data_7HAW
# 
_entry.id   7HAW 
# 
_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   7HAW         pdb_00007haw 10.2210/pdb7haw/pdb 
WWPDB D_1001407243 ?            ?                   
# 
_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                        7HAW 
_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-(2,4-difluorophenyl)-N'-methylthiourea" 202.224   1   ?        ? ? ? 
3 water       nat water                                      18.015    302 ?        ? ? ? 
# 
_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-(2,4-difluorophenyl)-N'-methylthiourea" A1AYD 
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 
A1AYD non-polymer         . "N-(2,4-difluorophenyl)-N'-methylthiourea" ? 'C8 H8 F2 N2 S'  202.224 
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        A1AYD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AYD 
_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 A1AYD 1   301 301 A1AYD A4O A . 
C 3 HOH   1   401 206 HOH   HOH A . 
C 3 HOH   2   402 236 HOH   HOH A . 
C 3 HOH   3   403 264 HOH   HOH A . 
C 3 HOH   4   404 225 HOH   HOH A . 
C 3 HOH   5   405 223 HOH   HOH A . 
C 3 HOH   6   406 128 HOH   HOH A . 
C 3 HOH   7   407 231 HOH   HOH A . 
C 3 HOH   8   408 40  HOH   HOH A . 
C 3 HOH   9   409 218 HOH   HOH A . 
C 3 HOH   10  410 262 HOH   HOH A . 
C 3 HOH   11  411 277 HOH   HOH A . 
C 3 HOH   12  412 256 HOH   HOH A . 
C 3 HOH   13  413 263 HOH   HOH A . 
C 3 HOH   14  414 160 HOH   HOH A . 
C 3 HOH   15  415 88  HOH   HOH A . 
C 3 HOH   16  416 217 HOH   HOH A . 
C 3 HOH   17  417 122 HOH   HOH A . 
C 3 HOH   18  418 118 HOH   HOH A . 
C 3 HOH   19  419 255 HOH   HOH A . 
C 3 HOH   20  420 45  HOH   HOH A . 
C 3 HOH   21  421 199 HOH   HOH A . 
C 3 HOH   22  422 133 HOH   HOH A . 
C 3 HOH   23  423 110 HOH   HOH A . 
C 3 HOH   24  424 259 HOH   HOH A . 
C 3 HOH   25  425 18  HOH   HOH A . 
C 3 HOH   26  426 74  HOH   HOH A . 
C 3 HOH   27  427 171 HOH   HOH A . 
C 3 HOH   28  428 72  HOH   HOH A . 
C 3 HOH   29  429 35  HOH   HOH A . 
C 3 HOH   30  430 63  HOH   HOH A . 
C 3 HOH   31  431 34  HOH   HOH A . 
C 3 HOH   32  432 71  HOH   HOH A . 
C 3 HOH   33  433 89  HOH   HOH A . 
C 3 HOH   34  434 56  HOH   HOH A . 
C 3 HOH   35  435 108 HOH   HOH A . 
C 3 HOH   36  436 120 HOH   HOH A . 
C 3 HOH   37  437 145 HOH   HOH A . 
C 3 HOH   38  438 78  HOH   HOH A . 
C 3 HOH   39  439 91  HOH   HOH A . 
C 3 HOH   40  440 95  HOH   HOH A . 
C 3 HOH   41  441 24  HOH   HOH A . 
C 3 HOH   42  442 148 HOH   HOH A . 
C 3 HOH   43  443 166 HOH   HOH A . 
C 3 HOH   44  444 169 HOH   HOH A . 
C 3 HOH   45  445 23  HOH   HOH A . 
C 3 HOH   46  446 173 HOH   HOH A . 
C 3 HOH   47  447 125 HOH   HOH A . 
C 3 HOH   48  448 121 HOH   HOH A . 
C 3 HOH   49  449 96  HOH   HOH A . 
C 3 HOH   50  450 14  HOH   HOH A . 
C 3 HOH   51  451 196 HOH   HOH A . 
C 3 HOH   52  452 12  HOH   HOH A . 
C 3 HOH   53  453 55  HOH   HOH A . 
C 3 HOH   54  454 43  HOH   HOH A . 
C 3 HOH   55  455 41  HOH   HOH A . 
C 3 HOH   56  456 297 HOH   HOH A . 
C 3 HOH   57  457 106 HOH   HOH A . 
C 3 HOH   58  458 2   HOH   HOH A . 
C 3 HOH   59  459 86  HOH   HOH A . 
C 3 HOH   60  460 52  HOH   HOH A . 
C 3 HOH   61  461 53  HOH   HOH A . 
C 3 HOH   62  462 82  HOH   HOH A . 
C 3 HOH   63  463 67  HOH   HOH A . 
C 3 HOH   64  464 3   HOH   HOH A . 
C 3 HOH   65  465 11  HOH   HOH A . 
C 3 HOH   66  466 188 HOH   HOH A . 
C 3 HOH   67  467 222 HOH   HOH A . 
C 3 HOH   68  468 57  HOH   HOH A . 
C 3 HOH   69  469 295 HOH   HOH A . 
C 3 HOH   70  470 251 HOH   HOH A . 
C 3 HOH   71  471 65  HOH   HOH A . 
C 3 HOH   72  472 19  HOH   HOH A . 
C 3 HOH   73  473 54  HOH   HOH A . 
C 3 HOH   74  474 6   HOH   HOH A . 
C 3 HOH   75  475 123 HOH   HOH A . 
C 3 HOH   76  476 8   HOH   HOH A . 
C 3 HOH   77  477 102 HOH   HOH A . 
C 3 HOH   78  478 61  HOH   HOH A . 
C 3 HOH   79  479 116 HOH   HOH A . 
C 3 HOH   80  480 151 HOH   HOH A . 
C 3 HOH   81  481 28  HOH   HOH A . 
C 3 HOH   82  482 17  HOH   HOH A . 
C 3 HOH   83  483 252 HOH   HOH A . 
C 3 HOH   84  484 66  HOH   HOH A . 
C 3 HOH   85  485 58  HOH   HOH A . 
C 3 HOH   86  486 38  HOH   HOH A . 
C 3 HOH   87  487 153 HOH   HOH A . 
C 3 HOH   88  488 20  HOH   HOH A . 
C 3 HOH   89  489 42  HOH   HOH A . 
C 3 HOH   90  490 300 HOH   HOH A . 
C 3 HOH   91  491 235 HOH   HOH A . 
C 3 HOH   92  492 204 HOH   HOH A . 
C 3 HOH   93  493 212 HOH   HOH A . 
C 3 HOH   94  494 48  HOH   HOH A . 
C 3 HOH   95  495 245 HOH   HOH A . 
C 3 HOH   96  496 94  HOH   HOH A . 
C 3 HOH   97  497 170 HOH   HOH A . 
C 3 HOH   98  498 4   HOH   HOH A . 
C 3 HOH   99  499 90  HOH   HOH A . 
C 3 HOH   100 500 138 HOH   HOH A . 
C 3 HOH   101 501 36  HOH   HOH A . 
C 3 HOH   102 502 112 HOH   HOH A . 
C 3 HOH   103 503 104 HOH   HOH A . 
C 3 HOH   104 504 13  HOH   HOH A . 
C 3 HOH   105 505 31  HOH   HOH A . 
C 3 HOH   106 506 33  HOH   HOH A . 
C 3 HOH   107 507 184 HOH   HOH A . 
C 3 HOH   108 508 284 HOH   HOH A . 
C 3 HOH   109 509 16  HOH   HOH A . 
C 3 HOH   110 510 143 HOH   HOH A . 
C 3 HOH   111 511 103 HOH   HOH A . 
C 3 HOH   112 512 7   HOH   HOH A . 
C 3 HOH   113 513 101 HOH   HOH A . 
C 3 HOH   114 514 85  HOH   HOH A . 
C 3 HOH   115 515 27  HOH   HOH A . 
C 3 HOH   116 516 22  HOH   HOH A . 
C 3 HOH   117 517 220 HOH   HOH A . 
C 3 HOH   118 518 9   HOH   HOH A . 
C 3 HOH   119 519 134 HOH   HOH A . 
C 3 HOH   120 520 59  HOH   HOH A . 
C 3 HOH   121 521 84  HOH   HOH A . 
C 3 HOH   122 522 292 HOH   HOH A . 
C 3 HOH   123 523 203 HOH   HOH A . 
C 3 HOH   124 524 80  HOH   HOH A . 
C 3 HOH   125 525 241 HOH   HOH A . 
C 3 HOH   126 526 76  HOH   HOH A . 
C 3 HOH   127 527 49  HOH   HOH A . 
C 3 HOH   128 528 186 HOH   HOH A . 
C 3 HOH   129 529 165 HOH   HOH A . 
C 3 HOH   130 530 202 HOH   HOH A . 
C 3 HOH   131 531 29  HOH   HOH A . 
C 3 HOH   132 532 114 HOH   HOH A . 
C 3 HOH   133 533 194 HOH   HOH A . 
C 3 HOH   134 534 178 HOH   HOH A . 
C 3 HOH   135 535 25  HOH   HOH A . 
C 3 HOH   136 536 191 HOH   HOH A . 
C 3 HOH   137 537 198 HOH   HOH A . 
C 3 HOH   138 538 21  HOH   HOH A . 
C 3 HOH   139 539 172 HOH   HOH A . 
C 3 HOH   140 540 190 HOH   HOH A . 
C 3 HOH   141 541 81  HOH   HOH A . 
C 3 HOH   142 542 161 HOH   HOH A . 
C 3 HOH   143 543 92  HOH   HOH A . 
C 3 HOH   144 544 129 HOH   HOH A . 
C 3 HOH   145 545 269 HOH   HOH A . 
C 3 HOH   146 546 119 HOH   HOH A . 
C 3 HOH   147 547 237 HOH   HOH A . 
C 3 HOH   148 548 79  HOH   HOH A . 
C 3 HOH   149 549 175 HOH   HOH A . 
C 3 HOH   150 550 239 HOH   HOH A . 
C 3 HOH   151 551 278 HOH   HOH A . 
C 3 HOH   152 552 227 HOH   HOH A . 
C 3 HOH   153 553 273 HOH   HOH A . 
C 3 HOH   154 554 98  HOH   HOH A . 
C 3 HOH   155 555 64  HOH   HOH A . 
C 3 HOH   156 556 50  HOH   HOH A . 
C 3 HOH   157 557 193 HOH   HOH A . 
C 3 HOH   158 558 174 HOH   HOH A . 
C 3 HOH   159 559 254 HOH   HOH A . 
C 3 HOH   160 560 168 HOH   HOH A . 
C 3 HOH   161 561 87  HOH   HOH A . 
C 3 HOH   162 562 5   HOH   HOH A . 
C 3 HOH   163 563 157 HOH   HOH A . 
C 3 HOH   164 564 147 HOH   HOH A . 
C 3 HOH   165 565 250 HOH   HOH A . 
C 3 HOH   166 566 51  HOH   HOH A . 
C 3 HOH   167 567 39  HOH   HOH A . 
C 3 HOH   168 568 301 HOH   HOH A . 
C 3 HOH   169 569 26  HOH   HOH A . 
C 3 HOH   170 570 158 HOH   HOH A . 
C 3 HOH   171 571 15  HOH   HOH A . 
C 3 HOH   172 572 132 HOH   HOH A . 
C 3 HOH   173 573 162 HOH   HOH A . 
C 3 HOH   174 574 291 HOH   HOH A . 
C 3 HOH   175 575 287 HOH   HOH A . 
C 3 HOH   176 576 156 HOH   HOH A . 
C 3 HOH   177 577 293 HOH   HOH A . 
C 3 HOH   178 578 276 HOH   HOH A . 
C 3 HOH   179 579 285 HOH   HOH A . 
C 3 HOH   180 580 46  HOH   HOH A . 
C 3 HOH   181 581 140 HOH   HOH A . 
C 3 HOH   182 582 136 HOH   HOH A . 
C 3 HOH   183 583 32  HOH   HOH A . 
C 3 HOH   184 584 75  HOH   HOH A . 
C 3 HOH   185 585 113 HOH   HOH A . 
C 3 HOH   186 586 111 HOH   HOH A . 
C 3 HOH   187 587 302 HOH   HOH A . 
C 3 HOH   188 588 214 HOH   HOH A . 
C 3 HOH   189 589 130 HOH   HOH A . 
C 3 HOH   190 590 210 HOH   HOH A . 
C 3 HOH   191 591 195 HOH   HOH A . 
C 3 HOH   192 592 298 HOH   HOH A . 
C 3 HOH   193 593 37  HOH   HOH A . 
C 3 HOH   194 594 154 HOH   HOH A . 
C 3 HOH   195 595 142 HOH   HOH A . 
C 3 HOH   196 596 135 HOH   HOH A . 
C 3 HOH   197 597 144 HOH   HOH A . 
C 3 HOH   198 598 100 HOH   HOH A . 
C 3 HOH   199 599 47  HOH   HOH A . 
C 3 HOH   200 600 244 HOH   HOH A . 
C 3 HOH   201 601 228 HOH   HOH A . 
C 3 HOH   202 602 60  HOH   HOH A . 
C 3 HOH   203 603 10  HOH   HOH A . 
C 3 HOH   204 604 69  HOH   HOH A . 
C 3 HOH   205 605 109 HOH   HOH A . 
C 3 HOH   206 606 247 HOH   HOH A . 
C 3 HOH   207 607 1   HOH   HOH A . 
C 3 HOH   208 608 182 HOH   HOH A . 
C 3 HOH   209 609 248 HOH   HOH A . 
C 3 HOH   210 610 267 HOH   HOH A . 
C 3 HOH   211 611 44  HOH   HOH A . 
C 3 HOH   212 612 290 HOH   HOH A . 
C 3 HOH   213 613 30  HOH   HOH A . 
C 3 HOH   214 614 179 HOH   HOH A . 
C 3 HOH   215 615 272 HOH   HOH A . 
C 3 HOH   216 616 215 HOH   HOH A . 
C 3 HOH   217 617 260 HOH   HOH A . 
C 3 HOH   218 618 280 HOH   HOH A . 
C 3 HOH   219 619 281 HOH   HOH A . 
C 3 HOH   220 620 189 HOH   HOH A . 
C 3 HOH   221 621 177 HOH   HOH A . 
C 3 HOH   222 622 124 HOH   HOH A . 
C 3 HOH   223 623 164 HOH   HOH A . 
C 3 HOH   224 624 70  HOH   HOH A . 
C 3 HOH   225 625 270 HOH   HOH A . 
C 3 HOH   226 626 207 HOH   HOH A . 
C 3 HOH   227 627 183 HOH   HOH A . 
C 3 HOH   228 628 105 HOH   HOH A . 
C 3 HOH   229 629 282 HOH   HOH A . 
C 3 HOH   230 630 275 HOH   HOH A . 
C 3 HOH   231 631 201 HOH   HOH A . 
C 3 HOH   232 632 131 HOH   HOH A . 
C 3 HOH   233 633 294 HOH   HOH A . 
C 3 HOH   234 634 62  HOH   HOH A . 
C 3 HOH   235 635 232 HOH   HOH A . 
C 3 HOH   236 636 127 HOH   HOH A . 
C 3 HOH   237 637 208 HOH   HOH A . 
C 3 HOH   238 638 283 HOH   HOH A . 
C 3 HOH   239 639 288 HOH   HOH A . 
C 3 HOH   240 640 115 HOH   HOH A . 
C 3 HOH   241 641 289 HOH   HOH A . 
C 3 HOH   242 642 181 HOH   HOH A . 
C 3 HOH   243 643 213 HOH   HOH A . 
C 3 HOH   244 644 200 HOH   HOH A . 
C 3 HOH   245 645 93  HOH   HOH A . 
C 3 HOH   246 646 279 HOH   HOH A . 
C 3 HOH   247 647 68  HOH   HOH A . 
C 3 HOH   248 648 229 HOH   HOH A . 
C 3 HOH   249 649 216 HOH   HOH A . 
C 3 HOH   250 650 83  HOH   HOH A . 
C 3 HOH   251 651 233 HOH   HOH A . 
C 3 HOH   252 652 205 HOH   HOH A . 
C 3 HOH   253 653 268 HOH   HOH A . 
C 3 HOH   254 654 137 HOH   HOH A . 
C 3 HOH   255 655 163 HOH   HOH A . 
C 3 HOH   256 656 209 HOH   HOH A . 
C 3 HOH   257 657 77  HOH   HOH A . 
C 3 HOH   258 658 240 HOH   HOH A . 
C 3 HOH   259 659 226 HOH   HOH A . 
C 3 HOH   260 660 141 HOH   HOH A . 
C 3 HOH   261 661 192 HOH   HOH A . 
C 3 HOH   262 662 211 HOH   HOH A . 
C 3 HOH   263 663 187 HOH   HOH A . 
C 3 HOH   264 664 149 HOH   HOH A . 
C 3 HOH   265 665 246 HOH   HOH A . 
C 3 HOH   266 666 167 HOH   HOH A . 
C 3 HOH   267 667 230 HOH   HOH A . 
C 3 HOH   268 668 97  HOH   HOH A . 
C 3 HOH   269 669 73  HOH   HOH A . 
C 3 HOH   270 670 238 HOH   HOH A . 
C 3 HOH   271 671 219 HOH   HOH A . 
C 3 HOH   272 672 271 HOH   HOH A . 
C 3 HOH   273 673 261 HOH   HOH A . 
C 3 HOH   274 674 221 HOH   HOH A . 
C 3 HOH   275 675 117 HOH   HOH A . 
C 3 HOH   276 676 257 HOH   HOH A . 
C 3 HOH   277 677 243 HOH   HOH A . 
C 3 HOH   278 678 253 HOH   HOH A . 
C 3 HOH   279 679 234 HOH   HOH A . 
C 3 HOH   280 680 159 HOH   HOH A . 
C 3 HOH   281 681 146 HOH   HOH A . 
C 3 HOH   282 682 249 HOH   HOH A . 
C 3 HOH   283 683 258 HOH   HOH A . 
C 3 HOH   284 684 266 HOH   HOH A . 
C 3 HOH   285 685 274 HOH   HOH A . 
C 3 HOH   286 686 180 HOH   HOH A . 
C 3 HOH   287 687 107 HOH   HOH A . 
C 3 HOH   288 688 242 HOH   HOH A . 
C 3 HOH   289 689 152 HOH   HOH A . 
C 3 HOH   290 690 299 HOH   HOH A . 
C 3 HOH   291 691 126 HOH   HOH A . 
C 3 HOH   292 692 155 HOH   HOH A . 
C 3 HOH   293 693 139 HOH   HOH A . 
C 3 HOH   294 694 197 HOH   HOH A . 
C 3 HOH   295 695 286 HOH   HOH A . 
C 3 HOH   296 696 224 HOH   HOH A . 
C 3 HOH   297 697 99  HOH   HOH A . 
C 3 HOH   298 698 296 HOH   HOH A . 
C 3 HOH   299 699 150 HOH   HOH A . 
C 3 HOH   300 700 176 HOH   HOH A . 
C 3 HOH   301 701 265 HOH   HOH A . 
C 3 HOH   302 702 185 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             588863.711 
_cell.length_a           65.820 
_cell.length_b           89.430 
_cell.length_c           100.040 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HAW 
_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                         7HAW 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HAW 
# 
_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 EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2024-01-21 
_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   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HAW 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             29.510 
_reflns.d_resolution_high            1.650 
_reflns.number_obs                   35867 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.122 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.200 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.700 
_reflns.pdbx_Rrim_I_all              0.127 
_reflns.pdbx_Rpim_I_all              0.035 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     456460 
_reflns.pdbx_scaling_rejects         63 
_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 1.650 1.690  ? 28044 2624 ? 1.843 ? ? ? 10.700 ? 1.500  ? ? ? ? ? ? 100.000 1.937 0.590 0.527 
1 2 7.380 29.510 ? 4467  447  ? 0.040 ? ? ? 10.000 ? 40.200 ? ? ? ? ? ? 98.000  0.042 0.013 0.999 
# 
_refine.entry_id                                 7HAW 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.75 
_refine.pdbx_overall_phase_error                 18.1004 
_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                          0.1660 
_refine.B_iso_mean                               28.62 
_refine.ls_number_reflns_R_free                  1703 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_R_factor_R_work                       0.1650 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.65 
_refine.ls_number_reflns_obs                     35859 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.ls_number_reflns_R_work                  34156 
_refine.ls_d_res_low                             27.49 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1864 
_refine.overall_SU_ML                            0.2100 
_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         13 
_refine_hist.number_atoms_solvent             302 
_refine_hist.number_atoms_total               1959 
_refine_hist.d_res_high                       1.65 
_refine_hist.d_res_low                        27.49 
# 
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           1683 0.0134 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2268 1.2944 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0855 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0090 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 225  5.6829 ? ? ? 
# 
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' 1.65 1.70  2818 0.2976 100.00 0.3340 140 . . . . . 
'X-RAY DIFFRACTION' 1.70 1.75  2766 0.2654 99.93  0.3000 160 . . . . . 
'X-RAY DIFFRACTION' 1.75 1.82  2841 0.2191 99.97  0.2385 140 . . . . . 
'X-RAY DIFFRACTION' 1.82 1.89  2808 0.1873 99.97  0.2113 133 . . . . . 
'X-RAY DIFFRACTION' 1.89 1.97  2840 0.1737 99.93  0.1947 131 . . . . . 
'X-RAY DIFFRACTION' 1.97 2.08  2828 0.1802 100.00 0.1961 126 . . . . . 
'X-RAY DIFFRACTION' 2.08 2.21  2821 0.1510 100.00 0.1686 154 . . . . . 
'X-RAY DIFFRACTION' 2.21 2.38  2823 0.1597 100.00 0.1925 152 . . . . . 
'X-RAY DIFFRACTION' 2.38 2.62  2861 0.1691 100.00 0.2049 118 . . . . . 
'X-RAY DIFFRACTION' 2.62 3.00  2879 0.1724 100.00 0.2072 150 . . . . . 
'X-RAY DIFFRACTION' 3.00 3.77  2869 0.1489 100.00 0.1858 152 . . . . . 
'X-RAY DIFFRACTION' 3.77 27.49 3002 0.1438 99.68  0.1381 147 . . . . . 
# 
_struct.entry_id                  7HAW 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr12961' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HAW 
_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              7HAW 
_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 7HAW MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HAW LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HAW GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HAW HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HAW HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HAW HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HAW HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HAW HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HAW 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  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3  AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4  AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5  AA5 ASN A 99  ? THR A 102 ? ASN A 106 THR A 109 5 ? 4  
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 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_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 VAL A 179 ? O VAL A 186 N ILE A 84  ? N ILE A 91  
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                   7HAW 
_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 609 ? ? O A HOH 659 ? ? 1.86 
2 1 O   A HOH 411 ? ? O A HOH 579 ? ? 1.97 
3 1 O   A HOH 401 ? ? O A HOH 633 ? ? 2.01 
4 1 O   A HOH 502 ? ? O A HOH 667 ? ? 2.07 
5 1 OE2 A GLU 18  ? ? O A HOH 401 ? ? 2.16 
6 1 OE1 A GLU 16  ? ? O A HOH 402 ? ? 2.16 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 643 ? ? 1_555 O A HOH 684 ? ? 2_555 2.05 
2 1 O A HOH 412 ? ? 1_555 O A HOH 633 ? ? 8_444 2.16 
3 1 O A HOH 638 ? ? 1_555 O A HOH 684 ? ? 2_555 2.17 
# 
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  ? ? -160.98 108.07  
2 1 ALA A 166 ? ? 62.80   -145.68 
3 1 ARG A 182 ? ? -171.31 136.95  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     669 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 12.3364498018  -17.833073247  -18.79599441   0.175938133209 0.224039724088 0.224580081984 
0.00442456812095  -0.0279942782464  -0.038707765361   2.45732907694  1.16538506105 5.20668981361 -0.828032608925 -2.9085720845   
0.506761529811  0.143226455413    -0.276113472297  0.00300829607262 0.0217235644544 -0.0334470553655 -0.056890200335  
0.00529471757583 0.289533337291   -0.103437613768  
2  ? 'X-RAY DIFFRACTION' refined -5.21519061375 -6.21860286531 -20.902722707  0.178862070163 0.168735484401 0.207593700276 
-0.0129244835825  -0.00226823741788 -0.0351259848986  1.62074357192  3.75448058005 4.83662151984 -1.37276973869  1.64524459574   
-2.76925032526  -0.0554483031996  0.0850634767703  0.108785266386   0.118162069489  -0.0527079318394 0.054400204186   
-0.404881931299  0.219606039311   0.0625365736284  
3  ? 'X-RAY DIFFRACTION' refined -13.6359510863 -10.7315904842 -27.9641407623 0.182748978538 0.201654824578 0.225004051427 
0.0143621624598   -0.064791209386   -0.0184988455793  1.34927034313  3.92175569337 5.19327255722 -0.833395530491 0.652859580962  
-3.1686649932   0.0942617300311   0.188002480631   -0.0396681095742 -0.241357959986 0.0709382178685  0.406505225084   
-0.14733285019   -0.241687666733  -0.281276529963  
4  ? 'X-RAY DIFFRACTION' refined -6.07773099211 -19.7442483148 -21.828793519  0.193433888303 0.142998546978 0.209142742199 
-0.00213853246622 -0.0248223279051  -0.0296914390123  1.8787813395   2.13657640306 3.57432930573 -0.770201500257 0.0239301418964 
-1.51226382864  0.00201182915929  -0.0412384757043 -0.225029397306  -0.108870129506 0.104814666832   0.186061419323   
0.345519999795   -0.0896356801056 -0.0863628685972 
5  ? 'X-RAY DIFFRACTION' refined 6.89507686299  -11.0593624579 -29.773467114  0.188660255161 0.182199006548 0.247832391405 
0.0109142041645   0.00190953620859  -0.00924822607816 2.82946761791  1.76027049514 5.2013834335  -0.198892924544 1.69337749238   
1.4022554626    -0.0418304689797  0.191886689549   0.218758908581   -0.283951261662 -0.157540760817  -0.0789920305101 
-0.142956854685  0.151977173787   0.0299747894373  
6  ? 'X-RAY DIFFRACTION' refined 15.806392652   -5.51124061013 -14.7834422106 0.220975443901 0.520912273065 0.323482521217 
-0.117125751302   0.0179063716408   -0.109246654095   0.816048671395 4.78796392424 4.13904259055 -0.248023819661 1.42366187487   
0.650611426989  0.441532064735    -0.918280277512  0.722195387468   0.34946806152   -0.113631981842  -0.548129433592  
-0.461789656282  1.70168434376    -0.0570447549386 
7  ? 'X-RAY DIFFRACTION' refined 8.49706963727  -5.85847086798 -10.5129718873 0.243656589169 0.367783520537 0.309723895586 
-0.0961478885294  0.0395260233843   -0.119079335137   3.56754523431  4.24044073247 4.50507803403 0.759588931294  2.10114987594   
0.22880769395   0.330578559058    -1.07992531652   0.717641967912   0.377434345899  -0.254579842248  -0.0444109167366 
-0.728559615691  0.681871402319   -0.202489025241  
8  ? 'X-RAY DIFFRACTION' refined 0.859101786733 -19.2532901909 -27.8555561798 0.154559450965 0.137558818972 0.178241230874 
-0.00676777125428 -0.011930733296   -0.0357199599926  2.66647706212  1.76541591049 2.21566698151 -1.10387179998  0.491747867548  
-0.283942095578 0.153433347839    0.241392709304   -0.275207886101  -0.172811790972 -0.0755321850925 0.161775453364   
0.184506431282   0.0343387259642  -0.108791025164  
9  ? 'X-RAY DIFFRACTION' refined -2.59973574746 -23.6021402468 -13.6865159619 0.167272520497 0.134111272934 0.184192210489 
0.00458094019013  -0.0105963067159  0.00798784172391  2.65465179026  3.34265273011 5.88750993412 -0.269087949707 -0.350616275991 
-1.86082403788  -0.041141192596   -0.222076083709  -0.296029592887  0.0970129920514 -0.0165081666313 -0.0377517320921 
0.441980856078   0.168276061548   0.0106578041592  
10 ? 'X-RAY DIFFRACTION' refined -12.1196555155 -14.1329234721 -10.4634198523 0.137483441853 0.185069092326 0.145203466497 
0.00618435274543  0.0125479347932   -0.018019859362   3.31133039386  2.09814874431 4.28108195503 -0.732628631557 0.664406995658  
-0.881920177387 -0.00293785640176 -0.340611019423  -0.110769771451  0.248524688951  0.0404864181002  0.0937223419988  
-0.150850580834  -0.140303458199  0.0200462804515  
# 
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 65  A 50  . 
;chain 'A' and (resid 41 through 65 )
;
3  3  'X-RAY DIFFRACTION' A 66  A 51  A 83  A 68  . 
;chain 'A' and (resid 66 through 83 )
;
4  4  'X-RAY DIFFRACTION' A 84  A 69  A 99  A 84  . 
;chain 'A' and (resid 84 through 99 )
;
5  5  'X-RAY DIFFRACTION' A 100 A 85  A 110 A 95  . 
;chain 'A' and (resid 100 through 110 )
;
6  6  'X-RAY DIFFRACTION' A 111 A 96  A 123 A 108 . 
;chain 'A' and (resid 111 through 123 )
;
7  7  'X-RAY DIFFRACTION' A 124 A 109 A 136 A 121 . 
;chain 'A' and (resid 124 through 136 )
;
8  8  'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
9  9  'X-RAY DIFFRACTION' A 183 A 168 A 199 A 184 . 
;chain 'A' and (resid 183 through 199 )
;
10 10 'X-RAY DIFFRACTION' A 200 A 185 A 224 A 209 . 
;chain 'A' and (resid 200 through 224 )
;
# 
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 
A1AYD N1   N N N 1   
A1AYD C2   C N N 2   
A1AYD C4   C Y N 3   
A1AYD C5   C Y N 4   
A1AYD C6   C Y N 5   
A1AYD N2   N N N 6   
A1AYD C7   C Y N 7   
A1AYD C1   C N N 8   
A1AYD C3   C Y N 9   
A1AYD C8   C Y N 10  
A1AYD F1   F N N 11  
A1AYD F2   F N N 12  
A1AYD S1   S N N 13  
A1AYD H4   H N N 14  
A1AYD H6   H N N 15  
A1AYD H7   H N N 16  
A1AYD H5   H N N 17  
A1AYD H8   H N N 18  
A1AYD H1   H N N 19  
A1AYD H2   H N N 20  
A1AYD H3   H N N 21  
ALA   N    N N N 22  
ALA   CA   C N S 23  
ALA   C    C N N 24  
ALA   O    O N N 25  
ALA   CB   C N N 26  
ALA   OXT  O N N 27  
ALA   H    H N N 28  
ALA   H2   H N N 29  
ALA   HA   H N N 30  
ALA   HB1  H N N 31  
ALA   HB2  H N N 32  
ALA   HB3  H N N 33  
ALA   HXT  H N N 34  
ARG   N    N N N 35  
ARG   CA   C N S 36  
ARG   C    C N N 37  
ARG   O    O N N 38  
ARG   CB   C N N 39  
ARG   CG   C N N 40  
ARG   CD   C N N 41  
ARG   NE   N N N 42  
ARG   CZ   C N N 43  
ARG   NH1  N N N 44  
ARG   NH2  N N N 45  
ARG   OXT  O N N 46  
ARG   H    H N N 47  
ARG   H2   H N N 48  
ARG   HA   H N N 49  
ARG   HB2  H N N 50  
ARG   HB3  H N N 51  
ARG   HG2  H N N 52  
ARG   HG3  H N N 53  
ARG   HD2  H N N 54  
ARG   HD3  H N N 55  
ARG   HE   H N N 56  
ARG   HH11 H N N 57  
ARG   HH12 H N N 58  
ARG   HH21 H N N 59  
ARG   HH22 H N N 60  
ARG   HXT  H N N 61  
ASN   N    N N N 62  
ASN   CA   C N S 63  
ASN   C    C N N 64  
ASN   O    O N N 65  
ASN   CB   C N N 66  
ASN   CG   C N N 67  
ASN   OD1  O N N 68  
ASN   ND2  N N N 69  
ASN   OXT  O N N 70  
ASN   H    H N N 71  
ASN   H2   H N N 72  
ASN   HA   H N N 73  
ASN   HB2  H N N 74  
ASN   HB3  H N N 75  
ASN   HD21 H N N 76  
ASN   HD22 H N N 77  
ASN   HXT  H N N 78  
ASP   N    N N N 79  
ASP   CA   C N S 80  
ASP   C    C N N 81  
ASP   O    O N N 82  
ASP   CB   C N N 83  
ASP   CG   C N N 84  
ASP   OD1  O N N 85  
ASP   OD2  O N N 86  
ASP   OXT  O N N 87  
ASP   H    H N N 88  
ASP   H2   H N N 89  
ASP   HA   H N N 90  
ASP   HB2  H N N 91  
ASP   HB3  H N N 92  
ASP   HD2  H N N 93  
ASP   HXT  H N N 94  
GLN   N    N N N 95  
GLN   CA   C N S 96  
GLN   C    C N N 97  
GLN   O    O N N 98  
GLN   CB   C N N 99  
GLN   CG   C N N 100 
GLN   CD   C N N 101 
GLN   OE1  O N N 102 
GLN   NE2  N N N 103 
GLN   OXT  O N N 104 
GLN   H    H N N 105 
GLN   H2   H N N 106 
GLN   HA   H N N 107 
GLN   HB2  H N N 108 
GLN   HB3  H N N 109 
GLN   HG2  H N N 110 
GLN   HG3  H N N 111 
GLN   HE21 H N N 112 
GLN   HE22 H N N 113 
GLN   HXT  H N N 114 
GLU   N    N N N 115 
GLU   CA   C N S 116 
GLU   C    C N N 117 
GLU   O    O N N 118 
GLU   CB   C N N 119 
GLU   CG   C N N 120 
GLU   CD   C N N 121 
GLU   OE1  O N N 122 
GLU   OE2  O N N 123 
GLU   OXT  O N N 124 
GLU   H    H N N 125 
GLU   H2   H N N 126 
GLU   HA   H N N 127 
GLU   HB2  H N N 128 
GLU   HB3  H N N 129 
GLU   HG2  H N N 130 
GLU   HG3  H N N 131 
GLU   HE2  H N N 132 
GLU   HXT  H N N 133 
GLY   N    N N N 134 
GLY   CA   C N N 135 
GLY   C    C N N 136 
GLY   O    O N N 137 
GLY   OXT  O N N 138 
GLY   H    H N N 139 
GLY   H2   H N N 140 
GLY   HA2  H N N 141 
GLY   HA3  H N N 142 
GLY   HXT  H N N 143 
HIS   N    N N N 144 
HIS   CA   C N S 145 
HIS   C    C N N 146 
HIS   O    O N N 147 
HIS   CB   C N N 148 
HIS   CG   C Y N 149 
HIS   ND1  N Y N 150 
HIS   CD2  C Y N 151 
HIS   CE1  C Y N 152 
HIS   NE2  N Y N 153 
HIS   OXT  O N N 154 
HIS   H    H N N 155 
HIS   H2   H N N 156 
HIS   HA   H N N 157 
HIS   HB2  H N N 158 
HIS   HB3  H N N 159 
HIS   HD1  H N N 160 
HIS   HD2  H N N 161 
HIS   HE1  H N N 162 
HIS   HE2  H N N 163 
HIS   HXT  H N N 164 
HOH   O    O N N 165 
HOH   H1   H N N 166 
HOH   H2   H N N 167 
ILE   N    N N N 168 
ILE   CA   C N S 169 
ILE   C    C N N 170 
ILE   O    O N N 171 
ILE   CB   C N S 172 
ILE   CG1  C N N 173 
ILE   CG2  C N N 174 
ILE   CD1  C N N 175 
ILE   OXT  O N N 176 
ILE   H    H N N 177 
ILE   H2   H N N 178 
ILE   HA   H N N 179 
ILE   HB   H N N 180 
ILE   HG12 H N N 181 
ILE   HG13 H N N 182 
ILE   HG21 H N N 183 
ILE   HG22 H N N 184 
ILE   HG23 H N N 185 
ILE   HD11 H N N 186 
ILE   HD12 H N N 187 
ILE   HD13 H N N 188 
ILE   HXT  H N N 189 
LEU   N    N N N 190 
LEU   CA   C N S 191 
LEU   C    C N N 192 
LEU   O    O N N 193 
LEU   CB   C N N 194 
LEU   CG   C N N 195 
LEU   CD1  C N N 196 
LEU   CD2  C N N 197 
LEU   OXT  O N N 198 
LEU   H    H N N 199 
LEU   H2   H N N 200 
LEU   HA   H N N 201 
LEU   HB2  H N N 202 
LEU   HB3  H N N 203 
LEU   HG   H N N 204 
LEU   HD11 H N N 205 
LEU   HD12 H N N 206 
LEU   HD13 H N N 207 
LEU   HD21 H N N 208 
LEU   HD22 H N N 209 
LEU   HD23 H N N 210 
LEU   HXT  H N N 211 
LYS   N    N N N 212 
LYS   CA   C N S 213 
LYS   C    C N N 214 
LYS   O    O N N 215 
LYS   CB   C N N 216 
LYS   CG   C N N 217 
LYS   CD   C N N 218 
LYS   CE   C N N 219 
LYS   NZ   N N N 220 
LYS   OXT  O N N 221 
LYS   H    H N N 222 
LYS   H2   H N N 223 
LYS   HA   H N N 224 
LYS   HB2  H N N 225 
LYS   HB3  H N N 226 
LYS   HG2  H N N 227 
LYS   HG3  H N N 228 
LYS   HD2  H N N 229 
LYS   HD3  H N N 230 
LYS   HE2  H N N 231 
LYS   HE3  H N N 232 
LYS   HZ1  H N N 233 
LYS   HZ2  H N N 234 
LYS   HZ3  H N N 235 
LYS   HXT  H N N 236 
MET   N    N N N 237 
MET   CA   C N S 238 
MET   C    C N N 239 
MET   O    O N N 240 
MET   CB   C N N 241 
MET   CG   C N N 242 
MET   SD   S N N 243 
MET   CE   C N N 244 
MET   OXT  O N N 245 
MET   H    H N N 246 
MET   H2   H N N 247 
MET   HA   H N N 248 
MET   HB2  H N N 249 
MET   HB3  H N N 250 
MET   HG2  H N N 251 
MET   HG3  H N N 252 
MET   HE1  H N N 253 
MET   HE2  H N N 254 
MET   HE3  H N N 255 
MET   HXT  H N N 256 
PHE   N    N N N 257 
PHE   CA   C N S 258 
PHE   C    C N N 259 
PHE   O    O N N 260 
PHE   CB   C N N 261 
PHE   CG   C Y N 262 
PHE   CD1  C Y N 263 
PHE   CD2  C Y N 264 
PHE   CE1  C Y N 265 
PHE   CE2  C Y N 266 
PHE   CZ   C Y N 267 
PHE   OXT  O N N 268 
PHE   H    H N N 269 
PHE   H2   H N N 270 
PHE   HA   H N N 271 
PHE   HB2  H N N 272 
PHE   HB3  H N N 273 
PHE   HD1  H N N 274 
PHE   HD2  H N N 275 
PHE   HE1  H N N 276 
PHE   HE2  H N N 277 
PHE   HZ   H N N 278 
PHE   HXT  H N N 279 
PRO   N    N N N 280 
PRO   CA   C N S 281 
PRO   C    C N N 282 
PRO   O    O N N 283 
PRO   CB   C N N 284 
PRO   CG   C N N 285 
PRO   CD   C N N 286 
PRO   OXT  O N N 287 
PRO   H    H N N 288 
PRO   HA   H N N 289 
PRO   HB2  H N N 290 
PRO   HB3  H N N 291 
PRO   HG2  H N N 292 
PRO   HG3  H N N 293 
PRO   HD2  H N N 294 
PRO   HD3  H N N 295 
PRO   HXT  H N N 296 
SER   N    N N N 297 
SER   CA   C N S 298 
SER   C    C N N 299 
SER   O    O N N 300 
SER   CB   C N N 301 
SER   OG   O N N 302 
SER   OXT  O N N 303 
SER   H    H N N 304 
SER   H2   H N N 305 
SER   HA   H N N 306 
SER   HB2  H N N 307 
SER   HB3  H N N 308 
SER   HG   H N N 309 
SER   HXT  H N N 310 
THR   N    N N N 311 
THR   CA   C N S 312 
THR   C    C N N 313 
THR   O    O N N 314 
THR   CB   C N R 315 
THR   OG1  O N N 316 
THR   CG2  C N N 317 
THR   OXT  O N N 318 
THR   H    H N N 319 
THR   H2   H N N 320 
THR   HA   H N N 321 
THR   HB   H N N 322 
THR   HG1  H N N 323 
THR   HG21 H N N 324 
THR   HG22 H N N 325 
THR   HG23 H N N 326 
THR   HXT  H N N 327 
TRP   N    N N N 328 
TRP   CA   C N S 329 
TRP   C    C N N 330 
TRP   O    O N N 331 
TRP   CB   C N N 332 
TRP   CG   C Y N 333 
TRP   CD1  C Y N 334 
TRP   CD2  C Y N 335 
TRP   NE1  N Y N 336 
TRP   CE2  C Y N 337 
TRP   CE3  C Y N 338 
TRP   CZ2  C Y N 339 
TRP   CZ3  C Y N 340 
TRP   CH2  C Y N 341 
TRP   OXT  O N N 342 
TRP   H    H N N 343 
TRP   H2   H N N 344 
TRP   HA   H N N 345 
TRP   HB2  H N N 346 
TRP   HB3  H N N 347 
TRP   HD1  H N N 348 
TRP   HE1  H N N 349 
TRP   HE3  H N N 350 
TRP   HZ2  H N N 351 
TRP   HZ3  H N N 352 
TRP   HH2  H N N 353 
TRP   HXT  H N N 354 
TYR   N    N N N 355 
TYR   CA   C N S 356 
TYR   C    C N N 357 
TYR   O    O N N 358 
TYR   CB   C N N 359 
TYR   CG   C Y N 360 
TYR   CD1  C Y N 361 
TYR   CD2  C Y N 362 
TYR   CE1  C Y N 363 
TYR   CE2  C Y N 364 
TYR   CZ   C Y N 365 
TYR   OH   O N N 366 
TYR   OXT  O N N 367 
TYR   H    H N N 368 
TYR   H2   H N N 369 
TYR   HA   H N N 370 
TYR   HB2  H N N 371 
TYR   HB3  H N N 372 
TYR   HD1  H N N 373 
TYR   HD2  H N N 374 
TYR   HE1  H N N 375 
TYR   HE2  H N N 376 
TYR   HH   H N N 377 
TYR   HXT  H N N 378 
VAL   N    N N N 379 
VAL   CA   C N S 380 
VAL   C    C N N 381 
VAL   O    O N N 382 
VAL   CB   C N N 383 
VAL   CG1  C N N 384 
VAL   CG2  C N N 385 
VAL   OXT  O N N 386 
VAL   H    H N N 387 
VAL   H2   H N N 388 
VAL   HA   H N N 389 
VAL   HB   H N N 390 
VAL   HG11 H N N 391 
VAL   HG12 H N N 392 
VAL   HG13 H N N 393 
VAL   HG21 H N N 394 
VAL   HG22 H N N 395 
VAL   HG23 H N N 396 
VAL   HXT  H N N 397 
# 
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 
A1AYD C1  N1   sing N N 1   
A1AYD N1  C2   sing N N 2   
A1AYD C2  S1   doub N N 3   
A1AYD C2  N2   sing N N 4   
A1AYD N2  C3   sing N N 5   
A1AYD C3  C4   doub Y N 6   
A1AYD C4  C5   sing Y N 7   
A1AYD C5  C6   doub Y N 8   
A1AYD C6  F1   sing N N 9   
A1AYD C6  C7   sing Y N 10  
A1AYD C7  C8   doub Y N 11  
A1AYD C8  F2   sing N N 12  
A1AYD C3  C8   sing Y N 13  
A1AYD N1  H4   sing N N 14  
A1AYD C4  H6   sing N N 15  
A1AYD C5  H7   sing N N 16  
A1AYD N2  H5   sing N N 17  
A1AYD C7  H8   sing N N 18  
A1AYD C1  H1   sing N N 19  
A1AYD C1  H2   sing N N 20  
A1AYD C1  H3   sing N N 21  
ALA   N   CA   sing N N 22  
ALA   N   H    sing N N 23  
ALA   N   H2   sing N N 24  
ALA   CA  C    sing N N 25  
ALA   CA  CB   sing N N 26  
ALA   CA  HA   sing N N 27  
ALA   C   O    doub N N 28  
ALA   C   OXT  sing N N 29  
ALA   CB  HB1  sing N N 30  
ALA   CB  HB2  sing N N 31  
ALA   CB  HB3  sing N N 32  
ALA   OXT HXT  sing N N 33  
ARG   N   CA   sing N N 34  
ARG   N   H    sing N N 35  
ARG   N   H2   sing N N 36  
ARG   CA  C    sing N N 37  
ARG   CA  CB   sing N N 38  
ARG   CA  HA   sing N N 39  
ARG   C   O    doub N N 40  
ARG   C   OXT  sing N N 41  
ARG   CB  CG   sing N N 42  
ARG   CB  HB2  sing N N 43  
ARG   CB  HB3  sing N N 44  
ARG   CG  CD   sing N N 45  
ARG   CG  HG2  sing N N 46  
ARG   CG  HG3  sing N N 47  
ARG   CD  NE   sing N N 48  
ARG   CD  HD2  sing N N 49  
ARG   CD  HD3  sing N N 50  
ARG   NE  CZ   sing N N 51  
ARG   NE  HE   sing N N 52  
ARG   CZ  NH1  sing N N 53  
ARG   CZ  NH2  doub N N 54  
ARG   NH1 HH11 sing N N 55  
ARG   NH1 HH12 sing N N 56  
ARG   NH2 HH21 sing N N 57  
ARG   NH2 HH22 sing N N 58  
ARG   OXT HXT  sing N N 59  
ASN   N   CA   sing N N 60  
ASN   N   H    sing N N 61  
ASN   N   H2   sing N N 62  
ASN   CA  C    sing N N 63  
ASN   CA  CB   sing N N 64  
ASN   CA  HA   sing N N 65  
ASN   C   O    doub N N 66  
ASN   C   OXT  sing N N 67  
ASN   CB  CG   sing N N 68  
ASN   CB  HB2  sing N N 69  
ASN   CB  HB3  sing N N 70  
ASN   CG  OD1  doub N N 71  
ASN   CG  ND2  sing N N 72  
ASN   ND2 HD21 sing N N 73  
ASN   ND2 HD22 sing N N 74  
ASN   OXT HXT  sing N N 75  
ASP   N   CA   sing N N 76  
ASP   N   H    sing N N 77  
ASP   N   H2   sing N N 78  
ASP   CA  C    sing N N 79  
ASP   CA  CB   sing N N 80  
ASP   CA  HA   sing N N 81  
ASP   C   O    doub N N 82  
ASP   C   OXT  sing N N 83  
ASP   CB  CG   sing N N 84  
ASP   CB  HB2  sing N N 85  
ASP   CB  HB3  sing N N 86  
ASP   CG  OD1  doub N N 87  
ASP   CG  OD2  sing N N 88  
ASP   OD2 HD2  sing N N 89  
ASP   OXT HXT  sing N N 90  
GLN   N   CA   sing N N 91  
GLN   N   H    sing N N 92  
GLN   N   H2   sing N N 93  
GLN   CA  C    sing N N 94  
GLN   CA  CB   sing N N 95  
GLN   CA  HA   sing N N 96  
GLN   C   O    doub N N 97  
GLN   C   OXT  sing N N 98  
GLN   CB  CG   sing N N 99  
GLN   CB  HB2  sing N N 100 
GLN   CB  HB3  sing N N 101 
GLN   CG  CD   sing N N 102 
GLN   CG  HG2  sing N N 103 
GLN   CG  HG3  sing N N 104 
GLN   CD  OE1  doub N N 105 
GLN   CD  NE2  sing N N 106 
GLN   NE2 HE21 sing N N 107 
GLN   NE2 HE22 sing N N 108 
GLN   OXT HXT  sing N N 109 
GLU   N   CA   sing N N 110 
GLU   N   H    sing N N 111 
GLU   N   H2   sing N N 112 
GLU   CA  C    sing N N 113 
GLU   CA  CB   sing N N 114 
GLU   CA  HA   sing N N 115 
GLU   C   O    doub N N 116 
GLU   C   OXT  sing N N 117 
GLU   CB  CG   sing N N 118 
GLU   CB  HB2  sing N N 119 
GLU   CB  HB3  sing N N 120 
GLU   CG  CD   sing N N 121 
GLU   CG  HG2  sing N N 122 
GLU   CG  HG3  sing N N 123 
GLU   CD  OE1  doub N N 124 
GLU   CD  OE2  sing N N 125 
GLU   OE2 HE2  sing N N 126 
GLU   OXT HXT  sing N N 127 
GLY   N   CA   sing N N 128 
GLY   N   H    sing N N 129 
GLY   N   H2   sing N N 130 
GLY   CA  C    sing N N 131 
GLY   CA  HA2  sing N N 132 
GLY   CA  HA3  sing N N 133 
GLY   C   O    doub N N 134 
GLY   C   OXT  sing N N 135 
GLY   OXT HXT  sing N N 136 
HIS   N   CA   sing N N 137 
HIS   N   H    sing N N 138 
HIS   N   H2   sing N N 139 
HIS   CA  C    sing N N 140 
HIS   CA  CB   sing N N 141 
HIS   CA  HA   sing N N 142 
HIS   C   O    doub N N 143 
HIS   C   OXT  sing N N 144 
HIS   CB  CG   sing N N 145 
HIS   CB  HB2  sing N N 146 
HIS   CB  HB3  sing N N 147 
HIS   CG  ND1  sing Y N 148 
HIS   CG  CD2  doub Y N 149 
HIS   ND1 CE1  doub Y N 150 
HIS   ND1 HD1  sing N N 151 
HIS   CD2 NE2  sing Y N 152 
HIS   CD2 HD2  sing N N 153 
HIS   CE1 NE2  sing Y N 154 
HIS   CE1 HE1  sing N N 155 
HIS   NE2 HE2  sing N N 156 
HIS   OXT HXT  sing N N 157 
HOH   O   H1   sing N N 158 
HOH   O   H2   sing N N 159 
ILE   N   CA   sing N N 160 
ILE   N   H    sing N N 161 
ILE   N   H2   sing N N 162 
ILE   CA  C    sing N N 163 
ILE   CA  CB   sing N N 164 
ILE   CA  HA   sing N N 165 
ILE   C   O    doub N N 166 
ILE   C   OXT  sing N N 167 
ILE   CB  CG1  sing N N 168 
ILE   CB  CG2  sing N N 169 
ILE   CB  HB   sing N N 170 
ILE   CG1 CD1  sing N N 171 
ILE   CG1 HG12 sing N N 172 
ILE   CG1 HG13 sing N N 173 
ILE   CG2 HG21 sing N N 174 
ILE   CG2 HG22 sing N N 175 
ILE   CG2 HG23 sing N N 176 
ILE   CD1 HD11 sing N N 177 
ILE   CD1 HD12 sing N N 178 
ILE   CD1 HD13 sing N N 179 
ILE   OXT HXT  sing N N 180 
LEU   N   CA   sing N N 181 
LEU   N   H    sing N N 182 
LEU   N   H2   sing N N 183 
LEU   CA  C    sing N N 184 
LEU   CA  CB   sing N N 185 
LEU   CA  HA   sing N N 186 
LEU   C   O    doub N N 187 
LEU   C   OXT  sing N N 188 
LEU   CB  CG   sing N N 189 
LEU   CB  HB2  sing N N 190 
LEU   CB  HB3  sing N N 191 
LEU   CG  CD1  sing N N 192 
LEU   CG  CD2  sing N N 193 
LEU   CG  HG   sing N N 194 
LEU   CD1 HD11 sing N N 195 
LEU   CD1 HD12 sing N N 196 
LEU   CD1 HD13 sing N N 197 
LEU   CD2 HD21 sing N N 198 
LEU   CD2 HD22 sing N N 199 
LEU   CD2 HD23 sing N N 200 
LEU   OXT HXT  sing N N 201 
LYS   N   CA   sing N N 202 
LYS   N   H    sing N N 203 
LYS   N   H2   sing N N 204 
LYS   CA  C    sing N N 205 
LYS   CA  CB   sing N N 206 
LYS   CA  HA   sing N N 207 
LYS   C   O    doub N N 208 
LYS   C   OXT  sing N N 209 
LYS   CB  CG   sing N N 210 
LYS   CB  HB2  sing N N 211 
LYS   CB  HB3  sing N N 212 
LYS   CG  CD   sing N N 213 
LYS   CG  HG2  sing N N 214 
LYS   CG  HG3  sing N N 215 
LYS   CD  CE   sing N N 216 
LYS   CD  HD2  sing N N 217 
LYS   CD  HD3  sing N N 218 
LYS   CE  NZ   sing N N 219 
LYS   CE  HE2  sing N N 220 
LYS   CE  HE3  sing N N 221 
LYS   NZ  HZ1  sing N N 222 
LYS   NZ  HZ2  sing N N 223 
LYS   NZ  HZ3  sing N N 224 
LYS   OXT HXT  sing N N 225 
MET   N   CA   sing N N 226 
MET   N   H    sing N N 227 
MET   N   H2   sing N N 228 
MET   CA  C    sing N N 229 
MET   CA  CB   sing N N 230 
MET   CA  HA   sing N N 231 
MET   C   O    doub N N 232 
MET   C   OXT  sing N N 233 
MET   CB  CG   sing N N 234 
MET   CB  HB2  sing N N 235 
MET   CB  HB3  sing N N 236 
MET   CG  SD   sing N N 237 
MET   CG  HG2  sing N N 238 
MET   CG  HG3  sing N N 239 
MET   SD  CE   sing N N 240 
MET   CE  HE1  sing N N 241 
MET   CE  HE2  sing N N 242 
MET   CE  HE3  sing N N 243 
MET   OXT HXT  sing N N 244 
PHE   N   CA   sing N N 245 
PHE   N   H    sing N N 246 
PHE   N   H2   sing N N 247 
PHE   CA  C    sing N N 248 
PHE   CA  CB   sing N N 249 
PHE   CA  HA   sing N N 250 
PHE   C   O    doub N N 251 
PHE   C   OXT  sing N N 252 
PHE   CB  CG   sing N N 253 
PHE   CB  HB2  sing N N 254 
PHE   CB  HB3  sing N N 255 
PHE   CG  CD1  doub Y N 256 
PHE   CG  CD2  sing Y N 257 
PHE   CD1 CE1  sing Y N 258 
PHE   CD1 HD1  sing N N 259 
PHE   CD2 CE2  doub Y N 260 
PHE   CD2 HD2  sing N N 261 
PHE   CE1 CZ   doub Y N 262 
PHE   CE1 HE1  sing N N 263 
PHE   CE2 CZ   sing Y N 264 
PHE   CE2 HE2  sing N N 265 
PHE   CZ  HZ   sing N N 266 
PHE   OXT HXT  sing N N 267 
PRO   N   CA   sing N N 268 
PRO   N   CD   sing N N 269 
PRO   N   H    sing N N 270 
PRO   CA  C    sing N N 271 
PRO   CA  CB   sing N N 272 
PRO   CA  HA   sing N N 273 
PRO   C   O    doub N N 274 
PRO   C   OXT  sing N N 275 
PRO   CB  CG   sing N N 276 
PRO   CB  HB2  sing N N 277 
PRO   CB  HB3  sing N N 278 
PRO   CG  CD   sing N N 279 
PRO   CG  HG2  sing N N 280 
PRO   CG  HG3  sing N N 281 
PRO   CD  HD2  sing N N 282 
PRO   CD  HD3  sing N N 283 
PRO   OXT HXT  sing N N 284 
SER   N   CA   sing N N 285 
SER   N   H    sing N N 286 
SER   N   H2   sing N N 287 
SER   CA  C    sing N N 288 
SER   CA  CB   sing N N 289 
SER   CA  HA   sing N N 290 
SER   C   O    doub N N 291 
SER   C   OXT  sing N N 292 
SER   CB  OG   sing N N 293 
SER   CB  HB2  sing N N 294 
SER   CB  HB3  sing N N 295 
SER   OG  HG   sing N N 296 
SER   OXT HXT  sing N N 297 
THR   N   CA   sing N N 298 
THR   N   H    sing N N 299 
THR   N   H2   sing N N 300 
THR   CA  C    sing N N 301 
THR   CA  CB   sing N N 302 
THR   CA  HA   sing N N 303 
THR   C   O    doub N N 304 
THR   C   OXT  sing N N 305 
THR   CB  OG1  sing N N 306 
THR   CB  CG2  sing N N 307 
THR   CB  HB   sing N N 308 
THR   OG1 HG1  sing N N 309 
THR   CG2 HG21 sing N N 310 
THR   CG2 HG22 sing N N 311 
THR   CG2 HG23 sing N N 312 
THR   OXT HXT  sing N N 313 
TRP   N   CA   sing N N 314 
TRP   N   H    sing N N 315 
TRP   N   H2   sing N N 316 
TRP   CA  C    sing N N 317 
TRP   CA  CB   sing N N 318 
TRP   CA  HA   sing N N 319 
TRP   C   O    doub N N 320 
TRP   C   OXT  sing N N 321 
TRP   CB  CG   sing N N 322 
TRP   CB  HB2  sing N N 323 
TRP   CB  HB3  sing N N 324 
TRP   CG  CD1  doub Y N 325 
TRP   CG  CD2  sing Y N 326 
TRP   CD1 NE1  sing Y N 327 
TRP   CD1 HD1  sing N N 328 
TRP   CD2 CE2  doub Y N 329 
TRP   CD2 CE3  sing Y N 330 
TRP   NE1 CE2  sing Y N 331 
TRP   NE1 HE1  sing N N 332 
TRP   CE2 CZ2  sing Y N 333 
TRP   CE3 CZ3  doub Y N 334 
TRP   CE3 HE3  sing N N 335 
TRP   CZ2 CH2  doub Y N 336 
TRP   CZ2 HZ2  sing N N 337 
TRP   CZ3 CH2  sing Y N 338 
TRP   CZ3 HZ3  sing N N 339 
TRP   CH2 HH2  sing N N 340 
TRP   OXT HXT  sing N N 341 
TYR   N   CA   sing N N 342 
TYR   N   H    sing N N 343 
TYR   N   H2   sing N N 344 
TYR   CA  C    sing N N 345 
TYR   CA  CB   sing N N 346 
TYR   CA  HA   sing N N 347 
TYR   C   O    doub N N 348 
TYR   C   OXT  sing N N 349 
TYR   CB  CG   sing N N 350 
TYR   CB  HB2  sing N N 351 
TYR   CB  HB3  sing N N 352 
TYR   CG  CD1  doub Y N 353 
TYR   CG  CD2  sing Y N 354 
TYR   CD1 CE1  sing Y N 355 
TYR   CD1 HD1  sing N N 356 
TYR   CD2 CE2  doub Y N 357 
TYR   CD2 HD2  sing N N 358 
TYR   CE1 CZ   doub Y N 359 
TYR   CE1 HE1  sing N N 360 
TYR   CE2 CZ   sing Y N 361 
TYR   CE2 HE2  sing N N 362 
TYR   CZ  OH   sing N N 363 
TYR   OH  HH   sing N N 364 
TYR   OXT HXT  sing N N 365 
VAL   N   CA   sing N N 366 
VAL   N   H    sing N N 367 
VAL   N   H2   sing N N 368 
VAL   CA  C    sing N N 369 
VAL   CA  CB   sing N N 370 
VAL   CA  HA   sing N N 371 
VAL   C   O    doub N N 372 
VAL   C   OXT  sing N N 373 
VAL   CB  CG1  sing N N 374 
VAL   CB  CG2  sing N N 375 
VAL   CB  HB   sing N N 376 
VAL   CG1 HG11 sing N N 377 
VAL   CG1 HG12 sing N N 378 
VAL   CG1 HG13 sing N N 379 
VAL   CG2 HG21 sing N N 380 
VAL   CG2 HG22 sing N N 381 
VAL   CG2 HG23 sing N N 382 
VAL   OXT HXT  sing N N 383 
# 
_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                    7HAW 
_atom_sites.fract_transf_matrix[1][1]   0.015193 
_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]   0.011182 
_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]   0.009996 
_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.
;
? 
F ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 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   ? 4.37532   -28.71614 -38.98791 1.000 47.68313  ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.54285   -27.86738 -39.18392 1.000 54.01509  ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 5.78086   -26.94009 -37.97905 1.000 45.87864  ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 5.07412   -25.94015 -37.79928 1.000 44.16033  ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.37682   -27.03566 -40.45512 1.000 65.92058  ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 6.42463   -25.94358 -40.60088 1.000 72.97222  ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 7.82772   -26.50516 -40.76579 1.000 87.23349  ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 8.78876   -25.84444 -40.30264 1.000 76.95299  ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 7.97004   -27.58528 -41.39195 1.000 86.00156  ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 6.78594   -27.25197 -37.15936 1.000 31.00402  ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 6.98705   -26.57761 -35.88720 1.000 28.83082  ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.34611   -25.90944 -35.93973 1.000 32.43034  ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.33369   -26.56114 -36.28591 1.000 29.89743  ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 6.94766   -27.57231 -34.72014 1.000 30.75275  ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.30799   -26.86513 -33.40769 1.000 32.49633  ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 5.63741   -28.31386 -34.68325 1.000 40.26491  ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.40699   -24.62943 -35.59174 1.000 25.23248  ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.67110   -23.90327 -35.54798 1.000 23.56852  ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 10.11251  -23.76369 -34.09976 1.000 22.09749  ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.31179   -23.38689 -33.25416 1.000 21.87625  ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.53695   -22.52312 -36.17918 1.000 23.41149  ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.37550   -22.60977 -37.71890 1.000 24.94547  ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 9.16741   -21.22839 -38.33197 1.000 34.62800  ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 8.14408   -20.57835 -38.05030 1.000 33.70757  ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 10.03389  -20.78261 -39.11248 1.000 39.88964  ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.38670  -24.04982 -33.82793 1.000 21.30543  ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 11.93841  -23.94614 -32.48622 1.000 20.23367  ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 12.95092  -22.81202 -32.45126 1.000 19.18276  ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 13.83963  -22.74495 -33.29391 1.000 19.27066  ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.61165  -25.25592 -32.06435 1.000 20.71681  ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.67755  -26.33426 -32.18302 1.000 23.04294  ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 13.12508  -25.15900 -30.58742 1.000 20.97313  ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 12.84580  -21.96571 -31.42794 1.000 18.79109  ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.61863  -20.74168 -31.27944 1.000 17.77663  ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.27116  -20.73501 -29.91829 1.000 19.65005  ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.69343  -21.23065 -28.94359 1.000 19.50765  ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.72846  -19.47675 -31.33363 1.000 17.95788  ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 11.98030  -19.30684 -32.60796 1.000 20.24710  ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.75183  -19.93355 -32.81080 1.000 21.58949  ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.49529  -18.46700 -33.60238 1.000 22.23228  ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 10.06938  -19.74812 -34.01737 1.000 24.07380  ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 11.78227  -18.24397 -34.78777 1.000 25.69791  ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.58964  -18.89658 -34.98743 1.000 23.92367  ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.47168  -20.15771 -29.84417 1.000 19.00573  ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 16.10312  -19.86052 -28.55432 1.000 17.03898  ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.58267  -18.54337 -27.98187 1.000 19.95106  ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.48635  -17.53941 -28.69302 1.000 20.09453  ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.61701  -19.77415 -28.70515 1.000 20.16942  ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.24547  -18.52755 -26.68293 1.000 16.76254  ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 15.05124  -17.23779 -26.05013 1.000 16.95747  ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.34483  -16.42764 -26.09836 1.000 17.78997  ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.46136  -16.97082 -25.97312 1.000 20.53576  ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.68977  -17.39578 -24.56475 1.000 18.57591  ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.29606  -17.92371 -24.32731 1.000 16.85237  ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.14633  -17.15986 -24.64493 1.000 17.51741  ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.11208  -19.19913 -23.80873 1.000 17.12628  ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.83958  -17.63314 -24.42060 1.000 17.14684  ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.79788  -19.70106 -23.61769 1.000 17.47605  ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.64771  -18.91756 -23.90524 1.000 17.60393  ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.18662  -15.10373 -26.21871 1.000 18.67775  ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.32380  -14.22584 -25.92492 1.000 21.55353  ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.84601  -14.50868 -24.51797 1.000 20.62081  ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.08130  -14.86700 -23.62411 1.000 21.22965  ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.91306  -12.75736 -26.04052 1.000 22.75595  ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.62581  -12.29115 -27.41687 1.000 27.65570  ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 16.03525  -10.88047 -27.35023 1.000 35.87025  ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.83273  -10.74017 -27.26722 1.000 34.34079  ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.89092  -9.83631  -27.34490 1.000 38.49321  ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.17193  -14.37575 -24.34562 1.000 22.80656  ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.80927  -14.72413 -23.07853 1.000 23.74320  ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.13718  -14.04294 -21.90556 1.000 22.45221  ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 18.91690  -14.66373 -20.85431 1.000 25.96488  ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.28646  -14.34024 -23.11789 1.000 26.06231  ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.76608  -12.77480 -22.06816 1.000 25.34245  ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.19808  -12.04143 -20.93595 1.000 25.60237  ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.81913  -12.57483 -20.54163 1.000 23.27392  ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.45350  -12.57066 -19.35819 1.000 22.50099  ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.11773  -10.55414 -21.27771 1.000 31.06057  ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.46144  -9.87815  -21.56221 1.000 34.96013  ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.02025  -10.08192 -22.97352 1.000 37.55873  ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.41664  -10.79540 -23.80537 1.000 32.87276  ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.10689  -9.51401  -23.25682 1.000 46.49297  ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.04697  -13.04740 -21.51222 1.000 21.00967  ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.73044  -13.59056 -21.21191 1.000 19.52259  ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.87111  -14.96813 -20.57835 1.000 19.40924  ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.12306  -15.32709 -19.65691 1.000 20.15462  ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.86846  -13.62284 -22.48869 1.000 19.27561  ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.35243  -12.20933 -22.81429 1.000 23.08761  ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.58008  -14.54358 -22.32104 1.000 19.13653  ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.41416  -11.16627 -23.19306 1.000 31.23914  ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.84030  -15.76001 -21.04634 1.000 19.26893  ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.09072  -17.03589 -20.39072 1.000 21.87515  ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.46497  -16.80982 -18.93085 1.000 21.84248  ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.01637  -17.55658 -18.04202 1.000 25.21896  ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.20093  -17.81031 -21.11589 1.000 20.98212  ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.24823  -15.75575 -18.66775 1.000 22.34596  ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.63541  -15.43447 -17.29502 1.000 21.19527  ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.43218  -15.00426 -16.47083 1.000 25.00936  ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.30551  -15.41032 -15.31115 1.000 26.13117  ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.69259  -14.32340 -17.25189 1.000 24.17505  ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 19.97985  -14.60926 -18.02887 1.000 52.51149  ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.86427  -13.36809 -18.26839 1.000 65.30839  ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 20.58878  -12.27344 -17.75085 1.000 50.54354  ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 21.89734  -13.52943 -19.11342 1.000 50.31426  ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.55507  -14.16440 -17.04533 1.000 22.38530  ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.30362  -13.79206 -16.35415 1.000 22.06326  ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.47973  -15.02656 -16.00142 1.000 24.21654  ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 12.96753  -15.16383 -14.88238 1.000 22.16237  ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.47138  -12.86485 -17.24575 1.000 24.76318  ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.04251  -12.55320 -16.74685 1.000 25.11335  ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.18424  -11.71921 -15.48572 1.000 25.79536  ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.24105  -11.81649 -17.78088 1.000 26.79325  ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.30207  -15.93545 -16.96468 1.000 20.77687  ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.51336  -17.12839 -16.68116 1.000 21.12187  ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.15951  -18.00602 -15.61518 1.000 21.90870  ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.45058  -18.52066 -14.73645 1.000 21.96796  ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.22125  -17.92975 -17.95209 1.000 18.87126  ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.40620  -17.08975 -18.94774 1.000 17.10525  ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.27122  -17.92155 -20.56994 1.000 20.51221  ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.12183  -19.23476 -20.12937 1.000 21.12755  ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.48552  -18.19267 -15.66297 1.000 22.03395  ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.09111  -19.01043 -14.61416 1.000 21.55598  ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 14.96142  -18.33512 -13.25250 1.000 27.14746  ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.73476  -19.02714 -12.24649 1.000 28.12590  ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.53636  -19.35728 -14.96577 1.000 32.43671  ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.36090  -18.23726 -14.85031 1.000 49.89861  ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.01990  -16.99429 -13.20010 1.000 22.57786  ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.85120  -16.31201 -11.91145 1.000 23.69090  ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.43773  -16.53406 -11.36549 1.000 28.27076  ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.24494  -16.73610 -10.15685 1.000 25.58782  ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.13724  -14.80717 -12.06413 1.000 25.91663  ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 14.86198  -13.87579 -10.84271 1.000 31.93583  ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 15.63005  -12.57550 -11.00709 1.000 42.19568  ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 13.40470  -13.54640 -10.58296 1.000 33.80230  ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.43977  -16.46475 -12.24255 1.000 21.09447  ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.04993  -16.65129 -11.82058 1.000 22.17195  ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.83332  -18.07833 -11.32751 1.000 24.90213  ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.10185  -18.32770 -10.34682 1.000 26.12949  ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.10810  -16.31695 -12.98878 1.000 19.89088  ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.11303  -14.79962 -13.21510 1.000 22.13980  ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.67361   -16.85810 -12.67931 1.000 20.08590  ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.44097   -14.33614 -14.53304 1.000 23.98995  ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.47340  -19.03603 -11.98890 1.000 22.88127  ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.26810  -20.43914 -11.65254 1.000 27.05960  ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.01566  -20.81817 -10.39249 1.000 28.55531  ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.52346  -21.61379 -9.59016  1.000 31.15458  ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.68230  -21.32044 -12.84504 1.000 26.79891  ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.65924  -21.15938 -13.96597 1.000 22.78863  ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.86072  -22.78095 -12.43234 1.000 32.39795  ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.16687  -21.64793 -15.33168 1.000 25.33541  ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.21809  -20.27204 -10.18193 1.000 26.44374  ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.07547  -20.77321 -9.09966  1.000 28.33573  ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.06569  -19.94271 -7.82386  1.000 36.01917  ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.48954  -20.45313 -6.78182  1.000 38.27653  ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.51467  -20.88389 -9.60857  1.000 29.58572  ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.60732  -21.83869 -10.72712 1.000 39.88964  ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 14.91548  -22.85823 -10.71897 1.000 40.46753  ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.35971  -21.48276 -11.75607 1.000 44.69338  ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.61408  -18.69445 -7.86218  1.000 25.89931  ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.64263  -17.87591 -6.65739  1.000 28.05343  ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.56943  -18.32356 -5.68401  1.000 28.87357  ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.41554  -18.51404 -6.07055  1.000 30.78730  ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.44025  -16.40096 -7.00148  1.000 32.24214  ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.46905  -15.99210 -7.90263  1.000 30.81480  ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.52906  -15.54559 -5.74849  1.000 33.57099  ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.93710  -18.47854 -4.41044  1.000 27.51473  ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.88305  -18.75414 -3.44901  1.000 27.49554  ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.03304  -17.49487 -3.22021  1.000 30.05780  ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.55303  -16.45058 -2.80863  1.000 29.34526  ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.48581  -19.26677 -2.14741  1.000 29.83015  ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.45187  -19.52399 -1.10362  1.000 30.14251  ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.62950  -20.63816 -1.17915  1.000 37.44093  ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.29492  -18.65652 -0.02362  1.000 31.18719  ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.64683   -20.88571 -0.20937  1.000 32.66515  ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.31160  -18.89928 0.93499   1.000 33.07489  ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.49229   -20.02213 0.85205   1.000 32.59815  ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.72350   -17.59693 -3.46518  1.000 25.37484  ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.83352   -16.43452 -3.43841  1.000 24.67250  ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.40219   -16.94729 -3.28170  1.000 23.95505  ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.85670   -17.52198 -4.21670  1.000 24.98349  ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 8.99025   -15.61445 -4.73803  1.000 23.58479  ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.05009   -14.43465 -4.76934  1.000 27.14456  ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.32213   -13.33321 -3.97893  1.000 28.72731  ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 6.89383   -14.41667 -5.58613  1.000 31.52906  ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.49849   -12.25005 -3.94057  1.000 35.92573  ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.03704   -13.28421 -5.55224  1.000 30.69455  ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.37743   -12.21539 -4.72543  1.000 32.23968  ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.62884   -11.06609 -4.61367  1.000 44.06921  ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.79483   -16.76173 -2.11163  1.000 24.72688  ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.56391   -17.48823 -1.81832  1.000 24.50985  ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.32947   -16.86513 -2.48314  1.000 23.39146  ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.33852   -17.57670 -2.70268  1.000 25.62608  ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.35703   -17.57047 -0.30963  1.000 25.91316  ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.42382   -18.34178 0.23933   1.000 27.26258  ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.37983   -15.57764 -2.82548  1.000 23.06965  ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.19767   -14.82139 -3.27910  1.000 23.20036  ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 2.94229   -15.05861 -4.77462  1.000 24.03840  ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 2.93024   -14.13838 -5.59524  1.000 22.59428  ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.44048   -13.35143 -2.94971  1.000 26.83908  ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.28917   -12.42756 -3.32480  1.000 28.94235  ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.13108   -12.78291 -3.21969  1.000 30.03836  ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.63218   -11.20240 -3.72571  1.000 29.34793  ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.71588   -16.33236 -5.12132  1.000 20.03054  ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.62103   -16.69809 -6.53413  1.000 18.94255  ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.32861   -16.22872 -7.17978  1.000 19.67511  ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.26209   -16.13828 -8.42432  1.000 18.23845  ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.71901   -18.21626 -6.67198  1.000 20.85447  ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.09446   -18.83154 -6.29892  1.000 20.47693  ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.03178   -20.36184 -6.47754  1.000 24.65970  ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.38841   -21.04937 -6.20625  1.000 23.97939  ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.34408   -20.81187 -7.33926  1.000 21.71190  ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.30143   -15.92971 -6.38715  1.000 19.52855  ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -1.01641  -15.64719 -6.96209  1.000 18.67231  ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -1.00851  -14.44729 -7.88747  1.000 22.75005  ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.95345  -14.28287 -8.67136  1.000 20.13474  ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -2.03797  -15.40159 -5.86040  1.000 21.26280  ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.83032  -14.12521 -5.10217  1.000 21.67097  ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.76432  -13.99385 -3.87229  1.000 30.67463  ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.96473  -14.98886 -3.17252  1.000 33.13794  ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.24914  -12.88598 -3.58448  1.000 36.17883  ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.01866   -13.59551 -7.80636  1.000 19.94391  ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.04324   -12.41176 -8.65184  1.000 18.69085  ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.14041   -12.75519 -10.13158 1.000 19.03690  ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? -0.11949  -11.86642 -10.95457 1.000 18.40674  ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.16289   -11.43538 -8.23165  1.000 22.65540  ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.54273   -12.06367 -8.36225  1.000 24.87202  ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 0.90096   -10.94284 -6.80074  1.000 24.25631  ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.14270   -11.86993 -9.76488  1.000 25.83261  ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.48275   -14.00082 -10.49759 1.000 17.36412  ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.48994   -14.32873 -11.92131 1.000 18.25934  ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.87062  -14.00627 -12.55465 1.000 18.64419  ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.93778  -13.57329 -13.71260 1.000 17.53617  ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.84471   -15.82191 -12.15293 1.000 15.75977  ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.36613  -16.73176 -11.97508 1.000 17.41523  ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.71399  -17.19719 -10.69906 1.000 18.93554  ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.19677  -17.05099 -13.05617 1.000 19.53606  ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.87359  -18.00282 -10.49590 1.000 18.39322  ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.35849  -17.83020 -12.85725 1.000 17.04397  ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.69863  -18.31007 -11.56943 1.000 17.37855  ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.97288  -14.22747 -11.82808 1.000 16.12047  ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.27753  -14.08495 -12.47562 1.000 16.33168  ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.58159  -12.61328 -12.70388 1.000 18.37528  ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.12992  -12.23253 -13.75398 1.000 17.22370  ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.36067  -14.71432 -11.61415 1.000 15.80940  ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.78536  -14.70304 -12.23376 1.000 16.33122  ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.75709  -15.41801 -13.53692 1.000 16.54878  ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.73539  -15.42167 -11.28523 1.000 22.23859  ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.20281  -11.76262 -11.72994 1.000 17.95380  ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.35935  -10.32620 -11.90644 1.000 17.18608  ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.59349  -9.85153  -13.12747 1.000 18.86495  ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -3.09447  -9.02577  -13.91852 1.000 18.03911  ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.86850  -9.60007  -10.65299 1.000 19.65355  ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.73977  -8.11565  -10.82571 1.000 23.41789  ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -2.10448  -7.51212  -9.56975  1.000 24.75736  ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.64535  -7.64530  -9.59805  1.000 30.49519  ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.15704   -7.50096  -8.55160  1.000 33.19444  ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.30637  -7.15633  -7.36247  1.000 31.42331  ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.46441   -7.70009  -8.70374  1.000 33.78337  ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.38178  -10.38377 -13.31268 1.000 17.42600  ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.54551  -9.91599  -14.41316 1.000 15.85455  ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.13555  -10.35036 -15.74111 1.000 17.97868  ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -1.10563  -9.59091  -16.71487 1.000 18.07838  ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.89255   -10.44729 -14.26720 1.000 16.55590  ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.62883   -9.89806  -13.04668 1.000 20.35778  ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.51737   -8.37700  -12.91036 1.000 27.21074  ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.58324   -7.66869  -13.92981 1.000 25.54218  ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.36182   -7.89264  -11.76750 1.000 29.24845  ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.65450  -11.57589 -15.81550 1.000 16.80533  ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.22576  -12.00230 -17.09324 1.000 15.40083  ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.53167  -11.29334 -17.39113 1.000 16.70682  ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.82999  -10.98897 -18.55903 1.000 18.06748  ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.44383  -13.52255 -17.12211 1.000 16.23719  ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.11202  -14.28553 -17.07775 1.000 17.34817  ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.41572  -15.82677 -16.93698 1.000 17.70804  ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.20158  -14.06107 -18.33618 1.000 17.54769  ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.35758  -11.06058 -16.37286 1.000 15.06165  ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.57877  -10.30369 -16.61753 1.000 15.44093  ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.24998  -8.88375  -17.04900 1.000 17.45180  ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.94585  -8.29179  -17.89395 1.000 17.51619  ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.45956  -10.35360 -15.35269 1.000 16.75012  ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -7.00864  -11.78489 -15.23028 1.000 14.93350  ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.59849  -9.28118  -15.40334 1.000 19.18208  ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.80138  -11.97710 -13.88533 1.000 17.17150  ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.19693  -8.30031  -16.46346 1.000 15.51110  ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.83613  -6.94349  -16.85093 1.000 17.24683  ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.37532  -6.92622  -18.30912 1.000 17.46416  ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.74374  -6.02130  -19.07493 1.000 17.92489  ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.75346  -6.41824  -15.88375 1.000 20.37420  ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.25934  -5.18524  -16.36573 1.000 24.77302  ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.61451  -7.95688  -18.72945 1.000 17.01208  ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.20916  -8.04007  -20.12669 1.000 18.40098  ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.42418  -8.16539  -21.03487 1.000 17.87802  ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.46972  -7.56745  -22.12052 1.000 16.64845  ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.30287  -9.25270  -20.34276 1.000 16.64339  ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.08142   -9.03156  -19.81680 1.000 26.56602  ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.41860   -7.96014  -19.29140 1.000 23.31449  ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 0.90112   -10.04430 -19.95196 1.000 25.21460  ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.39365  -8.97567  -20.62821 1.000 14.45175  ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.61575  -9.09788  -21.42928 1.000 16.21324  ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.32938  -7.75598  -21.51862 1.000 18.57459  ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.79352  -7.35932  -22.58894 1.000 16.81242  ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.56123  -10.13543 -20.80573 1.000 17.46196  ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -6.04795  -11.45321 -20.95644 1.000 18.03109  ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.44856  -7.04193  -20.38588 1.000 16.38191  ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.10107  -5.73299  -20.43131 1.000 16.43177  ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.36730  -4.78749  -21.40100 1.000 17.50149  ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -7.00324  -4.07310  -22.19084 1.000 18.51836  ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.16367  -5.14974  -19.00600 1.000 17.86151  ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.72643  -3.82411  -19.02154 1.000 19.79113  ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -5.02771  -4.78567  -21.36860 1.000 16.70007  ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.26021  -3.95355  -22.29330 1.000 16.88941  ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.56406  -4.32099  -23.74211 1.000 18.75679  ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.68360  -3.43410  -24.60403 1.000 18.30574  ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.76291  -4.12948  -22.01944 1.000 17.01310  ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.31677  -3.43153  -20.72222 1.000 24.76770  ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -1.15618  -3.65079  -20.29543 1.000 26.87783  ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -3.11517  -2.66041  -20.10685 1.000 24.78705  ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.68279  -5.61959  -24.03374 1.000 17.34858  ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -4.95650  -6.06656  -25.39984 1.000 18.08478  ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.35969  -5.67064  -25.83471 1.000 17.45124  ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.60195  -5.34960  -27.00369 1.000 16.73202  ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.75434  -7.59440  -25.49035 1.000 15.55575  ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.31555  -5.75152  -24.90920 1.000 15.37369  ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.66761  -5.28928  -25.19443 1.000 16.45643  ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.70543  -3.78113  -25.42432 1.000 17.43289  ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.36932  -3.29981  -26.35177 1.000 18.35052  ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.57011  -5.70997  -24.03986 1.000 16.93015  ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.79660  -7.23278  -24.07230 1.000 17.77182  ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.19329 -7.65714  -22.63128 1.000 18.39215  ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.91679 -7.62370  -25.05123 1.000 16.21542  ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.98324  -3.01236  -24.61553 1.000 16.68084  ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.92126  -1.57115  -24.86266 1.000 17.49733  ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.42070  -1.28048  -26.27277 1.000 20.77692  ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.89495  -0.33999  -26.91645 1.000 18.69205  ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.97560  -0.86911  -23.87842 1.000 18.23823  ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.48437  -0.84879  -22.46028 1.000 24.55459  ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.65043  -1.18847  -22.18630 1.000 24.48244  ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.69599  -0.44978  -21.59683 1.000 22.98045  ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.40688  -2.03692  -26.74382 1.000 17.62407  ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.84782  -1.74897  -28.07358 1.000 18.38154  ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.85989  -1.96957  -29.17906 1.000 18.41596  ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -6.97114  -1.14238  -30.08960 1.000 20.55679  ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.58513  -2.59837  -28.33069 1.000 18.93631  ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.48111  -2.27458  -27.33122 1.000 19.06617  ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.23554  -3.18044  -27.62538 1.000 19.45299  ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.19133  -3.07450  -26.49244 1.000 30.35629  ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? -0.03181  -3.99878  -26.74716 1.000 36.96911  ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.58287  -3.08639  -29.15315 1.000 17.78295  ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.53748  -3.30332  -30.23650 1.000 18.21645  ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.70401  -2.34010  -30.09183 1.000 19.58347  ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.23460 -1.86597  -31.09762 1.000 19.28982  ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -9.00572  -4.77257  -30.33566 1.000 19.28135  ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.79849  -5.03437  -31.64700 1.000 20.78847  ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.83022  -5.18201  -29.12149 1.000 17.46974  ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -9.00369  -4.75440  -32.95734 1.000 22.78536  ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.09288 -1.98872  -28.86541 1.000 18.63600  ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.13224 -0.96704  -28.72885 1.000 19.00403  ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.69547 0.36371   -29.33852 1.000 20.94355  ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.44872 0.98250   -30.09946 1.000 22.28143  ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.51977 -0.77610  -27.26757 1.000 20.88138  ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.70030 0.19590   -27.20034 1.000 29.02035  ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -13.09026 0.54924   -25.80416 1.000 40.94543  ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.21211 -0.24197  -25.30780 1.000 47.91946  ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.21514 -0.83307  -24.12154 1.000 47.23218  ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.19041 -0.70370  -23.28838 1.000 39.13256  ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.28638 -1.53356  -23.74142 1.000 35.94608  ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.45738  0.79800   -29.07348 1.000 19.88261  ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -8.99758  2.06086   -29.64236 1.000 21.03241  ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -9.00660  2.01018   -31.17703 1.000 21.48528  ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.42449  2.97619   -31.84610 1.000 22.82325  ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.59772  2.40505   -29.10808 1.000 21.40460  ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.15454  3.76712   -29.58549 1.000 24.02612  ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.69090  4.93940   -29.04350 1.000 24.10638  ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.25325  3.88183   -30.62070 1.000 24.89897  ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.32332  6.18314   -29.53797 1.000 25.85459  ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.87930  5.11672   -31.11571 1.000 27.50405  ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.41075  6.25675   -30.57348 1.000 28.43575  ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -6.01918  7.47948   -31.06879 1.000 30.38451  ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.49040  0.92086   -31.76033 1.000 21.01869  ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.48840  0.83484   -33.22640 1.000 22.92583  ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -9.90359  0.89933   -33.77262 1.000 25.46782  ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.15482 1.51415   -34.82119 1.000 27.00302  ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.78859  -0.44972  -33.67647 1.000 23.64872  ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.29966  -0.36252  -33.51733 1.000 28.32952  ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.55801  -1.48280  -34.27590 1.000 41.47126  ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -6.23986  -2.32170  -34.91227 1.000 40.03691  ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -4.30205  -1.52305  -34.25057 1.000 41.56894  ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.85150 0.28346   -33.07299 1.000 21.74288  ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.22735 0.25829   -33.56791 1.000 24.34765  ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -12.87847 1.63202   -33.52821 1.000 24.55947  ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -13.90496 1.84824   -34.18376 1.000 25.12202  ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.05378 -0.74302  -32.74242 1.000 24.22178  ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.42039 -0.18305  -31.46884 1.000 26.92332  ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.31421 2.57961   -32.78501 1.000 23.46884  ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -12.97440 3.87239   -32.67299 1.000 28.80170  ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -12.98209 4.59601   -33.99452 1.000 29.93856  ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.85250 5.44074   -34.23962 1.000 32.92397  ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.27377 4.74352   -31.64066 1.000 27.23599  ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.40328 4.18283   -30.23477 1.000 26.16842  ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.74426 5.18308   -29.29713 1.000 30.42892  ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.83663 3.94453   -29.82747 1.000 31.03951  ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -11.98643 4.33715   -34.82503 1.000 27.51127  ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -11.91733 4.99345   -36.12216 1.000 27.66929  ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.16974 4.03372   -37.27735 1.000 37.26835  ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.42910 4.48997   -38.38893 1.000 36.92336  ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.56082 5.69632   -36.30669 1.000 40.10919  ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.49774  4.74537   -36.20510 1.000 38.29690  ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.36722 6.77639   -35.24201 1.000 34.57383  ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.15068 2.72691   -37.03337 1.000 36.11601  ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.37979 1.72712   -38.07608 1.000 33.42063  ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.23023 0.61030   -37.47840 1.000 29.40726  ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.69917 -0.36190  -36.92702 1.000 27.91540  ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -11.04972 1.18901   -38.61372 1.000 32.48613  ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.24062 0.14827   -39.71413 1.000 38.11784  ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.40681 -0.12171  -40.06338 1.000 39.93573  ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.23313 -0.38013  -40.23431 1.000 39.09787  ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.55969 0.72279   -37.54314 1.000 36.37594  ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.40716 -0.30085  -36.90729 1.000 33.55992  ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.17700 -1.69281  -37.47170 1.000 29.67225  ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.47967 -2.67776  -36.78460 1.000 31.49190  ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.83505 0.17018   -37.21661 1.000 38.10491  ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.71511 1.44940   -37.91145 1.000 50.09138  ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.31835 1.92151   -37.91313 1.000 44.53614  ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.68255 -1.80752  -38.71594 1.000 30.53105  ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.46968 -3.12328  -39.29451 1.000 28.44248  ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.42283 -3.91537  -38.53864 1.000 31.63954  ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.33596 -5.13615  -38.72166 1.000 29.16683  ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.06979 -3.02341  -40.77516 1.000 34.13857  ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -12.75365 -2.51812  -40.92627 1.000 36.30233  ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.64654 -3.26659  -37.66307 1.000 24.70729  ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.69193 -4.00101  -36.86320 1.000 22.71374  ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.38688 -5.00033  -35.94213 1.000 26.70123  ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.72855 -5.90577  -35.41215 1.000 24.11741  ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.88290 -3.01356  -36.03048 1.000 27.71303  ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -10.05395 -2.06100  -36.88406 1.000 35.20274  ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.62527  -2.51828  -36.90366 1.000 34.54584  ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.78689  -1.77763  -37.91234 1.000 36.97562  ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.38083  -2.19022  -37.64434 1.000 42.05404  ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.69137 -4.82451  -35.68936 1.000 25.12212  ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.42137 -5.75060  -34.83613 1.000 24.55663  ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.22371 -6.75524  -35.63587 1.000 24.20025  ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -16.03238 -7.49048  -35.04829 1.000 27.79357  ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.34630 -4.99919  -33.85660 1.000 26.52823  ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.59169 -4.07906  -32.87902 1.000 25.29664  ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.57258 -3.32258  -31.96882 1.000 26.17544  ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.62336 -4.90085  -32.02928 1.000 26.72779  ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -14.99655 -6.84570  -36.95079 1.000 24.67973  ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.70669 -7.87237  -37.71554 1.000 30.16132  ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.36625 -9.27313  -37.23830 1.000 29.18168  ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.15828 -10.20054 -37.44325 1.000 29.44577  ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.39455 -7.75133  -39.21546 1.000 30.95984  ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -16.09425 -6.56746  -39.86775 1.000 38.62746  ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -16.93297 -5.91203  -39.19901 1.000 40.03584  ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.80090 -6.29374  -41.05298 1.000 40.07155  ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.19503 -9.45009  -36.63448 1.000 24.37997  ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.73485 -10.71056 -36.08492 1.000 22.83531  ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.27924 -10.96359 -34.69809 1.000 30.20222  ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -13.84254 -11.91197 -34.03776 1.000 31.89455  ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.19383 -10.70332 -36.03515 1.000 27.66097  ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.74011 -9.45955  -35.45721 1.000 24.61268  ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.18120 -10.10092 -34.21664 1.000 27.50489  ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.78282 -10.31437 -32.91869 1.000 31.70252  ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -16.05282 -9.00645  -32.20259 1.000 28.06018  ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.11244 -8.26971  -31.91651 1.000 24.78021  ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.31625 -8.70723  -31.87517 1.000 25.76937  ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.62626 -7.42118  -31.24141 1.000 21.88414  ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.45853 -7.44305  -29.73056 1.000 23.44422  ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.27253 -6.37834  -29.13307 1.000 29.34002  ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -19.07891 -7.00297  -31.54843 1.000 26.86683  ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.36040 -6.74330  -33.02349 1.000 39.92957  ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -19.88604 -5.34046  -33.30262 1.000 58.69216  ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -19.77210 -4.98364  -34.79763 1.000 64.63480  ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -18.86029 -3.81654  -35.12604 1.000 58.11748  ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.53349 -8.61800  -29.10725 1.000 22.35645  ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.53321 -8.71647  -27.65155 1.000 26.96164  ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.11295 -8.55925  -27.11999 1.000 22.19989  ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.19328 -9.18729  -27.62749 1.000 24.67477  ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -18.06248 -10.07749 -27.23222 1.000 29.09879  ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -19.58697 -10.21255 -27.27719 1.000 40.73181  ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -20.06672 -11.47229 -26.53140 1.000 87.62215  ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -20.95875 -11.36025 -25.64737 1.000 81.65829  ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -19.53207 -12.57529 -26.82009 1.000 73.37607  ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -15.95049 -7.77330  -26.06789 1.000 19.49761  ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.63596 -7.50653  -25.47256 1.000 18.72767  ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.68886 -8.03859  -24.05060 1.000 17.97830  ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.34130 -7.42722  -23.18656 1.000 19.21493  ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.36620 -5.99670  -25.50724 1.000 18.57003  ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.29113 -5.38239  -26.92307 1.000 22.98387  ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.78670 -3.95773  -26.78337 1.000 28.18554  ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.33474 -6.16775  -27.81785 1.000 22.56863  ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -14.06166 -9.19162  -23.79791 1.000 18.27880  ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.21743 -9.81063  -22.49073 1.000 17.77882  ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -13.01941 -10.69276 -22.18229 1.000 16.32784  ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.16375 -10.94776 -23.04069 1.000 16.59262  ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.49133 -10.64421 -22.43953 1.000 20.50041  ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.50643 -11.75459 -23.44274 1.000 18.98184  ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.50647 -11.87807 -24.37691 1.000 26.94164  ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.67243 -12.80641 -23.63882 1.000 23.16282  ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.27764 -12.94464 -25.12165 1.000 25.67022  ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.18365 -13.53718 -24.68578 1.000 24.58726  ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -12.99923 -11.18550 -20.93195 1.000 16.54066  ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -11.96123 -12.06041 -20.40319 1.000 14.27009  ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.65409 -13.25455 -19.75302 1.000 18.06045  ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.52521 -13.06240 -18.89968 1.000 16.81926  ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.09330 -11.34557 -19.34089 1.000 15.55391  ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.46291 -10.08407 -19.92199 1.000 14.85864  ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -10.05443 -12.33678 -18.74690 1.000 18.24301  ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.74928  -9.20105  -18.84525 1.000 16.85642  ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.26566 -14.47195 -20.14527 1.000 16.23546  ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.80083 -15.68685 -19.53144 1.000 16.02864  ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.68905 -16.43776 -18.80889 1.000 17.74484  ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.57866 -16.54587 -19.30507 1.000 16.85574  ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.47241 -16.62100 -20.57062 1.000 16.45221  ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.63568 -15.98034 -21.24975 1.000 18.10653  ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.36035 -15.18726 -20.63709 1.000 19.78708  ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.89280 -16.37363 -22.51314 1.000 22.38071  ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -11.99993 -16.97450 -17.62975 1.000 17.17933  ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -11.06972 -17.79926 -16.88227 1.000 14.26156  ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.64542 -19.19888 -16.84947 1.000 17.10637  ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.76783 -19.38798 -16.36004 1.000 17.00029  ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.94156 -17.28171 -15.44265 1.000 16.44732  ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.60008 -15.79795 -15.36388 1.000 16.56081  ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.52011 -15.40390 -13.87494 1.000 16.76689  ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.28099  -15.48660 -16.02075 1.000 17.08676  ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.90890 -20.16664 -17.38247 1.000 15.85754  ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.41516 -21.51816 -17.58043 1.000 16.30087  ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.49378 -22.50232 -16.88263 1.000 16.31543  ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.45599  -22.88744 -17.43107 1.000 18.25498  ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.55698 -21.87604 -19.07240 1.000 17.78176  ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.29109 -20.73662 -19.77146 1.000 19.04650  ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.31082 -23.20592 -19.19557 1.000 17.19358  ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.45579 -20.90876 -21.28350 1.000 19.72298  ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.88102 -23.00050 -15.71212 1.000 19.26939  ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.10818 -24.05401 -15.05747 1.000 19.52999  ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.57113 -25.40611 -15.55256 1.000 20.00795  ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.74663 -25.60703 -15.86870 1.000 21.04762  ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.45075 -23.85384 -13.57103 1.000 18.37708  ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.86858 -23.32790 -13.58323 1.000 22.07339  ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -12.04400 -22.56173 -14.91146 1.000 23.03705  ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.60399  -26.31967 -15.66767 1.000 20.73553  ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.89661  -27.70020 -16.06460 1.000 22.17120  ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -9.08667  -28.62675 -15.16537 1.000 23.02740  ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.87753  -28.78072 -15.35471 1.000 22.88291  ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.56099  -27.93698 -17.53552 1.000 22.87233  ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -10.06925 -29.28548 -18.01253 1.000 27.97168  ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.85999  -30.30889 -17.33856 1.000 29.60464  ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.77221 -29.29833 -19.13560 1.000 35.47639  ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.74344  -29.25291 -14.19682 1.000 25.94058  ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -8.99951  -30.07586 -13.25136 1.000 25.94266  ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.53836  -31.37796 -13.88862 1.000 32.38301  ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.54688  -31.95191 -13.44351 1.000 31.32046  ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.83816  -30.36883 -12.02516 1.000 29.94214  ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -10.03196 -29.14339 -11.14617 1.000 31.29597  ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.84265 -29.53987 -9.91515  1.000 33.77369  ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.07793 -28.35119 -9.01500  1.000 34.65996  ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -12.00374 -27.45956 -9.77237  1.000 41.78616  ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.24263  -31.86767 -14.91367 1.000 34.47677  ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.81825  -33.11671 -15.54907 1.000 36.52354  ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.50540  -32.93881 -16.29604 1.000 35.12619  ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.62701  -33.80501 -16.22333 1.000 39.30852  ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.89756  -33.63719 -16.49575 1.000 43.50558  ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -10.93278 -34.51344 -15.82539 1.000 55.98941  ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -11.76412 -33.74581 -14.80806 1.000 75.46059  ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -11.51654 -33.82325 -13.59902 1.000 73.05334  ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -12.70564 -32.94049 -15.29818 1.000 75.05381  ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.37149  -31.83437 -17.02218 1.000 28.71569  ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.18641  -31.48420 -17.79004 1.000 28.57999  ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.15152  -30.76251 -16.94789 1.000 28.90500  ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -4.02396  -30.60252 -17.40993 1.000 27.75217  ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.55270  -30.58073 -18.97214 1.000 31.68705  ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.48547  -31.26097 -19.97260 1.000 45.05125  ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.78954  -32.46974 -19.79065 1.000 46.41331  ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.97360  -30.55634 -20.89457 1.000 41.25264  ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.52110  -30.36251 -15.73192 1.000 25.71376  ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.69802  -29.53971 -14.83319 1.000 23.03613  ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.22573  -28.26278 -15.53857 1.000 22.29320  ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -3.03653  -27.89441 -15.52199 1.000 21.49781  ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.52149  -30.31765 -14.26241 1.000 24.90432  ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -3.06439  -29.67811 -12.99188 1.000 25.30554  ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.62761  -29.87479 -12.73990 1.000 40.41379  ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -1.39483  -31.19758 -12.22516 1.000 40.17774  ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? -0.26496  -31.87781 -12.36833 1.000 50.38509  ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 0.82082   -31.33289 -12.90888 1.000 35.69002  ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? -0.20822  -33.12011 -11.91711 1.000 45.21158  ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.17618  -27.56727 -16.15194 1.000 20.94798  ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.89266  -26.33000 -16.86116 1.000 19.36675  ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.78470  -25.19659 -16.37320 1.000 18.62545  ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.93251  -25.41642 -16.01011 1.000 19.97990  ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -5.06841  -26.43958 -18.38726 1.000 22.40349  ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.39483  -26.91083 -18.70165 1.000 23.32580  ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -4.02018  -27.40851 -18.97092 1.000 22.34452  ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.23187  -23.98586 -16.35900 1.000 17.50360  ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -6.01739  -22.77160 -16.16193 1.000 16.89630  ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.81885  -21.94282 -17.42119 1.000 18.34223  ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.68189  -21.60663 -17.75767 1.000 17.91285  ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.56393  -21.98715 -14.92133 1.000 19.61562  ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.30638  -20.64526 -14.76939 1.000 16.68469  ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.78948  -20.89152 -14.56185 1.000 18.94641  ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.73239  -19.96527 -13.49971 1.000 19.70071  ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.90072  -21.63475 -18.13154 1.000 16.82729  ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.78610  -20.88877 -19.38625 1.000 15.50335  ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.37983  -19.49841 -19.18656 1.000 18.69923  ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.48376  -19.36319 -18.62555 1.000 17.97596  ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.52638  -21.63565 -20.49571 1.000 17.83215  ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.99136  -22.96276 -20.66459 1.000 21.60245  ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.48266  -20.85114 -21.82921 1.000 19.84581  ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.65770  -18.47147 -19.64920 1.000 15.36364  ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.12658  -17.08041 -19.60145 1.000 16.21499  ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.38741  -16.69095 -21.04972 1.000 17.99616  ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.44551  -16.67102 -21.85712 1.000 18.89222  ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.11485  -16.13305 -18.93280 1.000 17.72809  ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.90452  -16.48297 -17.43421 1.000 23.19253  ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.61312  -14.67663 -19.05154 1.000 18.31847  ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.81085  -17.47436 -17.15419 1.000 26.56377  ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.65896  -16.42779 -21.40658 1.000 15.89873  ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -9.02874  -16.08716 -22.78601 1.000 16.51745  ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.42347  -14.63885 -22.84110 1.000 19.16403  ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.22094 -14.19020 -22.01405 1.000 19.20603  ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.21699 -16.90559 -23.31956 1.000 20.84917  ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.39588 -16.64292 -24.84094 1.000 20.92116  ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -10.03347 -18.38868 -22.96738 1.000 23.42231  ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -8.94356  -13.92229 -23.86107 1.000 16.73592  ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.46223  -12.57266 -24.08632 1.000 16.77470  ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.69249  -12.37445 -25.56015 1.000 19.25151  ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.15145  -13.09804 -26.41376 1.000 19.60345  ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.51029  -11.54056 -23.45822 1.000 17.18924  ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.22059  -11.31362 -24.27663 1.000 20.77790  ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -7.23970  -11.03267 -25.50796 1.000 21.42517  ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -6.13078  -11.65159 -23.70615 1.000 19.34007  ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.53429 -11.40025 -25.85786 1.000 15.64550  ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -10.85151 -11.09322 -27.24946 1.000 15.27613  ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.20086 -9.76731  -27.64185 1.000 19.49371  ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.78658 -8.94102  -28.34218 1.000 17.33566  ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.37791 -11.08101 -27.45861 1.000 18.46922  ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -13.04386 -10.22764 -26.50945 1.000 17.34063  ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -12.97481 -12.52466 -27.28108 1.000 19.24568  ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -8.98163  -9.53303  -27.16212 1.000 17.70825  ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.29124  -8.30342  -27.48727 1.000 18.46104  ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.65492  -8.37845  -28.86513 1.000 15.57315  ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -8.04024  -9.16717  -29.74066 1.000 17.28743  ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.64593  -7.51808  -29.05566 1.000 15.64755  ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.11108  -7.31878  -30.41363 1.000 15.64482  ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.33137  -8.52815  -30.91542 1.000 19.49302  ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.14568  -8.67647  -32.13653 1.000 18.17425  ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.24716  -6.02719  -30.42682 1.000 18.40526  ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -4.95561  -5.57144  -31.87614 1.000 20.76253  ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -3.95923  -6.22483  -29.61112 1.000 19.23605  ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.55977  -4.11343  -31.94966 1.000 25.04190  ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -4.91660  -9.44758  -30.03406 1.000 17.30996  ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.15181  -10.60417 -30.47622 1.000 19.05984  ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.73223  -10.22319 -30.86202 1.000 17.42752  ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.26905  -9.08908  -30.67226 1.000 18.24488  ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -2.00284  -11.23609 -31.33376 1.000 17.00050  ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.61941  -11.03435 -31.74584 1.000 19.51865  ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.35591  -11.69260 -33.08100 1.000 18.00348  ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -0.87339  -12.77314 -33.36879 1.000 19.25424  ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.45164   -11.53650 -30.74554 1.000 20.03471  ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.33414   -10.96013 -29.33117 1.000 19.39307  ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.38252   -11.85504 -28.12208 1.000 20.31902  ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.16988   -13.04445 -27.57940 1.000 21.38520  ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.47730   -11.03354 -33.87879 1.000 18.95373  ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 0.95996   -11.64600 -35.10619 1.000 19.30027  ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 2.07414   -12.64427 -34.80177 1.000 20.62227  ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.57826   -12.72402 -33.68455 1.000 19.22829  ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.51847   -10.59218 -36.04833 1.000 20.75977  ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.68319   -10.02327 -35.43949 1.000 22.84958  ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.48781   -9.49210  -36.32238 1.000 21.61144  ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.41838   -13.46277 -35.80514 1.000 19.27748  ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.53893   -14.38442 -35.63997 1.000 19.00171  ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 4.78827   -13.63393 -35.23699 1.000 21.39133  ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.52603   -14.07248 -34.35519 1.000 20.16926  ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 3.79466   -15.14062 -36.93760 1.000 21.38583  ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 4.85805   -16.25064 -36.74972 1.000 21.46279  ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 5.17890   -16.90384 -38.11566 1.000 26.16360  ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 6.07634   -18.13018 -37.93688 1.000 30.24185  ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 6.77733   -18.51026 -39.21001 1.000 30.81986  ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 5.00993   -12.47244 -35.85251 1.000 21.39224  ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 6.19796   -11.68303 -35.53110 1.000 24.21089  ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 6.15498   -11.21434 -34.08946 1.000 23.45737  ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 7.17724   -11.24863 -33.39116 1.000 22.97595  ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.31236   -10.48371 -36.47472 1.000 23.61745  ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 4.97005   -10.79703 -33.61445 1.000 21.41956  ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.84207   -10.41565 -32.20062 1.000 22.46163  ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 5.17559   -11.58537 -31.29205 1.000 19.37805  ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.85400   -11.42678 -30.26819 1.000 19.87081  ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.41195   -9.95953  -31.85415 1.000 22.37168  ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 3.00886   -8.65176  -32.51497 1.000 29.62550  ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 3.85032   -7.73170  -32.57641 1.000 30.14588  ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 1.78649   -8.49440  -32.81193 1.000 28.67297  ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.62976   -12.76475 -31.59562 1.000 19.31018  ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 4.90280   -13.92425 -30.74121 1.000 20.24188  ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.38750   -14.16906 -30.62418 1.000 22.06746  ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 6.91307   -14.37683 -29.52635 1.000 19.57543  ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.27944   -15.20098 -31.30249 1.000 20.62908  ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.80626   -15.36708 -31.11811 1.000 19.00878  ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.35916   -16.66727 -31.84783 1.000 20.06148  ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.42242   -15.43207 -29.61765 1.000 17.81969  ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 7.08742   -14.15912 -31.76057 1.000 20.09243  ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.51407   -14.45546 -31.71712 1.000 21.81483  ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 9.26241   -13.35855 -30.97799 1.000 22.38352  ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 10.23722  -13.62308 -30.26896 1.000 21.91124  ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 9.04739   -14.64609 -33.14153 1.000 22.21737  ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.43756   -15.90521 -33.72618 1.000 21.95608  ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.59974  -14.67773 -33.15772 1.000 20.83367  ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.56738   -15.97823 -35.28501 1.000 22.02858  ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 8.83858   -12.11117 -31.15285 1.000 18.69848  ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 9.47682   -10.98306 -30.49479 1.000 21.67876  ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 8.94320   -10.84028 -29.06133 1.000 21.13168  ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.35064   -9.83928  -28.66621 1.000 19.69185  ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.22083   -9.72311  -31.30661 1.000 24.04598  ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.21102  -8.63363  -31.00572 1.000 47.18245  ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 11.13450  -8.78153  -30.15528 1.000 40.80178  ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 9.99426   -7.49095  -31.64438 1.000 49.58611  ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 9.11728   -11.90662 -28.29335 1.000 19.98211  ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.75836   -11.93609 -26.87972 1.000 19.88592  ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.30233   -11.54986 -26.60138 1.000 21.80019  ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 7.00667   -10.81716 -25.66309 1.000 18.77578  ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.73193   -11.05769 -26.06535 1.000 19.47304  ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.18426  -11.54395 -26.21507 1.000 17.83872  ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.46927  -12.71722 -26.01299 1.000 20.78555  ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 12.08941  -10.63640 -26.53725 1.000 20.91458  ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.37578   -12.15698 -27.34318 1.000 17.56435  ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 4.93481   -11.95163 -27.11177 1.000 20.09597  ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.57547   -10.46596 -27.05129 1.000 22.42966  ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.80406   -10.01560 -26.19942 1.000 21.15392  ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.46969   -12.68626 -25.85710 1.000 18.93890  ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.89033   -14.16381 -26.06960 1.000 23.94242  ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 6.05373   -14.57449 -25.15244 1.000 22.51304  ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.78894   -15.12056 -26.02416 1.000 26.06209  ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 5.14056   -9.70270  -27.98774 1.000 20.23433  ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.80147   -8.28772  -28.11876 1.000 21.90830  ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.30173   -7.36803  -27.02081 1.000 22.89796  ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.74815   -6.26692  -26.83469 1.000 26.34026  ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.33386   -7.76726  -26.28649 1.000 19.99573  ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.86795   -7.00031  -25.17486 1.000 23.14604  ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.24915   -6.48067  -25.54120 1.000 22.55021  ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.87556   -6.97625  -26.48142 1.000 23.86026  ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 6.97619   -7.85810  -23.90364 1.000 21.34231  ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 8.03609   -8.82555  -24.05338 1.000 22.89622  ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.67331   -8.54567  -23.58949 1.000 24.51552  ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.72802   -5.49333  -24.78159 1.000 19.27992  ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 10.11802  -5.06002  -24.86849 1.000 20.04532  ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.90787  -5.77707  -23.77953 1.000 19.96544  ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.49211  -5.15930  -22.86596 1.000 19.98584  ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.27515  -3.54025  -24.76223 1.000 28.06841  ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.51085   -2.99526  -23.56531 1.000 28.51382  ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.74702   -2.90123  -26.07919 1.000 26.91965  ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 9.69862   -1.47968  -23.41931 1.000 33.27649  ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 10.94547  -7.09999  -23.89097 1.000 20.31284  ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.35192  -7.89638  -22.76234 1.000 18.39026  ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.84314  -7.75113  -22.44674 1.000 20.23410  ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.22770  -7.90112  -21.28357 1.000 21.15906  ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 10.98984  -9.36730  -23.03374 1.000 22.97310  ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.69148  -7.47780  -23.43936 1.000 21.76395  ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.10887  -7.27932  -23.11974 1.000 26.34539  ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.29874  -6.07161  -22.20649 1.000 29.21922  ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 15.90465  -6.18052  -21.13246 1.000 25.67423  ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.94856  -7.15713  -24.39032 1.000 23.84168  ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.44346  -7.14297  -24.11769 1.000 34.21719  ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.26304  -7.02085  -25.41571 1.000 31.26888  ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 19.61208  -6.35551  -25.19501 1.000 50.63551  ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.27532  -6.84575  -23.97008 1.000 58.75559  ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.73876  -4.92352  -22.58228 1.000 24.82817  ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 14.95739  -3.76065  -21.73462 1.000 25.08469  ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.11205  -3.85318  -20.47615 1.000 25.16341  ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.53561  -3.36945  -19.42041 1.000 29.78465  ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.67376  -2.45991  -22.49707 1.000 33.22393  ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.32831  -2.41985  -22.93205 1.000 31.64614  ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 12.91955  -4.45949  -20.55993 1.000 23.25665  ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.10706  -4.65748  -19.35774 1.000 25.47664  ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.78728  -5.53919  -18.32661 1.000 24.36844  ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.76161  -5.24538  -17.12341 1.000 24.25015  ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.44857  -6.61399  -18.77918 1.000 20.98797  ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.18366  -7.45576  -17.83909 1.000 25.71029  ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.32815  -6.69063  -17.20533 1.000 27.26298  ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.53813  -6.78219  -15.99687 1.000 27.69126  ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.69487  -8.70208  -18.56471 1.000 25.62407  ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.55312  -9.41855  -19.05120 1.000 24.52395  ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.49715  -9.56972  -17.67910 1.000 27.00126  ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.07032  -5.92266  -18.00072 1.000 25.17383  ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.15053  -5.11078  -17.44321 1.000 29.00543  ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.62594  -4.18602  -16.33827 1.000 34.10084  ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.22971  -4.06761  -15.26262 1.000 36.55885  ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.81834  -4.31635  -18.55973 1.000 31.95485  ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 18.86791  -3.29403  -18.10506 1.000 44.19026  ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.28465  -2.41597  -19.28066 1.000 47.32887  ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.29551  -1.34827  -18.88362 1.000 56.92724  ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 21.33146  -1.95291  -18.01215 1.000 58.74292  ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.51071  -3.50573  -16.59633 1.000 30.10087  ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 14.96483  -2.59815  -15.58492 1.000 33.37455  ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.50254  -3.36990  -14.34401 1.000 31.98674  ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.73356  -2.93488  -13.20150 1.000 33.12851  ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 13.82045  -1.77813  -16.19472 1.000 31.13727  ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.85600  -4.51986  -14.55430 1.000 28.89263  ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.34009  -5.34359  -13.45005 1.000 25.56619  ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.48470  -5.82395  -12.56783 1.000 31.96146  ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.41301  -5.75539  -11.33974 1.000 31.62182  ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.56312  -6.52261  -14.04386 1.000 23.74846  ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.87381  -7.38963  -13.03886 1.000 24.15637  ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.25737  -6.84765  -11.92340 1.000 24.19959  ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.77220  -8.76317  -13.24479 1.000 25.97866  ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.56471  -7.67070  -11.03204 1.000 27.64540  ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.09312  -9.56960  -12.35677 1.000 29.12789  ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.49868  -9.00157  -11.23419 1.000 25.43141  ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.57374  -6.28770  -13.18457 1.000 32.66804  ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.72191  -6.73531  -12.38995 1.000 33.79736  ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.31042  -5.59737  -11.58484 1.000 39.75359  ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.65980  -5.76128  -10.41176 1.000 42.51363  ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.80994  -7.32893  -13.29185 1.000 35.68733  ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 17.25264  -8.39897  -14.13916 1.000 38.52715  ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 16.80381  -9.79445  -13.10446 1.000 47.07582  ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 17.14760  -11.08552 -14.32855 1.000 46.47594  ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.45897  -4.44308  -12.21628 1.000 39.00396  ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 17.96190  -3.27748  -11.50283 1.000 40.98914  ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.06706  -2.94386  -10.31018 1.000 44.77019  ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.55968  -2.55531  -9.24186  1.000 45.14925  ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.05900  -2.11482  -12.48413 1.000 51.63588  ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 18.87279  -0.92185  -12.02918 1.000 71.41306  ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.03697  0.09654   -13.14575 1.000 85.26002  ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 18.87502  -0.30316  -14.33507 1.000 76.05264  ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 19.29961  1.28564   -12.82378 1.000 81.31372  ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.75061  -3.11910  -10.46591 1.000 41.21024  ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 14.81838  -2.81203  -9.38176  1.000 39.01217  ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 14.90116  -3.84442  -8.26862  1.000 37.96204  ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 14.80264  -3.49434  -7.08106  1.000 44.70799  ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.39450  -2.72588  -9.93125  1.000 34.93798  ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.08687  -5.11855  -8.62942  1.000 37.84644  ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.14834  -6.16988  -7.62166  1.000 37.11689  ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.36853  -5.97830  -6.73929  1.000 49.67659  ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.33161  -6.25653  -5.53713  1.000 47.02110  ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.18842  -7.54259  -8.28699  1.000 36.43953  ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.87704  -8.06983  -8.88144  1.000 36.55892  ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.11941  -9.37832  -9.62500  1.000 35.90226  ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.75648  -8.23197  -7.83739  1.000 31.54079  ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.45910  -5.48894  -7.30423  1.000 52.46359  ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.57307  -5.26297  -6.40556  1.000 56.77754  ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.43245  -3.95835  -5.62198  1.000 56.19720  ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.18675  -3.73919  -4.67070  1.000 62.36863  ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.88638  -5.34065  -7.18582  1.000 59.83639  ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.27175  -6.80392  -7.47753  1.000 64.48332  ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.71718  -7.12387  -7.10060  1.000 92.90026  ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 22.42778  -6.27317  -6.55854  1.000 102.18054 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 22.14606  -8.36393  -7.35609  1.000 91.24284  ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.44874  -3.12316  -5.95738  1.000 55.05115  ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.18277  -1.85749  -5.28591  1.000 55.54538  ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 15.93415  -1.90478  -4.40033  1.000 65.86424  ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.34233  -0.85759  -4.10034  1.000 58.17982  ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 17.05951  -0.74761  -6.32572  1.000 55.59890  ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.51435  -3.10002  -3.99532  1.000 51.21815  ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.49575  -3.27398  -2.98890  1.000 55.27210  ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.25032  -3.97921  -3.46510  1.000 52.27344  ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.52841  -4.54870  -2.63652  1.000 50.37156  ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 12.99590  -3.98420  -4.77480  1.000 40.41614  ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.76330  -4.52718  -5.31530  1.000 41.19152  ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.66055  -6.03912  -5.08382  1.000 41.45541  ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.62757  -6.72796  -4.75375  1.000 41.89803  ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.66965  -4.21806  -6.80785  1.000 39.90229  ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.44728  -6.54889  -5.26673  1.000 43.76207  ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.16364  -7.97416  -5.21562  1.000 37.22031  ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.45956   -8.39699  -6.48787  1.000 31.78432  ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.08601   -7.57277  -7.32993  1.000 31.66383  ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.32821   -8.34371  -3.99142  1.000 40.62083  ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 7.94705   -7.80714  -4.08769  1.000 45.21472  ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.81042   -6.57045  -4.05858  1.000 64.11936  ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 7.01604   -8.59242  -4.30259  1.000 46.44054  ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.30192   -9.71539  -6.63452  1.000 31.83688  ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.81079   -10.26646 -7.89569  1.000 29.48071  ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.42683   -9.75400  -8.21610  1.000 28.15444  ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.05621   -9.65000  -9.39463  1.000 30.57429  ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.89198   -11.80574 -7.84250  1.000 28.15690  ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.38306  -12.17639 -8.01573  1.000 36.38651  ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 7.98426   -12.46852 -8.88132  1.000 29.25165  ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.75705  -13.59904 -7.65369  1.000 39.72948  ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.66174   -9.34562  -7.19634  1.000 29.27192  ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.28917   -8.92219  -7.47387  1.000 32.01085  ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.22785   -7.65911  -8.33413  1.000 31.81221  ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.17849   -7.38675  -8.92896  1.000 33.06033  ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.51307   -8.70215  -6.18137  1.000 30.87947  ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.90879   -7.51184  -5.53458  1.000 37.84259  ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.31403   -6.89005  -8.42297  1.000 26.39512  ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.34819   -5.66717  -9.22301  1.000 25.62096  ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.66224   -5.90808  -10.69154 1.000 25.92842  ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 6.78511   -4.94452  -11.46096 1.000 23.97414  ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.32105   -4.67558  -8.59528  1.000 29.12024  ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 7.01936   -4.62026  -7.07009  1.000 33.85439  ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.18181   -3.71417  -6.09677  1.000 43.36530  ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 8.27153   -2.16003  -7.01701  1.000 43.56233  ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.71847   -7.16919  -11.10880 1.000 22.64420  ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.16442   -7.51929  -12.46586 1.000 23.65852  ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.37619   -6.79182  -13.55675 1.000 21.66730  ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.94110   -6.39801  -14.59057 1.000 20.97442  ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.07098   -9.04544  -12.65073 1.000 22.89458  ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.67344   -9.43133  -14.01581 1.000 22.63639  ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.61938   -9.53634  -12.51227 1.000 21.98035  ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.83869   -10.96162 -14.16011 1.000 24.70014  ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.08083   -6.59658  -13.34426 1.000 25.00980  ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.24303   -5.94947  -14.34923 1.000 24.58801  ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.62827   -4.50982  -14.65087 1.000 28.70630  ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.33460   -4.00518  -15.73779 1.000 29.17296  ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.23177   -3.80955  -13.68753 1.000 24.51488  ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.71165   -2.44849  -13.93225 1.000 26.72219  ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.83403   -2.37393  -14.95150 1.000 29.12978  ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.18983   -1.26420  -15.35787 1.000 30.27432  ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.22140   -1.82075  -12.65097 1.000 29.38071  ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.12278   -1.77474  -11.62819 1.000 35.56559  ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.60348   -1.26299  -10.31431 1.000 41.39499  ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.43759   -0.34115  -10.24607 1.000 46.20652  ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.08173   -1.85359  -9.23748  1.000 41.75639  ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.41758   -3.50375  -15.32768 1.000 25.27016  ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.54558   -3.53959  -16.26015 1.000 24.79827  ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.15494   -4.20034  -17.56825 1.000 24.78434  ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 9.02882   -4.51117  -18.39480 1.000 27.84126  ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.72882   -4.24999  -15.60101 1.000 22.80377  ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.09468  -3.64053  -14.27514 1.000 25.09470  ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 10.81662  -2.46683  -14.22387 1.000 33.12593  ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 9.61645   -4.19442  -13.10025 1.000 26.59089  ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 11.11294  -1.88275  -12.99379 1.000 34.44416  ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 9.89015   -3.62741  -11.87450 1.000 28.22215  ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.64904  -2.47341  -11.81572 1.000 32.99973  ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.85995   -4.42423  -17.76921 1.000 23.48832  ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.38901   -4.84716  -19.06854 1.000 23.39447  ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.60817   -6.29574  -19.40342 1.000 23.22843  ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.39452   -6.67020  -20.56688 1.000 25.32682  ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 6.98511   -7.13354  -18.43024 1.000 19.52095  ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.27028   -8.54658  -18.66690 1.000 16.28546  ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.41762   -9.41280  -17.73554 1.000 19.06874  ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.80591   -10.53245 -17.38385 1.000 18.72044  ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.77286   -8.84738  -18.48895 1.000 19.51428  ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.54419   -8.20935  -19.65556 1.000 21.50362  ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.31645   -8.25768  -17.16697 1.000 20.59556  ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.25412   -8.89706  -17.33730 1.000 19.60969  ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.38410   -9.64552  -16.43703 1.000 18.02307  ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 3.92223   -10.98482 -16.99592 1.000 17.28687  ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.60627   -11.88349 -16.20908 1.000 18.89165  ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 3.91913   -11.15233 -18.32858 1.000 17.68543  ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.54955   -12.44396 -18.90543 1.000 17.50567  ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.35367   -13.57184 -18.27629 1.000 17.03049  ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.80808   -14.63766 -17.97314 1.000 16.46091  ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.76989   -12.47381 -20.42386 1.000 19.26697  ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.72525   -13.86381 -20.98240 1.000 19.97128  ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.51611   -14.51927 -21.12652 1.000 19.69273  ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 4.90017   -14.53730 -21.30078 1.000 16.87195  ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.44744   -15.83369 -21.60407 1.000 16.35412  ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 4.82301   -15.86406 -21.83198 1.000 16.28833  ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.60056   -16.49936 -21.95737 1.000 20.29997  ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.66731   -13.35499 -18.08130 1.000 17.71399  ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.51578   -14.45897 -17.65673 1.000 16.11140  ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.25807   -14.88175 -16.20933 1.000 17.94980  ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.75438   -15.94070 -15.79162 1.000 16.97135  ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.00265   -14.08485 -17.87923 1.000 17.06565  ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.27604   -13.82581 -19.35199 1.000 18.76057  ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.54494   -14.87758 -20.21249 1.000 19.00732  ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.22744   -12.52504 -19.86309 1.000 17.06916  ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.77055   -14.64631 -21.59532 1.000 17.33631  ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.44220   -12.27215 -21.21161 1.000 22.91096  ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.71088   -13.32910 -22.06420 1.000 21.02650  ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 8.93184   -13.08059 -23.40942 1.000 21.24391  ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.48740   -14.10966 -15.44561 1.000 17.12095  ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.06791   -14.59756 -14.13408 1.000 18.02311  ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.20305   -15.83803 -14.22161 1.000 16.23969  ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 3.98753   -16.50196 -13.19531 1.000 17.51995  ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.32015   -13.49851 -13.35542 1.000 19.05274  ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.05042   -13.23883 -13.88809 1.000 18.49606  ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.69907   -16.16821 -15.41398 1.000 15.86218  ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.01375   -17.45468 -15.56736 1.000 16.47620  ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.85844   -18.60668 -15.04413 1.000 17.44641  ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.30795   -19.58881 -14.53015 1.000 17.40837  ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.67950   -17.65773 -17.05964 1.000 14.65991  ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.21400   -18.51027 -15.16681 1.000 16.48291  ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.06322   -19.61841 -14.76122 1.000 17.74846  ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.23399   -19.71314 -13.25009 1.000 20.05519  ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 6.92675   -20.62179 -12.78214 1.000 20.72326  ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.41532   -19.51833 -15.49124 1.000 15.13859  ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.20864   -19.85537 -16.94880 1.000 16.91199  ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.21215   -21.18775 -17.38516 1.000 17.88530  ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 6.92897   -18.85110 -17.86104 1.000 19.01025  ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 6.97179   -21.49455 -18.74775 1.000 18.20261  ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.71148   -19.15252 -19.23249 1.000 18.25180  ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.71800   -20.45080 -19.63046 1.000 20.93426  ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.47526   -20.69526 -20.96743 1.000 17.86793  ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.58213   -18.82368 -12.48486 1.000 19.13042  ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.43241   -19.04568 -11.05001 1.000 18.22088  ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.57971   -20.27332 -10.76024 1.000 20.53605  ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.76979   -20.93931 -9.74400  1.000 21.85870  ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.77683   -17.83298 -10.36755 1.000 19.71802  ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.57457   -16.51213 -10.33614 1.000 18.04638  ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.72155   -15.33361 -9.84297  1.000 20.28658  ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.83744   -16.71569 -9.48337  1.000 20.73035  ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.62829   -20.58886 -11.63725 1.000 20.82376  ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.67922   -21.64445 -11.32029 1.000 17.39271  ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.61190   -22.69141 -12.42972 1.000 18.66113  ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.10320   -23.78191 -12.19231 1.000 21.83189  ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.27830   -21.07913 -11.03733 1.000 18.95764  ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.28665   -20.17789 -9.76274  1.000 20.44151  ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.75138   -20.28221 -12.25978 1.000 21.27322  ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.12983   -22.39996 -13.61642 1.000 19.54754  ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 2.99256   -23.33305 -14.73331 1.000 19.48651  ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.31569   -23.98425 -15.07771 1.000 20.40860  ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.34304   -23.29390 -15.18069 1.000 22.97575  ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.49303   -22.61880 -15.99206 1.000 18.04451  ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.26516   -25.29268 -15.33186 1.000 17.37061  ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.44543   -25.95871 -15.90864 1.000 20.74079  ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.54631   -25.75571 -17.41672 1.000 25.64214  ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.63682   -25.84050 -17.98142 1.000 23.19437  ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.43570   -27.45302 -15.56502 1.000 26.09540  ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.41152   -28.25895 -16.30366 1.000 36.76275  ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.22027   -29.67305 -15.72351 1.000 59.11561  ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 4.60936   -29.91142 -14.55528 1.000 46.11525  ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 3.60112   -30.52285 -16.41772 1.000 50.87602  ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.43334   -25.48555 -18.07845 1.000 20.06509  ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.41925   -25.25536 -19.51259 1.000 20.19873  ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.34169   -24.21517 -19.76812 1.000 17.79915  ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.31801   -24.18812 -19.07986 1.000 17.73634  ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.11914   -26.55633 -20.26845 1.000 20.81867  ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 4.13789   -26.41110 -21.77856 1.000 21.69274  ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 4.05435   -27.79546 -22.37031 1.000 27.81534  ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.66075   -28.14636 -22.76874 1.000 31.98904  ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.55000   -29.61590 -23.11503 1.000 36.94195  ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.56822   -23.36033 -20.74463 1.000 15.79673  ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.57172   -22.35596 -21.11432 1.000 15.75371  ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.39085   -22.45104 -22.61618 1.000 20.21367  ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.38785   -22.45240 -23.34984 1.000 16.29702  ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 3.02004   -20.93840 -20.74317 1.000 16.51315  ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 1.97451   -19.87695 -21.22389 1.000 18.24136  ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.27442   -20.81429 -19.18096 1.000 16.74100  ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 1.13663   -22.50083 -23.05025 1.000 17.74262  ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.75520   -22.46764 -24.46417 1.000 18.25256  ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? -0.00679  -21.16697 -24.72593 1.000 18.36977  ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.93040  -20.83116 -23.98204 1.000 21.39828  ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? -0.10755  -23.68649 -24.82326 1.000 19.21471  ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.54427   -24.90438 -24.45200 1.000 22.42198  ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.34363  -23.73239 -26.33706 1.000 21.37286  ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.34728   -20.43536 -25.77950 1.000 16.05387  ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.36776  -19.19905 -26.11447 1.000 16.54807  ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -0.93071  -19.37029 -27.50642 1.000 19.80120  ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.16243  -19.56942 -28.45549 1.000 18.98437  ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.56384   -17.97928 -26.04410 1.000 16.42428  ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? -0.15941  -16.68657 -26.49884 1.000 18.77473  ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.10876   -17.82769 -24.60351 1.000 18.43532  ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.25188  -19.31579 -27.62725 1.000 16.23860  ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -2.92368  -19.39611 -28.92043 1.000 14.82194  ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.38769  -17.98859 -29.22857 1.000 19.17596  ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -3.99783  -17.34419 -28.36427 1.000 18.60533  ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -4.12909  -20.34945 -28.88405 1.000 18.72901  ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.84999  -21.66621 -28.17872 1.000 28.56539  ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.64107  -20.55271 -30.32431 1.000 21.17961  ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -2.90530  -22.51103 -28.92583 1.000 26.68457  ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -3.14055  -17.49787 -30.44338 1.000 17.65414  ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.46584  -16.09344 -30.67379 1.000 18.90809  ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -3.91279  -15.88541 -32.11158 1.000 21.42841  ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.48994  -16.59325 -33.02000 1.000 20.57625  ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.27216  -15.17702 -30.31550 1.000 19.71139  ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.70192  -13.80237 -30.24566 1.000 19.21209  ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -1.08650  -15.35788 -31.32828 1.000 20.70546  ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.77747  -14.89432 -32.30127 1.000 17.32689  ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.23820  -14.51797 -33.63982 1.000 17.27437  ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.34665  -13.00693 -33.69175 1.000 18.80930  ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -6.13920  -12.41100 -32.94675 1.000 19.99868  ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.58932  -15.15401 -33.93505 1.000 21.11070  ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.24219  -14.72849 -35.27355 1.000 22.63348  ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.43720  -15.20153 -36.50229 1.000 23.02006  ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.17208  -14.86609 -37.80833 1.000 23.26498  ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.14483  -13.41798 -38.15583 1.000 23.70569  ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.56668  -12.40027 -34.57220 1.000 20.00747  ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.58557  -10.97146 -34.82472 1.000 19.93531  ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.28278  -10.74441 -36.16280 1.000 21.70380  ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.19579  -11.58866 -37.05339 1.000 23.34277  ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.13738  -10.43629 -34.82457 1.000 18.63595  ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -3.01241  -8.95042  -34.96814 1.000 20.54533  ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.23511  -8.28736  -36.15666 1.000 23.47130  ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.66533  -8.00091  -34.06662 1.000 19.49651  ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -3.05978  -6.98948  -35.97756 1.000 25.46516  ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.68407  -6.79097  -34.72561 1.000 22.64007  ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -5.99928  -9.61322  -36.30390 1.000 20.43716  ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.70768  -9.37952  -37.57209 1.000 19.75325  ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.77684  -9.47382  -38.78740 1.000 23.13049  ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.23881  -9.78967  -39.89274 1.000 26.12133  ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.39770  -7.99568  -37.57982 1.000 21.60613  ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.65041  -7.96830  -36.78360 1.000 27.33048  ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.31132  -8.99501  -36.61813 1.000 26.45270  ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -9.01446  -6.77245  -36.26947 1.000 24.63533  ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.49070  -9.14982  -38.63150 1.000 24.92644  ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.58383  -9.07653  -39.77177 1.000 27.23104  ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.76870  -10.34566 -39.98797 1.000 29.87872  ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -1.84575  -10.32606 -40.81494 1.000 29.81239  ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.62229  -7.88724  -39.62455 1.000 30.89414  ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.32461  -6.54077  -39.65002 1.000 31.57386  ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.48066  -6.46727  -40.10957 1.000 31.97066  ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.70960  -5.56454  -39.18228 1.000 37.93652  ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -3.06527  -11.44001 -39.28476 1.000 25.24828  ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.27782  -12.66430 -39.46634 1.000 21.52780  ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.17229  -13.88906 -39.23419 1.000 27.12720  ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.36264  -13.76724 -38.92947 1.000 24.46902  ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -1.06526  -12.66161 -38.51931 1.000 24.57588  ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 0.11256   -13.46477 -39.05519 1.000 26.24044  ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? -0.03808  -14.18997 -40.07974 1.000 26.66497  ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.19626   -13.33002 -38.45785 1.000 28.09966  ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.57976  -15.08168 -39.35246 1.000 26.86870  ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.28389  -16.33617 -39.11914 1.000 23.10517  ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.17304  -16.72621 -37.65283 1.000 19.38880  ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.50032  -16.07738 -36.86815 1.000 23.59476  ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -2.72011  -17.45782 -39.97598 1.000 26.25692  ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -2.73153  -17.11075 -41.44040 1.000 39.48908  ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -4.14165  -16.92969 -41.96232 1.000 68.48080  ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -4.95333  -17.86704 -41.80039 1.000 88.26243  ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -4.43992  -15.84643 -42.52414 1.000 68.25626  ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -3.89843  -17.77468 -37.27656 1.000 22.85857  ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -3.88585  -18.22588 -35.88619 1.000 21.11471  ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.63502  -19.06411 -35.61624 1.000 19.94068  ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.35575  -20.02289 -36.34484 1.000 23.22530  ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -5.13985  -19.04440 -35.58300 1.000 22.14020  ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.33699  -19.37994 -34.08722 1.000 21.69134  ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.76418  -19.79795 -33.82389 1.000 29.67685  ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.69081  -19.08433 -34.19962 1.000 30.81821  ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -6.95745  -20.96900 -33.21126 1.000 27.01971  ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -1.89850  -18.71089 -34.55596 1.000 18.64462  ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.64850  -19.37124 -34.20621 1.000 19.76768  ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.70799  -19.87258 -32.76502 1.000 20.55739  ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.42552  -19.31592 -31.92143 1.000 19.24149  ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.53180   -18.41100 -34.35897 1.000 19.05711  ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 0.92107   -18.23065 -35.79702 1.000 22.09544  ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 1.74660   -19.15659 -36.40407 1.000 22.33470  ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 0.44826   -17.16760 -36.55381 1.000 26.22963  ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 2.10496   -19.03813 -37.70995 1.000 28.00088  ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 0.80611   -17.05589 -37.89376 1.000 27.76988  ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.64235   -17.99681 -38.44817 1.000 31.35783  ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 2.04812   -17.94932 -39.76884 1.000 37.16363  ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 0.08124   -20.91491 -32.48866 1.000 19.44726  ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.32986   -21.41048 -31.13080 1.000 17.93703  ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 1.80715   -21.27077 -30.78571 1.000 19.29699  ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.66966   -21.80281 -31.49284 1.000 20.08834  ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? -0.08643  -22.87772 -31.01067 1.000 22.19628  ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 2.08501   -20.55750 -29.70589 1.000 16.15415  ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.41172   -20.47921 -29.09802 1.000 15.41841  ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.43120   -21.40844 -27.89941 1.000 19.18066  ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.41275   -21.57236 -27.21566 1.000 18.10293  ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.61013   -19.02842 -28.63758 1.000 17.76074  ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 4.86480   -18.65110 -27.87823 1.000 17.44989  ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 5.95027   -17.94481 -28.38886 1.000 15.30214  ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 5.12151   -18.82665 -26.46706 1.000 16.59577  ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 6.85498   -17.70761 -27.37194 1.000 16.08068  ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.36893   -18.23216 -26.19440 1.000 17.26523  ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.41323   -19.43983 -25.41545 1.000 15.64297  ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 6.94838   -18.25342 -24.91883 1.000 17.70580  ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 4.98411   -19.46063 -24.16241 1.000 16.77790  ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.24347   -18.84521 -23.92167 1.000 16.22655  ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.58819   -21.99963 -27.61235 1.000 15.66007  ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.64513   -22.85243 -26.42716 1.000 14.85405  ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 6.04641   -22.91356 -25.83545 1.000 14.53761  ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 7.03614   -22.90888 -26.57875 1.000 16.75642  ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.17755   -24.26478 -26.79215 1.000 21.12897  ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 3.92784   -25.17406 -25.59669 1.000 25.86141  ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 3.25485   -26.46613 -26.02435 1.000 43.51844  ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 3.96692   -27.38659 -26.49701 1.000 37.11727  ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 2.00570   -26.56244 -25.84268 1.000 33.54803  ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.12931   -22.98344 -24.50255 1.000 17.30475  ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.44459   -23.12429 -23.89583 1.000 15.67189  ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.31066   -23.79270 -22.53084 1.000 15.22682  ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.39860   -23.45769 -21.74400 1.000 17.98206  ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.17805   -21.79056 -23.75069 1.000 17.12614  ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.47740   -22.04284 -23.17546 1.000 17.46470  ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.21793   -24.73347 -22.26777 1.000 17.30045  ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.41576   -25.26247 -20.91166 1.000 17.29475  ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.67876   -24.68472 -20.29334 1.000 22.33059  ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.31505  -25.32300 -19.43404 1.000 23.59314  ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.49287   -26.79060 -20.91616 1.000 22.80785  ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.26769   -27.34280 -21.41230 1.000 23.97927  ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.04832  -23.48179 -20.71369 1.000 19.01901  ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.27460  -22.78231 -20.28649 1.000 20.55611  ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.46381  -23.63605 -20.75095 1.000 23.81996  ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.41661  -24.23529 -21.83147 1.000 25.74594  ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.20783  -22.45494 -18.79311 1.000 23.16736  ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.56982  -23.69341 -20.00901 1.000 26.36777  ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.70657  -24.42659 -20.55431 1.000 28.38624  ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.34765  -23.85218 -21.80950 1.000 26.31971  ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 16.12930  -24.53534 -22.48370 1.000 26.24072  ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 15.06271  -22.61342 -22.13626 1.000 21.14864  ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.85264  -21.89031 -23.10252 1.000 19.16656  ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.23460  -21.80637 -24.47815 1.000 19.61214  ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.81261  -21.15627 -25.35481 1.000 20.24920  ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 14.09587  -22.45089 -24.70336 1.000 18.35039  ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.54808  -22.46399 -26.05610 1.000 16.59676  ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 12.02918  -22.36741 -26.01866 1.000 17.18265  ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.38115  -22.64449 -24.99474 1.000 20.00166  ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 13.95801  -23.72059 -26.83329 1.000 21.62929  ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.35828  -24.87362 -26.27425 1.000 23.25784  ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.48149  -21.96433 -27.17271 1.000 18.04292  ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 10.03080  -21.92167 -27.37748 1.000 17.44433  ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.72456   -22.38852 -28.80001 1.000 16.73065  ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.60587  -22.42896 -29.66578 1.000 20.05094  ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.43768   -20.50929 -27.13346 1.000 16.19909  ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 9.93219   -19.43847 -28.06425 1.000 15.03059  ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 11.08771  -18.72267 -27.74808 1.000 18.24501  ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 9.22055   -19.11067 -29.21611 1.000 15.85954  ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 11.53795  -17.68153 -28.59069 1.000 20.79753  ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 9.63903   -18.13147 -30.05165 1.000 17.25141  ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.80942  -17.37193 -29.73661 1.000 16.69302  ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.47424   -22.80096 -29.02507 1.000 17.31957  ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 8.08597   -23.23298 -30.35943 1.000 17.40933  ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 6.95390   -22.36080 -30.86110 1.000 16.15985  ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 6.19550   -21.80426 -30.06791 1.000 17.21586  ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.66544   -24.71559 -30.39637 1.000 18.88146  ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.52185   -24.91621 -29.55044 1.000 21.67202  ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 8.80414   -25.64705 -29.95566 1.000 20.91994  ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 6.86440   -22.26015 -32.19346 1.000 17.65553  ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.74874   -21.57369 -32.84395 1.000 19.54595  ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.25902   -22.45915 -33.97291 1.000 21.64345  ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 6.05317   -22.94831 -34.77807 1.000 21.79812  ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 6.12974   -20.17116 -33.37196 1.000 19.80779  ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 4.93183   -19.52320 -34.12724 1.000 20.21597  ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.57241   -19.28453 -32.22834 1.000 18.62033  ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 3.94195   -22.63142 -34.06424 1.000 19.37866  ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.37210   -23.39742 -35.15733 1.000 19.78185  ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 2.03938   -22.77674 -35.54180 1.000 21.85787  ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.41981   -22.07658 -34.74962 1.000 20.01747  ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 3.19406   -24.87609 -34.79090 1.000 23.82965  ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 2.10634   -25.13503 -33.72996 1.000 26.73830  ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 2.25692   -26.50614 -33.05901 1.000 33.49199  ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.38391   -26.52915 -32.11824 1.000 36.29180  ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 4.00064   -27.63109 -31.68815 1.000 44.67037  ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 3.61308   -28.83982 -32.07001 1.000 40.07713  ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 5.04557   -27.51694 -30.86642 1.000 44.23781  ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.61881   -23.03087 -36.78082 1.000 22.83243  ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 0.25951   -22.66381 -37.15293 1.000 24.99425  ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.69702  -23.48588 -36.30787 1.000 30.21079  ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.46491  -24.66932 -36.06378 1.000 31.25650  ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 0.03366   -22.94622 -38.63729 1.000 29.99462  ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 0.89125   -22.07716 -39.37204 1.000 36.57786  ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? -1.38179  -22.57036 -39.00131 1.000 40.84857  ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.75871  -22.85886 -35.81669 1.000 25.42049  ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.68176  -23.57234 -34.95441 1.000 30.60185  ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.82456  -24.09700 -35.80134 1.000 39.89853  ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.53658  -23.31307 -36.43145 1.000 38.77030  ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -3.22052  -22.66565 -33.85250 1.000 28.55816  ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -4.05409  -23.42078 -32.84617 1.000 40.72389  ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -3.60501  -24.48318 -32.36545 1.000 48.54473  ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -5.16874  -22.96049 -32.54965 1.000 35.82121  ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -3.99758  -25.41160 -35.79592 1.000 46.16924  ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -5.11068  -26.07118 -36.45529 1.000 63.95177  ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.27793  -26.31651 -35.50558 1.000 60.87682  ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.29011  -26.89133 -35.91824 1.000 55.31880  ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.63454  -27.38382 -37.07864 1.000 67.66597  ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.67243  -28.00030 -36.20113 1.000 60.18738  ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -4.00161  -27.10541 -38.44509 1.000 54.13514  ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -6.16586  -25.87053 -34.25273 1.000 59.44799  ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -7.24796  -25.97005 -33.29367 1.000 59.23382  ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.49955  -25.16736 -33.61309 1.000 46.97183  ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.69060  -24.64586 -34.71801 1.000 43.82806  ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -9.37573  -25.09940 -32.63073 1.000 43.67533  ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.60909 -24.34239 -32.75674 1.000 39.73267  ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -10.30146 -22.88956 -33.13533 1.000 38.85799  ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.49967  -22.24726 -32.45731 1.000 33.17175  ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -11.33938 -24.42413 -31.41223 1.000 46.57779  ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -12.81317 -24.31215 -31.52183 1.000 54.63654  ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -13.36511 -25.38967 -32.41655 1.000 50.33288  ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -13.12489 -26.58608 -32.16407 1.000 47.94489  ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -13.94721 -25.01672 -33.44066 1.000 54.81806  ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -10.88702 -22.35387 -34.21040 1.000 37.52073  ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.63225 -20.94624 -34.56707 1.000 38.67535  ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -11.11090 -20.00120 -33.47116 1.000 37.92736  ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -12.20796 -20.16224 -32.93414 1.000 44.63752  ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.44992 -20.73605 -35.84930 1.000 42.69150  ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -11.97031 -22.08631 -36.26839 1.000 48.57688  ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.56138 -23.11955 -35.27843 1.000 45.43470  ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.30203 -18.98804 -33.15298 1.000 29.94179  ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.70781 -18.02684 -32.12709 1.000 30.85901  ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.31505 -16.72036 -32.61630 1.000 35.40467  ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -11.78725 -15.94236 -31.77806 1.000 39.80553  ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -9.54965  -17.65854 -31.22576 1.000 32.73539  ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -8.55225  -18.71389 -31.00114 1.000 49.50679  ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -7.12964  -17.89562 -30.29741 1.000 43.16772  ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -7.84084  -16.67864 -29.21287 1.000 32.17256  ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.24285 -16.40307 -33.88407 1.000 30.26518  ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -11.84761 -15.14161 -34.29337 1.000 28.02497  ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -10.87453 -13.99521 -34.15580 1.000 26.94142  ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.39449 -13.46056 -35.15948 1.000 23.90514  ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.53378 -13.66003 -32.90792 1.000 20.21333  ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.54155  -12.64197 -32.59392 1.000 19.90166  ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.26439  -12.68692 -31.10622 1.000 20.29752  ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.21405 -12.75873 -30.32245 1.000 19.61337  ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -10.04177 -11.22669 -32.96098 1.000 18.64484  ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -8.92896  -10.13610 -32.81503 1.000 19.26394  ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.51510  -8.68826  -32.65945 1.000 17.32151  ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.44698 -8.60305  -31.51381 1.000 17.25900  ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.77287 -8.50012  -31.62359 1.000 18.31961  ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.38780 -8.48626  -32.80827 1.000 21.22734  ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.53360 -8.39817  -30.52196 1.000 18.28206  ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -7.99280  -12.59518 -30.72771 1.000 18.67857  ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.65426  -12.49122 -29.31814 1.000 17.12248  ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.54498  -13.45016 -28.92906 1.000 21.43068  ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -5.78777  -13.94512 -29.77096 1.000 19.82017  ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.42569  -13.68956 -27.63538 1.000 16.09090  ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.34093  -14.51922 -27.12467 1.000 17.13931  ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -5.85086  -15.44497 -26.04892 1.000 22.95336  ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.66979  -15.04834 -25.22179 1.000 17.62858  ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.21128  -13.64225 -26.57662 1.000 17.76106  ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.66119  -12.87745 -27.65145 1.000 21.04447  ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -3.09789  -14.44883 -25.84448 1.000 21.70651  ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.34846  -16.67708 -26.05937 1.000 16.59746  ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.68710  -17.66436 -25.03808 1.000 17.37551  ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.36441  -18.09306 -24.42042 1.000 17.30814  ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.47814  -18.54827 -25.13898 1.000 18.56528  ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.38431  -18.84197 -25.72561 1.000 21.25864  ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -6.62689  -20.07197 -24.99176 1.000 30.37819  ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -7.92004  -20.74086 -25.58819 1.000 38.93623  ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -7.60535  -21.71170 -26.70894 1.000 52.55393  ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -7.91209  -23.15380 -26.34278 1.000 59.23306  ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.20898  -17.91328 -23.10993 1.000 16.37768  ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -2.99775  -18.35619 -22.40449 1.000 16.11002  ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.36795  -19.60595 -21.61791 1.000 18.13746  ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.21489  -19.54325 -20.71719 1.000 17.90755  ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.46607  -17.26460 -21.46891 1.000 16.06808  ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.22325  -17.77257 -20.66442 1.000 18.14788  ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -2.03067  -16.04416 -22.26256 1.000 15.84594  ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.75962  -20.73809 -21.96652 1.000 16.65172  ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -3.05061  -22.01560 -21.32436 1.000 16.70640  ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.91816  -22.30878 -20.36686 1.000 15.99144  ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.78992  -22.53231 -20.80566 1.000 16.15987  ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.20929  -23.15492 -22.33616 1.000 15.37149  ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.27559  -22.75751 -23.38093 1.000 18.41630  ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.56170  -24.48180 -21.57632 1.000 16.96678  ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.29209  -23.67789 -24.59051 1.000 22.57904  ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.22647  -22.32306 -19.06054 1.000 17.14788  ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.24102  -22.62834 -18.02502 1.000 18.02952  ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.33994  -24.09315 -17.64068 1.000 18.29594  ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.34741  -24.51453 -17.05840 1.000 18.84825  ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.46136  -21.74432 -16.79827 1.000 16.31595  ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.55073  -20.26040 -17.07546 1.000 18.42265  ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.89163  -19.58722 -15.75216 1.000 20.76415  ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.27375  -19.74823 -17.63138 1.000 19.85924  ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.28553  -24.86666 -17.92886 1.000 18.21840  ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.24121  -26.27786 -17.52517 1.000 18.59998  ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.38812   -26.27577 -16.14863 1.000 21.22757  ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.59561   -26.09320 -16.02210 1.000 20.38324  ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.55611   -27.10753 -18.52333 1.000 18.93810  ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.07403   -26.96293 -19.94090 1.000 23.17351  ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.70239  -27.92558 -20.55797 1.000 29.01481  ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.21843   -25.95775 -20.84380 1.000 26.32960  ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -0.99375  -27.53028 -21.79097 1.000 25.38953  ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.45006  -26.33780 -21.98832 1.000 24.50707  ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.44123  -26.39468 -15.11870 1.000 19.81937  ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 0.01064   -26.03072 -13.77702 1.000 19.00946  ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 0.97349   -27.06611 -13.21275 1.000 23.91719  ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.88254   -28.27543 -13.49825 1.000 23.22115  ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.19446  -25.87885 -12.84297 1.000 20.00744  ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -2.15001  -24.70640 -13.15831 1.000 18.55848  ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.29484  -24.67505 -12.14867 1.000 25.32140  ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.39456  -23.37014 -13.12528 1.000 21.94861  ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 1.90627   -26.58519 -12.37213 1.000 22.89420  ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.74306   -27.48347 -11.58774 1.000 24.94843  ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.87106   -28.28640 -10.63287 1.000 25.54731  ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.82059   -27.82637 -10.19360 1.000 24.77375  ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.79898   -26.69387 -10.78483 1.000 27.07273  ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.72864   -25.80962 -11.65046 1.000 28.09064  ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.67900   -24.95049 -10.77068 1.000 30.29403  ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.29551   -23.74882 -11.49096 1.000 37.38380  ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.31141   -22.92718 -10.67560 1.000 38.75655  ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.31812   -29.50852 -10.33735 1.000 28.93772  ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.54015   -30.43409 -9.52106  1.000 32.37340  ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.15333   -29.83421 -8.17402  1.000 33.83846  ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.08727   -30.16528 -7.63553  1.000 34.73624  ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.35340   -31.71889 -9.32386  1.000 40.02065  ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 1.57381   -32.93402 -8.91122  1.000 61.39461  ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.46983   -34.15406 -8.77892  1.000 79.65895  ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 3.70659   -33.97299 -8.70120  1.000 68.42341  ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 1.93858   -35.28588 -8.74264  1.000 94.14625  ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 1.99205   -28.96547 -7.59978  1.000 30.08371  ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.69270   -28.42735 -6.27694  1.000 28.60699  ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 0.99284   -27.06722 -6.34347  1.000 26.25982  ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.86187   -26.39907 -5.30628  1.000 25.43088  ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 2.95246   -28.33798 -5.42955  1.000 34.45772  ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 3.98876   -27.39741 -5.99457  1.000 35.80324  ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 3.87177   -26.99986 -7.17528  1.000 43.50460  ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 4.94437   -27.06890 -5.24752  1.000 51.58542  ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.52531   -26.65660 -7.52273  1.000 22.29733  ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.11826  -25.36428 -7.70516  1.000 21.33435  ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.58110  -25.52601 -8.12931  1.000 19.32142  ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.15707  -24.64202 -8.76468  1.000 21.44194  ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.65833   -24.49703 -8.70794  1.000 22.88681  ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.11996   -24.26226 -8.26906  1.000 23.89995  ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.23200   -23.56979 -6.91191  1.000 26.36934  ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.41319   -22.72600 -6.57968  1.000 28.79626  ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.27655   -23.88629 -6.14928  1.000 27.20646  ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.22342  -26.61765 -7.73424  1.000 24.93942  ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.59050  -26.82532 -8.21579  1.000 25.52692  ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.63613  -26.01268 -7.44796  1.000 24.59394  ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.82376  -26.05304 -7.81433  1.000 25.65365  ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.96778  -28.30977 -8.15382  1.000 27.21476  ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.82813  -28.79742 -6.81655  1.000 31.12235  ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -3.08561  -29.11455 -9.12053  1.000 31.23633  ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.24139  -25.27372 -6.40614  1.000 24.09985  ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.20236  -24.37569 -5.76538  1.000 23.31834  ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.78834  -23.38034 -6.75380  1.000 22.87935  ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.92171  -22.91775 -6.56016  1.000 23.52096  ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.55667  -23.63739 -4.58696  1.000 24.11923  ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.50313  -22.63195 -5.02215  1.000 22.37841  ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.77143  -22.10736 -3.83028  1.000 30.46916  ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.83997  -22.81044 -3.39955  1.000 32.48658  ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -3.13325  -21.03381 -3.29475  1.000 28.75539  ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -5.05143  -23.05740 -7.81755  1.000 22.19732  ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.48487  -22.06722 -8.80933  1.000 18.80417  ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.49628  -22.64076 -9.79201  1.000 22.43453  ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.88137  -21.94844 -10.73309 1.000 22.21399  ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.26598  -21.46776 -9.53897  1.000 20.04465  ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.34779  -20.82131 -8.51861  1.000 17.90995  ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.78042  -19.71360 -7.78068  1.000 19.90074  ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.08948  -21.36451 -8.22086  1.000 20.66584  ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.99062  -19.15338 -6.80470  1.000 21.52531  ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.28411  -20.79830 -7.24278  1.000 23.20149  ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.74896  -19.68384 -6.53592  1.000 19.44653  ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.99972  -19.12229 -5.54479  1.000 21.99624  ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.95327  -23.86445 -9.56712  1.000 21.06610  ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.08975  -24.40836 -10.28708 1.000 23.40919  ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.36072  -24.37148 -9.46679  1.000 25.44456  ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.41692 -24.77066 -9.97066  1.000 24.86969  ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.82028  -25.86247 -10.67054 1.000 23.24493  ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.58728  -26.06829 -11.53580 1.000 20.53966  ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.35690  -27.56115 -11.77970 1.000 25.48115  ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.73889  -25.29657 -12.84015 1.000 25.80836  ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.26814  -24.03045 -8.18096  1.000 21.70152  ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.42640 -24.03555 -7.29070  1.000 23.26662  ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.20939 -22.74095 -7.44372  1.000 26.93112  ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.62749 -21.64126 -7.41546  1.000 24.97845  ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -9.99309  -24.18683 -5.83930  1.000 29.05636  ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.33084  -25.51955 -5.51957  1.000 34.72761  ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -10.29587 -26.69095 -5.69340  1.000 67.16125  ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -11.52086 -26.52477 -5.42160  1.000 60.87691  ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -9.82129  -27.78248 -6.08992  1.000 62.38774  ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.52477 -22.87132 -7.64521  1.000 24.18815  ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.36124 -21.69327 -7.85287  1.000 21.38110  ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.16421 -20.63378 -6.75249  1.000 20.90669  ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.98541 -19.44375 -7.03874  1.000 22.07932  ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.84435 -22.11941 -7.93153  1.000 22.91716  ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.72036 -20.92721 -8.24517  1.000 30.66252  ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.21972 -21.24062 -8.37659  1.000 55.65458  ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.67317 -22.27121 -7.83317  1.000 40.88549  ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.94683 -20.40658 -8.97648  1.000 42.40572  ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.18505 -21.05386 -5.49329  1.000 24.16003  ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.13725 -20.05262 -4.43548  1.000 24.35817  ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.79766 -19.31788 -4.41841  1.000 25.90917  ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.75035 -18.13267 -4.07715  1.000 23.42904  ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.45922 -20.69652 -3.08572  1.000 25.68861  ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.41264 -21.54726 -2.48668  1.000 32.62132  ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -13.02303 -22.31360 -1.28785  1.000 33.25620  ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.05402 -23.25660 -0.76617  1.000 46.44308  ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.13524 -23.76674 0.45295   1.000 46.22322  ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.15479 -23.47679 1.24518   1.000 47.86524  ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.17120 -24.57973 0.88286   1.000 49.00837  ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.71527 -20.00107 -4.78847  1.000 21.45744  ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.39043  -19.38000 -4.80654  1.000 20.96824  ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.28320  -18.38828 -5.95565  1.000 22.43468  ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.75149  -17.28362 -5.79112  1.000 20.37714  ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.32645  -20.47305 -4.94252  1.000 22.23065  ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.86301  -19.97276 -4.90649  1.000 19.86856  ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.49579  -19.39042 -3.54018  1.000 23.98126  ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -5.05627  -19.14469 -3.47312  1.000 21.64443  ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.49664  -17.95488 -3.28695  1.000 25.93592  ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.22438  -16.87111 -3.09827  1.000 26.20828  ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.16834  -17.85068 -3.30255  1.000 25.54998  ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.78097  -18.76307 -7.13575  1.000 19.25629  ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.72080  -17.83584 -8.26279  1.000 17.50618  ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.56834 -16.60887 -7.98726  1.000 20.07415  ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.11791 -15.48005 -8.21905  1.000 19.97256  ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.15964 -18.51947 -9.56649  1.000 18.02529  ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.22945  -19.67948 -9.90190  1.000 19.75013  ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.22192 -17.45966 -10.69592 1.000 19.12376  ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.90337  -20.68331 -10.92581 1.000 21.61931  ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.78063 -16.79976 -7.44475  1.000 19.05818  ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.62773 -15.66205 -7.09092  1.000 19.13936  ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.91806 -14.71812 -6.13508  1.000 22.14536  ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -12.01048 -13.49730 -6.28046  1.000 20.94309  ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.92966 -16.10856 -6.40982  1.000 20.39872  ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.95968 -16.56209 -7.33712  1.000 27.19419  ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.24071 -16.82450 -6.52294  1.000 34.20096  ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -17.23368 -17.69681 -7.27570  1.000 53.29041  ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -17.62871 -18.91017 -6.49687  1.000 57.68534  ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.28153 -15.27533 -5.09897  1.000 18.49503  ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.58893 -14.44468 -4.12074  1.000 20.67822  ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.50573  -13.60442 -4.78315  1.000 20.06906  ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.35519  -12.41836 -4.47154  1.000 19.76804  ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -10.00138 -15.33439 -3.00890  1.000 20.86397  ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -9.00796  -14.64597 -2.05817  1.000 25.68933  ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.33139  -15.63827 -1.11104  1.000 24.96754  ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.78106  -16.63481 -1.65017  1.000 26.27454  ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.34192  -15.40943 0.13619   1.000 25.64388  ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.74089  -14.20271 -5.70194  1.000 18.20481  ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.64412  -13.48685 -6.35402  1.000 20.04844  ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.19089  -12.38489 -7.24057  1.000 20.37403  ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.64315  -11.27894 -7.27907  1.000 19.76077  ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.78582  -14.47830 -7.16403  1.000 17.87856  ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -6.17420  -15.46065 -6.16714  1.000 22.24099  ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.66795  -13.76247 -7.92360  1.000 21.58493  ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.53096  -16.69344 -6.81466  1.000 22.67394  ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.24402  -12.68953 -8.00667  1.000 18.11900  ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.80385  -11.68278 -8.89765  1.000 16.36679  ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.34075 -10.51699 -8.09661  1.000 17.15433  ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -10.09732 -9.35794  -8.43731  1.000 20.58649  ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.89400 -12.29534 -9.78430  1.000 19.91443  ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.63225 -11.19004 -10.53105 1.000 20.00037  ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.22865 -13.30071 -10.77028 1.000 19.65784  ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -11.03663 -10.79893 -6.98041  1.000 17.42328  ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.56490 -9.71440  -6.16682  1.000 21.04734  ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.43884 -8.89817  -5.53501  1.000 22.80218  ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.55851 -7.67584  -5.40174  1.000 26.00905  ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.49557 -10.29085 -5.09393  1.000 24.05896  ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.10880 -9.26814  -4.18057  1.000 30.88180  ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -14.06050 -9.93366  -3.21253  1.000 37.06668  ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.44935 -9.00565  -2.08528  1.000 45.56241  ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.37600 -9.72285  -1.17326  1.000 55.77557  ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.34138  -9.55925  -5.13507  1.000 21.44429  ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.24002  -8.86241  -4.45670  1.000 23.47493  ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.48553  -7.93553  -5.39886  1.000 23.60092  ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.10362  -6.82603  -5.00102  1.000 23.49696  ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.26492  -9.87336  -3.85428  1.000 22.12284  ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.10848  -9.23614  -3.06497  1.000 27.56257  ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.26459  -10.34618 -2.46570  1.000 32.02268  ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.12544  -9.81313  -1.61355  1.000 39.83886  ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.38915  -10.94159 -0.93696  1.000 45.22661  ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.21637  -8.39948  -6.63402  1.000 21.90820  ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.23065  -7.75820  -7.50529  1.000 25.13690  ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.79428  -7.18855  -8.79679  1.000 26.86135  ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -6.11540  -6.35840  -9.42163  1.000 25.90495  ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -5.12548  -8.76359  -7.90386  1.000 23.20631  ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.29309  -9.23497  -6.75475  1.000 24.46521  ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.47179  -8.39943  -6.02663  1.000 28.99633  ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -4.19595  -10.45768 -6.17280  1.000 29.19915  ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.88031  -9.09147  -5.06565  1.000 30.66378  ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.31156  -10.34092 -5.12286  1.000 31.42816  ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.99973  -7.58583  -9.21065  1.000 21.60377  ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.51223  -7.25320  -10.53671 1.000 20.52161  ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.90618  -6.64121  -10.43335 1.000 22.56698  ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.68209 -6.68431  -11.40024 1.000 23.37194  ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.51724  -8.48759  -11.44374 1.000 22.81095  ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -7.18561  -8.99773  -11.53056 1.000 23.55988  ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.21343 -6.02651  -9.28453  1.000 24.51554  ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.59278 -5.60123  -9.05703  1.000 31.80774  ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.98726 -4.42027  -9.93908  1.000 34.18970  ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -13.18340 -4.21492  -10.17871 1.000 35.84603  ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.83159 -5.26153  -7.57099  1.000 32.27586  ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -11.08617 -4.05574  -7.05251  1.000 38.18450  ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -9.70667  -4.36230  -6.39420  1.000 59.58771  ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -8.84902  -5.10374  -6.94666  1.000 36.03242  ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -9.49497  -3.77747  -5.20323  1.000 49.22011  ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -11.02207 -3.67994  -10.48382 1.000 23.44601  ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.34373 -2.51047  -11.29614 1.000 28.38744  ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -11.06074 -2.68786  -12.78293 1.000 29.33200  ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -11.12535 -1.71235  -13.52661 1.000 34.10303  ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.58311 -1.29735  -10.77847 1.000 29.65463  ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.98602 -0.90459  -9.37382  1.000 36.03929  ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.31679 -0.71084  -9.05741  1.000 36.16221  ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -10.04858 -0.84052  -8.36384  1.000 38.14231  ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.70557 -0.37837  -7.76897  1.000 42.40372  ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.43210 -0.50946  -7.07782  1.000 39.27052  ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.77134 -0.28513  -6.78838  1.000 35.23007  ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.79603 -3.91050  -13.24330 1.000 21.09607  ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.59405 -4.15082  -14.67135 1.000 18.44975  ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.88035 -3.85184  -15.43889 1.000 26.41632  ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.96759 -4.30008  -15.04837 1.000 25.88059  ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -10.13914 -5.60363  -14.86678 1.000 19.44206  ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.71916  -5.78880  -14.29266 1.000 20.78056  ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -10.22147 -6.03568  -16.34254 1.000 20.76666  ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.60468  -5.06933  -15.10503 1.000 22.22539  ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.76512 -3.09450  -16.53619 1.000 19.83272  ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.92195 -2.54339  -17.21473 1.000 21.65572  ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.56666 -3.42650  -18.26370 1.000 22.56060  ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.19338 -2.92820  -19.21075 1.000 23.87571  ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.44449 -4.73271  -18.09657 1.000 20.09801  ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -14.03178 -5.71592  -19.00411 1.000 19.99498  ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.61934 -6.83105  -18.14996 1.000 22.71885  ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -14.06487 -7.15270  -17.09930 1.000 21.56015  ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.98800 -6.30484  -19.98039 1.000 18.89000  ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.38650 -5.22605  -20.83892 1.000 19.05398  ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -13.02451 -4.81188  -21.98914 1.000 19.87317  ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.17634 -4.61722  -20.49346 1.000 18.93150  ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.50833 -3.81119  -22.77104 1.000 19.13663  ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.64681 -3.61877  -21.27087 1.000 18.33929  ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.33256 -3.20175  -22.39838 1.000 18.22501  ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.85668 -2.20608  -23.19963 1.000 22.01690  ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.69002 -7.47884  -18.61327 1.000 19.66107  ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.28246 -8.58244  -17.82695 1.000 18.95857  ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.34228 -9.77072  -17.75215 1.000 20.73497  ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.79143 -10.22332 -18.75894 1.000 21.35983  ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.57629 -8.92498  -18.58828 1.000 22.02413  ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.40806 -8.37836  -19.94819 1.000 25.94111  ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.44241 -7.18551  -19.84643 1.000 20.97287  ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.15015 -10.26810 -16.53781 1.000 19.06965  ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.28941 -11.42255 -16.27928 1.000 16.18231  ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.22819 -12.51037 -15.82693 1.000 16.08675  ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.93921 -12.34240 -14.81746 1.000 20.94480  ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.23172 -11.14004 -15.19674 1.000 19.46771  ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.30759 -9.97759  -15.60319 1.000 17.50684  ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.46748 -12.42729 -14.85660 1.000 18.96674  ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.45174 -9.48377  -14.39214 1.000 17.97113  ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.32417 -13.57323 -16.61511 1.000 17.43533  ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.27299 -14.64392 -16.31038 1.000 15.90044  ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.45114 -15.84369 -15.89332 1.000 16.12381  ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.61407 -16.31589 -16.66284 1.000 16.68522  ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -17.13383 -15.00320 -17.52773 1.000 18.26456  ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.90154 -13.86363 -17.96345 1.000 19.06481  ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -18.06021 -16.17372 -17.16654 1.000 21.24595  ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.67103 -16.31952 -14.67150 1.000 17.84637  ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -15.03306 -17.53753 -14.18855 1.000 18.32137  ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.95689 -18.70969 -14.51998 1.000 17.81888  ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -17.06258 -18.80347 -13.98205 1.000 18.59924  ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.78160 -17.42999 -12.67910 1.000 18.02380  ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.25668 -18.67941 -11.97104 1.000 21.98084  ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -13.01045 -19.27561 -12.62467 1.000 19.71600  ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.97819 -18.28852 -10.47575 1.000 22.20878  ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.50321 -19.59037 -15.41265 1.000 16.88882  ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.27734 -20.75574 -15.79773 1.000 17.86321  ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.24523 -21.77711 -14.66806 1.000 19.87720  ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.26746 -21.85648 -13.91567 1.000 21.64668  ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.66382 -21.41126 -17.04967 1.000 19.01085  ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.92934 -20.69554 -18.35668 1.000 17.39705  ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -16.02939 -19.30745 -18.44619 1.000 17.91238  ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -16.04403 -21.47005 -19.50387 1.000 18.09250  ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.25438 -18.67051 -19.68103 1.000 17.27992  ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.24266 -20.87564 -20.76779 1.000 19.43104  ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.36630 -19.45928 -20.86602 1.000 18.15533  ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.30498 -22.55635 -14.54925 1.000 21.41629  ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.33698 -23.63151 -13.56877 1.000 24.35746  ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.19694 -24.95260 -14.30283 1.000 28.05873  ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.31130 -25.02697 -15.52730 1.000 25.44144  ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.60406 -23.60047 -12.70130 1.000 33.81644  ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.50051 -22.46016 -11.66622 1.000 40.32903  ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.78649 -23.45101 -13.53511 1.000 27.97564  ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -16.93893 -26.00316 -13.54569 1.000 26.89439  ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.73086 -27.32487 -14.12126 1.000 31.11973  ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.82932 -28.27867 -13.68858 1.000 34.81723  ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.37167 -28.14649 -12.59149 1.000 38.60739  ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.38582 -27.89417 -13.67883 1.000 32.14716  ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.25921 -26.98827 -14.02903 1.000 29.16546  ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.92888 -27.53654 -13.56080 1.000 37.06532  ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.52197 -28.63468 -14.01099 1.000 33.27638  ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.32978 -26.87985 -12.68091 1.000 35.74545  ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -18.11901 -29.26195 -14.55009 1.000 36.43135  ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -19.00866 -30.39123 -14.22420 1.000 47.59960  ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -18.77935 -30.97387 -12.82061 1.000 60.37736  ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -17.65238 -31.29948 -12.44928 1.000 54.46212  ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -18.84014 -31.51215 -15.25767 1.000 45.71448  ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -19.78306 -32.69853 -15.05377 1.000 66.26242  ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -19.79457 -33.65004 -16.26459 1.000 71.81989  ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -18.54069 -33.46336 -17.13410 1.000 75.19287  ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -18.41652 -34.48897 -18.21279 1.000 81.51615  ? 224 LYS   A NZ  1 
HETATM 1645 N N1  . A1AYD B 2 .   ? 16.57669  4.02400   -16.73081 1.000 42.94867  ? 301 A1AYD A N1  1 
HETATM 1646 C C2  . A1AYD B 2 .   ? 16.51524  4.05099   -15.40446 0.531 47.97172  ? 301 A1AYD A C2  1 
HETATM 1647 C C4  . A1AYD B 2 .   ? 14.94179  1.14876   -13.61680 1.000 60.70337  ? 301 A1AYD A C4  1 
HETATM 1648 C C5  . A1AYD B 2 .   ? 14.78102  0.51533   -12.39141 1.000 63.55841  ? 301 A1AYD A C5  1 
HETATM 1649 C C6  . A1AYD B 2 .   ? 15.34914  1.07767   -11.27553 1.000 66.25194  ? 301 A1AYD A C6  1 
HETATM 1650 N N2  . A1AYD B 2 .   ? 15.84836  2.96858   -14.97309 1.000 53.88369  ? 301 A1AYD A N2  1 
HETATM 1651 C C7  . A1AYD B 2 .   ? 16.07174  2.24329   -11.31181 1.000 74.35333  ? 301 A1AYD A C7  1 
HETATM 1652 C C1  . A1AYD B 2 .   ? 17.36813  4.93568   -17.52526 1.000 33.04723  ? 301 A1AYD A C1  1 
HETATM 1653 C C3  . A1AYD B 2 .   ? 15.65933  2.34447   -13.70861 1.000 77.84994  ? 301 A1AYD A C3  1 
HETATM 1654 C C8  . A1AYD B 2 .   ? 16.21070  2.84361   -12.53887 1.000 82.66032  ? 301 A1AYD A C8  1 
HETATM 1655 F F1  . A1AYD B 2 .   ? 15.19661  0.46217   -10.07477 0.376 47.48239  ? 301 A1AYD A F1  1 
HETATM 1656 F F2  . A1AYD B 2 .   ? 16.92266  3.99121   -12.60710 0.730 78.05190  ? 301 A1AYD A F2  1 
HETATM 1657 S S1  . A1AYD B 2 .   ? 17.23894  5.28354   -14.52308 0.561 75.88462  ? 301 A1AYD A S1  1 
HETATM 1658 O O   . HOH   C 3 .   ? 11.47624  -21.69462 -40.42961 1.000 42.85112  ? 401 HOH   A O   1 
HETATM 1659 O O   . HOH   C 3 .   ? 9.13498   -23.98556 -41.34479 1.000 53.93830  ? 402 HOH   A O   1 
HETATM 1660 O O   . HOH   C 3 .   ? -16.92457 -20.24545 -4.74922  1.000 44.08699  ? 403 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? -17.82976 -4.89162  -37.29799 1.000 46.22307  ? 404 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? 22.93725  -15.69440 -19.00018 1.000 46.17933  ? 405 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -2.87443  -3.15613  -35.42038 1.000 40.26956  ? 406 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? 15.16110  -26.22471 -25.25721 1.000 50.78127  ? 407 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? -1.57609  -28.94019 -5.75482  1.000 32.34384  ? 408 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? -0.29193  -5.62343  -38.52303 1.000 44.63027  ? 409 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? 3.40591   -29.96114 -18.85417 1.000 50.54666  ? 410 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? 5.87725   -25.47339 -7.16455  1.000 43.41756  ? 411 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? -20.44664 -20.56499 -9.26317  1.000 50.14331  ? 412 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? -18.13915 -33.51283 -11.33378 1.000 51.74204  ? 413 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? 13.91035  -11.41128 -29.52906 1.000 41.66836  ? 414 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 3.10347   -24.53451 -38.56469 1.000 37.07970  ? 415 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? -17.48565 -24.65378 -8.69462  1.000 46.74327  ? 416 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? -13.08492 -7.31248  -11.96676 1.000 31.53521  ? 417 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? 3.53729   -29.70968 -25.51764 1.000 49.34224  ? 418 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? 0.18630   -28.35730 -25.68498 1.000 49.31660  ? 419 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? -16.20634 -25.60999 -17.77392 1.000 24.80477  ? 420 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 5.05011   -9.56713  -2.59993  1.000 45.45044  ? 421 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? 1.79858   -15.72574 -41.06978 1.000 44.70960  ? 422 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? 6.59107   -26.61372 -27.59521 1.000 31.72978  ? 423 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? 20.28427  -10.79564 -26.26134 1.000 39.90476  ? 424 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? 9.77790   -14.76072 -25.24108 1.000 22.57758  ? 425 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? -14.35251 -6.72263  -14.52394 1.000 35.41473  ? 426 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? -6.96689  -27.83876 -21.09490 1.000 43.37694  ? 427 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? 6.02973   -20.92258 -0.09541  1.000 30.83397  ? 428 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? -8.72805  -11.81487 -36.37026 1.000 25.70025  ? 429 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? 5.92427   -21.87937 -37.18671 1.000 32.00409  ? 430 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? 1.44119   -7.74551  -16.56458 1.000 22.54121  ? 431 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? 9.05270   -26.34579 -17.04392 1.000 31.36815  ? 432 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 7.62913   -27.82236 -23.98367 1.000 31.87183  ? 433 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? 7.78762   -23.12362 -14.19351 1.000 28.79962  ? 434 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? -20.53683 -14.01833 -18.13358 1.000 37.29697  ? 435 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? 7.66973   1.28180   -14.81802 1.000 35.58647  ? 436 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? 0.37324   -1.55752  -19.76268 1.000 36.51178  ? 437 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? -18.81027 -10.83014 -23.60276 1.000 31.64592  ? 438 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? -10.98543 -14.09816 -37.66046 1.000 37.29885  ? 439 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -2.89812  -5.84069  -6.39932  1.000 36.96567  ? 440 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? 11.17750  -8.16566  -27.57937 1.000 22.67690  ? 441 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? -8.21519  1.85882   -36.59503 1.000 37.20735  ? 442 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? -17.88601 -3.79273  -28.99998 1.000 44.37847  ? 443 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? -4.27767  0.48743   -22.19819 1.000 36.14829  ? 444 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? -3.60325  -10.85583 -23.96660 1.000 25.48106  ? 445 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? -14.15331 -11.37002 0.52531   1.000 42.84375  ? 446 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? -15.80888 0.22971   -30.36274 1.000 37.21938  ? 447 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? 2.97438   -20.21604 -2.72177  1.000 36.32935  ? 448 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? 0.76492   -5.13798  -14.10843 1.000 38.20913  ? 449 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? -5.82617  -2.01057  -19.48948 1.000 23.76650  ? 450 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -6.45342  -5.05500  -38.99807 1.000 43.12363  ? 451 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? -9.32868  -2.24825  -17.58007 1.000 20.43466  ? 452 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? 11.29670  -28.35959 -30.48419 1.000 34.00444  ? 453 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 7.68103   -18.63114 -6.55617  1.000 24.88563  ? 454 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? -0.31539  -5.30509  -18.36448 1.000 26.81143  ? 455 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? -3.09602  -31.58447 -19.72599 1.000 49.57024  ? 456 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? 6.54652   -29.62846 -20.20404 1.000 36.23598  ? 457 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? -5.38516  -10.35450 -27.33338 1.000 18.28973  ? 458 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? -13.39898 -0.69342  -20.48583 1.000 32.54667  ? 459 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? 0.83178   -20.86766 -4.62255  1.000 28.83310  ? 460 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? -10.64941 -14.36382 1.05876   1.000 27.38934  ? 461 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? -13.00302 -24.80768 -10.73462 1.000 30.42386  ? 462 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -8.38384  4.77967   -33.56105 1.000 30.29026  ? 463 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? -8.18658  -24.73259 -19.00702 1.000 18.82356  ? 464 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -16.33383 -12.58597 -19.75818 1.000 20.37266  ? 465 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? 0.23397   -14.79845 -1.65154  1.000 42.52761  ? 466 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? -4.26376  -4.63239  -8.45952  1.000 41.95994  ? 467 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -16.04645 -2.99396  -21.18699 1.000 28.33348  ? 468 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? -7.58978  -5.21232  -2.87432  1.000 45.75561  ? 469 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -13.91260 -14.90145 -30.44772 1.000 51.68345  ? 470 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? -7.68834  -24.32382 -22.90825 1.000 29.25156  ? 471 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? 13.58067  -14.21855 -26.83253 1.000 22.96727  ? 472 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? -17.05123 -5.35831  -22.75342 1.000 28.17708  ? 473 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? -2.30414  -13.67189 -35.60809 1.000 19.74097  ? 474 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? 18.33537  -7.21673  -20.46648 1.000 36.03162  ? 475 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? -6.40167  -7.73961  -34.36618 1.000 20.74265  ? 476 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? 18.00361  -19.30110 -24.66831 1.000 32.12803  ? 477 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? 12.89632  -13.88511 -29.70668 1.000 27.32963  ? 478 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? -2.19412  -0.49022  -18.72736 1.000 39.56111  ? 479 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? -1.03709  -11.12659 -3.08733  1.000 36.06298  ? 480 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? 3.27433   -6.02716  -11.19272 1.000 26.82728  ? 481 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? 15.41620  -20.13842 -18.71177 1.000 24.73462  ? 482 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? 0.61806   -26.82778 -37.35356 1.000 43.16221  ? 483 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? -7.73942  -28.11036 -7.84112  1.000 32.46221  ? 484 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? -14.66049 -22.52125 -11.32328 1.000 29.39910  ? 485 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? 11.45476  -27.43209 -34.68831 1.000 27.29209  ? 486 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -12.091   -28.036   -30.074   1.000 37.39692  ? 487 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? 9.69871   -17.20869 -7.77944  1.000 25.09784  ? 488 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? -1.17878  -7.36049  -23.63108 1.000 25.58409  ? 489 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? 0.27423   -31.14312 -22.84890 1.000 55.13600  ? 490 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? 3.01371   -5.69652  -6.37283  1.000 47.08985  ? 491 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -3.73917  -13.19854 -42.82449 1.000 43.44204  ? 492 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? -8.03650  -22.73774 -30.17268 1.000 42.85518  ? 493 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? -13.46169 -26.41051 -17.87306 1.000 28.67771  ? 494 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 1.57635   -25.85309 -2.69559  1.000 47.90144  ? 495 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? 0.98075   -6.27061  -34.23795 1.000 41.43946  ? 496 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 0.63387   -29.57316 -15.92806 1.000 34.63563  ? 497 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? -5.47842  -7.53891  -13.15028 1.000 19.61852  ? 498 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? 8.00894   -23.02548 -7.22083  1.000 37.67359  ? 499 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? 3.57933   -7.69460  -36.65259 1.000 34.82789  ? 500 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? -13.73839 -16.86682 -2.60935  1.000 25.88696  ? 501 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? -1.31994  -26.05830 -32.18510 1.000 40.72480  ? 502 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? 8.43358   -16.28603 -39.45846 1.000 36.22531  ? 503 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? 10.52405  -25.33200 -23.71206 1.000 23.13498  ? 504 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? -5.80396  -31.06707 -11.45344 1.000 29.98395  ? 505 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? -15.21767 -11.00894 -29.74280 1.000 25.21036  ? 506 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? 9.51692   -11.08907 -34.91009 1.000 42.76124  ? 507 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? -19.84581 -12.56503 -16.43202 1.000 50.24080  ? 508 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -6.32604  -5.01642  -35.65280 1.000 22.88330  ? 509 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? 14.08953  -15.50097 -2.10833  1.000 36.94527  ? 510 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? 4.25567   -19.44466 -40.61719 1.000 37.49476  ? 511 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? 4.05840   -24.15212 -30.63520 1.000 20.54720  ? 512 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? -6.27652  -11.20351 -10.05962 1.000 26.85039  ? 513 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? 8.30525   -20.35942 -9.28996  1.000 32.33398  ? 514 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? -19.800   -19.400   -14.124   1.000 21.68291  ? 515 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? -10.40631 -11.36462 -2.09155  1.000 25.23105  ? 516 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 12.30500  -27.30276 -19.58744 1.000 43.89430  ? 517 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? 8.80876   -15.52231 -27.79480 1.000 19.59770  ? 518 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? 19.77543  -16.68071 -27.54331 1.000 38.42196  ? 519 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? 10.69541  -25.65066 -26.74540 1.000 31.33563  ? 520 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -2.46096  -10.59937 -26.51720 1.000 32.63864  ? 521 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? -3.374    -20.913   -0.494    1.000 38.36643  ? 522 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? -3.91033  -13.96574 -0.72632  1.000 41.11742  ? 523 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? -8.20886  -3.82947  -10.63393 1.000 28.03571  ? 524 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -5.94633  -7.27840  -42.38252 1.000 48.66581  ? 525 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? 14.28142  -16.03015 -30.75769 1.000 34.26122  ? 526 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? -14.20950 -12.56658 -7.79798  1.000 25.92328  ? 527 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? 18.43605  -15.93926 -13.52401 1.000 36.39121  ? 528 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? -17.74882 -18.61109 -11.24071 1.000 35.77929  ? 529 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? -19.39932 -10.26345 -33.00732 1.000 43.56444  ? 530 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? 3.62473   -6.66155  -17.97011 1.000 24.21220  ? 531 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? -10.25099 -0.51678  -19.94000 1.000 35.42329  ? 532 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? 2.03980   -6.07261  -26.00367 1.000 39.91057  ? 533 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? -17.23809 -28.59861 -17.16810 1.000 38.22022  ? 534 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -1.60080  -6.30427  -26.16505 1.000 24.00461  ? 535 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? -10.53363 -6.18128  -2.97589  1.000 41.68068  ? 536 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? -4.23900  -3.24226  -15.71038 1.000 45.33260  ? 537 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? 3.98103   -9.17087  -20.37775 1.000 21.56771  ? 538 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -18.09876 -36.80171 -19.85043 1.000 42.28089  ? 539 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? -5.98406  -18.58774 -39.04538 1.000 35.78729  ? 540 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -3.21395  -1.03265  -24.14255 1.000 28.11853  ? 541 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? -9.04122  -17.77095 -36.34565 1.000 41.43434  ? 542 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? -6.09425  -13.80857 0.87080   1.000 29.85831  ? 543 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? -0.28803  -7.05324  -31.00048 1.000 34.94109  ? 544 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -15.756   6.351     -32.308   1.000 44.48310  ? 545 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? 15.65679  -0.74125  -19.67405 1.000 33.51235  ? 546 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? -13.49601 -30.81648 -12.41758 1.000 47.07380  ? 547 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -10.27792 -14.92786 -28.32390 1.000 26.31531  ? 548 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? 10.48975  -21.09882 -6.93107  1.000 40.91996  ? 549 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? -1.70523  -32.41853 -7.74941  1.000 50.91821  ? 550 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? 21.46861  -2.71580  -15.23222 1.000 52.16673  ? 551 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? 19.94880  -4.95949  -14.88022 1.000 44.69284  ? 552 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? -11.82385 -7.55880  -38.27655 1.000 37.55565  ? 553 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? -4.60686  0.47897   -30.49840 1.000 31.11755  ? 554 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? 8.77894   -20.20177 -4.33098  1.000 27.62678  ? 555 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? -1.81731  -25.48598 -4.65688  1.000 25.35910  ? 556 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? -1.22734  -29.81811 -17.22935 1.000 41.16115  ? 557 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? -7.26347  1.27303   -19.31736 1.000 32.86773  ? 558 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? 4.84030   -0.94359  -6.48072  1.000 52.53332  ? 559 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? 17.43997  -15.60055 -29.64750 1.000 40.37726  ? 560 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? -15.19174 -12.13228 -12.00094 1.000 33.24007  ? 561 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? -5.13253  -14.16255 -22.59052 1.000 18.73568  ? 562 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? -7.58044  -13.61838 -41.04320 1.000 46.41577  ? 563 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? -1.28475  -4.45744  -33.64363 1.000 39.29154  ? 564 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? -7.34705  -22.51694 -36.69958 1.000 48.83089  ? 565 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? -17.78295 -15.07286 -13.06130 1.000 25.50874  ? 566 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? 3.71722   -11.83052 -38.56914 1.000 25.14012  ? 567 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? 18.51306  -22.28583 -25.63975 1.000 50.38251  ? 568 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? -3.44796  -13.01259 -20.66275 1.000 22.31131  ? 569 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? -16.45894 -9.03322  -14.19792 1.000 36.30425  ? 570 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? 13.65429  -20.42826 -20.73493 1.000 21.22251  ? 571 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? 4.89019   -30.27677 -11.56964 1.000 40.79292  ? 572 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? 1.31485   -3.13432  -24.26328 1.000 43.38065  ? 573 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? -5.596    -11.118   1.024     1.000 43.15244  ? 574 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? -18.69436 -11.27487 -15.03778 1.000 57.55368  ? 575 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? 0.44849   -5.47778  -21.98892 1.000 40.49669  ? 576 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 10.33567  -17.84041 -38.91676 1.000 46.88683  ? 577 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? -12.37530 -27.37689 -34.92290 1.000 44.67827  ? 578 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? 6.90608   -24.87205 -5.60012  1.000 50.79449  ? 579 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? -13.05075 -12.15131 -30.95409 1.000 28.21992  ? 580 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? -16.27832 -25.26345 -10.74363 1.000 37.16427  ? 581 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? -9.08162  -10.50580 -40.43934 1.000 40.54514  ? 582 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? 13.31145  -6.81948  -26.32311 1.000 22.55268  ? 583 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? 20.89368  -14.27002 -26.78187 1.000 34.83059  ? 584 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? 11.12633  -11.15870 -4.76373  1.000 38.39682  ? 585 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? -14.01236 -23.82827 -4.76055  1.000 30.33880  ? 586 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? 0.96068   -9.37044  -40.37632 1.000 50.68725  ? 587 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? -2.32438  -15.42650 -0.27708  1.000 43.89171  ? 588 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? 4.04825   -22.70357 -3.49958  1.000 37.18331  ? 589 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? 2.98272   -4.01370  -9.06728  1.000 47.27529  ? 590 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? -14.55855 -29.06310 -9.66362  1.000 45.67330  ? 591 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? 10.00638  -5.78333  -1.52706  1.000 49.79204  ? 592 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? 0.07737   -16.45449 -3.41642  1.000 27.87079  ? 593 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? 17.07841  -24.72982 -25.35156 1.000 40.08991  ? 594 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? 20.45287  -6.00614  -21.06657 1.000 38.60431  ? 595 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? -7.45066  7.55305   -33.74851 1.000 36.80158  ? 596 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? 1.18327   -8.62522  -26.85866 1.000 31.76263  ? 597 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? -14.24569 -16.07896 -26.07267 1.000 28.97970  ? 598 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? -13.50287 -25.75399 -7.64805  1.000 32.36646  ? 599 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? -6.54424  -35.22185 -19.37779 1.000 52.08850  ? 600 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? -5.22651  -31.50719 -6.89600  1.000 46.30887  ? 601 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? -1.55199  -8.55384  -27.75306 1.000 32.80520  ? 602 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? -13.75032 -18.50217 -24.38243 1.000 22.98814  ? 603 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? 15.45433  -7.20723  -27.95003 1.000 33.28537  ? 604 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? -5.01436  -5.16226  -12.02593 1.000 39.23537  ? 605 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? 8.46065   -19.85952 -41.58647 1.000 47.87796  ? 606 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? 13.67428  -4.04417  -25.51928 1.000 18.58684  ? 607 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? -18.06093 -5.58249  -25.57201 1.000 36.76535  ? 608 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 6.79575   -29.70179 -29.56660 1.000 52.51760  ? 609 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? -12.44657 -20.53701 -29.87121 1.000 43.05298  ? 610 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? -12.26180 -26.84270 -20.29652 1.000 27.48686  ? 611 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? 15.88495  -17.78824 -3.64911  1.000 33.94655  ? 612 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? 2.75705   -10.14570 -23.23749 1.000 31.37180  ? 613 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? -5.44400  -11.92010 -42.08607 1.000 43.21782  ? 614 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? -0.58127  -12.44175 -21.45426 1.000 33.95183  ? 615 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? -3.76508  -32.86991 -10.82192 1.000 50.39386  ? 616 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? 1.800     -18.178   0.081     1.000 38.39701  ? 617 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? 3.13209   -6.50423  -20.46004 1.000 40.80528  ? 618 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? 1.89273   -25.75282 -29.30649 1.000 36.86979  ? 619 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? 8.27757   -25.87103 -25.90672 1.000 36.86294  ? 620 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? 4.63653   -1.87358  -18.22365 1.000 40.20084  ? 621 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? 7.29114   1.91536   -12.52573 1.000 33.73216  ? 622 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? 5.55592   -3.05434  -26.10710 1.000 40.51125  ? 623 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? 14.40236  -22.13380 -17.09450 1.000 34.16761  ? 624 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? -0.16588  -19.19439 -1.94590  1.000 44.84602  ? 625 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? 6.07349   -29.79196 -24.89438 1.000 44.91170  ? 626 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? 1.87097   -3.03750  -12.70473 1.000 43.99346  ? 627 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? -13.95851 -14.08391 -3.03100  1.000 34.78322  ? 628 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? 16.95109  0.56692   -17.63556 1.000 41.37542  ? 629 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? -0.41162  -1.16706  -22.81037 1.000 42.48199  ? 630 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? 5.517     1.646     -16.694   1.000 41.80572  ? 631 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? 12.10336  -25.35894 -38.31434 1.000 34.30410  ? 632 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? 11.03028  -22.99648 -41.89508 1.000 56.99492  ? 633 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? -12.44660 -16.30757 -28.15724 1.000 35.26139  ? 634 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? 3.44805   -7.85650  -2.14823  1.000 45.49781  ? 635 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? -14.29242 -9.80691  -8.44738  1.000 39.36807  ? 636 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? -9.15553  -5.70182  -39.84888 1.000 41.22004  ? 637 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? -3.82455  1.80863   -32.56919 1.000 49.87945  ? 638 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? -19.58783 -13.06070 -14.07066 1.000 52.08360  ? 639 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? 18.99357  -8.37389  -17.73393 1.000 37.49752  ? 640 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? -17.823   0.721     -21.960   1.000 53.57850  ? 641 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? 3.54738   -9.11044  -39.07605 1.000 37.73414  ? 642 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? -6.11131  3.81636   -34.60173 1.000 42.22828  ? 643 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? -3.41237  -26.89733 -2.99592  1.000 48.98259  ? 644 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 3.64960   -0.17015  -16.48702 1.000 46.39100  ? 645 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? -11.91010 -9.72014  -39.77811 1.000 51.23329  ? 646 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? -9.81210  -25.89062 -20.76437 1.000 29.71382  ? 647 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? 2.199     -0.859    -26.124   1.000 41.89235  ? 648 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? -2.34269  -0.96051  -30.92342 1.000 46.25163  ? 649 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? -18.62684 -11.53944 -21.11022 1.000 31.14086  ? 650 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? 11.021    -1.227    -17.659   1.000 39.84998  ? 651 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? 7.75309   -13.86612 -38.27429 1.000 36.98875  ? 652 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? -0.82797  -29.33196 -3.30137  1.000 49.76958  ? 653 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? -6.153    6.870     -36.169   1.000 46.17669  ? 654 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? 15.56197  -12.24641 -7.06625  1.000 46.68731  ? 655 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? -10.58188 -8.56140  -1.46853  1.000 39.42514  ? 656 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 5.73881   -12.99502 -39.80773 1.000 31.84533  ? 657 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? -12.143   -9.333    1.276     1.000 45.17914  ? 658 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? 7.75918   -28.93607 -28.16781 1.000 42.81995  ? 659 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? 10.96479  -27.86299 -27.82860 1.000 37.02014  ? 660 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? 1.58886   -7.46779  -23.22784 1.000 44.69690  ? 661 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? -16.194   3.215     -26.452   1.000 39.42755  ? 662 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? 5.35125   -3.31952  -23.74779 1.000 43.23748  ? 663 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? 6.80147   -21.39189 -2.68768  1.000 33.03215  ? 664 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? -3.91991  -34.04941 -20.27004 1.000 51.01756  ? 665 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? -10.477   -22.471   4.492     1.000 46.12926  ? 666 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? -0.54657  -26.63312 -30.35394 1.000 45.02247  ? 667 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? -7.02516  -30.61911 -9.03845  1.000 36.91247  ? 668 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.32772 0.50  26.58715  ? 669 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? 20.87910  -18.19878 -22.43358 1.000 43.58393  ? 670 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? -21.54340 -14.57308 -15.70568 1.000 43.24511  ? 671 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? -4.31592  -27.93464 -23.29928 1.000 39.80223  ? 672 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? 1.66429   -5.86631  -36.52567 1.000 46.87936  ? 673 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? -6.744    -22.978   -1.646    1.000 42.25543  ? 674 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? -12.31555 -12.90898 -0.92307  1.000 30.55920  ? 675 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? -16.39163 -12.76563 -6.30400  1.000 44.47970  ? 676 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? 4.66788   -14.86460 -41.61598 1.000 46.52917  ? 677 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? 20.63175  -6.77805  -16.31648 1.000 43.52251  ? 678 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? -15.88554 -13.30661 -3.81483  1.000 46.93577  ? 679 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? 3.992     -2.025    -28.124   1.000 41.66962  ? 680 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? 3.12303   -2.09071  -20.35241 1.000 43.73952  ? 681 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? 21.90404  -17.95976 -25.04668 1.000 44.45517  ? 682 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? 11.14538  -29.81224 -19.30999 1.000 53.37194  ? 683 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? 4.193     -3.402    -34.003   1.000 50.71339  ? 684 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? -6.78482  -26.75251 -23.26243 1.000 50.74664  ? 685 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? 9.61065   -25.02887 -14.57808 1.000 39.27869  ? 686 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? 0.60707   -1.30104  -16.73974 1.000 33.60018  ? 687 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? 19.22598  -20.50037 -22.24671 1.000 41.37566  ? 688 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? -14.82617 -9.46920  -11.31670 1.000 40.76453  ? 689 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? 20.70581  -20.22067 -26.79141 1.000 43.95499  ? 690 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? -17.05405 -15.51021 -10.27242 1.000 40.94989  ? 691 HOH   A O   1 
HETATM 1949 O O   . HOH   C 3 .   ? -8.66168  -10.73807 0.03057   1.000 42.59409  ? 692 HOH   A O   1 
HETATM 1950 O O   . HOH   C 3 .   ? -14.58575 -14.04915 -10.17663 1.000 30.15333  ? 693 HOH   A O   1 
HETATM 1951 O O   . HOH   C 3 .   ? 14.58829  -12.80960 -2.95457  1.000 43.09059  ? 694 HOH   A O   1 
HETATM 1952 O O   . HOH   C 3 .   ? -2.24317  -26.69350 -28.35527 1.000 52.84882  ? 695 HOH   A O   1 
HETATM 1953 O O   . HOH   C 3 .   ? 9.77055   -12.75525 -37.13350 1.000 45.26243  ? 696 HOH   A O   1 
HETATM 1954 O O   . HOH   C 3 .   ? 13.74048  -11.41909 -5.16811  1.000 41.65601  ? 697 HOH   A O   1 
HETATM 1955 O O   . HOH   C 3 .   ? -18.54412 -1.89761  -30.45016 1.000 55.01154  ? 698 HOH   A O   1 
HETATM 1956 O O   . HOH   C 3 .   ? -10.524   -11.451   2.004     1.000 38.50459  ? 699 HOH   A O   1 
HETATM 1957 O O   . HOH   C 3 .   ? -19.60493 -5.77668  -21.37780 1.000 41.62569  ? 700 HOH   A O   1 
HETATM 1958 O O   . HOH   C 3 .   ? 17.33412  -4.92968  -28.28911 1.000 46.40716  ? 701 HOH   A O   1 
HETATM 1959 O O   . HOH   C 3 .   ? -8.90596  -32.51112 -8.51504  1.000 43.39166  ? 702 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   ? 0.55676 0.75613 0.49885 -0.07730 -0.04281 -0.24695 16  GLU A N   
2    C CA  . GLU A 9   ? 0.64721 0.82624 0.57888 -0.04479 -0.04935 -0.23103 16  GLU A CA  
3    C C   . GLU A 9   ? 0.54280 0.71084 0.48954 -0.02825 -0.05269 -0.20710 16  GLU A C   
4    O O   . GLU A 9   ? 0.50025 0.71836 0.45928 -0.01417 -0.06270 -0.19940 16  GLU A O   
5    C CB  . GLU A 9   ? 0.78182 1.01450 0.70837 -0.01852 -0.06069 -0.22711 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.87991 1.09438 0.79832 0.01919  -0.06460 -0.20337 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.08870 1.23181 0.99397 0.02179  -0.05332 -0.19514 16  GLU A CD  
8    O OE1 . GLU A 9   ? 0.96862 1.07700 0.87825 0.04161  -0.04996 -0.16959 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.08443 1.20915 0.97409 0.00422  -0.04674 -0.21521 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.37681 0.47888 0.32232 -0.02724 -0.04239 -0.19121 17  VAL A N   
11   C CA  . VAL A 10  ? 0.34899 0.43686 0.30959 -0.01800 -0.04279 -0.16934 17  VAL A CA  
12   C C   . VAL A 10  ? 0.40655 0.46203 0.36362 0.00864  -0.04156 -0.14548 17  VAL A C   
13   O O   . VAL A 10  ? 0.39217 0.40706 0.33674 0.01063  -0.03364 -0.14385 17  VAL A O   
14   C CB  . VAL A 10  ? 0.38676 0.43255 0.34916 -0.04120 -0.03059 -0.17248 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.40918 0.44072 0.38481 -0.02911 -0.03155 -0.14918 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.49690 0.57057 0.46241 -0.07304 -0.02758 -0.19906 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.30644 0.37887 0.27341 0.02804  -0.04701 -0.12798 18  GLU A N   
18   C CA  . GLU A 11  ? 0.29485 0.33991 0.26074 0.04843  -0.04351 -0.10784 18  GLU A CA  
19   C C   . GLU A 11  ? 0.28016 0.30135 0.25810 0.04437  -0.03992 -0.09533 18  GLU A C   
20   O O   . GLU A 11  ? 0.26816 0.30642 0.25662 0.03848  -0.04287 -0.09459 18  GLU A O   
21   C CB  . GLU A 11  ? 0.28443 0.35688 0.24822 0.07214  -0.04671 -0.09761 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.30169 0.39678 0.24935 0.08309  -0.04947 -0.10643 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.41840 0.53840 0.35891 0.11152  -0.04922 -0.09345 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.39358 0.54901 0.33815 0.11817  -0.05294 -0.09172 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.49490 0.59722 0.42351 0.12923  -0.04294 -0.08385 18  GLU A OE2 
26   N N   . THR A 12  ? 0.28217 0.26925 0.25809 0.04914  -0.03365 -0.08562 19  THR A N   
27   C CA  . THR A 12  ? 0.27047 0.24209 0.25622 0.04760  -0.03080 -0.07420 19  THR A CA  
28   C C   . THR A 12  ? 0.25485 0.22777 0.24624 0.06210  -0.02933 -0.06094 19  THR A C   
29   O O   . THR A 12  ? 0.26057 0.22562 0.24601 0.07236  -0.02585 -0.05789 19  THR A O   
30   C CB  . THR A 12  ? 0.29055 0.22819 0.26841 0.04269  -0.02275 -0.07361 19  THR A CB  
31   O OG1 . THR A 12  ? 0.32606 0.25442 0.29505 0.02545  -0.01893 -0.08860 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.29313 0.22392 0.27983 0.04414  -0.02076 -0.06113 19  THR A CG2 
33   N N   . PHE A 13  ? 0.24353 0.22468 0.24576 0.06065  -0.02997 -0.05444 20  PHE A N   
34   C CA  . PHE A 13  ? 0.22836 0.21140 0.23568 0.06832  -0.02549 -0.04584 20  PHE A CA  
35   C C   . PHE A 13  ? 0.24920 0.23065 0.26677 0.06175  -0.02441 -0.04105 20  PHE A C   
36   O O   . PHE A 13  ? 0.24598 0.22844 0.26678 0.05362  -0.02773 -0.04214 20  PHE A O   
37   C CB  . PHE A 13  ? 0.22665 0.22255 0.23312 0.07308  -0.02411 -0.04429 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.25528 0.26370 0.25032 0.08444  -0.02553 -0.04737 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.26553 0.29550 0.25928 0.07972  -0.03364 -0.05671 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.28584 0.28836 0.27053 0.10008  -0.01734 -0.04143 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.29285 0.34618 0.27567 0.09188  -0.03616 -0.06082 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.32884 0.34785 0.29971 0.11545  -0.01834 -0.04255 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.29680 0.34493 0.26726 0.11185  -0.02905 -0.05255 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.23894 0.22180 0.26140 0.06477  -0.01900 -0.03665 21  ALA A N   
45   C CA  . ALA A 14  ? 0.20695 0.20053 0.23993 0.05804  -0.01816 -0.03441 21  ALA A CA  
46   C C   . ALA A 14  ? 0.24149 0.23900 0.27756 0.05120  -0.01421 -0.03607 21  ALA A C   
47   O O   . ALA A 14  ? 0.24755 0.23767 0.27828 0.05475  -0.00605 -0.03611 21  ALA A O   
48   C CB  . ALA A 14  ? 0.24146 0.24469 0.28019 0.06118  -0.01325 -0.03229 21  ALA A CB  
49   N N   . PHE A 15  ? 0.19667 0.20218 0.23806 0.04302  -0.01745 -0.03665 22  PHE A N   
50   C CA  . PHE A 15  ? 0.19821 0.20505 0.24104 0.03553  -0.01055 -0.03918 22  PHE A CA  
51   C C   . PHE A 15  ? 0.20542 0.21775 0.25276 0.02930  -0.00046 -0.04284 22  PHE A C   
52   O O   . PHE A 15  ? 0.23168 0.26166 0.28692 0.02846  -0.00304 -0.04337 22  PHE A O   
53   C CB  . PHE A 15  ? 0.21359 0.23107 0.26114 0.02712  -0.01544 -0.04010 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.19437 0.20728 0.23866 0.02862  -0.02151 -0.03836 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.20619 0.21411 0.24529 0.03153  -0.01816 -0.03862 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.19718 0.21146 0.24208 0.02821  -0.02820 -0.03619 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.19963 0.21321 0.23866 0.03137  -0.02368 -0.03874 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.20338 0.21434 0.24629 0.02537  -0.03120 -0.03707 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.20374 0.21914 0.24599 0.02561  -0.03021 -0.03935 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.22345 0.22154 0.26467 0.02464  0.01345  -0.04583 23  GLN A N   
61   C CA  . GLN A 16  ? 0.25639 0.26013 0.30241 0.01022  0.02654  -0.05392 23  GLN A CA  
62   C C   . GLN A 16  ? 0.23000 0.26535 0.28815 -0.00303 0.01889  -0.06049 23  GLN A C   
63   O O   . GLN A 16  ? 0.23646 0.27610 0.29407 -0.00253 0.00981  -0.05852 23  GLN A O   
64   C CB  . GLN A 16  ? 0.28615 0.26003 0.31844 0.00539  0.04733  -0.05681 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.36282 0.30818 0.37979 0.02106  0.05947  -0.04949 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.48507 0.39528 0.48256 0.02149  0.08283  -0.04909 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.47200 0.37373 0.45906 0.03492  0.08076  -0.04211 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.52704 0.41687 0.51866 0.00602  0.10743  -0.05734 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.24494 0.30761 0.31400 -0.01387 0.02274  -0.06840 24  ALA A N   
70   C CA  . ALA A 17  ? 0.23862 0.34443 0.31908 -0.02276 0.01402  -0.07459 24  ALA A CA  
71   C C   . ALA A 17  ? 0.22466 0.32784 0.30058 -0.03578 0.01644  -0.08169 24  ALA A C   
72   O O   . ALA A 17  ? 0.26103 0.38634 0.33918 -0.03296 0.00412  -0.07950 24  ALA A O   
73   C CB  . ALA A 17  ? 0.25139 0.39406 0.34480 -0.03654 0.02150  -0.08624 24  ALA A CB  
74   N N   . GLU A 18  ? 0.27501 0.34678 0.34111 -0.04792 0.03449  -0.08898 25  GLU A N   
75   C CA  . GLU A 18  ? 0.28232 0.34877 0.34168 -0.06135 0.04002  -0.09726 25  GLU A CA  
76   C C   . GLU A 18  ? 0.26019 0.31158 0.31253 -0.04604 0.02849  -0.08507 25  GLU A C   
77   O O   . GLU A 18  ? 0.24656 0.31032 0.29806 -0.05207 0.02369  -0.08854 25  GLU A O   
78   C CB  . GLU A 18  ? 0.36962 0.39586 0.41469 -0.07557 0.06751  -0.10666 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.41286 0.45132 0.46416 -0.09810 0.08454  -0.12300 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.44827 0.47671 0.50208 -0.08748 0.08946  -0.11563 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.39508 0.40865 0.44528 -0.06198 0.07843  -0.09834 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.55636 0.59431 0.61585 -0.10691 0.10567  -0.12912 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.24062 0.26953 0.28811 -0.02738 0.02432  -0.07216 26  ILE A N   
84   C CA  . ILE A 19  ? 0.22580 0.24686 0.26911 -0.01579 0.01438  -0.06297 26  ILE A CA  
85   C C   . ILE A 19  ? 0.21266 0.25992 0.26488 -0.01121 -0.00325 -0.05826 26  ILE A C   
86   O O   . ILE A 19  ? 0.22134 0.27232 0.27212 -0.01066 -0.00941 -0.05558 26  ILE A O   
87   C CB  . ILE A 19  ? 0.23312 0.23084 0.26842 0.00079  0.01631  -0.05386 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.29683 0.26418 0.31622 0.00289  0.03650  -0.05423 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.22946 0.23205 0.26559 0.01070  0.00288  -0.04652 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.40784 0.35785 0.42126 -0.00804 0.05718  -0.06206 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.20330 0.26645 0.26239 -0.00612 -0.00903 -0.05610 27  ALA A N   
92   C CA  . ALA A 20  ? 0.22852 0.31190 0.29074 0.00176  -0.02084 -0.04983 27  ALA A CA  
93   C C   . ALA A 20  ? 0.21742 0.33059 0.28191 -0.00661 -0.02309 -0.05526 27  ALA A C   
94   O O   . ALA A 20  ? 0.25968 0.37828 0.32025 -0.00018 -0.02973 -0.04883 27  ALA A O   
95   C CB  . ALA A 20  ? 0.21144 0.30775 0.27804 0.01140  -0.02340 -0.04604 27  ALA A CB  
96   N N   . GLN A 21  ? 0.21603 0.34792 0.28510 -0.02233 -0.01570 -0.06839 28  GLN A N   
97   C CA  . GLN A 21  ? 0.18927 0.35620 0.25986 -0.03339 -0.01757 -0.07770 28  GLN A CA  
98   C C   . GLN A 21  ? 0.24786 0.39348 0.30890 -0.03803 -0.01553 -0.07810 28  GLN A C   
99   O O   . GLN A 21  ? 0.25576 0.42294 0.31417 -0.03573 -0.02262 -0.07661 28  GLN A O   
100  C CB  . GLN A 21  ? 0.21669 0.40794 0.29391 -0.05555 -0.00693 -0.09670 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.56189 0.78221 0.65109 -0.05374 -0.00711 -0.09865 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.71789 0.95022 0.81331 -0.08069 0.00931  -0.11947 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.53781 0.75612 0.62650 -0.10244 0.02233  -0.13424 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.51760 0.77015 0.62396 -0.07995 0.01188  -0.12095 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.23047 0.33558 0.28449 -0.04199 -0.00463 -0.07906 29  LEU A N   
106  C CA  . LEU A 22  ? 0.23641 0.32097 0.28092 -0.04245 -0.00182 -0.07717 29  LEU A CA  
107  C C   . LEU A 22  ? 0.26322 0.34894 0.30796 -0.02784 -0.01445 -0.06362 29  LEU A C   
108  O O   . LEU A 22  ? 0.23629 0.32898 0.27680 -0.02876 -0.01727 -0.06261 29  LEU A O   
109  C CB  . LEU A 22  ? 0.28733 0.33092 0.32264 -0.04025 0.01215  -0.07565 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.30142 0.32557 0.32720 -0.03476 0.01534  -0.07045 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.31147 0.33898 0.32966 -0.05046 0.02382  -0.08234 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.33677 0.32874 0.35251 -0.02408 0.02789  -0.06493 29  LEU A CD2 
113  N N   . MET A 23  ? 0.22194 0.29771 0.26978 -0.01559 -0.01983 -0.05405 30  MET A N   
114  C CA  . MET A 23  ? 0.22849 0.29943 0.27461 -0.00597 -0.02710 -0.04378 30  MET A CA  
115  C C   . MET A 23  ? 0.23137 0.32549 0.27557 -0.00076 -0.03301 -0.03936 30  MET A C   
116  O O   . MET A 23  ? 0.23511 0.32601 0.27356 0.00222  -0.03416 -0.03372 30  MET A O   
117  C CB  . MET A 23  ? 0.20502 0.25952 0.25249 0.00252  -0.02915 -0.03806 30  MET A CB  
118  C CG  . MET A 23  ? 0.18838 0.22659 0.23496 0.00227  -0.02385 -0.04051 30  MET A CG  
119  S SD  . MET A 23  ? 0.23472 0.26271 0.28194 0.01104  -0.02691 -0.03762 30  MET A SD  
120  C CE  . MET A 23  ? 0.24383 0.26863 0.29029 0.00974  -0.03132 -0.03458 30  MET A CE  
121  N N   . SER A 24  ? 0.22310 0.34325 0.27084 0.00252  -0.03562 -0.04089 31  SER A N   
122  C CA  . SER A 24  ? 0.20926 0.35773 0.25203 0.01343  -0.04051 -0.03444 31  SER A CA  
123  C C   . SER A 24  ? 0.27362 0.44493 0.31293 0.00466  -0.04115 -0.04156 31  SER A C   
124  O O   . SER A 24  ? 0.28645 0.46590 0.31631 0.01520  -0.04346 -0.03295 31  SER A O   
125  C CB  . SER A 24  ? 0.33456 0.51561 0.38227 0.02221  -0.04329 -0.03390 31  SER A CB  
126  O OG  . SER A 24  ? 0.54141 0.75580 0.59870 0.00639  -0.04241 -0.04957 31  SER A OG  
127  N N   . LEU A 25  ? 0.21290 0.38865 0.25630 -0.01433 -0.03641 -0.05703 32  LEU A N   
128  C CA  . LEU A 25  ? 0.22293 0.41679 0.26043 -0.02498 -0.03521 -0.06632 32  LEU A CA  
129  C C   . LEU A 25  ? 0.29385 0.45776 0.32254 -0.02058 -0.03368 -0.05757 32  LEU A C   
130  O O   . LEU A 25  ? 0.25733 0.43713 0.27776 -0.01761 -0.03603 -0.05574 32  LEU A O   
131  C CB  . LEU A 25  ? 0.25098 0.44318 0.29055 -0.04851 -0.02479 -0.08610 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.32758 0.52804 0.35780 -0.06454 -0.01903 -0.10003 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.45501 0.66188 0.48635 -0.09034 -0.00603 -0.12298 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.36869 0.52693 0.38871 -0.06255 -0.01263 -0.09402 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.21523 0.34074 0.24553 -0.01992 -0.02932 -0.05279 33  ILE A N   
136  C CA  . ILE A 26  ? 0.23797 0.34143 0.26303 -0.01718 -0.02710 -0.04587 33  ILE A CA  
137  C C   . ILE A 26  ? 0.27384 0.37800 0.29433 -0.00413 -0.03137 -0.03239 33  ILE A C   
138  O O   . ILE A 26  ? 0.29277 0.39411 0.30592 -0.00229 -0.02958 -0.02765 33  ILE A O   
139  C CB  . ILE A 26  ? 0.21730 0.29202 0.24644 -0.01728 -0.02233 -0.04445 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.25034 0.31483 0.27603 -0.02668 -0.01205 -0.05499 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.22441 0.28662 0.25214 -0.01334 -0.02163 -0.03657 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.28131 0.32243 0.30776 -0.02113 -0.00579 -0.05229 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.24786 0.35165 0.26988 0.00582  -0.03414 -0.02554 34  ILE A N   
144  C CA  . ILE A 27  ? 0.30781 0.39991 0.32042 0.01924  -0.03234 -0.01188 34  ILE A CA  
145  C C   . ILE A 27  ? 0.32124 0.44147 0.32225 0.03167  -0.03407 -0.00574 34  ILE A C   
146  O O   . ILE A 27  ? 0.36238 0.47104 0.35032 0.04125  -0.02895 0.00523  34  ILE A O   
147  C CB  . ILE A 27  ? 0.30952 0.38523 0.32348 0.02674  -0.03131 -0.00691 34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.26456 0.31476 0.28655 0.01620  -0.02925 -0.01200 34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.39053 0.45180 0.38864 0.04367  -0.02491 0.00765  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.29965 0.33854 0.32444 0.01995  -0.02948 -0.01220 34  ILE A CD1 
151  N N   . ASN A 28  ? 0.27973 0.44075 0.28426 0.03218  -0.04011 -0.01298 35  ASN A N   
152  C CA  . ASN A 28  ? 0.29442 0.49482 0.28739 0.04923  -0.04319 -0.00621 35  ASN A CA  
153  C C   . ASN A 28  ? 0.38188 0.61604 0.37064 0.04100  -0.04638 -0.01611 35  ASN A C   
154  O O   . ASN A 28  ? 0.40458 0.67003 0.37972 0.05805  -0.04834 -0.00826 35  ASN A O   
155  C CB  . ASN A 28  ? 0.29531 0.53412 0.29469 0.05782  -0.04834 -0.00807 35  ASN A CB  
156  C CG  . ASN A 28  ? 0.43704 0.64304 0.43555 0.07000  -0.04396 0.00331  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.46230 0.62782 0.44747 0.08134  -0.03597 0.01723  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.48978 0.70669 0.50167 0.06446  -0.04666 -0.00425 35  ASN A ND2 
159  N N   . THR A 29  ? 0.25304 0.48129 0.24973 0.01758  -0.04523 -0.03258 36  THR A N   
160  C CA  . THR A 29  ? 0.27269 0.53040 0.26282 0.00749  -0.04624 -0.04470 36  THR A CA  
161  C C   . THR A 29  ? 0.29457 0.53216 0.27033 0.01621  -0.04253 -0.03321 36  THR A C   
162  O O   . THR A 29  ? 0.33339 0.52596 0.31043 0.01426  -0.03643 -0.02611 36  THR A O   
163  C CB  . THR A 29  ? 0.32715 0.57311 0.32480 -0.01945 -0.04062 -0.06522 36  THR A CB  
164  O OG1 . THR A 29  ? 0.29941 0.56203 0.30938 -0.02875 -0.04119 -0.07604 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.33777 0.61195 0.32583 -0.03269 -0.03930 -0.08091 36  THR A CG2 
166  N N   . PHE A 30  ? 0.26928 0.54488 0.23127 0.02576  -0.04577 -0.03209 37  PHE A N   
167  C CA  . PHE A 30  ? 0.28089 0.53550 0.22832 0.03191  -0.04028 -0.02254 37  PHE A CA  
168  C C   . PHE A 30  ? 0.31833 0.55527 0.26846 0.00866  -0.03556 -0.03811 37  PHE A C   
169  O O   . PHE A 30  ? 0.29997 0.56553 0.24949 -0.00726 -0.03707 -0.05769 37  PHE A O   
170  C CB  . PHE A 30  ? 0.30167 0.60175 0.22998 0.05213  -0.04399 -0.01545 37  PHE A CB  
171  C CG  . PHE A 30  ? 0.31838 0.59726 0.22964 0.05900  -0.03683 -0.00541 37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.42919 0.66170 0.33170 0.07395  -0.02638 0.01604  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.32615 0.63019 0.22863 0.04881  -0.03830 -0.01876 37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.38070 0.59265 0.26777 0.07896  -0.01733 0.02530  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.36239 0.64566 0.24864 0.05603  -0.03070 -0.00863 37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.37372 0.61200 0.25286 0.07162  -0.02020 0.01412  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.27375 0.46499 0.22539 0.00659  -0.02792 -0.03028 38  TYR A N   
178  C CA  . TYR A 31  ? 0.27134 0.44116 0.22494 -0.01040 -0.02108 -0.04165 38  TYR A CA  
179  C C   . TYR A 31  ? 0.27381 0.41066 0.22572 -0.00470 -0.01389 -0.02808 38  TYR A C   
180  O O   . TYR A 31  ? 0.29120 0.40440 0.25366 -0.00264 -0.01198 -0.02004 38  TYR A O   
181  C CB  . TYR A 31  ? 0.25834 0.41187 0.22590 -0.02372 -0.01884 -0.05231 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.31337 0.43977 0.27823 -0.03518 -0.00799 -0.06056 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.33450 0.46947 0.28754 -0.04860 -0.00186 -0.07721 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.37703 0.47174 0.34919 -0.03165 -0.00235 -0.05236 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.43828 0.54322 0.38351 -0.05612 0.01178  -0.08358 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.37581 0.44860 0.34185 -0.03655 0.00966  -0.05772 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.39997 0.47384 0.35115 -0.04785 0.01772  -0.07242 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.56283 0.60928 0.50231 -0.05111 0.03348  -0.07770 38  TYR A OH  
189  N N   . SER A 32  ? 0.28733 0.42590 0.22627 -0.00343 -0.00931 -0.02690 39  SER A N   
190  C CA  . SER A 32  ? 0.29327 0.40781 0.23018 0.00318  -0.00167 -0.01263 39  SER A CA  
191  C C   . SER A 32  ? 0.28303 0.37359 0.23215 -0.00625 0.00514  -0.01547 39  SER A C   
192  O O   . SER A 32  ? 0.31438 0.38941 0.26988 -0.00435 0.01064  -0.00582 39  SER A O   
193  C CB  . SER A 32  ? 0.31366 0.43994 0.23099 0.01034  0.00181  -0.00863 39  SER A CB  
194  O OG  . SER A 32  ? 0.32632 0.47881 0.23073 0.02558  -0.00381 -0.00180 39  SER A OG  
195  N N   . ASN A 33  ? 0.27894 0.36753 0.23007 -0.01569 0.00689  -0.02860 40  ASN A N   
196  C CA  . ASN A 33  ? 0.28491 0.35497 0.24163 -0.01840 0.01570  -0.02958 40  ASN A CA  
197  C C   . ASN A 33  ? 0.29244 0.35436 0.26655 -0.01757 0.01364  -0.02673 40  ASN A C   
198  O O   . ASN A 33  ? 0.27620 0.32942 0.25286 -0.01913 0.01729  -0.03273 40  ASN A O   
199  C CB  . ASN A 33  ? 0.33707 0.40142 0.28127 -0.02602 0.02321  -0.04378 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.37102 0.41430 0.31436 -0.02310 0.03592  -0.04304 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.38306 0.42634 0.33192 -0.01585 0.03907  -0.03304 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.38502 0.41081 0.31926 -0.02822 0.04573  -0.05396 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.27110 0.27667 0.21330 0.00730  -0.03476 -0.01852 41  LYS A N   
204  C CA  . LYS A 34  ? 0.23772 0.26950 0.21251 0.00943  -0.02644 -0.01806 41  LYS A CA  
205  C C   . LYS A 34  ? 0.25101 0.26997 0.22658 0.01052  -0.01437 -0.02411 41  LYS A C   
206  O O   . LYS A 34  ? 0.22074 0.25540 0.21684 0.00948  -0.01125 -0.02486 41  LYS A O   
207  C CB  . LYS A 34  ? 0.25412 0.29735 0.24091 0.02179  -0.02044 -0.01521 41  LYS A CB  
208  C CG  . LYS A 34  ? 0.23995 0.30502 0.23306 0.02551  -0.03073 -0.00709 41  LYS A CG  
209  C CD  . LYS A 34  ? 0.29186 0.35670 0.28840 0.04156  -0.02442 -0.00602 41  LYS A CD  
210  C CE  . LYS A 34  ? 0.27276 0.36201 0.27634 0.05101  -0.03249 0.00320  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.22260 0.35143 0.25092 0.05598  -0.03253 0.01024  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.26528 0.25822 0.21850 0.01485  -0.00684 -0.02668 42  GLU A N   
213  C CA  . GLU A 35  ? 0.25370 0.24189 0.21387 0.01855  0.00609  -0.02836 42  GLU A CA  
214  C C   . GLU A 35  ? 0.30409 0.29220 0.26811 0.01149  0.00234  -0.03268 42  GLU A C   
215  O O   . GLU A 35  ? 0.26556 0.25669 0.24277 0.01375  0.01086  -0.03336 42  GLU A O   
216  C CB  . GLU A 35  ? 0.30250 0.26851 0.23687 0.02860  0.01714  -0.02629 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.33156 0.26670 0.22513 0.03032  0.01065  -0.03180 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.46578 0.37634 0.32338 0.04816  0.02446  -0.02869 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.49430 0.41176 0.35303 0.05458  0.03246  -0.02103 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.55606 0.43832 0.38025 0.05771  0.02728  -0.03293 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.27328 0.25762 0.22687 0.00136  -0.01226 -0.03346 43  ILE A N   
222  C CA  . ILE A 36  ? 0.25795 0.23887 0.21335 -0.00739 -0.01750 -0.03529 43  ILE A CA  
223  C C   . ILE A 36  ? 0.24070 0.25246 0.23016 -0.00906 -0.01284 -0.03296 43  ILE A C   
224  O O   . ILE A 36  ? 0.23263 0.24173 0.22501 -0.01395 -0.01340 -0.03407 43  ILE A O   
225  C CB  . ILE A 36  ? 0.31800 0.28660 0.25621 -0.02254 -0.03885 -0.03254 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.32528 0.33054 0.28921 -0.03098 -0.04916 -0.02228 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.36991 0.29232 0.25940 -0.01778 -0.04560 -0.03784 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.31328 0.35620 0.31203 -0.03840 -0.04910 -0.01379 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.20522 0.24037 0.21416 -0.00285 -0.00881 -0.03009 44  PHE A N   
230  C CA  . PHE A 37  ? 0.20323 0.25790 0.23264 0.00045  -0.00442 -0.02940 44  PHE A CA  
231  C C   . PHE A 37  ? 0.21250 0.25300 0.24289 0.00244  0.00279  -0.03444 44  PHE A C   
232  O O   . PHE A 37  ? 0.19332 0.24097 0.23201 0.00090  0.00311  -0.03477 44  PHE A O   
233  C CB  . PHE A 37  ? 0.16472 0.23178 0.20230 0.01239  -0.00167 -0.02786 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.19330 0.24055 0.22784 0.01841  0.00358  -0.03155 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.21983 0.25454 0.24509 0.01929  0.00508  -0.02974 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.22023 0.26103 0.26103 0.02126  0.00522  -0.03424 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.21635 0.23806 0.24445 0.02164  0.00950  -0.02731 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.19323 0.21791 0.23646 0.02151  0.00582  -0.03285 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.20084 0.21885 0.24062 0.02097  0.00865  -0.02775 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.18818 0.21231 0.21201 0.00674  0.00903  -0.03571 45  LEU A N   
241  C CA  . LEU A 38  ? 0.18919 0.20899 0.22234 0.00909  0.01509  -0.03594 45  LEU A CA  
242  C C   . LEU A 38  ? 0.22160 0.23123 0.24534 0.00636  0.01533  -0.03830 45  LEU A C   
243  O O   . LEU A 38  ? 0.20269 0.21515 0.23658 0.00569  0.01594  -0.03888 45  LEU A O   
244  C CB  . LEU A 38  ? 0.18371 0.19815 0.21883 0.01457  0.02292  -0.03036 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.18273 0.20126 0.23652 0.01565  0.02762  -0.02470 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.17939 0.20167 0.24772 0.01127  0.01839  -0.02642 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.25348 0.27602 0.31546 0.01959  0.03576  -0.01254 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.23039 0.22226 0.22952 0.00511  0.01228  -0.03991 46  ARG A N   
249  C CA  . ARG A 39  ? 0.23335 0.20491 0.21473 0.00261  0.00851  -0.04275 46  ARG A CA  
250  C C   . ARG A 39  ? 0.24577 0.23054 0.24048 -0.00919 -0.00000 -0.04148 46  ARG A C   
251  O O   . ARG A 39  ? 0.23765 0.21545 0.23230 -0.00997 0.00034  -0.04230 46  ARG A O   
252  C CB  . ARG A 39  ? 0.28757 0.22786 0.23131 0.00191  0.00023  -0.04530 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.35429 0.26344 0.27204 -0.00390 -0.01077 -0.04830 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.39933 0.26865 0.27269 -0.00686 -0.02586 -0.05119 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.46267 0.34768 0.34833 -0.02782 -0.04474 -0.04517 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.51326 0.37598 0.37199 -0.03535 -0.06224 -0.04443 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.52385 0.33840 0.33169 -0.02235 -0.06412 -0.05195 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.50387 0.39394 0.38581 -0.05485 -0.07862 -0.03421 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.21597 0.22307 0.22307 -0.01646 -0.00636 -0.03712 47  GLU A N   
260  C CA  . GLU A 40  ? 0.18502 0.21163 0.20575 -0.02598 -0.01209 -0.03091 47  GLU A CA  
261  C C   . GLU A 40  ? 0.20238 0.24223 0.23850 -0.01815 -0.00348 -0.03229 47  GLU A C   
262  O O   . GLU A 40  ? 0.20180 0.24443 0.24066 -0.02268 -0.00492 -0.02947 47  GLU A O   
263  C CB  . GLU A 40  ? 0.17965 0.23575 0.21365 -0.03135 -0.01828 -0.02142 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.23743 0.27986 0.25622 -0.04374 -0.03336 -0.01761 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.34285 0.35171 0.33932 -0.05776 -0.04680 -0.01763 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.31616 0.33211 0.32221 -0.06527 -0.04825 -0.01221 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.39249 0.36258 0.35624 -0.05978 -0.05682 -0.02309 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.18372 0.22791 0.22689 -0.00732 0.00290  -0.03573 48  LEU A N   
269  C CA  . LEU A 41  ? 0.16225 0.20997 0.21294 -0.00081 0.00571  -0.03756 48  LEU A CA  
270  C C   . LEU A 41  ? 0.18417 0.21612 0.23450 -0.00138 0.00708  -0.04017 48  LEU A C   
271  O O   . LEU A 41  ? 0.20039 0.23301 0.25308 -0.00063 0.00585  -0.04030 48  LEU A O   
272  C CB  . LEU A 41  ? 0.17223 0.21927 0.22544 0.00879  0.00637  -0.03978 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.18117 0.24512 0.23286 0.01536  0.00620  -0.03656 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.19188 0.24276 0.23819 0.02580  0.00433  -0.03986 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.17696 0.26109 0.22868 0.02157  0.00827  -0.03151 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.16894 0.18800 0.21534 0.00022  0.01057  -0.04076 49  ILE A N   
277  C CA  . ILE A 42  ? 0.17665 0.18584 0.22420 0.00354  0.01370  -0.04020 49  ILE A CA  
278  C C   . ILE A 42  ? 0.21063 0.20791 0.24454 -0.00124 0.00988  -0.04132 49  ILE A C   
279  O O   . ILE A 42  ? 0.21168 0.20520 0.24865 0.00061  0.00971  -0.04076 49  ILE A O   
280  C CB  . ILE A 42  ? 0.19685 0.19897 0.24061 0.01161  0.02196  -0.03719 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.16226 0.17846 0.22668 0.01286  0.02360  -0.03164 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.23235 0.22467 0.27182 0.02043  0.02779  -0.03456 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.19058 0.20759 0.25427 0.02147  0.03464  -0.02361 49  ILE A CD1 
284  N N   . SER A 43  ? 0.19404 0.18304 0.21227 -0.00901 0.00410  -0.04130 50  SER A N   
285  C CA  . SER A 43  ? 0.22625 0.19891 0.23015 -0.01755 -0.00378 -0.03981 50  SER A CA  
286  C C   . SER A 43  ? 0.21675 0.21052 0.23630 -0.02330 -0.00542 -0.03482 50  SER A C   
287  O O   . SER A 43  ? 0.22780 0.21085 0.24241 -0.02511 -0.00762 -0.03350 50  SER A O   
288  C CB  . SER A 43  ? 0.27719 0.23496 0.26197 -0.02898 -0.01533 -0.03785 50  SER A CB  
289  O OG  . SER A 43  ? 0.34173 0.28404 0.31550 -0.04241 -0.02742 -0.03293 50  SER A OG  
290  N N   . ASN A 44  ? 0.19650 0.21861 0.23126 -0.02256 -0.00319 -0.03159 51  ASN A N   
291  C CA  . ASN A 44  ? 0.20502 0.24626 0.24787 -0.02151 -0.00165 -0.02626 51  ASN A CA  
292  C C   . ASN A 44  ? 0.20190 0.23289 0.24449 -0.01265 0.00068  -0.03181 51  ASN A C   
293  O O   . ASN A 44  ? 0.18725 0.21841 0.22690 -0.01344 -0.00035 -0.02845 51  ASN A O   
294  C CB  . ASN A 44  ? 0.17091 0.23914 0.22233 -0.01399 0.00246  -0.02282 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.28654 0.37736 0.34549 -0.02346 -0.00083 -0.01119 51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.24903 0.33151 0.30530 -0.03951 -0.00984 -0.00551 51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.25799 0.37535 0.32471 -0.01331 0.00422  -0.00624 51  ASN A ND2 
298  N N   . SER A 45  ? 0.15932 0.18331 0.20648 -0.00535 0.00233  -0.03772 52  SER A N   
299  C CA  . SER A 45  ? 0.18272 0.19902 0.23429 -0.00008 0.00028  -0.03965 52  SER A CA  
300  C C   . SER A 45  ? 0.21824 0.22148 0.26602 -0.00166 0.00002  -0.03822 52  SER A C   
301  O O   . SER A 45  ? 0.19730 0.19715 0.24435 -0.00022 -0.00338 -0.03711 52  SER A O   
302  C CB  . SER A 45  ? 0.19499 0.21004 0.25844 0.00376  -0.00004 -0.04049 52  SER A CB  
303  O OG  . SER A 45  ? 0.20179 0.21977 0.26354 0.00670  -0.00323 -0.04252 52  SER A OG  
304  N N   . SER A 46  ? 0.19728 0.18809 0.23707 -0.00209 0.00283  -0.03852 53  SER A N   
305  C CA  . SER A 46  ? 0.20870 0.17916 0.23648 0.00087  0.00226  -0.03779 53  SER A CA  
306  C C   . SER A 46  ? 0.22800 0.19175 0.24523 -0.00860 -0.00445 -0.03488 53  SER A C   
307  O O   . SER A 46  ? 0.24515 0.19934 0.25912 -0.00556 -0.00648 -0.03334 53  SER A O   
308  C CB  . SER A 46  ? 0.24097 0.18920 0.24848 0.00554  0.00506  -0.03991 53  SER A CB  
309  O OG  . SER A 46  ? 0.28232 0.20143 0.26823 0.01232  0.00358  -0.04014 53  SER A OG  
310  N N   . ASP A 47  ? 0.21582 0.18828 0.23043 -0.02033 -0.00807 -0.03106 54  ASP A N   
311  C CA  . ASP A 47  ? 0.21911 0.19333 0.22928 -0.03126 -0.01359 -0.02248 54  ASP A CA  
312  C C   . ASP A 47  ? 0.23534 0.22455 0.25279 -0.02452 -0.01020 -0.02068 54  ASP A C   
313  O O   . ASP A 47  ? 0.23511 0.21541 0.24501 -0.02749 -0.01340 -0.01558 54  ASP A O   
314  C CB  . ASP A 47  ? 0.21152 0.20689 0.22801 -0.04420 -0.01675 -0.01308 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.32285 0.29381 0.32440 -0.05616 -0.02755 -0.01253 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.34053 0.33014 0.35056 -0.06792 -0.03296 -0.00375 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.34424 0.27525 0.32231 -0.05210 -0.03175 -0.02009 54  ASP A OD2 
318  N N   . ALA A 48  ? 0.20883 0.21488 0.23546 -0.01504 -0.00581 -0.02478 55  ALA A N   
319  C CA  . ALA A 48  ? 0.21765 0.22850 0.24098 -0.00651 -0.00593 -0.02474 55  ALA A CA  
320  C C   . ALA A 48  ? 0.21571 0.20864 0.23872 -0.00219 -0.01110 -0.02840 55  ALA A C   
321  O O   . ALA A 48  ? 0.21104 0.19928 0.22542 0.00080  -0.01450 -0.02605 55  ALA A O   
322  C CB  . ALA A 48  ? 0.18207 0.20278 0.20620 0.00355  -0.00428 -0.02953 55  ALA A CB  
323  N N   . LEU A 49  ? 0.18828 0.17434 0.22151 0.00006  -0.01120 -0.03209 56  LEU A N   
324  C CA  . LEU A 49  ? 0.20307 0.17998 0.24222 0.00564  -0.01488 -0.03107 56  LEU A CA  
325  C C   . LEU A 49  ? 0.22597 0.18540 0.25100 0.00443  -0.01556 -0.02787 56  LEU A C   
326  O O   . LEU A 49  ? 0.24034 0.19350 0.26340 0.00820  -0.02049 -0.02524 56  LEU A O   
327  C CB  . LEU A 49  ? 0.20195 0.18367 0.25765 0.01080  -0.01094 -0.03068 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.20327 0.19775 0.27423 0.00990  -0.01532 -0.03110 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.20365 0.20665 0.28852 0.01237  -0.00749 -0.02829 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.17893 0.17464 0.26255 0.01092  -0.02767 -0.02667 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.22513 0.17178 0.23688 -0.00163 -0.01368 -0.02749 57  ASP A N   
332  C CA  . ASP A 50  ? 0.25074 0.17136 0.24272 -0.00498 -0.01849 -0.02383 57  ASP A CA  
333  C C   . ASP A 50  ? 0.29148 0.21811 0.27983 -0.01170 -0.02241 -0.01701 57  ASP A C   
334  O O   . ASP A 50  ? 0.27477 0.18333 0.25211 -0.00979 -0.02692 -0.01363 57  ASP A O   
335  C CB  . ASP A 50  ? 0.27314 0.17327 0.24656 -0.01595 -0.02247 -0.02291 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.36283 0.24456 0.32558 -0.00575 -0.01912 -0.02968 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.35711 0.24418 0.32894 0.01120  -0.01121 -0.03223 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.35596 0.21749 0.29971 -0.01469 -0.02532 -0.03029 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.24126 0.19272 0.23565 -0.01731 -0.01960 -0.01332 58  LYS A N   
340  C CA  . LYS A 51  ? 0.25044 0.21043 0.23754 -0.02015 -0.01995 -0.00380 58  LYS A CA  
341  C C   . LYS A 51  ? 0.25421 0.20868 0.23683 -0.00815 -0.02288 -0.00727 58  LYS A C   
342  O O   . LYS A 51  ? 0.28884 0.23291 0.25931 -0.00897 -0.02621 -0.00067 58  LYS A O   
343  C CB  . LYS A 51  ? 0.24508 0.23679 0.23763 -0.02143 -0.01285 0.00283  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.24073 0.24235 0.24135 -0.03670 -0.01342 0.01095  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.22872 0.27083 0.23957 -0.03372 -0.00428 0.02100  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.35710 0.41422 0.38208 -0.04909 -0.00741 0.02953  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.42140 0.52347 0.45979 -0.04196 0.00305  0.04132  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.24163 0.20119 0.23286 0.00137  -0.02436 -0.01586 59  ILE A N   
349  C CA  . ILE A 52  ? 0.25164 0.20299 0.23751 0.00984  -0.03278 -0.01748 59  ILE A CA  
350  C C   . ILE A 52  ? 0.27148 0.20874 0.26386 0.01179  -0.03793 -0.01590 59  ILE A C   
351  O O   . ILE A 52  ? 0.27406 0.20149 0.25737 0.01562  -0.04506 -0.01259 59  ILE A O   
352  C CB  . ILE A 52  ? 0.26231 0.21704 0.25325 0.01615  -0.03915 -0.02456 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.29087 0.23105 0.26794 0.02276  -0.05352 -0.02515 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.22876 0.18915 0.24586 0.01435  -0.03983 -0.02703 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.32959 0.26278 0.27337 0.02923  -0.05133 -0.02176 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.25655 0.19112 0.26041 0.01222  -0.03375 -0.01731 60  ARG A N   
357  C CA  . ARG A 53  ? 0.26596 0.18584 0.27026 0.02012  -0.03588 -0.01420 60  ARG A CA  
358  C C   . ARG A 53  ? 0.30655 0.20273 0.28648 0.01625  -0.03871 -0.00939 60  ARG A C   
359  O O   . ARG A 53  ? 0.32857 0.21427 0.30375 0.02304  -0.04470 -0.00547 60  ARG A O   
360  C CB  . ARG A 53  ? 0.28875 0.20534 0.29931 0.02675  -0.02816 -0.01601 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.39668 0.30025 0.40571 0.04240  -0.02826 -0.01123 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.55255 0.44672 0.55647 0.05593  -0.01828 -0.01204 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.61909 0.54549 0.65614 0.06824  -0.01182 -0.00539 60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.60414 0.54182 0.64865 0.07250  -0.00167 -0.00581 60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.51742 0.43346 0.53598 0.06672  0.00177  -0.01465 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.43805 0.41029 0.51745 0.08226  0.00410  0.00547  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.30031 0.18903 0.26611 0.00357  -0.03655 -0.00703 61  TYR A N   
368  C CA  . TYR A 54  ? 0.32992 0.19517 0.27405 -0.00442 -0.04189 0.00141  61  TYR A CA  
369  C C   . TYR A 54  ? 0.33446 0.20825 0.27364 -0.00329 -0.04452 0.00789  61  TYR A C   
370  O O   . TYR A 54  ? 0.36330 0.21588 0.28800 -0.00113 -0.05056 0.01345  61  TYR A O   
371  C CB  . TYR A 54  ? 0.33790 0.20066 0.27471 -0.02306 -0.04248 0.00782  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.38763 0.22213 0.30313 -0.03551 -0.05167 0.01997  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.41278 0.19930 0.30386 -0.03270 -0.06091 0.01769  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.39202 0.24551 0.30852 -0.04753 -0.05097 0.03530  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.45354 0.20715 0.32166 -0.04530 -0.07260 0.02967  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.43887 0.26797 0.33819 -0.06120 -0.06035 0.05015  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.47608 0.25305 0.35131 -0.06189 -0.07280 0.04686  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.51770 0.26401 0.37277 -0.07747 -0.08524 0.06261  61  TYR A OH  
379  N N   . GLU A 55  ? 0.31794 0.21805 0.26262 -0.00276 -0.04028 0.00762  62  GLU A N   
380  C CA  . GLU A 55  ? 0.34618 0.24869 0.27622 0.00251  -0.04260 0.01307  62  GLU A CA  
381  C C   . GLU A 55  ? 0.38300 0.27179 0.31287 0.01393  -0.05309 0.00853  62  GLU A C   
382  O O   . GLU A 55  ? 0.41231 0.28837 0.32531 0.01703  -0.05875 0.01474  62  GLU A O   
383  C CB  . GLU A 55  ? 0.34877 0.27405 0.27572 0.00798  -0.03650 0.01125  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.40068 0.34766 0.32805 -0.00097 -0.02531 0.02303  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.56423 0.53255 0.47894 0.01228  -0.01641 0.02497  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.55559 0.51124 0.45440 0.02720  -0.02241 0.01422  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.55496 0.55106 0.47340 0.00904  -0.00475 0.03864  62  GLU A OE2 
388  N N   . SER A 56  ? 0.32707 0.22118 0.27788 0.01981  -0.05640 0.00062  63  SER A N   
389  C CA  . SER A 56  ? 0.35849 0.24868 0.31793 0.02916  -0.06831 0.00093  63  SER A CA  
390  C C   . SER A 56  ? 0.36848 0.24058 0.32409 0.03454  -0.07021 0.00685  63  SER A C   
391  O O   . SER A 56  ? 0.37520 0.24447 0.33485 0.04292  -0.08066 0.01087  63  SER A O   
392  C CB  . SER A 56  ? 0.34081 0.24879 0.33072 0.03199  -0.07083 -0.00301 63  SER A CB  
393  O OG  . SER A 56  ? 0.36912 0.27940 0.37444 0.03597  -0.06158 -0.00194 63  SER A OG  
394  N N   . LEU A 57  ? 0.36376 0.21942 0.30852 0.03046  -0.06290 0.00811  64  LEU A N   
395  C CA  . LEU A 57  ? 0.44410 0.27285 0.37738 0.03939  -0.06602 0.01241  64  LEU A CA  
396  C C   . LEU A 57  ? 0.47078 0.28325 0.38350 0.03858  -0.07441 0.02015  64  LEU A C   
397  O O   . LEU A 57  ? 0.51670 0.31109 0.42318 0.05043  -0.08031 0.02432  64  LEU A O   
398  C CB  . LEU A 57  ? 0.43980 0.24085 0.35420 0.03371  -0.06162 0.01139  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.41852 0.22914 0.34663 0.03890  -0.05328 0.00384  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.49599 0.26624 0.39393 0.03405  -0.05434 0.00239  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.46836 0.29329 0.41771 0.06065  -0.04990 0.00410  64  LEU A CD2 
402  N N   . THR A 58  ? 0.44241 0.26081 0.34209 0.02698  -0.07357 0.02396  65  THR A N   
403  C CA  . THR A 58  ? 0.45684 0.26091 0.33355 0.02674  -0.07983 0.03342  65  THR A CA  
404  C C   . THR A 58  ? 0.57473 0.39376 0.44754 0.03311  -0.08532 0.03199  65  THR A C   
405  O O   . THR A 58  ? 0.58151 0.38724 0.43417 0.03759  -0.09284 0.03860  65  THR A O   
406  C CB  . THR A 58  ? 0.62349 0.41910 0.48138 0.01006  -0.07474 0.04517  65  THR A CB  
407  O OG1 . THR A 58  ? 0.58784 0.41357 0.45370 0.00232  -0.06470 0.04555  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.56557 0.33100 0.41707 0.00190  -0.07709 0.04687  65  THR A CG2 
409  N N   . ASP A 59  ? 0.58784 0.40159 0.38282 0.04899  -0.07017 0.07295  66  ASP A N   
410  C CA  . ASP A 59  ? 0.53744 0.38791 0.34448 0.05621  -0.07364 0.06984  66  ASP A CA  
411  C C   . ASP A 59  ? 0.46928 0.34439 0.30367 0.06300  -0.07724 0.05686  66  ASP A C   
412  O O   . ASP A 59  ? 0.43977 0.33184 0.28905 0.05399  -0.07461 0.04857  66  ASP A O   
413  C CB  . ASP A 59  ? 0.52020 0.38908 0.32505 0.04369  -0.06836 0.07434  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.58475 0.47722 0.38634 0.05444  -0.07141 0.06960  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.60648 0.50124 0.40965 0.06624  -0.08203 0.06346  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.59473 0.50147 0.38934 0.05181  -0.06382 0.07393  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.55263 0.43276 0.39673 0.07863  -0.08337 0.05783  67  PRO A N   
418  C CA  . PRO A 60  ? 0.49739 0.40489 0.37285 0.08225  -0.08751 0.05051  67  PRO A CA  
419  C C   . PRO A 60  ? 0.43764 0.36910 0.32067 0.07407  -0.09630 0.04205  67  PRO A C   
420  O O   . PRO A 60  ? 0.44706 0.39614 0.35335 0.07008  -0.09863 0.03482  67  PRO A O   
421  C CB  . PRO A 60  ? 0.54828 0.46492 0.43462 0.10062  -0.09427 0.06094  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.71940 0.60757 0.57627 0.10851  -0.09231 0.07099  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.66770 0.52719 0.49728 0.09373  -0.08450 0.06905  67  PRO A CD  
424  N N   . SER A 61  ? 0.45787 0.38559 0.31658 0.07325  -0.10098 0.04343  68  SER A N   
425  C CA  . SER A 61  ? 0.43052 0.36781 0.28236 0.06958  -0.10903 0.03450  68  SER A CA  
426  C C   . SER A 61  ? 0.46774 0.40908 0.32533 0.06080  -0.09770 0.02620  68  SER A C   
427  O O   . SER A 61  ? 0.43671 0.38169 0.28981 0.05944  -0.10322 0.01716  68  SER A O   
428  C CB  . SER A 61  ? 0.51942 0.44460 0.33310 0.07516  -0.11276 0.03841  68  SER A CB  
429  O OG  . SER A 61  ? 0.55466 0.47266 0.35200 0.07307  -0.09557 0.04470  68  SER A OG  
430  N N   . LYS A 62  ? 0.37885 0.31622 0.24369 0.05432  -0.08400 0.02981  69  LYS A N   
431  C CA  . LYS A 62  ? 0.34735 0.29343 0.22224 0.04557  -0.07503 0.02467  69  LYS A CA  
432  C C   . LYS A 62  ? 0.38615 0.34305 0.28533 0.04393  -0.08011 0.01389  69  LYS A C   
433  O O   . LYS A 62  ? 0.34865 0.31325 0.25445 0.03893  -0.07517 0.00804  69  LYS A O   
434  C CB  . LYS A 62  ? 0.41294 0.34969 0.29034 0.03508  -0.06549 0.03266  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.51734 0.44586 0.37434 0.03188  -0.06085 0.04747  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.50150 0.44918 0.36190 0.02358  -0.05090 0.05558  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.53693 0.48675 0.38123 0.02186  -0.04455 0.07471  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.58719 0.56490 0.44577 0.01278  -0.03366 0.08787  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.35959 0.32016 0.27477 0.04875  -0.08863 0.01435  70  LEU A N   
440  C CA  . LEU A 63  ? 0.33831 0.31408 0.28066 0.04635  -0.09322 0.00884  70  LEU A CA  
441  C C   . LEU A 63  ? 0.33032 0.31479 0.27439 0.04545  -0.11176 0.00640  70  LEU A C   
442  O O   . LEU A 63  ? 0.36188 0.36186 0.33229 0.04115  -0.11951 0.00623  70  LEU A O   
443  C CB  . LEU A 63  ? 0.35507 0.33458 0.31830 0.05322  -0.08838 0.01548  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.35084 0.30819 0.30212 0.05204  -0.07354 0.01573  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.36183 0.31223 0.32050 0.06561  -0.06661 0.02201  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.36641 0.32670 0.32242 0.03999  -0.06793 0.00754  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.35083 0.32280 0.26409 0.04803  -0.12033 0.00562  71  ASP A N   
448  C CA  . ASP A 64  ? 0.42459 0.39323 0.32818 0.04419  -0.14271 0.00196  71  ASP A CA  
449  C C   . ASP A 64  ? 0.41467 0.37710 0.31699 0.03639  -0.14500 -0.00913 71  ASP A C   
450  O O   . ASP A 64  ? 0.41864 0.37785 0.32232 0.02780  -0.16631 -0.01105 71  ASP A O   
451  C CB  . ASP A 64  ? 0.45776 0.40372 0.31485 0.05070  -0.15036 0.00144  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.55289 0.50409 0.41069 0.05716  -0.15669 0.01380  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.55148 0.52383 0.44587 0.05840  -0.15635 0.02331  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.59028 0.52312 0.40914 0.06377  -0.16043 0.01522  71  ASP A OD2 
455  N N   . SER A 65  ? 0.35614 0.31554 0.25465 0.03806  -0.12546 -0.01450 72  SER A N   
456  C CA  . SER A 65  ? 0.33937 0.29223 0.23603 0.03395  -0.12364 -0.02377 72  SER A CA  
457  C C   . SER A 65  ? 0.41159 0.38487 0.35108 0.02518  -0.12205 -0.02258 72  SER A C   
458  O O   . SER A 65  ? 0.43316 0.40318 0.37551 0.02158  -0.11793 -0.02890 72  SER A O   
459  C CB  . SER A 65  ? 0.40779 0.35667 0.28653 0.04172  -0.10193 -0.02487 72  SER A CB  
460  O OG  . SER A 65  ? 0.35690 0.32250 0.25577 0.04016  -0.08747 -0.01585 72  SER A OG  
461  N N   . GLY A 66  ? 0.36051 0.35385 0.33070 0.02490  -0.12248 -0.01311 73  GLY A N   
462  C CA  . GLY A 66  ? 0.39453 0.40772 0.40230 0.02063  -0.11845 -0.00929 73  GLY A CA  
463  C C   . GLY A 66  ? 0.33984 0.36287 0.36345 0.02939  -0.10418 -0.00060 73  GLY A C   
464  O O   . GLY A 66  ? 0.30816 0.31759 0.31579 0.03230  -0.09010 -0.00317 73  GLY A O   
465  N N   . LYS A 67  ? 0.29381 0.33858 0.34673 0.03416  -0.10768 0.01180  74  LYS A N   
466  C CA  . LYS A 67  ? 0.24321 0.28783 0.30046 0.04876  -0.09216 0.02042  74  LYS A CA  
467  C C   . LYS A 67  ? 0.26056 0.30361 0.32661 0.05179  -0.07514 0.01910  74  LYS A C   
468  O O   . LYS A 67  ? 0.34747 0.37049 0.39682 0.06283  -0.06096 0.02059  74  LYS A O   
469  C CB  . LYS A 67  ? 0.28826 0.36008 0.37247 0.05942  -0.09935 0.03879  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.45790 0.52922 0.53003 0.05861  -0.11734 0.04271  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.69749 0.76723 0.76531 0.07796  -0.11039 0.05562  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.78498 0.84322 0.82764 0.07653  -0.12574 0.05575  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.72752 0.74966 0.73103 0.08409  -0.11306 0.05078  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.23528 0.29291 0.32125 0.04235  -0.07739 0.01659  75  GLU A N   
475  C CA  . GLU A 68  ? 0.29017 0.34897 0.38528 0.04651  -0.06180 0.01754  75  GLU A CA  
476  C C   . GLU A 68  ? 0.24977 0.27894 0.31478 0.04063  -0.05311 0.00405  75  GLU A C   
477  O O   . GLU A 68  ? 0.28626 0.31016 0.34111 0.02919  -0.05963 -0.00500 75  GLU A O   
478  C CB  . GLU A 68  ? 0.29809 0.38260 0.42493 0.03614  -0.06882 0.02136  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.41849 0.54238 0.58676 0.04060  -0.07491 0.04267  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.99325 1.14155 1.19444 0.02886  -0.07850 0.05021  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.89758 1.07537 1.12970 0.03976  -0.06593 0.06880  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.81973 0.95533 1.01290 0.01051  -0.09244 0.03884  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.22734 0.23682 0.27666 0.04912  -0.03900 0.00468  76  LEU A N   
484  C CA  . LEU A 69  ? 0.23653 0.21767 0.25737 0.04020  -0.03474 -0.00442 76  LEU A CA  
485  C C   . LEU A 69  ? 0.22565 0.20645 0.25099 0.04128  -0.02572 -0.00539 76  LEU A C   
486  O O   . LEU A 69  ? 0.24915 0.21656 0.26437 0.05645  -0.01412 -0.00005 76  LEU A O   
487  C CB  . LEU A 69  ? 0.25867 0.20287 0.24404 0.04626  -0.03093 -0.00275 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.31725 0.26020 0.29584 0.04577  -0.03885 0.00008  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.41120 0.30972 0.35000 0.04657  -0.03633 0.00174  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.30465 0.26368 0.28917 0.03070  -0.04751 -0.00459 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.22120 0.21479 0.25853 0.02869  -0.02940 -0.01095 77  HIS A N   
492  C CA  . HIS A 70  ? 0.21159 0.20811 0.25582 0.03004  -0.02137 -0.01033 77  HIS A CA  
493  C C   . HIS A 70  ? 0.19383 0.19066 0.23589 0.01564  -0.02534 -0.01753 77  HIS A C   
494  O O   . HIS A 70  ? 0.19681 0.19711 0.23653 0.00711  -0.03273 -0.02124 77  HIS A O   
495  C CB  . HIS A 70  ? 0.22289 0.25195 0.30408 0.03525  -0.02074 -0.00105 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.19023 0.23876 0.29223 0.02242  -0.03600 -0.00321 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.27727 0.34588 0.40051 0.02263  -0.04672 0.00497  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.24504 0.29075 0.34429 0.01040  -0.04316 -0.01175 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.25973 0.32969 0.38593 0.00946  -0.06182 -0.00051 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.25603 0.31122 0.36695 0.00410  -0.05812 -0.01081 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.19698 0.19189 0.23959 0.01600  -0.01857 -0.01723 78  ILE A N   
502  C CA  . ILE A 71  ? 0.16773 0.16462 0.20985 0.00519  -0.02089 -0.02135 78  ILE A CA  
503  C C   . ILE A 71  ? 0.20202 0.21632 0.26788 0.00699  -0.01707 -0.01823 78  ILE A C   
504  O O   . ILE A 71  ? 0.18546 0.19972 0.25387 0.01665  -0.00724 -0.01194 78  ILE A O   
505  C CB  . ILE A 71  ? 0.20358 0.17311 0.21429 0.00085  -0.01910 -0.02248 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.21012 0.15829 0.19615 -0.00477 -0.02531 -0.02238 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.23265 0.21183 0.24867 -0.00951 -0.02222 -0.02321 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.26176 0.17097 0.20774 -0.01262 -0.02888 -0.02215 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.17027 0.19654 0.25006 -0.00065 -0.02369 -0.02091 79  ASN A N   
510  C CA  . ASN A 72  ? 0.15736 0.19481 0.25685 -0.00263 -0.02258 -0.01712 79  ASN A CA  
511  C C   . ASN A 72  ? 0.18410 0.21554 0.27458 -0.00718 -0.02126 -0.02051 79  ASN A C   
512  O O   . ASN A 72  ? 0.17738 0.20573 0.25733 -0.00996 -0.02522 -0.02472 79  ASN A O   
513  C CB  . ASN A 72  ? 0.15309 0.20058 0.27144 -0.00834 -0.03467 -0.01595 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.16490 0.22512 0.29795 -0.00533 -0.03871 -0.00876 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.18063 0.24992 0.32126 0.00420  -0.02823 0.00008  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.21860 0.27823 0.35353 -0.01160 -0.05414 -0.01074 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.17446 0.20763 0.27065 -0.00627 -0.01456 -0.01579 80  LEU A N   
518  C CA  . LEU A 73  ? 0.14086 0.17015 0.23086 -0.00972 -0.01388 -0.01687 80  LEU A CA  
519  C C   . LEU A 73  ? 0.16848 0.20376 0.27772 -0.01304 -0.01642 -0.01325 80  LEU A C   
520  O O   . LEU A 73  ? 0.15819 0.20295 0.28479 -0.01274 -0.01219 -0.00449 80  LEU A O   
521  C CB  . LEU A 73  ? 0.17777 0.19661 0.25054 -0.00645 -0.00525 -0.01378 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.19457 0.19497 0.23969 -0.00493 -0.00530 -0.01655 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.21449 0.19227 0.23031 -0.00113 0.00111  -0.01453 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.20398 0.20424 0.24099 -0.01428 -0.01547 -0.01946 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.15636 0.18494 0.26121 -0.01534 -0.02295 -0.01760 81  ILE A N   
526  C CA  . ILE A 74  ? 0.16151 0.18279 0.27505 -0.02034 -0.02974 -0.01568 81  ILE A CA  
527  C C   . ILE A 74  ? 0.16814 0.17988 0.27189 -0.01775 -0.02657 -0.01545 81  ILE A C   
528  O O   . ILE A 74  ? 0.20117 0.20355 0.28889 -0.01136 -0.02793 -0.02011 81  ILE A O   
529  C CB  . ILE A 74  ? 0.18760 0.19519 0.29283 -0.02244 -0.04268 -0.02188 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.19666 0.21669 0.31033 -0.02325 -0.04558 -0.02124 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.18421 0.17531 0.29376 -0.03253 -0.05459 -0.01841 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.21457 0.21980 0.31502 -0.02512 -0.05967 -0.02723 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.20153 0.21612 0.31450 -0.02036 -0.02129 -0.00781 82  PRO A N   
534  C CA  . PRO A 75  ? 0.21138 0.21528 0.31539 -0.01767 -0.01936 -0.00604 82  PRO A CA  
535  C C   . PRO A 75  ? 0.22523 0.20682 0.32816 -0.02315 -0.02890 -0.00536 82  PRO A C   
536  O O   . PRO A 75  ? 0.23354 0.21473 0.35144 -0.03441 -0.03688 -0.00072 82  PRO A O   
537  C CB  . PRO A 75  ? 0.19129 0.20530 0.30166 -0.01814 -0.00940 0.00275  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.22728 0.25430 0.35711 -0.02201 -0.00680 0.00943  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.23825 0.26780 0.36925 -0.02267 -0.01433 0.00205  82  PRO A CD  
540  N N   . ASN A 76  ? 0.24800 0.20910 0.33076 -0.01493 -0.02938 -0.00836 83  ASN A N   
541  C CA  . ASN A 76  ? 0.28323 0.20777 0.35141 -0.01846 -0.03937 -0.00878 83  ASN A CA  
542  C C   . ASN A 76  ? 0.30152 0.21468 0.35873 -0.00941 -0.03238 -0.00396 83  ASN A C   
543  O O   . ASN A 76  ? 0.30682 0.21643 0.34620 0.00772  -0.02624 -0.00628 83  ASN A O   
544  C CB  . ASN A 76  ? 0.31191 0.20656 0.35057 -0.01112 -0.04796 -0.01949 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.40218 0.24521 0.41541 -0.01828 -0.06330 -0.02119 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.43352 0.25442 0.43691 -0.01675 -0.06214 -0.01657 83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.50956 0.32917 0.50922 -0.02802 -0.07999 -0.02682 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.36151 0.22673 0.39739 -0.03735 -0.00655 0.07521  84  LYS A N   
549  C CA  . LYS A 77  ? 0.37172 0.22007 0.39390 -0.02524 0.00027  0.08297  84  LYS A CA  
550  C C   . LYS A 77  ? 0.47590 0.27413 0.48038 -0.02898 -0.00560 0.07940  84  LYS A C   
551  O O   . LYS A 77  ? 0.47431 0.25424 0.46148 -0.01315 -0.00089 0.08005  84  LYS A O   
552  C CB  . LYS A 77  ? 0.41197 0.27797 0.44773 -0.02858 0.00889  0.10542  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.41229 0.32184 0.45497 -0.01649 0.01778  0.10848  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.43468 0.36088 0.48768 -0.01704 0.02833  0.13266  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.43284 0.39760 0.48648 -0.00239 0.03815  0.13528  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.50949 0.49647 0.58172 -0.01176 0.03524  0.13161  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.50984 0.28400 0.51612 -0.04887 -0.01624 0.07589  85  GLN A N   
558  C CA  . GLN A 78  ? 0.56247 0.28023 0.54503 -0.05165 -0.02232 0.07054  85  GLN A CA  
559  C C   . GLN A 78  ? 0.55834 0.25986 0.51644 -0.03168 -0.02231 0.05152  85  GLN A C   
560  O O   . GLN A 78  ? 0.63063 0.29696 0.56595 -0.01758 -0.01888 0.05050  85  GLN A O   
561  C CB  . GLN A 78  ? 0.65741 0.35137 0.64423 -0.07960 -0.03637 0.06965  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.81311 0.49864 0.81560 -0.10059 -0.03746 0.09141  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.02893 0.77323 1.06500 -0.10319 -0.02849 0.11007  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.99292 0.75129 1.03149 -0.08990 -0.01558 0.12385  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 1.00401 0.78428 1.06341 -0.11695 -0.03445 0.11029  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.46688 0.19435 0.42984 -0.02940 -0.02523 0.03827  86  ASP A N   
567  C CA  . ASP A 79  ? 0.47307 0.19490 0.41794 -0.01162 -0.02440 0.02228  86  ASP A CA  
568  C C   . ASP A 79  ? 0.46451 0.22023 0.41352 0.00919  -0.01465 0.02403  86  ASP A C   
569  O O   . ASP A 79  ? 0.45466 0.20875 0.39104 0.02552  -0.01243 0.01500  86  ASP A O   
570  C CB  . ASP A 79  ? 0.50639 0.24200 0.45558 -0.02012 -0.03211 0.00926  86  ASP A CB  
571  C CG  . ASP A 79  ? 0.68948 0.39148 0.63079 -0.04111 -0.04507 0.00497  86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.72338 0.38600 0.65411 -0.05004 -0.04849 0.01097  86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.63504 0.35092 0.58145 -0.05018 -0.05270 -0.00324 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.40860 0.19456 0.37385 0.00867  -0.00926 0.03619  87  ARG A N   
575  C CA  . ARG A 80  ? 0.36200 0.18251 0.33076 0.02466  -0.00277 0.03747  87  ARG A CA  
576  C C   . ARG A 80  ? 0.34317 0.18797 0.31589 0.02769  -0.00533 0.02370  87  ARG A C   
577  O O   . ARG A 80  ? 0.33104 0.18754 0.29824 0.04188  -0.00353 0.01871  87  ARG A O   
578  C CB  . ARG A 80  ? 0.39486 0.20287 0.34852 0.04368  0.00234  0.04225  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.38639 0.22982 0.34528 0.05436  0.00707  0.04899  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.57945 0.42811 0.52798 0.07432  0.00920  0.04886  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.58957 0.41115 0.52585 0.08393  0.01379  0.06108  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.72738 0.53641 0.65062 0.10253  0.01645  0.06257  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.53460 0.36324 0.45822 0.11395  0.01529  0.05426  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.67645 0.45455 0.58683 0.11088  0.02121  0.07471  87  ARG A NH2 
585  N N   . THR A 81  ? 0.31905 0.17375 0.30313 0.01380  -0.00964 0.01944  88  THR A N   
586  C CA  . THR A 81  ? 0.29095 0.16583 0.27907 0.01496  -0.01183 0.00811  88  THR A CA  
587  C C   . THR A 81  ? 0.26662 0.17086 0.27021 0.00866  -0.01045 0.01125  88  THR A C   
588  O O   . THR A 81  ? 0.27907 0.18698 0.29310 -0.00101 -0.00981 0.02083  88  THR A O   
589  C CB  . THR A 81  ? 0.33769 0.19392 0.31962 0.00802  -0.01852 -0.00229 88  THR A CB  
590  O OG1 . THR A 81  ? 0.35110 0.19568 0.33949 -0.00954 -0.02440 0.00204  88  THR A OG1 
591  C CG2 . THR A 81  ? 0.35412 0.17989 0.31498 0.01962  -0.01804 -0.00756 88  THR A CG2 
592  N N   . LEU A 82  ? 0.24531 0.16988 0.24987 0.01477  -0.00956 0.00422  89  LEU A N   
593  C CA  . LEU A 82  ? 0.22730 0.17317 0.24151 0.01111  -0.00824 0.00426  89  LEU A CA  
594  C C   . LEU A 82  ? 0.24477 0.19229 0.25986 0.00847  -0.01244 -0.00645 89  LEU A C   
595  O O   . LEU A 82  ? 0.24129 0.18930 0.25002 0.01472  -0.01323 -0.01363 89  LEU A O   
596  C CB  . LEU A 82  ? 0.25783 0.22021 0.26727 0.02055  -0.00386 0.00530  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.21434 0.19189 0.22771 0.01990  -0.00160 0.00357  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.23672 0.22136 0.26180 0.01470  0.00248  0.01505  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.25401 0.23976 0.25476 0.02956  0.00106  0.00234  89  LEU A CD2 
600  N N   . THR A 83  ? 0.22146 0.17243 0.24548 -0.00056 -0.01509 -0.00573 90  THR A N   
601  C CA  . THR A 83  ? 0.20451 0.15654 0.22801 -0.00252 -0.01901 -0.01442 90  THR A CA  
602  C C   . THR A 83  ? 0.23611 0.20724 0.26713 -0.00129 -0.01602 -0.01347 90  THR A C   
603  O O   . THR A 83  ? 0.21988 0.20268 0.26045 -0.00334 -0.01312 -0.00473 90  THR A O   
604  C CB  . THR A 83  ? 0.23816 0.17703 0.26236 -0.01314 -0.02628 -0.01486 90  THR A CB  
605  O OG1 . THR A 83  ? 0.29881 0.21151 0.31048 -0.01302 -0.02875 -0.01663 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.26369 0.20511 0.28525 -0.01404 -0.03032 -0.02279 90  THR A CG2 
607  N N   . ILE A 84  ? 0.19447 0.16831 0.22097 0.00279  -0.01593 -0.02105 91  ILE A N   
608  C CA  . ILE A 84  ? 0.20086 0.18515 0.23009 0.00503  -0.01316 -0.02135 91  ILE A CA  
609  C C   . ILE A 84  ? 0.22262 0.20668 0.25447 0.00112  -0.01710 -0.02435 91  ILE A C   
610  O O   . ILE A 84  ? 0.23819 0.21577 0.26386 0.00163  -0.01931 -0.03055 91  ILE A O   
611  C CB  . ILE A 84  ? 0.22314 0.20706 0.24339 0.01072  -0.01105 -0.02674 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.29403 0.27913 0.30805 0.01556  -0.00822 -0.02378 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.23053 0.21624 0.24925 0.01310  -0.00847 -0.02805 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.33891 0.32095 0.34944 0.01678  -0.01063 -0.02435 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.18966 0.18350 0.23092 -0.00188 -0.01781 -0.01842 92  VAL A N   
616  C CA  . VAL A 85  ? 0.19624 0.19216 0.23918 -0.00529 -0.02273 -0.01991 92  VAL A CA  
617  C C   . VAL A 85  ? 0.22614 0.23089 0.27111 0.00110  -0.01808 -0.01779 92  VAL A C   
618  O O   . VAL A 85  ? 0.22151 0.23609 0.27215 0.00593  -0.01263 -0.01096 92  VAL A O   
619  C CB  . VAL A 85  ? 0.24564 0.24810 0.29843 -0.01489 -0.02981 -0.01352 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.24791 0.25015 0.29685 -0.01808 -0.03709 -0.01702 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.28375 0.27237 0.33382 -0.02186 -0.03357 -0.01353 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.19865 0.19928 0.23796 0.00241  -0.01938 -0.02221 93  ASP A N   
623  C CA  . ASP A 86  ? 0.19710 0.20280 0.23747 0.00861  -0.01533 -0.01864 93  ASP A CA  
624  C C   . ASP A 86  ? 0.22730 0.23664 0.26753 0.00676  -0.02026 -0.01790 93  ASP A C   
625  O O   . ASP A 86  ? 0.23559 0.23932 0.26993 0.00196  -0.02586 -0.02279 93  ASP A O   
626  C CB  . ASP A 86  ? 0.21006 0.20286 0.24019 0.01353  -0.00989 -0.02371 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.26030 0.24484 0.28432 0.01022  -0.01199 -0.02947 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.26809 0.25432 0.29165 0.00988  -0.01358 -0.02823 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.24476 0.22468 0.26540 0.00797  -0.01243 -0.03402 93  ASP A OD2 
630  N N   . THR A 87  ? 0.17727 0.19556 0.22163 0.01259  -0.01770 -0.01115 94  THR A N   
631  C CA  . THR A 87  ? 0.17092 0.19520 0.21430 0.01248  -0.02242 -0.00861 94  THR A CA  
632  C C   . THR A 87  ? 0.23121 0.24411 0.26536 0.01943  -0.01635 -0.00937 94  THR A C   
633  O O   . THR A 87  ? 0.20187 0.22046 0.23635 0.02538  -0.01527 -0.00274 94  THR A O   
634  C CB  . THR A 87  ? 0.19887 0.24657 0.25631 0.01349  -0.02567 0.00271  94  THR A CB  
635  O OG1 . THR A 87  ? 0.18017 0.23486 0.24384 0.02432  -0.01607 0.01052  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.20181 0.25989 0.26955 0.00136  -0.03460 0.00443  94  THR A CG2 
637  N N   . GLY A 88  ? 0.21632 0.21355 0.24295 0.01818  -0.01267 -0.01606 95  GLY A N   
638  C CA  . GLY A 88  ? 0.23254 0.21714 0.25175 0.02110  -0.00792 -0.01579 95  GLY A CA  
639  C C   . GLY A 88  ? 0.19678 0.18318 0.21174 0.01894  -0.01022 -0.01550 95  GLY A C   
640  O O   . GLY A 88  ? 0.21549 0.21165 0.22971 0.01790  -0.01588 -0.01526 95  GLY A O   
641  N N   . ILE A 89  ? 0.20275 0.17852 0.21326 0.01788  -0.00598 -0.01507 96  ILE A N   
642  C CA  . ILE A 89  ? 0.20319 0.18212 0.20912 0.01853  -0.00525 -0.01125 96  ILE A CA  
643  C C   . ILE A 89  ? 0.25054 0.23658 0.25352 0.01624  -0.00805 -0.01597 96  ILE A C   
644  O O   . ILE A 89  ? 0.23494 0.22554 0.23006 0.01959  -0.00813 -0.01356 96  ILE A O   
645  C CB  . ILE A 89  ? 0.24288 0.20907 0.24737 0.01627  0.00059  -0.00683 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.27285 0.24330 0.27273 0.01930  0.00356  0.00134  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.25289 0.21640 0.26160 0.00768  0.00050  -0.01145 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.33270 0.28743 0.33135 0.01743  0.00929  0.00908  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.22194 0.20778 0.22798 0.01280  -0.00996 -0.02232 97  GLY A N   
650  C CA  . GLY A 90  ? 0.24500 0.23373 0.24546 0.01373  -0.01122 -0.02637 97  GLY A CA  
651  C C   . GLY A 90  ? 0.22252 0.21588 0.22376 0.01448  -0.00520 -0.02268 97  GLY A C   
652  O O   . GLY A 90  ? 0.23071 0.22387 0.23865 0.01062  -0.00156 -0.01735 97  GLY A O   
653  N N   . MET A 91  ? 0.21826 0.21512 0.21256 0.01939  -0.00410 -0.02493 98  MET A N   
654  C CA  . MET A 91  ? 0.24542 0.25348 0.24271 0.02223  0.00293  -0.01887 98  MET A CA  
655  C C   . MET A 91  ? 0.23152 0.24086 0.21168 0.03332  0.00627  -0.01844 98  MET A C   
656  O O   . MET A 91  ? 0.25640 0.25441 0.22077 0.03827  0.00173  -0.02638 98  MET A O   
657  C CB  . MET A 91  ? 0.24567 0.26218 0.25338 0.02067  0.00410  -0.01916 98  MET A CB  
658  C CG  . MET A 91  ? 0.23435 0.24823 0.25427 0.01037  -0.00005 -0.02081 98  MET A CG  
659  S SD  . MET A 91  ? 0.23977 0.26431 0.26795 0.01038  -0.00146 -0.02215 98  MET A SD  
660  C CE  . MET A 91  ? 0.26250 0.27024 0.27979 0.01415  -0.00609 -0.03141 98  MET A CE  
661  N N   . THR A 92  ? 0.23894 0.26053 0.22069 0.03692  0.01423  -0.00869 99  THR A N   
662  C CA  . THR A 92  ? 0.24851 0.27326 0.21155 0.05072  0.02013  -0.00697 99  THR A CA  
663  C C   . THR A 92  ? 0.26272 0.29509 0.22574 0.05936  0.02544  -0.00730 99  THR A C   
664  O O   . THR A 92  ? 0.23650 0.27659 0.21749 0.05325  0.02443  -0.00661 99  THR A O   
665  C CB  . THR A 92  ? 0.26128 0.30017 0.22732 0.05303  0.02902  0.00672  99  THR A CB  
666  O OG1 . THR A 92  ? 0.27331 0.33116 0.26372 0.04618  0.03482  0.01717  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.27449 0.30551 0.24114 0.04624  0.02508  0.00947  99  THR A CG2 
668  N N   . LYS A 93  ? 0.25655 0.23792 0.23798 0.04481  -0.01558 -0.03930 100 LYS A N   
669  C CA  . LYS A 93  ? 0.25334 0.23471 0.23393 0.04283  -0.00531 -0.03595 100 LYS A CA  
670  C C   . LYS A 93  ? 0.28069 0.26474 0.26735 0.03942  0.00171  -0.02205 100 LYS A C   
671  O O   . LYS A 93  ? 0.26050 0.24784 0.25800 0.03611  0.00700  -0.02133 100 LYS A O   
672  C CB  . LYS A 93  ? 0.28986 0.27191 0.25079 0.05157  -0.00327 -0.03900 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.29124 0.27346 0.25079 0.05480  0.00409  -0.04108 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.35616 0.34304 0.29490 0.06714  0.00554  -0.04664 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.40968 0.39389 0.34548 0.07569  0.00848  -0.05432 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.41778 0.41753 0.33570 0.09078  0.01258  -0.05913 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.28448 0.26555 0.26277 0.03899  0.00034  -0.01076 101 ALA A N   
678  C CA  . ALA A 94  ? 0.31724 0.30157 0.30110 0.03082  0.00663  0.00298  101 ALA A CA  
679  C C   . ALA A 94  ? 0.30192 0.28261 0.30674 0.02454  0.00313  0.00116  101 ALA A C   
680  O O   . ALA A 94  ? 0.28850 0.27882 0.30567 0.01881  0.00956  0.00510  101 ALA A O   
681  C CB  . ALA A 94  ? 0.31960 0.29296 0.28480 0.02730  0.00366  0.01741  101 ALA A CB  
682  N N   . ASP A 95  ? 0.27750 0.24925 0.28709 0.02711  -0.00759 -0.00712 102 ASP A N   
683  C CA  . ASP A 95  ? 0.28396 0.25706 0.31242 0.02300  -0.01098 -0.01205 102 ASP A CA  
684  C C   . ASP A 95  ? 0.23740 0.22255 0.27633 0.01990  -0.00351 -0.01757 102 ASP A C   
685  O O   . ASP A 95  ? 0.23818 0.22765 0.28916 0.01521  -0.00121 -0.01553 102 ASP A O   
686  C CB  . ASP A 95  ? 0.28170 0.25387 0.31445 0.02914  -0.02312 -0.02494 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.38407 0.33673 0.40483 0.03619  -0.03601 -0.02116 102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.39845 0.33315 0.41381 0.03071  -0.03738 -0.00803 102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.37217 0.32730 0.38997 0.04692  -0.04686 -0.03301 102 ASP A OD2 
690  N N   . LEU A 96  ? 0.23806 0.22524 0.27040 0.02222  -0.00188 -0.02524 103 LEU A N   
691  C CA  . LEU A 96  ? 0.24857 0.23670 0.28383 0.01871  0.00243  -0.02882 103 LEU A CA  
692  C C   . LEU A 96  ? 0.27046 0.26122 0.30678 0.02124  0.00895  -0.02118 103 LEU A C   
693  O O   . LEU A 96  ? 0.23557 0.22843 0.27977 0.01885  0.00997  -0.02051 103 LEU A O   
694  C CB  . LEU A 96  ? 0.26003 0.24116 0.28262 0.01947  0.00174  -0.03661 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.23714 0.22312 0.26199 0.01280  -0.00371 -0.04739 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.25892 0.23412 0.26921 0.01127  -0.00521 -0.05463 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.21596 0.20964 0.25146 0.00172  -0.00316 -0.05018 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.24668 0.24210 0.27464 0.02687  0.01327  -0.01645 104 ILE A N   
699  C CA  . ILE A 97  ? 0.26288 0.27170 0.29428 0.03081  0.01990  -0.01257 104 ILE A CA  
700  C C   . ILE A 97  ? 0.26090 0.28088 0.30869 0.02246  0.02129  -0.00502 104 ILE A C   
701  O O   . ILE A 97  ? 0.24735 0.27998 0.30520 0.02391  0.02371  -0.00531 104 ILE A O   
702  C CB  . ILE A 97  ? 0.26832 0.28880 0.28704 0.03791  0.02554  -0.01093 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.27464 0.28214 0.27745 0.04797  0.02221  -0.02179 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.23874 0.28724 0.26560 0.04100  0.03367  -0.00794 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.27768 0.29559 0.26372 0.05584  0.02581  -0.02251 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.21589 0.22941 0.26516 0.01460  0.01778  0.00085  105 ASN A N   
707  C CA  . ASN A 98  ? 0.24798 0.26512 0.31059 0.00462  0.01646  0.00726  105 ASN A CA  
708  C C   . ASN A 98  ? 0.23912 0.25008 0.31371 0.00381  0.00953  -0.00026 105 ASN A C   
709  O O   . ASN A 98  ? 0.22347 0.22309 0.30163 0.00046  0.00151  -0.00157 105 ASN A O   
710  C CB  . ASN A 98  ? 0.28601 0.28872 0.33891 -0.00270 0.01237  0.01684  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.57521 0.58053 0.63698 -0.01724 0.01260  0.02651  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.48209 0.50676 0.56143 -0.02137 0.01623  0.02440  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.61770 0.60032 0.66602 -0.02574 0.00650  0.03686  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.22153 0.23878 0.29892 0.00850  0.01159  -0.00609 106 ASN A N   
715  C CA  . ASN A 99  ? 0.21802 0.23440 0.30315 0.00684  0.00701  -0.01209 106 ASN A CA  
716  C C   . ASN A 99  ? 0.24529 0.25413 0.32889 0.00547  0.00081  -0.01938 106 ASN A C   
717  O O   . ASN A 99  ? 0.20295 0.21488 0.29557 0.00338  -0.00455 -0.02431 106 ASN A O   
718  C CB  . ASN A 99  ? 0.20410 0.23098 0.30480 0.00167  0.00521  -0.00981 106 ASN A CB  
719  C CG  . ASN A 99  ? 0.17526 0.22109 0.28143 0.00400  0.01121  -0.00611 106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.21373 0.26222 0.31381 0.01331  0.01287  -0.00918 106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.20624 0.26533 0.32309 -0.00466 0.01316  -0.00042 106 ASN A ND2 
722  N N   . LEU A 100 ? 0.19700 0.20054 0.26982 0.00775  0.00107  -0.02288 107 LEU A N   
723  C CA  . LEU A 100 ? 0.22775 0.23439 0.30141 0.00700  -0.00444 -0.03299 107 LEU A CA  
724  C C   . LEU A 100 ? 0.25524 0.26054 0.33644 0.01040  -0.01332 -0.03612 107 LEU A C   
725  O O   . LEU A 100 ? 0.23302 0.24859 0.32214 0.01173  -0.01897 -0.04694 107 LEU A O   
726  C CB  . LEU A 100 ? 0.20956 0.22542 0.28461 0.00071  -0.00286 -0.03917 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.28170 0.28540 0.34261 -0.00146 0.00230  -0.03442 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.26515 0.26525 0.32499 -0.00043 0.00413  -0.02845 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.31229 0.31440 0.36355 -0.01010 0.00249  -0.04030 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.23377 0.22527 0.30978 0.01196  -0.01539 -0.02689 108 GLY A N   
731  C CA  . GLY A 101 ? 0.25989 0.23696 0.33557 0.01569  -0.02728 -0.02793 108 GLY A CA  
732  C C   . GLY A 101 ? 0.26972 0.24333 0.35697 0.01269  -0.03313 -0.02993 108 GLY A C   
733  O O   . GLY A 101 ? 0.31792 0.27787 0.40502 0.01902  -0.04667 -0.03683 108 GLY A O   
734  N N   . THR A 102 ? 0.22633 0.21078 0.32263 0.00529  -0.02556 -0.02590 109 THR A N   
735  C CA  . THR A 102 ? 0.26219 0.24696 0.37029 0.00196  -0.03126 -0.02952 109 THR A CA  
736  C C   . THR A 102 ? 0.25622 0.23386 0.36673 -0.00945 -0.02890 -0.01627 109 THR A C   
737  O O   . THR A 102 ? 0.27316 0.25549 0.37793 -0.01394 -0.01946 -0.00529 109 THR A O   
738  C CB  . THR A 102 ? 0.22908 0.23649 0.34534 0.00194  -0.02583 -0.03653 109 THR A CB  
739  O OG1 . THR A 102 ? 0.24614 0.26197 0.36184 -0.00209 -0.01548 -0.02715 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.26627 0.28654 0.37866 0.00678  -0.02471 -0.04721 109 THR A CG2 
741  N N   . ILE A 103 ? 0.21430 0.18448 0.33376 -0.01492 -0.03753 -0.01892 110 ILE A N   
742  C CA  . ILE A 103 ? 0.22079 0.19335 0.34749 -0.03019 -0.03470 -0.00859 110 ILE A CA  
743  C C   . ILE A 103 ? 0.20439 0.20736 0.34684 -0.03002 -0.02886 -0.01414 110 ILE A C   
744  O O   . ILE A 103 ? 0.19938 0.20599 0.35400 -0.03565 -0.03554 -0.01931 110 ILE A O   
745  C CB  . ILE A 103 ? 0.33329 0.27476 0.45843 -0.03966 -0.04957 -0.00742 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.33977 0.27327 0.47036 -0.02787 -0.06391 -0.02583 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.33783 0.24441 0.44059 -0.04129 -0.05526 0.00365  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.41425 0.30910 0.54100 -0.03542 -0.08239 -0.02701 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.29326 0.17351 0.30503 0.03318  0.02438  0.01993  111 ALA A N   
750  C CA  . ALA A 104 ? 0.25962 0.16203 0.27709 0.04217  0.01535  0.02088  111 ALA A CA  
751  C C   . ALA A 104 ? 0.26377 0.19244 0.31259 0.05555  0.04394  0.02948  111 ALA A C   
752  O O   . ALA A 104 ? 0.24864 0.24655 0.30876 0.04310  0.03685  0.01686  111 ALA A O   
753  C CB  . ALA A 104 ? 0.31605 0.23554 0.32129 0.05282  0.00443  0.02956  111 ALA A CB  
754  N N   . LYS A 105 ? 0.28045 0.21557 0.33091 0.05362  0.05837  0.03459  112 LYS A N   
755  C CA  . LYS A 105 ? 0.29638 0.33125 0.37338 0.03302  0.06746  0.02311  112 LYS A CA  
756  C C   . LYS A 105 ? 0.31583 0.37890 0.41547 -0.01811 0.07860  -0.00605 112 LYS A C   
757  O O   . LYS A 105 ? 0.23797 0.38137 0.35617 -0.03167 0.06944  -0.01990 112 LYS A O   
758  C CB  . LYS A 105 ? 0.26431 0.30088 0.34068 0.03755  0.08642  0.03376  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.34514 0.49718 0.45777 0.02211  0.09476  0.02412  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.30637 0.46243 0.41928 0.02593  0.11952  0.03496  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.50234 0.75928 0.66230 -0.01364 0.13914  0.01783  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.55684 0.92263 0.75298 -0.01342 0.11761  0.00473  112 LYS A NZ  
763  N N   . SER A 106 ? 0.28651 0.27708 0.37976 -0.04536 0.09485  -0.01636 113 SER A N   
764  C CA  . SER A 106 ? 0.27726 0.28918 0.38666 -0.09351 0.10378  -0.04472 113 SER A CA  
765  C C   . SER A 106 ? 0.28105 0.28942 0.38563 -0.09375 0.08986  -0.05790 113 SER A C   
766  O O   . SER A 106 ? 0.31880 0.37785 0.43503 -0.12365 0.08841  -0.07985 113 SER A O   
767  C CB  . SER A 106 ? 0.41168 0.34600 0.50467 -0.11674 0.11884  -0.05181 113 SER A CB  
768  O OG  . SER A 106 ? 0.42601 0.29076 0.48564 -0.08044 0.10092  -0.04005 113 SER A OG  
769  N N   . GLY A 107 ? 0.28272 0.23140 0.36952 -0.06211 0.07996  -0.04521 114 GLY A N   
770  C CA  . GLY A 107 ? 0.31188 0.26228 0.39384 -0.06112 0.07037  -0.05583 114 GLY A CA  
771  C C   . GLY A 107 ? 0.26846 0.30623 0.35120 -0.05463 0.05425  -0.05545 114 GLY A C   
772  O O   . GLY A 107 ? 0.25807 0.32495 0.33838 -0.07523 0.05190  -0.07520 114 GLY A O   
773  N N   . THR A 108 ? 0.21252 0.29057 0.29436 -0.02495 0.04162  -0.03417 115 THR A N   
774  C CA  . THR A 108 ? 0.24569 0.40522 0.32597 -0.01640 0.02223  -0.03450 115 THR A CA  
775  C C   . THR A 108 ? 0.23269 0.46671 0.33646 -0.05358 0.02576  -0.05863 115 THR A C   
776  O O   . THR A 108 ? 0.22584 0.50284 0.32345 -0.06504 0.01286  -0.07285 115 THR A O   
777  C CB  . THR A 108 ? 0.23882 0.42164 0.31314 0.02591  0.00726  -0.00831 115 THR A CB  
778  O OG1 . THR A 108 ? 0.25827 0.36599 0.30754 0.05785  -0.00016 0.01354  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.23074 0.49333 0.30185 0.03829  -0.01610 -0.00901 115 THR A CG2 
780  N N   . LYS A 109 ? 0.19370 0.44068 0.32211 -0.07454 0.04259  -0.06341 116 LYS A N   
781  C CA  . LYS A 109 ? 0.20975 0.52645 0.36587 -0.11540 0.04586  -0.08676 116 LYS A CA  
782  C C   . LYS A 109 ? 0.28636 0.57874 0.43058 -0.15036 0.04705  -0.11301 116 LYS A C   
783  O O   . LYS A 109 ? 0.30066 0.64397 0.44444 -0.16567 0.03349  -0.12861 116 LYS A O   
784  C CB  . LYS A 109 ? 0.23931 0.55536 0.41947 -0.13766 0.06909  -0.08639 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.37907 0.72808 0.57188 -0.17409 0.06992  -0.10397 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.42805 0.74334 0.62689 -0.19164 0.09227  -0.09852 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.53611 0.87955 0.74731 -0.22704 0.09309  -0.11369 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.51873 0.95742 0.75581 -0.22377 0.07429  -0.12000 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.27119 0.47439 0.39811 -0.15721 0.06162  -0.11684 117 ALA A N   
790  C CA  . ALA A 110 ? 0.33207 0.49912 0.43690 -0.17761 0.06344  -0.13822 117 ALA A CA  
791  C C   . ALA A 110 ? 0.31083 0.50452 0.40000 -0.17064 0.04863  -0.14597 117 ALA A C   
792  O O   . ALA A 110 ? 0.32521 0.53590 0.39763 -0.18590 0.04324  -0.16231 117 ALA A O   
793  C CB  . ALA A 110 ? 0.34300 0.41080 0.42928 -0.16909 0.07792  -0.13428 117 ALA A CB  
794  N N   . PHE A 111 ? 0.28183 0.45845 0.35751 -0.13062 0.04075  -0.12235 118 PHE A N   
795  C CA  . PHE A 111 ? 0.24630 0.43194 0.29316 -0.11505 0.02713  -0.12071 118 PHE A CA  
796  C C   . PHE A 111 ? 0.30103 0.56990 0.34346 -0.11968 0.00494  -0.12699 118 PHE A C   
797  O O   . PHE A 111 ? 0.30111 0.58245 0.31792 -0.13286 -0.00271 -0.14320 118 PHE A O   
798  C CB  . PHE A 111 ? 0.23834 0.38971 0.27428 -0.07301 0.02079  -0.09053 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.25576 0.40304 0.25903 -0.05841 0.01017  -0.08495 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.26781 0.39958 0.25209 -0.07977 0.02004  -0.10640 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.28317 0.43417 0.26974 -0.02270 -0.00843 -0.05726 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.32560 0.44905 0.27575 -0.06771 0.01450  -0.09936 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.33835 0.47806 0.29031 -0.01233 -0.01699 -0.04996 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.30144 0.42919 0.23565 -0.03659 -0.00375 -0.07124 118 PHE A CZ  
805  N N   . MET A 112 ? 0.28268 0.60911 0.34945 -0.10833 -0.00599 -0.11568 119 MET A N   
806  C CA  . MET A 112 ? 0.26789 0.67864 0.33761 -0.11033 -0.03086 -0.12331 119 MET A CA  
807  C C   . MET A 112 ? 0.33879 0.75970 0.41197 -0.14787 -0.02541 -0.14774 119 MET A C   
808  O O   . MET A 112 ? 0.37502 0.81399 0.42631 -0.14941 -0.04033 -0.15495 119 MET A O   
809  C CB  . MET A 112 ? 0.26439 0.72720 0.36437 -0.08746 -0.03736 -0.10638 119 MET A CB  
810  C CG  . MET A 112 ? 0.31330 0.74856 0.40200 -0.04458 -0.04152 -0.07833 119 MET A CG  
811  S SD  . MET A 112 ? 0.44918 0.85631 0.48318 -0.01017 -0.06470 -0.06231 119 MET A SD  
812  C CE  . MET A 112 ? 0.45123 0.83185 0.48279 0.03684  -0.06663 -0.03035 119 MET A CE  
813  N N   . GLU A 113 ? 0.32908 0.72802 0.42487 -0.17456 -0.00476 -0.15673 120 GLU A N   
814  C CA  . GLU A 113 ? 0.35609 0.75199 0.44932 -0.20661 -0.00084 -0.17633 120 GLU A CA  
815  C C   . GLU A 113 ? 0.43162 0.78406 0.48538 -0.21457 -0.00002 -0.19048 120 GLU A C   
816  O O   . GLU A 113 ? 0.43524 0.80425 0.47597 -0.22931 -0.01034 -0.20378 120 GLU A O   
817  C CB  . GLU A 113 ? 0.49764 0.85548 0.60881 -0.22712 0.02117  -0.17799 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.74381 1.10935 0.86021 -0.25872 0.02189  -0.19326 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.92730 1.25522 1.05698 -0.27437 0.04092  -0.18959 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.81068 1.12627 0.95271 -0.25959 0.05121  -0.17362 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.88637 1.19302 1.01016 -0.30025 0.04417  -0.20159 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.41177 0.70734 0.44670 -0.20343 0.01206  -0.18730 121 ALA A N   
823  C CA  . ALA A 114 ? 0.41052 0.66269 0.40908 -0.20763 0.01806  -0.19920 121 ALA A CA  
824  C C   . ALA A 114 ? 0.39754 0.68026 0.36458 -0.19378 -0.00238 -0.19621 121 ALA A C   
825  O O   . ALA A 114 ? 0.49663 0.76790 0.43418 -0.20401 -0.00453 -0.20853 121 ALA A O   
826  C CB  . ALA A 114 ? 0.38358 0.56642 0.37748 -0.19566 0.03837  -0.19444 121 ALA A CB  
827  N N   . LEU A 115 ? 0.38523 0.69963 0.35314 -0.16680 -0.01865 -0.17696 122 LEU A N   
828  C CA  . LEU A 115 ? 0.38392 0.71083 0.31553 -0.14651 -0.03869 -0.16658 122 LEU A CA  
829  C C   . LEU A 115 ? 0.52923 0.89762 0.46063 -0.15679 -0.05777 -0.17576 122 LEU A C   
830  O O   . LEU A 115 ? 0.51239 0.86899 0.40521 -0.15461 -0.06954 -0.17859 122 LEU A O   
831  C CB  . LEU A 115 ? 0.37023 0.71112 0.30319 -0.10949 -0.05311 -0.13855 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.39268 0.68574 0.31066 -0.09183 -0.04229 -0.12448 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.38008 0.68187 0.30217 -0.05219 -0.05900 -0.09262 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.36010 0.60487 0.23343 -0.09359 -0.03276 -0.12663 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.53579 0.94897 0.50862 -0.16877 -0.06114 -0.18080 123 GLN A N   
836  C CA  . GLN A 116 ? 0.57825 1.02741 0.55162 -0.18000 -0.08092 -0.19160 123 GLN A CA  
837  C C   . GLN A 116 ? 0.58537 1.00592 0.54395 -0.21366 -0.07264 -0.21520 123 GLN A C   
838  O O   . GLN A 116 ? 0.66106 1.09937 0.60929 -0.22395 -0.09199 -0.22606 123 GLN A O   
839  C CB  . GLN A 116 ? 0.57915 1.09159 0.60278 -0.17799 -0.08946 -0.18719 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.62858 1.16753 0.65396 -0.13754 -0.10677 -0.16478 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.96216 1.55777 1.00986 -0.13203 -0.13105 -0.16713 123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.06690 1.68634 1.12916 -0.15953 -0.13797 -0.18526 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.93573 1.54636 0.98472 -0.09598 -0.14523 -0.14901 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.55645 0.91546 0.61978 -0.26506 -0.04113 -0.16264 124 ALA A N   
845  C CA  . ALA A 117 ? 0.58434 0.90292 0.62321 -0.28685 -0.03923 -0.18975 124 ALA A CA  
846  C C   . ALA A 117 ? 0.73624 1.03061 0.73568 -0.27859 -0.03205 -0.20834 124 ALA A C   
847  O O   . ALA A 117 ? 0.66106 0.90833 0.64118 -0.28665 -0.02429 -0.23320 124 ALA A O   
848  C CB  . ALA A 117 ? 0.59679 0.86580 0.64992 -0.29705 -0.02739 -0.19477 124 ALA A CB  
849  N N   . GLY A 118 ? 0.54458 0.86894 0.53254 -0.26114 -0.03452 -0.19581 125 GLY A N   
850  C CA  . GLY A 118 ? 0.61142 0.92754 0.56113 -0.25653 -0.02847 -0.20973 125 GLY A CA  
851  C C   . GLY A 118 ? 0.57682 0.88378 0.52555 -0.23453 -0.01441 -0.20301 125 GLY A C   
852  O O   . GLY A 118 ? 0.55820 0.87664 0.47905 -0.22870 -0.01170 -0.20367 125 GLY A O   
853  N N   . ALA A 119 ? 0.42335 0.71072 0.40155 -0.22340 -0.00631 -0.19467 126 ALA A N   
854  C CA  . ALA A 119 ? 0.43760 0.70940 0.41809 -0.20348 0.00563  -0.19116 126 ALA A CA  
855  C C   . ALA A 119 ? 0.42864 0.74252 0.40396 -0.18837 -0.00618 -0.16359 126 ALA A C   
856  O O   . ALA A 119 ? 0.42176 0.77099 0.39919 -0.18794 -0.02374 -0.14341 126 ALA A O   
857  C CB  . ALA A 119 ? 0.42107 0.65998 0.43506 -0.19617 0.01315  -0.18476 126 ALA A CB  
858  N N   . ASP A 120 ? 0.46370 0.76577 0.43328 -0.17244 0.00326  -0.16052 127 ASP A N   
859  C CA  . ASP A 120 ? 0.37395 0.70050 0.33975 -0.15447 -0.00768 -0.12859 127 ASP A CA  
860  C C   . ASP A 120 ? 0.30700 0.60002 0.30063 -0.12595 0.00039  -0.10828 127 ASP A C   
861  O O   . ASP A 120 ? 0.31338 0.56439 0.32531 -0.12006 0.01538  -0.11911 127 ASP A O   
862  C CB  . ASP A 120 ? 0.42552 0.76710 0.35079 -0.16075 -0.00349 -0.13383 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.49508 0.80275 0.42012 -0.15087 0.02365  -0.15109 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.74320 1.02381 0.66923 -0.15842 0.03837  -0.18439 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.50998 0.81493 0.43961 -0.13419 0.02852  -0.13119 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.30256 0.61034 0.29675 -0.10867 -0.01338 -0.07751 128 ILE A N   
867  C CA  . ILE A 121 ? 0.27478 0.55206 0.29329 -0.08142 -0.01211 -0.05596 128 ILE A CA  
868  C C   . ILE A 121 ? 0.27045 0.50606 0.29323 -0.07248 0.00884  -0.06602 128 ILE A C   
869  O O   . ILE A 121 ? 0.30643 0.50444 0.35081 -0.05474 0.01353  -0.05853 128 ILE A O   
870  C CB  . ILE A 121 ? 0.25313 0.55004 0.26666 -0.06618 -0.03519 -0.02321 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.34324 0.66992 0.36936 -0.06434 -0.05433 -0.01470 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.27478 0.53423 0.30242 -0.03985 -0.03441 -0.00285 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.39345 0.70742 0.40867 -0.04748 -0.07129 0.01137  128 ILE A CD1 
874  N N   . SER A 122 ? 0.28898 0.53129 0.29193 -0.08434 0.02215  -0.08559 129 SER A N   
875  C CA  . SER A 122 ? 0.33016 0.54090 0.34521 -0.07220 0.04168  -0.09596 129 SER A CA  
876  C C   . SER A 122 ? 0.33630 0.49966 0.37276 -0.06758 0.05322  -0.11698 129 SER A C   
877  O O   . SER A 122 ? 0.35698 0.48631 0.41285 -0.05089 0.06314  -0.11960 129 SER A O   
878  C CB  . SER A 122 ? 0.31578 0.55082 0.30668 -0.08486 0.05729  -0.11661 129 SER A CB  
879  O OG  . SER A 122 ? 0.40965 0.64305 0.38514 -0.10208 0.06741  -0.15374 129 SER A OG  
880  N N   . MET A 123 ? 0.26970 0.42908 0.30411 -0.08326 0.04984  -0.13022 130 MET A N   
881  C CA  . MET A 123 ? 0.27150 0.38078 0.32120 -0.08413 0.05762  -0.14703 130 MET A CA  
882  C C   . MET A 123 ? 0.27792 0.35945 0.34778 -0.07051 0.05098  -0.12174 130 MET A C   
883  O O   . MET A 123 ? 0.26499 0.30238 0.34354 -0.07408 0.05508  -0.12966 130 MET A O   
884  C CB  . MET A 123 ? 0.31827 0.43377 0.35439 -0.11250 0.05663  -0.17303 130 MET A CB  
885  C CG  . MET A 123 ? 0.37747 0.52493 0.38392 -0.12511 0.06183  -0.19728 130 MET A CG  
886  S SD  . MET A 123 ? 0.50085 0.66416 0.48268 -0.16038 0.05440  -0.22685 130 MET A SD  
887  C CE  . MET A 123 ? 0.52038 0.61240 0.52240 -0.16316 0.05967  -0.24270 130 MET A CE  
888  N N   . ILE A 124 ? 0.22846 0.32964 0.30228 -0.05456 0.04028  -0.09179 131 ILE A N   
889  C CA  . ILE A 124 ? 0.24360 0.32535 0.32997 -0.04115 0.03381  -0.06910 131 ILE A CA  
890  C C   . ILE A 124 ? 0.23633 0.25429 0.33264 -0.02958 0.04113  -0.07061 131 ILE A C   
891  O O   . ILE A 124 ? 0.23511 0.22764 0.33418 -0.03145 0.04129  -0.06324 131 ILE A O   
892  C CB  . ILE A 124 ? 0.22674 0.33051 0.31264 -0.02097 0.01942  -0.04061 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.22586 0.31430 0.31992 -0.00605 0.01352  -0.02153 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.22074 0.30652 0.30789 -0.00571 0.02028  -0.03415 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.24534 0.35579 0.33736 0.01460  -0.00475 0.00318  131 ILE A CD1 
896  N N   . GLY A 125 ? 0.28484 0.27853 0.38688 -0.01831 0.04680  -0.07959 132 GLY A N   
897  C CA  . GLY A 125 ? 0.29596 0.22804 0.41024 -0.00437 0.04890  -0.08019 132 GLY A CA  
898  C C   . GLY A 125 ? 0.36257 0.25500 0.47313 -0.01965 0.05333  -0.09723 132 GLY A C   
899  O O   . GLY A 125 ? 0.38331 0.24456 0.48057 -0.01033 0.04278  -0.07710 132 GLY A O   
900  N N   . GLN A 126 ? 0.30619 0.21528 0.40999 -0.04318 0.05999  -0.12367 133 GLN A N   
901  C CA  . GLN A 126 ? 0.34825 0.22450 0.44258 -0.05866 0.05816  -0.13146 133 GLN A CA  
902  C C   . GLN A 126 ? 0.38307 0.24913 0.47459 -0.07331 0.05487  -0.11390 133 GLN A C   
903  O O   . GLN A 126 ? 0.41146 0.24688 0.49195 -0.08469 0.05008  -0.11253 133 GLN A O   
904  C CB  . GLN A 126 ? 0.37759 0.27608 0.46266 -0.08262 0.06299  -0.16245 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.45233 0.36232 0.53668 -0.06948 0.07003  -0.18213 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.52359 0.45909 0.59013 -0.09096 0.07383  -0.21136 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.59320 0.51267 0.64977 -0.11026 0.06780  -0.21831 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.51723 0.49390 0.57542 -0.08861 0.08252  -0.22655 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.32072 0.22221 0.41722 -0.07004 0.05402  -0.09471 134 PHE A N   
910  C CA  . PHE A 127 ? 0.31254 0.22227 0.40741 -0.08201 0.05396  -0.07616 134 PHE A CA  
911  C C   . PHE A 127 ? 0.32262 0.20489 0.41418 -0.05753 0.05139  -0.05013 134 PHE A C   
912  O O   . PHE A 127 ? 0.35718 0.25547 0.44519 -0.06089 0.05354  -0.03309 134 PHE A O   
913  C CB  . PHE A 127 ? 0.25948 0.24736 0.35960 -0.09337 0.05145  -0.07322 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.28051 0.29439 0.37858 -0.11833 0.05059  -0.09901 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.38692 0.38705 0.48467 -0.15075 0.05258  -0.11295 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.29123 0.33589 0.38321 -0.11082 0.04707  -0.10944 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.39981 0.41763 0.49129 -0.17385 0.04914  -0.13939 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.30852 0.37313 0.39066 -0.13328 0.04601  -0.13502 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.37382 0.42439 0.45563 -0.16390 0.04616  -0.15137 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.31769 0.16756 0.40720 -0.03186 0.04508  -0.04616 135 GLY A N   
921  C CA  . GLY A 128 ? 0.32928 0.16422 0.39539 -0.01009 0.03166  -0.02094 135 GLY A CA  
922  C C   . GLY A 128 ? 0.31793 0.17713 0.38752 0.00717  0.02924  -0.00475 135 GLY A C   
923  O O   . GLY A 128 ? 0.35695 0.20875 0.39660 0.01809  0.01622  0.00825  135 GLY A O   
924  N N   . VAL A 129 ? 0.25020 0.15076 0.34075 0.00926  0.03254  -0.00772 136 VAL A N   
925  C CA  . VAL A 129 ? 0.19950 0.13162 0.28765 0.02953  0.02261  0.01039  136 VAL A CA  
926  C C   . VAL A 129 ? 0.22675 0.17692 0.32086 0.04162  0.01257  0.01190  136 VAL A C   
927  O O   . VAL A 129 ? 0.21004 0.19817 0.30308 0.05075  0.00181  0.02245  136 VAL A O   
928  C CB  . VAL A 129 ? 0.21920 0.21126 0.31099 0.01889  0.02526  0.01107  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.25177 0.22846 0.33681 0.00901  0.03666  0.01578  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.21561 0.25024 0.31669 -0.00777 0.02918  -0.00788 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.25669 0.22480 0.26360 -0.02205 -0.00865 -0.03728 137 GLY A N   
932  C CA  . GLY A 130 ? 0.23897 0.21157 0.23425 -0.01287 -0.00556 -0.03704 137 GLY A CA  
933  C C   . GLY A 130 ? 0.22587 0.20686 0.22410 -0.01212 0.00084  -0.02836 137 GLY A C   
934  O O   . GLY A 130 ? 0.24609 0.23319 0.23852 -0.00684 0.00304  -0.02563 137 GLY A O   
935  N N   . PHE A 131 ? 0.22810 0.20899 0.23488 -0.01701 0.00330  -0.02392 138 PHE A N   
936  C CA  . PHE A 131 ? 0.22293 0.20940 0.23281 -0.01633 0.00698  -0.01838 138 PHE A CA  
937  C C   . PHE A 131 ? 0.21490 0.20795 0.22423 -0.01449 0.00574  -0.01735 138 PHE A C   
938  O O   . PHE A 131 ? 0.20760 0.20187 0.21597 -0.01156 0.00812  -0.01299 138 PHE A O   
939  C CB  . PHE A 131 ? 0.24290 0.22992 0.25923 -0.02023 0.00804  -0.01609 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.24955 0.24084 0.26843 -0.01893 0.00914  -0.01381 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.24622 0.23589 0.26612 -0.01742 0.01044  -0.01173 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.20745 0.20449 0.22912 -0.01885 0.00819  -0.01428 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.20269 0.19251 0.22618 -0.01687 0.00957  -0.01102 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.19956 0.19684 0.22248 -0.01598 0.00813  -0.01391 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.25195 0.24370 0.27565 -0.01552 0.00816  -0.01275 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.22122 0.21886 0.23297 -0.01632 0.00166  -0.02050 139 TYR A N   
947  C CA  . TYR A 132 ? 0.19825 0.20338 0.21053 -0.01318 0.00003  -0.01905 139 TYR A CA  
948  C C   . TYR A 132 ? 0.22463 0.23073 0.22666 -0.00668 -0.00095 -0.01803 139 TYR A C   
949  O O   . TYR A 132 ? 0.21124 0.22153 0.21206 -0.00239 -0.00173 -0.01450 139 TYR A O   
950  C CB  . TYR A 132 ? 0.20444 0.21887 0.22510 -0.01662 -0.00421 -0.02222 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.22212 0.23883 0.25186 -0.02151 -0.00097 -0.02022 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.22272 0.24441 0.25506 -0.01831 0.00188  -0.01766 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.20059 0.21330 0.23467 -0.02803 -0.00080 -0.02065 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.19849 0.22451 0.23570 -0.02045 0.00554  -0.01577 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.27139 0.28745 0.31168 -0.03138 0.00332  -0.01642 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.24461 0.26888 0.28542 -0.02709 0.00675  -0.01413 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.24447 0.27445 0.28825 -0.02822 0.01135  -0.00995 139 TYR A OH  
958  N N   . SER A 133 ? 0.21817 0.22076 0.21159 -0.00423 -0.00054 -0.02038 140 SER A N   
959  C CA  . SER A 133 ? 0.23255 0.23838 0.21387 0.00382  0.00082  -0.01721 140 SER A CA  
960  C C   . SER A 133 ? 0.20939 0.21474 0.19290 0.00530  0.00753  -0.00646 140 SER A C   
961  O O   . SER A 133 ? 0.22709 0.23623 0.20236 0.01161  0.00990  0.00011  140 SER A O   
962  C CB  . SER A 133 ? 0.25006 0.25353 0.22033 0.00840  0.00095  -0.02260 140 SER A CB  
963  O OG  . SER A 133 ? 0.24323 0.24282 0.21671 0.00751  0.00713  -0.01952 140 SER A OG  
964  N N   . ALA A 134 ? 0.20245 0.20322 0.19703 -0.00036 0.01013  -0.00413 141 ALA A N   
965  C CA  . ALA A 134 ? 0.20906 0.20744 0.20952 -0.00083 0.01404  0.00492  141 ALA A CA  
966  C C   . ALA A 134 ? 0.22214 0.22012 0.22062 0.00311  0.01222  0.00984  141 ALA A C   
967  O O   . ALA A 134 ? 0.22220 0.21778 0.22146 0.00484  0.01573  0.01983  141 ALA A O   
968  C CB  . ALA A 134 ? 0.18395 0.17721 0.19585 -0.00689 0.01349  0.00290  141 ALA A CB  
969  N N   . TYR A 135 ? 0.20923 0.21030 0.20675 0.00469  0.00678  0.00406  142 TYR A N   
970  C CA  . TYR A 135 ? 0.22560 0.22680 0.22196 0.01021  0.00437  0.00845  142 TYR A CA  
971  C C   . TYR A 135 ? 0.25723 0.26430 0.24047 0.01805  0.00389  0.01346  142 TYR A C   
972  O O   . TYR A 135 ? 0.26646 0.27395 0.24699 0.02436  0.00159  0.01861  142 TYR A O   
973  C CB  . TYR A 135 ? 0.18868 0.19544 0.19108 0.01017  -0.00067 0.00114  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.21003 0.21066 0.22188 0.00606  0.00083  -0.00117 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.22417 0.21564 0.23976 0.00938  0.00052  0.00189  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.23486 0.23710 0.25034 -0.00011 0.00201  -0.00638 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.22813 0.21367 0.24982 0.00713  0.00053  -0.00263 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.22473 0.22301 0.24574 -0.00207 0.00299  -0.00874 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.26050 0.25115 0.28376 0.00179  0.00192  -0.00779 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.22194 0.20893 0.24803 0.00124  0.00156  -0.01237 142 TYR A OH  
981  N N   . LEU A 136 ? 0.24726 0.25878 0.22082 0.01954  0.00598  0.01218  143 LEU A N   
982  C CA  . LEU A 136 ? 0.23892 0.25649 0.19690 0.02888  0.00756  0.01896  143 LEU A CA  
983  C C   . LEU A 136 ? 0.26919 0.28198 0.22910 0.03023  0.01527  0.03535  143 LEU A C   
984  O O   . LEU A 136 ? 0.28844 0.30441 0.23768 0.03851  0.01652  0.04533  143 LEU A O   
985  C CB  . LEU A 136 ? 0.26001 0.28311 0.20607 0.03199  0.00902  0.01305  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.23927 0.26476 0.18164 0.03130  0.00001  -0.00314 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.27120 0.29666 0.20294 0.03478  0.00164  -0.01003 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.27341 0.30739 0.20685 0.03829  -0.00880 -0.00647 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.27052 0.27588 0.24481 0.02195  0.02001  0.03904  144 VAL A N   
990  C CA  . VAL A 137 ? 0.22641 0.22786 0.20658 0.02080  0.02722  0.05518  144 VAL A CA  
991  C C   . VAL A 137 ? 0.24146 0.22797 0.23961 0.01309  0.02507  0.05717  144 VAL A C   
992  O O   . VAL A 137 ? 0.28168 0.26048 0.28735 0.01135  0.02855  0.07074  144 VAL A O   
993  C CB  . VAL A 137 ? 0.24278 0.25296 0.22456 0.01889  0.03555  0.05983  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.26411 0.28833 0.22425 0.03003  0.03808  0.05822  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.26874 0.27698 0.26256 0.01063  0.03376  0.04848  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.25203 0.23391 0.25678 0.00902  0.01923  0.04422  145 ALA A N   
997  C CA  . ALA A 138 ? 0.25110 0.21895 0.27035 0.00344  0.01629  0.04319  145 ALA A CA  
998  C C   . ALA A 138 ? 0.26566 0.22674 0.28303 0.00920  0.01011  0.03841  145 ALA A C   
999  O O   . ALA A 138 ? 0.29718 0.26767 0.30813 0.01310  0.00685  0.02947  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.22988 0.19865 0.25707 -0.00352 0.01469  0.03234  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.22999 0.17476 0.25526 0.00938  0.00813  0.04386  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.27530 0.21248 0.30028 0.01629  0.00196  0.03708  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.33607 0.27111 0.36711 0.01332  -0.00176 0.02285  146 GLU A C   
1004 O O   . GLU A 139 ? 0.30488 0.24291 0.33349 0.02012  -0.00524 0.01455  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.34835 0.26541 0.37775 0.01993  0.00028  0.04771  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.48488 0.38259 0.52934 0.01124  -0.00143 0.04868  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.77328 0.64855 0.82430 0.01249  -0.00226 0.06321  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.61068 0.48865 0.65284 0.01946  0.00119  0.07671  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.67102 0.52551 0.73654 0.00593  -0.00674 0.06180  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.26379 0.19624 0.30235 0.00443  -0.00090 0.02035  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.26473 0.19647 0.30626 0.00271  -0.00455 0.00750  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.23029 0.17137 0.27463 -0.00556 -0.00157 0.00665  147 LYS A C   
1013 O O   . LYS A 140 ? 0.22747 0.16923 0.27720 -0.01102 0.00198  0.01556  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.27678 0.18764 0.32660 0.00277  -0.01076 0.00386  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.28813 0.19878 0.33732 0.00381  -0.01552 -0.01078 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.37152 0.25896 0.42637 0.00673  -0.02353 -0.01653 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.42355 0.30025 0.49164 -0.00402 -0.02822 -0.01729 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.49284 0.34150 0.56929 -0.00273 -0.03765 -0.02185 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.20326 0.15276 0.24418 -0.00553 -0.00237 -0.00277 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.19951 0.15655 0.24251 -0.01160 -0.00042 -0.00392 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.25645 0.21086 0.30072 -0.01152 -0.00522 -0.01371 148 VAL A C   
1022 O O   . VAL A 141 ? 0.20827 0.16497 0.24596 -0.00557 -0.00661 -0.02044 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.20736 0.17766 0.24240 -0.01088 0.00352  -0.00432 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.22694 0.20253 0.26362 -0.01531 0.00505  -0.00566 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.21062 0.18471 0.24075 -0.00871 0.00679  0.00316  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.22304 0.17552 0.27558 -0.01721 -0.00761 -0.01423 149 THR A N   
1027 C CA  . THR A 142 ? 0.22968 0.18191 0.28193 -0.01669 -0.01337 -0.02394 149 THR A CA  
1028 C C   . THR A 142 ? 0.22732 0.19203 0.27862 -0.01940 -0.01065 -0.02263 149 THR A C   
1029 O O   . THR A 142 ? 0.26159 0.23075 0.32070 -0.02424 -0.00760 -0.01569 149 THR A O   
1030 C CB  . THR A 142 ? 0.24201 0.18113 0.30694 -0.02090 -0.02140 -0.02717 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.28730 0.21072 0.35391 -0.01809 -0.02398 -0.02691 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.27077 0.20963 0.33167 -0.01775 -0.02956 -0.04018 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.19911 0.17007 0.24079 -0.01524 -0.01125 -0.02824 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.20284 0.18302 0.24290 -0.01645 -0.00937 -0.02632 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.24421 0.22586 0.28228 -0.01391 -0.01649 -0.03391 150 VAL A C   
1036 O O   . VAL A 143 ? 0.23741 0.21910 0.26481 -0.00759 -0.01842 -0.04011 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.20260 0.18874 0.23270 -0.01397 -0.00326 -0.02338 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.23137 0.22301 0.25898 -0.01398 -0.00200 -0.02101 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.22793 0.21316 0.25937 -0.01587 0.00143  -0.01808 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.19459 0.17967 0.24273 -0.01772 -0.02055 -0.03364 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.17595 0.16477 0.22245 -0.01492 -0.02919 -0.04144 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.22937 0.22888 0.27034 -0.01222 -0.02584 -0.03661 151 ILE A C   
1043 O O   . ILE A 144 ? 0.21810 0.22175 0.26707 -0.01553 -0.02105 -0.02931 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.21969 0.20666 0.28527 -0.02167 -0.03810 -0.04474 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.34538 0.31845 0.42152 -0.02684 -0.03972 -0.04477 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.25100 0.24128 0.31244 -0.01730 -0.04999 -0.05631 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.32934 0.29031 0.39424 -0.02038 -0.04545 -0.05555 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.21341 0.21736 0.24000 -0.00494 -0.02811 -0.04005 152 THR A N   
1049 C CA  . THR A 145 ? 0.22898 0.23985 0.24959 -0.00182 -0.02405 -0.03306 152 THR A CA  
1050 C C   . THR A 145 ? 0.26197 0.28021 0.27200 0.00589  -0.03115 -0.03740 152 THR A C   
1051 O O   . THR A 145 ? 0.25450 0.27274 0.25456 0.01105  -0.03641 -0.04563 152 THR A O   
1052 C CB  . THR A 145 ? 0.24333 0.25121 0.25440 -0.00098 -0.01402 -0.02574 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.23716 0.24650 0.24631 0.00038  -0.01038 -0.01818 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.26015 0.27016 0.25641 0.00507  -0.01258 -0.02800 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.20757 0.23242 0.21836 0.00839  -0.03157 -0.03209 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.20812 0.24147 0.20675 0.01746  -0.03815 -0.03402 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.22957 0.26380 0.22130 0.02185  -0.03162 -0.02222 153 LYS A C   
1058 O O   . LYS A 146 ? 0.24053 0.27532 0.24401 0.01968  -0.03011 -0.01768 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.24932 0.29134 0.26145 0.01647  -0.05086 -0.04210 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.26879 0.32236 0.26882 0.02709  -0.05997 -0.04471 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.28144 0.33502 0.25819 0.03625  -0.06404 -0.05246 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.28472 0.35151 0.24774 0.04815  -0.07468 -0.05582 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.29355 0.36427 0.24288 0.05619  -0.06678 -0.04064 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.25093 0.28524 0.22402 0.02871  -0.02753 -0.01678 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.25341 0.28557 0.21848 0.03342  -0.02196 -0.00415 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.27678 0.31958 0.22829 0.04503  -0.02955 -0.00383 154 HIS A C   
1067 O O   . HIS A 147 ? 0.29819 0.34914 0.23959 0.05029  -0.03625 -0.01260 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.24203 0.26764 0.19841 0.03143  -0.01098 0.00477  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.27027 0.28879 0.22157 0.03359  -0.00471 0.01927  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.31085 0.33407 0.24688 0.04355  -0.00524 0.02801  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.25879 0.26396 0.21803 0.02734  0.00153  0.02654  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.33995 0.35133 0.27628 0.04267  0.00084  0.04143  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.30334 0.30293 0.25395 0.03255  0.00456  0.03976  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.26129 0.30372 0.21151 0.05054  -0.02952 0.00543  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.25338 0.30749 0.18967 0.06322  -0.03774 0.00649  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.30276 0.36169 0.21440 0.07138  -0.03510 0.00978  155 ASN A C   
1077 O O   . ASN A 148 ? 0.34120 0.41290 0.23839 0.08241  -0.04436 0.00472  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.27836 0.32856 0.21401 0.06995  -0.03615 0.01924  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.34251 0.39711 0.29881 0.06832  -0.04183 0.01437  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.32286 0.38942 0.29280 0.06441  -0.05037 0.00219  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.31025 0.35532 0.27046 0.07164  -0.03712 0.02419  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.32981 0.38112 0.23616 0.06724  -0.02271 0.01874  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.36389 0.42315 0.24761 0.07596  -0.01718 0.02574  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.39680 0.46310 0.27536 0.07601  -0.01758 0.01296  156 ASP A C   
1085 O O   . ASP A 149 ? 0.39895 0.47398 0.25980 0.08337  -0.01043 0.01896  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.41370 0.46377 0.29636 0.07194  -0.00275 0.04578  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.42554 0.46571 0.30841 0.07522  -0.00225 0.06010  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.43039 0.47630 0.30805 0.08479  -0.01210 0.05701  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.50855 0.53460 0.39827 0.06819  0.00715  0.07383  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.33429 0.39733 0.22770 0.06895  -0.02508 -0.00335 157 ASP A N   
1091 C CA  . ASP A 150 ? 0.28775 0.35388 0.17633 0.07025  -0.02615 -0.01595 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.35565 0.41951 0.25555 0.06753  -0.04114 -0.03529 157 ASP A C   
1093 O O   . ASP A 150 ? 0.31770 0.38122 0.23079 0.06385  -0.04950 -0.03761 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.32497 0.38404 0.22476 0.06019  -0.01404 -0.01048 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.34738 0.41448 0.23515 0.06677  -0.00978 -0.01585 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.35582 0.43129 0.22604 0.07925  -0.01724 -0.02709 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.36861 0.43473 0.26432 0.06049  0.00068  -0.00918 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.35393 0.41617 0.25079 0.06913  -0.04442 -0.04869 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.30404 0.36019 0.21366 0.06501  -0.05873 -0.06669 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.25285 0.29620 0.18763 0.04991  -0.05455 -0.06526 158 GLU A C   
1101 O O   . GLU A 151 ? 0.30558 0.34556 0.24535 0.04413  -0.04193 -0.05304 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.34931 0.40616 0.24218 0.07579  -0.06564 -0.08299 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.52177 0.59346 0.38517 0.09334  -0.06893 -0.08459 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.88644 0.96458 0.75094 0.09586  -0.08418 -0.09016 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.13384 1.20612 1.01361 0.09033  -0.09992 -0.10646 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 0.88412 0.97336 0.73594 0.10307  -0.08075 -0.07743 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.29352 0.33003 0.24497 0.04330  -0.06605 -0.07740 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.26747 0.29282 0.24197 0.02987  -0.06222 -0.07466 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.25739 0.27288 0.22738 0.03101  -0.05766 -0.07902 159 GLN A C   
1110 O O   . GLN A 152 ? 0.30347 0.31503 0.26395 0.03845  -0.06588 -0.09283 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.27386 0.29655 0.27082 0.02134  -0.07528 -0.08306 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.26267 0.27720 0.28431 0.00757  -0.06983 -0.07612 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.35384 0.37309 0.40066 -0.00141 -0.07994 -0.07866 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.36253 0.39585 0.41257 0.00061  -0.08364 -0.07639 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.31734 0.32573 0.38355 -0.01116 -0.08476 -0.08260 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.24004 0.25161 0.21676 0.02477  -0.04561 -0.06833 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.25735 0.26259 0.23114 0.02655  -0.04030 -0.07026 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.26453 0.25860 0.25795 0.01542  -0.03832 -0.06654 160 TYR A C   
1119 O O   . TYR A 153 ? 0.24335 0.23817 0.24957 0.00686  -0.03565 -0.05828 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.24906 0.26417 0.21086 0.03107  -0.02726 -0.05969 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.29094 0.31777 0.23081 0.04454  -0.02720 -0.06279 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.29745 0.32560 0.22557 0.05524  -0.02865 -0.07311 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.34345 0.38022 0.27294 0.04841  -0.02571 -0.05528 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.37235 0.41353 0.27803 0.06971  -0.02784 -0.07617 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.36642 0.41560 0.27311 0.06247  -0.02514 -0.05696 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.41486 0.46718 0.30941 0.07312  -0.02579 -0.06754 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.49188 0.55892 0.36125 0.08946  -0.02426 -0.06976 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.25345 0.23793 0.24753 0.01743  -0.03912 -0.07216 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.23288 0.20745 0.24119 0.00965  -0.03559 -0.06664 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.25129 0.22947 0.25244 0.01451  -0.02643 -0.06241 161 ALA A C   
1131 O O   . ALA A 154 ? 0.26452 0.24380 0.25494 0.02465  -0.02718 -0.06973 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.28899 0.24666 0.30771 0.00746  -0.04604 -0.07581 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.20826 0.18983 0.21570 0.00814  -0.01843 -0.05146 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.19801 0.18364 0.20418 0.01029  -0.01145 -0.04703 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.24632 0.21997 0.26248 0.00675  -0.01319 -0.04541 162 TRP A C   
1136 O O   . TRP A 155 ? 0.23187 0.19833 0.25763 -0.00067 -0.01533 -0.04194 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.22413 0.21966 0.23104 0.00503  -0.00378 -0.03703 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.21712 0.21946 0.22644 0.00424  0.00231  -0.03167 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.18635 0.20251 0.19255 0.00670  0.00806  -0.02826 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.20524 0.20357 0.22176 0.00015  0.00300  -0.02806 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.19227 0.21297 0.20575 0.00337  0.01079  -0.02422 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.20949 0.21920 0.22732 0.00032  0.00737  -0.02465 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.19479 0.18263 0.21694 -0.00333 0.00047  -0.02649 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.21310 0.22366 0.23597 -0.00181 0.00748  -0.02193 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.20808 0.19662 0.23278 -0.00439 0.00223  -0.02218 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.19753 0.19727 0.22173 -0.00326 0.00492  -0.02092 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.20239 0.17574 0.21688 0.01267  -0.01159 -0.04637 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.19342 0.15512 0.21585 0.01052  -0.01295 -0.04262 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.18746 0.15665 0.20825 0.01623  -0.00887 -0.03969 163 GLU A C   
1150 O O   . GLU A 156 ? 0.21402 0.19345 0.22920 0.02462  -0.00718 -0.04419 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.27809 0.22090 0.30381 0.01317  -0.02158 -0.05026 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.33973 0.26720 0.37568 0.00901  -0.02311 -0.04332 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.56823 0.47391 0.61136 0.00838  -0.03287 -0.05025 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.49263 0.38675 0.53091 0.01835  -0.03784 -0.05899 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.43971 0.33999 0.49497 -0.00212 -0.03587 -0.04686 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.22174 0.18832 0.24744 0.01269  -0.00731 -0.03187 164 SER A N   
1157 C CA  . SER A 157 ? 0.19853 0.17331 0.22362 0.01886  -0.00543 -0.02967 164 SER A CA  
1158 C C   . SER A 157 ? 0.19525 0.15986 0.22344 0.01816  -0.00667 -0.02224 164 SER A C   
1159 O O   . SER A 157 ? 0.23059 0.19185 0.26079 0.01067  -0.00514 -0.01565 164 SER A O   
1160 C CB  . SER A 157 ? 0.21026 0.20510 0.23535 0.01596  -0.00052 -0.02679 164 SER A CB  
1161 O OG  . SER A 157 ? 0.21032 0.21554 0.23772 0.02210  -0.00037 -0.02548 164 SER A OG  
1162 N N   . SER A 158 ? 0.22285 0.18383 0.25066 0.02746  -0.00891 -0.02258 165 SER A N   
1163 C CA  . SER A 158 ? 0.22438 0.18002 0.25272 0.02949  -0.00946 -0.01361 165 SER A CA  
1164 C C   . SER A 158 ? 0.28195 0.25785 0.30866 0.03431  -0.00824 -0.01216 165 SER A C   
1165 O O   . SER A 158 ? 0.29862 0.27364 0.32417 0.04171  -0.01033 -0.00735 165 SER A O   
1166 C CB  . SER A 158 ? 0.30077 0.23515 0.33067 0.03721  -0.01418 -0.01337 165 SER A CB  
1167 O OG  . SER A 158 ? 0.32049 0.23524 0.35537 0.03054  -0.01707 -0.01488 165 SER A OG  
1168 N N   . ALA A 159 ? 0.23356 0.22773 0.26135 0.02999  -0.00558 -0.01567 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.24467 0.26085 0.27551 0.03189  -0.00549 -0.01560 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.28231 0.30645 0.31629 0.04434  -0.00691 -0.01894 166 ALA A C   
1171 O O   . ALA A 159 ? 0.30915 0.32720 0.34188 0.04991  -0.00627 -0.02436 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.27824 0.29616 0.30586 0.02978  -0.00740 -0.00978 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.30812 0.34776 0.34597 0.05042  -0.00936 -0.01698 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.32837 0.37941 0.37077 0.06362  -0.00992 -0.02048 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.29291 0.36519 0.34194 0.06401  -0.00489 -0.02535 167 GLY A C   
1176 O O   . GLY A 160 ? 0.28828 0.36951 0.33924 0.07690  -0.00381 -0.02925 167 GLY A O   
1177 N N   . GLY A 161 ? 0.22335 0.30455 0.27565 0.05144  -0.00130 -0.02440 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.18676 0.29342 0.24807 0.05034  0.00433  -0.02488 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.19688 0.29774 0.25055 0.05067  0.00964  -0.02779 168 GLY A C   
1180 O O   . GLY A 161 ? 0.19582 0.31831 0.25524 0.04989  0.01596  -0.02597 168 GLY A O   
1181 N N   . SER A 162 ? 0.19385 0.26790 0.23548 0.05197  0.00706  -0.03163 169 SER A N   
1182 C CA  . SER A 162 ? 0.17590 0.24589 0.20881 0.05457  0.01010  -0.03629 169 SER A CA  
1183 C C   . SER A 162 ? 0.19391 0.23928 0.21967 0.04571  0.00682  -0.03715 169 SER A C   
1184 O O   . SER A 162 ? 0.23484 0.26363 0.26150 0.04049  0.00263  -0.03471 169 SER A O   
1185 C CB  . SER A 162 ? 0.24301 0.30989 0.26892 0.07201  0.00883  -0.04489 169 SER A CB  
1186 O OG  . SER A 162 ? 0.27451 0.31294 0.29625 0.07575  0.00124  -0.04876 169 SER A OG  
1187 N N   . PHE A 163 ? 0.20688 0.25299 0.22567 0.04502  0.00920  -0.03979 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.20771 0.23431 0.22078 0.03848  0.00543  -0.04187 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.20319 0.22754 0.20497 0.04766  0.00392  -0.05079 170 PHE A C   
1190 O O   . PHE A 163 ? 0.24137 0.28243 0.23804 0.05814  0.00826  -0.05335 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.18966 0.22017 0.20566 0.02550  0.00858  -0.03449 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.16897 0.21826 0.18386 0.02471  0.01524  -0.03040 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.19996 0.26847 0.22479 0.02168  0.02024  -0.02394 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.18301 0.23133 0.18825 0.02628  0.01610  -0.03179 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.22590 0.31158 0.25273 0.01898  0.02734  -0.01711 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.19579 0.26050 0.19918 0.02588  0.02304  -0.02528 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.17862 0.26180 0.19384 0.02131  0.02947  -0.01670 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.21829 0.22334 0.21644 0.04464  -0.00274 -0.05601 171 THR A N   
1199 C CA  . THR A 164 ? 0.22443 0.22643 0.21062 0.05347  -0.00678 -0.06661 171 THR A CA  
1200 C C   . THR A 164 ? 0.20951 0.21191 0.19258 0.04554  -0.00768 -0.06455 171 THR A C   
1201 O O   . THR A 164 ? 0.22180 0.21880 0.21352 0.03349  -0.00773 -0.05750 171 THR A O   
1202 C CB  . THR A 164 ? 0.25144 0.22918 0.23679 0.05942  -0.01725 -0.07824 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.28926 0.24863 0.28555 0.04651  -0.02260 -0.07455 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.27750 0.25277 0.26459 0.07026  -0.01698 -0.08052 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.23047 0.24064 0.19971 0.05443  -0.00838 -0.07089 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.25608 0.26658 0.21999 0.05017  -0.01124 -0.07049 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.28937 0.29271 0.24027 0.06114  -0.02132 -0.08611 172 VAL A C   
1208 O O   . VAL A 165 ? 0.29339 0.30388 0.23096 0.07585  -0.02038 -0.09398 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.25451 0.28549 0.21261 0.04957  -0.00109 -0.05896 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.26240 0.29286 0.21285 0.04800  -0.00519 -0.05867 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.23346 0.26831 0.20572 0.03786  0.00623  -0.04601 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.26342 0.25462 0.21825 0.05478  -0.03137 -0.09124 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.27461 0.25898 0.21802 0.06406  -0.04368 -0.10778 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.29952 0.28645 0.24453 0.05737  -0.05003 -0.10698 173 ARG A C   
1215 O O   . ARG A 166 ? 0.27126 0.25892 0.23040 0.04458  -0.04663 -0.09547 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.33110 0.29093 0.28339 0.06411  -0.05518 -0.12054 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.36531 0.30937 0.34125 0.04661  -0.06073 -0.11533 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.45517 0.37448 0.44290 0.04510  -0.06747 -0.12089 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.48939 0.41018 0.47935 0.04684  -0.05671 -0.11073 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.60026 0.50361 0.59340 0.05224  -0.05966 -0.11468 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.54939 0.42850 0.54486 0.05554  -0.07306 -0.12868 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.59224 0.50195 0.58664 0.05491  -0.04999 -0.10481 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.31619 0.30596 0.24537 0.06797  -0.05967 -0.12002 174 THR A N   
1224 C CA  . THR A 167 ? 0.34172 0.33325 0.27469 0.06245  -0.06934 -0.12201 174 THR A CA  
1225 C C   . THR A 167 ? 0.40542 0.37856 0.36389 0.04833  -0.07994 -0.12637 174 THR A C   
1226 O O   . THR A 167 ? 0.42261 0.37772 0.38727 0.04855  -0.08678 -0.13645 174 THR A O   
1227 C CB  . THR A 167 ? 0.41071 0.40835 0.32059 0.07810  -0.08025 -0.13785 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.49494 0.51286 0.38199 0.09061  -0.06768 -0.12924 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.54488 0.54669 0.46049 0.07268  -0.09171 -0.14002 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.33783 0.31557 0.31246 0.03622  -0.08049 -0.11736 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.39874 0.36354 0.40045 0.02183  -0.08804 -0.11785 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.51502 0.47872 0.52222 0.02127  -0.10648 -0.13258 175 ASP A C   
1233 O O   . ASP A 168 ? 0.49700 0.47674 0.49935 0.02372  -0.10977 -0.13183 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.36461 0.33748 0.38299 0.00975  -0.07793 -0.10006 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.51266 0.47534 0.55932 -0.00460 -0.08222 -0.09703 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.61529 0.56051 0.66869 -0.00711 -0.08412 -0.09994 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.44179 0.41473 0.50453 -0.01271 -0.08339 -0.09080 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.59656 0.54262 0.61505 0.01802  -0.11605 -0.14149 176 THR A N   
1239 C CA  . THR A 169 ? 0.81837 0.76341 0.84809 0.01463  -0.12981 -0.14926 176 THR A CA  
1240 C C   . THR A 169 ? 0.76854 0.71224 0.83226 -0.00413 -0.13193 -0.13994 176 THR A C   
1241 O O   . THR A 169 ? 0.69336 0.63715 0.77135 -0.00951 -0.14308 -0.14510 176 THR A O   
1242 C CB  . THR A 169 ? 0.87362 0.80144 0.89593 0.02263  -0.13742 -0.16184 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.78354 0.69469 0.80861 0.02147  -0.12981 -0.15726 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.70956 0.64745 0.69988 0.04258  -0.13907 -0.17269 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.74572 0.69025 0.82279 -0.01366 -0.12091 -0.12581 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.73125 0.67993 0.83944 -0.02993 -0.11946 -0.11371 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.56439 0.53596 0.68437 -0.03385 -0.12416 -0.11178 177 GLY A C   
1248 O O   . GLY A 170 ? 0.52601 0.50893 0.63033 -0.02411 -0.13158 -0.12116 177 GLY A O   
1249 N N   . GLU A 171 ? 0.51066 0.49065 0.65815 -0.04702 -0.11931 -0.09849 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.44729 0.45194 0.61042 -0.05080 -0.12226 -0.09447 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.43720 0.45787 0.58135 -0.03967 -0.11882 -0.09449 178 GLU A C   
1252 O O   . GLU A 171 ? 0.37087 0.38871 0.50079 -0.03581 -0.10255 -0.08330 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.52143 0.53402 0.71429 -0.06453 -0.11238 -0.07702 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.60800 0.64264 0.82530 -0.07146 -0.11753 -0.07362 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.55421 0.58092 0.77730 -0.07468 -0.13261 -0.08571 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.52901 0.53481 0.75787 -0.08089 -0.13418 -0.08649 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.60785 0.64802 0.82697 -0.06920 -0.14368 -0.09544 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.41771 0.45382 0.55409 -0.03185 -0.12918 -0.10254 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.43629 0.48516 0.54804 -0.01889 -0.11978 -0.09544 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.41815 0.47954 0.54338 -0.02305 -0.10533 -0.07763 179 PRO A C   
1261 O O   . PRO A 172 ? 0.48878 0.56350 0.64375 -0.03240 -0.10774 -0.07292 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.48339 0.54800 0.59069 -0.01114 -0.13642 -0.10673 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.55622 0.61195 0.67753 -0.01832 -0.14996 -0.11860 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.51803 0.55352 0.65476 -0.03046 -0.14375 -0.11471 179 PRO A CD  
1265 N N   . MET A 173 ? 0.32510 0.38337 0.42918 -0.01559 -0.09056 -0.06799 180 MET A N   
1266 C CA  . MET A 173 ? 0.33059 0.39825 0.44366 -0.01703 -0.07773 -0.05350 180 MET A CA  
1267 C C   . MET A 173 ? 0.38567 0.46843 0.49111 -0.00685 -0.07727 -0.04891 180 MET A C   
1268 O O   . MET A 173 ? 0.43581 0.52652 0.55009 -0.00660 -0.06811 -0.03866 180 MET A O   
1269 C CB  . MET A 173 ? 0.36355 0.41735 0.46290 -0.01659 -0.06240 -0.04530 180 MET A CB  
1270 C CG  . MET A 173 ? 0.58307 0.61952 0.67845 -0.02089 -0.06197 -0.04984 180 MET A CG  
1271 S SD  . MET A 173 ? 0.51318 0.53939 0.58760 -0.01641 -0.04615 -0.04137 180 MET A SD  
1272 C CE  . MET A 173 ? 0.36773 0.40432 0.45037 -0.01671 -0.03584 -0.02897 180 MET A CE  
1273 N N   . GLY A 174 ? 0.32582 0.41156 0.41256 0.00326  -0.08564 -0.05524 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.29542 0.39409 0.37531 0.01373  -0.08494 -0.04866 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.29367 0.38029 0.34969 0.02110  -0.07130 -0.03863 181 GLY A C   
1276 O O   . GLY A 174 ? 0.26383 0.34830 0.29616 0.03120  -0.07247 -0.03802 181 GLY A O   
1277 N N   . ARG A 175 ? 0.20906 0.28766 0.27129 0.01576  -0.05860 -0.03067 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.21574 0.28052 0.25991 0.01972  -0.04655 -0.02227 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.21956 0.27730 0.27435 0.01206  -0.03636 -0.01807 182 ARG A C   
1280 O O   . ARG A 175 ? 0.20119 0.26920 0.27483 0.00936  -0.03547 -0.01609 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.20142 0.26956 0.23743 0.03059  -0.04505 -0.01423 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.22127 0.27172 0.23896 0.03360  -0.03428 -0.00540 182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.19828 0.24588 0.21398 0.04251  -0.03110 0.00350  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.18887 0.24341 0.22349 0.04142  -0.02908 0.00280  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.19189 0.26433 0.23984 0.04743  -0.03480 0.00237  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.22560 0.31042 0.27052 0.05476  -0.04478 0.00147  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.18290 0.26393 0.24781 0.04734  -0.03057 0.00300  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.24390 0.28078 0.18502 0.02153  -0.04083 0.03727  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.22005 0.24736 0.18318 0.02075  -0.03209 0.03207  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.27872 0.29513 0.24042 0.01109  -0.02621 0.01808  183 GLY A C   
1291 O O   . GLY A 176 ? 0.26663 0.27731 0.20914 0.00865  -0.02332 0.01378  183 GLY A O   
1292 N N   . THR A 177 ? 0.20580 0.21961 0.18597 0.00844  -0.02303 0.01233  184 THR A N   
1293 C CA  . THR A 177 ? 0.22106 0.22718 0.20297 0.00259  -0.01734 0.00241  184 THR A CA  
1294 C C   . THR A 177 ? 0.28878 0.29891 0.28444 -0.00169 -0.02153 -0.00463 184 THR A C   
1295 O O   . THR A 177 ? 0.21437 0.23140 0.22404 0.00037  -0.02302 -0.00098 184 THR A O   
1296 C CB  . THR A 177 ? 0.23010 0.22677 0.21797 0.00170  -0.00748 0.00600  184 THR A CB  
1297 O OG1 . THR A 177 ? 0.27733 0.27026 0.25201 0.00289  -0.00217 0.01464  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.27644 0.27516 0.27315 -0.00263 -0.00304 -0.00083 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.21272 0.21610 0.20180 -0.00572 -0.02142 -0.01352 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.21998 0.22150 0.21871 -0.01078 -0.02413 -0.01868 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.22150 0.21420 0.22192 -0.00737 -0.01572 -0.02204 185 LYS A C   
1302 O O   . LYS A 178 ? 0.24421 0.22972 0.23147 -0.00277 -0.01053 -0.02502 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.27640 0.27127 0.26006 -0.01929 -0.03353 -0.02491 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.39537 0.37859 0.38027 -0.02728 -0.03611 -0.03007 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.50522 0.49153 0.48265 -0.04332 -0.05086 -0.03146 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.70084 0.65541 0.64057 -0.04863 -0.05541 -0.04332 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.79976 0.72453 0.72630 -0.06326 -0.06066 -0.05069 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.20365 0.19967 0.21896 -0.00777 -0.01387 -0.02028 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.19911 0.19407 0.21893 -0.00475 -0.00888 -0.02089 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.22798 0.21380 0.24736 -0.00590 -0.01112 -0.02368 186 VAL A C   
1311 O O   . VAL A 179 ? 0.22164 0.21047 0.24830 -0.01040 -0.01398 -0.02184 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.19250 0.19493 0.22309 -0.00704 -0.00771 -0.01672 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.21348 0.22419 0.25186 -0.00553 -0.00619 -0.01498 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.18966 0.19417 0.21825 -0.00891 -0.00500 -0.01234 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.21744 0.18952 0.22573 -0.00040 -0.00808 -0.02697 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.22637 0.17980 0.22860 -0.00143 -0.00937 -0.02850 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.21277 0.17171 0.22312 0.00875  -0.00456 -0.02313 187 ILE A C   
1318 O O   . ILE A 180 ? 0.21454 0.17651 0.22295 0.02114  0.00195  -0.02173 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.22849 0.15103 0.20452 -0.00111 -0.00951 -0.03629 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.26929 0.19381 0.23664 -0.01309 -0.01782 -0.04051 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.26118 0.15534 0.22814 -0.00511 -0.01095 -0.03641 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.34480 0.23614 0.27696 -0.01397 -0.01935 -0.05082 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.22283 0.18676 0.24195 0.00478  -0.00738 -0.01850 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.22926 0.20136 0.25441 0.01330  -0.00602 -0.01164 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.24575 0.19103 0.25838 0.01905  -0.00399 -0.00910 188 LEU A C   
1326 O O   . LEU A 181 ? 0.25863 0.19072 0.26679 0.00926  -0.00640 -0.00793 188 LEU A O   
1327 C CB  . LEU A 181 ? 0.19935 0.18785 0.23273 0.00619  -0.01043 -0.00834 188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.21998 0.22136 0.25863 -0.00072 -0.01215 -0.01142 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.24979 0.25390 0.28525 -0.00567 -0.01508 -0.01052 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.23001 0.24783 0.27673 0.00153  -0.01149 -0.00917 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.24938 0.18657 0.25627 0.03604  0.00185  -0.00622 189 HIS A N   
1332 C CA  . HIS A 182 ? 0.27109 0.17421 0.26141 0.04554  0.00527  -0.00216 189 HIS A CA  
1333 C C   . HIS A 182 ? 0.29286 0.21814 0.29554 0.05271  0.00282  0.01069  189 HIS A C   
1334 O O   . HIS A 182 ? 0.26847 0.22192 0.28408 0.06738  0.00422  0.01820  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.28939 0.16801 0.26217 0.06574  0.01503  -0.00496 189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.35487 0.21522 0.31039 0.05894  0.01640  -0.01845 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.45725 0.26511 0.38007 0.05176  0.01566  -0.02834 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.38378 0.26972 0.34691 0.05590  0.01692  -0.02298 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.41673 0.22133 0.32662 0.04570  0.01466  -0.03912 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.38163 0.23351 0.31601 0.04952  0.01639  -0.03517 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.27809 0.19702 0.27793 0.04112  -0.00142 0.01451  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.25617 0.20182 0.26429 0.04329  -0.00632 0.02469  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.32186 0.26187 0.32502 0.06395  -0.00428 0.03823  190 LEU A C   
1344 O O   . LEU A 183 ? 0.33213 0.23185 0.31832 0.07416  0.00240  0.04085  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.27262 0.21280 0.27477 0.02780  -0.00829 0.02591  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.24739 0.20097 0.25679 0.01236  -0.00958 0.01620  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.33499 0.28785 0.33926 0.00267  -0.00766 0.02081  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.27759 0.25998 0.29638 0.01256  -0.01426 0.01218  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.29182 0.27064 0.30742 0.06998  -0.01109 0.04780  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.31763 0.30001 0.33029 0.09016  -0.01172 0.06485  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.34407 0.29190 0.33471 0.08625  -0.01062 0.07172  191 LYS A C   
1352 O O   . LYS A 184 ? 0.33808 0.28078 0.32243 0.06659  -0.01227 0.06596  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.32006 0.35811 0.35047 0.09087  -0.02395 0.07430  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.31036 0.39006 0.36690 0.08985  -0.02567 0.07113  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.31437 0.44925 0.38742 0.08111  -0.04195 0.08024  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.38412 0.55593 0.48037 0.06627  -0.04597 0.07506  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.37803 0.60416 0.49038 0.05196  -0.06482 0.08463  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.39913 0.32276 0.37761 0.10709  -0.00590 0.08601  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.46395 0.34723 0.41886 0.10378  -0.00278 0.09568  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.47486 0.38427 0.42658 0.09059  -0.01068 0.10205  192 GLU A C   
1361 O O   . GLU A 185 ? 0.49973 0.38403 0.43605 0.07684  -0.00652 0.10493  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.57421 0.43058 0.51581 0.13370  0.00286  0.11346  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.87540 0.66974 0.78758 0.13067  0.00984  0.12205  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.11486 0.89256 1.01925 0.15336  0.01414  0.13090  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 0.95197 0.77368 0.87412 0.17442  0.01126  0.13703  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.32432 1.04705 1.20576 0.14887  0.02031  0.13271  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.40685 0.36592 0.37027 0.09322  -0.02188 0.10486  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.38663 0.36370 0.33660 0.08249  -0.02965 0.10949  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.35136 0.34269 0.30371 0.06014  -0.03198 0.09107  193 ASP A C   
1370 O O   . ASP A 186 ? 0.34110 0.34722 0.27793 0.05228  -0.03845 0.09101  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.44662 0.46395 0.39867 0.09581  -0.04345 0.12434  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.43909 0.50319 0.41808 0.09394  -0.05377 0.11770  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.53228 0.59274 0.52795 0.08867  -0.04738 0.10370  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.62335 0.73021 0.60645 0.09637  -0.06927 0.12828  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.29916 0.28242 0.26562 0.05163  -0.02635 0.07592  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.28273 0.27617 0.25171 0.03496  -0.02714 0.06020  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.26575 0.23523 0.23315 0.02446  -0.01605 0.05445  194 GLN A C   
1378 O O   . GLN A 187 ? 0.28816 0.26264 0.26389 0.01529  -0.01422 0.04214  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.28854 0.30337 0.27769 0.03302  -0.03226 0.05000  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.28673 0.33729 0.28407 0.03914  -0.04495 0.05840  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.32010 0.38439 0.29743 0.02957  -0.05673 0.05947  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.36096 0.41187 0.32130 0.01702  -0.05504 0.04788  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.32167 0.41331 0.29875 0.03676  -0.06899 0.07349  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.34818 0.29404 0.30536 0.02449  -0.00915 0.06545  195 THR A N   
1385 C CA  . THR A 188 ? 0.35919 0.29005 0.32066 0.01044  -0.00070 0.06238  195 THR A CA  
1386 C C   . THR A 188 ? 0.34293 0.29105 0.30048 0.00183  0.00490  0.06196  195 THR A C   
1387 O O   . THR A 188 ? 0.35287 0.30151 0.32034 -0.00964 0.01184  0.06189  195 THR A O   
1388 C CB  . THR A 188 ? 0.39557 0.29100 0.34746 0.00826  0.00475  0.07511  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.45200 0.34453 0.38598 0.01434  0.00670  0.09176  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.45585 0.32434 0.40665 0.01984  0.00277  0.07270  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.33689 0.30004 0.27875 0.00745  0.00218  0.06201  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.32630 0.30097 0.25872 0.00405  0.01034  0.05881  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.31201 0.29541 0.26189 -0.00011 0.01264  0.04523  196 GLU A C   
1394 O O   . GLU A 189 ? 0.31642 0.30945 0.26783 -0.00130 0.02353  0.04605  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.34417 0.32477 0.24748 0.01029  0.00490  0.05649  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.31933 0.30650 0.22445 0.00975  -0.00857 0.04222  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.43135 0.42189 0.30445 0.01091  -0.01848 0.04117  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.45518 0.45378 0.32539 0.01483  -0.02893 0.05209  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.42060 0.40390 0.26807 0.00899  -0.01603 0.03021  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.29903 0.28183 0.26254 -0.00037 0.00393  0.03517  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.24941 0.23850 0.22656 -0.00302 0.00490  0.02379  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.28799 0.27868 0.28573 -0.01046 0.00914  0.02656  197 TYR A C   
1403 O O   . TYR A 190 ? 0.27864 0.27665 0.28874 -0.01197 0.00864  0.01953  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.26336 0.25313 0.24511 -0.00200 -0.00537 0.01435  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.24215 0.23447 0.20387 -0.00056 -0.01277 0.01218  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.27684 0.26306 0.21624 -0.00082 -0.00976 0.00518  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.27444 0.27461 0.23616 0.00181  -0.02287 0.01812  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.30729 0.29008 0.22050 -0.00329 -0.01881 0.00153  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.31033 0.31791 0.25331 -0.00068 -0.03327 0.01740  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.27556 0.27164 0.19168 -0.00552 -0.03225 0.00775  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.31642 0.31346 0.20588 -0.01143 -0.04457 0.00488  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.27275 0.25566 0.27201 -0.01684 0.01222  0.03762  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.29556 0.28214 0.31174 -0.03006 0.01464  0.04193  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.31205 0.32050 0.33422 -0.03485 0.02583  0.05434  198 LEU A C   
1415 O O   . LEU A 191 ? 0.29384 0.31593 0.33516 -0.04901 0.02711  0.06115  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.30504 0.26168 0.31647 -0.03852 0.01060  0.04657  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.27997 0.21555 0.28490 -0.02984 0.00323  0.03645  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.36037 0.25586 0.35194 -0.03347 0.00249  0.04143  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.33920 0.28558 0.35583 -0.03239 -0.00121 0.02398  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.26896 0.28196 0.27364 -0.02481 0.03378  0.05928  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.28052 0.31602 0.28749 -0.02583 0.04848  0.07329  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.31467 0.37734 0.33125 -0.01529 0.05695  0.06863  199 GLU A C   
1423 O O   . GLU A 192 ? 0.29855 0.35161 0.29891 -0.00173 0.05507  0.05479  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.36730 0.39326 0.34345 -0.01669 0.05480  0.08022  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.45144 0.45151 0.41654 -0.02305 0.04906  0.09038  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.85688 0.85633 0.83861 -0.04217 0.05470  0.10734  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.76196 0.79212 0.75897 -0.04889 0.06729  0.11838  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.80817 0.77564 0.78664 -0.05051 0.04705  0.11061  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.28182 0.30372 0.33350 -0.01953 0.00346  0.06578  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.23863 0.28240 0.29135 -0.02093 0.01002  0.05661  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.23195 0.29674 0.26567 -0.01380 0.01671  0.05609  200 GLU A C   
1432 O O   . GLU A 193 ? 0.24760 0.31790 0.27342 -0.00821 0.01771  0.04149  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.24904 0.30269 0.31902 -0.03347 0.01385  0.06640  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.33808 0.41606 0.41090 -0.03100 0.02024  0.05698  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.64057 0.73920 0.73485 -0.04266 0.02394  0.06688  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.44959 0.54950 0.55438 -0.05493 0.02459  0.08529  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.46461 0.58084 0.56578 -0.03945 0.02630  0.05795  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.27338 0.34737 0.29723 -0.01383 0.02050  0.07186  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.27663 0.37048 0.27839 -0.00638 0.02642  0.06907  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.30354 0.39091 0.28998 0.00069  0.01867  0.05492  201 ARG A C   
1441 O O   . ARG A 194 ? 0.27523 0.36975 0.24522 0.00548  0.02033  0.04258  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.29191 0.40062 0.28352 -0.00723 0.03250  0.09040  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.38600 0.48437 0.36909 -0.00513 0.02537  0.10252  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.39135 0.50452 0.36771 -0.00833 0.03305  0.12886  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.56513 0.66509 0.53441 -0.00529 0.02527  0.14386  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.56306 0.67612 0.51710 -0.00393 0.02941  0.16653  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.57735 0.71873 0.52258 -0.00600 0.04244  0.17688  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.60500 0.70518 0.55191 0.00148  0.02083  0.18013  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.24967 0.32375 0.24187 0.00147  0.00978  0.05660  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.24599 0.32135 0.22935 0.00610  0.00183  0.04599  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.26413 0.33424 0.25405 0.00467  0.00073  0.02834  202 ARG A C   
1452 O O   . ARG A 195 ? 0.24053 0.31469 0.21901 0.00465  -0.00225 0.01739  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.26179 0.32986 0.25301 0.01031  -0.00595 0.05481  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.22955 0.30859 0.21678 0.01476  -0.01477 0.04771  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.28315 0.37984 0.24820 0.01518  -0.01811 0.04950  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.24845 0.35950 0.21444 0.01733  -0.02900 0.04623  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.30219 0.42399 0.25926 0.01143  -0.03506 0.03337  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.31305 0.42751 0.25524 0.00591  -0.03137 0.02107  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.28887 0.42898 0.25294 0.01117  -0.04570 0.03307  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.22168 0.28128 0.22869 0.00259  0.00208  0.02584  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.19918 0.25525 0.21073 0.00207  0.00156  0.01177  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.23381 0.29394 0.23497 0.00202  0.00708  0.00457  203 ILE A C   
1463 O O   . ILE A 196 ? 0.23634 0.29296 0.22957 0.00214  0.00488  -0.00582 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.20373 0.24931 0.23184 0.00109  0.00103  0.00999  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.22648 0.26283 0.26110 0.00533  -0.00468 0.01388  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.21728 0.26239 0.24695 0.00139  0.00149  -0.00227 203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.25195 0.27101 0.29847 0.00383  -0.00658 0.01256  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.21848 0.28631 0.21933 0.00236  0.01435  0.01095  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.22129 0.29521 0.21070 0.00728  0.02091  0.00409  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.26873 0.33986 0.23284 0.01109  0.01837  -0.00410 204 LYS A C   
1471 O O   . LYS A 197 ? 0.26056 0.32205 0.21314 0.01485  0.01832  -0.01663 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.22993 0.32234 0.22279 0.00854  0.03056  0.01535  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.30614 0.40458 0.32254 0.00412  0.03284  0.01954  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.38437 0.50969 0.40541 0.00465  0.04354  0.03234  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.61303 0.74868 0.66308 -0.00608 0.04328  0.04211  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.66172 0.80885 0.72121 -0.01678 0.04655  0.06302  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.22375 0.30181 0.17716 0.01047  0.01548  0.00317  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.26050 0.33754 0.18764 0.01279  0.01044  -0.00563 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.25723 0.32034 0.18496 0.00692  0.00023  -0.01797 205 GLU A C   
1480 O O   . GLU A 198 ? 0.26365 0.31510 0.17235 0.00711  -0.00335 -0.03144 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.26154 0.35196 0.17923 0.01298  0.00713  0.00685  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.33067 0.42286 0.22254 0.01306  -0.00289 -0.00217 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.31825 0.42658 0.20381 0.01420  -0.00792 0.01285  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.32718 0.43648 0.23464 0.01207  -0.01123 0.02455  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.33280 0.45174 0.18981 0.01901  -0.00888 0.01249  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.22640 0.29003 0.17527 0.00170  -0.00451 -0.01324 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.25002 0.30844 0.20329 -0.00531 -0.01296 -0.02083 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.25983 0.30116 0.21313 -0.00634 -0.00998 -0.03050 206 ILE A C   
1489 O O   . ILE A 199 ? 0.25907 0.28855 0.20320 -0.01259 -0.01616 -0.03931 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.21173 0.28007 0.18751 -0.00633 -0.01592 -0.01236 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.26317 0.34578 0.23611 -0.00307 -0.02030 -0.00197 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.25479 0.32634 0.23899 -0.01386 -0.02241 -0.01704 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.26001 0.34881 0.25269 0.00196  -0.02168 0.00759  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.22818 0.26751 0.19275 -0.00124 -0.00188 -0.02786 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.21073 0.23565 0.17548 0.00022  0.00063  -0.03480 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.23343 0.24372 0.17463 0.00561  0.00191  -0.04478 207 VAL A C   
1497 O O   . VAL A 200 ? 0.28686 0.27618 0.21915 0.00327  -0.00201 -0.05286 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.24827 0.27908 0.22931 0.00517  0.00735  -0.02989 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.25438 0.27300 0.23255 0.01016  0.01003  -0.03575 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.23678 0.27390 0.23623 0.00108  0.00421  -0.02447 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.23791 0.25758 0.16651 0.01347  0.00734  -0.04409 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.29730 0.30331 0.19910 0.02293  0.00947  -0.05584 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.33304 0.32038 0.21295 0.01526  -0.00248 -0.06723 208 LYS A C   
1504 O O   . LYS A 201 ? 0.38965 0.34938 0.24919 0.01879  -0.00553 -0.08078 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.33117 0.35894 0.22402 0.03369  0.01937  -0.05058 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.43113 0.44924 0.29299 0.04840  0.02371  -0.06360 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.50099 0.54996 0.35741 0.05938  0.03618  -0.05453 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.62347 0.66596 0.44174 0.07640  0.04023  -0.06906 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.74117 0.82193 0.55612 0.08701  0.05465  -0.05647 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.30992 0.31113 0.19374 0.00483  -0.01057 -0.06193 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.34542 0.33585 0.21067 -0.00504 -0.02435 -0.07198 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.35106 0.32063 0.22503 -0.01868 -0.03302 -0.07670 209 LYS A C   
1513 O O   . LYS A 202 ? 0.36522 0.30900 0.21856 -0.02541 -0.04293 -0.08993 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.31712 0.33484 0.18861 -0.01130 -0.03114 -0.06222 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.39288 0.40764 0.24673 -0.02283 -0.04774 -0.07182 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.43587 0.48341 0.29743 -0.02471 -0.05349 -0.05931 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.53843 0.59134 0.38392 -0.03640 -0.07184 -0.06767 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.59298 0.68128 0.44415 -0.03404 -0.07730 -0.05358 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.31636 0.29656 0.21949 -0.02377 -0.03010 -0.06557 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.35545 0.32842 0.27122 -0.03934 -0.03796 -0.06421 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.38006 0.33567 0.30488 -0.03722 -0.03158 -0.06189 210 HIS A C   
1522 O O   . HIS A 203 ? 0.37099 0.31328 0.30000 -0.05047 -0.03767 -0.06083 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.31097 0.31825 0.25251 -0.04668 -0.04079 -0.05163 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.32206 0.34961 0.25789 -0.05066 -0.05013 -0.05121 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.38571 0.40775 0.30826 -0.06461 -0.06442 -0.05940 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.37249 0.42454 0.31240 -0.04224 -0.04839 -0.04310 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.39953 0.44680 0.31875 -0.06384 -0.07126 -0.05636 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.40012 0.46481 0.32920 -0.04940 -0.06110 -0.04556 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.31172 0.26900 0.24012 -0.02223 -0.02037 -0.05954 211 SER A N   
1530 C CA  . SER A 204 ? 0.29708 0.24616 0.23649 -0.01892 -0.01503 -0.05489 211 SER A CA  
1531 C C   . SER A 204 ? 0.33379 0.26423 0.25942 -0.00287 -0.00839 -0.06108 211 SER A C   
1532 O O   . SER A 204 ? 0.33958 0.27285 0.27560 0.00511  -0.00241 -0.05601 211 SER A O   
1533 C CB  . SER A 204 ? 0.30878 0.28596 0.27198 -0.01670 -0.00969 -0.04441 211 SER A CB  
1534 O OG  . SER A 204 ? 0.30804 0.30385 0.28328 -0.02752 -0.01505 -0.03896 211 SER A OG  
1535 N N   . GLN A 205 ? 0.37253 0.28540 0.27355 0.00340  -0.00992 -0.07257 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.47189 0.37591 0.36074 0.02356  -0.00137 -0.07802 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.51446 0.38628 0.39831 0.02941  -0.00192 -0.07981 212 GLN A C   
1538 O O   . GLN A 205 ? 0.53504 0.40836 0.41859 0.04792  0.00611  -0.07959 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.49055 0.38575 0.35003 0.03285  -0.00149 -0.09109 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.58830 0.44209 0.42045 0.02575  -0.01354 -0.10580 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.85780 0.71908 0.68719 0.00520  -0.02616 -0.10748 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.54274 0.42856 0.39777 -0.01007 -0.02930 -0.09510 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.74389 0.58551 0.54073 0.00666  -0.03396 -0.12366 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.38732 0.23363 0.26990 0.01388  -0.01107 -0.07883 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.46427 0.27452 0.33980 0.01858  -0.01235 -0.07789 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.46460 0.28717 0.36272 0.01035  -0.01120 -0.06190 213 PHE A C   
1547 O O   . PHE A 206 ? 0.53680 0.32952 0.42943 0.01077  -0.01338 -0.05731 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.50423 0.26632 0.35619 0.00695  -0.02431 -0.08821 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.60224 0.34378 0.42331 0.01971  -0.02605 -0.10753 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.60713 0.34900 0.41787 0.04766  -0.01561 -0.11303 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.63523 0.37111 0.44289 0.00436  -0.03685 -0.11766 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.69240 0.43412 0.48463 0.05893  -0.01380 -0.12531 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.65716 0.39057 0.44437 0.01644  -0.03586 -0.13128 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.60824 0.34361 0.38673 0.04395  -0.02364 -0.13503 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.33894 0.20290 0.25971 0.00494  -0.00766 -0.05327 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.29467 0.17350 0.23284 0.00074  -0.00570 -0.04007 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.39676 0.27239 0.33455 0.01924  -0.00030 -0.03671 214 ILE A C   
1558 O O   . ILE A 207 ? 0.38447 0.27496 0.32391 0.03442  0.00491  -0.04107 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.28696 0.20690 0.24485 -0.00444 -0.00340 -0.03563 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.30061 0.22744 0.26151 -0.02194 -0.00969 -0.03567 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.29279 0.23161 0.26464 -0.00241 -0.00005 -0.02552 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.31894 0.24027 0.28525 -0.03847 -0.01399 -0.02615 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.31895 0.17894 0.25567 0.01782  -0.00163 -0.02694 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.34637 0.19752 0.27893 0.03657  0.00130  -0.02287 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.33968 0.22894 0.28858 0.04415  0.00492  -0.01563 215 GLY A C   
1566 O O   . GLY A 208 ? 0.35798 0.24409 0.30510 0.05512  0.00512  -0.00745 215 GLY A O   
1567 N N   . TYR A 209 ? 0.29245 0.21553 0.25565 0.03891  0.00650  -0.01878 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.27525 0.23178 0.25268 0.04369  0.00755  -0.01537 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.29844 0.27794 0.28683 0.04529  0.00959  -0.02257 216 TYR A C   
1570 O O   . TYR A 209 ? 0.28541 0.26176 0.27202 0.03806  0.01022  -0.02759 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.25445 0.22571 0.23757 0.03221  0.00624  -0.00964 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.26557 0.21916 0.23923 0.02851  0.00555  0.00147  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.27646 0.23271 0.24592 0.03876  0.00524  0.01007  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.27126 0.20724 0.24081 0.01337  0.00441  0.00518  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.27606 0.21520 0.23584 0.03520  0.00515  0.02366  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.27151 0.19111 0.23419 0.00701  0.00383  0.01846  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.27210 0.19142 0.22895 0.01852  0.00484  0.02845  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.32847 0.23078 0.27729 0.01255  0.00479  0.04502  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.24731 0.25193 0.24779 0.05271  0.00965  -0.02165 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.22658 0.25367 0.24008 0.05088  0.01141  -0.02522 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.24513 0.27804 0.26466 0.03727  0.00925  -0.02688 217 PRO A C   
1582 O O   . PRO A 210 ? 0.25112 0.28780 0.27267 0.03297  0.00571  -0.02609 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.25201 0.30542 0.27938 0.05846  0.00932  -0.02222 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.30543 0.35369 0.32652 0.06225  0.00504  -0.01815 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.25981 0.27439 0.26267 0.06219  0.00707  -0.01593 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.22347 0.25732 0.24377 0.03284  0.01169  -0.02894 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.18387 0.22153 0.20945 0.02276  0.00963  -0.02926 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.17248 0.22723 0.21152 0.02103  0.01035  -0.02717 218 ILE A C   
1589 O O   . ILE A 211 ? 0.23153 0.29371 0.27057 0.02443  0.01537  -0.02519 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.23296 0.25871 0.24800 0.01791  0.01032  -0.03067 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.21752 0.22600 0.22166 0.01529  0.00833  -0.03122 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.22184 0.25493 0.24388 0.01110  0.00817  -0.02905 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.23142 0.22759 0.22381 0.00924  0.00658  -0.03441 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.18376 0.24516 0.23355 0.01612  0.00531  -0.02741 219 THR A N   
1595 C CA  . THR A 212 ? 0.15461 0.22979 0.21975 0.01038  0.00388  -0.02400 219 THR A CA  
1596 C C   . THR A 212 ? 0.16055 0.22525 0.22684 0.00282  0.00132  -0.02308 219 THR A C   
1597 O O   . THR A 212 ? 0.17242 0.22636 0.23518 0.00277  -0.00342 -0.02796 219 THR A O   
1598 C CB  . THR A 212 ? 0.17713 0.26375 0.25308 0.00908  -0.00312 -0.02614 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.18372 0.28192 0.25874 0.01891  -0.00134 -0.02522 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.20434 0.30395 0.29896 -0.00196 -0.00649 -0.02151 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.17990 0.24862 0.24956 -0.00134 0.00509  -0.01598 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.18901 0.24670 0.26042 -0.00749 0.00226  -0.01194 220 LEU A CA  
1603 C C   . LEU A 213 ? 0.17669 0.23582 0.26452 -0.01765 -0.00326 -0.00812 220 LEU A C   
1604 O O   . LEU A 213 ? 0.17656 0.25376 0.27636 -0.02360 0.00001  0.00045  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.18649 0.24792 0.25042 -0.00702 0.00852  -0.00408 220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.23928 0.29128 0.30461 -0.01211 0.00622  0.00456  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.21780 0.25140 0.27993 -0.00890 -0.00052 -0.00091 220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.24366 0.30413 0.29604 -0.00918 0.01248  0.01163  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.17090 0.21174 0.25906 -0.01967 -0.01189 -0.01471 221 PHE A N   
1610 C CA  . PHE A 214 ? 0.18128 0.21486 0.28258 -0.03150 -0.02048 -0.01367 221 PHE A CA  
1611 C C   . PHE A 214 ? 0.20862 0.23138 0.31524 -0.04020 -0.01961 -0.00042 221 PHE A C   
1612 O O   . PHE A 214 ? 0.23766 0.25104 0.33378 -0.03363 -0.01561 0.00377  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.20626 0.21648 0.29959 -0.02783 -0.03052 -0.02763 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.18372 0.20493 0.27237 -0.02213 -0.03402 -0.03908 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.18451 0.22657 0.26950 -0.01443 -0.02670 -0.03780 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.19869 0.20515 0.28359 -0.02372 -0.04576 -0.05140 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.17547 0.22652 0.25457 -0.00831 -0.03024 -0.04554 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.21457 0.23232 0.29140 -0.01719 -0.04983 -0.06161 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.19105 0.23291 0.26586 -0.00956 -0.04168 -0.05701 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.22142 0.24726 0.34504 -0.05585 -0.02405 0.00784  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.26133 0.27349 0.39065 -0.06655 -0.02415 0.02352  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.32057 0.29384 0.45169 -0.07503 -0.03843 0.01758  222 VAL A C   
1623 O O   . VAL A 215 ? 0.29116 0.25483 0.42067 -0.07459 -0.04813 0.00120  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.36410 0.40864 0.51212 -0.08018 -0.01734 0.04188  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.44025 0.51379 0.57828 -0.06732 -0.00222 0.04773  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.27656 0.34289 0.44350 -0.09037 -0.02305 0.03800  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.31402 0.26218 0.44567 -0.08160 -0.04031 0.03075  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.38390 0.28475 0.51376 -0.08786 -0.05452 0.02520  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.42654 0.31965 0.57671 -0.11459 -0.06065 0.04259  223 GLU A C   
1630 O O   . GLU A 216 ? 0.46161 0.38191 0.62338 -0.12407 -0.05072 0.06487  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.41349 0.28194 0.52601 -0.07152 -0.05385 0.02701  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.37658 0.25831 0.47326 -0.04817 -0.04771 0.01328  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.48865 0.34761 0.57205 -0.03113 -0.04725 0.01671  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.45677 0.27367 0.53391 -0.02573 -0.05679 0.01089  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.46533 0.34855 0.54428 -0.02296 -0.03808 0.02570  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.45876 0.31373 0.61173 -0.12688 -0.07743 0.03239  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.60136 0.44284 0.76437 -0.14874 -0.08239 0.04591  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.76595 0.59866 0.92945 -0.15210 -0.07389 0.07299  224 LYS A C   
1639 O O   . LYS A 217 ? 0.70709 0.50761 0.85461 -0.13656 -0.07334 0.07506  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.59953 0.38995 0.74746 -0.14868 -0.09768 0.02633  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.86196 0.63581 1.01991 -0.17241 -0.10397 0.03732  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.95204 0.68105 1.09573 -0.17407 -0.12001 0.01393  224 LYS A CD  
1643 C CE  . LYS A 217 ? 1.01304 0.71464 1.12931 -0.14534 -0.12310 -0.01107 224 LYS A CE  
1644 N NZ  . LYS A 217 ? 1.11500 0.77003 1.21221 -0.14266 -0.13660 -0.03324 224 LYS A NZ  
# 
