data_7HAU
# 
_entry.id   7HAU 
# 
_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   7HAU         pdb_00007hau 10.2210/pdb7hau/pdb 
WWPDB D_1001407241 ?            ?                   
# 
_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                        7HAU 
_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 '[2-(4-methylpiperazin-1-yl)phenyl]methanol' 206.284   1   ?        ? ? ? 
3 water       nat water                                        18.015    345 ?        ? ? ? 
# 
_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 '[2-(4-methylpiperazin-1-yl)phenyl]methanol' A1AYA 
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 
A1AYA non-polymer         . '[2-(4-methylpiperazin-1-yl)phenyl]methanol' ? 'C12 H18 N2 O'   206.284 
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        A1AYA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AYA 
_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 A1AYA 1   301 301 A1AYA A2U A . 
C 3 HOH   1   401 314 HOH   HOH A . 
C 3 HOH   2   402 293 HOH   HOH A . 
C 3 HOH   3   403 223 HOH   HOH A . 
C 3 HOH   4   404 202 HOH   HOH A . 
C 3 HOH   5   405 331 HOH   HOH A . 
C 3 HOH   6   406 158 HOH   HOH A . 
C 3 HOH   7   407 57  HOH   HOH A . 
C 3 HOH   8   408 243 HOH   HOH A . 
C 3 HOH   9   409 248 HOH   HOH A . 
C 3 HOH   10  410 51  HOH   HOH A . 
C 3 HOH   11  411 45  HOH   HOH A . 
C 3 HOH   12  412 278 HOH   HOH A . 
C 3 HOH   13  413 297 HOH   HOH A . 
C 3 HOH   14  414 136 HOH   HOH A . 
C 3 HOH   15  415 307 HOH   HOH A . 
C 3 HOH   16  416 150 HOH   HOH A . 
C 3 HOH   17  417 95  HOH   HOH A . 
C 3 HOH   18  418 86  HOH   HOH A . 
C 3 HOH   19  419 304 HOH   HOH A . 
C 3 HOH   20  420 120 HOH   HOH A . 
C 3 HOH   21  421 249 HOH   HOH A . 
C 3 HOH   22  422 283 HOH   HOH A . 
C 3 HOH   23  423 149 HOH   HOH A . 
C 3 HOH   24  424 191 HOH   HOH A . 
C 3 HOH   25  425 77  HOH   HOH A . 
C 3 HOH   26  426 39  HOH   HOH A . 
C 3 HOH   27  427 309 HOH   HOH A . 
C 3 HOH   28  428 332 HOH   HOH A . 
C 3 HOH   29  429 65  HOH   HOH A . 
C 3 HOH   30  430 37  HOH   HOH A . 
C 3 HOH   31  431 329 HOH   HOH A . 
C 3 HOH   32  432 184 HOH   HOH A . 
C 3 HOH   33  433 138 HOH   HOH A . 
C 3 HOH   34  434 50  HOH   HOH A . 
C 3 HOH   35  435 143 HOH   HOH A . 
C 3 HOH   36  436 8   HOH   HOH A . 
C 3 HOH   37  437 31  HOH   HOH A . 
C 3 HOH   38  438 91  HOH   HOH A . 
C 3 HOH   39  439 141 HOH   HOH A . 
C 3 HOH   40  440 85  HOH   HOH A . 
C 3 HOH   41  441 16  HOH   HOH A . 
C 3 HOH   42  442 84  HOH   HOH A . 
C 3 HOH   43  443 159 HOH   HOH A . 
C 3 HOH   44  444 61  HOH   HOH A . 
C 3 HOH   45  445 337 HOH   HOH A . 
C 3 HOH   46  446 36  HOH   HOH A . 
C 3 HOH   47  447 60  HOH   HOH A . 
C 3 HOH   48  448 41  HOH   HOH A . 
C 3 HOH   49  449 302 HOH   HOH A . 
C 3 HOH   50  450 171 HOH   HOH A . 
C 3 HOH   51  451 221 HOH   HOH A . 
C 3 HOH   52  452 24  HOH   HOH A . 
C 3 HOH   53  453 90  HOH   HOH A . 
C 3 HOH   54  454 261 HOH   HOH A . 
C 3 HOH   55  455 170 HOH   HOH A . 
C 3 HOH   56  456 224 HOH   HOH A . 
C 3 HOH   57  457 133 HOH   HOH A . 
C 3 HOH   58  458 69  HOH   HOH A . 
C 3 HOH   59  459 94  HOH   HOH A . 
C 3 HOH   60  460 29  HOH   HOH A . 
C 3 HOH   61  461 204 HOH   HOH A . 
C 3 HOH   62  462 15  HOH   HOH A . 
C 3 HOH   63  463 47  HOH   HOH A . 
C 3 HOH   64  464 265 HOH   HOH A . 
C 3 HOH   65  465 34  HOH   HOH A . 
C 3 HOH   66  466 40  HOH   HOH A . 
C 3 HOH   67  467 99  HOH   HOH A . 
C 3 HOH   68  468 3   HOH   HOH A . 
C 3 HOH   69  469 128 HOH   HOH A . 
C 3 HOH   70  470 73  HOH   HOH A . 
C 3 HOH   71  471 115 HOH   HOH A . 
C 3 HOH   72  472 20  HOH   HOH A . 
C 3 HOH   73  473 44  HOH   HOH A . 
C 3 HOH   74  474 131 HOH   HOH A . 
C 3 HOH   75  475 43  HOH   HOH A . 
C 3 HOH   76  476 6   HOH   HOH A . 
C 3 HOH   77  477 23  HOH   HOH A . 
C 3 HOH   78  478 185 HOH   HOH A . 
C 3 HOH   79  479 42  HOH   HOH A . 
C 3 HOH   80  480 5   HOH   HOH A . 
C 3 HOH   81  481 25  HOH   HOH A . 
C 3 HOH   82  482 38  HOH   HOH A . 
C 3 HOH   83  483 101 HOH   HOH A . 
C 3 HOH   84  484 300 HOH   HOH A . 
C 3 HOH   85  485 113 HOH   HOH A . 
C 3 HOH   86  486 137 HOH   HOH A . 
C 3 HOH   87  487 237 HOH   HOH A . 
C 3 HOH   88  488 72  HOH   HOH A . 
C 3 HOH   89  489 9   HOH   HOH A . 
C 3 HOH   90  490 33  HOH   HOH A . 
C 3 HOH   91  491 323 HOH   HOH A . 
C 3 HOH   92  492 18  HOH   HOH A . 
C 3 HOH   93  493 193 HOH   HOH A . 
C 3 HOH   94  494 279 HOH   HOH A . 
C 3 HOH   95  495 145 HOH   HOH A . 
C 3 HOH   96  496 63  HOH   HOH A . 
C 3 HOH   97  497 126 HOH   HOH A . 
C 3 HOH   98  498 76  HOH   HOH A . 
C 3 HOH   99  499 81  HOH   HOH A . 
C 3 HOH   100 500 14  HOH   HOH A . 
C 3 HOH   101 501 285 HOH   HOH A . 
C 3 HOH   102 502 124 HOH   HOH A . 
C 3 HOH   103 503 212 HOH   HOH A . 
C 3 HOH   104 504 276 HOH   HOH A . 
C 3 HOH   105 505 26  HOH   HOH A . 
C 3 HOH   106 506 17  HOH   HOH A . 
C 3 HOH   107 507 242 HOH   HOH A . 
C 3 HOH   108 508 67  HOH   HOH A . 
C 3 HOH   109 509 54  HOH   HOH A . 
C 3 HOH   110 510 105 HOH   HOH A . 
C 3 HOH   111 511 83  HOH   HOH A . 
C 3 HOH   112 512 82  HOH   HOH A . 
C 3 HOH   113 513 112 HOH   HOH A . 
C 3 HOH   114 514 32  HOH   HOH A . 
C 3 HOH   115 515 207 HOH   HOH A . 
C 3 HOH   116 516 166 HOH   HOH A . 
C 3 HOH   117 517 180 HOH   HOH A . 
C 3 HOH   118 518 66  HOH   HOH A . 
C 3 HOH   119 519 7   HOH   HOH A . 
C 3 HOH   120 520 181 HOH   HOH A . 
C 3 HOH   121 521 55  HOH   HOH A . 
C 3 HOH   122 522 106 HOH   HOH A . 
C 3 HOH   123 523 21  HOH   HOH A . 
C 3 HOH   124 524 198 HOH   HOH A . 
C 3 HOH   125 525 80  HOH   HOH A . 
C 3 HOH   126 526 264 HOH   HOH A . 
C 3 HOH   127 527 103 HOH   HOH A . 
C 3 HOH   128 528 280 HOH   HOH A . 
C 3 HOH   129 529 12  HOH   HOH A . 
C 3 HOH   130 530 214 HOH   HOH A . 
C 3 HOH   131 531 4   HOH   HOH A . 
C 3 HOH   132 532 10  HOH   HOH A . 
C 3 HOH   133 533 35  HOH   HOH A . 
C 3 HOH   134 534 98  HOH   HOH A . 
C 3 HOH   135 535 175 HOH   HOH A . 
C 3 HOH   136 536 187 HOH   HOH A . 
C 3 HOH   137 537 59  HOH   HOH A . 
C 3 HOH   138 538 178 HOH   HOH A . 
C 3 HOH   139 539 186 HOH   HOH A . 
C 3 HOH   140 540 172 HOH   HOH A . 
C 3 HOH   141 541 345 HOH   HOH A . 
C 3 HOH   142 542 274 HOH   HOH A . 
C 3 HOH   143 543 93  HOH   HOH A . 
C 3 HOH   144 544 62  HOH   HOH A . 
C 3 HOH   145 545 13  HOH   HOH A . 
C 3 HOH   146 546 134 HOH   HOH A . 
C 3 HOH   147 547 225 HOH   HOH A . 
C 3 HOH   148 548 110 HOH   HOH A . 
C 3 HOH   149 549 240 HOH   HOH A . 
C 3 HOH   150 550 282 HOH   HOH A . 
C 3 HOH   151 551 218 HOH   HOH A . 
C 3 HOH   152 552 30  HOH   HOH A . 
C 3 HOH   153 553 139 HOH   HOH A . 
C 3 HOH   154 554 52  HOH   HOH A . 
C 3 HOH   155 555 117 HOH   HOH A . 
C 3 HOH   156 556 53  HOH   HOH A . 
C 3 HOH   157 557 22  HOH   HOH A . 
C 3 HOH   158 558 56  HOH   HOH A . 
C 3 HOH   159 559 226 HOH   HOH A . 
C 3 HOH   160 560 317 HOH   HOH A . 
C 3 HOH   161 561 89  HOH   HOH A . 
C 3 HOH   162 562 284 HOH   HOH A . 
C 3 HOH   163 563 88  HOH   HOH A . 
C 3 HOH   164 564 111 HOH   HOH A . 
C 3 HOH   165 565 260 HOH   HOH A . 
C 3 HOH   166 566 177 HOH   HOH A . 
C 3 HOH   167 567 194 HOH   HOH A . 
C 3 HOH   168 568 156 HOH   HOH A . 
C 3 HOH   169 569 216 HOH   HOH A . 
C 3 HOH   170 570 245 HOH   HOH A . 
C 3 HOH   171 571 176 HOH   HOH A . 
C 3 HOH   172 572 146 HOH   HOH A . 
C 3 HOH   173 573 301 HOH   HOH A . 
C 3 HOH   174 574 153 HOH   HOH A . 
C 3 HOH   175 575 256 HOH   HOH A . 
C 3 HOH   176 576 19  HOH   HOH A . 
C 3 HOH   177 577 213 HOH   HOH A . 
C 3 HOH   178 578 235 HOH   HOH A . 
C 3 HOH   179 579 289 HOH   HOH A . 
C 3 HOH   180 580 64  HOH   HOH A . 
C 3 HOH   181 581 109 HOH   HOH A . 
C 3 HOH   182 582 46  HOH   HOH A . 
C 3 HOH   183 583 205 HOH   HOH A . 
C 3 HOH   184 584 96  HOH   HOH A . 
C 3 HOH   185 585 148 HOH   HOH A . 
C 3 HOH   186 586 11  HOH   HOH A . 
C 3 HOH   187 587 104 HOH   HOH A . 
C 3 HOH   188 588 70  HOH   HOH A . 
C 3 HOH   189 589 79  HOH   HOH A . 
C 3 HOH   190 590 273 HOH   HOH A . 
C 3 HOH   191 591 123 HOH   HOH A . 
C 3 HOH   192 592 275 HOH   HOH A . 
C 3 HOH   193 593 330 HOH   HOH A . 
C 3 HOH   194 594 27  HOH   HOH A . 
C 3 HOH   195 595 254 HOH   HOH A . 
C 3 HOH   196 596 1   HOH   HOH A . 
C 3 HOH   197 597 28  HOH   HOH A . 
C 3 HOH   198 598 338 HOH   HOH A . 
C 3 HOH   199 599 320 HOH   HOH A . 
C 3 HOH   200 600 2   HOH   HOH A . 
C 3 HOH   201 601 49  HOH   HOH A . 
C 3 HOH   202 602 195 HOH   HOH A . 
C 3 HOH   203 603 327 HOH   HOH A . 
C 3 HOH   204 604 188 HOH   HOH A . 
C 3 HOH   205 605 277 HOH   HOH A . 
C 3 HOH   206 606 322 HOH   HOH A . 
C 3 HOH   207 607 122 HOH   HOH A . 
C 3 HOH   208 608 102 HOH   HOH A . 
C 3 HOH   209 609 68  HOH   HOH A . 
C 3 HOH   210 610 97  HOH   HOH A . 
C 3 HOH   211 611 236 HOH   HOH A . 
C 3 HOH   212 612 155 HOH   HOH A . 
C 3 HOH   213 613 288 HOH   HOH A . 
C 3 HOH   214 614 144 HOH   HOH A . 
C 3 HOH   215 615 231 HOH   HOH A . 
C 3 HOH   216 616 255 HOH   HOH A . 
C 3 HOH   217 617 253 HOH   HOH A . 
C 3 HOH   218 618 321 HOH   HOH A . 
C 3 HOH   219 619 114 HOH   HOH A . 
C 3 HOH   220 620 119 HOH   HOH A . 
C 3 HOH   221 621 241 HOH   HOH A . 
C 3 HOH   222 622 220 HOH   HOH A . 
C 3 HOH   223 623 299 HOH   HOH A . 
C 3 HOH   224 624 319 HOH   HOH A . 
C 3 HOH   225 625 107 HOH   HOH A . 
C 3 HOH   226 626 227 HOH   HOH A . 
C 3 HOH   227 627 246 HOH   HOH A . 
C 3 HOH   228 628 118 HOH   HOH A . 
C 3 HOH   229 629 190 HOH   HOH A . 
C 3 HOH   230 630 238 HOH   HOH A . 
C 3 HOH   231 631 92  HOH   HOH A . 
C 3 HOH   232 632 306 HOH   HOH A . 
C 3 HOH   233 633 316 HOH   HOH A . 
C 3 HOH   234 634 196 HOH   HOH A . 
C 3 HOH   235 635 257 HOH   HOH A . 
C 3 HOH   236 636 147 HOH   HOH A . 
C 3 HOH   237 637 328 HOH   HOH A . 
C 3 HOH   238 638 174 HOH   HOH A . 
C 3 HOH   239 639 233 HOH   HOH A . 
C 3 HOH   240 640 250 HOH   HOH A . 
C 3 HOH   241 641 183 HOH   HOH A . 
C 3 HOH   242 642 303 HOH   HOH A . 
C 3 HOH   243 643 208 HOH   HOH A . 
C 3 HOH   244 644 125 HOH   HOH A . 
C 3 HOH   245 645 48  HOH   HOH A . 
C 3 HOH   246 646 100 HOH   HOH A . 
C 3 HOH   247 647 75  HOH   HOH A . 
C 3 HOH   248 648 251 HOH   HOH A . 
C 3 HOH   249 649 129 HOH   HOH A . 
C 3 HOH   250 650 270 HOH   HOH A . 
C 3 HOH   251 651 167 HOH   HOH A . 
C 3 HOH   252 652 239 HOH   HOH A . 
C 3 HOH   253 653 305 HOH   HOH A . 
C 3 HOH   254 654 232 HOH   HOH A . 
C 3 HOH   255 655 78  HOH   HOH A . 
C 3 HOH   256 656 132 HOH   HOH A . 
C 3 HOH   257 657 258 HOH   HOH A . 
C 3 HOH   258 658 168 HOH   HOH A . 
C 3 HOH   259 659 291 HOH   HOH A . 
C 3 HOH   260 660 334 HOH   HOH A . 
C 3 HOH   261 661 58  HOH   HOH A . 
C 3 HOH   262 662 286 HOH   HOH A . 
C 3 HOH   263 663 268 HOH   HOH A . 
C 3 HOH   264 664 325 HOH   HOH A . 
C 3 HOH   265 665 315 HOH   HOH A . 
C 3 HOH   266 666 339 HOH   HOH A . 
C 3 HOH   267 667 161 HOH   HOH A . 
C 3 HOH   268 668 71  HOH   HOH A . 
C 3 HOH   269 669 192 HOH   HOH A . 
C 3 HOH   270 670 199 HOH   HOH A . 
C 3 HOH   271 671 247 HOH   HOH A . 
C 3 HOH   272 672 182 HOH   HOH A . 
C 3 HOH   273 673 121 HOH   HOH A . 
C 3 HOH   274 674 230 HOH   HOH A . 
C 3 HOH   275 675 244 HOH   HOH A . 
C 3 HOH   276 676 295 HOH   HOH A . 
C 3 HOH   277 677 189 HOH   HOH A . 
C 3 HOH   278 678 313 HOH   HOH A . 
C 3 HOH   279 679 154 HOH   HOH A . 
C 3 HOH   280 680 157 HOH   HOH A . 
C 3 HOH   281 681 229 HOH   HOH A . 
C 3 HOH   282 682 74  HOH   HOH A . 
C 3 HOH   283 683 201 HOH   HOH A . 
C 3 HOH   284 684 294 HOH   HOH A . 
C 3 HOH   285 685 160 HOH   HOH A . 
C 3 HOH   286 686 298 HOH   HOH A . 
C 3 HOH   287 687 173 HOH   HOH A . 
C 3 HOH   288 688 271 HOH   HOH A . 
C 3 HOH   289 689 287 HOH   HOH A . 
C 3 HOH   290 690 318 HOH   HOH A . 
C 3 HOH   291 691 206 HOH   HOH A . 
C 3 HOH   292 692 335 HOH   HOH A . 
C 3 HOH   293 693 108 HOH   HOH A . 
C 3 HOH   294 694 219 HOH   HOH A . 
C 3 HOH   295 695 272 HOH   HOH A . 
C 3 HOH   296 696 217 HOH   HOH A . 
C 3 HOH   297 697 210 HOH   HOH A . 
C 3 HOH   298 698 259 HOH   HOH A . 
C 3 HOH   299 699 165 HOH   HOH A . 
C 3 HOH   300 700 130 HOH   HOH A . 
C 3 HOH   301 701 336 HOH   HOH A . 
C 3 HOH   302 702 215 HOH   HOH A . 
C 3 HOH   303 703 326 HOH   HOH A . 
C 3 HOH   304 704 228 HOH   HOH A . 
C 3 HOH   305 705 116 HOH   HOH A . 
C 3 HOH   306 706 197 HOH   HOH A . 
C 3 HOH   307 707 163 HOH   HOH A . 
C 3 HOH   308 708 266 HOH   HOH A . 
C 3 HOH   309 709 281 HOH   HOH A . 
C 3 HOH   310 710 162 HOH   HOH A . 
C 3 HOH   311 711 200 HOH   HOH A . 
C 3 HOH   312 712 290 HOH   HOH A . 
C 3 HOH   313 713 151 HOH   HOH A . 
C 3 HOH   314 714 342 HOH   HOH A . 
C 3 HOH   315 715 310 HOH   HOH A . 
C 3 HOH   316 716 209 HOH   HOH A . 
C 3 HOH   317 717 164 HOH   HOH A . 
C 3 HOH   318 718 311 HOH   HOH A . 
C 3 HOH   319 719 252 HOH   HOH A . 
C 3 HOH   320 720 169 HOH   HOH A . 
C 3 HOH   321 721 135 HOH   HOH A . 
C 3 HOH   322 722 324 HOH   HOH A . 
C 3 HOH   323 723 142 HOH   HOH A . 
C 3 HOH   324 724 140 HOH   HOH A . 
C 3 HOH   325 725 343 HOH   HOH A . 
C 3 HOH   326 726 292 HOH   HOH A . 
C 3 HOH   327 727 234 HOH   HOH A . 
C 3 HOH   328 728 211 HOH   HOH A . 
C 3 HOH   329 729 203 HOH   HOH A . 
C 3 HOH   330 730 267 HOH   HOH A . 
C 3 HOH   331 731 152 HOH   HOH A . 
C 3 HOH   332 732 87  HOH   HOH A . 
C 3 HOH   333 733 341 HOH   HOH A . 
C 3 HOH   334 734 179 HOH   HOH A . 
C 3 HOH   335 735 262 HOH   HOH A . 
C 3 HOH   336 736 340 HOH   HOH A . 
C 3 HOH   337 737 222 HOH   HOH A . 
C 3 HOH   338 738 127 HOH   HOH A . 
C 3 HOH   339 739 308 HOH   HOH A . 
C 3 HOH   340 740 344 HOH   HOH A . 
C 3 HOH   341 741 269 HOH   HOH A . 
C 3 HOH   342 742 312 HOH   HOH A . 
C 3 HOH   343 743 333 HOH   HOH A . 
C 3 HOH   344 744 263 HOH   HOH A . 
C 3 HOH   345 745 296 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             593974.226 
_cell.length_a           66.086 
_cell.length_b           89.696 
_cell.length_c           100.204 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HAU 
_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                         7HAU 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HAU 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 S 9M' 
_diffrn_detector.pdbx_collection_date   2023-07-22 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HAU 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             66.830 
_reflns.d_resolution_high            1.750 
_reflns.number_obs                   28753 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         94.400 
_reflns.pdbx_Rmerge_I_obs            0.058 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        18.500 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              6.000 
_reflns.pdbx_Rrim_I_all              0.063 
_reflns.pdbx_Rpim_I_all              0.024 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     171190 
_reflns.pdbx_scaling_rejects         40 
_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 1.750 1.840  ? 7723 3305 ? 0.253 ? ? ? 2.300 ? 2.600  ? ? ? ? ? ? 76.100 0.313 0.181 0.905 
1 2 5.530 66.830 ? 7248 1061 ? 0.037 ? ? ? 6.800 ? 37.900 ? ? ? ? ? ? 99.600 0.040 0.015 0.999 
# 
_refine.entry_id                                 7HAU 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 5.14 
_refine.pdbx_overall_phase_error                 22.7422 
_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                          0.1842 
_refine.B_iso_mean                               26.99 
_refine.ls_number_reflns_R_free                  1463 
_refine.ls_percent_reflns_obs                    93.18 
_refine.ls_R_factor_R_work                       0.1826 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.75 
_refine.ls_number_reflns_obs                     28436 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.ls_number_reflns_R_work                  26973 
_refine.ls_d_res_low                             33.04 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2121 
_refine.overall_SU_ML                            0.2129 
_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         15 
_refine_hist.number_atoms_solvent             345 
_refine_hist.number_atoms_total               2004 
_refine_hist.d_res_high                       1.75 
_refine_hist.d_res_low                        33.04 
# 
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           1686 0.0040 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2272 0.7252 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     260  0.0483 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0056 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 230  8.3705 ? ? ? 
# 
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' 1.75 1.81  2067 0.3161 72.75  0.3420 98  . . . . . 
'X-RAY DIFFRACTION' 1.81 1.88  2410 0.2423 82.92  0.3175 104 . . . . . 
'X-RAY DIFFRACTION' 1.88 1.97  2395 0.3128 83.78  0.3639 130 . . . . . 
'X-RAY DIFFRACTION' 1.97 2.07  2810 0.1841 97.83  0.2305 162 . . . . . 
'X-RAY DIFFRACTION' 2.07 2.20  2848 0.1785 99.64  0.2172 161 . . . . . 
'X-RAY DIFFRACTION' 2.20 2.37  2722 0.2378 94.97  0.3120 147 . . . . . 
'X-RAY DIFFRACTION' 2.37 2.61  2896 0.1841 100.00 0.2131 149 . . . . . 
'X-RAY DIFFRACTION' 2.61 2.99  2908 0.1761 100.00 0.2075 168 . . . . . 
'X-RAY DIFFRACTION' 2.99 3.76  2905 0.1561 99.45  0.1802 165 . . . . . 
'X-RAY DIFFRACTION' 3.76 33.04 3012 0.1485 99.44  0.1645 179 . . . . . 
# 
_struct.entry_id                  7HAU 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13098' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HAU 
_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              7HAU 
_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 7HAU MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HAU LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HAU GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HAU HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HAU HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HAU HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HAU HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HAU HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HAU 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  ? ILE A 97  ? THR A 99  ILE A 104 1 ? 6  
HELX_P HELX_P5  AA5 ASN A 98  ? THR A 102 ? ASN A 105 THR A 109 5 ? 5  
HELX_P HELX_P6  AA6 ILE A 103 ? ALA A 117 ? ILE A 110 ALA A 124 1 ? 15 
HELX_P HELX_P7  AA7 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P8  AA8 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P9  AA9 GLN A 187 ? LEU A 191 ? GLN A 194 LEU A 198 5 ? 5  
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 VAL A 85  ? O VAL A 92  N ASN A 72  ? N ASN A 79  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HAU 
_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 671 ? ? O A HOH 683 ? ? 1.85 
2  1 O   A HOH 469 ? ? O A HOH 593 ? ? 1.87 
3  1 O   A HOH 627 ? ? O A HOH 640 ? ? 1.99 
4  1 O   A HOH 494 ? ? O A HOH 579 ? ? 2.00 
5  1 O   A HOH 610 ? ? O A HOH 657 ? ? 2.03 
6  1 O   A HOH 550 ? ? O A HOH 626 ? ? 2.10 
7  1 O   A HOH 435 ? ? O A HOH 640 ? ? 2.11 
8  1 O   A HOH 478 ? ? O A HOH 575 ? ? 2.14 
9  1 O   A HOH 565 ? ? O A HOH 659 ? ? 2.15 
10 1 OD1 A ASN 105 ? ? O A HOH 401 ? ? 2.16 
11 1 O   A HOH 493 ? ? O A HOH 503 ? ? 2.18 
# 
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 542 ? ? 1_555 O A HOH 650 ? ? 2_555 1.86 
2 1 O A HOH 449 ? ? 1_555 O A HOH 666 ? ? 8_444 1.91 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ALA 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     166 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             64.79 
_pdbx_validate_torsion.psi             -144.03 
# 
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 12.3602367183  -17.938721856  -18.7687750419 0.0991478245628 0.120353803267 0.154718607379 
0.0192005367792   -0.0319286638701  -0.0164449774915 2.9133168025  1.30000224772 6.73246666505 -0.861278449027 -2.95286821377  
0.701034218749  0.0869818600686  -0.254509112188 -0.0783725746486 -0.00164108668503 -0.0856451373263 -0.0381108367612 
0.0129814089667  0.178438551719  -0.0579273968758 
2 ? 'X-RAY DIFFRACTION' refined -5.21914406655 -6.34800550312 -20.8793523727 0.108674887889  0.101664826004 0.14718258673  
-0.00684438587287 0.00860895735288  -0.0398370076742 2.97316041188 5.72378752785 9.25665937444 -2.96423752155  4.10142922248   
-6.10800680877  -0.0832178988346 0.0445821926189 0.196328533341   0.118598764235    -0.0267313390213 0.050894547815   
-0.328793616304  0.197884491106  0.109380338382   
3 ? 'X-RAY DIFFRACTION' refined -10.1075026912 -15.0588365836 -25.1933118076 0.0993556989934 0.10911693775  0.14406707634  
-0.00209800483483 -0.0478431239403  -0.0472562167435 1.80329212935 3.11140015385 4.4971967648  -0.498069507937 -0.237652087828 
-2.15101259211  0.0712458511893  0.113002043839  -0.136646029403  -0.23543718144    0.0129732161976  0.277172138945   
0.115342373541   -0.221435852069 -0.161723325526  
4 ? 'X-RAY DIFFRACTION' refined 10.7033551994  -7.5781635764  -17.848504981  0.130851141857  0.193854919627 0.262145497138 
-0.0270652752417  0.0241213871414   -0.0608276220665 3.00800990659 2.8830376172  6.55830722253 0.946297948775  -0.162282171765 
0.993745382694  0.098062086438   -0.312252182989 0.42686539476    0.116810846696    -0.152576548478  -0.119548027381  
-0.351988035161  0.724879190185  0.0262976072966  
5 ? 'X-RAY DIFFRACTION' refined 0.918860600781 -19.3261818371 -27.8878471629 0.134070504323  0.109111850335 0.164582514175 
-0.00773924057792 -0.0104773648578  -0.0376925932757 3.24333636518 1.69442233063 2.51364331421 -1.55156791616  0.828377232383  
-0.412506822179 0.167817789648   0.272012745386  -0.301311772314  -0.154348671443   -0.07318870264   0.174858826506   
0.20743794087    0.081636688441  -0.109210305413  
6 ? 'X-RAY DIFFRACTION' refined -5.61832920259 -20.2572060488 -10.4075837727 0.0952060252227 0.129204006864 0.137976104878 
-0.0475327234097  -0.0292573696487  0.0144938181331  3.05407855663 3.45887680919 5.38714503056 -1.3865573912   -0.780153668331 
-0.889958225112 -0.120010747132  -0.395317896463 -0.245758904328  0.265917641663    0.097043347222   0.0591523364021  
0.292954596227   0.008525409575  0.0245775311124  
7 ? 'X-RAY DIFFRACTION' refined -13.9469729645 -13.3902810886 -14.5663018262 0.101489699159  0.131355159694 0.105466385827 
0.00138562682252  -0.00608551832627 -0.0227921070045 5.09268861706 4.97765602374 4.7590938198  0.0765220459577 -0.322315501856 
-0.247148298375 0.0712403344379  -0.262105685948 0.0561454203225  0.433413981937    -0.084688685954  -0.0855760499868 
-0.0745962240465 -0.174569841995 0.0735628076268  
# 
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 99  A 84  . 
;chain 'A' and (resid 66 through 99 )
;
4 4 'X-RAY DIFFRACTION' A 100 A 85  A 136 A 121 . 
;chain 'A' and (resid 100 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
6 6 'X-RAY DIFFRACTION' A 183 A 168 A 210 A 195 . 
;chain 'A' and (resid 183 through 210 )
;
7 7 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 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 
A1AYA C10  C Y N 1   
A1AYA C12  C N N 2   
A1AYA C1   C N N 3   
A1AYA C11  C Y N 4   
A1AYA C2   C N N 5   
A1AYA C3   C N N 6   
A1AYA C4   C N N 7   
A1AYA C5   C N N 8   
A1AYA C6   C Y N 9   
A1AYA C7   C Y N 10  
A1AYA C8   C Y N 11  
A1AYA C9   C Y N 12  
A1AYA N1   N N N 13  
A1AYA N2   N N N 14  
A1AYA O1   O N N 15  
A1AYA HC11 H N N 16  
A1AYA HC12 H N N 17  
A1AYA HC13 H N N 18  
A1AYA HC15 H N N 19  
A1AYA HC16 H N N 20  
A1AYA HC14 H N N 21  
A1AYA HC3  H N N 22  
A1AYA HC2  H N N 23  
A1AYA HC5  H N N 24  
A1AYA HC4  H N N 25  
A1AYA HC7  H N N 26  
A1AYA HC6  H N N 27  
A1AYA HC8  H N N 28  
A1AYA HC9  H N N 29  
A1AYA HC   H N N 30  
A1AYA HC1  H N N 31  
A1AYA HC10 H N N 32  
A1AYA HO   H N N 33  
ALA   N    N N N 34  
ALA   CA   C N S 35  
ALA   C    C N N 36  
ALA   O    O N N 37  
ALA   CB   C N N 38  
ALA   OXT  O N N 39  
ALA   H    H N N 40  
ALA   H2   H N N 41  
ALA   HA   H N N 42  
ALA   HB1  H N N 43  
ALA   HB2  H N N 44  
ALA   HB3  H N N 45  
ALA   HXT  H N N 46  
ARG   N    N N N 47  
ARG   CA   C N S 48  
ARG   C    C N N 49  
ARG   O    O N N 50  
ARG   CB   C N N 51  
ARG   CG   C N N 52  
ARG   CD   C N N 53  
ARG   NE   N N N 54  
ARG   CZ   C N N 55  
ARG   NH1  N N N 56  
ARG   NH2  N N N 57  
ARG   OXT  O N N 58  
ARG   H    H N N 59  
ARG   H2   H N N 60  
ARG   HA   H N N 61  
ARG   HB2  H N N 62  
ARG   HB3  H N N 63  
ARG   HG2  H N N 64  
ARG   HG3  H N N 65  
ARG   HD2  H N N 66  
ARG   HD3  H N N 67  
ARG   HE   H N N 68  
ARG   HH11 H N N 69  
ARG   HH12 H N N 70  
ARG   HH21 H N N 71  
ARG   HH22 H N N 72  
ARG   HXT  H N N 73  
ASN   N    N N N 74  
ASN   CA   C N S 75  
ASN   C    C N N 76  
ASN   O    O N N 77  
ASN   CB   C N N 78  
ASN   CG   C N N 79  
ASN   OD1  O N N 80  
ASN   ND2  N N N 81  
ASN   OXT  O N N 82  
ASN   H    H N N 83  
ASN   H2   H N N 84  
ASN   HA   H N N 85  
ASN   HB2  H N N 86  
ASN   HB3  H N N 87  
ASN   HD21 H N N 88  
ASN   HD22 H N N 89  
ASN   HXT  H N N 90  
ASP   N    N N N 91  
ASP   CA   C N S 92  
ASP   C    C N N 93  
ASP   O    O N N 94  
ASP   CB   C N N 95  
ASP   CG   C N N 96  
ASP   OD1  O N N 97  
ASP   OD2  O N N 98  
ASP   OXT  O N N 99  
ASP   H    H N N 100 
ASP   H2   H N N 101 
ASP   HA   H N N 102 
ASP   HB2  H N N 103 
ASP   HB3  H N N 104 
ASP   HD2  H N N 105 
ASP   HXT  H N N 106 
GLN   N    N N N 107 
GLN   CA   C N S 108 
GLN   C    C N N 109 
GLN   O    O N N 110 
GLN   CB   C N N 111 
GLN   CG   C N N 112 
GLN   CD   C N N 113 
GLN   OE1  O N N 114 
GLN   NE2  N N N 115 
GLN   OXT  O N N 116 
GLN   H    H N N 117 
GLN   H2   H N N 118 
GLN   HA   H N N 119 
GLN   HB2  H N N 120 
GLN   HB3  H N N 121 
GLN   HG2  H N N 122 
GLN   HG3  H N N 123 
GLN   HE21 H N N 124 
GLN   HE22 H N N 125 
GLN   HXT  H N N 126 
GLU   N    N N N 127 
GLU   CA   C N S 128 
GLU   C    C N N 129 
GLU   O    O N N 130 
GLU   CB   C N N 131 
GLU   CG   C N N 132 
GLU   CD   C N N 133 
GLU   OE1  O N N 134 
GLU   OE2  O N N 135 
GLU   OXT  O N N 136 
GLU   H    H N N 137 
GLU   H2   H N N 138 
GLU   HA   H N N 139 
GLU   HB2  H N N 140 
GLU   HB3  H N N 141 
GLU   HG2  H N N 142 
GLU   HG3  H N N 143 
GLU   HE2  H N N 144 
GLU   HXT  H N N 145 
GLY   N    N N N 146 
GLY   CA   C N N 147 
GLY   C    C N N 148 
GLY   O    O N N 149 
GLY   OXT  O N N 150 
GLY   H    H N N 151 
GLY   H2   H N N 152 
GLY   HA2  H N N 153 
GLY   HA3  H N N 154 
GLY   HXT  H N N 155 
HIS   N    N N N 156 
HIS   CA   C N S 157 
HIS   C    C N N 158 
HIS   O    O N N 159 
HIS   CB   C N N 160 
HIS   CG   C Y N 161 
HIS   ND1  N Y N 162 
HIS   CD2  C Y N 163 
HIS   CE1  C Y N 164 
HIS   NE2  N Y N 165 
HIS   OXT  O N N 166 
HIS   H    H N N 167 
HIS   H2   H N N 168 
HIS   HA   H N N 169 
HIS   HB2  H N N 170 
HIS   HB3  H N N 171 
HIS   HD1  H N N 172 
HIS   HD2  H N N 173 
HIS   HE1  H N N 174 
HIS   HE2  H N N 175 
HIS   HXT  H N N 176 
HOH   O    O N N 177 
HOH   H1   H N N 178 
HOH   H2   H N N 179 
ILE   N    N N N 180 
ILE   CA   C N S 181 
ILE   C    C N N 182 
ILE   O    O N N 183 
ILE   CB   C N S 184 
ILE   CG1  C N N 185 
ILE   CG2  C N N 186 
ILE   CD1  C N N 187 
ILE   OXT  O N N 188 
ILE   H    H N N 189 
ILE   H2   H N N 190 
ILE   HA   H N N 191 
ILE   HB   H N N 192 
ILE   HG12 H N N 193 
ILE   HG13 H N N 194 
ILE   HG21 H N N 195 
ILE   HG22 H N N 196 
ILE   HG23 H N N 197 
ILE   HD11 H N N 198 
ILE   HD12 H N N 199 
ILE   HD13 H N N 200 
ILE   HXT  H N N 201 
LEU   N    N N N 202 
LEU   CA   C N S 203 
LEU   C    C N N 204 
LEU   O    O N N 205 
LEU   CB   C N N 206 
LEU   CG   C N N 207 
LEU   CD1  C N N 208 
LEU   CD2  C N N 209 
LEU   OXT  O N N 210 
LEU   H    H N N 211 
LEU   H2   H N N 212 
LEU   HA   H N N 213 
LEU   HB2  H N N 214 
LEU   HB3  H N N 215 
LEU   HG   H N N 216 
LEU   HD11 H N N 217 
LEU   HD12 H N N 218 
LEU   HD13 H N N 219 
LEU   HD21 H N N 220 
LEU   HD22 H N N 221 
LEU   HD23 H N N 222 
LEU   HXT  H N N 223 
LYS   N    N N N 224 
LYS   CA   C N S 225 
LYS   C    C N N 226 
LYS   O    O N N 227 
LYS   CB   C N N 228 
LYS   CG   C N N 229 
LYS   CD   C N N 230 
LYS   CE   C N N 231 
LYS   NZ   N N N 232 
LYS   OXT  O N N 233 
LYS   H    H N N 234 
LYS   H2   H N N 235 
LYS   HA   H N N 236 
LYS   HB2  H N N 237 
LYS   HB3  H N N 238 
LYS   HG2  H N N 239 
LYS   HG3  H N N 240 
LYS   HD2  H N N 241 
LYS   HD3  H N N 242 
LYS   HE2  H N N 243 
LYS   HE3  H N N 244 
LYS   HZ1  H N N 245 
LYS   HZ2  H N N 246 
LYS   HZ3  H N N 247 
LYS   HXT  H N N 248 
MET   N    N N N 249 
MET   CA   C N S 250 
MET   C    C N N 251 
MET   O    O N N 252 
MET   CB   C N N 253 
MET   CG   C N N 254 
MET   SD   S N N 255 
MET   CE   C N N 256 
MET   OXT  O N N 257 
MET   H    H N N 258 
MET   H2   H N N 259 
MET   HA   H N N 260 
MET   HB2  H N N 261 
MET   HB3  H N N 262 
MET   HG2  H N N 263 
MET   HG3  H N N 264 
MET   HE1  H N N 265 
MET   HE2  H N N 266 
MET   HE3  H N N 267 
MET   HXT  H N N 268 
PHE   N    N N N 269 
PHE   CA   C N S 270 
PHE   C    C N N 271 
PHE   O    O N N 272 
PHE   CB   C N N 273 
PHE   CG   C Y N 274 
PHE   CD1  C Y N 275 
PHE   CD2  C Y N 276 
PHE   CE1  C Y N 277 
PHE   CE2  C Y N 278 
PHE   CZ   C Y N 279 
PHE   OXT  O N N 280 
PHE   H    H N N 281 
PHE   H2   H N N 282 
PHE   HA   H N N 283 
PHE   HB2  H N N 284 
PHE   HB3  H N N 285 
PHE   HD1  H N N 286 
PHE   HD2  H N N 287 
PHE   HE1  H N N 288 
PHE   HE2  H N N 289 
PHE   HZ   H N N 290 
PHE   HXT  H N N 291 
PRO   N    N N N 292 
PRO   CA   C N S 293 
PRO   C    C N N 294 
PRO   O    O N N 295 
PRO   CB   C N N 296 
PRO   CG   C N N 297 
PRO   CD   C N N 298 
PRO   OXT  O N N 299 
PRO   H    H N N 300 
PRO   HA   H N N 301 
PRO   HB2  H N N 302 
PRO   HB3  H N N 303 
PRO   HG2  H N N 304 
PRO   HG3  H N N 305 
PRO   HD2  H N N 306 
PRO   HD3  H N N 307 
PRO   HXT  H N N 308 
SER   N    N N N 309 
SER   CA   C N S 310 
SER   C    C N N 311 
SER   O    O N N 312 
SER   CB   C N N 313 
SER   OG   O N N 314 
SER   OXT  O N N 315 
SER   H    H N N 316 
SER   H2   H N N 317 
SER   HA   H N N 318 
SER   HB2  H N N 319 
SER   HB3  H N N 320 
SER   HG   H N N 321 
SER   HXT  H N N 322 
THR   N    N N N 323 
THR   CA   C N S 324 
THR   C    C N N 325 
THR   O    O N N 326 
THR   CB   C N R 327 
THR   OG1  O N N 328 
THR   CG2  C N N 329 
THR   OXT  O N N 330 
THR   H    H N N 331 
THR   H2   H N N 332 
THR   HA   H N N 333 
THR   HB   H N N 334 
THR   HG1  H N N 335 
THR   HG21 H N N 336 
THR   HG22 H N N 337 
THR   HG23 H N N 338 
THR   HXT  H N N 339 
TRP   N    N N N 340 
TRP   CA   C N S 341 
TRP   C    C N N 342 
TRP   O    O N N 343 
TRP   CB   C N N 344 
TRP   CG   C Y N 345 
TRP   CD1  C Y N 346 
TRP   CD2  C Y N 347 
TRP   NE1  N Y N 348 
TRP   CE2  C Y N 349 
TRP   CE3  C Y N 350 
TRP   CZ2  C Y N 351 
TRP   CZ3  C Y N 352 
TRP   CH2  C Y N 353 
TRP   OXT  O N N 354 
TRP   H    H N N 355 
TRP   H2   H N N 356 
TRP   HA   H N N 357 
TRP   HB2  H N N 358 
TRP   HB3  H N N 359 
TRP   HD1  H N N 360 
TRP   HE1  H N N 361 
TRP   HE3  H N N 362 
TRP   HZ2  H N N 363 
TRP   HZ3  H N N 364 
TRP   HH2  H N N 365 
TRP   HXT  H N N 366 
TYR   N    N N N 367 
TYR   CA   C N S 368 
TYR   C    C N N 369 
TYR   O    O N N 370 
TYR   CB   C N N 371 
TYR   CG   C Y N 372 
TYR   CD1  C Y N 373 
TYR   CD2  C Y N 374 
TYR   CE1  C Y N 375 
TYR   CE2  C Y N 376 
TYR   CZ   C Y N 377 
TYR   OH   O N N 378 
TYR   OXT  O N N 379 
TYR   H    H N N 380 
TYR   H2   H N N 381 
TYR   HA   H N N 382 
TYR   HB2  H N N 383 
TYR   HB3  H N N 384 
TYR   HD1  H N N 385 
TYR   HD2  H N N 386 
TYR   HE1  H N N 387 
TYR   HE2  H N N 388 
TYR   HH   H N N 389 
TYR   HXT  H N N 390 
VAL   N    N N N 391 
VAL   CA   C N S 392 
VAL   C    C N N 393 
VAL   O    O N N 394 
VAL   CB   C N N 395 
VAL   CG1  C N N 396 
VAL   CG2  C N N 397 
VAL   OXT  O N N 398 
VAL   H    H N N 399 
VAL   H2   H N N 400 
VAL   HA   H N N 401 
VAL   HB   H N N 402 
VAL   HG11 H N N 403 
VAL   HG12 H N N 404 
VAL   HG13 H N N 405 
VAL   HG21 H N N 406 
VAL   HG22 H N N 407 
VAL   HG23 H N N 408 
VAL   HXT  H N N 409 
# 
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 
A1AYA C1  N1   sing N N 1   
A1AYA N1  C2   sing N N 2   
A1AYA N1  C5   sing N N 3   
A1AYA C2  C3   sing N N 4   
A1AYA C3  N2   sing N N 5   
A1AYA N2  C4   sing N N 6   
A1AYA N2  C6   sing N N 7   
A1AYA C4  C5   sing N N 8   
A1AYA C6  C7   doub Y N 9   
A1AYA C6  C11  sing Y N 10  
A1AYA C7  C8   sing Y N 11  
A1AYA C8  C9   doub Y N 12  
A1AYA C9  C10  sing Y N 13  
A1AYA C10 C11  doub Y N 14  
A1AYA C11 C12  sing N N 15  
A1AYA C12 O1   sing N N 16  
A1AYA C10 HC11 sing N N 17  
A1AYA C12 HC12 sing N N 18  
A1AYA C12 HC13 sing N N 19  
A1AYA C1  HC15 sing N N 20  
A1AYA C1  HC16 sing N N 21  
A1AYA C1  HC14 sing N N 22  
A1AYA C2  HC3  sing N N 23  
A1AYA C2  HC2  sing N N 24  
A1AYA C3  HC5  sing N N 25  
A1AYA C3  HC4  sing N N 26  
A1AYA C4  HC7  sing N N 27  
A1AYA C4  HC6  sing N N 28  
A1AYA C5  HC8  sing N N 29  
A1AYA C5  HC9  sing N N 30  
A1AYA C7  HC   sing N N 31  
A1AYA C8  HC1  sing N N 32  
A1AYA C9  HC10 sing N N 33  
A1AYA O1  HO   sing N N 34  
ALA   N   CA   sing N N 35  
ALA   N   H    sing N N 36  
ALA   N   H2   sing N N 37  
ALA   CA  C    sing N N 38  
ALA   CA  CB   sing N N 39  
ALA   CA  HA   sing N N 40  
ALA   C   O    doub N N 41  
ALA   C   OXT  sing N N 42  
ALA   CB  HB1  sing N N 43  
ALA   CB  HB2  sing N N 44  
ALA   CB  HB3  sing N N 45  
ALA   OXT HXT  sing N N 46  
ARG   N   CA   sing N N 47  
ARG   N   H    sing N N 48  
ARG   N   H2   sing N N 49  
ARG   CA  C    sing N N 50  
ARG   CA  CB   sing N N 51  
ARG   CA  HA   sing N N 52  
ARG   C   O    doub N N 53  
ARG   C   OXT  sing N N 54  
ARG   CB  CG   sing N N 55  
ARG   CB  HB2  sing N N 56  
ARG   CB  HB3  sing N N 57  
ARG   CG  CD   sing N N 58  
ARG   CG  HG2  sing N N 59  
ARG   CG  HG3  sing N N 60  
ARG   CD  NE   sing N N 61  
ARG   CD  HD2  sing N N 62  
ARG   CD  HD3  sing N N 63  
ARG   NE  CZ   sing N N 64  
ARG   NE  HE   sing N N 65  
ARG   CZ  NH1  sing N N 66  
ARG   CZ  NH2  doub N N 67  
ARG   NH1 HH11 sing N N 68  
ARG   NH1 HH12 sing N N 69  
ARG   NH2 HH21 sing N N 70  
ARG   NH2 HH22 sing N N 71  
ARG   OXT HXT  sing N N 72  
ASN   N   CA   sing N N 73  
ASN   N   H    sing N N 74  
ASN   N   H2   sing N N 75  
ASN   CA  C    sing N N 76  
ASN   CA  CB   sing N N 77  
ASN   CA  HA   sing N N 78  
ASN   C   O    doub N N 79  
ASN   C   OXT  sing N N 80  
ASN   CB  CG   sing N N 81  
ASN   CB  HB2  sing N N 82  
ASN   CB  HB3  sing N N 83  
ASN   CG  OD1  doub N N 84  
ASN   CG  ND2  sing N N 85  
ASN   ND2 HD21 sing N N 86  
ASN   ND2 HD22 sing N N 87  
ASN   OXT HXT  sing N N 88  
ASP   N   CA   sing N N 89  
ASP   N   H    sing N N 90  
ASP   N   H2   sing N N 91  
ASP   CA  C    sing N N 92  
ASP   CA  CB   sing N N 93  
ASP   CA  HA   sing N N 94  
ASP   C   O    doub N N 95  
ASP   C   OXT  sing N N 96  
ASP   CB  CG   sing N N 97  
ASP   CB  HB2  sing N N 98  
ASP   CB  HB3  sing N N 99  
ASP   CG  OD1  doub N N 100 
ASP   CG  OD2  sing N N 101 
ASP   OD2 HD2  sing N N 102 
ASP   OXT HXT  sing N N 103 
GLN   N   CA   sing N N 104 
GLN   N   H    sing N N 105 
GLN   N   H2   sing N N 106 
GLN   CA  C    sing N N 107 
GLN   CA  CB   sing N N 108 
GLN   CA  HA   sing N N 109 
GLN   C   O    doub N N 110 
GLN   C   OXT  sing N N 111 
GLN   CB  CG   sing N N 112 
GLN   CB  HB2  sing N N 113 
GLN   CB  HB3  sing N N 114 
GLN   CG  CD   sing N N 115 
GLN   CG  HG2  sing N N 116 
GLN   CG  HG3  sing N N 117 
GLN   CD  OE1  doub N N 118 
GLN   CD  NE2  sing N N 119 
GLN   NE2 HE21 sing N N 120 
GLN   NE2 HE22 sing N N 121 
GLN   OXT HXT  sing N N 122 
GLU   N   CA   sing N N 123 
GLU   N   H    sing N N 124 
GLU   N   H2   sing N N 125 
GLU   CA  C    sing N N 126 
GLU   CA  CB   sing N N 127 
GLU   CA  HA   sing N N 128 
GLU   C   O    doub N N 129 
GLU   C   OXT  sing N N 130 
GLU   CB  CG   sing N N 131 
GLU   CB  HB2  sing N N 132 
GLU   CB  HB3  sing N N 133 
GLU   CG  CD   sing N N 134 
GLU   CG  HG2  sing N N 135 
GLU   CG  HG3  sing N N 136 
GLU   CD  OE1  doub N N 137 
GLU   CD  OE2  sing N N 138 
GLU   OE2 HE2  sing N N 139 
GLU   OXT HXT  sing N N 140 
GLY   N   CA   sing N N 141 
GLY   N   H    sing N N 142 
GLY   N   H2   sing N N 143 
GLY   CA  C    sing N N 144 
GLY   CA  HA2  sing N N 145 
GLY   CA  HA3  sing N N 146 
GLY   C   O    doub N N 147 
GLY   C   OXT  sing N N 148 
GLY   OXT HXT  sing N N 149 
HIS   N   CA   sing N N 150 
HIS   N   H    sing N N 151 
HIS   N   H2   sing N N 152 
HIS   CA  C    sing N N 153 
HIS   CA  CB   sing N N 154 
HIS   CA  HA   sing N N 155 
HIS   C   O    doub N N 156 
HIS   C   OXT  sing N N 157 
HIS   CB  CG   sing N N 158 
HIS   CB  HB2  sing N N 159 
HIS   CB  HB3  sing N N 160 
HIS   CG  ND1  sing Y N 161 
HIS   CG  CD2  doub Y N 162 
HIS   ND1 CE1  doub Y N 163 
HIS   ND1 HD1  sing N N 164 
HIS   CD2 NE2  sing Y N 165 
HIS   CD2 HD2  sing N N 166 
HIS   CE1 NE2  sing Y N 167 
HIS   CE1 HE1  sing N N 168 
HIS   NE2 HE2  sing N N 169 
HIS   OXT HXT  sing N N 170 
HOH   O   H1   sing N N 171 
HOH   O   H2   sing N N 172 
ILE   N   CA   sing N N 173 
ILE   N   H    sing N N 174 
ILE   N   H2   sing N N 175 
ILE   CA  C    sing N N 176 
ILE   CA  CB   sing N N 177 
ILE   CA  HA   sing N N 178 
ILE   C   O    doub N N 179 
ILE   C   OXT  sing N N 180 
ILE   CB  CG1  sing N N 181 
ILE   CB  CG2  sing N N 182 
ILE   CB  HB   sing N N 183 
ILE   CG1 CD1  sing N N 184 
ILE   CG1 HG12 sing N N 185 
ILE   CG1 HG13 sing N N 186 
ILE   CG2 HG21 sing N N 187 
ILE   CG2 HG22 sing N N 188 
ILE   CG2 HG23 sing N N 189 
ILE   CD1 HD11 sing N N 190 
ILE   CD1 HD12 sing N N 191 
ILE   CD1 HD13 sing N N 192 
ILE   OXT HXT  sing N N 193 
LEU   N   CA   sing N N 194 
LEU   N   H    sing N N 195 
LEU   N   H2   sing N N 196 
LEU   CA  C    sing N N 197 
LEU   CA  CB   sing N N 198 
LEU   CA  HA   sing N N 199 
LEU   C   O    doub N N 200 
LEU   C   OXT  sing N N 201 
LEU   CB  CG   sing N N 202 
LEU   CB  HB2  sing N N 203 
LEU   CB  HB3  sing N N 204 
LEU   CG  CD1  sing N N 205 
LEU   CG  CD2  sing N N 206 
LEU   CG  HG   sing N N 207 
LEU   CD1 HD11 sing N N 208 
LEU   CD1 HD12 sing N N 209 
LEU   CD1 HD13 sing N N 210 
LEU   CD2 HD21 sing N N 211 
LEU   CD2 HD22 sing N N 212 
LEU   CD2 HD23 sing N N 213 
LEU   OXT HXT  sing N N 214 
LYS   N   CA   sing N N 215 
LYS   N   H    sing N N 216 
LYS   N   H2   sing N N 217 
LYS   CA  C    sing N N 218 
LYS   CA  CB   sing N N 219 
LYS   CA  HA   sing N N 220 
LYS   C   O    doub N N 221 
LYS   C   OXT  sing N N 222 
LYS   CB  CG   sing N N 223 
LYS   CB  HB2  sing N N 224 
LYS   CB  HB3  sing N N 225 
LYS   CG  CD   sing N N 226 
LYS   CG  HG2  sing N N 227 
LYS   CG  HG3  sing N N 228 
LYS   CD  CE   sing N N 229 
LYS   CD  HD2  sing N N 230 
LYS   CD  HD3  sing N N 231 
LYS   CE  NZ   sing N N 232 
LYS   CE  HE2  sing N N 233 
LYS   CE  HE3  sing N N 234 
LYS   NZ  HZ1  sing N N 235 
LYS   NZ  HZ2  sing N N 236 
LYS   NZ  HZ3  sing N N 237 
LYS   OXT HXT  sing N N 238 
MET   N   CA   sing N N 239 
MET   N   H    sing N N 240 
MET   N   H2   sing N N 241 
MET   CA  C    sing N N 242 
MET   CA  CB   sing N N 243 
MET   CA  HA   sing N N 244 
MET   C   O    doub N N 245 
MET   C   OXT  sing N N 246 
MET   CB  CG   sing N N 247 
MET   CB  HB2  sing N N 248 
MET   CB  HB3  sing N N 249 
MET   CG  SD   sing N N 250 
MET   CG  HG2  sing N N 251 
MET   CG  HG3  sing N N 252 
MET   SD  CE   sing N N 253 
MET   CE  HE1  sing N N 254 
MET   CE  HE2  sing N N 255 
MET   CE  HE3  sing N N 256 
MET   OXT HXT  sing N N 257 
PHE   N   CA   sing N N 258 
PHE   N   H    sing N N 259 
PHE   N   H2   sing N N 260 
PHE   CA  C    sing N N 261 
PHE   CA  CB   sing N N 262 
PHE   CA  HA   sing N N 263 
PHE   C   O    doub N N 264 
PHE   C   OXT  sing N N 265 
PHE   CB  CG   sing N N 266 
PHE   CB  HB2  sing N N 267 
PHE   CB  HB3  sing N N 268 
PHE   CG  CD1  doub Y N 269 
PHE   CG  CD2  sing Y N 270 
PHE   CD1 CE1  sing Y N 271 
PHE   CD1 HD1  sing N N 272 
PHE   CD2 CE2  doub Y N 273 
PHE   CD2 HD2  sing N N 274 
PHE   CE1 CZ   doub Y N 275 
PHE   CE1 HE1  sing N N 276 
PHE   CE2 CZ   sing Y N 277 
PHE   CE2 HE2  sing N N 278 
PHE   CZ  HZ   sing N N 279 
PHE   OXT HXT  sing N N 280 
PRO   N   CA   sing N N 281 
PRO   N   CD   sing N N 282 
PRO   N   H    sing N N 283 
PRO   CA  C    sing N N 284 
PRO   CA  CB   sing N N 285 
PRO   CA  HA   sing N N 286 
PRO   C   O    doub N N 287 
PRO   C   OXT  sing N N 288 
PRO   CB  CG   sing N N 289 
PRO   CB  HB2  sing N N 290 
PRO   CB  HB3  sing N N 291 
PRO   CG  CD   sing N N 292 
PRO   CG  HG2  sing N N 293 
PRO   CG  HG3  sing N N 294 
PRO   CD  HD2  sing N N 295 
PRO   CD  HD3  sing N N 296 
PRO   OXT HXT  sing N N 297 
SER   N   CA   sing N N 298 
SER   N   H    sing N N 299 
SER   N   H2   sing N N 300 
SER   CA  C    sing N N 301 
SER   CA  CB   sing N N 302 
SER   CA  HA   sing N N 303 
SER   C   O    doub N N 304 
SER   C   OXT  sing N N 305 
SER   CB  OG   sing N N 306 
SER   CB  HB2  sing N N 307 
SER   CB  HB3  sing N N 308 
SER   OG  HG   sing N N 309 
SER   OXT HXT  sing N N 310 
THR   N   CA   sing N N 311 
THR   N   H    sing N N 312 
THR   N   H2   sing N N 313 
THR   CA  C    sing N N 314 
THR   CA  CB   sing N N 315 
THR   CA  HA   sing N N 316 
THR   C   O    doub N N 317 
THR   C   OXT  sing N N 318 
THR   CB  OG1  sing N N 319 
THR   CB  CG2  sing N N 320 
THR   CB  HB   sing N N 321 
THR   OG1 HG1  sing N N 322 
THR   CG2 HG21 sing N N 323 
THR   CG2 HG22 sing N N 324 
THR   CG2 HG23 sing N N 325 
THR   OXT HXT  sing N N 326 
TRP   N   CA   sing N N 327 
TRP   N   H    sing N N 328 
TRP   N   H2   sing N N 329 
TRP   CA  C    sing N N 330 
TRP   CA  CB   sing N N 331 
TRP   CA  HA   sing N N 332 
TRP   C   O    doub N N 333 
TRP   C   OXT  sing N N 334 
TRP   CB  CG   sing N N 335 
TRP   CB  HB2  sing N N 336 
TRP   CB  HB3  sing N N 337 
TRP   CG  CD1  doub Y N 338 
TRP   CG  CD2  sing Y N 339 
TRP   CD1 NE1  sing Y N 340 
TRP   CD1 HD1  sing N N 341 
TRP   CD2 CE2  doub Y N 342 
TRP   CD2 CE3  sing Y N 343 
TRP   NE1 CE2  sing Y N 344 
TRP   NE1 HE1  sing N N 345 
TRP   CE2 CZ2  sing Y N 346 
TRP   CE3 CZ3  doub Y N 347 
TRP   CE3 HE3  sing N N 348 
TRP   CZ2 CH2  doub Y N 349 
TRP   CZ2 HZ2  sing N N 350 
TRP   CZ3 CH2  sing Y N 351 
TRP   CZ3 HZ3  sing N N 352 
TRP   CH2 HH2  sing N N 353 
TRP   OXT HXT  sing N N 354 
TYR   N   CA   sing N N 355 
TYR   N   H    sing N N 356 
TYR   N   H2   sing N N 357 
TYR   CA  C    sing N N 358 
TYR   CA  CB   sing N N 359 
TYR   CA  HA   sing N N 360 
TYR   C   O    doub N N 361 
TYR   C   OXT  sing N N 362 
TYR   CB  CG   sing N N 363 
TYR   CB  HB2  sing N N 364 
TYR   CB  HB3  sing N N 365 
TYR   CG  CD1  doub Y N 366 
TYR   CG  CD2  sing Y N 367 
TYR   CD1 CE1  sing Y N 368 
TYR   CD1 HD1  sing N N 369 
TYR   CD2 CE2  doub Y N 370 
TYR   CD2 HD2  sing N N 371 
TYR   CE1 CZ   doub Y N 372 
TYR   CE1 HE1  sing N N 373 
TYR   CE2 CZ   sing Y N 374 
TYR   CE2 HE2  sing N N 375 
TYR   CZ  OH   sing N N 376 
TYR   OH  HH   sing N N 377 
TYR   OXT HXT  sing N N 378 
VAL   N   CA   sing N N 379 
VAL   N   H    sing N N 380 
VAL   N   H2   sing N N 381 
VAL   CA  C    sing N N 382 
VAL   CA  CB   sing N N 383 
VAL   CA  HA   sing N N 384 
VAL   C   O    doub N N 385 
VAL   C   OXT  sing N N 386 
VAL   CB  CG1  sing N N 387 
VAL   CB  CG2  sing N N 388 
VAL   CB  HB   sing N N 389 
VAL   CG1 HG11 sing N N 390 
VAL   CG1 HG12 sing N N 391 
VAL   CG1 HG13 sing N N 392 
VAL   CG2 HG21 sing N N 393 
VAL   CG2 HG22 sing N N 394 
VAL   CG2 HG23 sing N N 395 
VAL   OXT HXT  sing N N 396 
# 
_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                    7HAU 
_atom_sites.fract_transf_matrix[1][1]   0.015132 
_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]   0.011149 
_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]   0.009980 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU   A 1 9   ? 4.46869   -28.45579 -39.20195 1.000 40.90567 ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.75127   -27.76208 -39.25439 1.000 53.38599 ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 5.96079   -26.90530 -38.01086 1.000 45.19337 ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 5.27655   -25.90098 -37.81614 1.000 47.02449 ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.84216   -26.89721 -40.51272 1.000 64.37385 ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 7.26219   -26.51511 -40.90069 1.000 76.65269 ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 7.49763   -26.58762 -42.39820 1.000 98.99388 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 7.14632   -25.61965 -43.10741 1.000 97.46883 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 8.03657   -27.61380 -42.86577 1.000 97.76421 ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 6.91324   -27.30881 -37.17395 1.000 35.58711 ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 7.19238   -26.65517 -35.90088 1.000 26.21784 ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.54250   -25.96290 -35.99576 1.000 26.93247 ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.53676   -26.58205 -36.39051 1.000 28.78303 ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 7.18004   -27.66265 -34.73863 1.000 31.45099 ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.39143   -26.95108 -33.41659 1.000 32.28753 ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 5.87984   -28.44732 -34.73106 1.000 37.80851 ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.58045   -24.68539 -35.63037 1.000 21.88119 ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.81825   -23.91896 -35.57533 1.000 21.60898 ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 10.24636  -23.75992 -34.12298 1.000 20.35711 ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.44048   -23.36124 -33.27909 1.000 18.21283 ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.64189   -22.54649 -36.22760 1.000 24.05645 ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.44809   -22.59121 -37.72773 1.000 21.42728 ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 9.21398   -21.21577 -38.33233 1.000 36.03952 ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 8.12291   -20.64843 -38.11241 1.000 39.21399 ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 10.11356  -20.70364 -39.03209 1.000 39.29008 ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.50601  -24.08158 -33.83359 1.000 16.96781 ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 12.05999  -23.96169 -32.49091 1.000 15.56976 ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 13.02801  -22.78821 -32.44535 1.000 17.67346 ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 13.90404  -22.66476 -33.31031 1.000 15.63088 ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.76534  -25.25349 -32.07166 1.000 16.18945 ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.86184  -26.35482 -32.21084 1.000 19.82808 ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 13.23456  -25.17028 -30.62667 1.000 18.29815 ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 12.86078  -21.93293 -31.44064 1.000 16.86662 ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.64638  -20.72102 -31.27388 1.000 16.69450 ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.32269  -20.72941 -29.91310 1.000 21.72346 ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.79150  -21.27520 -28.94162 1.000 18.51460 ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.77926  -19.45753 -31.34307 1.000 13.16539 ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 12.03826  -19.28251 -32.62989 1.000 14.60569 ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.82356  -19.91932 -32.83750 1.000 20.11246 ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.53940  -18.45659 -33.62565 1.000 18.16408 ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 10.13635  -19.75333 -34.02224 1.000 21.27347 ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 11.84644  -18.27691 -34.81042 1.000 21.94130 ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.64541  -18.92835 -35.00846 1.000 23.18406 ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.47379  -20.07187 -29.83995 1.000 16.24141 ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 16.14997  -19.84380 -28.57262 1.000 13.81041 ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.68171  -18.52089 -27.97948 1.000 16.12374 ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.59962  -17.51190 -28.68630 1.000 15.77900 ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.66849  -19.83513 -28.76398 1.000 13.52495 ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.34992  -18.53004 -26.68879 1.000 12.97653 ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 15.12636  -17.27132 -25.99240 1.000 18.84249 ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.39063  -16.42687 -26.04321 1.000 16.46013 ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.50763  -16.95144 -25.98681 1.000 17.73323 ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.74479  -17.51426 -24.52951 1.000 16.58716 ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.33114  -17.98379 -24.32742 1.000 13.93920 ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.25809  -17.15688 -24.62041 1.000 17.23835 ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.07794  -19.25679 -23.84027 1.000 14.80742 ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.95507  -17.58572 -24.42085 1.000 17.77704 ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.78248  -19.69218 -23.63969 1.000 15.55088 ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.71768  -18.85327 -23.92933 1.000 14.21748 ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.21701  -15.11260 -26.14851 1.000 18.55071 ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.33507  -14.22615 -25.86089 1.000 19.88949 ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.85503  -14.51595 -24.45833 1.000 17.62362 ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.09066  -14.85790 -23.55082 1.000 16.39989 ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.91251  -12.76307 -25.97134 1.000 19.68258 ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.54179  -12.31555 -27.36254 1.000 23.37362 ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 16.04317  -10.88978 -27.37927 1.000 34.46759 ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.83840  -10.64636 -27.35557 1.000 33.13712 ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.96913  -9.93437  -27.42431 1.000 36.56301 ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.17400  -14.38656 -24.28952 1.000 16.81940 ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.80716  -14.77150 -23.03109 1.000 17.21648 ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.15613  -14.08486 -21.83724 1.000 16.70915 ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 18.93909  -14.71134 -20.79329 1.000 20.56023 ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.30602  -14.46139 -23.08285 1.000 19.82526 ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.81322  -12.80262 -21.97673 1.000 21.66575 ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.21090  -12.07759 -20.86505 1.000 24.84830 ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.82990  -12.61620 -20.51048 1.000 19.51621 ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.44978  -12.61390 -19.33508 1.000 19.44700 ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.13819  -10.58367 -21.18487 1.000 32.31368 ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.49228  -9.90793  -21.41228 1.000 37.12853 ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.05103  -10.08565 -22.81925 1.000 43.06507 ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.48061  -10.85903 -23.62079 1.000 28.25928 ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.06828  -9.43121  -23.12815 1.000 50.38297 ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.06833  -13.08975 -21.50073 1.000 18.66840 ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.74729  -13.63640 -21.20460 1.000 18.83368 ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.87795  -15.01627 -20.56678 1.000 16.24719 ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.12835  -15.36533 -19.64539 1.000 18.18665 ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.86649  -13.66616 -22.47270 1.000 19.59663 ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.30111  -12.27845 -22.81224 1.000 21.83093 ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.69300  -14.61914 -22.29283 1.000 16.89886 ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.31708  -11.17992 -23.07825 1.000 28.39569 ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.84555  -15.81501 -21.02635 1.000 15.25604 ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.11568  -17.08867 -20.36797 1.000 14.36987 ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.49035  -16.87128 -18.90800 1.000 17.02033 ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.07310  -17.63288 -18.02644 1.000 21.07874 ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.23523  -17.83706 -21.09867 1.000 16.63986 ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.27627  -15.82982 -18.63424 1.000 20.14929 ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.67680  -15.55345 -17.26047 1.000 21.60175 ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.48076  -15.11061 -16.42730 1.000 19.18677 ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.37614  -15.46235 -15.24603 1.000 22.10540 ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.78321  -14.49836 -17.25057 1.000 20.63102 ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 19.44452  -14.27366 -15.89894 1.000 36.12431 ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.44595  -13.12750 -15.92783 1.000 46.06772 ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 20.65752  -12.49593 -16.96774 1.000 49.15710 ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 21.07241  -12.85907 -14.78597 1.000 44.24025 ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.55861  -14.35674 -17.03484 1.000 19.07982 ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.34262  -13.95920 -16.33135 1.000 19.52178 ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.50118  -15.17246 -15.95380 1.000 25.04097 ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.03309  -15.28178 -14.81162 1.000 21.73195 ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.52928  -12.98549 -17.18485 1.000 22.34682 ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.11994  -12.67618 -16.66539 1.000 22.72892 ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.16488  -11.76721 -15.44436 1.000 24.65254 ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.25248  -12.07038 -17.76266 1.000 20.58936 ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.29471  -16.10861 -16.88984 1.000 15.34303 ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.45253  -17.24376 -16.53508 1.000 19.72699 ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.13105  -18.15707 -15.52618 1.000 20.71791 ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.45554  -18.72476 -14.66128 1.000 19.01675 ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 11.97178  -18.06782 -17.73664 1.000 19.08941 ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.15724  -17.33896 -18.82577 1.000 19.15721 ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.40687  -17.93964 -20.52195 1.000 18.68333 ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.32959  -19.35914 -20.43272 1.000 16.92994 ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.45495  -18.32780 -15.61199 1.000 19.70984 ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.10564  -19.15695 -14.60025 1.000 18.02048 ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 15.00030  -18.51747 -13.21763 1.000 21.56053 ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.83309  -19.22411 -12.21606 1.000 25.49546 ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.56307  -19.43502 -14.97866 1.000 25.62874 ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.32681  -18.24424 -15.05572 1.000 44.96697 ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.05555  -17.18674 -13.14215 1.000 18.86149 ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.87024  -16.52147 -11.85534 1.000 18.75320 ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.45447  -16.73089 -11.33092 1.000 25.02269 ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.25830  -17.00461 -10.14074 1.000 22.39374 ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.19007  -15.02857 -11.98652 1.000 26.30349 ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 15.14497  -14.12874 -10.73932 1.000 33.17178 ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 16.08129  -12.94100 -10.92045 1.000 37.96236 ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 13.73386  -13.62755 -10.45174 1.000 34.11809 ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.45524  -16.59395 -12.20226 1.000 17.35227 ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.07099  -16.79314 -11.78484 1.000 18.08068 ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.86112  -18.22395 -11.30674 1.000 24.26976 ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.12346  -18.47658 -10.34333 1.000 23.88350 ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.12257  -16.42839 -12.94068 1.000 15.79661 ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.08532  -14.90830 -13.11788 1.000 17.78187 ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.72392   -17.00116 -12.69160 1.000 15.17925 ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.51241   -14.44786 -14.44469 1.000 22.42694 ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.53408  -19.17787 -11.94787 1.000 17.69485 ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.30891  -20.58365 -11.63769 1.000 22.06411 ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.03033  -20.98584 -10.35655 1.000 25.01792 ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.50682  -21.77352 -9.55976  1.000 29.22176 ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.73756  -21.45318 -12.83612 1.000 23.46249 ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.72196  -21.32989 -13.97484 1.000 21.39883 ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.92944  -22.91103 -12.42462 1.000 26.00372 ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.24409  -21.84058 -15.30928 1.000 18.94352 ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.22410  -20.43812 -10.11913 1.000 25.59307 ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.10247  -20.95987 -9.07702  1.000 24.94675 ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.10702  -20.14825 -7.78759  1.000 32.07829 ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.52554  -20.67833 -6.75112  1.000 34.51864 ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.53623  -21.05602 -9.60361  1.000 30.71846 ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.66016  -22.02531 -10.75182 1.000 32.34119 ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.21302  -23.16981 -10.66231 1.000 39.13659 ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.25822  -21.57204 -11.84585 1.000 44.96458 ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.67391  -18.89048 -7.81519  1.000 21.95293 ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.67774  -18.07870 -6.60320  1.000 23.84578 ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.58951  -18.55095 -5.64717  1.000 29.06856 ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.44651  -18.77365 -6.05881  1.000 28.71925 ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.46213  -16.60331 -6.94704  1.000 27.98025 ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.52347  -16.14359 -7.79376  1.000 28.32015 ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.41865  -15.75205 -5.67985  1.000 28.85296 ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.93716  -18.70369 -4.36954  1.000 22.89796 ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.91099  -18.97491 -3.37315  1.000 25.19223 ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.06226  -17.72572 -3.18246  1.000 27.14114 ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.56972  -16.67615 -2.76693  1.000 23.26642 ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.51535  -19.41036 -2.04289  1.000 24.22457 ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.47778  -19.74193 -1.00284  1.000 28.08003 ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.72127  -20.89871 -1.10353  1.000 29.99105 ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.23246  -18.87943 0.05455   1.000 27.83802 ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.75230   -21.20011 -0.15599  1.000 28.87343 ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.26260  -19.17418 1.00402   1.000 34.64239 ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.52715   -20.33743 0.90002   1.000 29.35015 ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.76953   -17.84438 -3.47398  1.000 22.55249 ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.86958   -16.69662 -3.42978  1.000 19.79990 ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.44540   -17.22666 -3.29999  1.000 19.41859 ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.91591   -17.81383 -4.24612  1.000 22.07361 ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.04844   -15.83856 -4.67641  1.000 22.10403 ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.02715   -14.74716 -4.80321  1.000 24.68061 ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.08482   -13.61753 -3.99680  1.000 28.14296 ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 6.99699   -14.84645 -5.72939  1.000 26.29770 ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.13718   -12.61864 -4.10650  1.000 31.75294 ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.05033   -13.85520 -5.84592  1.000 26.91523 ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.12634   -12.74745 -5.03581  1.000 32.52123 ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.17822   -11.76785 -5.15888  1.000 46.53162 ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.83070   -17.02228 -2.13280  1.000 19.47137 ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.57917   -17.70236 -1.81642  1.000 19.58151 ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.35438   -17.05843 -2.45498  1.000 22.92801 ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.34548   -17.74558 -2.64756  1.000 24.89989 ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.38981   -17.76285 -0.29918  1.000 25.50736 ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.37833   -18.58942 0.28483   1.000 25.71176 ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.41252   -15.77167 -2.79425  1.000 23.06645 ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.22884   -15.03194 -3.23524  1.000 19.91856 ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 2.97020   -15.26154 -4.73171  1.000 23.98542 ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 2.96231   -14.34666 -5.55499  1.000 21.71101 ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.40669   -13.55685 -2.89411  1.000 22.96422 ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.19582   -12.71531 -3.24542  1.000 23.14562 ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.05248   -13.14004 -3.06815  1.000 27.85881 ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.44312   -11.50321 -3.72649  1.000 28.77308 ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.73032   -16.53053 -5.07483  1.000 14.20858 ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.63596   -16.92119 -6.47811  1.000 15.69652 ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.35181   -16.44656 -7.14189  1.000 16.42727 ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.30082   -16.38108 -8.37570  1.000 16.88723 ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.73322   -18.44212 -6.61259  1.000 20.22693 ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.10948   -19.03415 -6.31339  1.000 19.00641 ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.09316   -20.55134 -6.50524  1.000 24.05230 ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.46909   -21.18656 -6.30120  1.000 17.69809 ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.38314   -20.92150 -7.45075  1.000 21.65776 ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.31964   -16.11738 -6.35989  1.000 16.53392 ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -1.00080  -15.85057 -6.92671  1.000 18.12495 ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -1.01348  -14.65011 -7.86433  1.000 20.32599 ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.94151  -14.52286 -8.67272  1.000 21.44914 ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -2.02137  -15.63262 -5.80667  1.000 19.01592 ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.83719  -14.33611 -5.03453  1.000 18.68455 ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.72620  -14.24881 -3.80763  1.000 27.59936 ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.81879  -15.24696 -3.06174  1.000 29.44957 ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.32835  -13.17831 -3.58518  1.000 36.84468 ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? -0.01044  -13.77151 -7.78171  1.000 17.78990 ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.01622   -12.57220 -8.61173  1.000 14.66324 ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.09784   -12.89099 -10.09621 1.000 14.93053 ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? -0.11578  -11.99696 -10.92083 1.000 16.33452 ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.18890   -11.65343 -8.21069  1.000 19.87187 ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.53451   -12.36051 -8.39967  1.000 18.92400 ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 1.01589   -11.16712 -6.77516  1.000 23.43997 ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.24736   -12.00546 -9.70358  1.000 21.74520 ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.42819   -14.13391 -10.46428 1.000 13.92105 ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.45412   -14.49756 -11.88137 1.000 17.25525 ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.88111  -14.18092 -12.55189 1.000 17.30639 ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.91968  -13.71714 -13.69824 1.000 13.89656 ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.79467   -15.98663 -12.05052 1.000 16.40343 ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.39222  -16.90067 -11.87207 1.000 15.37245 ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.73584  -17.37120 -10.61847 1.000 17.55450 ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.18403  -17.26350 -12.95891 1.000 18.18862 ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.84418  -18.19661 -10.44738 1.000 17.07743 ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.29404  -18.07881 -12.78947 1.000 16.79812 ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.62293  -18.54625 -11.52942 1.000 13.27386 ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.99184  -14.43849 -11.85664 1.000 14.33978 ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.29380  -14.24711 -12.48300 1.000 13.00172 ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.57389  -12.76834 -12.70362 1.000 15.19547 ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.09644  -12.37864 -13.75730 1.000 15.36434 ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.38638  -14.88920 -11.63184 1.000 12.90266 ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.76345  -14.93944 -12.28807 1.000 14.82029 ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.68057  -15.68828 -13.61524 1.000 14.62433 ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.77287  -15.59344 -11.35697 1.000 19.42941 ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.21817  -11.93076 -11.72429 1.000 15.30860 ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.34754  -10.48730 -11.89492 1.000 16.65570 ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.57674  -10.01269 -13.11856 1.000 17.64718 ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -3.07630  -9.19512  -13.90242 1.000 18.08867 ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.84782  -9.76869  -10.64063 1.000 19.14513 ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.70583  -8.25580  -10.79948 1.000 19.73456 ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -2.05641  -7.62619  -9.57048  1.000 22.43641 ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.61187  -7.84212  -9.53767  1.000 30.50524 ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.14657   -7.70424  -8.45626  1.000 27.43788 ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.36599  -7.33853  -7.29144  1.000 28.79421 ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.45504   -7.93183  -8.54637  1.000 30.26508 ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.35529  -10.52062 -13.30193 1.000 13.40854 ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.52773  -10.06496 -14.41270 1.000 13.60451 ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.12667  -10.47170 -15.75302 1.000 16.12069 ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -1.14888  -9.67376  -16.69815 1.000 15.03167 ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.89170   -10.61464 -14.26754 1.000 12.54989 ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.63547   -10.11941 -13.02736 1.000 21.01471 ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.58135   -8.60850  -12.85515 1.000 27.24031 ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.65664   -7.88217  -13.86854 1.000 25.77660 ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.45997   -8.14538  -11.70032 1.000 31.38076 ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.62858  -11.70341 -15.85407 1.000 13.96181 ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.19700  -12.15287 -17.12270 1.000 15.05601 ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.52060  -11.46023 -17.42100 1.000 15.78981 ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.81766  -11.15574 -18.58299 1.000 15.49272 ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.38052  -13.66587 -17.11328 1.000 12.05741 ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.10156  -14.48533 -16.97080 1.000 15.68791 ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.43439  -15.96878 -16.83455 1.000 14.10219 ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.15577  -14.22063 -18.14196 1.000 15.93685 ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.33944  -11.21969 -16.39459 1.000 11.00012 ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.58074  -10.48880 -16.62085 1.000 15.08020 ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.26976  -9.05936  -17.04143 1.000 17.56638 ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.92340  -8.50058  -17.93144 1.000 16.35446 ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.47570  -10.55372 -15.36823 1.000 14.86817 ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -7.06423  -11.96383 -15.22940 1.000 13.33450 ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.57937  -9.49084  -15.41930 1.000 17.72329 ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.79106  -12.20934 -13.89971 1.000 19.04273 ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.22871  -8.46597  -16.45321 1.000 14.40220 ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.84832  -7.11229  -16.83199 1.000 16.70350 ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.33512  -7.07776  -18.26846 1.000 17.02195 ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.66935  -6.16477  -19.03215 1.000 15.76064 ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.80834  -6.57450  -15.84845 1.000 21.93154 ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.05760  -5.51961  -16.41300 1.000 26.17194 ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.54632  -8.08161  -18.65915 1.000 13.29627 ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.15286  -8.22045  -20.05762 1.000 17.78693 ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.36962  -8.29529  -20.96982 1.000 20.55964 ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.39127  -7.68006  -22.04470 1.000 13.34762 ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.29703  -9.47110  -20.22976 1.000 17.50266 ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.11327   -9.27002  -19.75846 1.000 26.46186 ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.51452   -8.15466  -19.41741 1.000 19.81328 ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 0.88655   -10.34595 -19.74895 1.000 21.35299 ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.38137  -9.06512  -20.56589 1.000 12.21599 ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.58690  -9.19943  -21.37610 1.000 14.22866 ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.31879  -7.86825  -21.49006 1.000 14.24200 ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.76974  -7.49150  -22.57813 1.000 14.94614 ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.50168  -10.27098 -20.77819 1.000 13.19463 ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -5.96690  -11.57251 -20.95420 1.000 14.22190 ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.43069  -7.13306  -20.37834 1.000 14.78736 ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.07960  -5.82652  -20.42168 1.000 18.47537 ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.34135  -4.87682  -21.35918 1.000 18.90130 ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.97483  -4.13541  -22.11972 1.000 15.65989 ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.16819  -5.23593  -19.01358 1.000 14.36965 ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.76944  -3.94721  -19.02979 1.000 19.38420 ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -5.00108  -4.88379  -21.31876 1.000 16.13767 ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.21940  -4.06336  -22.24359 1.000 16.78120 ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.52043  -4.41188  -23.69869 1.000 19.82893 ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.63126  -3.51827  -24.54458 1.000 16.56855 ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.71668  -4.20828  -21.97308 1.000 15.50378 ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.26944  -3.53246  -20.67890 1.000 22.69079 ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -3.08648  -2.83866  -20.03063 1.000 21.39512 ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -1.07944  -3.68268  -20.31816 1.000 23.79691 ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.65076  -5.70838  -24.01204 1.000 15.34187 ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -4.89011  -6.11850  -25.39590 1.000 16.22210 ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.30495  -5.77007  -25.84096 1.000 16.04668 ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.53480  -5.44147  -27.00959 1.000 14.02715 ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.63746  -7.61874  -25.56000 1.000 13.60842 ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.26590  -5.84049  -24.92129 1.000 10.79155 ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.62004  -5.39929  -25.22627 1.000 12.92383 ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.67627  -3.89175  -25.43702 1.000 15.82549 ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.38687  -3.41792  -26.33106 1.000 14.07489 ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.56340  -5.83805  -24.10870 1.000 14.52925 ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.80795  -7.34867  -24.08261 1.000 12.93053 ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.18143 -7.81286  -22.67716 1.000 15.01604 ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.89684 -7.73128  -25.07003 1.000 12.35067 ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.93434  -3.12146  -24.62834 1.000 15.34992 ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.85214  -1.67901  -24.84852 1.000 16.59444 ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.39630  -1.36733  -26.26832 1.000 17.25389 ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.89722  -0.42947  -26.90057 1.000 16.08953 ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.88755  -1.02651  -23.85309 1.000 15.51096 ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.44107  -0.94270  -22.44184 1.000 19.41473 ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.61915  -1.29210  -22.21324 1.000 20.91272 ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.67807  -0.50854  -21.55055 1.000 24.74238 ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.44438  -2.15295  -26.78448 1.000 12.80136 ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.84464  -1.85894  -28.08325 1.000 16.73389 ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.83725  -2.05388  -29.21960 1.000 16.39090 ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -6.91531  -1.22298  -30.13369 1.000 19.42713 ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.61199  -2.73334  -28.30592 1.000 16.06330 ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.41592  -2.35818  -27.44342 1.000 19.27844 ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.24948  -3.30780  -27.71141 1.000 21.25584 ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.24939  -3.31400  -26.56713 1.000 29.49266 ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 0.01872   -3.99166  -26.96437 1.000 38.41940 ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.57931  -3.16407  -29.20859 1.000 15.66545 ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.55124  -3.36437  -30.27993 1.000 17.06758 ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.71908  -2.39568  -30.13123 1.000 18.26739 ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.27755 -1.93652  -31.13515 1.000 18.89440 ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -9.01846  -4.83336  -30.34759 1.000 18.35249 ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.83308  -5.07406  -31.62270 1.000 21.56069 ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.83385  -5.22105  -29.12117 1.000 16.08736 ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -9.08442  -4.76228  -32.91010 1.000 23.52969 ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.09324 -2.03847  -28.89754 1.000 15.87803 ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.15047 -1.04608  -28.72229 1.000 16.23836 ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.74966 0.29591   -29.32338 1.000 18.41702 ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.54041 0.93207   -30.03014 1.000 19.79114 ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.50965 -0.87929  -27.24417 1.000 18.36707 ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.64548 0.12008   -27.06857 1.000 24.81169 ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -13.03793 0.35564   -25.62367 1.000 38.49616 ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.18003 -0.45769  -25.22289 1.000 46.42091 ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.35183 -0.95603  -24.00674 1.000 41.40103 ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.46674 -0.74972  -23.04522 1.000 40.85626 ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.44381 -1.66926  -23.74563 1.000 34.04380 ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.51642  0.74171   -29.06192 1.000 17.27030 ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -9.07532  2.01956   -29.61223 1.000 17.99236 ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -9.06808  1.99206   -31.13498 1.000 20.77725 ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.46317  2.96862   -31.78086 1.000 22.37775 ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.68695  2.38804   -29.08865 1.000 18.34778 ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.23046  3.74010   -29.59438 1.000 26.26912 ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.73463  4.91244   -29.04698 1.000 22.19719 ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.32718  3.84335   -30.64499 1.000 23.82048 ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.33952  6.14711   -29.51755 1.000 22.58014 ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.92480  5.07392   -31.12035 1.000 25.22408 ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.43151  6.22130   -30.55359 1.000 27.67134 ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -6.03295  7.44950   -31.02745 1.000 36.41249 ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.62230  0.88187   -31.72842 1.000 18.11923 ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.59422  0.79242   -33.18585 1.000 22.81767 ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -10.00044 0.83777   -33.76379 1.000 29.39900 ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.23432 1.45612   -34.80953 1.000 26.74328 ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.88679  -0.48776  -33.62350 1.000 24.31904 ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.39690  -0.50674  -33.33995 1.000 28.88306 ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.65612  -1.50173  -34.21056 1.000 38.28088 ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -6.29261  -2.46524  -34.68230 1.000 38.70107 ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -4.43520  -1.33275  -34.41023 1.000 37.06357 ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.95248 0.19429   -33.08876 1.000 22.16734 ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.33022 0.17029   -33.56140 1.000 20.85600 ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -13.00751 1.52992   -33.45918 1.000 24.34042 ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -14.06379 1.72496   -34.06744 1.000 23.79544 ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.13100 -0.86546  -32.77569 1.000 21.15125 ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.45241 -0.38618  -31.47850 1.000 23.97691 ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.43496 2.46959   -32.70192 1.000 18.73384 ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -13.04865 3.78961   -32.58373 1.000 25.27005 ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -13.07023 4.52309   -33.91627 1.000 26.47604 ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.99643 5.29673   -34.18276 1.000 30.18596 ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.30997 4.62543   -31.53913 1.000 26.17614 ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.47366 4.17673   -30.08815 1.000 26.48879 ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.83677 5.18854   -29.14665 1.000 27.06381 ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.94587 3.97698   -29.75398 1.000 29.38987 ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -12.06150 4.31096   -34.75865 1.000 26.39256 ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -12.01656 4.94365   -36.06951 1.000 31.42095 ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.23226 3.97338   -37.22221 1.000 31.74025 ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.36786 4.42081   -38.36545 1.000 43.18188 ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.67758 5.66954   -36.26989 1.000 39.16473 ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.61029  4.71310   -36.28641 1.000 42.53432 ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.44277 6.68071   -35.15658 1.000 31.27658 ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.26316 2.66826   -36.96080 1.000 35.16027 ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.46495 1.66398   -38.00413 1.000 33.84219 ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.29849 0.54350   -37.40220 1.000 27.12444 ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.76188 -0.40486  -36.81453 1.000 27.85842 ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -11.12875 1.14570   -38.54023 1.000 31.20264 ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.29244 0.14397   -39.67285 1.000 42.79328 ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.43616 -0.09317  -40.11261 1.000 40.78259 ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.26691 -0.40721  -40.12741 1.000 43.12145 ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.62680 0.62790   -37.50931 1.000 37.78665 ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.47659 -0.39088  -36.87059 1.000 30.83029 ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.29061 -1.78852  -37.43821 1.000 35.47305 ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.54760 -2.76896  -36.72835 1.000 28.44844 ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.89518 0.13844   -37.12107 1.000 40.44494 ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.71002 1.61608   -37.30361 1.000 41.65204 ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.42549 1.72903   -38.07074 1.000 34.38545 ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.83827 -1.91862  -38.69010 1.000 32.05181 ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.62952 -3.24559  -39.25888 1.000 31.04333 ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.54574 -4.03071  -38.53065 1.000 36.07412 ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.44702 -5.24684  -38.72585 1.000 25.97399 ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.28677 -3.13998  -40.74722 1.000 29.42634 ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -13.00832 -2.56629  -40.94137 1.000 31.02787 ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.74105 -3.37569  -37.69109 1.000 21.93863 ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.76245 -4.09837  -36.89047 1.000 23.40242 ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.41824 -5.07316  -35.92182 1.000 27.33983 ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.73752 -5.96059  -35.39615 1.000 23.81694 ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.88900 -3.10462  -36.12697 1.000 29.48732 ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -10.07715 -2.20075  -37.03729 1.000 36.34777 ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.59520  -2.48730  -36.92697 1.000 32.10341 ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.78752  -1.57015  -37.83300 1.000 24.41309 ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.37828  -2.04749  -37.93883 1.000 44.02329 ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.71646 -4.92590  -35.66372 1.000 26.40745 ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.44611 -5.84831  -34.80707 1.000 21.12640 ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.25907 -6.86401  -35.59793 1.000 27.55859 ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -16.07941 -7.57508  -35.00871 1.000 23.88287 ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.35972 -5.07793  -33.85253 1.000 27.60745 ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.66394 -4.15751  -32.85242 1.000 24.79008 ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.68293 -3.51908  -31.91325 1.000 28.41182 ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.61152 -4.93335  -32.07147 1.000 23.89349 ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -15.05218 -6.95013  -36.91639 1.000 22.75320 ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.74804 -7.96793  -37.70307 1.000 25.08578 ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.38788 -9.37140  -37.23421 1.000 30.54619 ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.18426 -10.30509 -37.39005 1.000 30.27914 ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.42051 -7.80806  -39.18738 1.000 25.49821 ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -16.10910 -6.60775  -39.81573 1.000 40.70041 ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -16.87193 -5.90990  -39.11305 1.000 35.04613 ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.87974 -6.36029  -41.01899 1.000 36.54221 ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.20095 -9.53373  -36.65996 1.000 23.90054 ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.74176 -10.79137 -36.09054 1.000 25.22485 ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.30119 -11.05102 -34.69867 1.000 33.92078 ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -13.92201 -12.04811 -34.07517 1.000 29.73206 ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.21179 -10.80121 -36.04355 1.000 27.64230 ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.71713 -9.57248  -35.52818 1.000 22.61480 ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.17974 -10.18240 -34.19874 1.000 27.15135 ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.78796 -10.36151 -32.89351 1.000 28.20083 ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -16.04924 -9.05491  -32.17016 1.000 22.69918 ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.11030 -8.32239  -31.84406 1.000 20.52955 ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.32151 -8.75001  -31.90420 1.000 21.27675 ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.66555 -7.50585  -31.22554 1.000 21.82775 ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.49768 -7.57879  -29.71100 1.000 25.20269 ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.31780 -6.53592  -29.07409 1.000 29.01532 ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -19.10734 -7.10394  -31.55633 1.000 21.46741 ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.42263 -7.09426  -33.04520 1.000 47.43025 ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.25248 -5.87526  -33.42517 1.000 46.02781 ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.40968 -5.75355  -34.93439 1.000 67.67553 ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -20.22144 -7.06030  -35.62370 1.000 69.01144 ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.54704 -8.76946  -29.11872 1.000 23.64263 ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.50763 -8.88617  -27.66535 1.000 19.60139 ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.08132 -8.72927  -27.15350 1.000 20.25980 ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.14951 -9.33518  -27.68791 1.000 23.81059 ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -18.08175 -10.22956 -27.21435 1.000 28.29399 ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -19.58982 -10.37425 -27.38313 1.000 33.72910 ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -20.01210 -10.56179 -28.82854 1.000 62.07240 ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -21.03560 -9.96773  -29.23520 1.000 67.40759 ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -19.32311 -11.30847 -29.55610 1.000 62.32909 ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -15.92093 -7.92720  -26.10665 1.000 19.03525 ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.62466 -7.63873  -25.48979 1.000 15.56192 ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.68667 -8.15423  -24.05508 1.000 16.24122 ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.30036 -7.51465  -23.19373 1.000 16.68338 ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.34211 -6.13888  -25.53951 1.000 18.74818 ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.21776 -5.50375  -26.93035 1.000 28.96326 ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.76168 -4.05929  -26.81688 1.000 34.93760 ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.26232 -6.28873  -27.82301 1.000 19.09806 ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -14.07576 -9.31140  -23.79252 1.000 15.80111 ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.21741 -9.94881  -22.48896 1.000 15.07557 ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -13.00983 -10.82064 -22.17213 1.000 12.82919 ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.14714 -11.07420 -23.01961 1.000 13.65630 ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.49402 -10.79284 -22.42911 1.000 17.62098 ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.52843 -11.89955 -23.43923 1.000 19.83340 ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.53022 -12.01803 -24.37561 1.000 27.73547 ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.69085 -12.94230 -23.65079 1.000 22.97550 ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.30422 -13.08016 -25.12838 1.000 23.97713 ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.19474 -13.65867 -24.70995 1.000 23.19203 ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -12.98663 -11.30301 -20.92864 1.000 13.76478 ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -11.95644 -12.19390 -20.41001 1.000 12.65907 ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.63934 -13.40200 -19.78300 1.000 17.22682 ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.52014 -13.24063 -18.93163 1.000 13.67737 ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.07222 -11.49262 -19.36162 1.000 13.97552 ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.46894 -10.20666 -19.93050 1.000 13.02413 ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -9.99435  -12.46035 -18.86855 1.000 13.38700 ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.67405  -9.39035  -18.90859 1.000 13.48967 ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.23196 -14.60706 -20.18897 1.000 13.56381 ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.75009 -15.83912 -19.60497 1.000 16.62240 ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.64094 -16.60209 -18.89149 1.000 17.61084 ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.51986 -16.71702 -19.39735 1.000 14.58773 ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.39439 -16.75463 -20.66222 1.000 15.13375 ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.60967 -16.14010 -21.30427 1.000 17.54643 ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.31406 -15.33189 -20.68904 1.000 17.65820 ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.87899 -16.53006 -22.54736 1.000 18.83273 ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -11.96694 -17.13175 -17.71757 1.000 14.00087 ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -11.06854 -17.97877 -16.94443 1.000 10.67070 ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.64998 -19.38392 -16.92007 1.000 12.89049 ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.75371 -19.59417 -16.40082 1.000 12.14297 ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.89327 -17.44137 -15.52476 1.000 11.66458 ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.51317 -15.96425 -15.39948 1.000 16.61607 ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.45564 -15.55388 -13.94252 1.000 11.66650 ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.18222  -15.70602 -16.07757 1.000 13.82007 ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.92697 -20.33925 -17.48021 1.000 13.71780 ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.43107 -21.68598 -17.69938 1.000 13.53990 ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.51646 -22.67217 -16.99489 1.000 16.55492 ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.45787  -23.03643 -17.52970 1.000 14.87765 ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.56338 -22.00668 -19.19380 1.000 14.19523 ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.29061 -20.87379 -19.92724 1.000 16.86941 ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.27180 -23.33175 -19.38793 1.000 14.97711 ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.41503 -21.08597 -21.42401 1.000 22.00261 ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.87215 -23.14214 -15.81011 1.000 16.18191 ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.10739 -24.21077 -15.17443 1.000 16.81689 ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.57442 -25.57493 -15.65804 1.000 18.35137 ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.75122 -25.78793 -15.95914 1.000 19.77104 ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.40324 -24.01552 -13.68411 1.000 16.83060 ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.79637 -23.43726 -13.65876 1.000 18.02608 ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -12.03056 -22.73036 -14.98753 1.000 17.06115 ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.62278  -26.50056 -15.74698 1.000 16.80474 ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.90533  -27.87742 -16.14781 1.000 16.77141 ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -9.07065  -28.79880 -15.27064 1.000 21.50449 ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.85722  -28.90653 -15.46399 1.000 20.84853 ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.59608  -28.10038 -17.62900 1.000 19.15040 ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -10.09388 -29.44241 -18.13631 1.000 26.25260 ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.75724  -30.49297 -17.59118 1.000 26.44727 ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.89965 -29.41104 -19.18958 1.000 35.35974 ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.71829  -29.47428 -14.31810 1.000 25.25324 ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -8.97578  -30.30831 -13.37632 1.000 26.78136 ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.47193  -31.59370 -14.02177 1.000 30.82607 ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.44113  -32.12814 -13.59898 1.000 25.81518 ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.84490  -30.64010 -12.16225 1.000 24.44809 ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -10.08981 -29.46465 -11.22847 1.000 30.26211 ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.99744 -29.86321 -10.07678 1.000 32.55578 ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.28502 -28.69157 -9.15036  1.000 34.11615 ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -12.12062 -27.65380 -9.81412  1.000 38.80701 ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.17652  -32.10782 -15.03518 1.000 32.81523 ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.74832  -33.35124 -15.66916 1.000 32.89961 ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.46695  -33.15054 -16.46821 1.000 31.91151 ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.58900  -34.01980 -16.47264 1.000 34.53593 ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.85578  -33.91135 -16.56500 1.000 38.59860 ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -11.08653 -34.43615 -15.82715 1.000 51.56676 ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -11.89701 -33.33463 -15.16416 1.000 62.68599 ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -12.38792 -32.42073 -15.83186 1.000 64.06864 ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -12.04262 -33.41676 -13.84616 1.000 57.37540 ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.34732  -32.01205 -17.15001 1.000 26.98191 ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.14693  -31.64643 -17.88940 1.000 28.90109 ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.10978  -30.95271 -17.01737 1.000 28.65875 ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -3.96088  -30.80808 -17.45085 1.000 27.82336 ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.51104  -30.71673 -19.05377 1.000 25.52721 ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.36867  -31.39755 -20.09835 1.000 41.33227 ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.53357  -32.63304 -20.02535 1.000 41.71910 ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.88418  -30.69207 -20.98950 1.000 42.79085 ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.49538  -30.52797 -15.81172 1.000 19.78013 ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.66727  -29.70038 -14.93074 1.000 18.06880 ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.19688  -28.42986 -15.64164 1.000 25.67164 ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -3.01369  -28.07660 -15.62819 1.000 20.96902 ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.48299  -30.49067 -14.36486 1.000 23.90300 ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -3.07827  -30.02327 -12.97412 1.000 22.54304 ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.60990  -30.25394 -12.66463 1.000 31.60674 ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -1.27802  -31.66192 -12.49990 1.000 49.60365 ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? -0.07825  -32.17755 -12.73036 1.000 52.84427 ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 0.92917   -31.42713 -13.14704 1.000 37.23413 ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 0.11880   -33.47693 -12.52745 1.000 49.68500 ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.14365  -27.73141 -16.26596 1.000 17.57127 ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.84987  -26.49367 -16.97238 1.000 19.47150 ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.77074  -25.38287 -16.49533 1.000 16.64110 ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.94743  -25.61619 -16.20793 1.000 18.49899 ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -4.99253  -26.64419 -18.50123 1.000 22.33327 ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.32696  -27.05162 -18.82874 1.000 19.31964 ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -3.98467  -27.64919 -19.05515 1.000 23.88632 ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.21877  -24.17621 -16.40673 1.000 15.48808 ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -5.99249  -22.95218 -16.25529 1.000 16.22936 ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.78087  -22.11523 -17.50798 1.000 16.01354 ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.64334  -21.77488 -17.84567 1.000 16.05959 ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.57452  -22.17084 -15.00862 1.000 18.93164 ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.28624  -20.82633 -14.80824 1.000 14.83886 ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.78775  -21.02880 -14.66192 1.000 18.24492 ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.70671  -20.09071 -13.59378 1.000 15.11372 ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.86748  -21.78721 -18.19378 1.000 11.91481 ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.80473  -21.05142 -19.44826 1.000 15.41144 ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.40448  -19.66218 -19.26548 1.000 16.27985 ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.51076  -19.52346 -18.72883 1.000 15.20519 ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.54589  -21.80069 -20.55443 1.000 18.20473 ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.97019  -23.10302 -20.73203 1.000 18.17375 ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.45421  -21.03032 -21.85086 1.000 15.02415 ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.67106  -18.64487 -19.70552 1.000 12.14978 ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.11903  -17.25613 -19.68784 1.000 15.95421 ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.34404  -16.84074 -21.13743 1.000 16.84080 ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.38852  -16.73862 -21.92050 1.000 15.96288 ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.10996  -16.32941 -18.98844 1.000 14.11341 ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.89920  -16.73979 -17.52489 1.000 20.89536 ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.57812  -14.88271 -19.04251 1.000 14.15697 ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.68196  -17.61511 -17.29333 1.000 25.63300 ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.60364  -16.59410 -21.49223 1.000 13.56671 ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -9.01196  -16.24771 -22.84815 1.000 13.29936 ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.43108  -14.78833 -22.86516 1.000 17.15730 ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.20671 -14.34871 -22.00663 1.000 15.39689 ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.16823 -17.13470 -23.34230 1.000 18.75685 ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.44877 -16.86179 -24.81362 1.000 16.13486 ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -9.85763  -18.60724 -23.12342 1.000 22.42756 ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -8.94043  -14.04256 -23.85083 1.000 15.81284 ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.42054  -12.69196 -24.09063 1.000 13.94677 ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.65632  -12.50968 -25.58399 1.000 17.93089 ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.10564  -13.22989 -26.42119 1.000 17.55570 ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.44579  -11.62699 -23.53304 1.000 15.68875 ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.15192  -11.51139 -24.33778 1.000 23.46880 ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -7.20176  -11.11900 -25.52505 1.000 20.25328 ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -6.07471  -11.81518 -23.77606 1.000 17.20669 ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.50382 -11.54597 -25.90943 1.000 15.24973 ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -10.80871 -11.20597 -27.29195 1.000 15.84292 ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.13729 -9.88983  -27.67803 1.000 23.30566 ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.70346 -9.06115  -28.39010 1.000 14.88004 ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.31897 -11.14687 -27.51053 1.000 17.03260 ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -12.92664 -10.30330 -26.52121 1.000 16.02193 ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -12.91371 -12.54667 -27.40387 1.000 15.49304 ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -8.91644  -9.68288  -27.19798 1.000 15.68477 ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.17645  -8.47688  -27.49893 1.000 14.98998 ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.63941  -8.47321  -28.91251 1.000 14.66044 ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -8.07055  -9.23784  -29.78133 1.000 15.90751 ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.65736  -7.59407  -29.13796 1.000 14.86443 ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.14248  -7.37180  -30.48346 1.000 14.15083 ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.38087  -8.58395  -31.00629 1.000 14.82164 ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.24513  -8.74811  -32.22249 1.000 16.68644 ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.27118  -6.09748  -30.49709 1.000 17.53559 ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -4.94992  -5.65592  -31.92859 1.000 21.20851 ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -3.98548  -6.29554  -29.67859 1.000 16.16621 ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.58897  -4.18699  -32.03110 1.000 23.32968 ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -4.88776  -9.45190  -30.12158 1.000 15.91625 ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.12044  -10.60165 -30.55271 1.000 15.87982 ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.69658  -10.23581 -30.93370 1.000 15.03504 ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.24635  -9.09737  -30.81015 1.000 16.72866 ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -1.97445  -11.23506 -31.42396 1.000 15.51791 ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.56971  -11.07360 -31.76465 1.000 13.61178 ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.28661  -11.69710 -33.12001 1.000 16.02895 ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -0.78943  -12.77968 -33.43150 1.000 19.15879 ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.34029   -11.72525 -30.71250 1.000 17.85700 ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.38149   -10.98302 -29.38704 1.000 21.76781 ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.42149   -11.81647 -28.17732 1.000 21.80556 ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.29752   -13.07800 -27.57610 1.000 18.56564 ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.53333   -11.01652 -33.91496 1.000 17.89864 ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 1.03888   -11.60683 -35.14480 1.000 18.59445 ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 2.10129   -12.65844 -34.82245 1.000 18.47006 ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.57186   -12.77908 -33.68706 1.000 21.37422 ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.63631   -10.53398 -36.05203 1.000 20.24136 ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.77529   -9.94830  -35.40500 1.000 21.70300 ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.60932   -9.44952  -36.35084 1.000 22.47611 ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.46701   -13.44302 -35.84005 1.000 18.79961 ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.60011   -14.35119 -35.68867 1.000 18.10000 ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 4.85221   -13.59017 -35.28087 1.000 17.51060 ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.60785   -14.03843 -34.40958 1.000 18.04388 ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 3.85186   -15.11631 -36.98649 1.000 19.75440 ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 4.84471   -16.25516 -36.82242 1.000 20.96232 ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 5.18950   -16.88025 -38.16696 1.000 25.71607 ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 6.05974   -18.10807 -37.97474 1.000 34.29051 ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 6.86180   -18.41202 -39.18860 1.000 30.80697 ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 5.08179   -12.42923 -35.89785 1.000 18.53689 ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 6.24756   -11.62279 -35.55652 1.000 20.89758 ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 6.16710   -11.11747 -34.12495 1.000 23.85796 ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 7.19724   -10.93080 -33.47341 1.000 25.86241 ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.38414   -10.45086 -36.52659 1.000 20.36534 ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 4.94875   -10.88122 -33.62755 1.000 18.04671 ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.75424   -10.48822 -32.23243 1.000 20.50756 ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 5.09053   -11.62410 -31.27655 1.000 17.81955 ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.67546   -11.38719 -30.21286 1.000 20.68985 ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.30921   -10.04500 -32.00782 1.000 21.68175 ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 3.03501   -8.65376  -32.52972 1.000 32.03961 ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 4.00373   -7.90679  -32.80788 1.000 31.56466 ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 1.83717   -8.31859  -32.68425 1.000 24.40864 ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.73149   -12.86370 -31.63379 1.000 17.59500 ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 4.98309   -14.00725 -30.75644 1.000 20.84654 ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.47582   -14.25233 -30.58852 1.000 19.77892 ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 6.98435   -14.31525 -29.46714 1.000 19.03644 ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.31611   -15.25596 -31.31538 1.000 20.23752 ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.81558   -15.42664 -31.11964 1.000 18.69785 ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.38460   -16.73317 -31.76695 1.000 17.41066 ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.43456   -15.39870 -29.63919 1.000 15.53526 ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 7.18832   -14.45458 -31.69488 1.000 22.80390 ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.61414   -14.16413 -31.69375 1.000 22.92522 ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 8.75008   -12.69572 -31.30179 1.000 19.63959 ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 7.78702   -11.94590 -31.37131 1.000 53.24546 ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 9.19634   -14.44838 -33.08899 1.000 22.06225 ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.63145   -15.77095 -33.61586 1.000 16.78115 ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.72581  -14.52607 -33.05078 1.000 19.52252 ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.69268   -15.90853 -35.13513 1.000 20.32682 ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 9.91553   -12.28258 -30.82762 1.000 41.32765 ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 10.00095  -10.92497 -30.27775 1.000 27.79248 ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 9.15493   -10.83308 -29.00724 1.000 20.80175 ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.45881   -9.84415  -28.77046 1.000 19.95094 ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.58265   -9.86041  -31.31190 1.000 22.26316 ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.08338  -8.48020  -30.97963 1.000 42.46204 ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 10.95181  -8.31279  -30.12234 1.000 38.80646 ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 9.53380   -7.47014  -31.66110 1.000 39.13062 ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 9.15452   -11.92425 -28.23657 1.000 20.19112 ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.80293   -11.91902 -26.81708 1.000 14.48153 ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.35191   -11.50507 -26.56938 1.000 18.37460 ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 7.05226   -10.70126 -25.68377 1.000 16.84689 ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.78251   -11.03422 -26.04111 1.000 19.01484 ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.22368  -11.49269 -26.20868 1.000 20.28988 ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.54261  -12.65540 -25.96286 1.000 20.01449 ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 12.10204  -10.57969 -26.61565 1.000 22.62400 ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.44309   -12.08864 -27.35191 1.000 17.14381 ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 4.99922   -11.91579 -27.17438 1.000 19.28593 ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.62483   -10.43577 -27.09256 1.000 18.42988 ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.86969   -10.00423 -26.21894 1.000 19.01038 ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.50575   -12.68692 -25.94551 1.000 15.18429 ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.73626   -14.19990 -26.06217 1.000 21.29026 ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 5.91993   -14.63703 -25.19800 1.000 22.48023 ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.49479   -14.99826 -25.72777 1.000 35.31096 ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 5.17599   -9.64852  -28.01831 1.000 16.19724 ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.81382   -8.24547  -28.11825 1.000 21.06045 ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.33003   -7.34714  -27.01732 1.000 23.36821 ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.81540   -6.23576  -26.84687 1.000 26.14631 ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.33251   -7.78339  -26.26224 1.000 19.73743 ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.87372   -6.98983  -25.16983 1.000 21.80371 ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.25887   -6.47577  -25.53762 1.000 17.16259 ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.90035   -6.96305  -26.47206 1.000 21.70278 ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 6.96362   -7.81027  -23.87714 1.000 17.98666 ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 7.94310   -8.84436  -24.04166 1.000 22.43472 ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.62277   -8.45495  -23.56931 1.000 25.42359 ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.71760   -5.47438  -24.79054 1.000 18.88001 ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 10.11262  -5.05559  -24.87639 1.000 17.18493 ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.86421  -5.76049  -23.75233 1.000 21.01366 ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.43369  -5.12630  -22.85578 1.000 20.88912 ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.25875  -3.52040  -24.83633 1.000 24.11060 ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.59468   -2.90761  -23.59945 1.000 27.10904 ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.66248   -2.90356  -26.09569 1.000 27.62570 ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 10.06194  -1.49848  -23.31365 1.000 33.04173 ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 10.88437  -7.09401  -23.82171 1.000 20.19082 ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.29860  -7.90731  -22.68457 1.000 23.50614 ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.77018  -7.72727  -22.33609 1.000 17.46326 ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.13965  -7.87521  -21.16688 1.000 20.07536 ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 10.99621  -9.38083  -22.96003 1.000 19.60860 ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.62533  -7.42416  -23.31583 1.000 19.71866 ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.05124  -7.29934  -23.02412 1.000 24.03129 ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.31491  -6.12068  -22.09243 1.000 26.48611 ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 15.95408  -6.27331  -21.04561 1.000 26.73499 ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.84977  -7.16780  -24.32459 1.000 23.02441 ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.34258  -7.44961  -24.18994 1.000 40.96726 ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.14792  -6.20507  -23.85730 1.000 54.23616 ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 18.21037  -5.26769  -25.05296 1.000 62.57297 ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 18.62331  -3.88200  -24.68194 1.000 58.78073 ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.81529  -4.93460  -22.44644 1.000 25.78009 ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 14.99780  -3.78704  -21.56418 1.000 29.80709 ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.15474  -3.91284  -20.30016 1.000 23.43953 ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.55694  -3.42284  -19.23827 1.000 26.79576 ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.66669  -2.48999  -22.30400 1.000 35.16351 ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.32643  -2.49091  -22.76101 1.000 31.43891 ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 12.99369  -4.56548  -20.38894 1.000 20.39370 ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.16942  -4.74748  -19.20359 1.000 21.36334 ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.80958  -5.67232  -18.18603 1.000 26.07344 ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.75578  -5.41520  -16.98054 1.000 22.74056 ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.43198  -6.75664  -18.65489 1.000 19.48889 ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.16406  -7.63529  -17.74574 1.000 22.55685 ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.32351  -6.90419  -17.08602 1.000 29.03549 ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.58114  -7.08509  -15.89017 1.000 29.56817 ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.67443  -8.86296  -18.49749 1.000 21.86907 ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.56097  -9.59233  -19.01948 1.000 23.65747 ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.47275  -9.76000  -17.57189 1.000 24.86352 ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.04082  -6.08324  -17.85557 1.000 25.19156 ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.14145  -5.30344  -17.30227 1.000 26.31828 ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.67839  -4.46589  -16.11979 1.000 30.96727 ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.24634  -4.54482  -15.02688 1.000 33.72741 ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.74599  -4.41393  -18.38874 1.000 28.61219 ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 18.95661  -3.60505  -17.93568 1.000 48.25715 ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.46568  -2.70091  -19.04979 1.000 36.96199 ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.80585  -2.07675  -18.69288 1.000 41.46160 ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 21.63628  -2.98092  -17.85570 1.000 64.77679 ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.63071  -3.66738  -16.31909 1.000 29.56790 ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 15.13904  -2.81663  -15.24329 1.000 31.92202 ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.58676  -3.64550  -14.08815 1.000 27.49618 ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.80006  -3.30660  -12.91918 1.000 30.73184 ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 14.08117  -1.85963  -15.78819 1.000 28.11432 ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.87944  -4.73662  -14.39549 1.000 28.90117 ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.32970  -5.58910  -13.34416 1.000 23.98177 ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.43242  -6.14845  -12.45126 1.000 32.65678 ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.33192  -6.09755  -11.21924 1.000 31.86961 ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.50779  -6.71239  -13.97960 1.000 21.80748 ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.84911  -7.63498  -12.99358 1.000 20.66169 ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.22445  -7.14108  -11.85553 1.000 25.75881 ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.81521  -9.00060  -13.22980 1.000 25.67392 ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.60033  -7.99810  -10.95844 1.000 22.66908 ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.18695  -9.86263  -12.33933 1.000 25.53190 ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.58583  -9.35784  -11.19781 1.000 24.78583 ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.51053  -6.65075  -13.05063 1.000 31.16181 ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.52179  -7.34401  -12.26559 1.000 42.52466 ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.37950  -6.38886  -11.44286 1.000 44.57643 ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.90013  -6.78509  -10.39237 1.000 40.74392 ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.38110  -8.21207  -13.18322 1.000 44.79719 ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 16.96033  -9.67706  -13.15297 1.000 25.76898 ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 18.09601  -10.73389 -14.05484 1.000 75.07696 ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 16.95687  -11.73509 -14.99583 1.000 30.21082 ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.53454  -5.13703  -11.88160 1.000 33.52156 ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 18.18973  -4.15660  -11.02141 1.000 41.43159 ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.27467  -3.73407  -9.88256  1.000 47.62076 ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.74916  -3.42740  -8.78152  1.000 43.58309 ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.63204  -2.92473  -11.82298 1.000 45.68334 ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.24905  -3.15802  -13.22718 1.000 60.05323 ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.98070  -4.48809  -13.41861 1.000 76.47725 ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 20.01960  -4.99145  -14.56453 1.000 61.15972 ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 20.59086  -4.99309  -12.45224 1.000 62.38996 ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.96564  -3.70609  -10.12848 1.000 35.86758 ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 15.02740  -3.38398  -9.06127  1.000 30.91248 ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 15.04225  -4.45378  -7.97916  1.000 35.69291 ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 14.99425  -4.13362  -6.78665  1.000 43.74427 ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.62492  -3.21114  -9.63400  1.000 32.80921 ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.12380  -5.72811  -8.37469  1.000 33.71923 ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.16110  -6.81294  -7.39671  1.000 43.45987 ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.37429  -6.69089  -6.48393  1.000 50.63748 ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.26529  -6.84044  -5.26088  1.000 42.20556 ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.15425  -8.16254  -8.11262  1.000 36.37481 ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.88955  -8.43880  -8.92034  1.000 25.64877 ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 13.92754  -9.82460  -9.52572  1.000 28.42980 ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.67330  -8.27705  -8.01196  1.000 28.40339 ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.54316  -6.41440  -7.06125  1.000 46.94441 ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.73490  -6.20118  -6.25146  1.000 53.06846 ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.66375  -4.91741  -5.43500  1.000 57.99236 ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.47192  -4.74251  -4.51619  1.000 61.98568 ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.97450  -6.18717  -7.14620  1.000 47.39743 ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.39860  -7.56827  -7.61835  1.000 64.03466 ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.88565  -7.81803  -7.44706  1.000 90.68707 ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 22.62840  -6.94196  -7.00243  1.000 92.46355 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 22.32785  -9.02014  -7.80149  1.000 92.82872 ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.71623  -4.02767  -5.73894  1.000 57.36973 ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.55882  -2.76103  -5.03528  1.000 49.45146 ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 16.33277  -2.74363  -4.12461  1.000 69.35521 ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.86031  -1.66526  -3.74919  1.000 54.27107 ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 17.49060  -1.60584  -6.03451  1.000 48.28741 ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.79576  -3.91116  -3.77541  1.000 44.39613 ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.74876  -4.02848  -2.77640  1.000 49.99059 ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.41012  -4.51086  -3.29745  1.000 50.08468 ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.55478  -4.90654  -2.49208  1.000 44.09829 ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.18614  -4.48696  -4.60903  1.000 36.15590 ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.90585  -4.91872  -5.14950  1.000 31.00837 ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.73667  -6.42784  -4.99340  1.000 31.07234 ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.69384  -7.16957  -4.75343  1.000 36.37547 ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.78326  -4.52864  -6.62379  1.000 33.68177 ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.49536  -6.88130  -5.13682  1.000 37.82551 ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.18155  -8.30031  -5.11910  1.000 34.30094 ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.47457   -8.68352  -6.41286  1.000 27.43115 ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.11923   -7.83274  -7.23249  1.000 25.74363 ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.32159   -8.67300  -3.90463  1.000 38.61482 ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 7.96617   -7.99981  -3.91874  1.000 43.43325 ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.90967   -6.76279  -3.75071  1.000 54.06811 ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 6.95726   -8.71213  -4.11080  1.000 45.50320 ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.26527   -9.99198  -6.57924  1.000 23.98473 ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.78620   -10.52515 -7.85147  1.000 23.28163 ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.37425   -10.03889 -8.16491  1.000 25.45655 ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 6.99721   -9.92937  -9.33867  1.000 27.14809 ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.90017   -12.06654 -7.83132  1.000 27.11546 ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.36717  -12.48149 -8.01546  1.000 35.80543 ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.02543   -12.72302 -8.88869  1.000 23.44716 ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.63433  -13.95736 -7.78296  1.000 26.77701 ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.58520   -9.69238  -7.13994  1.000 29.25322 ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.22374   -9.21716  -7.39110  1.000 33.61998 ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.18933   -7.94863  -8.23909  1.000 28.98929 ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.15149   -7.63927  -8.83496  1.000 28.25224 ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.49099   -8.95489  -6.07359  1.000 23.83550 ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.92098   -7.73612  -5.50288  1.000 31.61352 ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.28876   -7.20720  -8.30362  1.000 25.37329 ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.34549   -5.95311  -9.04013  1.000 21.78350 ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.68845   -6.14291  -10.51345 1.000 22.35308 ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 6.92203   -5.15199  -11.21323 1.000 23.68465 ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.34658   -5.01970  -8.36137  1.000 30.15791 ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 7.02221   -4.83218  -6.88112  1.000 31.05485 ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.27877   -3.96010  -5.94515  1.000 37.07503 ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 8.35434   -2.42410  -6.86502  1.000 36.08823 ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.67513   -7.38860  -10.99860 1.000 19.70350 ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.12986   -7.70378  -12.35267 1.000 24.70779 ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.33673   -6.93117  -13.40655 1.000 21.52677 ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.88449   -6.53192  -14.44180 1.000 18.66218 ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.05365   -9.22540  -12.58717 1.000 19.91699 ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.64732   -9.59026  -13.94968 1.000 22.83302 ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.61382   -9.73039  -12.45333 1.000 21.75495 ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.79813   -11.08453 -14.16496 1.000 22.79537 ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.04328   -6.70590  -13.16762 1.000 24.10449 ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.21318   -6.03741  -14.15765 1.000 20.42341 ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.60194   -4.59835  -14.42130 1.000 27.00227 ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.31736   -4.08040  -15.50607 1.000 26.32891 ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.24419   -3.94096  -13.45464 1.000 21.20941 ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.71398   -2.57639  -13.65464 1.000 22.44567 ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.83988   -2.48702  -14.67219 1.000 25.82077 ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.17570   -1.37975  -15.10538 1.000 23.94699 ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.17645   -1.98196  -12.32547 1.000 27.64891 ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.08168   -1.89730  -11.28749 1.000 32.58173 ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.57705   -1.37507  -9.96404  1.000 39.86213 ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.34890   -0.41654  -9.91318  1.000 41.45209 ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.13373   -2.00186  -8.87702  1.000 47.27354 ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.42828   -3.61657  -15.05565 1.000 21.11385 ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.53549   -3.65031  -16.00050 1.000 23.98266 ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.13859   -4.28153  -17.32893 1.000 28.01783 ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 9.00945   -4.57955  -18.15315 1.000 24.32889 ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.71596   -4.38753  -15.36898 1.000 22.43373 ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.13202  -3.81112  -14.04931 1.000 22.08492 ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 10.93750  -2.68714  -13.98985 1.000 33.65883 ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 9.66647   -4.35736  -12.86742 1.000 28.82858 ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 11.30383  -2.14264  -12.77164 1.000 32.46925 ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 10.02669  -3.82233  -11.64748 1.000 23.01393 ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.84346  -2.70968  -11.59637 1.000 27.77081 ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.84439   -4.50122  -17.54946 1.000 21.18277 ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.35014   -4.92129  -18.84249 1.000 19.62437 ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.61834   -6.35880  -19.21481 1.000 21.95307 ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.46358   -6.70961  -20.39065 1.000 21.44685 ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.00713   -7.20503  -18.26036 1.000 17.92205 ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.31155   -8.60547  -18.54923 1.000 15.00748 ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.46206   -9.50700  -17.66012 1.000 17.02584 ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.85596   -10.63271 -17.33087 1.000 16.10484 ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.81491   -8.89555  -18.37781 1.000 17.47278 ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.59781   -8.24789  -19.50209 1.000 19.09984 ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.31823   -8.38978  -17.03072 1.000 20.01482 ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.27633   -9.02161  -17.28887 1.000 16.78894 ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.39209   -9.76714  -16.40725 1.000 18.37807 ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 3.93547   -11.10767 -16.94814 1.000 15.68429 ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.56462   -11.98428 -16.15704 1.000 17.37285 ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 3.94961   -11.29136 -18.27565 1.000 13.50471 ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.57278   -12.58317 -18.84700 1.000 12.86173 ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.38597   -13.71898 -18.24227 1.000 16.94383 ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.84933   -14.79587 -17.95956 1.000 14.60308 ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.75723   -12.58428 -20.36779 1.000 15.80256 ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.73825   -13.96708 -20.97015 1.000 20.10192 ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.53878   -14.64458 -21.14768 1.000 20.18338 ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 4.92140   -14.60278 -21.32711 1.000 15.49133 ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.51636   -15.92090 -21.68844 1.000 16.27267 ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 4.90517   -15.88241 -21.86000 1.000 17.23085 ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.70466   -16.54068 -22.04205 1.000 17.93536 ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.68876   -13.50187 -18.04740 1.000 15.26610 ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.56414   -14.59160 -17.63403 1.000 10.50841 ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.32169   -15.03027 -16.19498 1.000 15.47830 ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.86247   -16.06374 -15.78492 1.000 16.45248 ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.02790   -14.19065 -17.84380 1.000 11.33601 ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.31566   -13.89041 -19.30037 1.000 14.95415 ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.59887   -14.91382 -20.19700 1.000 13.34986 ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.25445   -12.59102 -19.78838 1.000 15.31591 ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.84224   -14.64500 -21.55138 1.000 16.04417 ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.50436   -12.31259 -21.13170 1.000 18.59113 ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.78965   -13.34225 -22.00560 1.000 17.60256 ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 9.02841   -13.06328 -23.33600 1.000 18.86459 ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.51916   -14.28800 -15.42934 1.000 14.80092 ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.10290   -14.75802 -14.11264 1.000 16.28900 ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.22109   -15.99487 -14.19724 1.000 16.63066 ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 3.96774   -16.62589 -13.16433 1.000 15.33656 ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.36509   -13.65444 -13.35181 1.000 16.39953 ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.09064   -13.39823 -13.91514 1.000 15.39873 ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.74431   -16.34719 -15.39576 1.000 14.15047 ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.05856   -17.62186 -15.58205 1.000 12.68025 ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.88832   -18.79098 -15.06945 1.000 14.60768 ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.33176   -19.77020 -14.55705 1.000 14.58729 ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.72804   -17.82636 -17.06301 1.000 12.45424 ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.21701   -18.70709 -15.18223 1.000 14.47387 ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.06893   -19.81376 -14.76577 1.000 13.30691 ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.24139   -19.88594 -13.25355 1.000 14.08311 ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 6.98837   -20.74205 -12.77067 1.000 16.93552 ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.41836   -19.72697 -15.49225 1.000 12.67977 ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.22121   -20.00526 -16.96298 1.000 13.19187 ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.21276   -21.30882 -17.44610 1.000 15.31616 ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 6.95211   -18.97237 -17.85437 1.000 12.34275 ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 6.99196   -21.57629 -18.79408 1.000 14.93604 ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.72469   -19.22822 -19.19872 1.000 13.87336 ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.74354   -20.52808 -19.65905 1.000 15.68879 ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.52413   -20.78014 -20.99292 1.000 15.08801 ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.54789   -19.02932 -12.50092 1.000 17.97614 ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.42222   -19.23664 -11.06388 1.000 16.56197 ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.57904   -20.46886 -10.74836 1.000 17.16746 ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.78688   -21.11320 -9.71349  1.000 19.76437 ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.81026   -17.99600 -10.41097 1.000 17.87952 ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.66497   -16.72858 -10.35096 1.000 14.99081 ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.84198   -15.55957 -9.82796  1.000 19.17379 ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.88702   -16.96815 -9.47240  1.000 19.94645 ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.63820   -20.82074 -11.62838 1.000 17.02331 ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.68436   -21.88646 -11.33565 1.000 17.91465 ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.62495   -22.92550 -12.45132 1.000 18.41276 ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.10133   -24.02465 -12.24828 1.000 19.43024 ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.27811   -21.31589 -11.05689 1.000 18.86248 ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.27809   -20.47162 -9.78124  1.000 20.99420 ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.76380   -20.50424 -12.24398 1.000 15.84748 ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.15804   -22.60407 -13.62697 1.000 18.95357 ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 3.02455   -23.46095 -14.79999 1.000 16.86819 ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.36256   -24.09403 -15.15754 1.000 18.19858 ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.38813   -23.40601 -15.19492 1.000 18.90214 ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.48557   -22.66579 -15.99085 1.000 15.46068 ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.35145   -25.40506 -15.42045 1.000 15.06325 ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.53924   -26.05437 -15.96892 1.000 18.56448 ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.63969   -25.87332 -17.47484 1.000 20.47276 ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.73446   -25.98954 -18.03639 1.000 20.44274 ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.55181   -27.55071 -15.64619 1.000 21.15299 ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.22812   -28.25421 -15.82986 1.000 27.62150 ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.25607   -29.68971 -15.32544 1.000 53.69322 ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 3.72682   -30.57699 -16.03080 1.000 52.42767 ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 4.80989   -29.93255 -14.23088 1.000 49.81110 ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.52088   -25.59223 -18.13203 1.000 17.46111 ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.48020   -25.35856 -19.56457 1.000 15.81473 ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.37885   -24.34659 -19.82739 1.000 12.81174 ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.34282   -24.37331 -19.15963 1.000 15.21885 ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.22525   -26.66698 -20.32086 1.000 18.08439 ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 4.09973   -26.54300 -21.82639 1.000 18.61302 ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 4.09866   -27.93111 -22.43562 1.000 23.97073 ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.79955   -28.23354 -23.14830 1.000 34.20664 ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.58896   -29.70965 -23.27124 1.000 39.90560 ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.61739   -23.43738 -20.76902 1.000 11.94121 ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.63190   -22.43247 -21.15935 1.000 15.06454 ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.44346   -22.50439 -22.67064 1.000 18.41648 ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.42313   -22.49465 -23.42460 1.000 13.50667 ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 3.05594   -21.01142 -20.73617 1.000 18.26374 ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 2.02256   -19.98995 -21.21036 1.000 14.87961 ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.25537   -20.92514 -19.21090 1.000 12.54192 ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 1.18778   -22.58238 -23.10700 1.000 14.19650 ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.82089   -22.52581 -24.51625 1.000 16.05431 ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 0.03400   -21.24346 -24.75987 1.000 16.02973 ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.90071  -20.93695 -24.01262 1.000 18.52340 ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? -0.02298  -23.73758 -24.92671 1.000 15.68206 ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.62529   -24.95535 -24.53344 1.000 21.62843 ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.24365  -23.74477 -26.43435 1.000 16.05535 ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.40860   -20.49610 -25.79526 1.000 13.10258 ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.28393  -19.26363 -26.16224 1.000 13.01438 ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -0.84721  -19.44261 -27.56561 1.000 14.11129 ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.08325  -19.58700 -28.52878 1.000 18.07633 ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.64365   -18.03642 -26.10170 1.000 16.07293 ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? -0.11511  -16.76906 -26.51203 1.000 12.57404 ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.25696   -17.87914 -24.72124 1.000 13.67237 ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.17595  -19.43624 -27.68341 1.000 13.04297 ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -2.86162  -19.44590 -28.97420 1.000 12.66128 ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.34398  -18.03152 -29.25672 1.000 18.89185 ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -3.96404  -17.40198 -28.39175 1.000 13.83160 ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -4.04378  -20.42895 -28.98326 1.000 19.81606 ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.68911  -21.73734 -28.27699 1.000 26.27444 ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.51452  -20.67250 -30.41146 1.000 24.01425 ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -2.70317  -22.56554 -29.02926 1.000 24.11702 ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -3.08439  -17.52483 -30.45957 1.000 13.70010 ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.41734  -16.13007 -30.71556 1.000 14.46543 ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -3.85744  -15.94637 -32.16101 1.000 17.84227 ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.44256  -16.69056 -33.05303 1.000 17.34578 ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.23171  -15.21379 -30.36998 1.000 18.45458 ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.67931  -13.85588 -30.29210 1.000 18.75371 ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -1.11229  -15.34045 -31.40319 1.000 15.06270 ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.72493  -14.95499 -32.37180 1.000 13.73812 ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.21705  -14.59873 -33.69912 1.000 17.60755 ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.34253  -13.08601 -33.77295 1.000 17.39493 ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -6.12733  -12.48614 -33.03097 1.000 17.46573 ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.56544  -15.25820 -34.00051 1.000 17.14960 ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.19327  -14.82536 -35.33092 1.000 17.34564 ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.41755  -15.38232 -36.51554 1.000 24.00689 ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.10289  -15.06274 -37.84129 1.000 18.06485 ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.12581  -13.61168 -38.17001 1.000 18.02240 ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.55804  -12.47983 -34.65056 1.000 17.66683 ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.58177  -11.05119 -34.91670 1.000 15.49390 ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.27037  -10.83934 -36.26242 1.000 21.25840 ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.21099  -11.70384 -37.14189 1.000 19.87502 ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.14073  -10.51069 -34.91945 1.000 18.37648 ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -3.02860  -9.01976  -35.01944 1.000 22.36910 ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.24603  -8.33115  -36.19282 1.000 20.17417 ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.69061  -8.08850  -34.09634 1.000 20.26271 ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -3.06719  -7.04000  -35.98405 1.000 25.80445 ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.72520  -6.86591  -34.72018 1.000 22.81074 ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -5.96414  -9.70344  -36.41188 1.000 19.60320 ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.68824  -9.46034  -37.65867 1.000 19.02456 ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.78010  -9.53947  -38.88407 1.000 21.43718 ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.24203  -9.89533  -39.97364 1.000 23.01391 ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.39273  -8.09966  -37.62862 1.000 20.20184 ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.65129  -8.10172  -36.77672 1.000 24.53444 ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.28872  -9.13919  -36.58552 1.000 27.21109 ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -9.03352  -6.92759  -36.28545 1.000 24.50937 ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.49459  -9.21755  -38.73747 1.000 23.48380 ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.58892  -9.13508  -39.87761 1.000 23.46340 ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.77528  -10.40422 -40.10144 1.000 32.26114 ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -1.87979  -10.40507 -40.95403 1.000 28.75796 ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.63910  -7.94639  -39.71471 1.000 27.14806 ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.36526  -6.62046  -39.68396 1.000 32.14916 ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.51794  -6.56262  -40.15802 1.000 30.56209 ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.78731  -5.63950  -39.16924 1.000 39.82879 ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -3.05650  -11.48086 -39.37054 1.000 25.21751 ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.25764  -12.69386 -39.48502 1.000 20.71233 ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.15439  -13.90906 -39.27873 1.000 28.33851 ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.36562  -13.79095 -39.06467 1.000 25.70345 ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -1.09659  -12.68253 -38.48123 1.000 22.83404 ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 0.13866   -13.39636 -39.00042 1.000 26.76485 ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 0.03047   -14.14561 -39.99635 1.000 27.55303 ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.22141   -13.20689 -38.40477 1.000 27.58264 ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.54252  -15.08607 -39.35347 1.000 24.03403 ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.22453  -16.34812 -39.12566 1.000 24.74474 ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.11224  -16.75150 -37.65659 1.000 18.25983 ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.41495  -16.11719 -36.86024 1.000 20.72440 ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -2.64548  -17.43879 -40.03009 1.000 29.79193 ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -2.72423  -17.15089 -41.53821 1.000 34.28745 ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -4.06679  -16.58534 -42.00235 1.000 58.44262 ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -4.07137  -15.83461 -43.00220 1.000 62.08041 ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -5.11992  -16.91871 -41.41141 1.000 62.61600 ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -3.81450  -17.82413 -37.29905 1.000 21.51244 ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -3.80218  -18.31009 -35.92546 1.000 18.82919 ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.53201  -19.11305 -35.66855 1.000 20.72766 ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.19284  -20.01928 -36.43663 1.000 19.19489 ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -5.03998  -19.16195 -35.64301 1.000 19.31579 ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.25691  -19.47074 -34.15686 1.000 21.00093 ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.68637  -19.88407 -33.84111 1.000 27.02990 ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.63079  -19.14561 -34.11592 1.000 26.10344 ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -6.85140  -21.07081 -33.26610 1.000 25.42735 ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -1.83632  -18.78348 -34.58116 1.000 15.07314 ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.56480  -19.40510 -34.25076 1.000 19.48085 ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.58674  -19.92271 -32.82110 1.000 20.20568 ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.34510  -19.43451 -31.97526 1.000 18.65207 ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.59773   -18.42063 -34.42651 1.000 16.14505 ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 1.00084   -18.23760 -35.86909 1.000 19.24711 ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 1.89121   -19.11300 -36.47249 1.000 23.02150 ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 0.49110   -17.19250 -36.62822 1.000 22.32243 ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 2.26239   -18.95935 -37.79507 1.000 24.66032 ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 0.85717   -17.02993 -37.95541 1.000 26.92830 ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.74440   -17.91690 -38.52959 1.000 30.99878 ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 2.12349   -17.77048 -39.84386 1.000 36.02260 ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 0.26965   -20.91219 -32.56475 1.000 15.91254 ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.46316   -21.49560 -31.24239 1.000 16.60817 ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 1.92369   -21.34588 -30.83403 1.000 18.19711 ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.81922   -21.86087 -31.51544 1.000 16.93562 ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 0.05692   -22.97006 -31.23010 1.000 18.25429 ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 2.15376   -20.64266 -29.72707 1.000 14.77673 ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.45649   -20.50601 -29.08544 1.000 15.33230 ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.49558   -21.43131 -27.87459 1.000 16.57618 ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.48722   -21.59485 -27.18368 1.000 16.62612 ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.66201   -19.04227 -28.67414 1.000 15.62409 ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 4.89728   -18.66429 -27.89790 1.000 15.32436 ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 5.97593   -17.96893 -28.37247 1.000 12.18421 ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 5.14952   -18.88321 -26.49914 1.000 16.55146 ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 6.88822   -17.76396 -27.36781 1.000 12.84815 ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.40803   -18.31879 -26.21028 1.000 15.36167 ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.44024   -19.51119 -25.46806 1.000 13.65669 ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 6.97281   -18.36214 -24.93695 1.000 16.65748 ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 5.00815   -19.55661 -24.20329 1.000 13.44866 ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.26145   -18.98457 -23.95237 1.000 12.38528 ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.64887   -22.04892 -27.61539 1.000 13.69688 ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.72899   -22.97425 -26.49229 1.000 12.81029 ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 6.13248   -22.98941 -25.90539 1.000 12.58708 ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 7.11759   -22.93853 -26.64544 1.000 14.53588 ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.34448   -24.39236 -26.92150 1.000 16.95387 ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 4.09038   -25.34505 -25.76785 1.000 19.44120 ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 3.28311   -26.55460 -26.19609 1.000 38.62154 ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 3.85995   -27.42548 -26.87862 1.000 33.55466 ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 2.07619   -26.62944 -25.86778 1.000 33.60632 ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.21901   -23.09910 -24.57934 1.000 16.88807 ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.52255   -23.22502 -23.93891 1.000 13.10168 ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.39358   -23.88232 -22.57231 1.000 12.94442 ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.52100   -23.52227 -21.77305 1.000 15.00443 ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.21216   -21.86699 -23.78815 1.000 12.92432 ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.48944   -22.03524 -23.19458 1.000 15.33036 ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.28740   -24.83498 -22.30736 1.000 16.48007 ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.48445   -25.37629 -20.96937 1.000 19.14740 ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.72157   -24.78169 -20.30486 1.000 19.99615 ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.32870  -25.41851 -19.43629 1.000 21.02691 ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.58144   -26.90058 -21.02406 1.000 19.91827 ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.38061   -27.46152 -21.52891 1.000 21.64402 ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.09361  -23.56845 -20.70199 1.000 14.47772 ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.32431  -22.87321 -20.28079 1.000 17.61280 ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.49894  -23.69250 -20.82486 1.000 19.91509 ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.39966  -24.24157 -21.93159 1.000 25.44236 ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.32516  -22.64081 -18.78205 1.000 20.71718 ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.61294  -23.79670 -20.10369 1.000 19.78664 ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.73501  -24.54384 -20.64156 1.000 22.11749 ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.42935  -23.89897 -21.81894 1.000 21.94692 ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 16.23391  -24.55901 -22.48717 1.000 24.65588 ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 15.13154  -22.63397 -22.10627 1.000 19.58588 ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.88293  -21.85957 -23.06889 1.000 19.20172 ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.32051  -21.80667 -24.47210 1.000 16.57718 ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.94405  -21.18307 -25.33785 1.000 18.65006 ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 14.17485  -22.43150 -24.73418 1.000 15.55646 ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.64210  -22.46666 -26.08749 1.000 17.23914 ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 12.12169  -22.38277 -26.06295 1.000 16.40436 ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.47577  -22.69407 -25.06064 1.000 16.11614 ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 14.08815  -23.73135 -26.83187 1.000 20.16062 ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.44261  -24.89102 -26.33240 1.000 19.21100 ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.55820  -21.94610 -27.18904 1.000 16.69177 ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 10.11762  -21.95971 -27.40376 1.000 14.40500 ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.84640   -22.40428 -28.83362 1.000 14.67363 ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.71659  -22.33104 -29.70400 1.000 15.33466 ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.46977   -20.58780 -27.12402 1.000 14.86856 ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 9.95225   -19.47329 -28.02915 1.000 13.33691 ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 11.06666  -18.71948 -27.69359 1.000 15.66399 ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 9.27258   -19.16219 -29.19416 1.000 17.83305 ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 11.50507  -17.68449 -28.51301 1.000 17.54107 ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 9.70637   -18.13634 -30.02080 1.000 13.60170 ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.81800  -17.38949 -29.67570 1.000 18.74951 ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.62781   -22.88697 -29.07219 1.000 14.31188 ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 8.21755   -23.28038 -30.41039 1.000 15.30645 ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 7.07958   -22.39276 -30.89257 1.000 14.72336 ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 6.32314   -21.83157 -30.09386 1.000 14.95717 ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.77860   -24.75227 -30.47519 1.000 17.19844 ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.64185   -24.95477 -29.62702 1.000 17.38594 ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 8.90812   -25.68515 -30.05265 1.000 18.30181 ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 6.97944   -22.26393 -32.21491 1.000 16.93794 ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.87302   -21.57815 -32.87101 1.000 17.26445 ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.41670   -22.44534 -34.03090 1.000 20.40161 ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 6.24050   -22.95054 -34.80334 1.000 19.44683 ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 6.26384   -20.16922 -33.37176 1.000 20.10399 ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 5.11073   -19.53222 -34.13557 1.000 19.33837 ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.67991   -19.28226 -32.21264 1.000 15.86080 ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 4.10360   -22.61765 -34.15409 1.000 17.70576 ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.54143   -23.39956 -35.24332 1.000 19.57231 ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 2.18538   -22.82153 -35.60693 1.000 25.79406 ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.53499   -22.15648 -34.79689 1.000 18.60022 ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 3.39889   -24.88095 -34.87191 1.000 22.50234 ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 2.28866   -25.16456 -33.86747 1.000 26.32885 ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 2.42532   -26.54869 -33.25024 1.000 34.41796 ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.48131   -26.59229 -32.24489 1.000 36.67164 ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 4.00551   -27.70710 -31.75248 1.000 46.20443 ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 3.60439   -28.90006 -32.16153 1.000 35.70074 ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 4.96005   -27.62282 -30.82953 1.000 44.79849 ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.77086   -23.07471 -36.84514 1.000 24.28258 ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 0.40932   -22.75755 -37.24579 1.000 25.46100 ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.56087  -23.58230 -36.41155 1.000 29.06944 ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.37998  -24.79090 -36.24378 1.000 33.45185 ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 0.22060   -23.04175 -38.73682 1.000 30.19231 ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 0.83018   -21.99358 -39.50081 1.000 35.74376 ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? -1.25038  -23.12036 -39.08556 1.000 49.84229 ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.57376  -22.92722 -35.85784 1.000 21.95589 ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.53832  -23.60980 -35.00776 1.000 30.02862 ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.67510  -24.15040 -35.86523 1.000 37.36463 ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.37755  -23.38441 -36.53384 1.000 37.02600 ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -3.07845  -22.67841 -33.92568 1.000 28.08731 ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -3.98461  -23.39860 -32.94844 1.000 40.76287 ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -3.59717  -24.48619 -32.47239 1.000 38.28692 ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -5.09099  -22.89178 -32.67324 1.000 32.95696 ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -3.84749  -25.46785 -35.84573 1.000 42.21981 ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -4.93770  -26.13154 -36.54228 1.000 59.32034 ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.13137  -26.39306 -35.63777 1.000 57.07487 ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.12842  -26.95965 -36.09685 1.000 62.88977 ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.45215  -27.45316 -37.14480 1.000 61.79469 ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.56524  -28.10000 -36.22078 1.000 54.87958 ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -3.72894  -27.20348 -38.45970 1.000 48.52017 ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -6.05266  -25.99589 -34.36955 1.000 60.13731 ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -7.13407  -26.20787 -33.43085 1.000 49.30539 ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.35270  -25.35037 -33.70195 1.000 38.73503 ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.52024  -24.81167 -34.80004 1.000 42.79453 ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -9.20443  -25.21979 -32.69432 1.000 46.97874 ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.45410 -24.48490 -32.83748 1.000 38.44670 ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -10.18429 -23.01628 -33.15824 1.000 32.42241 ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.41864  -22.36332 -32.43767 1.000 27.07589 ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -11.25859 -24.60831 -31.54589 1.000 43.05366 ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -12.70504 -24.16481 -31.65196 1.000 40.30876 ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -13.60611 -25.21044 -32.28405 1.000 38.43021 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -13.17416 -26.36934 -32.46429 1.000 38.08610 ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -14.75704 -24.86140 -32.59922 1.000 49.66763 ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -10.74451 -22.47884 -34.24688 1.000 38.06185 ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.53478 -21.06472 -34.56590 1.000 34.46502 ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -10.98585 -20.14872 -33.43885 1.000 43.75408 ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -11.95097 -20.43225 -32.72623 1.000 38.28650 ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.39551 -20.86997 -35.81232 1.000 36.21465 ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -11.22529 -22.16363 -36.54444 1.000 45.08570 ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.13398 -23.23675 -35.45127 1.000 48.33663 ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.28811 -19.01692 -33.30470 1.000 23.19751 ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.54742 -18.06626 -32.23092 1.000 26.57510 ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.26092 -16.79428 -32.66407 1.000 31.19316 ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -11.78310 -16.07855 -31.80295 1.000 36.85924 ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -9.23461  -17.64979 -31.56156 1.000 27.37803 ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -8.48987  -18.76380 -30.89304 1.000 49.99085 ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -7.05120  -18.08699 -30.06303 1.000 48.18965 ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -7.74291  -16.66288 -29.24192 1.000 33.30514 ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.26551 -16.47169 -33.95100 1.000 26.72145 ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -11.82433 -15.20883 -34.39339 1.000 26.38082 ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -10.84987 -14.06218 -34.22243 1.000 21.58510 ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.36864 -13.49304 -35.20815 1.000 21.00338 ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.55157 -13.72260 -32.96926 1.000 16.27704 ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.56004  -12.71273 -32.62015 1.000 15.72347 ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.30435  -12.77948 -31.12207 1.000 20.47413 ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.24283 -12.94762 -30.33850 1.000 19.57762 ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -10.02663 -11.30028 -33.00450 1.000 14.77266 ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -8.94529  -10.23033 -32.85361 1.000 17.37358 ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.55509  -8.84099  -32.69087 1.000 14.56476 ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.45068 -8.76582  -31.53989 1.000 15.86021 ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.76704 -8.61398  -31.62087 1.000 19.58884 ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.38289 -8.51490  -32.78815 1.000 17.76685 ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.48554 -8.56444  -30.50172 1.000 15.31134 ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -8.03775  -12.64917 -30.72956 1.000 17.43572 ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.70497  -12.57243 -29.32681 1.000 15.39633 ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.55056  -13.48011 -28.98938 1.000 19.34763 ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -5.80140  -13.92710 -29.86600 1.000 16.64474 ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.40800  -13.75664 -27.69957 1.000 14.24112 ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.30168  -14.56143 -27.20884 1.000 13.86295 ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -5.78773  -15.49290 -26.11253 1.000 19.35067 ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.62370  -15.11672 -25.28342 1.000 17.33980 ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.15597  -13.67407 -26.69666 1.000 18.45985 ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.64245  -12.89940 -27.78517 1.000 19.23271 ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -3.02677  -14.50689 -26.10276 1.000 19.65837 ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.25080  -16.71044 -26.12346 1.000 14.33258 ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.55948  -17.74607 -25.14702 1.000 14.32833 ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.25915  -18.19849 -24.49565 1.000 16.71316 ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.36361  -18.69394 -25.18713 1.000 16.28877 ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.26022  -18.90852 -25.85344 1.000 18.92945 ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -6.58105  -20.09574 -25.00680 1.000 24.51978 ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -7.40230  -21.12074 -25.78724 1.000 31.48837 ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -8.21758  -20.47128 -26.89454 1.000 35.17500 ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -8.65638  -21.48103 -27.89702 1.000 56.96052 ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.13903  -18.01191 -23.18039 1.000 13.72037 ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -2.96482  -18.46336 -22.43368 1.000 9.89423  ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.35693  -19.71813 -21.66737 1.000 14.54268 ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.20315  -19.67009 -20.76896 1.000 14.81480 ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.42871  -17.38187 -21.48476 1.000 12.68755 ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.24006  -17.92250 -20.67772 1.000 13.07564 ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -2.01787  -16.15770 -22.26360 1.000 13.82952 ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.75593  -20.84701 -22.02966 1.000 13.07606 ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -3.03434  -22.12668 -21.39061 1.000 13.86635 ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.88984  -22.42897 -20.43641 1.000 14.57953 ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.73998  -22.58199 -20.86247 1.000 16.11124 ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.21343  -23.24465 -22.42819 1.000 13.40214 ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.30552  -22.85207 -23.42589 1.000 16.72317 ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.56328  -24.55961 -21.73914 1.000 15.39064 ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.24079  -23.60784 -24.73784 1.000 20.66235 ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.19723  -22.48712 -19.14497 1.000 12.58255 ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.20566  -22.76784 -18.11721 1.000 12.36053 ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.29986  -24.23913 -17.74453 1.000 16.74116 ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.31340  -24.67663 -17.19173 1.000 17.98243 ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.42598  -21.88884 -16.88573 1.000 16.12513 ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.47815  -20.37507 -17.09457 1.000 18.99560 ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.74590  -19.68712 -15.76925 1.000 24.43687 ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.17808  -19.86553 -17.70743 1.000 17.51362 ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.25101  -25.00084 -18.04653 1.000 13.70251 ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.17782  -26.40051 -17.63576 1.000 15.52643 ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.44914   -26.39988 -16.24933 1.000 14.93326 ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.66449   -26.25983 -16.10377 1.000 18.19927 ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.61738   -27.22264 -18.64407 1.000 16.48540 ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.14379   -27.05839 -20.05616 1.000 22.24117 ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.60702  -28.01446 -20.70703 1.000 25.18246 ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.29003   -26.03482 -20.93183 1.000 18.46800 ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -0.88731  -27.59400 -21.92843 1.000 27.36606 ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.35444  -26.39562 -22.09017 1.000 22.70640 ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.38814  -26.52336 -15.22581 1.000 15.42876 ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 0.03012   -26.18000 -13.87433 1.000 18.27117 ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 0.97140   -27.22713 -13.29641 1.000 20.89038 ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.87425   -28.42100 -13.59630 1.000 21.04372 ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.18578  -26.03606 -12.95881 1.000 14.97328 ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -2.12584  -24.86283 -13.23398 1.000 14.23495 ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.26587  -24.85330 -12.22625 1.000 19.99217 ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.36591  -23.56118 -13.18160 1.000 20.11488 ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 1.88140   -26.76071 -12.44223 1.000 17.15263 ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.72044   -27.65930 -11.66427 1.000 20.54978 ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.85868   -28.50442 -10.73428 1.000 23.58926 ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.76224   -28.10458 -10.33374 1.000 24.78450 ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.74644   -26.86435 -10.85196 1.000 23.21629 ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.78363   -26.11934 -11.68603 1.000 24.10256 ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.63751   -25.20996 -10.80555 1.000 32.22406 ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.29544   -24.09572 -11.60839 1.000 42.01036 ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.26205   -23.28871 -10.79435 1.000 33.92243 ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.37896   -29.68324 -10.38358 1.000 26.18360 ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.60461   -30.65801 -9.62118  1.000 30.65953 ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.14949   -30.10873 -8.27280  1.000 35.90676 ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.07083   -30.47227 -7.78883  1.000 34.44767 ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.43301   -31.93298 -9.44070  1.000 39.40747 ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 1.94720   -32.87455 -8.35567  1.000 53.82677 ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.91211   -34.01766 -8.11126  1.000 73.71499 ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 2.45725   -35.10454 -7.69355  1.000 70.29151 ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 4.12526   -33.83085 -8.34672  1.000 62.79786 ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 1.93476   -29.22697 -7.65725  1.000 27.71924 ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.60387   -28.70203 -6.33972  1.000 31.24702 ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 0.92925   -27.33512 -6.39550  1.000 24.93077 ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.80065   -26.67923 -5.35677  1.000 27.07247 ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 2.85840   -28.63687 -5.46465  1.000 32.74354 ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 3.93483   -27.74776 -6.04718  1.000 39.49480 ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 3.86060   -27.41838 -7.25082  1.000 46.57294 ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 4.86575   -27.38240 -5.29878  1.000 50.25304 ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.48558   -26.89843 -7.57663  1.000 20.84217 ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.15825  -25.60145 -7.75786  1.000 18.14922 ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.60429  -25.75215 -8.22629  1.000 18.10692 ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.14914  -24.85620 -8.87340  1.000 21.12547 ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.63456   -24.73874 -8.74294  1.000 20.13272 ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.08126   -24.45257 -8.32354  1.000 19.11341 ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.18315   -23.77578 -6.96863  1.000 23.60472 ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.37525   -22.91012 -6.63358  1.000 25.72164 ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.18783   -24.15510 -6.18898  1.000 24.69876 ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.24412  -26.87674 -7.90277  1.000 25.16051 ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.60779  -27.11018 -8.36761  1.000 29.70474 ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.65006  -26.30917 -7.59507  1.000 18.65435 ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.83822  -26.38819 -7.93040  1.000 23.75737 ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.95790  -28.60238 -8.29354  1.000 25.42293 ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.82175  -29.06836 -6.94526  1.000 28.01589 ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -3.04784  -29.42082 -9.21304  1.000 22.96387 ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.24653  -25.54916 -6.57145  1.000 22.43848 ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.20269  -24.68250 -5.88641  1.000 23.68435 ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.77231  -23.62540 -6.82102  1.000 24.22564 ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.87261  -23.11862 -6.58367  1.000 18.87072 ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.54946  -24.01136 -4.67822  1.000 21.45955 ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.57131  -22.90387 -5.03274  1.000 20.88095 ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.77668  -22.43471 -3.83369  1.000 31.49738 ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.83239  -23.14925 -3.43659  1.000 33.38804 ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -3.09903  -21.35845 -3.28609  1.000 29.17138 ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -5.04668  -23.27702 -7.87936  1.000 20.75396 ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.50886  -22.27423 -8.83148  1.000 21.90579 ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.48404  -22.83850 -9.85670  1.000 19.76035 ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.80696  -22.14727 -10.82943 1.000 21.39095 ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.30079  -21.62107 -9.50838  1.000 19.78346 ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.38189  -20.99865 -8.48145  1.000 13.37295 ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.78421  -19.88138 -7.75946  1.000 19.67645 ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.14305  -21.55595 -8.19038  1.000 18.72516 ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.96832  -19.31826 -6.79798  1.000 19.32733 ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.31520  -20.99371 -7.22741  1.000 20.52199 ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.73706  -19.87141 -6.53855  1.000 19.46059 ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.93471  -19.30755 -5.57143  1.000 21.35760 ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.95041  -24.07021 -9.65338  1.000 19.55794 ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.08373  -24.63208 -10.37274 1.000 17.89275 ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.35441  -24.64024 -9.53557  1.000 20.02344 ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.41058 -25.03817 -10.03721 1.000 20.03944 ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.77059  -26.06089 -10.82571 1.000 19.72470 ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.58550  -26.24376 -11.77377 1.000 20.16697 ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.37224  -27.71780 -12.09229 1.000 24.30851 ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.78477  -25.43678 -13.04483 1.000 24.00048 ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.27066  -24.24632 -8.26695  1.000 20.10899 ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.42151 -24.25421 -7.37068  1.000 19.05194 ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.19432 -22.94737 -7.50051  1.000 24.34437 ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.60346 -21.86059 -7.48784  1.000 22.61349 ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -9.98271  -24.46827 -5.92193  1.000 25.03619 ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.26302  -25.78315 -5.66038  1.000 33.60511 ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -10.13475 -26.99512 -5.94937  1.000 63.19653 ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -11.36910 -26.90485 -5.76290  1.000 59.99509 ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -9.58622  -28.03850 -6.36592  1.000 71.31251 ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.51910 -23.06890 -7.61585  1.000 24.61490 ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.37965 -21.91450 -7.85189  1.000 21.05566 ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.16670 -20.82414 -6.80523  1.000 17.59834 ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.94153 -19.65755 -7.14520  1.000 21.73031 ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.83951 -22.36819 -7.86809  1.000 23.13098 ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.80711 -21.32579 -8.37753  1.000 27.32478 ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.26040 -21.73301 -8.18798  1.000 56.54487 ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.51317 -22.76367 -7.52750  1.000 46.42199 ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -18.15076 -21.02216 -8.70018  1.000 56.87214 ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.23305 -21.18512 -5.52164  1.000 24.86230 ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.16511 -20.15955 -4.48491  1.000 25.08093 ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.80416 -19.48141 -4.44726  1.000 23.53797 ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.71270 -18.30628 -4.07678  1.000 21.53128 ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.49181 -20.75300 -3.11783  1.000 24.59201 ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.72245 -22.00436 -2.77483  1.000 32.60869 ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -13.08386 -22.46423 -1.36995  1.000 40.04086 ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.08012 -23.35951 -0.80755  1.000 43.14348 ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.16508 -23.91264 0.39477   1.000 40.15201 ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.20619 -23.69605 1.18273   1.000 45.45238 ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.18057 -24.70083 0.81769   1.000 42.88617 ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.74146 -20.19938 -4.81867  1.000 16.85243 ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.41636  -19.59207 -4.83837  1.000 18.85440 ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.28989  -18.59289 -5.98284  1.000 16.26536 ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.72769  -17.50631 -5.80364  1.000 16.75882 ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.34611  -20.67889 -4.94085  1.000 21.01414 ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.91995  -20.15577 -4.95454  1.000 18.92270 ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.49214  -19.68030 -3.57117  1.000 20.35522 ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -5.05777  -19.42995 -3.50124  1.000 21.09630 ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.50987  -18.23674 -3.31318  1.000 19.83914 ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.25143  -17.15197 -3.15793  1.000 21.52593 ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.18358  -18.12954 -3.28294  1.000 22.10766 ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.81664  -18.93527 -7.16156  1.000 17.93006 ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.74170  -18.01394 -8.29302  1.000 17.97470 ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.58531 -16.77182 -8.02476  1.000 15.53229 ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.12848 -15.64408 -8.25238  1.000 17.19716 ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.16052 -18.70822 -9.60151  1.000 19.56514 ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.18384  -19.83624 -9.94941  1.000 17.49145 ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.20364 -17.68733 -10.74360 1.000 17.97550 ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.78534  -20.90101 -10.86384 1.000 20.55591 ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.81897 -16.95454 -7.52752  1.000 18.21740 ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.64967 -15.80569 -7.15853  1.000 19.10410 ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.94261 -14.88687 -6.17438  1.000 20.97356 ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -12.01828 -13.65824 -6.29866  1.000 18.41846 ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.98931 -16.24104 -6.55769  1.000 21.52073 ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.93595 -16.99974 -7.45406  1.000 29.62460 ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.18907 -17.38759 -6.64961  1.000 27.37802 ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -17.37182 -17.74311 -7.53752  1.000 54.17555 ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -17.03040 -18.52202 -8.75389  1.000 64.14618 ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.27987 -15.46470 -5.17014  1.000 16.98756 ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.57345 -14.65385 -4.18180  1.000 19.60367 ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.47494  -13.82311 -4.83207  1.000 19.74661 ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.30704  -12.63945 -4.51290  1.000 19.08235 ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.98904  -15.55188 -3.08885  1.000 18.65814 ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -9.05229  -14.84844 -2.11162  1.000 24.48419 ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.37164  -15.81917 -1.16435  1.000 21.98101 ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.82784  -16.83212 -1.65123  1.000 23.38841 ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.40470  -15.58355 0.06429   1.000 22.07880 ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.71456  -14.42595 -5.74548  1.000 16.01433 ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.61538  -13.70536 -6.38309  1.000 17.91310 ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.14582  -12.59580 -7.28175  1.000 13.64186 ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.60958  -11.48168 -7.29262  1.000 18.57292 ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.71867  -14.68463 -7.15858  1.000 15.34896 ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -6.02492  -15.64082 -6.18689  1.000 16.58196 ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.70014  -13.93388 -7.99617  1.000 18.10126 ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.49064  -16.88018 -6.86013  1.000 17.41600 ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.20512  -12.87865 -8.04334  1.000 15.38521 ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.77307  -11.87716 -8.94305  1.000 15.47410 ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.32275 -10.69665 -8.15053  1.000 17.68869 ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -10.09274 -9.53113  -8.49802  1.000 19.27009 ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.85367 -12.52156 -9.83318  1.000 19.10013 ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.67642 -11.45603 -10.53632 1.000 16.50228 ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.21407 -13.47972 -10.84776 1.000 15.03863 ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -11.04162 -10.97732 -7.06469  1.000 16.12088 ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.57996 -9.90365  -6.23631  1.000 17.63807 ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.46236 -9.10122  -5.58032  1.000 21.58686 ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.56626 -7.87756  -5.44194  1.000 26.88930 ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.52245 -10.49211 -5.18802  1.000 20.61255 ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.16032 -9.47112  -4.26246  1.000 26.93903 ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.86001 -10.15929 -3.10589  1.000 31.17620 ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.49125 -9.15593  -2.15808  1.000 40.88128 ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.43745 -9.82399  -1.22333  1.000 52.69937 ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.37479  -9.77074  -5.19468  1.000 19.25235 ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.29307  -9.09056  -4.49051  1.000 24.63525 ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.49878  -8.17094  -5.41340  1.000 20.59882 ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.16841  -7.04055  -5.03399  1.000 23.25874 ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.36642  -10.12124 -3.84985  1.000 21.23693 ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.28237  -9.51480  -2.98090  1.000 28.77570 ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.40240  -10.60053 -2.39611  1.000 32.40910 ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.31756  -10.00794 -1.51408  1.000 43.58955 ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.51023  -11.07993 -0.86933  1.000 50.27053 ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.18067  -8.63326  -6.62493  1.000 23.10937 ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.19801  -7.96777  -7.46819  1.000 27.19727 ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.74686  -7.38580  -8.76014  1.000 23.31566 ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -6.03480  -6.61408  -9.40974  1.000 24.89334 ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -5.06784  -8.94034  -7.83787  1.000 24.34966 ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.23843  -9.37242  -6.67471  1.000 19.75010 ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.49725  -8.48904  -5.92022  1.000 24.34341 ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -4.03557  -10.59575 -6.13113  1.000 26.26557 ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.86914  -9.15064  -4.96530  1.000 31.23840 ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.18205  -10.43066 -5.06946  1.000 24.46610 ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.96396  -7.73453  -9.16930  1.000 21.47224 ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.44949  -7.32947  -10.48491 1.000 20.13164 ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.83316  -6.69335  -10.40386 1.000 21.58644 ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.62967 -6.81325  -11.33831 1.000 19.38651 ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.45815  -8.51806  -11.44938 1.000 21.47367 ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -7.18303  -9.14883  -11.48943 1.000 25.24904 ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.12492 -5.98934  -9.30662  1.000 26.58436 ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.47239 -5.46804  -9.10087  1.000 32.87902 ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.80423 -4.29918  -10.02202 1.000 33.80392 ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -12.98574 -3.99010  -10.20319 1.000 31.25282 ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.66736 -5.04126  -7.64102  1.000 34.10208 ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -10.67872 -4.00753  -7.12922  1.000 49.89019 ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -9.43241  -4.61751  -6.50500  1.000 52.26990 ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -8.71393  -5.39419  -7.13827  1.000 36.09445 ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -9.16865  -4.25853  -5.25239  1.000 59.66558 ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.80266 -3.64644  -10.61008 1.000 27.49588 ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.02850 -2.47910  -11.45292 1.000 28.94003 ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.66958 -2.73541  -12.91521 1.000 24.25857 ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.36601 -1.79900  -13.65740 1.000 35.55225 ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.24988 -1.28690  -10.90717 1.000 30.15109 ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.72384 -0.83274  -9.55313  1.000 35.34427 ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.03563 -0.42772  -9.36501  1.000 37.87638 ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -9.86677  -0.83551  -8.46580  1.000 35.31841 ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.48005 -0.01666  -8.12203  1.000 36.97465 ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.30664 -0.42984  -7.22033  1.000 43.39794 ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.61392 -0.02014  -7.04891  1.000 40.09698 ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.69766 -3.99062  -13.34526 1.000 19.13904 ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.52305 -4.30687  -14.75974 1.000 19.25905 ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.82483 -3.99902  -15.48813 1.000 22.44575 ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.90094 -4.45401  -15.08045 1.000 20.75018 ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -10.10277 -5.77480  -14.94184 1.000 18.49194 ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.71494  -6.00437  -14.33451 1.000 17.11851 ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -10.11309 -6.15938  -16.41563 1.000 16.39049 ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.59712  -5.33827  -15.09928 1.000 23.57881 ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.73327 -3.21441  -16.56036 1.000 17.78541 ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.90916 -2.67665  -17.21767 1.000 22.42195 ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.53031 -3.57243  -18.26931 1.000 21.69656 ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.10125 -3.08163  -19.24738 1.000 21.38609 ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.43056 -4.88285  -18.08043 1.000 18.19691 ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -14.02070 -5.85896  -18.98339 1.000 22.47812 ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.59261 -6.99081  -18.15886 1.000 20.97567 ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -14.04571 -7.32876  -17.09938 1.000 18.28283 ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.98869 -6.41029  -19.98248 1.000 14.77381 ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.37106 -5.33370  -20.83505 1.000 19.01933 ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -13.00835 -4.88508  -21.98392 1.000 19.36115 ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.16691 -4.73937  -20.47805 1.000 20.34528 ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.46218 -3.88251  -22.75787 1.000 17.28718 ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.60784 -3.72964  -21.25591 1.000 16.96058 ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.26541 -3.30937  -22.39267 1.000 17.97381 ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.73310 -2.31148  -23.17103 1.000 20.73480 ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.69265 -7.59993  -18.59902 1.000 17.62929 ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.26676 -8.71918  -17.84297 1.000 15.80083 ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.29675 -9.89035  -17.76070 1.000 21.88563 ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.72132 -10.31908 -18.76565 1.000 23.14755 ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.53311 -9.08103  -18.63071 1.000 21.93445 ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.38047 -8.44240  -19.97517 1.000 21.24980 ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.48110 -7.25426  -19.79801 1.000 16.80754 ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.09708 -10.38405 -16.54269 1.000 17.77215 ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.25902 -11.54564 -16.27429 1.000 16.92132 ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.19014 -12.66425 -15.84286 1.000 15.54396 ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.82136 -12.57910 -14.78130 1.000 21.50318 ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.20868 -11.26970 -15.19222 1.000 16.34229 ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.29237 -10.10400 -15.58909 1.000 13.43241 ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.42418 -12.53644 -14.90433 1.000 14.83595 ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.41753 -9.61221  -14.44897 1.000 16.89038 ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.27780 -13.71441 -16.64999 1.000 14.21750 ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.20119 -14.81135 -16.39204 1.000 14.66117 ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.40544 -16.03774 -15.97635 1.000 12.82538 ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.57788 -16.53537 -16.74796 1.000 16.50878 ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -17.05616 -15.12425 -17.61986 1.000 16.72241 ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.82728 -13.96958 -17.97695 1.000 16.48395 ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -18.00650 -16.28679 -17.31285 1.000 19.67131 ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.65669 -16.51470 -14.76119 1.000 16.50156 ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -15.04297 -17.73442 -14.25020 1.000 15.97483 ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.95291 -18.91153 -14.58826 1.000 13.46741 ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -17.04335 -19.04459 -14.02076 1.000 15.28579 ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.81799 -17.62615 -12.74422 1.000 15.71376 ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.29471 -18.86709 -12.02489 1.000 20.29217 ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -13.06397 -19.42300 -12.72126 1.000 17.62434 ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.97548 -18.51215 -10.57706 1.000 18.22871 ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.50971 -19.75434 -15.51756 1.000 15.55466 ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.25599 -20.95210 -15.87953 1.000 15.65060 ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.24948 -21.94457 -14.72046 1.000 21.16298 ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.29005 -22.02549 -13.94950 1.000 18.11994 ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.63847 -21.62438 -17.11270 1.000 13.82706 ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.91169 -20.91827 -18.42549 1.000 14.93757 ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -16.00630 -19.53446 -18.49658 1.000 14.80897 ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -16.02044 -21.65079 -19.60155 1.000 14.71611 ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.23468 -18.89303 -19.70317 1.000 15.03737 ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.24496 -21.01586 -20.82055 1.000 16.06342 ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.35802 -19.63147 -20.86895 1.000 15.52864 ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.31934 -22.72792 -14.61713 1.000 16.05648 ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.39555 -23.80263 -13.63785 1.000 19.26116 ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.22285 -25.13633 -14.36089 1.000 25.60880 ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.30365 -25.22110 -15.58630 1.000 22.76037 ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.70530 -23.76279 -12.82692 1.000 33.00596 ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.58216 -22.75877 -11.69038 1.000 43.24664 ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.87117 -23.40919 -13.71463 1.000 24.35036 ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -16.96660 -26.18640 -13.58596 1.000 23.25778 ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.70754 -27.50738 -14.13901 1.000 27.74772 ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.77765 -28.50775 -13.72206 1.000 32.40226 ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.54396 -28.27077 -12.78363 1.000 36.92759 ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.33335 -28.03629 -13.71479 1.000 32.51343 ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.18011 -27.09596 -14.00104 1.000 28.79747 ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.86691 -27.62615 -13.46489 1.000 42.10478 ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.38575 -28.65430 -13.99414 1.000 31.68564 ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.30425 -27.00052 -12.53819 1.000 36.36724 ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -17.80110 -29.61656 -14.47591 1.000 40.54826 ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -18.55962 -30.87218 -14.28679 1.000 48.34927 ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -19.44324 -31.11735 -15.50213 1.000 58.40208 ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -19.23218 -32.07337 -16.25151 1.000 64.52405 ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -19.41432 -30.89979 -13.01367 1.000 57.36013 ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -18.66532 -31.37825 -11.77996 1.000 51.24227 ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -19.33667 -32.59941 -11.16514 1.000 62.29570 ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -18.33389 -33.44666 -10.39621 1.000 60.23933 ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -17.57153 -32.63539 -9.40658  1.000 61.42541 ? 224 LYS   A NZ  1 
HETATM 1645 C C10 . A1AYA B 2 .   ? -1.04495  -12.83411 -23.44398 1.000 59.78088 ? 301 A1AYA A C10 1 
HETATM 1646 C C12 . A1AYA B 2 .   ? -2.46734  -10.78910 -23.30815 1.000 51.79088 ? 301 A1AYA A C12 1 
HETATM 1647 C C1  . A1AYA B 2 .   ? 1.66313   -6.58540  -25.83364 1.000 43.93240 ? 301 A1AYA A C1  1 
HETATM 1648 C C11 . A1AYA B 2 .   ? -1.12895  -11.44521 -23.53696 1.000 73.53088 ? 301 A1AYA A C11 1 
HETATM 1649 C C2  . A1AYA B 2 .   ? -0.53763  -7.09179  -24.83036 1.000 63.48520 ? 301 A1AYA A C2  1 
HETATM 1650 C C3  . A1AYA B 2 .   ? -0.56380  -8.57843  -25.09686 1.000 73.76923 ? 301 A1AYA A C3  1 
HETATM 1651 C C4  . A1AYA B 2 .   ? 0.57615   -8.43706  -22.91539 1.000 69.24599 ? 301 A1AYA A C4  1 
HETATM 1652 C C5  . A1AYA B 2 .   ? 1.53200   -7.44291  -23.52991 1.000 49.52800 ? 301 A1AYA A C5  1 
HETATM 1653 C C6  . A1AYA B 2 .   ? 0.03624   -10.72543 -23.85169 1.000 55.01088 ? 301 A1AYA A C6  1 
HETATM 1654 C C7  . A1AYA B 2 .   ? 1.23103   -11.40056 -24.04233 1.000 37.94189 ? 301 A1AYA A C7  1 
HETATM 1655 C C8  . A1AYA B 2 .   ? 1.28465   -12.77788 -23.94427 1.000 33.90194 ? 301 A1AYA A C8  1 
HETATM 1656 C C9  . A1AYA B 2 .   ? 0.14929   -13.49318 -23.64549 1.000 50.81753 ? 301 A1AYA A C9  1 
HETATM 1657 N N1  . A1AYA B 2 .   ? 0.85975   -6.61789  -24.58199 1.000 78.62833 ? 301 A1AYA A N1  1 
HETATM 1658 N N2  . A1AYA B 2 .   ? 0.00726   -9.29581  -23.95559 1.000 65.28271 ? 301 A1AYA A N2  1 
HETATM 1659 O O1  . A1AYA B 2 .   ? -3.36898  -10.97824 -24.39283 1.000 36.64088 ? 301 A1AYA A O1  1 
HETATM 1660 O O   . HOH   C 3 .   ? 12.93032  -9.16526  -30.01937 1.000 39.95992 ? 401 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? -14.19273 -7.32980  -42.24145 1.000 50.07351 ? 402 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? -1.53237  -12.14524 -0.33472  1.000 45.93237 ? 403 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -8.18697  -22.40745 -30.41399 1.000 40.01806 ? 404 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? -18.01410 -24.62629 -8.95168  1.000 50.86157 ? 405 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? 2.04893   -15.72574 -41.12549 1.000 36.54813 ? 406 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? -1.62305  -29.17137 -5.94689  1.000 28.87004 ? 407 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? 11.69783  -21.58049 -40.65760 1.000 47.81879 ? 408 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? -2.77757  -3.07818  -17.59647 1.000 43.72243 ? 409 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? 7.69206   -23.11767 -14.32544 1.000 23.37730 ? 410 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? -7.73104  -28.36495 -7.97837  1.000 29.63728 ? 411 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -2.54040  -10.61876 -26.71336 1.000 34.59052 ? 412 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 3.39149   -24.46625 -38.59096 1.000 34.87549 ? 413 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? 0.43899   -14.84878 -1.34508  1.000 33.02122 ? 414 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? -3.95387  -28.05451 -33.74819 1.000 51.69003 ? 415 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? 13.93994  -11.26145 -29.61119 1.000 35.06327 ? 416 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? -3.09320  -3.21256  -35.39335 1.000 37.90416 ? 417 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? -18.79952 -11.09301 -23.80566 1.000 27.45801 ? 418 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 0.63697   -26.93770 -37.11068 1.000 44.37932 ? 419 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? -13.01971 -7.37428  -11.95429 1.000 29.84307 ? 420 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? 3.36824   -5.79090  -5.99434  1.000 37.70373 ? 421 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? -12.16034 -25.83982 -3.58417  1.000 46.29163 ? 422 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? 3.62079   -29.75549 -25.83982 1.000 44.33416 ? 423 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? -3.66479  -13.33892 -42.58512 1.000 41.98730 ? 424 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? 7.57677   -27.90819 -24.04587 1.000 27.26075 ? 425 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? -8.70154  -12.00568 -36.47464 1.000 24.25956 ? 426 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? -17.89283 -2.79938  -35.67883 1.000 44.10731 ? 427 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? 21.59540  -2.98880  -15.28080 1.000 47.85543 ? 428 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? 11.45501  -28.26850 -30.53039 1.000 28.97720 ? 429 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? -16.23872 -25.59410 -17.91327 1.000 22.30213 ? 430 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 1.57466   -26.48506 -2.88366  1.000 40.95555 ? 431 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? 3.48479   -7.76950  -36.65509 1.000 28.86628 ? 432 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? -4.30664  0.43422   -22.12710 1.000 30.64304 ? 433 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? 7.73201   -18.86326 -6.54803  1.000 21.48501 ? 434 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? -0.93737  -11.42514 -3.05287  1.000 33.83577 ? 435 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? -6.45623  -7.82440  -34.37449 1.000 16.13048 ? 436 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? -16.34672 -12.83265 -19.83885 1.000 19.06771 ? 437 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -15.21663 -23.34335 -30.48954 1.000 34.06261 ? 438 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? 18.23861  -7.24934  -20.14277 1.000 33.84102 ? 439 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? 6.67147   -26.81214 -27.74365 1.000 32.30010 ? 440 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? -9.25169  -2.30485  -17.57929 1.000 21.16404 ? 441 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? -8.26538  1.80610   -36.54386 1.000 30.25168 ? 442 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? -6.47086  -5.06219  -39.16429 1.000 37.68605 ? 443 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? 5.91957   -21.92749 -37.36014 1.000 26.00717 ? 444 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? 0.23924   -30.91849 -23.55493 1.000 46.53731 ? 445 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -10.75940 -14.64815 0.87097   1.000 25.38769 ? 446 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -8.46273  4.75514   -33.47776 1.000 28.91149 ? 447 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? 6.06262   -21.20107 -0.11908  1.000 23.13282 ? 448 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -20.716   -21.010   -9.415    1.000 47.96562 ? 449 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? 1.58049   -3.24890  -24.93873 1.000 41.94055 ? 450 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? -0.20750  -5.53676  -38.50772 1.000 44.84078 ? 451 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 9.16229   -26.46705 -17.03945 1.000 23.73959 ? 452 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? -11.13197 -14.24663 -37.65924 1.000 32.62975 ? 453 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? 9.54009   -23.72221 -9.45497  1.000 46.17280 ? 454 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? 1.01978   -6.25882  -34.18942 1.000 42.75748 ? 455 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? -4.30484  -4.74642  -8.56916  1.000 38.72700 ? 456 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? -2.92131  -5.94068  -6.52993  1.000 35.13883 ? 457 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? -13.27928 -0.78362  -20.36885 1.000 30.81098 ? 458 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? 0.72925   -5.36065  -13.89435 1.000 35.07879 ? 459 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? 9.81927   -17.44725 -7.73568  1.000 21.02487 ? 460 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -1.80742  -33.73201 -10.67149 1.000 41.80924 ? 461 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? 11.23338  -8.13380  -27.45521 1.000 20.37955 ? 462 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? 11.51599  -27.38435 -34.67054 1.000 25.39937 ? 463 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? 7.69601   -7.49867  -33.62468 1.000 36.87453 ? 464 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? 10.66592  -25.35139 -23.66614 1.000 20.87772 ? 465 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -15.17061 -11.14675 -29.67942 1.000 23.70013 ? 466 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 7.66332   1.23862   -14.68541 1.000 29.93138 ? 467 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -5.35939  -10.46225 -27.38230 1.000 16.90218 ? 468 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? 5.19979   -29.49533 -8.33536  1.000 44.43237 ? 469 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? 6.72249   -29.72666 -20.21485 1.000 32.26356 ? 470 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? 3.02980   -20.43283 -2.65025  1.000 33.79562 ? 471 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? 13.58627  -14.19576 -26.84320 1.000 24.27921 ? 472 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? -0.27884  -5.47815  -18.45599 1.000 26.18935 ? 473 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? 9.13718   -3.35634  -20.56730 1.000 35.56810 ? 474 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? 0.88906   -21.07448 -4.62137  1.000 23.74927 ? 475 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? -8.15885  -24.95707 -19.14852 1.000 17.68966 ? 476 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? 9.91155   -14.71975 -25.29981 1.000 21.35039 ? 477 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 0.66821   -29.62449 -16.02277 1.000 30.75576 ? 478 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? -17.05505 -5.47898  -22.79624 1.000 24.38398 ? 479 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -2.20802  -13.71137 -35.61067 1.000 18.96932 ? 480 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? 1.38805   -7.88037  -16.57527 1.000 20.31241 ? 481 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? 3.25916   -6.19112  -11.09880 1.000 24.79657 ? 482 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? -14.26860 -11.79789 0.25691   1.000 34.52063 ? 483 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? -2.27220  -0.47034  -18.94240 1.000 45.64870 ? 484 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -17.81194 -18.89016 -11.34466 1.000 30.84733 ? 485 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? 19.77647  -16.76141 -27.49571 1.000 33.03426 ? 486 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? 9.54367   -11.18987 -34.85111 1.000 34.67983 ? 487 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? -8.08316  -3.87372  -10.76943 1.000 29.30945 ? 488 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? 8.85189   -15.41264 -27.79556 1.000 17.22004 ? 489 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -5.77411  -31.33988 -11.57270 1.000 28.12756 ? 490 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? -9.56915  -13.61845 -39.41983 1.000 45.89787 ? 491 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? 3.67335   -6.82768  -17.68790 1.000 23.82278 ? 492 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? -20.568   -14.159   -18.057   1.000 34.98113 ? 493 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? 5.85237   -25.52696 -7.14553  1.000 40.28537 ? 494 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 0.45205   -22.22856 -2.21300  1.000 42.08740 ? 495 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? 18.01877  -19.26879 -24.59632 1.000 24.36443 ? 496 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? -15.88254 0.19813   -30.32734 1.000 34.77294 ? 497 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? -13.06466 -24.95551 -10.77021 1.000 26.99257 ? 498 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? 8.59669   -16.29188 -39.48287 1.000 33.06156 ? 499 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? -5.70821  -2.14540  -19.36510 1.000 18.70143 ? 500 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? 20.62857  -16.77388 -20.07498 1.000 32.44544 ? 501 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? 10.31774  -21.59930 -7.06722  1.000 43.30347 ? 502 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? -19.85703 -12.87399 -16.44702 1.000 42.48541 ? 503 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? -3.379    -21.160   -0.539    1.000 30.96610 ? 504 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -19.76829 -19.47688 -14.26918 1.000 17.70592 ? 505 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? 15.45857  -20.23778 -18.74789 1.000 24.75165 ? 506 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -3.55769  -20.90784 -38.68016 1.000 36.03889 ? 507 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? 14.43066  -15.95368 -30.66005 1.000 34.13803 ? 508 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? -14.51861 -22.75963 -11.38621 1.000 26.24769 ? 509 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -6.24707  -11.37415 -10.11794 1.000 24.87688 ? 510 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? -7.72289  -24.46294 -23.03368 1.000 29.07618 ? 511 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? -6.18217  -14.10462 0.86141   1.000 24.71203 ? 512 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? -14.54558 -6.85028  -14.40059 1.000 33.61347 ? 513 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? -13.78174 -17.08922 -2.65710  1.000 22.12768 ? 514 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 14.42376  -9.30949  -4.29635  1.000 47.62154 ? 515 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? -18.06018 -3.84800  -29.00463 1.000 40.11408 ? 516 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? -19.27086 -10.13492 -33.34377 1.000 40.92548 ? 517 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? -1.75191  -25.73439 -4.72924  1.000 22.79006 ? 518 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? 4.12211   -24.17198 -30.63249 1.000 17.34932 ? 519 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? 8.58604   -0.37001  -17.30467 1.000 41.35720 ? 520 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? 10.76634  -25.64865 -26.67798 1.000 26.92868 ? 521 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? 4.69924   -30.74163 -11.54660 1.000 36.59081 ? 522 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -14.24811 -12.74136 -7.73182  1.000 18.47761 ? 523 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? 16.59738  -14.34508 -7.21525  1.000 40.75900 ? 524 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? 8.54537   -20.51582 -9.23160  1.000 27.29827 ? 525 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? 12.49896  -27.19391 -19.25547 1.000 43.12080 ? 526 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? -0.27829  -7.11342  -31.10878 1.000 31.39345 ? 527 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? -7.82603  -13.56483 -40.89179 1.000 45.48032 ? 528 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? -10.42580 -11.54393 -2.17140  1.000 23.42226 ? 529 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? -14.39678 -3.52504  -12.59718 1.000 41.24513 ? 530 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? -5.46128  -7.66045  -13.15202 1.000 15.23113 ? 531 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? -5.10580  -14.33945 -22.65753 1.000 16.83553 ? 532 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -6.31508  -5.12478  -35.61796 1.000 21.50361 ? 533 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? 14.09565  -15.59125 -2.13117  1.000 32.75502 ? 534 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? 18.41359  -16.17795 -13.42929 1.000 39.04984 ? 535 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? -4.53624  -4.31262  -37.39357 1.000 41.37763 ? 536 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -16.12822 -2.97954  -21.22006 1.000 28.95864 ? 537 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? -0.40904  -14.18543 -42.79704 1.000 43.53420 ? 538 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -11.882   -0.270    -15.508   1.000 39.73102 ? 539 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? -17.35085 -28.67212 -17.11841 1.000 35.49930 ? 540 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? 20.81463  -3.49511  -26.45261 1.000 50.05793 ? 541 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? 14.86536  -0.49323  -12.46119 1.000 43.05987 ? 542 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? 7.98235   -23.28039 -7.22685  1.000 31.22002 ? 543 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? 8.82179   -20.39129 -4.38705  1.000 26.50828 ? 544 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? 13.72685  -20.54397 -20.73181 1.000 17.26501 ? 545 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -9.02666  -10.44119 -40.44282 1.000 33.46353 ? 546 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? -10.75062 -6.42483  -2.96596  1.000 41.25184 ? 547 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? -1.12671  -25.96284 -32.45235 1.000 34.29957 ? 548 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? -1.42547  -4.39829  -34.00547 1.000 35.86408 ? 549 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? -0.06655  -28.53193 -25.57810 1.000 48.35731 ? 550 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? 7.44052   -4.68761  -22.19668 1.000 31.45297 ? 551 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? -13.50858 -26.45769 -18.14306 1.000 22.78643 ? 552 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? -11.93304 -7.64467  -38.21010 1.000 37.59778 ? 553 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? -17.64266 -15.20400 -13.13153 1.000 22.05573 ? 554 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? 4.40738   -19.33895 -40.64940 1.000 33.05750 ? 555 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? -3.07898  -1.11681  -24.15053 1.000 27.16367 ? 556 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? 4.03267   -9.23682  -20.30329 1.000 17.88225 ? 557 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? -10.16956 -15.07563 -28.37257 1.000 25.94455 ? 558 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? 9.64796   -5.73247  -1.68262  1.000 41.74159 ? 559 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? -7.257    1.262     -19.338   1.000 35.47517 ? 560 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? -4.61226  0.47528   -30.58148 1.000 27.83195 ? 561 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? 4.86119   -1.07425  -6.14564  1.000 44.83192 ? 562 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? 15.68940  -18.27888 -3.54295  1.000 27.87161 ? 563 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? 15.38991  -0.63621  -19.35625 1.000 33.76095 ? 564 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? -14.50089 -22.09578 -33.50485 1.000 42.45344 ? 565 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? 20.71906  -7.59575  -15.69506 1.000 42.92614 ? 566 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? -3.98116  -13.99099 -0.69028  1.000 38.36015 ? 567 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? 5.12883   -10.15992 -2.34529  1.000 35.90651 ? 568 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? -12.76437 -27.16879 -35.24824 1.000 43.54932 ? 569 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? 0.77407   -4.76288  -16.26500 1.000 42.08983 ? 570 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? -5.75191  -19.06534 -39.13847 1.000 36.16067 ? 571 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? 10.95922  -11.57773 -4.76327  1.000 33.61629 ? 572 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? 16.30550  -2.99393  -26.28073 1.000 36.81314 ? 573 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? -16.41091 -9.14375  -14.20226 1.000 33.33517 ? 574 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? -1.17368  -29.88423 -17.08992 1.000 38.74920 ? 575 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? -13.05850 -12.32103 -31.00093 1.000 19.33748 ? 576 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? -5.13285  -31.73227 -6.86877  1.000 42.58066 ? 577 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? -3.04583  -31.72945 -20.12203 1.000 47.56313 ? 578 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? 6.95707   -25.28068 -5.49124  1.000 46.58335 ? 579 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? -15.09311 -12.16882 -11.93000 1.000 25.44408 ? 580 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? -16.13714 -25.55659 -10.79563 1.000 35.37495 ? 581 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? -12.18034 -26.96085 -20.29944 1.000 24.45976 ? 582 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? 21.99676  -13.26872 -19.51483 1.000 45.33532 ? 583 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? -10.12439 -0.55749  -19.74886 1.000 33.10764 ? 584 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? -8.71113  -18.03763 -36.67324 1.000 38.55733 ? 585 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? -3.33936  -13.23467 -20.67843 1.000 20.09319 ? 586 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? 3.72426   -23.32263 -3.36663  1.000 36.38103 ? 587 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? 3.82453   -11.75029 -38.69904 1.000 26.73445 ? 588 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? 20.96900  -14.02893 -26.67941 1.000 30.37998 ? 589 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? 20.10583  -10.28857 -26.51179 1.000 41.06053 ? 590 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? -2.26812  -15.89123 -0.15837  1.000 34.16421 ? 591 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? 12.21811  -3.75767  0.28850   1.000 44.49639 ? 592 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? 6.58920   -28.25160 -8.27145  1.000 46.05885 ? 593 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? -13.58138 -25.90687 -7.76866  1.000 23.58726 ? 594 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? -14.57633 -29.44184 -9.76879  1.000 46.00363 ? 595 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? 13.70096  -4.01005  -25.36651 1.000 16.71354 ? 596 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? 13.34441  -6.71943  -26.26668 1.000 20.27664 ? 597 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? -5.90421  -24.44164 -30.17501 1.000 48.03984 ? 598 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? 11.77727  -1.87594  -3.88687  1.000 43.31387 ? 599 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? -13.76889 -18.67398 -24.41958 1.000 18.23034 ? 600 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? -0.07354  -16.59994 -3.35731  1.000 24.71461 ? 601 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? 2.93235   -4.12104  -9.14709  1.000 40.49521 ? 602 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? 6.83879   -30.00813 -30.35247 1.000 42.70166 ? 603 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? 16.985    -25.108   -25.423   1.000 35.94737 ? 604 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? -1.81305  -8.54379  -27.81082 1.000 29.60140 ? 605 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? 3.15098   -4.99625  -29.12539 1.000 40.25048 ? 606 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 3.67154   -30.11807 -19.10407 1.000 38.62857 ? 607 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? -4.97736  -5.25562  -12.00215 1.000 38.96274 ? 608 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? -14.10186 -16.13123 -26.26096 1.000 27.65055 ? 609 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? 15.51627  -7.19437  -27.74071 1.000 30.81076 ? 610 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? -17.83737 -16.17030 -23.51423 1.000 29.63172 ? 611 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? -5.69269  -12.36954 -41.85234 1.000 40.66435 ? 612 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? -19.11023 -13.56335 -27.35710 1.000 44.31630 ? 613 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? 1.852     -18.523   0.031     1.000 32.74732 ? 614 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? 10.64697  -17.57848 -38.87772 1.000 40.41719 ? 615 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? -14.22478 -24.14434 -4.93653  1.000 30.24457 ? 616 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? -15.98671 -3.84832  -15.76558 1.000 46.68928 ? 617 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? -18.47703 -10.78954 -14.34619 1.000 44.69866 ? 618 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? -4.13876  -3.30449  -15.30712 1.000 35.28028 ? 619 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? -18.09722 -5.58693  -25.55656 1.000 33.99068 ? 620 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? 14.49449  -22.58184 -17.20498 1.000 35.83842 ? 621 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? -9.197    -24.976   3.419     1.000 46.75598 ? 622 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? 8.09499   -25.99326 -25.84258 1.000 37.18431 ? 623 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? 4.82734   -1.96280  -18.23177 1.000 43.45966 ? 624 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? 2.05389   -26.01157 -29.30916 1.000 38.41423 ? 625 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? -1.68162  -27.26014 -25.13572 1.000 42.58058 ? 626 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? 1.07571   -8.49711  -4.07331  1.000 40.87396 ? 627 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? 11.29861  -1.70617  -20.21305 1.000 37.54499 ? 628 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? 5.417     -3.072    -26.001   1.000 39.52002 ? 629 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? -17.11180 -4.73141  -17.59729 1.000 33.15543 ? 630 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? -16.96995 -15.57186 -10.37480 1.000 34.91672 ? 631 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? 0.63445   -4.81923  -30.18759 1.000 44.30876 ? 632 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? 18.60612  -9.58048  -30.39743 1.000 52.40883 ? 633 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? -1.25787  -5.61797  -12.08390 1.000 57.45494 ? 634 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? -8.09860  -23.98159 -25.54475 1.000 45.64294 ? 635 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? 7.038     1.862     -12.493   1.000 39.58105 ? 636 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? -3.99808  -33.43463 -11.16476 1.000 47.05063 ? 637 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? -6.52139  3.71907   -34.91678 1.000 39.71100 ? 638 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? 4.34910   -21.99770 -39.33937 1.000 48.62705 ? 639 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? -0.30040  -9.41377  -2.97061  1.000 42.23696 ? 640 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 12.244    -25.349   -38.367   1.000 28.77647 ? 641 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? -9.41396  -5.85690  -39.67599 1.000 44.96414 ? 642 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 0.03784   -19.03161 -1.85175  1.000 35.65419 ? 643 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? -14.06843 -14.29855 -3.13698  1.000 34.48970 ? 644 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? 12.94031  -13.98005 -29.66128 1.000 22.20912 ? 645 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? -0.53415  -1.55707  -23.28260 1.000 37.93640 ? 646 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? -12.34602 -16.38464 -28.16195 1.000 28.63832 ? 647 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? -16.46446 -13.61663 -29.10770 1.000 38.91656 ? 648 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? -14.45321 -10.11216 -8.32415  1.000 37.77801 ? 649 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? -13.93112 -0.67531  -13.57342 1.000 37.06624 ? 650 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? 14.93038  -8.02205  -30.03297 1.000 40.05925 ? 651 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? 5.586     1.662     -16.618   1.000 41.07417 ? 652 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? 1.62744   -3.12718  -12.76444 1.000 41.08526 ? 653 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? -16.88940 -20.43480 -4.62075  1.000 44.08923 ? 654 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 3.77858   -0.28388  -16.44036 1.000 39.92619 ? 655 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? 19.09180  -8.35826  -17.65414 1.000 38.03859 ? 656 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? 16.75711  -6.54887  -29.20595 1.000 41.81532 ? 657 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? -19.47727 -13.25854 -13.80923 1.000 45.44900 ? 658 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? -15.78899 -20.67832 -32.51858 1.000 51.02083 ? 659 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? 10.45088  -21.22929 -42.83282 1.000 50.75964 ? 660 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? -9.84778  -26.10020 -20.86102 1.000 26.28424 ? 661 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? 11.90327  -27.73291 -23.50604 1.000 48.51465 ? 662 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? -6.448    6.949     -36.338   1.000 45.99707 ? 663 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? 7.80529   -29.01130 -28.56168 1.000 40.97465 ? 664 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? -20.66575 -7.46059  -26.25061 1.000 46.04315 ? 665 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 10.94005  -23.27378 -41.87748 1.000 57.46076 ? 666 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? 15.46799  -12.40565 -7.06496  1.000 35.83940 ? 667 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? -18.72124 -11.74616 -21.12282 1.000 26.06453 ? 668 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? 3.43452   -8.99708  -39.17876 1.000 37.83585 ? 669 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? -2.29309  -1.11090  -31.08526 1.000 39.71338 ? 670 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? -14.79506 -14.52398 -37.05105 1.000 49.91559 ? 671 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? -12.478   -10.027   1.448     1.000 44.23059 ? 672 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? 6.73804   -21.47843 -2.65249  1.000 32.48694 ? 673 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? 17.36340  -17.41961 -5.25038  1.000 43.33796 ? 674 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? 10.04498  -29.28431 -23.98972 1.000 43.63212 ? 675 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? -5.92764  -21.20907 -39.59096 1.000 46.77419 ? 676 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? 7.94262   -14.10200 -38.24765 1.000 38.20871 ? 677 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? -21.28815 -33.87772 -8.28875  1.000 56.92195 ? 678 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? 20.32589  -6.00644  -21.03998 1.000 41.18306 ? 679 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? -4.26854  -29.50436 -22.47035 1.000 45.24976 ? 680 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? 6.33743   -30.00097 -24.90095 1.000 46.97202 ? 681 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? 5.77553   -12.97806 -39.90574 1.000 29.66575 ? 682 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? -13.80200 -13.53642 -38.25425 1.000 42.54245 ? 683 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? 2.28635   -0.71629  -14.31356 1.000 55.76144 ? 684 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? 11.15154  -1.16477  -17.28750 1.000 41.53721 ? 685 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? -19.52285 -1.96678  -37.56393 1.000 48.15356 ? 686 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? -11.73236 -9.81034  -39.98378 1.000 50.00864 ? 687 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? -16.94887 -0.46329  -17.71240 1.000 44.87043 ? 688 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? 18.22386  -18.68039 -6.96966  1.000 42.33765 ? 689 HOH   A O   1 
HETATM 1949 O O   . HOH   C 3 .   ? -10.524   -22.645   4.444     1.000 42.33839 ? 690 HOH   A O   1 
HETATM 1950 O O   . HOH   C 3 .   ? -10.61969 -17.00144 -38.08826 1.000 41.83903 ? 691 HOH   A O   1 
HETATM 1951 O O   . HOH   C 3 .   ? -16.82240 -5.75539  -14.10958 1.000 53.80541 ? 692 HOH   A O   1 
HETATM 1952 O O   . HOH   C 3 .   ? -6.96732  -30.80427 -9.25960  1.000 35.18238 ? 693 HOH   A O   1 
HETATM 1953 O O   . HOH   C 3 .   ? -1.950    -23.211   0.843     1.000 44.35993 ? 694 HOH   A O   1 
HETATM 1954 O O   . HOH   C 3 .   ? 8.234     -8.194    0.274     1.000 47.16030 ? 695 HOH   A O   1 
HETATM 1955 O O   . HOH   C 3 .   ? -6.54367  -27.18414 -23.12026 1.000 46.71417 ? 696 HOH   A O   1 
HETATM 1956 O O   . HOH   C 3 .   ? -10.50600 -8.73724  -1.17513  1.000 39.78982 ? 697 HOH   A O   1 
HETATM 1957 O O   . HOH   C 3 .   ? 22.88193  -15.66203 -19.32669 1.000 44.45200 ? 698 HOH   A O   1 
HETATM 1958 O O   . HOH   C 3 .   ? -12.07099 -20.51194 -25.44631 1.000 37.16321 ? 699 HOH   A O   1 
HETATM 1959 O O   . HOH   C 3 .   ? 11.07656  -28.16157 -27.86070 1.000 36.00874 ? 700 HOH   A O   1 
HETATM 1960 O O   . HOH   C 3 .   ? 19.29654  -7.21740  -29.87379 1.000 49.19263 ? 701 HOH   A O   1 
HETATM 1961 O O   . HOH   C 3 .   ? 4.77196   -14.77412 -41.58450 1.000 46.82441 ? 702 HOH   A O   1 
HETATM 1962 O O   . HOH   C 3 .   ? 14.31933  -28.39956 -23.28751 1.000 48.93587 ? 703 HOH   A O   1 
HETATM 1963 O O   . HOH   C 3 .   ? -21.04209 -4.25602  -29.14877 1.000 40.13119 ? 704 HOH   A O   1 
HETATM 1964 O O   . HOH   C 3 .   ? -0.57133  -26.74531 -30.22783 1.000 37.84192 ? 705 HOH   A O   1 
HETATM 1965 O O   . HOH   C 3 .   ? 3.007     -2.069    -20.390   1.000 42.68830 ? 706 HOH   A O   1 
HETATM 1966 O O   . HOH   C 3 .   ? 11.33864  -30.15673 -34.35424 1.000 35.36338 ? 707 HOH   A O   1 
HETATM 1967 O O   . HOH   C 3 .   ? -16.06942 -1.37979  -15.29972 1.000 48.57370 ? 708 HOH   A O   1 
HETATM 1968 O O   . HOH   C 3 .   ? 12.97196  -25.05005 -15.89435 1.000 45.49745 ? 709 HOH   A O   1 
HETATM 1969 O O   . HOH   C 3 .   ? -4.02052  -27.91521 -24.08540 1.000 47.44381 ? 710 HOH   A O   1 
HETATM 1970 O O   . HOH   C 3 .   ? -6.749    -23.312   -1.634    1.000 39.56947 ? 711 HOH   A O   1 
HETATM 1971 O O   . HOH   C 3 .   ? 6.481     -6.621    0.491     1.000 48.21931 ? 712 HOH   A O   1 
HETATM 1972 O O   . HOH   C 3 .   ? 9.58147   -25.26234 -14.64703 1.000 40.56619 ? 713 HOH   A O   1 
HETATM 1973 O O   . HOH   C 3 .   ? -21.02578 -12.35116 -24.82451 1.000 44.96046 ? 714 HOH   A O   1 
HETATM 1974 O O   . HOH   C 3 .   ? -6.36149  -25.37351 -27.52199 1.000 43.84282 ? 715 HOH   A O   1 
HETATM 1975 O O   . HOH   C 3 .   ? -16.50876 -12.99801 -6.50450  1.000 44.38129 ? 716 HOH   A O   1 
HETATM 1976 O O   . HOH   C 3 .   ? 2.01840   -5.63444  -36.61464 1.000 46.86031 ? 717 HOH   A O   1 
HETATM 1977 O O   . HOH   C 3 .   ? -12.35642 -13.16770 -0.97661  1.000 28.00600 ? 718 HOH   A O   1 
HETATM 1978 O O   . HOH   C 3 .   ? -19.05225 -4.51022  -18.80371 1.000 47.54603 ? 719 HOH   A O   1 
HETATM 1979 O O   . HOH   C 3 .   ? 19.286    -20.725   -22.202   1.000 37.16548 ? 720 HOH   A O   1 
HETATM 1980 O O   . HOH   C 3 .   ? -14.85243 -9.69326  -11.36780 1.000 33.09041 ? 721 HOH   A O   1 
HETATM 1981 O O   . HOH   C 3 .   ? -20.45049 -34.07790 -6.15832  1.000 45.98715 ? 722 HOH   A O   1 
HETATM 1982 O O   . HOH   C 3 .   ? 4.044     -1.979    -28.346   1.000 41.30477 ? 723 HOH   A O   1 
HETATM 1983 O O   . HOH   C 3 .   ? -10.463   -11.928   1.998     1.000 38.83985 ? 724 HOH   A O   1 
HETATM 1984 O O   . HOH   C 3 .   ? 23.69779  -5.85615  -24.49976 1.000 56.72982 ? 725 HOH   A O   1 
HETATM 1985 O O   . HOH   C 3 .   ? -21.968   -34.715   -13.579   1.000 53.69684 ? 726 HOH   A O   1 
HETATM 1986 O O   . HOH   C 3 .   ? -20.75494 -10.68960 -19.48782 1.000 43.28336 ? 727 HOH   A O   1 
HETATM 1987 O O   . HOH   C 3 .   ? -16.14335 -13.66387 -3.76557  1.000 38.42693 ? 728 HOH   A O   1 
HETATM 1988 O O   . HOH   C 3 .   ? 9.70037   -12.56869 -37.05019 1.000 41.68501 ? 729 HOH   A O   1 
HETATM 1989 O O   . HOH   C 3 .   ? -19.05452 -8.47897  -14.96143 1.000 46.54417 ? 730 HOH   A O   1 
HETATM 1990 O O   . HOH   C 3 .   ? -14.52157 -14.18135 -10.24078 1.000 27.74755 ? 731 HOH   A O   1 
HETATM 1991 O O   . HOH   C 3 .   ? 13.66337  -11.77825 -5.11207  1.000 26.93155 ? 732 HOH   A O   1 
HETATM 1992 O O   . HOH   C 3 .   ? -5.314    -25.824   -1.684    1.000 49.58372 ? 733 HOH   A O   1 
HETATM 1993 O O   . HOH   C 3 .   ? 14.70015  -13.03704 -2.94134  1.000 40.11320 ? 734 HOH   A O   1 
HETATM 1994 O O   . HOH   C 3 .   ? -8.76131  -10.78421 -0.02875  1.000 42.12603 ? 735 HOH   A O   1 
HETATM 1995 O O   . HOH   C 3 .   ? -22.45665 -8.10351  -24.96157 1.000 45.75502 ? 736 HOH   A O   1 
HETATM 1996 O O   . HOH   C 3 .   ? -16.45947 -18.36148 -2.86277  1.000 40.65857 ? 737 HOH   A O   1 
HETATM 1997 O O   . HOH   C 3 .   ? -19.51995 -5.65315  -21.51663 1.000 36.43978 ? 738 HOH   A O   1 
HETATM 1998 O O   . HOH   C 3 .   ? -15.31284 -7.38841  -7.43314  1.000 50.75219 ? 739 HOH   A O   1 
HETATM 1999 O O   . HOH   C 3 .   ? 19.614    1.346     -16.444   1.000 47.16156 ? 740 HOH   A O   1 
HETATM 2000 O O   . HOH   C 3 .   ? -16.31877 -9.08543  -6.10395  1.000 51.69180 ? 741 HOH   A O   1 
HETATM 2001 O O   . HOH   C 3 .   ? -9.505    0.612     -3.430    1.000 48.07494 ? 742 HOH   A O   1 
HETATM 2002 O O   . HOH   C 3 .   ? 7.30271   -0.95068  -4.19109  1.000 49.40083 ? 743 HOH   A O   1 
HETATM 2003 O O   . HOH   C 3 .   ? -9.29225  -32.89912 -8.62389  1.000 42.90215 ? 744 HOH   A O   1 
HETATM 2004 O O   . HOH   C 3 .   ? 7.08381   -11.12965 -40.90591 1.000 48.95531 ? 745 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   ? 0.45497 0.68094 0.41832 -0.08253 -0.02345 -0.25438 16  GLU A N   
2    C CA  . GLU A 9   ? 0.63074 0.81630 0.58138 -0.05153 -0.02893 -0.23397 16  GLU A CA  
3    C C   . GLU A 9   ? 0.52632 0.70119 0.48963 -0.03706 -0.03318 -0.21374 16  GLU A C   
4    O O   . GLU A 9   ? 0.52630 0.75504 0.50538 -0.02128 -0.04262 -0.20602 16  GLU A O   
5    C CB  . GLU A 9   ? 0.75527 0.98900 0.70165 -0.02196 -0.04027 -0.23022 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.93300 1.11934 0.86011 0.00428  -0.04014 -0.21473 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.21523 1.42005 1.12603 0.01561  -0.04203 -0.22164 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.17600 1.43643 1.09094 0.04215  -0.05162 -0.21384 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.22087 1.38143 1.11229 0.00049  -0.03227 -0.23365 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.43080 0.53558 0.38577 -0.03993 -0.02453 -0.20477 17  VAL A N   
11   C CA  . VAL A 10  ? 0.31345 0.40257 0.28014 -0.03018 -0.02680 -0.18806 17  VAL A CA  
12   C C   . VAL A 10  ? 0.33550 0.39361 0.29420 0.00002  -0.02928 -0.17176 17  VAL A C   
13   O O   . VAL A 10  ? 0.37980 0.39088 0.32295 0.00336  -0.02001 -0.17100 17  VAL A O   
14   C CB  . VAL A 10  ? 0.39693 0.43485 0.36321 -0.05485 -0.01264 -0.18871 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.40576 0.43519 0.38582 -0.04508 -0.01594 -0.17250 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.46594 0.53190 0.43871 -0.08594 -0.00623 -0.20609 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.26049 0.34277 0.22813 0.02360  -0.03956 -0.15735 18  GLU A N   
18   C CA  . GLU A 11  ? 0.26842 0.31932 0.23330 0.04953  -0.03791 -0.13207 18  GLU A CA  
19   C C   . GLU A 11  ? 0.25816 0.27837 0.23695 0.04626  -0.03394 -0.11456 18  GLU A C   
20   O O   . GLU A 11  ? 0.21992 0.26122 0.21086 0.04019  -0.03831 -0.11351 18  GLU A O   
21   C CB  . GLU A 11  ? 0.28896 0.37619 0.24888 0.07759  -0.04562 -0.12055 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.25140 0.36949 0.19325 0.08912  -0.04922 -0.13276 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.42948 0.57872 0.36114 0.12187  -0.05317 -0.11679 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.45222 0.64479 0.39293 0.12765  -0.05829 -0.11511 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.48328 0.61017 0.39940 0.14228  -0.04730 -0.10300 18  GLU A OE2 
26   N N   . THR A 12  ? 0.23053 0.20725 0.20692 0.05182  -0.02571 -0.10140 19  THR A N   
27   C CA  . THR A 12  ? 0.21633 0.17128 0.20398 0.05147  -0.02239 -0.08498 19  THR A CA  
28   C C   . THR A 12  ? 0.24067 0.19806 0.23279 0.06977  -0.02361 -0.06627 19  THR A C   
29   O O   . THR A 12  ? 0.21965 0.17028 0.20397 0.08191  -0.02010 -0.06212 19  THR A O   
30   C CB  . THR A 12  ? 0.24148 0.15239 0.22126 0.04598  -0.01024 -0.08386 19  THR A CB  
31   O OG1 . THR A 12  ? 0.29495 0.19347 0.26496 0.02427  -0.00370 -0.10416 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.26895 0.16769 0.25860 0.04816  -0.00787 -0.06711 19  THR A CG2 
33   N N   . PHE A 13  ? 0.22386 0.18999 0.22701 0.06928  -0.02649 -0.05681 20  PHE A N   
34   C CA  . PHE A 13  ? 0.22069 0.18741 0.22622 0.07883  -0.02427 -0.04276 20  PHE A CA  
35   C C   . PHE A 13  ? 0.28256 0.24311 0.29972 0.07102  -0.02174 -0.03317 20  PHE A C   
36   O O   . PHE A 13  ? 0.24064 0.19882 0.26401 0.06387  -0.02441 -0.03588 20  PHE A O   
37   C CB  . PHE A 13  ? 0.17197 0.15514 0.17311 0.08441  -0.02645 -0.04046 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.18869 0.19030 0.17596 0.09770  -0.02957 -0.04757 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.24855 0.27835 0.23728 0.09265  -0.03736 -0.06279 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.24088 0.23729 0.21198 0.10614  -0.02262 -0.03711 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.25725 0.31798 0.23306 0.10542  -0.04151 -0.07067 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.28744 0.30472 0.24151 0.12169  -0.02576 -0.04159 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.28921 0.34458 0.24710 0.12775  -0.03669 -0.06040 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.21165 0.17399 0.23145 0.07148  -0.01583 -0.02338 21  ALA A N   
45   C CA  . ALA A 14  ? 0.17520 0.14309 0.20645 0.06815  -0.01567 -0.01820 21  ALA A CA  
46   C C   . ALA A 14  ? 0.20334 0.17350 0.23579 0.06438  -0.01600 -0.01892 21  ALA A C   
47   O O   . ALA A 14  ? 0.20482 0.16764 0.22706 0.06832  -0.01026 -0.01841 21  ALA A O   
48   C CB  . ALA A 14  ? 0.16698 0.14347 0.20344 0.07394  -0.01063 -0.01345 21  ALA A CB  
49   N N   . PHE A 15  ? 0.15888 0.13547 0.19869 0.05640  -0.01940 -0.01852 22  PHE A N   
50   C CA  . PHE A 15  ? 0.23376 0.21033 0.27184 0.04949  -0.01604 -0.01899 22  PHE A CA  
51   C C   . PHE A 15  ? 0.20263 0.18177 0.24101 0.04234  -0.00679 -0.01868 22  PHE A C   
52   O O   . PHE A 15  ? 0.20948 0.20672 0.25758 0.04076  -0.00691 -0.01729 22  PHE A O   
53   C CB  . PHE A 15  ? 0.19927 0.18586 0.24510 0.04167  -0.02091 -0.01905 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.16657 0.15162 0.21144 0.04313  -0.02621 -0.02139 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.21154 0.19486 0.24859 0.04776  -0.02534 -0.02410 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.17561 0.16179 0.22521 0.04065  -0.02952 -0.02071 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.21367 0.20867 0.25311 0.04770  -0.03028 -0.02810 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.18433 0.17234 0.23419 0.03627  -0.03178 -0.02547 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.16469 0.16328 0.21222 0.03870  -0.03347 -0.03020 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.23929 0.20059 0.26496 0.03812  0.00370  -0.02042 23  GLN A N   
61   C CA  . GLN A 16  ? 0.25572 0.21867 0.28132 0.02160  0.01588  -0.02459 23  GLN A CA  
62   C C   . GLN A 16  ? 0.21082 0.20617 0.25262 0.00769  0.00933  -0.02923 23  GLN A C   
63   O O   . GLN A 16  ? 0.19282 0.19281 0.23750 0.00962  0.00061  -0.02859 23  GLN A O   
64   C CB  . GLN A 16  ? 0.27328 0.19894 0.27562 0.01763  0.03286  -0.02652 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.33757 0.23255 0.31797 0.03548  0.04295  -0.01960 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.50336 0.35309 0.45316 0.03806  0.06349  -0.01818 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.49284 0.33578 0.43044 0.05516  0.05984  -0.01281 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.54285 0.36662 0.47976 0.01919  0.08578  -0.02283 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.18758 0.21174 0.23975 -0.00572 0.01397  -0.03416 24  ALA A N   
70   C CA  . ALA A 17  ? 0.17210 0.24224 0.23981 -0.01437 0.00617  -0.03814 24  ALA A CA  
71   C C   . ALA A 17  ? 0.16970 0.23386 0.23131 -0.02707 0.00656  -0.04522 24  ALA A C   
72   O O   . ALA A 17  ? 0.20813 0.29634 0.27672 -0.02270 -0.00453 -0.04292 24  ALA A O   
73   C CB  . ALA A 17  ? 0.18708 0.29965 0.26654 -0.03027 0.01330  -0.04626 24  ALA A CB  
74   N N   . GLU A 18  ? 0.25058 0.27771 0.29491 -0.04054 0.02163  -0.05280 25  GLU A N   
75   C CA  . GLU A 18  ? 0.29784 0.31399 0.33229 -0.05215 0.02497  -0.06077 25  GLU A CA  
76   C C   . GLU A 18  ? 0.23590 0.23818 0.26744 -0.03243 0.01364  -0.05129 25  GLU A C   
77   O O   . GLU A 18  ? 0.23051 0.24540 0.26299 -0.03711 0.00864  -0.05473 25  GLU A O   
78   C CB  . GLU A 18  ? 0.41738 0.38400 0.42640 -0.06774 0.04911  -0.06984 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.47422 0.45236 0.48413 -0.09679 0.06569  -0.08383 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.55188 0.52159 0.56281 -0.08891 0.07214  -0.07611 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.36653 0.32784 0.37936 -0.06030 0.06096  -0.06067 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.64430 0.61691 0.65312 -0.11388 0.09002  -0.08734 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.23310 0.21493 0.26129 -0.01199 0.00995  -0.04096 26  ILE A N   
84   C CA  . ILE A 19  ? 0.23652 0.21447 0.26460 0.00236  0.00029  -0.03500 26  ILE A CA  
85   C C   . ILE A 19  ? 0.18781 0.19663 0.23287 0.00560  -0.01373 -0.03030 26  ILE A C   
86   O O   . ILE A 19  ? 0.20978 0.22479 0.25644 0.00680  -0.01919 -0.02883 26  ILE A O   
87   C CB  . ILE A 19  ? 0.25652 0.21309 0.27498 0.02084  0.00132  -0.02904 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.30506 0.22606 0.29835 0.02711  0.01698  -0.02940 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.21535 0.18525 0.24148 0.03082  -0.01078 -0.02585 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.40243 0.29604 0.38044 0.01373  0.03631  -0.03414 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.16646 0.19212 0.22108 0.00897  -0.01704 -0.02677 27  ALA A N   
92   C CA  . ALA A 20  ? 0.14488 0.19287 0.20824 0.01629  -0.02538 -0.01998 27  ALA A CA  
93   C C   . ALA A 20  ? 0.16756 0.24529 0.23385 0.00821  -0.02784 -0.02263 27  ALA A C   
94   O O   . ALA A 20  ? 0.21690 0.30141 0.28258 0.01505  -0.03267 -0.01621 27  ALA A O   
95   C CB  . ALA A 20  ? 0.16717 0.22880 0.23627 0.02520  -0.02541 -0.01524 27  ALA A CB  
96   N N   . GLN A 21  ? 0.20086 0.29661 0.26811 -0.00803 -0.02275 -0.03331 28  GLN A N   
97   C CA  . GLN A 21  ? 0.20645 0.33872 0.27560 -0.01850 -0.02540 -0.03989 28  GLN A CA  
98   C C   . GLN A 21  ? 0.18657 0.29695 0.24549 -0.02208 -0.02488 -0.04226 28  GLN A C   
99   O O   . GLN A 21  ? 0.21552 0.35013 0.27426 -0.02018 -0.03059 -0.04056 28  GLN A O   
100  C CB  . GLN A 21  ? 0.18482 0.34241 0.25665 -0.04196 -0.01732 -0.05608 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.36117 0.57432 0.43707 -0.05546 -0.02117 -0.06712 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.48441 0.70980 0.55615 -0.08279 -0.00791 -0.08525 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.53237 0.73209 0.60328 -0.09606 0.00388  -0.09192 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.45099 0.71290 0.51704 -0.09081 -0.00715 -0.09321 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.20319 0.27022 0.25154 -0.02356 -0.01731 -0.04473 29  LEU A N   
106  C CA  . LEU A 22  ? 0.21831 0.26680 0.25663 -0.02240 -0.01589 -0.04568 29  LEU A CA  
107  C C   . LEU A 22  ? 0.28411 0.33882 0.32851 -0.00835 -0.02526 -0.03407 29  LEU A C   
108  O O   . LEU A 22  ? 0.23949 0.30490 0.28132 -0.00929 -0.02753 -0.03358 29  LEU A O   
109  C CB  . LEU A 22  ? 0.27349 0.27879 0.29680 -0.01861 -0.00480 -0.04751 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.28663 0.27685 0.30011 -0.00989 -0.00329 -0.04586 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.31610 0.30361 0.31698 -0.02330 0.00424  -0.05656 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.27451 0.23338 0.27441 0.00569  0.00490  -0.04213 29  LEU A CD2 
113  N N   . MET A 23  ? 0.16229 0.20823 0.21245 0.00275  -0.02855 -0.02587 30  MET A N   
114  C CA  . MET A 23  ? 0.21752 0.26210 0.26992 0.01015  -0.03238 -0.01783 30  MET A CA  
115  C C   . MET A 23  ? 0.22297 0.28835 0.27587 0.01456  -0.03520 -0.00991 30  MET A C   
116  O O   . MET A 23  ? 0.20303 0.26757 0.25195 0.01686  -0.03464 -0.00437 30  MET A O   
117  C CB  . MET A 23  ? 0.21411 0.24209 0.26911 0.01662  -0.03261 -0.01489 30  MET A CB  
118  C CG  . MET A 23  ? 0.21990 0.23572 0.27226 0.01876  -0.03085 -0.02060 30  MET A CG  
119  S SD  . MET A 23  ? 0.21685 0.22283 0.27020 0.02543  -0.03145 -0.02088 30  MET A SD  
120  C CE  . MET A 23  ? 0.19358 0.19938 0.25030 0.02158  -0.03260 -0.02186 30  MET A CE  
121  N N   . SER A 24  ? 0.20185 0.28910 0.25793 0.01818  -0.03690 -0.00817 31  SER A N   
122  C CA  . SER A 24  ? 0.17253 0.28693 0.22523 0.02949  -0.03908 0.00161  31  SER A CA  
123  C C   . SER A 24  ? 0.20991 0.35067 0.25862 0.02211  -0.04142 -0.00350 31  SER A C   
124  O O   . SER A 24  ? 0.25930 0.40972 0.29970 0.03284  -0.04160 0.00664  31  SER A O   
125  C CB  . SER A 24  ? 0.25683 0.40235 0.31460 0.03856  -0.04078 0.00431  31  SER A CB  
126  O OG  . SER A 24  ? 0.48916 0.66422 0.55516 0.02178  -0.04197 -0.01043 31  SER A OG  
127  N N   . LEU A 25  ? 0.17310 0.32013 0.22342 0.00410  -0.04061 -0.01923 32  LEU A N   
128  C CA  . LEU A 25  ? 0.16740 0.33439 0.21075 -0.00534 -0.04115 -0.02738 32  LEU A CA  
129  C C   . LEU A 25  ? 0.25815 0.39835 0.29425 -0.00126 -0.03897 -0.02158 32  LEU A C   
130  O O   . LEU A 25  ? 0.22128 0.37948 0.25011 0.00272  -0.04042 -0.01758 32  LEU A O   
131  C CB  . LEU A 25  ? 0.26436 0.42977 0.30529 -0.02813 -0.03528 -0.04760 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.34896 0.53214 0.37928 -0.04381 -0.03287 -0.06250 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.40805 0.59875 0.43559 -0.06895 -0.02390 -0.08324 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.37882 0.52051 0.39700 -0.04278 -0.02672 -0.06274 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.17271 0.27622 0.21038 -0.00151 -0.03513 -0.02141 33  ILE A N   
136  C CA  . ILE A 26  ? 0.18828 0.27633 0.22238 0.00101  -0.03251 -0.01764 33  ILE A CA  
137  C C   . ILE A 26  ? 0.26673 0.35596 0.29945 0.01052  -0.03222 -0.00322 33  ILE A C   
138  O O   . ILE A 26  ? 0.26328 0.35436 0.28982 0.01119  -0.02926 0.00099  33  ILE A O   
139  C CB  . ILE A 26  ? 0.16674 0.22938 0.20408 0.00157  -0.02936 -0.02089 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.19889 0.24948 0.22726 -0.00341 -0.02370 -0.03225 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.15937 0.21883 0.19854 0.00398  -0.02731 -0.01666 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.26545 0.29429 0.29238 0.00374  -0.01975 -0.03318 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.18460 0.26845 0.21928 0.01883  -0.03235 0.00509  34  ILE A N   
144  C CA  . ILE A 27  ? 0.24785 0.31644 0.27404 0.02872  -0.02598 0.01948  34  ILE A CA  
145  C C   . ILE A 27  ? 0.28140 0.37440 0.29477 0.04224  -0.02584 0.03066  34  ILE A C   
146  O O   . ILE A 27  ? 0.34335 0.42364 0.34330 0.04883  -0.01769 0.04223  34  ILE A O   
147  C CB  . ILE A 27  ? 0.27276 0.31875 0.29995 0.03484  -0.02280 0.02379  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.25088 0.27535 0.28684 0.02253  -0.02149 0.01368  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.31808 0.34214 0.32781 0.04943  -0.01177 0.04043  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.22470 0.23262 0.26245 0.02620  -0.02058 0.01279  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.27466 0.40715 0.29061 0.04622  -0.03364 0.02677  35  ASN A N   
152  C CA  . ASN A 28  ? 0.25851 0.42739 0.26197 0.06519  -0.03490 0.03844  35  ASN A CA  
153  C C   . ASN A 28  ? 0.33698 0.54591 0.33594 0.05887  -0.04025 0.03028  35  ASN A C   
154  O O   . ASN A 28  ? 0.36285 0.60170 0.34700 0.07724  -0.04027 0.04207  35  ASN A O   
155  C CB  . ASN A 28  ? 0.31799 0.52172 0.32745 0.07627  -0.04014 0.03908  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.35195 0.51681 0.36006 0.08816  -0.03320 0.04947  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.45679 0.58224 0.44798 0.10264  -0.02191 0.06533  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.50477 0.67595 0.52772 0.08055  -0.03726 0.03964  35  ASN A ND2 
159  N N   . THR A 29  ? 0.20600 0.41498 0.21313 0.03595  -0.04306 0.01093  36  THR A N   
160  C CA  . THR A 29  ? 0.22132 0.46381 0.22090 0.02744  -0.04612 -0.00014 36  THR A CA  
161  C C   . THR A 29  ? 0.29764 0.52326 0.28357 0.03495  -0.04037 0.01102  36  THR A C   
162  O O   . THR A 29  ? 0.30659 0.48962 0.29499 0.03118  -0.03352 0.01490  36  THR A O   
163  C CB  . THR A 29  ? 0.27527 0.50734 0.28051 0.00190  -0.04508 -0.02360 36  THR A CB  
164  O OG1 . THR A 29  ? 0.27109 0.51802 0.28693 -0.00798 -0.04724 -0.03443 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.28114 0.54079 0.27435 -0.00939 -0.04543 -0.03805 36  THR A CG2 
166  N N   . PHE A 30  ? 0.21129 0.47611 0.18261 0.04531  -0.04264 0.01542  37  PHE A N   
167  C CA  . PHE A 30  ? 0.24984 0.50088 0.20646 0.05004  -0.03579 0.02407  37  PHE A CA  
168  C C   . PHE A 30  ? 0.27698 0.51734 0.23692 0.02828  -0.03488 0.00427  37  PHE A C   
169  O O   . PHE A 30  ? 0.21890 0.48856 0.17656 0.01523  -0.03972 -0.01517 37  PHE A O   
170  C CB  . PHE A 30  ? 0.22896 0.52542 0.16604 0.06952  -0.03733 0.03422  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.28893 0.57083 0.20715 0.07610  -0.02867 0.04551  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.33226 0.56635 0.24092 0.08760  -0.01419 0.06752  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.27920 0.58820 0.19031 0.06683  -0.03117 0.03150  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.32858 0.54762 0.22086 0.09037  -0.00288 0.07717  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.37536 0.67272 0.26817 0.07337  -0.02229 0.04229  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.32578 0.57850 0.21089 0.08487  -0.00772 0.06561  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.23123 0.43114 0.19452 0.02435  -0.02676 0.00815  38  TYR A N   
178  C CA  . TYR A 31  ? 0.20039 0.38684 0.16508 0.01038  -0.02365 -0.00768 38  TYR A CA  
179  C C   . TYR A 31  ? 0.20306 0.36632 0.16844 0.01308  -0.01434 0.00248  38  TYR A C   
180  O O   . TYR A 31  ? 0.24035 0.38050 0.21785 0.01204  -0.01085 0.00827  38  TYR A O   
181  C CB  . TYR A 31  ? 0.23195 0.39921 0.20869 -0.00077 -0.02496 -0.02148 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.27338 0.41755 0.24683 -0.00728 -0.01794 -0.03314 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.32103 0.46972 0.27856 -0.01550 -0.01410 -0.04909 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.29849 0.41863 0.28207 -0.00351 -0.01381 -0.02890 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.37880 0.50008 0.32759 -0.01586 -0.00424 -0.05767 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.31338 0.41805 0.29123 -0.00210 -0.00647 -0.03696 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.39185 0.49292 0.35089 -0.00632 -0.00071 -0.04989 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.58006 0.65977 0.52816 0.00042  0.00979  -0.05585 38  TYR A OH  
189  N N   . SER A 32  ? 0.20447 0.37842 0.15694 0.01462  -0.00964 0.00274  39  SER A N   
190  C CA  . SER A 32  ? 0.21028 0.37126 0.16247 0.01638  0.00114  0.01394  39  SER A CA  
191  C C   . SER A 32  ? 0.25212 0.40155 0.21749 0.00896  0.00549  0.00435  39  SER A C   
192  O O   . SER A 32  ? 0.27630 0.41978 0.25000 0.00591  0.01378  0.01106  39  SER A O   
193  C CB  . SER A 32  ? 0.28578 0.46580 0.21759 0.02302  0.00575  0.01940  39  SER A CB  
194  O OG  . SER A 32  ? 0.28849 0.48310 0.20534 0.03654  0.00382  0.03347  39  SER A OG  
195  N N   . ASN A 33  ? 0.25466 0.40188 0.21987 0.00654  0.00230  -0.01132 40  ASN A N   
196  C CA  . ASN A 33  ? 0.21508 0.35598 0.18575 0.00811  0.00821  -0.01833 40  ASN A CA  
197  C C   . ASN A 33  ? 0.26361 0.39494 0.25279 0.00774  0.00601  -0.01794 40  ASN A C   
198  O O   . ASN A 33  ? 0.23871 0.35850 0.22771 0.01190  0.00567  -0.02619 40  ASN A O   
199  C CB  . ASN A 33  ? 0.26233 0.39458 0.21563 0.00935  0.01094  -0.03364 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.26790 0.39209 0.21943 0.01934  0.01992  -0.03824 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.31861 0.46088 0.27902 0.02466  0.02437  -0.03170 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.35263 0.45042 0.29020 0.02291  0.02500  -0.04941 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.18958 0.22578 0.12450 0.01725  -0.01215 -0.03420 41  LYS A N   
204  C CA  . LYS A 34  ? 0.19281 0.24832 0.15526 0.01954  -0.00410 -0.03187 41  LYS A CA  
205  C C   . LYS A 34  ? 0.20576 0.24854 0.16986 0.02011  0.00519  -0.03753 41  LYS A C   
206  O O   . LYS A 34  ? 0.20415 0.25425 0.18324 0.01993  0.00713  -0.03756 41  LYS A O   
207  C CB  . LYS A 34  ? 0.24804 0.30742 0.21307 0.03167  -0.00022 -0.02783 41  LYS A CB  
208  C CG  . LYS A 34  ? 0.22408 0.30604 0.19204 0.03939  -0.00593 -0.01864 41  LYS A CG  
209  C CD  . LYS A 34  ? 0.29793 0.36420 0.25175 0.05834  -0.00500 -0.01779 41  LYS A CD  
210  C CE  . LYS A 34  ? 0.20867 0.30158 0.16220 0.07637  -0.00689 -0.00621 41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.24137 0.37381 0.20772 0.09536  -0.00003 0.00626  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.21761 0.24591 0.16470 0.02551  0.01228  -0.03865 42  GLU A N   
213  C CA  . GLU A 35  ? 0.23375 0.26422 0.19069 0.02918  0.02317  -0.03502 42  GLU A CA  
214  C C   . GLU A 35  ? 0.26402 0.28611 0.22216 0.02509  0.02044  -0.04314 42  GLU A C   
215  O O   . GLU A 35  ? 0.27092 0.29921 0.24484 0.02560  0.02693  -0.03944 42  GLU A O   
216  C CB  . GLU A 35  ? 0.25126 0.28278 0.18848 0.04607  0.03655  -0.02593 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.27566 0.27250 0.16177 0.06199  0.03401  -0.03850 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.39902 0.39561 0.25402 0.09074  0.04946  -0.02665 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.41272 0.43260 0.27363 0.09514  0.05755  -0.01265 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.53200 0.50634 0.36159 0.10809  0.05046  -0.02673 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.24120 0.24948 0.18526 0.01734  0.00643  -0.04944 43  ILE A N   
222  C CA  . ILE A 36  ? 0.20570 0.20201 0.14943 0.00958  -0.00115 -0.05278 43  ILE A CA  
223  C C   . ILE A 36  ? 0.18801 0.21226 0.16702 0.00414  0.00422  -0.04793 43  ILE A C   
224  O O   . ILE A 36  ? 0.20618 0.22524 0.18921 -0.00081 0.00189  -0.04868 43  ILE A O   
225  C CB  . ILE A 36  ? 0.28468 0.25987 0.21049 -0.00704 -0.02828 -0.05059 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.24668 0.26568 0.20666 -0.01997 -0.03547 -0.03458 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.36749 0.28916 0.23396 0.00373  -0.04059 -0.06010 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.25644 0.31525 0.25453 -0.03208 -0.03867 -0.01698 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.16329 0.20821 0.15744 0.00909  0.00916  -0.04337 44  PHE A N   
230  C CA  . PHE A 37  ? 0.19804 0.25346 0.20411 0.01450  0.01259  -0.04104 44  PHE A CA  
231  C C   . PHE A 37  ? 0.20312 0.24295 0.21149 0.01325  0.01591  -0.04510 44  PHE A C   
232  O O   . PHE A 37  ? 0.15760 0.19952 0.17089 0.01336  0.01599  -0.04506 44  PHE A O   
233  C CB  . PHE A 37  ? 0.19085 0.24441 0.18800 0.02936  0.01254  -0.03924 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.19000 0.21492 0.17917 0.02802  0.00786  -0.04086 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.21787 0.24167 0.20745 0.02313  0.00767  -0.03632 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.23622 0.23649 0.21837 0.02887  -0.00047 -0.04114 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.21523 0.22515 0.20848 0.01608  0.00006  -0.02536 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.22619 0.20322 0.20884 0.01812  -0.01436 -0.03208 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.17447 0.16208 0.16780 0.01018  -0.01365 -0.02082 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.16813 0.20034 0.17638 0.01323  0.01917  -0.04277 45  LEU A N   
241  C CA  . LEU A 38  ? 0.14758 0.17855 0.16788 0.01127  0.02076  -0.03679 45  LEU A CA  
242  C C   . LEU A 38  ? 0.17727 0.20586 0.19423 0.01348  0.02621  -0.04169 45  LEU A C   
243  O O   . LEU A 38  ? 0.17646 0.20420 0.20312 0.01092  0.02494  -0.04069 45  LEU A O   
244  C CB  . LEU A 38  ? 0.13836 0.18173 0.17015 0.01126  0.02388  -0.01920 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.14990 0.20601 0.20719 0.00437  0.02021  0.00021  45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.15823 0.18510 0.21232 -0.00781 -0.00240 -0.00284 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.18969 0.27820 0.27034 0.00230  0.02322  0.03217  45  LEU A CD2 
248  N N   . ARG A 39  ? 0.19042 0.20675 0.18449 0.01922  0.02748  -0.04754 46  ARG A N   
249  C CA  . ARG A 39  ? 0.22206 0.21461 0.19616 0.02255  0.02394  -0.05404 46  ARG A CA  
250  C C   . ARG A 39  ? 0.22901 0.22406 0.21744 0.00630  0.01355  -0.05484 46  ARG A C   
251  O O   . ARG A 39  ? 0.23706 0.22366 0.22657 0.00609  0.01306  -0.05544 46  ARG A O   
252  C CB  . ARG A 39  ? 0.28147 0.23646 0.20950 0.03006  0.01409  -0.06180 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.31780 0.22330 0.20873 0.02936  -0.00364 -0.06956 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.38629 0.24075 0.22544 0.03093  -0.02581 -0.07368 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.48469 0.34032 0.33405 0.00022  -0.05160 -0.06981 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.46422 0.29223 0.28606 -0.00545 -0.07228 -0.06677 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.51171 0.29817 0.28417 0.02093  -0.07074 -0.07119 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.48407 0.33334 0.33252 -0.03682 -0.09555 -0.05274 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.16499 0.17879 0.16569 -0.00381 0.00716  -0.05000 47  GLU A N   
260  C CA  . GLU A 40  ? 0.15547 0.18840 0.17304 -0.01410 0.00117  -0.04016 47  GLU A CA  
261  C C   . GLU A 40  ? 0.18051 0.22339 0.20861 -0.00516 0.01126  -0.04057 47  GLU A C   
262  O O   . GLU A 40  ? 0.16390 0.20946 0.19778 -0.00968 0.00936  -0.03590 47  GLU A O   
263  C CB  . GLU A 40  ? 0.12568 0.19354 0.15762 -0.01809 -0.00299 -0.02526 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.24039 0.29571 0.26236 -0.03399 -0.02266 -0.01998 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.33988 0.35327 0.34186 -0.05286 -0.04727 -0.01887 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.31287 0.33609 0.33043 -0.06309 -0.05187 -0.00765 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.42307 0.38483 0.38443 -0.05467 -0.06470 -0.02917 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.15514 0.19515 0.18020 0.00583  0.01648  -0.04461 48  LEU A N   
269  C CA  . LEU A 41  ? 0.17352 0.20430 0.19424 0.01341  0.01570  -0.04544 48  LEU A CA  
270  C C   . LEU A 41  ? 0.18388 0.20311 0.21295 0.00674  0.01463  -0.04639 48  LEU A C   
271  O O   . LEU A 41  ? 0.18242 0.19617 0.21006 0.00796  0.01197  -0.04577 48  LEU A O   
272  C CB  . LEU A 41  ? 0.14791 0.15873 0.15149 0.02291  0.00874  -0.04732 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.19680 0.21580 0.18347 0.04008  0.01126  -0.04578 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.19973 0.17849 0.15759 0.04900  -0.00264 -0.04957 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.19673 0.23627 0.17253 0.06044  0.01913  -0.03836 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.12112 0.14040 0.15644 0.00496  0.01837  -0.04459 49  ILE A N   
277  C CA  . ILE A 42  ? 0.16938 0.18943 0.21416 0.00672  0.02150  -0.03904 49  ILE A CA  
278  C C   . ILE A 42  ? 0.20831 0.21635 0.24278 0.00687  0.02156  -0.04544 49  ILE A C   
279  O O   . ILE A 42  ? 0.19160 0.19749 0.23230 0.00704  0.02068  -0.04285 49  ILE A O   
280  C CB  . ILE A 42  ? 0.16065 0.19452 0.20976 0.01678  0.03136  -0.02821 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.12834 0.17890 0.19940 0.00807  0.02453  -0.01054 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.19404 0.23463 0.24474 0.03148  0.04076  -0.01981 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.18706 0.26785 0.26864 0.01881  0.03716  0.00995  49  ILE A CD1 
284  N N   . SER A 43  ? 0.17746 0.17402 0.19574 0.00289  0.01675  -0.05055 50  SER A N   
285  C CA  . SER A 43  ? 0.21761 0.19336 0.22368 -0.00452 0.00628  -0.05105 50  SER A CA  
286  C C   . SER A 43  ? 0.20801 0.20511 0.23363 -0.01406 0.00453  -0.04269 50  SER A C   
287  O O   . SER A 43  ? 0.19589 0.18237 0.22058 -0.01717 0.00056  -0.04039 50  SER A O   
288  C CB  . SER A 43  ? 0.29905 0.25160 0.28265 -0.01453 -0.01031 -0.05129 50  SER A CB  
289  O OG  . SER A 43  ? 0.35706 0.29743 0.33993 -0.03447 -0.03045 -0.04119 50  SER A OG  
290  N N   . ASN A 44  ? 0.14760 0.17334 0.18425 -0.01234 0.00889  -0.03679 51  ASN A N   
291  C CA  . ASN A 44  ? 0.19572 0.24219 0.23790 -0.00697 0.01260  -0.02736 51  ASN A CA  
292  C C   . ASN A 44  ? 0.23923 0.26657 0.27537 -0.00013 0.01336  -0.03477 51  ASN A C   
293  O O   . ASN A 44  ? 0.14688 0.17725 0.18301 0.00011  0.01291  -0.02883 51  ASN A O   
294  C CB  . ASN A 44  ? 0.18665 0.25558 0.22279 0.00972  0.01959  -0.02228 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.28105 0.39033 0.33405 0.00361  0.01928  -0.00222 51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.18938 0.30497 0.25847 -0.01982 0.00710  0.01047  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.21059 0.34375 0.25697 0.02454  0.02795  0.00447  51  ASN A ND2 
298  N N   . SER A 45  ? 0.13937 0.15114 0.17364 0.00300  0.01164  -0.04203 52  SER A N   
299  C CA  . SER A 45  ? 0.16928 0.16680 0.20454 0.00332  0.00484  -0.04112 52  SER A CA  
300  C C   . SER A 45  ? 0.16558 0.16335 0.21220 -0.00035 0.00746  -0.03866 52  SER A C   
301  O O   . SER A 45  ? 0.17658 0.16852 0.22279 -0.00054 0.00289  -0.03605 52  SER A O   
302  C CB  . SER A 45  ? 0.15575 0.14737 0.19822 -0.00027 -0.00342 -0.03647 52  SER A CB  
303  O OG  . SER A 45  ? 0.18351 0.15473 0.20213 0.00479  -0.01412 -0.03991 52  SER A OG  
304  N N   . SER A 46  ? 0.17319 0.16914 0.21953 0.00150  0.01308  -0.04023 53  SER A N   
305  C CA  . SER A 46  ? 0.22679 0.20839 0.26680 0.00729  0.01384  -0.03966 53  SER A CA  
306  C C   . SER A 46  ? 0.23852 0.20814 0.27150 -0.00298 0.00561  -0.03929 53  SER A C   
307  O O   . SER A 46  ? 0.20035 0.16125 0.23340 -0.00077 0.00347  -0.03665 53  SER A O   
308  C CB  . SER A 46  ? 0.18951 0.15131 0.20516 0.02095  0.01751  -0.04425 53  SER A CB  
309  O OG  . SER A 46  ? 0.27123 0.20300 0.26228 0.03600  0.01584  -0.04570 53  SER A OG  
310  N N   . ASP A 47  ? 0.20154 0.17830 0.23332 -0.01494 0.00031  -0.03552 54  ASP A N   
311  C CA  . ASP A 47  ? 0.20619 0.18918 0.24224 -0.02793 -0.00795 -0.02223 54  ASP A CA  
312  C C   . ASP A 47  ? 0.23660 0.23764 0.27916 -0.02011 -0.00071 -0.01768 54  ASP A C   
313  O O   . ASP A 47  ? 0.19665 0.19322 0.23966 -0.02511 -0.00538 -0.00961 54  ASP A O   
314  C CB  . ASP A 47  ? 0.17690 0.18814 0.22404 -0.04152 -0.01355 -0.00552 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.28381 0.26229 0.31605 -0.05707 -0.03371 -0.00578 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.29597 0.22047 0.29648 -0.05047 -0.04204 -0.02145 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.28437 0.28883 0.33097 -0.07253 -0.04325 0.01241  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.17792 0.18878 0.21622 -0.00676 0.00622  -0.02277 55  ALA A N   
319  C CA  . ALA A 48  ? 0.19443 0.20342 0.21851 0.00570  0.00646  -0.02082 55  ALA A CA  
320  C C   . ALA A 48  ? 0.19909 0.18518 0.22543 0.00289  -0.00155 -0.02583 55  ALA A C   
321  O O   . ALA A 48  ? 0.17882 0.15884 0.19530 0.00688  -0.00502 -0.02178 55  ALA A O   
322  C CB  . ALA A 48  ? 0.17251 0.17348 0.17107 0.02396  0.00627  -0.02662 55  ALA A CB  
323  N N   . LEU A 49  ? 0.12967 0.11008 0.17028 -0.00111 -0.00342 -0.02959 56  LEU A N   
324  C CA  . LEU A 49  ? 0.15395 0.12997 0.20713 -0.00139 -0.00858 -0.02444 56  LEU A CA  
325  C C   . LEU A 49  ? 0.19376 0.16221 0.24532 -0.00058 -0.00567 -0.02302 56  LEU A C   
326  O O   . LEU A 49  ? 0.17209 0.13625 0.22644 0.00062  -0.01068 -0.01781 56  LEU A O   
327  C CB  . LEU A 49  ? 0.16270 0.15305 0.23629 0.00064  -0.00616 -0.01757 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.14105 0.13137 0.21887 -0.00724 -0.01968 -0.01185 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.15271 0.16706 0.25077 -0.00597 -0.01192 -0.00220 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.13304 0.11632 0.21991 -0.01693 -0.04242 0.00296  56  LEU A CD2 
331  N N   . ASP A 50  ? 0.19463 0.15242 0.23618 -0.00276 -0.00351 -0.02642 57  ASP A N   
332  C CA  . ASP A 50  ? 0.22376 0.15531 0.25144 -0.00548 -0.01106 -0.02400 57  ASP A CA  
333  C C   . ASP A 50  ? 0.22745 0.16858 0.25955 -0.01543 -0.01550 -0.01370 57  ASP A C   
334  O O   . ASP A 50  ? 0.22001 0.14426 0.24706 -0.01495 -0.02136 -0.00973 57  ASP A O   
335  C CB  . ASP A 50  ? 0.22589 0.13030 0.23315 -0.01456 -0.02174 -0.02555 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.29294 0.16969 0.27504 0.00476  -0.01899 -0.03688 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.30462 0.19648 0.29349 0.02710  -0.00435 -0.03740 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.38168 0.22301 0.33541 -0.00159 -0.03357 -0.04049 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.16004 0.12955 0.19681 -0.01856 -0.01091 -0.00699 58  LYS A N   
340  C CA  . LYS A 51  ? 0.20406 0.19212 0.23964 -0.01987 -0.01024 0.00929  58  LYS A CA  
341  C C   . LYS A 51  ? 0.20711 0.18380 0.23187 -0.00806 -0.01123 0.00466  58  LYS A C   
342  O O   . LYS A 51  ? 0.24702 0.22175 0.26937 -0.01055 -0.01456 0.01509  58  LYS A O   
343  C CB  . LYS A 51  ? 0.18280 0.20995 0.21759 -0.01167 0.00026  0.02168  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.20856 0.26082 0.26312 -0.02952 -0.00339 0.03951  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.21502 0.32023 0.27238 -0.01263 0.01193  0.05784  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.30340 0.43340 0.38379 -0.03001 0.00615  0.07187  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.38917 0.58963 0.48096 -0.01102 0.02304  0.10357  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.20405 0.17020 0.22097 0.00162  -0.01365 -0.00721 59  ILE A N   
349  C CA  . ILE A 52  ? 0.23225 0.17979 0.23645 0.00721  -0.02482 -0.00790 59  ILE A CA  
350  C C   . ILE A 52  ? 0.24161 0.18422 0.26825 0.00050  -0.02962 -0.00481 59  ILE A C   
351  O O   . ILE A 52  ? 0.25420 0.18791 0.27579 0.00168  -0.03730 0.00053  59  ILE A O   
352  C CB  . ILE A 52  ? 0.26217 0.18807 0.24707 0.01272  -0.03897 -0.01510 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.32244 0.21595 0.28082 0.01611  -0.06084 -0.01314 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.22000 0.15420 0.23705 0.00125  -0.04280 -0.01453 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.36407 0.24924 0.28071 0.03562  -0.05501 -0.01117 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.20374 0.15095 0.24860 -0.00027 -0.02401 -0.00667 60  ARG A N   
357  C CA  . ARG A 53  ? 0.20634 0.14908 0.26157 0.00686  -0.02413 -0.00116 60  ARG A CA  
358  C C   . ARG A 53  ? 0.24651 0.16725 0.28601 0.00463  -0.02739 0.00072  60  ARG A C   
359  O O   . ARG A 53  ? 0.26556 0.17988 0.30653 0.00978  -0.03227 0.00706  60  ARG A O   
360  C CB  . ARG A 53  ? 0.23093 0.17674 0.29019 0.01969  -0.01420 -0.00276 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.31384 0.25612 0.37277 0.04183  -0.01021 0.00604  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.49169 0.43323 0.53776 0.06956  0.00340  0.00655  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.55969 0.55865 0.64545 0.08144  0.01354  0.02974  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.48718 0.50940 0.57647 0.09733  0.02728  0.03643  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.50662 0.49071 0.55503 0.10506  0.03144  0.01599  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.35640 0.44424 0.49287 0.10387  0.03412  0.06966  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.23935 0.15015 0.26669 -0.00628 -0.02870 0.00055  61  TYR A N   
368  C CA  . TYR A 54  ? 0.25993 0.14836 0.27534 -0.01633 -0.03955 0.01053  61  TYR A CA  
369  C C   . TYR A 54  ? 0.28810 0.19437 0.30697 -0.01849 -0.03942 0.02189  61  TYR A C   
370  O O   . TYR A 54  ? 0.31664 0.20428 0.32933 -0.01959 -0.04754 0.02896  61  TYR A O   
371  C CB  . TYR A 54  ? 0.26716 0.15136 0.27862 -0.03660 -0.04883 0.02026  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.37971 0.23683 0.38157 -0.05540 -0.06955 0.03905  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.36245 0.15066 0.33028 -0.05238 -0.08989 0.03204  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.32876 0.22675 0.34956 -0.07183 -0.06988 0.06746  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.37976 0.14382 0.33436 -0.06933 -0.11265 0.04842  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.35393 0.23217 0.37229 -0.09450 -0.09251 0.09273  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.41919 0.22821 0.40399 -0.09476 -0.11618 0.08000  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.53657 0.33300 0.51394 -0.11188 -0.14022 0.09875  61  TYR A OH  
379  N N   . GLU A 55  ? 0.24516 0.17973 0.26356 -0.01402 -0.03143 0.02335  62  GLU A N   
380  C CA  . GLU A 55  ? 0.30679 0.24928 0.31090 -0.00663 -0.03134 0.03300  62  GLU A CA  
381  C C   . GLU A 55  ? 0.39820 0.31945 0.39938 -0.00044 -0.04156 0.02633  62  GLU A C   
382  O O   . GLU A 55  ? 0.36987 0.28457 0.36168 0.00102  -0.04661 0.03528  62  GLU A O   
383  C CB  . GLU A 55  ? 0.32731 0.28731 0.30939 0.00983  -0.02261 0.03268  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.36895 0.36953 0.35895 0.00881  -0.00941 0.05125  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.49293 0.51448 0.44709 0.04067  0.00411  0.05953  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.52495 0.50809 0.43742 0.06156  -0.00304 0.04002  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.45687 0.53123 0.42015 0.04718  0.01909  0.08939  62  GLU A OE2 
388  N N   . SER A 56  ? 0.30367 0.22094 0.31764 0.00175  -0.04604 0.01685  63  SER A N   
389  C CA  . SER A 56  ? 0.28567 0.19726 0.30950 0.00380  -0.05935 0.02134  63  SER A CA  
390  C C   . SER A 56  ? 0.32665 0.23450 0.36368 0.00803  -0.05772 0.02831  63  SER A C   
391  O O   . SER A 56  ? 0.31561 0.22578 0.36274 0.01137  -0.06783 0.03798  63  SER A O   
392  C CB  . SER A 56  ? 0.27803 0.20190 0.32372 0.00139  -0.06613 0.02268  63  SER A CB  
393  O OG  . SER A 56  ? 0.29961 0.24156 0.36984 0.00790  -0.05204 0.02471  63  SER A OG  
394  N N   . LEU A 57  ? 0.26217 0.15668 0.29295 0.00910  -0.05005 0.02509  64  LEU A N   
395  C CA  . LEU A 57  ? 0.35552 0.22559 0.37904 0.02029  -0.05312 0.02909  64  LEU A CA  
396  C C   . LEU A 57  ? 0.37786 0.23591 0.39220 0.01444  -0.06271 0.03855  64  LEU A C   
397  O O   . LEU A 57  ? 0.42924 0.27502 0.44266 0.02740  -0.06725 0.04438  64  LEU A O   
398  C CB  . LEU A 57  ? 0.38801 0.22023 0.38633 0.02067  -0.05501 0.02234  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.39256 0.22583 0.38807 0.03584  -0.04533 0.01259  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.43552 0.20663 0.38615 0.03917  -0.05743 0.00476  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.41455 0.27491 0.42722 0.06543  -0.03386 0.01997  64  LEU A CD2 
402  N N   . THR A 58  ? 0.37698 0.24290 0.38292 -0.00001 -0.06374 0.04392  65  THR A N   
403  C CA  . THR A 58  ? 0.44602 0.30669 0.44114 -0.00344 -0.07052 0.05697  65  THR A CA  
404  C C   . THR A 58  ? 0.44899 0.32398 0.43302 0.00292  -0.07213 0.05782  65  THR A C   
405  O O   . THR A 58  ? 0.60077 0.46966 0.57028 0.00507  -0.07800 0.06798  65  THR A O   
406  C CB  . THR A 58  ? 0.54591 0.40759 0.53458 -0.02074 -0.07213 0.07437  65  THR A CB  
407  O OG1 . THR A 58  ? 0.57536 0.47443 0.56632 -0.02253 -0.05984 0.07954  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.46104 0.28309 0.44424 -0.03114 -0.08471 0.07363  65  THR A CG2 
409  N N   . ASP A 59  ? 0.55197 0.39824 0.38572 0.14493  -0.01000 0.07926  66  ASP A N   
410  C CA  . ASP A 59  ? 0.52070 0.40555 0.35959 0.14538  -0.02416 0.07873  66  ASP A CA  
411  C C   . ASP A 59  ? 0.41414 0.33554 0.28092 0.14328  -0.03546 0.06881  66  ASP A C   
412  O O   . ASP A 59  ? 0.41726 0.34617 0.29507 0.12690  -0.03757 0.05473  66  ASP A O   
413  C CB  . ASP A 59  ? 0.49188 0.37386 0.31981 0.12847  -0.02289 0.07322  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.63105 0.54201 0.45289 0.13018  -0.03583 0.07075  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.59578 0.53027 0.42351 0.13966  -0.04842 0.07325  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.63898 0.54931 0.45012 0.12071  -0.03298 0.06631  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.53407 0.48276 0.41889 0.15423  -0.04110 0.07546  67  PRO A N   
418  C CA  . PRO A 60  ? 0.42389 0.40876 0.33877 0.15041  -0.05120 0.06980  67  PRO A CA  
419  C C   . PRO A 60  ? 0.47415 0.48289 0.39078 0.13628  -0.06911 0.05992  67  PRO A C   
420  O O   . PRO A 60  ? 0.37218 0.39965 0.30908 0.12710  -0.07588 0.05128  67  PRO A O   
421  C CB  . PRO A 60  ? 0.53086 0.54142 0.46445 0.16256  -0.05274 0.08326  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.56487 0.54049 0.47722 0.17598  -0.03686 0.09241  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.49199 0.43989 0.37460 0.16851  -0.03622 0.08942  67  PRO A CD  
424  N N   . SER A 61  ? 0.44006 0.44471 0.33305 0.13332  -0.07558 0.06008  68  SER A N   
425  C CA  . SER A 61  ? 0.42562 0.44243 0.31145 0.11935  -0.09043 0.04815  68  SER A CA  
426  C C   . SER A 61  ? 0.49487 0.49670 0.37908 0.10670  -0.08407 0.03285  68  SER A C   
427  O O   . SER A 61  ? 0.36604 0.37425 0.24661 0.09554  -0.09465 0.02125  68  SER A O   
428  C CB  . SER A 61  ? 0.41822 0.42682 0.27303 0.12048  -0.09396 0.05111  68  SER A CB  
429  O OG  . SER A 61  ? 0.45649 0.43559 0.28684 0.12454  -0.07837 0.05265  68  SER A OG  
430  N N   . LYS A 62  ? 0.32204 0.30217 0.20936 0.10532  -0.06642 0.03243  69  LYS A N   
431  C CA  . LYS A 62  ? 0.34125 0.31341 0.23453 0.09103  -0.05980 0.01987  69  LYS A CA  
432  C C   . LYS A 62  ? 0.37633 0.36713 0.29533 0.08334  -0.06705 0.01103  69  LYS A C   
433  O O   . LYS A 62  ? 0.33126 0.31947 0.25420 0.07209  -0.06518 0.00040  69  LYS A O   
434  C CB  . LYS A 62  ? 0.42708 0.37424 0.31906 0.08845  -0.04331 0.02315  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.52822 0.45603 0.39680 0.09171  -0.03497 0.03349  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.47779 0.39884 0.34316 0.07862  -0.02610 0.03083  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.39206 0.29782 0.23771 0.08048  -0.01653 0.04463  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.63815 0.54984 0.48469 0.06998  -0.00820 0.04559  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.35116 0.36287 0.28933 0.09010  -0.07415 0.01761  70  LEU A N   
440  C CA  . LEU A 63  ? 0.26774 0.30185 0.23311 0.08239  -0.08096 0.01288  70  LEU A CA  
441  C C   . LEU A 63  ? 0.33965 0.39848 0.30897 0.07509  -0.10245 0.01198  70  LEU A C   
442  O O   . LEU A 63  ? 0.27645 0.35905 0.27194 0.06754  -0.11063 0.01229  70  LEU A O   
443  C CB  . LEU A 63  ? 0.33884 0.38366 0.32646 0.09436  -0.07267 0.02313  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.31680 0.32967 0.29544 0.09877  -0.05330 0.02148  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.35513 0.37494 0.34946 0.11417  -0.04390 0.03087  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.30988 0.31037 0.28760 0.08201  -0.04965 0.00747  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.29027 0.34242 0.23182 0.07589  -0.11236 0.01151  71  ASP A N   
448  C CA  . ASP A 64  ? 0.31604 0.38161 0.25550 0.06128  -0.12969 0.00908  71  ASP A CA  
449  C C   . ASP A 64  ? 0.38832 0.44426 0.32803 0.04411  -0.13224 -0.00580 71  ASP A C   
450  O O   . ASP A 64  ? 0.37741 0.44728 0.32578 0.02876  -0.14422 -0.00659 71  ASP A O   
451  C CB  . ASP A 64  ? 0.33822 0.38935 0.24124 0.06403  -0.13402 0.00954  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.52523 0.59051 0.43070 0.07739  -0.13540 0.02696  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.43706 0.52200 0.37254 0.08573  -0.13190 0.03891  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.48586 0.54053 0.36205 0.08093  -0.13813 0.02929  71  ASP A OD2 
455  N N   . SER A 65  ? 0.31510 0.34800 0.24501 0.04620  -0.12038 -0.01590 72  SER A N   
456  C CA  . SER A 65  ? 0.33558 0.35636 0.26649 0.03332  -0.11858 -0.02811 72  SER A CA  
457  C C   . SER A 65  ? 0.42739 0.46637 0.39507 0.02705  -0.11700 -0.02641 72  SER A C   
458  O O   . SER A 65  ? 0.37670 0.40561 0.34738 0.01728  -0.11346 -0.03449 72  SER A O   
459  C CB  . SER A 65  ? 0.38234 0.37730 0.29064 0.03968  -0.10487 -0.03570 72  SER A CB  
460  O OG  . SER A 65  ? 0.31442 0.31101 0.23383 0.04788  -0.08876 -0.02739 72  SER A OG  
461  N N   . GLY A 66  ? 0.32431 0.38875 0.31856 0.03489  -0.11711 -0.01452 73  GLY A N   
462  C CA  . GLY A 66  ? 0.31976 0.40351 0.34823 0.03196  -0.11258 -0.01041 73  GLY A CA  
463  C C   . GLY A 66  ? 0.24324 0.33377 0.28545 0.04837  -0.09667 0.00046  73  GLY A C   
464  O O   . GLY A 66  ? 0.22946 0.29461 0.25595 0.05495  -0.08167 -0.00294 73  GLY A O   
465  N N   . LYS A 67  ? 0.20485 0.32841 0.27516 0.05511  -0.09959 0.01472  74  LYS A N   
466  C CA  . LYS A 67  ? 0.20892 0.33364 0.28679 0.07516  -0.08235 0.02575  74  LYS A CA  
467  C C   . LYS A 67  ? 0.25107 0.36791 0.33861 0.07592  -0.06601 0.02254  74  LYS A C   
468  O O   . LYS A 67  ? 0.30993 0.40626 0.38626 0.09080  -0.04910 0.02497  74  LYS A O   
469  C CB  . LYS A 67  ? 0.18420 0.34442 0.28704 0.08415  -0.08739 0.04445  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.51441 0.68070 0.60702 0.07955  -0.10517 0.04809  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.49222 0.66758 0.58905 0.09852  -0.09874 0.06369  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.77106 0.94837 0.85194 0.09599  -0.11571 0.06713  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.79095 0.96806 0.86311 0.07295  -0.13822 0.05589  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.22238 0.35026 0.32568 0.06031  -0.07075 0.01719  75  GLU A N   
475  C CA  . GLU A 68  ? 0.16937 0.29365 0.28175 0.06200  -0.05580 0.01637  75  GLU A CA  
476  C C   . GLU A 68  ? 0.20084 0.28431 0.28463 0.05794  -0.04624 0.00185  75  GLU A C   
477  O O   . GLU A 68  ? 0.25519 0.32431 0.32519 0.04568  -0.05357 -0.00868 75  GLU A O   
478  C CB  . GLU A 68  ? 0.26138 0.41225 0.40141 0.04609  -0.06416 0.01834  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.30577 0.49843 0.47735 0.04684  -0.07029 0.03435  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.66367 0.86470 0.83011 0.03873  -0.08953 0.03391  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.72011 0.94215 0.89891 0.04763  -0.09056 0.04642  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.67906 0.86408 0.82508 0.02395  -0.10174 0.02171  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.19485 0.25995 0.26846 0.06861  -0.03000 0.00241  76  LEU A N   
484  C CA  . LEU A 69  ? 0.17173 0.20058 0.21897 0.06300  -0.02269 -0.00886 76  LEU A CA  
485  C C   . LEU A 69  ? 0.17819 0.20785 0.23105 0.06057  -0.01450 -0.01065 76  LEU A C   
486  O O   . LEU A 69  ? 0.18659 0.21152 0.23578 0.07456  -0.00170 -0.00501 76  LEU A O   
487  C CB  . LEU A 69  ? 0.23175 0.22846 0.25213 0.07523  -0.01313 -0.00735 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.36569 0.35792 0.37685 0.07911  -0.01911 -0.00363 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.46525 0.41636 0.44587 0.08758  -0.00868 -0.00267 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.24060 0.23575 0.24929 0.06331  -0.03040 -0.01094 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.16927 0.20301 0.22810 0.04530  -0.02040 -0.01746 77  HIS A N   
492  C CA  . HIS A 70  ? 0.15611 0.19451 0.22218 0.04279  -0.01369 -0.01707 77  HIS A CA  
493  C C   . HIS A 70  ? 0.13383 0.16125 0.19238 0.02842  -0.01793 -0.02606 77  HIS A C   
494  O O   . HIS A 70  ? 0.14866 0.16959 0.20062 0.02111  -0.02553 -0.03152 77  HIS A O   
495  C CB  . HIS A 70  ? 0.16523 0.23978 0.26450 0.04228  -0.01633 -0.00666 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.18382 0.27242 0.29734 0.02717  -0.03294 -0.00875 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.26871 0.38341 0.40171 0.02601  -0.04396 -0.00054 77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.22978 0.30648 0.33670 0.01333  -0.04059 -0.01788 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.22170 0.33461 0.35471 0.01006  -0.05894 -0.00665 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.22549 0.31371 0.34200 0.00394  -0.05557 -0.01724 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.14534 0.17272 0.20494 0.02674  -0.01154 -0.02552 78  ILE A N   
502  C CA  . ILE A 71  ? 0.13495 0.15606 0.18998 0.01592  -0.01416 -0.03062 78  ILE A CA  
503  C C   . ILE A 71  ? 0.18010 0.21885 0.25560 0.01222  -0.01301 -0.02513 78  ILE A C   
504  O O   . ILE A 71  ? 0.12982 0.17783 0.21202 0.01932  -0.00381 -0.01788 78  ILE A O   
505  C CB  . ILE A 71  ? 0.16768 0.16641 0.19691 0.01587  -0.00857 -0.03439 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.16957 0.14731 0.17798 0.01658  -0.00992 -0.03805 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.16003 0.15981 0.18881 0.00575  -0.01261 -0.03639 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.19462 0.14492 0.17301 0.01255  -0.00755 -0.04186 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.13046 0.17127 0.21364 0.00220  -0.02076 -0.02743 79  ASN A N   
510  C CA  . ASN A 72  ? 0.16038 0.21117 0.26002 -0.00421 -0.02043 -0.02192 79  ASN A CA  
511  C C   . ASN A 72  ? 0.18091 0.21872 0.26949 -0.00774 -0.01859 -0.02449 79  ASN A C   
512  O O   . ASN A 72  ? 0.15049 0.17686 0.22692 -0.00881 -0.02252 -0.03030 79  ASN A O   
513  C CB  . ASN A 72  ? 0.13384 0.19214 0.24903 -0.01408 -0.03219 -0.02106 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.15160 0.23154 0.28354 -0.01189 -0.03634 -0.01458 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.14495 0.24027 0.28570 -0.00163 -0.02670 -0.00633 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.16690 0.24764 0.30102 -0.02008 -0.05053 -0.01729 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.13180 0.17442 0.22575 -0.00803 -0.01163 -0.01775 80  LEU A N   
518  C CA  . LEU A 73  ? 0.09536 0.12894 0.18114 -0.01029 -0.00986 -0.01688 80  LEU A CA  
519  C C   . LEU A 73  ? 0.11765 0.15268 0.21944 -0.01814 -0.01139 -0.01077 80  LEU A C   
520  O O   . LEU A 73  ? 0.09801 0.14704 0.21634 -0.02048 -0.00676 -0.00159 80  LEU A O   
521  C CB  . LEU A 73  ? 0.11303 0.14551 0.18466 -0.00446 -0.00088 -0.01349 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.18607 0.20910 0.23617 0.00092  0.00034  -0.01944 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.13347 0.14813 0.16167 0.00578  0.00827  -0.01709 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.15643 0.17183 0.19684 -0.00368 -0.00838 -0.02580 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.13531 0.15458 0.23132 -0.02181 -0.01687 -0.01443 81  ILE A N   
526  C CA  . ILE A 74  ? 0.13381 0.14265 0.23798 -0.03140 -0.02064 -0.01091 81  ILE A CA  
527  C C   . ILE A 74  ? 0.18101 0.17366 0.27434 -0.02804 -0.01572 -0.00735 81  ILE A C   
528  O O   . ILE A 74  ? 0.17023 0.14643 0.24862 -0.02224 -0.01719 -0.01234 81  ILE A O   
529  C CB  . ILE A 74  ? 0.14854 0.14302 0.24779 -0.03764 -0.03219 -0.01930 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.17324 0.18659 0.28114 -0.03776 -0.03744 -0.02169 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.16217 0.14051 0.26639 -0.05204 -0.03868 -0.01599 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.24597 0.24579 0.34423 -0.04342 -0.05024 -0.02996 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.17235 0.17014 0.27234 -0.02934 -0.00854 0.00316  82  PRO A N   
534  C CA  . PRO A 75  ? 0.18922 0.17037 0.27937 -0.02579 -0.00423 0.00896  82  PRO A CA  
535  C C   . PRO A 75  ? 0.21685 0.17197 0.30845 -0.03613 -0.00795 0.01108  82  PRO A C   
536  O O   . PRO A 75  ? 0.22862 0.18702 0.33557 -0.05037 -0.01284 0.01361  82  PRO A O   
537  C CB  . PRO A 75  ? 0.18295 0.18016 0.27637 -0.02285 0.00525  0.02004  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.18532 0.20225 0.29734 -0.02905 0.00722  0.02348  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.17058 0.19063 0.28704 -0.03188 -0.00212 0.01256  82  PRO A CD  
540  N N   . ASN A 76  ? 0.21204 0.14008 0.28638 -0.02899 -0.00603 0.01112  83  ASN A N   
541  C CA  . ASN A 76  ? 0.22733 0.11714 0.29277 -0.03727 -0.00858 0.01232  83  ASN A CA  
542  C C   . ASN A 76  ? 0.29697 0.16957 0.35053 -0.02562 0.00107  0.02262  83  ASN A C   
543  O O   . ASN A 76  ? 0.29656 0.16101 0.33458 -0.00852 0.00489  0.02108  83  ASN A O   
544  C CB  . ASN A 76  ? 0.27409 0.13412 0.31942 -0.03674 -0.01655 -0.00155 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.38552 0.19719 0.41477 -0.04973 -0.02226 -0.00306 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.40175 0.18411 0.41901 -0.04585 -0.01544 0.00436  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.50518 0.30733 0.53100 -0.06546 -0.03518 -0.01228 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.34252 0.21217 0.40482 -0.03388 0.00574  0.03557  84  LYS A N   
549  C CA  . LYS A 77  ? 0.37022 0.22597 0.42138 -0.02166 0.01540  0.04798  84  LYS A CA  
550  C C   . LYS A 77  ? 0.44737 0.24977 0.47412 -0.01669 0.01628  0.04641  84  LYS A C   
551  O O   . LYS A 77  ? 0.39245 0.18329 0.40512 0.00232  0.02453  0.05418  84  LYS A O   
552  C CB  . LYS A 77  ? 0.33207 0.19918 0.39766 -0.03122 0.02182  0.06400  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.38614 0.29911 0.46458 -0.02760 0.02618  0.06810  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.40802 0.33077 0.49818 -0.03484 0.03540  0.08564  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.41356 0.37471 0.50799 -0.02820 0.04196  0.08887  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.45994 0.44363 0.57092 -0.03501 0.03771  0.07992  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.48693 0.25447 0.50543 -0.03271 0.00762  0.03718  85  GLN A N   
558  C CA  . GLN A 78  ? 0.52005 0.22454 0.50545 -0.02779 0.00886  0.03382  85  GLN A CA  
559  C C   . GLN A 78  ? 0.51837 0.21320 0.48092 -0.00225 0.01324  0.02463  85  GLN A C   
560  O O   . GLN A 78  ? 0.56605 0.23734 0.50882 0.01687  0.02103  0.02846  85  GLN A O   
561  C CB  . GLN A 78  ? 0.60014 0.28219 0.58424 -0.05226 -0.00269 0.02408  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.75567 0.44426 0.75938 -0.07631 -0.00255 0.03576  85  GLN A CG  
563  C CD  . GLN A 78  ? 0.86633 0.61117 0.90428 -0.08798 -0.00583 0.04426  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.86927 0.64390 0.92115 -0.09481 -0.01505 0.03530  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.78663 0.55127 0.84210 -0.08665 0.00366  0.06275  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.44218 0.16956 0.41345 -0.00100 0.00752  0.01372  86  ASP A N   
567  C CA  . ASP A 79  ? 0.47072 0.20056 0.42683 0.02225  0.01269  0.00793  86  ASP A CA  
568  C C   . ASP A 79  ? 0.44484 0.22465 0.41942 0.03981  0.02044  0.01972  86  ASP A C   
569  O O   . ASP A 79  ? 0.43467 0.22136 0.40113 0.06089  0.02692  0.02125  86  ASP A O   
570  C CB  . ASP A 79  ? 0.42417 0.16534 0.38042 0.01374  0.00245  -0.00759 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.64293 0.34659 0.58092 -0.00270 -0.00741 -0.01964 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.66291 0.33423 0.58799 -0.00567 -0.00556 -0.01733 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.65598 0.37343 0.59644 -0.01277 -0.01696 -0.03022 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.31311 0.12774 0.31071 0.03111  0.01960  0.02904  87  ARG A N   
575  C CA  . ARG A 80  ? 0.27055 0.13307 0.28291 0.04122  0.02202  0.03834  87  ARG A CA  
576  C C   . ARG A 80  ? 0.35431 0.24750 0.37359 0.04277  0.01697  0.02933  87  ARG A C   
577  O O   . ARG A 80  ? 0.28619 0.20291 0.30763 0.05709  0.01961  0.03561  87  ARG A O   
578  C CB  . ARG A 80  ? 0.34830 0.20753 0.35238 0.06351  0.03148  0.05396  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.31271 0.21359 0.33023 0.06550  0.03102  0.06785  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.42075 0.34216 0.43800 0.08827  0.03575  0.08332  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.66527 0.55155 0.66789 0.10569  0.04656  0.09575  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.70582 0.59831 0.70371 0.12747  0.05352  0.10494  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.49047 0.42385 0.50040 0.13504  0.05154  0.10677  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.68114 0.54367 0.66299 0.13706  0.06202  0.11052  87  ARG A NH2 
585  N N   . THR A 81  ? 0.24925 0.14445 0.27393 0.02726  0.00936  0.01674  88  THR A N   
586  C CA  . THR A 81  ? 0.26355 0.18303 0.29325 0.02703  0.00466  0.00842  88  THR A CA  
587  C C   . THR A 81  ? 0.21435 0.15894 0.25901 0.01248  -0.00103 0.00494  88  THR A C   
588  O O   . THR A 81  ? 0.23763 0.17611 0.28914 0.00054  -0.00263 0.00475  88  THR A O   
589  C CB  . THR A 81  ? 0.31368 0.20654 0.32834 0.02778  0.00198  -0.00399 88  THR A CB  
590  O OG1 . THR A 81  ? 0.28398 0.15335 0.29673 0.01071  -0.00516 -0.01122 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.35026 0.21414 0.34317 0.04762  0.01094  -0.00094 88  THR A CG2 
592  N N   . LEU A 82  ? 0.18908 0.16120 0.23820 0.01400  -0.00332 0.00380  89  LEU A N   
593  C CA  . LEU A 82  ? 0.19082 0.17898 0.24684 0.00421  -0.00748 -0.00187 89  LEU A CA  
594  C C   . LEU A 82  ? 0.18798 0.17851 0.24195 0.00445  -0.01171 -0.01096 89  LEU A C   
595  O O   . LEU A 82  ? 0.18645 0.18642 0.23732 0.01120  -0.01132 -0.00901 89  LEU A O   
596  C CB  . LEU A 82  ? 0.21864 0.22739 0.27328 0.00408  -0.00723 0.00390  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.16441 0.18149 0.21791 -0.00237 -0.00923 -0.00230 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.20599 0.21907 0.26817 -0.00687 -0.00552 -0.00249 89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.16869 0.19586 0.20971 -0.00296 -0.01048 0.00163  89  LEU A CD2 
600  N N   . THR A 83  ? 0.13666 0.12204 0.19401 -0.00285 -0.01571 -0.01844 90  THR A N   
601  C CA  . THR A 83  ? 0.18244 0.16756 0.23557 -0.00227 -0.01993 -0.02636 90  THR A CA  
602  C C   . THR A 83  ? 0.18631 0.18703 0.24522 -0.00662 -0.02191 -0.02854 90  THR A C   
603  O O   . THR A 83  ? 0.16799 0.17392 0.23582 -0.01128 -0.02141 -0.02688 90  THR A O   
604  C CB  . THR A 83  ? 0.22696 0.19045 0.27429 -0.00631 -0.02508 -0.03291 90  THR A CB  
605  O OG1 . THR A 83  ? 0.23954 0.17770 0.27328 -0.00039 -0.02180 -0.03194 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.18948 0.15276 0.22860 -0.00420 -0.02939 -0.04018 90  THR A CG2 
607  N N   . ILE A 84  ? 0.13365 0.14095 0.18703 -0.00410 -0.02279 -0.03049 91  ILE A N   
608  C CA  . ILE A 84  ? 0.18025 0.19337 0.23256 -0.00648 -0.02400 -0.03305 91  ILE A CA  
609  C C   . ILE A 84  ? 0.19367 0.20288 0.24332 -0.00513 -0.02777 -0.03816 91  ILE A C   
610  O O   . ILE A 84  ? 0.18522 0.19324 0.22805 -0.00183 -0.02769 -0.03838 91  ILE A O   
611  C CB  . ILE A 84  ? 0.15787 0.17640 0.20197 -0.00815 -0.02372 -0.03034 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.24347 0.26524 0.28522 -0.00952 -0.02181 -0.02512 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.16303 0.17617 0.19870 -0.00998 -0.02425 -0.03400 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.29959 0.33006 0.34428 -0.00724 -0.02227 -0.01778 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.14978 0.16022 0.20547 -0.00676 -0.03065 -0.04008 92  VAL A N   
616  C CA  . VAL A 85  ? 0.14832 0.15639 0.20061 -0.00574 -0.03628 -0.04384 92  VAL A CA  
617  C C   . VAL A 85  ? 0.19566 0.20901 0.24723 -0.00256 -0.03477 -0.04262 92  VAL A C   
618  O O   . VAL A 85  ? 0.16914 0.18841 0.22746 -0.00111 -0.03087 -0.03927 92  VAL A O   
619  C CB  . VAL A 85  ? 0.21493 0.22247 0.27528 -0.01143 -0.04385 -0.04471 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.18648 0.18973 0.23684 -0.01067 -0.05168 -0.04838 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.26732 0.26054 0.32429 -0.01536 -0.04431 -0.04568 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.18369 0.19243 0.22469 0.00034  -0.03619 -0.04421 93  ASP A N   
623  C CA  . ASP A 86  ? 0.16164 0.16951 0.19877 0.00458  -0.03504 -0.04248 93  ASP A CA  
624  C C   . ASP A 86  ? 0.21407 0.22154 0.24568 0.00769  -0.04093 -0.04330 93  ASP A C   
625  O O   . ASP A 86  ? 0.21337 0.21646 0.23721 0.00692  -0.04416 -0.04633 93  ASP A O   
626  C CB  . ASP A 86  ? 0.19149 0.18880 0.21582 0.00321  -0.03003 -0.04150 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.29302 0.28870 0.30999 0.00056  -0.03075 -0.04032 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.25489 0.24847 0.26618 0.00438  -0.03208 -0.03964 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.21215 0.21173 0.22990 -0.00458 -0.02954 -0.03800 93  ASP A OD2 
630  N N   . THR A 87  ? 0.17887 0.18922 0.21133 0.01339  -0.04149 -0.03982 94  THR A N   
631  C CA  . THR A 87  ? 0.18852 0.19964 0.21379 0.01751  -0.04775 -0.03874 94  THR A CA  
632  C C   . THR A 87  ? 0.29260 0.29056 0.30234 0.02238  -0.04205 -0.03588 94  THR A C   
633  O O   . THR A 87  ? 0.18769 0.18508 0.19261 0.02972  -0.04343 -0.03131 94  THR A O   
634  C CB  . THR A 87  ? 0.19262 0.22153 0.23301 0.02089  -0.05423 -0.03328 94  THR A CB  
635  O OG1 . THR A 87  ? 0.17556 0.20860 0.22460 0.02859  -0.04512 -0.02718 94  THR A OG1 
636  C CG2 . THR A 87  ? 0.16452 0.20501 0.21914 0.01095  -0.06321 -0.03503 94  THR A CG2 
637  N N   . GLY A 88  ? 0.20173 0.18989 0.20433 0.01730  -0.03626 -0.03671 95  GLY A N   
638  C CA  . GLY A 88  ? 0.20210 0.17647 0.19098 0.01698  -0.03187 -0.03251 95  GLY A CA  
639  C C   . GLY A 88  ? 0.20069 0.17618 0.18016 0.01972  -0.03292 -0.02966 95  GLY A C   
640  O O   . GLY A 88  ? 0.21477 0.19714 0.19251 0.02417  -0.03828 -0.03222 95  GLY A O   
641  N N   . ILE A 89  ? 0.20918 0.17585 0.17975 0.01584  -0.02797 -0.02362 96  ILE A N   
642  C CA  . ILE A 89  ? 0.20365 0.17079 0.16323 0.02015  -0.02593 -0.01782 96  ILE A CA  
643  C C   . ILE A 89  ? 0.20797 0.18747 0.16772 0.02228  -0.02424 -0.01910 96  ILE A C   
644  O O   . ILE A 89  ? 0.23653 0.21540 0.18208 0.03030  -0.02284 -0.01700 96  ILE A O   
645  C CB  . ILE A 89  ? 0.25279 0.20798 0.20550 0.01281  -0.02037 -0.00825 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.30394 0.25811 0.24378 0.01927  -0.01656 0.00045  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.22890 0.19311 0.19223 -0.00095 -0.01821 -0.00462 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.34047 0.27525 0.27069 0.01299  -0.01246 0.01069  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.21504 0.20303 0.18667 0.01754  -0.02335 -0.02199 97  GLY A N   
650  C CA  . GLY A 90  ? 0.21282 0.20845 0.18209 0.02319  -0.01908 -0.02186 97  GLY A CA  
651  C C   . GLY A 90  ? 0.19748 0.20520 0.16858 0.02321  -0.00929 -0.00894 97  GLY A C   
652  O O   . GLY A 90  ? 0.21669 0.22657 0.19235 0.01442  -0.00774 -0.00004 97  GLY A O   
653  N N   . MET A 91  ? 0.20280 0.21747 0.16934 0.03360  -0.00186 -0.00650 98  MET A N   
654  C CA  . MET A 91  ? 0.16957 0.20447 0.14314 0.03663  0.00999  0.00950  98  MET A CA  
655  C C   . MET A 91  ? 0.21023 0.23900 0.15980 0.05597  0.02030  0.01107  98  MET A C   
656  O O   . MET A 91  ? 0.26268 0.27267 0.19260 0.06671  0.01884  -0.00090 98  MET A O   
657  C CB  . MET A 91  ? 0.20859 0.26537 0.20453 0.03346  0.01286  0.01629  98  MET A CB  
658  C CG  . MET A 91  ? 0.24928 0.31344 0.26436 0.01320  0.00350  0.01804  98  MET A CG  
659  S SD  . MET A 91  ? 0.23219 0.32497 0.27135 0.01006  0.00424  0.02739  98  MET A SD  
660  C CE  . MET A 91  ? 0.20186 0.27226 0.23129 0.01814  -0.00025 0.00912  98  MET A CE  
661  N N   . THR A 92  ? 0.23008 0.27177 0.17822 0.05979  0.03097  0.02639  99  THR A N   
662  C CA  . THR A 92  ? 0.24828 0.28662 0.17160 0.08129  0.04518  0.03123  99  THR A CA  
663  C C   . THR A 92  ? 0.23724 0.29377 0.17076 0.09417  0.05840  0.03988  99  THR A C   
664  O O   . THR A 92  ? 0.25631 0.33509 0.22072 0.08419  0.05580  0.04570  99  THR A O   
665  C CB  . THR A 92  ? 0.26577 0.31639 0.18692 0.08228  0.05514  0.04871  99  THR A CB  
666  O OG1 . THR A 92  ? 0.26013 0.34662 0.21787 0.06958  0.06092  0.06922  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.30413 0.33528 0.21458 0.07192  0.04315  0.04244  99  THR A CG2 
668  N N   . LYS A 93  ? 0.27454 0.23612 0.20363 0.02627  -0.00940 -0.00149 100 LYS A N   
669  C CA  . LYS A 93  ? 0.27290 0.22463 0.19019 0.02483  0.01105  -0.00852 100 LYS A CA  
670  C C   . LYS A 93  ? 0.26154 0.21273 0.19105 0.02902  0.02092  0.00193  100 LYS A C   
671  O O   . LYS A 93  ? 0.26327 0.21578 0.20653 0.03385  0.03291  -0.00385 100 LYS A O   
672  C CB  . LYS A 93  ? 0.30922 0.25542 0.18593 0.01792  0.01716  -0.01308 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.33252 0.26698 0.19697 0.02188  0.03800  -0.02507 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.40887 0.33712 0.23110 0.01648  0.04658  -0.03131 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.52697 0.43908 0.33683 0.02609  0.06687  -0.04647 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.49359 0.40733 0.26961 0.02592  0.08129  -0.05142 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.27776 0.22656 0.20000 0.02580  0.01510  0.01787  101 ALA A N   
678  C CA  . ALA A 94  ? 0.30437 0.25360 0.23604 0.02289  0.02469  0.02725  101 ALA A CA  
679  C C   . ALA A 94  ? 0.33017 0.27919 0.29714 0.02784  0.02188  0.02480  101 ALA A C   
680  O O   . ALA A 94  ? 0.34815 0.30557 0.32893 0.02538  0.03243  0.02467  101 ALA A O   
681  C CB  . ALA A 94  ? 0.30978 0.24590 0.21811 0.01394  0.01850  0.04620  101 ALA A CB  
682  N N   . ASP A 95  ? 0.25293 0.19763 0.23513 0.03427  0.00784  0.02139  102 ASP A N   
683  C CA  . ASP A 95  ? 0.27351 0.21908 0.28661 0.03883  0.00662  0.01544  102 ASP A CA  
684  C C   . ASP A 95  ? 0.23236 0.18889 0.25582 0.04013  0.01766  0.00226  102 ASP A C   
685  O O   . ASP A 95  ? 0.26180 0.22203 0.30229 0.04026  0.02277  0.00004  102 ASP A O   
686  C CB  . ASP A 95  ? 0.28342 0.22924 0.31114 0.04724  -0.00919 0.01210  102 ASP A CB  
687  C CG  . ASP A 95  ? 0.42301 0.34910 0.44526 0.05256  -0.02220 0.02647  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.42835 0.33467 0.43630 0.04488  -0.01719 0.03889  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.32201 0.25254 0.35287 0.06438  -0.03775 0.02542  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.23397 0.19169 0.24287 0.04028  0.02068  -0.00629 103 LEU A N   
691  C CA  . LEU A 96  ? 0.27540 0.23127 0.28540 0.04263  0.03008  -0.01678 103 LEU A CA  
692  C C   . LEU A 96  ? 0.26078 0.22160 0.26913 0.04802  0.04220  -0.01401 103 LEU A C   
693  O O   . LEU A 96  ? 0.24471 0.21088 0.26770 0.05208  0.04527  -0.01569 103 LEU A O   
694  C CB  . LEU A 96  ? 0.27891 0.22450 0.26552 0.03890  0.03143  -0.02646 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.25569 0.20635 0.24839 0.03084  0.02180  -0.03485 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.25402 0.19084 0.21666 0.02151  0.02541  -0.04540 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.20696 0.16156 0.22175 0.02994  0.02319  -0.04053 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.30407 0.26814 0.29423 0.04857  0.04931  -0.01105 104 ILE A N   
699  C CA  . ILE A 97  ? 0.29645 0.28049 0.29412 0.05116  0.05945  -0.00655 104 ILE A CA  
700  C C   . ILE A 97  ? 0.24615 0.23730 0.26277 0.04094  0.05337  0.00307  104 ILE A C   
701  O O   . ILE A 97  ? 0.67649 0.65261 0.69399 0.03612  0.04215  0.00723  104 ILE A O   
702  C CB  . ILE A 97  ? 0.29154 0.28160 0.26512 0.04992  0.06925  -0.00581 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.24059 0.20964 0.18738 0.05622  0.07202  -0.01728 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.24540 0.26689 0.22948 0.05557  0.08360  -0.00649 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.29638 0.26436 0.21159 0.05010  0.07744  -0.01789 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.50813 0.52187 0.54026 0.03818  0.06007  0.00529  105 ASN A N   
707  C CA  . ASN A 98  ? 0.33237 0.34447 0.37914 0.02532  0.05453  0.01161  105 ASN A CA  
708  C C   . ASN A 98  ? 0.24281 0.24256 0.30501 0.02991  0.04543  0.00517  105 ASN A C   
709  O O   . ASN A 98  ? 0.23668 0.21798 0.30338 0.02482  0.03716  0.00739  105 ASN A O   
710  C CB  . ASN A 98  ? 0.27567 0.26560 0.30463 0.01328  0.04940  0.02355  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.53203 0.51453 0.56680 -0.00334 0.04857  0.03103  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.47225 0.47677 0.52544 -0.01004 0.05391  0.02637  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.50748 0.45600 0.52330 -0.01060 0.04075  0.04288  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.23152 0.23795 0.29771 0.04096  0.04751  -0.00314 106 ASN A N   
715  C CA  . ASN A 99  ? 0.15524 0.16020 0.23480 0.04233  0.04309  -0.00948 106 ASN A CA  
716  C C   . ASN A 99  ? 0.21030 0.19541 0.29245 0.04029  0.03512  -0.01357 106 ASN A C   
717  O O   . ASN A 99  ? 0.18737 0.17004 0.28270 0.03613  0.03140  -0.01740 106 ASN A O   
718  C CB  . ASN A 99  ? 0.20064 0.22519 0.29665 0.03333  0.04356  -0.00847 106 ASN A CB  
719  C CG  . ASN A 99  ? 0.20371 0.26291 0.30430 0.03682  0.05092  -0.00655 106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.19853 0.26648 0.29545 0.05294  0.05332  -0.00939 106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.22424 0.30326 0.33210 0.02189  0.05481  -0.00213 106 ASN A ND2 
722  N N   . LEU A 100 ? 0.20221 0.17700 0.27218 0.04346  0.03283  -0.01489 107 LEU A N   
723  C CA  . LEU A 100 ? 0.22924 0.19805 0.30549 0.04325  0.02527  -0.02113 107 LEU A CA  
724  C C   . LEU A 100 ? 0.21533 0.17888 0.30604 0.04324  0.01756  -0.01841 107 LEU A C   
725  O O   . LEU A 100 ? 0.21777 0.18361 0.32092 0.04406  0.01419  -0.02623 107 LEU A O   
726  C CB  . LEU A 100 ? 0.17637 0.14818 0.25238 0.04069  0.02727  -0.03041 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.26403 0.22664 0.31826 0.04182  0.03348  -0.03228 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.28062 0.24585 0.32768 0.04558  0.03594  -0.02856 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.44569 0.40177 0.49420 0.03453  0.03459  -0.04233 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.19324 0.14715 0.27503 0.04087  0.01541  -0.00666 108 GLY A N   
731  C CA  . GLY A 101 ? 0.25982 0.19448 0.34590 0.04220  0.00712  -0.00151 108 GLY A CA  
732  C C   . GLY A 101 ? 0.28804 0.21405 0.38580 0.03640  0.01013  -0.00573 108 GLY A C   
733  O O   . GLY A 101 ? 0.32969 0.23250 0.43125 0.04057  0.00361  -0.00615 108 GLY A O   
734  N N   . THR A 102 ? 0.23501 0.17800 0.33693 0.02804  0.01891  -0.00963 109 THR A N   
735  C CA  . THR A 102 ? 0.25929 0.19903 0.37012 0.01880  0.02112  -0.01563 109 THR A CA  
736  C C   . THR A 102 ? 0.20157 0.14520 0.30533 0.00209  0.02628  -0.00688 109 THR A C   
737  O O   . THR A 102 ? 0.25720 0.21509 0.35231 -0.00030 0.03076  0.00196  109 THR A O   
738  C CB  . THR A 102 ? 0.20023 0.16263 0.32055 0.01976  0.02502  -0.02722 109 THR A CB  
739  O OG1 . THR A 102 ? 0.25010 0.23649 0.36583 0.01975  0.03009  -0.02250 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.29337 0.25830 0.41431 0.02919  0.02229  -0.03482 109 THR A CG2 
741  N N   . ILE A 103 ? 0.22589 0.15883 0.33263 -0.01177 0.02689  -0.01138 110 ILE A N   
742  C CA  . ILE A 103 ? 0.20001 0.14867 0.30427 -0.03373 0.03301  -0.00694 110 ILE A CA  
743  C C   . ILE A 103 ? 0.22860 0.22125 0.34857 -0.03561 0.03549  -0.01663 110 ILE A C   
744  O O   . ILE A 103 ? 0.22321 0.22262 0.34786 -0.05197 0.03546  -0.02430 110 ILE A O   
745  C CB  . ILE A 103 ? 0.30582 0.21255 0.39772 -0.05323 0.03206  -0.00558 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.34990 0.23273 0.44739 -0.05012 0.02810  -0.02111 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.37274 0.23432 0.44259 -0.04912 0.02796  0.00909  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.44307 0.28621 0.52615 -0.07425 0.02944  -0.02404 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.20762 0.22760 0.33193 -0.01882 0.03674  -0.01599 111 ALA A N   
750  C CA  . ALA A 104 ? 0.23619 0.28737 0.36956 -0.01270 0.03568  -0.02324 111 ALA A CA  
751  C C   . ALA A 104 ? 0.14127 0.23653 0.28572 -0.02628 0.03740  -0.02368 111 ALA A C   
752  O O   . ALA A 104 ? 0.16485 0.28240 0.31552 -0.02798 0.03302  -0.03068 111 ALA A O   
753  C CB  . ALA A 104 ? 0.18637 0.24416 0.31451 0.00892  0.03679  -0.02074 111 ALA A CB  
754  N N   . LYS A 105 ? 0.16293 0.27673 0.30956 -0.03736 0.04361  -0.01681 112 LYS A N   
755  C CA  . LYS A 105 ? 0.19352 0.36334 0.35622 -0.05155 0.04599  -0.01902 112 LYS A CA  
756  C C   . LYS A 105 ? 0.22523 0.39130 0.38982 -0.07951 0.04223  -0.02723 112 LYS A C   
757  O O   . LYS A 105 ? 0.21111 0.41701 0.38768 -0.08335 0.03678  -0.03484 112 LYS A O   
758  C CB  . LYS A 105 ? 0.17263 0.36590 0.33630 -0.06181 0.05661  -0.01151 112 LYS A CB  
759  C CG  . LYS A 105 ? 0.36598 0.63703 0.55356 -0.06774 0.06091  -0.01506 112 LYS A CG  
760  C CD  . LYS A 105 ? 0.53025 0.81156 0.71892 -0.10361 0.06042  -0.01792 112 LYS A CD  
761  C CE  . LYS A 105 ? 0.65089 0.90469 0.82190 -0.13067 0.07119  -0.00979 112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.61417 0.84593 0.77330 -0.16588 0.06935  -0.01219 112 LYS A NZ  
763  N N   . SER A 106 ? 0.23857 0.35317 0.38778 -0.09859 0.04408  -0.02608 113 SER A N   
764  C CA  . SER A 106 ? 0.29645 0.39474 0.44134 -0.12580 0.04159  -0.03636 113 SER A CA  
765  C C   . SER A 106 ? 0.22264 0.30212 0.36583 -0.11304 0.03432  -0.04850 113 SER A C   
766  O O   . SER A 106 ? 0.26103 0.35222 0.40487 -0.13111 0.03106  -0.06073 113 SER A O   
767  C CB  . SER A 106 ? 0.39281 0.42813 0.51512 -0.14653 0.04556  -0.03111 113 SER A CB  
768  O OG  . SER A 106 ? 0.36834 0.34825 0.47794 -0.12233 0.04232  -0.02603 113 SER A OG  
769  N N   . GLY A 107 ? 0.19376 0.24775 0.33336 -0.08517 0.03248  -0.04663 114 GLY A N   
770  C CA  . GLY A 107 ? 0.21086 0.25277 0.34809 -0.07519 0.02840  -0.05877 114 GLY A CA  
771  C C   . GLY A 107 ? 0.25178 0.34351 0.39538 -0.07088 0.02381  -0.06224 114 GLY A C   
772  O O   . GLY A 107 ? 0.21027 0.30496 0.34880 -0.07948 0.02032  -0.07436 114 GLY A O   
773  N N   . THR A 108 ? 0.15315 0.28253 0.30481 -0.05599 0.02332  -0.05183 115 THR A N   
774  C CA  . THR A 108 ? 0.17512 0.35104 0.33090 -0.04755 0.01643  -0.05228 115 THR A CA  
775  C C   . THR A 108 ? 0.23949 0.45874 0.40498 -0.07266 0.01164  -0.05955 115 THR A C   
776  O O   . THR A 108 ? 0.23986 0.48231 0.40128 -0.07490 0.00309  -0.06593 115 THR A O   
777  C CB  . THR A 108 ? 0.15511 0.35842 0.31740 -0.02312 0.01744  -0.04067 115 THR A CB  
778  O OG1 . THR A 108 ? 0.19613 0.35756 0.34519 -0.00404 0.02128  -0.03611 115 THR A OG1 
779  C CG2 . THR A 108 ? 0.17729 0.42537 0.34205 -0.00878 0.00792  -0.03920 115 THR A CG2 
780  N N   . LYS A 109 ? 0.18319 0.41528 0.35869 -0.09469 0.01695  -0.05865 116 LYS A N   
781  C CA  . LYS A 109 ? 0.18571 0.45059 0.36367 -0.12138 0.01299  -0.06479 116 LYS A CA  
782  C C   . LYS A 109 ? 0.26112 0.49404 0.42146 -0.13917 0.00888  -0.07898 116 LYS A C   
783  O O   . LYS A 109 ? 0.28665 0.55147 0.44336 -0.14372 0.00017  -0.08496 116 LYS A O   
784  C CB  . LYS A 109 ? 0.21783 0.47449 0.39482 -0.14274 0.02157  -0.05938 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.45784 0.74305 0.63266 -0.16882 0.01895  -0.06468 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.32152 0.59236 0.49051 -0.19256 0.02900  -0.05932 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.36410 0.67674 0.53451 -0.21808 0.02788  -0.06537 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.62940 1.01357 0.81825 -0.20240 0.01804  -0.06912 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.26979 0.43718 0.41647 -0.14626 0.01507  -0.08474 117 ALA A N   
790  C CA  . ALA A 110 ? 0.31897 0.44875 0.44517 -0.15787 0.01347  -0.09936 117 ALA A CA  
791  C C   . ALA A 110 ? 0.25914 0.40365 0.38194 -0.14365 0.00812  -0.10780 117 ALA A C   
792  O O   . ALA A 110 ? 0.30279 0.45392 0.41095 -0.15459 0.00367  -0.11816 117 ALA A O   
793  C CB  . ALA A 110 ? 0.30067 0.35490 0.41264 -0.15763 0.02057  -0.10184 117 ALA A CB  
794  N N   . PHE A 111 ? 0.27544 0.41895 0.40373 -0.11626 0.00893  -0.09989 118 PHE A N   
795  C CA  . PHE A 111 ? 0.21558 0.36457 0.33104 -0.10122 0.00485  -0.10288 118 PHE A CA  
796  C C   . PHE A 111 ? 0.30604 0.51412 0.42064 -0.10501 -0.00739 -0.10109 118 PHE A C   
797  O O   . PHE A 111 ? 0.30014 0.51391 0.39686 -0.11369 -0.01254 -0.11148 118 PHE A O   
798  C CB  . PHE A 111 ? 0.19351 0.32622 0.30885 -0.07152 0.00837  -0.08997 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.18630 0.31601 0.28275 -0.05959 0.00663  -0.09108 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.26116 0.37628 0.34128 -0.07200 0.00898  -0.10757 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.24971 0.38560 0.34019 -0.03721 0.00435  -0.07626 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.23036 0.34258 0.28838 -0.06510 0.00945  -0.10780 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.25985 0.38459 0.32566 -0.03035 0.00386  -0.07539 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.25895 0.37436 0.30844 -0.04574 0.00663  -0.09050 118 PHE A CZ  
805  N N   . MET A 112 ? 0.26475 0.52102 0.39824 -0.09810 -0.01257 -0.08890 119 MET A N   
806  C CA  . MET A 112 ? 0.38729 0.70544 0.52302 -0.09213 -0.02695 -0.08482 119 MET A CA  
807  C C   . MET A 112 ? 0.40704 0.74925 0.53741 -0.12058 -0.03257 -0.09540 119 MET A C   
808  O O   . MET A 112 ? 0.35003 0.72783 0.47022 -0.11826 -0.04521 -0.09538 119 MET A O   
809  C CB  . MET A 112 ? 0.39379 0.75577 0.55253 -0.06872 -0.02918 -0.06959 119 MET A CB  
810  C CG  . MET A 112 ? 0.16271 0.50905 0.30734 -0.03023 -0.03243 -0.05546 119 MET A CG  
811  S SD  . MET A 112 ? 0.76110 1.16117 0.93031 0.00239  -0.03591 -0.04151 119 MET A SD  
812  C CE  . MET A 112 ? 0.22213 0.55240 0.37334 0.03020  -0.02384 -0.03137 119 MET A CE  
813  N N   . GLU A 113 ? 0.27614 0.59100 0.40653 -0.14496 -0.02329 -0.10207 120 GLU A N   
814  C CA  . GLU A 113 ? 0.37833 0.70019 0.49569 -0.17164 -0.02613 -0.11301 120 GLU A CA  
815  C C   . GLU A 113 ? 0.47921 0.76096 0.56921 -0.17985 -0.02500 -0.12765 120 GLU A C   
816  O O   . GLU A 113 ? 0.42651 0.72760 0.50185 -0.19396 -0.03141 -0.13585 120 GLU A O   
817  C CB  . GLU A 113 ? 0.43882 0.73813 0.55881 -0.19578 -0.01665 -0.11520 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.60617 0.92709 0.74849 -0.19035 -0.01157 -0.10183 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.78515 1.17170 0.94894 -0.16373 -0.01907 -0.09022 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.58468 0.97582 0.76330 -0.14818 -0.01298 -0.07957 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.59124 1.02403 0.75527 -0.15742 -0.03096 -0.09146 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.35076 0.57850 0.43354 -0.17042 -0.01588 -0.13187 121 ALA A N   
823  C CA  . ALA A 114 ? 0.30841 0.50031 0.36581 -0.17343 -0.01188 -0.14643 121 ALA A CA  
824  C C   . ALA A 114 ? 0.36154 0.58974 0.40489 -0.16514 -0.02231 -0.14532 121 ALA A C   
825  O O   . ALA A 114 ? 0.47183 0.69865 0.49161 -0.17662 -0.02376 -0.15572 121 ALA A O   
826  C CB  . ALA A 114 ? 0.35198 0.48566 0.40895 -0.15965 0.00064  -0.15020 121 ALA A CB  
827  N N   . LEU A 115 ? 0.32254 0.58194 0.37669 -0.14465 -0.03036 -0.13168 122 LEU A N   
828  C CA  . LEU A 115 ? 0.44320 0.73201 0.47606 -0.13392 -0.04344 -0.12635 122 LEU A CA  
829  C C   . LEU A 115 ? 0.52049 0.85704 0.54647 -0.14330 -0.05752 -0.12380 122 LEU A C   
830  O O   . LEU A 115 ? 0.42284 0.76219 0.41859 -0.14884 -0.06361 -0.12769 122 LEU A O   
831  C CB  . LEU A 115 ? 0.34968 0.64224 0.39016 -0.09833 -0.04618 -0.10225 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.23282 0.46792 0.27379 -0.08332 -0.02965 -0.09883 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.26865 0.50227 0.30928 -0.05131 -0.03242 -0.07686 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.29011 0.48687 0.30223 -0.09229 -0.02034 -0.11240 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.45199 0.82696 0.50472 -0.14588 -0.06168 -0.11752 123 GLN A N   
836  C CA  . GLN A 116 ? 0.51396 0.93781 0.56459 -0.15669 -0.07382 -0.11766 123 GLN A CA  
837  C C   . GLN A 116 ? 0.59081 0.99040 0.62224 -0.18911 -0.06709 -0.13671 123 GLN A C   
838  O O   . GLN A 116 ? 0.63199 1.06869 0.65449 -0.20126 -0.07753 -0.13983 123 GLN A O   
839  C CB  . GLN A 116 ? 0.41502 0.88628 0.49959 -0.15267 -0.07616 -0.10884 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.60766 1.11681 0.70855 -0.11494 -0.08633 -0.08950 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.91630 1.49410 1.03529 -0.10781 -0.09813 -0.08321 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.92950 1.53319 1.05050 -0.13497 -0.09923 -0.09365 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.93006 1.53573 1.06128 -0.07008 -0.10638 -0.06705 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.60595 0.94349 0.63035 -0.20057 -0.05040 -0.14923 124 ALA A N   
845  C CA  . ALA A 117 ? 0.52311 0.82793 0.52788 -0.22642 -0.04231 -0.16753 124 ALA A CA  
846  C C   . ALA A 117 ? 0.79880 1.06168 0.77470 -0.22381 -0.03463 -0.17906 124 ALA A C   
847  O O   . ALA A 117 ? 0.62644 0.84728 0.58833 -0.23789 -0.02348 -0.19517 124 ALA A O   
848  C CB  . ALA A 117 ? 0.51887 0.78111 0.53473 -0.23886 -0.02942 -0.17262 124 ALA A CB  
849  N N   . GLY A 118 ? 0.48321 0.75536 0.44829 -0.20539 -0.03954 -0.17105 125 GLY A N   
850  C CA  . GLY A 118 ? 0.57386 0.81716 0.50840 -0.20498 -0.03198 -0.18067 125 GLY A CA  
851  C C   . GLY A 118 ? 0.58774 0.79192 0.52333 -0.18674 -0.01883 -0.17998 125 GLY A C   
852  O O   . GLY A 118 ? 0.52495 0.71489 0.43569 -0.18404 -0.01251 -0.18418 125 GLY A O   
853  N N   . ALA A 119 ? 0.40767 0.59536 0.37072 -0.17532 -0.01358 -0.17472 126 ALA A N   
854  C CA  . ALA A 119 ? 0.35257 0.50605 0.31955 -0.15802 -0.00112 -0.17472 126 ALA A CA  
855  C C   . ALA A 119 ? 0.35177 0.52535 0.30349 -0.14514 -0.00898 -0.16230 126 ALA A C   
856  O O   . ALA A 119 ? 0.40776 0.62264 0.35171 -0.14296 -0.02703 -0.14956 126 ALA A O   
857  C CB  . ALA A 119 ? 0.38321 0.51513 0.38142 -0.14916 0.00429  -0.17047 126 ALA A CB  
858  N N   . ASP A 120 ? 0.44921 0.59300 0.39499 -0.13429 0.00428  -0.16432 127 ASP A N   
859  C CA  . ASP A 120 ? 0.41047 0.55543 0.33738 -0.11943 0.00140  -0.14721 127 ASP A CA  
860  C C   . ASP A 120 ? 0.32296 0.44298 0.27633 -0.09960 0.01109  -0.13744 127 ASP A C   
861  O O   . ASP A 120 ? 0.29726 0.40161 0.27928 -0.09880 0.01912  -0.14741 127 ASP A O   
862  C CB  . ASP A 120 ? 0.48235 0.61606 0.36877 -0.12907 0.01017  -0.15480 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.54712 0.65280 0.45035 -0.12842 0.03237  -0.16872 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.67847 0.77787 0.59800 -0.13390 0.03794  -0.18237 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.57909 0.67106 0.47877 -0.12150 0.04330  -0.16478 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.28678 0.39919 0.22533 -0.08409 0.00944  -0.11737 128 ILE A N   
867  C CA  . ILE A 121 ? 0.27728 0.37025 0.23708 -0.06618 0.01541  -0.10610 128 ILE A CA  
868  C C   . ILE A 121 ? 0.30767 0.37873 0.28083 -0.06982 0.03306  -0.12281 128 ILE A C   
869  O O   . ILE A 121 ? 0.32369 0.38379 0.32403 -0.05862 0.03698  -0.12016 128 ILE A O   
870  C CB  . ILE A 121 ? 0.33870 0.42062 0.27095 -0.05136 0.00983  -0.08291 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.43875 0.54693 0.37477 -0.03576 -0.00874 -0.06547 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.29854 0.35235 0.24000 -0.04037 0.02024  -0.07675 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.34143 0.43336 0.24261 -0.01709 -0.01734 -0.04269 128 ILE A CD1 
874  N N   . SER A 122 ? 0.36229 0.43137 0.31783 -0.08454 0.04363  -0.14150 129 SER A N   
875  C CA  . SER A 122 ? 0.41407 0.47281 0.39053 -0.08235 0.05916  -0.15432 129 SER A CA  
876  C C   . SER A 122 ? 0.34515 0.39679 0.35952 -0.07315 0.05856  -0.15924 129 SER A C   
877  O O   . SER A 122 ? 0.32995 0.37575 0.36776 -0.06256 0.06466  -0.15951 129 SER A O   
878  C CB  . SER A 122 ? 0.29343 0.35828 0.25393 -0.09486 0.06876  -0.16422 129 SER A CB  
879  O OG  . SER A 122 ? 0.38941 0.45729 0.35446 -0.10084 0.06702  -0.17635 129 SER A OG  
880  N N   . MET A 123 ? 0.29791 0.35083 0.31533 -0.07870 0.04982  -0.16188 130 MET A N   
881  C CA  . MET A 123 ? 0.24985 0.28637 0.29145 -0.07374 0.04961  -0.16449 130 MET A CA  
882  C C   . MET A 123 ? 0.25247 0.28184 0.31500 -0.06315 0.04444  -0.15271 130 MET A C   
883  O O   . MET A 123 ? 0.27066 0.28299 0.34626 -0.06177 0.04268  -0.15145 130 MET A O   
884  C CB  . MET A 123 ? 0.35893 0.39737 0.38956 -0.09053 0.04433  -0.17261 130 MET A CB  
885  C CG  . MET A 123 ? 0.37589 0.42085 0.38320 -0.10147 0.04967  -0.18486 130 MET A CG  
886  S SD  . MET A 123 ? 0.45555 0.50910 0.44403 -0.12446 0.04159  -0.19361 130 MET A SD  
887  C CE  . MET A 123 ? 0.44941 0.46559 0.45618 -0.12250 0.04354  -0.19790 130 MET A CE  
888  N N   . ILE A 124 ? 0.21656 0.25423 0.27785 -0.05510 0.04256  -0.14147 131 ILE A N   
889  C CA  . ILE A 124 ? 0.27508 0.31098 0.35272 -0.04308 0.03703  -0.12292 131 ILE A CA  
890  C C   . ILE A 124 ? 0.23541 0.24811 0.33440 -0.03391 0.04128  -0.12709 131 ILE A C   
891  O O   . ILE A 124 ? 0.19799 0.20301 0.30808 -0.03122 0.03689  -0.11695 131 ILE A O   
892  C CB  . ILE A 124 ? 0.21627 0.25816 0.28232 -0.03219 0.03565  -0.10616 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.24859 0.29081 0.32815 -0.01978 0.03095  -0.08933 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.24466 0.27600 0.30593 -0.03018 0.04592  -0.11335 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.25366 0.29530 0.31716 -0.00783 0.02906  -0.07397 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.26834 0.27801 0.36951 -0.02726 0.04633  -0.12928 132 GLY A N   
897  C CA  . GLY A 125 ? 0.22108 0.21788 0.33703 -0.01457 0.04425  -0.12332 132 GLY A CA  
898  C C   . GLY A 125 ? 0.31231 0.28425 0.42940 -0.01519 0.04158  -0.12624 132 GLY A C   
899  O O   . GLY A 125 ? 0.30784 0.26207 0.43047 -0.00501 0.03723  -0.11773 132 GLY A O   
900  N N   . GLN A 126 ? 0.24438 0.21101 0.35047 -0.02870 0.04350  -0.13774 133 GLN A N   
901  C CA  . GLN A 126 ? 0.27280 0.20775 0.37228 -0.03429 0.04112  -0.14064 133 GLN A CA  
902  C C   . GLN A 126 ? 0.31772 0.24389 0.41946 -0.04341 0.03611  -0.12933 133 GLN A C   
903  O O   . GLN A 126 ? 0.30792 0.20107 0.40089 -0.04975 0.03385  -0.12764 133 GLN A O   
904  C CB  . GLN A 126 ? 0.34439 0.27837 0.42777 -0.05101 0.04383  -0.15596 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.40599 0.34607 0.48590 -0.04436 0.05082  -0.16922 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.50459 0.44469 0.56530 -0.06199 0.05363  -0.18448 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.53644 0.45310 0.58545 -0.07464 0.05028  -0.18853 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.59213 0.55772 0.64633 -0.06556 0.05970  -0.19273 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.24611 0.19884 0.35727 -0.04560 0.03465  -0.12209 134 PHE A N   
910  C CA  . PHE A 127 ? 0.27913 0.23465 0.39745 -0.05679 0.03139  -0.11217 134 PHE A CA  
911  C C   . PHE A 127 ? 0.32809 0.28158 0.45488 -0.03896 0.03041  -0.09546 134 PHE A C   
912  O O   . PHE A 127 ? 0.27583 0.24433 0.40423 -0.04294 0.02868  -0.08065 134 PHE A O   
913  C CB  . PHE A 127 ? 0.24460 0.24672 0.36106 -0.06882 0.02737  -0.10835 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.24140 0.25089 0.34684 -0.08906 0.02630  -0.12546 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.39376 0.39381 0.49131 -0.11002 0.02496  -0.12765 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.32599 0.34873 0.42064 -0.08607 0.02695  -0.13559 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.38208 0.38831 0.46330 -0.12523 0.02318  -0.13925 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.25566 0.28563 0.33313 -0.10168 0.02567  -0.14685 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.32047 0.34246 0.39224 -0.12029 0.02344  -0.14897 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.24377 0.18797 0.37311 -0.01967 0.03115  -0.09571 135 GLY A N   
921  C CA  . GLY A 128 ? 0.22395 0.16427 0.35742 -0.00530 0.02843  -0.08167 135 GLY A CA  
922  C C   . GLY A 128 ? 0.24417 0.20949 0.38045 -0.00023 0.02941  -0.07373 135 GLY A C   
923  O O   . GLY A 128 ? 0.23882 0.20091 0.37514 0.00798  0.02755  -0.06208 135 GLY A O   
924  N N   . VAL A 129 ? 0.18696 0.17612 0.31788 -0.00410 0.03101  -0.07664 136 VAL A N   
925  C CA  . VAL A 129 ? 0.14645 0.15304 0.27072 0.00342  0.03094  -0.06590 136 VAL A CA  
926  C C   . VAL A 129 ? 0.17448 0.18336 0.28907 0.00599  0.03417  -0.07280 136 VAL A C   
927  O O   . VAL A 129 ? 0.16511 0.18161 0.26519 0.00887  0.03388  -0.06613 136 VAL A O   
928  C CB  . VAL A 129 ? 0.16993 0.20191 0.29205 -0.00126 0.02824  -0.05808 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.18704 0.22152 0.31715 -0.00634 0.02828  -0.04975 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.19851 0.24405 0.31791 -0.01461 0.02580  -0.06786 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.22207 0.17609 0.23974 -0.01076 -0.02709 -0.05068 137 GLY A N   
932  C CA  . GLY A 130 ? 0.24512 0.20588 0.24728 0.00248  -0.02198 -0.05061 137 GLY A CA  
933  C C   . GLY A 130 ? 0.20745 0.17814 0.21034 0.00158  -0.01101 -0.03930 137 GLY A C   
934  O O   . GLY A 130 ? 0.22868 0.20794 0.22347 0.01003  -0.00669 -0.03611 137 GLY A O   
935  N N   . PHE A 131 ? 0.17706 0.14652 0.18954 -0.00780 -0.00706 -0.03291 138 PHE A N   
936  C CA  . PHE A 131 ? 0.16620 0.14221 0.18028 -0.00847 0.00023  -0.02530 138 PHE A CA  
937  C C   . PHE A 131 ? 0.21547 0.19994 0.22838 -0.00522 0.00078  -0.02447 138 PHE A C   
938  O O   . PHE A 131 ? 0.18581 0.17261 0.19644 -0.00123 0.00535  -0.01883 138 PHE A O   
939  C CB  . PHE A 131 ? 0.20093 0.17653 0.22296 -0.01651 0.00215  -0.02154 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.25301 0.23399 0.27678 -0.01631 0.00604  -0.01796 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.25472 0.23382 0.27834 -0.01464 0.00887  -0.01472 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.19113 0.17929 0.21818 -0.01719 0.00576  -0.01851 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.20390 0.18359 0.23080 -0.01480 0.00964  -0.01337 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.21267 0.20214 0.23989 -0.01469 0.00750  -0.01754 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.22377 0.20672 0.25098 -0.01394 0.00859  -0.01562 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.19137 0.18081 0.20786 -0.00710 -0.00428 -0.02902 139 TYR A N   
947  C CA  . TYR A 132 ? 0.12818 0.12690 0.14419 -0.00297 -0.00413 -0.02798 139 TYR A CA  
948  C C   . TYR A 132 ? 0.19400 0.19574 0.19837 0.00810  -0.00448 -0.02779 139 TYR A C   
949  O O   . TYR A 132 ? 0.20510 0.21277 0.20725 0.01353  -0.00350 -0.02446 139 TYR A O   
950  C CB  . TYR A 132 ? 0.13218 0.14052 0.15801 -0.00780 -0.00963 -0.03230 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.17362 0.18411 0.21046 -0.01696 -0.00680 -0.02861 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.15059 0.16770 0.18895 -0.01542 -0.00180 -0.02465 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.17749 0.18266 0.22178 -0.02537 -0.00925 -0.02862 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.18052 0.20346 0.22563 -0.02062 0.00152  -0.02090 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.21448 0.22433 0.26757 -0.03233 -0.00524 -0.02209 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.19858 0.21935 0.25089 -0.02916 0.00060  -0.01828 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.20994 0.23905 0.26777 -0.03299 0.00514  -0.01159 139 TYR A OH  
958  N N   . SER A 133 ? 0.18932 0.18809 0.18496 0.01358  -0.00555 -0.03057 140 SER A N   
959  C CA  . SER A 133 ? 0.21039 0.21591 0.19260 0.02664  -0.00340 -0.02752 140 SER A CA  
960  C C   . SER A 133 ? 0.21402 0.22037 0.19751 0.02787  0.00639  -0.01340 140 SER A C   
961  O O   . SER A 133 ? 0.19801 0.21199 0.17271 0.03807  0.01020  -0.00584 140 SER A O   
962  C CB  . SER A 133 ? 0.21585 0.22023 0.18703 0.03492  -0.00625 -0.03432 140 SER A CB  
963  O OG  . SER A 133 ? 0.20390 0.20335 0.17784 0.03241  -0.00013 -0.02922 140 SER A OG  
964  N N   . ALA A 134 ? 0.18119 0.18032 0.17615 0.01797  0.00980  -0.00923 141 ALA A N   
965  C CA  . ALA A 134 ? 0.16116 0.15827 0.16236 0.01658  0.01595  0.00264  141 ALA A CA  
966  C C   . ALA A 134 ? 0.18596 0.18382 0.18524 0.02172  0.01593  0.00789  141 ALA A C   
967  O O   . ALA A 134 ? 0.18534 0.18270 0.18620 0.02483  0.02095  0.02051  141 ALA A O   
968  C CB  . ALA A 134 ? 0.15714 0.14585 0.17021 0.00608  0.01561  0.00148  141 ALA A CB  
969  N N   . TYR A 135 ? 0.18411 0.18418 0.18165 0.02288  0.01038  -0.00013 142 TYR A N   
970  C CA  . TYR A 135 ? 0.16965 0.17082 0.16513 0.02960  0.00961  0.00415  142 TYR A CA  
971  C C   . TYR A 135 ? 0.18057 0.19186 0.16267 0.04242  0.00992  0.00871  142 TYR A C   
972  O O   . TYR A 135 ? 0.21720 0.23076 0.19551 0.05032  0.00885  0.01305  142 TYR A O   
973  C CB  . TYR A 135 ? 0.15882 0.16388 0.15908 0.02746  0.00408  -0.00536 142 TYR A CB  
974  C CG  . TYR A 135 ? 0.16486 0.16156 0.17481 0.01926  0.00512  -0.00712 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.19404 0.18057 0.20734 0.02156  0.00570  -0.00333 142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.15233 0.14975 0.16689 0.01063  0.00479  -0.01251 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.18954 0.16890 0.20906 0.01665  0.00493  -0.00752 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.17148 0.16384 0.19180 0.00572  0.00561  -0.01401 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.19662 0.18088 0.21860 0.00929  0.00527  -0.01269 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.18935 0.16940 0.21453 0.00695  0.00429  -0.01690 142 TYR A OH  
981  N N   . LEU A 136 ? 0.23055 0.24869 0.20377 0.04692  0.01119  0.00776  143 LEU A N   
982  C CA  . LEU A 136 ? 0.21388 0.24376 0.17164 0.06200  0.01354  0.01488  143 LEU A CA  
983  C C   . LEU A 136 ? 0.22118 0.24911 0.18199 0.06427  0.02353  0.03597  143 LEU A C   
984  O O   . LEU A 136 ? 0.25490 0.29092 0.20515 0.07674  0.02635  0.04695  143 LEU A O   
985  C CB  . LEU A 136 ? 0.23167 0.26984 0.17784 0.06866  0.01225  0.00717  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.19613 0.23521 0.13824 0.06893  -0.00002 -0.01332 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.25203 0.29331 0.18318 0.07623  -0.00170 -0.02133 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.25840 0.30853 0.19094 0.07970  -0.00782 -0.01871 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.21753 0.23520 0.19407 0.05222  0.02823  0.04272  144 VAL A N   
990  C CA  . VAL A 137 ? 0.22642 0.24250 0.21175 0.05126  0.03693  0.06385  144 VAL A CA  
991  C C   . VAL A 137 ? 0.23305 0.22890 0.23766 0.03863  0.03491  0.06702  144 VAL A C   
992  O O   . VAL A 137 ? 0.24462 0.23348 0.26017 0.03644  0.03923  0.08444  144 VAL A O   
993  C CB  . VAL A 137 ? 0.23336 0.26198 0.22135 0.05082  0.04454  0.07130  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.26099 0.31011 0.22658 0.06825  0.04667  0.06928  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.19387 0.21597 0.19229 0.03876  0.04104  0.05845  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.24153 0.22785 0.25077 0.03098  0.02788  0.05077  145 ALA A N   
997  C CA  . ALA A 138 ? 0.21599 0.18416 0.24076 0.02123  0.02433  0.04952  145 ALA A CA  
998  C C   . ALA A 138 ? 0.23706 0.19637 0.25803 0.02632  0.01820  0.04192  145 ALA A C   
999  O O   . ALA A 138 ? 0.24584 0.21489 0.25746 0.03078  0.01490  0.03028  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.19618 0.16334 0.22791 0.01118  0.02175  0.03786  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.20039 0.14151 0.23043 0.02585  0.01600  0.04859  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.24889 0.18049 0.27598 0.03223  0.00949  0.03936  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.27320 0.19924 0.30543 0.02641  0.00395  0.02334  146 GLU A C   
1004 O O   . GLU A 139 ? 0.27384 0.20202 0.30087 0.03315  -0.00015 0.01255  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.28670 0.19714 0.31989 0.03673  0.00772  0.05165  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.36811 0.26128 0.42010 0.02540  0.00823  0.06352  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.70330 0.57352 0.76328 0.02922  0.00652  0.07941  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.68985 0.53489 0.76727 0.02137  -0.00037 0.07928  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.65576 0.53204 0.70480 0.04054  0.01093  0.09180  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.23307 0.15534 0.27502 0.01562  0.00398  0.02224  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.21227 0.13178 0.25684 0.01154  -0.00117 0.00788  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.16966 0.09841 0.21872 0.00188  0.00184  0.00819  147 LYS A C   
1013 O O   . LYS A 140 ? 0.19723 0.12673 0.25428 -0.00328 0.00576  0.01980  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.24573 0.14142 0.29997 0.01135  -0.00931 0.00432  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.25309 0.14651 0.30762 0.01004  -0.01600 -0.01168 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.32744 0.19496 0.38838 0.01408  -0.02671 -0.01854 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.45607 0.31117 0.53246 0.00350  -0.03431 -0.02205 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.53370 0.36335 0.61919 0.00380  -0.04387 -0.02276 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.15723 0.09516 0.20132 0.00059  0.00073  -0.00283 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.19331 0.13876 0.24031 -0.00666 0.00261  -0.00347 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.23635 0.17833 0.28506 -0.00825 -0.00321 -0.01422 148 VAL A C   
1022 O O   . VAL A 141 ? 0.17566 0.12099 0.21655 -0.00241 -0.00524 -0.02273 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.23196 0.19228 0.26970 -0.00571 0.00693  -0.00453 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.18677 0.15175 0.22683 -0.01129 0.00811  -0.00528 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.15944 0.12493 0.19216 -0.00110 0.01089  0.00334  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.18061 0.11919 0.23959 -0.01485 -0.00595 -0.01355 149 THR A N   
1027 C CA  . THR A 142 ? 0.20422 0.14237 0.26340 -0.01527 -0.01246 -0.02422 149 THR A CA  
1028 C C   . THR A 142 ? 0.19988 0.15097 0.25821 -0.01921 -0.00897 -0.02225 149 THR A C   
1029 O O   . THR A 142 ? 0.22737 0.18241 0.29402 -0.02417 -0.00536 -0.01362 149 THR A O   
1030 C CB  . THR A 142 ? 0.19962 0.12248 0.27375 -0.01930 -0.02200 -0.02733 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.27978 0.18580 0.35619 -0.01548 -0.02559 -0.02712 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.20546 0.12877 0.27580 -0.01611 -0.03108 -0.04198 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.16362 0.12251 0.21171 -0.01559 -0.00954 -0.02894 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.15997 0.12848 0.20603 -0.01769 -0.00714 -0.02683 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.17348 0.14404 0.21865 -0.01537 -0.01450 -0.03514 150 VAL A C   
1036 O O   . VAL A 143 ? 0.22626 0.19974 0.26082 -0.00834 -0.01679 -0.04220 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.19968 0.17590 0.23512 -0.01566 -0.00107 -0.02420 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.15425 0.13575 0.18775 -0.01693 0.00040  -0.02127 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.16969 0.14469 0.20511 -0.01651 0.00342  -0.01919 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.15573 0.12799 0.21185 -0.01981 -0.01840 -0.03437 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.14951 0.12676 0.20480 -0.01696 -0.02677 -0.04272 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.22666 0.21556 0.27558 -0.01533 -0.02211 -0.03727 151 ILE A C   
1043 O O   . ILE A 144 ? 0.15940 0.15108 0.21506 -0.01928 -0.01692 -0.02896 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.23477 0.20763 0.31052 -0.02353 -0.03661 -0.04612 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.31821 0.27500 0.40510 -0.02777 -0.03935 -0.04576 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.28763 0.26426 0.36054 -0.01833 -0.04904 -0.05960 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.29837 0.24393 0.37404 -0.01939 -0.04656 -0.05872 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.16310 0.15922 0.19822 -0.00780 -0.02390 -0.04126 152 THR A N   
1049 C CA  . THR A 145 ? 0.17249 0.17636 0.20078 -0.00553 -0.01904 -0.03377 152 THR A CA  
1050 C C   . THR A 145 ? 0.21499 0.22911 0.23382 0.00291  -0.02547 -0.03892 152 THR A C   
1051 O O   . THR A 145 ? 0.21048 0.22728 0.22130 0.00959  -0.03142 -0.04842 152 THR A O   
1052 C CB  . THR A 145 ? 0.22669 0.22890 0.24560 -0.00529 -0.00955 -0.02568 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.23099 0.23393 0.24764 -0.00505 -0.00578 -0.01745 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.18565 0.19495 0.19171 0.00162  -0.00848 -0.02755 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.16106 0.18148 0.17945 0.00473  -0.02486 -0.03323 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.20973 0.24194 0.21734 0.01451  -0.03050 -0.03581 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.20910 0.24284 0.20899 0.01784  -0.02330 -0.02274 153 LYS A C   
1058 O O   . LYS A 146 ? 0.20791 0.23875 0.21696 0.01461  -0.02165 -0.01792 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.19721 0.23649 0.21791 0.01403  -0.04287 -0.04542 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.19868 0.25273 0.20764 0.02589  -0.05028 -0.04882 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.28770 0.34686 0.27760 0.03717  -0.05538 -0.05843 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.21122 0.28762 0.18755 0.05128  -0.06438 -0.06315 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.21290 0.29608 0.17579 0.05819  -0.05474 -0.04614 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.21644 0.25482 0.20000 0.02511  -0.01886 -0.01616 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.19179 0.22909 0.16782 0.02879  -0.01287 -0.00181 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.26411 0.31634 0.22727 0.04191  -0.01857 -0.00185 154 HIS A C   
1067 O O   . HIS A 147 ? 0.24528 0.30984 0.20004 0.04946  -0.02505 -0.01207 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.23130 0.26510 0.20183 0.02612  -0.00304 0.00949  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.28518 0.31175 0.25300 0.02639  0.00285  0.02621  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.25861 0.29426 0.21366 0.03672  0.00387  0.03688  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.26140 0.27072 0.23777 0.01815  0.00697  0.03410  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.33358 0.35570 0.29117 0.03370  0.00877  0.05221  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.29692 0.30201 0.26778 0.02227  0.00984  0.04945  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.24448 0.29526 0.20509 0.04647  -0.01751 0.00829  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.23630 0.30277 0.18378 0.06069  -0.02353 0.00905  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.26913 0.34906 0.19633 0.07125  -0.02034 0.01405  155 ASN A C   
1077 O O   . ASN A 148 ? 0.28765 0.38526 0.20151 0.08484  -0.02821 0.00731  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.25373 0.31417 0.19968 0.06567  -0.02135 0.02240  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.30376 0.36240 0.26604 0.06274  -0.02702 0.01520  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.33021 0.39913 0.30456 0.05924  -0.03493 0.00118  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.30703 0.35338 0.27084 0.06492  -0.02334 0.02541  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.29745 0.37248 0.22234 0.06638  -0.00926 0.02574  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.29743 0.38996 0.20412 0.07735  -0.00311 0.03546  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.40667 0.51045 0.30866 0.08012  -0.00457 0.02155  156 ASP A C   
1085 O O   . ASP A 149 ? 0.36121 0.48299 0.24848 0.09018  0.00224  0.02956  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.34554 0.43054 0.25543 0.07078  0.01027  0.05992  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.41292 0.48446 0.32414 0.07154  0.01104  0.07496  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.39365 0.47064 0.29693 0.08239  0.00309  0.06981  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.51239 0.56714 0.43378 0.06157  0.01830  0.09106  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.31651 0.41098 0.23066 0.07272  -0.01289 0.00220  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.25881 0.35869 0.16947 0.07575  -0.01516 -0.01147 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.35491 0.44790 0.27393 0.07453  -0.03082 -0.03480 157 ASP A C   
1093 O O   . ASP A 150 ? 0.31966 0.40823 0.24872 0.07066  -0.03877 -0.03888 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.28484 0.37493 0.20782 0.06291  -0.00502 -0.00453 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.33300 0.43839 0.24555 0.07192  -0.00095 -0.00777 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.34391 0.46323 0.23974 0.08823  -0.00819 -0.02061 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.34070 0.44547 0.26185 0.06389  0.00865  0.00150  157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.30132 0.39391 0.21796 0.07803  -0.03557 -0.04949 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.31016 0.39197 0.23805 0.07513  -0.05120 -0.07100 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.22716 0.28832 0.17832 0.05684  -0.04816 -0.06967 158 GLU A C   
1101 O O   . GLU A 151 ? 0.25848 0.31486 0.21409 0.04858  -0.03523 -0.05539 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.37725 0.46615 0.28856 0.09135  -0.06005 -0.08917 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.43523 0.54853 0.31901 0.11378  -0.06382 -0.09229 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.73867 0.85881 0.62307 0.11569  -0.07264 -0.09240 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.78455 0.92395 0.65027 0.13013  -0.06766 -0.08241 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 0.78827 0.89582 0.69504 0.10295  -0.08339 -0.10064 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.26702 0.31639 0.23397 0.05071  -0.06106 -0.08435 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.23174 0.26335 0.22034 0.03491  -0.05845 -0.08165 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.26025 0.28347 0.24384 0.03758  -0.05554 -0.08605 159 GLN A C   
1110 O O   . GLN A 152 ? 0.24426 0.26714 0.21791 0.04898  -0.06505 -0.10144 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.23301 0.25665 0.24425 0.02612  -0.07258 -0.09183 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.25097 0.26108 0.28589 0.00973  -0.06744 -0.08321 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.31822 0.32909 0.37971 -0.00079 -0.07724 -0.08514 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.30050 0.32572 0.36559 -0.00021 -0.07846 -0.08165 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.29587 0.29233 0.37792 -0.01035 -0.08429 -0.08937 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.18864 0.20558 0.17849 0.02875  -0.04353 -0.07384 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.24738 0.25965 0.23315 0.03175  -0.03938 -0.07563 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.25623 0.25138 0.26011 0.01903  -0.03775 -0.07181 160 TYR A C   
1119 O O   . TYR A 153 ? 0.23342 0.22504 0.25023 0.00807  -0.03457 -0.06296 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.20406 0.23165 0.17772 0.03598  -0.02561 -0.06286 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.24353 0.29114 0.19663 0.05251  -0.02549 -0.06561 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.29307 0.34782 0.23382 0.06685  -0.02794 -0.07627 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.28098 0.34165 0.22552 0.05607  -0.02268 -0.05692 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.31338 0.39082 0.23279 0.08504  -0.02692 -0.07832 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.33912 0.42125 0.26278 0.07321  -0.02156 -0.05720 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.39171 0.48366 0.30244 0.08796  -0.02330 -0.06793 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.45454 0.57203 0.34213 0.10794  -0.02122 -0.06779 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.20510 0.19134 0.20817 0.02288  -0.03960 -0.07803 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.21439 0.18547 0.23117 0.01402  -0.03742 -0.07310 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.23521 0.21233 0.24387 0.01870  -0.02807 -0.06802 161 ALA A C   
1131 O O   . ALA A 154 ? 0.22131 0.20354 0.21862 0.03111  -0.02984 -0.07610 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.23844 0.18952 0.26562 0.01398  -0.05068 -0.08475 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.18941 0.16797 0.20407 0.01008  -0.01900 -0.05561 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.19535 0.17972 0.20749 0.01188  -0.01177 -0.05045 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.21334 0.18210 0.23438 0.00868  -0.01358 -0.04910 162 TRP A C   
1136 O O   . TRP A 155 ? 0.21405 0.17226 0.24541 0.00063  -0.01516 -0.04488 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.19513 0.19041 0.20811 0.00501  -0.00309 -0.03912 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.18816 0.19118 0.20292 0.00375  0.00282  -0.03341 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.14309 0.16404 0.15582 0.00567  0.00813  -0.02894 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.20410 0.20005 0.22473 -0.00000 0.00358  -0.03053 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.14800 0.17300 0.16717 0.00226  0.01057  -0.02521 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.18405 0.19369 0.20593 0.00001  0.00754  -0.02698 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.17050 0.15234 0.19605 -0.00282 0.00143  -0.02935 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.19943 0.20831 0.22516 -0.00149 0.00772  -0.02504 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.16740 0.14907 0.19452 -0.00307 0.00346  -0.02536 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.14992 0.14462 0.17605 -0.00182 0.00574  -0.02459 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.17780 0.14732 0.19531 0.01600  -0.01284 -0.05114 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.16941 0.12360 0.19372 0.01499  -0.01461 -0.04827 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.16463 0.12886 0.18476 0.02137  -0.01005 -0.04572 163 GLU A C   
1150 O O   . GLU A 156 ? 0.18678 0.16563 0.19989 0.03040  -0.00887 -0.05066 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.22772 0.16121 0.25524 0.01990  -0.02520 -0.05758 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.26220 0.17589 0.30059 0.01608  -0.02722 -0.05043 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.50982 0.39898 0.55864 0.01485  -0.03938 -0.05742 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.45142 0.32948 0.49402 0.02649  -0.04780 -0.07019 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.44356 0.32535 0.50798 0.00274  -0.04128 -0.05067 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.21926 0.17856 0.24386 0.01804  -0.00761 -0.03766 164 SER A N   
1157 C CA  . SER A 157 ? 0.16898 0.13821 0.19061 0.02504  -0.00528 -0.03604 164 SER A CA  
1158 C C   . SER A 157 ? 0.17016 0.12708 0.19459 0.02534  -0.00553 -0.02831 164 SER A C   
1159 O O   . SER A 157 ? 0.19640 0.14925 0.22445 0.01769  -0.00299 -0.02038 164 SER A O   
1160 C CB  . SER A 157 ? 0.15917 0.15100 0.18089 0.02079  0.00023  -0.03276 164 SER A CB  
1161 O OG  . SER A 157 ? 0.18540 0.18989 0.20719 0.02733  0.00084  -0.03216 164 SER A OG  
1162 N N   . SER A 158 ? 0.21708 0.17031 0.23878 0.03619  -0.00808 -0.02974 165 SER A N   
1163 C CA  . SER A 158 ? 0.25300 0.19986 0.27466 0.03970  -0.00741 -0.02061 165 SER A CA  
1164 C C   . SER A 158 ? 0.25748 0.22735 0.27493 0.04513  -0.00499 -0.02007 165 SER A C   
1165 O O   . SER A 158 ? 0.27187 0.24078 0.28628 0.05413  -0.00612 -0.01575 165 SER A O   
1166 C CB  . SER A 158 ? 0.27023 0.19385 0.29272 0.04890  -0.01334 -0.02119 165 SER A CB  
1167 O OG  . SER A 158 ? 0.29687 0.19794 0.32756 0.04164  -0.01778 -0.02162 165 SER A OG  
1168 N N   . ALA A 159 ? 0.18030 0.17068 0.19910 0.03953  -0.00253 -0.02376 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.21124 0.22641 0.23155 0.04185  -0.00212 -0.02488 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.23711 0.26261 0.25696 0.05493  -0.00382 -0.02971 166 ALA A C   
1171 O O   . ALA A 159 ? 0.30975 0.32946 0.32749 0.05977  -0.00435 -0.03507 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.25101 0.26770 0.26845 0.04243  -0.00292 -0.01950 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.22944 0.27186 0.25050 0.06274  -0.00547 -0.02912 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.25442 0.31036 0.27558 0.07713  -0.00666 -0.03369 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.24074 0.32421 0.26893 0.07593  -0.00309 -0.03741 167 GLY A C   
1176 O O   . GLY A 160 ? 0.27124 0.36760 0.29796 0.09007  -0.00288 -0.04179 167 GLY A O   
1177 N N   . GLY A 161 ? 0.20512 0.29837 0.24068 0.06076  0.00008  -0.03473 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.18672 0.31044 0.23241 0.05764  0.00463  -0.03343 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.15632 0.27732 0.19622 0.05812  0.00893  -0.03473 168 GLY A C   
1180 O O   . GLY A 161 ? 0.17072 0.31980 0.21810 0.05701  0.01437  -0.03082 168 GLY A O   
1181 N N   . SER A 162 ? 0.15748 0.24808 0.18551 0.05991  0.00642  -0.03920 169 SER A N   
1182 C CA  . SER A 162 ? 0.18183 0.27078 0.20240 0.06305  0.00829  -0.04288 169 SER A CA  
1183 C C   . SER A 162 ? 0.18273 0.24167 0.19889 0.05332  0.00530  -0.04382 169 SER A C   
1184 O O   . SER A 162 ? 0.18614 0.22302 0.20319 0.04824  0.00186  -0.04243 169 SER A O   
1185 C CB  . SER A 162 ? 0.22241 0.31136 0.23225 0.08380  0.00546  -0.05280 169 SER A CB  
1186 O OG  . SER A 162 ? 0.22415 0.27806 0.22772 0.08886  -0.00250 -0.05915 169 SER A OG  
1187 N N   . PHE A 163 ? 0.18687 0.24874 0.19860 0.05175  0.00711  -0.04495 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.16711 0.20498 0.17523 0.04506  0.00332  -0.04742 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.17355 0.21335 0.17063 0.05621  0.00063  -0.05643 170 PHE A C   
1190 O O   . PHE A 163 ? 0.17560 0.24002 0.16702 0.06737  0.00464  -0.05752 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.17047 0.20959 0.18488 0.02928  0.00715  -0.03853 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.14246 0.20587 0.15841 0.02696  0.01356  -0.03201 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.16114 0.24625 0.18777 0.02240  0.01829  -0.02414 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.20132 0.26650 0.20976 0.02884  0.01435  -0.03243 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.17574 0.28293 0.20781 0.01833  0.02469  -0.01454 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.13974 0.22749 0.14957 0.02721  0.02134  -0.02284 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.19381 0.30190 0.21668 0.02104  0.02702  -0.01267 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.17773 0.19382 0.17223 0.05412  -0.00667 -0.06302 171 THR A N   
1199 C CA  . THR A 164 ? 0.19406 0.21023 0.17729 0.06487  -0.01216 -0.07420 171 THR A CA  
1200 C C   . THR A 164 ? 0.18664 0.20252 0.17026 0.05496  -0.01190 -0.07071 171 THR A C   
1201 O O   . THR A 164 ? 0.18961 0.19546 0.18323 0.04024  -0.01047 -0.06278 171 THR A O   
1202 C CB  . THR A 164 ? 0.22811 0.21611 0.20925 0.07315  -0.02498 -0.08859 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.23464 0.19718 0.22877 0.05813  -0.02959 -0.08468 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.24346 0.22951 0.22242 0.08611  -0.02609 -0.09248 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.21445 0.24365 0.18547 0.06558  -0.01323 -0.07670 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.21932 0.24891 0.18774 0.06058  -0.01509 -0.07559 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.26482 0.29030 0.22005 0.07571  -0.02688 -0.09336 172 VAL A C   
1208 O O   . VAL A 165 ? 0.25303 0.29186 0.19400 0.09410  -0.02759 -0.10194 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.24765 0.30349 0.21272 0.05839  -0.00335 -0.06080 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.23972 0.29561 0.19945 0.05674  -0.00619 -0.06000 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.18886 0.24526 0.16852 0.04298  0.00496  -0.04619 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.23448 0.24339 0.19487 0.06914  -0.03696 -0.09978 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.26341 0.26693 0.21332 0.08223  -0.05157 -0.11901 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.34080 0.34399 0.29527 0.07388  -0.05687 -0.11831 173 ARG A C   
1215 O O   . ARG A 166 ? 0.24618 0.24478 0.21576 0.05695  -0.05171 -0.10539 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.30577 0.28219 0.26703 0.08135  -0.06423 -0.12852 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.35459 0.30656 0.33922 0.06175  -0.06964 -0.12460 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.46100 0.38893 0.45779 0.05938  -0.07681 -0.12604 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.49069 0.41551 0.48715 0.06000  -0.06750 -0.11881 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.61563 0.52397 0.61596 0.06330  -0.07128 -0.11941 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.48652 0.37812 0.49182 0.06560  -0.08427 -0.12724 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.59793 0.50679 0.59742 0.06515  -0.06254 -0.11237 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.32298 0.33399 0.26566 0.08664  -0.06660 -0.12960 174 THR A N   
1224 C CA  . THR A 167 ? 0.33625 0.34633 0.28482 0.08076  -0.07527 -0.13240 174 THR A CA  
1225 C C   . THR A 167 ? 0.38157 0.36575 0.35719 0.06410  -0.08544 -0.13492 174 THR A C   
1226 O O   . THR A 167 ? 0.43982 0.40719 0.42401 0.06470  -0.09278 -0.14065 174 THR A O   
1227 C CB  . THR A 167 ? 0.39623 0.42033 0.33060 0.09855  -0.08387 -0.14191 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.46429 0.51731 0.37651 0.11120  -0.07195 -0.13275 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.64294 0.66166 0.58918 0.09247  -0.09680 -0.14835 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.28713 0.27000 0.27709 0.04941  -0.08506 -0.12836 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.38589 0.35075 0.40432 0.03261  -0.09118 -0.12507 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.47567 0.44121 0.50281 0.03375  -0.10559 -0.13429 175 ASP A C   
1233 O O   . ASP A 168 ? 0.46771 0.44920 0.48991 0.03670  -0.10823 -0.13604 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.35553 0.32327 0.38840 0.01701  -0.08157 -0.10988 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.51093 0.46482 0.57305 0.00085  -0.08506 -0.10324 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.48278 0.42034 0.55161 -0.00093 -0.08636 -0.10220 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.40401 0.36635 0.48185 -0.00885 -0.08521 -0.09661 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.53858 0.48696 0.57863 0.03204  -0.11553 -0.14024 176 THR A N   
1239 C CA  . THR A 169 ? 0.75173 0.69756 0.80461 0.03129  -0.13075 -0.14983 176 THR A CA  
1240 C C   . THR A 169 ? 0.71509 0.65396 0.79953 0.01086  -0.13239 -0.13967 176 THR A C   
1241 O O   . THR A 169 ? 0.78416 0.72132 0.88404 0.00735  -0.14506 -0.14629 176 THR A O   
1242 C CB  . THR A 169 ? 0.78916 0.72044 0.83832 0.04262  -0.14284 -0.16364 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.70621 0.62070 0.75827 0.03923  -0.13714 -0.15741 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.62560 0.57242 0.64552 0.06615  -0.14522 -0.17615 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.75109 0.68808 0.84577 -0.00182 -0.11969 -0.12333 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.60473 0.54022 0.72843 -0.01954 -0.11823 -0.11029 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.46075 0.41648 0.59452 -0.02474 -0.11989 -0.10804 177 GLY A C   
1248 O O   . GLY A 170 ? 0.51274 0.48088 0.63238 -0.01424 -0.12631 -0.11932 177 GLY A O   
1249 N N   . GLU A 171 ? 0.55531 0.51696 0.71271 -0.03933 -0.11363 -0.09256 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.43536 0.41883 0.60661 -0.04468 -0.11516 -0.08889 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.35971 0.36027 0.51192 -0.03593 -0.10921 -0.08972 178 GLU A C   
1252 O O   . GLU A 171 ? 0.29534 0.29484 0.43858 -0.03553 -0.09708 -0.08151 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.48252 0.47224 0.68108 -0.05988 -0.10633 -0.06953 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.43269 0.44661 0.65225 -0.06647 -0.10940 -0.06512 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.40331 0.41434 0.64253 -0.07239 -0.12481 -0.07314 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.40620 0.39433 0.64656 -0.07287 -0.13262 -0.07994 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.53329 0.56584 0.78802 -0.07619 -0.12984 -0.07287 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.42846 0.44450 0.57322 -0.02777 -0.11808 -0.09968 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.38321 0.41652 0.50979 -0.01828 -0.11322 -0.09890 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.49166 0.53766 0.63313 -0.02640 -0.10092 -0.08180 179 PRO A C   
1261 O O   . PRO A 172 ? 0.41062 0.46404 0.58005 -0.03801 -0.09997 -0.07260 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.40162 0.45083 0.52355 -0.00937 -0.12565 -0.10943 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.52006 0.55325 0.63973 -0.00605 -0.13714 -0.12348 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.56025 0.57377 0.70256 -0.02110 -0.13393 -0.11581 179 PRO A CD  
1265 N N   . MET A 173 ? 0.23951 0.28682 0.35507 -0.01750 -0.08591 -0.07265 180 MET A N   
1266 C CA  . MET A 173 ? 0.27888 0.33281 0.39805 -0.02044 -0.07055 -0.05552 180 MET A CA  
1267 C C   . MET A 173 ? 0.33429 0.40569 0.44522 -0.01132 -0.06832 -0.05092 180 MET A C   
1268 O O   . MET A 173 ? 0.40101 0.48024 0.51923 -0.01251 -0.05890 -0.03919 180 MET A O   
1269 C CB  . MET A 173 ? 0.30050 0.33971 0.40003 -0.01826 -0.05628 -0.04814 180 MET A CB  
1270 C CG  . MET A 173 ? 0.59013 0.61273 0.69656 -0.02562 -0.05563 -0.04921 180 MET A CG  
1271 S SD  . MET A 173 ? 0.57791 0.58977 0.66331 -0.02227 -0.03973 -0.04031 180 MET A SD  
1272 C CE  . MET A 173 ? 0.38552 0.40859 0.47133 -0.02105 -0.02898 -0.02730 180 MET A CE  
1273 N N   . GLY A 174 ? 0.28125 0.35899 0.37505 -0.00006 -0.07637 -0.05941 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.27608 0.36756 0.35871 0.01062  -0.07361 -0.05314 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.22742 0.30758 0.28514 0.01742  -0.05933 -0.04213 181 GLY A C   
1276 O O   . GLY A 174 ? 0.22734 0.30834 0.26235 0.02846  -0.05929 -0.04174 181 GLY A O   
1277 N N   . ARG A 175 ? 0.16176 0.23219 0.22451 0.01103  -0.04769 -0.03262 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.16547 0.22197 0.20997 0.01433  -0.03599 -0.02347 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.22546 0.27284 0.27962 0.00622  -0.02736 -0.01826 182 ARG A C   
1280 O O   . ARG A 175 ? 0.20525 0.26194 0.27667 0.00304  -0.02686 -0.01592 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.15604 0.21584 0.18942 0.02496  -0.03353 -0.01541 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.20031 0.24292 0.21689 0.02728  -0.02408 -0.00587 182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.16746 0.20627 0.17966 0.03557  -0.02143 0.00280  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.17781 0.22054 0.20426 0.03470  -0.02014 0.00192  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.21624 0.27611 0.25194 0.04137  -0.02440 0.00134  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.18987 0.26315 0.22204 0.04921  -0.03177 0.00032  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.15537 0.22238 0.20401 0.04158  -0.02116 0.00208  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.27506 0.26524 0.12217 0.09003  -0.02575 0.00699  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.23623 0.22642 0.12234 0.07033  -0.02009 0.00660  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.28676 0.26584 0.18252 0.05773  -0.01346 0.00081  183 GLY A C   
1291 O O   . GLY A 176 ? 0.26431 0.23118 0.13693 0.06700  -0.00618 0.00096  183 GLY A O   
1292 N N   . THR A 177 ? 0.20964 0.19401 0.13744 0.03968  -0.01514 -0.00331 184 THR A N   
1293 C CA  . THR A 177 ? 0.20277 0.18070 0.14326 0.03004  -0.00904 -0.00641 184 THR A CA  
1294 C C   . THR A 177 ? 0.26288 0.24882 0.22354 0.01396  -0.02216 -0.01684 184 THR A C   
1295 O O   . THR A 177 ? 0.22752 0.22617 0.20514 0.00627  -0.02856 -0.01715 184 THR A O   
1296 C CB  . THR A 177 ? 0.25559 0.23026 0.21555 0.02547  0.00879  0.00543  184 THR A CB  
1297 O OG1 . THR A 177 ? 0.27497 0.23964 0.21615 0.03903  0.02438  0.01769  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.26338 0.24204 0.24151 0.01747  0.01296  0.00357  184 THR A CG2 
1299 N N   . LYS A 178 ? 0.20419 0.18018 0.16021 0.01128  -0.02377 -0.02384 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.19945 0.17509 0.16987 -0.00289 -0.03301 -0.03136 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.22765 0.19770 0.20968 -0.00294 -0.02257 -0.02699 185 LYS A C   
1302 O O   . LYS A 178 ? 0.23136 0.18934 0.19821 0.00877  -0.01439 -0.02649 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.26970 0.23181 0.21772 -0.00508 -0.04657 -0.04472 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.34033 0.29290 0.29840 -0.02076 -0.05403 -0.05145 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.43842 0.37984 0.37815 -0.02719 -0.06419 -0.06310 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.48429 0.44220 0.41000 -0.02162 -0.07368 -0.06643 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.77254 0.71673 0.67498 -0.02513 -0.08090 -0.07847 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.17756 0.15903 0.18472 -0.01330 -0.02259 -0.02323 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.12394 0.10772 0.14428 -0.01274 -0.01626 -0.01857 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.18678 0.15957 0.20620 -0.01881 -0.02359 -0.02295 186 VAL A C   
1311 O O   . VAL A 179 ? 0.18457 0.16401 0.21431 -0.03023 -0.03011 -0.02363 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.14499 0.14778 0.18931 -0.01969 -0.01251 -0.01185 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.14105 0.15497 0.20079 -0.01874 -0.00998 -0.00726 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.15834 0.16420 0.20291 -0.01638 -0.00294 -0.00605 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.17971 0.13272 0.18440 -0.00963 -0.02037 -0.02469 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.19885 0.13062 0.19739 -0.01396 -0.02455 -0.02721 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.20067 0.14136 0.21193 -0.00541 -0.01798 -0.01714 187 ILE A C   
1318 O O   . ILE A 180 ? 0.21973 0.16347 0.22895 0.01098  -0.00906 -0.01254 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.21637 0.11005 0.18280 -0.00821 -0.02601 -0.03749 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.26267 0.15616 0.21657 -0.01597 -0.03605 -0.04807 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.25447 0.11712 0.21319 -0.01584 -0.02902 -0.03936 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.33686 0.19622 0.25200 -0.00603 -0.03765 -0.06036 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.16799 0.11760 0.19248 -0.01457 -0.02208 -0.01254 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.15752 0.11995 0.19217 -0.00590 -0.01926 -0.00268 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.23031 0.15878 0.24700 -0.00005 -0.01746 0.00026  188 LEU A C   
1326 O O   . LEU A 181 ? 0.25288 0.16531 0.26506 -0.01332 -0.02101 -0.00038 188 LEU A O   
1327 C CB  . LEU A 181 ? 0.19009 0.18005 0.24255 -0.01659 -0.02469 0.00057  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.21424 0.22707 0.28044 -0.02467 -0.02611 -0.00301 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.27504 0.30412 0.34933 -0.03325 -0.03154 -0.00229 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.18538 0.21645 0.26360 -0.01697 -0.02051 0.00040  188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.19918 0.11578 0.20568 0.02061  -0.01007 0.00498  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.24228 0.11986 0.22780 0.03084  -0.00593 0.01011  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.22113 0.12571 0.22055 0.03893  -0.00686 0.02440  189 HIS A C   
1334 O O   . HIS A 182 ? 0.24848 0.18319 0.25982 0.05758  -0.00428 0.03254  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.27218 0.11991 0.23427 0.05440  0.00387  0.00834  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.35761 0.18528 0.30217 0.04950  0.00349  -0.00667 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.42488 0.19605 0.33589 0.04383  0.00168  -0.01912 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.29765 0.15311 0.25094 0.04887  0.00389  -0.01115 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.45766 0.22629 0.35584 0.04181  -0.00087 -0.03172 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.37379 0.19250 0.29645 0.04634  0.00179  -0.02562 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.22950 0.12846 0.22827 0.02513  -0.01085 0.02806  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.25058 0.18290 0.26074 0.02950  -0.01491 0.03895  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.29145 0.21363 0.28866 0.05553  -0.00988 0.05367  190 LEU A C   
1344 O O   . LEU A 183 ? 0.31799 0.19063 0.29095 0.06550  -0.00128 0.05730  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.21090 0.13886 0.21915 0.01067  -0.01747 0.04017  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.19010 0.13774 0.21302 -0.01035 -0.02259 0.02882  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.26393 0.21086 0.28482 -0.02340 -0.02166 0.03346  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.24482 0.23400 0.28546 -0.00848 -0.02865 0.02459  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.22377 0.19226 0.23569 0.06685  -0.01617 0.06192  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.27040 0.23949 0.27090 0.09403  -0.01392 0.07869  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.33157 0.25947 0.30525 0.09195  -0.00940 0.08866  191 LYS A C   
1352 O O   . LYS A 184 ? 0.34877 0.27104 0.32189 0.06872  -0.01125 0.08398  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.27408 0.30997 0.29806 0.10170  -0.02640 0.08357  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.25935 0.34130 0.31514 0.10426  -0.02868 0.07848  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.33283 0.47789 0.41365 0.09886  -0.04386 0.07778  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.43379 0.61498 0.54743 0.08321  -0.04531 0.06719  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.31076 0.53503 0.44310 0.07226  -0.05797 0.06172  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.38140 0.28086 0.33259 0.11856  -0.00138 0.10468  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.46255 0.31532 0.38705 0.11413  0.00678  0.11409  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.52044 0.40017 0.44369 0.10772  0.00069  0.12325  192 GLU A C   
1361 O O   . GLU A 185 ? 0.51733 0.36488 0.42665 0.09217  0.00825  0.12838  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.58602 0.41852 0.49276 0.13793  0.01505  0.12215  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.78725 0.58779 0.67013 0.13883  0.02243  0.13563  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.04955 0.83644 0.91484 0.16734  0.03042  0.14546  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.03027 0.76895 0.87154 0.16769  0.04128  0.15412  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 0.89449 0.72031 0.77123 0.18890  0.02676  0.14525  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.39116 0.33238 0.32966 0.11643  -0.01310 0.12316  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.42967 0.39711 0.36046 0.11218  -0.02043 0.12783  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.33411 0.32984 0.28331 0.08467  -0.02906 0.11003  193 ASP A C   
1370 O O   . ASP A 186 ? 0.35458 0.37742 0.29663 0.08272  -0.03729 0.10962  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.43250 0.44572 0.36589 0.13044  -0.03171 0.12959  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.48927 0.55531 0.45604 0.12937  -0.04486 0.11697  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.57368 0.63671 0.55916 0.12135  -0.04222 0.10925  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.60839 0.71793 0.58306 0.13495  -0.05704 0.11480  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.27889 0.26576 0.24726 0.06508  -0.02689 0.09449  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.23202 0.24070 0.21686 0.04151  -0.03309 0.07775  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.24287 0.21869 0.22642 0.02075  -0.02293 0.07364  194 GLN A C   
1378 O O   . GLN A 187 ? 0.27244 0.25848 0.27175 0.00411  -0.02557 0.05969  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.23872 0.27612 0.25012 0.03752  -0.04082 0.06427  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.20658 0.28961 0.23003 0.05293  -0.05265 0.06753  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.25613 0.36942 0.27132 0.05155  -0.06591 0.06638  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.28539 0.39632 0.29560 0.03460  -0.06808 0.05578  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.26250 0.40252 0.27342 0.07067  -0.07452 0.07569  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.35078 0.28841 0.31679 0.02115  -0.01125 0.08680  195 THR A N   
1385 C CA  . THR A 188 ? 0.41517 0.32748 0.38600 -0.00193 -0.00290 0.08357  195 THR A CA  
1386 C C   . THR A 188 ? 0.26570 0.20178 0.24130 -0.01476 -0.00113 0.08339  195 THR A C   
1387 O O   . THR A 188 ? 0.32942 0.25746 0.31579 -0.03422 0.00518  0.08176  195 THR A O   
1388 C CB  . THR A 188 ? 0.38460 0.24423 0.33713 -0.00192 0.01010  0.09796  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.42578 0.28176 0.35694 0.01268  0.01704  0.11821  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.36757 0.19428 0.31067 0.01252  0.01064  0.09580  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.30635 0.27280 0.27341 -0.00367 -0.00680 0.08459  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.31552 0.30218 0.28220 -0.01172 -0.00385 0.08219  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.30966 0.31149 0.29931 -0.02663 -0.00820 0.06467  196 GLU A C   
1394 O O   . GLU A 189 ? 0.23661 0.24924 0.23116 -0.03485 -0.00170 0.06404  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.28607 0.29715 0.23214 0.00410  -0.01187 0.08228  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.26679 0.30337 0.22322 0.00518  -0.02905 0.06417  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.40109 0.46014 0.33552 0.01897  -0.04106 0.06313  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.42639 0.49070 0.35151 0.03479  -0.04675 0.07355  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.37128 0.44188 0.29522 0.01546  -0.04540 0.05148  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.26043 0.26474 0.26338 -0.02763 -0.01743 0.05243  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.26544 0.28081 0.28607 -0.03858 -0.02092 0.03797  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.23886 0.23950 0.27245 -0.05256 -0.01615 0.03698  197 TYR A C   
1403 O O   . TYR A 190 ? 0.25262 0.26127 0.29887 -0.05886 -0.02008 0.02616  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.23266 0.25809 0.26092 -0.03393 -0.03084 0.02760  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.14775 0.19321 0.16715 -0.02523 -0.03915 0.02624  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.22665 0.28319 0.23777 -0.02790 -0.04166 0.01866  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.21369 0.26712 0.23066 -0.01309 -0.04513 0.03224  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.22128 0.29315 0.21993 -0.02243 -0.05215 0.01419  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.23046 0.30860 0.24068 -0.00705 -0.05655 0.02982  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.21798 0.30352 0.21791 -0.01365 -0.06106 0.01941  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.23859 0.34545 0.22746 -0.01006 -0.07517 0.01368  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.24534 0.22342 0.27436 -0.05806 -0.00843 0.04813  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.22341 0.19070 0.26573 -0.07700 -0.00508 0.04728  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.24219 0.22606 0.29255 -0.08571 0.00537  0.05676  198 LEU A C   
1415 O O   . LEU A 191 ? 0.23775 0.22323 0.30043 -0.09463 0.00933  0.05002  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.26470 0.18878 0.29597 -0.07978 -0.00232 0.05063  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.27989 0.18489 0.30148 -0.06778 -0.00914 0.04190  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.35548 0.20893 0.35920 -0.06772 -0.00365 0.04609  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.31868 0.24172 0.35150 -0.07097 -0.01644 0.02397  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.24247 0.24038 0.28120 -0.07533 0.01153  0.06732  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.22146 0.23702 0.26541 -0.08076 0.02523  0.08045  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.27130 0.32389 0.32979 -0.07942 0.02437  0.07172  199 GLU A C   
1423 O O   . GLU A 192 ? 0.25026 0.31070 0.29825 -0.06618 0.01665  0.05987  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.30850 0.31901 0.32374 -0.06409 0.03397  0.09507  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.43572 0.40848 0.43264 -0.05997 0.03746  0.10822  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.81551 0.76229 0.82339 -0.07977 0.04900  0.11671  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.76337 0.72928 0.78689 -0.09127 0.05811  0.11601  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.93573 0.84168 0.93214 -0.08047 0.04821  0.11725  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.26257 0.33183 0.34085 -0.08758 0.03198  0.07273  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.20144 0.30434 0.29425 -0.08252 0.03195  0.06593  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.15735 0.27913 0.23218 -0.06608 0.03934  0.07143  200 GLU A C   
1432 O O   . GLU A 193 ? 0.21014 0.33651 0.27900 -0.05499 0.03222  0.05767  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.21456 0.33478 0.32954 -0.09122 0.04062  0.06971  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.25033 0.40441 0.38348 -0.08514 0.03847  0.06333  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.60329 0.78388 0.76127 -0.09344 0.04807  0.07070  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.47747 0.64929 0.63706 -0.10465 0.05885  0.08117  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.59128 0.80214 0.76746 -0.08878 0.04539  0.06715  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.25647 0.37635 0.31184 -0.05817 0.05285  0.08567  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.26675 0.39382 0.29239 -0.03569 0.05869  0.08294  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.26418 0.36859 0.26157 -0.02492 0.04201  0.06549  201 ARG A C   
1441 O O   . ARG A 194 ? 0.24512 0.35058 0.22239 -0.01104 0.04026  0.05377  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.26682 0.39579 0.27178 -0.02764 0.07705  0.10284  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.38245 0.48303 0.37350 -0.03257 0.07608  0.11451  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.48571 0.58503 0.45063 -0.02045 0.09437  0.13307  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.54461 0.61421 0.48044 -0.01384 0.09125  0.14253  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.51919 0.57842 0.42798 -0.00210 0.10210  0.15534  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.58120 0.65710 0.48869 0.00294  0.11809  0.16147  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.57109 0.60433 0.45406 0.00662  0.09661  0.16280  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.18690 0.27064 0.18278 -0.03120 0.03026  0.06367  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.22214 0.29402 0.20022 -0.02385 0.01397  0.04870  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.18339 0.25675 0.17787 -0.02884 0.00452  0.03185  202 ARG A C   
1452 O O   . ARG A 195 ? 0.19608 0.26524 0.17545 -0.02254 -0.00309 0.01820  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.25569 0.31165 0.23110 -0.02538 0.00651  0.05457  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.23308 0.28778 0.19812 -0.01898 -0.01056 0.04184  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.26070 0.32118 0.19153 -0.00494 -0.01474 0.04015  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.26991 0.33599 0.19566 -0.00165 -0.03325 0.03071  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.25475 0.32686 0.17219 -0.00325 -0.04610 0.01269  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.28193 0.34752 0.18844 -0.00440 -0.04155 0.00139  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.27815 0.36288 0.19897 -0.00378 -0.06352 0.00617  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.19389 0.27078 0.21659 -0.04067 0.00475  0.03259  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.19024 0.26788 0.22483 -0.04263 -0.00265 0.01949  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.15754 0.24618 0.18644 -0.03238 0.00410  0.01516  203 ILE A C   
1463 O O   . ILE A 196 ? 0.18595 0.26339 0.20407 -0.02674 -0.00087 0.00306  203 ILE A O   
1464 C CB  . ILE A 196 ? 0.20130 0.28085 0.26124 -0.05542 -0.00540 0.02079  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.18246 0.24143 0.24071 -0.06114 -0.01120 0.02248  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.17777 0.26001 0.24521 -0.05346 -0.01123 0.00990  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.22141 0.26924 0.29038 -0.06861 -0.00981 0.02222  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.18229 0.29175 0.21813 -0.02913 0.01719  0.02606  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.19270 0.31341 0.21976 -0.01326 0.02678  0.02384  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.23752 0.33472 0.22465 0.00053  0.02573  0.01285  204 LYS A C   
1471 O O   . LYS A 197 ? 0.21415 0.29876 0.18691 0.01145  0.02627  0.00188  204 LYS A O   
1472 C CB  . LYS A 197 ? 0.20794 0.36090 0.24885 -0.00985 0.04392  0.04033  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.28606 0.46963 0.36991 -0.02580 0.04459  0.05016  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.24204 0.45816 0.34004 -0.02337 0.06277  0.06732  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.56372 0.79869 0.69601 -0.03380 0.05745  0.06762  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.69221 0.90791 0.83715 -0.05312 0.04031  0.05800  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.19696 0.28577 0.16272 0.00083  0.02392  0.01552  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.25057 0.31892 0.17536 0.01189  0.01894  0.00277  205 GLU A CA  
1479 C C   . GLU A 198 ? 0.26027 0.30707 0.18294 0.00407  0.00241  -0.01536 205 GLU A C   
1480 O O   . GLU A 198 ? 0.26762 0.29318 0.16424 0.01082  0.00029  -0.03024 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.24566 0.31407 0.14919 0.01401  0.01684  0.01061  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.33956 0.39030 0.20042 0.02214  0.00480  -0.00490 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.31275 0.36831 0.15412 0.02603  -0.00053 0.00462  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.32061 0.38237 0.18567 0.01675  -0.00595 0.01467  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.32969 0.38092 0.12829 0.04116  0.00162  0.00276  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.20351 0.25292 0.15204 -0.01031 -0.00792 -0.01404 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.23148 0.26605 0.18309 -0.01925 -0.02110 -0.02781 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.17981 0.20174 0.13678 -0.01740 -0.01601 -0.03430 206 ILE A C   
1489 O O   . ILE A 199 ? 0.25508 0.25346 0.19715 -0.01926 -0.02067 -0.04770 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.18750 0.23104 0.16465 -0.03049 -0.02954 -0.02214 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.20401 0.25588 0.17015 -0.02787 -0.03538 -0.01564 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.22173 0.25658 0.20946 -0.04002 -0.03876 -0.03266 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.20533 0.26340 0.19299 -0.03231 -0.03756 -0.00519 206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.19012 0.22678 0.16767 -0.01407 -0.00690 -0.02451 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.19269 0.22104 0.17421 -0.00770 -0.00202 -0.02757 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.23733 0.24684 0.18791 0.00925  0.00704  -0.03461 207 VAL A C   
1497 O O   . VAL A 200 ? 0.27232 0.25174 0.20812 0.01297  0.00742  -0.04415 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.21943 0.27647 0.22981 -0.00692 0.00282  -0.01546 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.18705 0.24276 0.19720 0.00726  0.00928  -0.01561 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.15913 0.22092 0.19135 -0.02235 -0.00681 -0.01317 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.21770 0.24021 0.15461 0.02087  0.01631  -0.02945 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.25580 0.25777 0.15659 0.04136  0.02705  -0.03671 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.33249 0.29201 0.19570 0.03639  0.01649  -0.05653 208 LYS A C   
1504 O O   . LYS A 201 ? 0.42213 0.34431 0.25524 0.04712  0.02089  -0.06884 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.28679 0.31578 0.18061 0.05529  0.04119  -0.02482 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.38736 0.39697 0.23923 0.08184  0.05571  -0.03115 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.43550 0.47227 0.27679 0.09437  0.07039  -0.01819 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.57973 0.59560 0.37797 0.12247  0.08514  -0.02413 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.71561 0.76564 0.52109 0.13244  0.10051  -0.00507 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.30095 0.26502 0.16553 0.01989  0.00175  -0.06004 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.38991 0.32348 0.22265 0.01194  -0.01210 -0.07946 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.34511 0.25052 0.18702 -0.00399 -0.02026 -0.09087 209 LYS A C   
1513 O O   . LYS A 202 ? 0.40053 0.26839 0.21480 -0.00599 -0.02301 -0.10731 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.33814 0.29452 0.17424 0.00142  -0.02644 -0.07701 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.45108 0.38723 0.25504 -0.00701 -0.04446 -0.09723 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.48395 0.45169 0.29575 -0.01318 -0.05807 -0.09026 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.62994 0.59611 0.43015 -0.02584 -0.07068 -0.10266 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.70534 0.69840 0.50631 -0.02734 -0.08355 -0.09183 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.35746 0.28081 0.23978 -0.01592 -0.02242 -0.08089 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.41137 0.31539 0.30661 -0.03397 -0.02984 -0.08804 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.36256 0.25279 0.27054 -0.02853 -0.01813 -0.08093 210 HIS A C   
1522 O O   . HIS A 203 ? 0.38691 0.25652 0.30241 -0.03975 -0.01972 -0.08429 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.35122 0.29016 0.28380 -0.04844 -0.04175 -0.08022 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.28865 0.24483 0.21694 -0.04988 -0.05472 -0.08449 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.35270 0.29995 0.27228 -0.05429 -0.06215 -0.09914 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.36204 0.34419 0.29175 -0.04775 -0.06097 -0.07610 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.43381 0.40357 0.34954 -0.05313 -0.07324 -0.09950 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.34155 0.32775 0.26030 -0.04745 -0.07351 -0.08428 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.30427 0.26189 0.24968 -0.05816 -0.09754 -0.08882 211 SER A N   
1530 C CA  . SER A 204 ? 0.28105 0.22905 0.25482 -0.05122 -0.08000 -0.08395 211 SER A CA  
1531 C C   . SER A 204 ? 0.31699 0.23875 0.26444 -0.03926 -0.05965 -0.09474 211 SER A C   
1532 O O   . SER A 204 ? 0.28299 0.20873 0.24488 -0.02644 -0.04250 -0.08436 211 SER A O   
1533 C CB  . SER A 204 ? 0.28008 0.25584 0.27998 -0.04117 -0.07262 -0.06225 211 SER A CB  
1534 O OG  . SER A 204 ? 0.30967 0.31157 0.33811 -0.04753 -0.08921 -0.05276 211 SER A OG  
1535 N N   . GLN A 205 ? 0.40123 0.29795 0.31090 -0.04234 -0.06168 -0.11682 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.49540 0.37195 0.38191 -0.02696 -0.03979 -0.12847 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.50750 0.35671 0.42019 -0.01958 -0.02706 -0.13059 212 GLN A C   
1538 O O   . GLN A 205 ? 0.47859 0.32058 0.38829 -0.00098 -0.00780 -0.13277 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.52723 0.39552 0.37297 -0.03176 -0.03693 -0.14798 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.73149 0.58400 0.58010 -0.04902 -0.04928 -0.16451 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.75249 0.63325 0.60027 -0.06486 -0.07508 -0.16015 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.53108 0.43435 0.40599 -0.06870 -0.08714 -0.13972 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.85494 0.73746 0.67462 -0.07096 -0.08429 -0.17984 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.42255 0.25888 0.36329 -0.03334 -0.03635 -0.12668 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.44498 0.24858 0.40603 -0.02807 -0.02462 -0.12353 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.36620 0.18798 0.36754 -0.02773 -0.02187 -0.09732 213 PHE A C   
1547 O O   . PHE A 206 ? 0.51124 0.30656 0.53302 -0.03191 -0.01746 -0.08995 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.47546 0.24347 0.42667 -0.04662 -0.03043 -0.13559 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.56341 0.30990 0.46961 -0.04554 -0.02625 -0.15933 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.60918 0.33517 0.49477 -0.01972 -0.01025 -0.16460 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.56351 0.32243 0.45600 -0.06686 -0.03926 -0.17509 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.61026 0.32745 0.46716 -0.00610 -0.01948 -0.18720 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.67427 0.43191 0.54275 -0.06406 -0.03375 -0.20173 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.63239 0.38569 0.50543 -0.03399 -0.02099 -0.21484 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.28462 0.14923 0.29335 -0.02327 -0.02238 -0.08134 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.27051 0.15454 0.30671 -0.01974 -0.01581 -0.05775 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.31404 0.19166 0.34713 0.00183  -0.00137 -0.04945 214 ILE A C   
1558 O O   . ILE A 207 ? 0.29332 0.18303 0.31207 0.01558  0.00363  -0.05510 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.24429 0.17064 0.28768 -0.02145 -0.02131 -0.04804 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.21874 0.15669 0.27499 -0.03984 -0.03791 -0.05221 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.20530 0.15028 0.26718 -0.01496 -0.01155 -0.02853 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.28889 0.22673 0.38027 -0.05435 -0.03765 -0.04363 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.25550 0.11662 0.30364 0.00451  0.00510  -0.03406 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.31820 0.16884 0.36489 0.02661  0.01477  -0.02444 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.29494 0.18501 0.34441 0.03827  0.01684  -0.00739 215 GLY A C   
1566 O O   . GLY A 208 ? 0.29127 0.17738 0.34392 0.05221  0.02080  0.00941  215 GLY A O   
1567 N N   . TYR A 209 ? 0.23975 0.16537 0.28628 0.03261  0.01267  -0.01146 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.28215 0.24281 0.32911 0.04004  0.01301  -0.00137 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.25720 0.24142 0.29836 0.03927  0.01090  -0.01350 216 TYR A C   
1570 O O   . TYR A 209 ? 0.22701 0.20618 0.26147 0.02908  0.00747  -0.02432 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.17839 0.15303 0.22992 0.02987  0.01306  0.01016  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.23774 0.19105 0.29386 0.02732  0.01870  0.02625  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.24497 0.19779 0.29288 0.04013  0.02206  0.04417  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.25660 0.19076 0.32566 0.01079  0.01971  0.02536  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.22663 0.15551 0.27470 0.03725  0.02895  0.06360  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.21886 0.13100 0.29456 0.00490  0.02749  0.04270  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.23766 0.14474 0.30053 0.01862  0.03341  0.06315  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.28040 0.16184 0.34558 0.01247  0.04271  0.08499  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.20520 0.21602 0.24860 0.04831  0.01182  -0.01071 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.17602 0.20780 0.21654 0.04394  0.01214  -0.01953 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.25308 0.28893 0.28954 0.02988  0.00719  -0.01994 217 PRO A C   
1582 O O   . PRO A 210 ? 0.26567 0.30776 0.30607 0.02724  0.00502  -0.01369 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.23971 0.30231 0.29139 0.05289  0.01194  -0.01467 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.23122 0.29177 0.28441 0.06083  0.00786  -0.00150 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.18855 0.21229 0.23777 0.06168  0.01110  0.00204  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.20585 0.23700 0.23241 0.02275  0.00616  -0.02687 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.19520 0.22827 0.21947 0.01310  0.00018  -0.02513 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.17541 0.22057 0.19462 0.00993  0.00365  -0.02531 218 ILE A C   
1589 O O   . ILE A 211 ? 0.25526 0.29997 0.26179 0.00907  0.00880  -0.02881 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.19595 0.21393 0.21105 0.00648  -0.00760 -0.02868 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.15944 0.16530 0.18563 0.00458  -0.01062 -0.02914 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.17486 0.19749 0.19135 0.00110  -0.01549 -0.02328 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.21044 0.20293 0.22839 -0.00464 -0.02134 -0.03700 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.15273 0.20702 0.18045 0.00680  0.00256  -0.02244 219 THR A N   
1595 C CA  . THR A 212 ? 0.15526 0.21845 0.18335 -0.00033 0.00604  -0.02222 219 THR A CA  
1596 C C   . THR A 212 ? 0.13918 0.18610 0.16202 -0.00711 0.00175  -0.01776 219 THR A C   
1597 O O   . THR A 212 ? 0.18543 0.22601 0.21582 -0.00520 -0.00233 -0.01812 219 THR A O   
1598 C CB  . THR A 212 ? 0.17032 0.25296 0.21210 -0.00081 0.00586  -0.02499 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.15922 0.25869 0.20841 0.00923  0.00762  -0.02529 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.20265 0.29420 0.25057 -0.01352 0.00902  -0.02580 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.19283 0.23247 0.20168 -0.01321 0.00405  -0.01248 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.19473 0.21522 0.19702 -0.01803 -0.00066 -0.00336 220 LEU A CA  
1603 C C   . LEU A 213 ? 0.16098 0.17921 0.17152 -0.02884 0.00565  -0.00192 220 LEU A C   
1604 O O   . LEU A 213 ? 0.18193 0.20982 0.18903 -0.03825 0.01513  0.00098  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.20341 0.21477 0.17887 -0.01989 -0.00278 0.00494  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.27255 0.26244 0.23601 -0.02324 -0.00896 0.02057  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.23526 0.21490 0.21949 -0.01455 -0.02036 0.02240  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.25969 0.24479 0.18813 -0.02361 -0.01473 0.02836  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.18742 0.19330 0.21029 -0.02853 0.00185  -0.00557 221 PHE A N   
1610 C CA  . PHE A 214 ? 0.18946 0.18494 0.22025 -0.04163 0.00565  -0.00752 221 PHE A CA  
1611 C C   . PHE A 214 ? 0.27209 0.24066 0.29135 -0.04997 0.00813  0.00898  221 PHE A C   
1612 O O   . PHE A 214 ? 0.24342 0.19544 0.24961 -0.04109 0.00202  0.02105  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.16814 0.14875 0.20848 -0.03730 0.00177  -0.01910 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.17222 0.17781 0.21753 -0.03370 0.00058  -0.03399 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.16233 0.19416 0.20619 -0.02564 0.00021  -0.03256 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.17127 0.16938 0.21850 -0.03767 -0.00066 -0.04926 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.15842 0.20994 0.20299 -0.02095 -0.00179 -0.04092 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.18186 0.20336 0.22512 -0.03392 -0.00334 -0.06069 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.16635 0.21526 0.20841 -0.02509 -0.00416 -0.05390 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.20658 0.17166 0.23183 -0.06825 0.01602  0.01123  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.26154 0.19490 0.27540 -0.07926 0.02068  0.03032  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.35020 0.24516 0.37765 -0.08619 0.01815  0.02589  222 VAL A C   
1623 O O   . VAL A 215 ? 0.30740 0.20694 0.35046 -0.08655 0.01474  0.00489  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.42978 0.38330 0.44100 -0.09798 0.03583  0.03946  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.56286 0.53381 0.54650 -0.08845 0.04017  0.04815  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.29729 0.28993 0.33798 -0.10859 0.04019  0.02199  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.33777 0.19068 0.35523 -0.09092 0.01975  0.04590  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.40720 0.21091 0.43618 -0.09502 0.01820  0.04272  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.47308 0.25187 0.50619 -0.12446 0.02907  0.05412  223 GLU A C   
1630 O O   . GLU A 216 ? 0.52588 0.32650 0.55070 -0.13718 0.03899  0.07112  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.48320 0.24804 0.50412 -0.07189 0.00939  0.05847  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.42614 0.21864 0.44940 -0.04548 -0.00077 0.05066  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.60406 0.36836 0.62737 -0.02268 -0.01137 0.06905  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.48028 0.20423 0.51940 -0.01338 -0.01103 0.06524  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.52982 0.31331 0.53866 -0.01296 -0.02109 0.08559  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.58248 0.32851 0.62966 -0.12906 0.02312  0.04214  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.68695 0.40619 0.74392 -0.14984 0.02332  0.05076  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.80206 0.53778 0.87917 -0.16652 0.01875  0.02134  224 LYS A C   
1639 O O   . LYS A 217 ? 0.89342 0.58917 0.96903 -0.16783 0.01109  0.00647  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.79321 0.53134 0.85487 -0.16469 0.03799  0.07947  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.73407 0.43822 0.77469 -0.14953 0.04524  0.11123  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.87895 0.55765 0.93035 -0.16720 0.05252  0.13233  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.88010 0.50186 0.90686 -0.14565 0.06313  0.15338  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.91135 0.53654 0.88599 -0.12701 0.06226  0.17203  224 LYS A NZ  
# 
