   
1043 C CB  . ALA A 126 ? 0.9281 0.8239 0.4444 -0.0848 0.1672  -0.1341 126 ALA A CB  
1044 N N   . VAL A 127 ? 0.9131 0.8444 0.4501 -0.0885 0.1700  -0.0780 127 VAL A N   
1045 C CA  . VAL A 127 ? 0.9448 0.8866 0.4726 -0.0944 0.1829  -0.0615 127 VAL A CA  
1046 C C   . VAL A 127 ? 0.9940 0.9305 0.4804 -0.1055 0.1631  -0.0409 127 VAL A C   
1047 O O   . VAL A 127 ? 0.9474 0.8801 0.4388 -0.1048 0.1363  -0.0329 127 VAL A O   
1048 C CB  . VAL A 127 ? 0.8883 0.8463 0.4751 -0.0857 0.1852  -0.0501 127 VAL A CB  
1049 C CG1 . VAL A 127 ? 0.8844 0.8490 0.5151 -0.0751 0.2043  -0.0683 127 VAL A CG1 
1050 C CG2 . VAL A 127 ? 0.8385 0.7972 0.4509 -0.0801 0.1569  -0.0369 127 VAL A CG2 
1051 N N   . PRO A 128 ? 1.1157 1.0517 0.5616 -0.1161 0.1760  -0.0306 128 PRO A N   
1052 C CA  . PRO A 128 ? 1.1898 1.1288 0.6208 -0.1187 0.2115  -0.0425 128 PRO A CA  
1053 C C   . PRO A 128 ? 1.2843 1.2082 0.6654 -0.1221 0.2214  -0.0683 128 PRO A C   
1054 O O   . PRO A 128 ? 1.2620 1.1729 0.6259 -0.1222 0.1989  -0.0779 128 PRO A O   
1055 C CB  . PRO A 128 ? 1.2072 1.1495 0.6114 -0.1299 0.2181  -0.0168 128 PRO A CB  
1056 C CG  . PRO A 128 ? 1.2115 1.1431 0.5842 -0.1364 0.1833  0.0012  128 PRO A CG  
1057 C CD  . PRO A 128 ? 1.1481 1.0808 0.5637 -0.1260 0.1579  -0.0050 128 PRO A CD  
1058 N N   . GLU A 129 ? 1.4006 1.3258 0.7580 -0.1256 0.2561  -0.0797 129 GLU A N   
1059 C CA  . GLU A 129 ? 1.4999 1.4159 0.8397 -0.1224 0.2758  -0.1128 129 GLU A CA  
1060 C C   . GLU A 129 ? 1.5927 1.4860 0.8569 -0.1317 0.2591  -0.1230 129 GLU A C   
1061 O O   . GLU A 129 ? 1.6566 1.5374 0.9180 -0.1275 0.2529  -0.1488 129 GLU A O   
1062 C CB  . GLU A 129 ? 1.5526 1.4782 0.8906 -0.1233 0.3212  -0.1222 129 GLU A CB  
1063 C CG  . GLU A 129 ? 1.5333 1.4811 0.9237 -0.1222 0.3366  -0.1000 129 GLU A CG  
1064 C CD  . GLU A 129 ? 1.4757 1.4356 0.9376 -0.1131 0.3115  -0.0844 129 GLU A CD  
1065 O OE1 . GLU A 129 ? 1.4069 1.3737 0.8761 -0.1184 0.3012  -0.0569 129 GLU A OE1 
1066 O OE2 . GLU A 129 ? 1.4620 1.4232 0.9708 -0.1008 0.3021  -0.0994 129 GLU A OE2 
1067 N N   . ASP A 130 ? 1.6052 1.4921 0.8100 -0.1447 0.2500  -0.1023 130 ASP A N   
1068 C CA  . ASP A 130 ? 1.6520 1.5170 0.7829 -0.1546 0.2281  -0.1084 130 ASP A CA  
1069 C C   . ASP A 130 ? 1.6025 1.4639 0.7546 -0.1540 0.1824  -0.0955 130 ASP A C   
1070 O O   . ASP A 130 ? 1.6042 1.4511 0.7407 -0.1547 0.1615  -0.1132 130 ASP A O   
1071 C CB  . ASP A 130 ? 1.7487 1.6068 0.8034 -0.1688 0.2371  -0.0902 130 ASP A CB  
1072 C CG  . ASP A 130 ? 1.7186 1.5888 0.7940 -0.1729 0.2280  -0.0506 130 ASP A CG  
1073 O OD1 . ASP A 130 ? 1.5937 1.4786 0.7427 -0.1641 0.2159  -0.0398 130 ASP A OD1 
1074 O OD2 . ASP A 130 ? 1.7773 1.6409 0.7940 -0.1850 0.2331  -0.0309 130 ASP A OD2 
1075 N N   . LEU A 131 ? 1.5368 1.4117 0.7285 -0.1527 0.1686  -0.0656 131 LEU A N   
1076 C CA  . LEU A 131 ? 1.4484 1.3214 0.6535 -0.1541 0.1282  -0.0481 131 LEU A CA  
1077 C C   . LEU A 131 ? 1.3308 1.2066 0.5940 -0.1434 0.1138  -0.0614 131 LEU A C   
1078 O O   . LEU A 131 ? 1.3081 1.1752 0.5672 -0.1460 0.0843  -0.0629 131 LEU A O   
1079 C CB  . LEU A 131 ? 1.4014 1.2876 0.6343 -0.1547 0.1222  -0.0146 131 LEU A CB  
1080 C CG  . LEU A 131 ? 1.4388 1.3177 0.6137 -0.1678 0.1177  0.0095  131 LEU A CG  
1081 C CD1 . LEU A 131 ? 1.4086 1.3001 0.6252 -0.1667 0.1118  0.0404  131 LEU A CD1 
1082 C CD2 . LEU A 131 ? 1.4544 1.3159 0.5775 -0.1767 0.0826  0.0120  131 LEU A CD2 
1083 N N   . GLU A 132 ? 1.2589 1.1471 0.5781 -0.1319 0.1337  -0.0687 132 GLU A N   
1084 C CA  . GLU A 132 ? 1.1915 1.0826 0.5668 -0.1214 0.1215  -0.0762 132 GLU A CA  
1085 C C   . GLU A 132 ? 1.1227 1.0169 0.5173 -0.1224 0.0893  -0.0548 132 GLU A C   
1086 O O   . GLU A 132 ? 1.1198 1.0063 0.5209 -0.1229 0.0681  -0.0609 132 GLU A O   
1087 C CB  . GLU A 132 ? 1.2092 1.0844 0.5723 -0.1208 0.1195  -0.1051 132 GLU A CB  
1088 C CG  . GLU A 132 ? 1.2545 1.1248 0.5974 -0.1193 0.1519  -0.1303 132 GLU A CG  
1089 C CD  . GLU A 132 ? 1.2825 1.1366 0.6270 -0.1160 0.1503  -0.1610 132 GLU A CD  
1090 O OE1 . GLU A 132 ? 1.3104 1.1584 0.6371 -0.1144 0.1765  -0.1852 132 GLU A OE1 
1091 O OE2 . GLU A 132 ? 1.2920 1.1395 0.6591 -0.1151 0.1241  -0.1607 132 GLU A OE2 
1092 N N   . LEU A 133 ? 1.0379 0.9435 0.4451 -0.1229 0.0869  -0.0303 133 LEU A N   
1093 C CA  . LEU A 133 ? 0.9602 0.8713 0.3959 -0.1212 0.0609  -0.0108 133 LEU A CA  
1094 C C   . LEU A 133 ? 0.8732 0.7910 0.3653 -0.1092 0.0594  -0.0164 133 LEU A C   
1095 O O   . LEU A 133 ? 0.8330 0.7526 0.3474 -0.1075 0.0389  -0.0077 133 LEU A O   
1096 C CB  . LEU A 133 ? 0.9434 0.8640 0.3860 -0.1227 0.0626  0.0136  133 LEU A CB  
1097 C CG  . LEU A 133 ? 0.9608 0.8743 0.3478 -0.1352 0.0641  0.0259  133 LEU A CG  
1098 C CD1 . LEU A 133 ? 0.9294 0.8521 0.3366 -0.1356 0.0659  0.0510  133 LEU A CD1 
1099 C CD2 . LEU A 133 ? 0.9847 0.8855 0.3324 -0.1443 0.0350  0.0297  133 LEU A CD2 
1100 N N   . LEU A 134 ? 0.8550 0.7770 0.3700 -0.1009 0.0816  -0.0291 134 LEU A N   
1101 C CA  . LEU A 134 ? 0.7965 0.7213 0.3578 -0.0894 0.0818  -0.0360 134 LEU A CA  
1102 C C   . LEU A 134 ? 0.8317 0.7476 0.3916 -0.0864 0.0967  -0.0607 134 LEU A C   
1103 O O   . LEU A 134 ? 0.8695 0.7864 0.4170 -0.0868 0.1187  -0.0713 134 LEU A O   
1104 C CB  . LEU A 134 ? 0.7353 0.6737 0.3345 -0.0805 0.0908  -0.0261 134 LEU A CB  
1105 C CG  . LEU A 134 ? 0.7241 0.6707 0.3297 -0.0822 0.0795  -0.0039 134 LEU A CG  
1106 C CD1 . LEU A 134 ? 0.6960 0.6538 0.3380 -0.0738 0.0890  0.0011  134 LEU A CD1 
1107 C CD2 . LEU A 134 ? 0.7004 0.6461 0.3176 -0.0810 0.0568  0.0054  134 LEU A CD2 
1108 N N   . ARG A 135 ? 0.8244 0.7323 0.4035 -0.0826 0.0860  -0.0687 135 ARG A N   
1109 C CA  . ARG A 135 ? 0.8490 0.7449 0.4315 -0.0797 0.0951  -0.0922 135 ARG A CA  
1110 C C   . ARG A 135 ? 0.8161 0.7109 0.4456 -0.0695 0.0886  -0.0903 135 ARG A C   
1111 O O   . ARG A 135 ? 0.8260 0.7230 0.4690 -0.0697 0.0720  -0.0755 135 ARG A O   
1112 C CB  . ARG A 135 ? 0.9195 0.8003 0.4614 -0.0907 0.0832  -0.1040 135 ARG A CB  
1113 C CG  . ARG A 135 ? 0.9728 0.8370 0.5174 -0.0890 0.0878  -0.1305 135 ARG A CG  
1114 C CD  . ARG A 135 ? 1.0363 0.8846 0.5387 -0.1010 0.0717  -0.1424 135 ARG A CD  
1115 N NE  . ARG A 135 ? 1.0154 0.8627 0.5314 -0.1061 0.0435  -0.1286 135 ARG A NE  
1116 C CZ  . ARG A 135 ? 0.9965 0.8322 0.5363 -0.1070 0.0297  -0.1373 135 ARG A CZ  
1117 N NH1 . ARG A 135 ? 0.9902 0.8144 0.5513 -0.1008 0.0407  -0.1565 135 ARG A NH1 
1118 N NH2 . ARG A 135 ? 0.9785 0.8146 0.5275 -0.1139 0.0049  -0.1253 135 ARG A NH2 
1119 N N   . MET A 136 ? 0.8264 0.7177 0.4814 -0.0606 0.1022  -0.1042 136 MET A N   
1120 C CA  . MET A 136 ? 0.8042 0.6939 0.5019 -0.0502 0.0966  -0.0988 136 MET A CA  
1121 C C   . MET A 136 ? 0.8055 0.6793 0.5197 -0.0460 0.1016  -0.1192 136 MET A C   
1122 O O   . MET A 136 ? 0.8533 0.7236 0.5609 -0.0451 0.1181  -0.1389 136 MET A O   
1123 C CB  . MET A 136 ? 0.8277 0.7314 0.5524 -0.0403 0.1054  -0.0902 136 MET A CB  
1124 C CG  . MET A 136 ? 0.8361 0.7369 0.5992 -0.0289 0.0982  -0.0835 136 MET A CG  
1125 S SD  . MET A 136 ? 0.8409 0.7576 0.6331 -0.0183 0.1037  -0.0750 136 MET A SD  
1126 C CE  . MET A 136 ? 0.8883 0.8044 0.6962 -0.0149 0.1256  -0.0989 136 MET A CE  
1127 N N   . GLU A 137 ? 0.7818 0.6455 0.5202 -0.0429 0.0890  -0.1141 137 GLU A N   
1128 C CA  . GLU A 137 ? 0.7837 0.6300 0.5444 -0.0384 0.0915  -0.1310 137 GLU A CA  
1129 C C   . GLU A 137 ? 0.7497 0.5895 0.5446 -0.0323 0.0794  -0.1150 137 GLU A C   
1130 O O   . GLU A 137 ? 0.6954 0.5429 0.4895 -0.0338 0.0694  -0.0937 137 GLU A O   
1131 C CB  . GLU A 137 ? 0.8252 0.6562 0.5593 -0.0489 0.0883  -0.1510 137 GLU A CB  
1132 C CG  . GLU A 137 ? 0.8464 0.6753 0.5657 -0.0599 0.0683  -0.1391 137 GLU A CG  
1133 C CD  . GLU A 137 ? 0.9183 0.7318 0.6089 -0.0713 0.0605  -0.1595 137 GLU A CD  
1134 O OE1 . GLU A 137 ? 0.9961 0.8087 0.6487 -0.0752 0.0704  -0.1758 137 GLU A OE1 
1135 O OE2 . GLU A 137 ? 0.9381 0.7399 0.6432 -0.0768 0.0444  -0.1589 137 GLU A OE2 
1136 N N   . LYS A 138 ? 0.7461 0.5711 0.5712 -0.0248 0.0821  -0.1256 138 LYS A N   
1137 C CA  . LYS A 138 ? 0.7322 0.5464 0.5887 -0.0190 0.0718  -0.1107 138 LYS A CA  
1138 C C   . LYS A 138 ? 0.7443 0.5501 0.5939 -0.0301 0.0589  -0.1025 138 LYS A C   
1139 O O   . LYS A 138 ? 0.7725 0.5679 0.6109 -0.0392 0.0563  -0.1195 138 LYS A O   
1140 C CB  . LYS A 138 ? 0.7617 0.5590 0.6520 -0.0100 0.0766  -0.1265 138 LYS A CB  
1141 C CG  . LYS A 138 ? 0.7744 0.5595 0.6997 -0.0014 0.0668  -0.1089 138 LYS A CG  
1142 C CD  . LYS A 138 ? 0.7678 0.5661 0.7017 0.0092  0.0646  -0.0895 138 LYS A CD  
1143 C CE  . LYS A 138 ? 0.7656 0.5504 0.7204 0.0156  0.0523  -0.0670 138 LYS A CE  
1144 N NZ  . LYS A 138 ? 0.7745 0.5712 0.7294 0.0252  0.0476  -0.0500 138 LYS A NZ  
1145 N N   . LYS A 139 ? 0.7141 0.5249 0.5705 -0.0295 0.0512  -0.0772 139 LYS A N   
1146 C CA  . LYS A 139 ? 0.7204 0.5277 0.5771 -0.0400 0.0411  -0.0669 139 LYS A CA  
1147 C C   . LYS A 139 ? 0.7098 0.5221 0.5777 -0.0363 0.0382  -0.0388 139 LYS A C   
1148 O O   . LYS A 139 ? 0.7139 0.5420 0.5691 -0.0314 0.0408  -0.0268 139 LYS A O   
1149 C CB  . LYS A 139 ? 0.7281 0.5481 0.5545 -0.0507 0.0375  -0.0716 139 LYS A CB  
1150 C CG  . LYS A 139 ? 0.7347 0.5537 0.5672 -0.0621 0.0251  -0.0624 139 LYS A CG  
1151 C CD  . LYS A 139 ? 0.7497 0.5669 0.5590 -0.0741 0.0163  -0.0794 139 LYS A CD  
1152 C CE  . LYS A 139 ? 0.7814 0.5763 0.5952 -0.0775 0.0142  -0.1044 139 LYS A CE  
1153 N NZ  . LYS A 139 ? 0.8138 0.6072 0.5877 -0.0827 0.0150  -0.1274 139 LYS A NZ  
1154 N N   . THR A 140 ? 0.7208 0.5189 0.6119 -0.0395 0.0336  -0.0286 140 THR A N   
1155 C CA  . THR A 140 ? 0.6907 0.4928 0.5885 -0.0388 0.0334  -0.0018 140 THR A CA  
1156 C C   . THR A 140 ? 0.6626 0.4808 0.5518 -0.0489 0.0308  0.0044  140 THR A C   
1157 O O   . THR A 140 ? 0.6576 0.4796 0.5375 -0.0573 0.0254  -0.0109 140 THR A O   
1158 C CB  . THR A 140 ? 0.7058 0.4870 0.6330 -0.0406 0.0312  0.0098  140 THR A CB  
1159 O OG1 . THR A 140 ? 0.7116 0.4855 0.6550 -0.0539 0.0250  0.0014  140 THR A OG1 
1160 C CG2 . THR A 140 ? 0.7123 0.4748 0.6550 -0.0306 0.0309  0.0042  140 THR A CG2 
1161 N N   . LEU A 141 ? 0.6483 0.4744 0.5414 -0.0479 0.0344  0.0272  141 LEU A N   
1162 C CA  . LEU A 141 ? 0.6378 0.4817 0.5291 -0.0548 0.0336  0.0352  141 LEU A CA  
1163 C C   . LEU A 141 ? 0.6792 0.5178 0.5977 -0.0682 0.0269  0.0352  141 LEU A C   
1164 O O   . LEU A 141 ? 0.7291 0.5789 0.6483 -0.0768 0.0191  0.0297  141 LEU A O   
1165 C CB  . LEU A 141 ? 0.6105 0.4635 0.4963 -0.0472 0.0429  0.0568  141 LEU A CB  
1166 C CG  . LEU A 141 ? 0.5904 0.4637 0.4779 -0.0513 0.0451  0.0656  141 LEU A CG  
1167 C CD1 . LEU A 141 ? 0.5758 0.4622 0.4486 -0.0541 0.0372  0.0515  141 LEU A CD1 
1168 C CD2 . LEU A 141 ? 0.5782 0.4584 0.4531 -0.0415 0.0564  0.0821  141 LEU A CD2 
1169 N N   . ASN A 142 ? 0.7103 0.5308 0.6537 -0.0705 0.0278  0.0412  142 ASN A N   
1170 C CA  . ASN A 142 ? 0.7321 0.5454 0.7075 -0.0840 0.0200  0.0395  142 ASN A CA  
1171 C C   . ASN A 142 ? 0.7521 0.5567 0.7216 -0.0909 0.0063  0.0114  142 ASN A C   
1172 O O   . ASN A 142 ? 0.7978 0.6055 0.7808 -0.1029 -0.0054 0.0051  142 ASN A O   
1173 C CB  . ASN A 142 ? 0.7542 0.5470 0.7602 -0.0855 0.0240  0.0528  142 ASN A CB  
1174 C CG  . ASN A 142 ? 0.7586 0.5595 0.7811 -0.0870 0.0361  0.0820  142 ASN A CG  
1175 O OD1 . ASN A 142 ? 0.7615 0.5791 0.8014 -0.0954 0.0368  0.0889  142 ASN A OD1 
1176 N ND2 . ASN A 142 ? 0.7734 0.5620 0.7917 -0.0789 0.0457  0.0998  142 ASN A ND2 
1177 N N   . GLU A 143 ? 0.7634 0.5560 0.7152 -0.0834 0.0078  -0.0058 143 GLU A N   
1178 C CA  . GLU A 143 ? 0.8071 0.5919 0.7430 -0.0882 -0.0010 -0.0348 143 GLU A CA  
1179 C C   . GLU A 143 ? 0.8018 0.6062 0.7086 -0.0932 -0.0070 -0.0392 143 GLU A C   
1180 O O   . GLU A 143 ? 0.8190 0.6199 0.7187 -0.1037 -0.0204 -0.0549 143 GLU A O   
1181 C CB  . GLU A 143 ? 0.8393 0.6122 0.7634 -0.0769 0.0071  -0.0499 143 GLU A CB  
1182 C CG  . GLU A 143 ? 0.9037 0.6516 0.8616 -0.0743 0.0073  -0.0507 143 GLU A CG  
1183 C CD  . GLU A 143 ? 0.9213 0.6581 0.8808 -0.0608 0.0153  -0.0600 143 GLU A CD  
1184 O OE1 . GLU A 143 ? 0.9360 0.6503 0.9268 -0.0584 0.0135  -0.0603 143 GLU A OE1 
1185 O OE2 . GLU A 143 ? 0.8423 0.5927 0.7768 -0.0525 0.0228  -0.0658 143 GLU A OE2 
1186 N N   . LEU A 144 ? 0.7582 0.5819 0.6490 -0.0860 0.0009  -0.0246 144 LEU A N   
1187 C CA  . LEU A 144 ? 0.7484 0.5899 0.6147 -0.0896 -0.0046 -0.0253 144 LEU A CA  
1188 C C   . LEU A 144 ? 0.7336 0.5849 0.6222 -0.1002 -0.0166 -0.0145 144 LEU A C   
1189 O O   . LEU A 144 ? 0.7400 0.5966 0.6152 -0.1084 -0.0306 -0.0223 144 LEU A O   
1190 C CB  . LEU A 144 ? 0.7201 0.5773 0.5706 -0.0783 0.0069  -0.0126 144 LEU A CB  
1191 C CG  . LEU A 144 ? 0.7267 0.6038 0.5660 -0.0813 0.0016  -0.0041 144 LEU A CG  
1192 C CD1 . LEU A 144 ? 0.7482 0.6249 0.5587 -0.0892 -0.0093 -0.0198 144 LEU A CD1 
1193 C CD2 . LEU A 144 ? 0.7101 0.5999 0.5388 -0.0700 0.0125  0.0072  144 LEU A CD2 
1194 N N   . ILE A 145 ? 0.6965 0.5513 0.6187 -0.0994 -0.0101 0.0050  145 ILE A N   
1195 C CA  . ILE A 145 ? 0.6868 0.5528 0.6417 -0.1088 -0.0177 0.0170  145 ILE A CA  
1196 C C   . ILE A 145 ? 0.7095 0.5624 0.6836 -0.1224 -0.0360 0.0024  145 ILE A C   
1197 O O   . ILE A 145 ? 0.6998 0.5623 0.6912 -0.1322 -0.0513 0.0033  145 ILE A O   
1198 C CB  . ILE A 145 ? 0.6590 0.5293 0.6444 -0.1051 -0.0019 0.0404  145 ILE A CB  
1199 C CG1 . ILE A 145 ? 0.6478 0.5326 0.6116 -0.0925 0.0129  0.0531  145 ILE A CG1 
1200 C CG2 . ILE A 145 ? 0.6527 0.5328 0.6834 -0.1164 -0.0076 0.0510  145 ILE A CG2 
1201 C CD1 . ILE A 145 ? 0.6575 0.5373 0.6295 -0.0853 0.0305  0.0715  145 ILE A CD1 
1202 N N   . GLU A 146 ? 0.7381 0.5682 0.7121 -0.1225 -0.0357 -0.0115 146 GLU A N   
1203 C CA  . GLU A 146 ? 0.8030 0.6164 0.7918 -0.1347 -0.0538 -0.0299 146 GLU A CA  
1204 C C   . GLU A 146 ? 0.8042 0.6204 0.7551 -0.1403 -0.0711 -0.0492 146 GLU A C   
1205 O O   . GLU A 146 ? 0.8231 0.6408 0.7877 -0.1522 -0.0919 -0.0539 146 GLU A O   
1206 C CB  . GLU A 146 ? 0.8632 0.6501 0.8546 -0.1312 -0.0486 -0.0443 146 GLU A CB  
1207 C CG  . GLU A 146 ? 0.9257 0.6924 0.9446 -0.1439 -0.0664 -0.0612 146 GLU A CG  
1208 C CD  . GLU A 146 ? 0.9773 0.7154 1.0023 -0.1403 -0.0627 -0.0788 146 GLU A CD  
1209 O OE1 . GLU A 146 ? 0.9968 0.7314 1.0054 -0.1269 -0.0462 -0.0775 146 GLU A OE1 
1210 O OE2 . GLU A 146 ? 0.9991 0.7181 1.0488 -0.1507 -0.0779 -0.0946 146 GLU A OE2 
1211 N N   . GLU A 147 ? 0.8042 0.6208 0.7080 -0.1319 -0.0627 -0.0593 147 GLU A N   
1212 C CA  . GLU A 147 ? 0.8267 0.6435 0.6856 -0.1367 -0.0754 -0.0763 147 GLU A CA  
1213 C C   . GLU A 147 ? 0.7957 0.6318 0.6587 -0.1434 -0.0912 -0.0622 147 GLU A C   
1214 O O   . GLU A 147 ? 0.8349 0.6668 0.6841 -0.1540 -0.1139 -0.0735 147 GLU A O   
1215 C CB  . GLU A 147 ? 0.8556 0.6758 0.6707 -0.1260 -0.0585 -0.0812 147 GLU A CB  
1216 C CG  . GLU A 147 ? 0.8958 0.6968 0.7022 -0.1198 -0.0457 -0.1012 147 GLU A CG  
1217 C CD  . GLU A 147 ? 0.9304 0.7361 0.6951 -0.1115 -0.0302 -0.1094 147 GLU A CD  
1218 O OE1 . GLU A 147 ? 0.9613 0.7838 0.7019 -0.1114 -0.0304 -0.0984 147 GLU A OE1 
1219 O OE2 . GLU A 147 ? 0.9694 0.7620 0.7302 -0.1052 -0.0179 -0.1264 147 GLU A OE2 
1220 N N   . ILE A 148 ? 0.7403 0.5968 0.6217 -0.1366 -0.0800 -0.0384 148 ILE A N   
1221 C CA  . ILE A 148 ? 0.7092 0.5852 0.6031 -0.1410 -0.0931 -0.0240 148 ILE A CA  
1222 C C   . ILE A 148 ? 0.7096 0.5854 0.6494 -0.1537 -0.1136 -0.0231 148 ILE A C   
1223 O O   . ILE A 148 ? 0.7113 0.5943 0.6517 -0.1617 -0.1366 -0.0231 148 ILE A O   
1224 C CB  . ILE A 148 ? 0.6637 0.5595 0.5747 -0.1304 -0.0745 -0.0012 148 ILE A CB  
1225 C CG1 . ILE A 148 ? 0.6546 0.5526 0.5225 -0.1194 -0.0598 -0.0025 148 ILE A CG1 
1226 C CG2 . ILE A 148 ? 0.6538 0.5697 0.5945 -0.1348 -0.0871 0.0133  148 ILE A CG2 
1227 C CD1 . ILE A 148 ? 0.6233 0.5345 0.5038 -0.1075 -0.0401 0.0152  148 ILE A CD1 
1228 N N   . ASN A 149 ? 0.7048 0.5722 0.6857 -0.1556 -0.1060 -0.0205 149 ASN A N   
1229 C CA  . ASN A 149 ? 0.7030 0.5714 0.7394 -0.1679 -0.1217 -0.0169 149 ASN A CA  
1230 C C   . ASN A 149 ? 0.6847 0.5803 0.7555 -0.1693 -0.1264 0.0032  149 ASN A C   
1231 O O   . ASN A 149 ? 0.6948 0.5964 0.7780 -0.1787 -0.1530 -0.0002 149 ASN A O   
1232 C CB  . ASN A 149 ? 0.7433 0.5926 0.7666 -0.1801 -0.1502 -0.0419 149 ASN A CB  
1233 C CG  . ASN A 149 ? 0.7595 0.6071 0.8460 -0.1937 -0.1682 -0.0404 149 ASN A CG  
1234 O OD1 . ASN A 149 ? 0.7456 0.6088 0.8878 -0.1944 -0.1576 -0.0189 149 ASN A OD1 
1235 N ND2 . ASN A 149 ? 0.8043 0.6330 0.8835 -0.2049 -0.1950 -0.0637 149 ASN A ND2 
1236 N N   . PRO A 150 ? 0.6702 0.5824 0.7568 -0.1592 -0.1016 0.0238  150 PRO A N   
1237 C CA  . PRO A 150 ? 0.6584 0.5968 0.7779 -0.1581 -0.1017 0.0411  150 PRO A CA  
1238 C C   . PRO A 150 ? 0.6720 0.6202 0.8642 -0.1662 -0.0995 0.0539  150 PRO A C   
1239 O O   . PRO A 150 ? 0.7030 0.6376 0.9157 -0.1702 -0.0903 0.0543  150 PRO A O   
1240 C CB  . PRO A 150 ? 0.6367 0.5837 0.7340 -0.1428 -0.0726 0.0533  150 PRO A CB  
1241 C CG  . PRO A 150 ? 0.6449 0.5737 0.7345 -0.1392 -0.0538 0.0524  150 PRO A CG  
1242 C CD  . PRO A 150 ? 0.6731 0.5788 0.7461 -0.1478 -0.0726 0.0308  150 PRO A CD  
1243 N N   . ASP A 151 ? 0.6509 0.6228 0.8850 -0.1685 -0.1070 0.0651  151 ASP A N   
1244 C CA  . ASP A 151 ? 0.6429 0.6288 0.9543 -0.1768 -0.1040 0.0780  151 ASP A CA  
1245 C C   . ASP A 151 ? 0.6156 0.6185 0.9486 -0.1664 -0.0664 0.0986  151 ASP A C   
1246 O O   . ASP A 151 ? 0.6376 0.6531 1.0336 -0.1719 -0.0543 0.1122  151 ASP A O   
1247 C CB  . ASP A 151 ? 0.6500 0.6511 1.0039 -0.1865 -0.1367 0.0764  151 ASP A CB  
1248 C CG  . ASP A 151 ? 0.6375 0.6574 0.9789 -0.1781 -0.1430 0.0819  151 ASP A CG  
1249 O OD1 . ASP A 151 ? 0.6311 0.6523 0.9301 -0.1648 -0.1209 0.0858  151 ASP A OD1 
1250 O OD2 . ASP A 151 ? 0.6406 0.6726 1.0173 -0.1850 -0.1719 0.0824  151 ASP A OD2 
1251 N N   . VAL A 152 ? 0.5739 0.5765 0.8551 -0.1519 -0.0472 0.1007  152 VAL A N   
1252 C CA  . VAL A 152 ? 0.5454 0.5581 0.8335 -0.1417 -0.0115 0.1173  152 VAL A CA  
1253 C C   . VAL A 152 ? 0.5316 0.5335 0.7507 -0.1277 0.0013  0.1131  152 VAL A C   
1254 O O   . VAL A 152 ? 0.5364 0.5346 0.7150 -0.1243 -0.0146 0.1014  152 VAL A O   
1255 C CB  . VAL A 152 ? 0.5302 0.5724 0.8649 -0.1381 -0.0025 0.1290  152 VAL A CB  
1256 C CG1 . VAL A 152 ? 0.5180 0.5695 0.8265 -0.1305 -0.0181 0.1222  152 VAL A CG1 
1257 C CG2 . VAL A 152 ? 0.5165 0.5672 0.8580 -0.1288 0.0374  0.1449  152 VAL A CG2 
1258 N N   . VAL A 153 ? 0.5281 0.5256 0.7359 -0.1201 0.0300  0.1243  153 VAL A N   
1259 C CA  . VAL A 153 ? 0.5262 0.5134 0.6741 -0.1067 0.0415  0.1215  153 VAL A CA  
1260 C C   . VAL A 153 ? 0.5221 0.5234 0.6697 -0.0956 0.0691  0.1349  153 VAL A C   
1261 O O   . VAL A 153 ? 0.5299 0.5365 0.7079 -0.0975 0.0898  0.1495  153 VAL A O   
1262 C CB  . VAL A 153 ? 0.5332 0.4945 0.6559 -0.1073 0.0442  0.1187  153 VAL A CB  
1263 C CG1 . VAL A 153 ? 0.5337 0.4863 0.6047 -0.0930 0.0585  0.1198  153 VAL A CG1 
1264 C CG2 . VAL A 153 ? 0.5356 0.4819 0.6484 -0.1158 0.0179  0.0998  153 VAL A CG2 
1265 N N   . PHE A 154 ? 0.5135 0.5209 0.6276 -0.0844 0.0696  0.1294  154 PHE A N   
1266 C CA  . PHE A 154 ? 0.5240 0.5421 0.6313 -0.0727 0.0942  0.1378  154 PHE A CA  
1267 C C   . PHE A 154 ? 0.5393 0.5422 0.5866 -0.0611 0.0999  0.1336  154 PHE A C   
1268 O O   . PHE A 154 ? 0.5487 0.5435 0.5662 -0.0595 0.0828  0.1215  154 PHE A O   
1269 C CB  . PHE A 154 ? 0.5086 0.5483 0.6393 -0.0690 0.0894  0.1349  154 PHE A CB  
1270 C CG  . PHE A 154 ? 0.5025 0.5612 0.7012 -0.0780 0.0876  0.1416  154 PHE A CG  
1271 C CD1 . PHE A 154 ? 0.5169 0.5877 0.7525 -0.0776 0.1154  0.1545  154 PHE A CD1 
1272 C CD2 . PHE A 154 ? 0.4951 0.5599 0.7217 -0.0872 0.0580  0.1354  154 PHE A CD2 
1273 C CE1 . PHE A 154 ? 0.5204 0.6114 0.8278 -0.0861 0.1145  0.1606  154 PHE A CE1 
1274 C CE2 . PHE A 154 ? 0.4954 0.5787 0.7907 -0.0956 0.0531  0.1415  154 PHE A CE2 
1275 C CZ  . PHE A 154 ? 0.5019 0.5994 0.8417 -0.0950 0.0817  0.1539  154 PHE A CZ  
1276 N N   . ILE A 155 ? 0.5554 0.5545 0.5861 -0.0534 0.1240  0.1440  155 ILE A N   
1277 C CA  . ILE A 155 ? 0.5688 0.5527 0.5454 -0.0423 0.1279  0.1415  155 ILE A CA  
1278 C C   . ILE A 155 ? 0.5772 0.5714 0.5371 -0.0301 0.1445  0.1421  155 ILE A C   
1279 O O   . ILE A 155 ? 0.5930 0.5915 0.5576 -0.0273 0.1681  0.1532  155 ILE A O   
1280 C CB  . ILE A 155 ? 0.5926 0.5565 0.5554 -0.0441 0.1365  0.1529  155 ILE A CB  
1281 C CG1 . ILE A 155 ? 0.5983 0.5515 0.5844 -0.0564 0.1197  0.1494  155 ILE A CG1 
1282 C CG2 . ILE A 155 ? 0.6029 0.5510 0.5123 -0.0322 0.1367  0.1509  155 ILE A CG2 
1283 C CD1 . ILE A 155 ? 0.6245 0.5579 0.6113 -0.0600 0.1271  0.1624  155 ILE A CD1 
1284 N N   . MET A 156 ? 0.5774 0.5744 0.5170 -0.0229 0.1327  0.1294  156 MET A N   
1285 C CA  . MET A 156 ? 0.5888 0.5940 0.5147 -0.0110 0.1450  0.1260  156 MET A CA  
1286 C C   . MET A 156 ? 0.6596 0.6486 0.5363 -0.0015 0.1572  0.1296  156 MET A C   
1287 O O   . MET A 156 ? 0.6547 0.6285 0.4990 0.0013  0.1443  0.1251  156 MET A O   
1288 C CB  . MET A 156 ? 0.5369 0.5473 0.4586 -0.0073 0.1267  0.1125  156 MET A CB  
1289 C CG  . MET A 156 ? 0.5049 0.5264 0.4657 -0.0178 0.1087  0.1106  156 MET A CG  
1290 S SD  . MET A 156 ? 0.4959 0.5382 0.5216 -0.0249 0.1187  0.1201  156 MET A SD  
1291 C CE  . MET A 156 ? 0.5033 0.5580 0.5328 -0.0105 0.1435  0.1189  156 MET A CE  
1292 N N   . HIS A 157 ? 0.7335 0.7260 0.6066 0.0030  0.1825  0.1383  157 HIS A N   
1293 C CA  . HIS A 157 ? 0.8131 0.7887 0.6402 0.0093  0.1961  0.1472  157 HIS A CA  
1294 C C   . HIS A 157 ? 0.8576 0.8411 0.6726 0.0181  0.2230  0.1483  157 HIS A C   
1295 O O   . HIS A 157 ? 0.8307 0.8319 0.6869 0.0145  0.2408  0.1525  157 HIS A O   
1296 C CB  . HIS A 157 ? 0.8777 0.8439 0.7176 -0.0009 0.2030  0.1652  157 HIS A CB  
1297 C CG  . HIS A 157 ? 0.9556 0.8987 0.7472 0.0037  0.2069  0.1764  157 HIS A CG  
1298 N ND1 . HIS A 157 ? 1.0571 0.9926 0.8001 0.0146  0.2221  0.1797  157 HIS A ND1 
1299 C CD2 . HIS A 157 ? 0.9672 0.8915 0.7518 -0.0009 0.1958  0.1851  157 HIS A CD2 
1300 C CE1 . HIS A 157 ? 1.0880 1.0008 0.7946 0.0160  0.2183  0.1921  157 HIS A CE1 
1301 N NE2 . HIS A 157 ? 1.0316 0.9375 0.7656 0.0071  0.2024  0.1955  157 HIS A NE2 
1302 N N   . GLU A 158 ? 0.9337 0.9034 0.6927 0.0297  0.2260  0.1440  158 GLU A N   
1303 C CA  . GLU A 158 ? 1.0116 0.9859 0.7487 0.0400  0.2499  0.1397  158 GLU A CA  
1304 C C   . GLU A 158 ? 1.0398 1.0177 0.7834 0.0358  0.2835  0.1581  158 GLU A C   
1305 O O   . GLU A 158 ? 1.0652 1.0546 0.8120 0.0416  0.3099  0.1547  158 GLU A O   
1306 C CB  . GLU A 158 ? 1.1177 1.0719 0.7872 0.0518  0.2418  0.1319  158 GLU A CB  
1307 C CG  . GLU A 158 ? 1.2766 1.2313 0.9129 0.0633  0.2659  0.1244  158 GLU A CG  
1308 C CD  . GLU A 158 ? 1.4009 1.3355 0.9717 0.0752  0.2521  0.1125  158 GLU A CD  
1309 O OE1 . GLU A 158 ? 1.5035 1.4352 1.0389 0.0852  0.2703  0.1036  158 GLU A OE1 
1310 O OE2 . GLU A 158 ? 1.3207 1.2427 0.8778 0.0744  0.2233  0.1113  158 GLU A OE2 
1311 N N   . GLU A 159 ? 1.0114 0.9795 0.7602 0.0257  0.2836  0.1772  159 GLU A N   
1312 C CA  . GLU A 159 ? 1.0360 1.0025 0.7834 0.0209  0.3150  0.1986  159 GLU A CA  
1313 C C   . GLU A 159 ? 0.9710 0.9568 0.7951 0.0070  0.3236  0.2082  159 GLU A C   
1314 O O   . GLU A 159 ? 0.9941 0.9781 0.8318 -0.0012 0.3452  0.2291  159 GLU A O   
1315 C CB  . GLU A 159 ? 1.1183 1.0568 0.8180 0.0195  0.3076  0.2155  159 GLU A CB  
1316 C CG  . GLU A 159 ? 1.1838 1.1032 0.8141 0.0326  0.2911  0.2049  159 GLU A CG  
1317 C CD  . GLU A 159 ? 1.2641 1.1549 0.8467 0.0327  0.2823  0.2230  159 GLU A CD  
1318 O OE1 . GLU A 159 ? 1.2815 1.1595 0.8499 0.0360  0.2513  0.2152  159 GLU A OE1 
1319 O OE2 . GLU A 159 ? 1.2398 1.1213 0.8018 0.0295  0.3069  0.2459  159 GLU A OE2 
1320 N N   . GLY A 160 ? 0.8948 0.8985 0.7696 0.0040  0.3058  0.1937  160 GLY A N   
1321 C CA  . GLY A 160 ? 0.8663 0.8882 0.8160 -0.0092 0.3066  0.2003  160 GLY A CA  
1322 C C   . GLY A 160 ? 0.8565 0.9049 0.8526 -0.0073 0.3344  0.1993  160 GLY A C   
1323 O O   . GLY A 160 ? 0.8444 0.8962 0.8112 0.0051  0.3540  0.1914  160 GLY A O   
1324 N N   . GLU A 161 ? 0.8660 0.9325 0.9369 -0.0198 0.3347  0.2064  161 GLU A N   
1325 C CA  . GLU A 161 ? 0.8799 0.9758 1.0178 -0.0205 0.3554  0.2057  161 GLU A CA  
1326 C C   . GLU A 161 ? 0.8963 1.0044 1.0398 -0.0088 0.3430  0.1841  161 GLU A C   
1327 O O   . GLU A 161 ? 0.8936 0.9988 1.0412 -0.0105 0.3071  0.1734  161 GLU A O   
1328 C CB  . GLU A 161 ? 0.8544 0.9634 1.0713 -0.0372 0.3408  0.2137  161 GLU A CB  
1329 C CG  . GLU A 161 ? 0.8292 0.9706 1.1296 -0.0388 0.3490  0.2104  161 GLU A CG  
1330 C CD  . GLU A 161 ? 0.8589 1.0176 1.1989 -0.0409 0.3949  0.2252  161 GLU A CD  
1331 O OE1 . GLU A 161 ? 0.8530 1.0057 1.2072 -0.0532 0.4070  0.2443  161 GLU A OE1 
1332 O OE2 . GLU A 161 ? 0.8899 1.0675 1.2481 -0.0301 0.4197  0.2175  161 GLU A OE2 
1333 N N   . LEU A 162 ? 0.9140 1.0344 1.0575 0.0030  0.3730  0.1777  162 LEU A N   
1334 C CA  . LEU A 162 ? 0.8929 1.0190 1.0326 0.0158  0.3607  0.1565  162 LEU A CA  
1335 C C   . LEU A 162 ? 0.8375 0.9887 1.0630 0.0113  0.3448  0.1521  162 LEU A C   
1336 O O   . LEU A 162 ? 0.8192 0.9919 1.1121 0.0051  0.3629  0.1611  162 LEU A O   
1337 C CB  . LEU A 162 ? 0.9186 1.0473 1.0290 0.0311  0.3963  0.1472  162 LEU A CB  
1338 C CG  . LEU A 162 ? 0.9119 1.0423 1.0164 0.0450  0.3824  0.1238  162 LEU A CG  
1339 C CD1 . LEU A 162 ? 0.9323 1.0351 0.9534 0.0521  0.3621  0.1141  162 LEU A CD1 
1340 C CD2 . LEU A 162 ? 0.9270 1.0731 1.0516 0.0579  0.4192  0.1124  162 LEU A CD2 
1341 N N   . MET A 163 ? 0.8284 0.9766 1.0509 0.0150  0.3112  0.1387  163 MET A N   
1342 C CA  . MET A 163 ? 0.8180 0.9873 1.1147 0.0128  0.2927  0.1344  163 MET A CA  
1343 C C   . MET A 163 ? 0.8102 0.9784 1.0958 0.0265  0.2805  0.1169  163 MET A C   
1344 O O   . MET A 163 ? 0.7826 0.9306 1.0037 0.0329  0.2695  0.1080  163 MET A O   
1345 C CB  . MET A 163 ? 0.7772 0.9431 1.0943 -0.0026 0.2546  0.1410  163 MET A CB  
1346 C CG  . MET A 163 ? 0.7537 0.9278 1.1149 -0.0169 0.2641  0.1568  163 MET A CG  
1347 S SD  . MET A 163 ? 0.7306 0.8994 1.1155 -0.0340 0.2166  0.1594  163 MET A SD  
1348 C CE  . MET A 163 ? 0.7288 0.9273 1.2072 -0.0348 0.2001  0.1568  163 MET A CE  
1349 N N   . ILE A 164 ? 0.8040 0.9946 1.1594 0.0313  0.2843  0.1124  164 ILE A N   
1350 C CA  . ILE A 164 ? 0.7686 0.9603 1.1393 0.0394  0.2598  0.1001  164 ILE A CA  
1351 C C   . ILE A 164 ? 0.7096 0.8909 1.0709 0.0278  0.2149  0.1052  164 ILE A C   
1352 O O   . ILE A 164 ? 0.6716 0.8596 1.0662 0.0140  0.1999  0.1165  164 ILE A O   
1353 C CB  . ILE A 164 ? 0.7957 1.0147 1.2568 0.0448  0.2686  0.0977  164 ILE A CB  
1354 C CG1 . ILE A 164 ? 0.8446 1.0766 1.3207 0.0551  0.3192  0.0929  164 ILE A CG1 
1355 C CG2 . ILE A 164 ? 0.7891 1.0061 1.2662 0.0533  0.2410  0.0870  164 ILE A CG2 
1356 C CD1 . ILE A 164 ? 0.8898 1.1020 1.2833 0.0681  0.3428  0.0796  164 ILE A CD1 
1357 N N   . PRO A 165 ? 0.6839 0.8478 0.9979 0.0328  0.1933  0.0964  165 PRO A N   
1358 C CA  . PRO A 165 ? 0.6487 0.8020 0.9478 0.0226  0.1538  0.1004  165 PRO A CA  
1359 C C   . PRO A 165 ? 0.6390 0.8082 1.0067 0.0143  0.1280  0.1079  165 PRO A C   
1360 O O   . PRO A 165 ? 0.6331 0.7984 0.9988 0.0007  0.1041  0.1154  165 PRO A O   
1361 C CB  . PRO A 165 ? 0.6520 0.7910 0.9124 0.0326  0.1423  0.0889  165 PRO A CB  
1362 C CG  . PRO A 165 ? 0.6752 0.8082 0.8995 0.0458  0.1750  0.0783  165 PRO A CG  
1363 C CD  . PRO A 165 ? 0.7018 0.8547 0.9741 0.0481  0.2067  0.0816  165 PRO A CD  
1364 N N   . LYS A 166 ? 0.6177 0.8037 1.0448 0.0234  0.1324  0.1045  166 LYS A N   
1365 C CA  . LYS A 166 ? 0.5660 0.7690 1.0673 0.0179  0.1075  0.1119  166 LYS A CA  
1366 C C   . LYS A 166 ? 0.5154 0.7271 1.0439 0.0025  0.1035  0.1229  166 LYS A C   
1367 O O   . LYS A 166 ? 0.4975 0.7067 1.0352 -0.0096 0.0685  0.1297  166 LYS A O   
1368 C CB  . LYS A 166 ? 0.5978 0.8212 1.1697 0.0313  0.1254  0.1063  166 LYS A CB  
1369 C CG  . LYS A 166 ? 0.5893 0.8298 1.2438 0.0283  0.0954  0.1138  166 LYS A CG  
1370 C CD  . LYS A 166 ? 0.5950 0.8537 1.3230 0.0436  0.1089  0.1069  166 LYS A CD  
1371 C CE  . LYS A 166 ? 0.5916 0.8720 1.4143 0.0382  0.0819  0.1176  166 LYS A CE  
1372 N NZ  . LYS A 166 ? 0.5739 0.8690 1.4719 0.0533  0.0846  0.1117  166 LYS A NZ  
1373 N N   . ASN A 167 ? 0.5035 0.7222 1.0362 0.0029  0.1400  0.1243  167 ASN A N   
1374 C CA  . ASN A 167 ? 0.4911 0.7224 1.0691 -0.0102 0.1445  0.1351  167 ASN A CA  
1375 C C   . ASN A 167 ? 0.4971 0.7085 1.0236 -0.0243 0.1249  0.1396  167 ASN A C   
1376 O O   . ASN A 167 ? 0.5160 0.7329 1.0804 -0.0381 0.1054  0.1467  167 ASN A O   
1377 C CB  . ASN A 167 ? 0.4925 0.7352 1.0854 -0.0059 0.1933  0.1374  167 ASN A CB  
1378 C CG  . ASN A 167 ? 0.4814 0.7488 1.1419 0.0065  0.2185  0.1326  167 ASN A CG  
1379 O OD1 . ASN A 167 ? 0.4520 0.7330 1.1723 0.0092  0.1961  0.1309  167 ASN A OD1 
1380 N ND2 . ASN A 167 ? 0.4978 0.7705 1.1493 0.0145  0.2656  0.1305  167 ASN A ND2 
1381 N N   . PHE A 168 ? 0.5025 0.6910 0.9468 -0.0203 0.1311  0.1344  168 PHE A N   
1382 C CA  . PHE A 168 ? 0.4912 0.6596 0.8862 -0.0317 0.1142  0.1366  168 PHE A CA  
1383 C C   . PHE A 168 ? 0.4878 0.6535 0.8940 -0.0416 0.0703  0.1365  168 PHE A C   
1384 O O   . PHE A 168 ? 0.4861 0.6491 0.9054 -0.0555 0.0532  0.1405  168 PHE A O   
1385 C CB  . PHE A 168 ? 0.4866 0.6328 0.7989 -0.0238 0.1242  0.1300  168 PHE A CB  
1386 C CG  . PHE A 168 ? 0.4859 0.6117 0.7506 -0.0334 0.1132  0.1315  168 PHE A CG  
1387 C CD1 . PHE A 168 ? 0.5031 0.6289 0.7900 -0.0451 0.1178  0.1399  168 PHE A CD1 
1388 C CD2 . PHE A 168 ? 0.4808 0.5871 0.6826 -0.0305 0.1002  0.1242  168 PHE A CD2 
1389 C CE1 . PHE A 168 ? 0.5045 0.6099 0.7511 -0.0530 0.1081  0.1398  168 PHE A CE1 
1390 C CE2 . PHE A 168 ? 0.4934 0.5816 0.6563 -0.0381 0.0922  0.1242  168 PHE A CE2 
1391 C CZ  . PHE A 168 ? 0.4950 0.5820 0.6796 -0.0489 0.0958  0.1314  168 PHE A CZ  
1392 N N   . GLY A 169 ? 0.4702 0.6361 0.8731 -0.0346 0.0523  0.1322  169 GLY A N   
1393 C CA  . GLY A 169 ? 0.4729 0.6362 0.8845 -0.0427 0.0110  0.1342  169 GLY A CA  
1394 C C   . GLY A 169 ? 0.4988 0.6785 0.9817 -0.0541 -0.0075 0.1414  169 GLY A C   
1395 O O   . GLY A 169 ? 0.5122 0.6834 0.9857 -0.0670 -0.0388 0.1426  169 GLY A O   
1396 N N   . LYS A 170 ? 0.5082 0.7116 1.0641 -0.0493 0.0118  0.1451  170 LYS A N   
1397 C CA  . LYS A 170 ? 0.5227 0.7447 1.1582 -0.0598 -0.0047 0.1520  170 LYS A CA  
1398 C C   . LYS A 170 ? 0.5407 0.7559 1.1696 -0.0741 -0.0016 0.1544  170 LYS A C   
1399 O O   . LYS A 170 ? 0.5469 0.7697 1.2257 -0.0869 -0.0257 0.1583  170 LYS A O   
1400 C CB  . LYS A 170 ? 0.5306 0.7813 1.2499 -0.0510 0.0231  0.1550  170 LYS A CB  
1401 C CG  . LYS A 170 ? 0.5346 0.7915 1.2636 -0.0339 0.0311  0.1501  170 LYS A CG  
1402 C CD  . LYS A 170 ? 0.5461 0.8334 1.3765 -0.0276 0.0432  0.1526  170 LYS A CD  
1403 C CE  . LYS A 170 ? 0.5508 0.8421 1.3999 -0.0116 0.0396  0.1473  170 LYS A CE  
1404 N NZ  . LYS A 170 ? 0.5418 0.8642 1.4995 -0.0051 0.0504  0.1490  170 LYS A NZ  
1405 N N   . LEU A 171 ? 0.5475 0.7481 1.1186 -0.0714 0.0275  0.1520  171 LEU A N   
1406 C CA  . LEU A 171 ? 0.5521 0.7440 1.1166 -0.0831 0.0361  0.1552  171 LEU A CA  
1407 C C   . LEU A 171 ? 0.5491 0.7171 1.0601 -0.0935 0.0015  0.1491  171 LEU A C   
1408 O O   . LEU A 171 ? 0.5349 0.7009 1.0726 -0.1076 -0.0198 0.1497  171 LEU A O   
1409 C CB  . LEU A 171 ? 0.5432 0.7278 1.0661 -0.0745 0.0798  0.1568  171 LEU A CB  
1410 C CG  . LEU A 171 ? 0.5342 0.7086 1.0515 -0.0849 0.0948  0.1634  171 LEU A CG  
1411 C CD1 . LEU A 171 ? 0.5462 0.7407 1.1526 -0.0968 0.0965  0.1727  171 LEU A CD1 
1412 C CD2 . LEU A 171 ? 0.5339 0.7007 1.0069 -0.0750 0.1363  0.1672  171 LEU A CD2 
1413 N N   . LEU A 172 ? 0.5512 0.7019 0.9896 -0.0861 -0.0035 0.1421  172 LEU A N   
1414 C CA  . LEU A 172 ? 0.5804 0.7088 0.9612 -0.0937 -0.0320 0.1347  172 LEU A CA  
1415 C C   . LEU A 172 ? 0.5952 0.7270 1.0054 -0.1047 -0.0742 0.1345  172 LEU A C   
1416 O O   . LEU A 172 ? 0.6042 0.7192 0.9825 -0.1156 -0.0982 0.1280  172 LEU A O   
1417 C CB  . LEU A 172 ? 0.5866 0.7029 0.9021 -0.0826 -0.0294 0.1293  172 LEU A CB  
1418 C CG  . LEU A 172 ? 0.5974 0.7023 0.8639 -0.0735 0.0024  0.1266  172 LEU A CG  
1419 C CD1 . LEU A 172 ? 0.5883 0.6866 0.8090 -0.0618 0.0039  0.1217  172 LEU A CD1 
1420 C CD2 . LEU A 172 ? 0.6140 0.6985 0.8409 -0.0818 0.0001  0.1221  172 LEU A CD2 
1421 N N   . ASP A 173 ? 0.5902 0.7422 1.0585 -0.1014 -0.0848 0.1406  173 ASP A N   
1422 C CA  . ASP A 173 ? 0.6119 0.7656 1.1035 -0.1110 -0.1293 0.1418  173 ASP A CA  
1423 C C   . ASP A 173 ? 0.6144 0.7733 1.1581 -0.1259 -0.1434 0.1421  173 ASP A C   
1424 O O   . ASP A 173 ? 0.6330 0.7848 1.1768 -0.1373 -0.1836 0.1393  173 ASP A O   
1425 C CB  . ASP A 173 ? 0.6019 0.7743 1.1444 -0.1029 -0.1414 0.1493  173 ASP A CB  
1426 C CG  . ASP A 173 ? 0.6044 0.7729 1.1535 -0.1123 -0.1923 0.1521  173 ASP A CG  
1427 O OD1 . ASP A 173 ? 0.6357 0.7818 1.1114 -0.1168 -0.2123 0.1479  173 ASP A OD1 
1428 O OD2 . ASP A 173 ? 0.5942 0.7817 1.2209 -0.1151 -0.2113 0.1586  173 ASP A OD2 
1429 N N   . LYS A 174 ? 0.6011 0.7702 1.1848 -0.1262 -0.1105 0.1456  174 LYS A N   
1430 C CA  . LYS A 174 ? 0.5858 0.7619 1.2315 -0.1405 -0.1194 0.1476  174 LYS A CA  
1431 C C   . LYS A 174 ? 0.5980 0.7469 1.1917 -0.1522 -0.1323 0.1379  174 LYS A C   
1432 O O   . LYS A 174 ? 0.6202 0.7699 1.2595 -0.1653 -0.1419 0.1376  174 LYS A O   
1433 C CB  . LYS A 174 ? 0.5567 0.7516 1.2610 -0.1376 -0.0758 0.1568  174 LYS A CB  
1434 C CG  . LYS A 174 ? 0.5294 0.7531 1.2938 -0.1254 -0.0535 0.1644  174 LYS A CG  
1435 C CD  . LYS A 174 ? 0.5238 0.7614 1.3256 -0.1225 -0.0036 0.1727  174 LYS A CD  
1436 C CE  . LYS A 174 ? 0.5168 0.7775 1.3532 -0.1067 0.0301  0.1763  174 LYS A CE  
1437 N NZ  . LYS A 174 ? 0.5146 0.8074 1.4621 -0.1093 0.0246  0.1823  174 LYS A NZ  
1438 N N   . PHE A 175 ? 0.5944 0.7198 1.0990 -0.1477 -0.1319 0.1294  175 PHE A N   
1439 C CA  . PHE A 175 ? 0.6093 0.7083 1.0647 -0.1575 -0.1444 0.1176  175 PHE A CA  
1440 C C   . PHE A 175 ? 0.6525 0.7342 1.0442 -0.1603 -0.1793 0.1070  175 PHE A C   
1441 O O   . PHE A 175 ? 0.6780 0.7653 1.0525 -0.1531 -0.1888 0.1109  175 PHE A O   
1442 C CB  . PHE A 175 ? 0.5780 0.6627 0.9867 -0.1506 -0.1078 0.1164  175 PHE A CB  
1443 C CG  . PHE A 175 ? 0.5486 0.6469 1.0053 -0.1474 -0.0702 0.1288  175 PHE A CG  
1444 C CD1 . PHE A 175 ? 0.5261 0.6421 0.9945 -0.1340 -0.0411 0.1381  175 PHE A CD1 
1445 C CD2 . PHE A 175 ? 0.5562 0.6481 1.0443 -0.1579 -0.0631 0.1311  175 PHE A CD2 
1446 C CE1 . PHE A 175 ? 0.5185 0.6456 1.0232 -0.1313 -0.0039 0.1496  175 PHE A CE1 
1447 C CE2 . PHE A 175 ? 0.5464 0.6496 1.0751 -0.1559 -0.0264 0.1453  175 PHE A CE2 
1448 C CZ  . PHE A 175 ? 0.5271 0.6481 1.0610 -0.1426 0.0040  0.1546  175 PHE A CZ  
1449 N N   . LYS A 176 ? 0.6811 0.7400 1.0371 -0.1708 -0.1968 0.0934  176 LYS A N   
1450 C CA  . LYS A 176 ? 0.7069 0.7473 1.0003 -0.1759 -0.2295 0.0817  176 LYS A CA  
1451 C C   . LYS A 176 ? 0.6917 0.7141 0.9022 -0.1674 -0.2091 0.0742  176 LYS A C   
1452 O O   . LYS A 176 ? 0.7084 0.7225 0.8644 -0.1658 -0.2235 0.0711  176 LYS A O   
1453 C CB  . LYS A 176 ? 0.7584 0.7818 1.0536 -0.1917 -0.2583 0.0670  176 LYS A CB  
1454 C CG  . LYS A 176 ? 0.7766 0.8152 1.1621 -0.2026 -0.2765 0.0719  176 LYS A CG  
1455 C CD  . LYS A 176 ? 0.8237 0.8423 1.2138 -0.2163 -0.2904 0.0562  176 LYS A CD  
1456 C CE  . LYS A 176 ? 0.8288 0.8627 1.3171 -0.2277 -0.3026 0.0620  176 LYS A CE  
1457 N NZ  . LYS A 176 ? 0.8511 0.8999 1.3793 -0.2336 -0.3443 0.0659  176 LYS A NZ  
1458 N N   . LYS A 177 ? 0.6709 0.6868 0.8742 -0.1626 -0.1767 0.0723  177 LYS A N   
1459 C CA  . LYS A 177 ? 0.6661 0.6641 0.7987 -0.1555 -0.1595 0.0634  177 LYS A CA  
1460 C C   . LYS A 177 ? 0.6281 0.6311 0.7677 -0.1440 -0.1204 0.0718  177 LYS A C   
1461 O O   . LYS A 177 ? 0.6306 0.6178 0.7451 -0.1424 -0.1049 0.0652  177 LYS A O   
1462 C CB  . LYS A 177 ? 0.6914 0.6643 0.7897 -0.1652 -0.1733 0.0443  177 LYS A CB  
1463 C CG  . LYS A 177 ? 0.7127 0.6677 0.7348 -0.1596 -0.1642 0.0321  177 LYS A CG  
1464 C CD  . LYS A 177 ? 0.7608 0.6909 0.7444 -0.1688 -0.1800 0.0098  177 LYS A CD  
1465 C CE  . LYS A 177 ? 0.7630 0.6792 0.6728 -0.1634 -0.1713 -0.0017 177 LYS A CE  
1466 N NZ  . LYS A 177 ? 0.7936 0.6849 0.6688 -0.1703 -0.1790 -0.0260 177 LYS A NZ  
1467 N N   . PRO A 178 ? 0.5980 0.6212 0.7666 -0.1347 -0.1038 0.0859  178 PRO A N   
1468 C CA  . PRO A 178 ? 0.5817 0.6083 0.7514 -0.1238 -0.0679 0.0935  178 PRO A CA  
1469 C C   . PRO A 178 ? 0.5743 0.5866 0.6789 -0.1140 -0.0541 0.0872  178 PRO A C   
1470 O O   . PRO A 178 ? 0.5581 0.5708 0.6290 -0.1089 -0.0608 0.0846  178 PRO A O   
1471 C CB  . PRO A 178 ? 0.5614 0.6121 0.7701 -0.1159 -0.0588 0.1056  178 PRO A CB  
1472 C CG  . PRO A 178 ? 0.5643 0.6178 0.7616 -0.1179 -0.0886 0.1029  178 PRO A CG  
1473 C CD  . PRO A 178 ? 0.5927 0.6345 0.7896 -0.1329 -0.1190 0.0941  178 PRO A CD  
1474 N N   . THR A 179 ? 0.5784 0.5786 0.6701 -0.1112 -0.0345 0.0865  179 THR A N   
1475 C CA  . THR A 179 ? 0.5876 0.5779 0.6290 -0.1002 -0.0196 0.0829  179 THR A CA  
1476 C C   . THR A 179 ? 0.5750 0.5761 0.6226 -0.0879 0.0061  0.0945  179 THR A C   
1477 O O   . THR A 179 ? 0.5842 0.5931 0.6675 -0.0882 0.0215  0.1052  179 THR A O   
1478 C CB  . THR A 179 ? 0.5983 0.5668 0.6169 -0.1026 -0.0166 0.0739  179 THR A CB  
1479 O OG1 . THR A 179 ? 0.6067 0.5650 0.6102 -0.1125 -0.0404 0.0594  179 THR A OG1 
1480 C CG2 . THR A 179 ? 0.5963 0.5559 0.5722 -0.0908 -0.0014 0.0714  179 THR A CG2 
1481 N N   . VAL A 180 ? 0.5464 0.5473 0.5576 -0.0776 0.0111  0.0917  180 VAL A N   
1482 C CA  . VAL A 180 ? 0.5258 0.5322 0.5307 -0.0650 0.0334  0.0985  180 VAL A CA  
1483 C C   . VAL A 180 ? 0.4993 0.4906 0.4564 -0.0572 0.0390  0.0921  180 VAL A C   
1484 O O   . VAL A 180 ? 0.4699 0.4555 0.4007 -0.0579 0.0268  0.0829  180 VAL A O   
1485 C CB  . VAL A 180 ? 0.5226 0.5459 0.5420 -0.0589 0.0325  0.1011  180 VAL A CB  
1486 C CG1 . VAL A 180 ? 0.5259 0.5522 0.5328 -0.0453 0.0553  0.1043  180 VAL A CG1 
1487 C CG2 . VAL A 180 ? 0.5288 0.5688 0.6036 -0.0658 0.0259  0.1076  180 VAL A CG2 
1488 N N   . ILE A 181 ? 0.4968 0.4823 0.4445 -0.0499 0.0577  0.0982  181 ILE A N   
1489 C CA  . ILE A 181 ? 0.5152 0.4857 0.4251 -0.0427 0.0613  0.0938  181 ILE A CA  
1490 C C   . ILE A 181 ? 0.5008 0.4750 0.3918 -0.0297 0.0743  0.0970  181 ILE A C   
1491 O O   . ILE A 181 ? 0.4977 0.4748 0.3949 -0.0257 0.0907  0.1066  181 ILE A O   
1492 C CB  . ILE A 181 ? 0.5526 0.5070 0.4640 -0.0461 0.0665  0.0982  181 ILE A CB  
1493 C CG1 . ILE A 181 ? 0.5678 0.5143 0.4933 -0.0582 0.0515  0.0899  181 ILE A CG1 
1494 C CG2 . ILE A 181 ? 0.5581 0.4982 0.4354 -0.0361 0.0709  0.0966  181 ILE A CG2 
1495 C CD1 . ILE A 181 ? 0.5987 0.5298 0.5393 -0.0631 0.0561  0.0957  181 ILE A CD1 
1496 N N   . VAL A 182 ? 0.5033 0.4759 0.3694 -0.0237 0.0672  0.0882  182 VAL A N   
1497 C CA  . VAL A 182 ? 0.5175 0.4913 0.3636 -0.0116 0.0743  0.0871  182 VAL A CA  
1498 C C   . VAL A 182 ? 0.5475 0.5066 0.3640 -0.0059 0.0718  0.0827  182 VAL A C   
1499 O O   . VAL A 182 ? 0.5673 0.5209 0.3792 -0.0099 0.0617  0.0754  182 VAL A O   
1500 C CB  . VAL A 182 ? 0.4983 0.4831 0.3494 -0.0098 0.0659  0.0811  182 VAL A CB  
1501 C CG1 . VAL A 182 ? 0.5045 0.4892 0.3383 0.0025  0.0719  0.0775  182 VAL A CG1 
1502 C CG2 . VAL A 182 ? 0.4914 0.4907 0.3779 -0.0157 0.0640  0.0856  182 VAL A CG2 
1503 N N   . GLY A 183 ? 0.5703 0.5229 0.3674 0.0035  0.0811  0.0872  183 GLY A N   
1504 C CA  . GLY A 183 ? 0.5865 0.5250 0.3587 0.0102  0.0763  0.0847  183 GLY A CA  
1505 C C   . GLY A 183 ? 0.5738 0.5153 0.3365 0.0153  0.0660  0.0730  183 GLY A C   
1506 O O   . GLY A 183 ? 0.5554 0.5054 0.3180 0.0192  0.0668  0.0696  183 GLY A O   
1507 N N   . GLY A 184 ? 0.5862 0.5208 0.3458 0.0149  0.0571  0.0667  184 GLY A N   
1508 C CA  . GLY A 184 ? 0.5751 0.5140 0.3332 0.0173  0.0487  0.0565  184 GLY A CA  
1509 C C   . GLY A 184 ? 0.5880 0.5194 0.3300 0.0283  0.0437  0.0539  184 GLY A C   
1510 O O   . GLY A 184 ? 0.5878 0.5188 0.3336 0.0301  0.0358  0.0462  184 GLY A O   
1511 N N   . PHE A 185 ? 0.6168 0.5422 0.3409 0.0352  0.0484  0.0605  185 PHE A N   
1512 C CA  . PHE A 185 ? 0.6450 0.5590 0.3481 0.0452  0.0408  0.0599  185 PHE A CA  
1513 C C   . PHE A 185 ? 0.6792 0.5933 0.3605 0.0530  0.0441  0.0586  185 PHE A C   
1514 O O   . PHE A 185 ? 0.6690 0.5889 0.3502 0.0512  0.0573  0.0630  185 PHE A O   
1515 C CB  . PHE A 185 ? 0.6676 0.5672 0.3629 0.0459  0.0416  0.0707  185 PHE A CB  
1516 C CG  . PHE A 185 ? 0.6760 0.5741 0.3695 0.0409  0.0564  0.0836  185 PHE A CG  
1517 C CD1 . PHE A 185 ? 0.7000 0.5944 0.3683 0.0460  0.0666  0.0920  185 PHE A CD1 
1518 C CD2 . PHE A 185 ? 0.6629 0.5633 0.3808 0.0307  0.0609  0.0865  185 PHE A CD2 
1519 C CE1 . PHE A 185 ? 0.6998 0.5945 0.3720 0.0407  0.0831  0.1050  185 PHE A CE1 
1520 C CE2 . PHE A 185 ? 0.6870 0.5867 0.4106 0.0251  0.0738  0.0988  185 PHE A CE2 
1521 C CZ  . PHE A 185 ? 0.6957 0.5935 0.3987 0.0299  0.0860  0.1089  185 PHE A CZ  
1522 N N   . PRO A 186 ? 0.7227 0.6301 0.3871 0.0620  0.0318  0.0514  186 PRO A N   
1523 C CA  . PRO A 186 ? 0.7537 0.6600 0.3966 0.0699  0.0328  0.0449  186 PRO A CA  
1524 C C   . PRO A 186 ? 0.7856 0.6841 0.3961 0.0741  0.0472  0.0541  186 PRO A C   
1525 O O   . PRO A 186 ? 0.7939 0.6977 0.3984 0.0766  0.0594  0.0502  186 PRO A O   
1526 C CB  . PRO A 186 ? 0.7591 0.6568 0.3917 0.0775  0.0124  0.0357  186 PRO A CB  
1527 C CG  . PRO A 186 ? 0.7435 0.6337 0.3821 0.0763  0.0040  0.0431  186 PRO A CG  
1528 C CD  . PRO A 186 ? 0.7097 0.6098 0.3776 0.0654  0.0155  0.0479  186 PRO A CD  
1529 N N   . HIS A 187 ? 0.8200 0.7054 0.4117 0.0748  0.0471  0.0668  187 HIS A N   
1530 C CA  . HIS A 187 ? 0.9052 0.7804 0.4603 0.0785  0.0613  0.0784  187 HIS A CA  
1531 C C   . HIS A 187 ? 0.9634 0.8262 0.5146 0.0749  0.0619  0.0966  187 HIS A C   
1532 O O   . HIS A 187 ? 0.9565 0.8172 0.5312 0.0716  0.0489  0.0970  187 HIS A O   
1533 C CB  . HIS A 187 ? 0.9231 0.7861 0.4328 0.0902  0.0527  0.0702  187 HIS A CB  
1534 C CG  . HIS A 187 ? 0.9483 0.7992 0.4489 0.0956  0.0250  0.0659  187 HIS A CG  
1535 N ND1 . HIS A 187 ? 0.9575 0.7955 0.4538 0.0954  0.0141  0.0792  187 HIS A ND1 
1536 C CD2 . HIS A 187 ? 0.9209 0.7710 0.4211 0.1015  0.0050  0.0495  187 HIS A CD2 
1537 C CE1 . HIS A 187 ? 0.9498 0.7809 0.4444 0.1016  -0.0116 0.0711  187 HIS A CE1 
1538 N NE2 . HIS A 187 ? 0.9359 0.7744 0.4331 0.1048  -0.0175 0.0529  187 HIS A NE2 
1539 N N   . GLY A 188 ? 0.9893 0.8433 0.5118 0.0755  0.0786  0.1118  188 GLY A N   
1540 C CA  . GLY A 188 ? 1.0117 0.8524 0.5319 0.0711  0.0820  0.1323  188 GLY A CA  
1541 C C   . GLY A 188 ? 0.9703 0.8228 0.5311 0.0591  0.1000  0.1403  188 GLY A C   
1542 O O   . GLY A 188 ? 0.8774 0.7486 0.4652 0.0550  0.1085  0.1303  188 GLY A O   
1543 N N   . ASP A 189 ? 0.9851 0.8253 0.5521 0.0537  0.1032  0.1584  189 ASP A N   
1544 C CA  . ASP A 189 ? 0.9661 0.8144 0.5734 0.0416  0.1175  0.1667  189 ASP A CA  
1545 C C   . ASP A 189 ? 0.8989 0.7505 0.5466 0.0356  0.1014  0.1560  189 ASP A C   
1546 O O   . ASP A 189 ? 0.8722 0.7178 0.5160 0.0411  0.0826  0.1465  189 ASP A O   
1547 C CB  . ASP A 189 ? 1.0672 0.8990 0.6614 0.0381  0.1308  0.1922  189 ASP A CB  
1548 C CG  . ASP A 189 ? 1.1128 0.9546 0.7468 0.0255  0.1510  0.2027  189 ASP A CG  
1549 O OD1 . ASP A 189 ? 1.0449 0.9082 0.7128 0.0204  0.1562  0.1902  189 ASP A OD1 
1550 O OD2 . ASP A 189 ? 1.1805 1.0077 0.8140 0.0205  0.1601  0.2245  189 ASP A OD2 
1551 N N   . PHE A 190 ? 0.8910 0.7526 0.5780 0.0243  0.1091  0.1564  190 PHE A N   
1552 C CA  . PHE A 190 ? 0.8722 0.7332 0.5928 0.0174  0.0965  0.1474  190 PHE A CA  
1553 C C   . PHE A 190 ? 0.9006 0.7388 0.6186 0.0193  0.0869  0.1566  190 PHE A C   
1554 O O   . PHE A 190 ? 0.8993 0.7225 0.5972 0.0218  0.0928  0.1757  190 PHE A O   
1555 C CB  . PHE A 190 ? 0.8510 0.7225 0.6102 0.0044  0.1052  0.1490  190 PHE A CB  
1556 C CG  . PHE A 190 ? 0.8054 0.6993 0.5804 0.0012  0.1072  0.1369  190 PHE A CG  
1557 C CD1 . PHE A 190 ? 0.7543 0.6556 0.5413 -0.0015 0.0932  0.1198  190 PHE A CD1 
1558 C CD2 . PHE A 190 ? 0.8075 0.7146 0.5863 0.0008  0.1238  0.1434  190 PHE A CD2 
1559 C CE1 . PHE A 190 ? 0.7387 0.6584 0.5392 -0.0046 0.0929  0.1116  190 PHE A CE1 
1560 C CE2 . PHE A 190 ? 0.7984 0.7253 0.5970 -0.0015 0.1235  0.1333  190 PHE A CE2 
1561 C CZ  . PHE A 190 ? 0.7699 0.7022 0.5781 -0.0042 0.1065  0.1184  190 PHE A CZ  
1562 N N   . LYS A 191 ? 0.8798 0.7152 0.6187 0.0183  0.0728  0.1430  191 LYS A N   
1563 C CA  . LYS A 191 ? 0.9039 0.7187 0.6529 0.0197  0.0632  0.1485  191 LYS A CA  
1564 C C   . LYS A 191 ? 0.9292 0.7390 0.7137 0.0077  0.0678  0.1507  191 LYS A C   
1565 O O   . LYS A 191 ? 0.9827 0.7744 0.7738 0.0056  0.0699  0.1677  191 LYS A O   
1566 C CB  . LYS A 191 ? 0.8695 0.6840 0.6261 0.0261  0.0474  0.1305  191 LYS A CB  
1567 C CG  . LYS A 191 ? 0.8754 0.6968 0.6062 0.0368  0.0394  0.1242  191 LYS A CG  
1568 C CD  . LYS A 191 ? 0.8755 0.6887 0.6167 0.0450  0.0229  0.1161  191 LYS A CD  
1569 C CE  . LYS A 191 ? 0.8402 0.6576 0.6173 0.0399  0.0221  0.0988  191 LYS A CE  
1570 N NZ  . LYS A 191 ? 0.8549 0.6532 0.6539 0.0435  0.0137  0.1018  191 LYS A NZ  
1571 N N   . SER A 192 ? 0.9283 0.7524 0.7347 -0.0003 0.0676  0.1338  192 SER A N   
1572 C CA  . SER A 192 ? 0.9492 0.7700 0.7888 -0.0128 0.0695  0.1325  192 SER A CA  
1573 C C   . SER A 192 ? 1.0176 0.8446 0.8648 -0.0202 0.0842  0.1504  192 SER A C   
1574 O O   . SER A 192 ? 1.1255 0.9711 0.9642 -0.0200 0.0920  0.1500  192 SER A O   
1575 C CB  . SER A 192 ? 0.9137 0.7472 0.7668 -0.0190 0.0631  0.1096  192 SER A CB  
1576 O OG  . SER A 192 ? 0.9277 0.7528 0.7825 -0.0146 0.0534  0.0932  192 SER A OG  
1577 N N   . LYS A 193 ? 1.0418 0.8530 0.9086 -0.0265 0.0889  0.1664  193 LYS A N   
1578 C CA  . LYS A 193 ? 1.0688 0.8870 0.9547 -0.0361 0.1043  0.1826  193 LYS A CA  
1579 C C   . LYS A 193 ? 1.0282 0.8486 0.9589 -0.0499 0.0978  0.1721  193 LYS A C   
1580 O O   . LYS A 193 ? 1.0401 0.8417 0.9900 -0.0536 0.0880  0.1677  193 LYS A O   
1581 C CB  . LYS A 193 ? 1.1914 0.9907 1.0697 -0.0354 0.1155  0.2107  193 LYS A CB  
1582 C CG  . LYS A 193 ? 1.2561 1.0528 1.0838 -0.0229 0.1227  0.2233  193 LYS A CG  
1583 C CD  . LYS A 193 ? 1.2287 1.0497 1.0357 -0.0186 0.1334  0.2161  193 LYS A CD  
1584 C CE  . LYS A 193 ? 1.2536 1.0690 1.0097 -0.0080 0.1438  0.2303  193 LYS A CE  
1585 N NZ  . LYS A 193 ? 1.2263 1.0219 0.9502 0.0029  0.1258  0.2303  193 LYS A NZ  
1586 N N   . VAL A 194 ? 0.9673 0.8099 0.9147 -0.0566 0.1017  0.1670  194 VAL A N   
1587 C CA  . VAL A 194 ? 0.9640 0.8109 0.9526 -0.0703 0.0926  0.1567  194 VAL A CA  
1588 C C   . VAL A 194 ? 0.9723 0.8360 0.9924 -0.0786 0.1071  0.1721  194 VAL A C   
1589 O O   . VAL A 194 ? 0.9296 0.8038 0.9336 -0.0725 0.1249  0.1859  194 VAL A O   
1590 C CB  . VAL A 194 ? 0.9209 0.7794 0.9010 -0.0704 0.0766  0.1311  194 VAL A CB  
1591 C CG1 . VAL A 194 ? 0.8973 0.7409 0.8533 -0.0632 0.0653  0.1145  194 VAL A CG1 
1592 C CG2 . VAL A 194 ? 0.9087 0.7907 0.8711 -0.0644 0.0823  0.1306  194 VAL A CG2 
1593 N N   . ASP A 195 ? 1.0342 0.8997 1.1006 -0.0927 0.0991  0.1682  195 ASP A N   
1594 C CA  . ASP A 195 ? 1.0091 0.8941 1.1183 -0.1022 0.1092  0.1792  195 ASP A CA  
1595 C C   . ASP A 195 ? 0.9394 0.8504 1.0413 -0.0980 0.1062  0.1683  195 ASP A C   
1596 O O   . ASP A 195 ? 0.9820 0.8936 1.0600 -0.0943 0.0889  0.1490  195 ASP A O   
1597 C CB  . ASP A 195 ? 1.0266 0.9065 1.1908 -0.1186 0.0955  0.1747  195 ASP A CB  
1598 C CG  . ASP A 195 ? 1.0413 0.9064 1.2405 -0.1271 0.1087  0.1968  195 ASP A CG  
1599 O OD1 . ASP A 195 ? 1.0594 0.9179 1.2359 -0.1202 0.1299  0.2180  195 ASP A OD1 
1600 O OD2 . ASP A 195 ? 1.0462 0.9057 1.2945 -0.1411 0.0970  0.1933  195 ASP A OD2 
1601 N N   . GLY A 196 ? 0.8479 0.7795 0.9724 -0.0984 0.1247  0.1817  196 GLY A N   
1602 C CA  . GLY A 196 ? 0.7649 0.7210 0.8914 -0.0940 0.1233  0.1736  196 GLY A CA  
1603 C C   . GLY A 196 ? 0.7376 0.7112 0.8735 -0.0888 0.1525  0.1897  196 GLY A C   
1604 O O   . GLY A 196 ? 0.7394 0.7037 0.8571 -0.0850 0.1750  0.2062  196 GLY A O   
1605 N N   . VAL A 197 ? 0.6797 0.6777 0.8419 -0.0880 0.1514  0.1841  197 VAL A N   
1606 C CA  . VAL A 197 ? 0.6609 0.6792 0.8410 -0.0828 0.1790  0.1947  197 VAL A CA  
1607 C C   . VAL A 197 ? 0.6424 0.6602 0.7657 -0.0662 0.1868  0.1879  197 VAL A C   
1608 O O   . VAL A 197 ? 0.6048 0.6239 0.7085 -0.0613 0.1666  0.1723  197 VAL A O   
1609 C CB  . VAL A 197 ? 0.6476 0.6922 0.8924 -0.0895 0.1709  0.1907  197 VAL A CB  
1610 C CG1 . VAL A 197 ? 0.6550 0.7220 0.9324 -0.0853 0.2036  0.2022  197 VAL A CG1 
1611 C CG2 . VAL A 197 ? 0.6463 0.6889 0.9441 -0.1066 0.1513  0.1913  197 VAL A CG2 
1612 N N   . LYS A 198 ? 0.6900 0.7051 0.7866 -0.0584 0.2158  0.1998  198 LYS A N   
1613 C CA  . LYS A 198 ? 0.7236 0.7340 0.7617 -0.0428 0.2220  0.1927  198 LYS A CA  
1614 C C   . LYS A 198 ? 0.7070 0.7410 0.7648 -0.0354 0.2372  0.1871  198 LYS A C   
1615 O O   . LYS A 198 ? 0.7158 0.7641 0.8063 -0.0372 0.2641  0.1977  198 LYS A O   
1616 C CB  . LYS A 198 ? 0.7926 0.7821 0.7804 -0.0377 0.2398  0.2068  198 LYS A CB  
1617 C CG  . LYS A 198 ? 0.8373 0.8019 0.8052 -0.0420 0.2195  0.2087  198 LYS A CG  
1618 C CD  . LYS A 198 ? 0.9175 0.8587 0.8403 -0.0378 0.2311  0.2250  198 LYS A CD  
1619 C CE  . LYS A 198 ? 0.9427 0.8608 0.8492 -0.0390 0.2060  0.2212  198 LYS A CE  
1620 N NZ  . LYS A 198 ? 1.0119 0.9055 0.8894 -0.0379 0.2144  0.2417  198 LYS A NZ  
1621 N N   . ILE A 199 ? 0.6965 0.7345 0.7378 -0.0272 0.2203  0.1702  199 ILE A N   
1622 C CA  . ILE A 199 ? 0.6972 0.7567 0.7662 -0.0205 0.2272  0.1620  199 ILE A CA  
1623 C C   . ILE A 199 ? 0.7228 0.7745 0.7366 -0.0051 0.2308  0.1506  199 ILE A C   
1624 O O   . ILE A 199 ? 0.7120 0.7491 0.6868 -0.0021 0.2097  0.1422  199 ILE A O   
1625 C CB  . ILE A 199 ? 0.6545 0.7264 0.7678 -0.0272 0.1980  0.1532  199 ILE A CB  
1626 C CG1 . ILE A 199 ? 0.6525 0.7269 0.8124 -0.0435 0.1859  0.1612  199 ILE A CG1 
1627 C CG2 . ILE A 199 ? 0.6386 0.7332 0.7918 -0.0204 0.2050  0.1474  199 ILE A CG2 
1628 C CD1 . ILE A 199 ? 0.6621 0.7555 0.8840 -0.0494 0.2088  0.1735  199 ILE A CD1 
1629 N N   . SER A 200 ? 0.7690 0.8306 0.7826 0.0043  0.2584  0.1496  200 SER A N   
1630 C CA  . SER A 200 ? 0.8102 0.8674 0.7833 0.0192  0.2607  0.1349  200 SER A CA  
1631 C C   . SER A 200 ? 0.8259 0.9044 0.8489 0.0237  0.2593  0.1237  200 SER A C   
1632 O O   . SER A 200 ? 0.8522 0.9506 0.9303 0.0210  0.2772  0.1291  200 SER A O   
1633 C CB  . SER A 200 ? 0.8620 0.9103 0.7884 0.0277  0.2918  0.1394  200 SER A CB  
1634 O OG  . SER A 200 ? 0.8954 0.9350 0.7757 0.0419  0.2894  0.1228  200 SER A OG  
1635 N N   . LEU A 201 ? 0.7948 0.8691 0.8032 0.0305  0.2375  0.1092  201 LEU A N   
1636 C CA  . LEU A 201 ? 0.7897 0.8807 0.8454 0.0351  0.2312  0.0995  201 LEU A CA  
1637 C C   . LEU A 201 ? 0.8210 0.9127 0.8602 0.0510  0.2525  0.0858  201 LEU A C   
1638 O O   . LEU A 201 ? 0.8329 0.9388 0.9162 0.0571  0.2543  0.0774  201 LEU A O   
1639 C CB  . LEU A 201 ? 0.7647 0.8496 0.8178 0.0317  0.1944  0.0936  201 LEU A CB  
1640 C CG  . LEU A 201 ? 0.7596 0.8482 0.8426 0.0164  0.1713  0.1030  201 LEU A CG  
1641 C CD1 . LEU A 201 ? 0.7407 0.8260 0.8237 0.0143  0.1394  0.0972  201 LEU A CD1 
1642 C CD2 . LEU A 201 ? 0.7906 0.9008 0.9424 0.0101  0.1802  0.1115  201 LEU A CD2 
1643 N N   . TYR A 202 ? 0.8664 0.9409 0.8410 0.0581  0.2665  0.0828  202 TYR A N   
1644 C CA  . TYR A 202 ? 0.9230 0.9933 0.8682 0.0733  0.2859  0.0674  202 TYR A CA  
1645 C C   . TYR A 202 ? 1.0901 1.1457 0.9734 0.0756  0.3095  0.0745  202 TYR A C   
1646 O O   . TYR A 202 ? 1.1164 1.1657 0.9879 0.0654  0.3081  0.0917  202 TYR A O   
1647 C CB  . TYR A 202 ? 0.8419 0.8997 0.7635 0.0802  0.2583  0.0511  202 TYR A CB  
1648 C CG  . TYR A 202 ? 0.8403 0.8923 0.7400 0.0961  0.2699  0.0301  202 TYR A CG  
1649 C CD1 . TYR A 202 ? 0.8446 0.9128 0.7908 0.1041  0.2900  0.0206  202 TYR A CD1 
1650 C CD2 . TYR A 202 ? 0.8440 0.8742 0.6820 0.1034  0.2580  0.0179  202 TYR A CD2 
1651 C CE1 . TYR A 202 ? 0.8671 0.9282 0.7952 0.1191  0.2997  -0.0017 202 TYR A CE1 
1652 C CE2 . TYR A 202 ? 0.8592 0.8821 0.6779 0.1176  0.2652  -0.0039 202 TYR A CE2 
1653 C CZ  . TYR A 202 ? 0.8766 0.9142 0.7392 0.1256  0.2866  -0.0145 202 TYR A CZ  
1654 O OH  . TYR A 202 ? 0.9143 0.9437 0.7604 0.1403  0.2951  -0.0387 202 TYR A OH  
1655 N N   . ARG A 203 ? 1.2464 1.2947 1.0889 0.0888  0.3306  0.0613  203 ARG A N   
1656 C CA  . ARG A 203 ? 1.4017 1.4334 1.1774 0.0909  0.3509  0.0696  203 ARG A CA  
1657 C C   . ARG A 203 ? 1.3653 1.3710 1.0734 0.0944  0.3234  0.0642  203 ARG A C   
1658 O O   . ARG A 203 ? 1.3883 1.3821 1.0736 0.0864  0.3106  0.0797  203 ARG A O   
1659 C CB  . ARG A 203 ? 1.6550 1.6897 1.4101 0.1026  0.3903  0.0597  203 ARG A CB  
1660 C CG  . ARG A 203 ? 1.9687 1.9850 1.6502 0.1029  0.4118  0.0729  203 ARG A CG  
1661 C CD  . ARG A 203 ? 2.1395 2.1626 1.8456 0.0884  0.4267  0.1022  203 ARG A CD  
1662 N NE  . ARG A 203 ? 2.2024 2.2131 1.9031 0.0775  0.3935  0.1166  203 ARG A NE  
1663 C CZ  . ARG A 203 ? 2.2681 2.2586 1.9190 0.0728  0.3925  0.1352  203 ARG A CZ  
1664 N NH1 . ARG A 203 ? 2.2626 2.2427 1.9160 0.0647  0.3603  0.1434  203 ARG A NH1 
1665 N NH2 . ARG A 203 ? 2.2917 2.2714 1.8896 0.0762  0.4235  0.1456  203 ARG A NH2 
1666 N N   . GLU A 204 ? 1.3211 1.3178 1.0018 0.1066  0.3145  0.0415  204 GLU A N   
1667 C CA  . GLU A 204 ? 1.2840 1.2583 0.9113 0.1103  0.2851  0.0337  204 GLU A CA  
1668 C C   . GLU A 204 ? 1.1724 1.1484 0.8300 0.0991  0.2528  0.0430  204 GLU A C   
1669 O O   . GLU A 204 ? 1.0709 1.0644 0.7893 0.0920  0.2471  0.0460  204 GLU A O   
1670 C CB  . GLU A 204 ? 1.3018 1.2698 0.9157 0.1234  0.2769  0.0062  204 GLU A CB  
1671 C CG  . GLU A 204 ? 1.4171 1.3679 0.9601 0.1357  0.2955  -0.0063 204 GLU A CG  
1672 C CD  . GLU A 204 ? 1.4929 1.4485 1.0172 0.1367  0.3386  0.0043  204 GLU A CD  
1673 O OE1 . GLU A 204 ? 1.5161 1.4526 0.9650 0.1433  0.3509  0.0028  204 GLU A OE1 
1674 O OE2 . GLU A 204 ? 1.5150 1.4933 1.0997 0.1307  0.3597  0.0148  204 GLU A OE2 
1675 N N   . PRO A 205 ? 1.1397 1.0973 0.7553 0.0973  0.2313  0.0478  205 PRO A N   
1676 C CA  . PRO A 205 ? 1.0593 1.0175 0.6996 0.0873  0.2039  0.0550  205 PRO A CA  
1677 C C   . PRO A 205 ? 0.9403 0.9052 0.6137 0.0879  0.1813  0.0403  205 PRO A C   
1678 O O   . PRO A 205 ? 0.9131 0.8732 0.5738 0.0975  0.1766  0.0227  205 PRO A O   
1679 C CB  . PRO A 205 ? 1.1206 1.0564 0.7053 0.0895  0.1890  0.0594  205 PRO A CB  
1680 C CG  . PRO A 205 ? 1.1688 1.0914 0.6996 0.1027  0.1960  0.0456  205 PRO A CG  
1681 C CD  . PRO A 205 ? 1.2049 1.1399 0.7473 0.1056  0.2310  0.0452  205 PRO A CD  
1682 N N   . LEU A 206 ? 0.8629 0.8371 0.5769 0.0770  0.1670  0.0479  206 LEU A N   
1683 C CA  . LEU A 206 ? 0.7879 0.7682 0.5333 0.0751  0.1462  0.0389  206 LEU A CA  
1684 C C   . LEU A 206 ? 0.7434 0.7157 0.4801 0.0682  0.1234  0.0426  206 LEU A C   
1685 O O   . LEU A 206 ? 0.7534 0.7190 0.4740 0.0634  0.1238  0.0533  206 LEU A O   
1686 C CB  . LEU A 206 ? 0.7437 0.7433 0.5458 0.0681  0.1507  0.0447  206 LEU A CB  
1687 C CG  . LEU A 206 ? 0.7723 0.7837 0.5974 0.0750  0.1746  0.0406  206 LEU A CG  
1688 C CD1 . LEU A 206 ? 0.7430 0.7742 0.6294 0.0666  0.1761  0.0496  206 LEU A CD1 
1689 C CD2 . LEU A 206 ? 0.7930 0.8008 0.6146 0.0871  0.1723  0.0214  206 LEU A CD2 
1690 N N   . MET A 207 ? 0.7018 0.6748 0.4524 0.0677  0.1049  0.0340  207 MET A N   
1691 C CA  . MET A 207 ? 0.6703 0.6384 0.4185 0.0610  0.0862  0.0362  207 MET A CA  
1692 C C   . MET A 207 ? 0.6028 0.5814 0.3826 0.0486  0.0834  0.0464  207 MET A C   
1693 O O   . MET A 207 ? 0.5399 0.5303 0.3498 0.0455  0.0890  0.0498  207 MET A O   
1694 C CB  . MET A 207 ? 0.6963 0.6613 0.4487 0.0644  0.0698  0.0243  207 MET A CB  
1695 C CG  . MET A 207 ? 0.7725 0.7260 0.4951 0.0766  0.0690  0.0111  207 MET A CG  
1696 S SD  . MET A 207 ? 0.8678 0.8054 0.5530 0.0794  0.0544  0.0095  207 MET A SD  
1697 C CE  . MET A 207 ? 0.9152 0.8466 0.5679 0.0803  0.0713  0.0229  207 MET A CE  
1698 N N   . ALA A 208 ? 0.6113 0.5848 0.3846 0.0418  0.0737  0.0503  208 ALA A N   
1699 C CA  . ALA A 208 ? 0.5740 0.5538 0.3689 0.0298  0.0687  0.0571  208 ALA A CA  
1700 C C   . ALA A 208 ? 0.5521 0.5431 0.3762 0.0257  0.0618  0.0565  208 ALA A C   
1701 O O   . ALA A 208 ? 0.5491 0.5493 0.3975 0.0200  0.0643  0.0629  208 ALA A O   
1702 C CB  . ALA A 208 ? 0.5570 0.5288 0.3395 0.0255  0.0585  0.0555  208 ALA A CB  
1703 N N   . TRP A 209 ? 0.5498 0.5396 0.3747 0.0284  0.0518  0.0500  209 TRP A N   
1704 C CA  . TRP A 209 ? 0.5501 0.5476 0.4010 0.0233  0.0422  0.0526  209 TRP A CA  
1705 C C   . TRP A 209 ? 0.5392 0.5465 0.4188 0.0272  0.0487  0.0544  209 TRP A C   
1706 O O   . TRP A 209 ? 0.5436 0.5591 0.4499 0.0205  0.0413  0.0614  209 TRP A O   
1707 C CB  . TRP A 209 ? 0.5622 0.5552 0.4119 0.0253  0.0316  0.0471  209 TRP A CB  
1708 C CG  . TRP A 209 ? 0.5718 0.5589 0.4144 0.0373  0.0341  0.0361  209 TRP A CG  
1709 C CD1 . TRP A 209 ? 0.6007 0.5894 0.4593 0.0454  0.0367  0.0302  209 TRP A CD1 
1710 C CD2 . TRP A 209 ? 0.5933 0.5707 0.4109 0.0428  0.0323  0.0280  209 TRP A CD2 
1711 N NE1 . TRP A 209 ? 0.6212 0.6006 0.4620 0.0553  0.0369  0.0176  209 TRP A NE1 
1712 C CE2 . TRP A 209 ? 0.6212 0.5937 0.4367 0.0537  0.0328  0.0168  209 TRP A CE2 
1713 C CE3 . TRP A 209 ? 0.5977 0.5697 0.3973 0.0401  0.0293  0.0284  209 TRP A CE3 
1714 C CZ2 . TRP A 209 ? 0.6329 0.5948 0.4255 0.0612  0.0278  0.0065  209 TRP A CZ2 
1715 C CZ3 . TRP A 209 ? 0.6214 0.5844 0.4037 0.0479  0.0247  0.0197  209 TRP A CZ3 
1716 C CH2 . TRP A 209 ? 0.6325 0.5903 0.4096 0.0579  0.0228  0.0092  209 TRP A CH2 
1717 N N   . THR A 210 ? 0.5292 0.5351 0.4031 0.0383  0.0617  0.0473  210 THR A N   
1718 C CA  . THR A 210 ? 0.5026 0.5186 0.4051 0.0437  0.0732  0.0469  210 THR A CA  
1719 C C   . THR A 210 ? 0.5128 0.5392 0.4365 0.0354  0.0794  0.0581  210 THR A C   
1720 O O   . THR A 210 ? 0.5156 0.5539 0.4793 0.0323  0.0760  0.0630  210 THR A O   
1721 C CB  . THR A 210 ? 0.5032 0.5137 0.3836 0.0565  0.0904  0.0367  210 THR A CB  
1722 O OG1 . THR A 210 ? 0.4800 0.4789 0.3397 0.0629  0.0804  0.0251  210 THR A OG1 
1723 C CG2 . THR A 210 ? 0.5209 0.5423 0.4324 0.0635  0.1064  0.0334  210 THR A CG2 
1724 N N   . ILE A 211 ? 0.5189 0.5398 0.4185 0.0319  0.0868  0.0624  211 ILE A N   
1725 C CA  . ILE A 211 ? 0.5286 0.5567 0.4479 0.0230  0.0921  0.0727  211 ILE A CA  
1726 C C   . ILE A 211 ? 0.5070 0.5402 0.4492 0.0115  0.0715  0.0775  211 ILE A C   
1727 O O   . ILE A 211 ? 0.5266 0.5721 0.5078 0.0067  0.0691  0.0833  211 ILE A O   
1728 C CB  . ILE A 211 ? 0.5574 0.5744 0.4452 0.0210  0.1005  0.0768  211 ILE A CB  
1729 C CG1 . ILE A 211 ? 0.5916 0.6012 0.4488 0.0324  0.1184  0.0736  211 ILE A CG1 
1730 C CG2 . ILE A 211 ? 0.5569 0.5797 0.4695 0.0107  0.1052  0.0874  211 ILE A CG2 
1731 C CD1 . ILE A 211 ? 0.6382 0.6593 0.5171 0.0395  0.1375  0.0719  211 ILE A CD1 
1732 N N   . VAL A 212 ? 0.4797 0.5035 0.3980 0.0073  0.0565  0.0749  212 VAL A N   
1733 C CA  . VAL A 212 ? 0.4799 0.5054 0.4074 -0.0039 0.0375  0.0791  212 VAL A CA  
1734 C C   . VAL A 212 ? 0.4862 0.5223 0.4498 -0.0037 0.0275  0.0831  212 VAL A C   
1735 O O   . VAL A 212 ? 0.4895 0.5325 0.4777 -0.0122 0.0158  0.0898  212 VAL A O   
1736 C CB  . VAL A 212 ? 0.4798 0.4941 0.3744 -0.0065 0.0281  0.0748  212 VAL A CB  
1737 C CG1 . VAL A 212 ? 0.4678 0.4829 0.3657 -0.0160 0.0099  0.0791  212 VAL A CG1 
1738 C CG2 . VAL A 212 ? 0.5015 0.5064 0.3710 -0.0095 0.0334  0.0723  212 VAL A CG2 
1739 N N   . ASN A 213 ? 0.4783 0.5145 0.4473 0.0062  0.0301  0.0784  213 ASN A N   
1740 C CA  . ASN A 213 ? 0.4691 0.5126 0.4737 0.0077  0.0190  0.0820  213 ASN A CA  
1741 C C   . ASN A 213 ? 0.4566 0.5151 0.5076 0.0104  0.0269  0.0851  213 ASN A C   
1742 O O   . ASN A 213 ? 0.4393 0.5058 0.5266 0.0064  0.0118  0.0925  213 ASN A O   
1743 C CB  . ASN A 213 ? 0.4860 0.5237 0.4879 0.0181  0.0202  0.0744  213 ASN A CB  
1744 C CG  . ASN A 213 ? 0.4987 0.5238 0.4644 0.0148  0.0123  0.0722  213 ASN A CG  
1745 O OD1 . ASN A 213 ? 0.4969 0.5190 0.4479 0.0039  0.0010  0.0790  213 ASN A OD1 
1746 N ND2 . ASN A 213 ? 0.5176 0.5353 0.4682 0.0240  0.0190  0.0618  213 ASN A ND2 
1747 N N   . GLU A 214 ? 0.4646 0.5266 0.5150 0.0175  0.0506  0.0802  214 GLU A N   
1748 C CA  . GLU A 214 ? 0.4797 0.5577 0.5754 0.0190  0.0637  0.0836  214 GLU A CA  
1749 C C   . GLU A 214 ? 0.4773 0.5619 0.5945 0.0051  0.0511  0.0941  214 GLU A C   
1750 O O   . GLU A 214 ? 0.4663 0.5643 0.6335 0.0021  0.0413  0.0999  214 GLU A O   
1751 C CB  . GLU A 214 ? 0.4974 0.5749 0.5757 0.0268  0.0937  0.0786  214 GLU A CB  
1752 C CG  . GLU A 214 ? 0.5075 0.5801 0.5711 0.0417  0.1074  0.0658  214 GLU A CG  
1753 C CD  . GLU A 214 ? 0.5126 0.5991 0.6282 0.0505  0.1157  0.0613  214 GLU A CD  
1754 O OE1 . GLU A 214 ? 0.5177 0.5981 0.6260 0.0623  0.1200  0.0487  214 GLU A OE1 
1755 O OE2 . GLU A 214 ? 0.5049 0.6078 0.6717 0.0458  0.1165  0.0695  214 GLU A OE2 
1756 N N   . VAL A 215 ? 0.4904 0.5646 0.5713 -0.0030 0.0491  0.0954  215 VAL A N   
1757 C CA  . VAL A 215 ? 0.5183 0.5955 0.6149 -0.0162 0.0384  0.1022  215 VAL A CA  
1758 C C   . VAL A 215 ? 0.5323 0.6106 0.6423 -0.0250 0.0077  0.1066  215 VAL A C   
1759 O O   . VAL A 215 ? 0.5462 0.6341 0.6946 -0.0332 -0.0049 0.1125  215 VAL A O   
1760 C CB  . VAL A 215 ? 0.5141 0.5767 0.5674 -0.0218 0.0421  0.1004  215 VAL A CB  
1761 C CG1 . VAL A 215 ? 0.5187 0.5805 0.5848 -0.0362 0.0253  0.1043  215 VAL A CG1 
1762 C CG2 . VAL A 215 ? 0.5165 0.5771 0.5591 -0.0152 0.0698  0.1005  215 VAL A CG2 
1763 N N   . ILE A 216 ? 0.5204 0.5880 0.5970 -0.0244 -0.0051 0.1045  216 ILE A N   
1764 C CA  . ILE A 216 ? 0.5177 0.5820 0.5915 -0.0342 -0.0336 0.1102  216 ILE A CA  
1765 C C   . ILE A 216 ? 0.5237 0.6004 0.6492 -0.0315 -0.0471 0.1176  216 ILE A C   
1766 O O   . ILE A 216 ? 0.5533 0.6343 0.7014 -0.0405 -0.0699 0.1248  216 ILE A O   
1767 C CB  . ILE A 216 ? 0.5004 0.5496 0.5235 -0.0352 -0.0396 0.1076  216 ILE A CB  
1768 C CG1 . ILE A 216 ? 0.4805 0.5183 0.4605 -0.0403 -0.0321 0.1008  216 ILE A CG1 
1769 C CG2 . ILE A 216 ? 0.5207 0.5667 0.5419 -0.0430 -0.0668 0.1165  216 ILE A CG2 
1770 C CD1 . ILE A 216 ? 0.4789 0.5042 0.4145 -0.0418 -0.0348 0.0975  216 ILE A CD1 
1771 N N   . VAL A 217 ? 0.5053 0.5867 0.6501 -0.0188 -0.0346 0.1148  217 VAL A N   
1772 C CA  . VAL A 217 ? 0.5118 0.6032 0.7082 -0.0142 -0.0472 0.1208  217 VAL A CA  
1773 C C   . VAL A 217 ? 0.5170 0.6273 0.7744 -0.0154 -0.0447 0.1242  217 VAL A C   
1774 O O   . VAL A 217 ? 0.5138 0.6324 0.8149 -0.0192 -0.0681 0.1331  217 VAL A O   
1775 C CB  . VAL A 217 ? 0.5034 0.5930 0.7054 0.0006  -0.0321 0.1134  217 VAL A CB  
1776 C CG1 . VAL A 217 ? 0.5159 0.6177 0.7830 0.0083  -0.0386 0.1167  217 VAL A CG1 
1777 C CG2 . VAL A 217 ? 0.4924 0.5649 0.6493 0.0001  -0.0411 0.1129  217 VAL A CG2 
1778 N N   . SER A 218 ? 0.5136 0.6306 0.7754 -0.0126 -0.0170 0.1186  218 SER A N   
1779 C CA  . SER A 218 ? 0.5132 0.6496 0.8366 -0.0141 -0.0090 0.1222  218 SER A CA  
1780 C C   . SER A 218 ? 0.5298 0.6679 0.8679 -0.0298 -0.0366 0.1301  218 SER A C   
1781 O O   . SER A 218 ? 0.5703 0.7249 0.9725 -0.0327 -0.0481 0.1362  218 SER A O   
1782 C CB  . SER A 218 ? 0.5103 0.6512 0.8293 -0.0088 0.0286  0.1168  218 SER A CB  
1783 O OG  . SER A 218 ? 0.5260 0.6526 0.7913 -0.0161 0.0332  0.1157  218 SER A OG  
1784 N N   . TYR A 219 ? 0.5316 0.6528 0.8129 -0.0397 -0.0483 0.1289  219 TYR A N   
1785 C CA  . TYR A 219 ? 0.5501 0.6688 0.8355 -0.0547 -0.0772 0.1333  219 TYR A CA  
1786 C C   . TYR A 219 ? 0.5795 0.6962 0.8718 -0.0574 -0.1120 0.1409  219 TYR A C   
1787 O O   . TYR A 219 ? 0.6144 0.7407 0.9525 -0.0641 -0.1365 0.1476  219 TYR A O   
1788 C CB  . TYR A 219 ? 0.5519 0.6519 0.7729 -0.0622 -0.0743 0.1269  219 TYR A CB  
1789 C CG  . TYR A 219 ? 0.5512 0.6440 0.7648 -0.0778 -0.0994 0.1264  219 TYR A CG  
1790 C CD1 . TYR A 219 ? 0.5644 0.6678 0.8283 -0.0855 -0.1027 0.1282  219 TYR A CD1 
1791 C CD2 . TYR A 219 ? 0.5572 0.6318 0.7122 -0.0851 -0.1186 0.1228  219 TYR A CD2 
1792 C CE1 . TYR A 219 ? 0.5824 0.6769 0.8385 -0.0999 -0.1275 0.1250  219 TYR A CE1 
1793 C CE2 . TYR A 219 ? 0.5771 0.6426 0.7189 -0.0988 -0.1412 0.1190  219 TYR A CE2 
1794 C CZ  . TYR A 219 ? 0.5838 0.6584 0.7757 -0.1062 -0.1470 0.1193  219 TYR A CZ  
1795 O OH  . TYR A 219 ? 0.5921 0.6554 0.7699 -0.1198 -0.1712 0.1131  219 TYR A OH  
1796 N N   . GLU A 220 ? 0.6093 0.7137 0.8598 -0.0524 -0.1148 0.1411  220 GLU A N   
1797 C CA  . GLU A 220 ? 0.6436 0.7426 0.8933 -0.0551 -0.1464 0.1512  220 GLU A CA  
1798 C C   . GLU A 220 ? 0.6512 0.7679 0.9794 -0.0527 -0.1642 0.1601  220 GLU A C   
1799 O O   . GLU A 220 ? 0.6537 0.7688 0.9920 -0.0618 -0.1993 0.1696  220 GLU A O   
1800 C CB  . GLU A 220 ? 0.6525 0.7421 0.8758 -0.0456 -0.1383 0.1515  220 GLU A CB  
1801 C CG  . GLU A 220 ? 0.6645 0.7346 0.8120 -0.0506 -0.1358 0.1482  220 GLU A CG  
1802 C CD  . GLU A 220 ? 0.6847 0.7468 0.8172 -0.0423 -0.1304 0.1499  220 GLU A CD  
1803 O OE1 . GLU A 220 ? 0.7356 0.7845 0.8149 -0.0447 -0.1232 0.1465  220 GLU A OE1 
1804 O OE2 . GLU A 220 ? 0.6969 0.7662 0.8762 -0.0335 -0.1335 0.1542  220 GLU A OE2 
1805 N N   . TRP A 221 ? 0.6698 0.8031 1.0534 -0.0403 -0.1403 0.1566  221 TRP A N   
1806 C CA  . TRP A 221 ? 0.7494 0.9004 1.2142 -0.0352 -0.1544 0.1640  221 TRP A CA  
1807 C C   . TRP A 221 ? 0.7437 0.9113 1.2631 -0.0441 -0.1640 0.1666  221 TRP A C   
1808 O O   . TRP A 221 ? 0.7407 0.9238 1.3322 -0.0431 -0.1839 0.1743  221 TRP A O   
1809 C CB  . TRP A 221 ? 0.8386 1.0005 1.3421 -0.0178 -0.1225 0.1567  221 TRP A CB  
1810 C CG  . TRP A 221 ? 1.0151 1.1594 1.4676 -0.0099 -0.1150 0.1526  221 TRP A CG  
1811 C CD1 . TRP A 221 ? 1.0832 1.2068 1.4744 -0.0166 -0.1345 0.1580  221 TRP A CD1 
1812 C CD2 . TRP A 221 ? 1.0832 1.2289 1.5414 0.0057  -0.0836 0.1408  221 TRP A CD2 
1813 N NE1 . TRP A 221 ? 1.0745 1.1876 1.4393 -0.0067 -0.1187 0.1516  221 TRP A NE1 
1814 C CE2 . TRP A 221 ? 1.1291 1.2543 1.5324 0.0071  -0.0893 0.1400  221 TRP A CE2 
1815 C CE3 . TRP A 221 ? 1.0665 1.2280 1.5694 0.0182  -0.0512 0.1303  221 TRP A CE3 
1816 C CZ2 . TRP A 221 ? 1.1934 1.3130 1.5880 0.0206  -0.0669 0.1280  221 TRP A CZ2 
1817 C CZ3 . TRP A 221 ? 1.1028 1.2576 1.5894 0.0321  -0.0277 0.1176  221 TRP A CZ3 
1818 C CH2 . TRP A 221 ? 1.1745 1.3082 1.6081 0.0330  -0.0372 0.1160  221 TRP A CH2 
1819 N N   . GLU A 222 ? 0.6966 0.8605 1.1849 -0.0527 -0.1509 0.1604  222 GLU A N   
1820 C CA  . GLU A 222 ? 0.6636 0.8400 1.1990 -0.0634 -0.1610 0.1622  222 GLU A CA  
1821 C C   . GLU A 222 ? 0.6998 0.8608 1.1973 -0.0793 -0.2020 0.1653  222 GLU A C   
1822 O O   . GLU A 222 ? 0.7777 0.9482 1.3253 -0.0878 -0.2311 0.1706  222 GLU A O   
1823 C CB  . GLU A 222 ? 0.6213 0.8018 1.1520 -0.0635 -0.1222 0.1545  222 GLU A CB  
1824 C CG  . GLU A 222 ? 0.5889 0.7870 1.1636 -0.0490 -0.0821 0.1518  222 GLU A CG  
1825 C CD  . GLU A 222 ? 0.5723 0.7979 1.2490 -0.0459 -0.0845 0.1573  222 GLU A CD  
1826 O OE1 . GLU A 222 ? 0.5615 0.7980 1.2869 -0.0576 -0.1021 0.1623  222 GLU A OE1 
1827 O OE2 . GLU A 222 ? 0.5465 0.7831 1.2576 -0.0315 -0.0677 0.1553  222 GLU A OE2 
1828 N N   . VAL A 223 ? 0.7161 0.8536 1.1270 -0.0836 -0.2043 0.1609  223 VAL A N   
1829 C CA  . VAL A 223 ? 0.7755 0.8971 1.1426 -0.0990 -0.2347 0.1592  223 VAL A CA  
1830 C C   . VAL A 223 ? 0.8358 0.9462 1.1770 -0.1026 -0.2736 0.1694  223 VAL A C   
1831 O O   . VAL A 223 ? 0.8526 0.9561 1.1859 -0.1149 -0.3104 0.1720  223 VAL A O   
1832 C CB  . VAL A 223 ? 0.7873 0.8899 1.0781 -0.1028 -0.2146 0.1474  223 VAL A CB  
1833 C CG1 . VAL A 223 ? 0.8032 0.8912 1.0290 -0.0956 -0.2024 0.1467  223 VAL A CG1 
1834 C CG2 . VAL A 223 ? 0.8007 0.8884 1.0572 -0.1186 -0.2418 0.1413  223 VAL A CG2 
1835 N N   . ILE A 224 ? 0.8727 0.9793 1.1982 -0.0924 -0.2660 0.1754  224 ILE A N   
1836 C CA  . ILE A 224 ? 0.9273 1.0221 1.2297 -0.0954 -0.3007 0.1888  224 ILE A CA  
1837 C C   . ILE A 224 ? 0.9584 1.0707 1.3468 -0.0927 -0.3278 0.2005  224 ILE A C   
1838 O O   . ILE A 224 ? 0.9122 1.0415 1.3643 -0.0798 -0.3099 0.2019  224 ILE A O   
1839 C CB  . ILE A 224 ? 0.9309 1.0143 1.1908 -0.0864 -0.2832 0.1918  224 ILE A CB  
1840 C CG1 . ILE A 224 ? 0.9107 0.9797 1.0952 -0.0888 -0.2562 0.1792  224 ILE A CG1 
1841 C CG2 . ILE A 224 ? 1.0037 1.0739 1.2425 -0.0903 -0.3186 0.2093  224 ILE A CG2 
1842 C CD1 . ILE A 224 ? 0.9258 0.9875 1.0818 -0.0791 -0.2332 0.1793  224 ILE A CD1 
1843 N N   . LYS A 225 ? 1.0694 1.1771 1.4588 -0.1051 -0.3712 0.2074  225 LYS A N   
1844 C CA  . LYS A 225 ? 1.1349 1.2601 1.6114 -0.1053 -0.4029 0.2174  225 LYS A CA  
1845 C C   . LYS A 225 ? 1.1566 1.2853 1.6706 -0.0935 -0.4132 0.2327  225 LYS A C   
1846 O O   . LYS A 225 ? 1.1221 1.2730 1.7281 -0.0838 -0.4101 0.2357  225 LYS A O   
1847 C CB  . LYS A 225 ? 1.2019 1.3150 1.6526 -0.1217 -0.4530 0.2219  225 LYS A CB  
1848 C CG  . LYS A 225 ? 1.2088 1.3182 1.6358 -0.1339 -0.4492 0.2055  225 LYS A CG  
1849 C CD  . LYS A 225 ? 1.2883 1.3795 1.6707 -0.1500 -0.4987 0.2066  225 LYS A CD  
1850 C CE  . LYS A 225 ? 1.3225 1.4113 1.6991 -0.1618 -0.4982 0.1888  225 LYS A CE  
1851 N NZ  . LYS A 225 ? 1.4006 1.4712 1.7371 -0.1773 -0.5503 0.1875  225 LYS A NZ  
1852 N N   . LYS A 226 ? 1.1874 1.2932 1.6298 -0.0948 -0.4234 0.2419  226 LYS A N   
1853 C CA  . LYS A 226 ? 1.1854 1.2876 1.6499 -0.0851 -0.4343 0.2579  226 LYS A CA  
1854 C C   . LYS A 226 ? 1.0805 1.2012 1.6118 -0.0672 -0.3953 0.2500  226 LYS A C   
1855 O O   . LYS A 226 ? 1.0630 1.1883 1.6493 -0.0569 -0.4055 0.2605  226 LYS A O   
1856 C CB  . LYS A 226 ? 1.2681 1.3427 1.6367 -0.0891 -0.4340 0.2653  226 LYS A CB  
1857 C CG  . LYS A 226 ? 1.3593 1.4135 1.6350 -0.1059 -0.4504 0.2636  226 LYS A CG  
1858 C CD  . LYS A 226 ? 1.4063 1.4356 1.5940 -0.1097 -0.4464 0.2723  226 LYS A CD  
1859 C CE  . LYS A 226 ? 1.3986 1.4294 1.5845 -0.0977 -0.4029 0.2655  226 LYS A CE  
1860 N NZ  . LYS A 226 ? 1.4682 1.4762 1.5709 -0.1032 -0.3966 0.2729  226 LYS A NZ  
1861 N N   . PHE A 227 ? 0.9931 1.1223 1.5160 -0.0635 -0.3512 0.2313  227 PHE A N   
1862 C CA  . PHE A 227 ? 0.9666 1.1108 1.5375 -0.0470 -0.3105 0.2210  227 PHE A CA  
1863 C C   . PHE A 227 ? 0.9599 1.1329 1.6252 -0.0428 -0.3012 0.2157  227 PHE A C   
1864 O O   . PHE A 227 ? 0.9949 1.1770 1.7108 -0.0495 -0.3375 0.2256  227 PHE A O   
1865 C CB  . PHE A 227 ? 0.9724 1.1082 1.4777 -0.0450 -0.2682 0.2053  227 PHE A CB  
1866 C CG  . PHE A 227 ? 1.0384 1.1497 1.4617 -0.0468 -0.2681 0.2082  227 PHE A CG  
1867 C CD1 . PHE A 227 ? 1.1262 1.2215 1.5262 -0.0521 -0.3028 0.2255  227 PHE A CD1 
1868 C CD2 . PHE A 227 ? 1.0708 1.1748 1.4420 -0.0435 -0.2325 0.1947  227 PHE A CD2 
1869 C CE1 . PHE A 227 ? 1.2103 1.2844 1.5388 -0.0545 -0.2985 0.2291  227 PHE A CE1 
1870 C CE2 . PHE A 227 ? 1.1270 1.2108 1.4310 -0.0454 -0.2306 0.1968  227 PHE A CE2 
1871 C CZ  . PHE A 227 ? 1.2047 1.2741 1.4884 -0.0512 -0.2620 0.2141  227 PHE A CZ  
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