data_7HAQ
# 
_entry.id   7HAQ 
# 
_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   7HAQ         pdb_00007haq 10.2210/pdb7haq/pdb 
WWPDB D_1001407237 ?            ?                   
# 
_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                        7HAQ 
_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-phenyl-5-(trifluoromethyl)-1,2-dihydro-3H-pyrazol-3-one' 228.171   1   ?        ? ? ? 
3 water       nat water                                                       18.015    306 ?        ? ? ? 
# 
_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-phenyl-5-(trifluoromethyl)-1,2-dihydro-3H-pyrazol-3-one' A1AYU 
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 
A1AYU non-polymer         . '2-phenyl-5-(trifluoromethyl)-1,2-dihydro-3H-pyrazol-3-one' ? 'C10 H7 F3 N2 O' 228.171 
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        A1AYU 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AYU 
_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 A1AYU 1   301 301 A1AYU EHN A . 
C 3 HOH   1   401 254 HOH   HOH A . 
C 3 HOH   2   402 231 HOH   HOH A . 
C 3 HOH   3   403 270 HOH   HOH A . 
C 3 HOH   4   404 108 HOH   HOH A . 
C 3 HOH   5   405 103 HOH   HOH A . 
C 3 HOH   6   406 97  HOH   HOH A . 
C 3 HOH   7   407 39  HOH   HOH A . 
C 3 HOH   8   408 183 HOH   HOH A . 
C 3 HOH   9   409 131 HOH   HOH A . 
C 3 HOH   10  410 265 HOH   HOH A . 
C 3 HOH   11  411 151 HOH   HOH A . 
C 3 HOH   12  412 171 HOH   HOH A . 
C 3 HOH   13  413 35  HOH   HOH A . 
C 3 HOH   14  414 298 HOH   HOH A . 
C 3 HOH   15  415 256 HOH   HOH A . 
C 3 HOH   16  416 237 HOH   HOH A . 
C 3 HOH   17  417 126 HOH   HOH A . 
C 3 HOH   18  418 60  HOH   HOH A . 
C 3 HOH   19  419 115 HOH   HOH A . 
C 3 HOH   20  420 250 HOH   HOH A . 
C 3 HOH   21  421 43  HOH   HOH A . 
C 3 HOH   22  422 301 HOH   HOH A . 
C 3 HOH   23  423 275 HOH   HOH A . 
C 3 HOH   24  424 306 HOH   HOH A . 
C 3 HOH   25  425 66  HOH   HOH A . 
C 3 HOH   26  426 25  HOH   HOH A . 
C 3 HOH   27  427 92  HOH   HOH A . 
C 3 HOH   28  428 32  HOH   HOH A . 
C 3 HOH   29  429 137 HOH   HOH A . 
C 3 HOH   30  430 29  HOH   HOH A . 
C 3 HOH   31  431 33  HOH   HOH A . 
C 3 HOH   32  432 12  HOH   HOH A . 
C 3 HOH   33  433 300 HOH   HOH A . 
C 3 HOH   34  434 169 HOH   HOH A . 
C 3 HOH   35  435 199 HOH   HOH A . 
C 3 HOH   36  436 53  HOH   HOH A . 
C 3 HOH   37  437 192 HOH   HOH A . 
C 3 HOH   38  438 27  HOH   HOH A . 
C 3 HOH   39  439 46  HOH   HOH A . 
C 3 HOH   40  440 67  HOH   HOH A . 
C 3 HOH   41  441 1   HOH   HOH A . 
C 3 HOH   42  442 22  HOH   HOH A . 
C 3 HOH   43  443 18  HOH   HOH A . 
C 3 HOH   44  444 9   HOH   HOH A . 
C 3 HOH   45  445 78  HOH   HOH A . 
C 3 HOH   46  446 6   HOH   HOH A . 
C 3 HOH   47  447 110 HOH   HOH A . 
C 3 HOH   48  448 102 HOH   HOH A . 
C 3 HOH   49  449 130 HOH   HOH A . 
C 3 HOH   50  450 71  HOH   HOH A . 
C 3 HOH   51  451 58  HOH   HOH A . 
C 3 HOH   52  452 206 HOH   HOH A . 
C 3 HOH   53  453 255 HOH   HOH A . 
C 3 HOH   54  454 76  HOH   HOH A . 
C 3 HOH   55  455 84  HOH   HOH A . 
C 3 HOH   56  456 45  HOH   HOH A . 
C 3 HOH   57  457 17  HOH   HOH A . 
C 3 HOH   58  458 90  HOH   HOH A . 
C 3 HOH   59  459 161 HOH   HOH A . 
C 3 HOH   60  460 63  HOH   HOH A . 
C 3 HOH   61  461 297 HOH   HOH A . 
C 3 HOH   62  462 94  HOH   HOH A . 
C 3 HOH   63  463 14  HOH   HOH A . 
C 3 HOH   64  464 26  HOH   HOH A . 
C 3 HOH   65  465 16  HOH   HOH A . 
C 3 HOH   66  466 15  HOH   HOH A . 
C 3 HOH   67  467 65  HOH   HOH A . 
C 3 HOH   68  468 268 HOH   HOH A . 
C 3 HOH   69  469 37  HOH   HOH A . 
C 3 HOH   70  470 240 HOH   HOH A . 
C 3 HOH   71  471 96  HOH   HOH A . 
C 3 HOH   72  472 40  HOH   HOH A . 
C 3 HOH   73  473 204 HOH   HOH A . 
C 3 HOH   74  474 288 HOH   HOH A . 
C 3 HOH   75  475 111 HOH   HOH A . 
C 3 HOH   76  476 163 HOH   HOH A . 
C 3 HOH   77  477 260 HOH   HOH A . 
C 3 HOH   78  478 165 HOH   HOH A . 
C 3 HOH   79  479 2   HOH   HOH A . 
C 3 HOH   80  480 125 HOH   HOH A . 
C 3 HOH   81  481 36  HOH   HOH A . 
C 3 HOH   82  482 30  HOH   HOH A . 
C 3 HOH   83  483 69  HOH   HOH A . 
C 3 HOH   84  484 4   HOH   HOH A . 
C 3 HOH   85  485 11  HOH   HOH A . 
C 3 HOH   86  486 50  HOH   HOH A . 
C 3 HOH   87  487 64  HOH   HOH A . 
C 3 HOH   88  488 123 HOH   HOH A . 
C 3 HOH   89  489 271 HOH   HOH A . 
C 3 HOH   90  490 294 HOH   HOH A . 
C 3 HOH   91  491 129 HOH   HOH A . 
C 3 HOH   92  492 56  HOH   HOH A . 
C 3 HOH   93  493 159 HOH   HOH A . 
C 3 HOH   94  494 8   HOH   HOH A . 
C 3 HOH   95  495 91  HOH   HOH A . 
C 3 HOH   96  496 31  HOH   HOH A . 
C 3 HOH   97  497 41  HOH   HOH A . 
C 3 HOH   98  498 62  HOH   HOH A . 
C 3 HOH   99  499 212 HOH   HOH A . 
C 3 HOH   100 500 210 HOH   HOH A . 
C 3 HOH   101 501 19  HOH   HOH A . 
C 3 HOH   102 502 55  HOH   HOH A . 
C 3 HOH   103 503 112 HOH   HOH A . 
C 3 HOH   104 504 134 HOH   HOH A . 
C 3 HOH   105 505 47  HOH   HOH A . 
C 3 HOH   106 506 59  HOH   HOH A . 
C 3 HOH   107 507 266 HOH   HOH A . 
C 3 HOH   108 508 106 HOH   HOH A . 
C 3 HOH   109 509 24  HOH   HOH A . 
C 3 HOH   110 510 228 HOH   HOH A . 
C 3 HOH   111 511 166 HOH   HOH A . 
C 3 HOH   112 512 51  HOH   HOH A . 
C 3 HOH   113 513 13  HOH   HOH A . 
C 3 HOH   114 514 70  HOH   HOH A . 
C 3 HOH   115 515 158 HOH   HOH A . 
C 3 HOH   116 516 21  HOH   HOH A . 
C 3 HOH   117 517 38  HOH   HOH A . 
C 3 HOH   118 518 180 HOH   HOH A . 
C 3 HOH   119 519 87  HOH   HOH A . 
C 3 HOH   120 520 233 HOH   HOH A . 
C 3 HOH   121 521 152 HOH   HOH A . 
C 3 HOH   122 522 217 HOH   HOH A . 
C 3 HOH   123 523 225 HOH   HOH A . 
C 3 HOH   124 524 121 HOH   HOH A . 
C 3 HOH   125 525 144 HOH   HOH A . 
C 3 HOH   126 526 83  HOH   HOH A . 
C 3 HOH   127 527 201 HOH   HOH A . 
C 3 HOH   128 528 54  HOH   HOH A . 
C 3 HOH   129 529 5   HOH   HOH A . 
C 3 HOH   130 530 75  HOH   HOH A . 
C 3 HOH   131 531 136 HOH   HOH A . 
C 3 HOH   132 532 52  HOH   HOH A . 
C 3 HOH   133 533 214 HOH   HOH A . 
C 3 HOH   134 534 179 HOH   HOH A . 
C 3 HOH   135 535 105 HOH   HOH A . 
C 3 HOH   136 536 242 HOH   HOH A . 
C 3 HOH   137 537 95  HOH   HOH A . 
C 3 HOH   138 538 219 HOH   HOH A . 
C 3 HOH   139 539 113 HOH   HOH A . 
C 3 HOH   140 540 153 HOH   HOH A . 
C 3 HOH   141 541 213 HOH   HOH A . 
C 3 HOH   142 542 133 HOH   HOH A . 
C 3 HOH   143 543 193 HOH   HOH A . 
C 3 HOH   144 544 198 HOH   HOH A . 
C 3 HOH   145 545 234 HOH   HOH A . 
C 3 HOH   146 546 10  HOH   HOH A . 
C 3 HOH   147 547 174 HOH   HOH A . 
C 3 HOH   148 548 61  HOH   HOH A . 
C 3 HOH   149 549 107 HOH   HOH A . 
C 3 HOH   150 550 122 HOH   HOH A . 
C 3 HOH   151 551 167 HOH   HOH A . 
C 3 HOH   152 552 150 HOH   HOH A . 
C 3 HOH   153 553 88  HOH   HOH A . 
C 3 HOH   154 554 119 HOH   HOH A . 
C 3 HOH   155 555 74  HOH   HOH A . 
C 3 HOH   156 556 173 HOH   HOH A . 
C 3 HOH   157 557 23  HOH   HOH A . 
C 3 HOH   158 558 101 HOH   HOH A . 
C 3 HOH   159 559 20  HOH   HOH A . 
C 3 HOH   160 560 124 HOH   HOH A . 
C 3 HOH   161 561 48  HOH   HOH A . 
C 3 HOH   162 562 7   HOH   HOH A . 
C 3 HOH   163 563 139 HOH   HOH A . 
C 3 HOH   164 564 145 HOH   HOH A . 
C 3 HOH   165 565 132 HOH   HOH A . 
C 3 HOH   166 566 68  HOH   HOH A . 
C 3 HOH   167 567 224 HOH   HOH A . 
C 3 HOH   168 568 81  HOH   HOH A . 
C 3 HOH   169 569 186 HOH   HOH A . 
C 3 HOH   170 570 93  HOH   HOH A . 
C 3 HOH   171 571 293 HOH   HOH A . 
C 3 HOH   172 572 34  HOH   HOH A . 
C 3 HOH   173 573 148 HOH   HOH A . 
C 3 HOH   174 574 157 HOH   HOH A . 
C 3 HOH   175 575 73  HOH   HOH A . 
C 3 HOH   176 576 282 HOH   HOH A . 
C 3 HOH   177 577 44  HOH   HOH A . 
C 3 HOH   178 578 252 HOH   HOH A . 
C 3 HOH   179 579 274 HOH   HOH A . 
C 3 HOH   180 580 205 HOH   HOH A . 
C 3 HOH   181 581 223 HOH   HOH A . 
C 3 HOH   182 582 28  HOH   HOH A . 
C 3 HOH   183 583 239 HOH   HOH A . 
C 3 HOH   184 584 295 HOH   HOH A . 
C 3 HOH   185 585 230 HOH   HOH A . 
C 3 HOH   186 586 182 HOH   HOH A . 
C 3 HOH   187 587 99  HOH   HOH A . 
C 3 HOH   188 588 143 HOH   HOH A . 
C 3 HOH   189 589 227 HOH   HOH A . 
C 3 HOH   190 590 221 HOH   HOH A . 
C 3 HOH   191 591 259 HOH   HOH A . 
C 3 HOH   192 592 272 HOH   HOH A . 
C 3 HOH   193 593 42  HOH   HOH A . 
C 3 HOH   194 594 209 HOH   HOH A . 
C 3 HOH   195 595 248 HOH   HOH A . 
C 3 HOH   196 596 89  HOH   HOH A . 
C 3 HOH   197 597 79  HOH   HOH A . 
C 3 HOH   198 598 211 HOH   HOH A . 
C 3 HOH   199 599 245 HOH   HOH A . 
C 3 HOH   200 600 127 HOH   HOH A . 
C 3 HOH   201 601 216 HOH   HOH A . 
C 3 HOH   202 602 77  HOH   HOH A . 
C 3 HOH   203 603 118 HOH   HOH A . 
C 3 HOH   204 604 304 HOH   HOH A . 
C 3 HOH   205 605 138 HOH   HOH A . 
C 3 HOH   206 606 170 HOH   HOH A . 
C 3 HOH   207 607 3   HOH   HOH A . 
C 3 HOH   208 608 258 HOH   HOH A . 
C 3 HOH   209 609 289 HOH   HOH A . 
C 3 HOH   210 610 128 HOH   HOH A . 
C 3 HOH   211 611 72  HOH   HOH A . 
C 3 HOH   212 612 160 HOH   HOH A . 
C 3 HOH   213 613 49  HOH   HOH A . 
C 3 HOH   214 614 155 HOH   HOH A . 
C 3 HOH   215 615 120 HOH   HOH A . 
C 3 HOH   216 616 273 HOH   HOH A . 
C 3 HOH   217 617 109 HOH   HOH A . 
C 3 HOH   218 618 196 HOH   HOH A . 
C 3 HOH   219 619 80  HOH   HOH A . 
C 3 HOH   220 620 176 HOH   HOH A . 
C 3 HOH   221 621 283 HOH   HOH A . 
C 3 HOH   222 622 117 HOH   HOH A . 
C 3 HOH   223 623 98  HOH   HOH A . 
C 3 HOH   224 624 247 HOH   HOH A . 
C 3 HOH   225 625 185 HOH   HOH A . 
C 3 HOH   226 626 104 HOH   HOH A . 
C 3 HOH   227 627 241 HOH   HOH A . 
C 3 HOH   228 628 146 HOH   HOH A . 
C 3 HOH   229 629 249 HOH   HOH A . 
C 3 HOH   230 630 147 HOH   HOH A . 
C 3 HOH   231 631 267 HOH   HOH A . 
C 3 HOH   232 632 190 HOH   HOH A . 
C 3 HOH   233 633 305 HOH   HOH A . 
C 3 HOH   234 634 85  HOH   HOH A . 
C 3 HOH   235 635 189 HOH   HOH A . 
C 3 HOH   236 636 175 HOH   HOH A . 
C 3 HOH   237 637 191 HOH   HOH A . 
C 3 HOH   238 638 277 HOH   HOH A . 
C 3 HOH   239 639 280 HOH   HOH A . 
C 3 HOH   240 640 208 HOH   HOH A . 
C 3 HOH   241 641 82  HOH   HOH A . 
C 3 HOH   242 642 57  HOH   HOH A . 
C 3 HOH   243 643 194 HOH   HOH A . 
C 3 HOH   244 644 279 HOH   HOH A . 
C 3 HOH   245 645 195 HOH   HOH A . 
C 3 HOH   246 646 253 HOH   HOH A . 
C 3 HOH   247 647 149 HOH   HOH A . 
C 3 HOH   248 648 202 HOH   HOH A . 
C 3 HOH   249 649 226 HOH   HOH A . 
C 3 HOH   250 650 269 HOH   HOH A . 
C 3 HOH   251 651 203 HOH   HOH A . 
C 3 HOH   252 652 140 HOH   HOH A . 
C 3 HOH   253 653 229 HOH   HOH A . 
C 3 HOH   254 654 197 HOH   HOH A . 
C 3 HOH   255 655 188 HOH   HOH A . 
C 3 HOH   256 656 184 HOH   HOH A . 
C 3 HOH   257 657 232 HOH   HOH A . 
C 3 HOH   258 658 276 HOH   HOH A . 
C 3 HOH   259 659 181 HOH   HOH A . 
C 3 HOH   260 660 291 HOH   HOH A . 
C 3 HOH   261 661 114 HOH   HOH A . 
C 3 HOH   262 662 244 HOH   HOH A . 
C 3 HOH   263 663 246 HOH   HOH A . 
C 3 HOH   264 664 281 HOH   HOH A . 
C 3 HOH   265 665 187 HOH   HOH A . 
C 3 HOH   266 666 86  HOH   HOH A . 
C 3 HOH   267 667 235 HOH   HOH A . 
C 3 HOH   268 668 220 HOH   HOH A . 
C 3 HOH   269 669 243 HOH   HOH A . 
C 3 HOH   270 670 287 HOH   HOH A . 
C 3 HOH   271 671 257 HOH   HOH A . 
C 3 HOH   272 672 290 HOH   HOH A . 
C 3 HOH   273 673 168 HOH   HOH A . 
C 3 HOH   274 674 261 HOH   HOH A . 
C 3 HOH   275 675 264 HOH   HOH A . 
C 3 HOH   276 676 218 HOH   HOH A . 
C 3 HOH   277 677 292 HOH   HOH A . 
C 3 HOH   278 678 135 HOH   HOH A . 
C 3 HOH   279 679 178 HOH   HOH A . 
C 3 HOH   280 680 251 HOH   HOH A . 
C 3 HOH   281 681 222 HOH   HOH A . 
C 3 HOH   282 682 207 HOH   HOH A . 
C 3 HOH   283 683 286 HOH   HOH A . 
C 3 HOH   284 684 296 HOH   HOH A . 
C 3 HOH   285 685 284 HOH   HOH A . 
C 3 HOH   286 686 262 HOH   HOH A . 
C 3 HOH   287 687 156 HOH   HOH A . 
C 3 HOH   288 688 238 HOH   HOH A . 
C 3 HOH   289 689 154 HOH   HOH A . 
C 3 HOH   290 690 164 HOH   HOH A . 
C 3 HOH   291 691 162 HOH   HOH A . 
C 3 HOH   292 692 303 HOH   HOH A . 
C 3 HOH   293 693 142 HOH   HOH A . 
C 3 HOH   294 694 299 HOH   HOH A . 
C 3 HOH   295 695 141 HOH   HOH A . 
C 3 HOH   296 696 116 HOH   HOH A . 
C 3 HOH   297 697 100 HOH   HOH A . 
C 3 HOH   298 698 302 HOH   HOH A . 
C 3 HOH   299 699 236 HOH   HOH A . 
C 3 HOH   300 700 172 HOH   HOH A . 
C 3 HOH   301 701 200 HOH   HOH A . 
C 3 HOH   302 702 177 HOH   HOH A . 
C 3 HOH   303 703 285 HOH   HOH A . 
C 3 HOH   304 704 278 HOH   HOH A . 
C 3 HOH   305 705 263 HOH   HOH A . 
C 3 HOH   306 706 215 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             593819.417 
_cell.length_a           66.110 
_cell.length_b           89.590 
_cell.length_c           100.260 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HAQ 
_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                         7HAQ 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HAQ 
# 
_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   2023-07-04 
_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                     7HAQ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             36.480 
_reflns.d_resolution_high            1.550 
_reflns.number_obs                   42917 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.700 
_reflns.pdbx_Rmerge_I_obs            0.055 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        23.700 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.100 
_reflns.pdbx_Rrim_I_all              0.057 
_reflns.pdbx_Rpim_I_all              0.016 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     519536 
_reflns.pdbx_scaling_rejects         25 
_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 1.550 1.590  ? 22475 2942 ? 0.961 ? ? ? 7.600  ? 2.000  ? ? ? ? ? ? 92.800 1.032 0.356 0.696 
1 2 6.930 36.480 ? 6280  543  ? 0.025 ? ? ? 11.600 ? 69.400 ? ? ? ? ? ? 98.600 0.026 0.008 0.999 
# 
_refine.entry_id                                 7HAQ 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.93 
_refine.pdbx_overall_phase_error                 20.8247 
_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                          0.1722 
_refine.B_iso_mean                               31.33 
_refine.ls_number_reflns_R_free                  2115 
_refine.ls_percent_reflns_obs                    98.52 
_refine.ls_R_factor_R_work                       0.1709 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.55 
_refine.ls_number_reflns_obs                     42893 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  40778 
_refine.ls_d_res_low                             36.48 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1968 
_refine.overall_SU_ML                            0.1735 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         16 
_refine_hist.number_atoms_solvent             306 
_refine_hist.number_atoms_total               1966 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        36.48 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           1687 0.0137 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2276 1.3521 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     260  0.0750 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0111 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 224  7.9570 ? ? ? 
# 
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' 1.55 1.59  2507 0.2569 91.52  0.2881 128 . . . . . 
'X-RAY DIFFRACTION' 1.59 1.63  2669 0.2426 98.22  0.2614 146 . . . . . 
'X-RAY DIFFRACTION' 1.63 1.67  2701 0.2425 98.92  0.2790 139 . . . . . 
'X-RAY DIFFRACTION' 1.67 1.72  2699 0.2216 99.16  0.2561 127 . . . . . 
'X-RAY DIFFRACTION' 1.72 1.77  2711 0.2038 99.17  0.2569 146 . . . . . 
'X-RAY DIFFRACTION' 1.77 1.84  2732 0.1882 99.17  0.2323 135 . . . . . 
'X-RAY DIFFRACTION' 1.84 1.91  2674 0.2054 97.53  0.2502 125 . . . . . 
'X-RAY DIFFRACTION' 1.91 2.00  2673 0.2289 97.75  0.2550 145 . . . . . 
'X-RAY DIFFRACTION' 2.00 2.10  2744 0.1770 99.72  0.2015 134 . . . . . 
'X-RAY DIFFRACTION' 2.10 2.24  2704 0.1719 98.41  0.1856 138 . . . . . 
'X-RAY DIFFRACTION' 2.24 2.41  2704 0.1892 98.62  0.2039 160 . . . . . 
'X-RAY DIFFRACTION' 2.41 2.65  2773 0.1730 99.97  0.2193 140 . . . . . 
'X-RAY DIFFRACTION' 2.65 3.03  2764 0.1633 100.00 0.1993 147 . . . . . 
'X-RAY DIFFRACTION' 3.03 3.82  2808 0.1526 99.93  0.1623 148 . . . . . 
'X-RAY DIFFRACTION' 3.82 36.48 2915 0.1421 99.51  0.1658 157 . . . . . 
# 
_struct.entry_id                  7HAQ 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13428' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HAQ 
_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              7HAQ 
_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 7HAQ MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HAQ LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HAQ GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HAQ HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HAQ HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HAQ HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HAQ HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HAQ HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HAQ HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2 AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3 AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4 AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5 AA5 ILE A 103 ? ALA A 117 ? ILE A 110 ALA A 124 1 ? 15 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P9 AA9 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 LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O THR A 83  ? O THR A 90  N ILE A 74  ? N ILE A 81  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HAQ 
_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 520 ? ? O A HOH 549 ? ? 1.98 
2 1 O A HOH 423 ? ? O A HOH 591 ? ? 1.98 
3 1 O A HOH 583 ? ? O A HOH 663 ? ? 1.99 
4 1 O A HOH 585 ? ? O A HOH 658 ? ? 2.17 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     449 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     614 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              2.11 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 38  ? ? -163.31 107.83  
2 1 ASP A 66  ? ? -151.16 87.53   
3 1 THR A 94  ? ? -105.21 41.60   
4 1 ALA A 166 ? ? 64.00   -143.78 
5 1 ARG A 182 ? ? -173.46 135.91  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     671 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1 ? 'X-RAY DIFFRACTION' refined 12.3756552157   -17.9002131435 -18.6818982584 0.159043046894 0.197424280353  0.20634045298  
0.0143084334544   -0.025126604413   -0.0243065810999 3.27427576346  1.12409497463  6.85954976412 -0.918032166406  -3.23746879417  
0.563440183065  0.11109034233    -0.238606192931 -0.0569111832224 0.0265373477512  -0.0913852651998  -0.0559249112507  
-0.018412822172   0.25436773758    -0.0567297479728 
2 ? 'X-RAY DIFFRACTION' refined -8.61820750397  -8.16126620549 -23.7035564286 0.160848516013 0.157861801423  0.191367295334 
0.0193862106829   -0.00430960058476 -0.0380024965922 1.64828459016  3.91327904114  4.13668327548 -1.25410627946   1.14986343169   
-2.61662100189  -0.0019499933719 0.150163275524  0.14618164875    -0.162728290269  -0.0380708109398  0.182296067929    
-0.183993761493   -0.0156212362006 -0.0122499189931 
3 ? 'X-RAY DIFFRACTION' refined -0.868012752206 -16.3195576454 -25.0506590538 0.190405556578 0.140317857713  0.199057564489 
0.0170358046378   -0.0150757579639  -0.0375569737146 2.1931124949   0.935131420902 2.17363453591 -0.606427099266  -0.337414288237 
-0.708330277717 -0.0119359555718 0.0876214997148 0.0365945367351  -0.109128618667  0.00664512016797  -0.00189856414159 
0.166792223541    0.0263807034835  0.00782696015481 
4 ? 'X-RAY DIFFRACTION' refined 15.7384338133   -5.69771673854 -14.6810065897 0.309599406703 0.653983335222  0.43410458916  
-0.154681314746   0.0189594675128   -0.191043732923  0.114273093813 4.80620586151  3.21694265634 -0.0318938995475 0.50297268167   
0.168557780111  0.668932336516   -1.17223218441  1.06861546591    0.392205181058   -0.113177961723   -0.53239746364    
-1.04680928049    1.88290120946    -0.251036955839  
5 ? 'X-RAY DIFFRACTION' refined 2.4102928988    -16.6694805085 -24.4118295198 0.120062701621 0.0828511699994 0.148126032356 
-0.00714160705536 0.00132065717813  -0.0201890916006 4.20338716223  1.9036714077   2.73476967215 -0.7032212652    -0.685592092407 
0.137414018538  0.0994449916212  0.132599870026  -0.0237056771053 -0.0969436073475 -0.00972642252245 0.0951213592075   
0.000462327879669 0.175977162639   -0.0629398179932 
6 ? 'X-RAY DIFFRACTION' refined -5.58604713175  -20.2470788524 -10.3860422725 0.158438028285 0.19237290976   0.193667396578 
-0.031894265799   -0.0278830469121  0.011975417993   3.32122410927  2.73018944522  5.0287396959  -1.19369754205   -0.525220221975 
-0.973141329306 -0.0721031129291 -0.365712691305 -0.217823841536  0.175787301738   0.108463213737    0.0450752699356   
0.256356478933    -0.0527663296155 -0.0212133152177 
7 ? 'X-RAY DIFFRACTION' refined -13.9204991643  -13.4563132849 -14.7373264149 0.150766580034 0.208963027893  0.14815265355  
0.00997608466507  -0.00033780449397 -0.028017026063  5.43231541858  3.97368367415  4.96039770047 -0.0577144555757 -0.207155787781 
-1.13274436218  0.041682097764   -0.37285307018  -0.0370077245055 0.302651935832   -0.0187922773512  0.00997010545988  
-0.14519787888    -0.258403275688  0.007174450193   
# 
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 83  A 68  . 
;chain 'A' and (resid 41 through 83 )
;
3 3 'X-RAY DIFFRACTION' A 84  A 69  A 110 A 95  . 
;chain 'A' and (resid 84 through 110 )
;
4 4 'X-RAY DIFFRACTION' A 111 A 96  A 123 A 108 . 
;chain 'A' and (resid 111 through 123 )
;
5 5 'X-RAY DIFFRACTION' A 124 A 109 A 182 A 167 . 
;chain 'A' and (resid 124 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 
A1AYU C1   C N N 1   
A1AYU C2   C N N 2   
A1AYU C10  C Y N 3   
A1AYU C3   C N N 4   
A1AYU C4   C N N 5   
A1AYU C5   C Y N 6   
A1AYU C6   C Y N 7   
A1AYU C7   C Y N 8   
A1AYU C8   C Y N 9   
A1AYU C9   C Y N 10  
A1AYU F1   F N N 11  
A1AYU F2   F N N 12  
A1AYU F3   F N N 13  
A1AYU N1   N N N 14  
A1AYU N2   N N N 15  
A1AYU O1   O N N 16  
A1AYU H7   H N N 17  
A1AYU H1   H N N 18  
A1AYU H3   H N N 19  
A1AYU H4   H N N 20  
A1AYU H5   H N N 21  
A1AYU H6   H N N 22  
A1AYU H2   H N N 23  
ALA   N    N N N 24  
ALA   CA   C N S 25  
ALA   C    C N N 26  
ALA   O    O N N 27  
ALA   CB   C N N 28  
ALA   OXT  O N N 29  
ALA   H    H N N 30  
ALA   H2   H N N 31  
ALA   HA   H N N 32  
ALA   HB1  H N N 33  
ALA   HB2  H N N 34  
ALA   HB3  H N N 35  
ALA   HXT  H N N 36  
ARG   N    N N N 37  
ARG   CA   C N S 38  
ARG   C    C N N 39  
ARG   O    O N N 40  
ARG   CB   C N N 41  
ARG   CG   C N N 42  
ARG   CD   C N N 43  
ARG   NE   N N N 44  
ARG   CZ   C N N 45  
ARG   NH1  N N N 46  
ARG   NH2  N N N 47  
ARG   OXT  O N N 48  
ARG   H    H N N 49  
ARG   H2   H N N 50  
ARG   HA   H N N 51  
ARG   HB2  H N N 52  
ARG   HB3  H N N 53  
ARG   HG2  H N N 54  
ARG   HG3  H N N 55  
ARG   HD2  H N N 56  
ARG   HD3  H N N 57  
ARG   HE   H N N 58  
ARG   HH11 H N N 59  
ARG   HH12 H N N 60  
ARG   HH21 H N N 61  
ARG   HH22 H N N 62  
ARG   HXT  H N N 63  
ASN   N    N N N 64  
ASN   CA   C N S 65  
ASN   C    C N N 66  
ASN   O    O N N 67  
ASN   CB   C N N 68  
ASN   CG   C N N 69  
ASN   OD1  O N N 70  
ASN   ND2  N N N 71  
ASN   OXT  O N N 72  
ASN   H    H N N 73  
ASN   H2   H N N 74  
ASN   HA   H N N 75  
ASN   HB2  H N N 76  
ASN   HB3  H N N 77  
ASN   HD21 H N N 78  
ASN   HD22 H N N 79  
ASN   HXT  H N N 80  
ASP   N    N N N 81  
ASP   CA   C N S 82  
ASP   C    C N N 83  
ASP   O    O N N 84  
ASP   CB   C N N 85  
ASP   CG   C N N 86  
ASP   OD1  O N N 87  
ASP   OD2  O N N 88  
ASP   OXT  O N N 89  
ASP   H    H N N 90  
ASP   H2   H N N 91  
ASP   HA   H N N 92  
ASP   HB2  H N N 93  
ASP   HB3  H N N 94  
ASP   HD2  H N N 95  
ASP   HXT  H N N 96  
GLN   N    N N N 97  
GLN   CA   C N S 98  
GLN   C    C N N 99  
GLN   O    O N N 100 
GLN   CB   C N N 101 
GLN   CG   C N N 102 
GLN   CD   C N N 103 
GLN   OE1  O N N 104 
GLN   NE2  N N N 105 
GLN   OXT  O N N 106 
GLN   H    H N N 107 
GLN   H2   H N N 108 
GLN   HA   H N N 109 
GLN   HB2  H N N 110 
GLN   HB3  H N N 111 
GLN   HG2  H N N 112 
GLN   HG3  H N N 113 
GLN   HE21 H N N 114 
GLN   HE22 H N N 115 
GLN   HXT  H N N 116 
GLU   N    N N N 117 
GLU   CA   C N S 118 
GLU   C    C N N 119 
GLU   O    O N N 120 
GLU   CB   C N N 121 
GLU   CG   C N N 122 
GLU   CD   C N N 123 
GLU   OE1  O N N 124 
GLU   OE2  O N N 125 
GLU   OXT  O N N 126 
GLU   H    H N N 127 
GLU   H2   H N N 128 
GLU   HA   H N N 129 
GLU   HB2  H N N 130 
GLU   HB3  H N N 131 
GLU   HG2  H N N 132 
GLU   HG3  H N N 133 
GLU   HE2  H N N 134 
GLU   HXT  H N N 135 
GLY   N    N N N 136 
GLY   CA   C N N 137 
GLY   C    C N N 138 
GLY   O    O N N 139 
GLY   OXT  O N N 140 
GLY   H    H N N 141 
GLY   H2   H N N 142 
GLY   HA2  H N N 143 
GLY   HA3  H N N 144 
GLY   HXT  H N N 145 
HIS   N    N N N 146 
HIS   CA   C N S 147 
HIS   C    C N N 148 
HIS   O    O N N 149 
HIS   CB   C N N 150 
HIS   CG   C Y N 151 
HIS   ND1  N Y N 152 
HIS   CD2  C Y N 153 
HIS   CE1  C Y N 154 
HIS   NE2  N Y N 155 
HIS   OXT  O N N 156 
HIS   H    H N N 157 
HIS   H2   H N N 158 
HIS   HA   H N N 159 
HIS   HB2  H N N 160 
HIS   HB3  H N N 161 
HIS   HD1  H N N 162 
HIS   HD2  H N N 163 
HIS   HE1  H N N 164 
HIS   HE2  H N N 165 
HIS   HXT  H N N 166 
HOH   O    O N N 167 
HOH   H1   H N N 168 
HOH   H2   H N N 169 
ILE   N    N N N 170 
ILE   CA   C N S 171 
ILE   C    C N N 172 
ILE   O    O N N 173 
ILE   CB   C N S 174 
ILE   CG1  C N N 175 
ILE   CG2  C N N 176 
ILE   CD1  C N N 177 
ILE   OXT  O N N 178 
ILE   H    H N N 179 
ILE   H2   H N N 180 
ILE   HA   H N N 181 
ILE   HB   H N N 182 
ILE   HG12 H N N 183 
ILE   HG13 H N N 184 
ILE   HG21 H N N 185 
ILE   HG22 H N N 186 
ILE   HG23 H N N 187 
ILE   HD11 H N N 188 
ILE   HD12 H N N 189 
ILE   HD13 H N N 190 
ILE   HXT  H N N 191 
LEU   N    N N N 192 
LEU   CA   C N S 193 
LEU   C    C N N 194 
LEU   O    O N N 195 
LEU   CB   C N N 196 
LEU   CG   C N N 197 
LEU   CD1  C N N 198 
LEU   CD2  C N N 199 
LEU   OXT  O N N 200 
LEU   H    H N N 201 
LEU   H2   H N N 202 
LEU   HA   H N N 203 
LEU   HB2  H N N 204 
LEU   HB3  H N N 205 
LEU   HG   H N N 206 
LEU   HD11 H N N 207 
LEU   HD12 H N N 208 
LEU   HD13 H N N 209 
LEU   HD21 H N N 210 
LEU   HD22 H N N 211 
LEU   HD23 H N N 212 
LEU   HXT  H N N 213 
LYS   N    N N N 214 
LYS   CA   C N S 215 
LYS   C    C N N 216 
LYS   O    O N N 217 
LYS   CB   C N N 218 
LYS   CG   C N N 219 
LYS   CD   C N N 220 
LYS   CE   C N N 221 
LYS   NZ   N N N 222 
LYS   OXT  O N N 223 
LYS   H    H N N 224 
LYS   H2   H N N 225 
LYS   HA   H N N 226 
LYS   HB2  H N N 227 
LYS   HB3  H N N 228 
LYS   HG2  H N N 229 
LYS   HG3  H N N 230 
LYS   HD2  H N N 231 
LYS   HD3  H N N 232 
LYS   HE2  H N N 233 
LYS   HE3  H N N 234 
LYS   HZ1  H N N 235 
LYS   HZ2  H N N 236 
LYS   HZ3  H N N 237 
LYS   HXT  H N N 238 
MET   N    N N N 239 
MET   CA   C N S 240 
MET   C    C N N 241 
MET   O    O N N 242 
MET   CB   C N N 243 
MET   CG   C N N 244 
MET   SD   S N N 245 
MET   CE   C N N 246 
MET   OXT  O N N 247 
MET   H    H N N 248 
MET   H2   H N N 249 
MET   HA   H N N 250 
MET   HB2  H N N 251 
MET   HB3  H N N 252 
MET   HG2  H N N 253 
MET   HG3  H N N 254 
MET   HE1  H N N 255 
MET   HE2  H N N 256 
MET   HE3  H N N 257 
MET   HXT  H N N 258 
PHE   N    N N N 259 
PHE   CA   C N S 260 
PHE   C    C N N 261 
PHE   O    O N N 262 
PHE   CB   C N N 263 
PHE   CG   C Y N 264 
PHE   CD1  C Y N 265 
PHE   CD2  C Y N 266 
PHE   CE1  C Y N 267 
PHE   CE2  C Y N 268 
PHE   CZ   C Y N 269 
PHE   OXT  O N N 270 
PHE   H    H N N 271 
PHE   H2   H N N 272 
PHE   HA   H N N 273 
PHE   HB2  H N N 274 
PHE   HB3  H N N 275 
PHE   HD1  H N N 276 
PHE   HD2  H N N 277 
PHE   HE1  H N N 278 
PHE   HE2  H N N 279 
PHE   HZ   H N N 280 
PHE   HXT  H N N 281 
PRO   N    N N N 282 
PRO   CA   C N S 283 
PRO   C    C N N 284 
PRO   O    O N N 285 
PRO   CB   C N N 286 
PRO   CG   C N N 287 
PRO   CD   C N N 288 
PRO   OXT  O N N 289 
PRO   H    H N N 290 
PRO   HA   H N N 291 
PRO   HB2  H N N 292 
PRO   HB3  H N N 293 
PRO   HG2  H N N 294 
PRO   HG3  H N N 295 
PRO   HD2  H N N 296 
PRO   HD3  H N N 297 
PRO   HXT  H N N 298 
SER   N    N N N 299 
SER   CA   C N S 300 
SER   C    C N N 301 
SER   O    O N N 302 
SER   CB   C N N 303 
SER   OG   O N N 304 
SER   OXT  O N N 305 
SER   H    H N N 306 
SER   H2   H N N 307 
SER   HA   H N N 308 
SER   HB2  H N N 309 
SER   HB3  H N N 310 
SER   HG   H N N 311 
SER   HXT  H N N 312 
THR   N    N N N 313 
THR   CA   C N S 314 
THR   C    C N N 315 
THR   O    O N N 316 
THR   CB   C N R 317 
THR   OG1  O N N 318 
THR   CG2  C N N 319 
THR   OXT  O N N 320 
THR   H    H N N 321 
THR   H2   H N N 322 
THR   HA   H N N 323 
THR   HB   H N N 324 
THR   HG1  H N N 325 
THR   HG21 H N N 326 
THR   HG22 H N N 327 
THR   HG23 H N N 328 
THR   HXT  H N N 329 
TRP   N    N N N 330 
TRP   CA   C N S 331 
TRP   C    C N N 332 
TRP   O    O N N 333 
TRP   CB   C N N 334 
TRP   CG   C Y N 335 
TRP   CD1  C Y N 336 
TRP   CD2  C Y N 337 
TRP   NE1  N Y N 338 
TRP   CE2  C Y N 339 
TRP   CE3  C Y N 340 
TRP   CZ2  C Y N 341 
TRP   CZ3  C Y N 342 
TRP   CH2  C Y N 343 
TRP   OXT  O N N 344 
TRP   H    H N N 345 
TRP   H2   H N N 346 
TRP   HA   H N N 347 
TRP   HB2  H N N 348 
TRP   HB3  H N N 349 
TRP   HD1  H N N 350 
TRP   HE1  H N N 351 
TRP   HE3  H N N 352 
TRP   HZ2  H N N 353 
TRP   HZ3  H N N 354 
TRP   HH2  H N N 355 
TRP   HXT  H N N 356 
TYR   N    N N N 357 
TYR   CA   C N S 358 
TYR   C    C N N 359 
TYR   O    O N N 360 
TYR   CB   C N N 361 
TYR   CG   C Y N 362 
TYR   CD1  C Y N 363 
TYR   CD2  C Y N 364 
TYR   CE1  C Y N 365 
TYR   CE2  C Y N 366 
TYR   CZ   C Y N 367 
TYR   OH   O N N 368 
TYR   OXT  O N N 369 
TYR   H    H N N 370 
TYR   H2   H N N 371 
TYR   HA   H N N 372 
TYR   HB2  H N N 373 
TYR   HB3  H N N 374 
TYR   HD1  H N N 375 
TYR   HD2  H N N 376 
TYR   HE1  H N N 377 
TYR   HE2  H N N 378 
TYR   HH   H N N 379 
TYR   HXT  H N N 380 
VAL   N    N N N 381 
VAL   CA   C N S 382 
VAL   C    C N N 383 
VAL   O    O N N 384 
VAL   CB   C N N 385 
VAL   CG1  C N N 386 
VAL   CG2  C N N 387 
VAL   OXT  O N N 388 
VAL   H    H N N 389 
VAL   H2   H N N 390 
VAL   HA   H N N 391 
VAL   HB   H N N 392 
VAL   HG11 H N N 393 
VAL   HG12 H N N 394 
VAL   HG13 H N N 395 
VAL   HG21 H N N 396 
VAL   HG22 H N N 397 
VAL   HG23 H N N 398 
VAL   HXT  H N N 399 
# 
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 
A1AYU F1  C1   sing N N 1   
A1AYU C1  F2   sing N N 2   
A1AYU C1  F3   sing N N 3   
A1AYU C1  C2   sing N N 4   
A1AYU C2  C3   doub N N 5   
A1AYU C3  C4   sing N N 6   
A1AYU C4  O1   doub N N 7   
A1AYU C4  N1   sing N N 8   
A1AYU N1  N2   sing N N 9   
A1AYU N1  C5   sing N N 10  
A1AYU C5  C6   doub Y N 11  
A1AYU C6  C7   sing Y N 12  
A1AYU C7  C8   doub Y N 13  
A1AYU C8  C9   sing Y N 14  
A1AYU C9  C10  doub Y N 15  
A1AYU C2  N2   sing N N 16  
A1AYU C5  C10  sing Y N 17  
A1AYU C10 H7   sing N N 18  
A1AYU C3  H1   sing N N 19  
A1AYU C6  H3   sing N N 20  
A1AYU C7  H4   sing N N 21  
A1AYU C8  H5   sing N N 22  
A1AYU C9  H6   sing N N 23  
A1AYU N2  H2   sing N N 24  
ALA   N   CA   sing N N 25  
ALA   N   H    sing N N 26  
ALA   N   H2   sing N N 27  
ALA   CA  C    sing N N 28  
ALA   CA  CB   sing N N 29  
ALA   CA  HA   sing N N 30  
ALA   C   O    doub N N 31  
ALA   C   OXT  sing N N 32  
ALA   CB  HB1  sing N N 33  
ALA   CB  HB2  sing N N 34  
ALA   CB  HB3  sing N N 35  
ALA   OXT HXT  sing N N 36  
ARG   N   CA   sing N N 37  
ARG   N   H    sing N N 38  
ARG   N   H2   sing N N 39  
ARG   CA  C    sing N N 40  
ARG   CA  CB   sing N N 41  
ARG   CA  HA   sing N N 42  
ARG   C   O    doub N N 43  
ARG   C   OXT  sing N N 44  
ARG   CB  CG   sing N N 45  
ARG   CB  HB2  sing N N 46  
ARG   CB  HB3  sing N N 47  
ARG   CG  CD   sing N N 48  
ARG   CG  HG2  sing N N 49  
ARG   CG  HG3  sing N N 50  
ARG   CD  NE   sing N N 51  
ARG   CD  HD2  sing N N 52  
ARG   CD  HD3  sing N N 53  
ARG   NE  CZ   sing N N 54  
ARG   NE  HE   sing N N 55  
ARG   CZ  NH1  sing N N 56  
ARG   CZ  NH2  doub N N 57  
ARG   NH1 HH11 sing N N 58  
ARG   NH1 HH12 sing N N 59  
ARG   NH2 HH21 sing N N 60  
ARG   NH2 HH22 sing N N 61  
ARG   OXT HXT  sing N N 62  
ASN   N   CA   sing N N 63  
ASN   N   H    sing N N 64  
ASN   N   H2   sing N N 65  
ASN   CA  C    sing N N 66  
ASN   CA  CB   sing N N 67  
ASN   CA  HA   sing N N 68  
ASN   C   O    doub N N 69  
ASN   C   OXT  sing N N 70  
ASN   CB  CG   sing N N 71  
ASN   CB  HB2  sing N N 72  
ASN   CB  HB3  sing N N 73  
ASN   CG  OD1  doub N N 74  
ASN   CG  ND2  sing N N 75  
ASN   ND2 HD21 sing N N 76  
ASN   ND2 HD22 sing N N 77  
ASN   OXT HXT  sing N N 78  
ASP   N   CA   sing N N 79  
ASP   N   H    sing N N 80  
ASP   N   H2   sing N N 81  
ASP   CA  C    sing N N 82  
ASP   CA  CB   sing N N 83  
ASP   CA  HA   sing N N 84  
ASP   C   O    doub N N 85  
ASP   C   OXT  sing N N 86  
ASP   CB  CG   sing N N 87  
ASP   CB  HB2  sing N N 88  
ASP   CB  HB3  sing N N 89  
ASP   CG  OD1  doub N N 90  
ASP   CG  OD2  sing N N 91  
ASP   OD2 HD2  sing N N 92  
ASP   OXT HXT  sing N N 93  
GLN   N   CA   sing N N 94  
GLN   N   H    sing N N 95  
GLN   N   H2   sing N N 96  
GLN   CA  C    sing N N 97  
GLN   CA  CB   sing N N 98  
GLN   CA  HA   sing N N 99  
GLN   C   O    doub N N 100 
GLN   C   OXT  sing N N 101 
GLN   CB  CG   sing N N 102 
GLN   CB  HB2  sing N N 103 
GLN   CB  HB3  sing N N 104 
GLN   CG  CD   sing N N 105 
GLN   CG  HG2  sing N N 106 
GLN   CG  HG3  sing N N 107 
GLN   CD  OE1  doub N N 108 
GLN   CD  NE2  sing N N 109 
GLN   NE2 HE21 sing N N 110 
GLN   NE2 HE22 sing N N 111 
GLN   OXT HXT  sing N N 112 
GLU   N   CA   sing N N 113 
GLU   N   H    sing N N 114 
GLU   N   H2   sing N N 115 
GLU   CA  C    sing N N 116 
GLU   CA  CB   sing N N 117 
GLU   CA  HA   sing N N 118 
GLU   C   O    doub N N 119 
GLU   C   OXT  sing N N 120 
GLU   CB  CG   sing N N 121 
GLU   CB  HB2  sing N N 122 
GLU   CB  HB3  sing N N 123 
GLU   CG  CD   sing N N 124 
GLU   CG  HG2  sing N N 125 
GLU   CG  HG3  sing N N 126 
GLU   CD  OE1  doub N N 127 
GLU   CD  OE2  sing N N 128 
GLU   OE2 HE2  sing N N 129 
GLU   OXT HXT  sing N N 130 
GLY   N   CA   sing N N 131 
GLY   N   H    sing N N 132 
GLY   N   H2   sing N N 133 
GLY   CA  C    sing N N 134 
GLY   CA  HA2  sing N N 135 
GLY   CA  HA3  sing N N 136 
GLY   C   O    doub N N 137 
GLY   C   OXT  sing N N 138 
GLY   OXT HXT  sing N N 139 
HIS   N   CA   sing N N 140 
HIS   N   H    sing N N 141 
HIS   N   H2   sing N N 142 
HIS   CA  C    sing N N 143 
HIS   CA  CB   sing N N 144 
HIS   CA  HA   sing N N 145 
HIS   C   O    doub N N 146 
HIS   C   OXT  sing N N 147 
HIS   CB  CG   sing N N 148 
HIS   CB  HB2  sing N N 149 
HIS   CB  HB3  sing N N 150 
HIS   CG  ND1  sing Y N 151 
HIS   CG  CD2  doub Y N 152 
HIS   ND1 CE1  doub Y N 153 
HIS   ND1 HD1  sing N N 154 
HIS   CD2 NE2  sing Y N 155 
HIS   CD2 HD2  sing N N 156 
HIS   CE1 NE2  sing Y N 157 
HIS   CE1 HE1  sing N N 158 
HIS   NE2 HE2  sing N N 159 
HIS   OXT HXT  sing N N 160 
HOH   O   H1   sing N N 161 
HOH   O   H2   sing N N 162 
ILE   N   CA   sing N N 163 
ILE   N   H    sing N N 164 
ILE   N   H2   sing N N 165 
ILE   CA  C    sing N N 166 
ILE   CA  CB   sing N N 167 
ILE   CA  HA   sing N N 168 
ILE   C   O    doub N N 169 
ILE   C   OXT  sing N N 170 
ILE   CB  CG1  sing N N 171 
ILE   CB  CG2  sing N N 172 
ILE   CB  HB   sing N N 173 
ILE   CG1 CD1  sing N N 174 
ILE   CG1 HG12 sing N N 175 
ILE   CG1 HG13 sing N N 176 
ILE   CG2 HG21 sing N N 177 
ILE   CG2 HG22 sing N N 178 
ILE   CG2 HG23 sing N N 179 
ILE   CD1 HD11 sing N N 180 
ILE   CD1 HD12 sing N N 181 
ILE   CD1 HD13 sing N N 182 
ILE   OXT HXT  sing N N 183 
LEU   N   CA   sing N N 184 
LEU   N   H    sing N N 185 
LEU   N   H2   sing N N 186 
LEU   CA  C    sing N N 187 
LEU   CA  CB   sing N N 188 
LEU   CA  HA   sing N N 189 
LEU   C   O    doub N N 190 
LEU   C   OXT  sing N N 191 
LEU   CB  CG   sing N N 192 
LEU   CB  HB2  sing N N 193 
LEU   CB  HB3  sing N N 194 
LEU   CG  CD1  sing N N 195 
LEU   CG  CD2  sing N N 196 
LEU   CG  HG   sing N N 197 
LEU   CD1 HD11 sing N N 198 
LEU   CD1 HD12 sing N N 199 
LEU   CD1 HD13 sing N N 200 
LEU   CD2 HD21 sing N N 201 
LEU   CD2 HD22 sing N N 202 
LEU   CD2 HD23 sing N N 203 
LEU   OXT HXT  sing N N 204 
LYS   N   CA   sing N N 205 
LYS   N   H    sing N N 206 
LYS   N   H2   sing N N 207 
LYS   CA  C    sing N N 208 
LYS   CA  CB   sing N N 209 
LYS   CA  HA   sing N N 210 
LYS   C   O    doub N N 211 
LYS   C   OXT  sing N N 212 
LYS   CB  CG   sing N N 213 
LYS   CB  HB2  sing N N 214 
LYS   CB  HB3  sing N N 215 
LYS   CG  CD   sing N N 216 
LYS   CG  HG2  sing N N 217 
LYS   CG  HG3  sing N N 218 
LYS   CD  CE   sing N N 219 
LYS   CD  HD2  sing N N 220 
LYS   CD  HD3  sing N N 221 
LYS   CE  NZ   sing N N 222 
LYS   CE  HE2  sing N N 223 
LYS   CE  HE3  sing N N 224 
LYS   NZ  HZ1  sing N N 225 
LYS   NZ  HZ2  sing N N 226 
LYS   NZ  HZ3  sing N N 227 
LYS   OXT HXT  sing N N 228 
MET   N   CA   sing N N 229 
MET   N   H    sing N N 230 
MET   N   H2   sing N N 231 
MET   CA  C    sing N N 232 
MET   CA  CB   sing N N 233 
MET   CA  HA   sing N N 234 
MET   C   O    doub N N 235 
MET   C   OXT  sing N N 236 
MET   CB  CG   sing N N 237 
MET   CB  HB2  sing N N 238 
MET   CB  HB3  sing N N 239 
MET   CG  SD   sing N N 240 
MET   CG  HG2  sing N N 241 
MET   CG  HG3  sing N N 242 
MET   SD  CE   sing N N 243 
MET   CE  HE1  sing N N 244 
MET   CE  HE2  sing N N 245 
MET   CE  HE3  sing N N 246 
MET   OXT HXT  sing N N 247 
PHE   N   CA   sing N N 248 
PHE   N   H    sing N N 249 
PHE   N   H2   sing N N 250 
PHE   CA  C    sing N N 251 
PHE   CA  CB   sing N N 252 
PHE   CA  HA   sing N N 253 
PHE   C   O    doub N N 254 
PHE   C   OXT  sing N N 255 
PHE   CB  CG   sing N N 256 
PHE   CB  HB2  sing N N 257 
PHE   CB  HB3  sing N N 258 
PHE   CG  CD1  doub Y N 259 
PHE   CG  CD2  sing Y N 260 
PHE   CD1 CE1  sing Y N 261 
PHE   CD1 HD1  sing N N 262 
PHE   CD2 CE2  doub Y N 263 
PHE   CD2 HD2  sing N N 264 
PHE   CE1 CZ   doub Y N 265 
PHE   CE1 HE1  sing N N 266 
PHE   CE2 CZ   sing Y N 267 
PHE   CE2 HE2  sing N N 268 
PHE   CZ  HZ   sing N N 269 
PHE   OXT HXT  sing N N 270 
PRO   N   CA   sing N N 271 
PRO   N   CD   sing N N 272 
PRO   N   H    sing N N 273 
PRO   CA  C    sing N N 274 
PRO   CA  CB   sing N N 275 
PRO   CA  HA   sing N N 276 
PRO   C   O    doub N N 277 
PRO   C   OXT  sing N N 278 
PRO   CB  CG   sing N N 279 
PRO   CB  HB2  sing N N 280 
PRO   CB  HB3  sing N N 281 
PRO   CG  CD   sing N N 282 
PRO   CG  HG2  sing N N 283 
PRO   CG  HG3  sing N N 284 
PRO   CD  HD2  sing N N 285 
PRO   CD  HD3  sing N N 286 
PRO   OXT HXT  sing N N 287 
SER   N   CA   sing N N 288 
SER   N   H    sing N N 289 
SER   N   H2   sing N N 290 
SER   CA  C    sing N N 291 
SER   CA  CB   sing N N 292 
SER   CA  HA   sing N N 293 
SER   C   O    doub N N 294 
SER   C   OXT  sing N N 295 
SER   CB  OG   sing N N 296 
SER   CB  HB2  sing N N 297 
SER   CB  HB3  sing N N 298 
SER   OG  HG   sing N N 299 
SER   OXT HXT  sing N N 300 
THR   N   CA   sing N N 301 
THR   N   H    sing N N 302 
THR   N   H2   sing N N 303 
THR   CA  C    sing N N 304 
THR   CA  CB   sing N N 305 
THR   CA  HA   sing N N 306 
THR   C   O    doub N N 307 
THR   C   OXT  sing N N 308 
THR   CB  OG1  sing N N 309 
THR   CB  CG2  sing N N 310 
THR   CB  HB   sing N N 311 
THR   OG1 HG1  sing N N 312 
THR   CG2 HG21 sing N N 313 
THR   CG2 HG22 sing N N 314 
THR   CG2 HG23 sing N N 315 
THR   OXT HXT  sing N N 316 
TRP   N   CA   sing N N 317 
TRP   N   H    sing N N 318 
TRP   N   H2   sing N N 319 
TRP   CA  C    sing N N 320 
TRP   CA  CB   sing N N 321 
TRP   CA  HA   sing N N 322 
TRP   C   O    doub N N 323 
TRP   C   OXT  sing N N 324 
TRP   CB  CG   sing N N 325 
TRP   CB  HB2  sing N N 326 
TRP   CB  HB3  sing N N 327 
TRP   CG  CD1  doub Y N 328 
TRP   CG  CD2  sing Y N 329 
TRP   CD1 NE1  sing Y N 330 
TRP   CD1 HD1  sing N N 331 
TRP   CD2 CE2  doub Y N 332 
TRP   CD2 CE3  sing Y N 333 
TRP   NE1 CE2  sing Y N 334 
TRP   NE1 HE1  sing N N 335 
TRP   CE2 CZ2  sing Y N 336 
TRP   CE3 CZ3  doub Y N 337 
TRP   CE3 HE3  sing N N 338 
TRP   CZ2 CH2  doub Y N 339 
TRP   CZ2 HZ2  sing N N 340 
TRP   CZ3 CH2  sing Y N 341 
TRP   CZ3 HZ3  sing N N 342 
TRP   CH2 HH2  sing N N 343 
TRP   OXT HXT  sing N N 344 
TYR   N   CA   sing N N 345 
TYR   N   H    sing N N 346 
TYR   N   H2   sing N N 347 
TYR   CA  C    sing N N 348 
TYR   CA  CB   sing N N 349 
TYR   CA  HA   sing N N 350 
TYR   C   O    doub N N 351 
TYR   C   OXT  sing N N 352 
TYR   CB  CG   sing N N 353 
TYR   CB  HB2  sing N N 354 
TYR   CB  HB3  sing N N 355 
TYR   CG  CD1  doub Y N 356 
TYR   CG  CD2  sing Y N 357 
TYR   CD1 CE1  sing Y N 358 
TYR   CD1 HD1  sing N N 359 
TYR   CD2 CE2  doub Y N 360 
TYR   CD2 HD2  sing N N 361 
TYR   CE1 CZ   doub Y N 362 
TYR   CE1 HE1  sing N N 363 
TYR   CE2 CZ   sing Y N 364 
TYR   CE2 HE2  sing N N 365 
TYR   CZ  OH   sing N N 366 
TYR   OH  HH   sing N N 367 
TYR   OXT HXT  sing N N 368 
VAL   N   CA   sing N N 369 
VAL   N   H    sing N N 370 
VAL   N   H2   sing N N 371 
VAL   CA  C    sing N N 372 
VAL   CA  CB   sing N N 373 
VAL   CA  HA   sing N N 374 
VAL   C   O    doub N N 375 
VAL   C   OXT  sing N N 376 
VAL   CB  CG1  sing N N 377 
VAL   CB  CG2  sing N N 378 
VAL   CB  HB   sing N N 379 
VAL   CG1 HG11 sing N N 380 
VAL   CG1 HG12 sing N N 381 
VAL   CG1 HG13 sing N N 382 
VAL   CG2 HG21 sing N N 383 
VAL   CG2 HG22 sing N N 384 
VAL   CG2 HG23 sing N N 385 
VAL   OXT HXT  sing N N 386 
# 
_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                    7HAQ 
_atom_sites.fract_transf_matrix[1][1]   0.015126 
_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]   0.011162 
_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]   0.009974 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU   A 1 9   ? 4.28331   -28.37661 -38.96551 1.000 54.57983 ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.59681   -27.74282 -39.12887 1.000 64.19260 ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 5.87536   -26.80182 -37.94539 1.000 54.17049 ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 5.20621   -25.77469 -37.77726 1.000 51.30853 ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.65881   -26.98650 -40.46517 1.000 66.63521 ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 7.01401   -27.01740 -41.19740 1.000 81.18675 ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 8.10056   -26.17676 -40.51701 1.000 87.63107 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 7.76903   -25.35611 -39.63368 1.000 83.17490 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 9.29137   -26.33274 -40.87133 1.000 93.82260 ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 6.85983   -27.16119 -37.12147 1.000 41.66360 ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 7.13979   -26.49103 -35.85145 1.000 33.79200 ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.49391   -25.82014 -35.93498 1.000 34.81608 ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.47978   -26.46971 -36.30068 1.000 36.00147 ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 7.13703   -27.48255 -34.68535 1.000 37.50277 ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.36831   -26.75152 -33.38572 1.000 38.08567 ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 5.84182   -28.27448 -34.68394 1.000 47.42260 ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.55680   -24.54228 -35.58444 1.000 27.14361 ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.81801   -23.80604 -35.53397 1.000 26.59990 ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 10.24902  -23.66437 -34.07788 1.000 23.08568 ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.45914   -23.25122 -33.21712 1.000 22.67828 ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.69944   -22.41988 -36.18866 1.000 25.66758 ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.53236   -22.44105 -37.70819 1.000 28.56494 ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 9.30032   -21.04099 -38.27895 1.000 37.83681 ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 8.23023   -20.45958 -38.04323 1.000 39.73169 ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 10.16280  -20.53511 -39.02654 1.000 45.95833 ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.51879  -23.98197 -33.78008 1.000 22.11477 ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 12.05821  -23.87040 -32.43763 1.000 20.66983 ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 13.04696  -22.71815 -32.40487 1.000 22.26526 ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 13.93083  -22.63423 -33.26578 1.000 21.17145 ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.74324  -25.17679 -32.01010 1.000 21.33279 ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.82980  -26.25508 -32.14333 1.000 24.12715 ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 13.31036  -25.11428 -30.58346 1.000 20.26167 ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 12.89175  -21.84166 -31.42705 1.000 20.34526 ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.71350  -20.65088 -31.24104 1.000 19.74244 ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.37345  -20.66329 -29.87404 1.000 24.37701 ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.79519  -21.14853 -28.89010 1.000 20.30614 ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.85595  -19.37567 -31.28773 1.000 21.36347 ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 12.08789  -19.19624 -32.55900 1.000 20.92800 ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.84449  -19.83128 -32.76678 1.000 21.67580 ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.60502  -18.39586 -33.57440 1.000 24.62235 ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 10.15933  -19.65996 -33.94136 1.000 26.34456 ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 11.87571  -18.19607 -34.75334 1.000 28.69744 ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.67621  -18.84864 -34.94156 1.000 27.14015 ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.57340  -20.06777 -29.78988 1.000 19.49205 ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 16.17561  -19.79212 -28.48713 1.000 19.61801 ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.64718  -18.48871 -27.90790 1.000 19.98759 ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.54814  -17.47311 -28.60510 1.000 20.46254 ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.68901  -19.67996 -28.60493 1.000 19.87868 ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.31303  -18.49360 -26.59789 1.000 18.56614 ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 15.10935  -17.20271 -25.94150 1.000 19.98723 ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.39033  -16.38168 -25.98147 1.000 20.72780 ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.50766  -16.92387 -25.87598 1.000 22.79453 ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.71088  -17.35576 -24.46951 1.000 18.12224 ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.29758  -17.88049 -24.25298 1.000 17.71006 ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.18271  -17.09487 -24.55162 1.000 20.60817 ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.12706  -19.17122 -23.75825 1.000 18.77466 ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.86040  -17.60459 -24.33641 1.000 20.84211 ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.85001  -19.68800 -23.57071 1.000 19.27269 ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.71589  -18.90251 -23.84777 1.000 19.19210 ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.22212  -15.06497 -26.11449 1.000 22.06975 ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.33975  -14.16101 -25.82610 1.000 20.42470 ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.85941  -14.45957 -24.43306 1.000 23.18577 ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.10411  -14.84932 -23.53273 1.000 21.93015 ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.87639  -12.71166 -25.87882 1.000 26.71445 ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.49923  -12.25155 -27.25425 1.000 26.97010 ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 15.94469  -10.87091 -27.18417 1.000 38.63314 ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.74210  -10.70966 -27.10902 1.000 40.39921 ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.81679  -9.84691  -27.26297 1.000 41.82360 ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.15301  -14.27587 -24.24801 1.000 25.04586 ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.76785  -14.72146 -23.01061 1.000 23.56259 ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.14843  -14.04508 -21.79214 1.000 24.50225 ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 18.91588  -14.70071 -20.77580 1.000 25.57466 ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.27199  -14.47652 -23.10831 1.000 25.90466 ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.77160  -12.77421 -21.91779 1.000 24.28491 ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.21703  -12.04602 -20.79286 1.000 25.00268 ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.84328  -12.58619 -20.42800 1.000 23.61515 ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.47287  -12.61125 -19.24118 1.000 24.19088 ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.16621  -10.55647 -21.13397 1.000 27.92236 ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.48907  -9.87884  -21.39053 1.000 36.73329 ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.06815  -10.11390 -22.78413 1.000 39.94473 ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.46297  -10.81260 -23.63658 1.000 33.77817 ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.15559  -9.54389  -23.05687 1.000 49.62950 ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.09079  -13.08545 -21.41083 1.000 22.42761 ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.75844  -13.60397 -21.10328 1.000 20.18196 ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.87536  -14.98897 -20.47219 1.000 21.57108 ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.12981  -15.34483 -19.54261 1.000 22.42638 ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.86979  -13.60467 -22.37345 1.000 22.15431 ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.35023  -12.20073 -22.75059 1.000 26.91532 ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.57437  -14.42878 -22.17860 1.000 20.47554 ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.39181  -11.10081 -22.89312 1.000 30.74958 ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.83207  -15.78075 -20.95362 1.000 20.56306 ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.08714  -17.06998 -20.32322 1.000 20.02050 ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.45010  -16.87170 -18.85304 1.000 20.50180 ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.02809  -17.65214 -17.98748 1.000 22.97894 ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.22384  -17.79452 -21.07053 1.000 24.20395 ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.22795  -15.82637 -18.56136 1.000 22.11402 ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.64281  -15.56176 -17.19419 1.000 24.89230 ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.45873  -15.13158 -16.34962 1.000 26.70669 ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.34170  -15.55611 -15.19908 1.000 26.32754 ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.73903  -14.50603 -17.19817 1.000 25.32259 ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 19.33227  -14.26203 -15.82620 1.000 42.56547 ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.50309  -13.26819 -15.85557 1.000 70.50665 ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 20.58823  -12.41205 -16.74937 1.000 64.11771 ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 21.36952  -13.33525 -14.83369 1.000 65.88345 ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.58003  -14.28283 -16.91343 1.000 22.19228 ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.35268  -13.89050 -16.20668 1.000 23.66395 ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.50810  -15.11697 -15.87914 1.000 25.72457 ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.01093  -15.27996 -14.74963 1.000 22.59737 ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.56729  -12.90844 -17.08314 1.000 24.12914 ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.14032  -12.63694 -16.56233 1.000 25.81154 ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.27141  -11.74421 -15.34699 1.000 32.08137 ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.25752  -11.99605 -17.64968 1.000 28.93909 ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.34642  -16.00659 -16.85129 1.000 22.15265 ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.55178  -17.19832 -16.61898 1.000 21.63463 ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.16979  -18.09268 -15.55886 1.000 20.96822 ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.45232  -18.62345 -14.69841 1.000 21.13007 ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.32206  -17.99605 -17.90794 1.000 17.92993 ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.46878  -17.17469 -18.88632 1.000 20.10505 ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.32770  -17.95827 -20.51032 1.000 20.45867 ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.21160  -19.35436 -20.17441 1.000 21.72565 ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.49481  -18.30549 -15.58619 1.000 21.45310 ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.05660  -19.15315 -14.53910 1.000 22.69036 ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 14.97556  -18.49350 -13.15317 1.000 25.46204 ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.73642  -19.18406 -12.16375 1.000 28.57686 ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.45515  -19.59243 -14.95802 1.000 34.27759 ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.34013  -18.52673 -14.92387 1.000 46.18013 ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.08627  -17.16779 -13.06467 1.000 22.42265 ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.90187  -16.50420 -11.78241 1.000 24.26010 ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.48128  -16.71962 -11.26796 1.000 26.45978 ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.27330  -16.97335 -10.07129 1.000 26.62406 ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.20771  -15.01537 -11.93747 1.000 29.09542 ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 14.98313  -14.11006 -10.71575 1.000 33.58269 ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 15.98294  -12.94719 -10.79571 1.000 41.57947 ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 13.53684  -13.58888 -10.56121 1.000 40.08755 ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.48727  -16.61348 -12.15956 1.000 20.68627 ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.09951  -16.80618 -11.73163 1.000 22.70652 ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.88053  -18.23800 -11.26666 1.000 21.70905 ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.17100  -18.49764 -10.27570 1.000 23.85697 ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.15726  -16.43038 -12.87470 1.000 21.07499 ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.15668  -14.91245 -13.01821 1.000 23.90170 ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.72742   -16.99881 -12.60867 1.000 21.54965 ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.52025   -14.44767 -14.33964 1.000 26.46378 ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.48589  -19.18640 -11.96459 1.000 23.66470 ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.30689  -20.58793 -11.63378 1.000 25.43796 ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.05892  -20.98982 -10.38051 1.000 27.10533 ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.56852  -21.81547 -9.59314  1.000 29.66614 ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.72172  -21.42405 -12.85627 1.000 25.18350 ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.65223  -21.27226 -13.93866 1.000 24.33102 ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.92849  -22.87346 -12.46022 1.000 26.96670 ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.14808  -21.77099 -15.31051 1.000 23.89354 ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.23730  -20.41072 -10.13468 1.000 24.83107 ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.13408  -20.92039 -9.09732  1.000 29.13089 ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.11259  -20.13233 -7.79682  1.000 30.07799 ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.55342  -20.67268 -6.77219  1.000 37.65432 ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.56019  -20.91846 -9.62272  1.000 31.22109 ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.77300  -21.95584 -10.66663 1.000 37.05881 ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.05927  -22.95818 -10.72216 1.000 41.28036 ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.67886  -21.66412 -11.59091 1.000 51.45472 ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.66237  -18.87531 -7.81327  1.000 29.17214 ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.63677  -18.07321 -6.58685  1.000 25.33289 ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.55173  -18.56073 -5.63543  1.000 26.93989 ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.41109  -18.78464 -6.05983  1.000 28.44603 ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.41134  -16.59368 -6.93472  1.000 31.51551 ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.46835  -16.14395 -7.78000  1.000 33.12970 ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.46449  -15.71788 -5.67819  1.000 34.07731 ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.91081  -18.76648 -4.37153  1.000 28.47307 ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.89244  -19.00701 -3.36687  1.000 27.52966 ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.02770  -17.75308 -3.18602  1.000 30.16947 ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.52632  -16.69641 -2.76441  1.000 30.98746 ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.51217  -19.41223 -2.03755  1.000 29.25753 ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.47836  -19.73506 -0.99417  1.000 31.45587 ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.71800  -20.89048 -1.09722  1.000 37.25348 ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.22095  -18.87057 0.04420   1.000 31.23938 ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.72590   -21.18006 -0.15768  1.000 32.51894 ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.24011  -19.17131 1.02135   1.000 34.34248 ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.51408   -20.32733 0.92286   1.000 34.33594 ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.72108   -17.88689 -3.41828  1.000 25.07674 ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.84901   -16.72060 -3.40402  1.000 24.22045 ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.42057   -17.25758 -3.27876  1.000 23.00240 ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.90161   -17.85077 -4.23403  1.000 24.65665 ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.04350   -15.90324 -4.69171  1.000 26.99812 ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.06214   -14.77030 -4.78588  1.000 27.25118 ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.24228   -13.65142 -4.01278  1.000 33.08183 ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 6.94758   -14.83268 -5.65625  1.000 27.01731 ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.36333   -12.61373 -4.04211  1.000 40.59875 ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.04059   -13.75188 -5.69266  1.000 31.01569 ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.28943   -12.66352 -4.88533  1.000 36.24508 ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.44740   -11.58208 -4.87399  1.000 53.44710 ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.81182   -17.08425 -2.11500  1.000 23.97306 ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.55700   -17.76704 -1.81361  1.000 23.97959 ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.33668   -17.10991 -2.46110  1.000 23.22428 ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.35093   -17.80905 -2.68900  1.000 26.26797 ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.35984   -17.85493 -0.30183  1.000 26.45868 ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.40739   -18.66607 0.25783   1.000 27.05904 ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.40061   -15.82346 -2.83012  1.000 24.67183 ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.22752   -15.06412 -3.27939  1.000 24.97514 ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 2.96656   -15.29888 -4.77238  1.000 22.99593 ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 2.93117   -14.37572 -5.59068  1.000 25.29397 ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.46139   -13.59669 -2.94349  1.000 27.57164 ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.27440   -12.69549 -3.26793  1.000 29.19246 ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.10778   -13.08685 -3.13736  1.000 31.22918 ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.57629   -11.45948 -3.64466  1.000 30.22571 ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.72397   -16.57267 -5.12237  1.000 22.00700 ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.61916   -16.92647 -6.53772  1.000 19.30124 ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.32259   -16.46140 -7.18070  1.000 20.18459 ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.28920   -16.36027 -8.40909  1.000 19.70899 ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.70969   -18.43933 -6.69578  1.000 18.21919 ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.09269   -19.02463 -6.31918  1.000 20.65325 ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.04724   -20.54619 -6.54625  1.000 24.61455 ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.37030   -21.27471 -6.22198  1.000 24.54979 ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.36386   -21.00368 -7.31786  1.000 25.57978 ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.30667   -16.13399 -6.37827  1.000 20.41431 ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -1.01355  -15.89880 -6.95161  1.000 21.23113 ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -1.02565  -14.69058 -7.87100  1.000 23.68746 ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.97723  -14.54698 -8.66182  1.000 21.45850 ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -2.05103  -15.68242 -5.82061  1.000 22.09308 ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.84385  -14.41024 -5.04150  1.000 22.80228 ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.71946  -14.29810 -3.79922  1.000 27.83767 ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.81077  -15.28380 -3.05300  1.000 34.39671 ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.24635  -13.21144 -3.55827  1.000 39.36378 ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? -0.02736  -13.80563 -7.76427  1.000 19.08044 ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.00703   -12.61681 -8.61888  1.000 20.01564 ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.15000   -12.95095 -10.10479 1.000 20.51251 ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? -0.06529  -12.05999 -10.92321 1.000 19.11207 ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.12617   -11.62767 -8.20231  1.000 25.33352 ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.48733   -12.28421 -8.31951  1.000 23.18222 ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 0.90530   -11.14122 -6.75963  1.000 25.75659 ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.17100   -12.03814 -9.65859  1.000 28.78651 ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.47254   -14.19898 -10.48574 1.000 17.79324 ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.50068   -14.51604 -11.92576 1.000 18.18042 ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.84659  -14.19093 -12.56176 1.000 18.19051 ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.90164  -13.70701 -13.70376 1.000 18.18907 ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.83860   -16.00044 -12.19252 1.000 19.09177 ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.35078  -16.88961 -11.98683 1.000 20.34148 ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.66415  -17.35931 -10.72642 1.000 20.49387 ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.18829  -17.23167 -13.07115 1.000 19.47104 ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.82160  -18.16877 -10.52045 1.000 21.73482 ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.34184  -18.00823 -12.85922 1.000 19.39125 ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.65346  -18.47850 -11.61195 1.000 17.95077 ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.96414  -14.38817 -11.82246 1.000 16.86781 ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.26456  -14.24008 -12.48518 1.000 18.61828 ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.56484  -12.76883 -12.73214 1.000 20.72378 ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.07200  -12.40701 -13.81529 1.000 19.94514 ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.34858  -14.88272 -11.64177 1.000 18.33336 ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.74047  -14.92650 -12.33580 1.000 18.33462 ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.69330  -15.64536 -13.66597 1.000 21.56330 ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.75008  -15.56106 -11.38012 1.000 25.22512 ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.19586  -11.90285 -11.76690 1.000 19.56309 ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.32941  -10.45680 -11.93963 1.000 18.80503 ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.53907  -9.99669  -13.15248 1.000 22.19637 ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -3.01644  -9.18627  -13.96205 1.000 21.34740 ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.85482  -9.71455  -10.69153 1.000 22.58704 ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.78494  -8.23823  -10.87369 1.000 27.61728 ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -2.04791  -7.56479  -9.71449  1.000 33.67258 ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.62853  -7.91676  -9.65407  1.000 38.97092 ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.14137   -7.78565  -8.57693  1.000 36.72440 ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.33703  -7.35026  -7.41580  1.000 36.69759 ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.43909   -8.07897  -8.66580  1.000 40.70101 ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.33989  -10.55318 -13.33344 1.000 19.51922 ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.50577  -10.09920 -14.43123 1.000 19.40832 ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.08535  -10.51090 -15.77736 1.000 20.17141 ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -1.04997  -9.72720  -16.74181 1.000 18.76107 ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.92139   -10.64852 -14.25915 1.000 17.19195 ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.64536   -10.12736 -13.00683 1.000 21.69290 ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.62746   -8.60760  -12.86383 1.000 25.51008 ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.68039   -7.86375  -13.86370 1.000 26.38633 ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.57654   -8.16489  -11.69167 1.000 32.26619 ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.60100  -11.72989 -15.86900 1.000 16.92799 ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.17352  -12.17083 -17.14645 1.000 17.79098 ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.46160  -11.42307 -17.44762 1.000 19.98941 ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.72431  -11.06943 -18.61875 1.000 18.75762 ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.42237  -13.67257 -17.13817 1.000 18.74999 ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.11150  -14.46546 -17.08015 1.000 20.02379 ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.40945  -15.97578 -16.94424 1.000 19.90016 ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.13917  -14.19413 -18.22603 1.000 19.52058 ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.29866  -11.21143 -16.43078 1.000 18.07400 ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.53066  -10.46793 -16.66171 1.000 18.67877 ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.19900  -9.04254  -17.07437 1.000 19.13217 ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.85221  -8.46393  -17.95666 1.000 19.30755 ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.43542  -10.52101 -15.41208 1.000 17.71966 ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -7.00700  -11.94530 -15.28271 1.000 18.96314 ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.57681  -9.46428  -15.49591 1.000 20.11549 ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.77124  -12.13028 -13.93483 1.000 19.70253 ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.14049  -8.46376  -16.48541 1.000 18.59463 ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.79205  -7.11116  -16.86234 1.000 17.46468 ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.31481  -7.08097  -18.31807 1.000 20.69519 ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.62751  -6.14439  -19.06826 1.000 19.60075 ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.72297  -6.60881  -15.89161 1.000 23.75807 ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.14812  -5.42865  -16.40063 1.000 30.07544 ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.57865  -8.11095  -18.74357 1.000 20.09701 ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.16561  -8.17334  -20.14833 1.000 21.01490 ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.37322  -8.27375  -21.06042 1.000 20.38170 ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.40807  -7.65089  -22.13129 1.000 19.79962 ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.23622  -9.36916  -20.40201 1.000 20.09585 ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.12790   -9.15745  -19.84841 1.000 29.43035 ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.49269   -8.06378  -19.37244 1.000 25.29608 ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 0.90293   -10.20911 -19.89357 1.000 29.22747 ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.34803  -9.08438  -20.64927 1.000 16.82782 ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.57581  -9.21991  -21.44111 1.000 19.76447 ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.30169  -7.87782  -21.52877 1.000 18.73797 ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.77074  -7.48391  -22.61645 1.000 18.63650 ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.48820  -10.28441 -20.80312 1.000 18.55442 ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -5.97047  -11.57771 -21.01600 1.000 19.27157 ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.39325  -7.15048  -20.40091 1.000 17.36814 ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.03794  -5.83876  -20.41557 1.000 18.34477 ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.30928  -4.89743  -21.38504 1.000 21.12348 ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.95666  -4.16053  -22.15130 1.000 20.23005 ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.07058  -5.28962  -18.98559 1.000 19.21239 ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.62512  -3.96660  -18.98558 1.000 21.76951 ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -4.96017  -4.92122  -21.38851 1.000 18.92732 ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.22226  -4.05382  -22.28426 1.000 20.05848 ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.51073  -4.39859  -23.73177 1.000 21.22480 ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.63630  -3.49646  -24.57446 1.000 19.93205 ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.72886  -4.20577  -22.01395 1.000 19.69610 ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.27755  -3.51863  -20.70185 1.000 30.32425 ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -3.06273  -2.75840  -20.04532 1.000 29.21463 ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -1.09462  -3.74827  -20.31638 1.000 31.77466 ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.62855  -5.71000  -24.03439 1.000 19.05111 ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -4.94854  -6.16969  -25.39066 1.000 19.20137 ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.35599  -5.75990  -25.82067 1.000 19.49397 ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.59621  -5.40588  -26.97960 1.000 18.85522 ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.80833  -7.69290  -25.47065 1.000 20.46286 ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.28740  -5.80965  -24.88396 1.000 17.79589 ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.65727  -5.38565  -25.16498 1.000 19.50814 ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.71313  -3.88749  -25.38836 1.000 19.67948 ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.43550  -3.43445  -26.28581 1.000 20.79968 ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.57922  -5.80443  -24.02333 1.000 18.87508 ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.80145  -7.32111  -24.03816 1.000 16.74793 ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.18358 -7.84313  -22.60945 1.000 19.66261 ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.89975 -7.70507  -25.05091 1.000 19.50905 ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.95886  -3.10282  -24.59216 1.000 19.47342 ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.90840  -1.65202  -24.82097 1.000 18.80855 ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.43018  -1.33263  -26.23082 1.000 22.20121 ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.93690  -0.40810  -26.86973 1.000 20.05617 ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.95702  -0.94327  -23.83488 1.000 18.60577 ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.43420  -0.94721  -22.40297 1.000 22.10456 ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.59960  -1.30985  -22.11193 1.000 26.19793 ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.62092  -0.53919  -21.54171 1.000 25.71374 ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.44900  -2.10640  -26.73362 1.000 19.85648 ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.86857  -1.82291  -28.03098 1.000 19.82862 ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.86902  -2.04942  -29.14541 1.000 20.01652 ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -6.99679  -1.20140  -30.03862 1.000 23.02935 ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.60828  -2.67787  -28.22387 1.000 24.18956 ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.42304  -2.22372  -27.37969 1.000 25.96861 ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.28056  -3.23567  -27.56103 1.000 26.53890 ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.16737  -3.03275  -26.52045 1.000 29.58050 ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? -0.06568  -4.06793  -26.67565 1.000 36.46161 ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.61540  -3.16076  -29.11530 1.000 20.12213 ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.58343  -3.35038  -30.20509 1.000 19.63017 ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.75517  -2.37928  -30.04599 1.000 22.73850 ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.29517 -1.88760  -31.05356 1.000 23.83117 ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -9.04148  -4.83152  -30.30796 1.000 22.02370 ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.88971  -5.05701  -31.59314 1.000 21.62248 ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.83668  -5.27248  -29.07364 1.000 20.40866 ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -9.13714  -4.82977  -32.87221 1.000 25.47997 ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.13694 -2.03019  -28.81253 1.000 20.44435 ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.17915 -1.01531  -28.65217 1.000 21.92378 ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.74422 0.31759   -29.25299 1.000 21.99502 ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.49825 0.95092   -29.99899 1.000 24.69352 ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.55578 -0.83450  -27.18570 1.000 25.04300 ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.69039 0.19466   -27.07864 1.000 31.49907 ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -13.13054 0.35061   -25.66579 1.000 44.35770 ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.21413 -0.54231  -25.27714 1.000 48.21617 ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.37697 -0.95452  -24.02679 1.000 54.06727 ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.51259 -0.62085  -23.07772 1.000 43.21404 ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.42678 -1.71620  -23.71934 1.000 40.90974 ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.49371  0.73730   -29.00164 1.000 20.55953 ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -9.04903  2.00719   -29.55156 1.000 22.88551 ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -9.08042  1.95923   -31.07565 1.000 24.95032 ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.52710  2.90548   -31.72861 1.000 24.86966 ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.63352  2.33876   -29.06115 1.000 22.63780 ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.18571  3.71490   -29.57177 1.000 25.61536 ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.69468  4.90531   -29.03628 1.000 26.02613 ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.29596  3.80890   -30.64001 1.000 25.66427 ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.31769  6.13070   -29.53309 1.000 27.31511 ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.90488  5.03083   -31.14577 1.000 29.62447 ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.41166  6.18995   -30.58824 1.000 30.22040 ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -6.03435  7.40817   -31.07995 1.000 34.20325 ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.61245  0.85575   -31.66160 1.000 25.41170 ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.59116  0.80086   -33.12306 1.000 28.38060 ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -9.98786  0.81377   -33.69792 1.000 29.73177 ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.20777 1.35607   -34.78722 1.000 30.42248 ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.90318  -0.45753  -33.62295 1.000 29.30885 ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.41436  -0.47049  -33.37744 1.000 29.19768 ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.71442  -1.54454  -34.18676 1.000 46.20187 ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -4.50072  -1.37522  -34.44860 1.000 56.67374 ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -6.38273  -2.50023  -34.64018 1.000 51.53810 ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.94035 0.22717   -32.98693 1.000 27.28408 ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.31909 0.20533   -33.47222 1.000 29.44113 ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -12.99279 1.57162   -33.41192 1.000 29.77318 ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -14.03096 1.77722   -34.06220 1.000 30.22831 ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.12610 -0.80170  -32.65540 1.000 27.00889 ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.52173 -0.26465  -31.37811 1.000 30.76004 ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.44781 2.51825   -32.64842 1.000 27.46145 ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -13.08592 3.82670   -32.56961 1.000 32.88920 ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -13.07589 4.51620   -33.91199 1.000 32.54722 ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.99784 5.26884   -34.23039 1.000 42.27462 ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.37572 4.70928   -31.54290 1.000 28.97478 ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.49692 4.18064   -30.11736 1.000 30.14630 ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.82154 5.18065   -29.19337 1.000 30.61472 ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.92601 3.96626   -29.69548 1.000 31.76514 ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -12.03293 4.31170   -34.69670 1.000 32.79174 ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -11.95130 4.93817   -36.00612 1.000 36.97028 ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.20587 3.95789   -37.14319 1.000 40.23936 ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.30268 4.39354   -38.29300 1.000 45.42328 ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.58020 5.60997   -36.20132 1.000 44.00417 ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.53712  4.63154   -36.10929 1.000 44.85841 ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.36116 6.74795   -35.19255 1.000 41.12202 ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.35497 2.67581   -36.85452 1.000 36.50017 ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.55462 1.65927   -37.89881 1.000 36.51644 ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.37528 0.51750   -37.29340 1.000 34.61922 ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.81962 -0.46098  -36.76877 1.000 34.34075 ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -11.21238 1.15588   -38.43257 1.000 34.74938 ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.36876 0.13551   -39.56456 1.000 50.01782 ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.51959 -0.21184  -39.92186 1.000 44.92344 ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.33296 -0.31867  -40.09934 1.000 47.02467 ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.70907 0.61843   -37.33772 1.000 39.79229 ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.53716 -0.43358  -36.72501 1.000 36.78136 ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.31131 -1.81702  -37.32174 1.000 35.02566 ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.60729 -2.81247  -36.64174 1.000 39.08171 ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.97155 0.03363   -36.99833 1.000 41.48535 ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.88247 1.37163   -37.56351 1.000 47.23260 ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.47987 1.84791   -37.57169 1.000 44.60017 ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.83603 -1.91371  -38.57782 1.000 36.98492 ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.61428 -3.22710  -39.16497 1.000 36.06684 ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.52774 -4.00614  -38.43628 1.000 34.43990 ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.43812 -5.22541  -38.61196 1.000 34.40563 ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.24876 -3.12233  -40.64389 1.000 34.51478 ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -12.91589 -2.67450  -40.80092 1.000 41.03498 ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.72317 -3.35089  -37.59140 1.000 29.56160 ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.77296 -4.11211  -36.79752 1.000 31.65485 ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.47096 -5.09331  -35.87189 1.000 32.07071 ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.83658 -6.02403  -35.35793 1.000 29.31948 ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.92298 -3.15785  -35.96963 1.000 34.85011 ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -10.13358 -2.21798  -36.85729 1.000 43.61649 ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.67634  -2.55401  -36.82680 1.000 36.59160 ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.88214  -1.70695  -37.79003 1.000 42.76924 ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.53085  -2.34627  -37.85691 1.000 50.66593 ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.74718 -4.87693  -35.57094 1.000 29.98533 ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.47060 -5.81520  -34.72438 1.000 28.86852 ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.28881 -6.82241  -35.52744 1.000 29.52521 ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -16.04111 -7.59298  -34.92941 1.000 31.68696 ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.38208 -5.06780  -33.73784 1.000 30.10064 ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.66365 -4.15062  -32.74924 1.000 33.60811 ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.67113 -3.50647  -31.82445 1.000 33.31559 ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.64592 -4.96228  -31.93824 1.000 29.06343 ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -15.07942 -6.91278  -36.83810 1.000 31.19633 ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.77733 -7.93855  -37.61182 1.000 34.36338 ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.43252 -9.34110  -37.10963 1.000 31.82788 ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.19373 -10.28721 -37.33023 1.000 36.88860 ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.42884 -7.79133  -39.09264 1.000 40.31100 ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -16.12622 -6.58463  -39.76910 1.000 49.41778 ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -16.89780 -5.83954  -39.11498 1.000 42.44949 ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.85529 -6.34027  -40.96866 1.000 50.40745 ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.27947 -9.49605  -36.47964 1.000 32.05070 ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.77835 -10.74609 -35.93823 1.000 31.66901 ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.28815 -11.03837 -34.53601 1.000 37.20486 ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -13.78303 -11.95633 -33.87180 1.000 36.80407 ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.24775 -10.70072 -35.96036 1.000 29.03761 ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.75483 -9.48494  -35.39194 1.000 27.90710 ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.25154 -10.25328 -34.05492 1.000 32.38200 ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.78316 -10.46317 -32.72849 1.000 37.02965 ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -16.06061 -9.13893  -32.05287 1.000 32.96845 ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.13654 -8.36714  -31.78902 1.000 28.29527 ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.33144 -8.84424  -31.77644 1.000 29.51435 ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.65493 -7.56153  -31.15246 1.000 30.59899 ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.47852 -7.56818  -29.63379 1.000 26.78464 ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.29668 -6.50337  -29.03884 1.000 34.71360 ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -19.09699 -7.16789  -31.47895 1.000 30.98436 ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.26432 -6.74851  -32.93647 1.000 42.23787 ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.54495 -5.95195  -33.12691 1.000 59.67311 ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.62793 -5.37115  -34.51794 1.000 63.79202 ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -20.43268 -6.44397  -35.51995 1.000 64.76913 ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.55404 -8.72349  -28.98807 1.000 29.19154 ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.53400 -8.74434  -27.52678 1.000 26.09485 ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.12161 -8.65052  -26.99171 1.000 25.77658 ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.25030 -9.35751  -27.46428 1.000 27.32133 ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -18.22048 -10.00777 -27.03414 1.000 37.60459 ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -18.87122 -9.84047  -25.65158 1.000 62.28221 ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -19.09435 -11.16421 -24.93069 1.000 67.67118 ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -19.16907 -12.21435 -25.62628 1.000 66.03462 ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -19.10550 -11.15680 -23.67040 1.000 55.67104 ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -15.90526 -7.75901  -26.03892 1.000 24.84618 ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.60379 -7.53599  -25.41706 1.000 22.20082 ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.64757 -8.07486  -23.98619 1.000 20.35276 ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.31440 -7.50291  -23.11607 1.000 23.52331 ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.29492 -6.03647  -25.46368 1.000 23.99034 ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.17402 -5.48401  -26.90161 1.000 27.35087 ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.57760 -4.09753  -26.81721 1.000 32.40959 ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.29436 -6.34676  -27.80222 1.000 24.62890 ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -14.00077 -9.21946  -23.76019 1.000 19.03540 ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.14839 -9.85316  -22.45133 1.000 22.00837 ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -12.98158 -10.77987 -22.18626 1.000 19.47068 ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.15752 -11.04356 -23.06389 1.000 17.77552 ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.47972 -10.62390 -22.38731 1.000 20.84927 ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.52474 -11.79310 -23.31259 1.000 23.00844 ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.46192 -11.90771 -24.29795 1.000 42.64504 ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.69485 -12.85588 -23.46605 1.000 31.61338 ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.25878 -13.01628 -24.97984 1.000 30.81316 ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.19723 -13.61542 -24.49495 1.000 35.10234 ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -12.97410 -11.32147 -20.96944 1.000 18.30299 ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -11.98389 -12.23888 -20.43807 1.000 18.61155 ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.69585 -13.43705 -19.81442 1.000 18.46619 ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.61498 -13.25527 -19.00351 1.000 20.52901 ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.10104 -11.53761 -19.37870 1.000 20.35363 ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.41792 -10.29044 -19.98184 1.000 19.83706 ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -10.12635 -12.55518 -18.75089 1.000 19.13299 ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.66652  -9.43159  -18.90806 1.000 20.42933 ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.30014 -14.64697 -20.21892 1.000 17.31734 ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.82144 -15.87790 -19.62137 1.000 17.85408 ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.68399 -16.58300 -18.88432 1.000 19.77899 ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.56032 -16.68149 -19.37288 1.000 17.36003 ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.41497 -16.83119 -20.66375 1.000 19.55106 ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.61251 -16.25558 -21.36442 1.000 21.11271 ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.35534 -15.46000 -20.77594 1.000 21.94334 ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.87139 -16.71478 -22.60753 1.000 23.75724 ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -11.99008 -17.14404 -17.73304 1.000 17.52043 ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -11.06147 -17.95970 -16.98150 1.000 15.75802 ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.63878 -19.36200 -16.94551 1.000 15.13477 ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.77828 -19.56857 -16.49575 1.000 18.24124 ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.89046 -17.41146 -15.56996 1.000 19.60466 ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.51253 -15.91909 -15.44843 1.000 19.48711 ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.51552 -15.61853 -13.93902 1.000 20.45510 ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.17623  -15.66821 -16.08871 1.000 18.24412 ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.88422 -20.31772 -17.48321 1.000 18.64723 ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.40298 -21.66080 -17.70747 1.000 19.27822 ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.50090 -22.64471 -17.00357 1.000 22.20783 ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.48192  -23.05834 -17.55756 1.000 20.27233 ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.51731 -22.00038 -19.20445 1.000 20.87889 ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.27688 -20.89496 -19.91810 1.000 19.38323 ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.19579 -23.37341 -19.34389 1.000 21.40205 ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.44839 -21.04354 -21.44381 1.000 21.47770 ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.88175 -23.11615 -15.82240 1.000 19.16107 ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.15241 -24.19794 -15.16063 1.000 20.70518 ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.59938 -25.55149 -15.69100 1.000 22.52857 ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.76174 -25.75559 -16.05412 1.000 24.58395 ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.53447 -24.02169 -13.68610 1.000 21.57672 ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.92980 -23.44303 -13.73309 1.000 24.27553 ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -12.09291 -22.70926 -15.05484 1.000 23.53394 ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.64673  -26.48657 -15.75707 1.000 21.95348 ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.90031  -27.85150 -16.19770 1.000 22.93437 ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -9.04842  -28.77248 -15.33482 1.000 27.55619 ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.85307  -28.93676 -15.58276 1.000 26.83865 ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.61636  -28.04395 -17.68759 1.000 27.34593 ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -10.10531 -29.39212 -18.19353 1.000 33.21456 ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.84650  -30.44194 -17.58324 1.000 33.63577 ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.83908 -29.37184 -19.29261 1.000 39.43299 ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.68205  -29.42835 -14.36188 1.000 26.29561 ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -8.93805  -30.25504 -13.42924 1.000 26.74188 ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.47583  -31.55361 -14.07790 1.000 31.22450 ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.48171  -32.12622 -13.63952 1.000 35.55241 ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.78295  -30.56502 -12.18753 1.000 28.71089 ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -10.00173 -29.33396 -11.28766 1.000 31.19542 ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.75548 -29.72461 -10.03487 1.000 33.38144 ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.21285 -28.52555 -9.20139  1.000 36.04746 ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -12.17520 -27.68190 -9.96382  1.000 39.52187 ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.17005  -32.02821 -15.11988 1.000 31.30249 ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.75967  -33.29126 -15.73389 1.000 38.74421 ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.46002  -33.12060 -16.50813 1.000 35.91765 ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.57902  -33.98121 -16.43986 1.000 39.91128 ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.84567  -33.85114 -16.65415 1.000 42.69812 ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -11.16493 -34.31025 -15.99834 1.000 64.44792 ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -11.75881 -33.30556 -15.00724 1.000 73.85605 ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -11.84219 -33.57492 -13.79601 1.000 68.24655 ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -12.13857 -32.12045 -15.51627 1.000 63.26308 ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.32421  -32.00939 -17.22027 1.000 28.50171 ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.12839  -31.63874 -17.97553 1.000 29.41519 ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.10670  -30.90711 -17.11524 1.000 28.41914 ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -3.98619  -30.68577 -17.57879 1.000 28.16285 ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.48483  -30.71060 -19.14359 1.000 34.98068 ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.42239  -31.35665 -20.14287 1.000 43.97151 ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.65913  -32.58789 -20.06024 1.000 49.25138 ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.94888  -30.60322 -20.99085 1.000 46.81588 ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.48810  -30.51243 -15.90006 1.000 27.76564 ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.65141  -29.67327 -15.01650 1.000 23.53641 ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.22146  -28.37148 -15.70036 1.000 24.86313 ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -3.04955  -27.95602 -15.64110 1.000 24.97577 ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.43926  -30.44766 -14.48109 1.000 27.25166 ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -2.99156  -29.85443 -13.14764 1.000 26.43887 ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.58702  -30.12683 -12.78697 1.000 42.04278 ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -1.36513  -31.53489 -12.58530 1.000 46.85996 ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? -0.18134  -32.11568 -12.70096 1.000 52.29371 ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 0.89535   -31.42743 -13.06702 1.000 37.97413 ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? -0.07220  -33.40976 -12.42330 1.000 52.71017 ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.17847  -27.68383 -16.32775 1.000 22.92356 ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.88978  -26.43998 -17.00803 1.000 23.05681 ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.79167  -25.33319 -16.50897 1.000 21.07100 ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.96169  -25.55717 -16.18761 1.000 20.99832 ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -5.03962  -26.55247 -18.53319 1.000 21.53141 ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.37584  -27.00309 -18.85078 1.000 24.44242 ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -3.98577  -27.49063 -19.09475 1.000 23.12162 ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.24490  -24.13158 -16.43306 1.000 17.98480 ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -6.01963  -22.92040 -16.26696 1.000 18.39376 ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.80774  -22.09465 -17.52638 1.000 20.43976 ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.66346  -21.78688 -17.88121 1.000 20.29847 ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.58136  -22.10622 -15.03156 1.000 18.66791 ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.32026  -20.77307 -14.84703 1.000 17.43053 ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.83178  -21.00984 -14.58754 1.000 19.79181 ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.71615  -19.98529 -13.67175 1.000 20.60872 ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.88883  -21.74319 -18.22325 1.000 17.72289 ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.79893  -21.00834 -19.46965 1.000 19.58128 ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.40687  -19.62554 -19.28038 1.000 20.29399 ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.50508  -19.49199 -18.70265 1.000 19.99570 ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.53591  -21.74212 -20.59261 1.000 20.36535 ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.98411  -23.05541 -20.79971 1.000 19.65788 ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.45608  -20.90871 -21.87182 1.000 22.45379 ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.68044  -18.59509 -19.69082 1.000 16.79343 ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.13847  -17.21414 -19.64729 1.000 17.07804 ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.37759  -16.82262 -21.09467 1.000 20.84104 ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.40791  -16.74384 -21.86169 1.000 20.02103 ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.11624  -16.27417 -18.99815 1.000 19.81549 ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.81857  -16.64847 -17.53293 1.000 23.16236 ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.60812  -14.85870 -19.01944 1.000 18.99622 ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.67865  -17.58677 -17.26385 1.000 28.63017 ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.61988  -16.54671 -21.48416 1.000 17.82950 ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -8.98325  -16.21385 -22.85841 1.000 18.30829 ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.38520  -14.76278 -22.89593 1.000 20.86969 ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.23003 -14.34445 -22.09370 1.000 20.77032 ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.17695 -17.04865 -23.37536 1.000 20.84818 ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.40142 -16.80269 -24.86486 1.000 21.58409 ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -9.93243  -18.52610 -23.10365 1.000 22.72352 ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -8.91533  -14.02388 -23.89923 1.000 18.98865 ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.41737  -12.66374 -24.09370 1.000 19.12157 ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.68059  -12.44997 -25.56771 1.000 20.87969 ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.12872  -13.14264 -26.43102 1.000 19.65136 ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.42880  -11.61698 -23.50904 1.000 18.70654 ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.15100  -11.45792 -24.35148 1.000 20.57268 ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -7.18168  -11.11616 -25.57440 1.000 21.07476 ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -6.08136  -11.82808 -23.78675 1.000 21.49169 ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.56400 -11.51899 -25.87122 1.000 17.56050 ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -10.85711 -11.17471 -27.24932 1.000 18.20623 ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.21232 -9.83560  -27.60471 1.000 22.51254 ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.77710 -8.99715  -28.30321 1.000 20.40759 ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.36376 -11.14424 -27.48444 1.000 20.88069 ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -12.97712 -10.31223 -26.49015 1.000 21.51199 ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -12.94614 -12.57963 -27.35886 1.000 21.07736 ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -8.98067  -9.64209  -27.14725 1.000 19.95838 ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.28697  -8.41889  -27.48224 1.000 22.14235 ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.68646  -8.43714  -28.87509 1.000 21.74333 ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -8.08689  -9.20288  -29.76018 1.000 20.80142 ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.68539  -7.57175  -29.05615 1.000 20.34498 ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.14680  -7.36051  -30.41021 1.000 21.41980 ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.39361  -8.57927  -30.95491 1.000 22.23500 ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.25612  -8.70830  -32.17929 1.000 21.80667 ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.28047  -6.08159  -30.42774 1.000 20.56644 ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -4.97159  -5.61086  -31.85946 1.000 27.02310 ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -4.01810  -6.27861  -29.57075 1.000 18.57606 ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.63515  -4.13284  -31.90003 1.000 28.53394 ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -4.89744  -9.48656  -30.10568 1.000 18.82857 ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.15009  -10.63267 -30.59571 1.000 18.43727 ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.72794  -10.24023 -30.95277 1.000 19.22344 ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.29681  -9.10365  -30.79750 1.000 22.04960 ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -1.98150  -11.22895 -31.41554 1.000 19.61967 ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.55642  -11.05952 -31.71875 1.000 20.13668 ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.29610  -11.65560 -33.08451 1.000 20.87162 ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -0.83257  -12.71674 -33.42033 1.000 21.67812 ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.28816   -11.78070 -30.66393 1.000 22.28975 ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.34021   -10.96611 -29.35166 1.000 22.67112 ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.37201   -11.77444 -28.11793 1.000 24.27943 ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.20942   -13.09984 -27.62132 1.000 25.18006 ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.54049   -10.97088 -33.87088 1.000 21.90065 ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 1.05455   -11.54912 -35.11146 1.000 23.84559 ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 2.15015   -12.56643 -34.78819 1.000 21.30358 ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.64128   -12.63917 -33.65861 1.000 20.41209 ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.64881   -10.45603 -35.99985 1.000 25.21141 ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.81065   -9.90974  -35.31962 1.000 24.27658 ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.58960   -9.37676  -36.27268 1.000 28.25178 ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.55503   -13.35433 -35.80420 1.000 22.81591 ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.67078   -14.28076 -35.62209 1.000 23.57962 ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 4.91366   -13.52945 -35.17806 1.000 22.27241 ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.63232   -13.97517 -34.28063 1.000 21.52917 ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 3.97065   -15.03143 -36.91316 1.000 25.39596 ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 4.97836   -16.14888 -36.70290 1.000 25.29671 ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 5.29357   -16.82362 -38.04938 1.000 26.08152 ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 6.17593   -18.04173 -37.80479 1.000 31.34879 ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 6.83738   -18.44231 -39.06945 1.000 34.29993 ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 5.16825   -12.36317 -35.79538 1.000 24.35514 ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 6.34012   -11.58435 -35.41167 1.000 28.60502 ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 6.24723   -11.13533 -33.96930 1.000 22.19108 ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 7.25402   -11.16905 -33.25078 1.000 26.30571 ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.52012   -10.38376 -36.33917 1.000 28.61848 ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 5.04462   -10.73369 -33.51761 1.000 23.22262 ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.84295   -10.40302 -32.10452 1.000 21.47262 ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 5.20826   -11.57170 -31.19452 1.000 22.19797 ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.90358   -11.40213 -30.18586 1.000 22.50868 ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.37525   -10.02320 -31.84112 1.000 25.03772 ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 2.98101   -8.65783  -32.37425 1.000 30.71769 ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 3.84982   -7.78308  -32.49195 1.000 30.01058 ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 1.76956   -8.46791  -32.67777 1.000 29.78911 ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.72800   -12.78108 -31.52668 1.000 20.91828 ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 4.99949   -13.92396 -30.67778 1.000 23.32896 ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.48435   -14.14022 -30.54164 1.000 22.31791 ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 6.98865   -14.31418 -29.42857 1.000 22.76563 ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.38317   -15.18604 -31.25326 1.000 21.80399 ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.89065   -15.27975 -31.05458 1.000 21.67787 ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.49761   -16.52075 -31.84491 1.000 20.25312 ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.44913   -15.35140 -29.54822 1.000 21.25713 ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 7.20011   -14.12224 -31.67002 1.000 21.79233 ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.63386   -14.37697 -31.63658 1.000 24.00835 ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 9.35266   -13.28375 -30.86301 1.000 23.52222 ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 10.28339  -13.56340 -30.08938 1.000 23.55138 ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 9.17720   -14.50175 -33.06947 1.000 22.24212 ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.56839   -15.74993 -33.70659 1.000 24.07638 ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.71610  -14.51710 -33.10631 1.000 23.25496 ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.71925   -15.75595 -35.23375 1.000 27.39583 ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 8.90142   -12.03779 -31.01097 1.000 24.29299 ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 9.51620   -10.90417 -30.31739 1.000 24.28280 ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 8.93080   -10.76999 -28.91155 1.000 22.04665 ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.33126   -9.76242  -28.54639 1.000 24.79347 ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.30358   -9.60883  -31.10759 1.000 25.06265 ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.29643  -9.45629  -32.22354 1.000 44.21422 ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 11.42577  -8.99328  -32.00058 1.000 49.31382 ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 9.91417   -9.90418  -33.43830 1.000 47.74565 ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 9.12662   -11.83058 -28.12178 1.000 22.80815 ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.75757   -11.86430 -26.70820 1.000 23.16294 ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.31157   -11.47691 -26.45859 1.000 23.13039 ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 6.98807   -10.73338 -25.52920 1.000 23.78490 ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.72272   -10.99193 -25.91602 1.000 20.43385 ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.15144  -11.47547 -26.07889 1.000 22.29902 ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.43778  -12.66746 -25.86209 1.000 23.65889 ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 12.05231  -10.57513 -26.41064 1.000 27.53685 ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.43306   -12.05416 -27.26823 1.000 20.07480 ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 4.97186   -11.88914 -27.09139 1.000 21.46342 ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.58367   -10.41785 -27.03671 1.000 22.54899 ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.83046   -9.97216  -26.15141 1.000 23.68328 ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.47608   -12.62563 -25.84959 1.000 20.35070 ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.83952   -14.13020 -25.95033 1.000 27.32210 ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 6.08977   -14.56321 -25.13657 1.000 25.82634 ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.66601   -15.04840 -25.69258 1.000 37.27479 ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 5.13602   -9.64433  -27.97110 1.000 23.32478 ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.79054   -8.23259  -28.08856 1.000 25.38518 ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.30080   -7.33420  -26.98735 1.000 28.46395 ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.75501   -6.22565  -26.80193 1.000 32.82465 ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.36160   -7.74301  -26.26824 1.000 24.86757 ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.88592   -6.96932  -25.15199 1.000 23.69389 ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.26558   -6.45568  -25.52076 1.000 25.17707 ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.89695   -6.93717  -26.47454 1.000 28.05529 ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 6.99601   -7.77386  -23.84125 1.000 23.67162 ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 8.05146   -8.73763  -23.96258 1.000 27.01793 ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.72841   -8.51925  -23.50484 1.000 26.74697 ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.72535   -5.45761  -24.77325 1.000 22.72158 ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 10.12207  -5.04324  -24.83757 1.000 23.05475 ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.86219  -5.74717  -23.70861 1.000 21.94161 ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.48208  -5.10549  -22.84625 1.000 22.62507 ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.26356  -3.51090  -24.82250 1.000 33.23941 ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.53758   -2.87110  -23.63184 1.000 27.16048 ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.66638   -2.93946  -26.11358 1.000 28.83233 ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 9.94035   -1.41602  -23.42180 1.000 33.92372 ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 10.90813  -7.08408  -23.79606 1.000 23.95629 ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.30308  -7.87141  -22.64638 1.000 21.55934 ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.78079  -7.71276  -22.31928 1.000 24.75589 ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.14428  -7.87127  -21.15926 1.000 23.20487 ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 10.98249  -9.36269  -22.85012 1.000 26.58737 ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.65265  -7.44669  -23.30043 1.000 23.21324 ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.06040  -7.28197  -22.92579 1.000 26.02603 ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.23548  -6.06439  -22.01500 1.000 32.47024 ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 15.82021  -6.17037  -20.92757 1.000 31.26339 ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.96009  -7.19986  -24.17260 1.000 25.32788 ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.46290  -7.10473  -23.87934 1.000 34.69801 ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.28873  -6.78308  -25.13711 1.000 34.62240 ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 19.76865  -6.73338  -24.77997 1.000 54.17916 ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.03885  -5.57650  -23.88759 1.000 73.14568 ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.73529  -4.89134  -22.42631 1.000 27.39739 ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 14.90860  -3.73539  -21.56250 1.000 30.87242 ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.06605  -3.85335  -20.30239 1.000 30.04781 ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.48190  -3.36123  -19.24574 1.000 33.02811 ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.62299  -2.41975  -22.30386 1.000 37.11678 ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.26909  -2.34857  -22.70122 1.000 39.80626 ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 12.90387  -4.50855  -20.36478 1.000 27.62230 ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.10889  -4.65737  -19.14813 1.000 27.88440 ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.75733  -5.57932  -18.13588 1.000 28.11346 ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.71314  -5.31651  -16.93073 1.000 28.66489 ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.36785  -6.67637  -18.60686 1.000 24.89191 ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.09041  -7.56102  -17.68779 1.000 26.84275 ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.23940  -6.83564  -17.01710 1.000 32.10357 ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.44900  -6.98396  -15.81231 1.000 34.07041 ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.63588  -8.76166  -18.45120 1.000 24.78517 ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.48340  -9.47014  -18.97589 1.000 26.48556 ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.43826  -9.64031  -17.51939 1.000 28.24103 ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 15.99140  -6.06406  -17.79515 1.000 32.55275 ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.08593  -5.27221  -17.24756 1.000 37.32652 ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.59516  -4.36746  -16.11773 1.000 39.39870 ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.19094  -4.32666  -15.03476 1.000 42.36223 ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.74938  -4.48079  -18.38006 1.000 39.20932 ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 18.87802  -3.53051  -17.96324 1.000 57.35173 ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.34263  -2.68577  -19.16182 1.000 55.56138 ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.63214  -1.93386  -18.85914 1.000 68.73076 ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 21.26569  -2.40955  -17.60593 1.000 69.72894 ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.51393  -3.62547  -16.35178 1.000 38.14768 ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 15.00389  -2.75111  -15.29816 1.000 40.27717 ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.50385  -3.55898  -14.10267 1.000 40.32914 ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.72970  -3.18394  -12.94513 1.000 42.28181 ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 13.88260  -1.87972  -15.86286 1.000 40.48675 ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.79542  -4.65913  -14.36551 1.000 37.92713 ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.23001  -5.45199  -13.28015 1.000 34.22149 ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.32487  -6.00467  -12.38805 1.000 36.71486 ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.24828  -5.92711  -11.15937 1.000 38.97232 ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.40078  -6.57949  -13.88420 1.000 30.38178 ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.76316  -7.50514  -12.89038 1.000 28.37345 ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.13776  -7.03346  -11.71922 1.000 30.11691 ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.70343  -8.86179  -13.17550 1.000 31.54626 ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.50383  -7.93000  -10.84399 1.000 29.11410 ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.05187  -9.76050  -12.31200 1.000 31.61457 ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.44663  -9.29423  -11.16250 1.000 29.67496 ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.38075  -6.52373  -12.98848 1.000 39.08726 ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.37720  -7.16929  -12.16475 1.000 47.07885 ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.21588  -6.14915  -11.39552 1.000 54.42069 ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.68083  -6.44050  -10.28475 1.000 48.54715 ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.18635  -8.09863  -13.05395 1.000 56.17738 ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 16.68309  -9.55492  -12.92122 1.000 34.49486 ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 17.84919  -10.37870 -13.97350 1.000 73.30150 ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 16.90829  -11.58467 -14.84809 1.000 41.18344 ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.36278  -4.92893  -11.91701 1.000 46.30231 ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 17.94837  -3.86361  -11.10732 1.000 51.21871 ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.05428  -3.53018  -9.91968  1.000 54.33088 ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.53304  -3.30040  -8.79641  1.000 55.49022 ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.17116  -2.62299  -11.96948 1.000 52.90787 ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.29856  -2.78319  -12.99050 1.000 75.17039 ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.32374  -1.66101  -14.02352 1.000 82.32256 ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 18.58973  -0.66953  -13.83379 1.000 83.03162 ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 20.06012  -1.77923  -15.03426 1.000 88.31963 ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.74869  -3.48629  -10.15024 1.000 48.53112 ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 14.81761  -3.19984  -9.07189  1.000 49.12364 ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 14.88926  -4.25961  -7.98505  1.000 49.20969 ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 14.75828  -3.94114  -6.80040  1.000 51.96920 ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.40110  -3.09559  -9.62710  1.000 45.51663 ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.09197  -5.52493  -8.36806  1.000 47.18573 ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.04925  -6.62117  -7.40239  1.000 46.12520 ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.21101  -6.54162  -6.43121  1.000 61.08457 ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.03372  -6.70430  -5.21480  1.000 56.61309 ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.06679  -7.96237  -8.12986  1.000 42.24522 ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.76445  -8.33133  -8.83683  1.000 37.60737 ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 13.92353  -9.63498  -9.59775  1.000 42.59430 ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.65526  -8.39779  -7.77383  1.000 41.56028 ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.40221  -6.28960  -6.94263  1.000 55.15499 ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.51491  -6.19300  -6.02368  1.000 59.58524 ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.49895  -4.85517  -5.29021  1.000 68.78531 ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.30225  -4.64940  -4.37609  1.000 73.20303 ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 19.82266  -6.44436  -6.78974  1.000 65.14929 ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.04211  -5.63375  -8.05750  1.000 59.46562 ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 20.55821  -4.21794  -7.76111  1.000 83.92970 ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 20.35298  -3.66812  -6.67652  1.000 95.75171 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 21.18588  -3.60273  -8.76643  1.000 86.80174 ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.56887  -3.96631  -5.65756  1.000 71.36605 ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.37316  -2.66175  -5.03557  1.000 69.52981 ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 16.05060  -2.59625  -4.26445  1.000 83.10064 ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.39031  -1.54521  -4.22429  1.000 69.72436 ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 17.43902  -1.55816  -6.09166  1.000 64.06960 ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.63588  -3.73281  -3.67672  1.000 74.79488 ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.54073  -3.79470  -2.72600  1.000 64.50331 ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.30389  -4.53120  -3.21943  1.000 70.03090 ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.60755  -5.16358  -2.40985  1.000 61.17746 ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.01003  -4.45184  -4.51902  1.000 53.47600 ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 11.73411  -4.91729  -5.05348  1.000 41.68963 ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.56838  -6.41782  -4.84289  1.000 47.41559 ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.52166  -7.14095  -4.52684  1.000 46.29315 ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.63988  -4.61013  -6.55298  1.000 50.60787 ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.34625  -6.89498  -5.06474  1.000 39.94294 ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.09292  -8.32423  -5.08230  1.000 37.19788 ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.40176   -8.71845  -6.37608  1.000 35.33996 ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 8.98307   -7.87586  -7.17413  1.000 36.16891 ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.25305   -8.76631  -3.87775  1.000 43.14780 ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 7.88901   -8.12866  -3.86239  1.000 48.30513 ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.77843   -6.90962  -3.57502  1.000 55.61266 ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 6.94553   -8.84192  -4.24597  1.000 39.50607 ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.29905   -10.03605 -6.58389  1.000 32.87046 ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.75343   -10.54276 -7.82542  1.000 30.20536 ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.35759   -10.00857 -8.11006  1.000 37.94131 ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 6.96255   -9.91846  -9.27692  1.000 34.64306 ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.83623   -12.09588 -7.83746  1.000 33.17887 ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.30477  -12.50134 -8.10834  1.000 43.56340 ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 7.92075   -12.72424 -8.88970  1.000 34.62099 ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.67632  -13.93738 -7.76505  1.000 40.77788 ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.60925   -9.59393  -7.08420  1.000 35.94073 ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.24662   -9.13773  -7.36480  1.000 34.57497 ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.20562   -7.84579  -8.17075  1.000 34.99985 ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.13961   -7.50146  -8.70457  1.000 34.92343 ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.46475   -8.93114  -6.06537  1.000 31.54933 ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.77719   -7.67742  -5.47098  1.000 36.95239 ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.31109   -7.11488  -8.27107  1.000 32.48743 ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.28510   -5.86902  -9.01990  1.000 30.33641 ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.61678   -6.05612  -10.50901 1.000 27.54532 ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 6.73730   -5.05989  -11.22801 1.000 30.58178 ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.23202   -4.85617  -8.39315  1.000 35.95088 ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 6.80673   -4.56975  -6.94877  1.000 37.97007 ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.16307   -4.01610  -5.92315  1.000 48.73935 ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 8.20222   -2.39825  -6.74827  1.000 45.05230 ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.66513   -7.29773  -10.99191 1.000 24.52632 ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.11970   -7.61349  -12.34165 1.000 23.76339 ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.33193   -6.86097  -13.42695 1.000 26.72945 ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.89716   -6.47881  -14.46273 1.000 24.55432 ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.04901   -9.14387  -12.54604 1.000 26.49369 ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.69524   -9.56892  -13.89290 1.000 25.31154 ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.58735   -9.63812  -12.43630 1.000 25.99291 ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.78134   -11.04081 -14.03334 1.000 29.81345 ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.04135   -6.63320  -13.22068 1.000 26.49165 ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.24748   -6.01274  -14.27224 1.000 27.47654 ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.56897   -4.54268  -14.48479 1.000 29.47825 ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.25541   -4.00900  -15.54963 1.000 33.05396 ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.23197   -3.89224  -13.51845 1.000 29.63688 ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.68821   -2.52196  -13.69327 1.000 33.00802 ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.81878   -2.41975  -14.69177 1.000 32.68679 ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.16502   -1.31203  -15.10800 1.000 34.40409 ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.14013   -1.93384  -12.37079 1.000 33.77741 ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.07340   -2.02304  -11.28995 1.000 37.92135 ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.51093   -1.36227  -10.02971 1.000 47.94355 ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.23239   -0.34703  -10.05517 1.000 49.32292 ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.10144   -1.93370  -8.89796  1.000 49.95018 ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.39233   -3.55196  -15.07182 1.000 27.61235 ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.48589   -3.59107  -16.02373 1.000 28.16433 ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.07787   -4.24378  -17.33639 1.000 28.49520 ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 8.94088   -4.49040  -18.18929 1.000 31.94775 ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.68793   -4.30412  -15.38002 1.000 27.64916 ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.06020  -3.72543  -14.04381 1.000 29.77638 ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 9.55928   -4.27944  -12.87598 1.000 33.36492 ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 10.84179  -2.58654  -13.96312 1.000 39.56021 ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 9.86259   -3.74954  -11.64886 1.000 33.55375 ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 11.14601  -2.02134  -12.72274 1.000 42.64238 ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.64361  -2.61364  -11.55242 1.000 39.75635 ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.79067   -4.50056  -17.53641 1.000 25.94922 ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.35747   -4.89958  -18.84831 1.000 25.40778 ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.62112   -6.34680  -19.21258 1.000 27.36527 ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.41859   -6.72596  -20.36666 1.000 29.08004 ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.02782   -7.17692  -18.24669 1.000 22.03973 ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.30605   -8.58902  -18.47842 1.000 20.98095 ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.48984   -9.46412  -17.53258 1.000 23.16740 ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.87658   -10.60403 -17.23581 1.000 21.95624 ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.83352   -8.82708  -18.34208 1.000 20.85563 ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.59568   -8.11627  -19.46122 1.000 24.69514 ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.38895   -8.36200  -17.04688 1.000 24.08168 ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.27135   -9.01660  -17.17490 1.000 21.14215 ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.41326   -9.80657  -16.31448 1.000 20.35341 ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 3.99596   -11.14809 -16.86763 1.000 20.51937 ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.66967   -12.03578 -16.08527 1.000 21.12343 ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 3.98355   -11.31467 -18.20037 1.000 18.43798 ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.60321   -12.58834 -18.78028 1.000 20.16873 ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.41468   -13.72113 -18.15300 1.000 18.36203 ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.88450   -14.80561 -17.86434 1.000 18.10924 ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.80628   -12.56462 -20.30724 1.000 20.99140 ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.80264   -13.95548 -20.90285 1.000 19.59371 ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.59794   -14.65005 -21.07601 1.000 19.51230 ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 5.02569   -14.57804 -21.25645 1.000 20.22818 ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.55960   -15.94065 -21.61925 1.000 18.35610 ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 5.01085   -15.87678 -21.76129 1.000 19.48139 ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.77876   -16.57279 -21.94127 1.000 20.46335 ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.70883   -13.46727 -17.92395 1.000 19.23208 ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.59617   -14.55866 -17.53644 1.000 20.05689 ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.33646   -15.01985 -16.10781 1.000 20.79553 ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.80442   -16.10009 -15.73090 1.000 20.56334 ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.06384   -14.12978 -17.72917 1.000 16.54746 ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.35575   -13.84205 -19.20669 1.000 20.37444 ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.61822   -14.87345 -20.10606 1.000 19.25158 ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.31283   -12.53514 -19.69866 1.000 20.97829 ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.82411   -14.62688 -21.50019 1.000 18.50114 ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.50384   -12.28246 -21.06100 1.000 21.87587 ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.77324   -13.32464 -21.95360 1.000 22.86329 ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 8.94272   -13.02237 -23.29157 1.000 23.85333 ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.56116   -14.26224 -15.32526 1.000 18.73525 ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.10364   -14.72690 -14.02014 1.000 19.00677 ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.22406   -15.97838 -14.14441 1.000 18.33280 ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.01023   -16.66793 -13.12478 1.000 20.48966 ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.36123   -13.61999 -13.25742 1.000 20.23884 ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.05161   -13.40928 -13.79360 1.000 21.68612 ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.72227   -16.29572 -15.35028 1.000 19.33934 ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.05049   -17.58705 -15.54710 1.000 18.68014 ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.88549   -18.75506 -15.02951 1.000 17.96711 ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.32677   -19.76922 -14.55223 1.000 19.13641 ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.72354   -17.78740 -17.04137 1.000 17.34142 ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.24686   -18.64034 -15.13604 1.000 18.11560 ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.10653   -19.76396 -14.75337 1.000 19.94064 ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.27686   -19.87911 -13.23613 1.000 20.76114 ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 6.92439   -20.81634 -12.76050 1.000 22.54728 ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.46105   -19.67766 -15.49305 1.000 17.97623 ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.26613   -19.94424 -16.96852 1.000 20.05353 ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.26138   -21.24549 -17.45968 1.000 19.03837 ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 6.98568   -18.89190 -17.85454 1.000 18.50973 ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 7.00180   -21.51362 -18.80021 1.000 19.04425 ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.72039   -19.14334 -19.19684 1.000 19.36901 ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.75282   -20.43899 -19.66070 1.000 19.50417 ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.50934   -20.69742 -20.99668 1.000 20.14487 ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.63041   -19.00110 -12.45534 1.000 20.93288 ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.47216   -19.27778 -11.03628 1.000 20.23915 ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.63350   -20.52582 -10.78107 1.000 19.84014 ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.82044   -21.21182 -9.78196  1.000 23.82560 ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.78082   -18.09160 -10.33512 1.000 23.01600 ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.60463   -16.78915 -10.28922 1.000 20.90862 ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.74089   -15.62595 -9.79342  1.000 21.57383 ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.86481   -16.94439 -9.41054  1.000 23.51922 ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.65972   -20.80247 -11.66745 1.000 20.55948 ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.67711   -21.83999 -11.35596 1.000 21.31946 ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.59302   -22.87506 -12.47526 1.000 20.00594 ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.06985   -23.97014 -12.24580 1.000 23.30911 ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.26987   -21.25488 -11.07271 1.000 20.76669 ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.30647   -20.38023 -9.81149  1.000 21.34077 ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.70204   -20.46869 -12.28240 1.000 19.82666 ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.17708   -22.59827 -13.62904 1.000 21.83277 ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 3.00848   -23.46412 -14.79809 1.000 19.78781 ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.32594   -24.10884 -15.18297 1.000 21.68878 ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.34779   -23.41805 -15.28287 1.000 23.86977 ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.46004   -22.69732 -16.00021 1.000 21.99418 ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.28458   -25.43085 -15.42025 1.000 20.91903 ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.43749   -26.11113 -16.01706 1.000 22.23822 ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.54761   -25.89558 -17.52364 1.000 24.31293 ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.65591   -25.96308 -18.08139 1.000 24.20342 ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.37888   -27.60078 -15.67761 1.000 25.02235 ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.07811   -28.25496 -16.02269 1.000 35.31773 ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.07330   -29.76607 -15.77124 1.000 56.58177 ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 4.77304   -30.22266 -14.83106 1.000 53.69679 ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 3.33855   -30.49018 -16.49495 1.000 59.43855 ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.44128   -25.59494 -18.19150 1.000 22.17890 ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.41852   -25.35911 -19.63012 1.000 21.07653 ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.35303   -24.30407 -19.86702 1.000 17.53537 ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.33507   -24.29778 -19.17217 1.000 19.85899 ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.10490   -26.65009 -20.39610 1.000 22.82934 ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 4.09118   -26.46316 -21.92842 1.000 20.08689 ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 4.10574   -27.82468 -22.57219 1.000 31.17701 ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.71101   -28.33773 -22.82196 1.000 34.21551 ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.68812   -29.76954 -23.30820 1.000 45.91923 ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.62240   -23.36484 -20.76236 1.000 16.66656 ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.65958   -22.34649 -21.14502 1.000 15.44394 ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.46481   -22.42395 -22.64467 1.000 19.40807 ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.44357   -22.47358 -23.39634 1.000 18.25161 ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 3.12170   -20.95001 -20.72475 1.000 19.32707 ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 2.07520   -19.90355 -21.25050 1.000 21.44681 ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.30017   -20.90104 -19.18437 1.000 20.35047 ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 1.20220   -22.48913 -23.08652 1.000 18.26788 ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.84123   -22.47245 -24.49485 1.000 18.67865 ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 0.03492   -21.20589 -24.75090 1.000 20.86072 ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.90798  -20.90621 -24.01143 1.000 21.66089 ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? 0.00657   -23.70512 -24.86069 1.000 19.47825 ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.63942   -24.93673 -24.46527 1.000 23.91644 ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.25718  -23.73828 -26.37798 1.000 20.79208 ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.38628   -20.45370 -25.77216 1.000 19.58526 ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.30975  -19.21995 -26.09759 1.000 18.25067 ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -0.86704  -19.37604 -27.50791 1.000 19.51124 ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.09030  -19.56278 -28.46245 1.000 20.44972 ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.59475   -17.98675 -25.98423 1.000 17.49004 ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? -0.11913  -16.69396 -26.46774 1.000 20.24740 ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.21295   -17.84397 -24.54242 1.000 17.50058 ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.19560  -19.33981 -27.65508 1.000 17.49411 ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -2.84798  -19.41924 -28.95578 1.000 17.33234 ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.33718  -18.01311 -29.26287 1.000 18.47949 ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -3.92594  -17.35993 -28.38291 1.000 20.12499 ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -4.04445  -20.38073 -28.93761 1.000 20.81227 ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.72667  -21.70193 -28.22753 1.000 30.16810 ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.62471  -20.54189 -30.39056 1.000 22.11903 ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -2.83162  -22.60440 -28.97876 1.000 31.30987 ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -3.08652  -17.50652 -30.46902 1.000 17.99422 ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.41004  -16.10596 -30.70305 1.000 18.10965 ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -3.84947  -15.91188 -32.13781 1.000 21.17192 ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.41454  -16.63428 -33.04389 1.000 22.37189 ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.20272  -15.19244 -30.31401 1.000 18.49560 ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.64703  -13.82794 -30.25850 1.000 20.41675 ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -0.99602  -15.36066 -31.28169 1.000 20.50681 ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.70554  -14.91487 -32.33739 1.000 19.68747 ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.20851  -14.54864 -33.64699 1.000 20.61382 ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.34566  -13.03702 -33.70269 1.000 24.64301 ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -6.13245  -12.45185 -32.96026 1.000 23.16136 ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.56582  -15.22142 -33.93680 1.000 22.49077 ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.26502  -14.78511 -35.22877 1.000 24.68823 ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.46698  -15.27674 -36.44442 1.000 25.41087 ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.17665  -14.94446 -37.73812 1.000 27.98116 ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.21396  -13.51880 -38.12801 1.000 31.42869 ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.58404  -12.41246 -34.57492 1.000 23.34163 ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.63303  -10.99388 -34.87884 1.000 22.37280 ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.36780  -10.80242 -36.20437 1.000 29.16207 ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.28025  -11.64814 -37.10394 1.000 29.43255 ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.18133  -10.43874 -34.94227 1.000 25.39107 ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -3.08077  -8.93902  -35.04260 1.000 25.11078 ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.28846  -8.23196  -36.20444 1.000 29.84969 ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.70018  -8.02653  -34.11534 1.000 26.52570 ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -3.11040  -6.94467  -35.97127 1.000 36.00732 ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.73104  -6.80293  -34.71072 1.000 28.83399 ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -6.09727  -9.69257  -36.34004 1.000 24.04280 ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.78119  -9.44070  -37.60921 1.000 26.54948 ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.82366  -9.53625  -38.81322 1.000 28.73040 ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.24808  -9.93588  -39.91127 1.000 35.35866 ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.46248  -8.05931  -37.60446 1.000 29.66647 ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.72115  -8.02567  -36.77017 1.000 30.90024 ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.36610  -9.04955  -36.57562 1.000 37.42861 ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -9.11167  -6.82968  -36.31645 1.000 31.44443 ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.54931  -9.16168  -38.64896 1.000 33.03056 ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.60325  -9.06283  -39.76923 1.000 47.42411 ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.76405  -10.32570 -39.99303 1.000 58.25032 ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -1.74458  -10.25502 -40.70694 1.000 48.84147 ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.65349  -7.86230  -39.59047 1.000 43.89768 ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.38648  -6.51170  -39.57904 1.000 52.07422 ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.51693  -6.43106  -40.10790 1.000 48.64975 ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.81010  -5.52118  -39.06362 1.000 55.07930 ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -3.16718  -11.46930 -39.43502 1.000 40.98343 ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.34717  -12.67573 -39.50904 1.000 36.24484 ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.23161  -13.91835 -39.27850 1.000 40.49269 ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.43623  -13.83210 -39.01279 1.000 35.89608 ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -1.17451  -12.58132 -38.51610 1.000 36.25663 ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 0.10304   -13.27716 -39.01128 1.000 41.33419 ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? -0.03265  -14.13252 -39.91282 1.000 41.99176 ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.22916   -13.03288 -38.44964 1.000 34.68721 ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.61206  -15.08857 -39.39180 1.000 31.44930 ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.23638  -16.37476 -39.13944 1.000 34.33444 ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.18955  -16.71505 -37.65679 1.000 26.49470 ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.51542  -16.06630 -36.86914 1.000 29.50054 ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -2.52604  -17.46135 -39.93859 1.000 38.91764 ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -2.36837  -17.08560 -41.39269 1.000 54.64906 ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -3.70006  -17.09785 -42.12252 1.000 72.82704 ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -4.16222  -16.02525 -42.59277 1.000 79.09168 ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -4.29190  -18.19478 -42.22134 1.000 86.72277 ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -3.84813  -17.80547 -37.29932 1.000 26.80189 ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -3.82620  -18.26759 -35.92349 1.000 22.57486 ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.55215  -19.05693 -35.63593 1.000 25.23406 ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.22276  -19.99945 -36.37151 1.000 26.02013 ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -5.05200  -19.12546 -35.64745 1.000 23.47416 ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.25736  -19.41682 -34.14849 1.000 24.41795 ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.67899  -19.84155 -33.86855 1.000 29.11225 ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.61410  -19.13508 -34.22663 1.000 31.73719 ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -6.84993  -20.98004 -33.21248 1.000 28.37984 ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -1.84856  -18.66849 -34.57652 1.000 20.01929 ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.57065  -19.28056 -34.22334 1.000 20.91688 ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.60977  -19.80806 -32.79647 1.000 24.27865 ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.32036  -19.25756 -31.93570 1.000 21.76830 ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.58217   -18.26287 -34.34712 1.000 22.72600 ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 0.91961   -17.97762 -35.76798 1.000 28.06017 ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 1.71182   -18.84899 -36.47549 1.000 29.19429 ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 0.39875   -16.85625 -36.41405 1.000 30.13877 ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 2.01664   -18.62054 -37.84151 1.000 33.63124 ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 0.68167   -16.60917 -37.75584 1.000 33.90604 ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.48496   -17.49565 -38.45318 1.000 40.01842 ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 1.78786   -17.26012 -39.78106 1.000 53.21961 ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 0.21576   -20.83081 -32.52909 1.000 21.71210 ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.47599   -21.34028 -31.17536 1.000 19.74360 ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 1.95267   -21.18217 -30.82711 1.000 19.34145 ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.81487   -21.71250 -31.54589 1.000 21.00769 ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 0.07901   -22.81301 -31.07351 1.000 24.58479 ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 2.21426   -20.47275 -29.74600 1.000 18.49205 ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.51173   -20.40280 -29.08067 1.000 16.37685 ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.52166   -21.34850 -27.88247 1.000 22.64600 ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.50258   -21.53478 -27.22588 1.000 18.97364 ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.70954   -18.95575 -28.62545 1.000 17.81790 ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 4.93180   -18.58414 -27.84665 1.000 15.43107 ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 6.01433   -17.89231 -28.36095 1.000 16.12862 ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 5.19141   -18.79873 -26.45634 1.000 19.51431 ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 6.91717   -17.67594 -27.36377 1.000 17.54085 ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.44705   -18.21382 -26.18791 1.000 17.78157 ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.48001   -19.41644 -25.40722 1.000 17.77534 ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 7.01679   -18.21305 -24.89701 1.000 18.66748 ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 5.08028   -19.41949 -24.09409 1.000 18.30368 ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.34120   -18.83386 -23.89307 1.000 19.73189 ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.65342   -21.98668 -27.59446 1.000 18.16239 ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.71235   -22.84709 -26.42779 1.000 17.80376 ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 6.11408   -22.86504 -25.83923 1.000 19.16453 ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 7.11427   -22.82223 -26.57669 1.000 18.75041 ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.30851   -24.26769 -26.80609 1.000 21.70207 ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 4.02968   -25.22097 -25.64946 1.000 24.91198 ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 3.33401   -26.46836 -26.13026 1.000 32.19204 ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 3.95257   -27.25411 -26.91605 1.000 33.22750 ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 2.13370   -26.65333 -25.77662 1.000 34.96310 ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.21142   -22.96178 -24.50839 1.000 18.50158 ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.53657   -23.11060 -23.90040 1.000 18.73220 ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.37870   -23.78652 -22.55152 1.000 17.55764 ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.47380   -23.40892 -21.76910 1.000 17.35713 ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.25394   -21.76610 -23.73491 1.000 17.98505 ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.51609   -22.05066 -23.13734 1.000 18.71160 ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.27687   -24.73782 -22.25742 1.000 20.03101 ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.49129   -25.27002 -20.91354 1.000 20.83014 ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.74367   -24.67437 -20.29716 1.000 20.70612 ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.35959  -25.30783 -19.41996 1.000 24.13704 ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.59497   -26.79640 -20.94710 1.000 23.09162 ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.34150   -27.30982 -21.45750 1.000 27.35419 ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.11740  -23.47410 -20.73701 1.000 19.52710 ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.38479  -22.79085 -20.32748 1.000 22.40239 ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.54280  -23.64964 -20.83719 1.000 24.35216 ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.46235  -24.19670 -21.95043 1.000 26.49424 ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.37074  -22.49044 -18.79987 1.000 25.73712 ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.63086  -23.75405 -20.10776 1.000 24.20188 ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.75765  -24.49135 -20.62181 1.000 26.22949 ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.43372  -23.84715 -21.81126 1.000 27.18759 ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 16.23229  -24.50937 -22.49096 1.000 29.00662 ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 15.15331  -22.57848 -22.07032 1.000 22.64113 ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.89566  -21.82505 -23.05907 1.000 22.07956 ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.27836  -21.75731 -24.44329 1.000 20.43050 ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.85734  -21.10410 -25.30812 1.000 22.77788 ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 14.15470  -22.42067 -24.69231 1.000 20.22066 ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.62754  -22.41958 -26.05326 1.000 19.56844 ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 12.12117  -22.33409 -25.99813 1.000 20.78574 ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.49327  -22.62850 -24.98615 1.000 21.26288 ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 14.01263  -23.67909 -26.85260 1.000 23.93228 ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.40648  -24.84088 -26.27618 1.000 25.17524 ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.56782  -21.92432 -27.13001 1.000 19.92945 ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 10.12240  -21.88583 -27.34618 1.000 17.20759 ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.85271   -22.34203 -28.77012 1.000 19.93680 ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.72597  -22.35327 -29.64221 1.000 21.00094 ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.48352   -20.47119 -27.07817 1.000 19.03144 ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 9.98978   -19.36425 -27.99731 1.000 17.01360 ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 11.11345  -18.59274 -27.66560 1.000 20.20999 ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 9.29309   -19.06665 -29.15899 1.000 18.52254 ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 11.57411  -17.55441 -28.53623 1.000 20.76951 ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 9.70827   -18.08994 -30.01443 1.000 19.17106 ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.83945  -17.28478 -29.71068 1.000 20.29732 ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.61683   -22.76115 -29.00996 1.000 18.96688 ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 8.21104   -23.15412 -30.34365 1.000 19.51339 ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 7.10075   -22.25211 -30.84862 1.000 19.54180 ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 6.28166   -21.75037 -30.07832 1.000 18.85508 ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.74109   -24.63176 -30.44911 1.000 19.20015 ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.58766   -24.81979 -29.62682 1.000 23.65816 ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 8.87675   -25.63106 -30.05346 1.000 22.15536 ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 7.02974   -22.12736 -32.17079 1.000 18.78423 ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.89406   -21.47602 -32.83172 1.000 19.90213 ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.42392   -22.37593 -33.96217 1.000 24.30155 ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 6.23336   -22.86932 -34.75489 1.000 22.87951 ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 6.24533   -20.07559 -33.39184 1.000 20.84935 ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 4.99957   -19.45961 -34.13791 1.000 24.68528 ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.69720   -19.15606 -32.26473 1.000 21.89911 ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 4.09996   -22.53815 -34.08966 1.000 23.37305 ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.51820   -23.26461 -35.20041 1.000 24.71380 ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 2.20322   -22.61367 -35.59488 1.000 24.05885 ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.60519   -21.89334 -34.79144 1.000 22.98656 ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 3.31047   -24.74856 -34.85806 1.000 27.46596 ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 2.20108   -25.01814 -33.84359 1.000 29.91468 ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 2.34599   -26.38487 -33.16624 1.000 34.59558 ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.56225   -26.43989 -32.34704 1.000 46.98586 ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 4.07675   -27.54095 -31.80131 1.000 52.19030 ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 3.56790   -28.73946 -32.04475 1.000 49.15661 ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 5.14974   -27.43875 -31.01154 1.000 51.89745 ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.77416   -22.84645 -36.84225 1.000 27.07111 ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 0.41691   -22.49274 -37.22244 1.000 28.45124 ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.53564  -23.38408 -36.44987 1.000 35.92117 ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.29088  -24.58447 -36.28964 1.000 36.17189 ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 0.23043   -22.64943 -38.71855 1.000 35.99256 ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 1.10536   -21.71476 -39.35006 1.000 37.78843 ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? -1.17833  -22.29001 -39.08697 1.000 41.15693 ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.61289  -22.79156 -35.93562 1.000 27.85960 ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.53438  -23.53590 -35.10525 1.000 31.57258 ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.69078  -24.03633 -35.95523 1.000 37.85445 ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.42640  -23.23882 -36.54419 1.000 41.14065 ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -3.04735  -22.66101 -33.98238 1.000 30.12574 ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -3.89751  -23.43082 -32.99978 1.000 41.61030 ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -3.53084  -24.56138 -32.62803 1.000 51.15244 ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -4.95999  -22.92035 -32.62625 1.000 34.69023 ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -3.84213  -25.34685 -35.99605 1.000 45.34482 ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -4.94442  -26.03658 -36.64391 1.000 66.05001 ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.08644  -26.32417 -35.67925 1.000 56.55408 ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.08020  -26.94154 -36.08235 1.000 58.26915 ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.44009  -27.35203 -37.25263 1.000 63.53519 ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.57682  -28.01520 -36.30715 1.000 64.03558 ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -3.67118  -27.06193 -38.53304 1.000 48.74284 ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -5.95254  -25.90704 -34.42481 1.000 53.95266 ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -6.98106  -26.07272 -33.42842 1.000 57.51234 ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.23948  -25.26656 -33.73405 1.000 45.96286 ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.44232  -24.69790 -34.80870 1.000 44.90606 ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -9.11098  -25.25502 -32.74860 1.000 41.15825 ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.37102 -24.54785 -32.86476 1.000 40.08361 ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -10.15558 -23.07619 -33.20934 1.000 38.77930 ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.42199  -22.38881 -32.49737 1.000 32.76583 ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -11.12926 -24.73602 -31.55074 1.000 43.22623 ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -12.53481 -24.30413 -31.68099 1.000 35.99287 ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -13.40237 -25.29563 -32.45673 1.000 43.40030 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -13.19960 -26.52767 -32.42580 1.000 44.61603 ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -14.20866 -24.78594 -33.24020 1.000 46.83900 ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -10.73570 -22.56310 -34.29049 1.000 39.36603 ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.48910 -21.15678 -34.64060 1.000 38.73011 ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -11.04143 -20.19197 -33.59381 1.000 39.41456 ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -12.16388 -20.35565 -33.10652 1.000 41.83124 ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.20902 -20.99104 -35.97634 1.000 39.91871 ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -11.37259 -22.35897 -36.52113 1.000 47.97449 ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.22180 -23.35703 -35.43240 1.000 48.72939 ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.28289 -19.12501 -33.32214 1.000 32.33075 ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.54853 -18.23360 -32.19376 1.000 30.18399 ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.28413 -16.95177 -32.55937 1.000 46.93565 ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -11.83251 -16.29417 -31.66984 1.000 46.42821 ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -9.24130  -17.78263 -31.55896 1.000 28.53225 ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -8.72840  -18.69291 -30.49679 1.000 44.32467 ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -7.13210  -17.99165 -30.10480 1.000 41.00568 ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -7.64954  -16.36819 -29.60841 1.000 36.09205 ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.19488 -16.49710 -33.78909 1.000 30.39705 ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -11.89801 -15.25815 -34.13513 1.000 29.98849 ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -10.94120 -14.07750 -34.05714 1.000 28.73275 ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.52396 -13.51627 -35.08049 1.000 31.07753 ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.54304 -13.74500 -32.83360 1.000 23.28857 ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.55032  -12.70935 -32.56708 1.000 24.00403 ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.24663  -12.73807 -31.07845 1.000 23.93740 ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.16844 -12.81066 -30.26640 1.000 24.91553 ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -10.06317 -11.30418 -32.96283 1.000 25.64549 ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -8.94341  -10.21548 -32.80663 1.000 24.30098 ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.53743  -8.81778  -32.66937 1.000 22.94657 ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.45501 -8.68802  -31.52412 1.000 25.84489 ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.77028 -8.55243  -31.57719 1.000 26.35958 ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.44167 -8.48764  -32.72600 1.000 27.59200 ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.46253 -8.43400  -30.43802 1.000 24.81701 ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -7.97046  -12.65563 -30.72464 1.000 23.05260 ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.62301  -12.52986 -29.32422 1.000 21.11881 ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.50891  -13.47811 -28.95281 1.000 21.63461 ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -5.75939  -13.95517 -29.81126 1.000 21.77366 ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.37324  -13.74070 -27.64888 1.000 19.50324 ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.29142  -14.56903 -27.16299 1.000 19.15407 ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -5.81907  -15.50749 -26.09542 1.000 22.77179 ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.66771  -15.11850 -25.27809 1.000 19.02511 ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.14744  -13.67866 -26.61310 1.000 19.81044 ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.62125  -12.89954 -27.67654 1.000 21.62938 ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -3.01629  -14.52954 -25.93759 1.000 21.38038 ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.30396  -16.73446 -26.09637 1.000 19.35187 ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.62939  -17.73721 -25.08366 1.000 18.47728 ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.31962  -18.16132 -24.45388 1.000 19.25537 ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.44624  -18.63204 -25.19044 1.000 20.95227 ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.30542  -18.92040 -25.79499 1.000 22.57158 ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -6.79153  -20.04560 -24.98553 1.000 34.37509 ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -7.29880  -21.23838 -25.88113 1.000 38.78619 ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -7.74237  -20.86615 -27.29409 1.000 50.46286 ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -8.99361  -20.04232 -27.34315 1.000 61.72216 ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.17737  -18.01811 -23.13626 1.000 18.74943 ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -2.97146  -18.45140 -22.42880 1.000 16.77222 ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.35896  -19.69054 -21.66341 1.000 20.03586 ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.21407  -19.61906 -20.75847 1.000 19.74003 ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.43528  -17.38507 -21.46413 1.000 16.24125 ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.26687  -17.95277 -20.61691 1.000 18.04804 ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -2.02134  -16.11399 -22.22032 1.000 17.87627 ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.77151  -20.82384 -22.02252 1.000 17.74994 ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -3.08368  -22.10010 -21.39255 1.000 16.97588 ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.94872  -22.41481 -20.43990 1.000 16.75230 ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.82108  -22.66994 -20.87697 1.000 19.49940 ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.25180  -23.21870 -22.43189 1.000 20.21511 ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.28298  -22.79710 -23.50435 1.000 19.46790 ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.60259  -24.55431 -21.72254 1.000 21.33468 ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.25775  -23.71327 -24.69035 1.000 25.22385 ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.22250  -22.42681 -19.14291 1.000 16.20416 ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.22587  -22.72669 -18.12013 1.000 15.47541 ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.34386  -24.20708 -17.78122 1.000 21.53513 ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.33458  -24.63503 -17.15629 1.000 20.23377 ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.46052  -21.88511 -16.86366 1.000 17.05473 ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.51975  -20.37980 -17.14427 1.000 18.03715 ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.88186  -19.63313 -15.82609 1.000 22.73048 ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.22055  -19.84961 -17.69805 1.000 21.19613 ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.30290  -24.97921 -18.08378 1.000 19.98819 ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.20608  -26.37650 -17.65848 1.000 23.64445 ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.39038   -26.36127 -16.26044 1.000 21.30551 ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.59638   -26.14031 -16.09718 1.000 23.45055 ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.63311   -27.16952 -18.66215 1.000 22.30883 ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.11600   -27.05543 -20.07543 1.000 30.12950 ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.74053  -27.99165 -20.62811 1.000 33.02047 ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.26711   -26.08163 -21.01738 1.000 29.90462 ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -1.06262  -27.61795 -21.85545 1.000 26.22579 ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.45175  -26.47231 -22.12320 1.000 35.84906 ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.46001  -26.47539 -15.23747 1.000 20.43882 ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 0.01475   -26.19541 -13.87891 1.000 19.24242 ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 0.95275   -27.24776 -13.32114 1.000 25.14902 ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.84110   -28.44827 -13.60383 1.000 25.65575 ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.17759  -26.05122 -12.91518 1.000 20.52989 ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -2.10650  -24.88324 -13.24883 1.000 21.83921 ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.27402  -24.89236 -12.22181 1.000 22.82708 ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.39997  -23.58382 -13.14980 1.000 24.09923 ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 1.87818   -26.77344 -12.46801 1.000 24.00294 ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.72931   -27.66408 -11.68942 1.000 24.24015 ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.87335   -28.50220 -10.74607 1.000 25.93099 ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.79302   -28.07106 -10.33247 1.000 26.44861 ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.76073   -26.84955 -10.88475 1.000 29.18766 ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.73173   -26.03769 -11.77573 1.000 27.56932 ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.79763   -25.29350 -10.94655 1.000 37.04027 ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.20010   -23.88822 -11.47582 1.000 39.89998 ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.40456   -23.20274 -10.70125 1.000 42.49751 ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.34807   -29.71199 -10.44180 1.000 32.10202 ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.58177   -30.66611 -9.64422  1.000 34.91733 ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.15844   -30.07898 -8.30649  1.000 34.91926 ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.06521   -30.38160 -7.81738  1.000 36.06116 ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.39926   -31.95552 -9.46060  1.000 39.50200 ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 1.89925   -32.91207 -8.40524  1.000 64.34195 ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.90630   -34.02219 -8.12424  1.000 81.47379 ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 4.07128   -33.88056 -8.56415  1.000 77.31869 ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 2.54067   -35.02261 -7.45582  1.000 76.62779 ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 1.97394   -29.21252 -7.71521  1.000 30.25967 ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.65982   -28.66573 -6.40423  1.000 31.46500 ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 0.96745   -27.30683 -6.44713  1.000 27.87245 ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.79768   -26.68850 -5.38800  1.000 28.08310 ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 2.92995   -28.61094 -5.55944  1.000 33.96427 ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 3.98683   -27.68279 -6.12210  1.000 38.89684 ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 3.90581   -27.30212 -7.30304  1.000 44.80301 ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 4.95250   -27.38033 -5.37786  1.000 53.89398 ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.49569   -26.87265 -7.62272  1.000 23.16658 ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.13760  -25.57729 -7.81707  1.000 23.04569 ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.59260  -25.73979 -8.25468  1.000 20.85141 ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.16633  -24.84454 -8.87380  1.000 24.74310 ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.65646   -24.72445 -8.82425  1.000 21.33109 ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.10374   -24.51114 -8.34482  1.000 24.77619 ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.19123   -23.83167 -6.97335  1.000 28.33087 ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.39180   -22.95951 -6.66128  1.000 27.56960 ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.18819   -24.17917 -6.19684  1.000 30.82685 ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.22127  -26.85145 -7.88765  1.000 26.82539 ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.58521  -27.06698 -8.38236  1.000 30.02457 ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.64689  -26.28532 -7.61856  1.000 26.12858 ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.82528  -26.31939 -8.01534  1.000 26.36332 ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.94120  -28.56277 -8.36593  1.000 30.91808 ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.85711  -29.08532 -7.03430  1.000 33.67059 ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -3.02973  -29.35739 -9.34301  1.000 30.16637 ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.27605  -25.56783 -6.56418  1.000 25.33529 ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.22691  -24.65887 -5.92398  1.000 25.26505 ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.78613  -23.63721 -6.90043  1.000 24.90083 ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.90336  -23.15959 -6.70501  1.000 23.28199 ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.56385  -23.94430 -4.73306  1.000 24.90647 ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.53332  -22.89536 -5.12577  1.000 24.25737 ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.74328  -22.45164 -3.91816  1.000 27.98606 ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.86508  -23.22066 -3.43937  1.000 32.58439 ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -3.08036  -21.36251 -3.37221  1.000 29.77573 ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -5.04086  -23.28699 -7.95790  1.000 22.01747 ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.50506  -22.26513 -8.91063  1.000 19.50583 ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.50260  -22.82533 -9.91731  1.000 22.83104 ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.87183  -22.09961 -10.85287 1.000 23.33912 ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.28648  -21.60718 -9.60333  1.000 21.19511 ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.36231  -21.00280 -8.56923  1.000 20.99454 ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.76625  -19.87714 -7.82178  1.000 23.53892 ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.12481  -21.58175 -8.26009  1.000 21.06481 ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.95013  -19.34275 -6.82786  1.000 22.44174 ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.27608  -21.02412 -7.26747  1.000 22.61282 ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.73009  -19.88416 -6.53603  1.000 21.99705 ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.96338  -19.33485 -5.52830  1.000 24.94178 ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.93630  -24.09036 -9.74961  1.000 24.19047 ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.09928  -24.61732 -10.45681 1.000 22.79627 ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.36328  -24.57542 -9.62345  1.000 26.37747 ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.41712 -25.01188 -10.09955 1.000 27.00054 ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.86247  -26.06436 -10.86647 1.000 22.58805 ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.61420  -26.18513 -11.71887 1.000 21.59012 ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.36086  -27.65981 -12.05263 1.000 29.02053 ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.72820  -25.26491 -12.98181 1.000 27.22224 ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.26412  -24.20891 -8.35270  1.000 21.93477 ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.42416 -24.25733 -7.46202  1.000 23.33606 ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.17813 -22.93373 -7.55071  1.000 26.22666 ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.57940 -21.84600 -7.47730  1.000 24.37670 ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -10.01046 -24.54340 -6.01426  1.000 28.94885 ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.19330  -25.83719 -5.83428  1.000 31.97144 ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -8.89310  -26.14963 -4.37456  1.000 62.40840 ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -9.83406  -26.06954 -3.54844  1.000 77.01310 ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -7.72171  -26.47195 -4.05052  1.000 81.46209 ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.50222 -23.03785 -7.70637  1.000 26.85170 ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.33119 -21.86083 -7.93364  1.000 26.83805 ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.15280 -20.81703 -6.82370  1.000 24.27892 ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.97740 -19.62119 -7.10975  1.000 25.41886 ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.79202 -22.28958 -8.03261  1.000 29.68911 ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.72239 -21.11122 -8.19513  1.000 36.04729 ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.17056 -21.50153 -8.49866  1.000 58.83840 ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.62298 -22.53262 -7.95933  1.000 45.18025 ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.84252 -20.76909 -9.26735  1.000 51.68324 ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.18470 -21.24980 -5.55403  1.000 28.23487 ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.13207 -20.24163 -4.49700  1.000 25.98316 ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.77232 -19.54511 -4.48010  1.000 27.78550 ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.70044 -18.35563 -4.15608  1.000 24.21473 ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.41104 -20.83170 -3.12055  1.000 29.69476 ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.49748 -21.90032 -2.74539  1.000 35.92627 ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -13.13396 -22.54403 -1.53451  1.000 44.43420 ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.23682 -23.46768 -0.86950  1.000 50.31946 ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.42107 -23.86410 0.38192   1.000 47.40855 ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.51694 -23.52199 1.05946   1.000 48.96289 ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.49970 -24.63099 0.96122   1.000 58.05461 ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.68748 -20.26280 -4.82426  1.000 24.14792 ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.37030  -19.64904 -4.84141  1.000 24.25769 ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.25908  -18.63671 -5.98797  1.000 21.57015 ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.74408  -17.52790 -5.79204  1.000 21.16454 ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.30678  -20.74936 -4.97394  1.000 24.67176 ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.84009  -20.26773 -4.93992  1.000 21.22985 ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.48678  -19.62563 -3.59397  1.000 23.41951 ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -5.04577  -19.42487 -3.54154  1.000 24.73708 ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.42937  -18.26754 -3.30294  1.000 25.57355 ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.09771  -17.16255 -3.04159  1.000 24.94981 ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.09592  -18.21884 -3.35868  1.000 23.51119 ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.73801  -19.00228 -7.19096  1.000 21.38354 ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.69850  -18.07533 -8.32280  1.000 19.25329 ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.54127 -16.83391 -8.03032  1.000 19.56541 ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.09483 -15.68953 -8.27316  1.000 21.21873 ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.17126 -18.76206 -9.62157  1.000 21.34458 ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.21980  -19.90190 -9.99394  1.000 21.68536 ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.31541 -17.70955 -10.76816 1.000 20.44984 ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.88864  -20.92161 -11.01189 1.000 22.53855 ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.73968 -17.03844 -7.45905  1.000 21.48648 ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.59713 -15.90007 -7.13762  1.000 24.11775 ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.90312 -14.95249 -6.16872  1.000 23.52689 ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.99314 -13.72870 -6.31735  1.000 23.66479 ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.93146 -16.33503 -6.52264  1.000 25.30039 ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.95125 -16.77108 -7.50716  1.000 29.71106 ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.19646 -17.26585 -6.71690  1.000 30.47501 ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -17.10724 -18.16910 -7.53215  1.000 50.57340 ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -18.17115 -18.83729 -6.68280  1.000 56.49762 ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.24578 -15.51051 -5.14355  1.000 21.60702 ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.53949 -14.69630 -4.16832  1.000 22.70594 ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.45314  -13.86112 -4.83547  1.000 21.33818 ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.29666  -12.67385 -4.51935  1.000 23.13396 ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.93542  -15.60681 -3.09120  1.000 23.48294 ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -8.98931  -14.89723 -2.09955  1.000 24.78889 ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.32241  -15.89246 -1.17044  1.000 23.89725 ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.73737  -16.85490 -1.74127  1.000 26.42996 ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.34550  -15.69555 0.04163   1.000 26.09568 ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.69769  -14.46502 -5.74187  1.000 20.55225 ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.58342  -13.75397 -6.37645  1.000 21.23537 ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.10128  -12.63948 -7.28260  1.000 20.07877 ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.55707  -11.52468 -7.27579  1.000 22.90712 ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.69960  -14.73581 -7.15604  1.000 21.03088 ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -5.98675  -15.67711 -6.17660  1.000 23.29831 ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.64542  -13.96728 -7.98609  1.000 22.31864 ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.54591  -16.94627 -6.91924  1.000 24.94610 ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.14960  -12.91841 -8.07146  1.000 18.92165 ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.71175  -11.88682 -8.93408  1.000 21.28886 ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.25444 -10.72760 -8.12038  1.000 22.70033 ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -10.01595 -9.56501  -8.45187  1.000 24.48267 ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.79611 -12.51210 -9.82033  1.000 21.08563 ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.58605 -11.42434 -10.54571 1.000 22.01854 ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.12100 -13.51122 -10.78901 1.000 19.68237 ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.95110 -11.01219 -7.01249  1.000 21.01079 ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.48623 -9.93256  -6.19545  1.000 22.63528 ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.36592 -9.11528  -5.55316  1.000 23.95463 ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.48132 -7.89193  -5.44077  1.000 32.03335 ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.42360 -10.50822 -5.12124  1.000 24.50758 ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.04954 -9.50816  -4.17448  1.000 30.84104 ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.77708 -10.24865 -3.06944  1.000 38.08118 ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.55082 -9.33695  -2.19117  1.000 46.21143 ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.54244 -10.12778 -1.39315  1.000 53.12398 ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.29194  -9.78885  -5.09820  1.000 25.54995 ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.17249  -9.10582  -4.42677  1.000 26.62395 ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.39982  -8.18238  -5.36527  1.000 24.40367 ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.04561  -7.04879  -4.98016  1.000 27.23815 ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.20709  -10.14508 -3.86310  1.000 26.40547 ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.07508  -9.56588  -3.04505  1.000 29.16834 ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.40601  -10.69005 -2.26390  1.000 43.13705 ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -3.97095  -10.35708 -1.89983  1.000 52.04192 ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.44853  -11.21005 -0.77037  1.000 56.96588 ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.06634  -8.67646  -6.56263  1.000 26.68718 ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.08472  -8.01709  -7.41100  1.000 28.48829 ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.63217  -7.47766  -8.72115  1.000 26.83538 ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.89247  -6.75604  -9.40228  1.000 30.98661 ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -4.93928  -8.97975  -7.77850  1.000 30.78804 ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.12207  -9.44062  -6.61511  1.000 31.88595 ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.36234  -8.58503  -5.85126  1.000 34.81231 ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -3.94229  -10.67947 -6.09218  1.000 34.34212 ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.73917  -9.27756  -4.91244  1.000 40.35243 ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.08260  -10.54894 -5.03053  1.000 35.50778 ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.85369  -7.84491  -9.13491  1.000 26.07242 ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.33725  -7.46575  -10.45582 1.000 25.43866 ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.71671  -6.79511  -10.38252 1.000 23.20550 ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.49988 -6.85554  -11.34793 1.000 26.27581 ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.35840  -8.68196  -11.39932 1.000 26.78540 ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -7.02392  -9.21966  -11.48924 1.000 28.41361 ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -9.99616  -6.11665  -9.28069  1.000 30.28443 ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.36622 -5.65498  -9.08085  1.000 35.02810 ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.71734 -4.44964  -9.95443  1.000 38.90907 ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -12.90408 -4.17618  -10.14881 1.000 42.29126 ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.61462 -5.34226  -7.60604  1.000 41.27900 ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -10.83730 -4.19178  -7.08005  1.000 42.51994 ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -9.49436  -4.56260  -6.41484  1.000 65.87361 ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -8.62040  -5.25000  -6.99897  1.000 44.04948 ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -9.32050  -4.07649  -5.18069  1.000 50.83843 ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.72937 -3.73327  -10.50031 1.000 33.68002 ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -10.99064 -2.57281  -11.34420 1.000 35.98949 ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.64091 -2.82427  -12.81749 1.000 33.20025 ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.27781 -1.89363  -13.54692 1.000 39.76956 ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.21635 -1.36911  -10.84177 1.000 40.11036 ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.65689 -0.91824  -9.47569  1.000 39.69260 ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -9.81845  -1.09736  -8.38322  1.000 43.97041 ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -11.93022 -0.41224  -9.26770  1.000 46.30052 ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -10.20653 -0.70384  -7.11408  1.000 52.31961 ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -12.32826 -0.01797  -7.99709  1.000 53.56936 ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.46679 -0.17499  -6.91875  1.000 50.89919 ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.65937 -4.06111  -13.25780 1.000 25.05062 ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.48777 -4.35285  -14.68333 1.000 21.36663 ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.78668 -4.02945  -15.41518 1.000 29.57501 ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.86645 -4.47849  -15.00465 1.000 31.54555 ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -10.06587 -5.82475  -14.88954 1.000 24.39440 ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.68581  -6.04954  -14.25430 1.000 23.00503 ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -10.10782 -6.24188  -16.38054 1.000 23.94804 ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.57967  -5.28601  -14.90717 1.000 27.37854 ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.69194 -3.25694  -16.49711 1.000 24.53761 ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.87178 -2.71432  -17.14777 1.000 25.41465 ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.52357 -3.58089  -18.20645 1.000 25.17308 ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.14114 -3.04322  -19.12939 1.000 26.85067 ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.44466 -4.89260  -18.05292 1.000 23.68091 ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -14.02181 -5.84300  -18.99524 1.000 22.73724 ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.58748 -6.95471  -18.14735 1.000 24.41919 ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -14.04370 -7.25054  -17.06712 1.000 24.49248 ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.97251 -6.40463  -19.96451 1.000 21.02232 ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.35463 -5.32446  -20.81468 1.000 23.16785 ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -12.98983 -4.86931  -21.98163 1.000 22.61117 ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.13536 -4.71743  -20.44819 1.000 22.34014 ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.48532 -3.84612  -22.72293 1.000 22.91677 ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.60181 -3.68093  -21.21688 1.000 21.14409 ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.27388 -3.26100  -22.37281 1.000 21.09212 ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.79207 -2.22920  -23.11413 1.000 23.71675 ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.63230 -7.62569  -18.60959 1.000 21.54592 ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.19754 -8.73280  -17.84121 1.000 21.01016 ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.22844 -9.89708  -17.76841 1.000 23.45375 ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.58870 -10.25301 -18.76330 1.000 24.04751 ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.47972 -9.11061  -18.60786 1.000 26.01503 ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.51987 -8.33186  -19.82711 1.000 31.66075 ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.45121 -7.22779  -19.77739 1.000 23.90112 ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.09414 -10.45572 -16.57503 1.000 21.99907 ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.22086 -11.60632 -16.31202 1.000 19.03609 ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.17020 -12.70393 -15.87761 1.000 18.74337 ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.82002 -12.58552 -14.82926 1.000 25.71899 ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.18892 -11.33641 -15.21444 1.000 20.48213 ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.24046 -10.18079 -15.62335 1.000 20.79295 ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.39441 -12.59836 -14.95018 1.000 22.05883 ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.36258 -9.71796  -14.42747 1.000 22.13841 ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.29675 -13.73605 -16.70516 1.000 19.83002 ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.23775 -14.81806 -16.41625 1.000 19.52333 ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.43564 -16.03005 -15.99519 1.000 19.21531 ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.59310 -16.50477 -16.76999 1.000 18.65046 ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -17.06692 -15.13882 -17.65185 1.000 21.89684 ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.85514 -14.00133 -18.03490 1.000 22.48779 ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -18.00987 -16.37604 -17.33253 1.000 22.23772 ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.67519 -16.52399 -14.79464 1.000 19.58444 ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -15.04895 -17.74991 -14.30639 1.000 19.55041 ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.96834 -18.92825 -14.64261 1.000 19.09692 ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -17.09762 -19.02489 -14.11388 1.000 21.58456 ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.77585 -17.63059 -12.80868 1.000 21.19904 ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.25755 -18.89486 -12.14009 1.000 22.42084 ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -12.96514 -19.45455 -12.77341 1.000 22.31957 ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -14.00062 -18.49223 -10.63133 1.000 23.67568 ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.52373 -19.76357 -15.58648 1.000 20.20741 ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.27371 -20.95335 -15.95584 1.000 19.83500 ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.24836 -21.96674 -14.82042 1.000 20.81391 ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.28237 -22.04003 -14.05134 1.000 22.42228 ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.68559 -21.61950 -17.19341 1.000 19.03496 ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.93454 -20.90307 -18.49223 1.000 17.63749 ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -16.04647 -19.50334 -18.56759 1.000 19.27349 ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -16.03896 -21.68645 -19.67247 1.000 19.26546 ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.23198 -18.87016 -19.80948 1.000 19.44566 ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.23647 -21.06679 -20.93625 1.000 19.71080 ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.34830 -19.65033 -20.98129 1.000 18.70530 ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.30673 -22.76212 -14.71340 1.000 23.11817 ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.34252 -23.83098 -13.73017 1.000 23.51953 ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.20884 -25.16375 -14.44289 1.000 27.27207 ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.34189 -25.25626 -15.67151 1.000 29.22065 ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.59783 -23.79097 -12.85219 1.000 41.12834 ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.40796 -22.74165 -11.73010 1.000 48.06448 ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.77765 -23.51181 -13.63830 1.000 29.56353 ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -16.92616 -26.19906 -13.67069 1.000 27.54364 ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.68770 -27.52554 -14.22338 1.000 34.36819 ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.80162 -28.48346 -13.84720 1.000 41.79791 ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.37828 -28.38103 -12.75874 1.000 41.07032 ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.34678 -28.08486 -13.76112 1.000 34.87698 ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.24623 -27.09007 -13.98722 1.000 33.44658 ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.89355 -27.62431 -13.56164 1.000 40.08704 ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.50126 -28.71232 -14.06708 1.000 36.38071 ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.25800 -26.94551 -12.70508 1.000 39.41013 ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -18.05933 -29.45392 -14.74615 1.000 42.93009 ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -18.99270 -30.56259 -14.52518 1.000 47.88254 ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -18.84237 -31.28759 -13.16443 1.000 64.70927 ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -17.73698 -31.44392 -12.63378 1.000 62.60985 ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -18.85276 -31.59657 -15.65642 1.000 52.49255 ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -19.79981 -32.77147 -15.53830 1.000 72.88793 ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -19.91135 -33.55436 -16.85226 1.000 75.15718 ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -18.77635 -34.57720 -17.01129 1.000 83.66835 ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -17.54959 -33.97278 -17.65121 1.000 75.23813 ? 224 LYS   A NZ  1 
HETATM 1645 C C1  . A1AYU B 2 .   ? -0.01827  -12.51730 -22.53162 0.656 36.36475 ? 301 A1AYU A C1  1 
HETATM 1646 C C2  . A1AYU B 2 .   ? -0.97982  -11.74513 -23.31869 0.656 37.65731 ? 301 A1AYU A C2  1 
HETATM 1647 C C10 . A1AYU B 2 .   ? -1.48629  -7.76172  -25.01851 0.656 38.42299 ? 301 A1AYU A C10 1 
HETATM 1648 C C3  . A1AYU B 2 .   ? -2.33927  -11.89585 -23.36462 0.656 26.77837 ? 301 A1AYU A C3  1 
HETATM 1649 C C4  . A1AYU B 2 .   ? -2.80795  -10.91850 -24.20221 0.656 25.64097 ? 301 A1AYU A C4  1 
HETATM 1650 C C5  . A1AYU B 2 .   ? -1.64255  -9.05721  -25.51854 0.656 38.44587 ? 301 A1AYU A C5  1 
HETATM 1651 C C6  . A1AYU B 2 .   ? -1.75097  -9.28666  -26.88553 0.656 34.25660 ? 301 A1AYU A C6  1 
HETATM 1652 C C7  . A1AYU B 2 .   ? -1.66561  -8.21553  -27.75592 0.656 20.59644 ? 301 A1AYU A C7  1 
HETATM 1653 C C8  . A1AYU B 2 .   ? -1.53836  -6.91232  -27.26029 0.656 30.77548 ? 301 A1AYU A C8  1 
HETATM 1654 C C9  . A1AYU B 2 .   ? -1.46083  -6.67816  -25.89913 0.656 17.31128 ? 301 A1AYU A C9  1 
HETATM 1655 F F1  . A1AYU B 2 .   ? -0.42128  -12.62507 -21.26577 0.656 26.87775 ? 301 A1AYU A F1  1 
HETATM 1656 F F2  . A1AYU B 2 .   ? 0.13545   -13.74655 -23.03851 0.656 40.20971 ? 301 A1AYU A F2  1 
HETATM 1657 F F3  . A1AYU B 2 .   ? 1.15314   -11.91782 -22.57946 0.656 39.17373 ? 301 A1AYU A F3  1 
HETATM 1658 N N1  . A1AYU B 2 .   ? -1.71411  -10.17509 -24.64020 0.656 33.99402 ? 301 A1AYU A N1  1 
HETATM 1659 N N2  . A1AYU B 2 .   ? -0.58523  -10.68785 -24.04450 0.656 29.95442 ? 301 A1AYU A N2  1 
HETATM 1660 O O1  . A1AYU B 2 .   ? -3.94450  -10.66625 -24.57113 0.656 24.58906 ? 301 A1AYU A O1  1 
HETATM 1661 O O   . HOH   C 3 .   ? -14.07619 -7.56170  -42.12313 1.000 57.70645 ? 401 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? 14.98008  -1.01167  -11.83857 1.000 48.44409 ? 402 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? 5.17342   -29.11307 -8.37076  1.000 47.81962 ? 403 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? 9.19344   -3.25982  -20.32038 1.000 36.39319 ? 404 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? 12.34103  -8.92879  -29.69906 1.000 40.48674 ? 405 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? 0.43000   -14.77026 -1.42949  1.000 37.25593 ? 406 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? -1.61797  -29.11419 -5.93072  1.000 34.10840 ? 407 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? -3.87627  -26.38052 -30.95010 1.000 57.96734 ? 408 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? 13.89868  -11.19490 -29.41255 1.000 43.54142 ? 409 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? -6.38944  -5.22552  -38.90131 1.000 52.13515 ? 410 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -15.76575 0.33630   -30.36406 1.000 44.16688 ? 411 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 11.74221  -21.72701 -40.63129 1.000 48.13344 ? 412 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? -16.24569 -25.63754 -17.95746 1.000 28.15361 ? 413 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? 1.38454   -26.41776 -2.90520  1.000 48.35599 ? 414 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? 8.37105   -0.55150  -17.25477 1.000 44.31430 ? 415 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? 0.32308   -30.80162 -23.29259 1.000 54.36535 ? 416 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? -12.96059 -7.35906  -11.93998 1.000 37.62161 ? 417 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 3.33841   -24.20062 -38.65087 1.000 37.23995 ? 418 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? -4.34583  0.56845   -22.12675 1.000 36.33615 ? 419 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? -7.33354  -28.07935 -21.23943 1.000 47.73903 ? 420 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? 7.70868   -18.92429 -6.48124  1.000 26.21950 ? 421 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? 3.07170   -5.78819  -6.08612  1.000 53.48744 ? 422 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? 12.93140  -1.98434  -5.40725  1.000 58.39348 ? 423 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? -3.22949  -3.32546  -40.43957 1.000 56.35440 ? 424 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? 6.61701   -26.61214 -27.70854 1.000 32.76052 ? 425 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? 9.83362   -14.64646 -25.15485 1.000 24.20854 ? 426 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? 7.60360   -27.65091 -24.04947 1.000 34.23172 ? 427 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? 3.20594   -6.18731  -11.05321 1.000 27.33937 ? 428 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? -8.18187  1.82497   -36.41557 1.000 39.32390 ? 429 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 6.01179   -21.26278 -0.04489  1.000 30.81349 ? 430 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? 9.06478   -26.49081 -17.12268 1.000 30.70399 ? 431 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? -6.53070  -7.74581  -34.29384 1.000 24.27081 ? 432 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? -3.04263  -3.33442  -35.48365 1.000 54.33219 ? 433 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? -18.76933 -11.67750 -21.08559 1.000 42.10720 ? 434 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 18.43877  -11.04031 -17.50062 1.000 46.15338 ? 435 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? 7.81406   -23.21345 -14.30323 1.000 29.13305 ? 436 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -3.17383  -5.99125  -6.43757  1.000 45.42635 ? 437 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? 1.43313   -7.90921  -16.52001 1.000 23.92667 ? 438 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? -8.76585  -11.94710 -36.34167 1.000 29.85562 ? 439 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? -8.57507  4.69580   -33.47095 1.000 33.47549 ? 440 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? -5.32738  -10.38635 -27.36219 1.000 19.72027 ? 441 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? -16.27456 -12.71673 -19.78099 1.000 24.36164 ? 442 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? 9.83095   -17.39738 -7.72832  1.000 25.10340 ? 443 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? -5.71291  -2.13100  -19.43654 1.000 26.45233 ? 444 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -11.15124 -14.21000 -37.60181 1.000 39.17587 ? 445 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -2.23286  -13.68646 -35.64406 1.000 23.21439 ? 446 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? 3.75601   -29.75429 -25.77934 1.000 46.27312 ? 447 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -0.91827  -11.30990 -3.16167  1.000 39.21419 ? 448 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? 7.49685   1.31472   -14.59564 1.000 39.62325 ? 449 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? 5.97705   -21.74107 -37.28514 1.000 34.55432 ? 450 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? 11.47334  -28.19689 -30.29152 1.000 34.44621 ? 451 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? -19.771   -12.965   -16.425   1.000 48.50881 ? 452 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? -8.03548  -3.95554  -10.67167 1.000 33.14215 ? 453 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? 3.16988   -20.50549 -2.88133  1.000 36.02577 ? 454 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? -13.31330 -0.76750  -20.34699 1.000 37.72929 ? 455 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? 0.91285   -21.09219 -4.66193  1.000 28.76132 ? 456 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? 15.46215  -20.22094 -18.65938 1.000 26.78236 ? 457 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? -13.00542 -25.02316 -10.92061 1.000 36.04131 ? 458 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? 0.23087   -22.11744 -2.10449  1.000 45.82560 ? 459 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? -7.67452  -28.31202 -7.94492  1.000 35.37842 ? 460 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? -7.40560  -5.52780  -2.75321  1.000 51.25695 ? 461 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -14.49323 -7.09489  -14.38610 1.000 35.39839 ? 462 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? -19.77422 -19.49040 -14.34541 1.000 23.25124 ? 463 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? 11.60404  -27.32842 -34.64298 1.000 27.57095 ? 464 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -9.21718  -2.31040  -17.50853 1.000 24.74936 ? 465 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? 13.54893  -14.18773 -26.69941 1.000 23.42535 ? 466 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? -3.26336  -12.15496 -8.97586  1.000 32.04464 ? 467 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? -16.82337 -20.44084 -4.92327  1.000 42.37408 ? 468 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? -10.72957 -14.72803 0.97566   1.000 28.42613 ? 469 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? -1.48432  -4.58173  -33.70716 1.000 50.33510 ? 470 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? 7.91900   -23.25624 -7.18270  1.000 40.94611 ? 471 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? -0.23382  -5.47542  -18.36147 1.000 30.17141 ? 472 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? -14.29952 -21.99878 -33.61698 1.000 44.30233 ? 473 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? -9.39707  -23.60557 -2.42054  1.000 52.66623 ? 474 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? 14.02127  -15.80764 -2.04141  1.000 34.84539 ? 475 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? 3.63484   -7.58431  -36.52871 1.000 42.40139 ? 476 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 0.32798   -1.46138  -19.76911 1.000 45.24561 ? 477 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? -7.99892  -22.88613 -30.19887 1.000 43.73865 ? 478 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? -8.14391  -24.90168 -19.12287 1.000 21.40104 ? 479 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -14.16774 -11.76287 0.34187   1.000 41.97333 ? 480 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? -6.43791  -5.07491  -35.61205 1.000 26.33555 ? 481 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? 11.20895  -8.11281  -27.39801 1.000 27.07812 ? 482 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? -6.16572  -11.40452 -10.04274 1.000 26.73387 ? 483 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? 4.15946   -24.10256 -30.71986 1.000 21.81792 ? 484 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? -5.41643  -7.72867  -13.16224 1.000 22.94711 ? 485 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? -14.69646 -22.76431 -11.45216 1.000 31.01301 ? 486 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? -16.94102 -5.31049  -22.69087 1.000 33.72297 ? 487 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -0.41878  -7.08929  -31.02764 1.000 36.86498 ? 488 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? 20.01735  -10.41981 -26.31609 1.000 47.80243 ? 489 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? -4.05473  -4.97483  -8.34808  1.000 51.44764 ? 490 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? 18.28479  -7.23550  -20.25006 1.000 38.20164 ? 491 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? -7.70488  -24.36805 -23.13061 1.000 31.63144 ? 492 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? 0.60371   -29.66256 -16.08371 1.000 39.08859 ? 493 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 8.88126   -15.43391 -27.74070 1.000 20.71333 ? 494 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? 6.70781   -29.67566 -20.15544 1.000 38.23298 ? 495 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? -13.69952 -17.08482 -2.71063  1.000 30.47582 ? 496 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? -5.81362  -31.17280 -11.63093 1.000 35.59634 ? 497 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? 18.07247  -19.29817 -24.54459 1.000 32.70022 ? 498 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? 5.90170   -25.36312 -7.26060  1.000 47.77718 ? 499 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? 16.51967  -14.38471 -7.10789  1.000 48.98422 ? 500 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? 10.62167  -25.33842 -23.70384 1.000 23.57546 ? 501 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? -15.26221 -11.10604 -29.64507 1.000 31.95276 ? 502 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? 4.60971   -19.31369 -40.52636 1.000 36.36470 ? 503 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -17.77426 -18.87827 -11.33479 1.000 34.69624 ? 504 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? 13.02868  -13.88252 -29.61230 1.000 28.97450 ? 505 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -14.15696 -12.75486 -7.81491  1.000 30.58704 ? 506 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? -10.69046 -6.56759  -2.96310  1.000 50.30109 ? 507 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? -10.21170 -0.57010  -19.92023 1.000 37.83893 ? 508 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -1.83074  -25.70486 -4.77536  1.000 25.94788 ? 509 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? -8.94635  -10.64124 -40.34209 1.000 45.23908 ? 510 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? -17.22629 -28.72156 -17.34504 1.000 42.08689 ? 511 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? -16.02229 -2.96232  -21.23780 1.000 29.96085 ? 512 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? 3.61661   -6.82707  -17.86356 1.000 27.28582 ? 513 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 14.41630  -15.93380 -30.69244 1.000 33.80714 ? 514 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? -11.91123 -0.38907  -15.30728 1.000 37.73582 ? 515 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? -10.35466 -11.60648 -2.11629  1.000 26.40929 ? 516 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? -13.55859 -26.57090 -18.08991 1.000 30.05017 ? 517 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? -8.88182  -18.28726 -36.62666 1.000 46.09000 ? 518 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? -12.33280 -27.97963 -30.13258 1.000 33.97544 ? 519 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? 0.61827   -4.83499  -16.02711 1.000 46.48858 ? 520 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? -7.10777  1.22356   -19.34910 1.000 36.56054 ? 521 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? -2.36294  -24.96802 -1.23672  1.000 46.91908 ? 522 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? -14.47824 -29.37245 -9.88306  1.000 48.81020 ? 523 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? -7.51399  7.54224   -33.52433 1.000 40.03452 ? 524 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? -2.50207  -15.74089 -0.24460  1.000 38.73913 ? 525 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? 8.42781   -20.53455 -9.26579  1.000 33.33189 ? 526 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? 18.44031  -16.06835 -13.31456 1.000 39.50442 ? 527 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? -6.11069  -14.10239 0.87064   1.000 29.74112 ? 528 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? -5.12004  -14.28416 -22.65525 1.000 19.79708 ? 529 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? -10.19333 -15.06145 -28.28167 1.000 31.35114 ? 530 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? 11.00265  -11.58339 -4.86764  1.000 42.81568 ? 531 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? 10.65245  -25.55337 -26.66884 1.000 29.28034 ? 532 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? 12.40828  -27.30832 -19.69429 1.000 46.09370 ? 533 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? 15.38146  -0.63037  -19.35506 1.000 46.00311 ? 534 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? -3.30714  -21.16549 -0.50496  1.000 36.00922 ? 535 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -1.73104  -32.62367 -8.06936  1.000 52.74461 ? 536 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? -4.64568  0.42142   -30.43495 1.000 34.17367 ? 537 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -3.09147  -31.46661 -20.20863 1.000 50.57171 ? 538 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? 10.47198  -21.37364 -6.92663  1.000 38.10976 ? 539 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? 1.45392   -3.08169  -24.42603 1.000 45.22396 ? 540 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? 8.55749   -20.05073 -41.38382 1.000 50.34135 ? 541 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -4.20318  -14.06770 -0.82560  1.000 46.13566 ? 542 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? -5.91926  -24.42019 -30.34283 1.000 50.85784 ? 543 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? -3.75886  -20.92248 -38.64666 1.000 49.24697 ? 544 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? -1.02669  -26.01813 -32.39545 1.000 47.13591 ? 545 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? 13.71147  -20.46886 -20.67340 1.000 22.44114 ? 546 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? 1.98419   -6.03276  -25.91777 1.000 40.35981 ? 547 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? -17.72391 -15.24750 -13.15353 1.000 29.93971 ? 548 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? 0.56231   -5.17417  -14.07547 1.000 40.50847 ? 549 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? -5.62514  -19.10431 -39.22530 1.000 42.04460 ? 550 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? 20.43478  -6.10190  -21.03279 1.000 43.50341 ? 551 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? -4.18425  -3.54749  -15.44511 1.000 43.16040 ? 552 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? 17.08821  -24.76652 -25.28396 1.000 34.78235 ? 553 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? 4.86289   -30.64770 -11.62927 1.000 45.58576 ? 554 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? -3.12739  -1.04563  -24.00181 1.000 33.92874 ? 555 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? 7.39603   -4.62680  -22.17399 1.000 39.91898 ? 556 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? 4.07546   -9.19572  -20.23996 1.000 23.90088 ? 557 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? 15.67753  -18.21956 -3.52959  1.000 32.00695 ? 558 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? -3.45019  -13.22326 -20.60691 1.000 25.71932 ? 559 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? 8.61835   -16.13776 -39.50314 1.000 41.50927 ? 560 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? 13.31556  -6.75073  -26.15139 1.000 27.23222 ? 561 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? -13.73919 -18.70189 -24.47868 1.000 25.09368 ? 562 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? -16.23333 -25.52623 -10.87673 1.000 37.58340 ? 563 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? -1.16359  -29.83265 -17.80390 1.000 43.26178 ? 564 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? -11.88809 -7.73370  -38.38103 1.000 45.23912 ? 565 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? 8.80971   -20.57298 -4.25967  1.000 31.02735 ? 566 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? -13.60114 -31.22592 -12.94250 1.000 55.46514 ? 567 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? 20.85632  -14.01317 -26.66389 1.000 35.60366 ? 568 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? 14.12257  -9.60379  -4.10072  1.000 55.25530 ? 569 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? -15.17095 -12.15859 -11.96120 1.000 36.02554 ? 570 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? -12.79403 -26.98973 -35.34061 1.000 50.77741 ? 571 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? -13.05008 -12.17684 -30.98774 1.000 28.63590 ? 572 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? -17.72475 -3.55352  -28.69442 1.000 50.69238 ? 573 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 0.84402   -6.13074  -34.31749 1.000 49.43591 ? 574 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? 3.94201   -11.74109 -38.49964 1.000 32.84415 ? 575 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? 19.756    -16.399   -27.801   1.000 39.37216 ? 576 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? -13.52187 -25.91873 -7.93167  1.000 30.35858 ? 577 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? 9.83168   -5.90635  -1.50941  1.000 49.16114 ? 578 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? -18.28926 -15.88272 -21.35247 1.000 38.09650 ? 579 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? 20.01224  -5.39336  -14.85278 1.000 54.78850 ? 580 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? -5.41936  -31.67181 -6.98464  1.000 48.60187 ? 581 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? -0.00703  -16.76963 -3.43887  1.000 28.15141 ? 582 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? 2.96658   -4.08503  -8.93982  1.000 52.81467 ? 583 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? -20.072   -27.758   -10.323   1.000 56.46000 ? 584 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? -15.85513 -4.18254  -15.42722 1.000 52.66947 ? 585 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? -14.58815 -3.55817  -12.59497 1.000 44.53066 ? 586 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? -5.06209  -5.25494  -11.90422 1.000 43.32645 ? 587 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? 3.96424   -22.97792 -3.51860  1.000 39.88270 ? 588 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? -14.00939 -24.11943 -4.97317  1.000 35.49691 ? 589 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? -15.79274 -1.28300  -27.77105 1.000 53.68485 ? 590 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? 12.20483  -1.66634  -3.58803  1.000 52.79851 ? 591 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? -17.91431 -3.22137  -40.31118 1.000 53.00985 ? 592 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? -12.32479 -26.93866 -20.38833 1.000 29.63075 ? 593 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? 21.881    -13.445   -19.323   1.000 52.44268 ? 594 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? -16.45305 -9.14924  -14.16127 1.000 35.76444 ? 595 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? -18.04766 -5.63312  -25.47198 1.000 36.72052 ? 596 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? 15.60380  -7.05520  -27.70328 1.000 38.40200 ? 597 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? -13.63625 -29.41884 -16.84141 1.000 53.70920 ? 598 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? 18.23652  -3.31260  -22.82734 1.000 48.77082 ? 599 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? -17.76067 -16.46639 -23.66150 1.000 38.89795 ? 600 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? -3.67616  -32.92245 -11.06065 1.000 51.61592 ? 601 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? 1.06564   -8.75600  -4.06785  1.000 36.44116 ? 602 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? 11.42764  -1.74077  -20.22559 1.000 40.30543 ? 603 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? -3.62669  -28.35289 -33.18039 1.000 60.19493 ? 604 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? 0.47375   -5.82583  -22.11349 1.000 40.25389 ? 605 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? 8.16195   -25.75361 -25.95524 1.000 41.93871 ? 606 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? 13.69635  -4.02041  -25.37857 1.000 23.90299 ? 607 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? 5.58591   -3.22229  -26.12711 1.000 40.48294 ? 608 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? 3.20624   -6.69525  -20.39764 1.000 49.12338 ? 609 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? 1.80292   -18.49760 0.04835   1.000 34.04309 ? 610 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? 14.49894  -22.51366 -17.25931 1.000 35.42739 ? 611 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? -1.98820  -26.99252 -24.96913 1.000 41.55412 ? 612 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? 2.70849   -10.05765 -23.06026 1.000 40.89404 ? 613 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? -7.097    -2.032    -12.653   1.000 46.82202 ? 614 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? 2.08304   -25.87720 -29.35900 1.000 41.47281 ? 615 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? -17.08722 -4.75730  -17.37994 1.000 38.70401 ? 616 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? -12.33268 -16.48883 -28.25827 1.000 42.60886 ? 617 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? -6.43512  3.73321   -34.81417 1.000 47.90309 ? 618 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? -15.36358 -23.36447 -30.28146 1.000 35.88491 ? 619 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? -11.89122 -20.68810 -25.50618 1.000 44.44860 ? 620 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? -5.80645  -12.78730 -42.08606 1.000 64.78236 ? 621 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? 4.63087   -1.78602  -18.30079 1.000 44.13654 ? 622 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? -13.86452 -14.32657 -3.05109  1.000 34.57344 ? 623 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? 10.77902  -17.04178 -38.60661 1.000 49.23303 ? 624 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? -1.26665  -5.85153  -12.49935 1.000 49.08815 ? 625 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? 0.06218   -19.22989 -1.95748  1.000 36.35754 ? 626 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? 16.077    1.471     -15.363   1.000 52.56232 ? 627 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? -14.15943 -9.86855  -8.29487  1.000 43.72430 ? 628 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? 1.74902   -2.91790  -13.02148 1.000 52.93294 ? 629 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? -0.33903  -1.20919  -22.83766 1.000 47.33742 ? 630 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? 3.12676   -7.94145  -2.21388  1.000 53.77414 ? 631 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? 12.220    -25.241   -38.436   1.000 32.75903 ? 632 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? 19.49082  1.58315   -16.64014 1.000 61.62270 ? 633 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? 18.88834  -8.38052  -17.70718 1.000 45.37250 ? 634 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? -13.85355 -0.82150  -13.60428 1.000 37.88815 ? 635 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? 5.48658   1.64276   -16.70381 1.000 44.46530 ? 636 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? -18.062   -36.874   -19.996   1.000 42.68024 ? 637 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? 11.90526  -27.68121 -23.33021 1.000 55.64219 ? 638 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? -0.85459  -29.18199 -3.05424  1.000 57.43928 ? 639 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? -3.27588  -27.36149 -3.36931  1.000 50.95617 ? 640 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? 3.85156   -0.20621  -16.61915 1.000 50.90236 ? 641 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? -9.81031  -26.09538 -20.96755 1.000 28.72971 ? 642 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? 7.83565   -13.85173 -38.11147 1.000 38.34439 ? 643 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? 1.69784   -7.60279  -22.98398 1.000 47.45513 ? 644 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? 3.63473   -8.88512  -38.94068 1.000 45.53719 ? 645 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? 5.67710   -3.43152  -23.55488 1.000 46.44098 ? 646 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? -6.352    6.859     -35.701   1.000 44.35950 ? 647 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? 2.24749   -0.94840  -26.05275 1.000 44.14466 ? 648 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? 8.043     -8.385    0.068     1.000 51.63964 ? 649 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? 7.64064   -28.77913 -28.26028 1.000 52.61145 ? 650 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? -10.47351 -8.81936  -1.45796  1.000 41.09503 ? 651 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? 6.61141   -21.46271 -2.65643  1.000 37.11824 ? 652 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? -16.834   -0.552    -17.580   1.000 48.82395 ? 653 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 11.129    -1.248    -17.364   1.000 42.14784 ? 654 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? 6.35258   -29.86493 -24.91613 1.000 48.60360 ? 655 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? -2.48173  -1.13630  -30.99086 1.000 47.53843 ? 656 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? 2.26135   -0.77233  -14.26810 1.000 52.29497 ? 657 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? -16.57166 -5.59634  -13.94064 1.000 56.80912 ? 658 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? -10.677   -22.631   4.418     1.000 47.14917 ? 659 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? -5.00530  -25.12711 -1.28428  1.000 56.23712 ? 660 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? -6.92232  -30.74167 -9.21550  1.000 39.03850 ? 661 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? 9.23878   -29.02921 -17.16632 1.000 57.49468 ? 662 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? 1.89855   -3.86840  -10.60889 1.000 55.22671 ? 663 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? -6.761    -23.164   -1.727    1.000 44.78138 ? 664 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 10.37466  -21.28326 -43.11088 1.000 51.31716 ? 665 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? 5.87850   -12.83588 -39.87660 1.000 36.19485 ? 666 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? -4.08345  -28.13282 -23.37866 1.000 43.26015 ? 667 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? 17.40016  -16.86584 -4.87289  1.000 51.31830 ? 668 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? -16.07883 -12.71689 -5.97993  1.000 47.95956 ? 669 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? 12.17565  -10.07586 -1.48413  1.000 52.16519 ? 670 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.63420 0.50  40.78142 ? 671 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? -1.820    -23.417   0.865     1.000 52.86168 ? 672 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? -10.11693 -29.10668 -30.87245 1.000 47.77967 ? 673 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? 21.001    -18.221   -22.170   1.000 47.48588 ? 674 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? -6.66855  -26.77905 -23.17431 1.000 55.92186 ? 675 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? -16.16645 -13.64028 -3.87410  1.000 48.87052 ? 676 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? 4.99497   -14.82538 -41.44408 1.000 51.35504 ? 677 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? 10.85996  -28.09719 -27.73669 1.000 44.01336 ? 678 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? 11.38428  -30.09353 -34.22005 1.000 45.86551 ? 679 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? 21.726    -17.838   -25.005   1.000 45.42357 ? 680 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? -16.284   3.254     -26.315   1.000 46.57373 ? 681 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? 9.81118   -12.69243 -36.91824 1.000 52.09293 ? 682 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? 2.983     -1.933    -20.667   1.000 56.04186 ? 683 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? -16.33588 -13.55407 -28.83888 1.000 47.55793 ? 684 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? 0.60988   -1.42838  -16.86221 1.000 52.13102 ? 685 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? -7.81542  -24.19990 -25.98169 1.000 52.70333 ? 686 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? 9.62125   -25.23070 -14.73239 1.000 46.68827 ? 687 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? 2.01856   -5.59587  -36.47216 1.000 50.30786 ? 688 HOH   A O   1 
HETATM 1949 O O   . HOH   C 3 .   ? 14.47475  -13.20265 -2.88624  1.000 39.38049 ? 689 HOH   A O   1 
HETATM 1950 O O   . HOH   C 3 .   ? 19.282    -20.589   -22.227   1.000 36.41420 ? 690 HOH   A O   1 
HETATM 1951 O O   . HOH   C 3 .   ? -4.13406  1.87187   -28.15654 1.000 44.60708 ? 691 HOH   A O   1 
HETATM 1952 O O   . HOH   C 3 .   ? 20.613    -20.242   -26.665   1.000 51.44284 ? 692 HOH   A O   1 
HETATM 1953 O O   . HOH   C 3 .   ? -10.466   -12.057   1.946     1.000 37.98711 ? 693 HOH   A O   1 
HETATM 1954 O O   . HOH   C 3 .   ? -10.73281 -23.07212 -24.28658 1.000 52.65391 ? 694 HOH   A O   1 
HETATM 1955 O O   . HOH   C 3 .   ? -16.81720 -15.41891 -10.38521 1.000 43.65889 ? 695 HOH   A O   1 
HETATM 1956 O O   . HOH   C 3 .   ? -14.46059 -14.13539 -10.28253 1.000 32.43012 ? 696 HOH   A O   1 
HETATM 1957 O O   . HOH   C 3 .   ? 13.54822  -11.71891 -4.99286  1.000 42.94777 ? 697 HOH   A O   1 
HETATM 1958 O O   . HOH   C 3 .   ? 15.030    -17.042   0.389     1.000 43.21017 ? 698 HOH   A O   1 
HETATM 1959 O O   . HOH   C 3 .   ? 20.58042  -7.64687  -15.78680 1.000 48.04485 ? 699 HOH   A O   1 
HETATM 1960 O O   . HOH   C 3 .   ? -14.60129 -9.45513  -11.38827 1.000 41.80026 ? 700 HOH   A O   1 
HETATM 1961 O O   . HOH   C 3 .   ? -2.72441  -26.45679 -27.57702 1.000 50.66266 ? 701 HOH   A O   1 
HETATM 1962 O O   . HOH   C 3 .   ? -9.06786  -32.86272 -8.95419  1.000 49.08089 ? 702 HOH   A O   1 
HETATM 1963 O O   . HOH   C 3 .   ? -19.69884 -5.75979  -21.35883 1.000 49.70660 ? 703 HOH   A O   1 
HETATM 1964 O O   . HOH   C 3 .   ? -9.543    0.733     -3.647    1.000 52.78142 ? 704 HOH   A O   1 
HETATM 1965 O O   . HOH   C 3 .   ? -5.24101  -25.68547 -27.98780 1.000 48.66839 ? 705 HOH   A O   1 
HETATM 1966 O O   . HOH   C 3 .   ? 17.33939  -4.71279  -28.10390 1.000 55.22205 ? 706 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   ? 0.57610 0.93072 0.56696 -0.08933 -0.00694 -0.30074 16  GLU A N   
2    C CA  . GLU A 9   ? 0.71652 1.02989 0.69262 -0.05519 -0.01412 -0.27992 16  GLU A CA  
3    C C   . GLU A 9   ? 0.59307 0.88877 0.57638 -0.03579 -0.02102 -0.25587 16  GLU A C   
4    O O   . GLU A 9   ? 0.53327 0.88611 0.53011 -0.01764 -0.03142 -0.24418 16  GLU A O   
5    C CB  . GLU A 9   ? 0.72763 1.10247 0.70173 -0.02488 -0.02555 -0.27547 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.93498 1.26328 0.88646 -0.00403 -0.02430 -0.26789 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.03361 1.31682 0.97915 0.02566  -0.02708 -0.24072 16  GLU A CD  
8    O OE1 . GLU A 9   ? 0.96893 1.26522 0.92612 0.03537  -0.03324 -0.22604 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.13305 1.36945 1.06234 0.03992  -0.02150 -0.23420 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.46456 0.68080 0.43766 -0.03748 -0.01300 -0.24827 17  VAL A N   
11   C CA  . VAL A 10  ? 0.37020 0.56300 0.35075 -0.02635 -0.01667 -0.23023 17  VAL A CA  
12   C C   . VAL A 10  ? 0.39728 0.55295 0.37263 0.00743  -0.01858 -0.20124 17  VAL A C   
13   O O   . VAL A 10  ? 0.43257 0.54018 0.39515 0.01036  -0.00916 -0.20052 17  VAL A O   
14   C CB  . VAL A 10  ? 0.43834 0.56817 0.41842 -0.05437 -0.00122 -0.23458 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.44775 0.55871 0.44062 -0.04069 -0.00540 -0.20673 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.55257 0.70938 0.53989 -0.08958 0.00680  -0.25312 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.29059 0.46548 0.27526 0.03201  -0.02766 -0.17576 18  GLU A N   
18   C CA  . GLU A 11  ? 0.29567 0.43637 0.27863 0.05800  -0.02658 -0.14699 18  GLU A CA  
19   C C   . GLU A 11  ? 0.26121 0.36076 0.25518 0.05376  -0.02343 -0.12879 18  GLU A C   
20   O O   . GLU A 11  ? 0.24762 0.36258 0.25148 0.04741  -0.02715 -0.12639 18  GLU A O   
21   C CB  . GLU A 11  ? 0.27181 0.45233 0.25111 0.08754  -0.03307 -0.13140 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.29946 0.52194 0.26394 0.10096  -0.03574 -0.14327 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.40790 0.66662 0.36310 0.13535  -0.03821 -0.12393 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.41649 0.71945 0.37368 0.14299  -0.04321 -0.12335 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.51986 0.76371 0.46264 0.15704  -0.03282 -0.10896 18  GLU A OE2 
26   N N   . THR A 12  ? 0.26497 0.31848 0.25681 0.05946  -0.01661 -0.11552 19  THR A N   
27   C CA  . THR A 12  ? 0.25354 0.27759 0.25423 0.05824  -0.01417 -0.09852 19  THR A CA  
28   C C   . THR A 12  ? 0.27154 0.29770 0.27673 0.07661  -0.01604 -0.07729 19  THR A C   
29   O O   . THR A 12  ? 0.26042 0.28419 0.25981 0.08925  -0.01312 -0.07281 19  THR A O   
30   C CB  . THR A 12  ? 0.28020 0.25748 0.27288 0.05238  -0.00258 -0.09953 19  THR A CB  
31   O OG1 . THR A 12  ? 0.32242 0.28823 0.30607 0.03064  0.00485  -0.12235 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.27116 0.22776 0.27093 0.05521  -0.00045 -0.08094 19  THR A CG2 
33   N N   . PHE A 13  ? 0.24301 0.27292 0.25709 0.07569  -0.01875 -0.06621 20  PHE A N   
34   C CA  . PHE A 13  ? 0.23473 0.26375 0.25164 0.08532  -0.01684 -0.05009 20  PHE A CA  
35   C C   . PHE A 13  ? 0.29458 0.31057 0.32107 0.07771  -0.01585 -0.04125 20  PHE A C   
36   O O   . PHE A 13  ? 0.24349 0.25421 0.27384 0.06794  -0.01793 -0.04396 20  PHE A O   
37   C CB  . PHE A 13  ? 0.25130 0.29604 0.26437 0.09179  -0.01752 -0.04628 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.24092 0.31170 0.24255 0.10522  -0.01908 -0.05249 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.24023 0.34091 0.24245 0.09933  -0.02588 -0.06865 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.29175 0.36291 0.28087 0.12346  -0.01250 -0.04305 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.29006 0.42916 0.28176 0.11305  -0.02859 -0.07584 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.33766 0.43981 0.31290 0.14119  -0.01385 -0.04684 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.30445 0.44510 0.28166 0.13662  -0.02324 -0.06383 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.23135 0.24786 0.26139 0.08131  -0.01184 -0.03131 21  ALA A N   
45   C CA  . ALA A 14  ? 0.22896 0.24825 0.26819 0.07336  -0.01177 -0.02488 21  ALA A CA  
46   C C   . ALA A 14  ? 0.23383 0.25307 0.27254 0.06576  -0.01015 -0.02384 21  ALA A C   
47   O O   . ALA A 14  ? 0.24423 0.25864 0.27462 0.06994  -0.00356 -0.02201 21  ALA A O   
48   C CB  . ALA A 14  ? 0.22610 0.25829 0.27091 0.07640  -0.00735 -0.01849 21  ALA A CB  
49   N N   . PHE A 15  ? 0.21381 0.23414 0.25748 0.05652  -0.01342 -0.02397 22  PHE A N   
50   C CA  . PHE A 15  ? 0.23396 0.25066 0.27480 0.04833  -0.00870 -0.02357 22  PHE A CA  
51   C C   . PHE A 15  ? 0.24138 0.26255 0.28364 0.04014  0.00006  -0.02239 22  PHE A C   
52   O O   . PHE A 15  ? 0.25742 0.29919 0.30948 0.03834  -0.00185 -0.02123 22  PHE A O   
53   C CB  . PHE A 15  ? 0.20739 0.22829 0.25288 0.03909  -0.01330 -0.02467 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.20394 0.22119 0.24778 0.04148  -0.01828 -0.02739 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.24413 0.25873 0.28016 0.04635  -0.01592 -0.02919 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.21586 0.23353 0.26396 0.03983  -0.02249 -0.02764 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.24314 0.26790 0.28086 0.04646  -0.02069 -0.03373 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.22284 0.23914 0.27029 0.03623  -0.02420 -0.03279 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.21948 0.24535 0.26438 0.03790  -0.02471 -0.03702 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.26857 0.27094 0.29904 0.03529  0.01230  -0.02297 23  GLN A N   
61   C CA  . GLN A 16  ? 0.24720 0.25096 0.27788 0.01710  0.02467  -0.02674 23  GLN A CA  
62   C C   . GLN A 16  ? 0.26794 0.30099 0.31202 0.00152  0.01705  -0.03270 23  GLN A C   
63   O O   . GLN A 16  ? 0.25099 0.28585 0.29641 0.00348  0.00803  -0.03280 23  GLN A O   
64   C CB  . GLN A 16  ? 0.34695 0.31198 0.35610 0.01222  0.04375  -0.02764 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.36518 0.30373 0.35583 0.03176  0.05534  -0.01889 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.53737 0.43033 0.50019 0.03353  0.07770  -0.01639 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.56730 0.44973 0.51796 0.05205  0.07610  -0.01139 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.59174 0.45589 0.54147 0.01492  0.10205  -0.01989 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.27846 0.34097 0.33220 -0.01353 0.02117  -0.03789 24  ALA A N   
70   C CA  . ALA A 17  ? 0.24026 0.34769 0.30732 -0.02266 0.01173  -0.04248 24  ALA A CA  
71   C C   . ALA A 17  ? 0.25753 0.35601 0.31744 -0.03764 0.01328  -0.05075 24  ALA A C   
72   O O   . ALA A 17  ? 0.26210 0.38255 0.32707 -0.03284 0.00144  -0.04899 24  ALA A O   
73   C CB  . ALA A 17  ? 0.25061 0.40386 0.32979 -0.03809 0.01740  -0.04933 24  ALA A CB  
74   N N   . GLU A 18  ? 0.27340 0.33224 0.31707 -0.05184 0.03004  -0.05789 25  GLU A N   
75   C CA  . GLU A 18  ? 0.29074 0.33564 0.32361 -0.06624 0.03494  -0.06728 25  GLU A CA  
76   C C   . GLU A 18  ? 0.28024 0.30808 0.30895 -0.04549 0.02383  -0.05798 25  GLU A C   
77   O O   . GLU A 18  ? 0.28417 0.32269 0.31228 -0.05118 0.01851  -0.06242 25  GLU A O   
78   C CB  . GLU A 18  ? 0.35239 0.34644 0.36208 -0.08334 0.06173  -0.07584 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.45904 0.46601 0.47064 -0.11307 0.07845  -0.08940 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.49839 0.50448 0.51485 -0.10260 0.08290  -0.07973 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.42384 0.41867 0.44090 -0.07142 0.07261  -0.06319 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.61638 0.63435 0.63496 -0.12864 0.09899  -0.09085 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.27218 0.28102 0.29895 -0.02269 0.01989  -0.04649 26  ILE A N   
84   C CA  . ILE A 19  ? 0.24699 0.24802 0.27181 -0.00746 0.01079  -0.04070 26  ILE A CA  
85   C C   . ILE A 19  ? 0.24902 0.28131 0.28927 -0.00303 -0.00529 -0.03688 26  ILE A C   
86   O O   . ILE A 19  ? 0.25880 0.29428 0.29902 -0.00181 -0.01092 -0.03594 26  ILE A O   
87   C CB  . ILE A 19  ? 0.28169 0.26196 0.29812 0.01289  0.01321  -0.03335 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.36264 0.30506 0.35495 0.01828  0.03224  -0.03227 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.25596 0.24537 0.27665 0.02502  0.00175  -0.03037 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.42358 0.34125 0.40351 0.00145  0.05243  -0.03757 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.22605 0.27876 0.27649 0.00135  -0.00995 -0.03334 27  ALA A N   
92   C CA  . ALA A 20  ? 0.20908 0.28435 0.26726 0.00984  -0.01967 -0.02709 27  ALA A CA  
93   C C   . ALA A 20  ? 0.20526 0.30895 0.26477 0.00034  -0.02245 -0.03027 27  ALA A C   
94   O O   . ALA A 20  ? 0.23538 0.34430 0.29342 0.00809  -0.02763 -0.02414 27  ALA A O   
95   C CB  . ALA A 20  ? 0.25369 0.34727 0.31867 0.01951  -0.02066 -0.02210 27  ALA A CB  
96   N N   . GLN A 21  ? 0.21916 0.34164 0.27944 -0.01805 -0.01706 -0.04113 28  GLN A N   
97   C CA  . GLN A 21  ? 0.24186 0.40116 0.30277 -0.03023 -0.01983 -0.04855 28  GLN A CA  
98   C C   . GLN A 21  ? 0.27713 0.41063 0.32697 -0.03437 -0.01854 -0.05152 28  GLN A C   
99   O O   . GLN A 21  ? 0.26473 0.42198 0.31361 -0.03140 -0.02501 -0.04952 28  GLN A O   
100  C CB  . GLN A 21  ? 0.23746 0.42347 0.30122 -0.05591 -0.01135 -0.06492 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.43703 0.67753 0.50274 -0.07161 -0.01514 -0.07710 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.77728 1.05400 0.84765 -0.10425 -0.00498 -0.09857 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.71128 0.94874 0.77616 -0.12040 0.01075  -0.10601 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.69067 1.04383 0.76877 -0.11544 -0.01178 -0.10979 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.23895 0.32608 0.27818 -0.03771 -0.00891 -0.05476 29  LEU A N   
106  C CA  . LEU A 22  ? 0.26932 0.33264 0.29716 -0.03667 -0.00654 -0.05583 29  LEU A CA  
107  C C   . LEU A 22  ? 0.29204 0.36001 0.32536 -0.01985 -0.01712 -0.04369 29  LEU A C   
108  O O   . LEU A 22  ? 0.25075 0.32728 0.28057 -0.02031 -0.01996 -0.04320 29  LEU A O   
109  C CB  . LEU A 22  ? 0.29555 0.31221 0.30903 -0.03314 0.00687  -0.05662 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.32723 0.32385 0.32963 -0.02372 0.00909  -0.05419 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.41232 0.40499 0.40164 -0.04063 0.01736  -0.06651 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.38265 0.34523 0.37167 -0.00731 0.01980  -0.04873 29  LEU A CD2 
113  N N   . MET A 23  ? 0.24700 0.30770 0.28700 -0.00690 -0.02077 -0.03509 30  MET A N   
114  C CA  . MET A 23  ? 0.24058 0.29838 0.28305 0.00341  -0.02564 -0.02663 30  MET A CA  
115  C C   . MET A 23  ? 0.22423 0.30522 0.26724 0.00794  -0.02965 -0.01946 30  MET A C   
116  O O   . MET A 23  ? 0.22876 0.30670 0.26739 0.01086  -0.02949 -0.01440 30  MET A O   
117  C CB  . MET A 23  ? 0.19693 0.24090 0.24342 0.01224  -0.02603 -0.02313 30  MET A CB  
118  C CG  . MET A 23  ? 0.23050 0.25981 0.27358 0.01367  -0.02247 -0.02806 30  MET A CG  
119  S SD  . MET A 23  ? 0.23569 0.25956 0.28209 0.02240  -0.02366 -0.02808 30  MET A SD  
120  C CE  . MET A 23  ? 0.25106 0.27405 0.30037 0.01920  -0.02507 -0.02942 30  MET A CE  
121  N N   . SER A 24  ? 0.22004 0.32824 0.26684 0.01132  -0.03194 -0.01740 31  SER A N   
122  C CA  . SER A 24  ? 0.22739 0.36415 0.27059 0.02321  -0.03465 -0.00747 31  SER A CA  
123  C C   . SER A 24  ? 0.25525 0.41866 0.29353 0.01404  -0.03700 -0.01348 31  SER A C   
124  O O   . SER A 24  ? 0.29454 0.46647 0.32478 0.02532  -0.03734 -0.00346 31  SER A O   
125  C CB  . SER A 24  ? 0.36180 0.53073 0.40986 0.03448  -0.03631 -0.00247 31  SER A CB  
126  O OG  . SER A 24  ? 0.49742 0.70402 0.55320 0.01819  -0.03840 -0.01579 31  SER A OG  
127  N N   . LEU A 25  ? 0.21432 0.38422 0.25342 -0.00643 -0.03569 -0.02997 32  LEU A N   
128  C CA  . LEU A 25  ? 0.23382 0.42293 0.26502 -0.01765 -0.03598 -0.03916 32  LEU A CA  
129  C C   . LEU A 25  ? 0.27497 0.43211 0.29827 -0.01207 -0.03384 -0.03300 32  LEU A C   
130  O O   . LEU A 25  ? 0.27329 0.44922 0.28908 -0.00807 -0.03572 -0.02957 32  LEU A O   
131  C CB  . LEU A 25  ? 0.29735 0.48247 0.32567 -0.04350 -0.02881 -0.06026 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.35500 0.55015 0.37084 -0.06062 -0.02515 -0.07575 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.45142 0.66321 0.46520 -0.09029 -0.01659 -0.09936 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.45874 0.60256 0.46184 -0.05883 -0.01758 -0.07547 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.21524 0.33082 0.23992 -0.01104 -0.02955 -0.03177 33  ILE A N   
136  C CA  . ILE A 26  ? 0.24909 0.34454 0.26912 -0.00729 -0.02697 -0.02756 33  ILE A CA  
137  C C   . ILE A 26  ? 0.23576 0.33369 0.25539 0.00497  -0.02775 -0.01269 33  ILE A C   
138  O O   . ILE A 26  ? 0.26492 0.36375 0.27779 0.00674  -0.02535 -0.00817 33  ILE A O   
139  C CB  . ILE A 26  ? 0.23735 0.30345 0.25995 -0.00641 -0.02282 -0.02997 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.28096 0.33331 0.29388 -0.01428 -0.01557 -0.04157 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.24557 0.30439 0.26883 -0.00200 -0.02101 -0.02490 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.32194 0.35006 0.33351 -0.00649 -0.01004 -0.04111 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.26057 0.35460 0.28398 0.01429  -0.02792 -0.00437 34  ILE A N   
144  C CA  . ILE A 27  ? 0.28964 0.37090 0.30598 0.02696  -0.02215 0.01052  34  ILE A CA  
145  C C   . ILE A 27  ? 0.30486 0.41528 0.30973 0.04086  -0.02248 0.02174  34  ILE A C   
146  O O   . ILE A 27  ? 0.34569 0.44345 0.33804 0.05016  -0.01444 0.03433  34  ILE A O   
147  C CB  . ILE A 27  ? 0.29239 0.35297 0.31149 0.03384  -0.01887 0.01453  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.28716 0.32309 0.31422 0.02159  -0.01717 0.00429  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.32627 0.36791 0.33043 0.05076  -0.00797 0.03144  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.28529 0.30686 0.31569 0.02538  -0.01603 0.00285  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.26057 0.41488 0.26801 0.04235  -0.03028 0.01706  35  ASN A N   
152  C CA  . ASN A 28  ? 0.30418 0.50195 0.30071 0.06151  -0.03178 0.02886  35  ASN A CA  
153  C C   . ASN A 28  ? 0.30453 0.54279 0.29551 0.05364  -0.03708 0.02023  35  ASN A C   
154  O O   . ASN A 28  ? 0.39290 0.66714 0.37066 0.07313  -0.03719 0.03261  35  ASN A O   
155  C CB  . ASN A 28  ? 0.31449 0.55357 0.31820 0.06962  -0.03723 0.02819  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.40030 0.60517 0.40260 0.08638  -0.03016 0.04121  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.47427 0.63005 0.46415 0.09722  -0.01884 0.05435  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.57201 0.79656 0.58647 0.08404  -0.03443 0.03468  35  ASN A ND2 
159  N N   . THR A 29  ? 0.29256 0.52624 0.28961 0.02832  -0.03966 -0.00023 36  THR A N   
160  C CA  . THR A 29  ? 0.23543 0.50309 0.22401 0.01798  -0.04256 -0.01223 36  THR A CA  
161  C C   . THR A 29  ? 0.26630 0.51546 0.24183 0.02781  -0.03742 -0.00031 36  THR A C   
162  O O   . THR A 29  ? 0.30086 0.50150 0.27846 0.02563  -0.03081 0.00425  36  THR A O   
163  C CB  . THR A 29  ? 0.31772 0.56974 0.30999 -0.01062 -0.04063 -0.03701 36  THR A CB  
164  O OG1 . THR A 29  ? 0.32913 0.59779 0.33186 -0.02210 -0.04222 -0.04803 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.34364 0.62749 0.32365 -0.02492 -0.04102 -0.05393 36  THR A CG2 
166  N N   . PHE A 30  ? 0.27540 0.56904 0.23741 0.03919  -0.03982 0.00482  37  PHE A N   
167  C CA  . PHE A 30  ? 0.27290 0.55221 0.22089 0.04518  -0.03380 0.01332  37  PHE A CA  
168  C C   . PHE A 30  ? 0.31190 0.57354 0.26087 0.02106  -0.03279 -0.00776 37  PHE A C   
169  O O   . PHE A 30  ? 0.31317 0.60541 0.25881 0.00476  -0.03700 -0.02902 37  PHE A O   
170  C CB  . PHE A 30  ? 0.28177 0.61810 0.21178 0.06527  -0.03641 0.02336  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.32077 0.64041 0.23400 0.07357  -0.02805 0.03483  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.41334 0.68314 0.31899 0.08894  -0.01399 0.05878  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.31133 0.66031 0.21532 0.06274  -0.03148 0.01973  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.36382 0.61719 0.25457 0.09355  -0.00357 0.06899  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.36064 0.69557 0.24864 0.07138  -0.02280 0.03117  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.37772 0.66693 0.25996 0.08699  -0.00896 0.05659  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.26230 0.47757 0.21293 0.01923  -0.02495 -0.00257 38  TYR A N   
178  C CA  . TYR A 31  ? 0.25838 0.45367 0.20822 0.00316  -0.02164 -0.01940 38  TYR A CA  
179  C C   . TYR A 31  ? 0.25243 0.41912 0.20243 0.00876  -0.01317 -0.00748 38  TYR A C   
180  O O   . TYR A 31  ? 0.27820 0.41848 0.24017 0.00945  -0.00974 -0.00048 38  TYR A O   
181  C CB  . TYR A 31  ? 0.29772 0.46950 0.25859 -0.00984 -0.02174 -0.03307 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.31273 0.45526 0.26744 -0.01828 -0.01384 -0.04543 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.39007 0.53833 0.32856 -0.03006 -0.00971 -0.06342 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.31731 0.42924 0.27999 -0.01290 -0.00887 -0.03965 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.50030 0.61547 0.42679 -0.03290 0.00147  -0.07290 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.37842 0.46865 0.33139 -0.01314 0.00017  -0.04831 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.45223 0.53929 0.38563 -0.02158 0.00630  -0.06353 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.68510 0.74315 0.60249 -0.01798 0.01924  -0.07090 38  TYR A OH  
189  N N   . SER A 32  ? 0.26565 0.44264 0.20258 0.01102  -0.00920 -0.00675 39  SER A N   
190  C CA  . SER A 32  ? 0.27145 0.43147 0.20820 0.01581  0.00049  0.00620  39  SER A CA  
191  C C   . SER A 32  ? 0.26529 0.40513 0.21199 0.00789  0.00516  -0.00269 39  SER A C   
192  O O   . SER A 32  ? 0.30433 0.43443 0.25930 0.00732  0.01253  0.00565  39  SER A O   
193  C CB  . SER A 32  ? 0.30180 0.48398 0.21954 0.02359  0.00416  0.01208  39  SER A CB  
194  O OG  . SER A 32  ? 0.30513 0.51144 0.21155 0.03836  0.00153  0.02569  39  SER A OG  
195  N N   . ASN A 33  ? 0.28626 0.42026 0.23090 0.00235  0.00333  -0.01925 40  ASN A N   
196  C CA  . ASN A 33  ? 0.29408 0.41395 0.24091 0.00352  0.01006  -0.02521 40  ASN A CA  
197  C C   . ASN A 33  ? 0.26705 0.37503 0.23166 0.00373  0.00876  -0.02364 40  ASN A C   
198  O O   . ASN A 33  ? 0.30142 0.39524 0.26440 0.00619  0.01049  -0.03172 40  ASN A O   
199  C CB  . ASN A 33  ? 0.33685 0.44593 0.26481 0.00100  0.01424  -0.04187 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.36511 0.45722 0.28686 0.01043  0.02496  -0.04545 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.38395 0.48963 0.31298 0.01868  0.02850  -0.03696 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.39327 0.45650 0.29867 0.01003  0.03289  -0.05808 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.30250 0.29176 0.24191 -0.00166 -0.04707 -0.02491 41  LYS A N   
204  C CA  . LYS A 34  ? 0.24707 0.26550 0.22079 0.00032  -0.03222 -0.02145 41  LYS A CA  
205  C C   . LYS A 34  ? 0.26469 0.26975 0.23248 0.00409  -0.01919 -0.03239 41  LYS A C   
206  O O   . LYS A 34  ? 0.24544 0.26775 0.23566 0.00271  -0.01303 -0.03015 41  LYS A O   
207  C CB  . LYS A 34  ? 0.22295 0.25996 0.20934 0.01191  -0.01758 -0.01723 41  LYS A CB  
208  C CG  . LYS A 34  ? 0.24116 0.30126 0.24232 0.01182  -0.02748 -0.00268 41  LYS A CG  
209  C CD  . LYS A 34  ? 0.28638 0.35582 0.29305 0.02700  -0.01124 -0.00038 41  LYS A CD  
210  C CE  . LYS A 34  ? 0.27211 0.36655 0.29412 0.03255  -0.01730 0.01549  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.26133 0.39310 0.31749 0.03308  -0.01687 0.03035  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.28740 0.26340 0.22485 0.01033  -0.01510 -0.04209 42  GLU A N   
213  C CA  . GLU A 35  ? 0.29913 0.27023 0.23733 0.01671  -0.00016 -0.04876 42  GLU A CA  
214  C C   . GLU A 35  ? 0.32881 0.29712 0.27408 0.00945  -0.00681 -0.05059 42  GLU A C   
215  O O   . GLU A 35  ? 0.29610 0.26833 0.25090 0.01344  0.00422  -0.05370 42  GLU A O   
216  C CB  . GLU A 35  ? 0.33036 0.27450 0.23458 0.02866  0.00769  -0.05465 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.36463 0.27194 0.22981 0.02894  -0.00720 -0.06075 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.45279 0.33025 0.27466 0.04682  0.00263  -0.06530 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.53564 0.41909 0.35218 0.05370  0.01154  -0.06101 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.61984 0.46578 0.41002 0.05539  0.00130  -0.07208 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.27438 0.23501 0.21557 -0.00229 -0.02643 -0.04705 43  ILE A N   
222  C CA  . ILE A 36  ? 0.28596 0.24123 0.23332 -0.01093 -0.03430 -0.04653 43  ILE A CA  
223  C C   . ILE A 36  ? 0.26863 0.25827 0.25248 -0.01294 -0.02445 -0.03958 43  ILE A C   
224  O O   . ILE A 36  ? 0.25041 0.23659 0.23917 -0.01736 -0.02651 -0.03928 43  ILE A O   
225  C CB  . ILE A 36  ? 0.36153 0.30086 0.30017 -0.02748 -0.06159 -0.04023 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.31123 0.28754 0.28205 -0.03738 -0.06969 -0.02408 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.39991 0.29076 0.28796 -0.02356 -0.07473 -0.05000 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.35660 0.36914 0.36801 -0.04648 -0.06871 -0.00907 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.21837 0.23570 0.22199 -0.00761 -0.01378 -0.03435 44  PHE A N   
230  C CA  . PHE A 37  ? 0.20817 0.24846 0.23415 -0.00486 -0.00367 -0.02975 44  PHE A CA  
231  C C   . PHE A 37  ? 0.21454 0.24201 0.23460 -0.00032 0.00469  -0.03926 44  PHE A C   
232  O O   . PHE A 37  ? 0.20898 0.24343 0.23869 -0.00201 0.00602  -0.03669 44  PHE A O   
233  C CB  . PHE A 37  ? 0.21045 0.26913 0.24581 0.00528  0.00719  -0.02599 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.23488 0.27916 0.25884 0.01342  0.01727  -0.03596 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.24522 0.27756 0.25590 0.01560  0.01754  -0.03908 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.22370 0.26587 0.25024 0.01771  0.02484  -0.04014 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.26571 0.28872 0.27140 0.02099  0.02700  -0.04359 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.22829 0.25874 0.24975 0.02086  0.03019  -0.04556 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.21480 0.23830 0.22895 0.02201  0.03211  -0.04588 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.20831 0.21899 0.21359 0.00604  0.01042  -0.04784 45  LEU A N   
241  C CA  . LEU A 38  ? 0.23061 0.23802 0.23878 0.01079  0.01850  -0.05252 45  LEU A CA  
242  C C   . LEU A 38  ? 0.26473 0.25752 0.26515 0.00841  0.01267  -0.05478 45  LEU A C   
243  O O   . LEU A 38  ? 0.25014 0.24758 0.26010 0.00853  0.01470  -0.05454 45  LEU A O   
244  C CB  . LEU A 38  ? 0.23084 0.23281 0.23294 0.01853  0.02775  -0.05506 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.22497 0.23213 0.23953 0.02202  0.03486  -0.05492 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.25736 0.27512 0.28683 0.01798  0.03295  -0.05359 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.31161 0.32039 0.32644 0.02875  0.04486  -0.05136 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.26466 0.23494 0.24370 0.00619  0.00298  -0.05685 46  ARG A N   
249  C CA  . ARG A 39  ? 0.26767 0.21429 0.23254 0.00348  -0.00620 -0.05899 46  ARG A CA  
250  C C   . ARG A 39  ? 0.29882 0.26039 0.28415 -0.00861 -0.01348 -0.05068 46  ARG A C   
251  O O   . ARG A 39  ? 0.28976 0.24501 0.27634 -0.00853 -0.01368 -0.05074 46  ARG A O   
252  C CB  . ARG A 39  ? 0.33862 0.24985 0.26974 0.00136  -0.02079 -0.06258 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.41966 0.29806 0.33161 -0.00401 -0.03535 -0.06412 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.52248 0.35945 0.39747 -0.01089 -0.05758 -0.06670 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.57583 0.43314 0.47175 -0.03038 -0.07380 -0.05536 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.56329 0.39651 0.43556 -0.03853 -0.09437 -0.05483 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.59818 0.37962 0.41654 -0.02725 -0.10098 -0.06729 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.59462 0.45572 0.49611 -0.05714 -0.10938 -0.03993 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.25118 0.23615 0.25431 -0.01701 -0.01752 -0.04106 47  GLU A N   
260  C CA  . GLU A 40  ? 0.23654 0.24047 0.26041 -0.02663 -0.02194 -0.02845 47  GLU A CA  
261  C C   . GLU A 40  ? 0.23682 0.25735 0.27226 -0.01825 -0.00786 -0.02855 47  GLU A C   
262  O O   . GLU A 40  ? 0.21659 0.23871 0.25753 -0.02210 -0.00957 -0.02270 47  GLU A O   
263  C CB  . GLU A 40  ? 0.19270 0.22429 0.23622 -0.03395 -0.02702 -0.01401 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.25901 0.27329 0.29193 -0.04659 -0.04779 -0.01094 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.32424 0.30416 0.34086 -0.06004 -0.06736 -0.01079 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.32953 0.31440 0.35863 -0.06643 -0.06836 -0.00286 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.43257 0.37501 0.41839 -0.06338 -0.08307 -0.01869 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.19251 0.22177 0.22891 -0.00767 0.00381  -0.03427 48  LEU A N   
269  C CA  . LEU A 41  ? 0.19961 0.23646 0.23990 -0.00044 0.01243  -0.03535 48  LEU A CA  
270  C C   . LEU A 41  ? 0.23479 0.25572 0.26900 0.00128  0.01165  -0.04226 48  LEU A C   
271  O O   . LEU A 41  ? 0.21784 0.24091 0.25395 0.00247  0.01227  -0.03990 48  LEU A O   
272  C CB  . LEU A 41  ? 0.21078 0.25224 0.24939 0.00825  0.02012  -0.03949 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.21942 0.27812 0.26327 0.01152  0.02318  -0.03088 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.22236 0.27568 0.25808 0.02094  0.02900  -0.03631 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.20413 0.28184 0.25572 0.01439  0.02690  -0.01800 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.21828 0.22437 0.24408 0.00410  0.01160  -0.04927 49  ILE A N   
277  C CA  . ILE A 42  ? 0.23071 0.22570 0.25330 0.00930  0.01265  -0.05285 49  ILE A CA  
278  C C   . ILE A 42  ? 0.24360 0.22418 0.25915 0.00446  0.00448  -0.05003 49  ILE A C   
279  O O   . ILE A 42  ? 0.24583 0.22417 0.26360 0.00719  0.00440  -0.04908 49  ILE A O   
280  C CB  . ILE A 42  ? 0.22499 0.20967 0.23860 0.01798  0.01805  -0.05746 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.23061 0.23234 0.25756 0.02067  0.02567  -0.05646 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.26138 0.23360 0.26932 0.02740  0.02010  -0.05845 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.24360 0.24115 0.26386 0.02994  0.03419  -0.05647 49  ILE A CD1 
284  N N   . SER A 43  ? 0.24306 0.21279 0.25066 -0.00454 -0.00505 -0.04685 50  SER A N   
285  C CA  . SER A 43  ? 0.23700 0.18873 0.23784 -0.01245 -0.01613 -0.04201 50  SER A CA  
286  C C   . SER A 43  ? 0.26433 0.23855 0.28344 -0.01761 -0.01415 -0.03109 50  SER A C   
287  O O   . SER A 43  ? 0.25494 0.21864 0.27115 -0.01865 -0.01746 -0.02789 50  SER A O   
288  C CB  . SER A 43  ? 0.32618 0.26049 0.31603 -0.02473 -0.03152 -0.03861 50  SER A CB  
289  O OG  . SER A 43  ? 0.41079 0.33156 0.40038 -0.03783 -0.04536 -0.02917 50  SER A OG  
290  N N   . ASN A 44  ? 0.24208 0.24525 0.27626 -0.01790 -0.00746 -0.02468 51  ASN A N   
291  C CA  . ASN A 44  ? 0.24378 0.26666 0.28803 -0.01695 -0.00193 -0.01389 51  ASN A CA  
292  C C   . ASN A 44  ? 0.24033 0.25696 0.27712 -0.00690 0.00313  -0.02132 51  ASN A C   
293  O O   . ASN A 44  ? 0.23332 0.25006 0.26891 -0.00685 0.00283  -0.01454 51  ASN A O   
294  C CB  . ASN A 44  ? 0.21949 0.27028 0.27379 -0.01215 0.00711  -0.00653 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.32675 0.39447 0.39701 -0.02297 0.00140  0.00844  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.27696 0.33361 0.35057 -0.03783 -0.01264 0.01481  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.31284 0.40544 0.39223 -0.01568 0.01016  0.01537  51  ASN A ND2 
298  N N   . SER A 45  ? 0.19775 0.21052 0.23111 0.00064  0.00659  -0.03281 52  SER A N   
299  C CA  . SER A 45  ? 0.23708 0.24595 0.26793 0.00759  0.00719  -0.03758 52  SER A CA  
300  C C   . SER A 45  ? 0.23007 0.22384 0.25805 0.00783  0.00219  -0.03738 52  SER A C   
301  O O   . SER A 45  ? 0.22984 0.22229 0.25597 0.01048  0.00007  -0.03446 52  SER A O   
302  C CB  . SER A 45  ? 0.21998 0.23046 0.25455 0.01197  0.00954  -0.04530 52  SER A CB  
303  O OG  . SER A 45  ? 0.22756 0.24504 0.25963 0.01353  0.01241  -0.04589 52  SER A OG  
304  N N   . SER A 46  ? 0.21996 0.19768 0.24227 0.00708  -0.00041 -0.04050 53  SER A N   
305  C CA  . SER A 46  ? 0.24285 0.19861 0.25556 0.01091  -0.00499 -0.04069 53  SER A CA  
306  C C   . SER A 46  ? 0.28092 0.23050 0.29118 0.00234  -0.01178 -0.03117 53  SER A C   
307  O O   . SER A 46  ? 0.27356 0.21459 0.28050 0.00683  -0.01393 -0.02879 53  SER A O   
308  C CB  . SER A 46  ? 0.26803 0.19838 0.26358 0.01405  -0.00732 -0.04653 53  SER A CB  
309  O OG  . SER A 46  ? 0.31609 0.21657 0.29449 0.02082  -0.01218 -0.04717 53  SER A OG  
310  N N   . ASP A 47  ? 0.24902 0.20629 0.26384 -0.00995 -0.01501 -0.02262 54  ASP A N   
311  C CA  . ASP A 47  ? 0.26257 0.21946 0.28010 -0.01942 -0.02028 -0.00845 54  ASP A CA  
312  C C   . ASP A 47  ? 0.27052 0.24479 0.29113 -0.01218 -0.01259 -0.00351 54  ASP A C   
313  O O   . ASP A 47  ? 0.25855 0.22399 0.27479 -0.01336 -0.01593 0.00438  54  ASP A O   
314  C CB  . ASP A 47  ? 0.24806 0.22159 0.27871 -0.03337 -0.02357 0.00473  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.39439 0.34118 0.41661 -0.04554 -0.03918 0.00324  54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.40102 0.30903 0.39997 -0.04127 -0.04678 -0.00818 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.40247 0.36572 0.43911 -0.05824 -0.04477 0.01468  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.23574 0.22931 0.25881 -0.00406 -0.00384 -0.00827 55  ALA A N   
319  C CA  . ALA A 48  ? 0.23761 0.23879 0.25316 0.00484  0.00074  -0.00613 55  ALA A CA  
320  C C   . ALA A 48  ? 0.24804 0.23502 0.25761 0.01101  -0.00508 -0.01286 55  ALA A C   
321  O O   . ALA A 48  ? 0.24402 0.22800 0.24439 0.01491  -0.00676 -0.00739 55  ALA A O   
322  C CB  . ALA A 48  ? 0.25091 0.26396 0.26263 0.01241  0.00739  -0.01189 55  ALA A CB  
323  N N   . LEU A 49  ? 0.22678 0.20728 0.24210 0.01337  -0.00751 -0.02251 56  LEU A N   
324  C CA  . LEU A 49  ? 0.25020 0.22402 0.26700 0.02068  -0.01223 -0.02507 56  LEU A CA  
325  C C   . LEU A 49  ? 0.26086 0.21614 0.27072 0.02086  -0.01658 -0.01921 56  LEU A C   
326  O O   . LEU A 49  ? 0.27701 0.22904 0.28424 0.02639  -0.02091 -0.01564 56  LEU A O   
327  C CB  . LEU A 49  ? 0.23729 0.21463 0.26524 0.02570  -0.01000 -0.03212 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.20251 0.19560 0.23824 0.02451  -0.00917 -0.03580 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.23375 0.23283 0.28051 0.02638  -0.00324 -0.03984 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.23393 0.23254 0.27478 0.02703  -0.01808 -0.03356 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.26543 0.20454 0.26993 0.01420  -0.01818 -0.01758 57  ASP A N   
332  C CA  . ASP A 50  ? 0.26953 0.18239 0.26271 0.01233  -0.02542 -0.01115 57  ASP A CA  
333  C C   . ASP A 50  ? 0.31063 0.23026 0.30265 0.00759  -0.02661 0.00174  57  ASP A C   
334  O O   . ASP A 50  ? 0.29128 0.19531 0.27545 0.01160  -0.03144 0.00669  57  ASP A O   
335  C CB  . ASP A 50  ? 0.27788 0.16705 0.26200 0.00084  -0.03248 -0.00953 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.33255 0.20214 0.30518 0.00867  -0.03255 -0.02199 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.38183 0.25723 0.35634 0.02479  -0.02496 -0.02952 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.38975 0.23697 0.35029 -0.00138 -0.04127 -0.02223 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.27131 0.21417 0.26898 0.00175  -0.02069 0.00863  58  LYS A N   
340  C CA  . LYS A 51  ? 0.26970 0.22065 0.26305 0.00008  -0.01821 0.02385  58  LYS A CA  
341  C C   . LYS A 51  ? 0.27615 0.22661 0.25778 0.01265  -0.01869 0.02080  58  LYS A C   
342  O O   . LYS A 51  ? 0.32059 0.26131 0.29311 0.01393  -0.02183 0.03072  58  LYS A O   
343  C CB  . LYS A 51  ? 0.31352 0.29163 0.31394 -0.00328 -0.00830 0.03325  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.32912 0.31199 0.34557 -0.01949 -0.01143 0.04459  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.32109 0.33851 0.34876 -0.01801 0.00083  0.05521  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.34891 0.37676 0.39825 -0.03482 -0.00500 0.06569  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.41818 0.48510 0.48210 -0.02983 0.00870  0.07835  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.27499 0.23346 0.25609 0.02066  -0.01829 0.00850  59  ILE A N   
349  C CA  . ILE A 52  ? 0.27395 0.22888 0.24302 0.02985  -0.02444 0.00709  59  ILE A CA  
350  C C   . ILE A 52  ? 0.31510 0.25797 0.29088 0.03367  -0.03301 0.00617  59  ILE A C   
351  O O   . ILE A 52  ? 0.33459 0.27055 0.30034 0.03903  -0.03953 0.01191  59  ILE A O   
352  C CB  . ILE A 52  ? 0.30316 0.26538 0.26826 0.03433  -0.02666 -0.00338 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.30738 0.26065 0.25353 0.04147  -0.03813 -0.00310 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.27333 0.24171 0.26040 0.03228  -0.02896 -0.01315 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.36871 0.31430 0.28512 0.04754  -0.03391 0.00654  59  ILE A CD1 
356  N N   . ARG A 53  ? 0.28317 0.22142 0.27220 0.03370  -0.03240 0.00037  60  ARG A N   
357  C CA  . ARG A 53  ? 0.30552 0.23038 0.29710 0.04261  -0.03746 0.00159  60  ARG A CA  
358  C C   . ARG A 53  ? 0.31902 0.22091 0.29578 0.04062  -0.04112 0.01189  60  ARG A C   
359  O O   . ARG A 53  ? 0.35719 0.25171 0.32935 0.04875  -0.04706 0.01731  60  ARG A O   
360  C CB  . ARG A 53  ? 0.34466 0.26306 0.34379 0.04768  -0.03319 -0.00568 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.43130 0.33577 0.42975 0.06327  -0.03568 -0.00283 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.59681 0.49288 0.59570 0.07440  -0.02854 -0.00906 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.62665 0.55464 0.65070 0.08388  -0.02306 -0.00896 60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.69802 0.63042 0.72587 0.09009  -0.01341 -0.01378 60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.57766 0.48208 0.58220 0.08751  -0.01039 -0.02154 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.51108 0.47656 0.56674 0.09819  -0.00808 -0.00876 60  ARG A NH2 
367  N N   . TYR A 54  ? 0.30618 0.19792 0.27707 0.02829  -0.03922 0.01742  61  TYR A N   
368  C CA  . TYR A 54  ? 0.34722 0.21597 0.30636 0.02298  -0.04460 0.03049  61  TYR A CA  
369  C C   . TYR A 54  ? 0.37243 0.25172 0.32385 0.02608  -0.04420 0.04139  61  TYR A C   
370  O O   . TYR A 54  ? 0.38063 0.24229 0.32201 0.03074  -0.05018 0.04918  61  TYR A O   
371  C CB  . TYR A 54  ? 0.34556 0.20811 0.30647 0.00490  -0.04533 0.03918  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.39561 0.23107 0.34658 -0.00427 -0.05393 0.05585  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.42089 0.21198 0.35600 -0.00148 -0.06516 0.05288  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.38934 0.24185 0.34394 -0.01333 -0.04998 0.07611  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.45084 0.21222 0.37480 -0.01080 -0.07513 0.06869  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.44912 0.27909 0.39738 -0.02328 -0.05786 0.09467  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.47742 0.26009 0.41073 -0.02374 -0.07199 0.09057  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.54019 0.29440 0.46498 -0.03496 -0.08222 0.10950  61  TYR A OH  
379  N N   . GLU A 55  ? 0.37032 0.27420 0.32101 0.02587  -0.03727 0.04201  62  GLU A N   
380  C CA  . GLU A 55  ? 0.41253 0.32016 0.34565 0.03191  -0.03654 0.05212  62  GLU A CA  
381  C C   . GLU A 55  ? 0.43409 0.33517 0.36041 0.04385  -0.04704 0.04615  62  GLU A C   
382  O O   . GLU A 55  ? 0.45143 0.34343 0.36106 0.04908  -0.05143 0.05600  62  GLU A O   
383  C CB  . GLU A 55  ? 0.42074 0.34830 0.34456 0.03498  -0.02701 0.05189  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.41143 0.35417 0.34378 0.02583  -0.01485 0.06515  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.62690 0.58677 0.54178 0.03621  -0.00213 0.06995  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.75213 0.72951 0.67171 0.03341  0.01042  0.08962  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.70340 0.65726 0.59755 0.04819  -0.00542 0.05663  62  GLU A OE2 
388  N N   . SER A 56  ? 0.39584 0.30388 0.33695 0.04799  -0.05166 0.03284  63  SER A N   
389  C CA  . SER A 56  ? 0.42192 0.33111 0.36560 0.05774  -0.06374 0.03110  63  SER A CA  
390  C C   . SER A 56  ? 0.43030 0.32353 0.37742 0.06492  -0.06853 0.03787  63  SER A C   
391  O O   . SER A 56  ? 0.43518 0.33002 0.38334 0.07404  -0.07915 0.04188  63  SER A O   
392  C CB  . SER A 56  ? 0.37772 0.30482 0.34368 0.05869  -0.06645 0.02022  63  SER A CB  
393  O OG  . SER A 56  ? 0.41863 0.34557 0.40455 0.06219  -0.06112 0.01724  63  SER A OG  
394  N N   . LEU A 57  ? 0.40744 0.28187 0.35411 0.06157  -0.06316 0.03983  64  LEU A N   
395  C CA  . LEU A 57  ? 0.48571 0.33579 0.42814 0.07131  -0.06825 0.04533  64  LEU A CA  
396  C C   . LEU A 57  ? 0.49104 0.32963 0.41597 0.07301  -0.07479 0.05883  64  LEU A C   
397  O O   . LEU A 57  ? 0.61855 0.44606 0.54164 0.08568  -0.08201 0.06383  64  LEU A O   
398  C CB  . LEU A 57  ? 0.44876 0.26858 0.38357 0.06550  -0.06540 0.04433  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.45848 0.28293 0.40401 0.06773  -0.05939 0.03089  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.48423 0.26717 0.41182 0.06247  -0.06191 0.02987  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.46946 0.30781 0.42967 0.08754  -0.05769 0.02608  64  LEU A CD2 
402  N N   . THR A 58  ? 0.49771 0.33922 0.40901 0.06257  -0.07103 0.06696  65  THR A N   
403  C CA  . THR A 58  ? 0.56101 0.39183 0.45186 0.06512  -0.07513 0.08199  65  THR A CA  
404  C C   . THR A 58  ? 0.60172 0.44934 0.47785 0.07099  -0.07818 0.08155  65  THR A C   
405  O O   . THR A 58  ? 0.67793 0.51588 0.53207 0.07644  -0.08283 0.09315  65  THR A O   
406  C CB  . THR A 58  ? 0.65677 0.47622 0.53897 0.05121  -0.06810 0.09795  65  THR A CB  
407  O OG1 . THR A 58  ? 0.65811 0.50168 0.54463 0.04258  -0.05668 0.09781  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.62864 0.41750 0.51630 0.04350  -0.07232 0.09968  65  THR A CG2 
409  N N   . ASP A 59  ? 0.54570 0.41243 0.42871 0.07064  -0.07770 0.06859  66  ASP A N   
410  C CA  . ASP A 59  ? 0.55191 0.42382 0.41173 0.07598  -0.08417 0.06605  66  ASP A CA  
411  C C   . ASP A 59  ? 0.51674 0.40355 0.39508 0.07533  -0.09290 0.05103  66  ASP A C   
412  O O   . ASP A 59  ? 0.50928 0.40508 0.39043 0.07020  -0.08544 0.04207  66  ASP A O   
413  C CB  . ASP A 59  ? 0.53727 0.41081 0.37224 0.07435  -0.06963 0.07166  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.74582 0.61253 0.54210 0.08448  -0.07632 0.06790  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.68513 0.54537 0.47638 0.08828  -0.09640 0.06072  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.71708 0.58348 0.48617 0.08956  -0.06231 0.07350  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.57518 0.46715 0.46959 0.08021  -0.10906 0.05071  67  PRO A N   
418  C CA  . PRO A 60  ? 0.52236 0.43319 0.44198 0.07701  -0.11831 0.04158  67  PRO A CA  
419  C C   . PRO A 60  ? 0.51025 0.41584 0.40473 0.07264  -0.12719 0.03364  67  PRO A C   
420  O O   . PRO A 60  ? 0.55132 0.46909 0.46451 0.06619  -0.13082 0.02554  67  PRO A O   
421  C CB  . PRO A 60  ? 0.57187 0.49221 0.51217 0.08393  -0.13606 0.04993  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.65508 0.55869 0.58085 0.09234  -0.13396 0.06050  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.63576 0.52116 0.53769 0.08844  -0.11601 0.06107  67  PRO A CD  
424  N N   . SER A 61  ? 0.55757 0.44155 0.40614 0.07764  -0.13133 0.03638  68  SER A N   
425  C CA  . SER A 61  ? 0.56314 0.43131 0.37592 0.07772  -0.14046 0.02739  68  SER A CA  
426  C C   . SER A 61  ? 0.54158 0.41390 0.35308 0.07510  -0.12080 0.01896  68  SER A C   
427  O O   . SER A 61  ? 0.55357 0.41231 0.34137 0.07520  -0.12826 0.00924  68  SER A O   
428  C CB  . SER A 61  ? 0.57253 0.41203 0.32685 0.08898  -0.14526 0.03250  68  SER A CB  
429  O OG  . SER A 61  ? 0.66168 0.50002 0.39745 0.09542  -0.11844 0.03963  68  SER A OG  
430  N N   . LYS A 62  ? 0.46664 0.35447 0.30209 0.07236  -0.09848 0.02272  69  LYS A N   
431  C CA  . LYS A 62  ? 0.48863 0.38479 0.32932 0.06897  -0.08244 0.01602  69  LYS A CA  
432  C C   . LYS A 62  ? 0.48224 0.38766 0.34864 0.06128  -0.09171 0.00436  69  LYS A C   
433  O O   . LYS A 62  ? 0.44789 0.35483 0.31129 0.05959  -0.08341 -0.00303 69  LYS A O   
434  C CB  . LYS A 62  ? 0.51603 0.42615 0.38196 0.06386  -0.06338 0.02347  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.63620 0.53977 0.48126 0.06834  -0.05391 0.03938  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.54661 0.46022 0.38349 0.06919  -0.03389 0.04664  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.63139 0.54385 0.44979 0.07390  -0.02305 0.06756  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.72859 0.65748 0.53900 0.07914  -0.00253 0.07653  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.44265 0.35804 0.33862 0.05709  -0.10706 0.00528  70  LEU A N   
440  C CA  . LEU A 63  ? 0.41448 0.34324 0.33914 0.04900  -0.11571 -0.00088 70  LEU A CA  
441  C C   . LEU A 63  ? 0.43338 0.34758 0.34086 0.04488  -0.14334 -0.00326 70  LEU A C   
442  O O   . LEU A 63  ? 0.44740 0.37376 0.38280 0.03526  -0.15517 -0.00418 70  LEU A O   
443  C CB  . LEU A 63  ? 0.40532 0.35981 0.37855 0.04814  -0.11343 0.00528  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.44402 0.40346 0.42948 0.05111  -0.09083 0.00531  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.42195 0.39937 0.44452 0.05609  -0.08885 0.01055  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.38692 0.34768 0.36968 0.04554  -0.07719 -0.00354 70  LEU A CD2 
447  N N   . ASP A 64  ? 0.48066 0.36572 0.33895 0.05144  -0.15438 -0.00376 71  ASP A N   
448  C CA  . ASP A 64  ? 0.53835 0.39798 0.36932 0.04666  -0.18531 -0.00788 71  ASP A CA  
449  C C   . ASP A 64  ? 0.51436 0.36033 0.33463 0.04065  -0.18729 -0.01919 71  ASP A C   
450  O O   . ASP A 64  ? 0.58629 0.41512 0.40018 0.03023  -0.21616 -0.02173 71  ASP A O   
451  C CB  . ASP A 64  ? 0.64784 0.46997 0.41383 0.05917  -0.19369 -0.00814 71  ASP A CB  
452  C CG  . ASP A 64  ? 0.75803 0.58766 0.53196 0.06256  -0.20345 0.00431  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.64007 0.50329 0.46952 0.05704  -0.20356 0.01324  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.79803 0.59846 0.51876 0.07388  -0.20872 0.00614  71  ASP A OD2 
455  N N   . SER A 65  ? 0.51682 0.36755 0.33341 0.04641  -0.15944 -0.02462 72  SER A N   
456  C CA  . SER A 65  ? 0.51990 0.35818 0.32519 0.04410  -0.15631 -0.03470 72  SER A CA  
457  C C   . SER A 65  ? 0.55985 0.43009 0.42367 0.02987  -0.15379 -0.03341 72  SER A C   
458  O O   . SER A 65  ? 0.55703 0.42260 0.41876 0.02780  -0.14656 -0.04036 72  SER A O   
459  C CB  . SER A 65  ? 0.49761 0.33158 0.27411 0.05930  -0.12628 -0.03723 72  SER A CB  
460  O OG  . SER A 65  ? 0.46026 0.32794 0.27214 0.05962  -0.10297 -0.02840 72  SER A OG  
461  N N   . GLY A 66  ? 0.47110 0.37400 0.38527 0.02295  -0.15727 -0.02329 73  GLY A N   
462  C CA  . GLY A 66  ? 0.50145 0.43660 0.46891 0.01353  -0.15171 -0.01921 73  GLY A CA  
463  C C   . GLY A 66  ? 0.42617 0.39381 0.43266 0.01908  -0.13462 -0.01055 73  GLY A C   
464  O O   . GLY A 66  ? 0.37018 0.33733 0.36758 0.02722  -0.11294 -0.01343 73  GLY A O   
465  N N   . LYS A 67  ? 0.35918 0.35383 0.40840 0.01553  -0.14510 0.00189  74  LYS A N   
466  C CA  . LYS A 67  ? 0.35495 0.37390 0.43378 0.02607  -0.12846 0.00998  74  LYS A CA  
467  C C   . LYS A 67  ? 0.29128 0.32973 0.39669 0.02868  -0.10600 0.00903  74  LYS A C   
468  O O   . LYS A 67  ? 0.38887 0.43110 0.49899 0.04007  -0.08846 0.00987  74  LYS A O   
469  C CB  . LYS A 67  ? 0.33984 0.38342 0.45400 0.02677  -0.14576 0.02678  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.49883 0.52195 0.58406 0.02838  -0.16586 0.02882  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.69760 0.74907 0.82063 0.03448  -0.17651 0.04724  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.76786 0.79713 0.85881 0.03834  -0.19418 0.04929  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.80414 0.80177 0.85501 0.02577  -0.22024 0.04155  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.31466 0.36097 0.43352 0.01900  -0.10763 0.00770  75  GLU A N   
475  C CA  . GLU A 68  ? 0.26051 0.32667 0.40431 0.02291  -0.08712 0.00911  75  GLU A CA  
476  C C   . GLU A 68  ? 0.27291 0.31905 0.38743 0.02582  -0.06876 -0.00519 75  GLU A C   
477  O O   . GLU A 68  ? 0.30863 0.33451 0.39495 0.01983  -0.07251 -0.01453 75  GLU A O   
478  C CB  . GLU A 68  ? 0.39038 0.47506 0.56337 0.01038  -0.09663 0.01697  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.67777 0.79739 0.89128 0.01806  -0.07817 0.02914  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.73473 0.86721 0.96926 0.00496  -0.08073 0.03472  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.72083 0.83918 0.94901 -0.01254 -0.10442 0.03395  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.57191 0.72158 0.82176 0.01288  -0.05953 0.03862  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.25837 0.30827 0.37740 0.03625  -0.05038 -0.00565 76  LEU A N   
484  C CA  . LEU A 69  ? 0.23835 0.27101 0.33416 0.03715  -0.03619 -0.01628 76  LEU A CA  
485  C C   . LEU A 69  ? 0.20635 0.25056 0.31639 0.03827  -0.02401 -0.01712 76  LEU A C   
486  O O   . LEU A 69  ? 0.23830 0.29285 0.36262 0.04966  -0.01404 -0.01140 76  LEU A O   
487  C CB  . LEU A 69  ? 0.27074 0.28817 0.35262 0.04641  -0.03004 -0.01616 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.32271 0.32816 0.38834 0.04546  -0.04079 -0.01349 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.39909 0.38419 0.44814 0.05074  -0.03457 -0.01317 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.29864 0.29499 0.34215 0.03671  -0.04636 -0.01829 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.19266 0.23416 0.29644 0.02902  -0.02432 -0.02303 77  HIS A N   
492  C CA  . HIS A 70  ? 0.22157 0.27509 0.33956 0.02948  -0.01419 -0.02181 77  HIS A CA  
493  C C   . HIS A 70  ? 0.19934 0.24095 0.29951 0.02209  -0.01206 -0.03098 77  HIS A C   
494  O O   . HIS A 70  ? 0.18958 0.21687 0.26894 0.01802  -0.01785 -0.03666 77  HIS A O   
495  C CB  . HIS A 70  ? 0.18687 0.26600 0.33931 0.02535  -0.02139 -0.00864 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.21760 0.28942 0.36720 0.01043  -0.04087 -0.00938 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.45975 0.53763 0.62294 0.00410  -0.06048 -0.00056 77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.34051 0.39260 0.46806 0.00230  -0.04569 -0.01866 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.32213 0.37996 0.46867 -0.00832 -0.07833 -0.00520 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.38948 0.43086 0.51340 -0.00809 -0.06839 -0.01633 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.17930 0.22847 0.28767 0.02277  -0.00264 -0.03036 78  ILE A N   
502  C CA  . ILE A 71  ? 0.19001 0.23137 0.28578 0.01790  0.00093  -0.03689 78  ILE A CA  
503  C C   . ILE A 71  ? 0.17740 0.23148 0.29275 0.01271  0.00019  -0.03016 78  ILE A C   
504  O O   . ILE A 71  ? 0.19008 0.26274 0.32719 0.01778  0.00795  -0.02035 78  ILE A O   
505  C CB  . ILE A 71  ? 0.21955 0.25280 0.30099 0.02374  0.01258  -0.04199 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.22296 0.24240 0.28836 0.02526  0.01035  -0.04507 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.20819 0.23795 0.28083 0.01926  0.01556  -0.04630 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.24072 0.24528 0.29022 0.02836  0.01559  -0.04867 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.16956 0.21248 0.27594 0.00410  -0.00877 -0.03349 79  ASN A N   
510  C CA  . ASN A 72  ? 0.16935 0.21797 0.29105 -0.00366 -0.01183 -0.02656 79  ASN A CA  
511  C C   . ASN A 72  ? 0.20414 0.24053 0.30684 -0.00221 -0.00382 -0.03399 79  ASN A C   
512  O O   . ASN A 72  ? 0.18752 0.20726 0.26482 0.00066  -0.00430 -0.04349 79  ASN A O   
513  C CB  . ASN A 72  ? 0.19437 0.23114 0.31734 -0.01597 -0.03394 -0.02331 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.20114 0.25338 0.34767 -0.01955 -0.04564 -0.01286 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.19269 0.27357 0.36748 -0.01327 -0.03496 -0.00212 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.24582 0.27766 0.37918 -0.02832 -0.06882 -0.01451 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.16753 0.21435 0.28381 -0.00329 0.00377  -0.02708 80  LEU A N   
518  C CA  . LEU A 73  ? 0.15390 0.18999 0.25485 -0.00256 0.00935  -0.03167 80  LEU A CA  
519  C C   . LEU A 73  ? 0.14462 0.17505 0.25539 -0.01366 -0.00084 -0.02379 80  LEU A C   
520  O O   . LEU A 73  ? 0.16764 0.21742 0.30802 -0.01976 -0.00109 -0.00880 80  LEU A O   
521  C CB  . LEU A 73  ? 0.19864 0.24579 0.30046 0.00620  0.02594  -0.02978 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.20126 0.24746 0.29170 0.01570  0.03257  -0.03584 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.21532 0.26328 0.29859 0.02515  0.04598  -0.03358 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.19692 0.22927 0.26701 0.01457  0.02766  -0.04583 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.20653 0.20956 0.29242 -0.01575 -0.01008 -0.03173 81  ILE A N   
526  C CA  . ILE A 74  ? 0.22081 0.20474 0.30694 -0.02781 -0.02622 -0.02611 81  ILE A CA  
527  C C   . ILE A 74  ? 0.27007 0.23676 0.33697 -0.02389 -0.02083 -0.02970 81  ILE A C   
528  O O   . ILE A 74  ? 0.26516 0.20592 0.29918 -0.01540 -0.02298 -0.04080 81  ILE A O   
529  C CB  . ILE A 74  ? 0.25892 0.21205 0.32233 -0.03215 -0.04782 -0.03271 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.22810 0.19976 0.30862 -0.03380 -0.05233 -0.02954 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.27464 0.20128 0.33726 -0.04814 -0.06996 -0.02535 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.27349 0.21463 0.32793 -0.03677 -0.07458 -0.03585 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.22080 0.20072 0.30652 -0.02838 -0.01374 -0.01846 82  PRO A N   
534  C CA  . PRO A 75  ? 0.25265 0.21337 0.32069 -0.02611 -0.01147 -0.01963 82  PRO A CA  
535  C C   . PRO A 75  ? 0.29030 0.21642 0.34926 -0.03909 -0.03294 -0.01550 82  PRO A C   
536  O O   . PRO A 75  ? 0.30807 0.23655 0.38945 -0.05545 -0.04845 -0.00390 82  PRO A O   
537  C CB  . PRO A 75  ? 0.24641 0.23586 0.33754 -0.02541 0.00498  -0.00706 82  PRO A CB  
538  C CG  . PRO A 75  ? 0.25884 0.27716 0.38635 -0.03328 0.00463  0.00758  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.25152 0.26619 0.37647 -0.03412 -0.00654 -0.00095 82  PRO A CD  
540  N N   . ASN A 76  ? 0.30618 0.19740 0.33055 -0.03144 -0.03580 -0.02402 83  ASN A N   
541  C CA  . ASN A 76  ? 0.34128 0.18574 0.34439 -0.04098 -0.05764 -0.02247 83  ASN A CA  
542  C C   . ASN A 76  ? 0.41172 0.23910 0.39618 -0.03209 -0.04949 -0.02272 83  ASN A C   
543  O O   . ASN A 76  ? 0.41976 0.22930 0.37068 -0.01268 -0.04255 -0.03489 83  ASN A O   
544  C CB  . ASN A 76  ? 0.42553 0.22645 0.38705 -0.03491 -0.07487 -0.03672 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.52822 0.27089 0.46290 -0.04773 -0.10404 -0.03504 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.54658 0.26320 0.46823 -0.04855 -0.10665 -0.03156 83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.61527 0.34144 0.54157 -0.05710 -0.12556 -0.03540 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.35120 0.24724 0.40068 -0.01979 0.01718  0.05167  84  LYS A N   
549  C CA  . LYS A 77  ? 0.36099 0.24796 0.40711 -0.00890 0.02569  0.06191  84  LYS A CA  
550  C C   . LYS A 77  ? 0.43262 0.28084 0.47293 -0.01384 0.02816  0.05999  84  LYS A C   
551  O O   . LYS A 77  ? 0.49398 0.33009 0.52675 -0.00158 0.03464  0.06427  84  LYS A O   
552  C CB  . LYS A 77  ? 0.37556 0.28114 0.43419 -0.00813 0.03177  0.08035  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.39400 0.33719 0.45410 0.00272  0.03164  0.08263  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.41176 0.37429 0.48230 0.00591  0.03897  0.10196  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.43285 0.43232 0.50448 0.01574  0.03888  0.10354  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.47106 0.48104 0.54956 0.00565  0.03211  0.09611  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.43925 0.26793 0.48217 -0.03099 0.02303  0.05319  85  GLN A N   
558  C CA  . GLN A 78  ? 0.54960 0.33733 0.58517 -0.03563 0.02555  0.04961  85  GLN A CA  
559  C C   . GLN A 78  ? 0.52483 0.29746 0.54242 -0.02460 0.02481  0.03573  85  GLN A C   
560  O O   . GLN A 78  ? 0.58686 0.33413 0.59546 -0.01551 0.03147  0.03742  85  GLN A O   
561  C CB  . GLN A 78  ? 0.60320 0.37398 0.64515 -0.05810 0.01911  0.04396  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.86853 0.64943 0.93076 -0.07239 0.02035  0.05925  85  GLN A CG  
563  C CD  . GLN A 78  ? 0.96869 0.79450 1.04301 -0.06631 0.02137  0.07106  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.89122 0.72856 0.97327 -0.05869 0.02964  0.08820  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.82595 0.67719 0.90057 -0.06786 0.01357  0.06206  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.42691 0.21614 0.43989 -0.02420 0.01763  0.02360  86  ASP A N   
567  C CA  . ASP A 79  ? 0.44572 0.22815 0.44378 -0.01387 0.01663  0.01159  86  ASP A CA  
568  C C   . ASP A 79  ? 0.42611 0.23131 0.42238 0.00383  0.02047  0.01623  86  ASP A C   
569  O O   . ASP A 79  ? 0.42749 0.22921 0.41337 0.01371  0.02107  0.00928  86  ASP A O   
570  C CB  . ASP A 79  ? 0.51376 0.30615 0.50920 -0.02195 0.00736  -0.00179 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.63413 0.40733 0.62926 -0.03981 0.00157  -0.00915 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.71018 0.45578 0.70536 -0.04652 0.00473  -0.00637 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.66551 0.45233 0.66094 -0.04744 -0.00635 -0.01735 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.40625 0.23634 0.41238 0.00761  0.02268  0.02744  87  ARG A N   
575  C CA  . ARG A 80  ? 0.34443 0.20065 0.34919 0.02253  0.02439  0.03013  87  ARG A CA  
576  C C   . ARG A 80  ? 0.35761 0.22825 0.35882 0.02359  0.01781  0.01747  87  ARG A C   
577  O O   . ARG A 80  ? 0.35866 0.23634 0.35397 0.03433  0.01847  0.01405  87  ARG A O   
578  C CB  . ARG A 80  ? 0.39693 0.24403 0.39448 0.03728  0.03193  0.03662  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.37541 0.25381 0.37533 0.05010  0.03414  0.04451  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.57463 0.45570 0.56710 0.06579  0.03854  0.04735  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.64445 0.50167 0.63435 0.07116  0.04710  0.05835  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.71922 0.56654 0.70116 0.08389  0.05218  0.06036  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.53502 0.39603 0.51180 0.09123  0.04906  0.05210  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.73291 0.55686 0.71298 0.08979  0.06112  0.07207  87  ARG A NH2 
585  N N   . THR A 81  ? 0.32916 0.20649 0.33534 0.01247  0.01157  0.01174  88  THR A N   
586  C CA  . THR A 81  ? 0.32748 0.21696 0.33161 0.01294  0.00604  0.00158  88  THR A CA  
587  C C   . THR A 81  ? 0.29113 0.20524 0.30423 0.01070  0.00295  0.00319  88  THR A C   
588  O O   . THR A 81  ? 0.28566 0.20525 0.30693 0.00373  0.00294  0.00970  88  THR A O   
589  C CB  . THR A 81  ? 0.31549 0.18853 0.31407 0.00402  0.00146  -0.00833 88  THR A CB  
590  O OG1 . THR A 81  ? 0.35195 0.22005 0.35670 -0.00975 -0.00156 -0.00667 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.34765 0.19642 0.33445 0.00937  0.00504  -0.01197 88  THR A CG2 
592  N N   . LEU A 82  ? 0.24745 0.17636 0.25953 0.01682  0.00073  -0.00234 89  LEU A N   
593  C CA  . LEU A 82  ? 0.24440 0.19174 0.26274 0.01539  -0.00245 -0.00382 89  LEU A CA  
594  C C   . LEU A 82  ? 0.27202 0.21629 0.28832 0.01181  -0.00711 -0.01285 89  LEU A C   
595  O O   . LEU A 82  ? 0.27313 0.21387 0.28425 0.01649  -0.00731 -0.01822 89  LEU A O   
596  C CB  . LEU A 82  ? 0.24171 0.20743 0.26016 0.02586  -0.00093 -0.00325 89  LEU A CB  
597  C CG  . LEU A 82  ? 0.21933 0.20057 0.24238 0.02635  -0.00342 -0.00620 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.24383 0.23358 0.27459 0.02168  -0.00224 0.00210  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.25578 0.25137 0.27589 0.03664  -0.00262 -0.00901 89  LEU A CD2 
600  N N   . THR A 83  ? 0.23484 0.18268 0.25587 0.00388  -0.01061 -0.01327 90  THR A N   
601  C CA  . THR A 83  ? 0.25947 0.20597 0.27855 0.00091  -0.01463 -0.01982 90  THR A CA  
602  C C   . THR A 83  ? 0.26070 0.22398 0.28640 0.00333  -0.01600 -0.01943 90  THR A C   
603  O O   . THR A 83  ? 0.25060 0.22590 0.28324 0.00226  -0.01554 -0.01378 90  THR A O   
604  C CB  . THR A 83  ? 0.27289 0.21035 0.29055 -0.00980 -0.01814 -0.02102 90  THR A CB  
605  O OG1 . THR A 83  ? 0.27334 0.19026 0.28331 -0.01168 -0.01637 -0.02266 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.29938 0.23955 0.31420 -0.01113 -0.02205 -0.02658 90  THR A CG2 
607  N N   . ILE A 84  ? 0.21659 0.18074 0.24074 0.00743  -0.01683 -0.02449 91  ILE A N   
608  C CA  . ILE A 84  ? 0.21486 0.18966 0.24437 0.01043  -0.01751 -0.02483 91  ILE A CA  
609  C C   . ILE A 84  ? 0.26302 0.23643 0.29242 0.00608  -0.02043 -0.02581 91  ILE A C   
610  O O   . ILE A 84  ? 0.25673 0.22252 0.28145 0.00641  -0.02081 -0.02956 91  ILE A O   
611  C CB  . ILE A 84  ? 0.24950 0.22501 0.27839 0.01745  -0.01624 -0.02958 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.29086 0.27117 0.31804 0.02286  -0.01394 -0.02910 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.23564 0.21673 0.26940 0.02045  -0.01638 -0.03056 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.36367 0.33849 0.38565 0.02447  -0.01281 -0.02967 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.21980 0.20323 0.25441 0.00296  -0.02224 -0.02157 92  VAL A N   
616  C CA  . VAL A 85  ? 0.22502 0.21140 0.25921 -0.00066 -0.02543 -0.02117 92  VAL A CA  
617  C C   . VAL A 85  ? 0.25229 0.24802 0.29264 0.00548  -0.02412 -0.01819 92  VAL A C   
618  O O   . VAL A 85  ? 0.24570 0.25130 0.29217 0.00906  -0.02240 -0.01418 92  VAL A O   
619  C CB  . VAL A 85  ? 0.25407 0.24784 0.29023 -0.00967 -0.02938 -0.01782 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.26300 0.26117 0.29592 -0.01309 -0.03354 -0.01866 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.28365 0.26469 0.31505 -0.01600 -0.02974 -0.02016 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.22965 0.22324 0.26859 0.00713  -0.02445 -0.01877 93  ASP A N   
623  C CA  . ASP A 86  ? 0.22684 0.22759 0.27211 0.01304  -0.02269 -0.01422 93  ASP A CA  
624  C C   . ASP A 86  ? 0.24734 0.25469 0.29131 0.01128  -0.02504 -0.01034 93  ASP A C   
625  O O   . ASP A 86  ? 0.23563 0.23886 0.27218 0.00680  -0.02746 -0.01338 93  ASP A O   
626  C CB  . ASP A 86  ? 0.22460 0.21468 0.27148 0.01911  -0.01902 -0.01787 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.25217 0.23343 0.29607 0.01765  -0.01888 -0.02022 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.25755 0.24198 0.30121 0.01746  -0.01922 -0.01593 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.26720 0.24086 0.30852 0.01684  -0.01844 -0.02568 93  ASP A OD2 
630  N N   . THR A 87  ? 0.19938 0.21827 0.24957 0.01597  -0.02409 -0.00323 94  THR A N   
631  C CA  . THR A 87  ? 0.20457 0.23338 0.25381 0.01622  -0.02593 0.00226  94  THR A CA  
632  C C   . THR A 87  ? 0.26045 0.28212 0.31281 0.02389  -0.02108 0.00593  94  THR A C   
633  O O   . THR A 87  ? 0.22920 0.26065 0.28554 0.02925  -0.01966 0.01455  94  THR A O   
634  C CB  . THR A 87  ? 0.22919 0.28005 0.28413 0.01614  -0.02850 0.01006  94  THR A CB  
635  O OG1 . THR A 87  ? 0.23338 0.28734 0.29664 0.02423  -0.02386 0.01451  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.23014 0.28780 0.28291 0.00517  -0.03429 0.00666  94  THR A CG2 
637  N N   . GLY A 88  ? 0.23399 0.23902 0.28532 0.02411  -0.01845 0.00017  95  GLY A N   
638  C CA  . GLY A 88  ? 0.26290 0.25953 0.31888 0.02900  -0.01403 0.00366  95  GLY A CA  
639  C C   . GLY A 88  ? 0.25789 0.25817 0.31009 0.02808  -0.01418 0.00798  95  GLY A C   
640  O O   . GLY A 88  ? 0.24440 0.25649 0.28947 0.02544  -0.01801 0.00914  95  GLY A O   
641  N N   . ILE A 89  ? 0.24193 0.23220 0.29888 0.03001  -0.00997 0.01015  96  ILE A N   
642  C CA  . ILE A 89  ? 0.25428 0.25032 0.30925 0.03126  -0.00838 0.01742  96  ILE A CA  
643  C C   . ILE A 89  ? 0.26738 0.26622 0.31123 0.02695  -0.01128 0.01177  96  ILE A C   
644  O O   . ILE A 89  ? 0.26078 0.26932 0.29845 0.02877  -0.01121 0.01680  96  ILE A O   
645  C CB  . ILE A 89  ? 0.24375 0.22837 0.30931 0.03352  -0.00245 0.02288  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.32241 0.31597 0.38838 0.03708  0.00089  0.03496  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.22185 0.19409 0.28987 0.02809  -0.00243 0.01384  96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.34070 0.32331 0.42015 0.04031  0.00755  0.04432  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.22816 0.21907 0.26816 0.02263  -0.01332 0.00186  97  GLY A N   
650  C CA  . GLY A 90  ? 0.22698 0.21767 0.25588 0.02042  -0.01486 -0.00329 97  GLY A CA  
651  C C   . GLY A 90  ? 0.23685 0.22492 0.26864 0.02215  -0.01051 -0.00060 97  GLY A C   
652  O O   . GLY A 90  ? 0.26964 0.25505 0.31310 0.02311  -0.00688 0.00487  97  GLY A O   
653  N N   . MET A 91  ? 0.24525 0.23363 0.26658 0.02242  -0.01066 -0.00449 98  MET A N   
654  C CA  . MET A 91  ? 0.25064 0.23995 0.27452 0.02454  -0.00628 -0.00159 98  MET A CA  
655  C C   . MET A 91  ? 0.26183 0.25917 0.27202 0.02895  -0.00523 0.00037  98  MET A C   
656  O O   . MET A 91  ? 0.27743 0.27327 0.27297 0.02879  -0.00885 -0.00652 98  MET A O   
657  C CB  . MET A 91  ? 0.28024 0.26240 0.30427 0.02286  -0.00651 -0.00909 98  MET A CB  
658  C CG  . MET A 91  ? 0.28216 0.25907 0.32016 0.01932  -0.00696 -0.01066 98  MET A CG  
659  S SD  . MET A 91  ? 0.30350 0.27748 0.34153 0.01838  -0.00762 -0.01808 98  MET A SD  
660  C CE  . MET A 91  ? 0.32147 0.28863 0.34662 0.01823  -0.01127 -0.02508 98  MET A CE  
661  N N   . THR A 92  ? 0.27052 0.27624 0.28536 0.03273  -0.00014 0.00969  99  THR A N   
662  C CA  . THR A 92  ? 0.29681 0.31162 0.29759 0.03891  0.00222  0.01161  99  THR A CA  
663  C C   . THR A 92  ? 0.26847 0.27847 0.26250 0.04105  0.00399  0.00498  99  THR A C   
664  O O   . THR A 92  ? 0.25642 0.25957 0.25957 0.03768  0.00385  0.00156  99  THR A O   
665  C CB  . THR A 92  ? 0.30687 0.33443 0.31662 0.04303  0.00838  0.02617  99  THR A CB  
666  O OG1 . THR A 92  ? 0.29007 0.31579 0.31654 0.04025  0.01240  0.03017  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.34150 0.37276 0.35917 0.04254  0.00781  0.03468  99  THR A CG2 
668  N N   . LYS A 93  ? 0.29176 0.30646 0.26869 0.04801  0.00600  0.00335  100 LYS A N   
669  C CA  . LYS A 93  ? 0.30494 0.31611 0.27487 0.05297  0.00939  -0.00104 100 LYS A CA  
670  C C   . LYS A 93  ? 0.27905 0.29937 0.26783 0.05310  0.01465  0.00829  100 LYS A C   
671  O O   . LYS A 93  ? 0.26936 0.28596 0.26269 0.05270  0.01527  0.00486  100 LYS A O   
672  C CB  . LYS A 93  ? 0.33348 0.34956 0.28190 0.06250  0.01214  -0.00290 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.33799 0.34703 0.27614 0.06952  0.01595  -0.00881 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.35433 0.36765 0.26900 0.08087  0.01954  -0.01124 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.42896 0.43103 0.33112 0.08941  0.02374  -0.01834 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.46992 0.48064 0.35268 0.10328  0.02997  -0.01747 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.29699 0.33044 0.29795 0.05318  0.01837  0.02100  101 ALA A N   
678  C CA  . ALA A 94  ? 0.34086 0.38372 0.36228 0.05087  0.02285  0.03041  101 ALA A CA  
679  C C   . ALA A 94  ? 0.25754 0.29061 0.29500 0.04118  0.01863  0.02564  101 ALA A C   
680  O O   . ALA A 94  ? 0.30462 0.34226 0.35262 0.03908  0.01959  0.02582  101 ALA A O   
681  C CB  . ALA A 94  ? 0.33277 0.38898 0.36562 0.05153  0.02788  0.04600  101 ALA A CB  
682  N N   . ASP A 95  ? 0.27399 0.29559 0.31277 0.03597  0.01386  0.02125  102 ASP A N   
683  C CA  . ASP A 95  ? 0.25145 0.26298 0.30143 0.02845  0.00975  0.01475  102 ASP A CA  
684  C C   . ASP A 95  ? 0.26449 0.27193 0.30700 0.02947  0.00739  0.00487  102 ASP A C   
685  O O   . ASP A 95  ? 0.26425 0.27338 0.31760 0.02574  0.00638  0.00285  102 ASP A O   
686  C CB  . ASP A 95  ? 0.30058 0.30183 0.34890 0.02573  0.00575  0.01133  102 ASP A CB  
687  C CG  . ASP A 95  ? 0.36828 0.37076 0.42809 0.02457  0.00826  0.02161  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.35316 0.35943 0.42767 0.02209  0.01212  0.02972  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.35898 0.35910 0.41377 0.02616  0.00650  0.02236  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.25644 0.25820 0.28017 0.03441  0.00630  -0.00142 103 LEU A N   
691  C CA  . LEU A 96  ? 0.29158 0.28678 0.30803 0.03624  0.00502  -0.00935 103 LEU A CA  
692  C C   . LEU A 96  ? 0.27335 0.27966 0.29497 0.04056  0.00920  -0.00542 103 LEU A C   
693  O O   . LEU A 96  ? 0.27623 0.28404 0.30472 0.03900  0.00786  -0.00796 103 LEU A O   
694  C CB  . LEU A 96  ? 0.28257 0.26775 0.27813 0.04071  0.00422  -0.01593 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.28564 0.26107 0.27695 0.03513  -0.00118 -0.02124 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.27737 0.24398 0.24817 0.03849  -0.00197 -0.02778 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.28005 0.24851 0.27911 0.03006  -0.00444 -0.02557 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.26412 0.28128 0.28261 0.04674  0.01442  0.00165  104 ILE A N   
699  C CA  . ILE A 97  ? 0.28564 0.31722 0.30935 0.05227  0.01925  0.00709  104 ILE A CA  
700  C C   . ILE A 97  ? 0.26723 0.31128 0.31523 0.04383  0.01811  0.01267  104 ILE A C   
701  O O   . ILE A 97  ? 0.26186 0.31578 0.31721 0.04449  0.01822  0.01294  104 ILE A O   
702  C CB  . ILE A 97  ? 0.26240 0.30513 0.27757 0.06151  0.02581  0.01462  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.29936 0.32758 0.28785 0.06985  0.02606  0.00566  104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.26488 0.32856 0.29015 0.06711  0.03181  0.02382  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.34271 0.37988 0.31833 0.07862  0.03109  0.01073  104 ILE A CD1 
706  N N   . ASN A 98  ? 0.27310 0.31618 0.33374 0.03562  0.01660  0.01667  105 ASN A N   
707  C CA  . ASN A 98  ? 0.26270 0.31343 0.34650 0.02569  0.01498  0.02049  105 ASN A CA  
708  C C   . ASN A 98  ? 0.23745 0.27616 0.32407 0.01887  0.00821  0.00960  105 ASN A C   
709  O O   . ASN A 98  ? 0.27234 0.30180 0.36790 0.01127  0.00539  0.00780  105 ASN A O   
710  C CB  . ASN A 98  ? 0.26830 0.31972 0.36424 0.02064  0.01744  0.03018  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.50262 0.57323 0.60410 0.02516  0.02458  0.04396  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.55590 0.64203 0.67577 0.02015  0.02619  0.05095  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.55228 0.62449 0.63734 0.03499  0.02882  0.04799  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.24990 0.28890 0.32780 0.02314  0.00639  0.00286  106 ASN A N   
715  C CA  . ASN A 99  ? 0.25603 0.28866 0.33539 0.01878  0.00067  -0.00645 106 ASN A CA  
716  C C   . ASN A 99  ? 0.26325 0.27794 0.33767 0.01549  -0.00250 -0.01240 106 ASN A C   
717  O O   . ASN A 99  ? 0.27055 0.28054 0.35263 0.00925  -0.00647 -0.01761 106 ASN A O   
718  C CB  . ASN A 99  ? 0.21062 0.25652 0.30925 0.01036  -0.00227 -0.00593 106 ASN A CB  
719  C CG  . ASN A 99  ? 0.22471 0.29326 0.32929 0.01428  0.00068  0.00102  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.24430 0.31711 0.33752 0.02374  0.00236  0.00014  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.27992 0.36331 0.40305 0.00735  0.00168  0.00865  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.23220 0.23789 0.29265 0.02036  -0.00087 -0.01218 107 LEU A N   
723  C CA  . LEU A 100 ? 0.25617 0.24835 0.31099 0.01847  -0.00372 -0.01668 107 LEU A CA  
724  C C   . LEU A 100 ? 0.26672 0.25548 0.33456 0.01251  -0.00451 -0.01446 107 LEU A C   
725  O O   . LEU A 100 ? 0.28303 0.26375 0.35308 0.00975  -0.00753 -0.01994 107 LEU A O   
726  C CB  . LEU A 100 ? 0.24606 0.23232 0.29485 0.01890  -0.00708 -0.02463 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.33889 0.32463 0.37459 0.02554  -0.00521 -0.02576 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.31507 0.31151 0.35471 0.02851  -0.00447 -0.02558 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.47302 0.44648 0.49678 0.02641  -0.00690 -0.03038 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.27168 0.26623 0.34832 0.01132  -0.00102 -0.00570 108 GLY A N   
731  C CA  . GLY A 101 ? 0.29561 0.28404 0.38487 0.00644  -0.00035 -0.00159 108 GLY A CA  
732  C C   . GLY A 101 ? 0.33103 0.31572 0.43475 -0.00141 -0.00301 -0.00638 108 GLY A C   
733  O O   . GLY A 101 ? 0.38768 0.36048 0.49903 -0.00488 -0.00305 -0.00652 108 GLY A O   
734  N N   . THR A 102 ? 0.28080 0.27556 0.38850 -0.00407 -0.00523 -0.01033 109 THR A N   
735  C CA  . THR A 102 ? 0.26222 0.25581 0.38222 -0.01247 -0.00937 -0.01708 109 THR A CA  
736  C C   . THR A 102 ? 0.27071 0.27813 0.40777 -0.01928 -0.00799 -0.00976 109 THR A C   
737  O O   . THR A 102 ? 0.30259 0.32359 0.43980 -0.01523 -0.00354 0.00012  109 THR A O   
738  C CB  . THR A 102 ? 0.26283 0.26130 0.37528 -0.01096 -0.01432 -0.02767 109 THR A CB  
739  O OG1 . THR A 102 ? 0.29955 0.31614 0.41086 -0.00764 -0.01337 -0.02396 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.31038 0.29927 0.40662 -0.00392 -0.01489 -0.03261 109 THR A CG2 
741  N N   . ILE A 103 ? 0.23583 0.24011 0.38738 -0.02981 -0.01175 -0.01471 110 ILE A N   
742  C CA  . ILE A 103 ? 0.22825 0.24933 0.39839 -0.03889 -0.01232 -0.00942 110 ILE A CA  
743  C C   . ILE A 103 ? 0.20895 0.24713 0.37760 -0.03989 -0.01833 -0.01797 110 ILE A C   
744  O O   . ILE A 103 ? 0.21204 0.25478 0.39283 -0.05068 -0.02428 -0.02498 110 ILE A O   
745  C CB  . ILE A 103 ? 0.35549 0.36310 0.54436 -0.05163 -0.01290 -0.00872 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.28686 0.27323 0.47189 -0.05584 -0.01868 -0.02464 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.30290 0.29883 0.49376 -0.04804 -0.00519 0.00436  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.37080 0.34310 0.57505 -0.07030 -0.02045 -0.02688 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.34491 0.18948 0.37585 0.05556  0.01386  0.02043  111 ALA A N   
750  C CA  . ALA A 104 ? 0.29925 0.18195 0.33796 0.06865  0.00175  0.01608  111 ALA A CA  
751  C C   . ALA A 104 ? 0.30376 0.23527 0.40158 0.06809  0.03357  0.01520  111 ALA A C   
752  O O   . ALA A 104 ? 0.25255 0.26774 0.36138 0.05048  0.02528  -0.00585 111 ALA A O   
753  C CB  . ALA A 104 ? 0.35063 0.27188 0.38769 0.07399  -0.01622 0.02979  111 ALA A CB  
754  N N   . LYS A 105 ? 0.28521 0.21284 0.38395 0.05894  0.04920  0.02125  112 LYS A N   
755  C CA  . LYS A 105 ? 0.27716 0.31084 0.40087 0.02421  0.05771  0.00001  112 LYS A CA  
756  C C   . LYS A 105 ? 0.34975 0.39717 0.48681 -0.03239 0.07728  -0.04299 112 LYS A C   
757  O O   . LYS A 105 ? 0.29743 0.43885 0.45159 -0.05453 0.06702  -0.06561 112 LYS A O   
758  C CB  . LYS A 105 ? 0.27028 0.29687 0.39520 0.02348  0.07611  0.01447  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.33738 0.48230 0.49868 -0.01002 0.08522  -0.00484 112 LYS A CG  
760  C CD  . LYS A 105 ? 0.34218 0.46744 0.50586 -0.01873 0.11407  0.00558  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.53082 0.78560 0.74214 -0.05183 0.12218  -0.01407 112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.75496 1.03586 0.98838 -0.11345 0.13566  -0.05548 112 LYS A NZ  
763  N N   . SER A 106 ? 0.32214 0.27182 0.44702 -0.05631 0.10358  -0.05537 113 SER A N   
764  C CA  . SER A 106 ? 0.36158 0.31844 0.49299 -0.10979 0.12162  -0.09631 113 SER A CA  
765  C C   . SER A 106 ? 0.35070 0.31501 0.47598 -0.10578 0.10772  -0.11136 113 SER A C   
766  O O   . SER A 106 ? 0.36943 0.38513 0.50035 -0.14446 0.11064  -0.14422 113 SER A O   
767  C CB  . SER A 106 ? 0.48316 0.32936 0.59775 -0.13721 0.15345  -0.10716 113 SER A CB  
768  O OG  . SER A 106 ? 0.55204 0.32610 0.63432 -0.09043 0.13672  -0.08104 113 SER A OG  
769  N N   . GLY A 107 ? 0.34068 0.25524 0.45360 -0.06098 0.09268  -0.08832 114 GLY A N   
770  C CA  . GLY A 107 ? 0.34264 0.26670 0.45014 -0.05756 0.08350  -0.10223 114 GLY A CA  
771  C C   . GLY A 107 ? 0.30591 0.34440 0.41788 -0.05602 0.05890  -0.10660 114 GLY A C   
772  O O   . GLY A 107 ? 0.30475 0.37453 0.40986 -0.07983 0.05868  -0.13420 114 GLY A O   
773  N N   . THR A 108 ? 0.24320 0.34073 0.36185 -0.02668 0.03706  -0.07965 115 THR A N   
774  C CA  . THR A 108 ? 0.23017 0.43785 0.35189 -0.02410 0.01067  -0.08402 115 THR A CA  
775  C C   . THR A 108 ? 0.26712 0.54777 0.40490 -0.07632 0.01786  -0.12037 115 THR A C   
776  O O   . THR A 108 ? 0.27527 0.61351 0.40575 -0.09179 0.00323  -0.14139 115 THR A O   
777  C CB  . THR A 108 ? 0.18742 0.44023 0.31407 0.01643  -0.01141 -0.04951 115 THR A CB  
778  O OG1 . THR A 108 ? 0.23951 0.41996 0.34686 0.06394  -0.02241 -0.01596 115 THR A OG1 
779  C CG2 . THR A 108 ? 0.19259 0.55825 0.32219 0.01979  -0.04056 -0.05535 115 THR A CG2 
780  N N   . LYS A 109 ? 0.26779 0.54383 0.42524 -0.10444 0.03945  -0.12747 116 LYS A N   
781  C CA  . LYS A 109 ? 0.29994 0.64060 0.47770 -0.15909 0.04775  -0.16222 116 LYS A CA  
782  C C   . LYS A 109 ? 0.34349 0.65267 0.50081 -0.19589 0.05649  -0.19787 116 LYS A C   
783  O O   . LYS A 109 ? 0.35704 0.73713 0.51541 -0.22337 0.04219  -0.22341 116 LYS A O   
784  C CB  . LYS A 109 ? 0.32537 0.64151 0.52289 -0.18426 0.07641  -0.16209 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.52881 0.90053 0.74976 -0.24494 0.08869  -0.19659 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.52084 0.84134 0.74890 -0.26565 0.12118  -0.19233 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.66792 1.03665 0.90689 -0.30328 0.12498  -0.21164 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.64723 1.10851 0.89364 -0.30497 0.09449  -0.22426 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.37110 0.57089 0.50745 -0.19590 0.07912  -0.20050 117 ALA A N   
790  C CA  . ALA A 110 ? 0.41807 0.58086 0.53142 -0.22780 0.09062  -0.23445 117 ALA A CA  
791  C C   . ALA A 110 ? 0.41395 0.61166 0.50671 -0.20756 0.06795  -0.23657 117 ALA A C   
792  O O   . ALA A 110 ? 0.43659 0.65932 0.51061 -0.23529 0.06538  -0.26350 117 ALA A O   
793  C CB  . ALA A 110 ? 0.46820 0.50519 0.56493 -0.22153 0.11816  -0.23198 117 ALA A CB  
794  N N   . PHE A 111 ? 0.38726 0.57730 0.47649 -0.15562 0.05215  -0.20368 118 PHE A N   
795  C CA  . PHE A 111 ? 0.34065 0.55375 0.40586 -0.13555 0.03347  -0.20322 118 PHE A CA  
796  C C   . PHE A 111 ? 0.33764 0.65804 0.39932 -0.15072 0.00553  -0.21659 118 PHE A C   
797  O O   . PHE A 111 ? 0.37166 0.70400 0.40511 -0.16540 0.00071  -0.23624 118 PHE A O   
798  C CB  . PHE A 111 ? 0.29997 0.48889 0.36550 -0.07872 0.01949  -0.16215 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.27690 0.48436 0.31680 -0.05497 0.00122  -0.15628 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.31634 0.49802 0.32995 -0.07440 0.01441  -0.18329 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.30708 0.54714 0.34439 -0.01106 -0.02698 -0.12187 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.30914 0.50172 0.29534 -0.05171 0.00075  -0.17563 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.31418 0.56324 0.32379 0.01147  -0.04302 -0.11367 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.30576 0.53103 0.29073 -0.00926 -0.02801 -0.14011 118 PHE A CZ  
805  N N   . MET A 112 ? 0.33444 0.72699 0.42371 -0.14461 -0.01116 -0.20286 119 MET A N   
806  C CA  . MET A 112 ? 0.41586 0.87685 0.49607 -0.13782 -0.03263 -0.19661 119 MET A CA  
807  C C   . MET A 112 ? 0.50311 0.98199 0.58264 -0.18454 -0.02345 -0.22697 119 MET A C   
808  O O   . MET A 112 ? 0.42486 0.93322 0.48649 -0.18563 -0.03840 -0.23065 119 MET A O   
809  C CB  . MET A 112 ? 0.51089 1.01232 0.61128 -0.10512 -0.04598 -0.16467 119 MET A CB  
810  C CG  . MET A 112 ? 0.25254 0.73181 0.32630 -0.05178 -0.06289 -0.12810 119 MET A CG  
811  S SD  . MET A 112 ? 0.73109 1.23322 0.82081 -0.02713 -0.06780 -0.09985 119 MET A SD  
812  C CE  . MET A 112 ? 0.35954 0.77955 0.42569 0.02125  -0.06838 -0.05800 119 MET A CE  
813  N N   . GLU A 113 ? 0.40539 0.85361 0.50028 -0.22257 0.00178  -0.24707 120 GLU A N   
814  C CA  . GLU A 113 ? 0.47151 0.91833 0.55623 -0.26486 0.01151  -0.27425 120 GLU A CA  
815  C C   . GLU A 113 ? 0.54107 0.93910 0.58416 -0.27131 0.01642  -0.28985 120 GLU A C   
816  O O   . GLU A 113 ? 0.55524 0.97380 0.57934 -0.28896 0.00702  -0.30379 120 GLU A O   
817  C CB  . GLU A 113 ? 0.50196 0.90543 0.60287 -0.29795 0.04096  -0.28606 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.75283 1.20918 0.89412 -0.30032 0.03936  -0.27412 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.86065 1.25554 1.01169 -0.32562 0.07171  -0.27881 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.90602 1.21919 1.02961 -0.34143 0.09313  -0.29221 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.91723 1.33923 1.09928 -0.32529 0.07675  -0.26608 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.49574 0.82386 0.52437 -0.25632 0.03168  -0.28728 121 ALA A N   
823  C CA  . ALA A 114 ? 0.53326 0.80994 0.52327 -0.25767 0.04065  -0.29917 121 ALA A CA  
824  C C   . ALA A 114 ? 0.52695 0.84904 0.49375 -0.23737 0.01322  -0.29071 121 ALA A C   
825  O O   . ALA A 114 ? 0.57836 0.88407 0.51216 -0.25090 0.01409  -0.30484 121 ALA A O   
826  C CB  . ALA A 114 ? 0.51666 0.70995 0.50282 -0.23653 0.06210  -0.29247 121 ALA A CB  
827  N N   . LEU A 115 ? 0.48081 0.85116 0.46088 -0.20206 -0.01078 -0.26437 122 LEU A N   
828  C CA  . LEU A 115 ? 0.46812 0.86125 0.42318 -0.17535 -0.03436 -0.24831 122 LEU A CA  
829  C C   . LEU A 115 ? 0.64570 1.08219 0.59304 -0.19447 -0.05120 -0.25840 122 LEU A C   
830  O O   . LEU A 115 ? 0.60614 1.02783 0.51707 -0.19595 -0.05962 -0.26420 122 LEU A O   
831  C CB  . LEU A 115 ? 0.40507 0.82403 0.37603 -0.12985 -0.05278 -0.21177 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.36243 0.73521 0.33126 -0.10174 -0.04510 -0.19686 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.41551 0.80452 0.39836 -0.05668 -0.06258 -0.15588 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.44138 0.76654 0.37118 -0.09856 -0.03772 -0.20360 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.54313 1.02945 0.52306 -0.20923 -0.05671 -0.26121 123 GLN A N   
836  C CA  . GLN A 116 ? 0.58754 1.11349 0.56294 -0.22761 -0.07513 -0.27247 123 GLN A CA  
837  C C   . GLN A 116 ? 0.72152 1.21624 0.67577 -0.27256 -0.06131 -0.30525 123 GLN A C   
838  O O   . GLN A 116 ? 0.77380 1.29088 0.71670 -0.29146 -0.07819 -0.31824 123 GLN A O   
839  C CB  . GLN A 116 ? 0.62168 1.21260 0.64110 -0.22597 -0.08595 -0.26355 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.53642 1.13135 0.59166 -0.24591 -0.06396 -0.26978 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.84738 1.43556 0.90601 -0.29753 -0.05053 -0.30057 123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.01690 1.57801 1.04322 -0.31871 -0.05140 -0.31947 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.86670 1.47021 0.96116 -0.31734 -0.03612 -0.30410 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.74385 1.11233 0.85541 -0.14072 -0.03365 -0.30693 124 ALA A N   
845  C CA  . ALA A 117 ? 0.72191 1.07787 0.84203 -0.15331 -0.03044 -0.33327 124 ALA A CA  
846  C C   . ALA A 117 ? 0.90638 1.24727 1.00380 -0.14302 -0.02807 -0.33645 124 ALA A C   
847  O O   . ALA A 117 ? 0.74654 1.05267 0.85000 -0.15068 -0.02017 -0.34929 124 ALA A O   
848  C CB  . ALA A 117 ? 0.65920 0.96992 0.80523 -0.17078 -0.01925 -0.33535 124 ALA A CB  
849  N N   . GLY A 118 ? 0.80151 1.16730 0.87305 -0.12480 -0.03421 -0.32314 125 GLY A N   
850  C CA  . GLY A 118 ? 0.67940 1.04428 0.72715 -0.11384 -0.03373 -0.32682 125 GLY A CA  
851  C C   . GLY A 118 ? 0.76502 1.09979 0.79605 -0.10122 -0.02773 -0.30208 125 GLY A C   
852  O O   . GLY A 118 ? 0.65617 1.00582 0.66248 -0.08697 -0.03011 -0.29590 125 GLY A O   
853  N N   . ALA A 119 ? 0.56469 0.85869 0.60846 -0.10616 -0.01976 -0.28776 126 ALA A N   
854  C CA  . ALA A 119 ? 0.43074 0.69096 0.46232 -0.09693 -0.01292 -0.26859 126 ALA A CA  
855  C C   . ALA A 119 ? 0.50218 0.78712 0.51227 -0.08037 -0.01922 -0.24742 126 ALA A C   
856  O O   . ALA A 119 ? 0.47579 0.79998 0.48316 -0.07533 -0.02829 -0.24329 126 ALA A O   
857  C CB  . ALA A 119 ? 0.55146 0.76974 0.60167 -0.10494 -0.00458 -0.25634 126 ALA A CB  
858  N N   . ASP A 120 ? 0.42037 0.68102 0.41627 -0.07127 -0.01379 -0.23271 127 ASP A N   
859  C CA  . ASP A 120 ? 0.38695 0.66178 0.36462 -0.05639 -0.01772 -0.20957 127 ASP A CA  
860  C C   . ASP A 120 ? 0.37450 0.61151 0.35674 -0.05625 -0.01130 -0.19242 127 ASP A C   
861  O O   . ASP A 120 ? 0.39239 0.59233 0.38954 -0.06574 -0.00330 -0.19682 127 ASP A O   
862  C CB  . ASP A 120 ? 0.46586 0.75706 0.41650 -0.04273 -0.01779 -0.20632 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.54433 0.80071 0.49034 -0.04339 -0.00705 -0.21120 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.63774 0.88211 0.59318 -0.05228 -0.00327 -0.23267 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.44218 0.68123 0.37764 -0.03508 -0.00166 -0.19312 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.34417 0.59135 0.31340 -0.04421 -0.01489 -0.17150 128 ILE A N   
867  C CA  . ILE A 121 ? 0.31932 0.53596 0.29239 -0.04379 -0.01040 -0.15648 128 ILE A CA  
868  C C   . ILE A 121 ? 0.43072 0.60866 0.40221 -0.04545 0.00057  -0.15789 128 ILE A C   
869  O O   . ILE A 121 ? 0.39574 0.54188 0.37865 -0.04996 0.00585  -0.15184 128 ILE A O   
870  C CB  . ILE A 121 ? 0.35599 0.59164 0.31302 -0.02846 -0.01604 -0.13395 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.47397 0.73789 0.44335 -0.02820 -0.02538 -0.13142 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.38590 0.58525 0.34429 -0.02450 -0.00912 -0.11487 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.43432 0.72533 0.38973 -0.00960 -0.03247 -0.10959 128 ILE A CD1 
874  N N   . SER A 122 ? 0.40856 0.58920 0.36782 -0.04133 0.00458  -0.16591 129 SER A N   
875  C CA  . SER A 122 ? 0.40258 0.54876 0.36235 -0.04041 0.01586  -0.16576 129 SER A CA  
876  C C   . SER A 122 ? 0.41150 0.52303 0.39530 -0.05229 0.02144  -0.17594 129 SER A C   
877  O O   . SER A 122 ? 0.41928 0.49920 0.40846 -0.05047 0.03028  -0.17158 129 SER A O   
878  C CB  . SER A 122 ? 0.36593 0.52467 0.30813 -0.03240 0.01993  -0.17230 129 SER A CB  
879  O OG  . SER A 122 ? 0.43138 0.59089 0.38176 -0.04007 0.01958  -0.19487 129 SER A OG  
880  N N   . MET A 123 ? 0.37261 0.49000 0.37176 -0.06312 0.01757  -0.18712 130 MET A N   
881  C CA  . MET A 123 ? 0.34933 0.43331 0.37000 -0.07299 0.02456  -0.19262 130 MET A CA  
882  C C   . MET A 123 ? 0.31598 0.37974 0.35088 -0.07740 0.02623  -0.17681 130 MET A C   
883  O O   . MET A 123 ? 0.35729 0.39566 0.40902 -0.08462 0.03209  -0.17690 130 MET A O   
884  C CB  . MET A 123 ? 0.41254 0.50974 0.44368 -0.08318 0.02228  -0.21317 130 MET A CB  
885  C CG  . MET A 123 ? 0.43703 0.55228 0.45338 -0.07827 0.02122  -0.23014 130 MET A CG  
886  S SD  . MET A 123 ? 0.55926 0.71226 0.58036 -0.08737 0.01292  -0.25430 130 MET A SD  
887  C CE  . MET A 123 ? 0.51805 0.62621 0.56752 -0.10160 0.02286  -0.26433 130 MET A CE  
888  N N   . ILE A 124 ? 0.27729 0.35028 0.30431 -0.07185 0.02197  -0.16229 131 ILE A N   
889  C CA  . ILE A 124 ? 0.26786 0.32885 0.30619 -0.07532 0.02217  -0.14850 131 ILE A CA  
890  C C   . ILE A 124 ? 0.31528 0.33554 0.36479 -0.07615 0.03141  -0.13848 131 ILE A C   
891  O O   . ILE A 124 ? 0.28738 0.29624 0.34933 -0.08173 0.03381  -0.13089 131 ILE A O   
892  C CB  . ILE A 124 ? 0.30169 0.37775 0.32720 -0.06702 0.01610  -0.13647 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.28464 0.35517 0.32191 -0.06978 0.01503  -0.12333 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.30524 0.36338 0.31900 -0.05541 0.02095  -0.12445 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.34049 0.42472 0.36756 -0.05614 0.00926  -0.10463 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.32023 0.32128 0.36506 -0.06923 0.03682  -0.13689 132 GLY A N   
897  C CA  . GLY A 125 ? 0.34056 0.30836 0.39506 -0.06654 0.04387  -0.12409 132 GLY A CA  
898  C C   . GLY A 125 ? 0.36697 0.31757 0.43550 -0.07328 0.04929  -0.12949 132 GLY A C   
899  O O   . GLY A 125 ? 0.41735 0.34456 0.49399 -0.07175 0.05399  -0.11622 132 GLY A O   
900  N N   . GLN A 126 ? 0.36385 0.32694 0.43528 -0.08070 0.04836  -0.14859 133 GLN A N   
901  C CA  . GLN A 126 ? 0.40689 0.35334 0.49393 -0.08935 0.05363  -0.15589 133 GLN A CA  
902  C C   . GLN A 126 ? 0.39895 0.34576 0.49723 -0.09831 0.05361  -0.14760 133 GLN A C   
903  O O   . GLN A 126 ? 0.42203 0.35044 0.53473 -0.10573 0.05947  -0.14877 133 GLN A O   
904  C CB  . GLN A 126 ? 0.41104 0.37352 0.49883 -0.09571 0.05175  -0.18077 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.46675 0.43281 0.54128 -0.08655 0.05231  -0.19060 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.58845 0.57062 0.66257 -0.09228 0.05039  -0.21609 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.60332 0.57775 0.69298 -0.10321 0.05243  -0.22789 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.61193 0.61811 0.66784 -0.08509 0.04653  -0.22522 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.32977 0.29712 0.42225 -0.09767 0.04778  -0.13945 134 PHE A N   
910  C CA  . PHE A 127 ? 0.33177 0.30417 0.43418 -0.10533 0.04803  -0.13151 134 PHE A CA  
911  C C   . PHE A 127 ? 0.34134 0.30184 0.43951 -0.09844 0.04956  -0.10937 134 PHE A C   
912  O O   . PHE A 127 ? 0.38050 0.34889 0.48449 -0.10329 0.04991  -0.10137 134 PHE A O   
913  C CB  . PHE A 127 ? 0.31234 0.32401 0.41420 -0.11061 0.03974  -0.14264 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.33297 0.36149 0.43691 -0.11625 0.03676  -0.16530 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.37747 0.42430 0.46595 -0.10883 0.03110  -0.17470 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.45225 0.47740 0.57346 -0.12901 0.04016  -0.17723 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.37392 0.43879 0.46218 -0.11292 0.02809  -0.19579 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.48525 0.52623 0.60874 -0.13452 0.03708  -0.20046 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.44753 0.50963 0.55340 -0.12580 0.03074  -0.20997 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.31768 0.26137 0.40690 -0.08744 0.05075  -0.09989 135 GLY A N   
921  C CA  . GLY A 128 ? 0.31588 0.24696 0.40253 -0.08126 0.05243  -0.07997 135 GLY A CA  
922  C C   . GLY A 128 ? 0.33720 0.28673 0.41583 -0.07807 0.04650  -0.07392 135 GLY A C   
923  O O   . GLY A 128 ? 0.36190 0.30425 0.43875 -0.07421 0.04783  -0.05916 135 GLY A O   
924  N N   . VAL A 129 ? 0.26333 0.23734 0.33673 -0.07890 0.03994  -0.08523 136 VAL A N   
925  C CA  . VAL A 129 ? 0.24572 0.23822 0.31323 -0.07557 0.03390  -0.08103 136 VAL A CA  
926  C C   . VAL A 129 ? 0.27570 0.27474 0.32982 -0.06587 0.02861  -0.08268 136 VAL A C   
927  O O   . VAL A 129 ? 0.25592 0.27639 0.30193 -0.05869 0.02172  -0.07851 136 VAL A O   
928  C CB  . VAL A 129 ? 0.23122 0.25504 0.30616 -0.08318 0.03004  -0.08833 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.27770 0.29567 0.36494 -0.09061 0.03683  -0.08117 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.26537 0.30823 0.34140 -0.08787 0.02646  -0.10508 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.25746 0.23694 0.30890 -0.06213 0.03272  -0.08374 137 GLY A N   
932  C CA  . GLY A 130 ? 0.24920 0.23578 0.28836 -0.05197 0.02991  -0.08142 137 GLY A CA  
933  C C   . GLY A 130 ? 0.25273 0.24101 0.28591 -0.04176 0.02563  -0.06434 137 GLY A C   
934  O O   . GLY A 130 ? 0.25946 0.25931 0.28381 -0.03486 0.02296  -0.06071 137 GLY A O   
935  N N   . PHE A 131 ? 0.22863 0.20551 0.26643 -0.04070 0.02552  -0.05397 138 PHE A N   
936  C CA  . PHE A 131 ? 0.25172 0.22915 0.28546 -0.03218 0.02103  -0.04202 138 PHE A CA  
937  C C   . PHE A 131 ? 0.22407 0.22176 0.25184 -0.02797 0.01567  -0.04129 138 PHE A C   
938  O O   . PHE A 131 ? 0.22213 0.21985 0.24609 -0.02058 0.01347  -0.03358 138 PHE A O   
939  C CB  . PHE A 131 ? 0.26377 0.23328 0.30052 -0.03200 0.02088  -0.03502 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.24590 0.21986 0.27871 -0.02445 0.01529  -0.02851 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.24770 0.21277 0.28091 -0.01901 0.01290  -0.02324 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.24973 0.23772 0.28113 -0.02301 0.01283  -0.02934 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.23315 0.19878 0.26552 -0.01353 0.00805  -0.02027 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.24090 0.22946 0.26984 -0.01497 0.00851  -0.02577 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.25757 0.23295 0.28700 -0.01085 0.00605  -0.02199 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.22860 0.24431 0.25782 -0.03254 0.01397  -0.04855 139 TYR A N   
947  C CA  . TYR A 132 ? 0.23313 0.27035 0.25859 -0.02575 0.00829  -0.04563 139 TYR A CA  
948  C C   . TYR A 132 ? 0.24134 0.29158 0.25722 -0.02012 0.00619  -0.04494 139 TYR A C   
949  O O   . TYR A 132 ? 0.23529 0.29922 0.24680 -0.01077 0.00204  -0.03725 139 TYR A O   
950  C CB  . TYR A 132 ? 0.17894 0.23792 0.21188 -0.03199 0.00677  -0.05360 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.22830 0.27710 0.26874 -0.03567 0.01063  -0.05026 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.21421 0.26402 0.25324 -0.02663 0.00889  -0.04249 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.23737 0.27422 0.28549 -0.04725 0.01707  -0.05438 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.20582 0.24944 0.24770 -0.02847 0.01307  -0.03929 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.25020 0.27885 0.30213 -0.04903 0.02183  -0.04749 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.26221 0.29695 0.30954 -0.03955 0.01961  -0.04033 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.27609 0.30642 0.32381 -0.04055 0.02493  -0.03397 139 TYR A OH  
958  N N   . SER A 133 ? 0.21799 0.26393 0.22993 -0.02382 0.00992  -0.05140 140 SER A N   
959  C CA  . SER A 133 ? 0.22130 0.27966 0.22121 -0.01716 0.01000  -0.04839 140 SER A CA  
960  C C   . SER A 133 ? 0.21750 0.26322 0.21584 -0.00798 0.01155  -0.03035 140 SER A C   
961  O O   . SER A 133 ? 0.24416 0.30165 0.23271 -0.00060 0.01230  -0.02175 140 SER A O   
962  C CB  . SER A 133 ? 0.23902 0.29448 0.23549 -0.02224 0.01549  -0.06086 140 SER A CB  
963  O OG  . SER A 133 ? 0.26386 0.29363 0.26648 -0.02192 0.02174  -0.05538 140 SER A OG  
964  N N   . ALA A 134 ? 0.23438 0.25804 0.24239 -0.00857 0.01225  -0.02446 141 ALA A N   
965  C CA  . ALA A 134 ? 0.22897 0.24102 0.23976 -0.00195 0.01269  -0.01023 141 ALA A CA  
966  C C   . ALA A 134 ? 0.21757 0.24171 0.22338 0.00748  0.00945  -0.00055 141 ALA A C   
967  O O   . ALA A 134 ? 0.23448 0.25259 0.24002 0.01355  0.01220  0.01319  141 ALA A O   
968  C CB  . ALA A 134 ? 0.21495 0.20784 0.23610 -0.00400 0.01107  -0.01004 141 ALA A CB  
969  N N   . TYR A 135 ? 0.21409 0.25592 0.21830 0.00927  0.00425  -0.00627 142 TYR A N   
970  C CA  . TYR A 135 ? 0.23379 0.28838 0.23548 0.02124  0.00061  0.00392  142 TYR A CA  
971  C C   . TYR A 135 ? 0.24055 0.31954 0.22873 0.02785  0.00008  0.01025  142 TYR A C   
972  O O   . TYR A 135 ? 0.26016 0.35178 0.24475 0.04040  -0.00273 0.02239  142 TYR A O   
973  C CB  . TYR A 135 ? 0.20216 0.27083 0.21003 0.02233  -0.00438 -0.00370 142 TYR A CB  
974  C CG  . TYR A 135 ? 0.23293 0.27881 0.25021 0.02049  -0.00308 -0.00567 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.22335 0.25466 0.24536 0.03061  -0.00334 0.00249  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.21504 0.25250 0.23575 0.00921  -0.00106 -0.01553 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.22757 0.24006 0.25596 0.02911  -0.00274 -0.00244 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.22999 0.25046 0.25549 0.00890  -0.00034 -0.01662 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.23410 0.24440 0.26257 0.01849  -0.00173 -0.01187 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.24571 0.24271 0.27700 0.01847  -0.00185 -0.01646 142 TYR A OH  
981  N N   . LEU A 136 ? 0.24333 0.32898 0.22305 0.02158  0.00339  0.00345  143 LEU A N   
982  C CA  . LEU A 136 ? 0.23292 0.33949 0.19659 0.02939  0.00491  0.01221  143 LEU A CA  
983  C C   . LEU A 136 ? 0.23354 0.32311 0.19718 0.03794  0.01141  0.03582  143 LEU A C   
984  O O   . LEU A 136 ? 0.28257 0.38864 0.23406 0.04928  0.01233  0.05157  143 LEU A O   
985  C CB  . LEU A 136 ? 0.26850 0.38238 0.22362 0.02126  0.00923  -0.00201 143 LEU A CB  
986  C CG  . LEU A 136 ? 0.23580 0.36754 0.19110 0.01163  0.00397  -0.02693 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.24699 0.37475 0.19797 0.00381  0.01028  -0.04255 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.25868 0.43183 0.20311 0.01804  -0.00505 -0.03045 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.24847 0.30610 0.22660 0.03204  0.01635  0.03882  144 VAL A N   
990  C CA  . VAL A 137 ? 0.26216 0.30326 0.24463 0.03577  0.02434  0.05885  144 VAL A CA  
991  C C   . VAL A 137 ? 0.24930 0.26072 0.25012 0.03620  0.02356  0.06475  144 VAL A C   
992  O O   . VAL A 137 ? 0.29400 0.28965 0.30199 0.04011  0.02950  0.08251  144 VAL A O   
993  C CB  . VAL A 137 ? 0.25613 0.29198 0.24094 0.02741  0.03293  0.05674  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.26028 0.32567 0.22490 0.02932  0.03544  0.05072  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.24520 0.26330 0.24482 0.01627  0.03120  0.04039  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.27222 0.27696 0.28037 0.03292  0.01700  0.05049  145 ALA A N   
997  C CA  . ALA A 138 ? 0.24992 0.22783 0.27410 0.03248  0.01599  0.05047  145 ALA A CA  
998  C C   . ALA A 138 ? 0.27275 0.25396 0.29737 0.04333  0.01074  0.05068  145 ALA A C   
999  O O   . ALA A 138 ? 0.29528 0.29831 0.31335 0.04457  0.00549  0.04079  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.27861 0.24636 0.31071 0.02136  0.01366  0.03417  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.26685 0.22588 0.30209 0.05081  0.01294  0.06118  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.28264 0.24014 0.32217 0.06241  0.00887  0.05884  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.30974 0.25731 0.35673 0.05655  0.00525  0.03930  146 GLU A C   
1004 O O   . GLU A 139 ? 0.30480 0.26307 0.35175 0.06424  0.00173  0.03205  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.32254 0.25659 0.37161 0.07421  0.01377  0.07709  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.45908 0.35900 0.52383 0.06453  0.01975  0.07951  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.73338 0.60785 0.80861 0.07232  0.02472  0.09332  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.69596 0.58128 0.76298 0.08598  0.02625  0.11073  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.77361 0.62328 0.86151 0.06208  0.02554  0.08304  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.28591 0.21809 0.33870 0.04395  0.00606  0.03089  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.27275 0.19879 0.32928 0.03897  0.00234  0.01350  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.22760 0.15594 0.28273 0.02550  0.00207  0.00768  147 LYS A C   
1013 O O   . LYS A 140 ? 0.25746 0.18039 0.31671 0.02004  0.00567  0.01557  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.29959 0.19783 0.36999 0.04207  0.00264  0.00928  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.26538 0.16173 0.33610 0.03851  -0.00191 -0.01061 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.40997 0.28139 0.49323 0.04453  -0.00180 -0.01817 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.45104 0.30847 0.54052 0.03127  -0.00177 -0.02103 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.60403 0.44138 0.69931 0.03362  -0.00056 -0.02726 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.21506 0.15365 0.26454 0.02138  -0.00098 -0.00389 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.19939 0.13902 0.24839 0.01144  -0.00140 -0.00846 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.25075 0.18537 0.30130 0.01022  -0.00563 -0.01979 148 VAL A C   
1022 O O   . VAL A 141 ? 0.23580 0.17707 0.28061 0.01525  -0.00697 -0.02611 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.24592 0.20287 0.28555 0.00784  0.00007  -0.00930 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.27333 0.22716 0.31439 0.00009  0.00036  -0.01281 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.25706 0.22372 0.29245 0.00971  0.00316  -0.00098 148 VAL A CG2 
1026 N N   . THR A 142 ? 0.23631 0.16285 0.29494 0.00426  -0.00779 -0.02273 149 THR A N   
1027 C CA  . THR A 142 ? 0.24144 0.16870 0.29957 0.00315  -0.01340 -0.03411 149 THR A CA  
1028 C C   . THR A 142 ? 0.26677 0.20342 0.32242 -0.00182 -0.01429 -0.03214 149 THR A C   
1029 O O   . THR A 142 ? 0.27449 0.20996 0.33857 -0.00630 -0.01215 -0.02614 149 THR A O   
1030 C CB  . THR A 142 ? 0.25135 0.16425 0.32448 0.00064  -0.01698 -0.04135 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.31063 0.20884 0.38924 0.00601  -0.01422 -0.04038 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.26714 0.18624 0.33662 0.00073  -0.02459 -0.05679 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.25104 0.19739 0.29572 0.00011  -0.01624 -0.03564 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.23265 0.18580 0.27499 -0.00199 -0.01643 -0.03124 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.24709 0.20805 0.28620 0.00038  -0.02408 -0.03836 150 VAL A C   
1036 O O   . VAL A 143 ? 0.26090 0.22826 0.28784 0.00491  -0.02552 -0.04402 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.22476 0.18273 0.25705 -0.00189 -0.01035 -0.02525 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.25941 0.21968 0.29022 -0.00211 -0.00948 -0.01902 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.22488 0.18059 0.25948 -0.00449 -0.00458 -0.02187 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.21674 0.18129 0.26667 -0.00197 -0.02919 -0.03903 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.21105 0.18938 0.25812 0.00069  -0.03855 -0.04639 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.22398 0.21218 0.26598 0.00460  -0.03776 -0.03460 151 ILE A C   
1043 O O   . ILE A 144 ? 0.24278 0.22642 0.29546 0.00271  -0.03317 -0.02608 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.24785 0.22776 0.31516 -0.00502 -0.04603 -0.05615 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.36848 0.33011 0.44766 -0.01010 -0.04312 -0.06248 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.25919 0.25943 0.32181 -0.00202 -0.05837 -0.06822 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.38767 0.34427 0.45769 -0.00636 -0.04575 -0.07598 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.21903 0.22020 0.24448 0.01129  -0.04085 -0.03281 152 THR A N   
1049 C CA  . THR A 145 ? 0.22058 0.22614 0.24136 0.01655  -0.03766 -0.01740 152 THR A CA  
1050 C C   . THR A 145 ? 0.25628 0.28394 0.26422 0.02519  -0.04647 -0.01641 152 THR A C   
1051 O O   . THR A 145 ? 0.27211 0.31130 0.26663 0.02745  -0.05185 -0.02731 152 THR A O   
1052 C CB  . THR A 145 ? 0.23277 0.22554 0.24444 0.01563  -0.02516 -0.00691 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.25779 0.24632 0.27163 0.01923  -0.02006 0.00790  152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.26196 0.26272 0.25449 0.01858  -0.02300 -0.00830 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.23393 0.26892 0.24518 0.03164  -0.04769 -0.00326 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.24186 0.30148 0.23990 0.04265  -0.05624 0.00249  153 LYS A CA  
1057 C C   . LYS A 146 ? 0.29581 0.34944 0.29107 0.05137  -0.04822 0.02634  153 LYS A C   
1058 O O   . LYS A 146 ? 0.27361 0.31928 0.28713 0.05238  -0.04582 0.03295  153 LYS A O   
1059 C CB  . LYS A 146 ? 0.25292 0.33593 0.26570 0.04321  -0.07163 -0.00956 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.27388 0.38973 0.27444 0.05649  -0.08313 -0.00323 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.28732 0.41925 0.25892 0.06072  -0.08754 -0.01169 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.31222 0.48267 0.26826 0.07484  -0.10056 -0.00665 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.35922 0.53222 0.30271 0.08935  -0.09382 0.02438  153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.28554 0.34216 0.25918 0.05803  -0.04275 0.03956  154 HIS A N   
1065 C CA  . HIS A 147 ? 0.27713 0.32683 0.24610 0.06758  -0.03421 0.06499  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.35762 0.43906 0.31134 0.08334  -0.04514 0.07531  154 HIS A C   
1067 O O   . HIS A 147 ? 0.35782 0.46580 0.29468 0.08563  -0.05549 0.06320  154 HIS A O   
1068 C CB  . HIS A 147 ? 0.32530 0.35743 0.28201 0.06269  -0.01849 0.07505  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.32734 0.34176 0.28500 0.06850  -0.00564 0.10129  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.38844 0.41594 0.32978 0.08281  -0.00484 0.12410  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.35062 0.33341 0.32382 0.06132  0.00806  0.10783  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.47259 0.47347 0.42206 0.08447  0.00947  0.14545  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.38438 0.35740 0.35379 0.07055  0.01737  0.13382  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.29135 0.37168 0.25048 0.09564  -0.04318 0.09709  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.31713 0.43154 0.26010 0.11339  -0.05405 0.11042  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.35071 0.48127 0.25964 0.11810  -0.05156 0.11742  155 ASN A C   
1077 O O   . ASN A 148 ? 0.42851 0.59473 0.32022 0.12671  -0.06400 0.11285  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.35673 0.46169 0.30878 0.12874  -0.04813 0.13928  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.36164 0.46806 0.34437 0.13071  -0.05481 0.13246  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.43310 0.56170 0.42732 0.12434  -0.06848 0.10978  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.37195 0.45304 0.36975 0.13647  -0.04355 0.14836  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.41599 0.52170 0.31732 0.11029  -0.03428 0.12554  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.60342 0.72445 0.47403 0.11560  -0.02760 0.13729  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.74024 0.87499 0.59802 0.10639  -0.03091 0.11030  156 ASP A C   
1085 O O   . ASP A 149 ? 0.62556 0.76886 0.46134 0.10792  -0.02098 0.11789  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.56858 0.65796 0.44137 0.11175  -0.00490 0.16304  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.67328 0.74370 0.56161 0.11873  0.00136  0.18474  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.62324 0.71426 0.51096 0.13088  -0.01072 0.18660  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.71826 0.75400 0.62050 0.11140  0.01848  0.19778  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.51603 0.65330 0.38785 0.09780  -0.04331 0.08025  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.45670 0.59931 0.32113 0.08957  -0.04481 0.05429  157 ASP A CA  
1092 C C   . ASP A 150 ? 0.50245 0.65578 0.38031 0.08502  -0.06277 0.02421  157 ASP A C   
1093 O O   . ASP A 150 ? 0.43684 0.59576 0.33129 0.08660  -0.07336 0.02362  157 ASP A O   
1094 C CB  . ASP A 150 ? 0.46313 0.57395 0.34051 0.07613  -0.02875 0.05396  157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.52963 0.65055 0.39033 0.07417  -0.02247 0.04245  157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.53507 0.68264 0.37779 0.08101  -0.03262 0.02597  157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.44873 0.55263 0.31660 0.06557  -0.00807 0.04672  157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.38858 0.54476 0.26158 0.07928  -0.06519 -0.00091 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.41897 0.57821 0.30737 0.07221  -0.07906 -0.03096 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.32109 0.44601 0.23958 0.05854  -0.07342 -0.03598 158 GLU A C   
1101 O O   . GLU A 151 ? 0.36503 0.46670 0.28915 0.05456  -0.05973 -0.02099 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.47845 0.65193 0.34832 0.07386  -0.08221 -0.05555 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.67739 0.88235 0.51668 0.08651  -0.08228 -0.04815 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.89841 1.12711 0.74158 0.09023  -0.09627 -0.05167 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.97618 1.21865 0.81030 0.09986  -0.09564 -0.02681 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.06846 1.30087 0.92574 0.08326  -0.10700 -0.07888 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.31925 0.44244 0.25666 0.05083  -0.08375 -0.05856 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.26685 0.36027 0.23062 0.03890  -0.07824 -0.06259 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.30781 0.38357 0.26740 0.03539  -0.06995 -0.07318 159 GLN A C   
1110 O O   . GLN A 152 ? 0.31803 0.40251 0.26811 0.03763  -0.07507 -0.09336 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.26838 0.36640 0.25714 0.03127  -0.09057 -0.07955 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.28031 0.35059 0.29687 0.02008  -0.08345 -0.07698 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.32724 0.40742 0.37147 0.01302  -0.09319 -0.08505 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.35178 0.45442 0.39966 0.01816  -0.10001 -0.07739 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.31605 0.38027 0.38198 0.00162  -0.09302 -0.09884 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.24676 0.29995 0.21393 0.03094  -0.05763 -0.06090 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.26328 0.30345 0.22802 0.02956  -0.04933 -0.06720 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.30633 0.32237 0.29378 0.02118  -0.04594 -0.06819 160 TYR A C   
1119 O O   . TYR A 153 ? 0.27259 0.28081 0.27369 0.01630  -0.04467 -0.05763 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.29021 0.33284 0.24043 0.03284  -0.03680 -0.05034 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.35811 0.42494 0.28311 0.04211  -0.03693 -0.04898 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.37315 0.45075 0.28535 0.04730  -0.03655 -0.06506 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.38393 0.46382 0.29738 0.04737  -0.03708 -0.03107 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.42928 0.53404 0.31452 0.05718  -0.03593 -0.06456 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.43191 0.53749 0.31888 0.05745  -0.03677 -0.02717 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.50974 0.62897 0.38180 0.06186  -0.03613 -0.04445 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.67694 0.82529 0.51987 0.07275  -0.03460 -0.04081 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.27643 0.28178 0.26675 0.02129  -0.04317 -0.07929 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.25284 0.23719 0.26014 0.01630  -0.03802 -0.07639 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.25037 0.23395 0.25058 0.02011  -0.02857 -0.07079 161 ALA A C   
1131 O O   . ALA A 154 ? 0.27232 0.26280 0.26308 0.02691  -0.02730 -0.08041 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.31375 0.28450 0.33586 0.01408  -0.04326 -0.09286 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.23955 0.21776 0.24531 0.01598  -0.02232 -0.05728 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.21244 0.19173 0.21807 0.01747  -0.01491 -0.05271 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.29218 0.25701 0.31126 0.01721  -0.01490 -0.05294 162 TRP A C   
1136 O O   . TRP A 155 ? 0.24604 0.19969 0.27518 0.01236  -0.01712 -0.05012 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.22970 0.21369 0.23360 0.01196  -0.00895 -0.03965 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.19659 0.18655 0.20318 0.01012  -0.00226 -0.03538 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.20221 0.20699 0.20361 0.00958  0.00417  -0.03244 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.24664 0.23261 0.26220 0.00800  -0.00133 -0.03329 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.21535 0.22636 0.22476 0.00608  0.00782  -0.03089 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.21956 0.22036 0.23570 0.00601  0.00391  -0.03149 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.22607 0.20011 0.24920 0.00750  -0.00395 -0.03190 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.22667 0.23332 0.24930 0.00428  0.00455  -0.03028 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.22999 0.20873 0.25673 0.00708  -0.00175 -0.02798 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.24262 0.23879 0.26831 0.00601  0.00137  -0.02834 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.23444 0.20105 0.25460 0.02354  -0.01180 -0.05480 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.23040 0.18431 0.26175 0.02561  -0.01113 -0.05074 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.24357 0.21020 0.27439 0.03212  -0.00701 -0.04626 163 GLU A C   
1150 O O   . GLU A 156 ? 0.23508 0.21640 0.26095 0.03783  -0.00488 -0.05165 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.28299 0.21884 0.32275 0.03003  -0.01434 -0.06087 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.32543 0.24195 0.37916 0.03106  -0.01264 -0.05309 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.42091 0.31535 0.48689 0.03068  -0.01523 -0.06390 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.43569 0.32782 0.49898 0.03808  -0.01512 -0.07493 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.45577 0.34269 0.52997 0.02046  -0.01567 -0.05880 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.23392 0.19903 0.27003 0.03218  -0.00583 -0.03641 164 SER A N   
1157 C CA  . SER A 157 ? 0.23088 0.21275 0.26811 0.04007  -0.00395 -0.03259 164 SER A CA  
1158 C C   . SER A 157 ? 0.21678 0.19120 0.25913 0.04456  -0.00411 -0.02150 164 SER A C   
1159 O O   . SER A 157 ? 0.21658 0.18473 0.25818 0.03703  -0.00374 -0.01483 164 SER A O   
1160 C CB  . SER A 157 ? 0.21463 0.22089 0.24783 0.03306  -0.00187 -0.03150 164 SER A CB  
1161 O OG  . SER A 157 ? 0.21547 0.24252 0.25296 0.04103  -0.00164 -0.02932 164 SER A OG  
1162 N N   . SER A 158 ? 0.24549 0.22302 0.29257 0.05817  -0.00381 -0.01817 165 SER A N   
1163 C CA  . SER A 158 ? 0.25416 0.23393 0.30336 0.06602  -0.00361 -0.00379 165 SER A CA  
1164 C C   . SER A 158 ? 0.24159 0.25730 0.28785 0.07034  -0.00539 -0.00153 165 SER A C   
1165 O O   . SER A 158 ? 0.28094 0.30710 0.32906 0.08315  -0.00653 0.00920  165 SER A O   
1166 C CB  . SER A 158 ? 0.28714 0.24430 0.34594 0.08038  -0.00201 0.00099  165 SER A CB  
1167 O OG  . SER A 158 ? 0.34990 0.27464 0.41480 0.07270  -0.00083 -0.00341 165 SER A OG  
1168 N N   . ALA A 159 ? 0.22106 0.25662 0.26426 0.05981  -0.00560 -0.01076 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.24415 0.31767 0.28937 0.06004  -0.00730 -0.01293 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.26139 0.34879 0.31510 0.07595  -0.00709 -0.01435 166 ALA A C   
1171 O O   . ALA A 159 ? 0.29324 0.36459 0.34883 0.08060  -0.00415 -0.02063 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.28258 0.37233 0.32298 0.05924  -0.01069 -0.00526 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.24681 0.36672 0.30604 0.08509  -0.01026 -0.01044 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.26327 0.40023 0.33310 0.10144  -0.00937 -0.01224 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.26752 0.42265 0.34283 0.09469  -0.00482 -0.02484 167 GLY A C   
1176 O O   . GLY A 160 ? 0.28436 0.44990 0.36785 0.10871  -0.00186 -0.02861 167 GLY A O   
1177 N N   . GLY A 161 ? 0.20974 0.36913 0.28140 0.07469  -0.00294 -0.03043 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.19314 0.37467 0.27111 0.06675  0.00292  -0.03846 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.18311 0.34112 0.25203 0.06314  0.00911  -0.04332 168 GLY A C   
1180 O O   . GLY A 161 ? 0.20565 0.38220 0.27760 0.05681  0.01569  -0.04722 168 GLY A O   
1181 N N   . SER A 162 ? 0.19607 0.31743 0.25479 0.06696  0.00738  -0.04304 169 SER A N   
1182 C CA  . SER A 162 ? 0.19611 0.30202 0.24539 0.06531  0.01145  -0.04977 169 SER A CA  
1183 C C   . SER A 162 ? 0.22591 0.29814 0.26572 0.05720  0.00782  -0.04818 169 SER A C   
1184 O O   . SER A 162 ? 0.23659 0.29328 0.27802 0.05656  0.00350  -0.04231 169 SER A O   
1185 C CB  . SER A 162 ? 0.25240 0.35437 0.30255 0.08340  0.01337  -0.05811 169 SER A CB  
1186 O OG  . SER A 162 ? 0.27705 0.34982 0.32967 0.09316  0.00866  -0.05663 169 SER A OG  
1187 N N   . PHE A 163 ? 0.22069 0.28586 0.25069 0.05190  0.01008  -0.05268 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.19762 0.23609 0.22010 0.04575  0.00612  -0.05308 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.23661 0.27161 0.24929 0.05136  0.00642  -0.06372 170 PHE A C   
1190 O O   . PHE A 163 ? 0.24506 0.29953 0.25335 0.05755  0.01156  -0.06889 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.22223 0.25932 0.24156 0.03069  0.00697  -0.04538 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.19276 0.24680 0.20688 0.02464  0.01365  -0.04318 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.22299 0.29939 0.24550 0.01876  0.01945  -0.03976 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.21771 0.26641 0.21965 0.02415  0.01419  -0.04342 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.22627 0.31620 0.24668 0.01156  0.02802  -0.03514 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.22325 0.28608 0.21908 0.01994  0.02167  -0.03748 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.22804 0.30935 0.23382 0.01270  0.02982  -0.03207 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.23268 0.24563 0.24234 0.04936  0.00079  -0.06832 171 THR A N   
1199 C CA  . THR A 164 ? 0.24340 0.25560 0.24242 0.05352  -0.00120 -0.08118 171 THR A CA  
1200 C C   . THR A 164 ? 0.24716 0.25847 0.23686 0.04423  -0.00464 -0.07732 171 THR A C   
1201 O O   . THR A 164 ? 0.24013 0.24039 0.23589 0.03563  -0.00719 -0.06838 171 THR A O   
1202 C CB  . THR A 164 ? 0.24456 0.23446 0.25050 0.06064  -0.00614 -0.09554 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.30506 0.27258 0.32126 0.05226  -0.01120 -0.09042 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.27910 0.26771 0.29500 0.07419  -0.00202 -0.09886 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.23828 0.26272 0.21271 0.04800  -0.00489 -0.08465 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.25519 0.28144 0.21956 0.04315  -0.01017 -0.08221 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.31296 0.34293 0.26746 0.04988  -0.01718 -0.10196 172 VAL A C   
1208 O O   . VAL A 165 ? 0.29402 0.33702 0.23827 0.05925  -0.01362 -0.11345 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.26528 0.31000 0.21690 0.04079  -0.00305 -0.06682 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.31651 0.36439 0.25702 0.03954  -0.00954 -0.06241 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.27609 0.31588 0.24009 0.03210  0.00351  -0.05151 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.30267 0.32501 0.26039 0.04512  -0.02717 -0.10740 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.32003 0.35023 0.26875 0.04934  -0.03602 -0.12853 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.30964 0.34972 0.25477 0.04440  -0.04537 -0.12415 173 ARG A C   
1215 O O   . ARG A 166 ? 0.29503 0.32702 0.25133 0.03727  -0.04511 -0.10757 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.35615 0.36349 0.32394 0.04805  -0.03970 -0.14570 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.38662 0.37218 0.37782 0.03695  -0.04467 -0.14129 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.44767 0.40740 0.45941 0.03499  -0.04122 -0.14388 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.60679 0.55812 0.62034 0.04186  -0.03224 -0.13463 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.67497 0.60738 0.70065 0.04541  -0.02750 -0.13417 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.63845 0.55478 0.67450 0.04237  -0.02930 -0.14378 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.67118 0.60203 0.69866 0.05306  -0.02071 -0.12412 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.34629 0.40707 0.27522 0.04963  -0.05369 -0.13958 174 THR A N   
1224 C CA  . THR A 167 ? 0.35937 0.43270 0.28895 0.04611  -0.06577 -0.13976 174 THR A CA  
1225 C C   . THR A 167 ? 0.45094 0.50260 0.41131 0.03509  -0.07193 -0.14901 174 THR A C   
1226 O O   . THR A 167 ? 0.45535 0.48933 0.42969 0.03245  -0.06919 -0.16051 174 THR A O   
1227 C CB  . THR A 167 ? 0.45192 0.55286 0.36278 0.05293  -0.07055 -0.14838 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.47713 0.59810 0.36055 0.06253  -0.06197 -0.13362 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.51074 0.62810 0.42494 0.05026  -0.08316 -0.14708 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.34422 0.39710 0.31722 0.02872  -0.07797 -0.13959 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.38703 0.42173 0.39086 0.01729  -0.08119 -0.14459 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.45828 0.51077 0.46924 0.01366  -0.09158 -0.15720 175 ASP A C   
1233 O O   . ASP A 168 ? 0.49368 0.57283 0.49665 0.01680  -0.10014 -0.15301 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.36673 0.39350 0.38441 0.01204  -0.07729 -0.12308 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.50761 0.51645 0.55694 0.00035  -0.07845 -0.12711 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.63206 0.62027 0.69123 -0.00278 -0.07224 -0.13202 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.41239 0.42959 0.47609 -0.00446 -0.08144 -0.11838 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.55275 0.59104 0.57910 0.00770  -0.09072 -0.17142 176 THR A N   
1239 C CA  . THR A 169 ? 0.80684 0.85726 0.84550 0.00129  -0.09980 -0.18657 176 THR A CA  
1240 C C   . THR A 169 ? 0.67950 0.71933 0.74996 -0.01172 -0.10041 -0.18171 176 THR A C   
1241 O O   . THR A 169 ? 0.69310 0.74232 0.77854 -0.01929 -0.10737 -0.19417 176 THR A O   
1242 C CB  . THR A 169 ? 0.77875 0.81827 0.81703 0.00171  -0.09799 -0.20629 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.79304 0.79919 0.84083 0.00085  -0.08666 -0.20089 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.59415 0.65656 0.60129 0.01438  -0.09976 -0.21437 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.64893 0.67109 0.72993 -0.01455 -0.09261 -0.16416 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.68713 0.70163 0.79645 -0.02563 -0.09048 -0.15588 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.52802 0.57291 0.64545 -0.02776 -0.10061 -0.15406 177 GLY A C   
1248 O O   . GLY A 170 ? 0.51054 0.58390 0.61179 -0.02071 -0.11083 -0.15970 177 GLY A O   
1249 N N   . GLU A 171 ? 0.46010 0.50072 0.60301 -0.03658 -0.09682 -0.14422 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.43208 0.50210 0.58882 -0.03857 -0.10496 -0.14070 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.41448 0.50592 0.55304 -0.02591 -0.11079 -0.12999 178 GLU A C   
1252 O O   . GLU A 171 ? 0.34525 0.42231 0.47738 -0.02155 -0.10398 -0.11699 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.46585 0.52483 0.65172 -0.04872 -0.09570 -0.12877 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.35701 0.44741 0.56314 -0.05231 -0.10311 -0.12785 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.44170 0.54609 0.66122 -0.06166 -0.11148 -0.14601 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.46237 0.54479 0.68805 -0.07009 -0.10732 -0.15651 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.47299 0.61255 0.69413 -0.05861 -0.12369 -0.15033 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.41374 0.53930 0.54269 -0.01884 -0.12305 -0.13356 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.40581 0.55067 0.51509 -0.00372 -0.12725 -0.11843 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.40772 0.55301 0.53684 -0.00193 -0.12229 -0.09870 179 PRO A C   
1261 O O   . PRO A 172 ? 0.42476 0.58092 0.58371 -0.00926 -0.12355 -0.09886 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.41254 0.59414 0.51005 0.00331  -0.13984 -0.12366 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.51414 0.69224 0.61643 -0.00717 -0.14282 -0.14710 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.52746 0.67077 0.65327 -0.02144 -0.13246 -0.15242 179 PRO A CD  
1265 N N   . MET A 173 ? 0.33045 0.46020 0.43777 0.00848  -0.11076 -0.07733 180 MET A N   
1266 C CA  . MET A 173 ? 0.30383 0.42010 0.42292 0.01015  -0.09842 -0.05739 180 MET A CA  
1267 C C   . MET A 173 ? 0.50891 0.64718 0.62725 0.02433  -0.10132 -0.04060 180 MET A C   
1268 O O   . MET A 173 ? 0.49862 0.63169 0.63375 0.02605  -0.09315 -0.02847 180 MET A O   
1269 C CB  . MET A 173 ? 0.30045 0.38384 0.39980 0.01176  -0.08313 -0.04587 180 MET A CB  
1270 C CG  . MET A 173 ? 0.50597 0.56310 0.61506 -0.00000 -0.07445 -0.05202 180 MET A CG  
1271 S SD  . MET A 173 ? 0.48133 0.51299 0.56371 0.00482  -0.06086 -0.04000 180 MET A SD  
1272 C CE  . MET A 173 ? 0.41791 0.45023 0.50319 0.01258  -0.05342 -0.02039 180 MET A CE  
1273 N N   . GLY A 174 ? 0.29952 0.45933 0.39610 0.03655  -0.11043 -0.03719 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.28794 0.46704 0.38445 0.05270  -0.11254 -0.01755 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.28865 0.44125 0.36182 0.06254  -0.09809 0.00465  181 GLY A C   
1276 O O   . GLY A 174 ? 0.32366 0.48597 0.37118 0.07456  -0.10031 0.01578  181 GLY A O   
1277 N N   . ARG A 175 ? 0.22779 0.34738 0.30969 0.05628  -0.08271 0.01023  182 ARG A N   
1278 C CA  . ARG A 175 ? 0.25213 0.34240 0.31751 0.06067  -0.06773 0.02666  182 ARG A CA  
1279 C C   . ARG A 175 ? 0.25637 0.31764 0.33550 0.04982  -0.05463 0.02322  182 ARG A C   
1280 O O   . ARG A 175 ? 0.25959 0.32475 0.36233 0.04764  -0.05373 0.02055  182 ARG A O   
1281 C CB  . ARG A 175 ? 0.27186 0.36632 0.33624 0.07803  -0.06508 0.04946  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.27123 0.33216 0.31994 0.08038  -0.04855 0.06599  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.25411 0.30502 0.31273 0.09481  -0.04106 0.08675  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.28296 0.32942 0.36960 0.09386  -0.03780 0.08090  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.27473 0.34563 0.38118 0.10475  -0.04529 0.08376  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.28047 0.38480 0.38310 0.11886  -0.05874 0.09284  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.24869 0.31425 0.37999 0.10286  -0.03896 0.07781  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.30647 0.37985 0.18957 0.08880  -0.01091 0.03538  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.27604 0.33592 0.19047 0.07286  -0.00610 0.03345  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.28529 0.33158 0.20515 0.06164  -0.00325 0.02269  183 GLY A C   
1291 O O   . GLY A 176 ? 0.29473 0.33739 0.19518 0.06934  0.00174  0.02101  183 GLY A O   
1292 N N   . THR A 177 ? 0.25217 0.29202 0.19684 0.04632  -0.00528 0.01650  184 THR A N   
1293 C CA  . THR A 177 ? 0.24874 0.27803 0.20100 0.03827  -0.00212 0.00914  184 THR A CA  
1294 C C   . THR A 177 ? 0.29078 0.31883 0.25561 0.02418  -0.01453 -0.00322 184 THR A C   
1295 O O   . THR A 177 ? 0.23620 0.27116 0.21551 0.01764  -0.01925 -0.00200 184 THR A O   
1296 C CB  . THR A 177 ? 0.25276 0.27546 0.22449 0.03470  0.01311  0.02015  184 THR A CB  
1297 O OG1 . THR A 177 ? 0.27949 0.30241 0.23992 0.04616  0.02671  0.03409  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.26884 0.28962 0.25390 0.02737  0.01487  0.01396  184 THR A CG2 
1299 N N   . LYS A 178 ? 0.25330 0.27095 0.21103 0.02146  -0.01787 -0.01358 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.24133 0.25168 0.20905 0.00833  -0.02695 -0.02270 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.25178 0.25190 0.22794 0.00925  -0.01874 -0.02180 185 LYS A C   
1302 O O   . LYS A 178 ? 0.28051 0.27333 0.24225 0.02013  -0.01267 -0.02351 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.30332 0.30481 0.24949 0.00533  -0.03985 -0.03630 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.45485 0.44393 0.40732 -0.00998 -0.04928 -0.04472 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.52552 0.49661 0.45157 -0.01492 -0.06220 -0.06087 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.67714 0.66087 0.57935 -0.00597 -0.06865 -0.06559 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.80284 0.82251 0.71981 -0.01134 -0.07748 -0.05913 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.23753 0.24009 0.23478 0.00045  -0.01849 -0.01892 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.21016 0.20990 0.21721 0.00184  -0.01333 -0.01728 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.25701 0.24276 0.26150 -0.00416 -0.02108 -0.02333 186 VAL A C   
1311 O O   . VAL A 179 ? 0.24896 0.23818 0.26289 -0.01480 -0.02663 -0.02275 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.19168 0.20436 0.22106 -0.00384 -0.00886 -0.01010 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.20893 0.22674 0.25007 -0.00296 -0.00742 -0.00872 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.20886 0.22877 0.24158 -0.00075 0.00053  -0.00217 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.23879 0.20677 0.22886 0.00385  -0.01998 -0.02797 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.23882 0.18383 0.22236 -0.00104 -0.02565 -0.03239 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.23152 0.17935 0.22564 0.00689  -0.02002 -0.02517 187 ILE A C   
1318 O O   . ILE A 180 ? 0.26758 0.21605 0.25726 0.02259  -0.01255 -0.02345 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.29990 0.21381 0.25437 0.00385  -0.02883 -0.04402 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.29224 0.21231 0.23514 -0.00237 -0.03653 -0.05151 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.32733 0.20851 0.27478 -0.00404 -0.03375 -0.04734 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.38618 0.27748 0.29473 0.00493  -0.03999 -0.06563 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.21838 0.17167 0.22563 -0.00166 -0.02324 -0.01998 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.20371 0.16446 0.21983 0.00620  -0.02054 -0.01240 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.29674 0.22439 0.29710 0.01037  -0.02132 -0.01178 188 LEU A C   
1326 O O   . LEU A 181 ? 0.28543 0.19952 0.28385 -0.00243 -0.02563 -0.01061 188 LEU A O   
1327 C CB  . LEU A 181 ? 0.21055 0.19396 0.24349 -0.00352 -0.02382 -0.00751 188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.21191 0.21656 0.25686 -0.00968 -0.02290 -0.00908 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.26399 0.28183 0.31783 -0.01811 -0.02655 -0.00758 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.24290 0.26469 0.29776 -0.00230 -0.01727 -0.00652 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.28461 0.19995 0.27490 0.02920  -0.01563 -0.01023 189 HIS A N   
1332 C CA  . HIS A 182 ? 0.34893 0.22725 0.32221 0.03783  -0.01417 -0.00716 189 HIS A CA  
1333 C C   . HIS A 182 ? 0.30726 0.20766 0.29460 0.04389  -0.01408 0.00643  189 HIS A C   
1334 O O   . HIS A 182 ? 0.32142 0.25015 0.31945 0.06029  -0.01076 0.01265  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.34744 0.20084 0.29936 0.06042  -0.00675 -0.01192 189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.45785 0.29503 0.39191 0.05624  -0.00787 -0.02662 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.51998 0.30786 0.42679 0.04803  -0.01282 -0.03902 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.44440 0.30886 0.38298 0.05735  -0.00580 -0.03050 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.43807 0.22676 0.33163 0.04617  -0.01520 -0.05128 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.53883 0.37301 0.45026 0.05358  -0.00976 -0.04497 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.29709 0.19288 0.28661 0.03002  -0.01818 0.01170  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.26853 0.19323 0.26937 0.03462  -0.01985 0.02323  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.35038 0.26382 0.34135 0.05732  -0.01599 0.03516  190 LEU A C   
1344 O O   . LEU A 183 ? 0.37899 0.24621 0.34960 0.06559  -0.01103 0.03734  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.28462 0.20878 0.28664 0.01699  -0.02287 0.02732  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.29104 0.23414 0.30460 -0.00110 -0.02624 0.01825  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.30263 0.24790 0.31679 -0.01404 -0.02646 0.02502  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.30257 0.28261 0.33049 0.00118  -0.02863 0.01449  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.31720 0.27303 0.32177 0.06756  -0.01911 0.04306  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.32253 0.27889 0.31959 0.09113  -0.01721 0.05787  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.36143 0.28362 0.34021 0.08744  -0.01559 0.06876  191 LYS A C   
1352 O O   . LYS A 184 ? 0.36773 0.28918 0.34802 0.06603  -0.01807 0.06634  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.35779 0.37577 0.37544 0.09775  -0.02489 0.06273  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.31664 0.37323 0.35764 0.09974  -0.02495 0.05576  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.40755 0.52748 0.47233 0.10218  -0.03472 0.06035  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.42160 0.58026 0.51416 0.08340  -0.03855 0.04998  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.42332 0.64807 0.54332 0.08243  -0.05030 0.05352  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.45518 0.34818 0.41637 0.10980  -0.00959 0.08242  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.51134 0.36255 0.45281 0.10718  -0.00490 0.09625  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.49799 0.38430 0.44448 0.09805  -0.00991 0.10527  192 GLU A C   
1361 O O   . GLU A 185 ? 0.52302 0.38574 0.46140 0.08215  -0.00607 0.11183  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.58767 0.40488 0.50835 0.13904  0.00309  0.11218  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.92141 0.70179 0.82150 0.14244  0.00917  0.13319  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.15195 0.91018 1.03350 0.17863  0.01640  0.14989  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.08512 0.87639 0.97625 0.20022  0.01484  0.14481  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.10853 0.82965 0.97333 0.17786  0.02300  0.16308  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.41543 0.35928 0.37501 0.10636  -0.01852 0.10492  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.42095 0.39642 0.37815 0.10134  -0.02411 0.11128  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.36209 0.36387 0.33307 0.07665  -0.03015 0.09433  193 ASP A C   
1370 O O   . ASP A 186 ? 0.35671 0.38704 0.32328 0.07425  -0.03552 0.09558  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.43741 0.45802 0.39506 0.12557  -0.03219 0.12097  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.47523 0.54408 0.45860 0.12615  -0.04173 0.10724  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.54853 0.60803 0.54575 0.11464  -0.03879 0.09352  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.64640 0.76506 0.63627 0.13882  -0.05230 0.11181  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.30284 0.29162 0.28576 0.06037  -0.02859 0.07922  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.29051 0.29948 0.28565 0.04060  -0.03276 0.06420  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.27291 0.25317 0.26618 0.02223  -0.02652 0.06203  194 GLN A C   
1378 O O   . GLN A 187 ? 0.31599 0.30424 0.31990 0.00843  -0.02805 0.04956  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.25583 0.28525 0.26941 0.03877  -0.03709 0.05027  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.28338 0.35219 0.30582 0.05350  -0.04447 0.05339  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.31911 0.42008 0.33725 0.05139  -0.05413 0.05329  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.31026 0.41189 0.32537 0.03652  -0.05582 0.04404  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.34183 0.47113 0.35832 0.06792  -0.06093 0.06246  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.36301 0.31234 0.34389 0.02141  -0.01955 0.07567  195 THR A N   
1385 C CA  . THR A 188 ? 0.40957 0.33707 0.39416 0.00045  -0.01507 0.07380  195 THR A CA  
1386 C C   . THR A 188 ? 0.34960 0.30374 0.33943 -0.01116 -0.01339 0.07579  195 THR A C   
1387 O O   . THR A 188 ? 0.35143 0.30015 0.35011 -0.02880 -0.01032 0.07491  195 THR A O   
1388 C CB  . THR A 188 ? 0.44098 0.32083 0.41294 -0.00169 -0.00769 0.08735  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.48002 0.36027 0.43904 0.00878  -0.00206 0.10796  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.44647 0.29064 0.40908 0.01124  -0.00780 0.08194  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.33124 0.31604 0.31534 -0.00113 -0.01575 0.07753  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.32171 0.33124 0.30701 -0.00795 -0.01331 0.07582  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.30886 0.32736 0.30990 -0.01945 -0.01590 0.05948  196 GLU A C   
1394 O O   . GLU A 189 ? 0.28243 0.31404 0.28814 -0.02667 -0.01098 0.06040  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.31282 0.34992 0.28360 0.00613  -0.01816 0.07444  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.29687 0.35061 0.27418 0.00885  -0.02957 0.05597  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.34110 0.41975 0.30250 0.02082  -0.03761 0.05459  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.40031 0.48371 0.35404 0.03405  -0.04127 0.06533  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.36189 0.45455 0.31490 0.01860  -0.04010 0.04326  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.27116 0.28515 0.28025 -0.01913 -0.02220 0.04657  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.23287 0.25434 0.25392 -0.02726 -0.02403 0.03326  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.27676 0.28414 0.30658 -0.04011 -0.02193 0.03378  197 TYR A C   
1403 O O   . TYR A 190 ? 0.27830 0.29193 0.31655 -0.04471 -0.02412 0.02429  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.25137 0.27675 0.27720 -0.02207 -0.03004 0.02184  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.24432 0.28884 0.26454 -0.01412 -0.03508 0.01974  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.27408 0.33195 0.28835 -0.01551 -0.03608 0.01298  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.24388 0.29406 0.26242 -0.00394 -0.03943 0.02431  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.25801 0.33154 0.26313 -0.01040 -0.04328 0.00808  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.25671 0.33145 0.27103 0.00157  -0.04738 0.02150  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.24828 0.33305 0.25446 -0.00355 -0.05016 0.01192  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.28136 0.38742 0.27889 -0.00031 -0.06022 0.00595  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.30149 0.28915 0.32849 -0.04663 -0.01841 0.04484  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.28334 0.26262 0.32020 -0.06431 -0.01796 0.04569  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.31819 0.31970 0.36434 -0.07383 -0.01125 0.05805  198 LEU A C   
1415 O O   . LEU A 191 ? 0.32090 0.32435 0.38065 -0.09160 -0.01141 0.06081  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.29737 0.23509 0.32579 -0.06992 -0.01808 0.04923  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.29498 0.21251 0.31283 -0.05654 -0.02226 0.03824  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.41039 0.27870 0.41355 -0.05759 -0.02067 0.04120  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.35916 0.29096 0.38420 -0.05910 -0.02816 0.02224  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.25888 0.27743 0.29711 -0.06290 -0.00519 0.06684  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.26686 0.30839 0.31142 -0.06856 0.00461  0.08176  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.28858 0.36531 0.34261 -0.06463 0.00584  0.07438  199 GLU A C   
1423 O O   . GLU A 192 ? 0.26672 0.34874 0.31074 -0.05065 0.00254  0.06196  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.34396 0.38668 0.36929 -0.05530 0.01205  0.09600  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.39862 0.40498 0.41117 -0.05326 0.01218  0.10642  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.78928 0.80091 0.78104 -0.03837 0.01990  0.12411  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.96684 1.00026 0.95905 -0.04062 0.03089  0.13810  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 1.04082 1.03890 1.01547 -0.02266 0.01539  0.12524  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.28183 0.38244 0.35598 -0.07723 0.01084  0.08285  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.26643 0.40170 0.35159 -0.07100 0.01276  0.07787  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.23609 0.38456 0.30184 -0.04872 0.02042  0.07642  200 GLU A C   
1432 O O   . GLU A 193 ? 0.25185 0.40278 0.31117 -0.03622 0.01781  0.06278  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.28224 0.45081 0.39500 -0.08715 0.01835  0.09208  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.34466 0.55518 0.46979 -0.07592 0.02216  0.09049  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.60694 0.86172 0.76693 -0.09304 0.02491  0.10424  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.42933 0.68739 0.59992 -0.10952 0.03101  0.11980  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.50096 0.78610 0.67666 -0.08888 0.02069  0.09962  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.28896 0.44219 0.34164 -0.04311 0.03006  0.09010  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.26388 0.43004 0.29332 -0.02125 0.03686  0.08642  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.30278 0.44355 0.30940 -0.01081 0.02555  0.06671  201 ARG A C   
1441 O O   . ARG A 194 ? 0.26210 0.40513 0.25282 0.00336  0.02599  0.05390  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.31167 0.49006 0.32653 -0.01483 0.04973  0.10550  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.40329 0.55590 0.40584 -0.01886 0.04593  0.11336  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.50817 0.67811 0.50201 -0.01490 0.06233  0.13834  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.59752 0.74407 0.57031 -0.01084 0.06111  0.14923  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.56403 0.72151 0.51576 0.00047  0.07395  0.16934  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.57220 0.76400 0.52417 0.00643  0.09064  0.18186  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.71343 0.84959 0.64279 0.00833  0.07121  0.17899  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.26530 0.38177 0.27044 -0.01766 0.01576  0.06422  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.27664 0.37790 0.26715 -0.01047 0.00469  0.04768  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.24101 0.33608 0.24248 -0.01324 -0.00113 0.03136  202 ARG A C   
1452 O O   . ARG A 195 ? 0.24167 0.33191 0.23058 -0.00591 -0.00502 0.01703  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.28802 0.37148 0.27792 -0.01412 -0.00209 0.05271  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.24945 0.32725 0.22994 -0.00757 -0.01402 0.03904  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.28138 0.37206 0.23639 0.00482  -0.01638 0.03439  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.29904 0.39041 0.25045 0.00721  -0.02981 0.02436  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.31083 0.40670 0.25415 0.00749  -0.03906 0.00621  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.30795 0.40049 0.23954 0.00890  -0.03567 -0.00542 202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.28064 0.38396 0.22872 0.00601  -0.05183 -0.00030 202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.23218 0.32536 0.25494 -0.02433 -0.00204 0.03341  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.20399 0.29268 0.23487 -0.02476 -0.00617 0.02135  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.20536 0.30684 0.23120 -0.01340 0.00071  0.01777  203 ILE A C   
1463 O O   . ILE A 196 ? 0.23353 0.32193 0.25076 -0.00683 -0.00139 0.00535  203 ILE A O   
1464 C CB  . ILE A 196 ? 0.22438 0.31226 0.27436 -0.03713 -0.00927 0.02444  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.23643 0.30228 0.28523 -0.04422 -0.01511 0.02494  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.21107 0.29946 0.26647 -0.03387 -0.01182 0.01515  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.24491 0.30492 0.30653 -0.05891 -0.01793 0.02839  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.22007 0.34590 0.25042 -0.01005 0.01036  0.02961  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.25086 0.39073 0.27477 0.00599  0.01934  0.02774  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.26024 0.38077 0.25290 0.02004  0.01995  0.01446  204 LYS A C   
1471 O O   . LYS A 197 ? 0.27004 0.37779 0.25133 0.03174  0.02212  0.00353  204 LYS A O   
1472 C CB  . LYS A 197 ? 0.24999 0.42657 0.28475 0.00912  0.03177  0.04509  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.28587 0.49002 0.35300 -0.00225 0.03131  0.05529  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.27646 0.52326 0.35820 -0.00192 0.04490  0.07524  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.50855 0.78537 0.62764 -0.02410 0.04139  0.08782  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.56361 0.88193 0.70110 -0.03009 0.05520  0.11032  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.24260 0.35953 0.21883 0.01955  0.01783  0.01543  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.27254 0.37353 0.21665 0.03043  0.01489  0.00066  205 GLU A CA  
1479 C C   . GLU A 198 ? 0.26506 0.33816 0.20753 0.02390  0.00317  -0.01758 205 GLU A C   
1480 O O   . GLU A 198 ? 0.30132 0.35488 0.22279 0.03187  0.00285  -0.03314 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.28533 0.39251 0.21441 0.03016  0.01181  0.00721  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.31762 0.41158 0.21266 0.03805  0.00305  -0.01032 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.30699 0.41188 0.18911 0.03910  -0.00201 -0.00117 205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.33197 0.43712 0.23512 0.02802  -0.00779 0.00826  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.34364 0.45468 0.19320 0.05253  -0.00034 -0.00375 205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.24954 0.31869 0.21266 0.00954  -0.00535 -0.01557 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.26416 0.31288 0.22981 0.00171  -0.01487 -0.02935 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.25327 0.28676 0.22288 0.00499  -0.00963 -0.03454 206 ILE A C   
1489 O O   . ILE A 199 ? 0.30101 0.31035 0.25901 0.00445  -0.01233 -0.04821 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.25357 0.30583 0.23968 -0.01021 -0.02217 -0.02346 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.28143 0.34440 0.25940 -0.00954 -0.02790 -0.01869 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.27189 0.30969 0.26643 -0.01852 -0.02867 -0.03397 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.29558 0.36070 0.29156 -0.01545 -0.02991 -0.00766 206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.22882 0.27569 0.21443 0.00789  -0.00267 -0.02322 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.26160 0.29785 0.24943 0.01536  0.00268  -0.02498 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.29245 0.31451 0.25554 0.03275  0.01091  -0.03278 207 VAL A C   
1497 O O   . VAL A 200 ? 0.32896 0.32042 0.28085 0.03730  0.01246  -0.04206 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.24285 0.30580 0.25250 0.01572  0.00610  -0.01094 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.25580 0.31573 0.26508 0.02992  0.01276  -0.00956 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.21902 0.28314 0.24568 -0.00051 -0.00271 -0.00802 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.26908 0.30914 0.22009 0.04365  0.01753  -0.02906 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.30446 0.32932 0.22626 0.06444  0.02699  -0.03770 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.34436 0.32885 0.23696 0.06044  0.01889  -0.05937 208 LYS A C   
1504 O O   . LYS A 201 ? 0.46611 0.41571 0.33530 0.07211  0.02359  -0.07194 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.31958 0.37756 0.23403 0.07763  0.03737  -0.02716 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.41530 0.46150 0.29502 0.10405  0.04971  -0.03538 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.49672 0.58045 0.36974 0.11470  0.06028  -0.02255 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.61280 0.69156 0.45146 0.14559  0.07589  -0.02812 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.68168 0.81108 0.52571 0.15694  0.09105  -0.00726 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.36297 0.35185 0.25596 0.04432  0.00630  -0.06386 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.39421 0.35431 0.26307 0.03658  -0.00513 -0.08492 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.37440 0.30070 0.25213 0.02262  -0.01057 -0.09486 209 LYS A C   
1513 O O   . LYS A 202 ? 0.43161 0.31904 0.28427 0.02183  -0.01319 -0.11363 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.38191 0.36538 0.25599 0.02386  -0.01807 -0.08303 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.43015 0.39690 0.28122 0.01501  -0.03300 -0.10417 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.59624 0.59568 0.44709 0.01181  -0.04335 -0.09793 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.71090 0.70838 0.55808 -0.00459 -0.06333 -0.11465 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.76809 0.79630 0.60006 0.00033  -0.07387 -0.11168 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.38819 0.32661 0.29919 0.01034  -0.01243 -0.08291 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.41478 0.32961 0.33803 -0.00631 -0.01790 -0.08874 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.39464 0.29504 0.32995 -0.00098 -0.00756 -0.07897 210 HIS A C   
1522 O O   . HIS A 203 ? 0.45350 0.32879 0.39505 -0.01309 -0.00882 -0.08225 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.42618 0.36755 0.37608 -0.02430 -0.02878 -0.08304 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.43771 0.39521 0.37859 -0.03073 -0.04156 -0.09150 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.48676 0.42583 0.41012 -0.04061 -0.05196 -0.11070 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.45639 0.44652 0.40194 -0.02825 -0.04634 -0.08277 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.54964 0.51565 0.46791 -0.04297 -0.06395 -0.11343 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.47419 0.46999 0.40496 -0.03393 -0.05959 -0.09534 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.36877 0.36211 0.25976 -0.05060 -0.07654 -0.10342 211 SER A N   
1530 C CA  . SER A 204 ? 0.35865 0.33296 0.27494 -0.04176 -0.06100 -0.09885 211 SER A CA  
1531 C C   . SER A 204 ? 0.34694 0.29450 0.24027 -0.02536 -0.04381 -0.11285 211 SER A C   
1532 O O   . SER A 204 ? 0.38097 0.32614 0.29125 -0.01183 -0.02985 -0.10364 211 SER A O   
1533 C CB  . SER A 204 ? 0.35671 0.35731 0.30370 -0.03345 -0.05424 -0.07503 211 SER A CB  
1534 O OG  . SER A 204 ? 0.36057 0.38581 0.33321 -0.04438 -0.06773 -0.06258 211 SER A OG  
1535 N N   . GLN A 205 ? 0.45538 0.38451 0.31079 -0.02554 -0.04501 -0.13569 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.52755 0.44052 0.36284 -0.00460 -0.02535 -0.14760 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.58594 0.45686 0.43556 0.00403  -0.01623 -0.15474 212 GLN A C   
1538 O O   . GLN A 205 ? 0.63101 0.49623 0.47963 0.02623  0.00134  -0.15630 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.62556 0.53260 0.41026 -0.00350 -0.02536 -0.17176 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.66156 0.52863 0.42538 -0.02012 -0.03729 -0.19481 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.95420 0.83943 0.70927 -0.04540 -0.06482 -0.19180 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.65562 0.57179 0.44626 -0.05732 -0.07917 -0.17517 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.78373 0.65241 0.49548 -0.05009 -0.07327 -0.20683 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.52295 0.36726 0.38947 -0.01256 -0.02733 -0.15563 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.56241 0.36220 0.44282 -0.00569 -0.01917 -0.15719 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.50932 0.32254 0.42960 -0.00849 -0.01822 -0.12858 213 PHE A C   
1547 O O   . PHE A 206 ? 0.59872 0.37808 0.53427 -0.01435 -0.01793 -0.12369 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.63617 0.38528 0.50256 -0.02435 -0.03013 -0.18069 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.64755 0.38531 0.47528 -0.02056 -0.02447 -0.20875 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.70205 0.45864 0.50998 -0.04306 -0.03994 -0.22247 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.73952 0.46261 0.55708 0.00631  -0.00235 -0.21778 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.81999 0.57464 0.59328 -0.03983 -0.03397 -0.24628 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.84299 0.56337 0.62904 0.00904  0.00598  -0.24292 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.81333 0.54744 0.57317 -0.01457 -0.00970 -0.25720 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.38569 0.24516 0.32096 -0.00628 -0.01780 -0.10978 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.32456 0.19806 0.28922 -0.00504 -0.01399 -0.08619 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.43016 0.29670 0.39685 0.01831  -0.00057 -0.07905 214 ILE A C   
1558 O O   . ILE A 207 ? 0.45231 0.33638 0.40989 0.03403  0.00637  -0.08293 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.34334 0.26291 0.32062 -0.00939 -0.01787 -0.07285 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.31999 0.25108 0.30301 -0.03007 -0.03260 -0.07524 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.32543 0.26056 0.32393 -0.00402 -0.01105 -0.05329 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.37145 0.29135 0.37747 -0.04689 -0.03699 -0.06883 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.36864 0.21431 0.34937 0.02038  0.00286  -0.06564 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.38217 0.21799 0.36548 0.04389  0.01272  -0.05699 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.36140 0.23915 0.35591 0.05410  0.01516  -0.03803 215 GLY A C   
1566 O O   . GLY A 208 ? 0.38189 0.25502 0.38330 0.06850  0.01907  -0.02278 215 GLY A O   
1567 N N   . TYR A 209 ? 0.32952 0.24570 0.32455 0.04726  0.01185  -0.03909 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.30273 0.25573 0.30545 0.05244  0.01201  -0.02662 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.31579 0.29625 0.31577 0.05196  0.01172  -0.03541 216 TYR A C   
1570 O O   . TYR A 209 ? 0.32090 0.29730 0.31241 0.04280  0.00950  -0.04592 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.27541 0.23968 0.28367 0.03931  0.00917  -0.01638 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.30919 0.25025 0.32083 0.03691  0.01166  -0.00298 216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.30166 0.24548 0.31198 0.04909  0.01431  0.01421  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.30448 0.22252 0.32183 0.02079  0.01036  -0.00477 216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.31273 0.23312 0.32489 0.04719  0.01781  0.03122  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.29501 0.18975 0.31862 0.01563  0.01400  0.01089  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.29569 0.19022 0.31549 0.02945  0.01892  0.03040  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.33564 0.20529 0.36020 0.02466  0.02354  0.05054  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.26686 0.27760 0.27418 0.05918  0.01256  -0.02945 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.25107 0.28767 0.25956 0.05523  0.01330  -0.03399 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.28129 0.32128 0.28856 0.03905  0.00785  -0.03438 217 PRO A C   
1582 O O   . PRO A 210 ? 0.28765 0.32739 0.29865 0.03377  0.00446  -0.02983 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.29873 0.36813 0.32159 0.06262  0.01284  -0.02560 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.37125 0.43519 0.39652 0.07123  0.00987  -0.01592 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.28994 0.31266 0.30553 0.07164  0.01217  -0.01670 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.26402 0.30715 0.26470 0.03341  0.00819  -0.03886 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.22518 0.27098 0.22713 0.02165  0.00295  -0.03617 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.21347 0.27918 0.21951 0.01875  0.00556  -0.03157 218 ILE A C   
1589 O O   . ILE A 211 ? 0.30139 0.37647 0.29934 0.02126  0.01107  -0.03213 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.25110 0.28556 0.24156 0.01603  -0.00171 -0.04041 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.26134 0.27583 0.25287 0.01382  -0.00504 -0.04457 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.26646 0.30853 0.26315 0.00835  -0.00748 -0.03282 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.28577 0.29082 0.26457 0.00523  -0.01298 -0.05260 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.22138 0.29301 0.23906 0.01280  0.00286  -0.02770 219 THR A N   
1595 C CA  . THR A 212 ? 0.20932 0.29668 0.23580 0.00527  0.00435  -0.02227 219 THR A CA  
1596 C C   . THR A 212 ? 0.20960 0.28360 0.23689 -0.00319 0.00125  -0.01682 219 THR A C   
1597 O O   . THR A 212 ? 0.20612 0.26523 0.23728 -0.00381 -0.00246 -0.01970 219 THR A O   
1598 C CB  . THR A 212 ? 0.23097 0.33116 0.26985 0.00211  0.00104  -0.02392 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.23213 0.34867 0.27364 0.01333  0.00280  -0.02431 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.22554 0.34055 0.27884 -0.01215 0.00096  -0.01811 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.21370 0.29346 0.23696 -0.00753 0.00408  -0.00754 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.21677 0.28333 0.24272 -0.01402 0.00097  0.00349  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.20584 0.27190 0.24786 -0.02644 0.00260  0.00940  220 LEU A C   
1604 O O   . LEU A 213 ? 0.22875 0.31607 0.27530 -0.03357 0.00859  0.01700  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.24116 0.31473 0.24958 -0.01297 0.00182  0.01383  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.25931 0.32259 0.27000 -0.01790 -0.00169 0.03239  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.26072 0.30261 0.28471 -0.01275 -0.00962 0.03235  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.27935 0.35727 0.26295 -0.01576 -0.00265 0.04161  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.22434 0.26746 0.27599 -0.02958 -0.00185 0.00396  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.21833 0.25092 0.28439 -0.04478 -0.00274 0.00578  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.23335 0.25376 0.30372 -0.05247 -0.00016 0.02692  221 PHE A C   
1612 O O   . PHE A 214 ? 0.25957 0.27086 0.32152 -0.04297 -0.00085 0.03804  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.21726 0.22014 0.28584 -0.04420 -0.00701 -0.00944 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.19761 0.21277 0.25977 -0.04133 -0.01007 -0.02779 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.21201 0.25379 0.26650 -0.03130 -0.00898 -0.02871 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.22522 0.22069 0.28610 -0.04865 -0.01439 -0.04444 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.21327 0.26507 0.26051 -0.02746 -0.01225 -0.04049 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.23036 0.23975 0.27881 -0.04582 -0.01839 -0.05991 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.20939 0.24906 0.25227 -0.03492 -0.01738 -0.05475 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.25691 0.27949 0.34199 -0.07101 0.00176  0.03514  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.26548 0.27188 0.35628 -0.08098 0.00512  0.05954  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.32349 0.28293 0.42979 -0.09242 0.00049  0.05562  222 VAL A C   
1623 O O   . VAL A 215 ? 0.35092 0.29797 0.46136 -0.09637 -0.00493 0.03161  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.47407 0.51704 0.57158 -0.09548 0.01413  0.07768  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.55953 0.63437 0.63233 -0.08009 0.02131  0.08543  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.31204 0.38313 0.42811 -0.10775 0.01350  0.06507  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.33480 0.26509 0.44664 -0.09689 0.00251  0.07906  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.43551 0.30864 0.56168 -0.10488 -0.00058 0.07624  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.52665 0.38890 0.67258 -0.13498 0.00193  0.09434  223 GLU A C   
1630 O O   . GLU A 216 ? 0.50671 0.40006 0.65372 -0.14368 0.00903  0.12238  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.45482 0.29225 0.57809 -0.08354 -0.00088 0.09095  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.43417 0.29281 0.54384 -0.05745 -0.00318 0.07790  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.52493 0.35910 0.63909 -0.03512 -0.00501 0.09369  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.49024 0.27333 0.61873 -0.03009 -0.00372 0.09056  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.50889 0.37585 0.61266 -0.02270 -0.00836 0.10863  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.55168 0.36736 0.71211 -0.15174 -0.00325 0.07788  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.61548 0.40766 0.79618 -0.18306 -0.00218 0.09158  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.83380 0.61273 1.01212 -0.18117 0.00727  0.13172  224 LYS A C   
1639 O O   . LYS A 217 ? 0.81845 0.57391 0.98653 -0.15721 0.00817  0.14769  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.69582 0.42594 0.87272 -0.18945 -0.00780 0.06055  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.95932 0.66488 1.14522 -0.21938 -0.00522 0.06614  224 LYS A CG  
1642 C CD  . LYS A 217 ? 1.00804 0.66385 1.18373 -0.23217 -0.01260 0.02760  224 LYS A CD  
1643 C CE  . LYS A 217 ? 1.14853 0.72361 1.30687 -0.21219 -0.01011 0.02314  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 1.04916 0.61772 1.19183 -0.17654 -0.01196 0.00273  224 LYS A NZ  
# 
