data_7HBG
# 
_entry.id   7HBG 
# 
_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   7HBG         pdb_00007hbg 10.2210/pdb7hbg/pdb 
WWPDB D_1001407263 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HBG 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, L.' 1  ? 
'Wang, W.'  2  ? 
'Zhu, Z.'   3  ? 
'Li, Q.'    4  ? 
'Li, M.'    5  ? 
'Zhou, H.'  6  ? 
'Xu, Q.'    7  ? 
'Wen, W.'   8  ? 
'Wang, Q.'  9  ? 
'Yu, F.'    10 ? 
# 
_citation.id                        primary 
_citation.title                     
;Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.
;
_citation.journal_abbrev            Iucrj 
_citation.journal_volume            12 
_citation.page_first                177 
_citation.page_last                 187 
_citation.year                      2025 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   39819741 
_citation.pdbx_database_id_DOI      10.1107/S2052252524012247 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Huang, L.' 0009-0001-8431-0182 1  
primary 'Wang, W.'  ?                   2  
primary 'Zhu, Z.'   ?                   3  
primary 'Li, Q.'    ?                   4  
primary 'Li, M.'    ?                   5  
primary 'Zhou, H.'  ?                   6  
primary 'Xu, Q.'    0000-0002-7137-0768 7  
primary 'Wen, W.'   ?                   8  
primary 'Wang, Q.'  ?                   9  
primary 'Yu, F.'    0000-0002-9502-3277 10 
# 
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 'Heat shock protein HSP 90-alpha'                     26859.117 1   3.6.4.10 ? ? ? 
2 non-polymer syn 'N-methyl-1-{4-[(pyridin-2-yl)oxy]phenyl}methanamine' 214.263   1   ?        ? ? ? 
3 water       nat water                                                 18.015    281 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Heat shock 86 kDa,HSP 86,HSP86,Heat shock protein family C member 1,Lipopolysaccharide-associated protein 2,LAP-2,LPS-associated protein 2,Renal carcinoma antigen NY-REN-38
;
# 
_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       
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_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 'N-methyl-1-{4-[(pyridin-2-yl)oxy]phenyl}methanamine' A1AYB 
3 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   ASP n 
1 3   GLN n 
1 4   PRO n 
1 5   MET n 
1 6   GLU n 
1 7   GLU n 
1 8   GLU n 
1 9   GLU n 
1 10  VAL n 
1 11  GLU n 
1 12  THR n 
1 13  PHE n 
1 14  ALA n 
1 15  PHE n 
1 16  GLN n 
1 17  ALA n 
1 18  GLU n 
1 19  ILE n 
1 20  ALA n 
1 21  GLN n 
1 22  LEU n 
1 23  MET n 
1 24  SER n 
1 25  LEU n 
1 26  ILE n 
1 27  ILE n 
1 28  ASN n 
1 29  THR n 
1 30  PHE n 
1 31  TYR n 
1 32  SER n 
1 33  ASN n 
1 34  LYS n 
1 35  GLU n 
1 36  ILE n 
1 37  PHE n 
1 38  LEU n 
1 39  ARG n 
1 40  GLU n 
1 41  LEU n 
1 42  ILE n 
1 43  SER n 
1 44  ASN n 
1 45  SER n 
1 46  SER n 
1 47  ASP n 
1 48  ALA n 
1 49  LEU n 
1 50  ASP n 
1 51  LYS n 
1 52  ILE n 
1 53  ARG n 
1 54  TYR n 
1 55  GLU n 
1 56  SER n 
1 57  LEU n 
1 58  THR n 
1 59  ASP n 
1 60  PRO n 
1 61  SER n 
1 62  LYS n 
1 63  LEU n 
1 64  ASP n 
1 65  SER n 
1 66  GLY n 
1 67  LYS n 
1 68  GLU n 
1 69  LEU n 
1 70  HIS n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ILE n 
1 75  PRO n 
1 76  ASN n 
1 77  LYS n 
1 78  GLN n 
1 79  ASP n 
1 80  ARG n 
1 81  THR n 
1 82  LEU n 
1 83  THR n 
1 84  ILE n 
1 85  VAL n 
1 86  ASP n 
1 87  THR n 
1 88  GLY n 
1 89  ILE n 
1 90  GLY n 
1 91  MET n 
1 92  THR n 
1 93  LYS n 
1 94  ALA n 
1 95  ASP n 
1 96  LEU n 
1 97  ILE n 
1 98  ASN n 
1 99  ASN n 
1 100 LEU n 
1 101 GLY n 
1 102 THR n 
1 103 ILE n 
1 104 ALA n 
1 105 LYS n 
1 106 SER n 
1 107 GLY n 
1 108 THR n 
1 109 LYS n 
1 110 ALA n 
1 111 PHE n 
1 112 MET n 
1 113 GLU n 
1 114 ALA n 
1 115 LEU n 
1 116 GLN n 
1 117 ALA n 
1 118 GLY n 
1 119 ALA n 
1 120 ASP n 
1 121 ILE n 
1 122 SER n 
1 123 MET n 
1 124 ILE n 
1 125 GLY n 
1 126 GLN n 
1 127 PHE n 
1 128 GLY n 
1 129 VAL n 
1 130 GLY n 
1 131 PHE n 
1 132 TYR n 
1 133 SER n 
1 134 ALA n 
1 135 TYR n 
1 136 LEU n 
1 137 VAL n 
1 138 ALA n 
1 139 GLU n 
1 140 LYS n 
1 141 VAL n 
1 142 THR n 
1 143 VAL n 
1 144 ILE n 
1 145 THR n 
1 146 LYS n 
1 147 HIS n 
1 148 ASN n 
1 149 ASP n 
1 150 ASP n 
1 151 GLU n 
1 152 GLN n 
1 153 TYR n 
1 154 ALA n 
1 155 TRP n 
1 156 GLU n 
1 157 SER n 
1 158 SER n 
1 159 ALA n 
1 160 GLY n 
1 161 GLY n 
1 162 SER n 
1 163 PHE n 
1 164 THR n 
1 165 VAL n 
1 166 ARG n 
1 167 THR n 
1 168 ASP n 
1 169 THR n 
1 170 GLY n 
1 171 GLU n 
1 172 PRO n 
1 173 MET n 
1 174 GLY n 
1 175 ARG n 
1 176 GLY n 
1 177 THR n 
1 178 LYS n 
1 179 VAL n 
1 180 ILE n 
1 181 LEU n 
1 182 HIS n 
1 183 LEU n 
1 184 LYS n 
1 185 GLU n 
1 186 ASP n 
1 187 GLN n 
1 188 THR n 
1 189 GLU n 
1 190 TYR n 
1 191 LEU n 
1 192 GLU n 
1 193 GLU n 
1 194 ARG n 
1 195 ARG n 
1 196 ILE n 
1 197 LYS n 
1 198 GLU n 
1 199 ILE n 
1 200 VAL n 
1 201 LYS n 
1 202 LYS n 
1 203 HIS n 
1 204 SER n 
1 205 GLN n 
1 206 PHE n 
1 207 ILE n 
1 208 GLY n 
1 209 TYR n 
1 210 PRO n 
1 211 ILE n 
1 212 THR n 
1 213 LEU n 
1 214 PHE n 
1 215 VAL n 
1 216 GLU n 
1 217 LYS n 
1 218 GLU n 
1 219 ARG n 
1 220 ASP n 
1 221 LYS n 
1 222 GLU n 
1 223 VAL n 
1 224 SER n 
1 225 ASP n 
1 226 ASP n 
1 227 GLU n 
1 228 ALA n 
1 229 GLU n 
1 230 LEU n 
1 231 GLU n 
1 232 HIS n 
1 233 HIS n 
1 234 HIS n 
1 235 HIS n 
1 236 HIS n 
1 237 HIS 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                   237 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HSP90AA1, HSP90A, HSPC1, HSPCA' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          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                       pET28 
_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 
A1AYB non-polymer         . 'N-methyl-1-{4-[(pyridin-2-yl)oxy]phenyl}methanamine' ? 'C13 H14 N2 O'   214.263 
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 
GLN   'L-peptide linking' y GLUTAMINE                                             ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                       ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                               ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                             ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                 ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                            ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                               ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                            ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                         ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                               ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                             ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                            ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                              ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   8   ?   ?   ?   A . n 
A 1 2   ASP 2   9   ?   ?   ?   A . n 
A 1 3   GLN 3   10  ?   ?   ?   A . n 
A 1 4   PRO 4   11  ?   ?   ?   A . n 
A 1 5   MET 5   12  ?   ?   ?   A . n 
A 1 6   GLU 6   13  ?   ?   ?   A . n 
A 1 7   GLU 7   14  ?   ?   ?   A . n 
A 1 8   GLU 8   15  ?   ?   ?   A . n 
A 1 9   GLU 9   16  16  GLU GLU A . n 
A 1 10  VAL 10  17  17  VAL VAL A . n 
A 1 11  GLU 11  18  18  GLU GLU A . n 
A 1 12  THR 12  19  19  THR THR A . n 
A 1 13  PHE 13  20  20  PHE PHE A . n 
A 1 14  ALA 14  21  21  ALA ALA A . n 
A 1 15  PHE 15  22  22  PHE PHE A . n 
A 1 16  GLN 16  23  23  GLN GLN A . n 
A 1 17  ALA 17  24  24  ALA ALA A . n 
A 1 18  GLU 18  25  25  GLU GLU A . n 
A 1 19  ILE 19  26  26  ILE ILE A . n 
A 1 20  ALA 20  27  27  ALA ALA A . n 
A 1 21  GLN 21  28  28  GLN GLN A . n 
A 1 22  LEU 22  29  29  LEU LEU A . n 
A 1 23  MET 23  30  30  MET MET A . n 
A 1 24  SER 24  31  31  SER SER A . n 
A 1 25  LEU 25  32  32  LEU LEU A . n 
A 1 26  ILE 26  33  33  ILE ILE A . n 
A 1 27  ILE 27  34  34  ILE ILE A . n 
A 1 28  ASN 28  35  35  ASN ASN A . n 
A 1 29  THR 29  36  36  THR THR A . n 
A 1 30  PHE 30  37  37  PHE PHE A . n 
A 1 31  TYR 31  38  38  TYR TYR A . n 
A 1 32  SER 32  39  39  SER SER A . n 
A 1 33  ASN 33  40  40  ASN ASN A . n 
A 1 34  LYS 34  41  41  LYS LYS A . n 
A 1 35  GLU 35  42  42  GLU GLU A . n 
A 1 36  ILE 36  43  43  ILE ILE A . n 
A 1 37  PHE 37  44  44  PHE PHE A . n 
A 1 38  LEU 38  45  45  LEU LEU A . n 
A 1 39  ARG 39  46  46  ARG ARG A . n 
A 1 40  GLU 40  47  47  GLU GLU A . n 
A 1 41  LEU 41  48  48  LEU LEU A . n 
A 1 42  ILE 42  49  49  ILE ILE A . n 
A 1 43  SER 43  50  50  SER SER A . n 
A 1 44  ASN 44  51  51  ASN ASN A . n 
A 1 45  SER 45  52  52  SER SER A . n 
A 1 46  SER 46  53  53  SER SER A . n 
A 1 47  ASP 47  54  54  ASP ASP A . n 
A 1 48  ALA 48  55  55  ALA ALA A . n 
A 1 49  LEU 49  56  56  LEU LEU A . n 
A 1 50  ASP 50  57  57  ASP ASP A . n 
A 1 51  LYS 51  58  58  LYS LYS A . n 
A 1 52  ILE 52  59  59  ILE ILE A . n 
A 1 53  ARG 53  60  60  ARG ARG A . n 
A 1 54  TYR 54  61  61  TYR TYR A . n 
A 1 55  GLU 55  62  62  GLU GLU A . n 
A 1 56  SER 56  63  63  SER SER A . n 
A 1 57  LEU 57  64  64  LEU LEU A . n 
A 1 58  THR 58  65  65  THR THR A . n 
A 1 59  ASP 59  66  66  ASP ASP A . n 
A 1 60  PRO 60  67  67  PRO PRO A . n 
A 1 61  SER 61  68  68  SER SER A . n 
A 1 62  LYS 62  69  69  LYS LYS A . n 
A 1 63  LEU 63  70  70  LEU LEU A . n 
A 1 64  ASP 64  71  71  ASP ASP A . n 
A 1 65  SER 65  72  72  SER SER A . n 
A 1 66  GLY 66  73  73  GLY GLY A . n 
A 1 67  LYS 67  74  74  LYS LYS A . n 
A 1 68  GLU 68  75  75  GLU GLU A . n 
A 1 69  LEU 69  76  76  LEU LEU A . n 
A 1 70  HIS 70  77  77  HIS HIS A . n 
A 1 71  ILE 71  78  78  ILE ILE A . n 
A 1 72  ASN 72  79  79  ASN ASN A . n 
A 1 73  LEU 73  80  80  LEU LEU A . n 
A 1 74  ILE 74  81  81  ILE ILE A . n 
A 1 75  PRO 75  82  82  PRO PRO A . n 
A 1 76  ASN 76  83  83  ASN ASN A . n 
A 1 77  LYS 77  84  84  LYS LYS A . n 
A 1 78  GLN 78  85  85  GLN GLN A . n 
A 1 79  ASP 79  86  86  ASP ASP A . n 
A 1 80  ARG 80  87  87  ARG ARG A . n 
A 1 81  THR 81  88  88  THR THR A . n 
A 1 82  LEU 82  89  89  LEU LEU A . n 
A 1 83  THR 83  90  90  THR THR A . n 
A 1 84  ILE 84  91  91  ILE ILE A . n 
A 1 85  VAL 85  92  92  VAL VAL A . n 
A 1 86  ASP 86  93  93  ASP ASP A . n 
A 1 87  THR 87  94  94  THR THR A . n 
A 1 88  GLY 88  95  95  GLY GLY A . n 
A 1 89  ILE 89  96  96  ILE ILE A . n 
A 1 90  GLY 90  97  97  GLY GLY A . n 
A 1 91  MET 91  98  98  MET MET A . n 
A 1 92  THR 92  99  99  THR THR A . n 
A 1 93  LYS 93  100 100 LYS LYS A . n 
A 1 94  ALA 94  101 101 ALA ALA A . n 
A 1 95  ASP 95  102 102 ASP ASP A . n 
A 1 96  LEU 96  103 103 LEU LEU A . n 
A 1 97  ILE 97  104 104 ILE ILE A . n 
A 1 98  ASN 98  105 105 ASN ASN A . n 
A 1 99  ASN 99  106 106 ASN ASN A . n 
A 1 100 LEU 100 107 107 LEU LEU A . n 
A 1 101 GLY 101 108 108 GLY GLY A . n 
A 1 102 THR 102 109 109 THR THR A . n 
A 1 103 ILE 103 110 110 ILE ILE A . n 
A 1 104 ALA 104 111 111 ALA ALA A . n 
A 1 105 LYS 105 112 112 LYS LYS A . n 
A 1 106 SER 106 113 113 SER SER A . n 
A 1 107 GLY 107 114 114 GLY GLY A . n 
A 1 108 THR 108 115 115 THR THR A . n 
A 1 109 LYS 109 116 116 LYS LYS A . n 
A 1 110 ALA 110 117 117 ALA ALA A . n 
A 1 111 PHE 111 118 118 PHE PHE A . n 
A 1 112 MET 112 119 119 MET MET A . n 
A 1 113 GLU 113 120 120 GLU GLU A . n 
A 1 114 ALA 114 121 121 ALA ALA A . n 
A 1 115 LEU 115 122 122 LEU LEU A . n 
A 1 116 GLN 116 123 123 GLN GLN A . n 
A 1 117 ALA 117 124 124 ALA ALA A . n 
A 1 118 GLY 118 125 125 GLY GLY A . n 
A 1 119 ALA 119 126 126 ALA ALA A . n 
A 1 120 ASP 120 127 127 ASP ASP A . n 
A 1 121 ILE 121 128 128 ILE ILE A . n 
A 1 122 SER 122 129 129 SER SER A . n 
A 1 123 MET 123 130 130 MET MET A . n 
A 1 124 ILE 124 131 131 ILE ILE A . n 
A 1 125 GLY 125 132 132 GLY GLY A . n 
A 1 126 GLN 126 133 133 GLN GLN A . n 
A 1 127 PHE 127 134 134 PHE PHE A . n 
A 1 128 GLY 128 135 135 GLY GLY A . n 
A 1 129 VAL 129 136 136 VAL VAL A . n 
A 1 130 GLY 130 137 137 GLY GLY A . n 
A 1 131 PHE 131 138 138 PHE PHE A . n 
A 1 132 TYR 132 139 139 TYR TYR A . n 
A 1 133 SER 133 140 140 SER SER A . n 
A 1 134 ALA 134 141 141 ALA ALA A . n 
A 1 135 TYR 135 142 142 TYR TYR A . n 
A 1 136 LEU 136 143 143 LEU LEU A . n 
A 1 137 VAL 137 144 144 VAL VAL A . n 
A 1 138 ALA 138 145 145 ALA ALA A . n 
A 1 139 GLU 139 146 146 GLU GLU A . n 
A 1 140 LYS 140 147 147 LYS LYS A . n 
A 1 141 VAL 141 148 148 VAL VAL A . n 
A 1 142 THR 142 149 149 THR THR A . n 
A 1 143 VAL 143 150 150 VAL VAL A . n 
A 1 144 ILE 144 151 151 ILE ILE A . n 
A 1 145 THR 145 152 152 THR THR A . n 
A 1 146 LYS 146 153 153 LYS LYS A . n 
A 1 147 HIS 147 154 154 HIS HIS A . n 
A 1 148 ASN 148 155 155 ASN ASN A . n 
A 1 149 ASP 149 156 156 ASP ASP A . n 
A 1 150 ASP 150 157 157 ASP ASP A . n 
A 1 151 GLU 151 158 158 GLU GLU A . n 
A 1 152 GLN 152 159 159 GLN GLN A . n 
A 1 153 TYR 153 160 160 TYR TYR A . n 
A 1 154 ALA 154 161 161 ALA ALA A . n 
A 1 155 TRP 155 162 162 TRP TRP A . n 
A 1 156 GLU 156 163 163 GLU GLU A . n 
A 1 157 SER 157 164 164 SER SER A . n 
A 1 158 SER 158 165 165 SER SER A . n 
A 1 159 ALA 159 166 166 ALA ALA A . n 
A 1 160 GLY 160 167 167 GLY GLY A . n 
A 1 161 GLY 161 168 168 GLY GLY A . n 
A 1 162 SER 162 169 169 SER SER A . n 
A 1 163 PHE 163 170 170 PHE PHE A . n 
A 1 164 THR 164 171 171 THR THR A . n 
A 1 165 VAL 165 172 172 VAL VAL A . n 
A 1 166 ARG 166 173 173 ARG ARG A . n 
A 1 167 THR 167 174 174 THR THR A . n 
A 1 168 ASP 168 175 175 ASP ASP A . n 
A 1 169 THR 169 176 176 THR THR A . n 
A 1 170 GLY 170 177 177 GLY GLY A . n 
A 1 171 GLU 171 178 178 GLU GLU A . n 
A 1 172 PRO 172 179 179 PRO PRO A . n 
A 1 173 MET 173 180 180 MET MET A . n 
A 1 174 GLY 174 181 181 GLY GLY A . n 
A 1 175 ARG 175 182 182 ARG ARG A . n 
A 1 176 GLY 176 183 183 GLY GLY A . n 
A 1 177 THR 177 184 184 THR THR A . n 
A 1 178 LYS 178 185 185 LYS LYS A . n 
A 1 179 VAL 179 186 186 VAL VAL A . n 
A 1 180 ILE 180 187 187 ILE ILE A . n 
A 1 181 LEU 181 188 188 LEU LEU A . n 
A 1 182 HIS 182 189 189 HIS HIS A . n 
A 1 183 LEU 183 190 190 LEU LEU A . n 
A 1 184 LYS 184 191 191 LYS LYS A . n 
A 1 185 GLU 185 192 192 GLU GLU A . n 
A 1 186 ASP 186 193 193 ASP ASP A . n 
A 1 187 GLN 187 194 194 GLN GLN A . n 
A 1 188 THR 188 195 195 THR THR A . n 
A 1 189 GLU 189 196 196 GLU GLU A . n 
A 1 190 TYR 190 197 197 TYR TYR A . n 
A 1 191 LEU 191 198 198 LEU LEU A . n 
A 1 192 GLU 192 199 199 GLU GLU A . n 
A 1 193 GLU 193 200 200 GLU GLU A . n 
A 1 194 ARG 194 201 201 ARG ARG A . n 
A 1 195 ARG 195 202 202 ARG ARG A . n 
A 1 196 ILE 196 203 203 ILE ILE A . n 
A 1 197 LYS 197 204 204 LYS LYS A . n 
A 1 198 GLU 198 205 205 GLU GLU A . n 
A 1 199 ILE 199 206 206 ILE ILE A . n 
A 1 200 VAL 200 207 207 VAL VAL A . n 
A 1 201 LYS 201 208 208 LYS LYS A . n 
A 1 202 LYS 202 209 209 LYS LYS A . n 
A 1 203 HIS 203 210 210 HIS HIS A . n 
A 1 204 SER 204 211 211 SER SER A . n 
A 1 205 GLN 205 212 212 GLN GLN A . n 
A 1 206 PHE 206 213 213 PHE PHE A . n 
A 1 207 ILE 207 214 214 ILE ILE A . n 
A 1 208 GLY 208 215 215 GLY GLY A . n 
A 1 209 TYR 209 216 216 TYR TYR A . n 
A 1 210 PRO 210 217 217 PRO PRO A . n 
A 1 211 ILE 211 218 218 ILE ILE A . n 
A 1 212 THR 212 219 219 THR THR A . n 
A 1 213 LEU 213 220 220 LEU LEU A . n 
A 1 214 PHE 214 221 221 PHE PHE A . n 
A 1 215 VAL 215 222 222 VAL VAL A . n 
A 1 216 GLU 216 223 223 GLU GLU A . n 
A 1 217 LYS 217 224 224 LYS LYS A . n 
A 1 218 GLU 218 225 ?   ?   ?   A . n 
A 1 219 ARG 219 226 ?   ?   ?   A . n 
A 1 220 ASP 220 227 ?   ?   ?   A . n 
A 1 221 LYS 221 228 ?   ?   ?   A . n 
A 1 222 GLU 222 229 ?   ?   ?   A . n 
A 1 223 VAL 223 230 ?   ?   ?   A . n 
A 1 224 SER 224 231 ?   ?   ?   A . n 
A 1 225 ASP 225 232 ?   ?   ?   A . n 
A 1 226 ASP 226 233 ?   ?   ?   A . n 
A 1 227 GLU 227 234 ?   ?   ?   A . n 
A 1 228 ALA 228 235 ?   ?   ?   A . n 
A 1 229 GLU 229 236 ?   ?   ?   A . n 
A 1 230 LEU 230 237 ?   ?   ?   A . n 
A 1 231 GLU 231 238 ?   ?   ?   A . n 
A 1 232 HIS 232 239 ?   ?   ?   A . n 
A 1 233 HIS 233 240 ?   ?   ?   A . n 
A 1 234 HIS 234 241 ?   ?   ?   A . n 
A 1 235 HIS 235 242 ?   ?   ?   A . n 
A 1 236 HIS 236 243 ?   ?   ?   A . n 
A 1 237 HIS 237 244 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AYB 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AYB 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1AYB 1   301 301 A1AYB BSN A . 
C 3 HOH   1   401 276 HOH   HOH A . 
C 3 HOH   2   402 281 HOH   HOH A . 
C 3 HOH   3   403 126 HOH   HOH A . 
C 3 HOH   4   404 202 HOH   HOH A . 
C 3 HOH   5   405 90  HOH   HOH A . 
C 3 HOH   6   406 157 HOH   HOH A . 
C 3 HOH   7   407 132 HOH   HOH A . 
C 3 HOH   8   408 277 HOH   HOH A . 
C 3 HOH   9   409 249 HOH   HOH A . 
C 3 HOH   10  410 205 HOH   HOH A . 
C 3 HOH   11  411 80  HOH   HOH A . 
C 3 HOH   12  412 272 HOH   HOH A . 
C 3 HOH   13  413 274 HOH   HOH A . 
C 3 HOH   14  414 118 HOH   HOH A . 
C 3 HOH   15  415 185 HOH   HOH A . 
C 3 HOH   16  416 130 HOH   HOH A . 
C 3 HOH   17  417 84  HOH   HOH A . 
C 3 HOH   18  418 150 HOH   HOH A . 
C 3 HOH   19  419 184 HOH   HOH A . 
C 3 HOH   20  420 77  HOH   HOH A . 
C 3 HOH   21  421 16  HOH   HOH A . 
C 3 HOH   22  422 114 HOH   HOH A . 
C 3 HOH   23  423 56  HOH   HOH A . 
C 3 HOH   24  424 222 HOH   HOH A . 
C 3 HOH   25  425 64  HOH   HOH A . 
C 3 HOH   26  426 245 HOH   HOH A . 
C 3 HOH   27  427 85  HOH   HOH A . 
C 3 HOH   28  428 23  HOH   HOH A . 
C 3 HOH   29  429 165 HOH   HOH A . 
C 3 HOH   30  430 148 HOH   HOH A . 
C 3 HOH   31  431 140 HOH   HOH A . 
C 3 HOH   32  432 92  HOH   HOH A . 
C 3 HOH   33  433 193 HOH   HOH A . 
C 3 HOH   34  434 228 HOH   HOH A . 
C 3 HOH   35  435 196 HOH   HOH A . 
C 3 HOH   36  436 60  HOH   HOH A . 
C 3 HOH   37  437 102 HOH   HOH A . 
C 3 HOH   38  438 50  HOH   HOH A . 
C 3 HOH   39  439 48  HOH   HOH A . 
C 3 HOH   40  440 252 HOH   HOH A . 
C 3 HOH   41  441 107 HOH   HOH A . 
C 3 HOH   42  442 58  HOH   HOH A . 
C 3 HOH   43  443 237 HOH   HOH A . 
C 3 HOH   44  444 62  HOH   HOH A . 
C 3 HOH   45  445 41  HOH   HOH A . 
C 3 HOH   46  446 263 HOH   HOH A . 
C 3 HOH   47  447 68  HOH   HOH A . 
C 3 HOH   48  448 36  HOH   HOH A . 
C 3 HOH   49  449 55  HOH   HOH A . 
C 3 HOH   50  450 3   HOH   HOH A . 
C 3 HOH   51  451 37  HOH   HOH A . 
C 3 HOH   52  452 17  HOH   HOH A . 
C 3 HOH   53  453 87  HOH   HOH A . 
C 3 HOH   54  454 183 HOH   HOH A . 
C 3 HOH   55  455 6   HOH   HOH A . 
C 3 HOH   56  456 97  HOH   HOH A . 
C 3 HOH   57  457 216 HOH   HOH A . 
C 3 HOH   58  458 110 HOH   HOH A . 
C 3 HOH   59  459 127 HOH   HOH A . 
C 3 HOH   60  460 121 HOH   HOH A . 
C 3 HOH   61  461 246 HOH   HOH A . 
C 3 HOH   62  462 12  HOH   HOH A . 
C 3 HOH   63  463 40  HOH   HOH A . 
C 3 HOH   64  464 93  HOH   HOH A . 
C 3 HOH   65  465 4   HOH   HOH A . 
C 3 HOH   66  466 218 HOH   HOH A . 
C 3 HOH   67  467 99  HOH   HOH A . 
C 3 HOH   68  468 67  HOH   HOH A . 
C 3 HOH   69  469 14  HOH   HOH A . 
C 3 HOH   70  470 32  HOH   HOH A . 
C 3 HOH   71  471 152 HOH   HOH A . 
C 3 HOH   72  472 7   HOH   HOH A . 
C 3 HOH   73  473 10  HOH   HOH A . 
C 3 HOH   74  474 22  HOH   HOH A . 
C 3 HOH   75  475 9   HOH   HOH A . 
C 3 HOH   76  476 231 HOH   HOH A . 
C 3 HOH   77  477 57  HOH   HOH A . 
C 3 HOH   78  478 194 HOH   HOH A . 
C 3 HOH   79  479 8   HOH   HOH A . 
C 3 HOH   80  480 61  HOH   HOH A . 
C 3 HOH   81  481 66  HOH   HOH A . 
C 3 HOH   82  482 156 HOH   HOH A . 
C 3 HOH   83  483 142 HOH   HOH A . 
C 3 HOH   84  484 34  HOH   HOH A . 
C 3 HOH   85  485 75  HOH   HOH A . 
C 3 HOH   86  486 262 HOH   HOH A . 
C 3 HOH   87  487 29  HOH   HOH A . 
C 3 HOH   88  488 198 HOH   HOH A . 
C 3 HOH   89  489 174 HOH   HOH A . 
C 3 HOH   90  490 46  HOH   HOH A . 
C 3 HOH   91  491 18  HOH   HOH A . 
C 3 HOH   92  492 112 HOH   HOH A . 
C 3 HOH   93  493 108 HOH   HOH A . 
C 3 HOH   94  494 86  HOH   HOH A . 
C 3 HOH   95  495 173 HOH   HOH A . 
C 3 HOH   96  496 94  HOH   HOH A . 
C 3 HOH   97  497 49  HOH   HOH A . 
C 3 HOH   98  498 76  HOH   HOH A . 
C 3 HOH   99  499 21  HOH   HOH A . 
C 3 HOH   100 500 33  HOH   HOH A . 
C 3 HOH   101 501 137 HOH   HOH A . 
C 3 HOH   102 502 19  HOH   HOH A . 
C 3 HOH   103 503 81  HOH   HOH A . 
C 3 HOH   104 504 188 HOH   HOH A . 
C 3 HOH   105 505 146 HOH   HOH A . 
C 3 HOH   106 506 30  HOH   HOH A . 
C 3 HOH   107 507 175 HOH   HOH A . 
C 3 HOH   108 508 72  HOH   HOH A . 
C 3 HOH   109 509 176 HOH   HOH A . 
C 3 HOH   110 510 125 HOH   HOH A . 
C 3 HOH   111 511 71  HOH   HOH A . 
C 3 HOH   112 512 44  HOH   HOH A . 
C 3 HOH   113 513 51  HOH   HOH A . 
C 3 HOH   114 514 2   HOH   HOH A . 
C 3 HOH   115 515 20  HOH   HOH A . 
C 3 HOH   116 516 190 HOH   HOH A . 
C 3 HOH   117 517 103 HOH   HOH A . 
C 3 HOH   118 518 131 HOH   HOH A . 
C 3 HOH   119 519 42  HOH   HOH A . 
C 3 HOH   120 520 27  HOH   HOH A . 
C 3 HOH   121 521 13  HOH   HOH A . 
C 3 HOH   122 522 111 HOH   HOH A . 
C 3 HOH   123 523 242 HOH   HOH A . 
C 3 HOH   124 524 234 HOH   HOH A . 
C 3 HOH   125 525 79  HOH   HOH A . 
C 3 HOH   126 526 78  HOH   HOH A . 
C 3 HOH   127 527 273 HOH   HOH A . 
C 3 HOH   128 528 25  HOH   HOH A . 
C 3 HOH   129 529 74  HOH   HOH A . 
C 3 HOH   130 530 164 HOH   HOH A . 
C 3 HOH   131 531 101 HOH   HOH A . 
C 3 HOH   132 532 267 HOH   HOH A . 
C 3 HOH   133 533 225 HOH   HOH A . 
C 3 HOH   134 534 35  HOH   HOH A . 
C 3 HOH   135 535 65  HOH   HOH A . 
C 3 HOH   136 536 172 HOH   HOH A . 
C 3 HOH   137 537 230 HOH   HOH A . 
C 3 HOH   138 538 95  HOH   HOH A . 
C 3 HOH   139 539 240 HOH   HOH A . 
C 3 HOH   140 540 105 HOH   HOH A . 
C 3 HOH   141 541 261 HOH   HOH A . 
C 3 HOH   142 542 203 HOH   HOH A . 
C 3 HOH   143 543 63  HOH   HOH A . 
C 3 HOH   144 544 96  HOH   HOH A . 
C 3 HOH   145 545 5   HOH   HOH A . 
C 3 HOH   146 546 73  HOH   HOH A . 
C 3 HOH   147 547 212 HOH   HOH A . 
C 3 HOH   148 548 139 HOH   HOH A . 
C 3 HOH   149 549 104 HOH   HOH A . 
C 3 HOH   150 550 255 HOH   HOH A . 
C 3 HOH   151 551 106 HOH   HOH A . 
C 3 HOH   152 552 207 HOH   HOH A . 
C 3 HOH   153 553 178 HOH   HOH A . 
C 3 HOH   154 554 151 HOH   HOH A . 
C 3 HOH   155 555 115 HOH   HOH A . 
C 3 HOH   156 556 192 HOH   HOH A . 
C 3 HOH   157 557 26  HOH   HOH A . 
C 3 HOH   158 558 256 HOH   HOH A . 
C 3 HOH   159 559 116 HOH   HOH A . 
C 3 HOH   160 560 141 HOH   HOH A . 
C 3 HOH   161 561 54  HOH   HOH A . 
C 3 HOH   162 562 169 HOH   HOH A . 
C 3 HOH   163 563 11  HOH   HOH A . 
C 3 HOH   164 564 24  HOH   HOH A . 
C 3 HOH   165 565 113 HOH   HOH A . 
C 3 HOH   166 566 134 HOH   HOH A . 
C 3 HOH   167 567 235 HOH   HOH A . 
C 3 HOH   168 568 1   HOH   HOH A . 
C 3 HOH   169 569 270 HOH   HOH A . 
C 3 HOH   170 570 248 HOH   HOH A . 
C 3 HOH   171 571 163 HOH   HOH A . 
C 3 HOH   172 572 229 HOH   HOH A . 
C 3 HOH   173 573 38  HOH   HOH A . 
C 3 HOH   174 574 28  HOH   HOH A . 
C 3 HOH   175 575 59  HOH   HOH A . 
C 3 HOH   176 576 236 HOH   HOH A . 
C 3 HOH   177 577 128 HOH   HOH A . 
C 3 HOH   178 578 170 HOH   HOH A . 
C 3 HOH   179 579 201 HOH   HOH A . 
C 3 HOH   180 580 243 HOH   HOH A . 
C 3 HOH   181 581 264 HOH   HOH A . 
C 3 HOH   182 582 275 HOH   HOH A . 
C 3 HOH   183 583 83  HOH   HOH A . 
C 3 HOH   184 584 15  HOH   HOH A . 
C 3 HOH   185 585 244 HOH   HOH A . 
C 3 HOH   186 586 69  HOH   HOH A . 
C 3 HOH   187 587 253 HOH   HOH A . 
C 3 HOH   188 588 91  HOH   HOH A . 
C 3 HOH   189 589 39  HOH   HOH A . 
C 3 HOH   190 590 215 HOH   HOH A . 
C 3 HOH   191 591 70  HOH   HOH A . 
C 3 HOH   192 592 232 HOH   HOH A . 
C 3 HOH   193 593 136 HOH   HOH A . 
C 3 HOH   194 594 238 HOH   HOH A . 
C 3 HOH   195 595 120 HOH   HOH A . 
C 3 HOH   196 596 266 HOH   HOH A . 
C 3 HOH   197 597 239 HOH   HOH A . 
C 3 HOH   198 598 123 HOH   HOH A . 
C 3 HOH   199 599 213 HOH   HOH A . 
C 3 HOH   200 600 271 HOH   HOH A . 
C 3 HOH   201 601 82  HOH   HOH A . 
C 3 HOH   202 602 149 HOH   HOH A . 
C 3 HOH   203 603 161 HOH   HOH A . 
C 3 HOH   204 604 211 HOH   HOH A . 
C 3 HOH   205 605 279 HOH   HOH A . 
C 3 HOH   206 606 31  HOH   HOH A . 
C 3 HOH   207 607 143 HOH   HOH A . 
C 3 HOH   208 608 100 HOH   HOH A . 
C 3 HOH   209 609 226 HOH   HOH A . 
C 3 HOH   210 610 45  HOH   HOH A . 
C 3 HOH   211 611 171 HOH   HOH A . 
C 3 HOH   212 612 43  HOH   HOH A . 
C 3 HOH   213 613 210 HOH   HOH A . 
C 3 HOH   214 614 47  HOH   HOH A . 
C 3 HOH   215 615 162 HOH   HOH A . 
C 3 HOH   216 616 181 HOH   HOH A . 
C 3 HOH   217 617 53  HOH   HOH A . 
C 3 HOH   218 618 117 HOH   HOH A . 
C 3 HOH   219 619 217 HOH   HOH A . 
C 3 HOH   220 620 119 HOH   HOH A . 
C 3 HOH   221 621 166 HOH   HOH A . 
C 3 HOH   222 622 241 HOH   HOH A . 
C 3 HOH   223 623 208 HOH   HOH A . 
C 3 HOH   224 624 260 HOH   HOH A . 
C 3 HOH   225 625 147 HOH   HOH A . 
C 3 HOH   226 626 268 HOH   HOH A . 
C 3 HOH   227 627 259 HOH   HOH A . 
C 3 HOH   228 628 265 HOH   HOH A . 
C 3 HOH   229 629 280 HOH   HOH A . 
C 3 HOH   230 630 88  HOH   HOH A . 
C 3 HOH   231 631 133 HOH   HOH A . 
C 3 HOH   232 632 200 HOH   HOH A . 
C 3 HOH   233 633 179 HOH   HOH A . 
C 3 HOH   234 634 52  HOH   HOH A . 
C 3 HOH   235 635 254 HOH   HOH A . 
C 3 HOH   236 636 124 HOH   HOH A . 
C 3 HOH   237 637 160 HOH   HOH A . 
C 3 HOH   238 638 199 HOH   HOH A . 
C 3 HOH   239 639 247 HOH   HOH A . 
C 3 HOH   240 640 191 HOH   HOH A . 
C 3 HOH   241 641 220 HOH   HOH A . 
C 3 HOH   242 642 168 HOH   HOH A . 
C 3 HOH   243 643 89  HOH   HOH A . 
C 3 HOH   244 644 145 HOH   HOH A . 
C 3 HOH   245 645 129 HOH   HOH A . 
C 3 HOH   246 646 177 HOH   HOH A . 
C 3 HOH   247 647 227 HOH   HOH A . 
C 3 HOH   248 648 158 HOH   HOH A . 
C 3 HOH   249 649 109 HOH   HOH A . 
C 3 HOH   250 650 155 HOH   HOH A . 
C 3 HOH   251 651 189 HOH   HOH A . 
C 3 HOH   252 652 204 HOH   HOH A . 
C 3 HOH   253 653 186 HOH   HOH A . 
C 3 HOH   254 654 98  HOH   HOH A . 
C 3 HOH   255 655 269 HOH   HOH A . 
C 3 HOH   256 656 206 HOH   HOH A . 
C 3 HOH   257 657 195 HOH   HOH A . 
C 3 HOH   258 658 153 HOH   HOH A . 
C 3 HOH   259 659 258 HOH   HOH A . 
C 3 HOH   260 660 167 HOH   HOH A . 
C 3 HOH   261 661 135 HOH   HOH A . 
C 3 HOH   262 662 154 HOH   HOH A . 
C 3 HOH   263 663 257 HOH   HOH A . 
C 3 HOH   264 664 182 HOH   HOH A . 
C 3 HOH   265 665 219 HOH   HOH A . 
C 3 HOH   266 666 251 HOH   HOH A . 
C 3 HOH   267 667 144 HOH   HOH A . 
C 3 HOH   268 668 180 HOH   HOH A . 
C 3 HOH   269 669 233 HOH   HOH A . 
C 3 HOH   270 670 214 HOH   HOH A . 
C 3 HOH   271 671 122 HOH   HOH A . 
C 3 HOH   272 672 197 HOH   HOH A . 
C 3 HOH   273 673 250 HOH   HOH A . 
C 3 HOH   274 674 138 HOH   HOH A . 
C 3 HOH   275 675 159 HOH   HOH A . 
C 3 HOH   276 676 209 HOH   HOH A . 
C 3 HOH   277 677 278 HOH   HOH A . 
C 3 HOH   278 678 187 HOH   HOH A . 
C 3 HOH   279 679 221 HOH   HOH A . 
C 3 HOH   280 680 223 HOH   HOH A . 
C 3 HOH   281 681 224 HOH   HOH A . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 XDS         .           ?               package 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://www.mpimf-heidelberg.mpg.de/~kabsch/xds/     ?   ? 
2 Aimless     0.7.7       23/04/21        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 DIMPLE      .           ?               program 'Marcin Wojdyr'   wojdyr@gmail.com                        phasing           
http://ccp4.github.io/dimple/                       ?   ? 
4 PHENIX      1.20.1_4487 ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                       C++ ? 
5 PDB_EXTRACT 3.28        'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.volume             582913.637 
_cell.length_a           65.731 
_cell.length_b           89.113 
_cell.length_c           99.516 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HBG 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.entry_id                         7HBG 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HBG 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 S 9M' 
_diffrn_detector.pdbx_collection_date   2023-07-23 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HBG 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             54.850 
_reflns.d_resolution_high            1.690 
_reflns.number_obs                   26570 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         79.900 
_reflns.pdbx_Rmerge_I_obs            0.053 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        26.100 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              10.500 
_reflns.pdbx_Rrim_I_all              0.056 
_reflns.pdbx_Rpim_I_all              0.016 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     278346 
_reflns.pdbx_scaling_rejects         2 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.690 1.780  ? 8931  2100 ? 0.386 ? ? ? 4.300  ? 2.900  ? ? ? ? ? ? 44.200 0.440 0.205 0.842 
1 2 5.330 54.850 ? 13717 1140 ? 0.035 ? ? ? 12.000 ? 50.400 ? ? ? ? ? ? 99.100 0.036 0.010 0.999 
# 
_refine.entry_id                                 7HBG 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.91 
_refine.pdbx_overall_phase_error                 19.3070 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_R_factor_obs                          0.1643 
_refine.B_iso_mean                               28.86 
_refine.ls_number_reflns_R_free                  1305 
_refine.ls_percent_reflns_obs                    79.64 
_refine.ls_R_factor_R_work                       0.1637 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.69 
_refine.ls_number_reflns_obs                     26564 
_refine.pdbx_ls_sigma_F                          1.38 
_refine.ls_number_reflns_R_work                  25259 
_refine.ls_d_res_low                             29.61 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1758 
_refine.overall_SU_ML                            0.1386 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         16 
_refine_hist.number_atoms_solvent             281 
_refine_hist.number_atoms_total               1941 
_refine_hist.d_res_high                       1.69 
_refine_hist.d_res_low                        29.61 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           1687 0.0065 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2272 0.9355 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0574 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0084 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 226  7.0380 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' 1.69 1.75  1455 0.2667 42.13 0.3029 83  . . . . . 
'X-RAY DIFFRACTION' 1.75 1.83  1802 0.2098 52.37 0.2347 107 . . . . . 
'X-RAY DIFFRACTION' 1.83 1.93  2080 0.1827 59.49 0.1968 102 . . . . . 
'X-RAY DIFFRACTION' 1.93 2.05  3206 0.1754 92.04 0.1922 160 . . . . . 
'X-RAY DIFFRACTION' 2.05 2.21  3196 0.1628 91.28 0.1895 176 . . . . . 
'X-RAY DIFFRACTION' 2.21 2.43  3065 0.1710 87.24 0.1922 155 . . . . . 
'X-RAY DIFFRACTION' 2.43 2.78  3523 0.1725 99.73 0.1837 179 . . . . . 
'X-RAY DIFFRACTION' 2.78 3.50  3421 0.1611 96.02 0.1772 171 . . . . . 
'X-RAY DIFFRACTION' 3.50 29.61 3511 0.1486 94.73 0.1491 172 . . . . . 
# 
_struct.entry_id                  7HBG 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13237' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HBG 
_struct_keywords.pdbx_keywords   CHAPERONE 
_struct_keywords.text            
'Crystallographic Fragment Screening; Fragment-Based Drug Discovery (FBDD); Heat shock protein 90 (HSP90), CHAPERONE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HS90A_HUMAN 
_struct_ref.pdbx_db_accession          P07900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRT
LTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGG
SFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAE
;
_struct_ref.pdbx_align_begin           9 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HBG 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_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             P07900 
_struct_ref_seq.db_align_beg                  9 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  236 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       9 
_struct_ref_seq.pdbx_auth_seq_align_end       236 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7HBG MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HBG LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HBG GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HBG HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HBG HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HBG HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HBG HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HBG HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HBG HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2  AA2 GLU A 35  ? LEU A 57  ? GLU A 42  LEU A 64  1 ? 23 
HELX_P HELX_P3  AA3 THR A 58  ? ASP A 64  ? THR A 65  ASP A 71  5 ? 7  
HELX_P HELX_P4  AA4 THR A 92  ? ILE A 97  ? THR A 99  ILE A 104 1 ? 6  
HELX_P HELX_P5  AA5 ASN A 98  ? THR A 102 ? ASN A 105 THR A 109 5 ? 5  
HELX_P HELX_P6  AA6 ILE A 103 ? ALA A 117 ? ILE A 110 ALA A 124 1 ? 15 
HELX_P HELX_P7  AA7 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P8  AA8 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P9  AA9 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P10 AB1 GLU A 192 ? GLN A 205 ? GLU A 199 GLN A 212 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_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 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? 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 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
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 PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O THR A 83  ? O THR A 90  N ILE A 74  ? N ILE A 81  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HBG 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 446 ? ? O A HOH 581 ? ? 1.96 
2 1 OE1 A GLU 178 ? ? O A HOH 401 ? ? 2.05 
3 1 O   A HOH 590 ? ? O A HOH 597 ? ? 2.07 
4 1 O   A HOH 496 ? ? O A HOH 530 ? ? 2.16 
5 1 O   A HOH 413 ? ? O A HOH 552 ? ? 2.16 
6 1 O   A HOH 431 ? ? O A HOH 592 ? ? 2.17 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     592 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     651 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   8_444 
_pdbx_validate_symm_contact.dist              2.00 
# 
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 TYR A 38  ? ? -161.02 108.19  
2 1 THR A 94  ? ? -104.23 41.56   
3 1 ILE A 110 ? ? -94.28  57.38   
4 1 ALA A 166 ? ? 60.08   -144.70 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 635 ? C HOH . 
2 1 A HOH 647 ? C HOH . 
3 1 A HOH 663 ? C HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1  ? 'X-RAY DIFFRACTION' refined 12.2224860587  -17.6507140355 -18.8303995049 0.127307370458 0.173663115955 0.191788157068 
0.022639034059    -0.0428867696947 -0.0171308039425  2.96678554047 1.99336934759 6.85187098884 -0.963486396794 -4.2504053525    
0.97416050561   0.106900363732   -0.308113963733 0.0311829872564 0.0176155073637 -0.0646194946538 -0.110293262806   
-0.00923018999629 0.362685541752   -0.0265386961894 
2  ? 'X-RAY DIFFRACTION' refined -5.03881943902 -6.51063415903 -20.4471182454 0.138090102265 0.144122627878 0.175293961402 
-0.00373007121518 0.00341421743243 -0.0398787390495  3.19855727283 7.75571816135 6.98321951857 -3.54724038058  3.3939418579     
-6.12197151792  -0.0392661478364 0.0507990328618 0.129139553331  0.111405732603  -0.0823085434782 0.000938775629202 
-0.305221807975   0.227867133867   0.067481337998   
3  ? 'X-RAY DIFFRACTION' refined -11.2877604816 -15.1047777731 -24.5729997724 0.120161587722 0.136175470655 0.180113597885 
-0.0136208171858  -0.036915240701  -0.0424632247899  2.32163427829 5.82875831318 6.50494528417 -1.26573617359  1.13435731313    
-3.99989373148  0.052801987555   0.160877681683  -0.111873802587 -0.210277570041 0.041448915818   0.278410433043    
0.0825460002764   -0.140737875706  -0.149377952827  
4  ? 'X-RAY DIFFRACTION' refined 3.12786852512  -10.7553375261 -30.1605425798 0.178961835358 0.172114395488 0.175795927935 
0.00738336141496  0.0136256295709  -0.00992439846816 4.52160272071 1.72524379151 1.30467186931 -1.30499141612  0.589146421931   
-0.571116600864 0.0835070923314  0.155710965417  0.254828235294  -0.17653519932  -0.0742966438944 -0.155304308869   
-0.0431405365457  0.125764105676   -0.0243916624205 
5  ? 'X-RAY DIFFRACTION' refined 15.7458105308  -5.06429168957 -14.5952034195 0.205650802116 0.265684367185 0.310482242618 
-0.0259767567591  -0.0173548432583 -0.0428241308426  4.62559189348 2.43581262604 8.90765854154 1.05650700247   -0.93316589235   
3.04622428174   0.263934076521   -0.486820515436 0.465484139066  0.190337823291  0.0724858514119  -0.741753492844   
-0.276258485623   1.18442867872    -0.283925014664  
6  ? 'X-RAY DIFFRACTION' refined 7.95126940487  -5.76796724459 -11.0876602038 0.18081480528  0.311595208327 0.288158433938 
-0.0133551614459  0.0103297714645  -0.0743116382105  4.53195116425 8.20002799644 8.00628334475 4.3639005409    3.49954238907    
1.00675806457   0.213735300924   -1.3065031321   0.679861277935  0.393164621898  -0.261879601124  0.152506714759    
-0.784091443902   0.053865757211   0.0664047268521  
7  ? 'X-RAY DIFFRACTION' refined 0.730525040209 -19.2689078822 -27.8253271093 0.13798674854  0.113852347273 0.176434061037 
-0.00185483821064 -0.0126105439646 -0.030572607461   2.94497979597 1.94628591088 3.65777713828 -1.2733803279   1.02438600481    
-0.447151905507 0.197795766994   0.255712459514  -0.306854537695 -0.235065118757 -0.0698796596721 0.160169757756    0.252536681114 
0.0248928799671  -0.12621634227   
8  ? 'X-RAY DIFFRACTION' refined -2.68668266318 -23.4256716382 -13.572899331  0.189763517938 0.157830367671 0.198699424596 
0.00305753699003  -0.0137111900881 -0.0152865407479  2.93608118834 6.96955340072 2.83195994554 -0.369982360841 -0.677590352413  
-4.10976104219  0.00138457424478 -0.214648500523 -0.279223608966 0.0898270559396 -0.115390851308  -0.0969351175077  0.418248763446 
0.197010939801   0.120105328989   
9  ? 'X-RAY DIFFRACTION' refined -9.90520884516 -14.3133433743 -5.88695385464 0.224151749257 0.243744721951 0.178192333969 
0.00262831916765  0.00462453307873 -0.0086134484493  7.08525484845 2.63323655649 2.64033765948 0.69034602532   0.00925602245816 
-2.51636220686  0.109493627553   -0.480294575875 -0.141719679677 0.434705797881  -0.0217922811107 0.330096328925    
-0.074355765884   -0.0816326020257 -0.114137675602  
10 ? 'X-RAY DIFFRACTION' refined -14.7164545889 -13.553146656  -14.7425470043 0.142256477441 0.183367867804 0.162296660915 
0.0253658929247   0.00892864705188 -0.00220405648292 4.91819196786 4.14904181522 5.94470533661 0.967635549071  -0.0913173873862 
-0.89961800897  0.0365344267678  -0.111052158442 -0.163589471375 0.452467229464  0.0404445978414  0.0325953766362   
-0.147654163346   -0.29895176996   -0.0340795689313 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  1  'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2  2  'X-RAY DIFFRACTION' A 41  A 26  A 64  A 49  . 
;chain 'A' and (resid 41 through 64 )
;
3  3  'X-RAY DIFFRACTION' A 65  A 50  A 93  A 78  . 
;chain 'A' and (resid 65 through 93 )
;
4  4  'X-RAY DIFFRACTION' A 94  A 79  A 110 A 95  . 
;chain 'A' and (resid 94 through 110 )
;
5  5  'X-RAY DIFFRACTION' A 111 A 96  A 124 A 109 . 
;chain 'A' and (resid 111 through 124 )
;
6  6  'X-RAY DIFFRACTION' A 125 A 110 A 136 A 121 . 
;chain 'A' and (resid 125 through 136 )
;
7  7  'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
8  8  'X-RAY DIFFRACTION' A 183 A 168 A 199 A 184 . 
;chain 'A' and (resid 183 through 199 )
;
9  9  'X-RAY DIFFRACTION' A 200 A 185 A 211 A 196 . 
;chain 'A' and (resid 200 through 211 )
;
10 10 'X-RAY DIFFRACTION' A 212 A 197 A 224 A 209 . 
;chain 'A' and (resid 212 through 224 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       681 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.90 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
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 
A1AYB C11  C Y N 1   
A1AYB C12  C Y N 2   
A1AYB C13  C Y N 3   
A1AYB C5   C Y N 4   
A1AYB C1   C N N 5   
A1AYB C2   C N N 6   
A1AYB C3   C Y N 7   
A1AYB C4   C Y N 8   
A1AYB C10  C Y N 9   
A1AYB C6   C Y N 10  
A1AYB C7   C Y N 11  
A1AYB C8   C Y N 12  
A1AYB C9   C Y N 13  
A1AYB N1   N N N 14  
A1AYB N2   N Y N 15  
A1AYB O1   O N N 16  
A1AYB H11  H N N 17  
A1AYB H12  H N N 18  
A1AYB H13  H N N 19  
A1AYB H5   H N N 20  
A1AYB H15  H N N 21  
A1AYB H16  H N N 22  
A1AYB H14  H N N 23  
A1AYB H22  H N N 24  
A1AYB H23  H N N 25  
A1AYB H4   H N N 26  
A1AYB H10  H N N 27  
A1AYB H8   H N N 28  
A1AYB H9   H N N 29  
A1AYB HN13 H N N 30  
ALA   N    N N N 31  
ALA   CA   C N S 32  
ALA   C    C N N 33  
ALA   O    O N N 34  
ALA   CB   C N N 35  
ALA   OXT  O N N 36  
ALA   H    H N N 37  
ALA   H2   H N N 38  
ALA   HA   H N N 39  
ALA   HB1  H N N 40  
ALA   HB2  H N N 41  
ALA   HB3  H N N 42  
ALA   HXT  H N N 43  
ARG   N    N N N 44  
ARG   CA   C N S 45  
ARG   C    C N N 46  
ARG   O    O N N 47  
ARG   CB   C N N 48  
ARG   CG   C N N 49  
ARG   CD   C N N 50  
ARG   NE   N N N 51  
ARG   CZ   C N N 52  
ARG   NH1  N N N 53  
ARG   NH2  N N N 54  
ARG   OXT  O N N 55  
ARG   H    H N N 56  
ARG   H2   H N N 57  
ARG   HA   H N N 58  
ARG   HB2  H N N 59  
ARG   HB3  H N N 60  
ARG   HG2  H N N 61  
ARG   HG3  H N N 62  
ARG   HD2  H N N 63  
ARG   HD3  H N N 64  
ARG   HE   H N N 65  
ARG   HH11 H N N 66  
ARG   HH12 H N N 67  
ARG   HH21 H N N 68  
ARG   HH22 H N N 69  
ARG   HXT  H N N 70  
ASN   N    N N N 71  
ASN   CA   C N S 72  
ASN   C    C N N 73  
ASN   O    O N N 74  
ASN   CB   C N N 75  
ASN   CG   C N N 76  
ASN   OD1  O N N 77  
ASN   ND2  N N N 78  
ASN   OXT  O N N 79  
ASN   H    H N N 80  
ASN   H2   H N N 81  
ASN   HA   H N N 82  
ASN   HB2  H N N 83  
ASN   HB3  H N N 84  
ASN   HD21 H N N 85  
ASN   HD22 H N N 86  
ASN   HXT  H N N 87  
ASP   N    N N N 88  
ASP   CA   C N S 89  
ASP   C    C N N 90  
ASP   O    O N N 91  
ASP   CB   C N N 92  
ASP   CG   C N N 93  
ASP   OD1  O N N 94  
ASP   OD2  O N N 95  
ASP   OXT  O N N 96  
ASP   H    H N N 97  
ASP   H2   H N N 98  
ASP   HA   H N N 99  
ASP   HB2  H N N 100 
ASP   HB3  H N N 101 
ASP   HD2  H N N 102 
ASP   HXT  H N N 103 
GLN   N    N N N 104 
GLN   CA   C N S 105 
GLN   C    C N N 106 
GLN   O    O N N 107 
GLN   CB   C N N 108 
GLN   CG   C N N 109 
GLN   CD   C N N 110 
GLN   OE1  O N N 111 
GLN   NE2  N N N 112 
GLN   OXT  O N N 113 
GLN   H    H N N 114 
GLN   H2   H N N 115 
GLN   HA   H N N 116 
GLN   HB2  H N N 117 
GLN   HB3  H N N 118 
GLN   HG2  H N N 119 
GLN   HG3  H N N 120 
GLN   HE21 H N N 121 
GLN   HE22 H N N 122 
GLN   HXT  H N N 123 
GLU   N    N N N 124 
GLU   CA   C N S 125 
GLU   C    C N N 126 
GLU   O    O N N 127 
GLU   CB   C N N 128 
GLU   CG   C N N 129 
GLU   CD   C N N 130 
GLU   OE1  O N N 131 
GLU   OE2  O N N 132 
GLU   OXT  O N N 133 
GLU   H    H N N 134 
GLU   H2   H N N 135 
GLU   HA   H N N 136 
GLU   HB2  H N N 137 
GLU   HB3  H N N 138 
GLU   HG2  H N N 139 
GLU   HG3  H N N 140 
GLU   HE2  H N N 141 
GLU   HXT  H N N 142 
GLY   N    N N N 143 
GLY   CA   C N N 144 
GLY   C    C N N 145 
GLY   O    O N N 146 
GLY   OXT  O N N 147 
GLY   H    H N N 148 
GLY   H2   H N N 149 
GLY   HA2  H N N 150 
GLY   HA3  H N N 151 
GLY   HXT  H N N 152 
HIS   N    N N N 153 
HIS   CA   C N S 154 
HIS   C    C N N 155 
HIS   O    O N N 156 
HIS   CB   C N N 157 
HIS   CG   C Y N 158 
HIS   ND1  N Y N 159 
HIS   CD2  C Y N 160 
HIS   CE1  C Y N 161 
HIS   NE2  N Y N 162 
HIS   OXT  O N N 163 
HIS   H    H N N 164 
HIS   H2   H N N 165 
HIS   HA   H N N 166 
HIS   HB2  H N N 167 
HIS   HB3  H N N 168 
HIS   HD1  H N N 169 
HIS   HD2  H N N 170 
HIS   HE1  H N N 171 
HIS   HE2  H N N 172 
HIS   HXT  H N N 173 
HOH   O    O N N 174 
HOH   H1   H N N 175 
HOH   H2   H N N 176 
ILE   N    N N N 177 
ILE   CA   C N S 178 
ILE   C    C N N 179 
ILE   O    O N N 180 
ILE   CB   C N S 181 
ILE   CG1  C N N 182 
ILE   CG2  C N N 183 
ILE   CD1  C N N 184 
ILE   OXT  O N N 185 
ILE   H    H N N 186 
ILE   H2   H N N 187 
ILE   HA   H N N 188 
ILE   HB   H N N 189 
ILE   HG12 H N N 190 
ILE   HG13 H N N 191 
ILE   HG21 H N N 192 
ILE   HG22 H N N 193 
ILE   HG23 H N N 194 
ILE   HD11 H N N 195 
ILE   HD12 H N N 196 
ILE   HD13 H N N 197 
ILE   HXT  H N N 198 
LEU   N    N N N 199 
LEU   CA   C N S 200 
LEU   C    C N N 201 
LEU   O    O N N 202 
LEU   CB   C N N 203 
LEU   CG   C N N 204 
LEU   CD1  C N N 205 
LEU   CD2  C N N 206 
LEU   OXT  O N N 207 
LEU   H    H N N 208 
LEU   H2   H N N 209 
LEU   HA   H N N 210 
LEU   HB2  H N N 211 
LEU   HB3  H N N 212 
LEU   HG   H N N 213 
LEU   HD11 H N N 214 
LEU   HD12 H N N 215 
LEU   HD13 H N N 216 
LEU   HD21 H N N 217 
LEU   HD22 H N N 218 
LEU   HD23 H N N 219 
LEU   HXT  H N N 220 
LYS   N    N N N 221 
LYS   CA   C N S 222 
LYS   C    C N N 223 
LYS   O    O N N 224 
LYS   CB   C N N 225 
LYS   CG   C N N 226 
LYS   CD   C N N 227 
LYS   CE   C N N 228 
LYS   NZ   N N N 229 
LYS   OXT  O N N 230 
LYS   H    H N N 231 
LYS   H2   H N N 232 
LYS   HA   H N N 233 
LYS   HB2  H N N 234 
LYS   HB3  H N N 235 
LYS   HG2  H N N 236 
LYS   HG3  H N N 237 
LYS   HD2  H N N 238 
LYS   HD3  H N N 239 
LYS   HE2  H N N 240 
LYS   HE3  H N N 241 
LYS   HZ1  H N N 242 
LYS   HZ2  H N N 243 
LYS   HZ3  H N N 244 
LYS   HXT  H N N 245 
MET   N    N N N 246 
MET   CA   C N S 247 
MET   C    C N N 248 
MET   O    O N N 249 
MET   CB   C N N 250 
MET   CG   C N N 251 
MET   SD   S N N 252 
MET   CE   C N N 253 
MET   OXT  O N N 254 
MET   H    H N N 255 
MET   H2   H N N 256 
MET   HA   H N N 257 
MET   HB2  H N N 258 
MET   HB3  H N N 259 
MET   HG2  H N N 260 
MET   HG3  H N N 261 
MET   HE1  H N N 262 
MET   HE2  H N N 263 
MET   HE3  H N N 264 
MET   HXT  H N N 265 
PHE   N    N N N 266 
PHE   CA   C N S 267 
PHE   C    C N N 268 
PHE   O    O N N 269 
PHE   CB   C N N 270 
PHE   CG   C Y N 271 
PHE   CD1  C Y N 272 
PHE   CD2  C Y N 273 
PHE   CE1  C Y N 274 
PHE   CE2  C Y N 275 
PHE   CZ   C Y N 276 
PHE   OXT  O N N 277 
PHE   H    H N N 278 
PHE   H2   H N N 279 
PHE   HA   H N N 280 
PHE   HB2  H N N 281 
PHE   HB3  H N N 282 
PHE   HD1  H N N 283 
PHE   HD2  H N N 284 
PHE   HE1  H N N 285 
PHE   HE2  H N N 286 
PHE   HZ   H N N 287 
PHE   HXT  H N N 288 
PRO   N    N N N 289 
PRO   CA   C N S 290 
PRO   C    C N N 291 
PRO   O    O N N 292 
PRO   CB   C N N 293 
PRO   CG   C N N 294 
PRO   CD   C N N 295 
PRO   OXT  O N N 296 
PRO   H    H N N 297 
PRO   HA   H N N 298 
PRO   HB2  H N N 299 
PRO   HB3  H N N 300 
PRO   HG2  H N N 301 
PRO   HG3  H N N 302 
PRO   HD2  H N N 303 
PRO   HD3  H N N 304 
PRO   HXT  H N N 305 
SER   N    N N N 306 
SER   CA   C N S 307 
SER   C    C N N 308 
SER   O    O N N 309 
SER   CB   C N N 310 
SER   OG   O N N 311 
SER   OXT  O N N 312 
SER   H    H N N 313 
SER   H2   H N N 314 
SER   HA   H N N 315 
SER   HB2  H N N 316 
SER   HB3  H N N 317 
SER   HG   H N N 318 
SER   HXT  H N N 319 
THR   N    N N N 320 
THR   CA   C N S 321 
THR   C    C N N 322 
THR   O    O N N 323 
THR   CB   C N R 324 
THR   OG1  O N N 325 
THR   CG2  C N N 326 
THR   OXT  O N N 327 
THR   H    H N N 328 
THR   H2   H N N 329 
THR   HA   H N N 330 
THR   HB   H N N 331 
THR   HG1  H N N 332 
THR   HG21 H N N 333 
THR   HG22 H N N 334 
THR   HG23 H N N 335 
THR   HXT  H N N 336 
TRP   N    N N N 337 
TRP   CA   C N S 338 
TRP   C    C N N 339 
TRP   O    O N N 340 
TRP   CB   C N N 341 
TRP   CG   C Y N 342 
TRP   CD1  C Y N 343 
TRP   CD2  C Y N 344 
TRP   NE1  N Y N 345 
TRP   CE2  C Y N 346 
TRP   CE3  C Y N 347 
TRP   CZ2  C Y N 348 
TRP   CZ3  C Y N 349 
TRP   CH2  C Y N 350 
TRP   OXT  O N N 351 
TRP   H    H N N 352 
TRP   H2   H N N 353 
TRP   HA   H N N 354 
TRP   HB2  H N N 355 
TRP   HB3  H N N 356 
TRP   HD1  H N N 357 
TRP   HE1  H N N 358 
TRP   HE3  H N N 359 
TRP   HZ2  H N N 360 
TRP   HZ3  H N N 361 
TRP   HH2  H N N 362 
TRP   HXT  H N N 363 
TYR   N    N N N 364 
TYR   CA   C N S 365 
TYR   C    C N N 366 
TYR   O    O N N 367 
TYR   CB   C N N 368 
TYR   CG   C Y N 369 
TYR   CD1  C Y N 370 
TYR   CD2  C Y N 371 
TYR   CE1  C Y N 372 
TYR   CE2  C Y N 373 
TYR   CZ   C Y N 374 
TYR   OH   O N N 375 
TYR   OXT  O N N 376 
TYR   H    H N N 377 
TYR   H2   H N N 378 
TYR   HA   H N N 379 
TYR   HB2  H N N 380 
TYR   HB3  H N N 381 
TYR   HD1  H N N 382 
TYR   HD2  H N N 383 
TYR   HE1  H N N 384 
TYR   HE2  H N N 385 
TYR   HH   H N N 386 
TYR   HXT  H N N 387 
VAL   N    N N N 388 
VAL   CA   C N S 389 
VAL   C    C N N 390 
VAL   O    O N N 391 
VAL   CB   C N N 392 
VAL   CG1  C N N 393 
VAL   CG2  C N N 394 
VAL   OXT  O N N 395 
VAL   H    H N N 396 
VAL   H2   H N N 397 
VAL   HA   H N N 398 
VAL   HB   H N N 399 
VAL   HG11 H N N 400 
VAL   HG12 H N N 401 
VAL   HG13 H N N 402 
VAL   HG21 H N N 403 
VAL   HG22 H N N 404 
VAL   HG23 H N N 405 
VAL   HXT  H N N 406 
# 
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 
A1AYB C1  N1   sing N N 1   
A1AYB N1  C2   sing N N 2   
A1AYB C2  C3   sing N N 3   
A1AYB C3  C4   doub Y N 4   
A1AYB C3  C13  sing Y N 5   
A1AYB C4  C5   sing Y N 6   
A1AYB C5  C6   doub Y N 7   
A1AYB C6  O1   sing N N 8   
A1AYB C6  C12  sing Y N 9   
A1AYB O1  C7   sing N N 10  
A1AYB C7  C8   doub Y N 11  
A1AYB C7  N2   sing Y N 12  
A1AYB C8  C9   sing Y N 13  
A1AYB C9  C10  doub Y N 14  
A1AYB C10 C11  sing Y N 15  
A1AYB C11 N2   doub Y N 16  
A1AYB C12 C13  doub Y N 17  
A1AYB C11 H11  sing N N 18  
A1AYB C12 H12  sing N N 19  
A1AYB C13 H13  sing N N 20  
A1AYB C5  H5   sing N N 21  
A1AYB C1  H15  sing N N 22  
A1AYB C1  H16  sing N N 23  
A1AYB C1  H14  sing N N 24  
A1AYB C2  H22  sing N N 25  
A1AYB C2  H23  sing N N 26  
A1AYB C4  H4   sing N N 27  
A1AYB C10 H10  sing N N 28  
A1AYB C8  H8   sing N N 29  
A1AYB C9  H9   sing N N 30  
A1AYB N1  HN13 sing N N 31  
ALA   N   CA   sing N N 32  
ALA   N   H    sing N N 33  
ALA   N   H2   sing N N 34  
ALA   CA  C    sing N N 35  
ALA   CA  CB   sing N N 36  
ALA   CA  HA   sing N N 37  
ALA   C   O    doub N N 38  
ALA   C   OXT  sing N N 39  
ALA   CB  HB1  sing N N 40  
ALA   CB  HB2  sing N N 41  
ALA   CB  HB3  sing N N 42  
ALA   OXT HXT  sing N N 43  
ARG   N   CA   sing N N 44  
ARG   N   H    sing N N 45  
ARG   N   H2   sing N N 46  
ARG   CA  C    sing N N 47  
ARG   CA  CB   sing N N 48  
ARG   CA  HA   sing N N 49  
ARG   C   O    doub N N 50  
ARG   C   OXT  sing N N 51  
ARG   CB  CG   sing N N 52  
ARG   CB  HB2  sing N N 53  
ARG   CB  HB3  sing N N 54  
ARG   CG  CD   sing N N 55  
ARG   CG  HG2  sing N N 56  
ARG   CG  HG3  sing N N 57  
ARG   CD  NE   sing N N 58  
ARG   CD  HD2  sing N N 59  
ARG   CD  HD3  sing N N 60  
ARG   NE  CZ   sing N N 61  
ARG   NE  HE   sing N N 62  
ARG   CZ  NH1  sing N N 63  
ARG   CZ  NH2  doub N N 64  
ARG   NH1 HH11 sing N N 65  
ARG   NH1 HH12 sing N N 66  
ARG   NH2 HH21 sing N N 67  
ARG   NH2 HH22 sing N N 68  
ARG   OXT HXT  sing N N 69  
ASN   N   CA   sing N N 70  
ASN   N   H    sing N N 71  
ASN   N   H2   sing N N 72  
ASN   CA  C    sing N N 73  
ASN   CA  CB   sing N N 74  
ASN   CA  HA   sing N N 75  
ASN   C   O    doub N N 76  
ASN   C   OXT  sing N N 77  
ASN   CB  CG   sing N N 78  
ASN   CB  HB2  sing N N 79  
ASN   CB  HB3  sing N N 80  
ASN   CG  OD1  doub N N 81  
ASN   CG  ND2  sing N N 82  
ASN   ND2 HD21 sing N N 83  
ASN   ND2 HD22 sing N N 84  
ASN   OXT HXT  sing N N 85  
ASP   N   CA   sing N N 86  
ASP   N   H    sing N N 87  
ASP   N   H2   sing N N 88  
ASP   CA  C    sing N N 89  
ASP   CA  CB   sing N N 90  
ASP   CA  HA   sing N N 91  
ASP   C   O    doub N N 92  
ASP   C   OXT  sing N N 93  
ASP   CB  CG   sing N N 94  
ASP   CB  HB2  sing N N 95  
ASP   CB  HB3  sing N N 96  
ASP   CG  OD1  doub N N 97  
ASP   CG  OD2  sing N N 98  
ASP   OD2 HD2  sing N N 99  
ASP   OXT HXT  sing N N 100 
GLN   N   CA   sing N N 101 
GLN   N   H    sing N N 102 
GLN   N   H2   sing N N 103 
GLN   CA  C    sing N N 104 
GLN   CA  CB   sing N N 105 
GLN   CA  HA   sing N N 106 
GLN   C   O    doub N N 107 
GLN   C   OXT  sing N N 108 
GLN   CB  CG   sing N N 109 
GLN   CB  HB2  sing N N 110 
GLN   CB  HB3  sing N N 111 
GLN   CG  CD   sing N N 112 
GLN   CG  HG2  sing N N 113 
GLN   CG  HG3  sing N N 114 
GLN   CD  OE1  doub N N 115 
GLN   CD  NE2  sing N N 116 
GLN   NE2 HE21 sing N N 117 
GLN   NE2 HE22 sing N N 118 
GLN   OXT HXT  sing N N 119 
GLU   N   CA   sing N N 120 
GLU   N   H    sing N N 121 
GLU   N   H2   sing N N 122 
GLU   CA  C    sing N N 123 
GLU   CA  CB   sing N N 124 
GLU   CA  HA   sing N N 125 
GLU   C   O    doub N N 126 
GLU   C   OXT  sing N N 127 
GLU   CB  CG   sing N N 128 
GLU   CB  HB2  sing N N 129 
GLU   CB  HB3  sing N N 130 
GLU   CG  CD   sing N N 131 
GLU   CG  HG2  sing N N 132 
GLU   CG  HG3  sing N N 133 
GLU   CD  OE1  doub N N 134 
GLU   CD  OE2  sing N N 135 
GLU   OE2 HE2  sing N N 136 
GLU   OXT HXT  sing N N 137 
GLY   N   CA   sing N N 138 
GLY   N   H    sing N N 139 
GLY   N   H2   sing N N 140 
GLY   CA  C    sing N N 141 
GLY   CA  HA2  sing N N 142 
GLY   CA  HA3  sing N N 143 
GLY   C   O    doub N N 144 
GLY   C   OXT  sing N N 145 
GLY   OXT HXT  sing N N 146 
HIS   N   CA   sing N N 147 
HIS   N   H    sing N N 148 
HIS   N   H2   sing N N 149 
HIS   CA  C    sing N N 150 
HIS   CA  CB   sing N N 151 
HIS   CA  HA   sing N N 152 
HIS   C   O    doub N N 153 
HIS   C   OXT  sing N N 154 
HIS   CB  CG   sing N N 155 
HIS   CB  HB2  sing N N 156 
HIS   CB  HB3  sing N N 157 
HIS   CG  ND1  sing Y N 158 
HIS   CG  CD2  doub Y N 159 
HIS   ND1 CE1  doub Y N 160 
HIS   ND1 HD1  sing N N 161 
HIS   CD2 NE2  sing Y N 162 
HIS   CD2 HD2  sing N N 163 
HIS   CE1 NE2  sing Y N 164 
HIS   CE1 HE1  sing N N 165 
HIS   NE2 HE2  sing N N 166 
HIS   OXT HXT  sing N N 167 
HOH   O   H1   sing N N 168 
HOH   O   H2   sing N N 169 
ILE   N   CA   sing N N 170 
ILE   N   H    sing N N 171 
ILE   N   H2   sing N N 172 
ILE   CA  C    sing N N 173 
ILE   CA  CB   sing N N 174 
ILE   CA  HA   sing N N 175 
ILE   C   O    doub N N 176 
ILE   C   OXT  sing N N 177 
ILE   CB  CG1  sing N N 178 
ILE   CB  CG2  sing N N 179 
ILE   CB  HB   sing N N 180 
ILE   CG1 CD1  sing N N 181 
ILE   CG1 HG12 sing N N 182 
ILE   CG1 HG13 sing N N 183 
ILE   CG2 HG21 sing N N 184 
ILE   CG2 HG22 sing N N 185 
ILE   CG2 HG23 sing N N 186 
ILE   CD1 HD11 sing N N 187 
ILE   CD1 HD12 sing N N 188 
ILE   CD1 HD13 sing N N 189 
ILE   OXT HXT  sing N N 190 
LEU   N   CA   sing N N 191 
LEU   N   H    sing N N 192 
LEU   N   H2   sing N N 193 
LEU   CA  C    sing N N 194 
LEU   CA  CB   sing N N 195 
LEU   CA  HA   sing N N 196 
LEU   C   O    doub N N 197 
LEU   C   OXT  sing N N 198 
LEU   CB  CG   sing N N 199 
LEU   CB  HB2  sing N N 200 
LEU   CB  HB3  sing N N 201 
LEU   CG  CD1  sing N N 202 
LEU   CG  CD2  sing N N 203 
LEU   CG  HG   sing N N 204 
LEU   CD1 HD11 sing N N 205 
LEU   CD1 HD12 sing N N 206 
LEU   CD1 HD13 sing N N 207 
LEU   CD2 HD21 sing N N 208 
LEU   CD2 HD22 sing N N 209 
LEU   CD2 HD23 sing N N 210 
LEU   OXT HXT  sing N N 211 
LYS   N   CA   sing N N 212 
LYS   N   H    sing N N 213 
LYS   N   H2   sing N N 214 
LYS   CA  C    sing N N 215 
LYS   CA  CB   sing N N 216 
LYS   CA  HA   sing N N 217 
LYS   C   O    doub N N 218 
LYS   C   OXT  sing N N 219 
LYS   CB  CG   sing N N 220 
LYS   CB  HB2  sing N N 221 
LYS   CB  HB3  sing N N 222 
LYS   CG  CD   sing N N 223 
LYS   CG  HG2  sing N N 224 
LYS   CG  HG3  sing N N 225 
LYS   CD  CE   sing N N 226 
LYS   CD  HD2  sing N N 227 
LYS   CD  HD3  sing N N 228 
LYS   CE  NZ   sing N N 229 
LYS   CE  HE2  sing N N 230 
LYS   CE  HE3  sing N N 231 
LYS   NZ  HZ1  sing N N 232 
LYS   NZ  HZ2  sing N N 233 
LYS   NZ  HZ3  sing N N 234 
LYS   OXT HXT  sing N N 235 
MET   N   CA   sing N N 236 
MET   N   H    sing N N 237 
MET   N   H2   sing N N 238 
MET   CA  C    sing N N 239 
MET   CA  CB   sing N N 240 
MET   CA  HA   sing N N 241 
MET   C   O    doub N N 242 
MET   C   OXT  sing N N 243 
MET   CB  CG   sing N N 244 
MET   CB  HB2  sing N N 245 
MET   CB  HB3  sing N N 246 
MET   CG  SD   sing N N 247 
MET   CG  HG2  sing N N 248 
MET   CG  HG3  sing N N 249 
MET   SD  CE   sing N N 250 
MET   CE  HE1  sing N N 251 
MET   CE  HE2  sing N N 252 
MET   CE  HE3  sing N N 253 
MET   OXT HXT  sing N N 254 
PHE   N   CA   sing N N 255 
PHE   N   H    sing N N 256 
PHE   N   H2   sing N N 257 
PHE   CA  C    sing N N 258 
PHE   CA  CB   sing N N 259 
PHE   CA  HA   sing N N 260 
PHE   C   O    doub N N 261 
PHE   C   OXT  sing N N 262 
PHE   CB  CG   sing N N 263 
PHE   CB  HB2  sing N N 264 
PHE   CB  HB3  sing N N 265 
PHE   CG  CD1  doub Y N 266 
PHE   CG  CD2  sing Y N 267 
PHE   CD1 CE1  sing Y N 268 
PHE   CD1 HD1  sing N N 269 
PHE   CD2 CE2  doub Y N 270 
PHE   CD2 HD2  sing N N 271 
PHE   CE1 CZ   doub Y N 272 
PHE   CE1 HE1  sing N N 273 
PHE   CE2 CZ   sing Y N 274 
PHE   CE2 HE2  sing N N 275 
PHE   CZ  HZ   sing N N 276 
PHE   OXT HXT  sing N N 277 
PRO   N   CA   sing N N 278 
PRO   N   CD   sing N N 279 
PRO   N   H    sing N N 280 
PRO   CA  C    sing N N 281 
PRO   CA  CB   sing N N 282 
PRO   CA  HA   sing N N 283 
PRO   C   O    doub N N 284 
PRO   C   OXT  sing N N 285 
PRO   CB  CG   sing N N 286 
PRO   CB  HB2  sing N N 287 
PRO   CB  HB3  sing N N 288 
PRO   CG  CD   sing N N 289 
PRO   CG  HG2  sing N N 290 
PRO   CG  HG3  sing N N 291 
PRO   CD  HD2  sing N N 292 
PRO   CD  HD3  sing N N 293 
PRO   OXT HXT  sing N N 294 
SER   N   CA   sing N N 295 
SER   N   H    sing N N 296 
SER   N   H2   sing N N 297 
SER   CA  C    sing N N 298 
SER   CA  CB   sing N N 299 
SER   CA  HA   sing N N 300 
SER   C   O    doub N N 301 
SER   C   OXT  sing N N 302 
SER   CB  OG   sing N N 303 
SER   CB  HB2  sing N N 304 
SER   CB  HB3  sing N N 305 
SER   OG  HG   sing N N 306 
SER   OXT HXT  sing N N 307 
THR   N   CA   sing N N 308 
THR   N   H    sing N N 309 
THR   N   H2   sing N N 310 
THR   CA  C    sing N N 311 
THR   CA  CB   sing N N 312 
THR   CA  HA   sing N N 313 
THR   C   O    doub N N 314 
THR   C   OXT  sing N N 315 
THR   CB  OG1  sing N N 316 
THR   CB  CG2  sing N N 317 
THR   CB  HB   sing N N 318 
THR   OG1 HG1  sing N N 319 
THR   CG2 HG21 sing N N 320 
THR   CG2 HG22 sing N N 321 
THR   CG2 HG23 sing N N 322 
THR   OXT HXT  sing N N 323 
TRP   N   CA   sing N N 324 
TRP   N   H    sing N N 325 
TRP   N   H2   sing N N 326 
TRP   CA  C    sing N N 327 
TRP   CA  CB   sing N N 328 
TRP   CA  HA   sing N N 329 
TRP   C   O    doub N N 330 
TRP   C   OXT  sing N N 331 
TRP   CB  CG   sing N N 332 
TRP   CB  HB2  sing N N 333 
TRP   CB  HB3  sing N N 334 
TRP   CG  CD1  doub Y N 335 
TRP   CG  CD2  sing Y N 336 
TRP   CD1 NE1  sing Y N 337 
TRP   CD1 HD1  sing N N 338 
TRP   CD2 CE2  doub Y N 339 
TRP   CD2 CE3  sing Y N 340 
TRP   NE1 CE2  sing Y N 341 
TRP   NE1 HE1  sing N N 342 
TRP   CE2 CZ2  sing Y N 343 
TRP   CE3 CZ3  doub Y N 344 
TRP   CE3 HE3  sing N N 345 
TRP   CZ2 CH2  doub Y N 346 
TRP   CZ2 HZ2  sing N N 347 
TRP   CZ3 CH2  sing Y N 348 
TRP   CZ3 HZ3  sing N N 349 
TRP   CH2 HH2  sing N N 350 
TRP   OXT HXT  sing N N 351 
TYR   N   CA   sing N N 352 
TYR   N   H    sing N N 353 
TYR   N   H2   sing N N 354 
TYR   CA  C    sing N N 355 
TYR   CA  CB   sing N N 356 
TYR   CA  HA   sing N N 357 
TYR   C   O    doub N N 358 
TYR   C   OXT  sing N N 359 
TYR   CB  CG   sing N N 360 
TYR   CB  HB2  sing N N 361 
TYR   CB  HB3  sing N N 362 
TYR   CG  CD1  doub Y N 363 
TYR   CG  CD2  sing Y N 364 
TYR   CD1 CE1  sing Y N 365 
TYR   CD1 HD1  sing N N 366 
TYR   CD2 CE2  doub Y N 367 
TYR   CD2 HD2  sing N N 368 
TYR   CE1 CZ   doub Y N 369 
TYR   CE1 HE1  sing N N 370 
TYR   CE2 CZ   sing Y N 371 
TYR   CE2 HE2  sing N N 372 
TYR   CZ  OH   sing N N 373 
TYR   OH  HH   sing N N 374 
TYR   OXT HXT  sing N N 375 
VAL   N   CA   sing N N 376 
VAL   N   H    sing N N 377 
VAL   N   H2   sing N N 378 
VAL   CA  C    sing N N 379 
VAL   CA  CB   sing N N 380 
VAL   CA  HA   sing N N 381 
VAL   C   O    doub N N 382 
VAL   C   OXT  sing N N 383 
VAL   CB  CG1  sing N N 384 
VAL   CB  CG2  sing N N 385 
VAL   CB  HB   sing N N 386 
VAL   CG1 HG11 sing N N 387 
VAL   CG1 HG12 sing N N 388 
VAL   CG1 HG13 sing N N 389 
VAL   CG2 HG21 sing N N 390 
VAL   CG2 HG22 sing N N 391 
VAL   CG2 HG23 sing N N 392 
VAL   OXT HXT  sing N N 393 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2021YFC2301405 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         'Crystallographic fragment screening of Human heat shock protein 90' 
_pdbx_deposit_group.group_description   
;Heat shock protein 90 (HSP90) is one of the most active molecular chaperones in cells. It plays a vital role in the cell maturation process and serves as a molecular chaperone involved in many oncogenic proteins folding, assembly and stabilization. Many HSP90 client proteins are kinases or transcription factors involved in signal transduction pathways and are key regulatory factors in tumor growth and maintenance. Therefore, HSP90 inhibitors can be used as drugs for cancer treatment.
;
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002298 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    7HBG 
_atom_sites.fract_transf_matrix[1][1]   0.015214 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011222 
_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]   0.010049 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU   A 1 9   ? 4.21417   -28.49369 -39.18912 1.000 45.25695 ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.44304   -27.72440 -39.20683 1.000 52.67213 ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 5.62678   -26.94046 -37.91468 1.000 47.91393 ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 4.89971   -25.98522 -37.64465 1.000 46.48925 ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.47136   -26.76019 -40.40369 1.000 55.50080 ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 6.60322   -25.71872 -40.36936 1.000 74.55438 ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 6.18601   -24.37702 -40.97063 1.000 89.21763 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 4.99872   -24.23573 -41.32760 1.000 86.79938 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 7.03111   -23.46279 -41.10188 1.000 89.64066 ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 6.60356   -27.34468 -37.10844 1.000 37.82835 ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 6.88192   -26.72389 -35.81577 1.000 33.85260 ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.24416   -26.04956 -35.89374 1.000 35.34964 ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.23574   -26.69184 -36.25290 1.000 30.19318 ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 6.85486   -27.76425 -34.68361 1.000 36.49475 ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.19747   -27.11574 -33.36290 1.000 30.35167 ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 5.50452   -28.44973 -34.63161 1.000 45.17022 ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.29837   -24.76573 -35.56000 1.000 26.18255 ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.55955   -24.03562 -35.49820 1.000 22.97205 ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 9.97371   -23.83423 -34.04889 1.000 21.99591 ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.15923   -23.44626 -33.20930 1.000 20.62561 ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.45657   -22.67947 -36.19760 1.000 24.36762 ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.08552   -22.75721 -37.65917 1.000 28.47242 ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 8.96535   -21.38151 -38.29027 1.000 38.87111 ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 7.93319   -20.72030 -38.05656 1.000 39.31135 ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 9.88530   -20.97140 -39.02871 1.000 44.38829 ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.24623  -24.09217 -33.76151 1.000 20.79527 ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 11.78979  -23.95673 -32.41752 1.000 18.07025 ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 12.78844  -22.80879 -32.39893 1.000 19.44593 ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 13.67750  -22.74273 -33.25865 1.000 17.97509 ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.46718  -25.25346 -31.96212 1.000 18.46789 ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.55790  -26.35405 -32.11579 1.000 22.13184 ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 12.91815  -25.14596 -30.48856 1.000 18.00502 ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 12.64229  -21.92495 -31.42016 1.000 19.35384 ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.45279  -20.72892 -31.26832 1.000 17.60233 ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.12663  -20.72602 -29.90633 1.000 21.76436 ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.59414  -21.26794 -28.93437 1.000 20.20123 ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.59656  -19.45661 -31.37355 1.000 17.10115 ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 11.85715  -19.31317 -32.67465 1.000 21.25602 ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.62952  -19.94304 -32.86923 1.000 20.98464 ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.37022  -18.52447 -33.69412 1.000 23.67293 ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 9.94176   -19.80028 -34.05927 1.000 24.25243 ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 11.68360  -18.38386 -34.88534 1.000 26.30420 ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.46843  -19.02174 -35.06718 1.000 27.60419 ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.29237  -20.08279 -29.82834 1.000 16.02124 ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 15.92676  -19.82801 -28.54220 1.000 16.68663 ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.44805  -18.48709 -27.99640 1.000 19.72730 ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.34769  -17.50582 -28.73604 1.000 20.09470 ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.45164  -19.83453 -28.68686 1.000 20.45207 ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.10803  -18.45719 -26.70424 1.000 19.07170 ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 14.90050  -17.18285 -26.02608 1.000 19.51373 ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.18449  -16.36604 -26.08991 1.000 17.39595 ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.28740  -16.91049 -25.96211 1.000 20.95513 ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.53177  -17.40369 -24.55193 1.000 19.85089 ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.12850  -17.91238 -24.32755 1.000 18.41454 ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.02932  -17.12142 -24.61477 1.000 21.74744 ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 12.92483  -19.18125 -23.80173 1.000 18.16650 ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.72923  -17.58529 -24.38728 1.000 17.44136 ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.63851  -19.66850 -23.58593 1.000 19.62247 ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.54086  -18.86786 -23.87107 1.000 15.71091 ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.05026  -15.05914 -26.29105 1.000 20.37130 ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.18526  -14.18450 -26.03180 1.000 22.90106 ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.70951  -14.44066 -24.62529 1.000 22.88312 ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 16.95127  -14.77266 -23.70861 1.000 20.62806 ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.79504  -12.71979 -26.17277 1.000 26.48439 ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.43119  -12.28946 -27.56674 1.000 30.31697 ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 15.87355  -10.87340 -27.56435 1.000 40.07829 ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.67758  -10.67900 -27.37985 1.000 40.20791 ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.74269  -9.88067  -27.73157 1.000 39.60787 ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.02242  -14.27790 -24.46148 1.000 21.58348 ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.66265  -14.60103 -23.18996 1.000 26.35339 ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 18.99131  -13.89968 -22.01668 1.000 27.23128 ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 18.78325  -14.50552 -20.96173 1.000 26.42203 ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.14677  -14.23502 -23.24661 1.000 28.98171 ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.65151  -12.62042 -22.17538 1.000 23.60710 ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.10329  -11.86839 -21.05062 1.000 22.80226 ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.72612  -12.38351 -20.64901 1.000 21.43447 ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.38686  -12.38446 -19.45260 1.000 22.62215 ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.05174  -10.38043 -21.40337 1.000 32.46421 ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.42350  -9.73695  -21.67849 1.000 35.05068 ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 19.96809  -9.97150  -23.08935 1.000 41.88110 ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.34320  -10.69645 -23.90054 1.000 29.81162 ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.04046  -9.40888  -23.39299 1.000 46.02594 ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 15.93379  -12.83586 -21.62240 1.000 22.47108 ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.61554  -13.39168 -21.32307 1.000 20.61961 ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.76591  -14.76070 -20.67204 1.000 20.93892 ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.03032  -15.11073 -19.74068 1.000 22.33494 ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.75059  -13.45044 -22.60144 1.000 22.14477 ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.23627  -12.05209 -22.98716 1.000 23.91279 ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.53994  -14.37538 -22.40601 1.000 24.81942 ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.29826  -11.04987 -23.44528 1.000 33.30099 ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.74725  -15.54300 -21.11933 1.000 20.95008 ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.01453  -16.80790 -20.44865 1.000 20.42963 ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.40122  -16.57657 -18.98974 1.000 20.63239 ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 15.96547  -17.32440 -18.10564 1.000 22.43664 ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.10313  -17.58345 -21.19066 1.000 21.95811 ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.20120  -15.53423 -18.71326 1.000 21.80218 ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.56638  -15.23276 -17.32430 1.000 19.11382 ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.35400  -14.80101 -16.51483 1.000 26.58790 ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.22579  -15.16876 -15.34254 1.000 26.39034 ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.64672  -14.14374 -17.24600 1.000 27.88300 ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 19.78086  -14.25349 -18.24488 1.000 43.17081 ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.71565  -13.04227 -18.25425 1.000 55.47785 ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 20.47768  -12.04111 -17.56821 1.000 50.36395 ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 21.78025  -13.12877 -19.05272 1.000 56.61130 ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.45999  -14.00688 -17.11817 1.000 21.95912 ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.23457  -13.60966 -16.42469 1.000 22.06087 ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.40546  -14.82610 -16.04876 1.000 21.20622 ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 12.89610  -14.92877 -14.92311 1.000 22.03061 ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.41165  -12.66807 -17.30762 1.000 24.19567 ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.01700  -12.31829 -16.77790 1.000 23.51903 ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.11428  -11.46394 -15.51555 1.000 29.26308 ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.18578  -11.62869 -17.85297 1.000 23.29345 ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.27913  -15.77217 -16.97233 1.000 19.45722 ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.44509  -16.93922 -16.71894 1.000 18.78164 ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.06784  -17.82029 -15.63858 1.000 21.25618 ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.36328  -18.33644 -14.76265 1.000 21.31410 ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.25079  -17.71149 -18.02581 1.000 18.55187 ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.13973  -17.12015 -18.89305 1.000 18.44754 ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.17928  -17.77760 -20.57494 1.000 21.51132 ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.03325  -19.11890 -20.32713 1.000 26.60240 ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.39194  -17.97418 -15.66664 1.000 20.84844 ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.08428  -18.74621 -14.63878 1.000 22.71950 ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 14.92606  -18.10309 -13.26847 1.000 28.53006 ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.76041  -18.80466 -12.26156 1.000 28.90818 ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.56189  -18.88948 -15.01446 1.000 28.35479 ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.21977  -19.82802 -14.18480 1.000 52.91859 ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 14.96931  -16.76611 -13.20572 1.000 23.12029 ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.77124  -16.09060 -11.92889 1.000 26.13397 ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.35746  -16.31404 -11.40442 1.000 27.22726 ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.15755  -16.53167 -10.20214 1.000 25.76762 ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.07357  -14.59948 -12.07793 1.000 30.74410 ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 14.80189  -13.68139 -10.87464 1.000 33.83458 ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 15.73404  -12.49543 -10.95025 1.000 38.09391 ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 13.35837  -13.19139 -10.81742 1.000 35.98772 ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.36349  -16.24914 -12.28761 1.000 22.22283 ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 10.98185  -16.43721 -11.85719 1.000 26.47577 ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.76557  -17.86378 -11.36708 1.000 26.91344 ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.02476  -18.10461 -10.40517 1.000 24.83285 ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.02860  -16.07056 -13.00477 1.000 20.49618 ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.01793  -14.54557 -13.21028 1.000 23.03566 ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.61880   -16.62275 -12.75846 1.000 21.87663 ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.42816   -14.10786 -14.56241 1.000 24.32113 ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.42149  -18.82864 -12.00223 1.000 23.05049 ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.21051  -20.22655 -11.63821 1.000 27.07865 ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 11.97433  -20.59630 -10.37456 1.000 32.24379 ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.49310  -21.39684 -9.56646  1.000 33.43779 ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.60582  -21.12825 -12.81960 1.000 25.89212 ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.55302  -21.00691 -13.92415 1.000 21.19744 ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.79475  -22.58391 -12.37429 1.000 30.42093 ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.06173  -21.40465 -15.28922 1.000 27.65918 ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.14855  -20.01219 -10.15690 1.000 25.94577 ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.05480  -20.52017 -9.13572  1.000 28.61330 ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.12196  -19.66610 -7.87783  1.000 39.99761 ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.64845  -20.14039 -6.86445  1.000 38.46838 ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.45860  -20.67817 -9.72350  1.000 34.28234 ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.50785  -21.74807 -10.78681 1.000 43.37968 ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 14.81788  -22.76634 -10.68659 1.000 45.88717 ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.31010  -21.52461 -11.81776 1.000 43.32671 ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.62630  -18.43060 -7.90440  1.000 29.55153 ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.65759  -17.60160 -6.70378  1.000 28.20457 ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.53708  -18.01109 -5.75532  1.000 27.86791 ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.38216  -18.14487 -6.17274  1.000 29.74495 ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.52388  -16.11751 -7.05401  1.000 32.10023 ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.56895  -15.73895 -7.95722  1.000 34.18643 ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.61691  -15.25374 -5.79249  1.000 36.51744 ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.87408  -18.20396 -4.47967  1.000 27.30970 ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.83383  -18.47328 -3.49313  1.000 30.36065 ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 10.98109  -17.22409 -3.28676  1.000 30.34868 ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.48925  -16.17355 -2.87889  1.000 30.23770 ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.44162  -18.92628 -2.17340  1.000 29.74271 ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.41484  -19.20531 -1.11621  1.000 32.47573 ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.65394  -20.36488 -1.15917  1.000 38.50639 ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.19032  -18.29879 -0.09065  1.000 35.91885 ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.69806   -20.62612 -0.18002  1.000 32.45859 ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.22992  -18.54688 0.88079   1.000 31.78992 ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.48519   -19.71230 0.83596   1.000 32.96695 ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.67873   -17.34011 -3.53971  1.000 26.08780 ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.79903   -16.17333 -3.50365  1.000 22.45938 ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.37442   -16.69456 -3.35790  1.000 21.92953 ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.82716   -17.25377 -4.30949  1.000 24.41320 ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 8.95789   -15.33221 -4.77538  1.000 27.82935 ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.07210   -14.11148 -4.78420  1.000 24.47384 ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.35127   -13.03966 -3.94430  1.000 33.93530 ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 6.94648   -14.03371 -5.61083  1.000 27.26288 ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.55069   -11.92200 -3.91446  1.000 37.55082 ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.12799   -12.89738 -5.58979  1.000 31.82690 ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.44587   -11.85098 -4.73546  1.000 29.80450 ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.67625   -10.71091 -4.67358  1.000 40.72878 ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.78008   -16.51276 -2.17701  1.000 23.92657 ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.53513   -17.20436 -1.86437  1.000 22.17560 ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.30348   -16.56623 -2.49770  1.000 27.24047 ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.28678   -17.25412 -2.65657  1.000 25.10320 ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.34149   -17.27063 -0.34669  1.000 23.66126 ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.40488   -17.99078 0.25421   1.000 25.59768 ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.36729   -15.28316 -2.86151  1.000 22.71510 ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.19891   -14.52337 -3.32137  1.000 22.50932 ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 2.92284   -14.78068 -4.81116  1.000 22.38676 ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 2.87486   -13.87457 -5.64494  1.000 24.17824 ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.43067   -13.04284 -3.02112  1.000 28.37851 ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.26542   -12.14623 -3.43103  1.000 28.85986 ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.10181   -12.51513 -3.29628  1.000 28.46842 ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.58698   -10.93706 -3.89084  1.000 28.45669 ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.72358   -16.05974 -5.13840  1.000 20.81391 ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.60285   -16.46080 -6.53981  1.000 18.71425 ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.31620   -15.98055 -7.19646  1.000 19.42396 ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.27330   -15.88803 -8.43214  1.000 18.17348 ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.69345   -17.98688 -6.65546  1.000 20.31071 ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.06668   -18.57338 -6.33650  1.000 22.71679 ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.01808   -20.10109 -6.40443  1.000 25.38681 ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.38607   -20.73173 -6.13911  1.000 23.49688 ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.30264   -20.65732 -7.33278  1.000 21.82558 ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.28020   -15.66919 -6.40702  1.000 19.59014 ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -1.03698  -15.33831 -6.95198  1.000 19.29925 ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -1.00634  -14.16081 -7.92536  1.000 25.60740 ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.95140  -13.99406 -8.71077  1.000 19.45026 ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -2.01383  -15.04108 -5.80443  1.000 19.79481 ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.94530  -13.60638 -5.27248  1.000 21.79041 ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.73034  -13.36738 -3.97663  1.000 36.35415 ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -3.10239  -14.33786 -3.28769  1.000 33.75132 ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -2.99981  -12.18644 -3.66739  1.000 49.30961 ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.04689   -13.33654 -7.89867  1.000 18.55994 ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.07751   -12.15349 -8.75192  1.000 17.83528 ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.10933   -12.51231 -10.23152 1.000 17.74321 ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? -0.19417  -11.65533 -11.07042 1.000 19.13566 ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.25757   -11.23067 -8.35672  1.000 23.23263 ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.61055   -11.93604 -8.50592  1.000 28.77247 ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 1.07055   -10.71748 -6.93736  1.000 27.22678 ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.27295   -11.69712 -9.84380  1.000 33.83414 ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.44808   -13.76129 -10.58432 1.000 17.37492 ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.42318   -14.14602 -11.99912 1.000 15.09061 ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.92473  -13.82519 -12.62032 1.000 16.53116 ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.99939  -13.39647 -13.77592 1.000 17.11414 ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.73904   -15.64589 -12.18108 1.000 16.74153 ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.45044  -16.55076 -11.96142 1.000 17.20791 ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.75686  -17.01096 -10.68610 1.000 16.70010 ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.28308  -16.91871 -13.01676 1.000 17.58490 ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.87920  -17.82430 -10.46926 1.000 21.12546 ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.40401  -17.70902 -12.79597 1.000 18.76855 ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.69679  -18.16837 -11.53435 1.000 17.66135 ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -2.00911  -14.01832 -11.86459 1.000 16.15665 ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.32082  -13.86793 -12.47399 1.000 16.11376 ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.65030  -12.39668 -12.68480 1.000 19.57838 ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.25052  -12.02933 -13.70147 1.000 19.04639 ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.37527  -14.55973 -11.60788 1.000 17.04076 ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.80434  -14.55928 -12.17242 1.000 19.36031 ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.83244  -15.19970 -13.57729 1.000 20.69107 ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.76739  -15.24390 -11.22260 1.000 21.41028 ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.25291  -11.54884 -11.73594 1.000 16.47053 ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.38302  -10.10695 -11.90774 1.000 18.18487 ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.65952  -9.65929  -13.16786 1.000 17.50309 ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -3.17558  -8.84307  -13.94084 1.000 18.93444 ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.81446  -9.38548  -10.68145 1.000 19.33214 ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.75803  -7.87301  -10.81218 1.000 27.25522 ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -2.07617  -7.24526  -9.61073  1.000 26.92708 ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.63429  -7.48394  -9.61952  1.000 27.58207 ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.17077   -7.25239  -8.59165  1.000 34.37332 ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.28776  -6.76647  -7.44725  1.000 35.34926 ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.46890   -7.51572  -8.71231  1.000 36.38536 ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.45464  -10.18656 -13.38594 1.000 16.61398 ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.64132  -9.73621  -14.50675 1.000 15.86601 ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.24990  -10.16846 -15.83163 1.000 16.39275 ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -1.24819  -9.39751  -16.79609 1.000 19.22581 ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.79063   -10.27142 -14.36996 1.000 17.05042 ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.61378   -9.67508  -13.22749 1.000 20.00931 ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.41751   -8.17377  -13.02783 1.000 30.51200 ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.45976   -7.42292  -14.02136 1.000 24.65362 ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.28752   -7.73270  -11.86027 1.000 33.69817 ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.77370  -11.39650 -15.90747 1.000 14.58311 ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.35323  -11.87095 -17.16517 1.000 16.95096 ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.67893  -11.18372 -17.45746 1.000 18.07118 ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.99173  -10.88862 -18.61921 1.000 18.89367 ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.52712  -13.38842 -17.12937 1.000 17.64383 ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.20044  -14.15763 -17.09556 1.000 15.56394 ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.46866  -15.66239 -16.90462 1.000 17.73565 ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.32098  -13.90549 -18.33025 1.000 20.10568 ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.47532  -10.91789 -16.42139 1.000 16.32228 ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.70779  -10.16525 -16.62725 1.000 16.98222 ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.38821  -8.74550  -17.06987 1.000 20.58691 ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -6.06665  -8.18188  -17.93950 1.000 17.82773 ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.56650  -10.19242 -15.34808 1.000 19.26472 ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -7.17399  -11.59195 -15.16665 1.000 18.54996 ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.66090  -9.12217  -15.39840 1.000 17.41635 ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.90152  -11.80440 -13.83723 1.000 20.17001 ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.34288  -8.14669  -16.48988 1.000 17.35055 ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.96922  -6.79856  -16.89849 1.000 17.23492 ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.50949  -6.80611  -18.35854 1.000 18.22302 ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.87795  -5.91957  -19.14395 1.000 17.80030 ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.88352  -6.25670  -15.96186 1.000 23.99728 ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.49462  -4.93798  -16.31633 1.000 25.69794 ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.72658  -7.81999  -18.74741 1.000 18.40448 ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.32042  -7.94526  -20.14177 1.000 17.72011 ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.52831  -8.08329  -21.05983 1.000 16.45575 ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.54765  -7.51972  -22.16447 1.000 16.27775 ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.40953  -9.15858  -20.32336 1.000 18.01233 ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? -0.01309  -8.91720  -19.80827 1.000 31.31917 ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.31011   -7.82526  -19.33915 1.000 25.08587 ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 0.82547   -9.94263  -19.88765 1.000 28.43191 ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.52372  -8.86711  -20.63773 1.000 15.60255 ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.73894  -9.01920  -21.43189 1.000 16.45080 ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.48373  -7.68783  -21.55333 1.000 17.84183 ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.95657  -7.33260  -22.64348 1.000 16.48462 ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.64032  -10.09239 -20.80825 1.000 14.75690 ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -6.13137  -11.40666 -21.00907 1.000 18.59434 ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.60279  -6.93482  -20.44773 1.000 18.82764 ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.22858  -5.61746  -20.53134 1.000 17.80289 ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.47105  -4.71175  -21.50516 1.000 20.00696 ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -7.08738  -3.98463  -22.29711 1.000 19.07084 ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.32221  -4.98896  -19.13213 1.000 16.75691 ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.82834  -3.65418  -19.17376 1.000 18.40144 ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -5.13262  -4.76634  -21.48801 1.000 15.83790 ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.35352  -3.94737  -22.41356 1.000 17.62729 ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.65735  -4.30977  -23.86345 1.000 20.35907 ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.76746  -3.42831  -24.73058 1.000 18.81924 ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.85857  -4.11292  -22.13311 1.000 16.26735 ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.41515  -3.39161  -20.86227 1.000 27.76311 ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -1.27710  -3.64834  -20.39621 1.000 26.22480 ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -3.21177  -2.59137  -20.30408 1.000 25.54953 ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.77102  -5.60775  -24.14920 1.000 15.20749 ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -5.02424  -6.05915  -25.51249 1.000 14.19500 ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.42720  -5.67801  -25.95390 1.000 15.47324 ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.65162  -5.34565  -27.12245 1.000 15.82539 ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.82827  -7.57349  -25.60417 1.000 15.82386 ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.38455  -5.73048  -25.03010 1.000 15.63356 ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.73769  -5.28965  -25.34154 1.000 14.77228 ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.77585  -3.78822  -25.59632 1.000 18.84384 ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.46506  -3.32874  -26.52172 1.000 17.94644 ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.67258  -5.69039  -24.19436 1.000 15.32299 ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.94758  -7.20232  -24.18570 1.000 17.43580 ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.39705 -7.66941  -22.80659 1.000 19.80046 ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.99167 -7.56740  -25.21341 1.000 18.50305 ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -8.02385  -3.00419  -24.80978 1.000 17.39210 ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.97570  -1.56349  -25.05183 1.000 17.05592 ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.47153  -1.26868  -26.45823 1.000 20.28412 ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.92886  -0.32247  -27.10305 1.000 19.11847 ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -7.06695  -0.84036  -24.04970 1.000 18.95719 ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.66901  -0.72192  -22.65145 1.000 25.16332 ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.90035  -0.88071  -22.47988 1.000 26.62306 ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.89861  -0.37295  -21.72764 1.000 26.19953 ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.49707  -2.04752  -26.92836 1.000 17.50640 ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.88001  -1.78712  -28.22579 1.000 18.01110 ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.87251  -1.99867  -29.36363 1.000 17.77860 ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -6.94142  -1.19105  -30.30047 1.000 20.36123 ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.66136  -2.69777  -28.40239 1.000 19.60576 ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.41358  -2.24249  -27.65924 1.000 22.23568 ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.32527  -3.31973  -27.70102 1.000 22.06261 ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.27879  -3.08285  -26.61829 1.000 29.01260 ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? -0.15165  -4.04489  -26.72571 1.000 36.61778 ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.63177  -3.09717  -29.32673 1.000 19.71178 ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.58884  -3.30598  -30.41095 1.000 17.36508 ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.75424  -2.33326  -30.26581 1.000 20.98690 ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.31853 -1.87495  -31.26938 1.000 19.70558 ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -9.05548  -4.77244  -30.48405 1.000 18.03528 ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.87057  -5.01500  -31.76550 1.000 24.59211 ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.85978  -5.16927  -29.23777 1.000 18.48764 ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -9.11278  -4.73602  -33.07334 1.000 27.03252 ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.12114 -1.95879  -29.03704 1.000 17.54232 ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.14910 -0.93115  -28.92800 1.000 18.13433 ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.68767 0.36599   -29.57944 1.000 21.55338 ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.43638 0.97849   -30.35047 1.000 20.50925 ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.55790 -0.69163  -27.47511 1.000 19.23499 ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.61134 0.40622   -27.39863 1.000 28.91582 ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -13.11778 0.65058   -26.00863 1.000 47.79326 ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.11772 -0.30883  -25.55790 1.000 52.16772 ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.16075 -0.79329  -24.32492 1.000 50.53074 ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.19211 -0.54724  -23.45630 1.000 41.70658 ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.20785 -1.52617  -23.94676 1.000 28.56643 ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.43914  0.77384   -29.32885 1.000 22.06681 ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -8.96915  2.04287   -29.87453 1.000 22.46401 ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -8.94209  2.00981   -31.39589 1.000 24.54183 ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.35061  2.97647   -32.04913 1.000 24.11664 ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.58216  2.39149   -29.32641 1.000 23.58704 ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.11628  3.74204   -29.80784 1.000 27.60163 ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.62363  4.90821   -29.24602 1.000 23.12412 ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.20575  3.85601   -30.85059 1.000 26.70835 ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.22188  6.14553   -29.68945 1.000 26.18649 ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.79889  5.08850   -31.30786 1.000 26.83704 ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.30713  6.23226   -30.72489 1.000 28.43931 ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -5.90236  7.45969   -31.17887 1.000 32.38192 ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.46136  0.90860   -31.98275 1.000 20.85737 ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.44313  0.81709   -33.43878 1.000 23.49728 ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -9.85287  0.87780   -34.00034 1.000 24.52086 ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.08741 1.48709   -35.05209 1.000 26.74479 ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.74370  -0.46664  -33.88831 1.000 24.36816 ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.24554  -0.44410  -33.64494 1.000 29.73133 ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.50536  -1.55288  -34.38045 1.000 53.34322 ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -4.25463  -1.50913  -34.40586 1.000 39.77644 ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -6.16719  -2.45545  -34.93956 1.000 42.09433 ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.81344 0.27258   -33.29638 1.000 21.31842 ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.19087 0.26327   -33.78452 1.000 23.21112 ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -12.85701 1.63415   -33.70731 1.000 26.24906 ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -13.92016 1.81846   -34.30888 1.000 27.50482 ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.01128 -0.75914  -32.99698 1.000 25.33344 ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.40517 -0.22518  -31.73933 1.000 28.50499 ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.26922 2.60023   -32.99266 1.000 24.36839 ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -12.87811 3.92746   -32.92442 1.000 32.00610 ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -12.82258 4.65948   -34.25743 1.000 37.71717 ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.64373 5.55162   -34.49618 1.000 33.72858 ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.18729 4.77707   -31.85623 1.000 26.12230 ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.32711 4.28976   -30.40794 1.000 24.68851 ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.62682 5.25735   -29.46506 1.000 29.17540 ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.78688 4.12081   -30.01665 1.000 32.73796 ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -11.86145 4.32444   -35.11571 1.000 32.36744 ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -11.74318 4.93541   -36.43078 1.000 35.77428 ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.01011 3.96543   -37.57334 1.000 36.51369 ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.23364 4.41439   -38.70124 1.000 38.01410 ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.34540 5.55067   -36.60496 1.000 51.28402 ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.35086  4.53809   -36.40312 1.000 51.02714 ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.12726 6.66593   -35.59033 1.000 45.63064 ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.00527 2.65887   -37.31356 1.000 35.98572 ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.28376 1.65353   -38.33788 1.000 35.89966 ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.16901 0.59512   -37.69413 1.000 29.66565 ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.67588 -0.35954  -37.08247 1.000 27.60379 ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -10.99426 1.04039   -38.88804 1.000 35.30523 ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.23902 0.06904   -40.03596 1.000 45.43583 ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.41405 -0.18011  -40.38943 1.000 45.90831 ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.24422 -0.45921  -40.58008 1.000 51.52160 ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.49372 0.75218   -37.79123 1.000 40.09256 ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.39223 -0.22123  -37.14371 1.000 37.90231 ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.21009 -1.64653  -37.63945 1.000 35.71265 ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.48580 -2.58998  -36.88742 1.000 32.40266 ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.79141 0.30980   -37.48563 1.000 36.33625 ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.61044 1.75197   -37.77825 1.000 44.61205 ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.18288 1.99514   -38.17557 1.000 37.13450 ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.76334 -1.83554  -38.88639 1.000 34.99199 ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.58671 -3.18177  -39.42076 1.000 34.40709 ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.54971 -3.99348  -38.65257 1.000 36.22290 ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.50702 -5.22045  -38.80524 1.000 32.67252 ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.20251 -3.11196  -40.89944 1.000 37.03385 ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -12.88889 -2.60680  -41.06202 1.000 39.96430 ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.73345 -3.35515  -37.81173 1.000 29.10784 ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.78235 -4.11173  -37.00872 1.000 25.26651 ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.47629 -5.08303  -36.06517 1.000 28.48106 ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.83863 -6.02235  -35.57830 1.000 26.69352 ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.89731 -3.15588  -36.21443 1.000 27.65401 ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -10.09972 -2.20318  -37.07954 1.000 36.54292 ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.61331  -2.42431  -36.88616 1.000 36.03598 ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.80925  -1.97863  -38.08899 1.000 39.34177 ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.35801  -2.24252  -37.88033 1.000 49.79776 ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.76289 -4.87425  -35.78689 1.000 25.24648 ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.53074 -5.77527  -34.94640 1.000 23.29026 ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.38077 -6.74402  -35.76127 1.000 25.84522 ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -16.21694 -7.44473  -35.18628 1.000 30.08064 ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.41795 -4.98151  -33.98000 1.000 27.70625 ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.71270 -4.07938  -32.95929 1.000 28.11901 ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.75163 -3.29633  -32.14275 1.000 29.92214 ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.78854 -4.87457  -32.04113 1.000 26.00528 ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -15.17218 -6.81884  -37.07692 1.000 27.81164 ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.84270 -7.85866  -37.85803 1.000 29.92559 ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.47721 -9.25312  -37.37088 1.000 29.30569 ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.25561 -10.19764 -37.55183 1.000 33.83393 ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.50112 -7.73968  -39.34091 1.000 30.16764 ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -16.07111 -6.49110  -39.98282 1.000 45.96282 ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -16.92024 -5.82227  -39.35325 1.000 48.04450 ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.69259 -6.20130  -41.13830 1.000 44.62847 ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.29973 -9.40485  -36.76640 1.000 26.66922 ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.85385 -10.67577 -36.21119 1.000 26.12130 ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.42042 -10.94775 -34.82255 1.000 35.79052 ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -14.04856 -11.94987 -34.20314 1.000 34.29624 ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.32428 -10.69889 -36.15578 1.000 30.48652 ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.84229 -9.48861  -35.58587 1.000 24.77551 ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.29354 -10.08170 -34.31377 1.000 28.99401 ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.89768 -10.28631 -33.01209 1.000 29.13621 ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -16.14785 -8.97286  -32.29657 1.000 30.28575 ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.20847 -8.21373  -32.04705 1.000 28.73156 ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.41050 -8.68231  -31.97387 1.000 26.16488 ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.74165 -7.41441  -31.33392 1.000 25.70990 ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.57550 -7.44754  -29.82340 1.000 30.38798 ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.40145 -6.38623  -29.21371 1.000 31.66107 ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -19.17894 -6.99928  -31.66430 1.000 26.50213 ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.29647 -6.23468  -32.96901 1.000 41.77585 ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.73945 -6.12851  -33.42711 1.000 47.86662 ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.89445 -5.03846  -34.47364 1.000 72.17815 ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -20.10859 -5.34726  -35.69936 1.000 62.72128 ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.62525 -8.62570  -29.20773 1.000 22.41299 ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.59714 -8.71226  -27.75332 1.000 22.48541 ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.17561 -8.55840  -27.22721 1.000 26.56648 ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.23370 -9.15572  -27.75143 1.000 30.02546 ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -18.17855 -10.04576 -27.27336 1.000 27.39704 ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -19.68749 -10.15387 -27.39009 1.000 34.35341 ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -20.13588 -10.40940 -28.81620 1.000 61.55013 ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -19.40722 -11.12054 -29.54410 1.000 66.77926 ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -21.21084 -9.90241  -29.21066 1.000 66.61982 ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -16.03507 -7.77160  -26.16743 1.000 19.36164 ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.74455 -7.44560  -25.55297 1.000 17.63247 ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.79173 -7.96998  -24.12110 1.000 19.54223 ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.43513 -7.35975  -23.26140 1.000 19.20200 ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.51261 -5.93270  -25.59060 1.000 19.90355 ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.44499 -5.31134  -26.99290 1.000 25.16443 ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -14.10657 -3.82572  -26.90120 1.000 31.67721 ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.40830 -6.02879  -27.83315 1.000 24.46666 ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -14.14143 -9.10337  -23.85428 1.000 18.95942 ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.32891 -9.74838  -22.55631 1.000 18.00071 ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -13.12117 -10.60659 -22.21048 1.000 16.36424 ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.24241 -10.84965 -23.04019 1.000 14.73819 ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.62191 -10.58530 -22.53512 1.000 19.16952 ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.63181 -11.72021 -23.51770 1.000 20.51974 ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.58171 -11.83161 -24.50950 1.000 26.22687 ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.82149 -12.79648 -23.65196 1.000 21.08095 ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.35651 -12.92649 -25.21390 1.000 26.25642 ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.29335 -13.52977 -24.71566 1.000 24.60673 ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -13.09724 -11.05490 -20.95345 1.000 15.27161 ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -12.06627 -11.93985 -20.41596 1.000 15.15247 ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.76150 -13.12913 -19.76080 1.000 17.97568 ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.64717 -12.94140 -18.91432 1.000 18.06194 ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.19045 -11.21672 -19.36765 1.000 17.52162 ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.51233 -9.96172  -19.96485 1.000 16.51450 ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -10.18461 -12.21497 -18.73840 1.000 15.37298 ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.90978  -9.01533  -18.92574 1.000 18.02910 ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.34115 -14.34573 -20.11364 1.000 17.15731 ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.87928 -15.55703 -19.50376 1.000 15.71386 ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.76696 -16.28390 -18.76424 1.000 15.53940 ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.63760 -16.36635 -19.25435 1.000 17.53008 ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.49680 -16.47951 -20.55547 1.000 17.79656 ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.73997 -15.89448 -21.18754 1.000 19.78816 ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.45507 -15.10424 -20.56761 1.000 20.28045 ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -15.00656 -16.28069 -22.44031 1.000 23.64529 ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -12.07333 -16.78335 -17.56813 1.000 16.66323 ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -11.15550 -17.62554 -16.80062 1.000 13.96164 ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.74601 -19.03042 -16.75776 1.000 17.09563 ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.86996 -19.20588 -16.27736 1.000 15.68112 ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.98632 -17.07753 -15.38359 1.000 14.79666 ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.61255 -15.59270 -15.30965 1.000 16.24929 ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.49754 -15.16309 -13.85069 1.000 16.39347 ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.29495  -15.35693 -16.06700 1.000 18.17252 ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -11.01696 -20.01775 -17.26853 1.000 15.32921 ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.54100 -21.36448 -17.44626 1.000 14.20500 ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.62415 -22.35102 -16.72790 1.000 19.40722 ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.59344  -22.76128 -17.26134 1.000 18.84512 ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.69284 -21.72821 -18.93417 1.000 17.89412 ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.43332 -20.59767 -19.66363 1.000 20.24972 ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.45870 -23.03772 -19.05766 1.000 15.55064 ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.56305 -20.78000 -21.19161 1.000 22.38923 ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.99039 -22.78321 -15.52955 1.000 19.24885 ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.22852 -23.84504 -14.86773 1.000 19.67797 ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.68297 -25.20587 -15.35601 1.000 20.55323 ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.85360 -25.41525 -15.68854 1.000 24.16337 ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.56756 -23.65144 -13.38711 1.000 19.76454 ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.95447 -23.06099 -13.40452 1.000 20.37048 ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -12.13654 -22.33115 -14.72536 1.000 19.71149 ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.73265  -26.14240 -15.40360 1.000 21.53588 ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -10.02217 -27.52324 -15.79956 1.000 20.82287 ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -9.19364  -28.44918 -14.91545 1.000 24.49395 ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.98906  -28.61823 -15.13374 1.000 24.14748 ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.72459  -27.75059 -17.27879 1.000 25.35123 ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -10.22976 -29.09109 -17.77529 1.000 28.87233 ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.94363  -30.12719 -17.18538 1.000 29.12917 ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.99502 -29.07507 -18.86106 1.000 37.72724 ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.84674  -29.06828 -13.93358 1.000 25.65943 ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -9.12525  -29.89479 -12.97110 1.000 27.71902 ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.64410  -31.20168 -13.58238 1.000 28.74811 ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.64872  -31.76372 -13.11416 1.000 32.62255 ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -10.01169 -30.16680 -11.76025 1.000 32.83685 ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -10.20737 -28.93027 -10.88286 1.000 32.62607 ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.71417 -29.29800 -9.49570  1.000 42.07738 ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.12554 -28.05768 -8.72475  1.000 30.08341 ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -12.08095 -27.21638 -9.49758  1.000 45.67705 ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.33445  -31.71314 -14.60836 1.000 31.37408 ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.89325  -32.95947 -15.23082 1.000 39.32023 ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.59118  -32.75928 -15.99048 1.000 33.88186 ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.69046  -33.60346 -15.92199 1.000 35.44368 ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.96989  -33.51038 -16.16951 1.000 37.00386 ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -10.77520 -34.66492 -15.59629 1.000 60.72879 ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -12.16856 -34.75617 -16.19118 1.000 87.89454 ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -12.73583 -33.75253 -16.62919 1.000 92.11454 ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -12.72903 -35.96389 -16.20917 1.000 68.65571 ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.48734  -31.65441 -16.72689 1.000 31.90901 ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.30786  -31.30820 -17.50511 1.000 37.96003 ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.25175  -30.60596 -16.66674 1.000 32.01536 ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -4.11458  -30.45842 -17.13097 1.000 28.63150 ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.71521  -30.40389 -18.67041 1.000 34.06987 ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.52140  -31.13853 -19.72367 1.000 45.16099 ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.88525  -30.50784 -20.73936 1.000 50.38071 ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.77309  -32.34980 -19.54396 1.000 42.64288 ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.61032  -30.18745 -15.45129 1.000 25.74295 ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.77366  -29.34764 -14.59524 1.000 20.99711 ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.29388  -28.10682 -15.34789 1.000 20.80270 ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -3.09763  -27.80279 -15.40230 1.000 23.28443 ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.59302  -30.12744 -14.02205 1.000 22.72010 ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -3.08601  -29.49664 -12.75093 1.000 27.23093 ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.63108  -29.77029 -12.50988 1.000 36.70520 ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -1.40021  -31.14371 -12.10424 1.000 41.44806 ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? -0.24291  -31.77855 -12.22619 1.000 48.63483 ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 0.82150   -31.18950 -12.75052 1.000 38.18590 ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? -0.14623  -33.02984 -11.79448 1.000 43.85869 ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.24535  -27.39186 -15.94046 1.000 19.55488 ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.96103  -26.17235 -16.68442 1.000 18.26398 ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.88031  -25.05326 -16.23578 1.000 19.47254 ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -7.06187  -25.27196 -15.93936 1.000 20.82814 ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -5.13825  -26.33105 -18.20986 1.000 23.18528 ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.47522  -26.76279 -18.48725 1.000 22.35611 ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -4.14441  -27.31682 -18.79264 1.000 24.24022 ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.33047  -23.84063 -16.22032 1.000 16.24610 ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -6.11662  -22.61931 -16.07390 1.000 15.51497 ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.92819  -21.81440 -17.34915 1.000 18.01457 ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.79748  -21.51818 -17.73020 1.000 17.45292 ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.68113  -21.81257 -14.84405 1.000 20.04230 ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.39572  -20.46767 -14.64711 1.000 16.56564 ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.88887  -20.69340 -14.42022 1.000 18.84316 ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.79074  -19.74980 -13.45221 1.000 17.97048 ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -7.02145  -21.47988 -18.02122 1.000 15.94321 ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.94669  -20.78536 -19.29764 1.000 15.52911 ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.53698  -19.39380 -19.12937 1.000 16.61761 ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.61398  -19.24406 -18.54536 1.000 18.73174 ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.68608  -21.55522 -20.39643 1.000 16.56242 ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -7.11654  -22.86034 -20.55174 1.000 18.66158 ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.52999  -20.83781 -21.71322 1.000 23.04349 ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.80707  -18.38002 -19.59024 1.000 16.28132 ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.27480  -16.99521 -19.60957 1.000 15.70418 ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.50992  -16.62325 -21.06576 1.000 20.13831 ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.56403  -16.61435 -21.86170 1.000 17.85441 ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.27167  -16.02744 -18.96214 1.000 17.91646 ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -6.00979  -16.40301 -17.49690 1.000 25.74165 ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.77154  -14.58254 -19.10818 1.000 19.25126 ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.82914  -17.32141 -17.28699 1.000 30.94761 ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.75999  -16.32927 -21.41408 1.000 15.52150 ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -9.15908  -16.00676 -22.78277 1.000 14.03473 ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.57592  -14.54817 -22.83024 1.000 19.14715 ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.32888 -14.08063 -21.96686 1.000 19.75295 ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.31850 -16.89434 -23.28642 1.000 17.97279 ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.59646 -16.62499 -24.78603 1.000 19.72915 ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -10.01092 -18.35675 -23.05796 1.000 23.15142 ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -9.09955  -13.82809 -23.84840 1.000 17.28214 ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.59313  -12.48035 -24.10061 1.000 15.50123 ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.84909  -12.30890 -25.58931 1.000 19.85665 ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.29283  -13.02237 -26.42924 1.000 18.93971 ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.62481  -11.41353 -23.56675 1.000 15.61124 ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.32133  -11.33079 -24.35180 1.000 22.77304 ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -7.34670  -10.95878 -25.54853 1.000 22.03968 ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -6.25480  -11.59731 -23.74096 1.000 18.88052 ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.72846 -11.36533 -25.90866 1.000 17.84241 ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -11.01525 -11.04251 -27.29912 1.000 14.99540 ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.34904 -9.74005  -27.71076 1.000 19.35724 ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.92444 -8.92210  -28.43493 1.000 18.32292 ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.52549 -11.00198 -27.52405 1.000 17.15139 ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -13.14766 -10.15846 -26.54669 1.000 18.26030 ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -13.09812 -12.41787 -27.37874 1.000 17.85030 ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -9.10637  -9.54602  -27.27823 1.000 16.52510 ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.35558  -8.35281  -27.59977 1.000 19.43649 ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.75982  -8.40640  -28.99357 1.000 17.24977 ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -8.18751  -9.16844  -29.86557 1.000 19.93163 ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.74880  -7.56092  -29.19868 1.000 15.83172 ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.19434  -7.36498  -30.53107 1.000 16.51365 ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.43282  -8.58800  -31.02739 1.000 18.81478 ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.23420  -8.73686  -32.23884 1.000 19.31372 ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.30559  -6.10197  -30.54848 1.000 18.04421 ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -5.04342  -5.65078  -31.99614 1.000 20.24367 ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -3.99382  -6.33860  -29.76049 1.000 18.64640 ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.55916  -4.23349  -32.10164 1.000 28.89773 ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -5.00944  -9.47514  -30.13377 1.000 19.80618 ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.27565  -10.65131 -30.55141 1.000 18.65786 ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.85690  -10.30697 -30.94959 1.000 19.78495 ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.37985  -9.18217  -30.79028 1.000 19.62883 ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -2.16012  -11.31499 -31.46601 1.000 17.19972 ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.75433  -11.16848 -31.81795 1.000 20.56553 ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.48633  -11.80068 -33.17718 1.000 21.59135 ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -1.01456  -12.87472 -33.48040 1.000 17.23625 ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.13039   -11.82913 -30.74930 1.000 19.86391 ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.23950   -11.02326 -29.47802 1.000 19.29219 ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.21679   -11.88052 -28.21766 1.000 21.90910 ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.09136   -13.18797 -27.72605 1.000 23.15137 ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.33962   -11.14124 -33.99366 1.000 18.82326 ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 0.80561   -11.76535 -35.22384 1.000 20.19648 ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 1.89954   -12.78601 -34.91225 1.000 21.98012 ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.44926   -12.82204 -33.80821 1.000 21.59136 ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.34891   -10.72309 -36.19528 1.000 23.75302 ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.49511   -10.09447 -35.60586 1.000 26.67424 ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.28682   -9.66480  -36.50626 1.000 23.21524 ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.21527   -13.62648 -35.90538 1.000 22.05845 ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.33335   -14.54979 -35.73897 1.000 21.65743 ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 4.59308   -13.78607 -35.36951 1.000 20.10362 ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.32714   -14.18026 -34.45163 1.000 23.97357 ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 3.55683   -15.36037 -37.01996 1.000 24.70385 ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 4.70073   -16.36951 -36.90027 1.000 26.39569 ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 4.96755   -17.07275 -38.22784 1.000 23.15479 ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 5.88593   -18.26577 -38.02563 1.000 29.52106 ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 6.39644   -18.79170 -39.31625 1.000 32.15588 ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 4.82039   -12.65259 -36.04555 1.000 22.38622 ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 5.97336   -11.81094 -35.75241 1.000 26.55553 ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 5.94136   -11.29864 -34.32004 1.000 28.35152 ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 6.98946   -11.23924 -33.67105 1.000 26.57580 ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.04065   -10.64586 -36.74177 1.000 25.33262 ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 4.76051   -10.90133 -33.81240 1.000 19.71686 ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.66084   -10.51661 -32.40010 1.000 22.53479 ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 4.97407   -11.67076 -31.46339 1.000 22.01706 ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.59769   -11.46325 -30.41844 1.000 22.84076 ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.28199   -9.96077  -32.02510 1.000 22.81290 ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 2.89438   -8.72646  -32.79261 1.000 34.60849 ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 3.75710   -7.83477  -32.95028 1.000 30.11875 ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 1.68709   -8.58833  -33.10492 1.000 30.51978 ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.52728   -12.88402 -31.79426 1.000 18.68630 ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 4.75447   -14.02391 -30.90531 1.000 21.19254 ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.24162   -14.28675 -30.72730 1.000 23.56078 ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 6.74336   -14.35014 -29.60217 1.000 23.81225 ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.06641   -15.26238 -31.46236 1.000 23.60041 ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.59303   -15.46672 -31.15581 1.000 22.80520 ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.15020   -16.77091 -31.82339 1.000 20.18517 ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.34233   -15.51000 -29.65096 1.000 17.96018 ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 6.95893   -14.48841 -31.83042 1.000 23.63407 ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.39205   -14.23346 -31.82707 1.000 22.26979 ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 8.55573   -12.75700 -31.46380 1.000 20.65008 ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 7.61249   -11.99950 -31.56625 1.000 52.88344 ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 8.94923   -14.55740 -33.22357 1.000 23.94268 ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.35310   -15.87546 -33.73926 1.000 21.80136 ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.50744  -14.61752 -33.21276 1.000 24.60469 ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.44416   -16.06047 -35.27135 1.000 25.27227 ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 9.70050   -12.34659 -30.96840 1.000 46.10575 ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 9.73952   -10.98561 -30.41093 1.000 28.95006 ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 8.91899   -10.93140 -29.12844 1.000 23.86572 ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.20936   -9.95909  -28.86486 1.000 20.86705 ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.25703   -9.90472  -31.40298 1.000 31.93885 ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.02469  -8.62213  -31.28171 1.000 47.79356 ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 11.04748  -8.56600  -30.59129 1.000 46.59388 ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 9.52550   -7.56509  -31.92532 1.000 46.06754 ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 8.98057   -12.01636 -28.36148 1.000 19.15149 ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.61618   -12.01008 -26.94262 1.000 20.75430 ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.16942   -11.58159 -26.71230 1.000 21.39405 ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 6.87158   -10.76584 -25.83372 1.000 18.73454 ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.59240   -11.13648 -26.14736 1.000 18.41350 ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.03348  -11.56815 -26.35376 1.000 19.09342 ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.36222  -12.72971 -26.13682 1.000 20.68012 ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 11.89396  -10.64380 -26.75852 1.000 19.79911 ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.26297   -12.15835 -27.50764 1.000 20.26523 ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 4.81792   -11.98658 -27.30534 1.000 23.98005 ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.43053   -10.50973 -27.26551 1.000 24.70596 ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.66679   -10.06682 -26.40314 1.000 21.51383 ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.34678   -12.71257 -26.03604 1.000 17.40977 ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.66709   -14.21874 -26.12151 1.000 24.47023 ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 5.85327   -14.57320 -25.24863 1.000 23.47019 ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.50015   -15.09443 -25.76227 1.000 28.93696 ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 4.97153   -9.73890  -28.20744 1.000 20.64902 ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.63295   -8.33186  -28.32989 1.000 23.89603 ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.15131   -7.41664  -27.23963 1.000 25.36947 ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.62360   -6.31259  -27.07982 1.000 25.87509 ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.17784   -7.82614  -26.49231 1.000 22.50561 ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.70794   -7.04071  -25.39005 1.000 23.84555 ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.07541   -6.47720  -25.74749 1.000 22.70291 ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.73126   -6.93041  -26.68839 1.000 21.93817 ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 6.86086   -7.88196  -24.11627 1.000 22.05946 ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 7.92467   -8.82764  -24.30843 1.000 25.07170 ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.56173   -8.62870  -23.78994 1.000 23.81145 ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.51074   -5.49634  -24.96101 1.000 19.73335 ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 9.87940   -4.99952  -25.02788 1.000 20.34961 ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.72327  -5.72806  -23.98599 1.000 24.98102 ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.38220  -5.10812  -23.14640 1.000 22.65720 ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 9.91368   -3.46182  -24.88118 1.000 30.70997 ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 8.93540   -2.93786  -23.80434 1.000 30.92420 ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.56540   -2.81208  -26.21942 1.000 30.22190 ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 9.25861   -3.20813  -22.33268 1.000 35.02966 ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 10.75560  -7.05970  -24.08036 1.000 24.21520 ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.20691  -7.86842  -22.95212 1.000 20.10793 ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.68925  -7.67051  -22.62975 1.000 19.56721 ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.06245  -7.77769  -21.45969 1.000 22.56546 ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 10.90797  -9.35089  -23.20575 1.000 22.23540 ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.55073  -7.40864  -23.61538 1.000 21.61319 ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 14.96598  -7.21966  -23.29222 1.000 26.08463 ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.16979  -5.98263  -22.41734 1.000 28.08662 ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 15.76341  -6.06301  -21.33366 1.000 23.45856 ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.80839  -7.12845  -24.56534 1.000 23.13136 ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.29399  -6.99517  -24.28572 1.000 30.26922 ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.15004  -7.21027  -25.53809 1.000 31.11525 ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 19.47899  -6.49429  -25.39146 1.000 42.32173 ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.55305  -7.13555  -26.20395 1.000 46.34713 ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.66673  -4.82753  -22.85877 1.000 25.27648 ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 14.85164  -3.61619  -22.06372 1.000 21.40646 ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 13.98425  -3.64632  -20.81004 1.000 24.26923 ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.37220  -3.09646  -19.77563 1.000 24.56301 ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.54847  -2.37410  -22.90434 1.000 31.79006 ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.20396  -2.38284  -23.34919 1.000 30.56967 ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 12.81103  -4.28233  -20.88009 1.000 20.86302 ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 11.97595  -4.41198  -19.69614 1.000 21.24715 ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.62683  -5.26130  -18.62092 1.000 22.87227 ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.57955  -4.92314  -17.43486 1.000 22.17702 ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.25594  -6.36859  -19.02112 1.000 19.87893 ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 13.96429  -7.21480  -18.06024 1.000 20.93809 ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.11677  -6.46009  -17.41089 1.000 22.90389 ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.34882  -6.57722  -16.20119 1.000 20.94605 ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.47722  -8.47259  -18.76037 1.000 28.31787 ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.35699  -9.21253  -19.26546 1.000 23.51499 ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.30172  -9.35127  -17.80567 1.000 20.19291 ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 15.84826  -5.68262  -18.20811 1.000 21.23055 ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 16.97162  -4.89740  -17.70087 1.000 21.99223 ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.48868  -3.90696  -16.63674 1.000 26.89051 ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.08785  -3.79089  -15.55888 1.000 27.41211 ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.62167  -4.21106  -18.91306 1.000 24.58510 ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 18.58611  -3.03550  -18.78766 1.000 41.39741 ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.75920  -3.34347  -17.90143 1.000 50.81423 ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.90212  -2.33668  -18.13667 1.000 58.14498 ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 20.54620  -1.27025  -19.12487 1.000 55.69528 ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.36053  -3.23304  -16.89389 1.000 24.01861 ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 14.82231  -2.28586  -15.91983 1.000 25.20964 ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.29104  -3.00355  -14.68278 1.000 24.26580 ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.42825  -2.49973  -13.55672 1.000 25.69924 ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 13.72256  -1.44452  -16.56783 1.000 25.23219 ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.66826  -4.17133  -14.88029 1.000 20.22432 ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.16950  -4.97651  -13.76570 1.000 22.26522 ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.32018  -5.44393  -12.87809 1.000 24.24797 ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.25929  -5.30844  -11.65244 1.000 22.60610 ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.36401  -6.16197  -14.32109 1.000 17.17283 ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.73992  -7.05540  -13.26733 1.000 19.89371 ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.17998  -6.52563  -12.11564 1.000 22.55191 ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.67361  -8.42631  -13.46291 1.000 20.54073 ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.60001  -7.34594  -11.16373 1.000 24.33726 ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.08530  -9.26118  -12.51150 1.000 24.41250 ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.55191  -8.71583  -11.35831 1.000 21.80972 ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.38836  -5.98237  -13.48776 1.000 22.17050 ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.61316  -6.31172  -12.74858 1.000 24.32606 ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.15919  -5.13861  -11.94486 1.000 29.52726 ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.51332  -5.30129  -10.76821 1.000 31.63338 ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.69069  -6.84565  -13.70187 1.000 26.03355 ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 17.54236  -8.26905  -14.26382 1.000 39.46143 ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 16.58223  -9.35380  -13.19113 1.000 34.79557 ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 17.89769  -9.88147  -12.09394 1.000 46.45861 ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.29076  -3.95376  -12.56079 1.000 31.88724 ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 17.77736  -2.81860  -11.77135 1.000 28.53152 ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 16.88227  -2.53969  -10.57601 1.000 32.61055 ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.37583  -2.22452  -9.48586  1.000 33.61040 ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 17.92516  -1.53379  -12.58720 1.000 43.06755 ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.24555  -1.35722  -13.30179 1.000 60.56748 ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.09147  -0.83496  -14.70130 1.000 66.10434 ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 18.46839  0.23179   -14.88446 1.000 72.45962 ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 19.65031  -1.45271  -15.61283 1.000 65.35943 ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.56461  -2.62488  -10.76687 1.000 29.19437 ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 14.64618  -2.34140  -9.66908  1.000 32.10954 ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 14.80444  -3.35404  -8.54036  1.000 33.27697 ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 14.81843  -2.98068  -7.36033  1.000 34.65882 ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.20399  -2.32317  -10.17843 1.000 25.63083 ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 14.93636  -4.63996  -8.88340  1.000 30.44040 ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.10537  -5.66481  -7.85464  1.000 30.47969 ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.34818  -5.40987  -7.02075  1.000 34.27824 ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.33906  -5.60177  -5.79777  1.000 36.15806 ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.18460  -7.05227  -8.48958  1.000 26.03306 ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.89748  -7.59153  -9.11575  1.000 27.54670 ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.16113  -8.94502  -9.75546  1.000 30.25010 ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.76544  -7.68050  -8.08996  1.000 32.63422 ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.43677  -4.99145  -7.66281  1.000 35.19560 ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.64501  -4.71484  -6.90129  1.000 35.04586 ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.50869  -3.45765  -6.05227  1.000 38.63743 ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.24890  -3.29777  -5.07622  1.000 47.02941 ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.84123  -4.61496  -7.84184  1.000 44.34330 ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 21.15249  -5.01081  -7.16697  1.000 71.04504 ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.28762  -6.51323  -6.97479  1.000 87.77359 ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 21.47662  -7.26270  -7.93516  1.000 88.76565 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 21.19520  -6.95935  -5.72268  1.000 73.27774 ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.56171  -2.58193  -6.38269  1.000 44.82011 ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.28514  -1.38289  -5.60467  1.000 50.49638 ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 16.14409  -1.57017  -4.60651  1.000 51.52802 ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.64983  -0.58102  -4.05585  1.000 50.77080 ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 16.97925  -0.20973  -6.53935  1.000 44.86041 ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.70629  -2.80606  -4.36439  1.000 44.48350 ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.75936  -3.08482  -3.30160  1.000 44.61947 ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.37063  -3.49163  -3.74370  1.000 52.36292 ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.55546  -3.85004  -2.88394  1.000 48.88196 ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.06389  -3.44693  -5.03873  1.000 40.67575 ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.77009  -3.91515  -5.51340  1.000 40.89695 ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.63692  -5.42222  -5.29339  1.000 36.52623 ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.60139  -6.12278  -5.00015  1.000 41.05863 ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.59050  -3.58627  -6.99397  1.000 39.84111 ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.41734  -5.92590  -5.43398  1.000 40.37622 ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.19764  -7.36134  -5.34147  1.000 42.19825 ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.53228   -7.86336  -6.61354  1.000 31.59509 ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.15474   -7.08642  -7.49690  1.000 35.16726 ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.36921   -7.72081  -4.10207  1.000 50.79406 ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 7.93056   -7.30853  -4.23377  1.000 57.42799 ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.67284   -6.08723  -4.18046  1.000 67.77094 ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 7.06152   -8.19635  -4.37843  1.000 47.49282 ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.40399   -9.19131  -6.69745  1.000 30.84681 ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.93395   -9.83287  -7.91955  1.000 29.86158 ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.55923   -9.31631  -8.31552  1.000 28.05657 ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.23588   -9.24557  -9.50841  1.000 30.27005 ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.94752   -11.37292 -7.75835  1.000 32.55810 ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.38395  -11.91481 -7.67591  1.000 42.12828 ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.18618   -12.06547 -8.86907  1.000 34.51063 ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 11.01414  -11.85010 -6.29370  1.000 55.36032 ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.73590   -8.91621  -7.34223  1.000 28.19457 ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.37112   -8.52983  -7.69931  1.000 31.11979 ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.30854   -7.24911  -8.52960  1.000 36.09111 ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.25260   -6.95448  -9.10085  1.000 28.85674 ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.50449   -8.38689  -6.44603  1.000 30.93341 ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.87488   -7.25645  -5.67382  1.000 35.11768 ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.39960   -6.49351  -8.62556  1.000 25.67594 ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.45160   -5.30988  -9.47983  1.000 26.28108 ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.67975   -5.63742  -10.95209 1.000 31.09160 ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 6.72282   -4.70984  -11.76460 1.000 22.26607 ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.54910   -4.35812  -8.97991  1.000 27.40454 ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 7.39233   -3.96736  -7.50639  1.000 57.75411 ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.26101   -2.43746  -7.05612  1.000 67.27112 ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 8.62765   -1.74722  -8.68400  1.000 38.16948 ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.78980   -6.92347  -11.31066 1.000 23.51919 ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.21038   -7.33751  -12.65714 1.000 18.95515 ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.39042   -6.65305  -13.74323 1.000 18.94507 ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.92709   -6.26465  -14.78806 1.000 18.67707 ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.13037   -8.87314  -12.78253 1.000 24.06391 ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.63597   -9.33885  -14.15328 1.000 20.19246 ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.69672   -9.36341  -12.52301 1.000 20.95553 ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.80570   -10.87309 -14.24913 1.000 19.78639 ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.08812   -6.47280  -13.50490 1.000 20.97709 ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.19762   -5.95892  -14.53934 1.000 24.29793 ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.45286   -4.51114  -14.91232 1.000 27.42221 ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.07835   -4.06972  -16.00484 1.000 27.34269 ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.07098   -3.74588  -14.01429 1.000 21.94059 ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.38859   -2.35981  -14.33125 1.000 24.96331 ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.51659   -2.23983  -15.34341 1.000 26.52205 ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 6.77065   -1.13375  -15.83887 1.000 30.26612 ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 5.74318   -1.59379  -13.05833 1.000 29.59605 ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 4.91170   -2.02346  -11.84910 1.000 39.50939 ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.11702   -1.11938  -10.65434 1.000 56.83463 ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 5.40092   0.06954   -10.80667 1.000 62.90757 ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 4.95878   -1.67215  -9.45495  1.000 57.75037 ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.19001   -3.34334  -15.65074 1.000 23.00048 ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.28082   -3.36132  -16.61315 1.000 25.70469 ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 7.89421   -4.06044  -17.90385 1.000 26.73142 ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 8.76071   -4.32063  -18.74696 1.000 24.90956 ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.51649   -3.98497  -15.95934 1.000 19.10176 ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 9.90786   -3.27482  -14.69767 1.000 21.51644 ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 10.50350  -2.01580  -14.76017 1.000 24.03281 ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 9.60738   -3.80673  -13.44791 1.000 23.11219 ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 10.83418  -1.32084  -13.60174 1.000 25.74110 ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 9.92602   -3.10824  -12.28359 1.000 27.81074 ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.54677  -1.86983  -12.36332 1.000 27.37940 ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.60704   -4.32865  -18.09703 1.000 24.23286 ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.12880   -4.81083  -19.37430 1.000 21.24335 ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.34901   -6.27940  -19.63313 1.000 21.16257 ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.07309   -6.73646  -20.75062 1.000 25.66815 ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 6.82551   -7.03884  -18.64381 1.000 19.62286 ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.13398   -8.45200  -18.83352 1.000 19.59595 ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.30234   -9.29452  -17.87073 1.000 19.03099 ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.69828   -10.40412 -17.48462 1.000 17.32713 ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.64493   -8.72222  -18.66191 1.000 20.51874 ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.41586   -8.16891  -19.85231 1.000 19.13618 ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.16956   -8.10465  -17.36220 1.000 21.02027 ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.12171   -8.78090  -17.50674 1.000 19.76414 ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.25524   -9.49716  -16.58322 1.000 19.75262 ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 3.82218   -10.86558 -17.07621 1.000 17.07886 ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.51713   -11.75194 -16.26700 1.000 18.73413 ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 3.78491   -11.06509 -18.39755 1.000 15.89394 ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.41325   -12.37713 -18.92985 1.000 14.98948 ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.25316   -13.48434 -18.31051 1.000 16.38979 ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.73521   -14.55866 -17.98327 1.000 15.64088 ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.55288   -12.40533 -20.45425 1.000 15.27679 ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.53431   -13.80151 -21.03357 1.000 18.21312 ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.33352   -14.44890 -21.24030 1.000 19.02137 ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 4.72369   -14.47282 -21.33309 1.000 17.10167 ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.30464   -15.73910 -21.74582 1.000 18.04647 ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 4.70482   -15.76526 -21.84244 1.000 17.38829 ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.49300   -16.39860 -22.03680 1.000 15.64565 ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.55216   -13.23778 -18.11915 1.000 16.55158 ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.42645   -14.32272 -17.69483 1.000 18.64354 ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.19368   -14.74219 -16.25048 1.000 17.33489 ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.68472   -15.80968 -15.85278 1.000 17.46321 ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 7.88167   -13.92365 -17.92529 1.000 15.60104 ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.14668   -13.70130 -19.40221 1.000 18.12444 ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.38839   -14.76445 -20.26666 1.000 18.58437 ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.10048   -12.41536 -19.94001 1.000 17.51810 ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.62034   -14.53410 -21.63979 1.000 17.23754 ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.31148   -12.18568 -21.29198 1.000 23.51605 ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.57087   -13.24162 -22.13084 1.000 22.97228 ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 8.77892   -12.97382 -23.46284 1.000 23.33463 ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.44111   -13.95229 -15.47537 1.000 17.13475 ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.00450   -14.38868 -14.15243 1.000 18.78839 ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.13067   -15.63686 -14.22058 1.000 18.12760 ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 3.95172   -16.30225 -13.19634 1.000 18.38762 ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.28030   -13.23740 -13.42810 1.000 20.28256 ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 2.96550   -13.03223 -13.93149 1.000 20.18400 ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.62487   -15.98986 -15.40905 1.000 17.05798 ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 2.94821   -17.27482 -15.58299 1.000 17.57068 ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.78293   -18.43216 -15.04995 1.000 19.05018 ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.23269   -19.39963 -14.50973 1.000 18.52337 ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.62776   -17.50396 -17.06460 1.000 15.52345 ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.10868   -18.34231 -15.15617 1.000 19.85311 ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 5.95343   -19.44891 -14.72438 1.000 18.00457 ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.13457   -19.51124 -13.20403 1.000 19.53111 ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 6.83099   -20.40339 -12.71443 1.000 19.60593 ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.30375   -19.37815 -15.45119 1.000 18.08215 ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.10109   -19.70487 -16.91345 1.000 16.76354 ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.14596   -21.02313 -17.36243 1.000 19.70299 ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 6.79693   -18.70400 -17.82991 1.000 17.39316 ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 6.92120   -21.33444 -18.69991 1.000 19.84111 ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.56348   -19.00466 -19.18030 1.000 20.51756 ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.64085   -20.32373 -19.60036 1.000 22.36129 ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.41440   -20.62358 -20.92779 1.000 20.20340 ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.50383   -18.60927 -12.44507 1.000 20.32273 ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.37520   -18.81757 -11.00804 1.000 19.74857 ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.53623   -20.05413 -10.69668 1.000 20.42938 ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.75214   -20.72054 -9.67713  1.000 21.20883 ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.74012   -17.58286 -10.35162 1.000 20.17919 ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.56319   -16.28650 -10.34359 1.000 19.80623 ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.69916   -15.11335 -9.85351  1.000 21.70913 ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.80936   -16.44517 -9.48768  1.000 20.51675 ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.56438   -20.36996 -11.55555 1.000 18.11965 ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.62808   -21.44846 -11.26135 1.000 22.26772 ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.57305   -22.50867 -12.34614 1.000 17.72134 ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.10415   -23.62622 -12.06728 1.000 21.45558 ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.21085   -20.88904 -10.99089 1.000 22.04817 ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.22066   -19.99759 -9.72930  1.000 24.57392 ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.65042   -20.14291 -12.21388 1.000 17.88368 ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.03748   -22.23163 -13.56178 1.000 20.51075 ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 2.90841   -23.15460 -14.68098 1.000 20.02349 ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.24476   -23.79377 -15.01615 1.000 20.25137 ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.28007   -23.11967 -15.04205 1.000 22.34749 ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.36946   -22.44458 -15.92208 1.000 17.84512 ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.20794   -25.09944 -15.28013 1.000 16.36862 ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.36952   -25.79602 -15.82223 1.000 19.83957 ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.45418   -25.65609 -17.33742 1.000 25.03521 ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.54608   -25.74376 -17.90903 1.000 21.15527 ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.30330   -27.26557 -15.39274 1.000 28.15336 ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.19154   -28.05408 -16.06494 1.000 34.17103 ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.10750   -29.49429 -15.56858 1.000 46.81268 ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 4.89441   -29.86582 -14.67203 1.000 43.83448 ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 3.24718   -30.25339 -16.06969 1.000 52.18851 ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.32706   -25.42094 -17.99642 1.000 21.55939 ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.31364   -25.17751 -19.42946 1.000 21.10853 ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.22201   -24.15665 -19.68565 1.000 19.95815 ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.20244   -24.13342 -18.98193 1.000 18.23103 ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.07435   -26.48046 -20.21076 1.000 22.48140 ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 3.79305   -26.31784 -21.68927 1.000 22.25955 ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 3.87245   -27.67633 -22.37100 1.000 26.26294 ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.50152   -28.30529 -22.50562 1.000 31.87143 ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.53131   -29.59107 -23.28140 1.000 34.47604 ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.44823   -23.29379 -20.67174 1.000 15.99962 ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.46306   -22.29081 -21.06387 1.000 15.75940 ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.25918   -22.39339 -22.56899 1.000 19.72230 ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.23537   -22.44756 -23.32578 1.000 17.68647 ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 2.90675   -20.86993 -20.67527 1.000 15.26140 ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 1.88562   -19.83603 -21.18787 1.000 17.33373 ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.11115   -20.74632 -19.14607 1.000 17.82917 ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 0.99352   -22.44593 -22.99570 1.000 16.87789 ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.60414   -22.44344 -24.40041 1.000 19.18506 ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? -0.18004  -21.16240 -24.66329 1.000 20.74715 ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -1.09301  -20.82488 -23.89852 1.000 20.78433 ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? -0.25727  -23.66746 -24.74928 1.000 21.18217 ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.38764   -24.87719 -24.32251 1.000 23.12644 ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.52220  -23.74275 -26.25005 1.000 25.50641 ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.18194   -20.43869 -25.72030 1.000 16.45555 ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.49891  -19.19820 -26.08682 1.000 16.98872 ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -1.07020  -19.38893 -27.48429 1.000 19.98680 ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.31541  -19.57045 -28.44861 1.000 19.79486 ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.43980   -17.98281 -26.04350 1.000 18.02356 ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? -0.29709  -16.72411 -26.45887 1.000 17.78024 ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.01783   -17.79871 -24.63353 1.000 16.77407 ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.39109  -19.37054 -27.59226 1.000 18.39414 ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -3.07605  -19.41461 -28.88170 1.000 19.12155 ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.52877  -17.99839 -29.19618 1.000 21.21281 ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -4.08261  -17.31848 -28.33330 1.000 18.67250 ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -4.28351  -20.37639 -28.85918 1.000 19.34766 ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.94275  -21.71019 -28.18355 1.000 27.48462 ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.80539  -20.60663 -30.27856 1.000 23.15414 ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -3.05514  -22.58522 -28.98340 1.000 31.87452 ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -3.31293  -17.54102 -30.42677 1.000 15.72881 ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.62188  -16.14495 -30.69394 1.000 18.28240 ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -4.04956  -15.96169 -32.14014 1.000 20.20582 ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.61022  -16.68592 -33.03924 1.000 19.86121 ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.42870  -15.23235 -30.34583 1.000 21.30985 ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.85012  -13.86270 -30.34092 1.000 19.73270 ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -1.27593  -15.41654 -31.34024 1.000 18.26679 ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.93832  -14.99068 -32.34193 1.000 16.74240 ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.40050  -14.61407 -33.67311 1.000 15.41929 ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.49902  -13.09834 -33.74311 1.000 17.48215 ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -6.28061  -12.48854 -33.00579 1.000 20.29282 ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.75383  -15.25266 -33.98696 1.000 19.59721 ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.36461  -14.81384 -35.32526 1.000 21.53159 ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.62823  -15.40304 -36.52562 1.000 24.48606 ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.33942  -15.05427 -37.84134 1.000 22.22756 ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.28132  -13.59465 -38.18318 1.000 21.56203 ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.70913  -12.50451 -34.63129 1.000 20.54393 ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.71255  -11.07811 -34.91915 1.000 21.37263 ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.42172  -10.86989 -36.25343 1.000 23.78823 ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.39257  -11.74942 -37.12156 1.000 24.05657 ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.26365  -10.56019 -34.96280 1.000 20.35404 ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -3.13174  -9.07447  -35.11137 1.000 23.06973 ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.31945  -8.41828  -36.30960 1.000 23.88196 ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.76771  -8.12508  -34.21659 1.000 20.52617 ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -3.12453  -7.12206  -36.13614 1.000 28.23259 ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.78789  -6.91871  -34.87302 1.000 23.10246 ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -6.08073  -9.71576  -36.42041 1.000 21.47593 ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.80577  -9.47401  -37.67046 1.000 22.46912 ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.89750  -9.59063  -38.89747 1.000 25.57699 ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.37105  -9.93851  -39.98320 1.000 26.68118 ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.47619  -8.09329  -37.66429 1.000 24.15666 ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.76038  -8.05718  -36.84483 1.000 28.05276 ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.42731  -9.07803  -36.66429 1.000 28.62342 ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -9.13093  -6.86497  -36.37519 1.000 25.09145 ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.59876  -9.32011  -38.75894 1.000 25.35842 ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.71182  -9.26803  -39.91816 1.000 27.89970 ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.92825  -10.55893 -40.14877 1.000 28.70833 ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -2.01928  -10.56670 -40.98621 1.000 30.04007 ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.71993  -8.10716  -39.78471 1.000 29.09969 ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.39058  -6.75061  -39.79276 1.000 37.08975 ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.52715  -6.63717  -40.29515 1.000 31.18017 ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.77627  -5.79470  -39.27349 1.000 35.70653 ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -3.23370  -11.64176 -39.43521 1.000 25.18547 ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.44334  -12.86294 -39.57348 1.000 23.07239 ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.33759  -14.07397 -39.31115 1.000 29.39364 ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.53045  -13.94227 -39.01652 1.000 25.71105 ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -1.22916  -12.81977 -38.63177 1.000 22.60952 ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? -0.04950  -13.63782 -39.14286 1.000 29.38097 ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? -0.18986  -14.36105 -40.15954 1.000 25.27765 ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.04043   -13.53150 -38.53390 1.000 28.83421 ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.75717  -15.26582 -39.44196 1.000 24.98420 ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.47788  -16.50276 -39.17428 1.000 24.63519 ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.36826  -16.86023 -37.69187 1.000 20.90077 ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.65840  -16.20982 -36.92248 1.000 23.99377 ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -2.94618  -17.63008 -40.05990 1.000 27.48618 ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -3.12210  -17.36139 -41.54455 1.000 38.49667 ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -4.55530  -16.99282 -41.91428 1.000 68.23655 ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -4.74204  -16.01145 -42.66701 1.000 70.54864 ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -5.49693  -17.67877 -41.45673 1.000 68.66071 ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -4.07261  -17.92030 -37.28599 1.000 22.63479 ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -4.06685  -18.36558 -35.89273 1.000 20.46058 ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.81599  -19.18997 -35.59417 1.000 20.65890 ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.53398  -20.16921 -36.29499 1.000 23.04304 ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -5.31566  -19.20349 -35.60628 1.000 25.12350 ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.55288  -19.48046 -34.12605 1.000 24.33054 ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.98377  -19.90626 -33.85129 1.000 32.54155 ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.92525  -19.20820 -34.21350 1.000 32.38294 ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -7.15269  -21.06342 -33.22110 1.000 26.40530 ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -2.09166  -18.82005 -34.53410 1.000 20.41297 ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.81126  -19.44070 -34.20351 1.000 20.44069 ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.81467  -19.90490 -32.75355 1.000 20.03425 ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.53918  -19.36529 -31.91784 1.000 18.73632 ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.35042   -18.45698 -34.40906 1.000 18.17425 ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 0.79034   -18.37116 -35.85197 1.000 24.98825 ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 1.64737   -19.31545 -36.39913 1.000 24.89632 ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 0.30013   -17.36777 -36.68108 1.000 24.91034 ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 2.03309   -19.24064 -37.72977 1.000 30.22111 ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 0.67349   -17.29207 -38.01068 1.000 31.08522 ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.53485   -18.22815 -38.52541 1.000 30.17493 ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 1.89768   -18.14573 -39.85025 1.000 40.55490 ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 0.00905   -20.91346 -32.46741 1.000 16.84419 ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.21276   -21.41331 -31.11355 1.000 15.65838 ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 1.69028   -21.30581 -30.76809 1.000 20.38366 ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.53652   -21.84778 -31.49108 1.000 19.02538 ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? -0.25539  -22.86259 -30.98615 1.000 19.23636 ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 1.97980   -20.61224 -29.66928 1.000 17.07553 ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.29160   -20.50204 -29.03649 1.000 15.21378 ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.30395   -21.41471 -27.81364 1.000 20.42114 ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.29095   -21.56412 -27.13694 1.000 17.58618 ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.49722   -19.04444 -28.63100 1.000 16.21928 ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 4.72773   -18.64733 -27.89292 1.000 15.86005 ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 5.79053   -17.97546 -28.40945 1.000 16.11714 ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 4.99279   -18.80435 -26.48195 1.000 17.09383 ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 6.71907   -17.72481 -27.41983 1.000 17.92205 ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.25286   -18.22633 -26.23312 1.000 17.97536 ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.30083   -19.39630 -25.41734 1.000 17.84726 ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 6.83186   -18.21027 -24.96089 1.000 18.02803 ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 4.88694   -19.37059 -24.14106 1.000 16.36711 ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.13198   -18.78866 -23.93723 1.000 17.43438 ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.44437   -22.03090 -27.52601 1.000 18.41182 ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.53074   -22.91994 -26.37163 1.000 16.24554 ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 5.93263   -22.90657 -25.78954 1.000 19.38003 ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 6.91506   -22.87388 -26.52641 1.000 18.29392 ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.17178   -24.36276 -26.72824 1.000 25.12519 ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 3.72600   -25.20018 -25.54457 1.000 26.79887 ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 2.95369   -26.42790 -25.97649 1.000 39.95746 ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 1.71502   -26.45180 -25.79667 1.000 32.88963 ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 3.58366   -27.34669 -26.54516 1.000 37.73772 ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.01719   -23.00105 -24.46346 1.000 18.59692 ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.32209   -23.12437 -23.82763 1.000 17.31174 ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.17749   -23.73311 -22.44316 1.000 15.94418 ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.28910   -23.35315 -21.67454 1.000 16.32465 ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.02281   -21.77030 -23.71749 1.000 15.30488 ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.32164   -21.93247 -23.13434 1.000 19.77129 ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.06606   -24.68057 -22.14203 1.000 17.80571 ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.28512   -25.16471 -20.78307 1.000 18.20093 ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.54860   -24.56191 -20.17659 1.000 20.69750 ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.21847  -25.20791 -19.35159 1.000 22.55813 ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.37421   -26.69072 -20.78345 1.000 21.92702 ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.18749   -27.25783 -21.32031 1.000 27.81099 ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 9.89325   -23.34768 -20.59497 1.000 17.36144 ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.13391  -22.65293 -20.21463 1.000 20.10937 ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.31341  -23.51896 -20.68355 1.000 22.29988 ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.25444  -24.14151 -21.74982 1.000 26.74676 ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.10143  -22.31635 -18.73187 1.000 23.78126 ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.41558  -23.56409 -19.94097 1.000 28.25783 ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.55619  -24.31165 -20.44459 1.000 25.87640 ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.19975  -23.75160 -21.70097 1.000 23.14954 ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 15.94587  -24.46173 -22.38356 1.000 27.61865 ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 14.92029  -22.49915 -22.04104 1.000 18.56588 ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.69572  -21.80737 -23.04589 1.000 19.27976 ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.09203  -21.74687 -24.42979 1.000 20.37966 ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.70610  -21.13776 -25.31421 1.000 20.47572 ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 13.92301  -22.35025 -24.66090 1.000 19.71174 ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.39570  -22.39343 -26.02108 1.000 17.11759 ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 11.87628  -22.32273 -25.99474 1.000 18.14315 ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.23505  -22.63064 -24.98494 1.000 19.08084 ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 13.85044  -23.65259 -26.77362 1.000 24.41677 ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.28085  -24.82333 -26.20627 1.000 24.91775 ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.31142  -21.91037 -27.13336 1.000 18.60107 ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 9.86975   -21.91038 -27.35594 1.000 17.32269 ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.60039   -22.38951 -28.77530 1.000 18.32753 ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.49578  -22.41518 -29.62484 1.000 20.17865 ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.21945   -20.52481 -27.12562 1.000 16.57932 ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 9.72777   -19.43663 -28.04104 1.000 18.62928 ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 10.87795  -18.72789 -27.71973 1.000 18.74501 ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 9.04233   -19.09943 -29.19786 1.000 19.18578 ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 11.34750  -17.71753 -28.54888 1.000 23.53626 ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 9.50980   -18.10091 -30.02926 1.000 17.67574 ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.65952  -17.39419 -29.70294 1.000 20.31079 ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.35235   -22.78847 -29.02280 1.000 17.40200 ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 7.95285   -23.24673 -30.34312 1.000 16.76736 ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 6.79452   -22.39180 -30.83033 1.000 17.90170 ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 6.04392   -21.81696 -30.02878 1.000 18.24340 ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.53794   -24.74991 -30.36458 1.000 20.26618 ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.36843   -24.94603 -29.55250 1.000 23.47266 ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 8.66020   -25.66850 -29.87777 1.000 22.57448 ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 6.68739   -22.29043 -32.15582 1.000 19.45228 ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.56840   -21.62895 -32.81726 1.000 20.15976 ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.10882   -22.53150 -33.95372 1.000 22.72573 ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 5.93060   -23.03677 -34.73169 1.000 21.14420 ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 5.93794   -20.22725 -33.34842 1.000 20.89668 ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 4.74711   -19.60225 -34.10566 1.000 20.06556 ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.39333   -19.31417 -32.22169 1.000 19.40193 ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 3.79827   -22.74743 -34.04399 1.000 19.61525 ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.21528   -23.51638 -35.12651 1.000 20.91987 ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 1.87618   -22.89451 -35.48465 1.000 21.03191 ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.24844   -22.21684 -34.67136 1.000 20.15139 ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 3.01995   -24.98899 -34.74688 1.000 25.89205 ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 2.01706   -25.19287 -33.61569 1.000 25.74547 ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 2.19894   -26.53762 -32.93261 1.000 38.27184 ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.26241   -26.47914 -31.93489 1.000 35.61904 ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 3.91534   -27.53316 -31.46112 1.000 47.59870 ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 3.60608   -28.76342 -31.83456 1.000 38.79035 ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 4.90394   -27.34744 -30.58849 1.000 40.81140 ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.45086   -23.12151 -36.71710 1.000 25.33964 ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 0.09231   -22.75576 -37.08655 1.000 27.33222 ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.86056  -23.56908 -36.22455 1.000 26.94952 ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.62928  -24.75530 -35.96912 1.000 34.78495 ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? -0.15834  -23.03598 -38.56773 1.000 33.08653 ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 0.35984   -24.32487 -38.89580 1.000 49.09796 ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? 0.56959   -22.01221 -39.41699 1.000 30.15175 ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.91740  -22.93236 -35.74000 1.000 28.11267 ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.82919  -23.61465 -34.83796 1.000 30.43778 ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.92131  -24.28946 -35.65096 1.000 44.68752 ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.64293  -23.62753 -36.40452 1.000 43.42004 ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -3.44367  -22.66032 -33.82015 1.000 30.73261 ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -4.27000  -23.39457 -32.77966 1.000 40.89248 ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -3.78986  -24.42761 -32.26413 1.000 47.51924 ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -5.40208  -22.95885 -32.49408 1.000 35.44531 ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -4.03915  -25.60396 -35.48772 1.000 50.87652 ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -5.09393  -26.36840 -36.13533 1.000 68.20880 ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.38380  -26.39264 -35.32445 1.000 65.01678 ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.42955  -26.77936 -35.85993 1.000 63.75893 ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.61203  -27.80097 -36.38417 1.000 68.65917 ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.96659  -28.29975 -35.20185 1.000 55.55485 ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -3.63173  -27.83491 -37.54455 1.000 61.81412 ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -6.33447  -25.97719 -34.05901 1.000 63.80978 ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -7.45821  -26.10861 -33.15128 1.000 58.42653 ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.67524  -25.26114 -33.46566 1.000 52.44719 ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.84505  -24.77075 -34.58723 1.000 48.45390 ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -9.53164  -25.09768 -32.46561 1.000 48.21998 ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.75689 -24.32135 -32.59133 1.000 43.93665 ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -10.45790 -22.88536 -33.01015 1.000 38.71524 ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.70045  -22.20020 -32.31413 1.000 33.52110 ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -11.49591 -24.34021 -31.25465 1.000 43.87774 ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -12.95887 -24.68965 -31.36825 1.000 55.94417 ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -13.18113 -26.00833 -32.07622 1.000 47.00005 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -13.62164 -25.98311 -33.23962 1.000 57.74155 ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -12.89032 -27.06620 -31.48337 1.000 59.18404 ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -11.01251 -22.40091 -34.12582 1.000 39.22414 ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.81201 -20.99446 -34.50601 1.000 42.27630 ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -11.27725 -20.05319 -33.40385 1.000 44.03210 ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -12.31858 -20.27159 -32.77962 1.000 41.61632 ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.67313 -20.83267 -35.76515 1.000 40.86553 ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -12.22600 -22.18496 -36.09321 1.000 38.77862 ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.59831 -23.20409 -35.21181 1.000 43.47943 ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.49938 -18.99200 -33.16404 1.000 33.11302 ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.87127 -18.05745 -32.10909 1.000 32.60422 ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.52689 -16.77829 -32.60141 1.000 35.31778 ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -12.11084 -16.05927 -31.78472 1.000 43.25103 ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -9.67728  -17.61267 -31.26568 1.000 29.98229 ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -9.09739  -18.61826 -30.32057 1.000 44.53533 ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -7.37932  -18.13653 -30.18413 1.000 41.94445 ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -7.66549  -16.57594 -29.38309 1.000 32.28004 ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.40329 -16.43865 -33.87521 1.000 34.06708 ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -11.97444 -15.18424 -34.33015 1.000 26.03090 ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -11.00479 -14.03385 -34.18202 1.000 26.27066 ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.53428 -13.47981 -35.17963 1.000 26.39905 ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.68575 -13.68725 -32.93281 1.000 21.46679 ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.70872  -12.64907 -32.61583 1.000 20.62207 ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.40083  -12.71020 -31.12873 1.000 22.60739 ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.32888 -12.80644 -30.31702 1.000 21.19276 ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -10.22857 -11.24412 -32.97998 1.000 19.50508 ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -9.12357  -10.17342 -32.89575 1.000 20.70492 ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.66925  -8.74404  -32.71797 1.000 21.80875 ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.60000 -8.61392  -31.59275 1.000 18.12579 ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.91324 -8.49191  -31.70910 1.000 19.25605 ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.51142 -8.51303  -32.89221 1.000 21.29353 ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.65061 -8.33937  -30.61133 1.000 20.24727 ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -8.12975  -12.64133 -30.75321 1.000 20.79725 ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.77812  -12.51087 -29.35328 1.000 18.11029 ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.65729  -13.44912 -28.97126 1.000 22.17596 ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -5.87030  -13.89051 -29.80690 1.000 18.97849 ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.58885  -13.75199 -27.68183 1.000 15.92098 ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.46977  -14.50630 -27.14085 1.000 16.43593 ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -5.97494  -15.43737 -26.05766 1.000 21.76690 ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.78865  -15.04332 -25.21849 1.000 18.33724 ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.39661  -13.56793 -26.57689 1.000 21.07970 ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.84159  -12.79778 -27.65308 1.000 19.70506 ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -3.26726  -14.37326 -25.90820 1.000 21.98891 ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.49285  -16.67308 -26.09392 1.000 17.62555 ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.78263  -17.68214 -25.08347 1.000 20.44464 ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.45940  -18.06676 -24.43797 1.000 15.47250 ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.56160  -18.53853 -25.13805 1.000 20.02184 ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.44962  -18.88785 -25.75586 1.000 24.50507 ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -7.04160  -19.93672 -24.88318 1.000 34.79782 ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -7.44831  -21.15862 -25.71217 1.000 42.38844 ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -8.76385  -20.92355 -26.42967 1.000 46.81632 ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -9.09973  -22.03734 -27.37639 1.000 46.34922 ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.32600  -17.84498 -23.12945 1.000 16.26682 ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -3.14437  -18.28183 -22.37821 1.000 19.94648 ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.52691  -19.52332 -21.57666 1.000 20.94930 ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.36648  -19.44761 -20.66834 1.000 20.59227 ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.61571  -17.17567 -21.45173 1.000 15.93644 ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.41055  -17.69194 -20.65342 1.000 17.88059 ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -2.23620  -15.91551 -22.24548 1.000 16.79122 ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.89962  -20.65318 -21.88804 1.000 17.77385 ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -3.18234  -21.92714 -21.22666 1.000 16.87459 ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -2.02361  -22.23342 -20.28326 1.000 16.59203 ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.90739  -22.52330 -20.73435 1.000 18.00651 ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.37948  -23.06690 -22.23073 1.000 18.21982 ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.40698  -22.68004 -23.30500 1.000 21.15770 ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.79063  -24.36048 -21.49333 1.000 20.10069 ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.48169  -23.65381 -24.43072 1.000 31.26889 ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.31030  -22.21798 -18.98871 1.000 15.38011 ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.33241  -22.49887 -17.93629 1.000 17.47965 ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.44334  -23.96873 -17.55309 1.000 19.03772 ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.44815  -24.37662 -16.96413 1.000 20.38544 ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.58912  -21.61904 -16.71624 1.000 17.34546 ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.65300  -20.12163 -16.96805 1.000 16.43798 ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -2.00903  -19.38182 -15.69865 1.000 23.79017 ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.30392  -19.66882 -17.51208 1.000 22.04497 ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.40258  -24.75600 -17.84460 1.000 17.22565 ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.34568  -26.14819 -17.39032 1.000 20.11587 ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.29902   -26.12316 -16.00591 1.000 20.52713 ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.51403   -25.98952 -15.87800 1.000 20.75806 ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.42309   -27.01889 -18.37994 1.000 22.82818 ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? -0.07190  -26.90832 -19.79266 1.000 25.35009 ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.87189  -27.86510 -20.38056 1.000 33.35829 ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.11445   -25.94600 -20.73146 1.000 24.53671 ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -1.15067  -27.50142 -21.62138 1.000 28.56451 ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.56764  -26.33856 -21.85754 1.000 30.66741 ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.51857  -26.21711 -14.96487 1.000 17.73534 ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? -0.06488  -25.87235 -13.62275 1.000 19.34407 ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 0.91047   -26.90463 -13.07083 1.000 23.28472 ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.82169   -28.10606 -13.35781 1.000 21.54442 ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.26646  -25.74989 -12.68234 1.000 17.36744 ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -2.20775  -24.59698 -13.02918 1.000 16.58374 ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.32468  -24.55722 -11.99255 1.000 23.50077 ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.49411  -23.25449 -13.06325 1.000 22.96420 ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 1.85028   -26.42695 -12.25393 1.000 22.68843 ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.67908   -27.33925 -11.48227 1.000 23.47982 ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.82939   -28.12765 -10.48983 1.000 24.75703 ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.78466   -27.66620 -10.02169 1.000 26.06670 ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.77438   -26.57699 -10.73554 1.000 27.70106 ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.61243   -25.67273 -11.61155 1.000 28.11683 ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.84400   -25.20195 -10.85975 1.000 34.59358 ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 5.74681   -23.73175 -10.49135 1.000 41.67791 ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 6.98109   -22.96844 -10.89348 1.000 45.59882 ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.30826   -29.32635 -10.15626 1.000 26.51778 ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.53627   -30.25049 -9.33321  1.000 29.25636 ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.13393   -29.63954 -7.99116  1.000 33.82499 ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.06346   -29.96003 -7.45924  1.000 34.01648 ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.35114   -31.53233 -9.13731  1.000 39.41874 ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 1.68812   -32.61006 -8.32539  1.000 51.75241 ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.48420   -33.89950 -8.36194  1.000 67.94013 ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 3.73244   -33.82064 -8.37573  1.000 64.34518 ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 1.86654   -34.98491 -8.38187  1.000 77.62145 ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 1.95413   -28.75218 -7.43084  1.000 29.24001 ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.66669   -28.18160 -6.12064  1.000 32.94792 ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 0.97634   -26.81372 -6.19826  1.000 28.34466 ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.88258   -26.11074 -5.18248  1.000 27.40289 ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 2.95131   -28.12806 -5.28429  1.000 38.33588 ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 3.96232   -27.11609 -5.80033  1.000 44.03852 ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 4.93169   -26.83158 -5.06610  1.000 52.97548 ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 3.82301   -26.62993 -6.94391  1.000 45.02709 ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.44570   -26.44358 -7.36389  1.000 23.06641 ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.19764  -25.14701 -7.53948  1.000 20.80889 ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.64239  -25.29352 -8.00308  1.000 20.14851 ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.18713  -24.40193 -8.66632  1.000 23.04759 ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.59778   -24.28353 -8.51732  1.000 22.22586 ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.04759   -24.06933 -8.07165  1.000 23.74700 ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.16270   -23.29331 -6.76308  1.000 27.32009 ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.32748   -22.44662 -6.45772  1.000 30.44841 ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.22181   -23.55459 -6.00553  1.000 27.76502 ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.28494  -26.40137 -7.65179  1.000 22.97674 ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.65789  -26.61303 -8.09663  1.000 22.51369 ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.67745  -25.79429 -7.31700  1.000 27.26852 ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.86731  -25.84912 -7.65191  1.000 26.94976 ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -4.03929  -28.09056 -8.00271  1.000 27.90326 ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.86434  -28.54167 -6.65423  1.000 29.38043 ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -3.19830  -28.92035 -8.96248  1.000 29.82174 ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.26324  -25.05458 -6.28365  1.000 25.08355 ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.21052  -24.15615 -5.63012  1.000 23.87941 ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.78260  -23.14093 -6.60587  1.000 22.82665 ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.89048  -22.64334 -6.38793  1.000 25.09370 ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.55424  -23.44129 -4.44480  1.000 26.49625 ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.74317  -22.21268 -4.81002  1.000 25.51935 ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.78211  -21.80547 -3.71643  1.000 34.50707 ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.90492  -22.61731 -3.33912  1.000 36.78603 ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -2.93846  -20.68099 -3.19446  1.000 32.23042 ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -5.07088  -22.85225 -7.69122  1.000 22.13989 ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.51116  -21.86719 -8.66776  1.000 22.22780 ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.53620  -22.43186 -9.64605  1.000 20.18190 ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.91579  -21.73563 -10.59205 1.000 24.70567 ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.28283  -21.28705 -9.38994  1.000 23.28757 ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.36900  -20.60319 -8.38277  1.000 18.58570 ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.78841  -19.46396 -7.69746  1.000 21.69411 ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.11711  -21.13073 -8.06076  1.000 20.69492 ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.99106  -18.85621 -6.75449  1.000 21.62018 ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.31052  -20.52941 -7.11780  1.000 22.97965 ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.74468  -19.38272 -6.46227  1.000 22.04830 ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.96082  -18.77416 -5.51259  1.000 27.02929 ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.98930  -23.67017 -9.42791  1.000 18.92070 ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.15034  -24.21852 -10.11274 1.000 22.41853 ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.41466  -24.15806 -9.27080  1.000 27.92880 ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.48793 -24.49266 -9.77973  1.000 26.30541 ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.89036  -25.67361 -10.51354 1.000 23.35174 ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.65053  -25.80514 -11.39867 1.000 24.58734 ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.34291  -27.27475 -11.66795 1.000 27.07910 ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.85500  -25.01681 -12.69047 1.000 29.53088 ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.30873  -23.76366 -8.00113  1.000 24.33109 ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.44376 -23.73831 -7.08383  1.000 25.75385 ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.24611 -22.46099 -7.29437  1.000 26.87367 ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.66899 -21.37091 -7.35561  1.000 25.81535 ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -9.94335  -23.79866 -5.63974  1.000 27.75683 ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.41994  -25.13685 -5.16194  1.000 30.54383 ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -10.35539 -26.30125 -5.44067  1.000 61.87751 ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -11.59243 -26.11079 -5.38669  1.000 62.68410 ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -9.85024  -27.41490 -5.70589  1.000 69.39025 ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.57387 -22.58895 -7.41589  1.000 25.41218 ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.39928 -21.40749 -7.66752  1.000 23.84597 ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.18385 -20.32782 -6.61116  1.000 21.28109 ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.99764 -19.14913 -6.93841  1.000 22.49773 ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.88558 -21.77897 -7.72805  1.000 24.09001 ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.72720 -20.63012 -8.27132  1.000 29.89050 ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.22859 -20.83362 -8.10226  1.000 48.42618 ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.63433 -21.83231 -7.47315  1.000 37.71911 ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -18.00205 -19.98880 -8.60711  1.000 41.31550 ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.22427 -20.70613 -5.32997  1.000 23.91196 ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.15681 -19.67738 -4.29709  1.000 24.88726 ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.80107 -18.97349 -4.28712  1.000 23.53913 ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.72769 -17.77985 -3.96256  1.000 22.97497 ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.49977 -20.28600 -2.93682  1.000 28.50366 ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.42014 -21.10905 -2.29228  1.000 31.06332 ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -13.03904 -21.90365 -1.14657  1.000 37.46934 ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.16602 -22.97556 -0.69741  1.000 52.93123 ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.17375 -23.46435 0.53374   1.000 49.27718 ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.06479 -23.06523 1.42812   1.000 52.96655 ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.26345 -24.37003 0.87716   1.000 51.02067 ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.72896 -19.68015 -4.66580  1.000 22.30771 ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.40536  -19.06669 -4.72147  1.000 19.77009 ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.30505  -18.08376 -5.88373  1.000 20.65042 ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.79072  -16.96932 -5.72897  1.000 19.32219 ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.33260  -20.14690 -4.85324  1.000 20.33882 ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.88978  -19.62269 -4.83032  1.000 21.42207 ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.49781  -18.99228 -3.49056  1.000 26.03362 ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -5.05558  -18.76286 -3.41764  1.000 20.84945 ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.48910  -17.57188 -3.25910  1.000 25.09456 ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.21276  -16.47987 -3.06296  1.000 24.48785 ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.16194  -17.47442 -3.29083  1.000 26.20564 ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.77831  -18.48216 -7.06539  1.000 18.33104 ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.73836  -17.57052 -8.20898  1.000 20.14496 ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.56818 -16.32803 -7.92187  1.000 18.92272 ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.12882 -15.19995 -8.17466  1.000 19.78380 ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.22345 -18.26735 -9.49402  1.000 22.10061 ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.32931  -19.45790 -9.84656  1.000 19.87527 ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.26423 -17.25036 -10.65618 1.000 18.80326 ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -10.03719 -20.49467 -10.76317 1.000 21.23682 ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.78920 -16.51849 -7.39622  1.000 19.81180 ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.63719 -15.38023 -7.04880  1.000 17.65398 ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.93033 -14.43181 -6.10175  1.000 20.11998 ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -12.05898 -13.21008 -6.23120  1.000 19.71144 ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.93484 -15.82663 -6.37567  1.000 22.33184 ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.98792 -16.45883 -7.24433  1.000 31.25700 ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.32308 -16.40218 -6.49025  1.000 36.38691 ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -16.84854 -17.78163 -6.15773  1.000 55.07093 ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -18.15823 -18.03710 -6.82251  1.000 58.25357 ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.25100 -14.98021 -5.08829  1.000 18.55509 ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.57337 -14.14134 -4.10445  1.000 20.57323 ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.48999  -13.30164 -4.76410  1.000 17.95512 ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.33227  -12.11418 -4.45437  1.000 19.97916 ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.97693  -15.02849 -3.00811  1.000 20.37091 ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -9.02442  -14.33053 -2.04126  1.000 22.31079 ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.32182  -15.32500 -1.13054  1.000 24.96182 ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.84457  -16.35379 -1.65796  1.000 27.16312 ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.26755  -15.09441 0.10258   1.000 26.42632 ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.73827  -13.90613 -5.68264  1.000 17.12596 ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.64140  -13.19967 -6.34002  1.000 18.63900 ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.17995  -12.12746 -7.27171  1.000 20.51554 ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.66451  -11.00260 -7.30878  1.000 22.10943 ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.74989  -14.19838 -7.09583  1.000 18.94571 ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -6.13976  -15.19652 -6.10983  1.000 19.54696 ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.65300  -13.46486 -7.86879  1.000 18.80536 ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.58522  -16.41430 -6.80564  1.000 22.86040 ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.22491  -12.45635 -8.03779  1.000 18.47337 ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.81137  -11.47739 -8.94376  1.000 18.40609 ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.34655 -10.28517 -8.16440  1.000 19.04792 ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -10.13034 -9.12904  -8.54725  1.000 21.14667 ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.90090 -12.14176 -9.80044  1.000 18.23263 ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.71200 -11.09492 -10.55996 1.000 22.96412 ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.26238 -13.16897 -10.75003 1.000 20.83583 ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -11.01622 -10.53399 -7.03385  1.000 17.62702 ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.56533 -9.42006  -6.26552  1.000 22.96063 ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.45634 -8.56716  -5.65087  1.000 23.67794 ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.56232 -7.33644  -5.61031  1.000 29.52952 ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.50756 -9.94514  -5.18706  1.000 23.22133 ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.06821 -8.85689  -4.28303  1.000 30.34616 ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -14.05532 -9.42984  -3.28898  1.000 36.00587 ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.52526 -8.34640  -2.32658  1.000 49.93100 ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -14.88786 -8.89043  -0.98422  1.000 54.49016 ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.36656  -9.20152  -5.20688  1.000 21.88364 ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.29568  -8.46890  -4.53696  1.000 23.05496 ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.55764  -7.55700  -5.50251  1.000 20.27376 ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.26002  -6.40800  -5.16422  1.000 22.98856 ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.31645  -9.45287  -3.89230  1.000 24.03354 ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.14556  -8.81851  -3.14152  1.000 27.02799 ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.46117  -9.89711  -2.31799  1.000 38.25239 ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.14262  -9.43698  -1.73664  1.000 46.58689 ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.44859  -10.57641 -1.06356  1.000 55.84280 ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.27415  -8.04609  -6.71765  1.000 19.79886 ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.35047  -7.38395  -7.63124  1.000 23.39794 ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.99765  -6.82442  -8.89385  1.000 27.87799 ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -6.37995  -5.98632  -9.56015  1.000 25.45434 ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -5.24379  -8.36548  -8.05957  1.000 23.65099 ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.38977  -8.84499  -6.92854  1.000 28.91547 ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.54658  -8.01196  -6.22056  1.000 27.00469 ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -4.25873  -10.07306 -6.37215  1.000 30.69370 ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.92917  -8.70847  -5.28214  1.000 31.77801 ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.34468  -9.96129  -5.35135  1.000 32.12990 ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -8.21033  -7.26238  -9.24622  1.000 19.11987 ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.77893  -6.94117  -10.55136 1.000 21.41384 ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -10.25224 -6.55783  -10.46666 1.000 22.35697 ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.95525 -6.60349  -11.48254 1.000 23.96863 ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.59537  -8.12347  -11.52329 1.000 21.97517 ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -7.24060  -8.54563  -11.54046 1.000 25.17326 ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.72523 -6.14600  -9.28749  1.000 27.09377 ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -12.14247 -5.85541  -9.11398  1.000 35.99875 ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -12.61750 -4.72463  -10.03010 1.000 36.61815 ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -13.78369 -4.71729  -10.43942 1.000 35.59968 ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -12.41175 -5.54555  -7.63871  1.000 34.94323 ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -13.76686 -4.95356  -7.32757  1.000 51.52882 ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -13.89241 -4.53486  -5.87629  1.000 49.27460 ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -12.91334 -4.13162  -5.23893  1.000 50.67132 ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -15.10472 -4.62777  -5.34249  1.000 73.44941 ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -11.73108 -3.80415  -10.42115 1.000 28.80519 ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -12.14092 -2.65245  -11.22006 1.000 31.00991 ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -11.74381 -2.72600  -12.70124 1.000 31.31579 ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -11.89078 -1.71859  -13.40267 1.000 28.23013 ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -11.59189 -1.35242  -10.61949 1.000 34.86109 ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -11.85788 -1.19291  -9.14858  1.000 38.00996 ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -13.15720 -1.18539  -8.65903  1.000 40.93202 ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -10.81060 -0.98006  -8.26080  1.000 42.06735 ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -13.40370 -1.02194  -7.30436  1.000 39.02206 ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -11.05042 -0.80856  -6.90465  1.000 50.14575 ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -12.34713 -0.82744  -6.42555  1.000 53.28576 ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -11.24656 -3.87055  -13.19126 1.000 22.48965 ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.97868 -4.02976  -14.62314 1.000 23.54805 ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -12.22493 -3.63371  -15.41156 1.000 28.98011 ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -13.34984 -3.96107  -15.02199 1.000 26.05268 ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -10.55585 -5.48076  -14.93554 1.000 21.15366 ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -9.14054  -5.77913  -14.43327 1.000 28.72616 ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -10.58788 -5.76407  -16.43278 1.000 23.35809 ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -8.06374  -5.20696  -15.32151 1.000 30.32164 ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -12.03013 -2.89858  -16.50975 1.000 20.92735 ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -13.14894 -2.34085  -17.25565 1.000 21.82061 ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.71857 -3.24129  -18.34231 1.000 23.69005 ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.30670 -2.75486  -19.31567 1.000 24.34302 ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.52798 -4.54765  -18.20271 1.000 18.60020 ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -14.12530 -5.54086  -19.08180 1.000 22.14068 ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.74103 -6.63159  -18.22855 1.000 24.27164 ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -14.26394 -6.88829  -17.12063 1.000 22.15270 ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -13.07762 -6.15111  -20.02272 1.000 17.11434 ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.48474 -5.10264  -20.90765 1.000 19.74676 ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -13.12293 -4.71330  -22.08062 1.000 19.80309 ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.29409 -4.47288  -20.56924 1.000 22.23552 ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.58992 -3.72008  -22.89066 1.000 24.09201 ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.75128 -3.48376  -21.37790 1.000 19.90300 ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.39851 -3.11340  -22.53797 1.000 20.88074 ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.89418 -2.12687  -23.35915 1.000 24.89520 ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.80028 -7.28731  -18.70244 1.000 20.86966 ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.40490 -8.36481  -17.90215 1.000 18.09865 ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.46208 -9.55783  -17.80382 1.000 19.27437 ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.93007 -10.03387 -18.81047 1.000 22.07158 ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.69206 -8.71289  -18.67282 1.000 21.19607 ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.43280 -8.27613  -20.05916 1.000 23.84801 ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.53878 -7.04594  -19.95706 1.000 23.41539 ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.23316 -10.01883 -16.57774 1.000 19.78593 ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.43549 -11.21414 -16.31062 1.000 18.55450 ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.39222 -12.29783 -15.84958 1.000 22.73880 ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -16.03895 -12.15549 -14.79768 1.000 22.68796 ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.35850 -10.96476 -15.24362 1.000 21.72881 ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.36459 -9.88082  -15.69257 1.000 20.58789 ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.65210 -12.28312 -14.86738 1.000 18.04219 ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.44852 -9.40884  -14.56399 1.000 17.99329 ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.48947 -13.37320 -16.62837 1.000 18.57511 ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.37301 -14.48719 -16.30555 1.000 15.52311 ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.53950 -15.66701 -15.84816 1.000 15.00094 ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.69054 -16.16014 -16.59745 1.000 17.68493 ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -17.23578 -14.88156 -17.50731 1.000 19.72388 ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -18.02836 -13.76096 -17.91007 1.000 18.97182 ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -18.17516 -16.04515 -17.14771 1.000 19.98173 ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.78442 -16.11304 -14.61964 1.000 19.87650 ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -15.13384 -17.30210 -14.08070 1.000 16.06371 ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -16.04204 -18.49123 -14.37013 1.000 17.45402 ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -17.15009 -18.58012 -13.82115 1.000 17.70267 ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.87618 -17.13048 -12.58647 1.000 15.39277 ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.36673 -18.36590 -11.85185 1.000 18.75298 ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -13.12825 -18.92026 -12.54720 1.000 21.03978 ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -14.06573 -18.01979 -10.39344 1.000 22.67315 ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.58426 -19.38148 -15.25290 1.000 17.17717 ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.34216 -20.57491 -15.61335 1.000 18.08762 ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.32146 -21.55892 -14.45183 1.000 20.97236 ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.35591 -21.61793 -13.68037 1.000 21.97484 ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.72956 -21.26797 -16.84498 1.000 17.94148 ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -16.00584 -20.57994 -18.17916 1.000 18.13436 ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -16.11679 -19.19831 -18.27914 1.000 17.68669 ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -16.09640 -21.33640 -19.34231 1.000 18.75529 ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.33676 -18.57912 -19.51802 1.000 17.72788 ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.33157 -20.73309 -20.59049 1.000 19.65321 ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.44832 -19.35441 -20.67684 1.000 21.51220 ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.37802 -22.35343 -14.33402 1.000 20.90589 ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.41996 -23.40824 -13.33385 1.000 23.38680 ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.28378 -24.75739 -14.03780 1.000 25.09203 ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.37200 -24.85676 -15.26131 1.000 27.81748 ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.68972 -23.32919 -12.47697 1.000 35.65548 ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.54518 -22.18413 -11.48039 1.000 35.08153 ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.87198 -23.10499 -13.35009 1.000 27.72403 ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -17.02976 -25.80081 -13.25336 1.000 27.44704 ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.84744 -27.14019 -13.79701 1.000 34.35677 ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.93426 -28.09128 -13.31097 1.000 41.19047 ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.56357 -27.87226 -12.27376 1.000 43.94259 ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.46801 -27.70858 -13.42835 1.000 35.78876 ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.32120 -26.77030 -13.74565 1.000 33.88586 ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.98775 -27.30901 -13.26916 1.000 41.64106 ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.59781 -28.42158 -13.70186 1.000 36.98176 ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.33924 -26.62224 -12.44867 1.000 40.86719 ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -18.13074 -29.16508 -14.07848 1.000 44.82610 ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -19.09941 -30.21625 -13.76358 1.000 49.01116 ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -18.86936 -30.86815 -12.39378 1.000 63.81832 ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -17.73195 -31.02929 -11.94199 1.000 60.51314 ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -19.07095 -31.29540 -14.85511 1.000 55.42884 ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -19.93044 -32.51548 -14.56504 1.000 58.36901 ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -19.96347 -33.46741 -15.76777 1.000 60.40112 ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -20.18964 -34.91593 -15.34637 1.000 68.57552 ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -21.22485 -35.04374 -14.28355 1.000 73.38337 ? 224 LYS   A NZ  1 
HETATM 1645 C C11 . A1AYB B 2 .   ? -6.80699  -2.33993  -8.22733  1.000 35.71609 ? 301 A1AYB A C11 1 
HETATM 1646 C C12 . A1AYB B 2 .   ? -8.35296  -1.82430  -13.19180 0.888 28.06644 ? 301 A1AYB A C12 1 
HETATM 1647 C C13 . A1AYB B 2 .   ? -7.56854  -1.66261  -14.32507 1.000 32.44020 ? 301 A1AYB A C13 1 
HETATM 1648 C C5  . A1AYB B 2 .   ? -6.82547  -3.48544  -12.37931 0.781 35.06786 ? 301 A1AYB A C5  1 
HETATM 1649 C C1  . A1AYB B 2 .   ? -3.58814  -1.23062  -14.53971 0.929 58.07876 ? 301 A1AYB A C1  1 
HETATM 1650 C C2  . A1AYB B 2 .   ? -5.55345  -2.21945  -15.73077 1.000 40.57711 ? 301 A1AYB A C2  1 
HETATM 1651 C C3  . A1AYB B 2 .   ? -6.40007  -2.39407  -14.49753 0.404 36.14474 ? 301 A1AYB A C3  1 
HETATM 1652 C C4  . A1AYB B 2 .   ? -6.04431  -3.30428  -13.50905 0.773 39.15553 ? 301 A1AYB A C4  1 
HETATM 1653 C C10 . A1AYB B 2 .   ? -7.45684  -3.05788  -7.25327  0.566 30.60965 ? 301 A1AYB A C10 1 
HETATM 1654 C C6  . A1AYB B 2 .   ? -7.97246  -2.73799  -12.23243 0.667 27.96703 ? 301 A1AYB A C6  1 
HETATM 1655 C C7  . A1AYB B 2 .   ? -8.30473  -2.95608  -9.81075  0.701 28.40698 ? 301 A1AYB A C7  1 
HETATM 1656 C C8  . A1AYB B 2 .   ? -9.04852  -3.70228  -8.90854  0.561 27.74037 ? 301 A1AYB A C8  1 
HETATM 1657 C C9  . A1AYB B 2 .   ? -8.59761  -3.75220  -7.60936  0.792 39.59147 ? 301 A1AYB A C9  1 
HETATM 1658 N N1  . A1AYB B 2 .   ? -4.58728  -1.09265  -15.61974 1.000 49.39947 ? 301 A1AYB A N1  1 
HETATM 1659 N N2  . A1AYB B 2 .   ? -7.22376  -2.27677  -9.50707  0.510 26.31401 ? 301 A1AYB A N2  1 
HETATM 1660 O O1  . A1AYB B 2 .   ? -8.78382  -2.92136  -11.09395 0.718 28.71166 ? 301 A1AYB A O1  1 
HETATM 1661 O O   . HOH   C 3 .   ? -12.60192 -27.24970 -34.49014 1.000 49.07267 ? 401 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? -13.87866 -7.09445  -42.19215 1.000 56.89785 ? 402 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? 11.37447  -22.03277 -40.48717 1.000 46.03312 ? 403 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? -14.23828 -10.59222 0.49994   1.000 49.05842 ? 404 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? 16.32797  1.16129   -15.22136 1.000 34.29165 ? 405 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? -13.85517 -15.35722 -30.31358 1.000 44.69158 ? 406 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? -12.10334 -28.12481 -29.49296 1.000 38.43752 ? 407 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? -17.55106 -33.16446 -10.83152 1.000 55.62422 ? 408 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? 9.31662   -24.22134 -41.30190 1.000 61.52597 ? 409 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? -10.58737 -4.54208  -4.68827  1.000 44.41920 ? 410 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? 2.79974   -25.00532 -38.45009 1.000 36.11519 ? 411 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 1.65451   -15.65777 -41.17344 1.000 43.29243 ? 412 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? -18.02193 -4.88789  -36.95491 1.000 47.45138 ? 413 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? -3.06029  -5.54990  -6.52205  1.000 43.79342 ? 414 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? -0.34729  -5.61566  -38.59437 1.000 42.82672 ? 415 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? -4.36373  -4.50628  -9.10657  1.000 40.97280 ? 416 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? 7.62477   -22.86836 -14.05190 1.000 30.87408 ? 417 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 0.16682   -14.21446 -1.61994  1.000 50.02201 ? 418 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? 5.112     -9.226    -2.657    1.000 44.79841 ? 419 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? 3.40584   -8.02829  -36.83758 1.000 32.41488 ? 420 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? -5.98442  -1.93849  -19.70638 1.000 22.33352 ? 421 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -8.85718  -10.42663 -40.50096 1.000 42.65058 ? 422 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? -16.25697 -25.38052 -17.53506 1.000 26.22213 ? 423 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? -8.36447  3.87474   -38.70300 1.000 45.35493 ? 424 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? -1.52601  -28.61317 -5.54232  1.000 33.40074 ? 425 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? -1.31730  -32.14566 -7.23766  1.000 52.03756 ? 426 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? 6.01487   -20.52418 -0.18201  1.000 30.82352 ? 427 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? -0.57140  -5.09139  -18.34581 1.000 26.93136 ? 428 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? -13.36707 -7.40162  -12.08160 1.000 39.62005 ? 429 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? -15.08300 -4.14552  -12.63895 1.000 41.61774 ? 430 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? -20.64309 -13.96911 -18.12091 1.000 47.97097 ? 431 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 6.29767   -29.40688 -20.08913 1.000 35.66105 ? 432 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? -7.65404  -4.83407  -3.08982  1.000 44.95974 ? 433 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? -3.70322  -13.96405 -0.74940  1.000 41.31443 ? 434 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 3.13294   -5.41017  -6.41552  1.000 47.93359 ? 435 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? 8.95374   -26.28216 -16.93513 1.000 30.55317 ? 436 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -13.45104 -0.59436  -20.60292 1.000 34.88129 ? 437 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? -8.39615  4.66276   -33.87004 1.000 31.69276 ? 438 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? 15.72057  -0.80599  -19.91210 1.000 29.68404 ? 439 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? 0.25862   -30.96944 -23.11876 1.000 50.85434 ? 440 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? 9.29399   -11.34421 -35.00256 1.000 35.85801 ? 441 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? -2.59892  -10.71784 -26.54557 1.000 33.83677 ? 442 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? 8.00752   -22.70566 -7.17265  1.000 38.00290 ? 443 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? -14.72635 -22.21840 -11.15383 1.000 30.90636 ? 444 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? 7.60572   -18.43652 -6.60603  1.000 26.68228 ? 445 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? 0.41857   -4.95798  -14.01321 1.000 44.27290 ? 446 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? -15.26406 -10.88787 -29.79138 1.000 27.86751 ? 447 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? 9.57242   -16.97585 -7.76173  1.000 25.77707 ? 448 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? 11.38979  -27.54828 -34.51298 1.000 26.98630 ? 449 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? -8.29789  -24.59326 -18.87366 1.000 19.69006 ? 450 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 0.83801   -20.51241 -4.52868  1.000 26.28102 ? 451 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? 3.26388   -5.89246  -11.36364 1.000 24.17615 ? 452 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? -18.92975 -10.72197 -23.81572 1.000 33.85661 ? 453 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? 18.28835  -15.64254 -13.68436 1.000 41.95580 ? 454 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? -2.39665  -13.70733 -35.63541 1.000 21.47260 ? 455 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? 6.45566   -26.70076 -27.51266 1.000 34.20276 ? 456 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? -19.94069 -21.68059 -6.08218  1.000 54.09735 ? 457 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? -7.81393  -24.31955 -22.71231 1.000 31.93684 ? 458 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? -6.12676  -18.65480 -39.02032 1.000 38.82697 ? 459 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -13.11958 -24.47629 -10.38558 1.000 36.97759 ? 460 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? 4.13376   -19.48917 -40.62515 1.000 39.73777 ? 461 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -3.71493  -10.72890 -24.11241 1.000 25.36112 ? 462 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? -13.61511 -26.19139 -17.59599 1.000 27.15498 ? 463 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? -7.34294  -27.64941 -20.89994 1.000 44.77267 ? 464 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -5.47888  -10.34423 -27.41863 1.000 19.46699 ? 465 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? -15.81432 6.13631   -32.97439 1.000 44.25652 ? 466 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -14.83489 -6.82577  -14.46443 1.000 39.68392 ? 467 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? 5.67428   -22.00086 -37.25375 1.000 34.22122 ? 468 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? 9.68224   -14.73431 -25.32813 1.000 21.22363 ? 469 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? 13.48166  -14.16100 -27.06532 1.000 24.59533 ? 470 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? -9.58263  -31.04652 -22.79642 1.000 49.76655 ? 471 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? -16.47989 -12.49214 -19.75465 1.000 19.97604 ? 472 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? -9.48471  -2.25235  -17.52062 1.000 20.22268 ? 473 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? 10.94543  -8.16173  -27.70488 1.000 21.90819 ? 474 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? -6.55870  -7.79305  -34.43135 1.000 21.94894 ? 475 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? -6.27292  -7.29249  -42.28936 1.000 50.80145 ? 476 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 10.99923  -28.38994 -30.38226 1.000 30.82944 ? 477 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? -17.32639 -24.33200 -8.54095  1.000 52.70713 ? 478 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -5.48767  -7.19152  -13.14583 1.000 19.68324 ? 479 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -5.85367  -30.86918 -11.24483 1.000 31.93553 ? 480 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? 7.40117   -27.68568 -24.02739 1.000 31.71990 ? 481 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? -1.42139  -4.69957  -33.98813 1.000 45.36721 ? 482 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? -18.28240 -3.78027  -29.12202 1.000 40.86925 ? 483 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -1.24018  -7.39050  -23.66365 1.000 24.01372 ? 484 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? -11.14326 -14.33061 -37.72832 1.000 33.74673 ? 485 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? -9.15485  -17.90086 -36.30721 1.000 39.06391 ? 486 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? 1.33018   -7.68818  -16.76411 1.000 24.53986 ? 487 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? 1.44526   -25.80023 -2.49923  1.000 50.50108 ? 488 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -16.58685 -8.97228  -14.40941 1.000 37.78321 ? 489 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? -13.64904 -16.43383 -2.49259  1.000 25.50398 ? 490 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? -6.39579  -5.10295  -35.71769 1.000 22.93011 ? 491 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 2.99554   -20.01300 -2.55800  1.000 42.87794 ? 492 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? 18.18601  -7.21420  -20.61298 1.000 35.42926 ? 493 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 14.22521  -15.91532 -30.72347 1.000 34.18413 ? 494 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? -17.305   -28.555   -16.664   1.000 42.54315 ? 495 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? 0.57629   -29.52818 -15.76741 1.000 35.63166 ? 496 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? -13.62867 -25.16741 -7.53298  1.000 33.59413 ? 497 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? 8.53680   -20.15089 -9.22678  1.000 30.97024 ? 498 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? 3.88112   -24.13320 -30.55188 1.000 22.58556 ? 499 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? -1.63717  -6.36157  -26.23785 1.000 24.36423 ? 500 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? -8.02836  1.63362   -36.93653 1.000 37.86351 ? 501 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? 10.41062  -25.22107 -23.56822 1.000 23.86159 ? 502 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? 17.81965  -19.41573 -24.68827 1.000 31.10228 ? 503 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -2.36418  -0.47740  -18.67953 1.000 46.64717 ? 504 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? -16.11314 -3.74015  -15.39888 1.000 44.92228 ? 505 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -17.14389 -5.18031  -22.86263 1.000 27.42530 ? 506 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? 0.59622   -26.88099 -37.31756 1.000 45.21292 ? 507 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? -10.64627 -14.01866 1.11989   1.000 32.64618 ? 508 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? 10.54531  -20.73076 -6.86822  1.000 40.74960 ? 509 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? 0.24832   -1.37568  -19.77535 1.000 38.83815 ? 510 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? -14.12267 -12.12931 -7.80726  1.000 26.88115 ? 511 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? -8.66161  -11.82950 -36.47725 1.000 30.85790 ? 512 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? 14.45876  0.29182   -13.19619 1.000 28.69270 ? 513 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 8.63449   -15.50407 -27.86060 1.000 18.18813 ? 514 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? -10.29293 -11.10522 -2.00463  1.000 24.51989 ? 515 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? -7.08977  1.09822   -19.32409 1.000 39.34424 ? 516 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? -15.95717 0.48954   -30.75644 1.000 37.29887 ? 517 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -4.65458  0.41453   -30.72843 1.000 35.11900 ? 518 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? 8.77747   -19.90817 -4.30719  1.000 27.51849 ? 519 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? -19.917   -19.190   -13.961   1.000 21.11419 ? 520 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? 15.41504  -20.04252 -18.70561 1.000 23.17090 ? 521 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -6.31013  -10.80542 -10.09480 1.000 25.48750 ? 522 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? 3.49052   1.91994   -9.78091  1.000 49.65046 ? 523 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? 19.38131  -0.22483  -9.86157  1.000 51.79208 ? 524 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? -1.78360  -25.22852 -4.50344  1.000 29.27053 ? 525 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? -16.36649 -3.01520  -21.28852 1.000 32.33162 ? 526 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? -6.63389  -5.10609  -39.09945 1.000 44.89871 ? 527 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? 3.42929   -6.52856  -18.03115 1.000 24.24438 ? 528 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? 0.19546   -11.59952 -22.13979 1.000 33.72974 ? 529 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? -1.29839  -29.51242 -16.83590 1.000 41.31237 ? 530 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? 19.70813  -16.72093 -27.48771 1.000 36.80420 ? 531 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -7.35219  -22.68080 -36.44347 1.000 48.72337 ? 532 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? 6.95222   -29.13034 -12.80541 1.000 59.31381 ? 533 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? 3.44877   -11.96808 -38.66234 1.000 26.58982 ? 534 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? -7.77815  -28.03779 -7.59829  1.000 31.90653 ? 535 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -4.30395  0.63341   -22.45207 1.000 42.50765 ? 536 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? 4.31938   -22.48988 -39.14571 1.000 58.83856 ? 537 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -5.93649  -13.54520 0.76668   1.000 32.61386 ? 538 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? 18.83910  -19.24399 -11.87668 1.000 49.07252 ? 539 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? 4.83842   -30.07603 -11.31820 1.000 35.70811 ? 540 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? -17.99604 -18.36262 -10.98947 1.000 35.73958 ? 541 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -19.40623 -10.53574 -32.93622 1.000 47.17375 ? 542 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? -10.32448 -15.02864 -28.23891 1.000 28.23432 ? 543 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? -1.52206  -26.21570 -32.07585 1.000 39.46285 ? 544 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -5.27895  -14.10016 -22.65096 1.000 20.14910 ? 545 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? 10.48103  -25.55854 -26.49020 1.000 30.76059 ? 546 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? -0.46036  -7.01148  -31.06835 1.000 34.95222 ? 547 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? 1.11900   -8.71835  -26.85631 1.000 33.03200 ? 548 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? 4.05985   -22.40791 -3.45601  1.000 34.25851 ? 549 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? -13.79335 -30.87429 -12.65029 1.000 53.07392 ? 550 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? -3.12853  -1.04138  -24.31731 1.000 32.70522 ? 551 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? -18.12804 -3.19322  -35.62300 1.000 44.07315 ? 552 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? 12.27348  -27.29161 -19.25873 1.000 41.61206 ? 553 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? 7.32950   -7.71439  -33.86178 1.000 41.96298 ? 554 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? 15.16638  -7.42540  -28.01771 1.000 35.77921 ? 555 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? 16.472    -25.063   -25.206   1.000 42.66161 ? 556 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? -3.66622  -12.98813 -20.64726 1.000 23.92174 ? 557 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? -2.08482  -30.37005 -19.42716 1.000 58.26444 ? 558 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? 0.46149   -5.40398  -21.99498 1.000 35.91639 ? 559 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? -15.44170 -12.14069 -11.91502 1.000 37.05019 ? 560 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? -17.94267 -14.84463 -13.06056 1.000 26.53156 ? 561 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? 1.26592   -3.91163  -16.87841 1.000 41.25960 ? 562 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? 13.53432  -20.27358 -20.68622 1.000 21.15179 ? 563 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? 3.95493   -9.03492  -20.53678 1.000 22.77288 ? 564 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? 13.70856  -11.60770 -30.01274 1.000 42.69856 ? 565 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? -3.37369  -20.58946 -0.27041  1.000 41.25264 ? 566 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? 0.60888   -22.28099 -1.81522  1.000 50.89400 ? 567 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? 13.51873  -3.99434  -25.82444 1.000 15.95251 ? 568 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? 6.10607   -4.84490  -23.04461 1.000 31.94560 ? 569 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? 19.85442  -4.67204  -14.91139 1.000 44.79275 ? 570 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? 2.84889   -3.74833  -9.14006  1.000 40.47881 ? 571 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? -12.13258 -7.82952  -38.35623 1.000 42.47614 ? 572 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? -12.31929 -26.72444 -20.16251 1.000 28.76762 ? 573 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 13.12443  -6.85404  -26.53168 1.000 23.40467 ? 574 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? -14.40075 -16.16360 -25.86763 1.000 26.63671 ? 575 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? 20.706    -13.976   -26.942   1.000 38.76374 ? 576 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? -5.55654  -11.06518 1.04028   1.000 44.72424 ? 577 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? -16.33869 -25.04005 -10.41552 1.000 39.50961 ? 578 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? 1.08159   -6.01323  -34.57337 1.000 50.84895 ? 579 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? -12.59924 -33.04707 -13.68640 1.000 56.87002 ? 580 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? -0.74100  -5.57909  -12.55667 1.000 45.13987 ? 581 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? 3.24778   -30.07784 -19.12080 1.000 46.05068 ? 582 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? -13.92521 -23.60168 -4.57418  1.000 34.67189 ? 583 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? -13.88966 -18.50498 -24.26606 1.000 25.43587 ? 584 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? -12.58586 -31.64191 -19.50576 1.000 58.21368 ? 585 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? -13.25961 -12.17391 -31.06191 1.000 30.90120 ? 586 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? 1.54644   -17.45368 -0.10556  1.000 44.68241 ? 587 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? 8.35954   -16.46988 -39.90742 1.000 37.63009 ? 588 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? -0.17791  -16.10517 -3.35671  1.000 28.46082 ? 589 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? -18.85766 -7.25935  -24.94549 1.000 47.33608 ? 590 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? -1.69436  -8.53162  -27.81705 1.000 29.15633 ? 591 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? -20.524   -12.898   -16.241   1.000 53.38036 ? 592 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? 14.23969  -14.97296 -1.96488  1.000 44.39260 ? 593 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? 15.79725  -17.38152 -3.66074  1.000 37.77437 ? 594 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? 1.83546   -25.79390 -29.15567 1.000 37.01190 ? 595 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? -14.73978 -11.78349 -39.94076 1.000 50.52211 ? 596 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? -18.11044 -5.37952  -25.37256 1.000 43.13819 ? 597 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? 17.06239  0.50792   -17.83933 1.000 37.05208 ? 598 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? -3.95269  -32.78400 -10.76257 1.000 45.88257 ? 599 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? 5.239     -3.151    -26.262   1.000 40.40902 ? 600 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? 14.32000  -22.05528 -17.12111 1.000 36.51889 ? 601 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? 2.54245   -5.73842  -20.72850 1.000 43.03138 ? 602 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? 8.22329   -25.82355 -25.53789 1.000 36.83112 ? 603 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? -2.30069  -0.95827  -31.66767 1.000 53.43657 ? 604 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? -2.36759  -26.86122 -24.83914 1.000 45.03928 ? 605 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 2.54666   -9.97920  -23.14879 1.000 30.99004 ? 606 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? -17.38589 -4.44081  -17.21462 1.000 41.23254 ? 607 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? 11.93004  -25.48626 -38.37609 1.000 38.31274 ? 608 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? 12.67120  -22.57053 -5.01356  1.000 57.50023 ? 609 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? -12.53300 -16.17660 -28.16544 1.000 32.49076 ? 610 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? 5.97690   -29.73111 -24.52125 1.000 43.96055 ? 611 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? 12.83803  -13.94289 -29.90256 1.000 27.05384 ? 612 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? 5.34994   -17.67640 -42.68168 1.000 62.14645 ? 613 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? -10.20540 -25.81163 -20.44502 1.000 31.22414 ? 614 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? 17.64089  -21.31137 -19.78142 1.000 33.45595 ? 615 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? 17.93226  -0.99681  -21.79065 1.000 45.69656 ? 616 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? -14.37810 -9.42037  -8.31976  1.000 31.89643 ? 617 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? -13.96668 -13.75123 -2.76151  1.000 36.78518 ? 618 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? 17.06817  -11.46025 -14.74190 1.000 48.06779 ? 619 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? 3.33423   -9.49465  -39.30930 1.000 40.49789 ? 620 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? -3.75315  -5.10792  -12.31355 1.000 40.80408 ? 621 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? -3.79671  -26.86071 -2.84822  1.000 49.93039 ? 622 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? 11.82804  -27.71562 -23.29149 1.000 47.54045 ? 623 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? 18.07675  -3.33305  -24.10513 1.000 45.17345 ? 624 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? 7.43461   -14.38279 -38.42523 1.000 35.83730 ? 625 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? -9.26456  -6.13482  -40.24774 1.000 46.61466 ? 626 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? -16.222   -1.696    -11.335   1.000 41.83725 ? 627 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? 5.87039   -7.06218  -36.25006 1.000 43.88922 ? 628 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? 1.20354   -8.23628  -40.61155 1.000 46.62883 ? 629 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? -18.79745 -11.47299 -21.09560 1.000 30.38964 ? 630 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? 19.03896  -8.08995  -17.83181 1.000 38.51085 ? 631 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? -10.57640 -8.29476  -1.46980  1.000 41.08701 ? 632 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? -1.04551  -26.24421 -29.82861 1.000 48.22049 ? 633 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? 5.53524   -13.29748 -40.07863 1.000 34.07561 ? 634 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? 16.45567  0.00000   0.00000   0.50  55.91002 ? 635 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? 6.61426   -21.15885 -2.84079  1.000 34.69210 ? 636 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? -1.93548  -12.13648 -22.20001 1.000 37.10361 ? 637 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? -12.064   -26.563   -27.362   1.000 38.64675 ? 638 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? -2.49146  -4.77721  -3.68932  1.000 52.97377 ? 639 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 16.11536  -3.36285  -26.58590 1.000 40.43011 ? 640 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? -10.378   -22.259   4.644     1.000 43.29313 ? 641 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 20.01727  -5.54589  -21.34559 1.000 43.14790 ? 642 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? -7.10481  -30.43928 -8.71854  1.000 35.10889 ? 643 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? 10.75620  -27.98139 -27.63322 1.000 37.61682 ? 644 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? -12.49942 -12.49598 -1.11632  1.000 37.46238 ? 645 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? -23.149   -31.569   -12.559   1.000 42.10618 ? 646 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.43799 0.50  46.17627 ? 647 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? 4.16669   -19.67949 -43.24841 1.000 66.46836 ? 648 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? 1.71718   -5.97083  -36.80984 1.000 42.91424 ? 649 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? 14.99530  -16.24052 -0.23873  1.000 50.22765 ? 650 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? 11.12105  -30.21401 -34.17708 1.000 42.17740 ? 651 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? 21.61660  -17.67379 -25.52193 1.000 48.06200 ? 652 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? -16.37357 -12.23378 -6.13186  1.000 41.71191 ? 653 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? -17.15625 -15.02509 -9.90904  1.000 40.03828 ? 654 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? 15.66081  -11.53433 -7.00592  1.000 54.24127 ? 655 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? -8.89139  -10.69039 -0.10050  1.000 42.92491 ? 656 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? -19.40732 -4.66685  -18.56485 1.000 51.92956 ? 657 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? -6.886    -22.462   -1.674    1.000 41.19738 ? 658 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? 4.009     -2.030    -28.245   1.000 40.55380 ? 659 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? 20.47846  -6.62205  -16.40437 1.000 47.23700 ? 660 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? 0.74958   -1.20701  -17.04276 1.000 48.52297 ? 661 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? -19.71885 -6.25363  -22.33646 1.000 50.39534 ? 662 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? 13.65581  0.00000   0.00000   0.50  63.05370 ? 663 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? 3.01740   -2.12201  -20.39018 1.000 43.04344 ? 664 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? -4.56028  -28.15755 -23.18627 1.000 43.16766 ? 665 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? 12.66655  -24.98189 -15.48213 1.000 47.18269 ? 666 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? 9.65194   -24.91150 -14.63666 1.000 40.96047 ? 667 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? 19.28314  -20.37614 -22.52322 1.000 41.45350 ? 668 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? -20.82628 -10.35321 -19.24331 1.000 45.53815 ? 669 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? -7.04125  -26.59065 -23.27765 1.000 44.45186 ? 670 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? -14.62801 -13.77589 -10.13988 1.000 32.57037 ? 671 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? 14.79305  -12.79923 -2.96818  1.000 53.38645 ? 672 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? -13.40491 -13.83399 -38.94854 1.000 51.47206 ? 673 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? -15.10799 -9.29066  -11.12052 1.000 37.95125 ? 674 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? -21.40991 -11.30142 -24.45672 1.000 47.89527 ? 675 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? 16.05737  -18.58642 -0.69073  1.000 52.20994 ? 676 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? 13.85198  -11.06909 -5.28551  1.000 58.89614 ? 677 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? -10.66708 -11.16229 2.16657   1.000 43.40608 ? 678 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? -9.20289  -32.15115 -7.97436  1.000 49.30649 ? 679 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? -11.69358 -32.95553 -9.50250  1.000 55.85825 ? 680 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? 23.18976  -6.93902  -16.39885 1.000 63.11480 ? 681 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 9   ? 0.51581 0.78057 0.42318 -0.11774 -0.00659 -0.26668 16  GLU A N   
2    C CA  . GLU A 9   ? 0.63269 0.84832 0.52029 -0.08337 -0.01529 -0.24144 16  GLU A CA  
3    C C   . GLU A 9   ? 0.57109 0.77382 0.47560 -0.06567 -0.02265 -0.22173 16  GLU A C   
4    O O   . GLU A 9   ? 0.52716 0.78802 0.45120 -0.04598 -0.03985 -0.21342 16  GLU A O   
5    C CB  . GLU A 9   ? 0.65723 0.91990 0.53165 -0.04852 -0.03531 -0.23266 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.91715 1.14106 0.77452 -0.00740 -0.04273 -0.20430 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.08330 1.36553 0.94103 0.03582  -0.06158 -0.18614 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.02199 1.37968 0.89631 0.03583  -0.06995 -0.19594 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.10477 1.35562 0.94554 0.07228  -0.06371 -0.16142 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.47161 0.59735 0.36834 -0.07040 -0.00698 -0.21330 17  VAL A N   
11   C CA  . VAL A 10  ? 0.42173 0.53038 0.33413 -0.05708 -0.01146 -0.19750 17  VAL A CA  
12   C C   . VAL A 10  ? 0.45909 0.51773 0.36631 -0.02217 -0.01272 -0.16163 17  VAL A C   
13   O O   . VAL A 10  ? 0.41857 0.41960 0.30903 -0.02327 0.00405  -0.15543 17  VAL A O   
14   C CB  . VAL A 10  ? 0.47047 0.52722 0.38895 -0.08531 0.01262  -0.20103 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.39276 0.43026 0.33020 -0.06684 0.00738  -0.17510 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.56107 0.66068 0.49451 -0.11614 0.01957  -0.22081 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.33155 0.41099 0.25228 0.00762  -0.02897 -0.13885 18  GLU A N   
18   C CA  . GLU A 11  ? 0.30562 0.34149 0.22572 0.03481  -0.02696 -0.10808 18  GLU A CA  
19   C C   . GLU A 11  ? 0.29488 0.30434 0.23653 0.03497  -0.02377 -0.09107 18  GLU A C   
20   O O   . GLU A 11  ? 0.26279 0.30073 0.22016 0.03166  -0.03180 -0.09334 18  GLU A O   
21   C CB  . GLU A 11  ? 0.31598 0.38167 0.22820 0.06758  -0.03963 -0.09502 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.36561 0.46422 0.25199 0.07549  -0.04454 -0.10853 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.49468 0.61627 0.36597 0.11562  -0.05231 -0.09084 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.48097 0.65596 0.35672 0.12938  -0.06384 -0.09188 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.58329 0.66772 0.43555 0.13521  -0.04370 -0.07533 18  GLU A OE2 
26   N N   . THR A 12  ? 0.29577 0.25675 0.23761 0.04037  -0.01211 -0.07437 19  THR A N   
27   C CA  . THR A 12  ? 0.26117 0.20451 0.22091 0.04260  -0.00944 -0.05874 19  THR A CA  
28   C C   . THR A 12  ? 0.27736 0.21634 0.24515 0.06305  -0.01267 -0.03910 19  THR A C   
29   O O   . THR A 12  ? 0.26770 0.18908 0.22620 0.07304  -0.00626 -0.03260 19  THR A O   
30   C CB  . THR A 12  ? 0.28288 0.18317 0.23564 0.03431  0.00946  -0.05590 19  THR A CB  
31   O OG1 . THR A 12  ? 0.33645 0.22912 0.27534 0.01025  0.02072  -0.07806 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.27372 0.16800 0.24239 0.04010  0.01029  -0.04019 19  THR A CG2 
33   N N   . PHE A 13  ? 0.26627 0.21914 0.24995 0.06634  -0.01937 -0.03194 20  PHE A N   
34   C CA  . PHE A 13  ? 0.24296 0.19211 0.23374 0.07836  -0.01814 -0.01898 20  PHE A CA  
35   C C   . PHE A 13  ? 0.28948 0.23843 0.29904 0.07282  -0.01684 -0.01191 20  PHE A C   
36   O O   . PHE A 13  ? 0.26560 0.22072 0.28124 0.06445  -0.02012 -0.01474 20  PHE A O   
37   C CB  . PHE A 13  ? 0.23262 0.19853 0.21861 0.08842  -0.02334 -0.01871 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.28763 0.26761 0.25239 0.10135  -0.02652 -0.02391 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.27362 0.28797 0.23573 0.09462  -0.03648 -0.03891 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.32986 0.29363 0.27597 0.12029  -0.01812 -0.01522 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.31193 0.35503 0.25452 0.10796  -0.04173 -0.04584 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.36507 0.34734 0.28703 0.13758  -0.02162 -0.01843 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.36680 0.39438 0.28765 0.13219  -0.03534 -0.03411 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.21488 0.16100 0.23285 0.07690  -0.01090 -0.00426 21  ALA A N   
45   C CA  . ALA A 14  ? 0.21204 0.17362 0.24835 0.07136  -0.01162 -0.00087 21  ALA A CA  
46   C C   . ALA A 14  ? 0.24751 0.21519 0.28685 0.06644  -0.01260 -0.00423 21  ALA A C   
47   O O   . ALA A 14  ? 0.26040 0.21425 0.28885 0.07140  -0.00502 -0.00440 21  ALA A O   
48   C CB  . ALA A 14  ? 0.25383 0.22238 0.30087 0.07431  -0.00344 0.00436  21  ALA A CB  
49   N N   . PHE A 15  ? 0.23105 0.21369 0.27990 0.05894  -0.01863 -0.00591 22  PHE A N   
50   C CA  . PHE A 15  ? 0.23512 0.22023 0.28609 0.05201  -0.01530 -0.00974 22  PHE A CA  
51   C C   . PHE A 15  ? 0.20511 0.19253 0.26332 0.04398  -0.00294 -0.01292 22  PHE A C   
52   O O   . PHE A 15  ? 0.23847 0.24721 0.31052 0.04171  -0.00348 -0.01235 22  PHE A O   
53   C CB  . PHE A 15  ? 0.23041 0.23356 0.29027 0.04416  -0.02325 -0.01161 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.21503 0.21568 0.26896 0.04663  -0.03064 -0.01215 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.26184 0.25742 0.30704 0.05096  -0.02976 -0.01434 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.21017 0.21444 0.26564 0.04571  -0.03492 -0.01053 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.20400 0.21016 0.24853 0.05130  -0.03652 -0.01768 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.23024 0.23343 0.28189 0.04232  -0.03769 -0.01503 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.17904 0.18932 0.22859 0.04346  -0.04026 -0.02002 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.25359 0.21956 0.30087 0.04014  0.01170  -0.01685 23  GLN A N   
61   C CA  . GLN A 16  ? 0.28185 0.25124 0.33705 0.02249  0.02816  -0.02645 23  GLN A CA  
62   C C   . GLN A 16  ? 0.25963 0.27357 0.33625 0.00652  0.01827  -0.03470 23  GLN A C   
63   O O   . GLN A 16  ? 0.22757 0.25177 0.30444 0.00817  0.00543  -0.03291 23  GLN A O   
64   C CB  . GLN A 16  ? 0.34811 0.27676 0.38142 0.01835  0.05186  -0.03069 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.41999 0.30591 0.42600 0.03921  0.06658  -0.02092 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.56939 0.40809 0.54531 0.04321  0.09400  -0.02054 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.57839 0.40997 0.53935 0.06038  0.08922  -0.01293 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.57783 0.38354 0.54355 0.02693  0.12641  -0.02953 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.22661 0.27260 0.32086 -0.00828 0.02500  -0.04457 24  ALA A N   
70   C CA  . ALA A 17  ? 0.26048 0.36572 0.37511 -0.01901 0.01353  -0.05253 24  ALA A CA  
71   C C   . ALA A 17  ? 0.27387 0.37873 0.38206 -0.03360 0.01329  -0.06227 24  ALA A C   
72   O O   . ALA A 17  ? 0.25117 0.38831 0.36443 -0.02915 -0.00322 -0.05965 24  ALA A O   
73   C CB  . ALA A 17  ? 0.27175 0.42186 0.40757 -0.03726 0.02427  -0.06752 24  ALA A CB  
74   N N   . GLU A 18  ? 0.24705 0.31036 0.33955 -0.04904 0.03503  -0.07247 25  GLU A N   
75   C CA  . GLU A 18  ? 0.24128 0.30014 0.32497 -0.06504 0.03971  -0.08358 25  GLU A CA  
76   C C   . GLU A 18  ? 0.23333 0.27507 0.30601 -0.04455 0.02369  -0.06838 25  GLU A C   
77   O O   . GLU A 18  ? 0.24179 0.30263 0.31512 -0.05169 0.01569  -0.07331 25  GLU A O   
78   C CB  . GLU A 18  ? 0.38908 0.39342 0.45099 -0.08336 0.07481  -0.09620 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.41323 0.43276 0.48577 -0.11356 0.09805  -0.11811 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.50531 0.50674 0.57924 -0.10074 0.10656  -0.10866 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.36178 0.34273 0.42820 -0.06822 0.09237  -0.08569 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.55248 0.56174 0.63456 -0.12613 0.12963  -0.12691 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.25986 0.27120 0.32274 -0.02076 0.01944  -0.05209 26  ILE A N   
84   C CA  . ILE A 19  ? 0.24095 0.24514 0.29736 -0.00472 0.00551  -0.04130 26  ILE A CA  
85   C C   . ILE A 19  ? 0.22803 0.26877 0.29879 0.00060  -0.01520 -0.03593 26  ILE A C   
86   O O   . ILE A 19  ? 0.24412 0.29128 0.31323 0.00216  -0.02368 -0.03393 26  ILE A O   
87   C CB  . ILE A 19  ? 0.27506 0.24911 0.31723 0.01667  0.00773  -0.03007 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.31948 0.25184 0.33726 0.02159  0.03104  -0.02997 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.30486 0.28964 0.34853 0.02897  -0.00925 -0.02313 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.45055 0.35574 0.45900 0.00859  0.05778  -0.03798 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.21759 0.27914 0.29927 0.00547  -0.01981 -0.03242 27  ALA A N   
92   C CA  . ALA A 20  ? 0.19929 0.28957 0.28737 0.01558  -0.03275 -0.02468 27  ALA A CA  
93   C C   . ALA A 20  ? 0.18706 0.31658 0.28030 0.00631  -0.03779 -0.03183 27  ALA A C   
94   O O   . ALA A 20  ? 0.20918 0.34651 0.29680 0.01590  -0.04580 -0.02457 27  ALA A O   
95   C CB  . ALA A 20  ? 0.21091 0.31654 0.30686 0.02623  -0.03252 -0.01827 27  ALA A CB  
96   N N   . GLN A 21  ? 0.19106 0.34500 0.29233 -0.01405 -0.03063 -0.04803 28  GLN A N   
97   C CA  . GLN A 21  ? 0.14063 0.34021 0.24540 -0.02667 -0.03569 -0.05973 28  GLN A CA  
98   C C   . GLN A 21  ? 0.25019 0.42037 0.33966 -0.03170 -0.03493 -0.06119 28  GLN A C   
99   O O   . GLN A 21  ? 0.23998 0.43708 0.32565 -0.02839 -0.04446 -0.06036 28  GLN A O   
100  C CB  . GLN A 21  ? 0.23650 0.46999 0.35293 -0.05580 -0.02398 -0.08377 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.41754 0.67232 0.55044 -0.05659 -0.01820 -0.08607 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.56191 0.84072 0.70528 -0.09321 0.00075  -0.11483 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.50667 0.77036 0.63657 -0.11706 0.01326  -0.13180 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.56242 0.86635 0.72221 -0.09584 0.00732  -0.11864 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.21318 0.32980 0.29136 -0.03627 -0.02220 -0.06205 29  LEU A N   
106  C CA  . LEU A 22  ? 0.22830 0.31761 0.29231 -0.03689 -0.01985 -0.06132 29  LEU A CA  
107  C C   . LEU A 22  ? 0.21751 0.30789 0.28034 -0.01766 -0.03423 -0.04618 29  LEU A C   
108  O O   . LEU A 22  ? 0.22797 0.32474 0.28435 -0.01873 -0.03811 -0.04652 29  LEU A O   
109  C CB  . LEU A 22  ? 0.27769 0.31395 0.32768 -0.03462 -0.00263 -0.05977 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.28240 0.29264 0.31858 -0.02800 0.00064  -0.05536 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.35801 0.36925 0.38460 -0.04847 0.01043  -0.06981 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.29822 0.26712 0.31970 -0.01285 0.01522  -0.04771 29  LEU A CD2 
113  N N   . MET A 23  ? 0.19723 0.27834 0.26372 -0.00205 -0.03896 -0.03446 30  MET A N   
114  C CA  . MET A 23  ? 0.19283 0.26566 0.25512 0.01095  -0.04519 -0.02373 30  MET A CA  
115  C C   . MET A 23  ? 0.21586 0.31646 0.27531 0.01881  -0.05122 -0.01796 30  MET A C   
116  O O   . MET A 23  ? 0.22225 0.31565 0.27194 0.02362  -0.05149 -0.01313 30  MET A O   
117  C CB  . MET A 23  ? 0.19539 0.25049 0.25901 0.02087  -0.04460 -0.01719 30  MET A CB  
118  C CG  . MET A 23  ? 0.20210 0.23595 0.26287 0.02091  -0.04089 -0.01997 30  MET A CG  
119  S SD  . MET A 23  ? 0.24447 0.26795 0.30491 0.02970  -0.04065 -0.01713 30  MET A SD  
120  C CE  . MET A 23  ? 0.31095 0.33084 0.36898 0.02884  -0.04205 -0.01781 30  MET A CE  
121  N N   . SER A 24  ? 0.19671 0.33245 0.26298 0.02263  -0.05443 -0.01784 31  SER A N   
122  C CA  . SER A 24  ? 0.20975 0.38333 0.27015 0.03777  -0.06000 -0.01015 31  SER A CA  
123  C C   . SER A 24  ? 0.27704 0.47561 0.33136 0.02777  -0.06409 -0.01940 31  SER A C   
124  O O   . SER A 24  ? 0.28385 0.49144 0.32309 0.04341  -0.06636 -0.00967 31  SER A O   
125  C CB  . SER A 24  ? 0.26126 0.48213 0.33396 0.04489  -0.06307 -0.01007 31  SER A CB  
126  O OG  . SER A 24  ? 0.56548 0.81842 0.62676 0.06879  -0.06522 0.00286  31  SER A OG  
127  N N   . LEU A 25  ? 0.20434 0.40868 0.26544 0.00212  -0.06136 -0.03829 32  LEU A N   
128  C CA  . LEU A 25  ? 0.23940 0.46205 0.29152 -0.01135 -0.06240 -0.05025 32  LEU A CA  
129  C C   . LEU A 25  ? 0.27287 0.45149 0.31014 -0.00557 -0.05932 -0.04171 32  LEU A C   
130  O O   . LEU A 25  ? 0.25400 0.44723 0.27782 -0.00087 -0.06267 -0.04019 32  LEU A O   
131  C CB  . LEU A 25  ? 0.29595 0.51903 0.35316 -0.04309 -0.05192 -0.07405 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.33708 0.56713 0.38135 -0.06431 -0.04695 -0.09159 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.38572 0.62853 0.43315 -0.09324 -0.03160 -0.11438 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.39068 0.55623 0.42046 -0.06505 -0.03581 -0.08693 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.22485 0.35535 0.26417 -0.00529 -0.05253 -0.03699 33  ILE A N   
136  C CA  . ILE A 26  ? 0.29255 0.39070 0.32270 -0.00183 -0.04854 -0.03155 33  ILE A CA  
137  C C   . ILE A 26  ? 0.30214 0.39755 0.32291 0.01641  -0.05014 -0.01702 33  ILE A C   
138  O O   . ILE A 26  ? 0.28352 0.36811 0.29191 0.01885  -0.04668 -0.01397 33  ILE A O   
139  C CB  . ILE A 26  ? 0.22597 0.29038 0.26242 -0.00296 -0.04205 -0.03116 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.26318 0.31527 0.29680 -0.01620 -0.03209 -0.04246 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.25098 0.29582 0.28441 0.00251  -0.03907 -0.02564 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.28719 0.31390 0.32300 -0.00922 -0.02490 -0.03926 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.25138 0.35054 0.27389 0.03029  -0.05109 -0.00736 34  ILE A N   
144  C CA  . ILE A 27  ? 0.31390 0.39499 0.31998 0.04914  -0.04391 0.00761  34  ILE A CA  
145  C C   . ILE A 27  ? 0.37471 0.48762 0.36278 0.06710  -0.04672 0.01617  34  ILE A C   
146  O O   . ILE A 27  ? 0.40444 0.49588 0.37016 0.08115  -0.03698 0.02734  34  ILE A O   
147  C CB  . ILE A 27  ? 0.30344 0.36832 0.31202 0.05885  -0.03864 0.01515  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.25039 0.28490 0.27011 0.04372  -0.03450 0.00680  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.37618 0.42007 0.35960 0.08285  -0.02487 0.03252  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.33247 0.35983 0.35862 0.04657  -0.03318 0.00786  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.27407 0.44197 0.26978 0.06702  -0.05831 0.00994  35  ASN A N   
152  C CA  . ASN A 28  ? 0.29740 0.51337 0.27641 0.09133  -0.06310 0.01948  35  ASN A CA  
153  C C   . ASN A 28  ? 0.42984 0.68735 0.40255 0.08025  -0.07183 0.00622  35  ASN A C   
154  O O   . ASN A 28  ? 0.40650 0.69392 0.36120 0.10019  -0.07131 0.01408  35  ASN A O   
155  C CB  . ASN A 28  ? 0.35044 0.60976 0.34237 0.09995  -0.06694 0.02029  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.47929 0.70077 0.46817 0.11890  -0.05683 0.03701  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.53502 0.70758 0.50090 0.13761  -0.04334 0.05360  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.46735 0.70277 0.47610 0.11130  -0.05856 0.03127  35  ASN A ND2 
159  N N   . THR A 29  ? 0.29663 0.54470 0.28149 0.04755  -0.07273 -0.01430 36  THR A N   
160  C CA  . THR A 29  ? 0.27197 0.55277 0.24691 0.03320  -0.07726 -0.02978 36  THR A CA  
161  C C   . THR A 29  ? 0.28891 0.53043 0.23952 0.04346  -0.07007 -0.01902 36  THR A C   
162  O O   . THR A 29  ? 0.33209 0.51353 0.28456 0.03911  -0.05955 -0.01366 36  THR A O   
163  C CB  . THR A 29  ? 0.31947 0.59138 0.30882 -0.00482 -0.07293 -0.05518 36  THR A CB  
164  O OG1 . THR A 29  ? 0.33113 0.62641 0.34139 -0.01582 -0.07243 -0.06443 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.37133 0.66862 0.34755 -0.02329 -0.07171 -0.07341 36  THR A CG2 
166  N N   . PHE A 30  ? 0.27629 0.55741 0.20395 0.05733  -0.07521 -0.01694 37  PHE A N   
167  C CA  . PHE A 30  ? 0.33618 0.57913 0.23826 0.06493  -0.06614 -0.00851 37  PHE A CA  
168  C C   . PHE A 30  ? 0.34281 0.55938 0.25092 0.03131  -0.06147 -0.02847 37  PHE A C   
169  O O   . PHE A 30  ? 0.32842 0.58249 0.23799 0.00862  -0.06683 -0.05066 37  PHE A O   
170  C CB  . PHE A 30  ? 0.32196 0.61318 0.19495 0.09050  -0.07109 -0.00087 37  PHE A CB  
171  C CG  . PHE A 30  ? 0.38034 0.63257 0.22102 0.10047  -0.06051 0.00854  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.48390 0.67258 0.30659 0.12381  -0.04178 0.03247  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.42149 0.69320 0.25007 0.08247  -0.06428 -0.00878 37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.43034 0.57793 0.22501 0.13034  -0.02719 0.04009  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.39228 0.62321 0.19239 0.09115  -0.05195 0.00018  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.43288 0.60265 0.21706 0.11551  -0.03351 0.02510  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.30922 0.46305 0.21894 0.02789  -0.04862 -0.02189 38  TYR A N   
178  C CA  . TYR A 31  ? 0.27097 0.39605 0.18634 0.00257  -0.04095 -0.03675 38  TYR A CA  
179  C C   . TYR A 31  ? 0.28269 0.35693 0.19361 0.00957  -0.02768 -0.02491 38  TYR A C   
180  O O   . TYR A 31  ? 0.31741 0.36607 0.24411 0.01317  -0.02270 -0.01735 38  TYR A O   
181  C CB  . TYR A 31  ? 0.33345 0.45038 0.27356 -0.01562 -0.03989 -0.04787 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.30288 0.38484 0.24217 -0.03424 -0.02677 -0.05934 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.42495 0.51588 0.34855 -0.05417 -0.02127 -0.07799 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.34725 0.39008 0.29854 -0.03047 -0.01770 -0.05213 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.48694 0.53685 0.40297 -0.06768 -0.00346 -0.08647 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.41679 0.42947 0.36302 -0.03962 -0.00294 -0.05898 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.39848 0.40879 0.32517 -0.05711 0.00591  -0.07475 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.55372 0.52520 0.46858 -0.06368 0.02626  -0.08019 38  TYR A OH  
189  N N   . SER A 32  ? 0.31847 0.38233 0.20829 0.00935  -0.02100 -0.02573 39  SER A N   
190  C CA  . SER A 32  ? 0.31216 0.33473 0.19568 0.01734  -0.00628 -0.01432 39  SER A CA  
191  C C   . SER A 32  ? 0.37852 0.37301 0.28348 0.00306  0.00324  -0.02048 39  SER A C   
192  O O   . SER A 32  ? 0.35721 0.32777 0.26883 0.00613  0.01479  -0.01404 39  SER A O   
193  C CB  . SER A 32  ? 0.34238 0.36358 0.19306 0.02490  -0.00078 -0.01160 39  SER A CB  
194  O OG  . SER A 32  ? 0.36419 0.41757 0.19084 0.04682  -0.00866 -0.00211 39  SER A OG  
195  N N   . ASN A 33  ? 0.31698 0.31537 0.23072 -0.01140 0.00176  -0.03320 40  ASN A N   
196  C CA  . ASN A 33  ? 0.31766 0.29329 0.24430 -0.01696 0.01321  -0.03629 40  ASN A CA  
197  C C   . ASN A 33  ? 0.30633 0.28405 0.26022 -0.01339 0.01056  -0.03303 40  ASN A C   
198  O O   . ASN A 33  ? 0.32696 0.30202 0.28968 -0.01557 0.01265  -0.03731 40  ASN A O   
199  C CB  . ASN A 33  ? 0.39867 0.36698 0.31261 -0.03009 0.01987  -0.04947 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.41174 0.35368 0.33112 -0.02796 0.03606  -0.04906 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.40612 0.34220 0.33335 -0.01911 0.04268  -0.04169 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.41416 0.34051 0.32656 -0.03508 0.04593  -0.05731 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.29830 0.28953 0.20300 0.01957  -0.06345 -0.00547 41  LYS A N   
204  C CA  . LYS A 34  ? 0.23759 0.27317 0.20029 0.01417  -0.04540 -0.00257 41  LYS A CA  
205  C C   . LYS A 34  ? 0.25048 0.27823 0.20932 0.02110  -0.02598 -0.01116 41  LYS A C   
206  O O   . LYS A 34  ? 0.21659 0.26542 0.20850 0.01490  -0.02030 -0.01188 41  LYS A O   
207  C CB  . LYS A 34  ? 0.23825 0.30276 0.23070 0.02215  -0.03077 0.00511  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.25502 0.34172 0.26639 0.01835  -0.04543 0.01809  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.27932 0.37935 0.30592 0.03195  -0.03148 0.02289  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.23965 0.36638 0.28674 0.03459  -0.04184 0.03884  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.19272 0.35899 0.27756 0.04022  -0.03733 0.05242  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.27572 0.27543 0.19319 0.03823  -0.01435 -0.01373 42  GLU A N   
213  C CA  . GLU A 35  ? 0.26836 0.27200 0.19292 0.04798  0.00709  -0.01282 42  GLU A CA  
214  C C   . GLU A 35  ? 0.35080 0.34483 0.27733 0.03765  -0.00151 -0.02333 42  GLU A C   
215  O O   . GLU A 35  ? 0.26164 0.26810 0.20928 0.04038  0.01310  -0.02167 42  GLU A O   
216  C CB  . GLU A 35  ? 0.29961 0.27900 0.17350 0.07791  0.02493  -0.00545 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.37103 0.28947 0.16744 0.09326  0.01189  -0.02002 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.59335 0.47488 0.31307 0.13801  0.03156  -0.01234 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.54810 0.45691 0.27739 0.15378  0.05346  0.00768  42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.80198 0.62400 0.44756 0.16162  0.02587  -0.02369 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.27406 0.24705 0.18408 0.02333  -0.02876 -0.02927 43  ILE A N   
222  C CA  . ILE A 36  ? 0.26819 0.22931 0.18017 0.01206  -0.03964 -0.03442 43  ILE A CA  
223  C C   . ILE A 36  ? 0.23188 0.23977 0.20251 0.00207  -0.02720 -0.02951 43  ILE A C   
224  O O   . ILE A 36  ? 0.24925 0.25310 0.22472 -0.00269 -0.02749 -0.03242 43  ILE A O   
225  C CB  . ILE A 36  ? 0.35503 0.28243 0.24527 -0.00737 -0.08118 -0.03236 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.39208 0.36582 0.33532 -0.02683 -0.09487 -0.01375 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.45950 0.31215 0.26284 0.00952  -0.10038 -0.04309 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.41851 0.44242 0.42462 -0.04337 -0.09422 0.00382  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.20414 0.24722 0.20882 0.00335  -0.01748 -0.02280 44  PHE A N   
230  C CA  . PHE A 37  ? 0.15621 0.22475 0.19242 0.00429  -0.00745 -0.02075 44  PHE A CA  
231  C C   . PHE A 37  ? 0.17933 0.23580 0.21299 0.00853  0.00267  -0.02793 44  PHE A C   
232  O O   . PHE A 37  ? 0.18180 0.24324 0.22522 0.00664  0.00382  -0.02933 44  PHE A O   
233  C CB  . PHE A 37  ? 0.16741 0.25145 0.21724 0.01459  -0.00113 -0.01639 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.17911 0.24822 0.22649 0.02049  0.00458  -0.01901 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.17664 0.24139 0.21650 0.02257  0.00659  -0.01354 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.18521 0.24360 0.23933 0.02289  0.00399  -0.02140 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.22948 0.29128 0.28191 0.02506  0.01102  -0.00357 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.20000 0.24760 0.26552 0.02087  0.00018  -0.01354 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.18158 0.23665 0.25283 0.02103  0.00510  -0.00129 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.18157 0.22702 0.20529 0.01641  0.01108  -0.02681 45  LEU A N   
241  C CA  . LEU A 38  ? 0.17625 0.22254 0.21346 0.01978  0.01949  -0.02347 45  LEU A CA  
242  C C   . LEU A 38  ? 0.23167 0.26239 0.24983 0.02161  0.02069  -0.02964 45  LEU A C   
243  O O   . LEU A 38  ? 0.21880 0.25292 0.25196 0.01897  0.02177  -0.02998 45  LEU A O   
244  C CB  . LEU A 38  ? 0.18157 0.23648 0.22943 0.02940  0.03087  -0.00629 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.19523 0.26397 0.27640 0.02998  0.03610  0.01081  45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.20641 0.26894 0.31082 0.01467  0.01593  0.00646  45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.20490 0.29743 0.31116 0.03956  0.04916  0.04234  45  LEU A CD2 
248  N N   . ARG A 39  ? 0.21492 0.21849 0.19240 0.02700  0.01543  -0.03503 46  ARG A N   
249  C CA  . ARG A 39  ? 0.25746 0.22902 0.20446 0.02868  0.00794  -0.04282 46  ARG A CA  
250  C C   . ARG A 39  ? 0.23548 0.21984 0.20971 0.00785  -0.00468 -0.04418 46  ARG A C   
251  O O   . ARG A 39  ? 0.25556 0.23300 0.23086 0.00742  -0.00332 -0.04631 46  ARG A O   
252  C CB  . ARG A 39  ? 0.31018 0.22960 0.19475 0.03564  -0.01028 -0.05003 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.44285 0.30876 0.28396 0.03467  -0.03090 -0.05915 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.48735 0.28124 0.25451 0.03868  -0.06385 -0.06723 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.48064 0.28797 0.27938 0.00451  -0.09651 -0.05899 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.59996 0.35475 0.35132 -0.00161 -0.13421 -0.06027 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.65929 0.34867 0.33515 0.02872  -0.13569 -0.06682 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.59887 0.38379 0.39981 -0.03511 -0.16275 -0.04287 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.20872 0.21629 0.20625 -0.00564 -0.01427 -0.03802 47  GLU A N   
260  C CA  . GLU A 40  ? 0.18290 0.21211 0.20782 -0.01901 -0.02130 -0.02864 47  GLU A CA  
261  C C   . GLU A 40  ? 0.17725 0.22557 0.22004 -0.01040 -0.00467 -0.03005 47  GLU A C   
262  O O   . GLU A 40  ? 0.21002 0.26132 0.25915 -0.01421 -0.00531 -0.02638 47  GLU A O   
263  C CB  . GLU A 40  ? 0.17859 0.23957 0.22968 -0.02754 -0.03000 -0.01147 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.22805 0.26622 0.26600 -0.04409 -0.06040 -0.00415 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.38882 0.37526 0.39524 -0.05685 -0.08702 -0.00820 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.30382 0.30115 0.33175 -0.06625 -0.08868 0.00117  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.46701 0.39418 0.41919 -0.05506 -0.10944 -0.01964 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.15122 0.20494 0.19792 0.00053  0.00487  -0.03384 48  LEU A N   
269  C CA  . LEU A 41  ? 0.18040 0.23298 0.23067 0.00845  0.00862  -0.03629 48  LEU A CA  
270  C C   . LEU A 41  ? 0.19914 0.23763 0.24985 0.00652  0.00870  -0.03982 48  LEU A C   
271  O O   . LEU A 41  ? 0.21163 0.24510 0.26114 0.00825  0.00656  -0.04112 48  LEU A O   
272  C CB  . LEU A 41  ? 0.19195 0.23785 0.24058 0.01726  0.00617  -0.03738 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.16263 0.22204 0.20669 0.02781  0.00905  -0.03235 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.20064 0.23881 0.23442 0.03695  0.00171  -0.03536 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.21827 0.29117 0.25448 0.04320  0.01688  -0.02452 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.17922 0.21224 0.22871 0.00799  0.01312  -0.03799 49  ILE A N   
277  C CA  . ILE A 42  ? 0.18807 0.21573 0.24144 0.01240  0.01779  -0.03438 49  ILE A CA  
278  C C   . ILE A 42  ? 0.24488 0.25721 0.28012 0.00954  0.01475  -0.04105 49  ILE A C   
279  O O   . ILE A 42  ? 0.20862 0.21862 0.25014 0.01012  0.01467  -0.04006 49  ILE A O   
280  C CB  . ILE A 42  ? 0.21696 0.24736 0.26765 0.02647  0.03099  -0.02320 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.18848 0.24123 0.27510 0.02422  0.03062  -0.00584 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.19673 0.22243 0.24258 0.04086  0.04163  -0.01585 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.20204 0.27108 0.29326 0.04169  0.04923  0.01583  49  ILE A CD1 
284  N N   . SER A 43  ? 0.21533 0.21398 0.22993 0.00361  0.00656  -0.04471 50  SER A N   
285  C CA  . SER A 43  ? 0.22515 0.20341 0.22629 -0.00482 -0.00517 -0.04562 50  SER A CA  
286  C C   . SER A 43  ? 0.22038 0.22433 0.24768 -0.01319 -0.00482 -0.03836 50  SER A C   
287  O O   . SER A 43  ? 0.21838 0.21373 0.24422 -0.01489 -0.00653 -0.03732 50  SER A O   
288  C CB  . SER A 43  ? 0.32690 0.27955 0.30534 -0.01587 -0.02657 -0.04442 50  SER A CB  
289  O OG  . SER A 43  ? 0.36116 0.28615 0.32910 -0.02960 -0.04775 -0.04022 50  SER A OG  
290  N N   . ASN A 44  ? 0.20750 0.24014 0.25165 -0.01219 -0.00038 -0.03188 51  ASN A N   
291  C CA  . ASN A 44  ? 0.18938 0.24172 0.24219 -0.00634 0.00582  -0.02289 51  ASN A CA  
292  C C   . ASN A 44  ? 0.18248 0.21815 0.22461 0.00312  0.00790  -0.03266 51  ASN A C   
293  O O   . ASN A 44  ? 0.18179 0.21746 0.21922 0.00658  0.00925  -0.02793 51  ASN A O   
294  C CB  . ASN A 44  ? 0.18409 0.25988 0.24042 0.00666  0.01376  -0.01513 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.33368 0.44165 0.41466 -0.00282 0.01105  0.00706  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.25148 0.35645 0.34522 -0.02410 -0.00438 0.01659  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.28655 0.42066 0.37307 0.01331  0.02133  0.01834  51  ASN A ND2 
298  N N   . SER A 45  ? 0.17568 0.19922 0.21793 0.00631  0.00529  -0.04080 52  SER A N   
299  C CA  . SER A 45  ? 0.19132 0.19975 0.23399 0.00930  -0.00228 -0.04280 52  SER A CA  
300  C C   . SER A 45  ? 0.20829 0.21327 0.25634 0.00555  -0.00028 -0.04091 52  SER A C   
301  O O   . SER A 45  ? 0.19536 0.19158 0.23940 0.00728  -0.00613 -0.04030 52  SER A O   
302  C CB  . SER A 45  ? 0.16534 0.17080 0.22455 0.00751  -0.01015 -0.03911 52  SER A CB  
303  O OG  . SER A 45  ? 0.22299 0.21526 0.26825 0.01265  -0.01991 -0.04243 52  SER A OG  
304  N N   . SER A 46  ? 0.22185 0.22479 0.26872 0.00488  0.00622  -0.04057 53  SER A N   
305  C CA  . SER A 46  ? 0.21663 0.20460 0.25519 0.00819  0.00763  -0.03990 53  SER A CA  
306  C C   . SER A 46  ? 0.24950 0.23086 0.27981 -0.00056 0.00107  -0.03962 53  SER A C   
307  O O   . SER A 46  ? 0.24048 0.21398 0.27014 0.00133  -0.00057 -0.03782 53  SER A O   
308  C CB  . SER A 46  ? 0.21885 0.18558 0.23226 0.01832  0.01262  -0.04219 53  SER A CB  
309  O OG  . SER A 46  ? 0.25770 0.19462 0.24685 0.02790  0.01173  -0.04357 53  SER A OG  
310  N N   . ASP A 47  ? 0.19322 0.18443 0.22412 -0.00993 -0.00243 -0.03481 54  ASP A N   
311  C CA  . ASP A 47  ? 0.21171 0.21026 0.24778 -0.01835 -0.00658 -0.02168 54  ASP A CA  
312  C C   . ASP A 47  ? 0.24335 0.25286 0.27734 -0.00647 0.00107  -0.01900 54  ASP A C   
313  O O   . ASP A 47  ? 0.22583 0.23156 0.25766 -0.00765 -0.00021 -0.01140 54  ASP A O   
314  C CB  . ASP A 47  ? 0.18029 0.20428 0.23351 -0.02899 -0.01022 -0.00401 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.33711 0.33393 0.38383 -0.04633 -0.03180 -0.00311 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.30451 0.32141 0.37050 -0.05830 -0.04109 0.01310  54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.33500 0.28476 0.35101 -0.04428 -0.04160 -0.01743 54  ASP A OD2 
318  N N   . ALA A 48  ? 0.17951 0.19292 0.20539 0.00672  0.00496  -0.02507 55  ALA A N   
319  C CA  . ALA A 48  ? 0.17829 0.18094 0.18011 0.02369  0.00446  -0.02569 55  ALA A CA  
320  C C   . ALA A 48  ? 0.20284 0.18196 0.20311 0.02072  -0.00798 -0.03306 55  ALA A C   
321  O O   . ALA A 48  ? 0.21829 0.18441 0.19859 0.02927  -0.01176 -0.03069 55  ALA A O   
322  C CB  . ALA A 48  ? 0.21053 0.20134 0.18936 0.04015  0.00180  -0.03276 55  ALA A CB  
323  N N   . LEU A 49  ? 0.19809 0.17546 0.22045 0.01195  -0.01304 -0.03697 56  LEU A N   
324  C CA  . LEU A 49  ? 0.18568 0.15453 0.22107 0.01035  -0.02233 -0.03382 56  LEU A CA  
325  C C   . LEU A 49  ? 0.23906 0.20514 0.27178 0.00913  -0.01605 -0.03077 56  LEU A C   
326  O O   . LEU A 49  ? 0.23155 0.18828 0.26205 0.01147  -0.02385 -0.02736 56  LEU A O   
327  C CB  . LEU A 49  ? 0.17778 0.15974 0.24469 0.00821  -0.02125 -0.02685 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.20217 0.18094 0.27937 0.00431  -0.03814 -0.02344 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.21301 0.21628 0.32304 0.00325  -0.02874 -0.01102 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.21870 0.17964 0.30470 -0.00077 -0.06748 -0.01423 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.22187 0.18801 0.25093 0.00423  -0.00813 -0.03093 57  ASP A N   
332  C CA  . ASP A 50  ? 0.22591 0.17580 0.24634 0.00075  -0.01038 -0.02692 57  ASP A CA  
333  C C   . ASP A 50  ? 0.26641 0.22254 0.28175 -0.00078 -0.01180 -0.01759 57  ASP A C   
334  O O   . ASP A 50  ? 0.25731 0.20076 0.26835 -0.00049 -0.01563 -0.01324 57  ASP A O   
335  C CB  . ASP A 50  ? 0.25908 0.19238 0.26883 -0.00903 -0.01560 -0.02616 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.35223 0.26044 0.34343 0.00255  -0.01392 -0.03581 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.36815 0.28000 0.36340 0.02022  -0.00332 -0.03605 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.38100 0.26343 0.35103 -0.00378 -0.02501 -0.03844 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.22591 0.20167 0.23758 0.00286  -0.00591 -0.01129 58  LYS A N   
340  C CA  . LYS A 51  ? 0.23261 0.21922 0.23251 0.01145  0.00025  0.00479  58  LYS A CA  
341  C C   . LYS A 51  ? 0.24630 0.20989 0.21932 0.02622  -0.00661 -0.00306 58  LYS A C   
342  O O   . LYS A 51  ? 0.28370 0.24317 0.24676 0.02994  -0.00602 0.00738  58  LYS A O   
343  C CB  . LYS A 51  ? 0.24521 0.25952 0.24020 0.02463  0.01400  0.01733  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.25524 0.30326 0.28635 0.00754  0.01734  0.04070  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.24117 0.32385 0.27326 0.02579  0.03390  0.05546  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.30409 0.41753 0.38073 0.00238  0.02787  0.07582  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.38214 0.54066 0.46851 0.02332  0.04735  0.09909  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.28107 0.22589 0.24200 0.03293  -0.01846 -0.01802 59  ILE A N   
349  C CA  . ILE A 52  ? 0.27079 0.18395 0.20505 0.04242  -0.03731 -0.02258 59  ILE A CA  
350  C C   . ILE A 52  ? 0.30643 0.21963 0.27135 0.02948  -0.04567 -0.01979 59  ILE A C   
351  O O   . ILE A 52  ? 0.30109 0.19698 0.25066 0.03429  -0.05687 -0.01634 59  ILE A O   
352  C CB  . ILE A 52  ? 0.29694 0.17909 0.20923 0.04878  -0.06032 -0.03370 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.41063 0.24351 0.28026 0.05888  -0.09132 -0.03677 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.28034 0.17820 0.24391 0.02925  -0.06830 -0.03368 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.47132 0.28204 0.27374 0.08895  -0.08094 -0.03462 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.24511 0.17486 0.24656 0.01880  -0.03879 -0.01939 60  ARG A N   
357  C CA  . ARG A 53  ? 0.24635 0.17504 0.26764 0.01768  -0.04041 -0.01307 60  ARG A CA  
358  C C   . ARG A 53  ? 0.29852 0.21714 0.30327 0.01749  -0.03552 -0.00851 60  ARG A C   
359  O O   . ARG A 53  ? 0.28910 0.19775 0.29240 0.02107  -0.04351 -0.00309 60  ARG A O   
360  C CB  . ARG A 53  ? 0.24902 0.18860 0.29323 0.01948  -0.02868 -0.01170 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.36977 0.30486 0.42404 0.03008  -0.02559 -0.00227 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.60530 0.54472 0.66590 0.04653  -0.00931 0.00242  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.63381 0.61003 0.73829 0.05251  -0.00656 0.02108  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.60616 0.59682 0.71696 0.06334  0.00889  0.02611  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.51718 0.48126 0.58622 0.06715  0.01781  0.00785  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.29639 0.32985 0.45915 0.06990  0.01275  0.05522  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.30603 0.22904 0.30338 0.01107  -0.02613 -0.00528 61  TYR A N   
368  C CA  . TYR A 54  ? 0.31561 0.23062 0.30731 0.00535  -0.02646 0.00755  61  TYR A CA  
369  C C   . TYR A 54  ? 0.34748 0.26482 0.32018 0.01554  -0.02629 0.01721  61  TYR A C   
370  O O   . TYR A 54  ? 0.34774 0.25241 0.31617 0.01560  -0.03104 0.02491  61  TYR A O   
371  C CB  . TYR A 54  ? 0.32349 0.24858 0.32413 -0.00939 -0.02443 0.02025  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.37640 0.29135 0.38098 -0.02190 -0.03268 0.04144  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.33769 0.20840 0.33252 -0.02861 -0.04869 0.03614  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.35157 0.29796 0.36527 -0.02238 -0.02428 0.07060  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.38222 0.23375 0.37899 -0.04298 -0.06337 0.05690  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.35039 0.29236 0.37694 -0.03708 -0.03388 0.09796  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.38994 0.28120 0.40942 -0.05112 -0.05708 0.08988  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.44062 0.31826 0.47149 -0.06880 -0.07347 0.11861  61  TYR A OH  
379  N N   . GLU A 55  ? 0.30533 0.23108 0.25607 0.02936  -0.02130 0.01684  62  GLU A N   
380  C CA  . GLU A 55  ? 0.35598 0.27016 0.26665 0.04957  -0.02136 0.02457  62  GLU A CA  
381  C C   . GLU A 55  ? 0.38335 0.26586 0.28247 0.05166  -0.04424 0.01360  62  GLU A C   
382  O O   . GLU A 55  ? 0.42388 0.29248 0.29982 0.06044  -0.04828 0.02209  62  GLU A O   
383  C CB  . GLU A 55  ? 0.38212 0.29322 0.25054 0.07495  -0.01390 0.02276  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.43028 0.38551 0.31386 0.07980  0.01301  0.04690  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.74948 0.70075 0.57657 0.12066  0.02836  0.05256  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.55693 0.55559 0.39880 0.13312  0.05574  0.08386  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.64537 0.54283 0.41120 0.14247  0.01039  0.02960  62  GLU A OE2 
388  N N   . SER A 56  ? 0.33738 0.21348 0.25915 0.04295  -0.06025 0.00098  63  SER A N   
389  C CA  . SER A 56  ? 0.36594 0.22242 0.29356 0.04143  -0.08674 0.00100  63  SER A CA  
390  C C   . SER A 56  ? 0.39175 0.25717 0.34843 0.03595  -0.08252 0.01077  63  SER A C   
391  O O   . SER A 56  ? 0.40900 0.26368 0.37238 0.03690  -0.10279 0.01723  63  SER A O   
392  C CB  . SER A 56  ? 0.38022 0.24115 0.34119 0.03181  -0.10451 -0.00152 63  SER A CB  
393  O OG  . SER A 56  ? 0.39233 0.28600 0.40473 0.02441  -0.08743 0.00461  63  SER A OG  
394  N N   . LEU A 57  ? 0.35945 0.23683 0.32960 0.03085  -0.06207 0.01349  64  LEU A N   
395  C CA  . LEU A 57  ? 0.45470 0.32416 0.43722 0.03112  -0.06125 0.02081  64  LEU A CA  
396  C C   . LEU A 57  ? 0.53977 0.39487 0.49844 0.03477  -0.06716 0.03070  64  LEU A C   
397  O O   . LEU A 57  ? 0.49007 0.33478 0.45668 0.03811  -0.07330 0.03712  64  LEU A O   
398  C CB  . LEU A 57  ? 0.38189 0.24406 0.36658 0.02509  -0.04934 0.01963  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.35762 0.22527 0.35516 0.02767  -0.04197 0.01027  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.43075 0.26787 0.40992 0.02362  -0.04124 0.00743  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.44766 0.32661 0.46962 0.04327  -0.04084 0.01522  64  LEU A CD2 
402  N N   . THR A 58  ? 0.58776 0.27328 0.36877 0.02216  -0.08900 0.13194  65  THR A N   
403  C CA  . THR A 58  ? 0.63539 0.32068 0.40319 0.02090  -0.09039 0.15480  65  THR A CA  
404  C C   . THR A 58  ? 0.61826 0.36787 0.40123 0.03011  -0.08376 0.15500  65  THR A C   
405  O O   . THR A 58  ? 0.64352 0.39242 0.40843 0.03773  -0.08550 0.17158  65  THR A O   
406  C CB  . THR A 58  ? 0.83833 0.50677 0.60345 -0.01366 -0.09305 0.17635  65  THR A CB  
407  O OG1 . THR A 58  ? 0.80811 0.52629 0.60440 -0.03404 -0.08628 0.17590  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.79194 0.39982 0.54199 -0.02456 -0.10196 0.16892  65  THR A CG2 
409  N N   . ASP A 59  ? 0.58783 0.38412 0.39534 0.03000  -0.07834 0.13699  66  ASP A N   
410  C CA  . ASP A 59  ? 0.57156 0.41273 0.37973 0.03855  -0.07655 0.13337  66  ASP A CA  
411  C C   . ASP A 59  ? 0.47604 0.34351 0.30761 0.04848  -0.08087 0.11073  66  ASP A C   
412  O O   . ASP A 59  ? 0.43767 0.32473 0.28642 0.03908  -0.07485 0.09683  66  ASP A O   
413  C CB  . ASP A 59  ? 0.55590 0.42315 0.36239 0.02417  -0.06323 0.14104  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.68269 0.57614 0.46753 0.03735  -0.06159 0.13632  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.69139 0.58548 0.46743 0.05104  -0.07670 0.12704  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.75727 0.66899 0.53133 0.03488  -0.04597 0.14377  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.60490 0.47651 0.44193 0.06737  -0.09158 0.11069  67  PRO A N   
418  C CA  . PRO A 60  ? 0.55621 0.45949 0.42442 0.07398  -0.09645 0.09634  67  PRO A CA  
419  C C   . PRO A 60  ? 0.51784 0.45166 0.38741 0.06359  -0.10173 0.08421  67  PRO A C   
420  O O   . PRO A 60  ? 0.46075 0.41461 0.35580 0.05984  -0.10251 0.07095  67  PRO A O   
421  C CB  . PRO A 60  ? 0.53032 0.44252 0.40777 0.09590  -0.10847 0.10960  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.65903 0.52766 0.50837 0.10520  -0.10519 0.12553  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.58169 0.42584 0.40340 0.08386  -0.09770 0.12776  67  PRO A CD  
424  N N   . SER A 61  ? 0.52087 0.45213 0.35654 0.06094  -0.10491 0.08900  68  SER A N   
425  C CA  . SER A 61  ? 0.51527 0.45814 0.33390 0.05594  -0.11048 0.07582  68  SER A CA  
426  C C   . SER A 61  ? 0.53322 0.48102 0.36207 0.04658  -0.09338 0.06251  68  SER A C   
427  O O   . SER A 61  ? 0.49079 0.44240 0.30822 0.04475  -0.09772 0.04849  68  SER A O   
428  C CB  . SER A 61  ? 0.57139 0.49945 0.33627 0.06127  -0.11227 0.08463  68  SER A CB  
429  O OG  . SER A 61  ? 0.61558 0.53609 0.36679 0.05914  -0.08785 0.09600  68  SER A OG  
430  N N   . LYS A 62  ? 0.43843 0.38175 0.28579 0.03995  -0.07741 0.06741  69  LYS A N   
431  C CA  . LYS A 62  ? 0.38121 0.33458 0.24423 0.03080  -0.06429 0.05802  69  LYS A CA  
432  C C   . LYS A 62  ? 0.40965 0.37447 0.29804 0.02965  -0.07144 0.03984  69  LYS A C   
433  O O   . LYS A 62  ? 0.38195 0.35501 0.27727 0.02476  -0.06374 0.02985  69  LYS A O   
434  C CB  . LYS A 62  ? 0.40960 0.35277 0.28835 0.01908  -0.05470 0.06936  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.53075 0.46587 0.39184 0.01454  -0.04781 0.09339  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.51279 0.46779 0.38862 0.00125  -0.03260 0.10632  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.55684 0.52251 0.41545 0.00225  -0.01942 0.13388  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.66916 0.66866 0.55427 -0.00887 -0.00243 0.15386  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.36155 0.33066 0.26704 0.03537  -0.08459 0.03938  70  LEU A N   
440  C CA  . LEU A 63  ? 0.32100 0.30794 0.25598 0.03369  -0.09091 0.02899  70  LEU A CA  
441  C C   . LEU A 63  ? 0.35160 0.34978 0.28062 0.03119  -0.11254 0.02595  70  LEU A C   
442  O O   . LEU A 63  ? 0.38865 0.40615 0.34813 0.02661  -0.12273 0.02388  70  LEU A O   
443  C CB  . LEU A 63  ? 0.36633 0.35699 0.32940 0.04388  -0.08854 0.03608  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.38263 0.34548 0.34028 0.04518  -0.07328 0.03579  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.40425 0.35960 0.37306 0.06494  -0.06926 0.04274  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.35345 0.31705 0.31758 0.03243  -0.06482 0.02321  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.39559 0.37874 0.28239 0.03269  -0.12146 0.02740  71  ASP A N   
448  C CA  . ASP A 64  ? 0.43147 0.40911 0.29645 0.02670  -0.14784 0.02135  71  ASP A CA  
449  C C   . ASP A 64  ? 0.42788 0.39666 0.28893 0.01778  -0.14774 0.00410  71  ASP A C   
450  O O   . ASP A 64  ? 0.48770 0.45175 0.34609 0.00653  -0.17416 -0.00043 71  ASP A O   
451  C CB  . ASP A 64  ? 0.46526 0.41447 0.26651 0.03351  -0.15471 0.02320  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.66361 0.61851 0.46426 0.04122  -0.16238 0.04206  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.66521 0.64569 0.51457 0.04298  -0.16657 0.05360  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.67210 0.60404 0.41954 0.04883  -0.16302 0.04688  71  ASP A OD2 
455  N N   . SER A 65  ? 0.39587 0.36083 0.25661 0.02104  -0.12131 -0.00302 72  SER A N   
456  C CA  . SER A 65  ? 0.39292 0.34868 0.25090 0.01641  -0.11760 -0.01764 72  SER A CA  
457  C C   . SER A 65  ? 0.48866 0.46898 0.40223 0.00657  -0.11823 -0.01817 72  SER A C   
458  O O   . SER A 65  ? 0.47090 0.44493 0.38727 0.00218  -0.11406 -0.02836 72  SER A O   
459  C CB  . SER A 65  ? 0.45594 0.40617 0.29624 0.02652  -0.08848 -0.01906 72  SER A CB  
460  O OG  . SER A 65  ? 0.36610 0.33707 0.23819 0.02568  -0.07215 -0.00620 72  SER A OG  
461  N N   . GLY A 66  ? 0.38058 0.38665 0.33441 0.00688  -0.12067 -0.00573 73  GLY A N   
462  C CA  . GLY A 66  ? 0.35843 0.38865 0.35997 0.00327  -0.11683 -0.00252 73  GLY A CA  
463  C C   . GLY A 66  ? 0.36123 0.40351 0.38598 0.01592  -0.10161 0.00869  73  GLY A C   
464  O O   . GLY A 66  ? 0.35302 0.37721 0.36144 0.02071  -0.08560 0.00610  73  GLY A O   
465  N N   . LYS A 67  ? 0.28765 0.35803 0.34846 0.02220  -0.10733 0.02385  74  LYS A N   
466  C CA  . LYS A 67  ? 0.27818 0.34946 0.34922 0.04215  -0.09111 0.03476  74  LYS A CA  
467  C C   . LYS A 67  ? 0.33492 0.40270 0.41698 0.04909  -0.07056 0.03092  74  LYS A C   
468  O O   . LYS A 67  ? 0.36508 0.40768 0.43022 0.06528  -0.05562 0.03223  74  LYS A O   
469  C CB  . LYS A 67  ? 0.26519 0.37198 0.36979 0.05441  -0.10149 0.05798  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.46924 0.56657 0.55148 0.05857  -0.11565 0.06536  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.51786 0.66036 0.64049 0.06548  -0.13400 0.09131  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.83783 0.96746 0.93715 0.07832  -0.14208 0.10207  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.74521 0.84348 0.79443 0.06103  -0.15874 0.08810  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.22178 0.30594 0.32387 0.03756  -0.07112 0.02635  75  GLU A N   
475  C CA  . GLU A 68  ? 0.22038 0.30311 0.33085 0.04597  -0.05188 0.02543  75  GLU A CA  
476  C C   . GLU A 68  ? 0.29753 0.34011 0.37177 0.04025  -0.04311 0.00765  75  GLU A C   
477  O O   . GLU A 68  ? 0.34832 0.38272 0.40979 0.02453  -0.05018 -0.00322 75  GLU A O   
478  C CB  . GLU A 68  ? 0.25936 0.37516 0.40644 0.03391  -0.05648 0.03109  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.31350 0.48058 0.51120 0.03881  -0.06316 0.05817  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.65089 0.83140 0.85634 0.02264  -0.09393 0.06404  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.73693 0.88889 0.91149 0.00306  -0.11074 0.04584  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.69455 0.90823 0.92847 0.03162  -0.09970 0.08618  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.22126 0.23763 0.27676 0.05457  -0.02836 0.00704  76  LEU A N   
484  C CA  . LEU A 69  ? 0.22436 0.20009 0.24550 0.04652  -0.02584 -0.00527 76  LEU A CA  
485  C C   . LEU A 69  ? 0.25067 0.22172 0.27012 0.05143  -0.01483 -0.00860 76  LEU A C   
486  O O   . LEU A 69  ? 0.25759 0.21094 0.26106 0.07362  -0.00173 -0.00356 76  LEU A O   
487  C CB  . LEU A 69  ? 0.28088 0.21069 0.26467 0.05625  -0.02541 -0.00327 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.34760 0.27909 0.32944 0.05239  -0.03502 0.00306  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.46245 0.33813 0.40301 0.05850  -0.03637 0.00607  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.33075 0.27937 0.31950 0.02985  -0.04313 -0.00123 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.23531 0.21900 0.26606 0.03499  -0.01809 -0.01571 77  HIS A N   
492  C CA  . HIS A 70  ? 0.22215 0.20706 0.25473 0.03981  -0.00787 -0.01592 77  HIS A CA  
493  C C   . HIS A 70  ? 0.20450 0.18425 0.23302 0.02176  -0.01397 -0.02548 77  HIS A C   
494  O O   . HIS A 70  ? 0.18146 0.16560 0.21293 0.00814  -0.02327 -0.02960 77  HIS A O   
495  C CB  . HIS A 70  ? 0.20791 0.23773 0.28272 0.04519  -0.00238 -0.00252 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.20647 0.26337 0.30981 0.02461  -0.01832 -0.00346 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.26005 0.34564 0.39080 0.02160  -0.02971 0.00753  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.21597 0.26794 0.31707 0.00797  -0.02643 -0.01367 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.25777 0.34608 0.39378 0.00215  -0.04646 0.00163  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.25025 0.31725 0.36745 -0.00376 -0.04236 -0.01152 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.19613 0.16774 0.21637 0.02562  -0.00634 -0.02612 78  ILE A N   
502  C CA  . ILE A 71  ? 0.19602 0.16522 0.21448 0.01224  -0.01124 -0.03179 78  ILE A CA  
503  C C   . ILE A 71  ? 0.21742 0.20823 0.25735 0.01478  -0.00274 -0.02638 78  ILE A C   
504  O O   . ILE A 71  ? 0.22008 0.21062 0.25558 0.03013  0.01106  -0.01824 78  ILE A O   
505  C CB  . ILE A 71  ? 0.25391 0.18107 0.23076 0.01111  -0.01567 -0.03598 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.25689 0.15773 0.21285 0.00334  -0.02796 -0.03689 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.22321 0.15615 0.20475 -0.00130 -0.02180 -0.03739 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.31251 0.15607 0.21645 0.00027  -0.03890 -0.03971 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.19561 0.20148 0.25481 0.00199  -0.00935 -0.02864 79  ASN A N   
510  C CA  . ASN A 72  ? 0.16654 0.18613 0.24438 -0.00051 -0.00502 -0.02200 79  ASN A CA  
511  C C   . ASN A 72  ? 0.17362 0.17888 0.23793 -0.00544 -0.00706 -0.02690 79  ASN A C   
512  O O   . ASN A 72  ? 0.20270 0.20248 0.26088 -0.01084 -0.01503 -0.03352 79  ASN A O   
513  C CB  . ASN A 72  ? 0.17746 0.21556 0.28317 -0.01187 -0.01549 -0.01892 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.18760 0.24886 0.31539 -0.00887 -0.01692 -0.00803 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.18872 0.26092 0.32092 0.00611  -0.00311 0.00282  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.23176 0.29773 0.36892 -0.02040 -0.03398 -0.00960 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.18985 0.19264 0.25063 -0.00132 0.00166  -0.01999 80  LEU A N   
518  C CA  . LEU A 73  ? 0.16286 0.15430 0.21332 -0.00523 -0.00119 -0.02131 80  LEU A CA  
519  C C   . LEU A 73  ? 0.19101 0.19331 0.26524 -0.01173 -0.00003 -0.01319 80  LEU A C   
520  O O   . LEU A 73  ? 0.16343 0.17980 0.25258 -0.00971 0.00977  0.00038  80  LEU A O   
521  C CB  . LEU A 73  ? 0.19251 0.16172 0.20798 0.00425  0.00523  -0.01912 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.23130 0.17401 0.21209 0.00887  0.00028  -0.02612 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.26295 0.16748 0.19245 0.01913  0.00319  -0.02564 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.25324 0.19737 0.23987 -0.00556 -0.01760 -0.03164 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.17030 0.16482 0.24732 -0.01835 -0.00943 -0.01839 81  ILE A N   
526  C CA  . ILE A 74  ? 0.15299 0.14268 0.24406 -0.02755 -0.01435 -0.01265 81  ILE A CA  
527  C C   . ILE A 74  ? 0.22935 0.20076 0.30727 -0.02475 -0.01457 -0.01199 81  ILE A C   
528  O O   . ILE A 74  ? 0.23021 0.18872 0.29709 -0.01956 -0.01968 -0.01987 81  ILE A O   
529  C CB  . ILE A 74  ? 0.20205 0.18272 0.29513 -0.03477 -0.02797 -0.02067 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.22135 0.22230 0.32575 -0.03538 -0.02907 -0.02057 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.17463 0.13965 0.27658 -0.04981 -0.03950 -0.01288 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.25505 0.24373 0.35191 -0.04138 -0.04462 -0.02906 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.22715 0.19850 0.30572 -0.02506 -0.00718 0.00032  82  PRO A N   
534  C CA  . PRO A 75  ? 0.24289 0.19508 0.30971 -0.02266 -0.00896 0.00363  82  PRO A CA  
535  C C   . PRO A 75  ? 0.25875 0.18940 0.33278 -0.03349 -0.01765 0.00777  82  PRO A C   
536  O O   . PRO A 75  ? 0.29581 0.23258 0.38971 -0.04818 -0.02188 0.01640  82  PRO A O   
537  C CB  . PRO A 75  ? 0.24537 0.20252 0.30307 -0.01820 0.00296  0.01668  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.23955 0.21905 0.31539 -0.02039 0.01363  0.02667  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.22350 0.21338 0.31207 -0.02371 0.00604  0.01503  82  PRO A CD  
540  N N   . ASN A 76  ? 0.28631 0.18904 0.34291 -0.02623 -0.02246 0.00386  83  ASN A N   
541  C CA  . ASN A 76  ? 0.29368 0.15601 0.34148 -0.03440 -0.03336 0.00609  83  ASN A CA  
542  C C   . ASN A 76  ? 0.35285 0.19305 0.38476 -0.02314 -0.03025 0.01300  83  ASN A C   
543  O O   . ASN A 76  ? 0.35687 0.18786 0.37276 -0.00326 -0.02852 0.00627  83  ASN A O   
544  C CB  . ASN A 76  ? 0.36795 0.20045 0.39482 -0.02996 -0.04404 -0.01045 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.43934 0.21352 0.44416 -0.04228 -0.06157 -0.01025 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.45871 0.19926 0.44881 -0.03944 -0.06286 -0.00352 83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.55783 0.31953 0.55610 -0.05630 -0.07643 -0.01647 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.36685 0.20216 0.40594 -0.03445 -0.02856 0.03042  84  LYS A N   
549  C CA  . LYS A 77  ? 0.40477 0.22038 0.42805 -0.02372 -0.02557 0.03986  84  LYS A CA  
550  C C   . LYS A 77  ? 0.44561 0.20361 0.44307 -0.01717 -0.03618 0.03526  84  LYS A C   
551  O O   . LYS A 77  ? 0.50543 0.24774 0.48634 0.00241  -0.03310 0.03863  84  LYS A O   
552  C CB  . LYS A 77  ? 0.46238 0.28811 0.49717 -0.03654 -0.01822 0.06276  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.44376 0.31258 0.48330 -0.03030 -0.00304 0.06730  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.56376 0.43619 0.59880 -0.03135 0.00949  0.09136  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.40440 0.30736 0.43127 -0.02141 0.02662  0.09522  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.58327 0.51526 0.63699 -0.02743 0.03158  0.09267  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.49441 0.21490 0.48277 -0.03191 -0.05049 0.02871  85  GLN A N   
558  C CA  . GLN A 78  ? 0.63141 0.28375 0.57883 -0.02199 -0.06041 0.02116  85  GLN A CA  
559  C C   . GLN A 78  ? 0.57439 0.21727 0.49570 0.01324  -0.05238 0.00497  85  GLN A C   
560  O O   . GLN A 78  ? 0.61125 0.22751 0.50794 0.03802  -0.04638 0.00574  85  GLN A O   
561  C CB  . GLN A 78  ? 0.61127 0.24368 0.55102 -0.04578 -0.07623 0.01619  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.91855 0.52838 0.86049 -0.06803 -0.08604 0.03301  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.25338 0.87371 1.21250 -0.10019 -0.10442 0.03884  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.28389 0.94679 1.26926 -0.10896 -0.10527 0.03759  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 1.02713 0.60925 0.97222 -0.11745 -0.12116 0.04740  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.53349 0.21263 0.46628 0.01681  -0.04820 -0.00641 86  ASP A N   
567  C CA  . ASP A 79  ? 0.61245 0.29977 0.53009 0.04905  -0.03663 -0.01620 86  ASP A CA  
568  C C   . ASP A 79  ? 0.50565 0.25594 0.45485 0.06444  -0.02264 -0.00451 86  ASP A C   
569  O O   . ASP A 79  ? 0.45818 0.22478 0.40491 0.09259  -0.01183 -0.00317 86  ASP A O   
570  C CB  . ASP A 79  ? 0.55848 0.25994 0.47609 0.04218  -0.03946 -0.02997 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.72652 0.37960 0.60980 0.02903  -0.05405 -0.04010 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.79166 0.45316 0.66942 0.02379  -0.05832 -0.04970 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.71532 0.32752 0.57739 0.02344  -0.06205 -0.03658 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.40601 0.19009 0.38202 0.04682  -0.02364 0.00657  87  ARG A N   
575  C CA  . ARG A 80  ? 0.32039 0.15771 0.31969 0.05273  -0.01874 0.01669  87  ARG A CA  
576  C C   . ARG A 80  ? 0.29870 0.17752 0.31419 0.05563  -0.01572 0.01060  87  ARG A C   
577  O O   . ARG A 80  ? 0.31524 0.22568 0.34379 0.07192  -0.01235 0.01958  87  ARG A O   
578  C CB  . ARG A 80  ? 0.34460 0.17907 0.33959 0.07676  -0.01614 0.03072  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.38205 0.25786 0.39474 0.07135  -0.02061 0.04490  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.48969 0.39056 0.51438 0.09554  -0.02088 0.06193  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.56850 0.43125 0.57508 0.11362  -0.01866 0.07165  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.65529 0.52570 0.66691 0.14529  -0.01361 0.08668  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.49536 0.41896 0.53657 0.16167  -0.00926 0.09743  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.61703 0.44333 0.60606 0.16194  -0.01210 0.09511  87  ARG A NH2 
585  N N   . THR A 81  ? 0.28089 0.16270 0.29941 0.03883  -0.01775 -0.00069 88  THR A N   
586  C CA  . THR A 81  ? 0.24932 0.16435 0.28027 0.03851  -0.01573 -0.00604 88  THR A CA  
587  C C   . THR A 81  ? 0.25479 0.18848 0.29659 0.01789  -0.01881 -0.00861 88  THR A C   
588  O O   . THR A 81  ? 0.27661 0.19707 0.31769 0.00487  -0.01985 -0.00924 88  THR A O   
589  C CB  . THR A 81  ? 0.32455 0.21796 0.33843 0.04645  -0.01361 -0.01847 88  THR A CB  
590  O OG1 . THR A 81  ? 0.32963 0.18858 0.33122 0.02872  -0.02285 -0.02700 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.35350 0.22258 0.34494 0.07657  -0.00529 -0.01635 88  THR A CG2 
592  N N   . LEU A 82  ? 0.20047 0.16445 0.25236 0.01603  -0.02006 -0.00712 89  LEU A N   
593  C CA  . LEU A 82  ? 0.18800 0.16080 0.24071 0.00292  -0.02150 -0.01184 89  LEU A CA  
594  C C   . LEU A 82  ? 0.21307 0.19920 0.27220 0.00364  -0.02116 -0.01797 89  LEU A C   
595  O O   . LEU A 82  ? 0.19658 0.20222 0.26433 0.00988  -0.02174 -0.01163 89  LEU A O   
596  C CB  . LEU A 82  ? 0.24602 0.22528 0.29021 -0.00194 -0.02769 -0.00515 89  LEU A CB  
597  C CG  . LEU A 82  ? 0.20776 0.18274 0.23892 -0.00930 -0.02816 -0.01071 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.24049 0.20651 0.26896 -0.00873 -0.01649 -0.01205 89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.23790 0.20133 0.24357 -0.01337 -0.03959 -0.00585 89  LEU A CD2 
600  N N   . THR A 83  ? 0.18914 0.16926 0.24737 -0.00248 -0.02021 -0.02613 90  THR A N   
601  C CA  . THR A 83  ? 0.18084 0.16912 0.24008 -0.00103 -0.02014 -0.03159 90  THR A CA  
602  C C   . THR A 83  ? 0.19099 0.18816 0.25225 -0.00947 -0.02171 -0.03254 90  THR A C   
603  O O   . THR A 83  ? 0.21942 0.21182 0.28048 -0.01345 -0.01987 -0.03233 90  THR A O   
604  C CB  . THR A 83  ? 0.20450 0.17131 0.25348 0.00002  -0.02235 -0.03992 90  THR A CB  
605  O OG1 . THR A 83  ? 0.24436 0.18689 0.27781 0.01166  -0.02110 -0.04066 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.28688 0.25949 0.32918 0.00423  -0.02181 -0.04466 90  THR A CG2 
607  N N   . ILE A 84  ? 0.18215 0.19164 0.24483 -0.01039 -0.02384 -0.03022 91  ILE A N   
608  C CA  . ILE A 84  ? 0.17768 0.18470 0.23431 -0.01645 -0.02666 -0.03163 91  ILE A CA  
609  C C   . ILE A 84  ? 0.23066 0.24418 0.29032 -0.01448 -0.02518 -0.03476 91  ILE A C   
610  O O   . ILE A 84  ? 0.19622 0.22232 0.25985 -0.01112 -0.02354 -0.02992 91  ILE A O   
611  C CB  . ILE A 84  ? 0.20819 0.21428 0.25827 -0.02454 -0.03624 -0.02411 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.31571 0.30920 0.35315 -0.02640 -0.04150 -0.02112 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.23647 0.22518 0.26981 -0.02916 -0.04033 -0.02689 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.36919 0.38269 0.42399 -0.02529 -0.04508 -0.01060 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.17424 0.18269 0.23282 -0.01470 -0.02486 -0.03935 92  VAL A N   
616  C CA  . VAL A 85  ? 0.15496 0.16624 0.21206 -0.01329 -0.02680 -0.04201 92  VAL A CA  
617  C C   . VAL A 85  ? 0.22148 0.23122 0.27481 -0.01415 -0.02767 -0.03949 92  VAL A C   
618  O O   . VAL A 85  ? 0.23210 0.23511 0.28331 -0.01169 -0.02513 -0.03816 92  VAL A O   
619  C CB  . VAL A 85  ? 0.20511 0.21193 0.26584 -0.01511 -0.03202 -0.04558 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.23222 0.23572 0.28167 -0.01393 -0.03870 -0.04874 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.27668 0.27015 0.33282 -0.01502 -0.03334 -0.04837 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.19867 0.21121 0.24676 -0.01442 -0.02923 -0.03711 93  ASP A N   
623  C CA  . ASP A 86  ? 0.18136 0.18566 0.22196 -0.01410 -0.03136 -0.03433 93  ASP A CA  
624  C C   . ASP A 86  ? 0.23540 0.24610 0.27296 -0.01125 -0.03331 -0.03352 93  ASP A C   
625  O O   . ASP A 86  ? 0.22339 0.23999 0.25624 -0.00899 -0.03176 -0.03452 93  ASP A O   
626  C CB  . ASP A 86  ? 0.19105 0.18142 0.22069 -0.02199 -0.03565 -0.02806 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.27295 0.28100 0.31132 -0.02910 -0.03664 -0.01742 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.26186 0.27699 0.29855 -0.02629 -0.03401 -0.01315 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.21712 0.23502 0.26524 -0.03673 -0.03972 -0.00963 93  ASP A OD2 
630  N N   . THR A 87  ? 0.19506 0.24500 0.23786 0.02106  -0.01112 0.01568  94  THR A N   
631  C CA  . THR A 87  ? 0.16495 0.19977 0.20504 0.01932  -0.01730 0.01325  94  THR A CA  
632  C C   . THR A 87  ? 0.22848 0.25059 0.25642 0.02257  -0.01434 0.00547  94  THR A C   
633  O O   . THR A 87  ? 0.21673 0.23397 0.24549 0.02540  -0.01602 0.00643  94  THR A O   
634  C CB  . THR A 87  ? 0.18392 0.22896 0.23879 0.02074  -0.02088 0.02052  94  THR A CB  
635  O OG1 . THR A 87  ? 0.19142 0.25147 0.25092 0.02805  -0.01367 0.02189  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.18335 0.23774 0.25714 0.01497  -0.02623 0.02971  94  THR A CG2 
637  N N   . GLY A 88  ? 0.19692 0.21407 0.21689 0.02194  -0.01047 -0.00075 95  GLY A N   
638  C CA  . GLY A 88  ? 0.23928 0.24438 0.25483 0.02349  -0.00804 -0.00662 95  GLY A CA  
639  C C   . GLY A 88  ? 0.21833 0.21069 0.22639 0.02062  -0.01024 -0.00379 95  GLY A C   
640  O O   . GLY A 88  ? 0.25357 0.24587 0.25788 0.01944  -0.01523 -0.00004 95  GLY A O   
641  N N   . ILE A 89  ? 0.20352 0.18704 0.21097 0.02027  -0.00681 -0.00589 96  ILE A N   
642  C CA  . ILE A 89  ? 0.21669 0.19283 0.21793 0.01977  -0.00649 0.00015  96  ILE A CA  
643  C C   . ILE A 89  ? 0.24920 0.22676 0.23892 0.01750  -0.00766 -0.00085 96  ILE A C   
644  O O   . ILE A 89  ? 0.25892 0.23588 0.23904 0.01962  -0.00850 0.00331  96  ILE A O   
645  C CB  . ILE A 89  ? 0.23549 0.20357 0.24654 0.01935  -0.00184 0.00138  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.26536 0.23055 0.27326 0.02101  0.00011  0.01390  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.24220 0.21068 0.25560 0.01533  0.00051  -0.00591 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.37143 0.32844 0.39812 0.02076  0.00404  0.02049  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.26028 0.24153 0.25073 0.01481  -0.00783 -0.00612 97  GLY A N   
650  C CA  . GLY A 90  ? 0.24821 0.22930 0.23140 0.01366  -0.00933 -0.00801 97  GLY A CA  
651  C C   . GLY A 90  ? 0.26449 0.24323 0.24401 0.01351  -0.00386 -0.00764 97  GLY A C   
652  O O   . GLY A 90  ? 0.26094 0.23759 0.24727 0.01263  0.00054  -0.00540 97  GLY A O   
653  N N   . MET A 91  ? 0.23393 0.21347 0.20612 0.01462  -0.00452 -0.01000 98  MET A N   
654  C CA  . MET A 91  ? 0.27665 0.25789 0.24685 0.01524  0.00152  -0.00868 98  MET A CA  
655  C C   . MET A 91  ? 0.29341 0.27757 0.24939 0.02149  0.00114  -0.00918 98  MET A C   
656  O O   . MET A 91  ? 0.24057 0.22335 0.19098 0.02406  -0.00593 -0.01622 98  MET A O   
657  C CB  . MET A 91  ? 0.26466 0.24839 0.24169 0.01228  0.00230  -0.01306 98  MET A CB  
658  C CG  . MET A 91  ? 0.25297 0.23879 0.24126 0.00845  0.00340  -0.01434 98  MET A CG  
659  S SD  . MET A 91  ? 0.28151 0.27564 0.27529 0.00684  0.00287  -0.01829 98  MET A SD  
660  C CE  . MET A 91  ? 0.29682 0.29315 0.28968 0.00795  -0.00237 -0.01679 98  MET A CE  
661  N N   . THR A 92  ? 0.25773 0.24764 0.20983 0.02471  0.00838  -0.00183 99  THR A N   
662  C CA  . THR A 92  ? 0.27766 0.27603 0.21368 0.03343  0.00976  -0.00315 99  THR A CA  
663  C C   . THR A 92  ? 0.29919 0.29929 0.23667 0.03455  0.01136  -0.01061 99  THR A C   
664  O O   . THR A 92  ? 0.29070 0.28764 0.24203 0.02813  0.01277  -0.01112 99  THR A O   
665  C CB  . THR A 92  ? 0.32011 0.32951 0.25289 0.03787  0.01900  0.01152  99  THR A CB  
666  O OG1 . THR A 92  ? 0.35070 0.36138 0.30141 0.03211  0.02712  0.01895  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.31337 0.32076 0.24794 0.03747  0.01744  0.02125  99  THR A CG2 
668  N N   . LYS A 93  ? 0.30283 0.30967 0.22562 0.04432  0.01049  -0.01740 100 LYS A N   
669  C CA  . LYS A 93  ? 0.29600 0.30556 0.22132 0.04760  0.01298  -0.02402 100 LYS A CA  
670  C C   . LYS A 93  ? 0.26960 0.28752 0.20673 0.04399  0.02421  -0.01246 100 LYS A C   
671  O O   . LYS A 93  ? 0.31485 0.33092 0.26512 0.03966  0.02481  -0.01465 100 LYS A O   
672  C CB  . LYS A 93  ? 0.33780 0.35658 0.24425 0.06173  0.01162  -0.03410 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.35701 0.37842 0.26749 0.06729  0.01406  -0.04248 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.31875 0.35215 0.20888 0.08430  0.01334  -0.05492 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.39757 0.42896 0.29514 0.09065  0.01269  -0.06735 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.43220 0.48027 0.30931 0.10995  0.01497  -0.07963 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.29546 0.32353 0.23158 0.04526  0.03243  0.00152  101 ALA A N   
678  C CA  . ALA A 94  ? 0.33943 0.37566 0.29390 0.04041  0.04218  0.01437  101 ALA A CA  
679  C C   . ALA A 94  ? 0.35898 0.38346 0.33478 0.02784  0.03815  0.01294  101 ALA A C   
680  O O   . ALA A 94  ? 0.32960 0.35849 0.32167 0.02351  0.04099  0.01407  101 ALA A O   
681  C CB  . ALA A 94  ? 0.31968 0.36807 0.27477 0.04337  0.05092  0.03310  101 ALA A CB  
682  N N   . ASP A 95  ? 0.25359 0.26584 0.22973 0.02306  0.03128  0.00983  102 ASP A N   
683  C CA  . ASP A 95  ? 0.28649 0.29099 0.27873 0.01422  0.02675  0.00500  102 ASP A CA  
684  C C   . ASP A 95  ? 0.27998 0.28458 0.27199 0.01357  0.02230  -0.00492 102 ASP A C   
685  O O   . ASP A 95  ? 0.28497 0.29229 0.29058 0.00865  0.02127  -0.00715 102 ASP A O   
686  C CB  . ASP A 95  ? 0.29357 0.28818 0.28504 0.01178  0.02105  0.00288  102 ASP A CB  
687  C CG  . ASP A 95  ? 0.44188 0.43496 0.43812 0.01223  0.02447  0.01407  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.37821 0.37456 0.39161 0.00939  0.03016  0.02345  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.39446 0.38293 0.38223 0.01463  0.02068  0.01433  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.24290 0.24508 0.22201 0.01877  0.01845  -0.01093 103 LEU A N   
691  C CA  . LEU A 96  ? 0.27343 0.27497 0.25683 0.01837  0.01404  -0.01701 103 LEU A CA  
692  C C   . LEU A 96  ? 0.29751 0.30835 0.28935 0.01952  0.01885  -0.01581 103 LEU A C   
693  O O   . LEU A 96  ? 0.29552 0.31067 0.29857 0.01559  0.01711  -0.01617 103 LEU A O   
694  C CB  . LEU A 96  ? 0.30894 0.30417 0.28361 0.02378  0.00815  -0.02352 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.30142 0.28891 0.27616 0.02101  0.00049  -0.02508 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.27113 0.25213 0.24368 0.02618  -0.00696 -0.03319 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.23532 0.22503 0.22206 0.01526  -0.00140 -0.02173 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.29824 0.31542 0.28433 0.02632  0.02479  -0.01435 104 ILE A N   
699  C CA  . ILE A 97  ? 0.27279 0.30278 0.27058 0.02659  0.03205  -0.00895 104 ILE A CA  
700  C C   . ILE A 97  ? 0.24665 0.27890 0.25906 0.01797  0.03449  -0.00101 104 ILE A C   
701  O O   . ILE A 97  ? 0.65854 0.68295 0.66784 0.01502  0.03255  0.00064  104 ILE A O   
702  C CB  . ILE A 97  ? 0.29421 0.33448 0.28103 0.03750  0.03971  -0.00705 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.27485 0.30772 0.24578 0.04681  0.03363  -0.01984 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.29234 0.34912 0.29341 0.03978  0.04782  -0.00139 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.32168 0.36506 0.27349 0.06029  0.03863  -0.02226 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.55934 0.60133 0.59114 0.01372  0.03714  0.00279  105 ASN A N   
707  C CA  . ASN A 98  ? 0.33615 0.37647 0.38735 0.00453  0.03541  0.00598  105 ASN A CA  
708  C C   . ASN A 98  ? 0.27514 0.30687 0.32478 0.00032  0.02549  -0.00489 105 ASN A C   
709  O O   . ASN A 98  ? 0.23817 0.26209 0.29259 -0.00366 0.02237  -0.00657 105 ASN A O   
710  C CB  . ASN A 98  ? 0.37458 0.41152 0.42743 0.00400  0.04064  0.01683  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.56345 0.60463 0.64786 -0.00384 0.04300  0.02598  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.53878 0.58782 0.64375 -0.00859 0.04103  0.02362  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.54069 0.57673 0.63294 -0.00550 0.04608  0.03689  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.21659 0.25139 0.25970 0.00277  0.02111  -0.01113 106 ASN A N   
715  C CA  . ASN A 99  ? 0.23562 0.27233 0.28062 0.00020  0.01302  -0.01887 106 ASN A CA  
716  C C   . ASN A 99  ? 0.25022 0.27721 0.28545 -0.00023 0.00966  -0.02229 106 ASN A C   
717  O O   . ASN A 99  ? 0.21404 0.24251 0.25527 -0.00270 0.00493  -0.02889 106 ASN A O   
718  C CB  . ASN A 99  ? 0.19570 0.24222 0.26171 -0.00511 0.00943  -0.02284 106 ASN A CB  
719  C CG  . ASN A 99  ? 0.19581 0.25485 0.27480 -0.00475 0.01276  -0.01807 106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.21601 0.28127 0.28847 0.00014  0.01277  -0.01718 106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.19589 0.25939 0.29700 -0.00974 0.01560  -0.01363 106 ASN A ND2 
722  N N   . LEU A 100 ? 0.24353 0.26192 0.26454 0.00323  0.01134  -0.01923 107 LEU A N   
723  C CA  . LEU A 100 ? 0.29563 0.30710 0.30840 0.00355  0.00805  -0.02100 107 LEU A CA  
724  C C   . LEU A 100 ? 0.30394 0.31073 0.32404 0.00057  0.00786  -0.02278 107 LEU A C   
725  O O   . LEU A 100 ? 0.26310 0.27064 0.28369 0.00069  0.00397  -0.02840 107 LEU A O   
726  C CB  . LEU A 100 ? 0.21053 0.22954 0.22143 0.00479  0.00333  -0.02325 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.29982 0.32059 0.30935 0.00771  0.00288  -0.01930 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.28016 0.31402 0.29758 0.00821  0.00214  -0.01912 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.35742 0.37704 0.36502 0.00914  -0.00054 -0.01549 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.25109 0.25443 0.27905 -0.00111 0.01246  -0.01699 108 GLY A N   
731  C CA  . GLY A 101 ? 0.29030 0.28663 0.33102 -0.00391 0.01232  -0.01593 108 GLY A CA  
732  C C   . GLY A 101 ? 0.30160 0.29968 0.36264 -0.00808 0.00719  -0.02540 108 GLY A C   
733  O O   . GLY A 101 ? 0.30678 0.29676 0.37959 -0.00919 0.00451  -0.02895 108 GLY A O   
734  N N   . THR A 102 ? 0.25970 0.26850 0.32691 -0.00967 0.00457  -0.03084 109 THR A N   
735  C CA  . THR A 102 ? 0.26893 0.28237 0.35472 -0.01263 -0.00307 -0.04356 109 THR A CA  
736  C C   . THR A 102 ? 0.24435 0.26062 0.35763 -0.01897 -0.00212 -0.03893 109 THR A C   
737  O O   . THR A 102 ? 0.23330 0.25315 0.34710 -0.01952 0.00581  -0.02532 109 THR A O   
738  C CB  . THR A 102 ? 0.24502 0.27386 0.31927 -0.00893 -0.00872 -0.05330 109 THR A CB  
739  O OG1 . THR A 102 ? 0.27997 0.31837 0.35427 -0.00950 -0.00585 -0.04630 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.27467 0.30478 0.32528 -0.00285 -0.00795 -0.05258 109 THR A CG2 
741  N N   . ILE A 103 ? 0.19837 0.21501 0.33640 -0.02300 -0.01084 -0.05131 110 ILE A N   
742  C CA  . ILE A 103 ? 0.19329 0.21582 0.36408 -0.03017 -0.01283 -0.04900 110 ILE A CA  
743  C C   . ILE A 103 ? 0.24674 0.28788 0.41455 -0.02898 -0.01974 -0.05960 110 ILE A C   
744  O O   . ILE A 103 ? 0.20737 0.25511 0.39839 -0.03248 -0.03082 -0.07375 110 ILE A O   
745  C CB  . ILE A 103 ? 0.31624 0.32668 0.52392 -0.03619 -0.02027 -0.05626 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.32335 0.32784 0.52379 -0.03114 -0.03108 -0.07945 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.31048 0.30742 0.53040 -0.03870 -0.01037 -0.03537 110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.37206 0.39317 0.56574 -0.02714 -0.04347 -0.10287 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.32192 0.27553 0.32263 0.05360  0.08245  0.04943  111 ALA A N   
750  C CA  . ALA A 104 ? 0.26402 0.22315 0.27684 0.05332  0.06997  0.03774  111 ALA A CA  
751  C C   . ALA A 104 ? 0.23975 0.21820 0.28552 0.04393  0.06735  0.03387  111 ALA A C   
752  O O   . ALA A 104 ? 0.27448 0.25473 0.32818 0.04287  0.05317  0.02608  111 ALA A O   
753  C CB  . ALA A 104 ? 0.29209 0.26020 0.29255 0.05898  0.06737  0.03158  111 ALA A CB  
754  N N   . LYS A 105 ? 0.25177 0.25324 0.31618 0.03542  0.08060  0.03668  112 LYS A N   
755  C CA  . LYS A 105 ? 0.28474 0.32145 0.38490 0.02346  0.07912  0.02644  112 LYS A CA  
756  C C   . LYS A 105 ? 0.31505 0.33449 0.41761 0.00293  0.07590  0.02351  112 LYS A C   
757  O O   . LYS A 105 ? 0.24323 0.28389 0.36420 0.00051  0.06188  0.01076  112 LYS A O   
758  C CB  . LYS A 105 ? 0.22964 0.30158 0.34767 0.01164  0.09806  0.02610  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.28735 0.41495 0.44779 -0.00250 0.09816  0.00869  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.27391 0.45248 0.45585 -0.01227 0.11744  0.00170  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.38626 0.61846 0.60332 -0.04316 0.12553  -0.01575 112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.40967 0.70228 0.64903 -0.03790 0.12737  -0.02891 112 LYS A NZ  
763  N N   . SER A 106 ? 0.30092 0.27853 0.38094 -0.01051 0.08822  0.03462  113 SER A N   
764  C CA  . SER A 106 ? 0.26201 0.21123 0.34011 -0.03181 0.08844  0.02894  113 SER A CA  
765  C C   . SER A 106 ? 0.30939 0.23719 0.37554 -0.01902 0.07111  0.02196  113 SER A C   
766  O O   . SER A 106 ? 0.30968 0.23798 0.38562 -0.03452 0.06493  0.00802  113 SER A O   
767  C CB  . SER A 106 ? 0.42234 0.31541 0.47013 -0.04595 0.10687  0.04465  113 SER A CB  
768  O OG  . SER A 106 ? 0.43018 0.28689 0.44444 -0.01875 0.10417  0.05983  113 SER A OG  
769  N N   . GLY A 107 ? 0.27759 0.19312 0.32199 0.00504  0.06473  0.02806  114 GLY A N   
770  C CA  . GLY A 107 ? 0.29039 0.19500 0.32190 0.01285  0.05054  0.01837  114 GLY A CA  
771  C C   . GLY A 107 ? 0.29542 0.23245 0.34116 0.01113  0.03458  0.00754  114 GLY A C   
772  O O   . GLY A 107 ? 0.28791 0.22318 0.33153 0.00293  0.02420  -0.00407 114 GLY A O   
773  N N   . THR A 108 ? 0.24386 0.20997 0.30148 0.02125  0.03173  0.01072  115 THR A N   
774  C CA  . THR A 108 ? 0.24553 0.23820 0.31183 0.02800  0.01358  0.00377  115 THR A CA  
775  C C   . THR A 108 ? 0.24863 0.27635 0.34526 0.01091  0.00788  -0.00918 115 THR A C   
776  O O   . THR A 108 ? 0.21963 0.26203 0.31420 0.01002  -0.00958 -0.01762 115 THR A O   
777  C CB  . THR A 108 ? 0.33032 0.34143 0.40420 0.04807  0.01303  0.00800  115 THR A CB  
778  O OG1 . THR A 108 ? 0.29103 0.26961 0.33282 0.05784  0.01962  0.01559  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.21812 0.25180 0.29731 0.06444  -0.00887 0.00319  115 THR A CG2 
780  N N   . LYS A 109 ? 0.21359 0.25807 0.33501 -0.00662 0.02364  -0.01221 116 LYS A N   
781  C CA  . LYS A 109 ? 0.20007 0.28434 0.35120 -0.03200 0.02338  -0.02971 116 LYS A CA  
782  C C   . LYS A 109 ? 0.27732 0.33117 0.41322 -0.05107 0.02028  -0.03929 116 LYS A C   
783  O O   . LYS A 109 ? 0.26688 0.35824 0.41642 -0.06134 0.00662  -0.05624 116 LYS A O   
784  C CB  . LYS A 109 ? 0.22440 0.31764 0.39208 -0.05504 0.04777  -0.02952 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.42360 0.53800 0.61131 -0.09753 0.06136  -0.04724 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.50121 0.70123 0.72827 -0.10281 0.04541  -0.07239 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.57111 0.81339 0.82474 -0.15179 0.06555  -0.09496 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.57482 0.74276 0.79858 -0.18373 0.09669  -0.08186 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.27191 0.26209 0.37860 -0.05206 0.03116  -0.03068 117 ALA A N   
790  C CA  . ALA A 110 ? 0.30265 0.26040 0.39480 -0.06596 0.02970  -0.04356 117 ALA A CA  
791  C C   . ALA A 110 ? 0.28998 0.26305 0.36896 -0.05297 0.00848  -0.05006 117 ALA A C   
792  O O   . ALA A 110 ? 0.30445 0.28777 0.38423 -0.06931 0.00106  -0.06849 117 ALA A O   
793  C CB  . ALA A 110 ? 0.33550 0.22373 0.39948 -0.06011 0.04450  -0.03349 117 ALA A CB  
794  N N   . PHE A 111 ? 0.24491 0.21695 0.30657 -0.02784 0.00058  -0.03620 118 PHE A N   
795  C CA  . PHE A 111 ? 0.27649 0.25512 0.31437 -0.01975 -0.01721 -0.03881 118 PHE A CA  
796  C C   . PHE A 111 ? 0.28091 0.30792 0.33248 -0.02150 -0.03668 -0.04528 118 PHE A C   
797  O O   . PHE A 111 ? 0.26034 0.29951 0.29908 -0.03122 -0.04970 -0.05660 118 PHE A O   
798  C CB  . PHE A 111 ? 0.22667 0.18704 0.23878 0.00123  -0.01679 -0.02313 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.27599 0.22937 0.25051 0.00367  -0.03048 -0.02325 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.31552 0.26825 0.27311 -0.01160 -0.03557 -0.03775 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.29625 0.23756 0.24665 0.01862  -0.03560 -0.00979 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.35438 0.30019 0.27014 -0.01527 -0.04564 -0.03715 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.36740 0.28907 0.27109 0.01529  -0.04528 -0.00735 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.33891 0.26543 0.22434 -0.00334 -0.05021 -0.02021 118 PHE A CZ  
805  N N   . MET A 112 ? 0.23397 0.29630 0.31211 -0.01034 -0.03961 -0.04038 119 MET A N   
806  C CA  . MET A 112 ? 0.23377 0.35754 0.33297 -0.00656 -0.05970 -0.05005 119 MET A CA  
807  C C   . MET A 112 ? 0.28138 0.43985 0.40067 -0.03855 -0.06008 -0.07415 119 MET A C   
808  O O   . MET A 112 ? 0.29770 0.49296 0.41127 -0.03943 -0.08094 -0.08384 119 MET A O   
809  C CB  . MET A 112 ? 0.22908 0.39616 0.36392 0.00969  -0.05816 -0.04855 119 MET A CB  
810  C CG  . MET A 112 ? 0.41092 0.55889 0.52955 0.04694  -0.06440 -0.03078 119 MET A CG  
811  S SD  . MET A 112 ? 0.39126 0.48454 0.44627 0.06587  -0.08417 -0.01452 119 MET A SD  
812  C CE  . MET A 112 ? 0.51482 0.67063 0.57977 0.08941  -0.11825 -0.02021 119 MET A CE  
813  N N   . GLU A 113 ? 0.30887 0.45500 0.44770 -0.06689 -0.03685 -0.08469 120 GLU A N   
814  C CA  . GLU A 113 ? 0.25390 0.42336 0.40681 -0.10306 -0.03368 -0.11156 120 GLU A CA  
815  C C   . GLU A 113 ? 0.32483 0.46752 0.44670 -0.10870 -0.04236 -0.11988 120 GLU A C   
816  O O   . GLU A 113 ? 0.32061 0.50794 0.44849 -0.12697 -0.05408 -0.14164 120 GLU A O   
817  C CB  . GLU A 113 ? 0.44613 0.58040 0.60984 -0.13631 -0.00388 -0.11986 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.63619 0.82709 0.83800 -0.15671 0.00725  -0.13016 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.72642 0.86370 0.92154 -0.16778 0.03555  -0.11567 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.84163 0.90093 1.01058 -0.18707 0.05428  -0.11398 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.69850 0.87219 0.91267 -0.15730 0.03925  -0.10736 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.31338 0.39267 0.40320 -0.09514 -0.03595 -0.10665 121 ALA A N   
823  C CA  . ALA A 114 ? 0.36597 0.42643 0.42762 -0.10195 -0.04128 -0.11905 121 ALA A CA  
824  C C   . ALA A 114 ? 0.37359 0.47577 0.41501 -0.09269 -0.06779 -0.11662 121 ALA A C   
825  O O   . ALA A 114 ? 0.38683 0.51166 0.41838 -0.11000 -0.07642 -0.13517 121 ALA A O   
826  C CB  . ALA A 114 ? 0.31271 0.31318 0.34796 -0.08638 -0.02947 -0.10854 121 ALA A CB  
827  N N   . LEU A 115 ? 0.34020 0.44671 0.36969 -0.06448 -0.08022 -0.09247 122 LEU A N   
828  C CA  . LEU A 115 ? 0.34355 0.47313 0.34141 -0.05152 -0.10642 -0.08409 122 LEU A CA  
829  C C   . LEU A 115 ? 0.35948 0.56281 0.38012 -0.05997 -0.12542 -0.10084 122 LEU A C   
830  O O   . LEU A 115 ? 0.38733 0.60732 0.37919 -0.06371 -0.14200 -0.10299 122 LEU A O   
831  C CB  . LEU A 115 ? 0.29955 0.40926 0.28033 -0.01733 -0.11457 -0.05614 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.35145 0.39665 0.29855 -0.01093 -0.09942 -0.04092 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.39765 0.42203 0.32969 0.01971  -0.10578 -0.01794 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.44087 0.46139 0.33769 -0.02719 -0.10099 -0.04489 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.33951 0.58790 0.40986 -0.06387 -0.12038 -0.11146 123 GLN A N   
836  C CA  . GLN A 116 ? 0.30527 0.62720 0.39911 -0.07215 -0.13309 -0.12809 123 GLN A CA  
837  C C   . GLN A 116 ? 0.35421 0.66811 0.44573 -0.10777 -0.11787 -0.14940 123 GLN A C   
838  O O   . GLN A 116 ? 0.44395 0.80507 0.53788 -0.11312 -0.12768 -0.15964 123 GLN A O   
839  C CB  . GLN A 116 ? 0.38803 0.76313 0.53368 -0.06964 -0.12648 -0.13604 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.69656 1.14633 0.85650 -0.05379 -0.14517 -0.14113 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.91651 1.36672 1.05176 -0.00323 -0.17345 -0.11504 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.92667 1.37183 1.07418 0.02599  -0.17394 -0.10263 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.74741 1.19390 0.84291 0.00689  -0.19458 -0.10546 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.45509 0.70816 0.53971 -0.12709 -0.09433 -0.15586 124 ALA A N   
845  C CA  . ALA A 117 ? 0.53595 0.76881 0.61387 -0.15187 -0.07884 -0.17402 124 ALA A CA  
846  C C   . ALA A 117 ? 0.57274 0.77463 0.61046 -0.14586 -0.08410 -0.16936 124 ALA A C   
847  O O   . ALA A 117 ? 0.57262 0.75143 0.60501 -0.16048 -0.06955 -0.18395 124 ALA A O   
848  C CB  . ALA A 117 ? 0.47839 0.65684 0.56927 -0.16956 -0.04957 -0.18224 124 ALA A CB  
849  N N   . GLY A 118 ? 0.50350 0.73589 0.45078 -0.23473 -0.11207 -0.12048 125 GLY A N   
850  C CA  . GLY A 118 ? 0.52792 0.75390 0.41352 -0.23884 -0.10415 -0.13174 125 GLY A CA  
851  C C   . GLY A 118 ? 0.62530 0.85483 0.50943 -0.21504 -0.07620 -0.14471 125 GLY A C   
852  O O   . GLY A 118 ? 0.59435 0.83053 0.43241 -0.21977 -0.06422 -0.15183 125 GLY A O   
853  N N   . ALA A 119 ? 0.46315 0.68527 0.39707 -0.18884 -0.06263 -0.14499 126 ALA A N   
854  C CA  . ALA A 119 ? 0.46301 0.68140 0.40949 -0.15465 -0.03662 -0.14493 126 ALA A CA  
855  C C   . ALA A 119 ? 0.38970 0.65370 0.34443 -0.15127 -0.04896 -0.10819 126 ALA A C   
856  O O   . ALA A 119 ? 0.43422 0.72688 0.39893 -0.16605 -0.08062 -0.08107 126 ALA A O   
857  C CB  . ALA A 119 ? 0.44509 0.62920 0.43949 -0.12674 -0.02542 -0.14107 126 ALA A CB  
858  N N   . ASP A 120 ? 0.43744 0.70621 0.39045 -0.13210 -0.02816 -0.10697 127 ASP A N   
859  C CA  . ASP A 120 ? 0.45059 0.74849 0.40426 -0.13126 -0.04261 -0.06957 127 ASP A CA  
860  C C   . ASP A 120 ? 0.30491 0.59085 0.30471 -0.09652 -0.03049 -0.05302 127 ASP A C   
861  O O   . ASP A 120 ? 0.35083 0.60720 0.37817 -0.07538 -0.01161 -0.07020 127 ASP A O   
862  C CB  . ASP A 120 ? 0.57321 0.89441 0.46233 -0.15853 -0.03424 -0.07657 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.65415 0.98112 0.54673 -0.14234 0.00806  -0.10620 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.79063 1.09921 0.68515 -0.13316 0.03149  -0.14994 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.51955 0.86901 0.41595 -0.13890 0.01490  -0.08675 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.29070 0.59009 0.29124 -0.09402 -0.04777 -0.01721 128 ILE A N   
867  C CA  . ILE A 121 ? 0.27247 0.55366 0.30847 -0.06565 -0.04346 0.00347  128 ILE A CA  
868  C C   . ILE A 121 ? 0.25023 0.52314 0.29266 -0.05209 -0.01321 -0.01484 128 ILE A C   
869  O O   . ILE A 121 ? 0.27758 0.52056 0.35198 -0.02899 -0.00722 -0.00905 128 ILE A O   
870  C CB  . ILE A 121 ? 0.30992 0.59573 0.33142 -0.06908 -0.07165 0.04317  128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.43415 0.69500 0.47153 -0.06155 -0.09583 0.05529  128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.33869 0.59538 0.37718 -0.04594 -0.06403 0.06155  128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.60939 0.88019 0.61386 -0.08825 -0.11526 0.05406  128 ILE A CD1 
874  N N   . SER A 122 ? 0.25211 0.55242 0.26673 -0.06680 0.00584  -0.03969 129 SER A N   
875  C CA  . SER A 122 ? 0.27845 0.58570 0.31827 -0.04887 0.03252  -0.05865 129 SER A CA  
876  C C   . SER A 122 ? 0.34306 0.60743 0.42081 -0.02139 0.04170  -0.08692 129 SER A C   
877  O O   . SER A 122 ? 0.24108 0.50047 0.35487 0.00117  0.05264  -0.09688 129 SER A O   
878  C CB  . SER A 122 ? 0.26929 0.62808 0.27796 -0.07077 0.05803  -0.08683 129 SER A CB  
879  O OG  . SER A 122 ? 0.33156 0.68539 0.31736 -0.07862 0.07148  -0.13029 129 SER A OG  
880  N N   . MET A 123 ? 0.22460 0.45568 0.29528 -0.02576 0.03239  -0.09753 130 MET A N   
881  C CA  . MET A 123 ? 0.24380 0.41816 0.33661 -0.00832 0.03279  -0.11759 130 MET A CA  
882  C C   . MET A 123 ? 0.31058 0.44398 0.42678 0.00314  0.02018  -0.08670 130 MET A C   
883  O O   . MET A 123 ? 0.21536 0.29151 0.33914 0.01013  0.01539  -0.09681 130 MET A O   
884  C CB  . MET A 123 ? 0.27415 0.42699 0.34011 -0.02829 0.02655  -0.13953 130 MET A CB  
885  C CG  . MET A 123 ? 0.66215 0.84352 0.68872 -0.04546 0.03871  -0.17362 130 MET A CG  
886  S SD  . MET A 123 ? 0.81167 0.94101 0.80332 -0.06362 0.03178  -0.21222 130 MET A SD  
887  C CE  . MET A 123 ? 0.45650 0.51283 0.48093 -0.04986 0.01609  -0.19928 130 MET A CE  
888  N N   . ILE A 124 ? 0.20724 0.35993 0.32645 0.00249  0.01305  -0.05060 131 ILE A N   
889  C CA  . ILE A 124 ? 0.15891 0.27283 0.28848 0.00816  0.00480  -0.02469 131 ILE A CA  
890  C C   . ILE A 124 ? 0.17431 0.23047 0.31504 0.02191  0.00377  -0.02807 131 ILE A C   
891  O O   . ILE A 124 ? 0.19072 0.19489 0.32403 0.01552  -0.00106 -0.02190 131 ILE A O   
892  C CB  . ILE A 124 ? 0.21731 0.35268 0.34433 0.01087  -0.00350 0.00926  131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.18088 0.27437 0.31197 0.01649  -0.00710 0.02913  131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.17153 0.32555 0.29914 0.01678  -0.00093 0.01677  131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.17420 0.27788 0.29971 0.02193  -0.01909 0.05794  131 ILE A CD1 
896  N N   . GLY A 125 ? 0.19050 0.25667 0.34986 0.03781  0.00657  -0.03856 132 GLY A N   
897  C CA  . GLY A 125 ? 0.24376 0.25641 0.42305 0.05394  -0.00496 -0.03655 132 GLY A CA  
898  C C   . GLY A 125 ? 0.30696 0.25301 0.48195 0.05534  -0.01506 -0.06054 132 GLY A C   
899  O O   . GLY A 125 ? 0.33004 0.22251 0.48635 0.05234  -0.03134 -0.04467 132 GLY A O   
900  N N   . GLN A 126 ? 0.23850 0.19430 0.40084 0.04755  -0.00692 -0.09066 133 GLN A N   
901  C CA  . GLN A 126 ? 0.30681 0.18751 0.45418 0.04352  -0.02139 -0.11242 133 GLN A CA  
902  C C   . GLN A 126 ? 0.35581 0.18826 0.46365 0.01204  -0.02998 -0.08666 133 GLN A C   
903  O O   . GLN A 126 ? 0.43413 0.21293 0.50292 -0.00147 -0.03946 -0.08488 133 GLN A O   
904  C CB  . GLN A 126 ? 0.36326 0.26355 0.49771 0.03918  -0.01090 -0.15224 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.45541 0.43471 0.61106 0.05570  0.01197  -0.17506 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.68144 0.66401 0.81400 0.05112  0.02304  -0.22171 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.78806 0.70169 0.90045 0.04964  0.00821  -0.23699 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.67202 0.72959 0.79263 0.04217  0.04650  -0.23481 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.30008 0.16721 0.40662 -0.00124 -0.01980 -0.06183 134 PHE A N   
910  C CA  . PHE A 127 ? 0.35309 0.19021 0.43337 -0.03151 -0.01874 -0.04509 134 PHE A CA  
911  C C   . PHE A 127 ? 0.38130 0.20310 0.43127 -0.02819 -0.01617 -0.01415 134 PHE A C   
912  O O   . PHE A 127 ? 0.37072 0.18409 0.39165 -0.04967 -0.00430 -0.00461 134 PHE A O   
913  C CB  . PHE A 127 ? 0.24114 0.15338 0.33125 -0.04596 -0.00326 -0.04461 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.26263 0.20292 0.35198 -0.05349 -0.00495 -0.07068 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.31835 0.21216 0.38263 -0.08017 -0.01309 -0.08771 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.25848 0.26002 0.35965 -0.03973 -0.00114 -0.07825 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.33891 0.24681 0.39233 -0.08993 -0.01720 -0.11337 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.31768 0.33499 0.40401 -0.05178 -0.00298 -0.10443 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.33562 0.30548 0.39920 -0.07511 -0.01105 -0.12284 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.34678 0.17256 0.40140 -0.00545 -0.02259 -0.00577 135 GLY A N   
921  C CA  . GLY A 128 ? 0.32255 0.13938 0.34521 -0.00686 -0.01665 0.01224  135 GLY A CA  
922  C C   . GLY A 128 ? 0.31391 0.15827 0.33190 -0.00530 -0.01002 0.02492  135 GLY A C   
923  O O   . GLY A 128 ? 0.37731 0.21416 0.38380 -0.00913 -0.01153 0.03432  135 GLY A O   
924  N N   . VAL A 129 ? 0.27143 0.15293 0.32121 -0.00007 -0.00949 0.02660  136 VAL A N   
925  C CA  . VAL A 129 ? 0.26442 0.17104 0.30909 0.00287  -0.00462 0.03755  136 VAL A CA  
926  C C   . VAL A 129 ? 0.23505 0.18278 0.30527 0.01537  -0.00985 0.04506  136 VAL A C   
927  O O   . VAL A 129 ? 0.20357 0.17778 0.27701 0.01740  -0.00872 0.05297  136 VAL A O   
928  C CB  . VAL A 129 ? 0.26042 0.18285 0.33635 -0.00550 0.00865  0.04100  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.26787 0.15366 0.30556 -0.02898 0.01634  0.03357  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.23949 0.20808 0.35111 -0.00785 0.01041  0.02612  136 VAL A CG2 
931  N N   . GLY A 130 ? 0.26778 0.20603 0.27713 -0.01768 -0.01557 -0.03061 137 GLY A N   
932  C CA  . GLY A 130 ? 0.26712 0.21532 0.26807 -0.00356 -0.01177 -0.03180 137 GLY A CA  
933  C C   . GLY A 130 ? 0.22382 0.19047 0.23463 -0.00257 -0.00242 -0.02315 137 GLY A C   
934  O O   . GLY A 130 ? 0.24129 0.22007 0.25045 0.00437  0.00058  -0.02079 137 GLY A O   
935  N N   . PHE A 131 ? 0.20556 0.17301 0.22533 -0.00923 0.00142  -0.01803 138 PHE A N   
936  C CA  . PHE A 131 ? 0.18712 0.16724 0.21518 -0.00861 0.00717  -0.01239 138 PHE A CA  
937  C C   . PHE A 131 ? 0.19947 0.19071 0.23256 -0.00827 0.00689  -0.01169 138 PHE A C   
938  O O   . PHE A 131 ? 0.18757 0.18420 0.22251 -0.00440 0.00964  -0.00730 138 PHE A O   
939  C CB  . PHE A 131 ? 0.18904 0.16870 0.22271 -0.01439 0.00930  -0.00965 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.22073 0.20982 0.26146 -0.01380 0.01185  -0.00748 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.23010 0.22003 0.27259 -0.01097 0.01290  -0.00522 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.20214 0.19937 0.24828 -0.01547 0.01195  -0.00828 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.21509 0.20736 0.26324 -0.01131 0.01227  -0.00475 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.20376 0.20391 0.25300 -0.01214 0.01238  -0.00845 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.18350 0.17791 0.23305 -0.01080 0.01165  -0.00715 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.19915 0.19425 0.23549 -0.01253 0.00283  -0.01498 139 TYR A N   
947  C CA  . TYR A 132 ? 0.21972 0.22729 0.26136 -0.01003 0.00208  -0.01414 139 TYR A CA  
948  C C   . TYR A 132 ? 0.20534 0.21495 0.23836 -0.00167 0.00032  -0.01366 139 TYR A C   
949  O O   . TYR A 132 ? 0.20388 0.22079 0.23885 0.00282  0.00008  -0.01059 139 TYR A O   
950  C CB  . TYR A 132 ? 0.17451 0.19294 0.22532 -0.01661 -0.00183 -0.01698 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.20272 0.22460 0.26133 -0.02330 0.00249  -0.01405 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.20385 0.23534 0.26693 -0.01890 0.00699  -0.01199 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.19798 0.21109 0.25653 -0.03240 0.00168  -0.01308 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.18363 0.22122 0.25010 -0.02233 0.01159  -0.00937 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.27085 0.28864 0.33402 -0.03762 0.00674  -0.00779 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.25797 0.29034 0.32452 -0.03197 0.01218  -0.00611 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.25978 0.29940 0.32743 -0.03478 0.01765  -0.00089 139 TYR A OH  
958  N N   . SER A 133 ? 0.20873 0.21209 0.23023 0.00272  -0.00073 -0.01611 140 SER A N   
959  C CA  . SER A 133 ? 0.23159 0.24038 0.24191 0.01312  0.00009  -0.01343 140 SER A CA  
960  C C   . SER A 133 ? 0.22034 0.23353 0.23490 0.01515  0.00763  -0.00179 140 SER A C   
961  O O   . SER A 133 ? 0.22365 0.24355 0.23145 0.02220  0.00954  0.00494  140 SER A O   
962  C CB  . SER A 133 ? 0.25765 0.26041 0.25259 0.02059  -0.00176 -0.01947 140 SER A CB  
963  O OG  . SER A 133 ? 0.25692 0.25766 0.25232 0.02253  0.00480  -0.01534 140 SER A OG  
964  N N   . ALA A 134 ? 0.20454 0.21361 0.22997 0.00851  0.01087  0.00127  141 ALA A N   
965  C CA  . ALA A 134 ? 0.20844 0.21803 0.24113 0.00699  0.01464  0.01126  141 ALA A CA  
966  C C   . ALA A 134 ? 0.22761 0.23630 0.25991 0.01004  0.01255  0.01584  141 ALA A C   
967  O O   . ALA A 134 ? 0.22105 0.22892 0.25383 0.01108  0.01510  0.02701  141 ALA A O   
968  C CB  . ALA A 134 ? 0.18121 0.18438 0.22423 -0.00020 0.01439  0.00959  141 ALA A CB  
969  N N   . TYR A 135 ? 0.23736 0.24748 0.26949 0.01170  0.00778  0.00881  142 TYR A N   
970  C CA  . TYR A 135 ? 0.21427 0.22415 0.24567 0.01761  0.00488  0.01249  142 TYR A CA  
971  C C   . TYR A 135 ? 0.23529 0.25234 0.25446 0.02628  0.00375  0.01728  142 TYR A C   
972  O O   . TYR A 135 ? 0.23728 0.25419 0.25347 0.03331  0.00075  0.02164  142 TYR A O   
973  C CB  . TYR A 135 ? 0.21098 0.22699 0.24906 0.01805  0.00072  0.00388  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.19411 0.20295 0.23987 0.01376  0.00250  0.00143  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.23483 0.23211 0.28169 0.01844  0.00088  0.00366  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.20039 0.21097 0.24950 0.00638  0.00473  -0.00317 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.23799 0.22761 0.28826 0.01667  0.00078  -0.00096 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.24046 0.24597 0.29315 0.00447  0.00598  -0.00550 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.26693 0.26299 0.31971 0.01009  0.00368  -0.00548 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.24143 0.23182 0.29438 0.01034  0.00315  -0.01026 142 TYR A OH  
981  N N   . LEU A 136 ? 0.24653 0.26956 0.25609 0.02846  0.00569  0.01641  143 LEU A N   
982  C CA  . LEU A 136 ? 0.24177 0.27257 0.23602 0.03895  0.00642  0.02329  143 LEU A CA  
983  C C   . LEU A 136 ? 0.25119 0.27878 0.24625 0.03930  0.01321  0.04162  143 LEU A C   
984  O O   . LEU A 136 ? 0.26357 0.29455 0.24771 0.04781  0.01346  0.05177  143 LEU A O   
985  C CB  . LEU A 136 ? 0.24930 0.28680 0.23062 0.04400  0.00750  0.01717  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.24657 0.28248 0.22349 0.04373  -0.00201 -0.00040 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.27592 0.31062 0.23831 0.05037  -0.00136 -0.00717 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.25540 0.29914 0.22500 0.05033  -0.01136 -0.00522 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.21971 0.24084 0.22792 0.02939  0.01790  0.04708  144 VAL A N   
990  C CA  . VAL A 137 ? 0.27145 0.29022 0.28440 0.02556  0.02354  0.06588  144 VAL A CA  
991  C C   . VAL A 137 ? 0.21558 0.21417 0.24358 0.01542  0.01988  0.06853  144 VAL A C   
992  O O   . VAL A 137 ? 0.26469 0.25367 0.29686 0.01109  0.02100  0.08457  144 VAL A O   
993  C CB  . VAL A 137 ? 0.26220 0.29800 0.27754 0.02350  0.03228  0.07299  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.29492 0.34910 0.28968 0.03818  0.03558  0.07090  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.20570 0.24034 0.23346 0.01561  0.03152  0.06197  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.25126 0.24175 0.28630 0.01183  0.01496  0.05400  145 ALA A N   
997  C CA  . ALA A 138 ? 0.24792 0.21902 0.29386 0.00463  0.01026  0.05300  145 ALA A CA  
998  C C   . ALA A 138 ? 0.25652 0.21488 0.29806 0.01290  0.00346  0.04553  145 ALA A C   
999  O O   . ALA A 138 ? 0.28063 0.25066 0.31782 0.01977  0.00227  0.03505  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.21657 0.19027 0.27120 -0.00256 0.00999  0.04243  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.21455 0.14917 0.25822 0.01227  -0.00176 0.05109  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.26462 0.18526 0.30394 0.02294  -0.00892 0.04205  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.33024 0.24654 0.37444 0.02137  -0.01223 0.02681  146 GLU A C   
1004 O O   . GLU A 139 ? 0.28141 0.20049 0.32191 0.03247  -0.01508 0.01583  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.38100 0.27206 0.41664 0.02562  -0.01467 0.05426  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.46269 0.32781 0.50784 0.01202  -0.01947 0.05874  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.63558 0.46563 0.67746 0.01221  -0.02647 0.07317  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.60268 0.42989 0.63293 0.02497  -0.02643 0.08075  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.70925 0.51349 0.76019 -0.00082 -0.03316 0.07735  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.28443 0.19815 0.33657 0.00919  -0.01165 0.02636  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.27859 0.19102 0.33242 0.00864  -0.01463 0.01237  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.25648 0.18419 0.31765 -0.00269 -0.00981 0.01355  147 LYS A C   
1013 O O   . LYS A 140 ? 0.23114 0.16247 0.29909 -0.01145 -0.00694 0.02519  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.30671 0.18765 0.35983 0.00920  -0.02534 0.00802  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.30489 0.18346 0.35741 0.00864  -0.02989 -0.00622 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.36926 0.21290 0.41571 0.01449  -0.04310 -0.01447 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.44379 0.26604 0.50115 -0.00245 -0.05208 -0.00930 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.48950 0.28409 0.53634 0.00213  -0.06409 -0.01937 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.20313 0.14218 0.26260 -0.00114 -0.00827 0.00290  148 VAL A N   
1020 C CA  . VAL A 141 ? 0.19448 0.14567 0.25864 -0.00890 -0.00494 0.00296  148 VAL A CA  
1021 C C   . VAL A 141 ? 0.24710 0.19255 0.30971 -0.00850 -0.01020 -0.00747 148 VAL A C   
1022 O O   . VAL A 141 ? 0.22395 0.16948 0.27858 0.00027  -0.01103 -0.01637 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.18322 0.15309 0.24356 -0.00695 0.00209  0.00216  148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.20603 0.18389 0.26868 -0.01193 0.00436  0.00165  148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.21441 0.19046 0.27255 -0.00494 0.00554  0.01007  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.20906 0.15298 0.27924 -0.01686 -0.01393 -0.00613 149 THR A N   
1027 C CA  . THR A 142 ? 0.24021 0.18111 0.30763 -0.01626 -0.02033 -0.01622 149 THR A CA  
1028 C C   . THR A 142 ? 0.25299 0.21249 0.32282 -0.01934 -0.01560 -0.01403 149 THR A C   
1029 O O   . THR A 142 ? 0.24672 0.21629 0.32670 -0.02567 -0.01249 -0.00504 149 THR A O   
1030 C CB  . THR A 142 ? 0.26915 0.19116 0.34452 -0.02365 -0.03265 -0.01792 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.30254 0.20107 0.37509 -0.02064 -0.03785 -0.01779 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.32778 0.24533 0.39602 -0.02000 -0.04188 -0.03178 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.20023 0.16534 0.25966 -0.01321 -0.01450 -0.02107 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.20299 0.18106 0.26145 -0.01383 -0.01116 -0.01880 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.24294 0.21996 0.29651 -0.01146 -0.01938 -0.02667 150 VAL A C   
1036 O O   . VAL A 143 ? 0.24608 0.21961 0.28643 -0.00365 -0.02089 -0.03437 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.21703 0.20161 0.26618 -0.00959 -0.00256 -0.01696 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.21299 0.20387 0.25871 -0.00896 -0.00072 -0.01410 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.19960 0.18531 0.25243 -0.01132 0.00275  -0.01163 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.21716 0.20057 0.28116 -0.01690 -0.02495 -0.02489 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.22698 0.21292 0.28663 -0.01432 -0.03453 -0.03258 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.25055 0.25072 0.30472 -0.00936 -0.02925 -0.02785 151 ILE A C   
1043 O O   . ILE A 144 ? 0.21220 0.22184 0.27543 -0.01163 -0.02366 -0.01955 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.22370 0.20962 0.30180 -0.02476 -0.04702 -0.03385 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.33028 0.29727 0.41674 -0.03234 -0.05141 -0.03355 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.27441 0.26006 0.34528 -0.02096 -0.06068 -0.04580 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.39872 0.34324 0.46913 -0.02456 -0.05946 -0.04702 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.18643 0.18750 0.22370 -0.00070 -0.03112 -0.03270 152 THR A N   
1049 C CA  . THR A 145 ? 0.21871 0.22778 0.24816 0.00485  -0.02585 -0.02605 152 THR A CA  
1050 C C   . THR A 145 ? 0.24618 0.26011 0.26144 0.01337  -0.03344 -0.03110 152 THR A C   
1051 O O   . THR A 145 ? 0.24701 0.25700 0.25062 0.01800  -0.03906 -0.04020 152 THR A O   
1052 C CB  . THR A 145 ? 0.26240 0.26562 0.28166 0.00666  -0.01379 -0.01944 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.24401 0.24796 0.25778 0.01032  -0.01015 -0.01188 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.22980 0.23141 0.23285 0.01227  -0.01128 -0.02262 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.19964 0.22245 0.21404 0.01782  -0.03427 -0.02571 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.18613 0.21510 0.18463 0.02811  -0.04122 -0.02818 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.21653 0.24405 0.20366 0.03565  -0.03397 -0.01667 153 LYS A C   
1058 O O   . LYS A 146 ? 0.24697 0.27886 0.24520 0.03597  -0.03309 -0.01167 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.22957 0.27273 0.24231 0.02641  -0.05639 -0.03550 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.25644 0.30918 0.25248 0.03887  -0.06578 -0.03856 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.30422 0.34996 0.27617 0.04652  -0.07085 -0.04862 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.27773 0.33530 0.23151 0.06017  -0.08222 -0.05246 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.27489 0.33378 0.21058 0.07138  -0.07244 -0.03751 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.26502 0.28621 0.22935 0.04258  -0.02886 -0.01183 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.28292 0.29667 0.23247 0.04954  -0.02343 0.00078  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.31638 0.33912 0.24835 0.06273  -0.03192 0.00043  154 HIS A C   
1067 O O   . HIS A 147 ? 0.31925 0.35136 0.24343 0.06658  -0.03898 -0.00923 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.27757 0.27979 0.21601 0.04534  -0.01116 0.01014  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.32128 0.30856 0.24671 0.04818  -0.00581 0.02528  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.33910 0.32584 0.24247 0.05870  -0.00668 0.03430  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.29381 0.26262 0.22348 0.04175  -0.00055 0.03320  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.40356 0.36982 0.29933 0.05780  -0.00211 0.04858  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.33740 0.29135 0.24905 0.04734  0.00084  0.04696  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.29122 0.30988 0.21489 0.07169  -0.03275 0.00990  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.30651 0.33510 0.21212 0.08632  -0.04184 0.01048  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.35479 0.38346 0.23355 0.09205  -0.03817 0.01367  155 ASN A C   
1077 O O   . ASN A 148 ? 0.36944 0.41132 0.23300 0.10360  -0.04802 0.00762  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.33399 0.35323 0.23062 0.09752  -0.04195 0.02280  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.37154 0.40367 0.29066 0.10048  -0.04928 0.01735  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.36429 0.41906 0.30421 0.09555  -0.05766 0.00559  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.34010 0.35834 0.25492 0.10930  -0.04666 0.02650  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.35768 0.37550 0.23032 0.08498  -0.02450 0.02298  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.39662 0.41996 0.24348 0.09189  -0.01789 0.03028  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.40251 0.43855 0.24973 0.09059  -0.01699 0.01669  156 ASP A C   
1085 O O   . ASP A 149 ? 0.42301 0.46804 0.25033 0.09691  -0.00862 0.02283  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.41902 0.42747 0.25916 0.08508  -0.00306 0.05204  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.52953 0.51871 0.36101 0.09002  -0.00481 0.06686  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.45608 0.45003 0.27860 0.10397  -0.01575 0.06326  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.51816 0.48626 0.35227 0.08020  0.00341  0.08154  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.35050 0.38762 0.21882 0.08367  -0.02494 -0.00040 157 ASP A N   
1091 C CA  . ASP A 150 ? 0.32209 0.36485 0.18970 0.08389  -0.02501 -0.01361 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.39738 0.43938 0.28007 0.08135  -0.04198 -0.03372 157 ASP A C   
1093 O O   . ASP A 150 ? 0.34578 0.38892 0.24221 0.07811  -0.05202 -0.03574 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.31311 0.35114 0.19481 0.07194  -0.01098 -0.00679 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.39881 0.44796 0.26957 0.07862  -0.00525 -0.01280 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.35076 0.40777 0.20190 0.09319  -0.01312 -0.02519 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.38767 0.43922 0.26868 0.07083  0.00663  -0.00566 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.34268 0.38331 0.22329 0.08318  -0.04572 -0.04809 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.33550 0.36941 0.23111 0.07804  -0.06282 -0.06633 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.28158 0.30533 0.20722 0.06096  -0.05854 -0.06367 158 GLU A C   
1101 O O   . GLU A 151 ? 0.31904 0.34137 0.25124 0.05515  -0.04355 -0.05087 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.37948 0.41041 0.25446 0.09078  -0.07149 -0.08456 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.52598 0.56909 0.36763 0.11026  -0.07724 -0.08893 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.89931 0.94881 0.74455 0.10993  -0.09243 -0.09058 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.93123 0.99279 0.75651 0.12110  -0.08832 -0.07960 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 0.89858 0.94273 0.76748 0.09847  -0.10859 -0.10146 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.29994 0.31636 0.24372 0.05235  -0.07277 -0.07542 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.26623 0.27407 0.23710 0.03683  -0.06949 -0.07158 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.27484 0.26926 0.24084 0.03855  -0.06449 -0.07675 159 GLN A C   
1110 O O   . GLN A 152 ? 0.31272 0.29737 0.26544 0.04688  -0.07480 -0.09184 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.31799 0.32471 0.31188 0.02518  -0.08644 -0.07876 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.29920 0.30323 0.32201 0.00892  -0.08139 -0.06966 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.39064 0.40537 0.44042 -0.00395 -0.09457 -0.06971 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.38040 0.41537 0.43463 -0.00143 -0.09820 -0.06681 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.31067 0.31308 0.37954 -0.01785 -0.10214 -0.07180 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.26863 0.26218 0.24479 0.03220  -0.05034 -0.06559 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.27275 0.25891 0.24500 0.03571  -0.04404 -0.06833 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.26335 0.23981 0.25804 0.02290  -0.04233 -0.06337 160 TYR A C   
1119 O O   . TYR A 153 ? 0.24002 0.22093 0.25094 0.01241  -0.03960 -0.05381 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.24337 0.24332 0.20385 0.04202  -0.02753 -0.05808 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.33489 0.34548 0.26907 0.05827  -0.02688 -0.06295 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.33853 0.34906 0.25836 0.07202  -0.02857 -0.07483 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.33475 0.35562 0.25611 0.06235  -0.02507 -0.05568 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.41041 0.43465 0.30320 0.08983  -0.02704 -0.07931 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.41790 0.45081 0.31239 0.07862  -0.02382 -0.05844 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.41006 0.44626 0.29019 0.09240  -0.02434 -0.07037 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.54610 0.59808 0.39672 0.11131  -0.02206 -0.07299 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.22756 0.19160 0.22085 0.02633  -0.04385 -0.06975 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.21016 0.16452 0.22027 0.01708  -0.04145 -0.06383 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.27010 0.23013 0.27426 0.02480  -0.03016 -0.06116 161 ALA A C   
1131 O O   . ALA A 154 ? 0.25806 0.21727 0.24755 0.03860  -0.03129 -0.07047 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.26142 0.19172 0.27776 0.01318  -0.05669 -0.07270 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.22180 0.18977 0.23722 0.01713  -0.02021 -0.04935 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.19534 0.17102 0.21170 0.02060  -0.01128 -0.04539 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.26254 0.22396 0.28941 0.01651  -0.01491 -0.04350 162 TRP A C   
1136 O O   . TRP A 155 ? 0.22585 0.17909 0.26325 0.00634  -0.01851 -0.03850 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.20157 0.19251 0.22218 0.01381  -0.00094 -0.03442 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.19150 0.19392 0.21719 0.01307  0.00685  -0.02912 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.18956 0.21046 0.21236 0.01562  0.01450  -0.02570 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.20474 0.20424 0.24051 0.00836  0.00730  -0.02531 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.20596 0.23602 0.23898 0.01160  0.01818  -0.02131 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.20922 0.22553 0.24824 0.00848  0.01344  -0.02194 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.21634 0.20311 0.25867 0.00418  0.00312  -0.02333 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.20619 0.22562 0.25317 0.00575  0.01368  -0.01910 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.19481 0.18465 0.24241 0.00283  0.00528  -0.01889 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.20272 0.20795 0.25175 0.00428  0.00955  -0.01812 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.23817 0.19912 0.26228 0.02537  -0.01356 -0.04607 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.21343 0.15925 0.24458 0.02356  -0.01720 -0.04268 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.24880 0.20773 0.27982 0.03208  -0.01121 -0.04086 163 GLU A C   
1150 O O   . GLU A 156 ? 0.23248 0.20592 0.25668 0.04384  -0.00806 -0.04663 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.33707 0.25404 0.36353 0.02814  -0.03016 -0.05122 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.36191 0.25825 0.39807 0.01993  -0.03502 -0.04270 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.53952 0.40336 0.57532 0.01679  -0.05015 -0.04889 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.44717 0.30668 0.49580 0.00078  -0.05440 -0.04254 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.52243 0.36605 0.54537 0.03084  -0.05862 -0.06088 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.23719 0.19371 0.27570 0.02739  -0.01007 -0.03257 164 SER A N   
1157 C CA  . SER A 157 ? 0.21644 0.18563 0.25569 0.03631  -0.00713 -0.03145 164 SER A CA  
1158 C C   . SER A 157 ? 0.20246 0.15850 0.24485 0.03444  -0.01004 -0.02343 164 SER A C   
1159 O O   . SER A 157 ? 0.20669 0.15980 0.25377 0.02316  -0.00847 -0.01509 164 SER A O   
1160 C CB  . SER A 157 ? 0.17929 0.17800 0.22423 0.03177  0.00133  -0.02797 164 SER A CB  
1161 O OG  . SER A 157 ? 0.22890 0.24465 0.27768 0.03990  0.00246  -0.02755 164 SER A OG  
1162 N N   . SER A 158 ? 0.22943 0.17938 0.26773 0.04776  -0.01391 -0.02536 165 SER A N   
1163 C CA  . SER A 158 ? 0.23643 0.17987 0.27525 0.04977  -0.01566 -0.01634 165 SER A CA  
1164 C C   . SER A 158 ? 0.25693 0.23045 0.29903 0.05646  -0.01181 -0.01598 165 SER A C   
1165 O O   . SER A 158 ? 0.28192 0.25395 0.32124 0.06694  -0.01523 -0.01267 165 SER A O   
1166 C CB  . SER A 158 ? 0.29686 0.20833 0.32794 0.06097  -0.02486 -0.01746 165 SER A CB  
1167 O OG  . SER A 158 ? 0.38113 0.26365 0.41191 0.05164  -0.03098 -0.01802 165 SER A OG  
1168 N N   . ALA A 159 ? 0.20364 0.20390 0.25212 0.05022  -0.00593 -0.01880 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.22508 0.25772 0.28127 0.05279  -0.00362 -0.01930 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.24888 0.29372 0.30469 0.07158  -0.00549 -0.02497 166 ALA A C   
1171 O O   . ALA A 159 ? 0.31043 0.34609 0.35973 0.08078  -0.00583 -0.03149 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.27072 0.30552 0.32733 0.04849  -0.00572 -0.01291 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.31467 0.38247 0.37653 0.07972  -0.00744 -0.02386 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.27819 0.36397 0.34102 0.10009  -0.00842 -0.02947 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.22987 0.34885 0.30086 0.10144  -0.00093 -0.03390 167 GLY A C   
1176 O O   . GLY A 160 ? 0.28298 0.41530 0.35110 0.12147  -0.00027 -0.03990 167 GLY A O   
1177 N N   . GLY A 161 ? 0.16453 0.29685 0.24404 0.08211  0.00499  -0.03034 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.15701 0.32804 0.24749 0.08054  0.01318  -0.02967 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.17748 0.33987 0.25699 0.08151  0.01900  -0.03237 168 GLY A C   
1180 O O   . GLY A 161 ? 0.16492 0.36124 0.25182 0.08028  0.02747  -0.02920 168 GLY A O   
1181 N N   . SER A 162 ? 0.18843 0.30930 0.25123 0.08330  0.01445  -0.03716 169 SER A N   
1182 C CA  . SER A 162 ? 0.16200 0.27614 0.21225 0.08738  0.01761  -0.04199 169 SER A CA  
1183 C C   . SER A 162 ? 0.19084 0.26598 0.23254 0.07475  0.01267  -0.04229 169 SER A C   
1184 O O   . SER A 162 ? 0.21070 0.26080 0.25348 0.06807  0.00661  -0.04000 169 SER A O   
1185 C CB  . SER A 162 ? 0.26020 0.37143 0.29610 0.11416  0.01468  -0.05351 169 SER A CB  
1186 O OG  . SER A 162 ? 0.28428 0.35261 0.30987 0.12143  0.00314  -0.05952 169 SER A OG  
1187 N N   . PHE A 163 ? 0.19969 0.27401 0.23306 0.07246  0.01572  -0.04405 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.19643 0.23963 0.22212 0.06339  0.01023  -0.04581 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.21646 0.25475 0.22515 0.07630  0.00796  -0.05588 170 PHE A C   
1190 O O   . PHE A 163 ? 0.23367 0.29722 0.23581 0.09061  0.01385  -0.05900 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.18330 0.23018 0.21646 0.04382  0.01481  -0.03606 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.20021 0.27395 0.23368 0.04086  0.02408  -0.03031 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.18745 0.29055 0.23422 0.03590  0.03090  -0.02260 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.21244 0.28271 0.23382 0.04176  0.02527  -0.03110 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.23917 0.36663 0.28846 0.03019  0.03974  -0.01380 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.18579 0.27978 0.20603 0.03892  0.03453  -0.02254 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.20493 0.32690 0.23990 0.03193  0.04232  -0.01269 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.21711 0.22535 0.21874 0.07187  -0.00113 -0.06111 171 THR A N   
1199 C CA  . THR A 164 ? 0.21783 0.21776 0.20150 0.08354  -0.00676 -0.07292 171 THR A CA  
1200 C C   . THR A 164 ? 0.23328 0.23072 0.21617 0.07028  -0.00719 -0.06900 171 THR A C   
1201 O O   . THR A 164 ? 0.23539 0.22648 0.23130 0.05328  -0.00687 -0.06000 171 THR A O   
1202 C CB  . THR A 164 ? 0.27776 0.24017 0.25209 0.09317  -0.02238 -0.08664 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.32333 0.25911 0.30942 0.07474  -0.03031 -0.08155 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.30842 0.26853 0.28077 0.10996  -0.02351 -0.09090 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.25607 0.26120 0.22182 0.08087  -0.00763 -0.07580 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.26769 0.26987 0.22843 0.07317  -0.01057 -0.07432 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.31193 0.29948 0.25206 0.08787  -0.02355 -0.09177 172 VAL A C   
1208 O O   . VAL A 165 ? 0.29495 0.29125 0.21718 0.10831  -0.02257 -0.10149 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.26826 0.29916 0.22657 0.07028  0.00326  -0.06116 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.26226 0.28823 0.21190 0.06621  -0.00129 -0.06008 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.23948 0.28013 0.21758 0.05490  0.01279  -0.04629 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.27848 0.24561 0.22120 0.07847  -0.03659 -0.09656 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.30631 0.25803 0.23052 0.08964  -0.05244 -0.11438 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.30590 0.25889 0.23432 0.07780  -0.05904 -0.11156 173 ARG A C   
1215 O O   . ARG A 166 ? 0.28668 0.24353 0.23545 0.06035  -0.05461 -0.09809 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.37947 0.29689 0.30742 0.08941  -0.06865 -0.12580 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.37594 0.27313 0.32914 0.06666  -0.07600 -0.11936 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.54095 0.41148 0.50173 0.06358  -0.08382 -0.11878 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.50448 0.37869 0.47019 0.06756  -0.07224 -0.11149 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.66227 0.51987 0.62639 0.07365  -0.07532 -0.11154 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.56118 0.39344 0.51924 0.07530  -0.08961 -0.11839 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.57179 0.43845 0.54041 0.07889  -0.06466 -0.10481 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.36787 0.31956 0.27536 0.08986  -0.07016 -0.12516 174 THR A N   
1224 C CA  . THR A 167 ? 0.39147 0.34324 0.30379 0.08018  -0.08107 -0.12560 174 THR A CA  
1225 C C   . THR A 167 ? 0.38604 0.31417 0.32375 0.06143  -0.09570 -0.12824 174 THR A C   
1226 O O   . THR A 167 ? 0.49130 0.39737 0.43299 0.06101  -0.10320 -0.13366 174 THR A O   
1227 C CB  . THR A 167 ? 0.47159 0.42648 0.35906 0.09650  -0.09178 -0.13837 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.68198 0.62008 0.56343 0.10644  -0.09951 -0.14865 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.43300 0.41643 0.29621 0.11261  -0.07608 -0.13113 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.39042 0.32833 0.34940 0.04472  -0.09561 -0.11679 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.41527 0.33895 0.40228 0.02505  -0.10614 -0.11439 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.59701 0.51456 0.58635 0.02138  -0.12579 -0.12465 175 ASP A C   
1233 O O   . ASP A 168 ? 0.57660 0.51185 0.56131 0.02420  -0.13091 -0.12706 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.40455 0.34759 0.41555 0.01033  -0.09401 -0.09474 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.52636 0.46042 0.56695 -0.00942 -0.10117 -0.08856 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.61731 0.52732 0.66089 -0.01273 -0.10515 -0.09105 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.44463 0.39680 0.50533 -0.02075 -0.10279 -0.08021 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.68075 0.57498 0.67735 0.01540  -0.13505 -0.12765 176 THR A N   
1239 C CA  . THR A 169 ? 0.90054 0.78770 0.90338 0.00865  -0.15243 -0.13461 176 THR A CA  
1240 C C   . THR A 169 ? 0.84556 0.74232 0.88246 -0.01579 -0.15580 -0.12210 176 THR A C   
1241 O O   . THR A 169 ? 0.82562 0.72536 0.87156 -0.02373 -0.16949 -0.12642 176 THR A O   
1242 C CB  . THR A 169 ? 0.91999 0.77581 0.91294 0.01430  -0.16230 -0.14424 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.75597 0.59650 0.75836 0.00820  -0.15414 -0.13448 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.84518 0.69931 0.80416 0.04107  -0.16250 -0.15872 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.82119 0.72616 0.87713 -0.02705 -0.14309 -0.10632 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.73807 0.65562 0.82625 -0.04870 -0.14281 -0.09145 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.64609 0.59705 0.74962 -0.05464 -0.14623 -0.08823 177 GLY A C   
1248 O O   . GLY A 170 ? 0.59751 0.55773 0.68579 -0.04308 -0.15377 -0.09963 177 GLY A O   
1249 N N   . GLU A 171 ? 0.57585 0.54782 0.70847 -0.07074 -0.14001 -0.07177 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.50265 0.51242 0.65432 -0.07590 -0.14185 -0.06621 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.43448 0.46329 0.57324 -0.05927 -0.13689 -0.06897 178 GLU A C   
1252 O O   . GLU A 171 ? 0.36959 0.39869 0.50537 -0.05393 -0.12385 -0.06250 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.48440 0.51619 0.66657 -0.09183 -0.13087 -0.04615 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.61990 0.67800 0.82772 -0.10629 -0.13909 -0.04202 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.51614 0.54792 0.72173 -0.11540 -0.15634 -0.05317 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.65294 0.68914 0.85184 -0.11134 -0.17110 -0.06686 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.67818 0.68355 0.88699 -0.12517 -0.15593 -0.04844 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.43880 0.48294 0.56859 -0.05010 -0.14731 -0.07813 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.47593 0.53881 0.59156 -0.03256 -0.14228 -0.07825 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.48324 0.57222 0.61755 -0.03456 -0.12481 -0.05912 179 PRO A C   
1261 O O   . PRO A 172 ? 0.43332 0.54695 0.60096 -0.04810 -0.12805 -0.05062 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.45576 0.53397 0.56298 -0.02507 -0.15659 -0.08718 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.43051 0.49582 0.54708 -0.03933 -0.16992 -0.09417 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.49698 0.53419 0.62085 -0.05181 -0.16459 -0.09084 179 PRO A CD  
1265 N N   . MET A 173 ? 0.35364 0.43812 0.46638 -0.02064 -0.10660 -0.05228 180 MET A N   
1266 C CA  . MET A 173 ? 0.33665 0.44053 0.46163 -0.01911 -0.09129 -0.03703 180 MET A CA  
1267 C C   . MET A 173 ? 0.36678 0.49153 0.48361 -0.00347 -0.08996 -0.03372 180 MET A C   
1268 O O   . MET A 173 ? 0.45645 0.60106 0.58584 -0.00024 -0.08093 -0.02317 180 MET A O   
1269 C CB  . MET A 173 ? 0.31493 0.39928 0.42498 -0.01523 -0.07304 -0.03047 180 MET A CB  
1270 C CG  . MET A 173 ? 0.50082 0.56986 0.62147 -0.02810 -0.06938 -0.02797 180 MET A CG  
1271 S SD  . MET A 173 ? 0.48652 0.52935 0.57783 -0.01812 -0.05549 -0.02887 180 MET A SD  
1272 C CE  . MET A 173 ? 0.35967 0.41728 0.44955 -0.00971 -0.04141 -0.01716 180 MET A CE  
1273 N N   . GLY A 174 ? 0.36050 0.48024 0.45365 0.00882  -0.09792 -0.04183 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.25714 0.39245 0.33947 0.02545  -0.09653 -0.03674 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.27631 0.39042 0.33143 0.03742  -0.08027 -0.02886 181 GLY A C   
1276 O O   . GLY A 174 ? 0.29108 0.39388 0.31808 0.04941  -0.08065 -0.02972 181 GLY A O   
1277 N N   . ARG A 175 ? 0.21461 0.32326 0.27777 0.03354  -0.06655 -0.02063 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.21882 0.30443 0.26029 0.04083  -0.05281 -0.01378 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.24067 0.32270 0.29561 0.03303  -0.04194 -0.00903 182 ARG A C   
1280 O O   . ARG A 175 ? 0.20837 0.31221 0.28465 0.03150  -0.04160 -0.00576 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.20914 0.29610 0.23586 0.05813  -0.05193 -0.00715 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.24275 0.29911 0.24484 0.06309  -0.04085 0.00010  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.26246 0.31223 0.25394 0.07884  -0.03897 0.00777  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.20329 0.27111 0.21430 0.08286  -0.03778 0.00755  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.20392 0.30066 0.22707 0.09381  -0.04464 0.00729  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.22683 0.33691 0.24531 0.10129  -0.05530 0.00601  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.20426 0.32065 0.24439 0.09882  -0.04081 0.00845  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.24152 0.31982 0.22886 -0.03367 -0.07747 0.04317  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.18113 0.28283 0.22415 -0.02850 -0.05749 0.03545  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.25861 0.32422 0.25975 -0.01279 -0.04340 0.01482  183 GLY A C   
1291 O O   . GLY A 176 ? 0.25002 0.28009 0.19098 0.00326  -0.03551 0.00871  183 GLY A O   
1292 N N   . THR A 177 ? 0.16628 0.23955 0.19910 -0.01569 -0.03767 0.00681  184 THR A N   
1293 C CA  . THR A 177 ? 0.18770 0.23819 0.19860 -0.00041 -0.02296 -0.00717 184 THR A CA  
1294 C C   . THR A 177 ? 0.25879 0.29589 0.27236 -0.01355 -0.03300 -0.01569 184 THR A C   
1295 O O   . THR A 177 ? 0.19163 0.25453 0.25057 -0.02668 -0.03692 -0.00978 184 THR A O   
1296 C CB  . THR A 177 ? 0.21903 0.30366 0.27823 0.01540  -0.00001 -0.00315 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.19836 0.29381 0.25654 0.03024  0.01205  0.00786  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.23985 0.30753 0.28810 0.02860  0.01115  -0.01107 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.23721 0.23105 0.20143 -0.00765 -0.03333 -0.02741 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.27834 0.25608 0.24239 -0.01653 -0.03981 -0.03451 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.21696 0.19036 0.18057 0.00324  -0.01959 -0.03961 185 LYS A C   
1302 O O   . LYS A 178 ? 0.29713 0.24155 0.22206 0.02120  -0.00721 -0.04221 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.36656 0.29135 0.27316 -0.02971 -0.06159 -0.04120 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.50117 0.40877 0.41221 -0.04367 -0.07320 -0.04429 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.64147 0.48383 0.48527 -0.05552 -0.09521 -0.05329 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.69250 0.54176 0.54455 -0.07946 -0.12370 -0.04008 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.72533 0.51812 0.51761 -0.08609 -0.13873 -0.04426 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.20450 0.20437 0.20920 0.00096  -0.01531 -0.03814 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.24985 0.24866 0.25936 0.01505  -0.00325 -0.03850 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.27609 0.25022 0.26966 0.00789  -0.01003 -0.04354 186 VAL A C   
1311 O O   . VAL A 179 ? 0.26088 0.24708 0.27446 -0.00608 -0.01738 -0.04268 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.16996 0.20853 0.22702 0.01562  0.00147  -0.03279 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.19189 0.23096 0.25653 0.02612  0.00638  -0.02831 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.16464 0.22823 0.24512 0.02209  0.00853  -0.02563 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.25956 0.19732 0.21844 0.01976  -0.00359 -0.04645 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.26269 0.17246 0.20600 0.01475  -0.00830 -0.04989 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.24800 0.17082 0.21160 0.02909  0.00391  -0.04176 187 ILE A C   
1318 O O   . ILE A 180 ? 0.27192 0.18413 0.22812 0.04922  0.01978  -0.03560 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.31930 0.16858 0.20439 0.01621  -0.01073 -0.05884 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.36935 0.20485 0.22970 0.00009  -0.02902 -0.06382 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.35550 0.17611 0.23212 0.00806  -0.01725 -0.06110 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.54567 0.31049 0.33192 0.00089  -0.03424 -0.07500 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.21791 0.16096 0.20551 0.01951  -0.00272 -0.03853 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.23384 0.19087 0.23944 0.02795  0.00133  -0.02828 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.27025 0.19576 0.25733 0.03023  0.00331  -0.02697 188 LEU A C   
1326 O O   . LEU A 181 ? 0.29114 0.20891 0.27450 0.01682  -0.00465 -0.02997 188 LEU A O   
1327 C CB  . LEU A 181 ? 0.21475 0.20192 0.24237 0.01616  -0.00751 -0.02641 188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.18862 0.20122 0.23473 0.01122  -0.00939 -0.02901 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.27606 0.30023 0.32762 0.00016  -0.01515 -0.03022 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.24747 0.27645 0.31369 0.02439  -0.00487 -0.01946 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.25513 0.16316 0.23621 0.04873  0.01679  -0.01880 189 HIS A N   
1332 C CA  . HIS A 182 ? 0.30557 0.18408 0.27466 0.05347  0.02174  -0.01443 189 HIS A CA  
1333 C C   . HIS A 182 ? 0.28823 0.20156 0.29015 0.05444  0.01729  0.00269  189 HIS A C   
1334 O O   . HIS A 182 ? 0.27597 0.20968 0.30307 0.06803  0.02337  0.02002  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.36290 0.19835 0.30611 0.07530  0.04305  -0.01215 189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.42375 0.21881 0.32062 0.07490  0.04555  -0.02918 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.56222 0.29641 0.40883 0.06685  0.04066  -0.04442 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.41271 0.21693 0.30264 0.08001  0.04965  -0.03211 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.52544 0.23038 0.32950 0.06610  0.03932  -0.05679 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.52881 0.27738 0.35903 0.07548  0.04674  -0.04897 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.25054 0.17067 0.25265 0.03974  0.00589  0.00107  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.25510 0.20566 0.27422 0.03638  -0.00340 0.01397  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.30115 0.25088 0.33268 0.04918  0.00117  0.03474  190 LEU A C   
1344 O O   . LEU A 183 ? 0.29211 0.21140 0.31508 0.05776  0.01321  0.03696  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.23447 0.18406 0.24135 0.02138  -0.01008 0.00836  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.22286 0.17984 0.22740 0.00980  -0.01258 -0.00539 190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.31402 0.26831 0.31059 0.00036  -0.01146 -0.00383 190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.29204 0.27395 0.30654 0.00921  -0.01833 -0.00708 190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.27597 0.25740 0.32869 0.04908  -0.01051 0.05200  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.27806 0.26637 0.34769 0.05768  -0.01141 0.07748  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.30693 0.27973 0.35399 0.05086  -0.01354 0.07675  191 LYS A C   
1352 O O   . LYS A 184 ? 0.33333 0.30102 0.35607 0.03754  -0.01916 0.06201  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.30996 0.33633 0.40622 0.05264  -0.03282 0.09861  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.29716 0.34498 0.42618 0.05764  -0.03238 0.10433  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.35362 0.43887 0.52191 0.05183  -0.05716 0.13468  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.44230 0.54002 0.60125 0.03035  -0.08336 0.12213  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.46272 0.59313 0.67670 0.03028  -0.09360 0.14511  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.32737 0.29320 0.38699 0.06238  -0.00560 0.09689  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.37292 0.32182 0.41686 0.05916  -0.00314 0.09999  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.43295 0.39754 0.45471 0.04539  -0.02061 0.10228  192 GLU A C   
1361 O O   . GLU A 185 ? 0.44738 0.39633 0.44877 0.04005  -0.01541 0.09701  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.49534 0.43930 0.56309 0.07556  0.00812  0.12671  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.66006 0.58705 0.71924 0.07485  0.01301  0.13498  192 GLU A CG  
1364 C CD  . GLU A 185 ? 0.85961 0.77588 0.94592 0.09351  0.02934  0.16048  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 0.79528 0.73656 0.91299 0.10506  0.02896  0.18460  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 0.99504 0.87779 1.07643 0.09670  0.04314  0.15937  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.36606 0.35647 0.38846 0.03938  -0.04093 0.11129  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.42525 0.41703 0.40959 0.02682  -0.05809 0.11232  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.37919 0.36368 0.33410 0.01459  -0.06190 0.08667  193 ASP A C   
1370 O O   . ASP A 186 ? 0.38348 0.36049 0.29721 0.00460  -0.07578 0.08465  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.48278 0.49789 0.47592 0.02365  -0.08440 0.14016  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.53757 0.57666 0.55904 0.01764  -0.10299 0.14328  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.64214 0.70038 0.67030 0.00843  -0.13280 0.16606  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.54369 0.58333 0.58380 0.02139  -0.08982 0.12658  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.30872 0.28950 0.27820 0.01567  -0.04866 0.06762  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.28765 0.26426 0.23874 0.00599  -0.04917 0.04677  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.28564 0.24615 0.23376 0.00580  -0.02911 0.03345  194 GLN A C   
1378 O O   . GLN A 187 ? 0.32081 0.28225 0.27264 0.00112  -0.02473 0.01870  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.29014 0.28528 0.26906 0.00510  -0.05681 0.04181  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.29652 0.31313 0.29263 0.00278  -0.08017 0.06181  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.35878 0.36647 0.31278 -0.01273 -0.10411 0.06160  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.41852 0.40470 0.33368 -0.02039 -0.10011 0.04170  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.35838 0.37881 0.31776 -0.01745 -0.12938 0.08543  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.32599 0.27370 0.27332 0.00980  -0.01825 0.04226  195 THR A N   
1385 C CA  . THR A 188 ? 0.32131 0.25673 0.27738 0.00674  -0.00371 0.03621  195 THR A CA  
1386 C C   . THR A 188 ? 0.39061 0.32011 0.32536 0.00291  0.00685  0.03475  195 THR A C   
1387 O O   . THR A 188 ? 0.38196 0.30731 0.33470 -0.00006 0.01918  0.03594  195 THR A O   
1388 C CB  . THR A 188 ? 0.38973 0.31129 0.35917 0.01072  0.00367  0.04900  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.41509 0.33558 0.36565 0.01565  0.00563  0.06595  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.41054 0.32548 0.39707 0.01697  0.00067  0.04839  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.37753 0.30229 0.27324 0.00290  0.00270  0.03452  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.37746 0.28589 0.24395 0.00277  0.01926  0.03110  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.35373 0.26971 0.24386 -0.00190 0.02549  0.01804  196 GLU A C   
1394 O O   . GLU A 189 ? 0.38590 0.29254 0.27501 0.00034  0.04692  0.02115  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.43774 0.32646 0.24253 0.00161  0.00998  0.02819  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.42725 0.31885 0.22351 -0.00753 -0.00890 0.01184  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.56657 0.43858 0.30596 -0.01433 -0.03249 0.01216  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.59073 0.47443 0.33254 -0.01534 -0.05241 0.02702  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.56503 0.40547 0.25411 -0.01924 -0.03151 -0.00096 196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.33086 0.26441 0.24595 -0.00637 0.01012  0.00765  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.32135 0.26449 0.25871 -0.01064 0.01392  -0.00291 197 TYR A CA  
1402 C C   . TYR A 190 ? 0.28003 0.23022 0.25657 -0.01331 0.02037  0.00227  197 TYR A C   
1403 O O   . TYR A 190 ? 0.32646 0.28733 0.32491 -0.01779 0.02029  -0.00324 197 TYR A O   
1404 C CB  . TYR A 190 ? 0.32688 0.28502 0.27292 -0.01304 -0.00411 -0.01266 197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.28190 0.23139 0.19289 -0.01610 -0.01705 -0.01502 197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.33989 0.26796 0.21642 -0.01963 -0.00989 -0.02357 197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.30636 0.26390 0.21605 -0.01615 -0.03708 -0.00627 197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.36015 0.26863 0.19269 -0.02617 -0.02681 -0.02762 197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.34927 0.29727 0.22659 -0.02373 -0.05671 -0.00534 197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.36149 0.28137 0.19488 -0.03037 -0.05402 -0.01815 197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.44633 0.34524 0.23542 -0.04152 -0.07854 -0.01955 197 TYR A OH  
1412 N N   . LEU A 191 ? 0.26338 0.20634 0.24918 -0.01239 0.02317  0.01448  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.29556 0.23911 0.31713 -0.01931 0.02571  0.02373  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.36153 0.30316 0.39648 -0.01758 0.04675  0.04322  198 LEU A C   
1415 O O   . LEU A 191 ? 0.32540 0.27252 0.40157 -0.02563 0.04729  0.05739  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.30929 0.24023 0.33775 -0.02112 0.01466  0.02664  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.33022 0.25802 0.34596 -0.01787 0.00174  0.01167  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.36983 0.27463 0.38442 -0.01578 -0.00258 0.01495  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.38784 0.32170 0.41250 -0.02444 -0.00535 0.00034  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.33123 0.26217 0.33106 -0.00733 0.06368  0.04690  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.35030 0.27312 0.35511 0.00037  0.09217  0.06877  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.35800 0.28526 0.37782 0.00206  0.11113  0.07149  199 GLU A C   
1423 O O   . GLU A 192 ? 0.35640 0.27801 0.34646 0.00305  0.10957  0.05268  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.40394 0.30285 0.34784 0.01264  0.10417  0.07022  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.44284 0.33859 0.37910 0.01455  0.09402  0.07879  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.81845 0.72239 0.81022 0.01172  0.09934  0.10143  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.81558 0.72368 0.84245 0.01333  0.12049  0.12124  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.90937 0.81402 0.91312 0.00780  0.08274  0.10208  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.28221 0.26284 0.42050 -0.02354 -0.03015 0.03912  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.26208 0.26145 0.38251 -0.02420 -0.02502 0.03394  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.23375 0.25071 0.32413 -0.01780 -0.01158 0.04318  200 GLU A C   
1432 O O   . GLU A 193 ? 0.25550 0.27735 0.32196 -0.01258 -0.00768 0.02996  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.25163 0.26045 0.40323 -0.03493 -0.02701 0.04652  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.32139 0.34988 0.46443 -0.03473 -0.02295 0.04164  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.53904 0.58626 0.71468 -0.04391 -0.02171 0.06247  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.39444 0.44068 0.59804 -0.05105 -0.02378 0.08218  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.44166 0.50779 0.62035 -0.04407 -0.01888 0.06324  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.26254 0.29095 0.35505 -0.01917 -0.00463 0.06597  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.27980 0.32701 0.33879 -0.01506 0.00890  0.06950  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.27656 0.31654 0.30127 -0.01056 0.00622  0.05482  201 ARG A C   
1441 O O   . ARG A 194 ? 0.27743 0.32256 0.27295 -0.00755 0.01414  0.04353  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.31566 0.38627 0.38107 -0.01899 0.01658  0.09865  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.34665 0.41974 0.41388 -0.02163 0.00991  0.11586  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.41071 0.51376 0.49920 -0.02755 0.01554  0.15247  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.59788 0.70393 0.70933 -0.03122 0.00660  0.17796  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.53729 0.68017 0.65485 -0.03654 0.01051  0.21434  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.57716 0.75739 0.67794 -0.03846 0.02428  0.22752  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.54951 0.69637 0.69267 -0.03919 0.00160  0.24032  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.26277 0.29004 0.29478 -0.00986 -0.00460 0.05481  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.24027 0.26499 0.24591 -0.00630 -0.00869 0.04580  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.25735 0.27390 0.25337 -0.00171 -0.01120 0.02261  202 ARG A C   
1452 O O   . ARG A 195 ? 0.24778 0.26734 0.21903 -0.00072 -0.01004 0.01465  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.24368 0.26088 0.26822 -0.00420 -0.01706 0.05626  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.26318 0.28438 0.26639 -0.00109 -0.02198 0.05474  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.32490 0.36740 0.29685 -0.00863 -0.02027 0.06739  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.26065 0.30994 0.22160 -0.00880 -0.02869 0.07341  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.32332 0.37759 0.25257 -0.01326 -0.03226 0.06288  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.32510 0.37549 0.22984 -0.01669 -0.02630 0.04398  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.33530 0.39817 0.26223 -0.01429 -0.04192 0.07274  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.22364 0.23220 0.24066 -0.00051 -0.01597 0.01265  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.24791 0.25899 0.25852 0.00271  -0.01894 -0.00363 203 ILE A CA  
1462 C C   . ILE A 196 ? 0.23189 0.25177 0.23532 0.00231  -0.01026 -0.00422 203 ILE A C   
1463 O O   . ILE A 196 ? 0.24589 0.26818 0.23762 0.00525  -0.01005 -0.01081 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.26691 0.27521 0.29760 0.00109  -0.02628 -0.01448 203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.24044 0.23447 0.28027 0.00452  -0.03195 -0.02014 203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.22231 0.24549 0.24663 0.00293  -0.02950 -0.02515 203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.25368 0.23725 0.31598 -0.00090 -0.03865 -0.03361 203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.23717 0.26237 0.25321 -0.00060 -0.00215 0.00445  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.20765 0.24095 0.22217 0.00226  0.01046  0.00432  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.25039 0.27903 0.23505 0.00504  0.01782  -0.00264 204 LYS A C   
1471 O O   . LYS A 197 ? 0.24684 0.27265 0.22946 0.00910  0.02392  -0.01171 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.25745 0.30207 0.28899 0.00036  0.02107  0.01878  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.35642 0.40897 0.42223 -0.00516 0.01469  0.02686  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.40935 0.47985 0.49334 -0.00446 0.02952  0.04449  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.63637 0.71207 0.74401 -0.01350 0.02400  0.06317  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.65893 0.74965 0.80479 -0.02063 0.01998  0.07618  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.23712 0.26633 0.20156 0.00156  0.01720  0.00281  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.27427 0.30233 0.20509 -0.00001 0.02166  -0.00545 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.24739 0.26424 0.17057 0.00000  0.01097  -0.01701 205 GLU A C   
1480 O O   . GLU A 198 ? 0.28045 0.28930 0.18937 -0.00033 0.01512  -0.03054 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.27334 0.31356 0.18710 -0.00653 0.01899  0.00899  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.30972 0.35373 0.18426 -0.01305 0.01732  0.00148  205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.33980 0.40428 0.20435 -0.02102 0.01070  0.02370  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.35921 0.42245 0.25042 -0.01973 0.00074  0.04028  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.36269 0.44661 0.19478 -0.02838 0.01615  0.02508  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.23297 0.24939 0.16835 0.00065  -0.00219 -0.01195 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.25424 0.26795 0.18601 0.00103  -0.01255 -0.01687 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.27261 0.28522 0.22167 0.00506  -0.01054 -0.02402 206 ILE A C   
1489 O O   . ILE A 199 ? 0.29545 0.30300 0.24162 0.00373  -0.01332 -0.02910 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.25307 0.27166 0.19512 0.00379  -0.02313 -0.00907 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.26239 0.28374 0.19657 0.00030  -0.02501 0.00416  206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.24946 0.27349 0.19156 0.00559  -0.03250 -0.00979 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.29749 0.31843 0.25267 0.00630  -0.03014 0.01104  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.23691 0.25633 0.20867 0.00844  -0.00718 -0.02161 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.22607 0.25267 0.22060 0.01157  -0.00576 -0.02140 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.23756 0.25253 0.23364 0.01370  0.00730  -0.02735 207 VAL A C   
1497 O O   . VAL A 200 ? 0.26049 0.27220 0.27078 0.01536  0.00629  -0.02847 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.21135 0.25270 0.22870 0.01149  -0.00616 -0.01544 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.25685 0.31272 0.30297 0.01384  -0.00302 -0.00835 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.24240 0.29194 0.25732 0.00987  -0.01900 -0.01735 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.22576 0.23481 0.20918 0.01419  0.02070  -0.03130 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.29754 0.29455 0.28032 0.01864  0.03715  -0.04244 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.32124 0.29955 0.27887 0.01363  0.03267  -0.05830 208 LYS A C   
1504 O O   . LYS A 201 ? 0.39663 0.35877 0.36659 0.01660  0.03914  -0.06954 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.30267 0.30554 0.27410 0.02107  0.05420  -0.04233 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.39890 0.39010 0.36401 0.02809  0.07570  -0.05908 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.46846 0.47577 0.42383 0.03220  0.09467  -0.05486 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.65285 0.64903 0.59528 0.04114  0.11942  -0.07754 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.71578 0.73159 0.62300 0.04106  0.13515  -0.07978 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.30779 0.28818 0.23551 0.00507  0.02030  -0.05760 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.33576 0.30272 0.23750 -0.00382 0.01291  -0.07068 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.29492 0.25483 0.22057 -0.00515 -0.00018 -0.06815 209 LYS A C   
1513 O O   . LYS A 202 ? 0.33608 0.27607 0.26131 -0.00958 -0.00061 -0.08264 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.35407 0.33373 0.22537 -0.01326 0.00139  -0.06207 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.40395 0.37706 0.24593 -0.02678 -0.01020 -0.07170 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.54802 0.54239 0.36301 -0.03560 -0.01784 -0.05741 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.66104 0.65795 0.45110 -0.05191 -0.03494 -0.05897 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.77413 0.79934 0.54830 -0.05960 -0.04344 -0.03577 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.27552 0.25294 0.22381 -0.00170 -0.01065 -0.05010 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.31264 0.29558 0.28080 -0.00385 -0.02513 -0.04057 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.35104 0.34665 0.36155 0.00364  -0.02356 -0.02887 210 HIS A C   
1522 O O   . HIS A 203 ? 0.31055 0.31213 0.34448 0.00173  -0.03337 -0.01866 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.31260 0.31531 0.27073 -0.00553 -0.03873 -0.02671 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.39162 0.39030 0.31674 -0.01445 -0.04419 -0.02889 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.37557 0.36413 0.28636 -0.02651 -0.05342 -0.03438 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.41755 0.42395 0.32472 -0.01476 -0.04306 -0.02348 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.44343 0.43871 0.32528 -0.03457 -0.05826 -0.03114 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.44410 0.45074 0.32595 -0.02662 -0.05135 -0.02254 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.23241 0.23750 0.25656 0.01048  -0.01304 -0.02582 211 SER A N   
1530 C CA  . SER A 204 ? 0.24054 0.26993 0.30316 0.01503  -0.01496 -0.00914 211 SER A CA  
1531 C C   . SER A 204 ? 0.24412 0.27189 0.33345 0.02106  0.00071  -0.00748 211 SER A C   
1532 O O   . SER A 204 ? 0.24556 0.30088 0.36426 0.02310  -0.00086 0.00929  211 SER A O   
1533 C CB  . SER A 204 ? 0.24044 0.29844 0.29608 0.01502  -0.02422 -0.00087 211 SER A CB  
1534 O OG  . SER A 204 ? 0.28727 0.34768 0.32152 0.01272  -0.03496 -0.00132 211 SER A OG  
1535 N N   . GLN A 205 ? 0.48099 0.29280 0.25565 -0.01530 -0.02699 -0.05974 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.60405 0.40073 0.36301 0.00889  -0.00227 -0.06571 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.61909 0.38642 0.38580 0.02237  0.00938  -0.06888 212 GLN A C   
1538 O O   . GLN A 205 ? 0.59718 0.37566 0.37979 0.04682  0.02756  -0.06473 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.62082 0.38700 0.31986 0.00733  0.00344  -0.08162 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.84538 0.58993 0.52256 0.03360  0.03240  -0.09308 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.84556 0.56234 0.46430 0.02930  0.03891  -0.11109 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.87989 0.57514 0.47024 0.00568  0.02024  -0.11984 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 1.14683 0.88050 0.76341 0.04964  0.06399  -0.11289 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.53335 0.26759 0.29352 0.00592  -0.00209 -0.07256 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.57399 0.26926 0.33498 0.01779  0.00765  -0.07237 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.55401 0.27689 0.35896 0.01255  0.00135  -0.05325 213 PHE A C   
1547 O O   . PHE A 206 ? 0.52749 0.21493 0.33020 0.01736  0.00544  -0.04849 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.66325 0.28498 0.37633 0.00228  0.00301  -0.09044 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.72513 0.32603 0.39305 0.00326  0.00852  -0.11031 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.76244 0.36814 0.42465 0.03389  0.03197  -0.11527 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.78853 0.37977 0.43007 -0.02749 -0.00974 -0.12024 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.75355 0.35004 0.37906 0.03315  0.03868  -0.13153 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.90754 0.48775 0.51002 -0.02747 -0.00494 -0.13620 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.95089 0.53102 0.54270 0.00260  0.02018  -0.14279 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.41071 0.19188 0.25192 0.00361  -0.00738 -0.04220 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.40151 0.21358 0.27962 0.00081  -0.00911 -0.02672 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.46895 0.27762 0.35454 0.02641  0.00464  -0.01798 214 ILE A C   
1558 O O   . ILE A 207 ? 0.42833 0.24731 0.31425 0.04829  0.01564  -0.02034 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.33934 0.21189 0.25251 -0.00382 -0.01488 -0.02102 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.42963 0.31446 0.34738 -0.02748 -0.03120 -0.02360 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.34545 0.25197 0.29008 -0.00154 -0.01139 -0.00914 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.44180 0.33389 0.37639 -0.04773 -0.03724 -0.01698 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.36846 0.16597 0.26072 0.02299  0.00358  -0.00542 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.38055 0.17096 0.27758 0.04783  0.01269  0.00691  215 GLY A CA  
1565 C C   . GLY A 208 ? 0.37253 0.22541 0.30217 0.05592  0.01317  0.02003  215 GLY A C   
1566 O O   . GLY A 208 ? 0.37732 0.23402 0.31358 0.06805  0.01433  0.03632  215 GLY A O   
1567 N N   . TYR A 209 ? 0.28676 0.18564 0.23432 0.04814  0.01075  0.01359  216 TYR A N   
1568 C CA  . TYR A 209 ? 0.30483 0.25790 0.27852 0.05289  0.01115  0.01996  216 TYR A CA  
1569 C C   . TYR A 209 ? 0.32091 0.29747 0.30383 0.05868  0.01501  0.01066  216 TYR A C   
1570 O O   . TYR A 209 ? 0.30354 0.26381 0.27435 0.05242  0.01430  0.00056  216 TYR A O   
1571 C CB  . TYR A 209 ? 0.22731 0.20921 0.21375 0.03268  0.00526  0.02142  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.26991 0.23405 0.24633 0.02315  0.00339  0.03408  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.26646 0.24345 0.24252 0.03051  0.00366  0.05048  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.31425 0.25003 0.28056 0.00418  -0.00004 0.03228  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.33193 0.28888 0.29457 0.02018  0.00222  0.06670  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.29415 0.21140 0.25068 -0.00898 -0.00077 0.04675  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.30488 0.23044 0.25806 -0.00053 0.00122  0.06486  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.36722 0.27180 0.30688 -0.01466 0.00075  0.08380  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.25812 0.27398 0.26085 0.06777  0.01786  0.01551  217 PRO A N   
1580 C CA  . PRO A 210 ? 0.21259 0.25027 0.22480 0.06849  0.02232  0.00934  217 PRO A CA  
1581 C C   . PRO A 210 ? 0.22276 0.26867 0.24091 0.05027  0.01576  0.00207  217 PRO A C   
1582 O O   . PRO A 210 ? 0.24855 0.31166 0.27841 0.04065  0.01051  0.00154  217 PRO A O   
1583 C CB  . PRO A 210 ? 0.22894 0.31130 0.26511 0.07687  0.02399  0.01807  217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.25876 0.35011 0.29725 0.07399  0.01599  0.02666  217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.27672 0.32029 0.29267 0.07546  0.01566  0.02891  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.23711 0.26953 0.24513 0.04725  0.01670  -0.00311 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.21713 0.25474 0.23311 0.03505  0.00990  -0.00642 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.26186 0.31581 0.28631 0.03459  0.01504  -0.00396 218 ILE A C   
1589 O O   . ILE A 211 ? 0.26801 0.31606 0.27797 0.03939  0.02256  -0.00169 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.27241 0.28392 0.26926 0.02912  0.00275  -0.00928 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.26492 0.26148 0.25585 0.02320  -0.00311 -0.01101 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.21896 0.23834 0.22822 0.02199  -0.00532 -0.00800 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.24803 0.21942 0.21621 0.01387  -0.01232 -0.01481 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.19588 0.26873 0.24115 0.02698  0.01241  -0.00525 219 THR A N   
1595 C CA  . THR A 212 ? 0.14984 0.23498 0.20499 0.02038  0.01603  -0.00218 219 THR A CA  
1596 C C   . THR A 212 ? 0.14900 0.21496 0.20601 0.01256  0.00980  -0.00267 219 THR A C   
1597 O O   . THR A 212 ? 0.18039 0.24262 0.24894 0.01056  0.00420  -0.00976 219 THR A O   
1598 C CB  . THR A 212 ? 0.18631 0.30197 0.26114 0.01441  0.01603  -0.00416 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.16916 0.30602 0.24566 0.02550  0.01962  0.00104  219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.18167 0.30933 0.26821 0.00135  0.01900  -0.00064 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.21860 0.27295 0.26366 0.00986  0.01187  0.00597  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.17688 0.21009 0.22338 0.00411  0.00475  0.01145  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.18876 0.22476 0.24965 -0.00867 0.00879  0.01406  220 LEU A C   
1604 O O   . LEU A 213 ? 0.18897 0.23798 0.24568 -0.01619 0.01753  0.02272  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.18269 0.20039 0.20178 0.00516  0.00269  0.02266  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.23318 0.22892 0.25043 0.00025  -0.00600 0.03588  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.25725 0.24347 0.29869 0.00681  -0.01774 0.03082  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.29807 0.28345 0.27996 0.00013  -0.01054 0.04767  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.18342 0.20801 0.26122 -0.01228 0.00382  0.00515  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.19379 0.21085 0.28261 -0.02859 0.00562  0.00391  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.24342 0.22895 0.32448 -0.03535 0.00407  0.02113  221 PHE A C   
1612 O O   . PHE A 214 ? 0.26612 0.23069 0.33814 -0.02424 -0.00267 0.03037  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.19234 0.19519 0.29416 -0.02891 0.00205  -0.01479 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.18287 0.21799 0.28816 -0.02998 0.00364  -0.03042 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.16900 0.23408 0.26893 -0.02064 0.00514  -0.02662 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.19105 0.22093 0.30064 -0.04042 0.00306  -0.04897 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.16019 0.25265 0.26074 -0.02127 0.00482  -0.03596 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.19294 0.25450 0.29929 -0.04317 0.00283  -0.06140 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.20679 0.30104 0.30953 -0.03319 0.00308  -0.05236 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.24183 0.22574 0.32675 -0.05573 0.00879  0.02783  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.28795 0.23650 0.36415 -0.06639 0.00768  0.04740  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.31927 0.22547 0.40864 -0.07795 0.00297  0.03909  222 VAL A C   
1623 O O   . VAL A 215 ? 0.34786 0.25944 0.44963 -0.08178 0.00253  0.01638  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.43754 0.41186 0.50535 -0.08402 0.01909  0.06513  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.43100 0.42655 0.47538 -0.06835 0.02442  0.07328  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.31567 0.33348 0.40423 -0.09850 0.02571  0.05458  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.36710 0.22610 0.44966 -0.08298 -0.00083 0.05752  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.47008 0.27325 0.56208 -0.09176 -0.00466 0.05029  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.56586 0.34606 0.65313 -0.12558 -0.00090 0.06801  223 GLU A C   
1630 O O   . GLU A 216 ? 0.59780 0.39922 0.67259 -0.13723 0.00454  0.09317  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.50371 0.25867 0.59743 -0.06545 -0.01401 0.05796  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.46694 0.25158 0.56899 -0.03512 -0.01790 0.04549  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.57333 0.32426 0.68458 -0.00847 -0.02855 0.05772  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.52676 0.22665 0.65172 -0.00105 -0.02923 0.05118  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.55754 0.33277 0.66246 0.00525  -0.03690 0.07374  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.62441 0.35910 0.71968 -0.14299 -0.00268 0.05352  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.68916 0.39114 0.78190 -0.18112 -0.00059 0.06828  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.89586 0.55944 0.96951 -0.17789 0.00036  0.10377  224 LYS A C   
1639 O O   . LYS A 217 ? 0.86796 0.49696 0.93431 -0.14785 -0.00701 0.11347  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.78755 0.43702 0.88147 -0.19198 -0.00122 0.03866  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.83607 0.45328 0.92841 -0.22220 0.00627  0.04723  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.87215 0.44791 0.97490 -0.23207 0.00621  0.01243  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.99736 0.50748 1.10071 -0.24679 0.01101  0.02350  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 1.04895 0.58545 1.15383 -0.27375 0.01494  0.05821  224 LYS A NZ  
# 
