data_7HB9
# 
_entry.id   7HB9 
# 
_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   7HB9         pdb_00007hb9 10.2210/pdb7hb9/pdb 
WWPDB D_1001407256 ?            ?                   
# 
_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                        7HB9 
_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 2,5-dichlorothiophene-3-sulfonamide 232.108   1   ?        ? ? ? 
3 water       nat water                               18.015    325 ?        ? ? ? 
# 
_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 2,5-dichlorothiophene-3-sulfonamide A1AYN 
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 
A1AYN non-polymer         . 2,5-dichlorothiophene-3-sulfonamide ? 'C4 H3 Cl2 N O2 S2' 232.108 
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        A1AYN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AYN 
_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 A1AYN 1   301 301 A1AYN BDN A . 
C 3 HOH   1   401 264 HOH   HOH A . 
C 3 HOH   2   402 185 HOH   HOH A . 
C 3 HOH   3   403 120 HOH   HOH A . 
C 3 HOH   4   404 175 HOH   HOH A . 
C 3 HOH   5   405 144 HOH   HOH A . 
C 3 HOH   6   406 274 HOH   HOH A . 
C 3 HOH   7   407 255 HOH   HOH A . 
C 3 HOH   8   408 165 HOH   HOH A . 
C 3 HOH   9   409 275 HOH   HOH A . 
C 3 HOH   10  410 320 HOH   HOH A . 
C 3 HOH   11  411 49  HOH   HOH A . 
C 3 HOH   12  412 64  HOH   HOH A . 
C 3 HOH   13  413 33  HOH   HOH A . 
C 3 HOH   14  414 31  HOH   HOH A . 
C 3 HOH   15  415 150 HOH   HOH A . 
C 3 HOH   16  416 164 HOH   HOH A . 
C 3 HOH   17  417 113 HOH   HOH A . 
C 3 HOH   18  418 179 HOH   HOH A . 
C 3 HOH   19  419 142 HOH   HOH A . 
C 3 HOH   20  420 86  HOH   HOH A . 
C 3 HOH   21  421 56  HOH   HOH A . 
C 3 HOH   22  422 8   HOH   HOH A . 
C 3 HOH   23  423 57  HOH   HOH A . 
C 3 HOH   24  424 14  HOH   HOH A . 
C 3 HOH   25  425 295 HOH   HOH A . 
C 3 HOH   26  426 25  HOH   HOH A . 
C 3 HOH   27  427 71  HOH   HOH A . 
C 3 HOH   28  428 110 HOH   HOH A . 
C 3 HOH   29  429 286 HOH   HOH A . 
C 3 HOH   30  430 4   HOH   HOH A . 
C 3 HOH   31  431 183 HOH   HOH A . 
C 3 HOH   32  432 223 HOH   HOH A . 
C 3 HOH   33  433 70  HOH   HOH A . 
C 3 HOH   34  434 248 HOH   HOH A . 
C 3 HOH   35  435 106 HOH   HOH A . 
C 3 HOH   36  436 315 HOH   HOH A . 
C 3 HOH   37  437 196 HOH   HOH A . 
C 3 HOH   38  438 228 HOH   HOH A . 
C 3 HOH   39  439 177 HOH   HOH A . 
C 3 HOH   40  440 19  HOH   HOH A . 
C 3 HOH   41  441 65  HOH   HOH A . 
C 3 HOH   42  442 146 HOH   HOH A . 
C 3 HOH   43  443 246 HOH   HOH A . 
C 3 HOH   44  444 32  HOH   HOH A . 
C 3 HOH   45  445 151 HOH   HOH A . 
C 3 HOH   46  446 15  HOH   HOH A . 
C 3 HOH   47  447 225 HOH   HOH A . 
C 3 HOH   48  448 256 HOH   HOH A . 
C 3 HOH   49  449 26  HOH   HOH A . 
C 3 HOH   50  450 214 HOH   HOH A . 
C 3 HOH   51  451 125 HOH   HOH A . 
C 3 HOH   52  452 302 HOH   HOH A . 
C 3 HOH   53  453 184 HOH   HOH A . 
C 3 HOH   54  454 60  HOH   HOH A . 
C 3 HOH   55  455 124 HOH   HOH A . 
C 3 HOH   56  456 81  HOH   HOH A . 
C 3 HOH   57  457 132 HOH   HOH A . 
C 3 HOH   58  458 236 HOH   HOH A . 
C 3 HOH   59  459 23  HOH   HOH A . 
C 3 HOH   60  460 50  HOH   HOH A . 
C 3 HOH   61  461 97  HOH   HOH A . 
C 3 HOH   62  462 117 HOH   HOH A . 
C 3 HOH   63  463 292 HOH   HOH A . 
C 3 HOH   64  464 96  HOH   HOH A . 
C 3 HOH   65  465 38  HOH   HOH A . 
C 3 HOH   66  466 173 HOH   HOH A . 
C 3 HOH   67  467 143 HOH   HOH A . 
C 3 HOH   68  468 73  HOH   HOH A . 
C 3 HOH   69  469 77  HOH   HOH A . 
C 3 HOH   70  470 54  HOH   HOH A . 
C 3 HOH   71  471 2   HOH   HOH A . 
C 3 HOH   72  472 76  HOH   HOH A . 
C 3 HOH   73  473 318 HOH   HOH A . 
C 3 HOH   74  474 244 HOH   HOH A . 
C 3 HOH   75  475 259 HOH   HOH A . 
C 3 HOH   76  476 69  HOH   HOH A . 
C 3 HOH   77  477 45  HOH   HOH A . 
C 3 HOH   78  478 5   HOH   HOH A . 
C 3 HOH   79  479 40  HOH   HOH A . 
C 3 HOH   80  480 11  HOH   HOH A . 
C 3 HOH   81  481 52  HOH   HOH A . 
C 3 HOH   82  482 41  HOH   HOH A . 
C 3 HOH   83  483 112 HOH   HOH A . 
C 3 HOH   84  484 100 HOH   HOH A . 
C 3 HOH   85  485 7   HOH   HOH A . 
C 3 HOH   86  486 39  HOH   HOH A . 
C 3 HOH   87  487 156 HOH   HOH A . 
C 3 HOH   88  488 21  HOH   HOH A . 
C 3 HOH   89  489 128 HOH   HOH A . 
C 3 HOH   90  490 22  HOH   HOH A . 
C 3 HOH   91  491 167 HOH   HOH A . 
C 3 HOH   92  492 148 HOH   HOH A . 
C 3 HOH   93  493 111 HOH   HOH A . 
C 3 HOH   94  494 63  HOH   HOH A . 
C 3 HOH   95  495 293 HOH   HOH A . 
C 3 HOH   96  496 6   HOH   HOH A . 
C 3 HOH   97  497 216 HOH   HOH A . 
C 3 HOH   98  498 239 HOH   HOH A . 
C 3 HOH   99  499 198 HOH   HOH A . 
C 3 HOH   100 500 48  HOH   HOH A . 
C 3 HOH   101 501 205 HOH   HOH A . 
C 3 HOH   102 502 28  HOH   HOH A . 
C 3 HOH   103 503 66  HOH   HOH A . 
C 3 HOH   104 504 107 HOH   HOH A . 
C 3 HOH   105 505 199 HOH   HOH A . 
C 3 HOH   106 506 58  HOH   HOH A . 
C 3 HOH   107 507 18  HOH   HOH A . 
C 3 HOH   108 508 47  HOH   HOH A . 
C 3 HOH   109 509 123 HOH   HOH A . 
C 3 HOH   110 510 43  HOH   HOH A . 
C 3 HOH   111 511 104 HOH   HOH A . 
C 3 HOH   112 512 116 HOH   HOH A . 
C 3 HOH   113 513 67  HOH   HOH A . 
C 3 HOH   114 514 17  HOH   HOH A . 
C 3 HOH   115 515 101 HOH   HOH A . 
C 3 HOH   116 516 79  HOH   HOH A . 
C 3 HOH   117 517 140 HOH   HOH A . 
C 3 HOH   118 518 105 HOH   HOH A . 
C 3 HOH   119 519 90  HOH   HOH A . 
C 3 HOH   120 520 168 HOH   HOH A . 
C 3 HOH   121 521 95  HOH   HOH A . 
C 3 HOH   122 522 309 HOH   HOH A . 
C 3 HOH   123 523 324 HOH   HOH A . 
C 3 HOH   124 524 130 HOH   HOH A . 
C 3 HOH   125 525 55  HOH   HOH A . 
C 3 HOH   126 526 53  HOH   HOH A . 
C 3 HOH   127 527 3   HOH   HOH A . 
C 3 HOH   128 528 61  HOH   HOH A . 
C 3 HOH   129 529 188 HOH   HOH A . 
C 3 HOH   130 530 206 HOH   HOH A . 
C 3 HOH   131 531 139 HOH   HOH A . 
C 3 HOH   132 532 72  HOH   HOH A . 
C 3 HOH   133 533 29  HOH   HOH A . 
C 3 HOH   134 534 174 HOH   HOH A . 
C 3 HOH   135 535 36  HOH   HOH A . 
C 3 HOH   136 536 9   HOH   HOH A . 
C 3 HOH   137 537 24  HOH   HOH A . 
C 3 HOH   138 538 136 HOH   HOH A . 
C 3 HOH   139 539 153 HOH   HOH A . 
C 3 HOH   140 540 212 HOH   HOH A . 
C 3 HOH   141 541 109 HOH   HOH A . 
C 3 HOH   142 542 75  HOH   HOH A . 
C 3 HOH   143 543 74  HOH   HOH A . 
C 3 HOH   144 544 118 HOH   HOH A . 
C 3 HOH   145 545 13  HOH   HOH A . 
C 3 HOH   146 546 252 HOH   HOH A . 
C 3 HOH   147 547 182 HOH   HOH A . 
C 3 HOH   148 548 314 HOH   HOH A . 
C 3 HOH   149 549 141 HOH   HOH A . 
C 3 HOH   150 550 162 HOH   HOH A . 
C 3 HOH   151 551 37  HOH   HOH A . 
C 3 HOH   152 552 209 HOH   HOH A . 
C 3 HOH   153 553 288 HOH   HOH A . 
C 3 HOH   154 554 30  HOH   HOH A . 
C 3 HOH   155 555 262 HOH   HOH A . 
C 3 HOH   156 556 27  HOH   HOH A . 
C 3 HOH   157 557 35  HOH   HOH A . 
C 3 HOH   158 558 10  HOH   HOH A . 
C 3 HOH   159 559 46  HOH   HOH A . 
C 3 HOH   160 560 287 HOH   HOH A . 
C 3 HOH   161 561 190 HOH   HOH A . 
C 3 HOH   162 562 187 HOH   HOH A . 
C 3 HOH   163 563 87  HOH   HOH A . 
C 3 HOH   164 564 127 HOH   HOH A . 
C 3 HOH   165 565 319 HOH   HOH A . 
C 3 HOH   166 566 88  HOH   HOH A . 
C 3 HOH   167 567 213 HOH   HOH A . 
C 3 HOH   168 568 158 HOH   HOH A . 
C 3 HOH   169 569 147 HOH   HOH A . 
C 3 HOH   170 570 232 HOH   HOH A . 
C 3 HOH   171 571 94  HOH   HOH A . 
C 3 HOH   172 572 261 HOH   HOH A . 
C 3 HOH   173 573 42  HOH   HOH A . 
C 3 HOH   174 574 152 HOH   HOH A . 
C 3 HOH   175 575 210 HOH   HOH A . 
C 3 HOH   176 576 237 HOH   HOH A . 
C 3 HOH   177 577 59  HOH   HOH A . 
C 3 HOH   178 578 197 HOH   HOH A . 
C 3 HOH   179 579 281 HOH   HOH A . 
C 3 HOH   180 580 278 HOH   HOH A . 
C 3 HOH   181 581 269 HOH   HOH A . 
C 3 HOH   182 582 20  HOH   HOH A . 
C 3 HOH   183 583 131 HOH   HOH A . 
C 3 HOH   184 584 92  HOH   HOH A . 
C 3 HOH   185 585 270 HOH   HOH A . 
C 3 HOH   186 586 267 HOH   HOH A . 
C 3 HOH   187 587 290 HOH   HOH A . 
C 3 HOH   188 588 242 HOH   HOH A . 
C 3 HOH   189 589 68  HOH   HOH A . 
C 3 HOH   190 590 44  HOH   HOH A . 
C 3 HOH   191 591 12  HOH   HOH A . 
C 3 HOH   192 592 89  HOH   HOH A . 
C 3 HOH   193 593 227 HOH   HOH A . 
C 3 HOH   194 594 93  HOH   HOH A . 
C 3 HOH   195 595 313 HOH   HOH A . 
C 3 HOH   196 596 34  HOH   HOH A . 
C 3 HOH   197 597 276 HOH   HOH A . 
C 3 HOH   198 598 62  HOH   HOH A . 
C 3 HOH   199 599 298 HOH   HOH A . 
C 3 HOH   200 600 102 HOH   HOH A . 
C 3 HOH   201 601 176 HOH   HOH A . 
C 3 HOH   202 602 234 HOH   HOH A . 
C 3 HOH   203 603 161 HOH   HOH A . 
C 3 HOH   204 604 240 HOH   HOH A . 
C 3 HOH   205 605 284 HOH   HOH A . 
C 3 HOH   206 606 241 HOH   HOH A . 
C 3 HOH   207 607 305 HOH   HOH A . 
C 3 HOH   208 608 194 HOH   HOH A . 
C 3 HOH   209 609 296 HOH   HOH A . 
C 3 HOH   210 610 155 HOH   HOH A . 
C 3 HOH   211 611 137 HOH   HOH A . 
C 3 HOH   212 612 249 HOH   HOH A . 
C 3 HOH   213 613 235 HOH   HOH A . 
C 3 HOH   214 614 303 HOH   HOH A . 
C 3 HOH   215 615 279 HOH   HOH A . 
C 3 HOH   216 616 122 HOH   HOH A . 
C 3 HOH   217 617 16  HOH   HOH A . 
C 3 HOH   218 618 1   HOH   HOH A . 
C 3 HOH   219 619 180 HOH   HOH A . 
C 3 HOH   220 620 301 HOH   HOH A . 
C 3 HOH   221 621 83  HOH   HOH A . 
C 3 HOH   222 622 247 HOH   HOH A . 
C 3 HOH   223 623 195 HOH   HOH A . 
C 3 HOH   224 624 220 HOH   HOH A . 
C 3 HOH   225 625 166 HOH   HOH A . 
C 3 HOH   226 626 203 HOH   HOH A . 
C 3 HOH   227 627 238 HOH   HOH A . 
C 3 HOH   228 628 178 HOH   HOH A . 
C 3 HOH   229 629 273 HOH   HOH A . 
C 3 HOH   230 630 133 HOH   HOH A . 
C 3 HOH   231 631 285 HOH   HOH A . 
C 3 HOH   232 632 99  HOH   HOH A . 
C 3 HOH   233 633 300 HOH   HOH A . 
C 3 HOH   234 634 126 HOH   HOH A . 
C 3 HOH   235 635 115 HOH   HOH A . 
C 3 HOH   236 636 289 HOH   HOH A . 
C 3 HOH   237 637 243 HOH   HOH A . 
C 3 HOH   238 638 204 HOH   HOH A . 
C 3 HOH   239 639 308 HOH   HOH A . 
C 3 HOH   240 640 217 HOH   HOH A . 
C 3 HOH   241 641 129 HOH   HOH A . 
C 3 HOH   242 642 230 HOH   HOH A . 
C 3 HOH   243 643 108 HOH   HOH A . 
C 3 HOH   244 644 189 HOH   HOH A . 
C 3 HOH   245 645 103 HOH   HOH A . 
C 3 HOH   246 646 82  HOH   HOH A . 
C 3 HOH   247 647 219 HOH   HOH A . 
C 3 HOH   248 648 159 HOH   HOH A . 
C 3 HOH   249 649 323 HOH   HOH A . 
C 3 HOH   250 650 154 HOH   HOH A . 
C 3 HOH   251 651 280 HOH   HOH A . 
C 3 HOH   252 652 186 HOH   HOH A . 
C 3 HOH   253 653 114 HOH   HOH A . 
C 3 HOH   254 654 226 HOH   HOH A . 
C 3 HOH   255 655 266 HOH   HOH A . 
C 3 HOH   256 656 257 HOH   HOH A . 
C 3 HOH   257 657 78  HOH   HOH A . 
C 3 HOH   258 658 304 HOH   HOH A . 
C 3 HOH   259 659 221 HOH   HOH A . 
C 3 HOH   260 660 51  HOH   HOH A . 
C 3 HOH   261 661 272 HOH   HOH A . 
C 3 HOH   262 662 149 HOH   HOH A . 
C 3 HOH   263 663 310 HOH   HOH A . 
C 3 HOH   264 664 311 HOH   HOH A . 
C 3 HOH   265 665 80  HOH   HOH A . 
C 3 HOH   266 666 231 HOH   HOH A . 
C 3 HOH   267 667 201 HOH   HOH A . 
C 3 HOH   268 668 250 HOH   HOH A . 
C 3 HOH   269 669 84  HOH   HOH A . 
C 3 HOH   270 670 191 HOH   HOH A . 
C 3 HOH   271 671 233 HOH   HOH A . 
C 3 HOH   272 672 271 HOH   HOH A . 
C 3 HOH   273 673 325 HOH   HOH A . 
C 3 HOH   274 674 282 HOH   HOH A . 
C 3 HOH   275 675 283 HOH   HOH A . 
C 3 HOH   276 676 265 HOH   HOH A . 
C 3 HOH   277 677 245 HOH   HOH A . 
C 3 HOH   278 678 218 HOH   HOH A . 
C 3 HOH   279 679 181 HOH   HOH A . 
C 3 HOH   280 680 307 HOH   HOH A . 
C 3 HOH   281 681 306 HOH   HOH A . 
C 3 HOH   282 682 277 HOH   HOH A . 
C 3 HOH   283 683 258 HOH   HOH A . 
C 3 HOH   284 684 299 HOH   HOH A . 
C 3 HOH   285 685 169 HOH   HOH A . 
C 3 HOH   286 686 254 HOH   HOH A . 
C 3 HOH   287 687 134 HOH   HOH A . 
C 3 HOH   288 688 260 HOH   HOH A . 
C 3 HOH   289 689 91  HOH   HOH A . 
C 3 HOH   290 690 200 HOH   HOH A . 
C 3 HOH   291 691 202 HOH   HOH A . 
C 3 HOH   292 692 317 HOH   HOH A . 
C 3 HOH   293 693 229 HOH   HOH A . 
C 3 HOH   294 694 321 HOH   HOH A . 
C 3 HOH   295 695 263 HOH   HOH A . 
C 3 HOH   296 696 193 HOH   HOH A . 
C 3 HOH   297 697 170 HOH   HOH A . 
C 3 HOH   298 698 294 HOH   HOH A . 
C 3 HOH   299 699 171 HOH   HOH A . 
C 3 HOH   300 700 172 HOH   HOH A . 
C 3 HOH   301 701 138 HOH   HOH A . 
C 3 HOH   302 702 135 HOH   HOH A . 
C 3 HOH   303 703 268 HOH   HOH A . 
C 3 HOH   304 704 98  HOH   HOH A . 
C 3 HOH   305 705 119 HOH   HOH A . 
C 3 HOH   306 706 316 HOH   HOH A . 
C 3 HOH   307 707 312 HOH   HOH A . 
C 3 HOH   308 708 163 HOH   HOH A . 
C 3 HOH   309 709 207 HOH   HOH A . 
C 3 HOH   310 710 160 HOH   HOH A . 
C 3 HOH   311 711 224 HOH   HOH A . 
C 3 HOH   312 712 121 HOH   HOH A . 
C 3 HOH   313 713 291 HOH   HOH A . 
C 3 HOH   314 714 297 HOH   HOH A . 
C 3 HOH   315 715 222 HOH   HOH A . 
C 3 HOH   316 716 208 HOH   HOH A . 
C 3 HOH   317 717 145 HOH   HOH A . 
C 3 HOH   318 718 215 HOH   HOH A . 
C 3 HOH   319 719 85  HOH   HOH A . 
C 3 HOH   320 720 157 HOH   HOH A . 
C 3 HOH   321 721 192 HOH   HOH A . 
C 3 HOH   322 722 322 HOH   HOH A . 
C 3 HOH   323 723 211 HOH   HOH A . 
C 3 HOH   324 724 251 HOH   HOH A . 
C 3 HOH   325 725 253 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             593015.527 
_cell.length_a           65.840 
_cell.length_b           89.630 
_cell.length_c           100.490 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HB9 
_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                         7HB9 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HB9 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2023-07-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HB9 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             34.760 
_reflns.d_resolution_high            1.890 
_reflns.number_obs                   23883 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.900 
_reflns.pdbx_Rmerge_I_obs            0.071 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        24.100 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              10.600 
_reflns.pdbx_Rrim_I_all              0.074 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     252619 
_reflns.pdbx_scaling_rejects         715 
_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 1.890 1.940  ? 8644 1533 ? 0.464 ? ? ? 5.600 ? 5.000  ? ? ? ? ? ? 87.900 0.513 0.211 0.902 
1 2 8.450 34.760 ? 2936 298  ? 0.048 ? ? ? 9.900 ? 42.200 ? ? ? ? ? ? 96.600 0.051 0.016 0.996 
# 
_refine.entry_id                                 7HB9 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.pdbx_overall_phase_error                 18.7678 
_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                          0.1615 
_refine.B_iso_mean                               24.85 
_refine.ls_number_reflns_R_free                  1182 
_refine.ls_percent_reflns_obs                    98.56 
_refine.ls_R_factor_R_work                       0.1604 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.89 
_refine.ls_number_reflns_obs                     23843 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  22661 
_refine.ls_d_res_low                             34.76 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1827 
_refine.overall_SU_ML                            0.1611 
_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         11 
_refine_hist.number_atoms_solvent             325 
_refine_hist.number_atoms_total               1980 
_refine_hist.d_res_high                       1.89 
_refine_hist.d_res_low                        34.76 
# 
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           1681 0.0036 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2268 0.7478 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     260  0.0455 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      290  0.0072 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 226  5.6679 ? ? ? 
# 
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' 1.89 1.98  2547 0.2325 90.27  0.2463 135 . . . . . 
'X-RAY DIFFRACTION' 1.98 2.08  2823 0.1723 99.73  0.2117 159 . . . . . 
'X-RAY DIFFRACTION' 2.08 2.21  2841 0.1558 99.90  0.2147 139 . . . . . 
'X-RAY DIFFRACTION' 2.21 2.38  2805 0.1847 98.89  0.2173 142 . . . . . 
'X-RAY DIFFRACTION' 2.38 2.62  2862 0.1692 100.00 0.2069 150 . . . . . 
'X-RAY DIFFRACTION' 2.62 3.00  2889 0.1647 99.97  0.1801 157 . . . . . 
'X-RAY DIFFRACTION' 3.00 3.78  2890 0.1475 99.93  0.1574 144 . . . . . 
'X-RAY DIFFRACTION' 3.78 34.76 3004 0.1422 99.62  0.1529 156 . . . . . 
# 
_struct.entry_id                  7HB9 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13464' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HB9 
_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              7HB9 
_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 7HB9 MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HB9 LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HB9 GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HB9 HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HB9 HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HB9 HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HB9 HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HB9 HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HB9 HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2  AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3  AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4  AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5  AA5 ASN A 99  ? THR A 102 ? ASN A 106 THR A 109 5 ? 4  
HELX_P HELX_P6  AA6 ILE A 103 ? ALA A 117 ? ILE A 110 ALA A 124 1 ? 15 
HELX_P HELX_P7  AA7 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P8  AA8 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P9  AA9 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P10 AB1 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O VAL A 85  ? O VAL A 92  N ASN A 72  ? N ASN A 79  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HB9 
_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 605 ? ? O A HOH 636 ? ? 1.84 
2 1 O A HOH 425 ? ? O A HOH 599 ? ? 1.90 
3 1 O A HOH 452 ? ? O A HOH 607 ? ? 1.93 
4 1 O A HOH 489 ? ? O A HOH 698 ? ? 1.94 
5 1 O A HOH 555 ? ? O A HOH 586 ? ? 2.03 
6 1 O A HOH 419 ? ? O A HOH 655 ? ? 2.05 
7 1 O A HOH 495 ? ? O A HOH 546 ? ? 2.17 
8 1 O A HOH 467 ? ? O A HOH 601 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 529 ? ? 1_555 O A HOH 715 ? ? 8_544 2.13 
2 1 O A HOH 505 ? ? 1_555 O A HOH 637 ? ? 8_444 2.14 
# 
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  ? ? -162.44 104.14  
2 1 ALA A 166 ? ? 62.12   -145.18 
# 
_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     689 
_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 12.3316816929  -17.9019028602 -18.7477009722 0.0940444362888 0.148070122496  0.131379293831  
0.00615551563556  -0.0251094250067  -0.0142767456786  2.63699493227 1.38617841455  5.40278803603 -0.820881025457 -2.90136635893   
0.341807335207  0.101951242507    -0.235952597264  -0.0226872175697 0.057279498665   -0.0122961737345 -0.0862940094173 
-0.0125014003138 0.295925026369   -0.0999061699885 
2  ? 'X-RAY DIFFRACTION' refined -5.21037542732 -6.26390021498 -20.862862565  0.136375508691  0.11509652144   0.15904511238   
-0.0190284825832  -0.00312486571581 -0.0299588244045  1.8187066086  4.38177570534  5.43100002104 -1.65499061792  1.71368451924    
-3.57032456563  -0.0357486032763  0.0694296372635  0.164697040976   0.0332486441921  -0.102494044612  0.00740383942475 
-0.233734317103  0.252724533294   0.12299556857    
3  ? 'X-RAY DIFFRACTION' refined -13.6769302151 -10.7182404109 -28.0149175964 0.115491825404  0.170122449385  0.185978860832  
0.000107934753965 -0.0597935219284  -0.00389739087348 1.19142456997 4.00185156579  4.78390191205 -0.845916144177 0.288956612952   
-3.20335705858  0.0596894339073   0.202937827051   0.00299913480483 -0.22482298765   0.165461657688   0.397202915989   
-0.125969517409  -0.349001284896  -0.266278143856  
4  ? 'X-RAY DIFFRACTION' refined -6.07025962968 -19.7782110743 -21.8832256626 0.125122495397  0.0997109026201 0.152587360144  
-0.0105176018967  -0.0232228798333  -0.0210978293915  2.02779285423 3.65151829616  4.80782829587 -0.700182616476 -0.0772609638577 
-2.5858725804   -0.0152408491363  -0.0791115018808 -0.210895694029  -0.0263235816488 0.111246355329   0.190327686365   
0.226618446277   -0.0554474260135 -0.134708199034  
5  ? 'X-RAY DIFFRACTION' refined 6.92044512381  -11.0626430886 -29.7341450891 0.159526330215  0.137436715552  0.203813707354  
0.022027014295    0.00463090782617  -0.00903574733689 2.61515355751 1.53281501126  8.21097462345 1.42529646936   1.36733982718    
2.50320238562   -0.0230397447671  0.0355421589643  0.230010213462   -0.250553411601  -0.248971586965  0.0503598563111  
-0.25920076313   -0.106247835312  0.0277086292524  
6  ? 'X-RAY DIFFRACTION' refined 12.3379497034  -5.93768024231 -12.6701466666 0.200763125151  0.406908401192  0.312005240267  
-0.108587112979   0.0231072020965   -0.147053285561   2.05524256675 2.60877863709  5.09865804757 0.884199217295  0.388393207546   
0.533113548557  0.589554461991    -1.08854247581   0.945733685151   0.177379822545   -0.0491018379884 -0.177054537241  
-0.722214540491  1.18552974309    0.144779940263   
7  ? 'X-RAY DIFFRACTION' refined 0.870999079689 -19.2853801243 -27.8240595605 0.116032817289  0.086451717763  0.12793380943   
-0.0108472964265  -0.0119429480446  -0.0237900756396  2.35029242015 1.35172039268  2.27659989053 -0.849345010077 0.345170429228   
-0.204771369286 0.0780024081132   0.203662467175   -0.201773784351  -0.164357861662  -0.0215670624187 0.106129495988   
0.163659001181   0.014385436089   -0.0756950112326 
8  ? 'X-RAY DIFFRACTION' refined -2.56944297186 -23.6631643413 -13.7071919574 0.117776986362  0.0887323349881 0.131693750195  
-0.0139915849057  -0.0144922928933  0.00579102940598  3.53938219661 4.48476596172  5.2576539584  -1.12885901866  -0.607308554192  
-1.64167788043  -0.0732358819514  -0.293282679341  -0.272295313043  0.166627452208   0.0121730621151  -0.0350012329051 
0.402421621658   0.135564568347   0.107328380428   
9  ? 'X-RAY DIFFRACTION' refined -9.93911890965 -15.1964288358 -5.62693868995 0.11176738756   0.224522211741  0.103916765685  
0.00438895694243  -0.0055481333147  -0.00703972688642 4.76763259277 8.29630649739  6.84907473312 -0.98426400977  -1.04075765386   
-1.58315425545  0.00246712055532  -0.398371477147  -0.0826963487692 0.343403804344   0.0716164213689  0.426300020601   
-0.0142184695893 -0.261642664229  -0.0187986554034 
10 ? 'X-RAY DIFFRACTION' refined -13.9734084964 -13.3679958706 -14.7357973328 0.108684539943  0.145000602866  0.0786727517867 
0.0239447380597   -0.00323306744006 -0.0263816376474  4.36181576208 0.685315036318 4.18642787127 -0.643858745517 -0.19322523622   
-0.992554645284 -0.00143932419776 -0.212696034621  -0.0371550863499 0.474502235071   0.0991967457152  0.0665265630597  
-0.215201433027  -0.136461732764  0.0263402022911  
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  1  'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2  2  'X-RAY DIFFRACTION' A 41  A 26  A 65  A 50  . 
;chain 'A' and (resid 41 through 65 )
;
3  3  'X-RAY DIFFRACTION' A 66  A 51  A 83  A 68  . 
;chain 'A' and (resid 66 through 83 )
;
4  4  'X-RAY DIFFRACTION' A 84  A 69  A 99  A 84  . 
;chain 'A' and (resid 84 through 99 )
;
5  5  'X-RAY DIFFRACTION' A 100 A 85  A 110 A 95  . 
;chain 'A' and (resid 100 through 110 )
;
6  6  'X-RAY DIFFRACTION' A 111 A 96  A 136 A 121 . 
;chain 'A' and (resid 111 through 136 )
;
7  7  'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
8  8  'X-RAY DIFFRACTION' A 183 A 168 A 199 A 184 . 
;chain 'A' and (resid 183 through 199 )
;
9  9  'X-RAY DIFFRACTION' A 200 A 185 A 210 A 195 . 
;chain 'A' and (resid 200 through 210 )
;
10 10 '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 
A1AYN C1   C  Y N 1   
A1AYN C2   C  Y N 2   
A1AYN C3   C  Y N 3   
A1AYN C4   C  Y N 4   
A1AYN N1   N  N N 5   
A1AYN O1   O  N N 6   
A1AYN O2   O  N N 7   
A1AYN S1   S  N N 8   
A1AYN S2   S  Y N 9   
A1AYN CL1  CL N N 10  
A1AYN CL2  CL N N 11  
A1AYN H2   H  N N 12  
A1AYN H12  H  N N 13  
A1AYN H11  H  N N 14  
ALA   N    N  N N 15  
ALA   CA   C  N S 16  
ALA   C    C  N N 17  
ALA   O    O  N N 18  
ALA   CB   C  N N 19  
ALA   OXT  O  N N 20  
ALA   H    H  N N 21  
ALA   H2   H  N N 22  
ALA   HA   H  N N 23  
ALA   HB1  H  N N 24  
ALA   HB2  H  N N 25  
ALA   HB3  H  N N 26  
ALA   HXT  H  N N 27  
ARG   N    N  N N 28  
ARG   CA   C  N S 29  
ARG   C    C  N N 30  
ARG   O    O  N N 31  
ARG   CB   C  N N 32  
ARG   CG   C  N N 33  
ARG   CD   C  N N 34  
ARG   NE   N  N N 35  
ARG   CZ   C  N N 36  
ARG   NH1  N  N N 37  
ARG   NH2  N  N N 38  
ARG   OXT  O  N N 39  
ARG   H    H  N N 40  
ARG   H2   H  N N 41  
ARG   HA   H  N N 42  
ARG   HB2  H  N N 43  
ARG   HB3  H  N N 44  
ARG   HG2  H  N N 45  
ARG   HG3  H  N N 46  
ARG   HD2  H  N N 47  
ARG   HD3  H  N N 48  
ARG   HE   H  N N 49  
ARG   HH11 H  N N 50  
ARG   HH12 H  N N 51  
ARG   HH21 H  N N 52  
ARG   HH22 H  N N 53  
ARG   HXT  H  N N 54  
ASN   N    N  N N 55  
ASN   CA   C  N S 56  
ASN   C    C  N N 57  
ASN   O    O  N N 58  
ASN   CB   C  N N 59  
ASN   CG   C  N N 60  
ASN   OD1  O  N N 61  
ASN   ND2  N  N N 62  
ASN   OXT  O  N N 63  
ASN   H    H  N N 64  
ASN   H2   H  N N 65  
ASN   HA   H  N N 66  
ASN   HB2  H  N N 67  
ASN   HB3  H  N N 68  
ASN   HD21 H  N N 69  
ASN   HD22 H  N N 70  
ASN   HXT  H  N N 71  
ASP   N    N  N N 72  
ASP   CA   C  N S 73  
ASP   C    C  N N 74  
ASP   O    O  N N 75  
ASP   CB   C  N N 76  
ASP   CG   C  N N 77  
ASP   OD1  O  N N 78  
ASP   OD2  O  N N 79  
ASP   OXT  O  N N 80  
ASP   H    H  N N 81  
ASP   H2   H  N N 82  
ASP   HA   H  N N 83  
ASP   HB2  H  N N 84  
ASP   HB3  H  N N 85  
ASP   HD2  H  N N 86  
ASP   HXT  H  N N 87  
GLN   N    N  N N 88  
GLN   CA   C  N S 89  
GLN   C    C  N N 90  
GLN   O    O  N N 91  
GLN   CB   C  N N 92  
GLN   CG   C  N N 93  
GLN   CD   C  N N 94  
GLN   OE1  O  N N 95  
GLN   NE2  N  N N 96  
GLN   OXT  O  N N 97  
GLN   H    H  N N 98  
GLN   H2   H  N N 99  
GLN   HA   H  N N 100 
GLN   HB2  H  N N 101 
GLN   HB3  H  N N 102 
GLN   HG2  H  N N 103 
GLN   HG3  H  N N 104 
GLN   HE21 H  N N 105 
GLN   HE22 H  N N 106 
GLN   HXT  H  N N 107 
GLU   N    N  N N 108 
GLU   CA   C  N S 109 
GLU   C    C  N N 110 
GLU   O    O  N N 111 
GLU   CB   C  N N 112 
GLU   CG   C  N N 113 
GLU   CD   C  N N 114 
GLU   OE1  O  N N 115 
GLU   OE2  O  N N 116 
GLU   OXT  O  N N 117 
GLU   H    H  N N 118 
GLU   H2   H  N N 119 
GLU   HA   H  N N 120 
GLU   HB2  H  N N 121 
GLU   HB3  H  N N 122 
GLU   HG2  H  N N 123 
GLU   HG3  H  N N 124 
GLU   HE2  H  N N 125 
GLU   HXT  H  N N 126 
GLY   N    N  N N 127 
GLY   CA   C  N N 128 
GLY   C    C  N N 129 
GLY   O    O  N N 130 
GLY   OXT  O  N N 131 
GLY   H    H  N N 132 
GLY   H2   H  N N 133 
GLY   HA2  H  N N 134 
GLY   HA3  H  N N 135 
GLY   HXT  H  N N 136 
HIS   N    N  N N 137 
HIS   CA   C  N S 138 
HIS   C    C  N N 139 
HIS   O    O  N N 140 
HIS   CB   C  N N 141 
HIS   CG   C  Y N 142 
HIS   ND1  N  Y N 143 
HIS   CD2  C  Y N 144 
HIS   CE1  C  Y N 145 
HIS   NE2  N  Y N 146 
HIS   OXT  O  N N 147 
HIS   H    H  N N 148 
HIS   H2   H  N N 149 
HIS   HA   H  N N 150 
HIS   HB2  H  N N 151 
HIS   HB3  H  N N 152 
HIS   HD1  H  N N 153 
HIS   HD2  H  N N 154 
HIS   HE1  H  N N 155 
HIS   HE2  H  N N 156 
HIS   HXT  H  N N 157 
HOH   O    O  N N 158 
HOH   H1   H  N N 159 
HOH   H2   H  N N 160 
ILE   N    N  N N 161 
ILE   CA   C  N S 162 
ILE   C    C  N N 163 
ILE   O    O  N N 164 
ILE   CB   C  N S 165 
ILE   CG1  C  N N 166 
ILE   CG2  C  N N 167 
ILE   CD1  C  N N 168 
ILE   OXT  O  N N 169 
ILE   H    H  N N 170 
ILE   H2   H  N N 171 
ILE   HA   H  N N 172 
ILE   HB   H  N N 173 
ILE   HG12 H  N N 174 
ILE   HG13 H  N N 175 
ILE   HG21 H  N N 176 
ILE   HG22 H  N N 177 
ILE   HG23 H  N N 178 
ILE   HD11 H  N N 179 
ILE   HD12 H  N N 180 
ILE   HD13 H  N N 181 
ILE   HXT  H  N N 182 
LEU   N    N  N N 183 
LEU   CA   C  N S 184 
LEU   C    C  N N 185 
LEU   O    O  N N 186 
LEU   CB   C  N N 187 
LEU   CG   C  N N 188 
LEU   CD1  C  N N 189 
LEU   CD2  C  N N 190 
LEU   OXT  O  N N 191 
LEU   H    H  N N 192 
LEU   H2   H  N N 193 
LEU   HA   H  N N 194 
LEU   HB2  H  N N 195 
LEU   HB3  H  N N 196 
LEU   HG   H  N N 197 
LEU   HD11 H  N N 198 
LEU   HD12 H  N N 199 
LEU   HD13 H  N N 200 
LEU   HD21 H  N N 201 
LEU   HD22 H  N N 202 
LEU   HD23 H  N N 203 
LEU   HXT  H  N N 204 
LYS   N    N  N N 205 
LYS   CA   C  N S 206 
LYS   C    C  N N 207 
LYS   O    O  N N 208 
LYS   CB   C  N N 209 
LYS   CG   C  N N 210 
LYS   CD   C  N N 211 
LYS   CE   C  N N 212 
LYS   NZ   N  N N 213 
LYS   OXT  O  N N 214 
LYS   H    H  N N 215 
LYS   H2   H  N N 216 
LYS   HA   H  N N 217 
LYS   HB2  H  N N 218 
LYS   HB3  H  N N 219 
LYS   HG2  H  N N 220 
LYS   HG3  H  N N 221 
LYS   HD2  H  N N 222 
LYS   HD3  H  N N 223 
LYS   HE2  H  N N 224 
LYS   HE3  H  N N 225 
LYS   HZ1  H  N N 226 
LYS   HZ2  H  N N 227 
LYS   HZ3  H  N N 228 
LYS   HXT  H  N N 229 
MET   N    N  N N 230 
MET   CA   C  N S 231 
MET   C    C  N N 232 
MET   O    O  N N 233 
MET   CB   C  N N 234 
MET   CG   C  N N 235 
MET   SD   S  N N 236 
MET   CE   C  N N 237 
MET   OXT  O  N N 238 
MET   H    H  N N 239 
MET   H2   H  N N 240 
MET   HA   H  N N 241 
MET   HB2  H  N N 242 
MET   HB3  H  N N 243 
MET   HG2  H  N N 244 
MET   HG3  H  N N 245 
MET   HE1  H  N N 246 
MET   HE2  H  N N 247 
MET   HE3  H  N N 248 
MET   HXT  H  N N 249 
PHE   N    N  N N 250 
PHE   CA   C  N S 251 
PHE   C    C  N N 252 
PHE   O    O  N N 253 
PHE   CB   C  N N 254 
PHE   CG   C  Y N 255 
PHE   CD1  C  Y N 256 
PHE   CD2  C  Y N 257 
PHE   CE1  C  Y N 258 
PHE   CE2  C  Y N 259 
PHE   CZ   C  Y N 260 
PHE   OXT  O  N N 261 
PHE   H    H  N N 262 
PHE   H2   H  N N 263 
PHE   HA   H  N N 264 
PHE   HB2  H  N N 265 
PHE   HB3  H  N N 266 
PHE   HD1  H  N N 267 
PHE   HD2  H  N N 268 
PHE   HE1  H  N N 269 
PHE   HE2  H  N N 270 
PHE   HZ   H  N N 271 
PHE   HXT  H  N N 272 
PRO   N    N  N N 273 
PRO   CA   C  N S 274 
PRO   C    C  N N 275 
PRO   O    O  N N 276 
PRO   CB   C  N N 277 
PRO   CG   C  N N 278 
PRO   CD   C  N N 279 
PRO   OXT  O  N N 280 
PRO   H    H  N N 281 
PRO   HA   H  N N 282 
PRO   HB2  H  N N 283 
PRO   HB3  H  N N 284 
PRO   HG2  H  N N 285 
PRO   HG3  H  N N 286 
PRO   HD2  H  N N 287 
PRO   HD3  H  N N 288 
PRO   HXT  H  N N 289 
SER   N    N  N N 290 
SER   CA   C  N S 291 
SER   C    C  N N 292 
SER   O    O  N N 293 
SER   CB   C  N N 294 
SER   OG   O  N N 295 
SER   OXT  O  N N 296 
SER   H    H  N N 297 
SER   H2   H  N N 298 
SER   HA   H  N N 299 
SER   HB2  H  N N 300 
SER   HB3  H  N N 301 
SER   HG   H  N N 302 
SER   HXT  H  N N 303 
THR   N    N  N N 304 
THR   CA   C  N S 305 
THR   C    C  N N 306 
THR   O    O  N N 307 
THR   CB   C  N R 308 
THR   OG1  O  N N 309 
THR   CG2  C  N N 310 
THR   OXT  O  N N 311 
THR   H    H  N N 312 
THR   H2   H  N N 313 
THR   HA   H  N N 314 
THR   HB   H  N N 315 
THR   HG1  H  N N 316 
THR   HG21 H  N N 317 
THR   HG22 H  N N 318 
THR   HG23 H  N N 319 
THR   HXT  H  N N 320 
TRP   N    N  N N 321 
TRP   CA   C  N S 322 
TRP   C    C  N N 323 
TRP   O    O  N N 324 
TRP   CB   C  N N 325 
TRP   CG   C  Y N 326 
TRP   CD1  C  Y N 327 
TRP   CD2  C  Y N 328 
TRP   NE1  N  Y N 329 
TRP   CE2  C  Y N 330 
TRP   CE3  C  Y N 331 
TRP   CZ2  C  Y N 332 
TRP   CZ3  C  Y N 333 
TRP   CH2  C  Y N 334 
TRP   OXT  O  N N 335 
TRP   H    H  N N 336 
TRP   H2   H  N N 337 
TRP   HA   H  N N 338 
TRP   HB2  H  N N 339 
TRP   HB3  H  N N 340 
TRP   HD1  H  N N 341 
TRP   HE1  H  N N 342 
TRP   HE3  H  N N 343 
TRP   HZ2  H  N N 344 
TRP   HZ3  H  N N 345 
TRP   HH2  H  N N 346 
TRP   HXT  H  N N 347 
TYR   N    N  N N 348 
TYR   CA   C  N S 349 
TYR   C    C  N N 350 
TYR   O    O  N N 351 
TYR   CB   C  N N 352 
TYR   CG   C  Y N 353 
TYR   CD1  C  Y N 354 
TYR   CD2  C  Y N 355 
TYR   CE1  C  Y N 356 
TYR   CE2  C  Y N 357 
TYR   CZ   C  Y N 358 
TYR   OH   O  N N 359 
TYR   OXT  O  N N 360 
TYR   H    H  N N 361 
TYR   H2   H  N N 362 
TYR   HA   H  N N 363 
TYR   HB2  H  N N 364 
TYR   HB3  H  N N 365 
TYR   HD1  H  N N 366 
TYR   HD2  H  N N 367 
TYR   HE1  H  N N 368 
TYR   HE2  H  N N 369 
TYR   HH   H  N N 370 
TYR   HXT  H  N N 371 
VAL   N    N  N N 372 
VAL   CA   C  N S 373 
VAL   C    C  N N 374 
VAL   O    O  N N 375 
VAL   CB   C  N N 376 
VAL   CG1  C  N N 377 
VAL   CG2  C  N N 378 
VAL   OXT  O  N N 379 
VAL   H    H  N N 380 
VAL   H2   H  N N 381 
VAL   HA   H  N N 382 
VAL   HB   H  N N 383 
VAL   HG11 H  N N 384 
VAL   HG12 H  N N 385 
VAL   HG13 H  N N 386 
VAL   HG21 H  N N 387 
VAL   HG22 H  N N 388 
VAL   HG23 H  N N 389 
VAL   HXT  H  N N 390 
# 
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 
A1AYN N1  S1   sing N N 1   
A1AYN S1  O1   doub N N 2   
A1AYN S1  O2   doub N N 3   
A1AYN S1  C1   sing N N 4   
A1AYN C1  C2   sing Y N 5   
A1AYN C1  C4   doub Y N 6   
A1AYN C2  C3   doub Y N 7   
A1AYN C3  CL1  sing N N 8   
A1AYN C3  S2   sing Y N 9   
A1AYN S2  C4   sing Y N 10  
A1AYN C4  CL2  sing N N 11  
A1AYN C2  H2   sing N N 12  
A1AYN N1  H12  sing N N 13  
A1AYN N1  H11  sing N N 14  
ALA   N   CA   sing N N 15  
ALA   N   H    sing N N 16  
ALA   N   H2   sing N N 17  
ALA   CA  C    sing N N 18  
ALA   CA  CB   sing N N 19  
ALA   CA  HA   sing N N 20  
ALA   C   O    doub N N 21  
ALA   C   OXT  sing N N 22  
ALA   CB  HB1  sing N N 23  
ALA   CB  HB2  sing N N 24  
ALA   CB  HB3  sing N N 25  
ALA   OXT HXT  sing N N 26  
ARG   N   CA   sing N N 27  
ARG   N   H    sing N N 28  
ARG   N   H2   sing N N 29  
ARG   CA  C    sing N N 30  
ARG   CA  CB   sing N N 31  
ARG   CA  HA   sing N N 32  
ARG   C   O    doub N N 33  
ARG   C   OXT  sing N N 34  
ARG   CB  CG   sing N N 35  
ARG   CB  HB2  sing N N 36  
ARG   CB  HB3  sing N N 37  
ARG   CG  CD   sing N N 38  
ARG   CG  HG2  sing N N 39  
ARG   CG  HG3  sing N N 40  
ARG   CD  NE   sing N N 41  
ARG   CD  HD2  sing N N 42  
ARG   CD  HD3  sing N N 43  
ARG   NE  CZ   sing N N 44  
ARG   NE  HE   sing N N 45  
ARG   CZ  NH1  sing N N 46  
ARG   CZ  NH2  doub N N 47  
ARG   NH1 HH11 sing N N 48  
ARG   NH1 HH12 sing N N 49  
ARG   NH2 HH21 sing N N 50  
ARG   NH2 HH22 sing N N 51  
ARG   OXT HXT  sing N N 52  
ASN   N   CA   sing N N 53  
ASN   N   H    sing N N 54  
ASN   N   H2   sing N N 55  
ASN   CA  C    sing N N 56  
ASN   CA  CB   sing N N 57  
ASN   CA  HA   sing N N 58  
ASN   C   O    doub N N 59  
ASN   C   OXT  sing N N 60  
ASN   CB  CG   sing N N 61  
ASN   CB  HB2  sing N N 62  
ASN   CB  HB3  sing N N 63  
ASN   CG  OD1  doub N N 64  
ASN   CG  ND2  sing N N 65  
ASN   ND2 HD21 sing N N 66  
ASN   ND2 HD22 sing N N 67  
ASN   OXT HXT  sing N N 68  
ASP   N   CA   sing N N 69  
ASP   N   H    sing N N 70  
ASP   N   H2   sing N N 71  
ASP   CA  C    sing N N 72  
ASP   CA  CB   sing N N 73  
ASP   CA  HA   sing N N 74  
ASP   C   O    doub N N 75  
ASP   C   OXT  sing N N 76  
ASP   CB  CG   sing N N 77  
ASP   CB  HB2  sing N N 78  
ASP   CB  HB3  sing N N 79  
ASP   CG  OD1  doub N N 80  
ASP   CG  OD2  sing N N 81  
ASP   OD2 HD2  sing N N 82  
ASP   OXT HXT  sing N N 83  
GLN   N   CA   sing N N 84  
GLN   N   H    sing N N 85  
GLN   N   H2   sing N N 86  
GLN   CA  C    sing N N 87  
GLN   CA  CB   sing N N 88  
GLN   CA  HA   sing N N 89  
GLN   C   O    doub N N 90  
GLN   C   OXT  sing N N 91  
GLN   CB  CG   sing N N 92  
GLN   CB  HB2  sing N N 93  
GLN   CB  HB3  sing N N 94  
GLN   CG  CD   sing N N 95  
GLN   CG  HG2  sing N N 96  
GLN   CG  HG3  sing N N 97  
GLN   CD  OE1  doub N N 98  
GLN   CD  NE2  sing N N 99  
GLN   NE2 HE21 sing N N 100 
GLN   NE2 HE22 sing N N 101 
GLN   OXT HXT  sing N N 102 
GLU   N   CA   sing N N 103 
GLU   N   H    sing N N 104 
GLU   N   H2   sing N N 105 
GLU   CA  C    sing N N 106 
GLU   CA  CB   sing N N 107 
GLU   CA  HA   sing N N 108 
GLU   C   O    doub N N 109 
GLU   C   OXT  sing N N 110 
GLU   CB  CG   sing N N 111 
GLU   CB  HB2  sing N N 112 
GLU   CB  HB3  sing N N 113 
GLU   CG  CD   sing N N 114 
GLU   CG  HG2  sing N N 115 
GLU   CG  HG3  sing N N 116 
GLU   CD  OE1  doub N N 117 
GLU   CD  OE2  sing N N 118 
GLU   OE2 HE2  sing N N 119 
GLU   OXT HXT  sing N N 120 
GLY   N   CA   sing N N 121 
GLY   N   H    sing N N 122 
GLY   N   H2   sing N N 123 
GLY   CA  C    sing N N 124 
GLY   CA  HA2  sing N N 125 
GLY   CA  HA3  sing N N 126 
GLY   C   O    doub N N 127 
GLY   C   OXT  sing N N 128 
GLY   OXT HXT  sing N N 129 
HIS   N   CA   sing N N 130 
HIS   N   H    sing N N 131 
HIS   N   H2   sing N N 132 
HIS   CA  C    sing N N 133 
HIS   CA  CB   sing N N 134 
HIS   CA  HA   sing N N 135 
HIS   C   O    doub N N 136 
HIS   C   OXT  sing N N 137 
HIS   CB  CG   sing N N 138 
HIS   CB  HB2  sing N N 139 
HIS   CB  HB3  sing N N 140 
HIS   CG  ND1  sing Y N 141 
HIS   CG  CD2  doub Y N 142 
HIS   ND1 CE1  doub Y N 143 
HIS   ND1 HD1  sing N N 144 
HIS   CD2 NE2  sing Y N 145 
HIS   CD2 HD2  sing N N 146 
HIS   CE1 NE2  sing Y N 147 
HIS   CE1 HE1  sing N N 148 
HIS   NE2 HE2  sing N N 149 
HIS   OXT HXT  sing N N 150 
HOH   O   H1   sing N N 151 
HOH   O   H2   sing N N 152 
ILE   N   CA   sing N N 153 
ILE   N   H    sing N N 154 
ILE   N   H2   sing N N 155 
ILE   CA  C    sing N N 156 
ILE   CA  CB   sing N N 157 
ILE   CA  HA   sing N N 158 
ILE   C   O    doub N N 159 
ILE   C   OXT  sing N N 160 
ILE   CB  CG1  sing N N 161 
ILE   CB  CG2  sing N N 162 
ILE   CB  HB   sing N N 163 
ILE   CG1 CD1  sing N N 164 
ILE   CG1 HG12 sing N N 165 
ILE   CG1 HG13 sing N N 166 
ILE   CG2 HG21 sing N N 167 
ILE   CG2 HG22 sing N N 168 
ILE   CG2 HG23 sing N N 169 
ILE   CD1 HD11 sing N N 170 
ILE   CD1 HD12 sing N N 171 
ILE   CD1 HD13 sing N N 172 
ILE   OXT HXT  sing N N 173 
LEU   N   CA   sing N N 174 
LEU   N   H    sing N N 175 
LEU   N   H2   sing N N 176 
LEU   CA  C    sing N N 177 
LEU   CA  CB   sing N N 178 
LEU   CA  HA   sing N N 179 
LEU   C   O    doub N N 180 
LEU   C   OXT  sing N N 181 
LEU   CB  CG   sing N N 182 
LEU   CB  HB2  sing N N 183 
LEU   CB  HB3  sing N N 184 
LEU   CG  CD1  sing N N 185 
LEU   CG  CD2  sing N N 186 
LEU   CG  HG   sing N N 187 
LEU   CD1 HD11 sing N N 188 
LEU   CD1 HD12 sing N N 189 
LEU   CD1 HD13 sing N N 190 
LEU   CD2 HD21 sing N N 191 
LEU   CD2 HD22 sing N N 192 
LEU   CD2 HD23 sing N N 193 
LEU   OXT HXT  sing N N 194 
LYS   N   CA   sing N N 195 
LYS   N   H    sing N N 196 
LYS   N   H2   sing N N 197 
LYS   CA  C    sing N N 198 
LYS   CA  CB   sing N N 199 
LYS   CA  HA   sing N N 200 
LYS   C   O    doub N N 201 
LYS   C   OXT  sing N N 202 
LYS   CB  CG   sing N N 203 
LYS   CB  HB2  sing N N 204 
LYS   CB  HB3  sing N N 205 
LYS   CG  CD   sing N N 206 
LYS   CG  HG2  sing N N 207 
LYS   CG  HG3  sing N N 208 
LYS   CD  CE   sing N N 209 
LYS   CD  HD2  sing N N 210 
LYS   CD  HD3  sing N N 211 
LYS   CE  NZ   sing N N 212 
LYS   CE  HE2  sing N N 213 
LYS   CE  HE3  sing N N 214 
LYS   NZ  HZ1  sing N N 215 
LYS   NZ  HZ2  sing N N 216 
LYS   NZ  HZ3  sing N N 217 
LYS   OXT HXT  sing N N 218 
MET   N   CA   sing N N 219 
MET   N   H    sing N N 220 
MET   N   H2   sing N N 221 
MET   CA  C    sing N N 222 
MET   CA  CB   sing N N 223 
MET   CA  HA   sing N N 224 
MET   C   O    doub N N 225 
MET   C   OXT  sing N N 226 
MET   CB  CG   sing N N 227 
MET   CB  HB2  sing N N 228 
MET   CB  HB3  sing N N 229 
MET   CG  SD   sing N N 230 
MET   CG  HG2  sing N N 231 
MET   CG  HG3  sing N N 232 
MET   SD  CE   sing N N 233 
MET   CE  HE1  sing N N 234 
MET   CE  HE2  sing N N 235 
MET   CE  HE3  sing N N 236 
MET   OXT HXT  sing N N 237 
PHE   N   CA   sing N N 238 
PHE   N   H    sing N N 239 
PHE   N   H2   sing N N 240 
PHE   CA  C    sing N N 241 
PHE   CA  CB   sing N N 242 
PHE   CA  HA   sing N N 243 
PHE   C   O    doub N N 244 
PHE   C   OXT  sing N N 245 
PHE   CB  CG   sing N N 246 
PHE   CB  HB2  sing N N 247 
PHE   CB  HB3  sing N N 248 
PHE   CG  CD1  doub Y N 249 
PHE   CG  CD2  sing Y N 250 
PHE   CD1 CE1  sing Y N 251 
PHE   CD1 HD1  sing N N 252 
PHE   CD2 CE2  doub Y N 253 
PHE   CD2 HD2  sing N N 254 
PHE   CE1 CZ   doub Y N 255 
PHE   CE1 HE1  sing N N 256 
PHE   CE2 CZ   sing Y N 257 
PHE   CE2 HE2  sing N N 258 
PHE   CZ  HZ   sing N N 259 
PHE   OXT HXT  sing N N 260 
PRO   N   CA   sing N N 261 
PRO   N   CD   sing N N 262 
PRO   N   H    sing N N 263 
PRO   CA  C    sing N N 264 
PRO   CA  CB   sing N N 265 
PRO   CA  HA   sing N N 266 
PRO   C   O    doub N N 267 
PRO   C   OXT  sing N N 268 
PRO   CB  CG   sing N N 269 
PRO   CB  HB2  sing N N 270 
PRO   CB  HB3  sing N N 271 
PRO   CG  CD   sing N N 272 
PRO   CG  HG2  sing N N 273 
PRO   CG  HG3  sing N N 274 
PRO   CD  HD2  sing N N 275 
PRO   CD  HD3  sing N N 276 
PRO   OXT HXT  sing N N 277 
SER   N   CA   sing N N 278 
SER   N   H    sing N N 279 
SER   N   H2   sing N N 280 
SER   CA  C    sing N N 281 
SER   CA  CB   sing N N 282 
SER   CA  HA   sing N N 283 
SER   C   O    doub N N 284 
SER   C   OXT  sing N N 285 
SER   CB  OG   sing N N 286 
SER   CB  HB2  sing N N 287 
SER   CB  HB3  sing N N 288 
SER   OG  HG   sing N N 289 
SER   OXT HXT  sing N N 290 
THR   N   CA   sing N N 291 
THR   N   H    sing N N 292 
THR   N   H2   sing N N 293 
THR   CA  C    sing N N 294 
THR   CA  CB   sing N N 295 
THR   CA  HA   sing N N 296 
THR   C   O    doub N N 297 
THR   C   OXT  sing N N 298 
THR   CB  OG1  sing N N 299 
THR   CB  CG2  sing N N 300 
THR   CB  HB   sing N N 301 
THR   OG1 HG1  sing N N 302 
THR   CG2 HG21 sing N N 303 
THR   CG2 HG22 sing N N 304 
THR   CG2 HG23 sing N N 305 
THR   OXT HXT  sing N N 306 
TRP   N   CA   sing N N 307 
TRP   N   H    sing N N 308 
TRP   N   H2   sing N N 309 
TRP   CA  C    sing N N 310 
TRP   CA  CB   sing N N 311 
TRP   CA  HA   sing N N 312 
TRP   C   O    doub N N 313 
TRP   C   OXT  sing N N 314 
TRP   CB  CG   sing N N 315 
TRP   CB  HB2  sing N N 316 
TRP   CB  HB3  sing N N 317 
TRP   CG  CD1  doub Y N 318 
TRP   CG  CD2  sing Y N 319 
TRP   CD1 NE1  sing Y N 320 
TRP   CD1 HD1  sing N N 321 
TRP   CD2 CE2  doub Y N 322 
TRP   CD2 CE3  sing Y N 323 
TRP   NE1 CE2  sing Y N 324 
TRP   NE1 HE1  sing N N 325 
TRP   CE2 CZ2  sing Y N 326 
TRP   CE3 CZ3  doub Y N 327 
TRP   CE3 HE3  sing N N 328 
TRP   CZ2 CH2  doub Y N 329 
TRP   CZ2 HZ2  sing N N 330 
TRP   CZ3 CH2  sing Y N 331 
TRP   CZ3 HZ3  sing N N 332 
TRP   CH2 HH2  sing N N 333 
TRP   OXT HXT  sing N N 334 
TYR   N   CA   sing N N 335 
TYR   N   H    sing N N 336 
TYR   N   H2   sing N N 337 
TYR   CA  C    sing N N 338 
TYR   CA  CB   sing N N 339 
TYR   CA  HA   sing N N 340 
TYR   C   O    doub N N 341 
TYR   C   OXT  sing N N 342 
TYR   CB  CG   sing N N 343 
TYR   CB  HB2  sing N N 344 
TYR   CB  HB3  sing N N 345 
TYR   CG  CD1  doub Y N 346 
TYR   CG  CD2  sing Y N 347 
TYR   CD1 CE1  sing Y N 348 
TYR   CD1 HD1  sing N N 349 
TYR   CD2 CE2  doub Y N 350 
TYR   CD2 HD2  sing N N 351 
TYR   CE1 CZ   doub Y N 352 
TYR   CE1 HE1  sing N N 353 
TYR   CE2 CZ   sing Y N 354 
TYR   CE2 HE2  sing N N 355 
TYR   CZ  OH   sing N N 356 
TYR   OH  HH   sing N N 357 
TYR   OXT HXT  sing N N 358 
VAL   N   CA   sing N N 359 
VAL   N   H    sing N N 360 
VAL   N   H2   sing N N 361 
VAL   CA  C    sing N N 362 
VAL   CA  CB   sing N N 363 
VAL   CA  HA   sing N N 364 
VAL   C   O    doub N N 365 
VAL   C   OXT  sing N N 366 
VAL   CB  CG1  sing N N 367 
VAL   CB  CG2  sing N N 368 
VAL   CB  HB   sing N N 369 
VAL   CG1 HG11 sing N N 370 
VAL   CG1 HG12 sing N N 371 
VAL   CG1 HG13 sing N N 372 
VAL   CG2 HG21 sing N N 373 
VAL   CG2 HG22 sing N N 374 
VAL   CG2 HG23 sing N N 375 
VAL   OXT HXT  sing N N 376 
# 
_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                    7HB9 
_atom_sites.fract_transf_matrix[1][1]   0.015188 
_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]   0.011157 
_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]   0.009951 
_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.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 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   ? 4.35159   -28.45288 -39.20165 1.000 37.62372 ? 16  GLU   A N   1 
ATOM   2    C  CA  . GLU   A 1 9   ? 5.61803   -27.74904 -39.32593 1.000 46.96733 ? 16  GLU   A CA  1 
ATOM   3    C  C   . GLU   A 1 9   ? 5.83488   -26.88025 -38.08374 1.000 43.50307 ? 16  GLU   A C   1 
ATOM   4    O  O   . GLU   A 1 9   ? 5.11791   -25.89763 -37.85664 1.000 44.01173 ? 16  GLU   A O   1 
ATOM   5    C  CB  . GLU   A 1 9   ? 5.63513   -26.91031 -40.61997 1.000 53.43681 ? 16  GLU   A CB  1 
ATOM   6    C  CG  . GLU   A 1 9   ? 6.41029   -25.56266 -40.60367 1.000 62.33125 ? 16  GLU   A CG  1 
ATOM   7    C  CD  . GLU   A 1 9   ? 7.91993   -25.71986 -40.45640 1.000 76.05779 ? 16  GLU   A CD  1 
ATOM   8    O  OE1 . GLU   A 1 9   ? 8.65262   -24.80163 -40.88146 1.000 65.70544 ? 16  GLU   A OE1 1 
ATOM   9    O  OE2 . GLU   A 1 9   ? 8.38135   -26.75870 -39.94105 1.000 78.31495 ? 16  GLU   A OE2 1 
ATOM   10   N  N   . VAL   A 1 10  ? 6.82245   -27.25231 -37.27368 1.000 29.45976 ? 17  VAL   A N   1 
ATOM   11   C  CA  . VAL   A 1 10  ? 7.06961   -26.63151 -35.97892 1.000 23.72826 ? 17  VAL   A CA  1 
ATOM   12   C  C   . VAL   A 1 10  ? 8.43378   -25.96266 -36.01747 1.000 27.53087 ? 17  VAL   A C   1 
ATOM   13   O  O   . VAL   A 1 10  ? 9.43430   -26.60586 -36.35353 1.000 26.20709 ? 17  VAL   A O   1 
ATOM   14   C  CB  . VAL   A 1 10  ? 7.00295   -27.66797 -34.84400 1.000 26.61340 ? 17  VAL   A CB  1 
ATOM   15   C  CG1 . VAL   A 1 10  ? 7.27534   -27.00869 -33.50432 1.000 26.06210 ? 17  VAL   A CG1 1 
ATOM   16   C  CG2 . VAL   A 1 10  ? 5.65194   -28.37186 -34.85320 1.000 34.20879 ? 17  VAL   A CG2 1 
ATOM   17   N  N   . GLU   A 1 11  ? 8.47634   -24.68119 -35.66487 1.000 20.04621 ? 18  GLU   A N   1 
ATOM   18   C  CA  . GLU   A 1 11  ? 9.72760   -23.93822 -35.59452 1.000 19.11214 ? 18  GLU   A CA  1 
ATOM   19   C  C   . GLU   A 1 11  ? 10.14524  -23.78876 -34.13835 1.000 22.32210 ? 18  GLU   A C   1 
ATOM   20   O  O   . GLU   A 1 11  ? 9.33464   -23.39846 -33.29472 1.000 16.29080 ? 18  GLU   A O   1 
ATOM   21   C  CB  . GLU   A 1 11  ? 9.58887   -22.56555 -36.25173 1.000 19.59461 ? 18  GLU   A CB  1 
ATOM   22   C  CG  . GLU   A 1 11  ? 9.26058   -22.61828 -37.73519 1.000 22.49527 ? 18  GLU   A CG  1 
ATOM   23   C  CD  . GLU   A 1 11  ? 9.06470   -21.23720 -38.33012 1.000 37.73125 ? 18  GLU   A CD  1 
ATOM   24   O  OE1 . GLU   A 1 11  ? 8.01765   -20.61570 -38.05049 1.000 35.66909 ? 18  GLU   A OE1 1 
ATOM   25   O  OE2 . GLU   A 1 11  ? 9.95391   -20.77019 -39.07078 1.000 36.94390 ? 18  GLU   A OE2 1 
ATOM   26   N  N   . THR   A 1 12  ? 11.40311  -24.10746 -33.84683 1.000 16.89144 ? 19  THR   A N   1 
ATOM   27   C  CA  . THR   A 1 12  ? 11.95165  -24.00641 -32.50199 1.000 14.68560 ? 19  THR   A CA  1 
ATOM   28   C  C   . THR   A 1 12  ? 12.94588  -22.85670 -32.45075 1.000 13.94415 ? 19  THR   A C   1 
ATOM   29   O  O   . THR   A 1 12  ? 13.83553  -22.76284 -33.30304 1.000 13.77158 ? 19  THR   A O   1 
ATOM   30   C  CB  . THR   A 1 12  ? 12.63204  -25.31143 -32.08501 1.000 16.91405 ? 19  THR   A CB  1 
ATOM   31   O  OG1 . THR   A 1 12  ? 11.70821  -26.39820 -32.22413 1.000 18.58617 ? 19  THR   A OG1 1 
ATOM   32   C  CG2 . THR   A 1 12  ? 13.10337  -25.22795 -30.63995 1.000 15.96370 ? 19  THR   A CG2 1 
ATOM   33   N  N   . PHE   A 1 13  ? 12.79381  -21.99625 -31.44845 1.000 15.64954 ? 20  PHE   A N   1 
ATOM   34   C  CA  . PHE   A 1 13  ? 13.59016  -20.79139 -31.28946 1.000 14.51919 ? 20  PHE   A CA  1 
ATOM   35   C  C   . PHE   A 1 13  ? 14.29278  -20.82043 -29.94152 1.000 18.83822 ? 20  PHE   A C   1 
ATOM   36   O  O   . PHE   A 1 13  ? 13.77044  -21.36902 -28.96788 1.000 15.91930 ? 20  PHE   A O   1 
ATOM   37   C  CB  . PHE   A 1 13  ? 12.71543  -19.53395 -31.33932 1.000 13.52720 ? 20  PHE   A CB  1 
ATOM   38   C  CG  . PHE   A 1 13  ? 11.97419  -19.34080 -32.62864 1.000 15.79768 ? 20  PHE   A CG  1 
ATOM   39   C  CD1 . PHE   A 1 13  ? 10.74100  -19.94565 -32.83093 1.000 17.65696 ? 20  PHE   A CD1 1 
ATOM   40   C  CD2 . PHE   A 1 13  ? 12.48001  -18.50904 -33.61738 1.000 17.90824 ? 20  PHE   A CD2 1 
ATOM   41   C  CE1 . PHE   A 1 13  ? 10.04054  -19.75056 -34.00730 1.000 17.09613 ? 20  PHE   A CE1 1 
ATOM   42   C  CE2 . PHE   A 1 13  ? 11.78487  -18.30994 -34.79580 1.000 19.80726 ? 20  PHE   A CE2 1 
ATOM   43   C  CZ  . PHE   A 1 13  ? 10.56322  -18.93266 -34.99013 1.000 19.23410 ? 20  PHE   A CZ  1 
ATOM   44   N  N   . ALA   A 1 14  ? 15.46356  -20.19468 -29.87571 1.000 12.37213 ? 21  ALA   A N   1 
ATOM   45   C  CA  . ALA   A 1 14  ? 16.12263  -19.95730 -28.60046 1.000 12.35598 ? 21  ALA   A CA  1 
ATOM   46   C  C   . ALA   A 1 14  ? 15.64432  -18.63298 -28.01530 1.000 16.70478 ? 21  ALA   A C   1 
ATOM   47   O  O   . ALA   A 1 14  ? 15.52820  -17.63283 -28.73082 1.000 15.00883 ? 21  ALA   A O   1 
ATOM   48   C  CB  . ALA   A 1 14  ? 17.64500  -19.93919 -28.76664 1.000 15.53670 ? 21  ALA   A CB  1 
ATOM   49   N  N   . PHE   A 1 15  ? 15.34417  -18.63457 -26.71557 1.000 14.89860 ? 22  PHE   A N   1 
ATOM   50   C  CA  . PHE   A 1 15  ? 15.12631  -17.37238 -26.01899 1.000 15.25623 ? 22  PHE   A CA  1 
ATOM   51   C  C   . PHE   A 1 15  ? 16.39510  -16.53292 -26.06437 1.000 16.27986 ? 22  PHE   A C   1 
ATOM   52   O  O   . PHE   A 1 15  ? 17.51112  -17.05719 -26.00218 1.000 13.70366 ? 22  PHE   A O   1 
ATOM   53   C  CB  . PHE   A 1 15  ? 14.73813  -17.60200 -24.55281 1.000 13.70054 ? 22  PHE   A CB  1 
ATOM   54   C  CG  . PHE   A 1 15  ? 13.32277  -18.07481 -24.35115 1.000 12.65637 ? 22  PHE   A CG  1 
ATOM   55   C  CD1 . PHE   A 1 15  ? 12.25474  -17.25719 -24.68112 1.000 13.37701 ? 22  PHE   A CD1 1 
ATOM   56   C  CD2 . PHE   A 1 15  ? 13.06244  -19.32272 -23.80336 1.000 14.07606 ? 22  PHE   A CD2 1 
ATOM   57   C  CE1 . PHE   A 1 15  ? 10.94758  -17.67787 -24.48655 1.000 12.72774 ? 22  PHE   A CE1 1 
ATOM   58   C  CE2 . PHE   A 1 15  ? 11.75764  -19.75405 -23.60880 1.000 14.13087 ? 22  PHE   A CE2 1 
ATOM   59   C  CZ  . PHE   A 1 15  ? 10.69820  -18.92664 -23.95099 1.000 12.76227 ? 22  PHE   A CZ  1 
ATOM   60   N  N   . GLN   A 1 16  ? 16.22324  -15.21496 -26.17056 1.000 14.74916 ? 23  GLN   A N   1 
ATOM   61   C  CA  . GLN   A 1 16  ? 17.33370  -14.32144 -25.87018 1.000 18.10893 ? 23  GLN   A CA  1 
ATOM   62   C  C   . GLN   A 1 16  ? 17.86487  -14.62852 -24.47838 1.000 15.85998 ? 23  GLN   A C   1 
ATOM   63   O  O   . GLN   A 1 16  ? 17.11010  -15.00449 -23.57805 1.000 13.85432 ? 23  GLN   A O   1 
ATOM   64   C  CB  . GLN   A 1 16  ? 16.90045  -12.85836 -25.94858 1.000 19.27645 ? 23  GLN   A CB  1 
ATOM   65   C  CG  . GLN   A 1 16  ? 16.73007  -12.32203 -27.35059 1.000 18.88185 ? 23  GLN   A CG  1 
ATOM   66   C  CD  . GLN   A 1 16  ? 16.10822  -10.93880 -27.35391 1.000 34.77028 ? 23  GLN   A CD  1 
ATOM   67   O  OE1 . GLN   A 1 16  ? 14.91135  -10.79322 -27.13405 1.000 26.45470 ? 23  GLN   A OE1 1 
ATOM   68   N  NE2 . GLN   A 1 16  ? 16.92401  -9.91438  -27.58438 1.000 30.72466 ? 23  GLN   A NE2 1 
ATOM   69   N  N   . ALA   A 1 17  ? 19.18104  -14.47682 -24.31086 1.000 17.30201 ? 24  ALA   A N   1 
ATOM   70   C  CA  . ALA   A 1 17  ? 19.81822  -14.84428 -23.05060 1.000 21.03691 ? 24  ALA   A CA  1 
ATOM   71   C  C   . ALA   A 1 17  ? 19.15865  -14.14761 -21.86701 1.000 17.98365 ? 24  ALA   A C   1 
ATOM   72   O  O   . ALA   A 1 17  ? 18.93227  -14.76704 -20.82078 1.000 20.22491 ? 24  ALA   A O   1 
ATOM   73   C  CB  . ALA   A 1 17  ? 21.31003  -14.51714 -23.10735 1.000 19.53947 ? 24  ALA   A CB  1 
ATOM   74   N  N   . GLU   A 1 18  ? 18.82368  -12.86405 -22.01950 1.000 19.80005 ? 25  GLU   A N   1 
ATOM   75   C  CA  . GLU   A 1 18  ? 18.21997  -12.12413 -20.91530 1.000 21.13766 ? 25  GLU   A CA  1 
ATOM   76   C  C   . GLU   A 1 18  ? 16.84223  -12.66722 -20.55055 1.000 18.28280 ? 25  GLU   A C   1 
ATOM   77   O  O   . GLU   A 1 18  ? 16.46053  -12.64270 -19.37346 1.000 18.64074 ? 25  GLU   A O   1 
ATOM   78   C  CB  . GLU   A 1 18  ? 18.13694  -10.63543 -21.26258 1.000 24.56361 ? 25  GLU   A CB  1 
ATOM   79   C  CG  . GLU   A 1 18  ? 19.48653  -9.95648  -21.47935 1.000 27.98619 ? 25  GLU   A CG  1 
ATOM   80   C  CD  . GLU   A 1 18  ? 20.07728  -10.18636 -22.86288 1.000 41.17555 ? 25  GLU   A CD  1 
ATOM   81   O  OE1 . GLU   A 1 18  ? 19.47867  -10.93241 -23.66772 1.000 26.01248 ? 25  GLU   A OE1 1 
ATOM   82   O  OE2 . GLU   A 1 18  ? 21.14588  -9.60744  -23.14920 1.000 37.98447 ? 25  GLU   A OE2 1 
ATOM   83   N  N   . ILE   A 1 19  ? 16.08612  -13.16208 -21.53154 1.000 16.94594 ? 26  ILE   A N   1 
ATOM   84   C  CA  . ILE   A 1 19  ? 14.75440  -13.69162 -21.24021 1.000 16.10475 ? 26  ILE   A CA  1 
ATOM   85   C  C   . ILE   A 1 19  ? 14.86173  -15.06770 -20.59004 1.000 15.76048 ? 26  ILE   A C   1 
ATOM   86   O  O   . ILE   A 1 19  ? 14.11147  -15.39047 -19.66108 1.000 13.84694 ? 26  ILE   A O   1 
ATOM   87   C  CB  . ILE   A 1 19  ? 13.88201  -13.73030 -22.51473 1.000 14.77936 ? 26  ILE   A CB  1 
ATOM   88   C  CG1 . ILE   A 1 19  ? 13.37468  -12.33403 -22.92687 1.000 18.89302 ? 26  ILE   A CG1 1 
ATOM   89   C  CG2 . ILE   A 1 19  ? 12.67192  -14.64658 -22.31927 1.000 12.56206 ? 26  ILE   A CG2 1 
ATOM   90   C  CD1 . ILE   A 1 19  ? 14.42990  -11.25617 -23.15508 1.000 22.92819 ? 26  ILE   A CD1 1 
ATOM   91   N  N   . ALA   A 1 20  ? 15.80260  -15.89489 -21.05485 1.000 13.08354 ? 27  ALA   A N   1 
ATOM   92   C  CA  . ALA   A 1 20  ? 16.05805  -17.16576 -20.38576 1.000 17.30856 ? 27  ALA   A CA  1 
ATOM   93   C  C   . ALA   A 1 20  ? 16.43375  -16.94641 -18.92555 1.000 18.35237 ? 27  ALA   A C   1 
ATOM   94   O  O   . ALA   A 1 20  ? 15.99522  -17.69251 -18.04126 1.000 18.27219 ? 27  ALA   A O   1 
ATOM   95   C  CB  . ALA   A 1 20  ? 17.16196  -17.93175 -21.11627 1.000 15.90041 ? 27  ALA   A CB  1 
ATOM   96   N  N   . GLN   A 1 21  ? 17.23109  -15.91334 -18.65205 1.000 16.90811 ? 28  GLN   A N   1 
ATOM   97   C  CA  . GLN   A 1 21  ? 17.64166  -15.64670 -17.28040 1.000 18.00395 ? 28  GLN   A CA  1 
ATOM   98   C  C   . GLN   A 1 21  ? 16.46756  -15.13304 -16.45203 1.000 18.18046 ? 28  GLN   A C   1 
ATOM   99   O  O   . GLN   A 1 21  ? 16.35291  -15.45544 -15.26323 1.000 17.65428 ? 28  GLN   A O   1 
ATOM   100  C  CB  . GLN   A 1 21  ? 18.81568  -14.66617 -17.28841 1.000 26.06392 ? 28  GLN   A CB  1 
ATOM   101  C  CG  . GLN   A 1 21  ? 19.14706  -14.01102 -15.96542 1.000 44.21582 ? 28  GLN   A CG  1 
ATOM   102  C  CD  . GLN   A 1 21  ? 20.12457  -12.85549 -16.12183 1.000 59.30126 ? 28  GLN   A CD  1 
ATOM   103  O  OE1 . GLN   A 1 21  ? 20.11837  -12.15100 -17.13420 1.000 51.39933 ? 28  GLN   A OE1 1 
ATOM   104  N  NE2 . GLN   A 1 21  ? 20.97012  -12.65679 -15.11693 1.000 44.60466 ? 28  GLN   A NE2 1 
ATOM   105  N  N   . LEU   A 1 22  ? 15.56104  -14.37059 -17.07250 1.000 16.97969 ? 29  LEU   A N   1 
ATOM   106  C  CA  . LEU   A 1 22  ? 14.34675  -13.94940 -16.37602 1.000 19.34572 ? 29  LEU   A CA  1 
ATOM   107  C  C   . LEU   A 1 22  ? 13.47857  -15.14509 -15.99041 1.000 21.25205 ? 29  LEU   A C   1 
ATOM   108  O  O   . LEU   A 1 22  ? 12.98982  -15.22765 -14.85627 1.000 16.77966 ? 29  LEU   A O   1 
ATOM   109  C  CB  . LEU   A 1 22  ? 13.55020  -12.97183 -17.23806 1.000 15.69211 ? 29  LEU   A CB  1 
ATOM   110  C  CG  . LEU   A 1 22  ? 12.14714  -12.65438 -16.71085 1.000 19.71531 ? 29  LEU   A CG  1 
ATOM   111  C  CD1 . LEU   A 1 22  ? 12.21846  -11.73140 -15.50506 1.000 20.88124 ? 29  LEU   A CD1 1 
ATOM   112  C  CD2 . LEU   A 1 22  ? 11.27240  -12.04952 -17.81424 1.000 21.71117 ? 29  LEU   A CD2 1 
ATOM   113  N  N   . MET   A 1 23  ? 13.25854  -16.08315 -16.92001 1.000 14.89338 ? 30  MET   A N   1 
ATOM   114  C  CA  . MET   A 1 23  ? 12.40481  -17.21016 -16.55675 1.000 15.93390 ? 30  MET   A CA  1 
ATOM   115  C  C   . MET   A 1 23  ? 13.08542  -18.13955 -15.56450 1.000 17.35120 ? 30  MET   A C   1 
ATOM   116  O  O   . MET   A 1 23  ? 12.40711  -18.71988 -14.71100 1.000 16.99669 ? 30  MET   A O   1 
ATOM   117  C  CB  . MET   A 1 23  ? 11.91712  -17.98617 -17.78691 1.000 14.81303 ? 30  MET   A CB  1 
ATOM   118  C  CG  . MET   A 1 23  ? 11.38635  -17.12717 -18.93736 1.000 20.11145 ? 30  MET   A CG  1 
ATOM   119  S  SD  . MET   A 1 23  ? 11.34869  -17.96951 -20.54400 1.000 17.53597 ? 30  MET   A SD  1 
ATOM   120  C  CE  . MET   A 1 23  ? 10.20370  -19.30836 -20.19834 1.000 15.52656 ? 30  MET   A CE  1 
ATOM   121  N  N   . SER   A 1 24  ? 14.41120  -18.28161 -15.63204 1.000 14.96469 ? 31  SER   A N   1 
ATOM   122  C  CA  . SER   A 1 24  ? 15.08604  -19.08907 -14.62017 1.000 13.79813 ? 31  SER   A CA  1 
ATOM   123  C  C   . SER   A 1 24  ? 14.96729  -18.44600 -13.24268 1.000 21.50292 ? 31  SER   A C   1 
ATOM   124  O  O   . SER   A 1 24  ? 14.80237  -19.14494 -12.23450 1.000 21.88616 ? 31  SER   A O   1 
ATOM   125  C  CB  . SER   A 1 24  ? 16.55300  -19.30691 -14.99378 1.000 17.40744 ? 31  SER   A CB  1 
ATOM   126  O  OG  . SER   A 1 24  ? 17.38229  -18.34653 -14.36863 1.000 49.65699 ? 31  SER   A OG  1 
ATOM   127  N  N   . LEU   A 1 25  ? 15.02511  -17.11189 -13.18280 1.000 18.65207 ? 32  LEU   A N   1 
ATOM   128  C  CA  . LEU   A 1 25  ? 14.83593  -16.41819 -11.91189 1.000 18.40498 ? 32  LEU   A CA  1 
ATOM   129  C  C   . LEU   A 1 25  ? 13.42491  -16.62934 -11.37042 1.000 20.54728 ? 32  LEU   A C   1 
ATOM   130  O  O   . LEU   A 1 25  ? 13.24010  -16.87193 -10.17220 1.000 20.29690 ? 32  LEU   A O   1 
ATOM   131  C  CB  . LEU   A 1 25  ? 15.12127  -14.92504 -12.08050 1.000 22.99460 ? 32  LEU   A CB  1 
ATOM   132  C  CG  . LEU   A 1 25  ? 15.06595  -14.07616 -10.80604 1.000 32.71947 ? 32  LEU   A CG  1 
ATOM   133  C  CD1 . LEU   A 1 25  ? 16.25032  -13.12606 -10.74303 1.000 42.16746 ? 32  LEU   A CD1 1 
ATOM   134  C  CD2 . LEU   A 1 25  ? 13.74606  -13.31500 -10.72289 1.000 39.96204 ? 32  LEU   A CD2 1 
ATOM   135  N  N   . ILE   A 1 26  ? 12.41508  -16.51587 -12.23454 1.000 16.54807 ? 33  ILE   A N   1 
ATOM   136  C  CA  . ILE   A 1 26  ? 11.03328  -16.72299 -11.80497 1.000 18.88298 ? 33  ILE   A CA  1 
ATOM   137  C  C   . ILE   A 1 26  ? 10.83410  -18.15339 -11.31512 1.000 21.39238 ? 33  ILE   A C   1 
ATOM   138  O  O   . ILE   A 1 26  ? 10.13517  -18.39877 -10.32370 1.000 21.68535 ? 33  ILE   A O   1 
ATOM   139  C  CB  . ILE   A 1 26  ? 10.06825  -16.37110 -12.95247 1.000 13.93529 ? 33  ILE   A CB  1 
ATOM   140  C  CG1 . ILE   A 1 26  ? 10.01359  -14.85481 -13.14935 1.000 18.35732 ? 33  ILE   A CG1 1 
ATOM   141  C  CG2 . ILE   A 1 26  ? 8.67185   -16.91332 -12.67077 1.000 19.09033 ? 33  ILE   A CG2 1 
ATOM   142  C  CD1 . ILE   A 1 26  ? 9.44955   -14.43095 -14.48709 1.000 19.16720 ? 33  ILE   A CD1 1 
ATOM   143  N  N   . ILE   A 1 27  ? 11.46854  -19.11633 -11.98352 1.000 16.82027 ? 34  ILE   A N   1 
ATOM   144  C  CA  . ILE   A 1 27  ? 11.25294  -20.52228 -11.65449 1.000 21.16425 ? 34  ILE   A CA  1 
ATOM   145  C  C   . ILE   A 1 27  ? 11.97724  -20.90030 -10.36535 1.000 26.57969 ? 34  ILE   A C   1 
ATOM   146  O  O   . ILE   A 1 27  ? 11.46211  -21.68074 -9.55513  1.000 23.86664 ? 34  ILE   A O   1 
ATOM   147  C  CB  . ILE   A 1 27  ? 11.69250  -21.40324 -12.83927 1.000 22.62076 ? 34  ILE   A CB  1 
ATOM   148  C  CG1 . ILE   A 1 27  ? 10.69015  -21.28177 -13.98721 1.000 17.54046 ? 34  ILE   A CG1 1 
ATOM   149  C  CG2 . ILE   A 1 27  ? 11.86344  -22.85860 -12.41691 1.000 26.09789 ? 34  ILE   A CG2 1 
ATOM   150  C  CD1 . ILE   A 1 27  ? 11.23575  -21.75189 -15.31307 1.000 21.48065 ? 34  ILE   A CD1 1 
ATOM   151  N  N   . ASN   A 1 28  ? 13.16887  -20.34499 -10.14066 1.000 21.38020 ? 35  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 28  ? 14.04821  -20.84649 -9.08980  1.000 22.78806 ? 35  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 28  ? 14.02432  -20.03166 -7.80227  1.000 29.88949 ? 35  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 28  ? 14.41129  -20.56032 -6.75445  1.000 29.51350 ? 35  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 28  ? 15.49135  -20.91517 -9.59944  1.000 25.49077 ? 35  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 28  ? 15.64976  -21.87495 -10.75399 1.000 31.27490 ? 35  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 28  ? 15.00194  -22.92016 -10.79835 1.000 35.51396 ? 35  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 28  ? 16.51278  -21.52459 -11.70056 1.000 34.28826 ? 35  ASN   A ND2 1 
ATOM   159  N  N   . THR   A 1 29  ? 13.59725  -18.77280 -7.84244  1.000 22.10626 ? 36  THR   A N   1 
ATOM   160  C  CA  . THR   A 1 29  ? 13.60423  -17.95113 -6.63697  1.000 24.12444 ? 36  THR   A CA  1 
ATOM   161  C  C   . THR   A 1 29  ? 12.51570  -18.41037 -5.67529  1.000 28.07990 ? 36  THR   A C   1 
ATOM   162  O  O   . THR   A 1 29  ? 11.36243  -18.59578 -6.07362  1.000 26.31035 ? 36  THR   A O   1 
ATOM   163  C  CB  . THR   A 1 29  ? 13.39695  -16.47894 -6.99488  1.000 29.57138 ? 36  THR   A CB  1 
ATOM   164  O  OG1 . THR   A 1 29  ? 14.44156  -16.04812 -7.87755  1.000 25.88991 ? 36  THR   A OG1 1 
ATOM   165  C  CG2 . THR   A 1 29  ? 13.39987  -15.60829 -5.74220  1.000 28.06698 ? 36  THR   A CG2 1 
ATOM   166  N  N   . PHE   A 1 30  ? 12.87751  -18.59844 -4.40734  1.000 21.72217 ? 37  PHE   A N   1 
ATOM   167  C  CA  . PHE   A 1 30  ? 11.86474  -18.86997 -3.39552  1.000 25.12957 ? 37  PHE   A CA  1 
ATOM   168  C  C   . PHE   A 1 30  ? 11.00257  -17.62998 -3.20025  1.000 24.23092 ? 37  PHE   A C   1 
ATOM   169  O  O   . PHE   A 1 30  ? 11.50593  -16.56762 -2.81824  1.000 23.75962 ? 37  PHE   A O   1 
ATOM   170  C  CB  . PHE   A 1 30  ? 12.49748  -19.28912 -2.07285  1.000 24.68065 ? 37  PHE   A CB  1 
ATOM   171  C  CG  . PHE   A 1 30  ? 11.48566  -19.59537 -1.00297  1.000 28.18954 ? 37  PHE   A CG  1 
ATOM   172  C  CD1 . PHE   A 1 30  ? 10.73306  -20.75845 -1.05364  1.000 32.50811 ? 37  PHE   A CD1 1 
ATOM   173  C  CD2 . PHE   A 1 30  ? 11.26402  -18.70596 0.03761   1.000 28.79885 ? 37  PHE   A CD2 1 
ATOM   174  C  CE1 . PHE   A 1 30  ? 9.78803   -21.03721 -0.07416  1.000 28.63631 ? 37  PHE   A CE1 1 
ATOM   175  C  CE2 . PHE   A 1 30  ? 10.31923  -18.97898 1.01911   1.000 29.11494 ? 37  PHE   A CE2 1 
ATOM   176  C  CZ  . PHE   A 1 30  ? 9.58320   -20.14577 0.96219   1.000 25.57687 ? 37  PHE   A CZ  1 
ATOM   177  N  N   . TYR   A 1 31  ? 9.69957   -17.76747 -3.45131  1.000 19.37336 ? 38  TYR   A N   1 
ATOM   178  C  CA  . TYR   A 1 31  ? 8.80725   -16.61299 -3.44784  1.000 18.67101 ? 38  TYR   A CA  1 
ATOM   179  C  C   . TYR   A 1 31  ? 7.37461   -17.13718 -3.32479  1.000 17.92514 ? 38  TYR   A C   1 
ATOM   180  O  O   . TYR   A 1 31  ? 6.81325   -17.64149 -4.30025  1.000 17.40800 ? 38  TYR   A O   1 
ATOM   181  C  CB  . TYR   A 1 31  ? 9.00306   -15.78103 -4.70470  1.000 19.66618 ? 38  TYR   A CB  1 
ATOM   182  C  CG  . TYR   A 1 31  ? 8.01773   -14.65702 -4.81627  1.000 25.39183 ? 38  TYR   A CG  1 
ATOM   183  C  CD1 . TYR   A 1 31  ? 8.13251   -13.53071 -4.01464  1.000 27.19702 ? 38  TYR   A CD1 1 
ATOM   184  C  CD2 . TYR   A 1 31  ? 6.95897   -14.72771 -5.70790  1.000 20.92709 ? 38  TYR   A CD2 1 
ATOM   185  C  CE1 . TYR   A 1 31  ? 7.22267   -12.50189 -4.10108  1.000 35.34843 ? 38  TYR   A CE1 1 
ATOM   186  C  CE2 . TYR   A 1 31  ? 6.04440   -13.70442 -5.80232  1.000 20.00283 ? 38  TYR   A CE2 1 
ATOM   187  C  CZ  . TYR   A 1 31  ? 6.18185   -12.59528 -4.99746  1.000 28.20697 ? 38  TYR   A CZ  1 
ATOM   188  O  OH  . TYR   A 1 31  ? 5.27088   -11.57523 -5.08942  1.000 39.86688 ? 38  TYR   A OH  1 
ATOM   189  N  N   . SER   A 1 32  ? 6.79908   -17.00842 -2.12876  1.000 18.86979 ? 39  SER   A N   1 
ATOM   190  C  CA  . SER   A 1 32  ? 5.54198   -17.68080 -1.82284  1.000 18.68051 ? 39  SER   A CA  1 
ATOM   191  C  C   . SER   A 1 32  ? 4.32610   -17.02075 -2.46453  1.000 23.05352 ? 39  SER   A C   1 
ATOM   192  O  O   . SER   A 1 32  ? 3.30673   -17.69351 -2.65013  1.000 23.73672 ? 39  SER   A O   1 
ATOM   193  C  CB  . SER   A 1 32  ? 5.34371   -17.74675 -0.30837  1.000 20.25594 ? 39  SER   A CB  1 
ATOM   194  O  OG  . SER   A 1 32  ? 6.36095   -18.52182 0.30141   1.000 21.67435 ? 39  SER   A OG  1 
ATOM   195  N  N   . ASN   A 1 33  ? 4.40539   -15.73570 -2.81318  1.000 17.25181 ? 40  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 33  ? 3.23683   -14.97175 -3.26067  1.000 19.81250 ? 40  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 33  ? 2.97352   -15.20241 -4.75549  1.000 17.58081 ? 40  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 33  ? 2.95845   -14.28597 -5.57842  1.000 16.98064 ? 40  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 33  ? 3.44412   -13.49611 -2.93505  1.000 23.51887 ? 40  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 33  ? 2.24880   -12.63084 -3.30307  1.000 32.54521 ? 40  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 33  ? 1.09845   -13.04085 -3.15692  1.000 26.32636 ? 40  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 33  ? 2.52140   -11.41704 -3.76583  1.000 26.09060 ? 40  ASN   A ND2 1 
ATOM   203  N  N   . LYS   A 1 34  ? 2.74319   -16.47382 -5.09911  1.000 17.22208 ? 41  LYS   A N   1 
ATOM   204  C  CA  . LYS   A 1 34  ? 2.63819   -16.86465 -6.50115  1.000 16.13759 ? 41  LYS   A CA  1 
ATOM   205  C  C   . LYS   A 1 34  ? 1.34527   -16.39303 -7.15495  1.000 16.03772 ? 41  LYS   A C   1 
ATOM   206  O  O   . LYS   A 1 34  ? 1.28816   -16.31532 -8.38711  1.000 14.27877 ? 41  LYS   A O   1 
ATOM   207  C  CB  . LYS   A 1 34  ? 2.74885   -18.38631 -6.63608  1.000 17.84429 ? 41  LYS   A CB  1 
ATOM   208  C  CG  . LYS   A 1 34  ? 4.12376   -18.97115 -6.30174  1.000 18.16562 ? 41  LYS   A CG  1 
ATOM   209  C  CD  . LYS   A 1 34  ? 4.09242   -20.49619 -6.35519  1.000 21.50512 ? 41  LYS   A CD  1 
ATOM   210  C  CE  . LYS   A 1 34  ? 5.49037   -21.11170 -6.21800  1.000 19.11911 ? 41  LYS   A CE  1 
ATOM   211  N  NZ  . LYS   A 1 34  ? 6.32209   -20.92558 -7.44231  1.000 19.80904 ? 41  LYS   A NZ  1 
ATOM   212  N  N   . GLU   A 1 35  ? 0.31477   -16.07151 -6.36683  1.000 15.32852 ? 42  GLU   A N   1 
ATOM   213  C  CA  . GLU   A 1 35  ? -1.00088  -15.78902 -6.93463  1.000 16.74563 ? 42  GLU   A CA  1 
ATOM   214  C  C   . GLU   A 1 35  ? -0.99815  -14.59110 -7.87565  1.000 20.12664 ? 42  GLU   A C   1 
ATOM   215  O  O   . GLU   A 1 35  ? -1.93688  -14.44208 -8.66541  1.000 17.69475 ? 42  GLU   A O   1 
ATOM   216  C  CB  . GLU   A 1 35  ? -2.02667  -15.54331 -5.82594  1.000 15.97230 ? 42  GLU   A CB  1 
ATOM   217  C  CG  . GLU   A 1 35  ? -1.81053  -14.24679 -5.06615  1.000 17.39619 ? 42  GLU   A CG  1 
ATOM   218  C  CD  . GLU   A 1 35  ? -2.72809  -14.10733 -3.86427  1.000 31.72921 ? 42  GLU   A CD  1 
ATOM   219  O  OE1 . GLU   A 1 35  ? -2.88497  -15.08921 -3.11026  1.000 26.42072 ? 42  GLU   A OE1 1 
ATOM   220  O  OE2 . GLU   A 1 35  ? -3.29548  -13.00959 -3.67731  1.000 32.83886 ? 42  GLU   A OE2 1 
ATOM   221  N  N   . ILE   A 1 36  ? 0.02599   -13.73515 -7.81455  1.000 16.27926 ? 43  ILE   A N   1 
ATOM   222  C  CA  . ILE   A 1 36  ? 0.05009   -12.53774 -8.64705  1.000 14.99682 ? 43  ILE   A CA  1 
ATOM   223  C  C   . ILE   A 1 36  ? 0.13534   -12.85315 -10.13471 1.000 15.55659 ? 43  ILE   A C   1 
ATOM   224  O  O   . ILE   A 1 36  ? -0.09320  -11.95989 -10.95803 1.000 13.28211 ? 43  ILE   A O   1 
ATOM   225  C  CB  . ILE   A 1 36  ? 1.20695   -11.60910 -8.21582  1.000 17.72029 ? 43  ILE   A CB  1 
ATOM   226  C  CG1 . ILE   A 1 36  ? 2.56357   -12.30572 -8.36198  1.000 20.59937 ? 43  ILE   A CG1 1 
ATOM   227  C  CG2 . ILE   A 1 36  ? 0.98926   -11.11947 -6.79224  1.000 21.72596 ? 43  ILE   A CG2 1 
ATOM   228  C  CD1 . ILE   A 1 36  ? 3.29631   -11.97326 -9.65716  1.000 26.32374 ? 43  ILE   A CD1 1 
ATOM   229  N  N   . PHE   A 1 37  ? 0.46168   -14.09769 -10.50843 1.000 13.17403 ? 44  PHE   A N   1 
ATOM   230  C  CA  . PHE   A 1 37  ? 0.47515   -14.45845 -11.92568 1.000 13.99334 ? 44  PHE   A CA  1 
ATOM   231  C  C   . PHE   A 1 37  ? -0.86409  -14.13635 -12.58512 1.000 15.29731 ? 44  PHE   A C   1 
ATOM   232  O  O   . PHE   A 1 37  ? -0.91208  -13.70243 -13.74198 1.000 11.59388 ? 44  PHE   A O   1 
ATOM   233  C  CB  . PHE   A 1 37  ? 0.80635   -15.94867 -12.09936 1.000 13.40833 ? 44  PHE   A CB  1 
ATOM   234  C  CG  . PHE   A 1 37  ? -0.38055  -16.85350 -11.91321 1.000 14.71190 ? 44  PHE   A CG  1 
ATOM   235  C  CD1 . PHE   A 1 37  ? -0.73649  -17.29970 -10.65247 1.000 13.82162 ? 44  PHE   A CD1 1 
ATOM   236  C  CD2 . PHE   A 1 37  ? -1.16726  -17.22772 -12.99775 1.000 18.58436 ? 44  PHE   A CD2 1 
ATOM   237  C  CE1 . PHE   A 1 37  ? -1.85173  -18.11683 -10.47554 1.000 15.76347 ? 44  PHE   A CE1 1 
ATOM   238  C  CE2 . PHE   A 1 37  ? -2.28181  -18.03417 -12.82226 1.000 14.82804 ? 44  PHE   A CE2 1 
ATOM   239  C  CZ  . PHE   A 1 37  ? -2.62017  -18.48020 -11.56278 1.000 12.41504 ? 44  PHE   A CZ  1 
ATOM   240  N  N   . LEU   A 1 38  ? -1.96620  -14.34600 -11.86256 1.000 12.72525 ? 45  LEU   A N   1 
ATOM   241  C  CA  . LEU   A 1 38  ? -3.27860  -14.16135 -12.46983 1.000 11.23073 ? 45  LEU   A CA  1 
ATOM   242  C  C   . LEU   A 1 38  ? -3.57657  -12.68264 -12.67770 1.000 15.56709 ? 45  LEU   A C   1 
ATOM   243  O  O   . LEU   A 1 38  ? -4.11628  -12.29250 -13.72094 1.000 15.28655 ? 45  LEU   A O   1 
ATOM   244  C  CB  . LEU   A 1 38  ? -4.35075  -14.82503 -11.60747 1.000 11.60615 ? 45  LEU   A CB  1 
ATOM   245  C  CG  . LEU   A 1 38  ? -5.77307  -14.80776 -12.16975 1.000 12.53350 ? 45  LEU   A CG  1 
ATOM   246  C  CD1 . LEU   A 1 38  ? -5.81112  -15.49638 -13.52568 1.000 12.64969 ? 45  LEU   A CD1 1 
ATOM   247  C  CD2 . LEU   A 1 38  ? -6.71952  -15.49537 -11.20107 1.000 17.98426 ? 45  LEU   A CD2 1 
ATOM   248  N  N   . ARG   A 1 39  ? -3.22030  -11.84701 -11.69669 1.000 12.83593 ? 46  ARG   A N   1 
ATOM   249  C  CA  . ARG   A 1 39  ? -3.32818  -10.40125 -11.86296 1.000 15.36114 ? 46  ARG   A CA  1 
ATOM   250  C  C   . ARG   A 1 39  ? -2.56837  -9.93217  -13.09605 1.000 18.03466 ? 46  ARG   A C   1 
ATOM   251  O  O   . ARG   A 1 39  ? -3.06961  -9.10598  -13.86956 1.000 14.12262 ? 46  ARG   A O   1 
ATOM   252  C  CB  . ARG   A 1 39  ? -2.79619  -9.69507  -10.61581 1.000 16.66083 ? 46  ARG   A CB  1 
ATOM   253  C  CG  . ARG   A 1 39  ? -2.78514  -8.18364  -10.71591 1.000 21.22105 ? 46  ARG   A CG  1 
ATOM   254  C  CD  . ARG   A 1 39  ? -2.05255  -7.55448  -9.54338  1.000 23.96362 ? 46  ARG   A CD  1 
ATOM   255  N  NE  . ARG   A 1 39  ? -0.61207  -7.76933  -9.62769  1.000 26.38393 ? 46  ARG   A NE  1 
ATOM   256  C  CZ  . ARG   A 1 39  ? 0.22521   -7.65200  -8.60590  1.000 31.71112 ? 46  ARG   A CZ  1 
ATOM   257  N  NH1 . ARG   A 1 39  ? -0.19682  -7.29727  -7.40315  1.000 27.00834 ? 46  ARG   A NH1 1 
ATOM   258  N  NH2 . ARG   A 1 39  ? 1.51958   -7.89307  -8.79639  1.000 28.64612 ? 46  ARG   A NH2 1 
ATOM   259  N  N   . GLU   A 1 40  ? -1.35582  -10.45530 -13.29749 1.000 13.36354 ? 47  GLU   A N   1 
ATOM   260  C  CA  . GLU   A 1 40  ? -0.52539  -9.99930  -14.40620 1.000 13.48482 ? 47  GLU   A CA  1 
ATOM   261  C  C   . GLU   A 1 40  ? -1.11481  -10.40853 -15.75056 1.000 14.08954 ? 47  GLU   A C   1 
ATOM   262  O  O   . GLU   A 1 40  ? -1.07522  -9.63185  -16.71135 1.000 12.41384 ? 47  GLU   A O   1 
ATOM   263  C  CB  . GLU   A 1 40  ? 0.89742   -10.54251 -14.25437 1.000 14.23120 ? 47  GLU   A CB  1 
ATOM   264  C  CG  . GLU   A 1 40  ? 1.65229   -10.02438 -13.03294 1.000 14.80750 ? 47  GLU   A CG  1 
ATOM   265  C  CD  . GLU   A 1 40  ? 1.57833   -8.51305  -12.88648 1.000 23.44330 ? 47  GLU   A CD  1 
ATOM   266  O  OE1 . GLU   A 1 40  ? 1.68532   -7.80292  -13.90964 1.000 20.70812 ? 47  GLU   A OE1 1 
ATOM   267  O  OE2 . GLU   A 1 40  ? 1.42234   -8.03605  -11.74127 1.000 31.07851 ? 47  GLU   A OE2 1 
ATOM   268  N  N   . LEU   A 1 41  ? -1.65650  -11.62628 -15.84572 1.000 11.16808 ? 48  LEU   A N   1 
ATOM   269  C  CA  . LEU   A 1 41  ? -2.21326  -12.08047 -17.11806 1.000 12.68860 ? 48  LEU   A CA  1 
ATOM   270  C  C   . LEU   A 1 41  ? -3.52607  -11.37403 -17.43158 1.000 14.07446 ? 48  LEU   A C   1 
ATOM   271  O  O   . LEU   A 1 41  ? -3.80606  -11.05617 -18.59391 1.000 14.44863 ? 48  LEU   A O   1 
ATOM   272  C  CB  . LEU   A 1 41  ? -2.40898  -13.59683 -17.09735 1.000 10.97026 ? 48  LEU   A CB  1 
ATOM   273  C  CG  . LEU   A 1 41  ? -1.11570  -14.41500 -17.03482 1.000 13.56114 ? 48  LEU   A CG  1 
ATOM   274  C  CD1 . LEU   A 1 41  ? -1.42253  -15.90881 -16.95540 1.000 12.51701 ? 48  LEU   A CD1 1 
ATOM   275  C  CD2 . LEU   A 1 41  ? -0.22409  -14.10997 -18.22677 1.000 12.57661 ? 48  LEU   A CD2 1 
ATOM   276  N  N   . ILE   A 1 42  ? -4.35128  -11.13481 -16.41264 1.000 10.83795 ? 49  ILE   A N   1 
ATOM   277  C  CA  . ILE   A 1 42  ? -5.58398  -10.38463 -16.62823 1.000 13.01607 ? 49  ILE   A CA  1 
ATOM   278  C  C   . ILE   A 1 42  ? -5.26482  -8.95453  -17.04697 1.000 13.32645 ? 49  ILE   A C   1 
ATOM   279  O  O   . ILE   A 1 42  ? -5.94686  -8.37167  -17.90178 1.000 14.78499 ? 49  ILE   A O   1 
ATOM   280  C  CB  . ILE   A 1 42  ? -6.46553  -10.43566 -15.36494 1.000 13.45450 ? 49  ILE   A CB  1 
ATOM   281  C  CG1 . ILE   A 1 42  ? -7.03483  -11.84796 -15.17923 1.000 12.45456 ? 49  ILE   A CG1 1 
ATOM   282  C  CG2 . ILE   A 1 42  ? -7.59141  -9.40782  -15.44578 1.000 11.30619 ? 49  ILE   A CG2 1 
ATOM   283  C  CD1 . ILE   A 1 42  ? -7.78545  -12.04512 -13.86696 1.000 16.84016 ? 49  ILE   A CD1 1 
ATOM   284  N  N   . SER   A 1 43  ? -4.21187  -8.37080  -16.46765 1.000 12.25128 ? 50  SER   A N   1 
ATOM   285  C  CA  . SER   A 1 43  ? -3.83668  -7.01566  -16.85076 1.000 15.38014 ? 50  SER   A CA  1 
ATOM   286  C  C   . SER   A 1 43  ? -3.33220  -6.98062  -18.28908 1.000 16.43847 ? 50  SER   A C   1 
ATOM   287  O  O   . SER   A 1 43  ? -3.63028  -6.03964  -19.03383 1.000 12.55578 ? 50  SER   A O   1 
ATOM   288  C  CB  . SER   A 1 43  ? -2.78915  -6.46259  -15.87879 1.000 16.13976 ? 50  SER   A CB  1 
ATOM   289  O  OG  . SER   A 1 43  ? -2.16906  -5.30020  -16.40083 1.000 26.63532 ? 50  SER   A OG  1 
ATOM   290  N  N   . ASN   A 1 44  ? -2.57289  -8.00233  -18.69928 1.000 13.94386 ? 51  ASN   A N   1 
ATOM   291  C  CA  . ASN   A 1 44  ? -2.17682  -8.11727  -20.09955 1.000 16.41405 ? 51  ASN   A CA  1 
ATOM   292  C  C   . ASN   A 1 44  ? -3.39600  -8.21120  -21.00484 1.000 14.56219 ? 51  ASN   A C   1 
ATOM   293  O  O   . ASN   A 1 44  ? -3.44131  -7.58161  -22.06776 1.000 11.57967 ? 51  ASN   A O   1 
ATOM   294  C  CB  . ASN   A 1 44  ? -1.29388  -9.34707  -20.29880 1.000 14.46039 ? 51  ASN   A CB  1 
ATOM   295  C  CG  . ASN   A 1 44  ? 0.10750   -9.15032  -19.78223 1.000 24.72449 ? 51  ASN   A CG  1 
ATOM   296  O  OD1 . ASN   A 1 44  ? 0.48127   -8.06094  -19.34211 1.000 18.93788 ? 51  ASN   A OD1 1 
ATOM   297  N  ND2 . ASN   A 1 44  ? 0.89599   -10.21345 -19.82734 1.000 18.11116 ? 51  ASN   A ND2 1 
ATOM   298  N  N   . SER   A 1 45  ? -4.38364  -9.01844  -20.61040 1.000 10.94918 ? 52  SER   A N   1 
ATOM   299  C  CA  . SER   A 1 45  ? -5.61059  -9.13285  -21.39186 1.000 13.09717 ? 52  SER   A CA  1 
ATOM   300  C  C   . SER   A 1 45  ? -6.32111  -7.78710  -21.48921 1.000 13.15570 ? 52  SER   A C   1 
ATOM   301  O  O   . SER   A 1 45  ? -6.79174  -7.39531  -22.56462 1.000 13.55449 ? 52  SER   A O   1 
ATOM   302  C  CB  . SER   A 1 45  ? -6.52818  -10.18713 -20.76861 1.000 10.98934 ? 52  SER   A CB  1 
ATOM   303  O  OG  . SER   A 1 45  ? -6.01549  -11.49795 -20.95076 1.000 14.57113 ? 52  SER   A OG  1 
ATOM   304  N  N   . SER   A 1 46  ? -6.40947  -7.06493  -20.36749 1.000 11.43786 ? 53  SER   A N   1 
ATOM   305  C  CA  . SER   A 1 46  ? -7.04524  -5.74942  -20.37991 1.000 14.22259 ? 53  SER   A CA  1 
ATOM   306  C  C   . SER   A 1 46  ? -6.32370  -4.79214  -21.32431 1.000 16.31741 ? 53  SER   A C   1 
ATOM   307  O  O   . SER   A 1 46  ? -6.96734  -4.03439  -22.06062 1.000 13.76680 ? 53  SER   A O   1 
ATOM   308  C  CB  . SER   A 1 46  ? -7.08998  -5.17546  -18.96327 1.000 12.66672 ? 53  SER   A CB  1 
ATOM   309  O  OG  . SER   A 1 46  ? -7.68819  -3.88671  -18.95143 1.000 18.13771 ? 53  SER   A OG  1 
ATOM   310  N  N   . ASP   A 1 47  ? -4.98606  -4.80882  -21.31439 1.000 14.49586 ? 54  ASP   A N   1 
ATOM   311  C  CA  . ASP   A 1 47  ? -4.22401  -3.96519  -22.23400 1.000 12.61966 ? 54  ASP   A CA  1 
ATOM   312  C  C   . ASP   A 1 47  ? -4.52450  -4.31390  -23.68702 1.000 14.53805 ? 54  ASP   A C   1 
ATOM   313  O  O   . ASP   A 1 47  ? -4.64739  -3.42141  -24.53375 1.000 14.17996 ? 54  ASP   A O   1 
ATOM   314  C  CB  . ASP   A 1 47  ? -2.72423  -4.10037  -21.96468 1.000 13.83904 ? 54  ASP   A CB  1 
ATOM   315  C  CG  . ASP   A 1 47  ? -2.29490  -3.44420  -20.66298 1.000 23.55971 ? 54  ASP   A CG  1 
ATOM   316  O  OD1 . ASP   A 1 47  ? -3.09888  -2.69780  -20.06375 1.000 24.20885 ? 54  ASP   A OD1 1 
ATOM   317  O  OD2 . ASP   A 1 47  ? -1.14142  -3.67111  -20.24147 1.000 20.44730 ? 54  ASP   A OD2 1 
ATOM   318  N  N   . ALA   A 1 48  ? -4.63290  -5.61015  -23.99592 1.000 12.07145 ? 55  ALA   A N   1 
ATOM   319  C  CA  . ALA   A 1 48  ? -4.90538  -6.03332  -25.36639 1.000 13.70993 ? 55  ALA   A CA  1 
ATOM   320  C  C   . ALA   A 1 48  ? -6.32100  -5.66258  -25.78445 1.000 13.47384 ? 55  ALA   A C   1 
ATOM   321  O  O   . ALA   A 1 48  ? -6.56887  -5.34159  -26.95218 1.000 12.80599 ? 55  ALA   A O   1 
ATOM   322  C  CB  . ALA   A 1 48  ? -4.68765  -7.54119  -25.50491 1.000 12.49682 ? 55  ALA   A CB  1 
ATOM   323  N  N   . LEU   A 1 49  ? -7.26545  -5.71660  -24.84646 1.000 11.81811 ? 56  LEU   A N   1 
ATOM   324  C  CA  . LEU   A 1 49  ? -8.62408  -5.29113  -25.14909 1.000 12.00170 ? 56  LEU   A CA  1 
ATOM   325  C  C   . LEU   A 1 49  ? -8.68932  -3.78315  -25.35872 1.000 12.40711 ? 56  LEU   A C   1 
ATOM   326  O  O   . LEU   A 1 49  ? -9.42940  -3.30603  -26.22621 1.000 13.52745 ? 56  LEU   A O   1 
ATOM   327  C  CB  . LEU   A 1 49  ? -9.56443  -5.73842  -24.03205 1.000 13.65142 ? 56  LEU   A CB  1 
ATOM   328  C  CG  . LEU   A 1 49  ? -9.81079  -7.25162  -24.01164 1.000 11.93778 ? 56  LEU   A CG  1 
ATOM   329  C  CD1 . LEU   A 1 49  ? -10.19532 -7.71646  -22.61880 1.000 15.60020 ? 56  LEU   A CD1 1 
ATOM   330  C  CD2 . LEU   A 1 49  ? -10.88612 -7.63477  -25.02336 1.000 12.86181 ? 56  LEU   A CD2 1 
ATOM   331  N  N   . ASP   A 1 50  ? -7.92077  -3.01768  -24.57537 1.000 12.49280 ? 57  ASP   A N   1 
ATOM   332  C  CA  . ASP   A 1 50  ? -7.84124  -1.57598  -24.79776 1.000 14.70971 ? 57  ASP   A CA  1 
ATOM   333  C  C   . ASP   A 1 50  ? -7.37168  -1.26650  -26.21361 1.000 16.95403 ? 57  ASP   A C   1 
ATOM   334  O  O   . ASP   A 1 50  ? -7.85857  -0.32270  -26.84793 1.000 14.38847 ? 57  ASP   A O   1 
ATOM   335  C  CB  . ASP   A 1 50  ? -6.88976  -0.92899  -23.78712 1.000 13.82325 ? 57  ASP   A CB  1 
ATOM   336  C  CG  . ASP   A 1 50  ? -7.45787  -0.87888  -22.38521 1.000 21.79596 ? 57  ASP   A CG  1 
ATOM   337  O  OD1 . ASP   A 1 50  ? -8.64020  -1.23721  -22.19197 1.000 19.31383 ? 57  ASP   A OD1 1 
ATOM   338  O  OD2 . ASP   A 1 50  ? -6.71251  -0.47015  -21.47333 1.000 20.03057 ? 57  ASP   A OD2 1 
ATOM   339  N  N   . LYS   A 1 51  ? -6.41983  -2.05293  -26.72326 1.000 15.18900 ? 58  LYS   A N   1 
ATOM   340  C  CA  . LYS   A 1 51  ? -5.82835  -1.75985  -28.02357 1.000 14.58001 ? 58  LYS   A CA  1 
ATOM   341  C  C   . LYS   A 1 51  ? -6.83835  -1.94877  -29.14625 1.000 15.34802 ? 58  LYS   A C   1 
ATOM   342  O  O   . LYS   A 1 51  ? -6.94683  -1.10387  -30.04153 1.000 16.31585 ? 58  LYS   A O   1 
ATOM   343  C  CB  . LYS   A 1 51  ? -4.59755  -2.63816  -28.24867 1.000 15.06158 ? 58  LYS   A CB  1 
ATOM   344  C  CG  . LYS   A 1 51  ? -3.37587  -2.19474  -27.45782 1.000 20.14935 ? 58  LYS   A CG  1 
ATOM   345  C  CD  . LYS   A 1 51  ? -2.25058  -3.21790  -27.56786 1.000 18.67846 ? 58  LYS   A CD  1 
ATOM   346  C  CE  . LYS   A 1 51  ? -1.17746  -2.97354  -26.51620 1.000 29.52473 ? 58  LYS   A CE  1 
ATOM   347  N  NZ  . LYS   A 1 51  ? -0.01845  -3.89477  -26.68680 1.000 34.98390 ? 58  LYS   A NZ  1 
ATOM   348  N  N   . ILE   A 1 52  ? -7.58446  -3.05502  -29.12393 1.000 15.14295 ? 59  ILE   A N   1 
ATOM   349  C  CA  . ILE   A 1 52  ? -8.54847  -3.27763  -30.19630 1.000 14.77648 ? 59  ILE   A CA  1 
ATOM   350  C  C   . ILE   A 1 52  ? -9.72908  -2.32330  -30.06643 1.000 15.03088 ? 59  ILE   A C   1 
ATOM   351  O  O   . ILE   A 1 52  ? -10.30010 -1.89935  -31.07873 1.000 15.66879 ? 59  ILE   A O   1 
ATOM   352  C  CB  . ILE   A 1 52  ? -8.99673  -4.75295  -30.24547 1.000 14.82509 ? 59  ILE   A CB  1 
ATOM   353  C  CG1 . ILE   A 1 52  ? -9.80720  -5.02104  -31.52063 1.000 18.20603 ? 59  ILE   A CG1 1 
ATOM   354  C  CG2 . ILE   A 1 52  ? -9.81308  -5.13385  -29.01294 1.000 14.11033 ? 59  ILE   A CG2 1 
ATOM   355  C  CD1 . ILE   A 1 52  ? -9.03956  -4.76496  -32.80567 1.000 20.04690 ? 59  ILE   A CD1 1 
ATOM   356  N  N   . ARG   A 1 53  ? -10.10228 -1.94093  -28.84118 1.000 14.99814 ? 60  ARG   A N   1 
ATOM   357  C  CA  . ARG   A 1 53  ? -11.15383 -0.93760  -28.69014 1.000 21.23830 ? 60  ARG   A CA  1 
ATOM   358  C  C   . ARG   A 1 53  ? -10.73450 0.39857   -29.29051 1.000 20.43847 ? 60  ARG   A C   1 
ATOM   359  O  O   . ARG   A 1 53  ? -11.51906 1.04670   -29.99410 1.000 17.09333 ? 60  ARG   A O   1 
ATOM   360  C  CB  . ARG   A 1 53  ? -11.54503 -0.75333  -27.22310 1.000 19.53738 ? 60  ARG   A CB  1 
ATOM   361  C  CG  . ARG   A 1 53  ? -12.54569 0.39303   -27.08511 1.000 29.58661 ? 60  ARG   A CG  1 
ATOM   362  C  CD  . ARG   A 1 53  ? -13.09651 0.61494   -25.69249 1.000 41.13515 ? 60  ARG   A CD  1 
ATOM   363  N  NE  . ARG   A 1 53  ? -14.10462 -0.36299  -25.30277 1.000 42.27942 ? 60  ARG   A NE  1 
ATOM   364  C  CZ  . ARG   A 1 53  ? -14.21347 -0.87817  -24.08610 1.000 46.54629 ? 60  ARG   A CZ  1 
ATOM   365  N  NH1 . ARG   A 1 53  ? -13.35298 -0.57442  -23.12884 1.000 33.23241 ? 60  ARG   A NH1 1 
ATOM   366  N  NH2 . ARG   A 1 53  ? -15.22107 -1.70465  -23.81783 1.000 31.64133 ? 60  ARG   A NH2 1 
ATOM   367  N  N   . TYR   A 1 54  ? -9.50159  0.83823   -29.01268 1.000 16.10109 ? 61  TYR   A N   1 
ATOM   368  C  CA  . TYR   A 1 54  ? -9.04863  2.10742   -29.57078 1.000 16.66232 ? 61  TYR   A CA  1 
ATOM   369  C  C   . TYR   A 1 54  ? -9.03991  2.06693   -31.09363 1.000 19.68693 ? 61  TYR   A C   1 
ATOM   370  O  O   . TYR   A 1 54  ? -9.46872  3.02331   -31.74836 1.000 18.13737 ? 61  TYR   A O   1 
ATOM   371  C  CB  . TYR   A 1 54  ? -7.66085  2.47378   -29.04458 1.000 17.06017 ? 61  TYR   A CB  1 
ATOM   372  C  CG  . TYR   A 1 54  ? -7.21559  3.82718   -29.55107 1.000 18.71918 ? 61  TYR   A CG  1 
ATOM   373  C  CD1 . TYR   A 1 54  ? -7.76243  4.99498   -29.03523 1.000 19.53112 ? 61  TYR   A CD1 1 
ATOM   374  C  CD2 . TYR   A 1 54  ? -6.27868  3.93644   -30.57010 1.000 21.54588 ? 61  TYR   A CD2 1 
ATOM   375  C  CE1 . TYR   A 1 54  ? -7.38165  6.23119   -29.50681 1.000 21.57599 ? 61  TYR   A CE1 1 
ATOM   376  C  CE2 . TYR   A 1 54  ? -5.88669  5.17575   -31.04918 1.000 21.22450 ? 61  TYR   A CE2 1 
ATOM   377  C  CZ  . TYR   A 1 54  ? -6.44091  6.31550   -30.51318 1.000 26.10256 ? 61  TYR   A CZ  1 
ATOM   378  O  OH  . TYR   A 1 54  ? -6.05423  7.54923   -30.98579 1.000 26.55188 ? 61  TYR   A OH  1 
ATOM   379  N  N   . GLU   A 1 55  ? -8.56268  0.96347   -31.67669 1.000 16.98568 ? 62  GLU   A N   1 
ATOM   380  C  CA  . GLU   A 1 55  ? -8.53462  0.85219   -33.13207 1.000 19.00386 ? 62  GLU   A CA  1 
ATOM   381  C  C   . GLU   A 1 55  ? -9.94151  0.90244   -33.70934 1.000 21.26479 ? 62  GLU   A C   1 
ATOM   382  O  O   . GLU   A 1 55  ? -10.17318 1.52087   -34.75553 1.000 25.20299 ? 62  GLU   A O   1 
ATOM   383  C  CB  . GLU   A 1 55  ? -7.83140  -0.44125  -33.54063 1.000 18.99399 ? 62  GLU   A CB  1 
ATOM   384  C  CG  . GLU   A 1 55  ? -6.31614  -0.37884  -33.42472 1.000 25.54057 ? 62  GLU   A CG  1 
ATOM   385  C  CD  . GLU   A 1 55  ? -5.63034  -1.49605  -34.18374 1.000 35.65823 ? 62  GLU   A CD  1 
ATOM   386  O  OE1 . GLU   A 1 55  ? -6.33696  -2.40997  -34.65901 1.000 34.27280 ? 62  GLU   A OE1 1 
ATOM   387  O  OE2 . GLU   A 1 55  ? -4.38704  -1.46240  -34.30540 1.000 40.78735 ? 62  GLU   A OE2 1 
ATOM   388  N  N   . SER   A 1 56  ? -10.90020 0.27510   -33.02630 1.000 19.23994 ? 63  SER   A N   1 
ATOM   389  C  CA  . SER   A 1 56  ? -12.27286 0.25143   -33.51281 1.000 22.31535 ? 63  SER   A CA  1 
ATOM   390  C  C   . SER   A 1 56  ? -12.94031 1.61926   -33.45121 1.000 23.75413 ? 63  SER   A C   1 
ATOM   391  O  O   . SER   A 1 56  ? -13.96309 1.82128   -34.11353 1.000 19.90026 ? 63  SER   A O   1 
ATOM   392  C  CB  . SER   A 1 56  ? -13.09567 -0.75620  -32.71020 1.000 21.90720 ? 63  SER   A CB  1 
ATOM   393  O  OG  . SER   A 1 56  ? -13.37376 -0.25887  -31.41192 1.000 24.20607 ? 63  SER   A OG  1 
ATOM   394  N  N   . LEU   A 1 57  ? -12.39403 2.55928   -32.67403 1.000 19.38854 ? 64  LEU   A N   1 
ATOM   395  C  CA  . LEU   A 1 57  ? -13.02935 3.86927   -32.55000 1.000 26.69810 ? 64  LEU   A CA  1 
ATOM   396  C  C   . LEU   A 1 57  ? -13.05814 4.61417   -33.87759 1.000 29.77123 ? 64  LEU   A C   1 
ATOM   397  O  O   . LEU   A 1 57  ? -13.97649 5.40401   -34.12609 1.000 29.65190 ? 64  LEU   A O   1 
ATOM   398  C  CB  . LEU   A 1 57  ? -12.31278 4.70853   -31.49232 1.000 23.35042 ? 64  LEU   A CB  1 
ATOM   399  C  CG  . LEU   A 1 57  ? -12.43480 4.20887   -30.05176 1.000 24.40897 ? 64  LEU   A CG  1 
ATOM   400  C  CD1 . LEU   A 1 57  ? -11.71495 5.15104   -29.09315 1.000 26.15016 ? 64  LEU   A CD1 1 
ATOM   401  C  CD2 . LEU   A 1 57  ? -13.89694 4.04248   -29.66223 1.000 29.23449 ? 64  LEU   A CD2 1 
ATOM   402  N  N   . THR   A 1 58  ? -12.06655 4.38743   -34.73676 1.000 25.14923 ? 65  THR   A N   1 
ATOM   403  C  CA  . THR   A 1 58  ? -12.02507 5.01816   -36.04705 1.000 29.24372 ? 65  THR   A CA  1 
ATOM   404  C  C   . THR   A 1 58  ? -12.27948 4.04774   -37.19098 1.000 33.47177 ? 65  THR   A C   1 
ATOM   405  O  O   . THR   A 1 58  ? -12.53951 4.49587   -38.31273 1.000 37.22967 ? 65  THR   A O   1 
ATOM   406  C  CB  . THR   A 1 58  ? -10.67099 5.70976   -36.26512 1.000 40.28065 ? 65  THR   A CB  1 
ATOM   407  O  OG1 . THR   A 1 58  ? -9.61760  4.74454   -36.15922 1.000 38.06186 ? 65  THR   A OG1 1 
ATOM   408  C  CG2 . THR   A 1 58  ? -10.45726 6.80672   -35.23061 1.000 36.15139 ? 65  THR   A CG2 1 
ATOM   409  N  N   . ASP   A 1 59  ? -12.21730 2.74046   -36.94146 1.000 31.12642 ? 66  ASP   A N   1 
ATOM   410  C  CA  . ASP   A 1 59  ? -12.45654 1.73239   -37.97254 1.000 31.27868 ? 66  ASP   A CA  1 
ATOM   411  C  C   . ASP   A 1 59  ? -13.31129 0.63172   -37.35781 1.000 27.75564 ? 66  ASP   A C   1 
ATOM   412  O  O   . ASP   A 1 59  ? -12.79002 -0.33622  -36.78740 1.000 23.25668 ? 66  ASP   A O   1 
ATOM   413  C  CB  . ASP   A 1 59  ? -11.13842 1.18269   -38.52272 1.000 29.00139 ? 66  ASP   A CB  1 
ATOM   414  C  CG  . ASP   A 1 59  ? -11.33637 0.16609   -39.63732 1.000 39.10251 ? 66  ASP   A CG  1 
ATOM   415  O  OD1 . ASP   A 1 59  ? -12.49428 -0.11273  -40.01174 1.000 35.82421 ? 66  ASP   A OD1 1 
ATOM   416  O  OD2 . ASP   A 1 59  ? -10.32205 -0.35568  -40.14664 1.000 38.02043 ? 66  ASP   A OD2 1 
ATOM   417  N  N   . PRO   A 1 60  ? -14.64001 0.76136   -37.43693 1.000 30.76615 ? 67  PRO   A N   1 
ATOM   418  C  CA  . PRO   A 1 60  ? -15.51563 -0.26576  -36.85074 1.000 27.05499 ? 67  PRO   A CA  1 
ATOM   419  C  C   . PRO   A 1 60  ? -15.26478 -1.66812  -37.37623 1.000 27.82795 ? 67  PRO   A C   1 
ATOM   420  O  O   . PRO   A 1 60  ? -15.50274 -2.64249  -36.64946 1.000 26.35610 ? 67  PRO   A O   1 
ATOM   421  C  CB  . PRO   A 1 60  ? -16.91146 0.23126   -37.23706 1.000 39.55738 ? 67  PRO   A CB  1 
ATOM   422  C  CG  . PRO   A 1 60  ? -16.77990 1.71281   -37.18980 1.000 41.09411 ? 67  PRO   A CG  1 
ATOM   423  C  CD  . PRO   A 1 60  ? -15.37243 2.01659   -37.68789 1.000 38.93599 ? 67  PRO   A CD  1 
ATOM   424  N  N   . SER   A 1 61  ? -14.79676 -1.80537  -38.62006 1.000 29.17362 ? 68  SER   A N   1 
ATOM   425  C  CA  . SER   A 1 61  ? -14.57177 -3.12862  -39.19196 1.000 23.65778 ? 68  SER   A CA  1 
ATOM   426  C  C   . SER   A 1 61  ? -13.49724 -3.91450  -38.45120 1.000 32.52468 ? 68  SER   A C   1 
ATOM   427  O  O   . SER   A 1 61  ? -13.40418 -5.13280  -38.63884 1.000 24.31735 ? 68  SER   A O   1 
ATOM   428  C  CB  . SER   A 1 61  ? -14.20598 -3.00711  -40.67257 1.000 26.67870 ? 68  SER   A CB  1 
ATOM   429  O  OG  . SER   A 1 61  ? -12.90216 -2.48220  -40.83560 1.000 26.90606 ? 68  SER   A OG  1 
ATOM   430  N  N   . LYS   A 1 62  ? -12.69584 -3.25810  -37.60852 1.000 22.11263 ? 69  LYS   A N   1 
ATOM   431  C  CA  . LYS   A 1 62  ? -11.73824 -3.98054  -36.78184 1.000 23.28202 ? 69  LYS   A CA  1 
ATOM   432  C  C   . LYS   A 1 62  ? -12.41797 -4.98375  -35.85931 1.000 24.82008 ? 69  LYS   A C   1 
ATOM   433  O  O   . LYS   A 1 62  ? -11.75858 -5.91034  -35.37624 1.000 21.73628 ? 69  LYS   A O   1 
ATOM   434  C  CB  . LYS   A 1 62  ? -10.91120 -2.99398  -35.95860 1.000 28.75623 ? 69  LYS   A CB  1 
ATOM   435  C  CG  . LYS   A 1 62  ? -10.08226 -2.03466  -36.79600 1.000 32.33903 ? 69  LYS   A CG  1 
ATOM   436  C  CD  . LYS   A 1 62  ? -8.65129  -2.52526  -36.93147 1.000 27.95432 ? 69  LYS   A CD  1 
ATOM   437  C  CE  . LYS   A 1 62  ? -7.81611  -1.58337  -37.78641 1.000 27.78506 ? 69  LYS   A CE  1 
ATOM   438  N  NZ  . LYS   A 1 62  ? -6.42796  -2.09740  -37.95037 1.000 41.36745 ? 69  LYS   A NZ  1 
ATOM   439  N  N   . LEU   A 1 63  ? -13.71489 -4.82281  -35.60052 1.000 20.25689 ? 70  LEU   A N   1 
ATOM   440  C  CA  . LEU   A 1 63  ? -14.45754 -5.74554  -34.75530 1.000 18.29114 ? 70  LEU   A CA  1 
ATOM   441  C  C   . LEU   A 1 63  ? -15.26581 -6.75961  -35.55455 1.000 19.85564 ? 70  LEU   A C   1 
ATOM   442  O  O   . LEU   A 1 63  ? -16.09447 -7.46574  -34.97160 1.000 21.35244 ? 70  LEU   A O   1 
ATOM   443  C  CB  . LEU   A 1 63  ? -15.38083 -4.97401  -33.80965 1.000 25.06045 ? 70  LEU   A CB  1 
ATOM   444  C  CG  . LEU   A 1 63  ? -14.70139 -4.03796  -32.81076 1.000 23.46203 ? 70  LEU   A CG  1 
ATOM   445  C  CD1 . LEU   A 1 63  ? -15.73903 -3.37156  -31.92108 1.000 26.86644 ? 70  LEU   A CD1 1 
ATOM   446  C  CD2 . LEU   A 1 63  ? -13.67933 -4.80120  -31.97846 1.000 23.39567 ? 70  LEU   A CD2 1 
ATOM   447  N  N   . ASP   A 1 64  ? -15.04959 -6.85272  -36.87123 1.000 21.10612 ? 71  ASP   A N   1 
ATOM   448  C  CA  . ASP   A 1 64  ? -15.74322 -7.87926  -37.64717 1.000 23.20646 ? 71  ASP   A CA  1 
ATOM   449  C  C   . ASP   A 1 64  ? -15.37216 -9.27792  -37.18096 1.000 24.90960 ? 71  ASP   A C   1 
ATOM   450  O  O   . ASP   A 1 64  ? -16.15405 -10.21785 -37.35838 1.000 24.51662 ? 71  ASP   A O   1 
ATOM   451  C  CB  . ASP   A 1 64  ? -15.44326 -7.73181  -39.13825 1.000 24.43451 ? 71  ASP   A CB  1 
ATOM   452  C  CG  . ASP   A 1 64  ? -16.01945 -6.45865  -39.72747 1.000 46.26484 ? 71  ASP   A CG  1 
ATOM   453  O  OD1 . ASP   A 1 64  ? -15.56106 -6.04741  -40.81502 1.000 35.15835 ? 71  ASP   A OD1 1 
ATOM   454  O  OD2 . ASP   A 1 64  ? -16.92582 -5.86783  -39.10262 1.000 37.43568 ? 71  ASP   A OD2 1 
ATOM   455  N  N   . SER   A 1 65  ? -14.19288 -9.43380  -36.58791 1.000 22.89593 ? 72  SER   A N   1 
ATOM   456  C  CA  . SER   A 1 65  ? -13.74367 -10.69757 -36.02210 1.000 21.63720 ? 72  SER   A CA  1 
ATOM   457  C  C   . SER   A 1 65  ? -14.29066 -10.94811 -34.62107 1.000 28.84859 ? 72  SER   A C   1 
ATOM   458  O  O   . SER   A 1 65  ? -13.83468 -11.88036 -33.95200 1.000 25.26576 ? 72  SER   A O   1 
ATOM   459  C  CB  . SER   A 1 65  ? -12.21366 -10.73215 -35.99335 1.000 25.13177 ? 72  SER   A CB  1 
ATOM   460  O  OG  . SER   A 1 65  ? -11.69998 -9.49928  -35.51411 1.000 19.72702 ? 72  SER   A OG  1 
ATOM   461  N  N   . GLY   A 1 66  ? -15.24452 -10.14315 -34.16169 1.000 27.44150 ? 73  GLY   A N   1 
ATOM   462  C  CA  . GLY   A 1 66  ? -15.81886 -10.33032 -32.84522 1.000 27.29088 ? 73  GLY   A CA  1 
ATOM   463  C  C   . GLY   A 1 66  ? -16.04923 -9.02162  -32.12117 1.000 22.19016 ? 73  GLY   A C   1 
ATOM   464  O  O   . GLY   A 1 66  ? -15.09924 -8.28385  -31.84790 1.000 19.45766 ? 73  GLY   A O   1 
ATOM   465  N  N   . LYS   A 1 67  ? -17.30892 -8.71981  -31.80095 1.000 20.49472 ? 74  LYS   A N   1 
ATOM   466  C  CA  . LYS   A 1 67  ? -17.61998 -7.43708  -31.17963 1.000 24.68981 ? 74  LYS   A CA  1 
ATOM   467  C  C   . LYS   A 1 67  ? -17.45293 -7.46306  -29.66431 1.000 25.68310 ? 74  LYS   A C   1 
ATOM   468  O  O   . LYS   A 1 67  ? -17.21263 -6.41293  -29.05887 1.000 24.06612 ? 74  LYS   A O   1 
ATOM   469  C  CB  . LYS   A 1 67  ? -19.04498 -7.01186  -31.54288 1.000 27.80442 ? 74  LYS   A CB  1 
ATOM   470  C  CG  . LYS   A 1 67  ? -19.28364 -6.90711  -33.04724 1.000 37.25483 ? 74  LYS   A CG  1 
ATOM   471  C  CD  . LYS   A 1 67  ? -19.91710 -5.57856  -33.43768 1.000 54.41394 ? 74  LYS   A CD  1 
ATOM   472  C  CE  . LYS   A 1 67  ? -20.56046 -5.64828  -34.81433 1.000 50.15973 ? 74  LYS   A CE  1 
ATOM   473  N  NZ  . LYS   A 1 67  ? -21.93155 -5.06695  -34.82066 1.000 69.68208 ? 74  LYS   A NZ  1 
ATOM   474  N  N   . GLU   A 1 68  ? -17.55928 -8.63250  -29.03784 1.000 20.32661 ? 75  GLU   A N   1 
ATOM   475  C  CA  . GLU   A 1 68  ? -17.53823 -8.71242  -27.58280 1.000 23.50235 ? 75  GLU   A CA  1 
ATOM   476  C  C   . GLU   A 1 68  ? -16.10824 -8.60391  -27.06779 1.000 22.23442 ? 75  GLU   A C   1 
ATOM   477  O  O   . GLU   A 1 68  ? -15.20484 -9.28091  -27.56561 1.000 21.47019 ? 75  GLU   A O   1 
ATOM   478  C  CB  . GLU   A 1 68  ? -18.17542 -10.01643 -27.09629 1.000 23.70787 ? 75  GLU   A CB  1 
ATOM   479  C  CG  . GLU   A 1 68  ? -19.68021 -10.13600 -27.33621 1.000 33.81195 ? 75  GLU   A CG  1 
ATOM   480  C  CD  . GLU   A 1 68  ? -20.04338 -10.24598 -28.80455 1.000 67.47156 ? 75  GLU   A CD  1 
ATOM   481  O  OE1 . GLU   A 1 68  ? -21.15543 -9.81336  -29.17687 1.000 61.48302 ? 75  GLU   A OE1 1 
ATOM   482  O  OE2 . GLU   A 1 68  ? -19.22218 -10.77630 -29.58293 1.000 63.79140 ? 75  GLU   A OE2 1 
ATOM   483  N  N   . LEU   A 1 69  ? -15.90936 -7.75387  -26.06507 1.000 14.99679 ? 76  LEU   A N   1 
ATOM   484  C  CA  . LEU   A 1 69  ? -14.60349 -7.51538  -25.45568 1.000 13.94910 ? 76  LEU   A CA  1 
ATOM   485  C  C   . LEU   A 1 69  ? -14.66953 -8.03143  -24.02390 1.000 14.70531 ? 76  LEU   A C   1 
ATOM   486  O  O   . LEU   A 1 69  ? -15.30206 -7.40337  -23.16927 1.000 14.80489 ? 76  LEU   A O   1 
ATOM   487  C  CB  . LEU   A 1 69  ? -14.26223 -6.02647  -25.48563 1.000 19.04555 ? 76  LEU   A CB  1 
ATOM   488  C  CG  . LEU   A 1 69  ? -14.17652 -5.34789  -26.85417 1.000 20.40362 ? 76  LEU   A CG  1 
ATOM   489  C  CD1 . LEU   A 1 69  ? -13.66140 -3.92433  -26.70422 1.000 27.77883 ? 76  LEU   A CD1 1 
ATOM   490  C  CD2 . LEU   A 1 69  ? -13.29499 -6.14095  -27.80954 1.000 16.58134 ? 76  LEU   A CD2 1 
ATOM   491  N  N   . HIS   A 1 70  ? -14.03285 -9.17236  -23.75576 1.000 13.83798 ? 77  HIS   A N   1 
ATOM   492  C  CA  . HIS   A 1 70  ? -14.19346 -9.79783  -22.44796 1.000 13.13735 ? 77  HIS   A CA  1 
ATOM   493  C  C   . HIS   A 1 70  ? -13.01513 -10.71344 -22.14498 1.000 13.31956 ? 77  HIS   A C   1 
ATOM   494  O  O   . HIS   A 1 70  ? -12.15764 -10.97084 -22.99399 1.000 11.90768 ? 77  HIS   A O   1 
ATOM   495  C  CB  . HIS   A 1 70  ? -15.51540 -10.57064 -22.36623 1.000 17.96166 ? 77  HIS   A CB  1 
ATOM   496  C  CG  . HIS   A 1 70  ? -15.67297 -11.61529 -23.42659 1.000 16.78359 ? 77  HIS   A CG  1 
ATOM   497  N  ND1 . HIS   A 1 70  ? -14.76404 -12.63492 -23.61358 1.000 26.73521 ? 77  HIS   A ND1 1 
ATOM   498  C  CD2 . HIS   A 1 70  ? -16.62989 -11.78962 -24.36709 1.000 23.39409 ? 77  HIS   A CD2 1 
ATOM   499  C  CE1 . HIS   A 1 70  ? -15.16123 -13.39883 -24.61487 1.000 22.50016 ? 77  HIS   A CE1 1 
ATOM   500  N  NE2 . HIS   A 1 70  ? -16.28936 -12.90558 -25.09164 1.000 25.89494 ? 77  HIS   A NE2 1 
ATOM   501  N  N   . ILE   A 1 71  ? -13.00471 -11.21102 -20.90853 1.000 11.54358 ? 78  ILE   A N   1 
ATOM   502  C  CA  . ILE   A 1 71  ? -11.97796 -12.10650 -20.39045 1.000 11.81685 ? 78  ILE   A CA  1 
ATOM   503  C  C   . ILE   A 1 71  ? -12.67099 -13.30953 -19.76764 1.000 16.45751 ? 78  ILE   A C   1 
ATOM   504  O  O   . ILE   A 1 71  ? -13.56307 -13.14465 -18.92798 1.000 14.00585 ? 78  ILE   A O   1 
ATOM   505  C  CB  . ILE   A 1 71  ? -11.09301 -11.41236 -19.33664 1.000 12.54555 ? 78  ILE   A CB  1 
ATOM   506  C  CG1 . ILE   A 1 71  ? -10.39258 -10.18811 -19.92845 1.000 12.68404 ? 78  ILE   A CG1 1 
ATOM   507  C  CG2 . ILE   A 1 71  ? -10.09647 -12.40985 -18.73408 1.000 15.50492 ? 78  ILE   A CG2 1 
ATOM   508  C  CD1 . ILE   A 1 71  ? -9.68825  -9.33072  -18.89054 1.000 11.97524 ? 78  ILE   A CD1 1 
ATOM   509  N  N   . ASN   A 1 72  ? -12.25932 -14.51317 -20.16491 1.000 12.34389 ? 79  ASN   A N   1 
ATOM   510  C  CA  . ASN   A 1 72  ? -12.77777 -15.74454 -19.58322 1.000 14.26100 ? 79  ASN   A CA  1 
ATOM   511  C  C   . ASN   A 1 72  ? -11.66429 -16.50634 -18.87840 1.000 13.70262 ? 79  ASN   A C   1 
ATOM   512  O  O   . ASN   A 1 72  ? -10.54915 -16.62439 -19.39674 1.000 14.41860 ? 79  ASN   A O   1 
ATOM   513  C  CB  . ASN   A 1 72  ? -13.42004 -16.65843 -20.63529 1.000 13.88133 ? 79  ASN   A CB  1 
ATOM   514  C  CG  . ASN   A 1 72  ? -14.62215 -16.03108 -21.30732 1.000 22.08928 ? 79  ASN   A CG  1 
ATOM   515  O  OD1 . ASN   A 1 72  ? -15.36575 -15.26358 -20.69293 1.000 16.05766 ? 79  ASN   A OD1 1 
ATOM   516  N  ND2 . ASN   A 1 72  ? -14.84308 -16.38813 -22.56714 1.000 19.08213 ? 79  ASN   A ND2 1 
ATOM   517  N  N   . LEU   A 1 73  ? -11.98376 -17.03519 -17.70244 1.000 12.38141 ? 80  LEU   A N   1 
ATOM   518  C  CA  . LEU   A 1 73  ? -11.08142 -17.87688 -16.92777 1.000 9.69645  ? 80  LEU   A CA  1 
ATOM   519  C  C   . LEU   A 1 73  ? -11.65339 -19.28722 -16.90789 1.000 14.27024 ? 80  LEU   A C   1 
ATOM   520  O  O   . LEU   A 1 73  ? -12.76224 -19.49859 -16.40466 1.000 11.14419 ? 80  LEU   A O   1 
ATOM   521  C  CB  . LEU   A 1 73  ? -10.92152 -17.33801 -15.50807 1.000 11.23389 ? 80  LEU   A CB  1 
ATOM   522  C  CG  . LEU   A 1 73  ? -10.55546 -15.86001 -15.37734 1.000 14.56660 ? 80  LEU   A CG  1 
ATOM   523  C  CD1 . LEU   A 1 73  ? -10.45068 -15.47712 -13.91561 1.000 13.54325 ? 80  LEU   A CD1 1 
ATOM   524  C  CD2 . LEU   A 1 73  ? -9.24992  -15.57754 -16.10318 1.000 13.13138 ? 80  LEU   A CD2 1 
ATOM   525  N  N   . ILE   A 1 74  ? -10.91487 -20.24101 -17.45266 1.000 13.68316 ? 81  ILE   A N   1 
ATOM   526  C  CA  . ILE   A 1 74  ? -11.41134 -21.59329 -17.67932 1.000 14.64104 ? 81  ILE   A CA  1 
ATOM   527  C  C   . ILE   A 1 74  ? -10.49813 -22.58061 -16.97013 1.000 15.95124 ? 81  ILE   A C   1 
ATOM   528  O  O   . ILE   A 1 74  ? -9.43890  -22.94674 -17.49462 1.000 16.00620 ? 81  ILE   A O   1 
ATOM   529  C  CB  . ILE   A 1 74  ? -11.52674 -21.91253 -19.17570 1.000 13.12939 ? 81  ILE   A CB  1 
ATOM   530  C  CG1 . ILE   A 1 74  ? -12.24348 -20.76875 -19.89691 1.000 17.28561 ? 81  ILE   A CG1 1 
ATOM   531  C  CG2 . ILE   A 1 74  ? -12.24302 -23.24637 -19.37382 1.000 13.31386 ? 81  ILE   A CG2 1 
ATOM   532  C  CD1 . ILE   A 1 74  ? -12.35909 -20.95006 -21.37955 1.000 20.49675 ? 81  ILE   A CD1 1 
ATOM   533  N  N   . PRO   A 1 75  ? -10.87244 -23.05409 -15.78927 1.000 16.66815 ? 82  PRO   A N   1 
ATOM   534  C  CA  . PRO   A 1 75  ? -10.11519 -24.12828 -15.14707 1.000 17.25999 ? 82  PRO   A CA  1 
ATOM   535  C  C   . PRO   A 1 75  ? -10.58173 -25.48928 -15.64229 1.000 17.23763 ? 82  PRO   A C   1 
ATOM   536  O  O   . PRO   A 1 75  ? -11.76457 -25.70052 -15.92527 1.000 15.82888 ? 82  PRO   A O   1 
ATOM   537  C  CB  . PRO   A 1 75  ? -10.42826 -23.93157 -13.66077 1.000 16.62432 ? 82  PRO   A CB  1 
ATOM   538  C  CG  . PRO   A 1 75  ? -11.83307 -23.38619 -13.66623 1.000 18.70163 ? 82  PRO   A CG  1 
ATOM   539  C  CD  . PRO   A 1 75  ? -12.02214 -22.62232 -14.96808 1.000 17.69471 ? 82  PRO   A CD  1 
ATOM   540  N  N   . ASN   A 1 76  ? -9.63270  -26.41716 -15.75998 1.000 17.44195 ? 83  ASN   A N   1 
ATOM   541  C  CA  . ASN   A 1 76  ? -9.93331  -27.78646 -16.18417 1.000 19.26301 ? 83  ASN   A CA  1 
ATOM   542  C  C   . ASN   A 1 76  ? -9.10025  -28.72344 -15.31464 1.000 17.06357 ? 83  ASN   A C   1 
ATOM   543  O  O   . ASN   A 1 76  ? -7.89103  -28.86260 -15.52244 1.000 17.20770 ? 83  ASN   A O   1 
ATOM   544  C  CB  . ASN   A 1 76  ? -9.64362  -27.98265 -17.66891 1.000 17.56715 ? 83  ASN   A CB  1 
ATOM   545  C  CG  . ASN   A 1 76  ? -10.10798 -29.33460 -18.18628 1.000 23.83793 ? 83  ASN   A CG  1 
ATOM   546  O  OD1 . ASN   A 1 76  ? -9.83188  -30.37458 -17.58816 1.000 23.10085 ? 83  ASN   A OD1 1 
ATOM   547  N  ND2 . ASN   A 1 76  ? -10.82577 -29.32229 -19.30415 1.000 26.48497 ? 83  ASN   A ND2 1 
ATOM   548  N  N   . LYS   A 1 77  ? -9.75273  -29.36598 -14.34253 1.000 23.37692 ? 84  LYS   A N   1 
ATOM   549  C  CA  . LYS   A 1 77  ? -9.02542  -30.21242 -13.40286 1.000 22.60628 ? 84  LYS   A CA  1 
ATOM   550  C  C   . LYS   A 1 77  ? -8.51349  -31.48898 -14.05838 1.000 26.32183 ? 84  LYS   A C   1 
ATOM   551  O  O   . LYS   A 1 77  ? -7.48654  -32.02717 -13.63215 1.000 25.63188 ? 84  LYS   A O   1 
ATOM   552  C  CB  . LYS   A 1 77  ? -9.91089  -30.55536 -12.20556 1.000 26.66044 ? 84  LYS   A CB  1 
ATOM   553  C  CG  . LYS   A 1 77  ? -10.19038 -29.38444 -11.27660 1.000 28.85524 ? 84  LYS   A CG  1 
ATOM   554  C  CD  . LYS   A 1 77  ? -10.94890 -29.84404 -10.03844 1.000 39.31133 ? 84  LYS   A CD  1 
ATOM   555  C  CE  . LYS   A 1 77  ? -11.16615 -28.70192 -9.06044  1.000 35.04090 ? 84  LYS   A CE  1 
ATOM   556  N  NZ  . LYS   A 1 77  ? -11.97802 -27.61315 -9.66238  1.000 43.18204 ? 84  LYS   A NZ  1 
ATOM   557  N  N   . GLN   A 1 78  ? -9.20734  -31.99302 -15.08231 1.000 25.29893 ? 85  GLN   A N   1 
ATOM   558  C  CA  . GLN   A 1 78  ? -8.76358  -33.22888 -15.72156 1.000 36.87912 ? 85  GLN   A CA  1 
ATOM   559  C  C   . GLN   A 1 78  ? -7.48147  -33.00898 -16.51216 1.000 28.43415 ? 85  GLN   A C   1 
ATOM   560  O  O   . GLN   A 1 78  ? -6.57836  -33.85277 -16.48758 1.000 30.30667 ? 85  GLN   A O   1 
ATOM   561  C  CB  . GLN   A 1 78  ? -9.86016  -33.78620 -16.62742 1.000 31.09001 ? 85  GLN   A CB  1 
ATOM   562  C  CG  . GLN   A 1 78  ? -11.00920 -34.45338 -15.88928 1.000 55.29029 ? 85  GLN   A CG  1 
ATOM   563  C  CD  . GLN   A 1 78  ? -11.89698 -33.46214 -15.16488 1.000 66.37158 ? 85  GLN   A CD  1 
ATOM   564  O  OE1 . GLN   A 1 78  ? -12.18268 -33.62181 -13.97764 1.000 65.38831 ? 85  GLN   A OE1 1 
ATOM   565  N  NE2 . GLN   A 1 78  ? -12.33764 -32.42882 -15.87687 1.000 52.27303 ? 85  GLN   A NE2 1 
ATOM   566  N  N   . ASP   A 1 79  ? -7.38777  -31.88576 -17.22081 1.000 22.60752 ? 86  ASP   A N   1 
ATOM   567  C  CA  . ASP   A 1 79  ? -6.17637  -31.51995 -17.93932 1.000 25.76804 ? 86  ASP   A CA  1 
ATOM   568  C  C   . ASP   A 1 79  ? -5.14978  -30.83733 -17.04802 1.000 20.33432 ? 86  ASP   A C   1 
ATOM   569  O  O   . ASP   A 1 79  ? -3.99336  -30.69771 -17.46234 1.000 22.56621 ? 86  ASP   A O   1 
ATOM   570  C  CB  . ASP   A 1 79  ? -6.52013  -30.59449 -19.10858 1.000 21.03192 ? 86  ASP   A CB  1 
ATOM   571  C  CG  . ASP   A 1 79  ? -7.39557  -31.26636 -20.14577 1.000 38.91636 ? 86  ASP   A CG  1 
ATOM   572  O  OD1 . ASP   A 1 79  ? -7.59199  -32.49655 -20.05724 1.000 35.75397 ? 86  ASP   A OD1 1 
ATOM   573  O  OD2 . ASP   A 1 79  ? -7.89188  -30.56179 -21.04867 1.000 34.48816 ? 86  ASP   A OD2 1 
ATOM   574  N  N   . ARG   A 1 80  ? -5.54785  -30.43484 -15.84040 1.000 21.00244 ? 87  ARG   A N   1 
ATOM   575  C  CA  . ARG   A 1 80  ? -4.74004  -29.60671 -14.94482 1.000 18.87496 ? 87  ARG   A CA  1 
ATOM   576  C  C   . ARG   A 1 80  ? -4.25649  -28.34150 -15.65263 1.000 20.52897 ? 87  ARG   A C   1 
ATOM   577  O  O   . ARG   A 1 80  ? -3.07033  -28.00320 -15.64722 1.000 16.88424 ? 87  ARG   A O   1 
ATOM   578  C  CB  . ARG   A 1 80  ? -3.56607  -30.39216 -14.35600 1.000 19.90240 ? 87  ARG   A CB  1 
ATOM   579  C  CG  . ARG   A 1 80  ? -3.17885  -29.89962 -12.97176 1.000 21.01185 ? 87  ARG   A CG  1 
ATOM   580  C  CD  . ARG   A 1 80  ? -1.70842  -30.08755 -12.68131 1.000 30.51439 ? 87  ARG   A CD  1 
ATOM   581  N  NE  . ARG   A 1 80  ? -1.36168  -31.49136 -12.51971 1.000 38.84270 ? 87  ARG   A NE  1 
ATOM   582  C  CZ  . ARG   A 1 80  ? -0.16187  -31.99700 -12.76562 1.000 41.91226 ? 87  ARG   A CZ  1 
ATOM   583  N  NH1 . ARG   A 1 80  ? 0.83633   -31.23658 -13.18503 1.000 35.43193 ? 87  ARG   A NH1 1 
ATOM   584  N  NH2 . ARG   A 1 80  ? 0.04351   -33.29628 -12.57844 1.000 35.30558 ? 87  ARG   A NH2 1 
ATOM   585  N  N   . THR   A 1 81  ? -5.19616  -27.63180 -16.26870 1.000 16.44494 ? 88  THR   A N   1 
ATOM   586  C  CA  . THR   A 1 81  ? -4.88916  -26.39040 -16.96072 1.000 15.03896 ? 88  THR   A CA  1 
ATOM   587  C  C   . THR   A 1 81  ? -5.80571  -25.27911 -16.47536 1.000 16.48177 ? 88  THR   A C   1 
ATOM   588  O  O   . THR   A 1 81  ? -6.97664  -25.50420 -16.16127 1.000 17.32033 ? 88  THR   A O   1 
ATOM   589  C  CB  . THR   A 1 81  ? -5.03616  -26.52036 -18.48330 1.000 21.44961 ? 88  THR   A CB  1 
ATOM   590  O  OG1 . THR   A 1 81  ? -6.36749  -26.94339 -18.79757 1.000 20.05383 ? 88  THR   A OG1 1 
ATOM   591  C  CG2 . THR   A 1 81  ? -4.02623  -27.51920 -19.04904 1.000 19.02750 ? 88  THR   A CG2 1 
ATOM   592  N  N   . LEU   A 1 82  ? -5.25220  -24.07381 -16.41261 1.000 13.46349 ? 89  LEU   A N   1 
ATOM   593  C  CA  . LEU   A 1 82  ? -6.02655  -22.85636 -16.22628 1.000 13.00027 ? 89  LEU   A CA  1 
ATOM   594  C  C   . LEU   A 1 82  ? -5.81300  -22.00551 -17.46790 1.000 13.76823 ? 89  LEU   A C   1 
ATOM   595  O  O   . LEU   A 1 82  ? -4.67077  -21.69513 -17.82004 1.000 13.99972 ? 89  LEU   A O   1 
ATOM   596  C  CB  . LEU   A 1 82  ? -5.60300  -22.10408 -14.96138 1.000 13.22743 ? 89  LEU   A CB  1 
ATOM   597  C  CG  . LEU   A 1 82  ? -6.30340  -20.75372 -14.76895 1.000 14.41896 ? 89  LEU   A CG  1 
ATOM   598  C  CD1 . LEU   A 1 82  ? -7.81113  -20.95245 -14.63209 1.000 13.79141 ? 89  LEU   A CD1 1 
ATOM   599  C  CD2 . LEU   A 1 82  ? -5.75147  -20.02725 -13.55844 1.000 16.07629 ? 89  LEU   A CD2 1 
ATOM   600  N  N   . THR   A 1 83  ? -6.89995  -21.65290 -18.14243 1.000 13.06607 ? 90  THR   A N   1 
ATOM   601  C  CA  . THR   A 1 83  ? -6.82978  -20.92523 -19.40032 1.000 12.92892 ? 90  THR   A CA  1 
ATOM   602  C  C   . THR   A 1 83  ? -7.41004  -19.53008 -19.21375 1.000 15.20653 ? 90  THR   A C   1 
ATOM   603  O  O   . THR   A 1 83  ? -8.51174  -19.37955 -18.67268 1.000 13.67114 ? 90  THR   A O   1 
ATOM   604  C  CB  . THR   A 1 83  ? -7.57992  -21.67152 -20.50630 1.000 15.09116 ? 90  THR   A CB  1 
ATOM   605  O  OG1 . THR   A 1 83  ? -6.97130  -22.95234 -20.72932 1.000 16.42280 ? 90  THR   A OG1 1 
ATOM   606  C  CG2 . THR   A 1 83  ? -7.54669  -20.88041 -21.78826 1.000 17.74256 ? 90  THR   A CG2 1 
ATOM   607  N  N   . ILE   A 1 84  ? -6.66304  -18.51687 -19.64640 1.000 11.20587 ? 91  ILE   A N   1 
ATOM   608  C  CA  . ILE   A 1 84  ? -7.11263  -17.12704 -19.62188 1.000 14.83346 ? 91  ILE   A CA  1 
ATOM   609  C  C   . ILE   A 1 84  ? -7.35868  -16.71660 -21.06642 1.000 16.65688 ? 91  ILE   A C   1 
ATOM   610  O  O   . ILE   A 1 84  ? -6.41594  -16.61874 -21.86161 1.000 14.80579 ? 91  ILE   A O   1 
ATOM   611  C  CB  . ILE   A 1 84  ? -6.09684  -16.19364 -18.94445 1.000 12.53814 ? 91  ILE   A CB  1 
ATOM   612  C  CG1 . ILE   A 1 84  ? -5.93055  -16.54468 -17.46473 1.000 20.94940 ? 91  ILE   A CG1 1 
ATOM   613  C  CG2 . ILE   A 1 84  ? -6.53667  -14.72957 -19.07886 1.000 13.31974 ? 91  ILE   A CG2 1 
ATOM   614  C  CD1 . ILE   A 1 84  ? -4.85970  -17.57543 -17.18115 1.000 26.90318 ? 91  ILE   A CD1 1 
ATOM   615  N  N   . VAL   A 1 85  ? -8.62307  -16.48326 -21.40997 1.000 11.90532 ? 92  VAL   A N   1 
ATOM   616  C  CA  . VAL   A 1 85  ? -9.02977  -16.11524 -22.76050 1.000 13.17074 ? 92  VAL   A CA  1 
ATOM   617  C  C   . VAL   A 1 85  ? -9.43005  -14.64953 -22.76935 1.000 17.03325 ? 92  VAL   A C   1 
ATOM   618  O  O   . VAL   A 1 85  ? -10.14983 -14.18875 -21.87680 1.000 15.25204 ? 92  VAL   A O   1 
ATOM   619  C  CB  . VAL   A 1 85  ? -10.19780 -16.99061 -23.26106 1.000 16.04801 ? 92  VAL   A CB  1 
ATOM   620  C  CG1 . VAL   A 1 85  ? -10.46494 -16.73961 -24.73956 1.000 18.15398 ? 92  VAL   A CG1 1 
ATOM   621  C  CG2 . VAL   A 1 85  ? -9.91095  -18.45328 -23.00823 1.000 20.12038 ? 92  VAL   A CG2 1 
ATOM   622  N  N   . ASP   A 1 86  ? -8.97740  -13.92144 -23.78827 1.000 12.67392 ? 93  ASP   A N   1 
ATOM   623  C  CA  . ASP   A 1 86  ? -9.45931  -12.57147 -24.03483 1.000 12.45311 ? 93  ASP   A CA  1 
ATOM   624  C  C   . ASP   A 1 86  ? -9.70741  -12.39549 -25.52683 1.000 16.78099 ? 93  ASP   A C   1 
ATOM   625  O  O   . ASP   A 1 86  ? -9.14454  -13.10886 -26.36085 1.000 15.93569 ? 93  ASP   A O   1 
ATOM   626  C  CB  . ASP   A 1 86  ? -8.47605  -11.51587 -23.48882 1.000 11.48719 ? 93  ASP   A CB  1 
ATOM   627  C  CG  . ASP   A 1 86  ? -7.17666  -11.43641 -24.28357 1.000 24.89150 ? 93  ASP   A CG  1 
ATOM   628  O  OD1 . ASP   A 1 86  ? -7.21165  -11.10423 -25.48884 1.000 20.99393 ? 93  ASP   A OD1 1 
ATOM   629  O  OD2 . ASP   A 1 86  ? -6.10882  -11.71606 -23.69262 1.000 16.43682 ? 93  ASP   A OD2 1 
ATOM   630  N  N   . THR   A 1 87  ? -10.57808 -11.44615 -25.85585 1.000 12.45940 ? 94  THR   A N   1 
ATOM   631  C  CA  . THR   A 1 87  ? -10.84818 -11.07731 -27.24133 1.000 12.20324 ? 94  THR   A CA  1 
ATOM   632  C  C   . THR   A 1 87  ? -10.17816 -9.75338  -27.60221 1.000 19.71129 ? 94  THR   A C   1 
ATOM   633  O  O   . THR   A 1 87  ? -10.74373 -8.92135  -28.31250 1.000 13.53089 ? 94  THR   A O   1 
ATOM   634  C  CB  . THR   A 1 87  ? -12.35027 -11.01805 -27.50328 1.000 17.33384 ? 94  THR   A CB  1 
ATOM   635  O  OG1 . THR   A 1 87  ? -12.98238 -10.19022 -26.51965 1.000 14.43680 ? 94  THR   A OG1 1 
ATOM   636  C  CG2 . THR   A 1 87  ? -12.94210 -12.41698 -27.42259 1.000 16.71146 ? 94  THR   A CG2 1 
ATOM   637  N  N   . GLY   A 1 88  ? -8.95455  -9.55164  -27.11974 1.000 13.55946 ? 95  GLY   A N   1 
ATOM   638  C  CA  . GLY   A 1 88  ? -8.20182  -8.35060  -27.41414 1.000 13.31649 ? 95  GLY   A CA  1 
ATOM   639  C  C   . GLY   A 1 88  ? -7.62463  -8.36510  -28.81696 1.000 12.00321 ? 95  GLY   A C   1 
ATOM   640  O  O   . GLY   A 1 88  ? -8.05180  -9.12175  -29.69233 1.000 14.32787 ? 95  GLY   A O   1 
ATOM   641  N  N   . ILE   A 1 89  ? -6.61506  -7.51526  -29.02394 1.000 13.11937 ? 96  ILE   A N   1 
ATOM   642  C  CA  . ILE   A 1 89  ? -6.10297  -7.28848  -30.37167 1.000 13.10822 ? 96  ILE   A CA  1 
ATOM   643  C  C   . ILE   A 1 89  ? -5.33568  -8.49382  -30.90858 1.000 14.84465 ? 96  ILE   A C   1 
ATOM   644  O  O   . ILE   A 1 89  ? -5.16119  -8.61971  -32.12674 1.000 15.35179 ? 96  ILE   A O   1 
ATOM   645  C  CB  . ILE   A 1 89  ? -5.23343  -6.01518  -30.38770 1.000 15.85344 ? 96  ILE   A CB  1 
ATOM   646  C  CG1 . ILE   A 1 89  ? -4.90182  -5.58992  -31.82155 1.000 15.34646 ? 96  ILE   A CG1 1 
ATOM   647  C  CG2 . ILE   A 1 89  ? -3.95952  -6.23017  -29.57699 1.000 13.64538 ? 96  ILE   A CG2 1 
ATOM   648  C  CD1 . ILE   A 1 89  ? -4.48760  -4.13891  -31.93510 1.000 16.82113 ? 96  ILE   A CD1 1 
ATOM   649  N  N   . GLY   A 1 90  ? -4.88217  -9.39603  -30.03734 1.000 13.09250 ? 97  GLY   A N   1 
ATOM   650  C  CA  . GLY   A 1 90  ? -4.12733  -10.55322 -30.47714 1.000 14.20555 ? 97  GLY   A CA  1 
ATOM   651  C  C   . GLY   A 1 90  ? -2.69267  -10.19839 -30.81848 1.000 13.72668 ? 97  GLY   A C   1 
ATOM   652  O  O   . GLY   A 1 90  ? -2.23481  -9.06541  -30.65838 1.000 15.24435 ? 97  GLY   A O   1 
ATOM   653  N  N   . MET   A 1 91  ? -1.96585  -11.20034 -31.30379 1.000 14.02928 ? 98  MET   A N   1 
ATOM   654  C  CA  . MET   A 1 91  ? -0.56991  -11.02863 -31.67370 1.000 14.81504 ? 98  MET   A CA  1 
ATOM   655  C  C   . MET   A 1 91  ? -0.31179  -11.65700 -33.03224 1.000 14.02609 ? 98  MET   A C   1 
ATOM   656  O  O   . MET   A 1 91  ? -0.84177  -12.72872 -33.34137 1.000 17.53316 ? 98  MET   A O   1 
ATOM   657  C  CB  . MET   A 1 91  ? 0.37747   -11.66188 -30.64619 1.000 16.12520 ? 98  MET   A CB  1 
ATOM   658  C  CG  . MET   A 1 91  ? 0.44467   -10.94341 -29.30946 1.000 23.60928 ? 98  MET   A CG  1 
ATOM   659  S  SD  . MET   A 1 91  ? 1.40318   -11.89400 -28.11452 1.000 19.58914 ? 98  MET   A SD  1 
ATOM   660  C  CE  . MET   A 1 91  ? 0.17791   -13.07257 -27.54579 1.000 13.87743 ? 98  MET   A CE  1 
ATOM   661  N  N   . THR   A 1 92  ? 0.50878   -10.98846 -33.83714 1.000 15.78075 ? 99  THR   A N   1 
ATOM   662  C  CA  . THR   A 1 92  ? 0.99346   -11.58619 -35.06896 1.000 16.25547 ? 99  THR   A CA  1 
ATOM   663  C  C   . THR   A 1 92  ? 2.06397   -12.62810 -34.75086 1.000 16.44728 ? 99  THR   A C   1 
ATOM   664  O  O   . THR   A 1 92  ? 2.55518   -12.72803 -33.62333 1.000 18.06309 ? 99  THR   A O   1 
ATOM   665  C  CB  . THR   A 1 92  ? 1.57364   -10.51882 -35.99231 1.000 17.08274 ? 99  THR   A CB  1 
ATOM   666  O  OG1 . THR   A 1 92  ? 2.73042   -9.94246  -35.36942 1.000 17.81134 ? 99  THR   A OG1 1 
ATOM   667  C  CG2 . THR   A 1 92  ? 0.54823   -9.41948  -36.25984 1.000 16.62928 ? 99  THR   A CG2 1 
ATOM   668  N  N   . LYS   A 1 93  ? 2.42841   -13.41585 -35.76602 1.000 16.52747 ? 100 LYS   A N   1 
ATOM   669  C  CA  . LYS   A 1 93  ? 3.53985   -14.34814 -35.59862 1.000 17.79419 ? 100 LYS   A CA  1 
ATOM   670  C  C   . LYS   A 1 93  ? 4.81517   -13.61117 -35.20400 1.000 16.81191 ? 100 LYS   A C   1 
ATOM   671  O  O   . LYS   A 1 93  ? 5.57021   -14.07577 -34.34216 1.000 16.29696 ? 100 LYS   A O   1 
ATOM   672  C  CB  . LYS   A 1 93  ? 3.75733   -15.14936 -36.88249 1.000 19.35961 ? 100 LYS   A CB  1 
ATOM   673  C  CG  . LYS   A 1 93  ? 4.80790   -16.24592 -36.74803 1.000 20.63283 ? 100 LYS   A CG  1 
ATOM   674  C  CD  . LYS   A 1 93  ? 5.10041   -16.90825 -38.08560 1.000 22.33093 ? 100 LYS   A CD  1 
ATOM   675  C  CE  . LYS   A 1 93  ? 5.99106   -18.12731 -37.90269 1.000 28.25991 ? 100 LYS   A CE  1 
ATOM   676  N  NZ  . LYS   A 1 93  ? 6.73030   -18.46526 -39.15146 1.000 28.30078 ? 100 LYS   A NZ  1 
ATOM   677  N  N   . ALA   A 1 94  ? 5.06255   -12.44946 -35.81503 1.000 17.56182 ? 101 ALA   A N   1 
ATOM   678  C  CA  . ALA   A 1 94  ? 6.24109   -11.66355 -35.46238 1.000 19.70782 ? 101 ALA   A CA  1 
ATOM   679  C  C   . ALA   A 1 94  ? 6.18065   -11.19869 -34.01153 1.000 22.84878 ? 101 ALA   A C   1 
ATOM   680  O  O   . ALA   A 1 94  ? 7.19313   -11.23005 -33.30129 1.000 21.09380 ? 101 ALA   A O   1 
ATOM   681  C  CB  . ALA   A 1 94  ? 6.37935   -10.47012 -36.40949 1.000 19.39378 ? 101 ALA   A CB  1 
ATOM   682  N  N   . ASP   A 1 95  ? 5.00058   -10.76366 -33.55568 1.000 17.28744 ? 102 ASP   A N   1 
ATOM   683  C  CA  . ASP   A 1 95  ? 4.82121   -10.40172 -32.15065 1.000 20.56634 ? 102 ASP   A CA  1 
ATOM   684  C  C   . ASP   A 1 95  ? 5.17207   -11.56672 -31.23526 1.000 16.57526 ? 102 ASP   A C   1 
ATOM   685  O  O   . ASP   A 1 95  ? 5.86443   -11.39311 -30.22689 1.000 17.27411 ? 102 ASP   A O   1 
ATOM   686  C  CB  . ASP   A 1 95  ? 3.37775   -9.95446  -31.89592 1.000 19.50914 ? 102 ASP   A CB  1 
ATOM   687  C  CG  . ASP   A 1 95  ? 3.05722   -8.60401  -32.50774 1.000 31.14205 ? 102 ASP   A CG  1 
ATOM   688  O  OD1 . ASP   A 1 95  ? 3.98623   -7.78850  -32.67926 1.000 26.97332 ? 102 ASP   A OD1 1 
ATOM   689  O  OD2 . ASP   A 1 95  ? 1.86496   -8.35468  -32.80876 1.000 27.32181 ? 102 ASP   A OD2 1 
ATOM   690  N  N   . LEU   A 1 96  ? 4.68974   -12.76495 -31.57124 1.000 18.03055 ? 103 LEU   A N   1 
ATOM   691  C  CA  . LEU   A 1 96  ? 4.94400   -13.94119 -30.74510 1.000 17.94193 ? 103 LEU   A CA  1 
ATOM   692  C  C   . LEU   A 1 96  ? 6.43842   -14.19098 -30.59370 1.000 17.43948 ? 103 LEU   A C   1 
ATOM   693  O  O   . LEU   A 1 96  ? 6.94936   -14.32309 -29.47473 1.000 18.28363 ? 103 LEU   A O   1 
ATOM   694  C  CB  . LEU   A 1 96  ? 4.27012   -15.16436 -31.36472 1.000 16.64948 ? 103 LEU   A CB  1 
ATOM   695  C  CG  . LEU   A 1 96  ? 2.79224   -15.43302 -31.09572 1.000 15.83029 ? 103 LEU   A CG  1 
ATOM   696  C  CD1 . LEU   A 1 96  ? 2.39167   -16.76531 -31.71961 1.000 17.81846 ? 103 LEU   A CD1 1 
ATOM   697  C  CD2 . LEU   A 1 96  ? 2.45716   -15.40171 -29.61928 1.000 15.22479 ? 103 LEU   A CD2 1 
ATOM   698  N  N   . ILE   A 1 97  ? 7.15456   -14.26421 -31.71940 1.000 16.27554 ? 104 ILE   A N   1 
ATOM   699  C  CA  . ILE   A 1 97  ? 8.59618   -14.50415 -31.67802 1.000 19.43027 ? 104 ILE   A CA  1 
ATOM   700  C  C   . ILE   A 1 97  ? 9.30688   -13.37811 -30.93941 1.000 18.55351 ? 104 ILE   A C   1 
ATOM   701  O  O   . ILE   A 1 97  ? 10.24813  -13.61545 -30.16964 1.000 20.25593 ? 104 ILE   A O   1 
ATOM   702  C  CB  . ILE   A 1 97  ? 9.14529   -14.68740 -33.10576 1.000 23.33004 ? 104 ILE   A CB  1 
ATOM   703  C  CG1 . ILE   A 1 97  ? 8.40968   -15.83562 -33.81249 1.000 15.94004 ? 104 ILE   A CG1 1 
ATOM   704  C  CG2 . ILE   A 1 97  ? 10.65812  -14.88778 -33.09102 1.000 19.18897 ? 104 ILE   A CG2 1 
ATOM   705  C  CD1 . ILE   A 1 97  ? 8.54366   -15.81489 -35.32549 1.000 21.12047 ? 104 ILE   A CD1 1 
ATOM   706  N  N   . ASN   A 1 98  ? 8.85837   -12.13901 -31.14176 1.000 15.65344 ? 105 ASN   A N   1 
ATOM   707  C  CA  . ASN   A 1 98  ? 9.44762   -10.98426 -30.46426 1.000 17.91397 ? 105 ASN   A CA  1 
ATOM   708  C  C   . ASN   A 1 98  ? 8.90007   -10.85026 -29.03847 1.000 19.29803 ? 105 ASN   A C   1 
ATOM   709  O  O   . ASN   A 1 98  ? 8.35690   -9.82037  -28.63988 1.000 18.40721 ? 105 ASN   A O   1 
ATOM   710  C  CB  . ASN   A 1 98  ? 9.20208   -9.71773  -31.27503 1.000 21.95543 ? 105 ASN   A CB  1 
ATOM   711  C  CG  . ASN   A 1 98  ? 10.22820  -8.64320  -31.00290 1.000 41.61188 ? 105 ASN   A CG  1 
ATOM   712  O  OD1 . ASN   A 1 98  ? 11.16540  -8.83617  -30.22301 1.000 45.13371 ? 105 ASN   A OD1 1 
ATOM   713  N  ND2 . ASN   A 1 98  ? 10.05590  -7.49670  -31.64453 1.000 45.94991 ? 105 ASN   A ND2 1 
ATOM   714  N  N   . ASN   A 1 99  ? 9.04867   -11.93759 -28.27509 1.000 15.58144 ? 106 ASN   A N   1 
ATOM   715  C  CA  . ASN   A 1 99  ? 8.79785   -11.94858 -26.83263 1.000 16.22142 ? 106 ASN   A CA  1 
ATOM   716  C  C   . ASN   A 1 99  ? 7.35325   -11.57773 -26.49707 1.000 17.59531 ? 106 ASN   A C   1 
ATOM   717  O  O   . ASN   A 1 99  ? 7.09263   -10.79948 -25.57673 1.000 14.17667 ? 106 ASN   A O   1 
ATOM   718  C  CB  . ASN   A 1 99  ? 9.78169   -11.02826 -26.10701 1.000 13.81004 ? 106 ASN   A CB  1 
ATOM   719  C  CG  . ASN   A 1 99  ? 11.21096  -11.52199 -26.21386 1.000 14.78202 ? 106 ASN   A CG  1 
ATOM   720  O  OD1 . ASN   A 1 99  ? 11.48931  -12.70274 -26.00087 1.000 15.19278 ? 106 ASN   A OD1 1 
ATOM   721  N  ND2 . ASN   A 1 99  ? 12.12134  -10.62465 -26.56789 1.000 14.99158 ? 106 ASN   A ND2 1 
ATOM   722  N  N   . LEU   A 1 100 ? 6.40638   -12.14943 -27.24378 1.000 14.52687 ? 107 LEU   A N   1 
ATOM   723  C  CA  . LEU   A 1 100 ? 4.97683   -11.95643 -26.98617 1.000 17.18657 ? 107 LEU   A CA  1 
ATOM   724  C  C   . LEU   A 1 100 ? 4.60149   -10.47514 -27.00974 1.000 17.24107 ? 107 LEU   A C   1 
ATOM   725  O  O   . LEU   A 1 100 ? 3.79198   -10.01092 -26.20560 1.000 14.97457 ? 107 LEU   A O   1 
ATOM   726  C  CB  . LEU   A 1 100 ? 4.56129   -12.58967 -25.65330 1.000 16.65334 ? 107 LEU   A CB  1 
ATOM   727  C  CG  . LEU   A 1 100 ? 4.63423   -14.10462 -25.41442 1.000 24.88496 ? 107 LEU   A CG  1 
ATOM   728  C  CD1 . LEU   A 1 100 ? 4.09257   -14.87859 -26.58765 1.000 24.76072 ? 107 LEU   A CD1 1 
ATOM   729  C  CD2 . LEU   A 1 100 ? 6.05769   -14.56455 -25.08969 1.000 18.14366 ? 107 LEU   A CD2 1 
ATOM   730  N  N   . GLY   A 1 101 ? 5.20930   -9.71817  -27.92104 1.000 19.79327 ? 108 GLY   A N   1 
ATOM   731  C  CA  . GLY   A 1 101 ? 4.87293   -8.31150  -28.04884 1.000 21.28881 ? 108 GLY   A CA  1 
ATOM   732  C  C   . GLY   A 1 101 ? 5.37098   -7.41672  -26.93604 1.000 23.87302 ? 108 GLY   A C   1 
ATOM   733  O  O   . GLY   A 1 101 ? 4.86482   -6.30029  -26.77704 1.000 20.70934 ? 108 GLY   A O   1 
ATOM   734  N  N   . THR   A 1 102 ? 6.34842   -7.86703  -26.15819 1.000 17.13334 ? 109 THR   A N   1 
ATOM   735  C  CA  . THR   A 1 102 ? 6.90689   -7.07560  -25.07319 1.000 17.94436 ? 109 THR   A CA  1 
ATOM   736  C  C   . THR   A 1 102 ? 8.27021   -6.52725  -25.47938 1.000 17.98583 ? 109 THR   A C   1 
ATOM   737  O  O   . THR   A 1 102 ? 8.88447   -6.98104  -26.44690 1.000 17.77423 ? 109 THR   A O   1 
ATOM   738  C  CB  . THR   A 1 102 ? 7.05659   -7.91700  -23.80015 1.000 16.10696 ? 109 THR   A CB  1 
ATOM   739  O  OG1 . THR   A 1 102 ? 7.98820   -8.98224  -24.04211 1.000 21.79693 ? 109 THR   A OG1 1 
ATOM   740  C  CG2 . THR   A 1 102 ? 5.71650   -8.52671  -23.40249 1.000 17.46219 ? 109 THR   A CG2 1 
ATOM   741  N  N   . ILE   A 1 103 ? 8.74110   -5.53798  -24.72274 1.000 16.59787 ? 110 ILE   A N   1 
ATOM   742  C  CA  . ILE   A 1 103 ? 10.12960  -5.09976  -24.83727 1.000 17.15722 ? 110 ILE   A CA  1 
ATOM   743  C  C   . ILE   A 1 103 ? 10.92763  -5.81075  -23.74978 1.000 16.27398 ? 110 ILE   A C   1 
ATOM   744  O  O   . ILE   A 1 103 ? 11.51667  -5.17885  -22.86395 1.000 16.96111 ? 110 ILE   A O   1 
ATOM   745  C  CB  . ILE   A 1 103 ? 10.26121  -3.56589  -24.75779 1.000 20.49779 ? 110 ILE   A CB  1 
ATOM   746  C  CG1 . ILE   A 1 103 ? 9.56212   -3.00065  -23.51813 1.000 23.86814 ? 110 ILE   A CG1 1 
ATOM   747  C  CG2 . ILE   A 1 103 ? 9.69612   -2.92651  -26.01810 1.000 24.45595 ? 110 ILE   A CG2 1 
ATOM   748  C  CD1 . ILE   A 1 103 ? 9.87619   -1.54502  -23.26799 1.000 30.84637 ? 110 ILE   A CD1 1 
ATOM   749  N  N   . ALA   A 1 104 ? 10.97256  -7.14166  -23.83868 1.000 16.79915 ? 111 ALA   A N   1 
ATOM   750  C  CA  . ALA   A 1 104 ? 11.38302  -7.96003  -22.70368 1.000 18.83989 ? 111 ALA   A CA  1 
ATOM   751  C  C   . ALA   A 1 104 ? 12.85898  -7.79378  -22.35804 1.000 17.04597 ? 111 ALA   A C   1 
ATOM   752  O  O   . ALA   A 1 104 ? 13.23481  -7.97239  -21.19514 1.000 17.74427 ? 111 ALA   A O   1 
ATOM   753  C  CB  . ALA   A 1 104 ? 11.06444  -9.42862  -22.98153 1.000 19.07397 ? 111 ALA   A CB  1 
ATOM   754  N  N   . LYS   A 1 105 ? 13.70827  -7.45927  -23.33136 1.000 16.22283 ? 112 LYS   A N   1 
ATOM   755  C  CA  . LYS   A 1 105 ? 15.12914  -7.28995  -23.03322 1.000 18.60228 ? 112 LYS   A CA  1 
ATOM   756  C  C   . LYS   A 1 105 ? 15.35348  -6.11469  -22.08579 1.000 27.64632 ? 112 LYS   A C   1 
ATOM   757  O  O   . LYS   A 1 105 ? 15.95652  -6.26530  -21.01730 1.000 22.83254 ? 112 LYS   A O   1 
ATOM   758  C  CB  . LYS   A 1 105 ? 15.92769  -7.10744  -24.32559 1.000 19.82074 ? 112 LYS   A CB  1 
ATOM   759  C  CG  . LYS   A 1 105 ? 17.43566  -7.02426  -24.11067 1.000 34.52364 ? 112 LYS   A CG  1 
ATOM   760  C  CD  . LYS   A 1 105 ? 18.20041  -7.32353  -25.39314 1.000 31.66818 ? 112 LYS   A CD  1 
ATOM   761  C  CE  . LYS   A 1 105 ? 19.50626  -6.54307  -25.46498 1.000 58.97103 ? 112 LYS   A CE  1 
ATOM   762  N  NZ  . LYS   A 1 105 ? 20.25244  -6.55692  -24.17466 1.000 48.72493 ? 112 LYS   A NZ  1 
ATOM   763  N  N   . SER   A 1 106 ? 14.86613  -4.92925  -22.45864 1.000 22.82916 ? 113 SER   A N   1 
ATOM   764  C  CA  . SER   A 1 106 ? 15.03361  -3.77107  -21.58741 1.000 24.76416 ? 113 SER   A CA  1 
ATOM   765  C  C   . SER   A 1 106 ? 14.17537  -3.88535  -20.33328 1.000 23.86428 ? 113 SER   A C   1 
ATOM   766  O  O   . SER   A 1 106 ? 14.56304  -3.38429  -19.27189 1.000 26.00167 ? 113 SER   A O   1 
ATOM   767  C  CB  . SER   A 1 106 ? 14.70844  -2.48529  -22.34895 1.000 31.99359 ? 113 SER   A CB  1 
ATOM   768  O  OG  . SER   A 1 106 ? 13.34517  -2.44597  -22.73217 1.000 29.58376 ? 113 SER   A OG  1 
ATOM   769  N  N   . GLY   A 1 107 ? 13.01804  -4.54269  -20.42907 1.000 20.98534 ? 114 GLY   A N   1 
ATOM   770  C  CA  . GLY   A 1 107 ? 12.19003  -4.73034  -19.24826 1.000 22.90490 ? 114 GLY   A CA  1 
ATOM   771  C  C   . GLY   A 1 107 ? 12.83922  -5.63748  -18.22050 1.000 23.94872 ? 114 GLY   A C   1 
ATOM   772  O  O   . GLY   A 1 107 ? 12.77925  -5.36996  -17.01722 1.000 22.98236 ? 114 GLY   A O   1 
ATOM   773  N  N   . THR   A 1 108 ? 13.47175  -6.72020  -18.67997 1.000 19.22753 ? 115 THR   A N   1 
ATOM   774  C  CA  . THR   A 1 108 ? 14.19819  -7.60313  -17.77213 1.000 19.95673 ? 115 THR   A CA  1 
ATOM   775  C  C   . THR   A 1 108 ? 15.36868  -6.87770  -17.12084 1.000 23.75825 ? 115 THR   A C   1 
ATOM   776  O  O   . THR   A 1 108 ? 15.61431  -7.03289  -15.91857 1.000 26.36472 ? 115 THR   A O   1 
ATOM   777  C  CB  . THR   A 1 108 ? 14.68499  -8.84041  -18.52939 1.000 18.67557 ? 115 THR   A CB  1 
ATOM   778  O  OG1 . THR   A 1 108 ? 13.55358  -9.57674  -19.01802 1.000 20.51255 ? 115 THR   A OG1 1 
ATOM   779  C  CG2 . THR   A 1 108 ? 15.51868  -9.73169  -17.62910 1.000 23.75106 ? 115 THR   A CG2 1 
ATOM   780  N  N   . LYS   A 1 109 ? 16.10484  -6.08750  -17.90673 1.000 24.94015 ? 116 LYS   A N   1 
ATOM   781  C  CA  . LYS   A 1 109 ? 17.18772  -5.26669  -17.37211 1.000 28.57638 ? 116 LYS   A CA  1 
ATOM   782  C  C   . LYS   A 1 109 ? 16.72053  -4.42750  -16.18768 1.000 30.05416 ? 116 LYS   A C   1 
ATOM   783  O  O   . LYS   A 1 109 ? 17.34322  -4.43390  -15.11936 1.000 34.88292 ? 116 LYS   A O   1 
ATOM   784  C  CB  . LYS   A 1 109 ? 17.73874  -4.37002  -18.48282 1.000 30.27976 ? 116 LYS   A CB  1 
ATOM   785  C  CG  . LYS   A 1 109 ? 19.09620  -3.74384  -18.20334 1.000 40.15840 ? 116 LYS   A CG  1 
ATOM   786  C  CD  . LYS   A 1 109 ? 19.30584  -2.52732  -19.09424 1.000 44.76750 ? 116 LYS   A CD  1 
ATOM   787  C  CE  . LYS   A 1 109 ? 20.57447  -1.76544  -18.73806 1.000 58.03615 ? 116 LYS   A CE  1 
ATOM   788  N  NZ  . LYS   A 1 109 ? 21.34425  -2.42710  -17.65129 1.000 52.82530 ? 116 LYS   A NZ  1 
ATOM   789  N  N   . ALA   A 1 110 ? 15.61461  -3.70052  -16.36053 1.000 29.25649 ? 117 ALA   A N   1 
ATOM   790  C  CA  . ALA   A 1 110 ? 15.13731  -2.81595  -15.30246 1.000 33.95883 ? 117 ALA   A CA  1 
ATOM   791  C  C   . ALA   A 1 110 ? 14.58741  -3.60732  -14.12181 1.000 29.89329 ? 117 ALA   A C   1 
ATOM   792  O  O   . ALA   A 1 110 ? 14.80857  -3.23865  -12.96240 1.000 32.12050 ? 117 ALA   A O   1 
ATOM   793  C  CB  . ALA   A 1 110 ? 14.07670  -1.86634  -15.85722 1.000 30.78799 ? 117 ALA   A CB  1 
ATOM   794  N  N   . PHE   A 1 111 ? 13.86908  -4.69659  -14.39842 1.000 26.67814 ? 118 PHE   A N   1 
ATOM   795  C  CA  . PHE   A 1 111 ? 13.30856  -5.52149  -13.33202 1.000 25.68507 ? 118 PHE   A CA  1 
ATOM   796  C  C   . PHE   A 1 111 ? 14.40534  -6.06102  -12.42056 1.000 27.47413 ? 118 PHE   A C   1 
ATOM   797  O  O   . PHE   A 1 111 ? 14.28684  -6.02019  -11.19130 1.000 28.85226 ? 118 PHE   A O   1 
ATOM   798  C  CB  . PHE   A 1 111 ? 12.49631  -6.65670  -13.95540 1.000 22.20652 ? 118 PHE   A CB  1 
ATOM   799  C  CG  . PHE   A 1 111 ? 11.82939  -7.56941  -12.96097 1.000 24.66786 ? 118 PHE   A CG  1 
ATOM   800  C  CD1 . PHE   A 1 111 ? 11.20261  -7.06772  -11.83074 1.000 23.85030 ? 118 PHE   A CD1 1 
ATOM   801  C  CD2 . PHE   A 1 111 ? 11.79247  -8.93736  -13.18876 1.000 23.94235 ? 118 PHE   A CD2 1 
ATOM   802  C  CE1 . PHE   A 1 111 ? 10.57525  -7.91942  -10.93237 1.000 22.87316 ? 118 PHE   A CE1 1 
ATOM   803  C  CE2 . PHE   A 1 111 ? 11.16805  -9.79186  -12.29819 1.000 25.54361 ? 118 PHE   A CE2 1 
ATOM   804  C  CZ  . PHE   A 1 111 ? 10.55753  -9.28036  -11.16635 1.000 27.19931 ? 118 PHE   A CZ  1 
ATOM   805  N  N   . MET   A 1 112 ? 15.49825  -6.54686  -13.00711 1.000 27.82248 ? 119 MET   A N   1 
ATOM   806  C  CA  . MET   A 1 112 ? 16.53689  -7.17543  -12.19951 1.000 41.11844 ? 119 MET   A CA  1 
ATOM   807  C  C   . MET   A 1 112 ? 17.34805  -6.15327  -11.41378 1.000 40.43441 ? 119 MET   A C   1 
ATOM   808  O  O   . MET   A 1 112 ? 17.85490  -6.47150  -10.33116 1.000 40.52869 ? 119 MET   A O   1 
ATOM   809  C  CB  . MET   A 1 112 ? 17.43071  -8.02777  -13.09288 1.000 41.14237 ? 119 MET   A CB  1 
ATOM   810  C  CG  . MET   A 1 112 ? 16.84724  -9.40981  -13.30658 1.000 26.28497 ? 119 MET   A CG  1 
ATOM   811  S  SD  . MET   A 1 112 ? 18.00812  -10.60062 -13.97493 1.000 68.43232 ? 119 MET   A SD  1 
ATOM   812  C  CE  . MET   A 1 112 ? 16.87263  -11.64616 -14.87527 1.000 32.84762 ? 119 MET   A CE  1 
ATOM   813  N  N   . GLU   A 1 113 ? 17.48329  -4.92865  -11.92718 1.000 34.97929 ? 120 GLU   A N   1 
ATOM   814  C  CA  . GLU   A 1 113 ? 18.07455  -3.87337  -11.11174 1.000 42.98058 ? 120 GLU   A CA  1 
ATOM   815  C  C   . GLU   A 1 113 ? 17.16432  -3.51753  -9.94534  1.000 49.28347 ? 120 GLU   A C   1 
ATOM   816  O  O   . GLU   A 1 113 ? 17.63854  -3.27274  -8.82929  1.000 43.43182 ? 120 GLU   A O   1 
ATOM   817  C  CB  . GLU   A 1 113 ? 18.36696  -2.63281  -11.95623 1.000 43.84635 ? 120 GLU   A CB  1 
ATOM   818  C  CG  . GLU   A 1 113 ? 19.51623  -2.78632  -12.93900 1.000 61.14938 ? 120 GLU   A CG  1 
ATOM   819  C  CD  . GLU   A 1 113 ? 19.43558  -1.79674  -14.08717 1.000 73.98628 ? 120 GLU   A CD  1 
ATOM   820  O  OE1 . GLU   A 1 113 ? 20.07395  -2.04222  -15.13236 1.000 80.13580 ? 120 GLU   A OE1 1 
ATOM   821  O  OE2 . GLU   A 1 113 ? 18.73045  -0.77392  -13.94529 1.000 70.90338 ? 120 GLU   A OE2 1 
ATOM   822  N  N   . ALA   A 1 114 ? 15.85255  -3.49082  -10.18487 1.000 37.10505 ? 121 ALA   A N   1 
ATOM   823  C  CA  . ALA   A 1 114 ? 14.91347  -3.18416  -9.11395  1.000 37.17254 ? 121 ALA   A CA  1 
ATOM   824  C  C   . ALA   A 1 114 ? 14.95456  -4.24802  -8.02633  1.000 37.46781 ? 121 ALA   A C   1 
ATOM   825  O  O   . ALA   A 1 114 ? 14.87166  -3.92899  -6.83432  1.000 45.13406 ? 121 ALA   A O   1 
ATOM   826  C  CB  . ALA   A 1 114 ? 13.50237  -3.04413  -9.68097  1.000 34.63961 ? 121 ALA   A CB  1 
ATOM   827  N  N   . LEU   A 1 115 ? 15.09319  -5.51866  -8.41754  1.000 35.10152 ? 122 LEU   A N   1 
ATOM   828  C  CA  . LEU   A 1 115 ? 15.10974  -6.59780  -7.43462  1.000 38.80815 ? 122 LEU   A CA  1 
ATOM   829  C  C   . LEU   A 1 115 ? 16.28774  -6.45546  -6.47820  1.000 53.42487 ? 122 LEU   A C   1 
ATOM   830  O  O   . LEU   A 1 115 ? 16.14333  -6.65496  -5.26626  1.000 48.22455 ? 122 LEU   A O   1 
ATOM   831  C  CB  . LEU   A 1 115 ? 15.15026  -7.95121  -8.14220  1.000 31.78476 ? 122 LEU   A CB  1 
ATOM   832  C  CG  . LEU   A 1 115 ? 13.85231  -8.37540  -8.83399  1.000 30.49301 ? 122 LEU   A CG  1 
ATOM   833  C  CD1 . LEU   A 1 115 ? 14.06913  -9.63058  -9.66498  1.000 31.76096 ? 122 LEU   A CD1 1 
ATOM   834  C  CD2 . LEU   A 1 115 ? 12.74135  -8.58229  -7.81413  1.000 29.90369 ? 122 LEU   A CD2 1 
ATOM   835  N  N   . GLN   A 1 116 ? 17.46156  -6.10330  -7.00079  1.000 51.48678 ? 123 GLN   A N   1 
ATOM   836  C  CA  . GLN   A 1 116 ? 18.60631  -5.86719  -6.13300  1.000 58.42921 ? 123 GLN   A CA  1 
ATOM   837  C  C   . GLN   A 1 116 ? 18.50078  -4.54883  -5.37897  1.000 56.92210 ? 123 GLN   A C   1 
ATOM   838  O  O   . GLN   A 1 116 ? 19.31600  -4.29986  -4.48396  1.000 70.48622 ? 123 GLN   A O   1 
ATOM   839  C  CB  . GLN   A 1 116 ? 19.89756  -5.90685  -6.95133  1.000 57.11628 ? 123 GLN   A CB  1 
ATOM   840  C  CG  . GLN   A 1 116 ? 20.25047  -7.29509  -7.46110  1.000 56.00565 ? 123 GLN   A CG  1 
ATOM   841  C  CD  . GLN   A 1 116 ? 21.72939  -7.61104  -7.33296  1.000 92.16926 ? 123 GLN   A CD  1 
ATOM   842  O  OE1 . GLN   A 1 116 ? 22.49245  -6.84447  -6.74420  1.000 90.42552 ? 123 GLN   A OE1 1 
ATOM   843  N  NE2 . GLN   A 1 116 ? 22.14112  -8.74795  -7.88445  1.000 85.24548 ? 123 GLN   A NE2 1 
ATOM   844  N  N   . ALA   A 1 117 ? 17.51693  -3.71035  -5.70986  1.000 65.93774 ? 124 ALA   A N   1 
ATOM   845  C  CA  . ALA   A 1 117 ? 17.30883  -2.42714  -5.05194  1.000 55.68866 ? 124 ALA   A CA  1 
ATOM   846  C  C   . ALA   A 1 117 ? 16.02134  -2.40495  -4.23049  1.000 68.78935 ? 124 ALA   A C   1 
ATOM   847  O  O   . ALA   A 1 117 ? 15.41287  -1.34772  -4.04818  1.000 58.82082 ? 124 ALA   A O   1 
ATOM   848  C  CB  . ALA   A 1 117 ? 17.30672  -1.29520  -6.07771  1.000 52.23542 ? 124 ALA   A CB  1 
ATOM   849  N  N   . GLY   A 1 118 ? 15.58623  -3.56584  -3.74045  1.000 57.93506 ? 125 GLY   A N   1 
ATOM   850  C  CA  . GLY   A 1 118 ? 14.50025  -3.65667  -2.78747  1.000 64.09354 ? 125 GLY   A CA  1 
ATOM   851  C  C   . GLY   A 1 118 ? 13.20946  -4.23558  -3.32908  1.000 49.93933 ? 125 GLY   A C   1 
ATOM   852  O  O   . GLY   A 1 118 ? 12.35978  -4.65562  -2.53353  1.000 46.73463 ? 125 GLY   A O   1 
ATOM   853  N  N   . ALA   A 1 119 ? 13.03080  -4.27197  -4.64742  1.000 39.69747 ? 126 ALA   A N   1 
ATOM   854  C  CA  . ALA   A 1 119 ? 11.77810  -4.74974  -5.21330  1.000 36.44798 ? 126 ALA   A CA  1 
ATOM   855  C  C   . ALA   A 1 119 ? 11.63442  -6.25856  -5.01947  1.000 34.31879 ? 126 ALA   A C   1 
ATOM   856  O  O   . ALA   A 1 119 ? 12.58534  -6.96832  -4.68292  1.000 42.38129 ? 126 ALA   A O   1 
ATOM   857  C  CB  . ALA   A 1 119 ? 11.69056  -4.39919  -6.69749  1.000 34.46544 ? 126 ALA   A CB  1 
ATOM   858  N  N   . ASP   A 1 120 ? 10.41509  -6.74781  -5.23376  1.000 37.03475 ? 127 ASP   A N   1 
ATOM   859  C  CA  . ASP   A 1 120 ? 10.13063  -8.17389  -5.20137  1.000 32.18760 ? 127 ASP   A CA  1 
ATOM   860  C  C   . ASP   A 1 120 ? 9.43660   -8.57408  -6.49626  1.000 29.08576 ? 127 ASP   A C   1 
ATOM   861  O  O   . ASP   A 1 120 ? 9.08889   -7.73245  -7.32975  1.000 28.09483 ? 127 ASP   A O   1 
ATOM   862  C  CB  . ASP   A 1 120 ? 9.27348   -8.55629  -3.98687  1.000 37.94224 ? 127 ASP   A CB  1 
ATOM   863  C  CG  . ASP   A 1 120 ? 7.92056   -7.88067  -3.99269  1.000 43.09746 ? 127 ASP   A CG  1 
ATOM   864  O  OD1 . ASP   A 1 120 ? 7.86670   -6.64314  -3.83228  1.000 53.04414 ? 127 ASP   A OD1 1 
ATOM   865  O  OD2 . ASP   A 1 120 ? 6.90926   -8.59324  -4.15652  1.000 44.34787 ? 127 ASP   A OD2 1 
ATOM   866  N  N   . ILE   A 1 121 ? 9.22787   -9.88451  -6.65091  1.000 24.78361 ? 128 ILE   A N   1 
ATOM   867  C  CA  . ILE   A 1 121 ? 8.74264   -10.42943 -7.91752  1.000 23.41282 ? 128 ILE   A CA  1 
ATOM   868  C  C   . ILE   A 1 121 ? 7.34215   -9.92041  -8.24150  1.000 25.48252 ? 128 ILE   A C   1 
ATOM   869  O  O   . ILE   A 1 121 ? 6.97174   -9.80544  -9.41740  1.000 23.53790 ? 128 ILE   A O   1 
ATOM   870  C  CB  . ILE   A 1 121 ? 8.81712   -11.97182 -7.87102  1.000 23.67844 ? 128 ILE   A CB  1 
ATOM   871  C  CG1 . ILE   A 1 121 ? 10.27543  -12.42155 -8.02447  1.000 34.25431 ? 128 ILE   A CG1 1 
ATOM   872  C  CG2 . ILE   A 1 121 ? 7.95018   -12.61377 -8.94728  1.000 19.56056 ? 128 ILE   A CG2 1 
ATOM   873  C  CD1 . ILE   A 1 121 ? 10.50788  -13.89278 -7.75179  1.000 36.90246 ? 128 ILE   A CD1 1 
ATOM   874  N  N   . SER   A 1 122 ? 6.55594   -9.56711  -7.22013  1.000 28.35619 ? 129 SER   A N   1 
ATOM   875  C  CA  . SER   A 1 122 ? 5.19281   -9.09703  -7.45866  1.000 30.97971 ? 129 SER   A CA  1 
ATOM   876  C  C   . SER   A 1 122 ? 5.14206   -7.82238  -8.29416  1.000 27.83310 ? 129 SER   A C   1 
ATOM   877  O  O   . SER   A 1 122 ? 4.09155   -7.51138  -8.86486  1.000 26.08289 ? 129 SER   A O   1 
ATOM   878  C  CB  . SER   A 1 122 ? 4.47177   -8.85711  -6.13182  1.000 23.86918 ? 129 SER   A CB  1 
ATOM   879  O  OG  . SER   A 1 122 ? 4.89541   -7.64670  -5.53249  1.000 30.82874 ? 129 SER   A OG  1 
ATOM   880  N  N   . MET   A 1 123 ? 6.24002   -7.07844  -8.38163  1.000 23.28908 ? 130 MET   A N   1 
ATOM   881  C  CA  . MET   A 1 123 ? 6.27254   -5.83663  -9.14106  1.000 24.29544 ? 130 MET   A CA  1 
ATOM   882  C  C   . MET   A 1 123 ? 6.66963   -6.04524  -10.59985 1.000 22.91721 ? 130 MET   A C   1 
ATOM   883  O  O   . MET   A 1 123 ? 6.89898   -5.06371  -11.31198 1.000 22.67111 ? 130 MET   A O   1 
ATOM   884  C  CB  . MET   A 1 123 ? 7.21449   -4.84275  -8.45546  1.000 30.31512 ? 130 MET   A CB  1 
ATOM   885  C  CG  . MET   A 1 123 ? 7.19541   -4.97928  -6.93067  1.000 40.80690 ? 130 MET   A CG  1 
ATOM   886  S  SD  . MET   A 1 123 ? 8.22501   -3.80800  -6.02896  1.000 44.41181 ? 130 MET   A SD  1 
ATOM   887  C  CE  . MET   A 1 123 ? 8.21697   -2.41395  -7.15495  1.000 43.69865 ? 130 MET   A CE  1 
ATOM   888  N  N   . ILE   A 1 124 ? 6.71375   -7.29888  -11.06190 1.000 19.38508 ? 131 ILE   A N   1 
ATOM   889  C  CA  . ILE   A 1 124 ? 7.16148   -7.62331  -12.41676 1.000 20.15190 ? 131 ILE   A CA  1 
ATOM   890  C  C   . ILE   A 1 124 ? 6.36273   -6.87817  -13.48257 1.000 17.36492 ? 131 ILE   A C   1 
ATOM   891  O  O   . ILE   A 1 124 ? 6.90750   -6.50217  -14.52834 1.000 16.54724 ? 131 ILE   A O   1 
ATOM   892  C  CB  . ILE   A 1 124 ? 7.09276   -9.15249  -12.62782 1.000 18.84975 ? 131 ILE   A CB  1 
ATOM   893  C  CG1 . ILE   A 1 124 ? 7.64958   -9.53424  -14.00161 1.000 20.77226 ? 131 ILE   A CG1 1 
ATOM   894  C  CG2 . ILE   A 1 124 ? 5.66128   -9.65732  -12.44117 1.000 13.94022 ? 131 ILE   A CG2 1 
ATOM   895  C  CD1 . ILE   A 1 124 ? 7.91090   -11.02109 -14.16205 1.000 21.17835 ? 131 ILE   A CD1 1 
ATOM   896  N  N   . GLY   A 1 125 ? 5.06913   -6.65050  -13.24471 1.000 19.07563 ? 132 GLY   A N   1 
ATOM   897  C  CA  . GLY   A 1 125 ? 4.23397   -6.00210  -14.24075 1.000 23.81021 ? 132 GLY   A CA  1 
ATOM   898  C  C   . GLY   A 1 125 ? 4.62410   -4.57031  -14.54225 1.000 26.44558 ? 132 GLY   A C   1 
ATOM   899  O  O   . GLY   A 1 125 ? 4.35660   -4.08572  -15.64741 1.000 24.55217 ? 132 GLY   A O   1 
ATOM   900  N  N   . GLN   A 1 126 ? 5.25041   -3.88088  -13.58591 1.000 21.29168 ? 133 GLN   A N   1 
ATOM   901  C  CA  . GLN   A 1 126 ? 5.69289   -2.51211  -13.81888 1.000 23.87146 ? 133 GLN   A CA  1 
ATOM   902  C  C   . GLN   A 1 126 ? 6.83821   -2.42738  -14.81587 1.000 26.42760 ? 133 GLN   A C   1 
ATOM   903  O  O   . GLN   A 1 126 ? 7.20442   -1.31916  -15.22058 1.000 25.65204 ? 133 GLN   A O   1 
ATOM   904  C  CB  . GLN   A 1 126 ? 6.11883   -1.86220  -12.50366 1.000 27.24211 ? 133 GLN   A CB  1 
ATOM   905  C  CG  . GLN   A 1 126 ? 5.05644   -1.89469  -11.42773 1.000 31.88736 ? 133 GLN   A CG  1 
ATOM   906  C  CD  . GLN   A 1 126 ? 5.52679   -1.28114  -10.12988 1.000 31.77595 ? 133 GLN   A CD  1 
ATOM   907  O  OE1 . GLN   A 1 126 ? 6.26893   -0.29769  -10.12713 1.000 41.53224 ? 133 GLN   A OE1 1 
ATOM   908  N  NE2 . GLN   A 1 126 ? 5.09510   -1.85847  -9.01278  1.000 46.66463 ? 133 GLN   A NE2 1 
ATOM   909  N  N   . PHE   A 1 127 ? 7.41409   -3.56038  -15.20878 1.000 21.67379 ? 134 PHE   A N   1 
ATOM   910  C  CA  . PHE   A 1 127 ? 8.52557   -3.59727  -16.14861 1.000 24.76313 ? 134 PHE   A CA  1 
ATOM   911  C  C   . PHE   A 1 127 ? 8.13790   -4.25272  -17.46682 1.000 22.72761 ? 134 PHE   A C   1 
ATOM   912  O  O   . PHE   A 1 127 ? 9.01503   -4.59050  -18.26844 1.000 24.22200 ? 134 PHE   A O   1 
ATOM   913  C  CB  . PHE   A 1 127 ? 9.71742   -4.30840  -15.50393 1.000 21.36800 ? 134 PHE   A CB  1 
ATOM   914  C  CG  . PHE   A 1 127 ? 10.08460  -3.74182  -14.16222 1.000 24.07643 ? 134 PHE   A CG  1 
ATOM   915  C  CD1 . PHE   A 1 127 ? 10.79851  -2.56048  -14.06886 1.000 31.01117 ? 134 PHE   A CD1 1 
ATOM   916  C  CD2 . PHE   A 1 127 ? 9.66334   -4.35709  -12.99589 1.000 26.03641 ? 134 PHE   A CD2 1 
ATOM   917  C  CE1 . PHE   A 1 127 ? 11.12001  -2.02141  -12.83392 1.000 34.27373 ? 134 PHE   A CE1 1 
ATOM   918  C  CE2 . PHE   A 1 127 ? 9.97775   -3.82497  -11.75792 1.000 27.45543 ? 134 PHE   A CE2 1 
ATOM   919  C  CZ  . PHE   A 1 127 ? 10.70787  -2.65358  -11.67781 1.000 31.79162 ? 134 PHE   A CZ  1 
ATOM   920  N  N   . GLY   A 1 128 ? 6.84352   -4.44922  -17.70295 1.000 17.99894 ? 135 GLY   A N   1 
ATOM   921  C  CA  . GLY   A 1 128 ? 6.36148   -4.89694  -18.99086 1.000 17.44515 ? 135 GLY   A CA  1 
ATOM   922  C  C   . GLY   A 1 128 ? 6.58954   -6.35417  -19.31833 1.000 19.22537 ? 135 GLY   A C   1 
ATOM   923  O  O   . GLY   A 1 128 ? 6.38944   -6.74386  -20.47367 1.000 22.44842 ? 135 GLY   A O   1 
ATOM   924  N  N   . VAL   A 1 129 ? 6.99033   -7.17590  -18.34920 1.000 15.10863 ? 136 VAL   A N   1 
ATOM   925  C  CA  . VAL   A 1 129 ? 7.26300   -8.58654  -18.60852 1.000 15.42037 ? 136 VAL   A CA  1 
ATOM   926  C  C   . VAL   A 1 129 ? 6.42046   -9.45186  -17.67900 1.000 18.57604 ? 136 VAL   A C   1 
ATOM   927  O  O   . VAL   A 1 129 ? 6.83590   -10.54616 -17.27546 1.000 14.32801 ? 136 VAL   A O   1 
ATOM   928  C  CB  . VAL   A 1 129 ? 8.76347   -8.89794  -18.45655 1.000 17.60323 ? 136 VAL   A CB  1 
ATOM   929  C  CG1 . VAL   A 1 129 ? 9.54664   -8.24108  -19.58085 1.000 19.97503 ? 136 VAL   A CG1 1 
ATOM   930  C  CG2 . VAL   A 1 129 ? 9.27404   -8.41638  -17.10559 1.000 17.52846 ? 136 VAL   A CG2 1 
ATOM   931  N  N   . GLY   A 1 130 ? 5.21788   -8.97390  -17.35336 1.000 16.83719 ? 137 GLY   A N   1 
ATOM   932  C  CA  . GLY   A 1 130 ? 4.34960   -9.69448  -16.44118 1.000 13.89807 ? 137 GLY   A CA  1 
ATOM   933  C  C   . GLY   A 1 130 ? 3.90380   -11.04832 -16.94820 1.000 16.25800 ? 137 GLY   A C   1 
ATOM   934  O  O   . GLY   A 1 130 ? 3.54700   -11.91178 -16.13927 1.000 14.06215 ? 137 GLY   A O   1 
ATOM   935  N  N   . PHE   A 1 131 ? 3.92332   -11.25960 -18.26882 1.000 13.06136 ? 138 PHE   A N   1 
ATOM   936  C  CA  . PHE   A 1 131 ? 3.51607   -12.55057 -18.81740 1.000 16.41574 ? 138 PHE   A CA  1 
ATOM   937  C  C   . PHE   A 1 131 ? 4.33562   -13.68897 -18.22940 1.000 13.83079 ? 138 PHE   A C   1 
ATOM   938  O  O   . PHE   A 1 131 ? 3.79889   -14.76228 -17.93394 1.000 11.41762 ? 138 PHE   A O   1 
ATOM   939  C  CB  . PHE   A 1 131 ? 3.64507   -12.55833 -20.34344 1.000 17.23950 ? 138 PHE   A CB  1 
ATOM   940  C  CG  . PHE   A 1 131 ? 3.66062   -13.94594 -20.93689 1.000 18.62563 ? 138 PHE   A CG  1 
ATOM   941  C  CD1 . PHE   A 1 131 ? 2.47455   -14.62792 -21.16164 1.000 14.17588 ? 138 PHE   A CD1 1 
ATOM   942  C  CD2 . PHE   A 1 131 ? 4.85984   -14.57219 -21.25909 1.000 14.76947 ? 138 PHE   A CD2 1 
ATOM   943  C  CE1 . PHE   A 1 131 ? 2.47959   -15.90827 -21.69622 1.000 15.06907 ? 138 PHE   A CE1 1 
ATOM   944  C  CE2 . PHE   A 1 131 ? 4.87203   -15.85341 -21.79138 1.000 16.00445 ? 138 PHE   A CE2 1 
ATOM   945  C  CZ  . PHE   A 1 131 ? 3.67805   -16.52095 -22.01022 1.000 17.32762 ? 138 PHE   A CZ  1 
ATOM   946  N  N   . TYR   A 1 132 ? 5.64296   -13.47549 -18.05465 1.000 11.68201 ? 139 TYR   A N   1 
ATOM   947  C  CA  . TYR   A 1 132 ? 6.52153   -14.56374 -17.64548 1.000 13.29471 ? 139 TYR   A CA  1 
ATOM   948  C  C   . TYR   A 1 132 ? 6.29295   -14.99130 -16.20472 1.000 14.90434 ? 139 TYR   A C   1 
ATOM   949  O  O   . TYR   A 1 132 ? 6.80519   -16.04081 -15.80279 1.000 12.58308 ? 139 TYR   A O   1 
ATOM   950  C  CB  . TYR   A 1 132 ? 7.98159   -14.16671 -17.87455 1.000 10.37081 ? 139 TYR   A CB  1 
ATOM   951  C  CG  . TYR   A 1 132 ? 8.26289   -13.89072 -19.33618 1.000 13.44334 ? 139 TYR   A CG  1 
ATOM   952  C  CD1 . TYR   A 1 132 ? 8.55732   -14.92678 -20.21525 1.000 16.77871 ? 139 TYR   A CD1 1 
ATOM   953  C  CD2 . TYR   A 1 132 ? 8.19048   -12.59918 -19.84685 1.000 14.64437 ? 139 TYR   A CD2 1 
ATOM   954  C  CE1 . TYR   A 1 132 ? 8.79670   -14.68181 -21.56017 1.000 12.95871 ? 139 TYR   A CE1 1 
ATOM   955  C  CE2 . TYR   A 1 132 ? 8.42855   -12.34501 -21.18736 1.000 16.52375 ? 139 TYR   A CE2 1 
ATOM   956  C  CZ  . TYR   A 1 132 ? 8.73040   -13.38851 -22.03820 1.000 17.02331 ? 139 TYR   A CZ  1 
ATOM   957  O  OH  . TYR   A 1 132 ? 8.96352   -13.13698 -23.37367 1.000 17.34326 ? 139 TYR   A OH  1 
ATOM   958  N  N   . SER   A 1 133 ? 5.52354   -14.22443 -15.42858 1.000 13.59519 ? 140 SER   A N   1 
ATOM   959  C  CA  . SER   A 1 133 ? 5.09369   -14.69339 -14.11765 1.000 15.94837 ? 140 SER   A CA  1 
ATOM   960  C  C   . SER   A 1 133 ? 4.20881   -15.92988 -14.21007 1.000 16.62044 ? 140 SER   A C   1 
ATOM   961  O  O   . SER   A 1 133 ? 3.96095   -16.57237 -13.18373 1.000 12.20091 ? 140 SER   A O   1 
ATOM   962  C  CB  . SER   A 1 133 ? 4.34940   -13.58426 -13.37006 1.000 14.04322 ? 140 SER   A CB  1 
ATOM   963  O  OG  . SER   A 1 133 ? 3.07487   -13.34915 -13.94057 1.000 15.75411 ? 140 SER   A OG  1 
ATOM   964  N  N   . ALA   A 1 134 ? 3.72595   -16.27630 -15.40758 1.000 12.23475 ? 141 ALA   A N   1 
ATOM   965  C  CA  . ALA   A 1 134 ? 3.00244   -17.53196 -15.57830 1.000 13.85486 ? 141 ALA   A CA  1 
ATOM   966  C  C   . ALA   A 1 134 ? 3.81900   -18.71824 -15.08627 1.000 13.16499 ? 141 ALA   A C   1 
ATOM   967  O  O   . ALA   A 1 134 ? 3.25561   -19.69689 -14.58368 1.000 12.52799 ? 141 ALA   A O   1 
ATOM   968  C  CB  . ALA   A 1 134 ? 2.62494   -17.72521 -17.04785 1.000 13.00660 ? 141 ALA   A CB  1 
ATOM   969  N  N   . TYR   A 1 135 ? 5.14738   -18.64294 -15.19632 1.000 12.99900 ? 142 TYR   A N   1 
ATOM   970  C  CA  . TYR   A 1 135 ? 5.99734   -19.75202 -14.78686 1.000 13.76273 ? 142 TYR   A CA  1 
ATOM   971  C  C   . TYR   A 1 135 ? 6.18326   -19.83125 -13.27669 1.000 16.14784 ? 142 TYR   A C   1 
ATOM   972  O  O   . TYR   A 1 135 ? 6.92298   -20.70029 -12.80561 1.000 14.65136 ? 142 TYR   A O   1 
ATOM   973  C  CB  . TYR   A 1 135 ? 7.34514   -19.66546 -15.51343 1.000 13.79334 ? 142 TYR   A CB  1 
ATOM   974  C  CG  . TYR   A 1 135 ? 7.16617   -19.96171 -16.98547 1.000 16.37528 ? 142 TYR   A CG  1 
ATOM   975  C  CD1 . TYR   A 1 135 ? 7.19702   -21.26707 -17.46189 1.000 14.06565 ? 142 TYR   A CD1 1 
ATOM   976  C  CD2 . TYR   A 1 135 ? 6.90201   -18.94169 -17.88841 1.000 14.16133 ? 142 TYR   A CD2 1 
ATOM   977  C  CE1 . TYR   A 1 135 ? 7.00036   -21.54608 -18.80699 1.000 14.59571 ? 142 TYR   A CE1 1 
ATOM   978  C  CE2 . TYR   A 1 135 ? 6.70315   -19.20790 -19.23563 1.000 12.59457 ? 142 TYR   A CE2 1 
ATOM   979  C  CZ  . TYR   A 1 135 ? 6.75396   -20.51040 -19.68826 1.000 13.03538 ? 142 TYR   A CZ  1 
ATOM   980  O  OH  . TYR   A 1 135 ? 6.55962   -20.77798 -21.02747 1.000 14.65825 ? 142 TYR   A OH  1 
ATOM   981  N  N   . LEU   A 1 136 ? 5.52468   -18.95818 -12.51024 1.000 15.47137 ? 143 LEU   A N   1 
ATOM   982  C  CA  . LEU   A 1 136 ? 5.42024   -19.17393 -11.07202 1.000 15.24624 ? 143 LEU   A CA  1 
ATOM   983  C  C   . LEU   A 1 136 ? 4.59128   -20.41537 -10.75478 1.000 16.94016 ? 143 LEU   A C   1 
ATOM   984  O  O   . LEU   A 1 136 ? 4.82126   -21.07085 -9.73127  1.000 15.00469 ? 143 LEU   A O   1 
ATOM   985  C  CB  . LEU   A 1 136 ? 4.80187   -17.94390 -10.40126 1.000 14.57415 ? 143 LEU   A CB  1 
ATOM   986  C  CG  . LEU   A 1 136 ? 5.62001   -16.65068 -10.33950 1.000 13.90760 ? 143 LEU   A CG  1 
ATOM   987  C  CD1 . LEU   A 1 136 ? 4.74229   -15.48910 -9.87846  1.000 17.48841 ? 143 LEU   A CD1 1 
ATOM   988  C  CD2 . LEU   A 1 136 ? 6.82354   -16.82172 -9.41212  1.000 16.69123 ? 143 LEU   A CD2 1 
ATOM   989  N  N   . VAL   A 1 137 ? 3.63186   -20.75938 -11.61511 1.000 12.91113 ? 144 VAL   A N   1 
ATOM   990  C  CA  . VAL   A 1 137 ? 2.67505   -21.81460 -11.29224 1.000 15.59605 ? 144 VAL   A CA  1 
ATOM   991  C  C   . VAL   A 1 137 ? 2.58681   -22.86698 -12.39268 1.000 13.52850 ? 144 VAL   A C   1 
ATOM   992  O  O   . VAL   A 1 137 ? 2.03410   -23.94945 -12.17582 1.000 17.25897 ? 144 VAL   A O   1 
ATOM   993  C  CB  . VAL   A 1 137 ? 1.28036   -21.22352 -11.01022 1.000 16.35440 ? 144 VAL   A CB  1 
ATOM   994  C  CG1 . VAL   A 1 137 ? 1.30647   -20.33273 -9.77271  1.000 16.91002 ? 144 VAL   A CG1 1 
ATOM   995  C  CG2 . VAL   A 1 137 ? 0.77721   -20.44869 -12.21528 1.000 11.36077 ? 144 VAL   A CG2 1 
ATOM   996  N  N   . ALA   A 1 138 ? 3.11816   -22.57145 -13.57470 1.000 16.17302 ? 145 ALA   A N   1 
ATOM   997  C  CA  . ALA   A 1 138 ? 2.97454   -23.45136 -14.72743 1.000 13.92058 ? 145 ALA   A CA  1 
ATOM   998  C  C   . ALA   A 1 138 ? 4.31434   -24.06407 -15.11617 1.000 14.38111 ? 145 ALA   A C   1 
ATOM   999  O  O   . ALA   A 1 138 ? 5.33310   -23.36854 -15.16398 1.000 19.14313 ? 145 ALA   A O   1 
ATOM   1000 C  CB  . ALA   A 1 138 ? 2.39173   -22.69369 -15.92206 1.000 13.10802 ? 145 ALA   A CB  1 
ATOM   1001 N  N   . GLU   A 1 139 ? 4.30643   -25.37080 -15.40391 1.000 12.08882 ? 146 GLU   A N   1 
ATOM   1002 C  CA  . GLU   A 1 139 ? 5.48893   -26.01408 -15.97074 1.000 15.87567 ? 146 GLU   A CA  1 
ATOM   1003 C  C   . GLU   A 1 139 ? 5.58566   -25.80997 -17.47605 1.000 17.55938 ? 146 GLU   A C   1 
ATOM   1004 O  O   . GLU   A 1 139 ? 6.68064   -25.90382 -18.03973 1.000 16.82706 ? 146 GLU   A O   1 
ATOM   1005 C  CB  . GLU   A 1 139 ? 5.49453   -27.51697 -15.66915 1.000 17.82609 ? 146 GLU   A CB  1 
ATOM   1006 C  CG  . GLU   A 1 139 ? 4.16066   -28.21540 -15.86518 1.000 29.42138 ? 146 GLU   A CG  1 
ATOM   1007 C  CD  . GLU   A 1 139 ? 4.22125   -29.70024 -15.53179 1.000 52.53637 ? 146 GLU   A CD  1 
ATOM   1008 O  OE1 . GLU   A 1 139 ? 4.78728   -30.05223 -14.47549 1.000 44.58670 ? 146 GLU   A OE1 1 
ATOM   1009 O  OE2 . GLU   A 1 139 ? 3.70925   -30.51583 -16.33105 1.000 51.62265 ? 146 GLU   A OE2 1 
ATOM   1010 N  N   . LYS   A 1 140 ? 4.46455   -25.53972 -18.13445 1.000 16.91855 ? 147 LYS   A N   1 
ATOM   1011 C  CA  . LYS   A 1 140 ? 4.42853   -25.31234 -19.56806 1.000 15.01163 ? 147 LYS   A CA  1 
ATOM   1012 C  C   . LYS   A 1 140 ? 3.32748   -24.30167 -19.83620 1.000 13.44923 ? 147 LYS   A C   1 
ATOM   1013 O  O   . LYS   A 1 140 ? 2.28399   -24.33031 -19.17937 1.000 12.45475 ? 147 LYS   A O   1 
ATOM   1014 C  CB  . LYS   A 1 140 ? 4.17993   -26.62141 -20.32836 1.000 15.53045 ? 147 LYS   A CB  1 
ATOM   1015 C  CG  . LYS   A 1 140 ? 4.06026   -26.47664 -21.83513 1.000 17.83303 ? 147 LYS   A CG  1 
ATOM   1016 C  CD  . LYS   A 1 140 ? 4.03768   -27.84734 -22.49042 1.000 21.75244 ? 147 LYS   A CD  1 
ATOM   1017 C  CE  . LYS   A 1 140 ? 2.64010   -28.24215 -22.92459 1.000 31.40023 ? 147 LYS   A CE  1 
ATOM   1018 N  NZ  . LYS   A 1 140 ? 2.54381   -29.70457 -23.21743 1.000 36.88299 ? 147 LYS   A NZ  1 
ATOM   1019 N  N   . VAL   A 1 141 ? 3.57652   -23.38889 -20.76892 1.000 10.83363 ? 148 VAL   A N   1 
ATOM   1020 C  CA  . VAL   A 1 141 ? 2.59301   -22.38423 -21.15338 1.000 12.11553 ? 148 VAL   A CA  1 
ATOM   1021 C  C   . VAL   A 1 141 ? 2.39045   -22.46527 -22.65699 1.000 16.75537 ? 148 VAL   A C   1 
ATOM   1022 O  O   . VAL   A 1 141 ? 3.36423   -22.47604 -23.41886 1.000 10.60165 ? 148 VAL   A O   1 
ATOM   1023 C  CB  . VAL   A 1 141 ? 3.02122   -20.96264 -20.73915 1.000 12.90758 ? 148 VAL   A CB  1 
ATOM   1024 C  CG1 . VAL   A 1 141 ? 1.98012   -19.93524 -21.19849 1.000 14.78040 ? 148 VAL   A CG1 1 
ATOM   1025 C  CG2 . VAL   A 1 141 ? 3.22383   -20.88618 -19.23304 1.000 10.08132 ? 148 VAL   A CG2 1 
ATOM   1026 N  N   . THR   A 1 142 ? 1.13115   -22.54187 -23.07790 1.000 14.73696 ? 149 THR   A N   1 
ATOM   1027 C  CA  . THR   A 1 142 ? 0.75228   -22.47569 -24.48096 1.000 17.44910 ? 149 THR   A CA  1 
ATOM   1028 C  C   . THR   A 1 142 ? -0.01633  -21.18075 -24.70857 1.000 16.73387 ? 149 THR   A C   1 
ATOM   1029 O  O   . THR   A 1 142 ? -0.93165  -20.85680 -23.94326 1.000 18.89507 ? 149 THR   A O   1 
ATOM   1030 C  CB  . THR   A 1 142 ? -0.10547  -23.67930 -24.88434 1.000 16.77027 ? 149 THR   A CB  1 
ATOM   1031 O  OG1 . THR   A 1 142 ? 0.56174   -24.89412 -24.52684 1.000 20.43825 ? 149 THR   A OG1 1 
ATOM   1032 C  CG2 . THR   A 1 142 ? -0.35698  -23.67789 -26.38880 1.000 22.35894 ? 149 THR   A CG2 1 
ATOM   1033 N  N   . VAL   A 1 143 ? 0.35867   -20.43754 -25.74574 1.000 14.08253 ? 150 VAL   A N   1 
ATOM   1034 C  CA  . VAL   A 1 143 ? -0.32297  -19.19819 -26.10861 1.000 14.10706 ? 150 VAL   A CA  1 
ATOM   1035 C  C   . VAL   A 1 143 ? -0.88907  -19.36482 -27.50965 1.000 15.50012 ? 150 VAL   A C   1 
ATOM   1036 O  O   . VAL   A 1 143 ? -0.13245  -19.52414 -28.47647 1.000 17.65790 ? 150 VAL   A O   1 
ATOM   1037 C  CB  . VAL   A 1 143 ? 0.61019   -17.97872 -26.04176 1.000 14.97301 ? 150 VAL   A CB  1 
ATOM   1038 C  CG1 . VAL   A 1 143 ? -0.13971  -16.71818 -26.46503 1.000 15.07880 ? 150 VAL   A CG1 1 
ATOM   1039 C  CG2 . VAL   A 1 143 ? 1.18020   -17.82013 -24.64542 1.000 13.94752 ? 150 VAL   A CG2 1 
ATOM   1040 N  N   . ILE   A 1 144 ? -2.21437  -19.33679 -27.61518 1.000 11.52110 ? 151 ILE   A N   1 
ATOM   1041 C  CA  . ILE   A 1 144 ? -2.91526  -19.33832 -28.89170 1.000 13.70429 ? 151 ILE   A CA  1 
ATOM   1042 C  C   . ILE   A 1 144 ? -3.37844  -17.91596 -29.15793 1.000 15.58823 ? 151 ILE   A C   1 
ATOM   1043 O  O   . ILE   A 1 144 ? -3.95909  -17.27410 -28.27479 1.000 14.05105 ? 151 ILE   A O   1 
ATOM   1044 C  CB  . ILE   A 1 144 ? -4.11436  -20.30154 -28.87268 1.000 14.78679 ? 151 ILE   A CB  1 
ATOM   1045 C  CG1 . ILE   A 1 144 ? -3.75247  -21.62419 -28.19292 1.000 25.32078 ? 151 ILE   A CG1 1 
ATOM   1046 C  CG2 . ILE   A 1 144 ? -4.64156  -20.51848 -30.28465 1.000 17.14609 ? 151 ILE   A CG2 1 
ATOM   1047 C  CD1 . ILE   A 1 144 ? -2.95998  -22.55338 -29.05690 1.000 20.99385 ? 151 ILE   A CD1 1 
ATOM   1048 N  N   . THR   A 1 145 ? -3.13500  -17.41616 -30.36575 1.000 12.70048 ? 152 THR   A N   1 
ATOM   1049 C  CA  . THR   A 1 145 ? -3.44143  -16.01789 -30.62466 1.000 18.01822 ? 152 THR   A CA  1 
ATOM   1050 C  C   . THR   A 1 145 ? -3.86214  -15.83833 -32.07521 1.000 17.24327 ? 152 THR   A C   1 
ATOM   1051 O  O   . THR   A 1 145 ? -3.40963  -16.55951 -32.96958 1.000 13.78612 ? 152 THR   A O   1 
ATOM   1052 C  CB  . THR   A 1 145 ? -2.24781  -15.11040 -30.27621 1.000 17.36051 ? 152 THR   A CB  1 
ATOM   1053 O  OG1 . THR   A 1 145 ? -2.66817  -13.74064 -30.24700 1.000 18.15827 ? 152 THR   A OG1 1 
ATOM   1054 C  CG2 . THR   A 1 145 ? -1.11255  -15.27613 -31.28145 1.000 16.94058 ? 152 THR   A CG2 1 
ATOM   1055 N  N   . LYS   A 1 146 ? -4.75615  -14.87624 -32.28872 1.000 12.40998 ? 153 LYS   A N   1 
ATOM   1056 C  CA  . LYS   A 1 146 ? -5.22792  -14.51812 -33.62038 1.000 14.90808 ? 153 LYS   A CA  1 
ATOM   1057 C  C   . LYS   A 1 146 ? -5.33341  -13.00482 -33.69874 1.000 16.47908 ? 153 LYS   A C   1 
ATOM   1058 O  O   . LYS   A 1 146 ? -6.14362  -12.40083 -32.98987 1.000 15.08469 ? 153 LYS   A O   1 
ATOM   1059 C  CB  . LYS   A 1 146 ? -6.58222  -15.16226 -33.92938 1.000 14.33118 ? 153 LYS   A CB  1 
ATOM   1060 C  CG  . LYS   A 1 146 ? -7.19810  -14.71679 -35.25368 1.000 14.16394 ? 153 LYS   A CG  1 
ATOM   1061 C  CD  . LYS   A 1 146 ? -6.46136  -15.30428 -36.45100 1.000 17.44288 ? 153 LYS   A CD  1 
ATOM   1062 C  CE  . LYS   A 1 146 ? -7.15179  -14.94744 -37.77049 1.000 19.34295 ? 153 LYS   A CE  1 
ATOM   1063 N  NZ  . LYS   A 1 146 ? -7.10787  -13.49092 -38.08393 1.000 16.14796 ? 153 LYS   A NZ  1 
ATOM   1064 N  N   . HIS   A 1 147 ? -4.52425  -12.40526 -34.56097 1.000 14.50715 ? 154 HIS   A N   1 
ATOM   1065 C  CA  . HIS   A 1 147 ? -4.55053  -10.97845 -34.84503 1.000 16.16035 ? 154 HIS   A CA  1 
ATOM   1066 C  C   . HIS   A 1 147 ? -5.25932  -10.76002 -36.17872 1.000 19.39324 ? 154 HIS   A C   1 
ATOM   1067 O  O   . HIS   A 1 147 ? -5.20763  -11.61627 -37.06530 1.000 16.30585 ? 154 HIS   A O   1 
ATOM   1068 C  CB  . HIS   A 1 147 ? -3.11491  -10.43717 -34.88617 1.000 13.86235 ? 154 HIS   A CB  1 
ATOM   1069 C  CG  . HIS   A 1 147 ? -3.01097  -8.94610  -34.97825 1.000 13.48024 ? 154 HIS   A CG  1 
ATOM   1070 N  ND1 . HIS   A 1 147 ? -3.20778  -8.25341  -36.15297 1.000 16.32541 ? 154 HIS   A ND1 1 
ATOM   1071 C  CD2 . HIS   A 1 147 ? -2.68479  -8.01947  -34.04597 1.000 16.78899 ? 154 HIS   A CD2 1 
ATOM   1072 C  CE1 . HIS   A 1 147 ? -3.03340  -6.96200  -35.93556 1.000 18.01275 ? 154 HIS   A CE1 1 
ATOM   1073 N  NE2 . HIS   A 1 147 ? -2.71227  -6.79362  -34.66518 1.000 15.23128 ? 154 HIS   A NE2 1 
ATOM   1074 N  N   . ASN   A 1 148 ? -5.94448  -9.61571  -36.31392 1.000 18.47057 ? 155 ASN   A N   1 
ATOM   1075 C  CA  . ASN   A 1 148 ? -6.67504  -9.34620  -37.55448 1.000 19.12060 ? 155 ASN   A CA  1 
ATOM   1076 C  C   . ASN   A 1 148 ? -5.77931  -9.43341  -38.78683 1.000 19.85141 ? 155 ASN   A C   1 
ATOM   1077 O  O   . ASN   A 1 148 ? -6.25289  -9.78975  -39.87223 1.000 20.09345 ? 155 ASN   A O   1 
ATOM   1078 C  CB  . ASN   A 1 148 ? -7.34680  -7.96733  -37.51413 1.000 20.02601 ? 155 ASN   A CB  1 
ATOM   1079 C  CG  . ASN   A 1 148 ? -8.61950  -7.95263  -36.68868 1.000 23.77781 ? 155 ASN   A CG  1 
ATOM   1080 O  OD1 . ASN   A 1 148 ? -9.27661  -8.98111  -36.51503 1.000 24.13003 ? 155 ASN   A OD1 1 
ATOM   1081 N  ND2 . ASN   A 1 148 ? -8.99531  -6.77038  -36.20397 1.000 22.57503 ? 155 ASN   A ND2 1 
ATOM   1082 N  N   . ASP   A 1 149 ? -4.49249  -9.12251  -38.64589 1.000 19.28259 ? 156 ASP   A N   1 
ATOM   1083 C  CA  . ASP   A 1 149 ? -3.58026  -9.05049  -39.77978 1.000 19.46779 ? 156 ASP   A CA  1 
ATOM   1084 C  C   . ASP   A 1 149 ? -2.75066  -10.31661 -39.97399 1.000 25.24847 ? 156 ASP   A C   1 
ATOM   1085 O  O   . ASP   A 1 149 ? -1.78659  -10.29191 -40.74612 1.000 23.33261 ? 156 ASP   A O   1 
ATOM   1086 C  CB  . ASP   A 1 149 ? -2.64210  -7.85004  -39.62690 1.000 22.21800 ? 156 ASP   A CB  1 
ATOM   1087 C  CG  . ASP   A 1 149 ? -3.38116  -6.53017  -39.58530 1.000 31.32641 ? 156 ASP   A CG  1 
ATOM   1088 O  OD1 . ASP   A 1 149 ? -4.53742  -6.47864  -40.05129 1.000 26.40297 ? 156 ASP   A OD1 1 
ATOM   1089 O  OD2 . ASP   A 1 149 ? -2.80480  -5.54473  -39.07761 1.000 32.11527 ? 156 ASP   A OD2 1 
ATOM   1090 N  N   . ASP   A 1 150 ? -3.09220  -11.41794 -39.30701 1.000 20.57109 ? 157 ASP   A N   1 
ATOM   1091 C  CA  . ASP   A 1 150 ? -2.30160  -12.63726 -39.42451 1.000 19.22135 ? 157 ASP   A CA  1 
ATOM   1092 C  C   . ASP   A 1 150 ? -3.19550  -13.84716 -39.17221 1.000 24.76051 ? 157 ASP   A C   1 
ATOM   1093 O  O   . ASP   A 1 150 ? -4.38945  -13.71806 -38.88632 1.000 19.91164 ? 157 ASP   A O   1 
ATOM   1094 C  CB  . ASP   A 1 150 ? -1.10864  -12.60705 -38.46164 1.000 17.23846 ? 157 ASP   A CB  1 
ATOM   1095 C  CG  . ASP   A 1 150 ? 0.08937   -13.37101 -38.99047 1.000 19.93430 ? 157 ASP   A CG  1 
ATOM   1096 O  OD1 . ASP   A 1 150 ? -0.07559  -14.14931 -39.95211 1.000 20.15892 ? 157 ASP   A OD1 1 
ATOM   1097 O  OD2 . ASP   A 1 150 ? 1.19803   -13.19203 -38.44225 1.000 22.31254 ? 157 ASP   A OD2 1 
ATOM   1098 N  N   . GLU   A 1 151 ? -2.60522  -15.03258 -39.29689 1.000 17.95691 ? 158 GLU   A N   1 
ATOM   1099 C  CA  . GLU   A 1 151 ? -3.29788  -16.28818 -39.05608 1.000 21.56373 ? 158 GLU   A CA  1 
ATOM   1100 C  C   . GLU   A 1 151 ? -3.19247  -16.67974 -37.58341 1.000 17.52834 ? 158 GLU   A C   1 
ATOM   1101 O  O   . GLU   A 1 151 ? -2.50098  -16.03971 -36.79011 1.000 17.69144 ? 158 GLU   A O   1 
ATOM   1102 C  CB  . GLU   A 1 151 ? -2.72311  -17.39574 -39.94003 1.000 24.91018 ? 158 GLU   A CB  1 
ATOM   1103 C  CG  . GLU   A 1 151 ? -2.73260  -17.08431 -41.42969 1.000 38.42985 ? 158 GLU   A CG  1 
ATOM   1104 C  CD  . GLU   A 1 151 ? -4.11321  -16.72618 -41.95709 1.000 63.00232 ? 158 GLU   A CD  1 
ATOM   1105 O  OE1 . GLU   A 1 151 ? -5.11025  -17.29217 -41.45798 1.000 66.36907 ? 158 GLU   A OE1 1 
ATOM   1106 O  OE2 . GLU   A 1 151 ? -4.20470  -15.88143 -42.87329 1.000 67.19458 ? 158 GLU   A OE2 1 
ATOM   1107 N  N   . GLN   A 1 152 ? -3.88862  -17.75623 -37.22201 1.000 16.53055 ? 159 GLN   A N   1 
ATOM   1108 C  CA  . GLN   A 1 152 ? -3.87203  -18.24660 -35.84883 1.000 17.84213 ? 159 GLN   A CA  1 
ATOM   1109 C  C   . GLN   A 1 152 ? -2.61085  -19.06301 -35.58627 1.000 17.38388 ? 159 GLN   A C   1 
ATOM   1110 O  O   . GLN   A 1 152 ? -2.31160  -20.01299 -36.31779 1.000 17.75970 ? 159 GLN   A O   1 
ATOM   1111 C  CB  . GLN   A 1 152 ? -5.10993  -19.09628 -35.57256 1.000 19.10927 ? 159 GLN   A CB  1 
ATOM   1112 C  CG  . GLN   A 1 152 ? -5.35896  -19.35550 -34.09766 1.000 15.63800 ? 159 GLN   A CG  1 
ATOM   1113 C  CD  . GLN   A 1 152 ? -6.78848  -19.78046 -33.81849 1.000 22.61336 ? 159 GLN   A CD  1 
ATOM   1114 O  OE1 . GLN   A 1 152 ? -7.73078  -19.06808 -34.15493 1.000 22.96123 ? 159 GLN   A OE1 1 
ATOM   1115 N  NE2 . GLN   A 1 152 ? -6.95549  -20.93550 -33.18375 1.000 21.75522 ? 159 GLN   A NE2 1 
ATOM   1116 N  N   . TYR   A 1 153 ? -1.88681  -18.70983 -34.52517 1.000 12.74284 ? 160 TYR   A N   1 
ATOM   1117 C  CA  . TYR   A 1 153 ? -0.62761  -19.36129 -34.19625 1.000 15.09134 ? 160 TYR   A CA  1 
ATOM   1118 C  C   . TYR   A 1 153 ? -0.63708  -19.85478 -32.75661 1.000 17.82968 ? 160 TYR   A C   1 
ATOM   1119 O  O   . TYR   A 1 153 ? -1.35806  -19.32880 -31.90314 1.000 16.57500 ? 160 TYR   A O   1 
ATOM   1120 C  CB  . TYR   A 1 153 ? 0.56280   -18.41473 -34.40850 1.000 13.99693 ? 160 TYR   A CB  1 
ATOM   1121 C  CG  . TYR   A 1 153 ? 0.92756   -18.22942 -35.86026 1.000 18.81610 ? 160 TYR   A CG  1 
ATOM   1122 C  CD1 . TYR   A 1 153 ? 1.78097   -19.11951 -36.49687 1.000 19.98815 ? 160 TYR   A CD1 1 
ATOM   1123 C  CD2 . TYR   A 1 153 ? 0.41374   -17.17118 -36.59715 1.000 18.20884 ? 160 TYR   A CD2 1 
ATOM   1124 C  CE1 . TYR   A 1 153 ? 2.11598   -18.96128 -37.82287 1.000 22.48717 ? 160 TYR   A CE1 1 
ATOM   1125 C  CE2 . TYR   A 1 153 ? 0.74248   -17.00543 -37.92931 1.000 20.94500 ? 160 TYR   A CE2 1 
ATOM   1126 C  CZ  . TYR   A 1 153 ? 1.59580   -17.90505 -38.53454 1.000 27.52796 ? 160 TYR   A CZ  1 
ATOM   1127 O  OH  . TYR   A 1 153 ? 1.93449   -17.75292 -39.85841 1.000 35.07673 ? 160 TYR   A OH  1 
ATOM   1128 N  N   . ALA   A 1 154 ? 0.18736   -20.86922 -32.49745 1.000 13.11927 ? 161 ALA   A N   1 
ATOM   1129 C  CA  . ALA   A 1 154 ? 0.38169   -21.42381 -31.16271 1.000 12.57023 ? 161 ALA   A CA  1 
ATOM   1130 C  C   . ALA   A 1 154 ? 1.84537   -21.27292 -30.77120 1.000 16.04807 ? 161 ALA   A C   1 
ATOM   1131 O  O   . ALA   A 1 154 ? 2.73011   -21.78454 -31.46506 1.000 14.84909 ? 161 ALA   A O   1 
ATOM   1132 C  CB  . ALA   A 1 154 ? -0.03209  -22.89686 -31.11129 1.000 15.92904 ? 161 ALA   A CB  1 
ATOM   1133 N  N   . TRP   A 1 155 ? 2.09202   -20.56766 -29.67031 1.000 12.14201 ? 162 TRP   A N   1 
ATOM   1134 C  CA  . TRP   A 1 155 ? 3.40647   -20.45326 -29.04778 1.000 11.34455 ? 162 TRP   A CA  1 
ATOM   1135 C  C   . TRP   A 1 155 ? 3.43505   -21.37745 -27.83532 1.000 15.97599 ? 162 TRP   A C   1 
ATOM   1136 O  O   . TRP   A 1 155 ? 2.41729   -21.54691 -27.15706 1.000 15.86097 ? 162 TRP   A O   1 
ATOM   1137 C  CB  . TRP   A 1 155 ? 3.65409   -18.99028 -28.64997 1.000 12.35308 ? 162 TRP   A CB  1 
ATOM   1138 C  CG  . TRP   A 1 155 ? 4.91034   -18.63592 -27.87442 1.000 13.01172 ? 162 TRP   A CG  1 
ATOM   1139 C  CD1 . TRP   A 1 155 ? 6.00918   -17.98343 -28.36046 1.000 11.22255 ? 162 TRP   A CD1 1 
ATOM   1140 C  CD2 . TRP   A 1 155 ? 5.15744   -18.83936 -26.47244 1.000 12.84144 ? 162 TRP   A CD2 1 
ATOM   1141 N  NE1 . TRP   A 1 155 ? 6.93244   -17.79444 -27.35955 1.000 12.86585 ? 162 TRP   A NE1 1 
ATOM   1142 C  CE2 . TRP   A 1 155 ? 6.43426   -18.31149 -26.19237 1.000 13.93540 ? 162 TRP   A CE2 1 
ATOM   1143 C  CE3 . TRP   A 1 155 ? 4.42959   -19.42830 -25.43219 1.000 13.86062 ? 162 TRP   A CE3 1 
ATOM   1144 C  CZ2 . TRP   A 1 155 ? 6.99901   -18.35602 -24.91744 1.000 12.62352 ? 162 TRP   A CZ2 1 
ATOM   1145 C  CZ3 . TRP   A 1 155 ? 4.99470   -19.47463 -24.16917 1.000 13.13252 ? 162 TRP   A CZ3 1 
ATOM   1146 C  CH2 . TRP   A 1 155 ? 6.26712   -18.93880 -23.92337 1.000 15.25399 ? 162 TRP   A CH2 1 
ATOM   1147 N  N   . GLU   A 1 156 ? 4.58458   -22.00036 -27.57302 1.000 10.82271 ? 163 GLU   A N   1 
ATOM   1148 C  CA  . GLU   A 1 156 ? 4.65390   -22.92396 -26.45004 1.000 10.48732 ? 163 GLU   A CA  1 
ATOM   1149 C  C   . GLU   A 1 156 ? 6.07254   -22.98434 -25.89885 1.000 12.12678 ? 163 GLU   A C   1 
ATOM   1150 O  O   . GLU   A 1 156 ? 7.04385   -22.96814 -26.65982 1.000 12.13325 ? 163 GLU   A O   1 
ATOM   1151 C  CB  . GLU   A 1 156 ? 4.18346   -24.32377 -26.86292 1.000 17.42725 ? 163 GLU   A CB  1 
ATOM   1152 C  CG  . GLU   A 1 156 ? 4.04783   -25.29582 -25.70894 1.000 18.64380 ? 163 GLU   A CG  1 
ATOM   1153 C  CD  . GLU   A 1 156 ? 3.28497   -26.54637 -26.09523 1.000 33.14954 ? 163 GLU   A CD  1 
ATOM   1154 O  OE1 . GLU   A 1 156 ? 3.92896   -27.50429 -26.56489 1.000 31.25516 ? 163 GLU   A OE1 1 
ATOM   1155 O  OE2 . GLU   A 1 156 ? 2.04463   -26.56890 -25.93584 1.000 30.15293 ? 163 GLU   A OE2 1 
ATOM   1156 N  N   . SER   A 1 157 ? 6.18478   -23.05750 -24.57265 1.000 13.12759 ? 164 SER   A N   1 
ATOM   1157 C  CA  . SER   A 1 157 ? 7.49230   -23.21495 -23.94579 1.000 13.29473 ? 164 SER   A CA  1 
ATOM   1158 C  C   . SER   A 1 157 ? 7.33943   -23.84493 -22.57197 1.000 13.38129 ? 164 SER   A C   1 
ATOM   1159 O  O   . SER   A 1 157 ? 6.46221   -23.44973 -21.79522 1.000 14.54244 ? 164 SER   A O   1 
ATOM   1160 C  CB  . SER   A 1 157 ? 8.22287   -21.87510 -23.81455 1.000 10.62557 ? 164 SER   A CB  1 
ATOM   1161 O  OG  . SER   A 1 157 ? 9.50970   -22.07130 -23.24039 1.000 12.55896 ? 164 SER   A OG  1 
ATOM   1162 N  N   . SER   A 1 158 ? 8.20093   -24.81816 -22.27940 1.000 14.61229 ? 165 SER   A N   1 
ATOM   1163 C  CA  . SER   A 1 158 ? 8.41248   -25.30948 -20.92502 1.000 12.96026 ? 165 SER   A CA  1 
ATOM   1164 C  C   . SER   A 1 158 ? 9.67221   -24.71474 -20.30538 1.000 16.85913 ? 165 SER   A C   1 
ATOM   1165 O  O   . SER   A 1 158 ? 10.32588  -25.36422 -19.48139 1.000 18.96764 ? 165 SER   A O   1 
ATOM   1166 C  CB  . SER   A 1 158 ? 8.48636   -26.83514 -20.92528 1.000 17.01275 ? 165 SER   A CB  1 
ATOM   1167 O  OG  . SER   A 1 158 ? 7.26987   -27.38682 -21.39993 1.000 21.28981 ? 165 SER   A OG  1 
ATOM   1168 N  N   . ALA   A 1 159 ? 10.02693  -23.49880 -20.70549 1.000 13.32835 ? 166 ALA   A N   1 
ATOM   1169 C  CA  . ALA   A 1 159 ? 11.26785  -22.81512 -20.30243 1.000 15.37038 ? 166 ALA   A CA  1 
ATOM   1170 C  C   . ALA   A 1 159 ? 12.43622  -23.66146 -20.81656 1.000 19.68399 ? 166 ALA   A C   1 
ATOM   1171 O  O   . ALA   A 1 159 ? 12.33790  -24.25973 -21.89851 1.000 24.85946 ? 166 ALA   A O   1 
ATOM   1172 C  CB  . ALA   A 1 159 ? 11.27216  -22.55043 -18.81212 1.000 19.07279 ? 166 ALA   A CB  1 
ATOM   1173 N  N   . GLY   A 1 160 ? 13.54653  -23.73132 -20.09007 1.000 22.29614 ? 167 GLY   A N   1 
ATOM   1174 C  CA  . GLY   A 1 160 ? 14.66899  -24.50494 -20.57640 1.000 18.10560 ? 167 GLY   A CA  1 
ATOM   1175 C  C   . GLY   A 1 160 ? 15.37710  -23.91055 -21.77023 1.000 24.21234 ? 167 GLY   A C   1 
ATOM   1176 O  O   . GLY   A 1 160 ? 16.16574  -24.60373 -22.41794 1.000 21.56449 ? 167 GLY   A O   1 
ATOM   1177 N  N   . GLY   A 1 161 ? 15.09852  -22.65139 -22.10028 1.000 16.41770 ? 168 GLY   A N   1 
ATOM   1178 C  CA  . GLY   A 1 161 ? 15.86202  -21.92800 -23.09376 1.000 16.05548 ? 168 GLY   A CA  1 
ATOM   1179 C  C   . GLY   A 1 161 ? 15.27766  -21.88644 -24.48787 1.000 14.91278 ? 168 GLY   A C   1 
ATOM   1180 O  O   . GLY   A 1 161 ? 15.87737  -21.25615 -25.36448 1.000 14.18250 ? 168 GLY   A O   1 
ATOM   1181 N  N   . SER   A 1 162 ? 14.13468  -22.52419 -24.73100 1.000 15.49703 ? 169 SER   A N   1 
ATOM   1182 C  CA  . SER   A 1 162 ? 13.58760  -22.56094 -26.07817 1.000 12.92938 ? 169 SER   A CA  1 
ATOM   1183 C  C   . SER   A 1 162 ? 12.06845  -22.46193 -26.04466 1.000 16.30651 ? 169 SER   A C   1 
ATOM   1184 O  O   . SER   A 1 162 ? 11.42020  -22.76349 -25.03856 1.000 14.26855 ? 169 SER   A O   1 
ATOM   1185 C  CB  . SER   A 1 162 ? 14.02021  -23.83368 -26.82467 1.000 14.67579 ? 169 SER   A CB  1 
ATOM   1186 O  OG  . SER   A 1 162 ? 13.34625  -24.97708 -26.32885 1.000 17.79512 ? 169 SER   A OG  1 
ATOM   1187 N  N   . PHE   A 1 163 ? 11.50981  -22.02660 -27.17437 1.000 15.46681 ? 170 PHE   A N   1 
ATOM   1188 C  CA  . PHE   A 1 163 ? 10.07162  -22.02467 -27.38964 1.000 15.48071 ? 170 PHE   A CA  1 
ATOM   1189 C  C   . PHE   A 1 163 ? 9.79790   -22.45738 -28.82338 1.000 15.73245 ? 170 PHE   A C   1 
ATOM   1190 O  O   . PHE   A 1 163 ? 10.68628  -22.44137 -29.67814 1.000 14.25853 ? 170 PHE   A O   1 
ATOM   1191 C  CB  . PHE   A 1 163 ? 9.44454   -20.64790 -27.09769 1.000 13.13763 ? 170 PHE   A CB  1 
ATOM   1192 C  CG  . PHE   A 1 163 ? 9.92728   -19.53688 -28.00000 1.000 10.75581 ? 170 PHE   A CG  1 
ATOM   1193 C  CD1 . PHE   A 1 163 ? 11.07150  -18.81845 -27.69142 1.000 17.58119 ? 170 PHE   A CD1 1 
ATOM   1194 C  CD2 . PHE   A 1 163 ? 9.21289   -19.18827 -29.13735 1.000 13.89378 ? 170 PHE   A CD2 1 
ATOM   1195 C  CE1 . PHE   A 1 163 ? 11.50806  -17.78528 -28.51003 1.000 17.86424 ? 170 PHE   A CE1 1 
ATOM   1196 C  CE2 . PHE   A 1 163 ? 9.64415   -18.16023 -29.96088 1.000 12.96638 ? 170 PHE   A CE2 1 
ATOM   1197 C  CZ  . PHE   A 1 163 ? 10.79141  -17.45307 -29.64260 1.000 15.16143 ? 170 PHE   A CZ  1 
ATOM   1198 N  N   . THR   A 1 164 ? 8.55912   -22.86929 -29.07949 1.000 13.38637 ? 171 THR   A N   1 
ATOM   1199 C  CA  . THR   A 1 164 ? 8.15142   -23.26981 -30.41504 1.000 12.68152 ? 171 THR   A CA  1 
ATOM   1200 C  C   . THR   A 1 164 ? 6.99576   -22.40237 -30.88602 1.000 12.17871 ? 171 THR   A C   1 
ATOM   1201 O  O   . THR   A 1 164 ? 6.23928   -21.85436 -30.08094 1.000 11.31385 ? 171 THR   A O   1 
ATOM   1202 C  CB  . THR   A 1 164 ? 7.73667   -24.74793 -30.47387 1.000 14.72434 ? 171 THR   A CB  1 
ATOM   1203 O  OG1 . THR   A 1 164 ? 6.56710   -24.94989 -29.66851 1.000 17.48310 ? 171 THR   A OG1 1 
ATOM   1204 C  CG2 . THR   A 1 164 ? 8.86946   -25.65464 -29.99415 1.000 14.41506 ? 171 THR   A CG2 1 
ATOM   1205 N  N   . VAL   A 1 165 ? 6.88528   -22.26831 -32.20341 1.000 13.22797 ? 172 VAL   A N   1 
ATOM   1206 C  CA  . VAL   A 1 165 ? 5.76996   -21.58294 -32.84102 1.000 15.13364 ? 172 VAL   A CA  1 
ATOM   1207 C  C   . VAL   A 1 165 ? 5.28907   -22.45545 -33.98877 1.000 14.48114 ? 172 VAL   A C   1 
ATOM   1208 O  O   . VAL   A 1 165 ? 6.09699   -22.99461 -34.75408 1.000 15.33149 ? 172 VAL   A O   1 
ATOM   1209 C  CB  . VAL   A 1 165 ? 6.15554   -20.17237 -33.34501 1.000 13.87945 ? 172 VAL   A CB  1 
ATOM   1210 C  CG1 . VAL   A 1 165 ? 5.00151   -19.54734 -34.13046 1.000 17.26182 ? 172 VAL   A CG1 1 
ATOM   1211 C  CG2 . VAL   A 1 165 ? 6.54557   -19.27160 -32.17971 1.000 14.25389 ? 172 VAL   A CG2 1 
ATOM   1212 N  N   . ARG   A 1 166 ? 3.97340   -22.61291 -34.09471 1.000 13.87733 ? 173 ARG   A N   1 
ATOM   1213 C  CA  . ARG   A 1 166 ? 3.39021   -23.37363 -35.18592 1.000 15.13184 ? 173 ARG   A CA  1 
ATOM   1214 C  C   . ARG   A 1 166 ? 2.04607   -22.75935 -35.52587 1.000 15.01021 ? 173 ARG   A C   1 
ATOM   1215 O  O   . ARG   A 1 166 ? 1.43750   -22.06663 -34.70787 1.000 13.98734 ? 173 ARG   A O   1 
ATOM   1216 C  CB  . ARG   A 1 166 ? 3.21317   -24.85214 -34.82358 1.000 16.10784 ? 173 ARG   A CB  1 
ATOM   1217 C  CG  . ARG   A 1 166 ? 2.21820   -25.09712 -33.69653 1.000 20.09382 ? 173 ARG   A CG  1 
ATOM   1218 C  CD  . ARG   A 1 166 ? 2.37298   -26.49499 -33.10908 1.000 28.81771 ? 173 ARG   A CD  1 
ATOM   1219 N  NE  . ARG   A 1 166 ? 3.48476   -26.56005 -32.16629 1.000 30.89437 ? 173 ARG   A NE  1 
ATOM   1220 C  CZ  . ARG   A 1 166 ? 4.00020   -27.68411 -31.68651 1.000 43.05346 ? 173 ARG   A CZ  1 
ATOM   1221 N  NH1 . ARG   A 1 166 ? 3.53207   -28.86787 -32.04602 1.000 31.55307 ? 173 ARG   A NH1 1 
ATOM   1222 N  NH2 . ARG   A 1 166 ? 5.01861   -27.61881 -30.83253 1.000 36.55045 ? 173 ARG   A NH2 1 
ATOM   1223 N  N   . THR   A 1 167 ? 1.59696   -23.00732 -36.75083 1.000 16.21721 ? 174 THR   A N   1 
ATOM   1224 C  CA  . THR   A 1 167 ? 0.22661   -22.67957 -37.11071 1.000 18.58532 ? 174 THR   A CA  1 
ATOM   1225 C  C   . THR   A 1 167 ? -0.72254  -23.53562 -36.28452 1.000 20.63651 ? 174 THR   A C   1 
ATOM   1226 O  O   . THR   A 1 167 ? -0.54704  -24.75167 -36.18035 1.000 20.92163 ? 174 THR   A O   1 
ATOM   1227 C  CB  . THR   A 1 167 ? 0.00470   -22.91298 -38.60501 1.000 24.48714 ? 174 THR   A CB  1 
ATOM   1228 O  OG1 . THR   A 1 167 ? 0.92408   -22.10609 -39.35075 1.000 28.15753 ? 174 THR   A OG1 1 
ATOM   1229 C  CG2 . THR   A 1 167 ? -1.41492  -22.55034 -39.00507 1.000 32.16979 ? 174 THR   A CG2 1 
ATOM   1230 N  N   . ASP   A 1 168 ? -1.71905  -22.90020 -35.67912 1.000 20.54953 ? 175 ASP   A N   1 
ATOM   1231 C  CA  . ASP   A 1 168 ? -2.61619  -23.59601 -34.76828 1.000 22.26564 ? 175 ASP   A CA  1 
ATOM   1232 C  C   . ASP   A 1 168 ? -3.74200  -24.26144 -35.55015 1.000 35.08327 ? 175 ASP   A C   1 
ATOM   1233 O  O   . ASP   A 1 168 ? -4.36359  -23.63606 -36.41559 1.000 29.39361 ? 175 ASP   A O   1 
ATOM   1234 C  CB  . ASP   A 1 168 ? -3.18613  -22.63310 -33.72699 1.000 24.33137 ? 175 ASP   A CB  1 
ATOM   1235 C  CG  . ASP   A 1 168 ? -4.09494  -23.32785 -32.73009 1.000 34.27560 ? 175 ASP   A CG  1 
ATOM   1236 O  OD1 . ASP   A 1 168 ? -3.65997  -24.32815 -32.12135 1.000 36.67747 ? 175 ASP   A OD1 1 
ATOM   1237 O  OD2 . ASP   A 1 168 ? -5.24666  -22.87546 -32.55901 1.000 29.61095 ? 175 ASP   A OD2 1 
ATOM   1238 N  N   . THR   A 1 169 ? -3.99587  -25.53217 -35.24504 1.000 37.77804 ? 176 THR   A N   1 
ATOM   1239 C  CA  . THR   A 1 169 ? -5.08593  -26.27711 -35.85644 1.000 50.88440 ? 176 THR   A CA  1 
ATOM   1240 C  C   . THR   A 1 169 ? -6.26571  -26.47956 -34.91706 1.000 51.19902 ? 176 THR   A C   1 
ATOM   1241 O  O   . THR   A 1 169 ? -7.21168  -27.19201 -35.28132 1.000 52.72164 ? 176 THR   A O   1 
ATOM   1242 C  CB  . THR   A 1 169 ? -4.59190  -27.64155 -36.34849 1.000 58.24463 ? 176 THR   A CB  1 
ATOM   1243 O  OG1 . THR   A 1 169 ? -3.74015  -28.22926 -35.35568 1.000 47.71026 ? 176 THR   A OG1 1 
ATOM   1244 C  CG2 . THR   A 1 169 ? -3.83123  -27.49029 -37.65872 1.000 45.51150 ? 176 THR   A CG2 1 
ATOM   1245 N  N   . GLY   A 1 170 ? -6.23758  -25.88382 -33.72695 1.000 44.39887 ? 177 GLY   A N   1 
ATOM   1246 C  CA  . GLY   A 1 170 ? -7.33980  -25.99755 -32.79802 1.000 47.06859 ? 177 GLY   A CA  1 
ATOM   1247 C  C   . GLY   A 1 170 ? -8.55761  -25.21824 -33.26938 1.000 35.63705 ? 177 GLY   A C   1 
ATOM   1248 O  O   . GLY   A 1 170 ? -8.69969  -24.84654 -34.43366 1.000 31.47942 ? 177 GLY   A O   1 
ATOM   1249 N  N   . GLU   A 1 171 ? -9.46045  -24.98683 -32.32827 1.000 40.67701 ? 178 GLU   A N   1 
ATOM   1250 C  CA  . GLU   A 1 171 ? -10.66558 -24.21464 -32.60257 1.000 36.07141 ? 178 GLU   A CA  1 
ATOM   1251 C  C   . GLU   A 1 171 ? -10.28534 -22.80729 -33.05448 1.000 21.39486 ? 178 GLU   A C   1 
ATOM   1252 O  O   . GLU   A 1 171 ? -9.44057  -22.16865 -32.41130 1.000 22.35465 ? 178 GLU   A O   1 
ATOM   1253 C  CB  . GLU   A 1 171 ? -11.53489 -24.13098 -31.34455 1.000 31.46238 ? 178 GLU   A CB  1 
ATOM   1254 C  CG  . GLU   A 1 171 ? -12.57038 -25.24051 -31.17307 1.000 40.09937 ? 178 GLU   A CG  1 
ATOM   1255 C  CD  . GLU   A 1 171 ? -13.34174 -25.53757 -32.44122 1.000 32.13213 ? 178 GLU   A CD  1 
ATOM   1256 O  OE1 . GLU   A 1 171 ? -14.22107 -24.72911 -32.80578 1.000 38.41943 ? 178 GLU   A OE1 1 
ATOM   1257 O  OE2 . GLU   A 1 171 ? -13.08044 -26.59122 -33.06158 1.000 37.54305 ? 178 GLU   A OE2 1 
ATOM   1258 N  N   . PRO   A 1 172 ? -10.83693 -22.31314 -34.16254 1.000 32.67130 ? 179 PRO   A N   1 
ATOM   1259 C  CA  . PRO   A 1 172 ? -10.65446 -20.90533 -34.51296 1.000 32.88624 ? 179 PRO   A CA  1 
ATOM   1260 C  C   . PRO   A 1 172 ? -11.00504 -19.98355 -33.35156 1.000 34.64579 ? 179 PRO   A C   1 
ATOM   1261 O  O   . PRO   A 1 172 ? -11.97445 -20.21346 -32.62670 1.000 34.57545 ? 179 PRO   A O   1 
ATOM   1262 C  CB  . PRO   A 1 172 ? -11.63082 -20.73018 -35.67497 1.000 38.11937 ? 179 PRO   A CB  1 
ATOM   1263 C  CG  . PRO   A 1 172 ? -11.58641 -22.07085 -36.39968 1.000 45.26036 ? 179 PRO   A CG  1 
ATOM   1264 C  CD  . PRO   A 1 172 ? -11.04322 -23.10291 -35.39043 1.000 38.55571 ? 179 PRO   A CD  1 
ATOM   1265 N  N   . MET   A 1 173 ? -10.21746 -18.91764 -33.18607 1.000 21.47120 ? 180 MET   A N   1 
ATOM   1266 C  CA  . MET   A 1 173 ? -10.47315 -17.95857 -32.11532 1.000 24.46566 ? 180 MET   A CA  1 
ATOM   1267 C  C   . MET   A 1 173 ? -11.27451 -16.74908 -32.56851 1.000 31.58027 ? 180 MET   A C   1 
ATOM   1268 O  O   . MET   A 1 173 ? -11.95126 -16.12130 -31.74579 1.000 40.99928 ? 180 MET   A O   1 
ATOM   1269 C  CB  . MET   A 1 173 ? -9.16030  -17.45399 -31.51863 1.000 27.77503 ? 180 MET   A CB  1 
ATOM   1270 C  CG  . MET   A 1 173 ? -8.22392  -18.52254 -31.02824 1.000 47.23658 ? 180 MET   A CG  1 
ATOM   1271 S  SD  . MET   A 1 173 ? -7.13139  -17.83659 -29.78285 1.000 47.86539 ? 180 MET   A SD  1 
ATOM   1272 C  CE  . MET   A 1 173 ? -8.31781  -17.29635 -28.55833 1.000 38.25987 ? 180 MET   A CE  1 
ATOM   1273 N  N   . GLY   A 1 174 ? -11.19441 -16.38770 -33.84287 1.000 23.99323 ? 181 GLY   A N   1 
ATOM   1274 C  CA  . GLY   A 1 174 ? -11.80957 -15.15499 -34.29358 1.000 24.36290 ? 181 GLY   A CA  1 
ATOM   1275 C  C   . GLY   A 1 174 ? -10.86205 -13.98643 -34.13350 1.000 19.83088 ? 181 GLY   A C   1 
ATOM   1276 O  O   . GLY   A 1 174 ? -10.37004 -13.43735 -35.12303 1.000 18.52757 ? 181 GLY   A O   1 
ATOM   1277 N  N   . ARG   A 1 175 ? -10.59290 -13.61024 -32.88321 1.000 14.39269 ? 182 ARG   A N   1 
ATOM   1278 C  CA  . ARG   A 1 175 ? -9.58305  -12.60890 -32.56110 1.000 15.14668 ? 182 ARG   A CA  1 
ATOM   1279 C  C   . ARG   A 1 175 ? -9.29741  -12.64287 -31.06780 1.000 17.31307 ? 182 ARG   A C   1 
ATOM   1280 O  O   . ARG   A 1 175 ? -10.23113 -12.69235 -30.25927 1.000 15.88153 ? 182 ARG   A O   1 
ATOM   1281 C  CB  . ARG   A 1 175 ? -10.03093 -11.19650 -32.95628 1.000 13.96590 ? 182 ARG   A CB  1 
ATOM   1282 C  CG  . ARG   A 1 175 ? -8.94356  -10.13835 -32.72483 1.000 14.22502 ? 182 ARG   A CG  1 
ATOM   1283 C  CD  . ARG   A 1 175 ? -9.52144  -8.72873  -32.58059 1.000 13.96280 ? 182 ARG   A CD  1 
ATOM   1284 N  NE  . ARG   A 1 175 ? -10.43449 -8.62238  -31.44582 1.000 13.93560 ? 182 ARG   A NE  1 
ATOM   1285 C  CZ  . ARG   A 1 175 ? -11.75169 -8.50263  -31.54851 1.000 14.82513 ? 182 ARG   A CZ  1 
ATOM   1286 N  NH1 . ARG   A 1 175 ? -12.35514 -8.48160  -32.72590 1.000 15.80598 ? 182 ARG   A NH1 1 
ATOM   1287 N  NH2 . ARG   A 1 175 ? -12.48399 -8.40364  -30.44161 1.000 15.09000 ? 182 ARG   A NH2 1 
ATOM   1288 N  N   . GLY   A 1 176 ? -8.02794  -12.60372 -30.68773 1.000 18.69699 ? 183 GLY   A N   1 
ATOM   1289 C  CA  . GLY   A 1 176 ? -7.68404  -12.49501 -29.28982 1.000 16.52683 ? 183 GLY   A CA  1 
ATOM   1290 C  C   . GLY   A 1 176 ? -6.54276  -13.41708 -28.93287 1.000 15.10241 ? 183 GLY   A C   1 
ATOM   1291 O  O   . GLY   A 1 176 ? -5.80000  -13.87493 -29.79925 1.000 17.29261 ? 183 GLY   A O   1 
ATOM   1292 N  N   . THR   A 1 177 ? -6.41202  -13.67955 -27.63354 1.000 14.85472 ? 184 THR   A N   1 
ATOM   1293 C  CA  . THR   A 1 177 ? -5.30760  -14.47050 -27.11398 1.000 13.42637 ? 184 THR   A CA  1 
ATOM   1294 C  C   . THR   A 1 177 ? -5.81245  -15.41883 -26.03861 1.000 20.83842 ? 184 THR   A C   1 
ATOM   1295 O  O   . THR   A 1 177 ? -6.66334  -15.05914 -25.22066 1.000 14.10143 ? 184 THR   A O   1 
ATOM   1296 C  CB  . THR   A 1 177 ? -4.18793  -13.57001 -26.56185 1.000 13.62139 ? 184 THR   A CB  1 
ATOM   1297 O  OG1 . THR   A 1 177 ? -3.63724  -12.79417 -27.63017 1.000 16.24377 ? 184 THR   A OG1 1 
ATOM   1298 C  CG2 . THR   A 1 177 ? -3.06989  -14.39459 -25.92081 1.000 15.28092 ? 184 THR   A CG2 1 
ATOM   1299 N  N   . LYS   A 1 178 ? -5.27935  -16.63610 -26.05577 1.000 11.33269 ? 185 LYS   A N   1 
ATOM   1300 C  CA  . LYS   A 1 178 ? -5.61917  -17.67518 -25.09622 1.000 13.49708 ? 185 LYS   A CA  1 
ATOM   1301 C  C   . LYS   A 1 178 ? -4.32728  -18.17283 -24.46585 1.000 15.75200 ? 185 LYS   A C   1 
ATOM   1302 O  O   . LYS   A 1 178 ? -3.47187  -18.72382 -25.16497 1.000 16.14731 ? 185 LYS   A O   1 
ATOM   1303 C  CB  . LYS   A 1 178 ? -6.36814  -18.80846 -25.80393 1.000 19.12873 ? 185 LYS   A CB  1 
ATOM   1304 C  CG  . LYS   A 1 178 ? -6.60817  -20.04667 -24.98569 1.000 28.25324 ? 185 LYS   A CG  1 
ATOM   1305 C  CD  . LYS   A 1 178 ? -7.66643  -20.93868 -25.64027 1.000 36.51555 ? 185 LYS   A CD  1 
ATOM   1306 C  CE  . LYS   A 1 178 ? -7.70941  -20.75978 -27.15470 1.000 38.27186 ? 185 LYS   A CE  1 
ATOM   1307 N  NZ  . LYS   A 1 178 ? -8.23616  -21.97158 -27.84971 1.000 48.85598 ? 185 LYS   A NZ  1 
ATOM   1308 N  N   . VAL   A 1 179 ? -4.17361  -17.96373 -23.16067 1.000 12.32294 ? 186 VAL   A N   1 
ATOM   1309 C  CA  . VAL   A 1 179 ? -2.98641  -18.40187 -22.42921 1.000 13.01243 ? 186 VAL   A CA  1 
ATOM   1310 C  C   . VAL   A 1 179 ? -3.36667  -19.64644 -21.63800 1.000 18.23397 ? 186 VAL   A C   1 
ATOM   1311 O  O   . VAL   A 1 179 ? -4.19939  -19.58650 -20.72595 1.000 13.10759 ? 186 VAL   A O   1 
ATOM   1312 C  CB  . VAL   A 1 179 ? -2.43905  -17.30220 -21.50821 1.000 13.75157 ? 186 VAL   A CB  1 
ATOM   1313 C  CG1 . VAL   A 1 179 ? -1.22888  -17.81657 -20.72594 1.000 13.10174 ? 186 VAL   A CG1 1 
ATOM   1314 C  CG2 . VAL   A 1 179 ? -2.06692  -16.06727 -22.30713 1.000 12.39541 ? 186 VAL   A CG2 1 
ATOM   1315 N  N   . ILE   A 1 180 ? -2.76237  -20.77616 -21.98664 1.000 13.52796 ? 187 ILE   A N   1 
ATOM   1316 C  CA  . ILE   A 1 180 ? -3.05827  -22.05792 -21.35914 1.000 12.12547 ? 187 ILE   A CA  1 
ATOM   1317 C  C   . ILE   A 1 180 ? -1.92400  -22.37114 -20.39618 1.000 13.09839 ? 187 ILE   A C   1 
ATOM   1318 O  O   . ILE   A 1 180 ? -0.78380  -22.58500 -20.81797 1.000 14.04418 ? 187 ILE   A O   1 
ATOM   1319 C  CB  . ILE   A 1 180 ? -3.22421  -23.17242 -22.39914 1.000 11.85038 ? 187 ILE   A CB  1 
ATOM   1320 C  CG1 . ILE   A 1 180 ? -4.30762  -22.79721 -23.41488 1.000 14.04235 ? 187 ILE   A CG1 1 
ATOM   1321 C  CG2 . ILE   A 1 180 ? -3.53925  -24.50021 -21.71245 1.000 14.35846 ? 187 ILE   A CG2 1 
ATOM   1322 C  CD1 . ILE   A 1 180 ? -4.35831  -23.71919 -24.61778 1.000 21.63016 ? 187 ILE   A CD1 1 
ATOM   1323 N  N   . LEU   A 1 181 ? -2.23533  -22.40458 -19.10507 1.000 12.53254 ? 188 LEU   A N   1 
ATOM   1324 C  CA  . LEU   A 1 181 ? -1.25896  -22.69625 -18.06166 1.000 12.18190 ? 188 LEU   A CA  1 
ATOM   1325 C  C   . LEU   A 1 181 ? -1.36290  -24.16914 -17.68617 1.000 16.00758 ? 188 LEU   A C   1 
ATOM   1326 O  O   . LEU   A 1 181 ? -2.34239  -24.58718 -17.06108 1.000 12.57825 ? 188 LEU   A O   1 
ATOM   1327 C  CB  . LEU   A 1 181 ? -1.49826  -21.81600 -16.83954 1.000 12.07123 ? 188 LEU   A CB  1 
ATOM   1328 C  CG  . LEU   A 1 181 ? -1.57397  -20.31696 -17.11215 1.000 15.37788 ? 188 LEU   A CG  1 
ATOM   1329 C  CD1 . LEU   A 1 181 ? -1.89605  -19.58158 -15.83130 1.000 19.91733 ? 188 LEU   A CD1 1 
ATOM   1330 C  CD2 . LEU   A 1 181 ? -0.26767  -19.82626 -17.70005 1.000 12.25657 ? 188 LEU   A CD2 1 
ATOM   1331 N  N   . HIS   A 1 182 ? -0.34997  -24.94944 -18.05295 1.000 15.33113 ? 189 HIS   A N   1 
ATOM   1332 C  CA  . HIS   A 1 182 ? -0.24567  -26.34050 -17.61297 1.000 12.53536 ? 189 HIS   A CA  1 
ATOM   1333 C  C   . HIS   A 1 182 ? 0.39189   -26.32690 -16.22954 1.000 14.61661 ? 189 HIS   A C   1 
ATOM   1334 O  O   . HIS   A 1 182 ? 1.61209   -26.21319 -16.09123 1.000 14.15395 ? 189 HIS   A O   1 
ATOM   1335 C  CB  . HIS   A 1 182 ? 0.55510   -27.16052 -18.61803 1.000 13.07720 ? 189 HIS   A CB  1 
ATOM   1336 C  CG  . HIS   A 1 182 ? 0.06132   -27.02169 -20.02552 1.000 18.99650 ? 189 HIS   A CG  1 
ATOM   1337 N  ND1 . HIS   A 1 182 ? -0.75592  -27.95662 -20.62403 1.000 24.36011 ? 189 HIS   A ND1 1 
ATOM   1338 C  CD2 . HIS   A 1 182 ? 0.25194   -26.04525 -20.94487 1.000 20.79756 ? 189 HIS   A CD2 1 
ATOM   1339 C  CE1 . HIS   A 1 182 ? -1.04091  -27.56594 -21.85375 1.000 25.08405 ? 189 HIS   A CE1 1 
ATOM   1340 N  NE2 . HIS   A 1 182 ? -0.44143  -26.40948 -22.07365 1.000 25.23899 ? 189 HIS   A NE2 1 
ATOM   1341 N  N   . LEU   A 1 183 ? -0.44206  -26.43539 -15.19967 1.000 13.74500 ? 190 LEU   A N   1 
ATOM   1342 C  CA  . LEU   A 1 183 ? -0.02114  -26.10701 -13.84445 1.000 13.38599 ? 190 LEU   A CA  1 
ATOM   1343 C  C   . LEU   A 1 183 ? 0.93830   -27.14330 -13.27618 1.000 19.50286 ? 190 LEU   A C   1 
ATOM   1344 O  O   . LEU   A 1 183 ? 0.85817   -28.33731 -13.58140 1.000 18.62956 ? 190 LEU   A O   1 
ATOM   1345 C  CB  . LEU   A 1 183 ? -1.23705  -25.98850 -12.92709 1.000 17.40034 ? 190 LEU   A CB  1 
ATOM   1346 C  CG  . LEU   A 1 183 ? -2.16915  -24.81015 -13.19451 1.000 18.07457 ? 190 LEU   A CG  1 
ATOM   1347 C  CD1 . LEU   A 1 183 ? -3.30086  -24.78741 -12.17680 1.000 15.91735 ? 190 LEU   A CD1 1 
ATOM   1348 C  CD2 . LEU   A 1 183 ? -1.38844  -23.50952 -13.16084 1.000 16.33619 ? 190 LEU   A CD2 1 
ATOM   1349 N  N   . LYS   A 1 184 ? 1.84822   -26.66727 -12.42526 1.000 16.04271 ? 191 LYS   A N   1 
ATOM   1350 C  CA  . LYS   A 1 184 ? 2.69515   -27.56273 -11.65191 1.000 20.06095 ? 191 LYS   A CA  1 
ATOM   1351 C  C   . LYS   A 1 184 ? 1.83991   -28.41775 -10.72536 1.000 22.36545 ? 191 LYS   A C   1 
ATOM   1352 O  O   . LYS   A 1 184 ? 0.73710   -28.03062 -10.33016 1.000 19.20325 ? 191 LYS   A O   1 
ATOM   1353 C  CB  . LYS   A 1 184 ? 3.71040   -26.76836 -10.82906 1.000 22.77789 ? 191 LYS   A CB  1 
ATOM   1354 C  CG  . LYS   A 1 184 ? 4.77661   -26.05455 -11.64194 1.000 24.05942 ? 191 LYS   A CG  1 
ATOM   1355 C  CD  . LYS   A 1 184 ? 5.56061   -25.09270 -10.75053 1.000 32.58213 ? 191 LYS   A CD  1 
ATOM   1356 C  CE  . LYS   A 1 184 ? 6.52452   -24.23683 -11.55078 1.000 42.91408 ? 191 LYS   A CE  1 
ATOM   1357 N  NZ  . LYS   A 1 184 ? 7.22246   -23.22055 -10.70317 1.000 47.52942 ? 191 LYS   A NZ  1 
ATOM   1358 N  N   . GLU   A 1 185 ? 2.37745   -29.58523 -10.36390 1.000 22.09163 ? 192 GLU   A N   1 
ATOM   1359 C  CA  . GLU   A 1 185 ? 1.62089   -30.55947 -9.58244  1.000 27.43239 ? 192 GLU   A CA  1 
ATOM   1360 C  C   . GLU   A 1 185 ? 1.14636   -29.98246 -8.25426  1.000 28.06515 ? 192 GLU   A C   1 
ATOM   1361 O  O   . GLU   A 1 185 ? 0.05248   -30.31551 -7.78339  1.000 30.10040 ? 192 GLU   A O   1 
ATOM   1362 C  CB  . GLU   A 1 185 ? 2.47554   -31.80462 -9.34220  1.000 33.41182 ? 192 GLU   A CB  1 
ATOM   1363 C  CG  . GLU   A 1 185 ? 1.68338   -33.07066 -9.08353  1.000 46.41222 ? 192 GLU   A CG  1 
ATOM   1364 C  CD  . GLU   A 1 185 ? 2.57518   -34.24789 -8.73531  1.000 67.87935 ? 192 GLU   A CD  1 
ATOM   1365 O  OE1 . GLU   A 1 185 ? 3.81255   -34.10765 -8.84026  1.000 58.73764 ? 192 GLU   A OE1 1 
ATOM   1366 O  OE2 . GLU   A 1 185 ? 2.04049   -35.30926 -8.34979  1.000 66.26375 ? 192 GLU   A OE2 1 
ATOM   1367 N  N   . ASP   A 1 186 ? 1.95241   -29.12423 -7.62802  1.000 21.00970 ? 193 ASP   A N   1 
ATOM   1368 C  CA  . ASP   A 1 186 ? 1.62472   -28.58115 -6.31645  1.000 25.06786 ? 193 ASP   A CA  1 
ATOM   1369 C  C   . ASP   A 1 186 ? 0.94442   -27.21553 -6.39147  1.000 20.07847 ? 193 ASP   A C   1 
ATOM   1370 O  O   . ASP   A 1 186 ? 0.86540   -26.51519 -5.37666  1.000 22.43027 ? 193 ASP   A O   1 
ATOM   1371 C  CB  . ASP   A 1 186 ? 2.87989   -28.50941 -5.44242  1.000 27.55930 ? 193 ASP   A CB  1 
ATOM   1372 C  CG  . ASP   A 1 186 ? 3.98120   -27.65533 -6.05317  1.000 33.49635 ? 193 ASP   A CG  1 
ATOM   1373 O  OD1 . ASP   A 1 186 ? 3.76713   -27.06299 -7.13168  1.000 38.14247 ? 193 ASP   A OD1 1 
ATOM   1374 O  OD2 . ASP   A 1 186 ? 5.07130   -27.57753 -5.44684  1.000 50.86541 ? 193 ASP   A OD2 1 
ATOM   1375 N  N   . GLN   A 1 187 ? 0.43811   -26.82971 -7.56388  1.000 17.57995 ? 194 GLN   A N   1 
ATOM   1376 C  CA  . GLN   A 1 187 ? -0.19425  -25.52942 -7.75719  1.000 16.22561 ? 194 GLN   A CA  1 
ATOM   1377 C  C   . GLN   A 1 187 ? -1.63883  -25.66249 -8.23265  1.000 17.01469 ? 194 GLN   A C   1 
ATOM   1378 O  O   . GLN   A 1 187 ? -2.16262  -24.76231 -8.89036  1.000 19.35982 ? 194 GLN   A O   1 
ATOM   1379 C  CB  . GLN   A 1 187 ? 0.60908   -24.67627 -8.74095  1.000 14.84865 ? 194 GLN   A CB  1 
ATOM   1380 C  CG  . GLN   A 1 187 ? 2.05742   -24.42611 -8.32260  1.000 16.85939 ? 194 GLN   A CG  1 
ATOM   1381 C  CD  . GLN   A 1 187 ? 2.17042   -23.73776 -6.97587  1.000 25.58176 ? 194 GLN   A CD  1 
ATOM   1382 O  OE1 . GLN   A 1 187 ? 1.34625   -22.89244 -6.62551  1.000 22.57894 ? 194 GLN   A OE1 1 
ATOM   1383 N  NE2 . GLN   A 1 187 ? 3.19432   -24.09779 -6.21178  1.000 25.04829 ? 194 GLN   A NE2 1 
ATOM   1384 N  N   . THR   A 1 188 ? -2.30061  -26.77107 -7.90008  1.000 20.94952 ? 195 THR   A N   1 
ATOM   1385 C  CA  . THR   A 1 188 ? -3.66554  -26.99863 -8.36543  1.000 24.60984 ? 195 THR   A CA  1 
ATOM   1386 C  C   . THR   A 1 188 ? -4.70712  -26.20190 -7.58793  1.000 20.31772 ? 195 THR   A C   1 
ATOM   1387 O  O   . THR   A 1 188 ? -5.89077  -26.25431 -7.94177  1.000 22.22884 ? 195 THR   A O   1 
ATOM   1388 C  CB  . THR   A 1 188 ? -4.01470  -28.49153 -8.30542  1.000 25.21653 ? 195 THR   A CB  1 
ATOM   1389 O  OG1 . THR   A 1 188 ? -3.92749  -28.95975 -6.95301  1.000 28.52446 ? 195 THR   A OG1 1 
ATOM   1390 C  CG2 . THR   A 1 188 ? -3.06951  -29.30261 -9.18823  1.000 24.11745 ? 195 THR   A CG2 1 
ATOM   1391 N  N   . GLU   A 1 189 ? -4.30848  -25.46854 -6.54546  1.000 19.06440 ? 196 GLU   A N   1 
ATOM   1392 C  CA  . GLU   A 1 189 ? -5.25268  -24.58401 -5.86979  1.000 25.42758 ? 196 GLU   A CA  1 
ATOM   1393 C  C   . GLU   A 1 189 ? -5.81252  -23.52724 -6.81169  1.000 17.23473 ? 196 GLU   A C   1 
ATOM   1394 O  O   . GLU   A 1 189 ? -6.91048  -23.01216 -6.57413  1.000 16.75405 ? 196 GLU   A O   1 
ATOM   1395 C  CB  . GLU   A 1 189 ? -4.58629  -23.90596 -4.67201  1.000 20.54533 ? 196 GLU   A CB  1 
ATOM   1396 C  CG  . GLU   A 1 189 ? -3.61890  -22.80279 -5.05456  1.000 17.21705 ? 196 GLU   A CG  1 
ATOM   1397 C  CD  . GLU   A 1 189 ? -2.80949  -22.31253 -3.87327  1.000 31.14740 ? 196 GLU   A CD  1 
ATOM   1398 O  OE1 . GLU   A 1 189 ? -1.85929  -23.01689 -3.47831  1.000 24.21522 ? 196 GLU   A OE1 1 
ATOM   1399 O  OE2 . GLU   A 1 189 ? -3.11928  -21.22121 -3.34413  1.000 23.46199 ? 196 GLU   A OE2 1 
ATOM   1400 N  N   . TYR   A 1 190 ? -5.08653  -23.19686 -7.87530  1.000 17.88377 ? 197 TYR   A N   1 
ATOM   1401 C  CA  . TYR   A 1 190 ? -5.53429  -22.19543 -8.83072  1.000 19.71564 ? 197 TYR   A CA  1 
ATOM   1402 C  C   . TYR   A 1 190 ? -6.52472  -22.76023 -9.84235  1.000 18.80800 ? 197 TYR   A C   1 
ATOM   1403 O  O   . TYR   A 1 190 ? -6.90635  -22.05745 -10.78231 1.000 19.02932 ? 197 TYR   A O   1 
ATOM   1404 C  CB  . TYR   A 1 190 ? -4.31530  -21.56921 -9.51374  1.000 15.49045 ? 197 TYR   A CB  1 
ATOM   1405 C  CG  . TYR   A 1 190 ? -3.40274  -20.92877 -8.48923  1.000 14.47594 ? 197 TYR   A CG  1 
ATOM   1406 C  CD1 . TYR   A 1 190 ? -3.81738  -19.81802 -7.76593  1.000 15.12050 ? 197 TYR   A CD1 1 
ATOM   1407 C  CD2 . TYR   A 1 190 ? -2.15700  -21.47363 -8.19405  1.000 16.31853 ? 197 TYR   A CD2 1 
ATOM   1408 C  CE1 . TYR   A 1 190 ? -3.00353  -19.24035 -6.80783  1.000 14.91145 ? 197 TYR   A CE1 1 
ATOM   1409 C  CE2 . TYR   A 1 190 ? -1.33516  -20.90243 -7.23077  1.000 18.34818 ? 197 TYR   A CE2 1 
ATOM   1410 C  CZ  . TYR   A 1 190 ? -1.76622  -19.78347 -6.54206  1.000 15.22040 ? 197 TYR   A CZ  1 
ATOM   1411 O  OH  . TYR   A 1 190 ? -0.97181  -19.20472 -5.58043  1.000 17.25323 ? 197 TYR   A OH  1 
ATOM   1412 N  N   . LEU   A 1 191 ? -6.95504  -24.00863 -9.65589  1.000 16.11798 ? 198 LEU   A N   1 
ATOM   1413 C  CA  . LEU   A 1 191 ? -8.10218  -24.55942 -10.36278 1.000 16.89751 ? 198 LEU   A CA  1 
ATOM   1414 C  C   . LEU   A 1 191 ? -9.38168  -24.50645 -9.54070  1.000 23.82530 ? 198 LEU   A C   1 
ATOM   1415 O  O   . LEU   A 1 191 ? -10.45449 -24.79578 -10.07840 1.000 19.20938 ? 198 LEU   A O   1 
ATOM   1416 C  CB  . LEU   A 1 191 ? -7.83646  -26.01571 -10.76940 1.000 16.02730 ? 198 LEU   A CB  1 
ATOM   1417 C  CG  . LEU   A 1 191 ? -6.61173  -26.25667 -11.64985 1.000 17.22133 ? 198 LEU   A CG  1 
ATOM   1418 C  CD1 . LEU   A 1 191 ? -6.41582  -27.74020 -11.91525 1.000 22.08890 ? 198 LEU   A CD1 1 
ATOM   1419 C  CD2 . LEU   A 1 191 ? -6.75827  -25.49617 -12.95478 1.000 19.29881 ? 198 LEU   A CD2 1 
ATOM   1420 N  N   . GLU   A 1 192 ? -9.29684  -24.17064 -8.25678  1.000 16.90662 ? 199 GLU   A N   1 
ATOM   1421 C  CA  . GLU   A 1 192 ? -10.46247 -24.16803 -7.38443  1.000 17.91868 ? 199 GLU   A CA  1 
ATOM   1422 C  C   . GLU   A 1 192 ? -11.21514 -22.85138 -7.50799  1.000 24.26672 ? 199 GLU   A C   1 
ATOM   1423 O  O   . GLU   A 1 192 ? -10.61566 -21.77150 -7.51279  1.000 18.78092 ? 199 GLU   A O   1 
ATOM   1424 C  CB  . GLU   A 1 192 ? -10.05971 -24.41125 -5.92897  1.000 23.70687 ? 199 GLU   A CB  1 
ATOM   1425 C  CG  . GLU   A 1 192 ? -9.23906  -25.67066 -5.71072  1.000 35.42341 ? 199 GLU   A CG  1 
ATOM   1426 C  CD  . GLU   A 1 192 ? -8.81515  -25.84434 -4.26521  1.000 60.93313 ? 199 GLU   A CD  1 
ATOM   1427 O  OE1 . GLU   A 1 192 ? -9.46737  -25.25489 -3.37534  1.000 73.35006 ? 199 GLU   A OE1 1 
ATOM   1428 O  OE2 . GLU   A 1 192 ? -7.83028  -26.57109 -4.01814  1.000 63.84401 ? 199 GLU   A OE2 1 
ATOM   1429 N  N   . GLU   A 1 193 ? -12.54175 -22.95511 -7.59449  1.000 20.31591 ? 200 GLU   A N   1 
ATOM   1430 C  CA  . GLU   A 1 193 ? -13.36484 -21.78806 -7.88717  1.000 19.80769 ? 200 GLU   A CA  1 
ATOM   1431 C  C   . GLU   A 1 193 ? -13.20505 -20.70700 -6.82058  1.000 18.28367 ? 200 GLU   A C   1 
ATOM   1432 O  O   . GLU   A 1 193 ? -13.02580 -19.52810 -7.14411  1.000 17.04882 ? 200 GLU   A O   1 
ATOM   1433 C  CB  . GLU   A 1 193 ? -14.82736 -22.21349 -8.02548  1.000 23.04810 ? 200 GLU   A CB  1 
ATOM   1434 C  CG  . GLU   A 1 193 ? -15.81475 -21.07180 -7.94250  1.000 31.11022 ? 200 GLU   A CG  1 
ATOM   1435 C  CD  . GLU   A 1 193 ? -17.22107 -21.49349 -8.32944  1.000 51.91972 ? 200 GLU   A CD  1 
ATOM   1436 O  OE1 . GLU   A 1 193 ? -17.86734 -20.77229 -9.12011  1.000 57.81935 ? 200 GLU   A OE1 1 
ATOM   1437 O  OE2 . GLU   A 1 193 ? -17.67913 -22.54745 -7.84232  1.000 39.07764 ? 200 GLU   A OE2 1 
ATOM   1438 N  N   . ARG   A 1 194 ? -13.25428 -21.08545 -5.53854  1.000 21.12014 ? 201 ARG   A N   1 
ATOM   1439 C  CA  . ARG   A 1 194 ? -13.18763 -20.06479 -4.49531  1.000 23.25230 ? 201 ARG   A CA  1 
ATOM   1440 C  C   . ARG   A 1 194 ? -11.82224 -19.39367 -4.45198  1.000 19.80716 ? 201 ARG   A C   1 
ATOM   1441 O  O   . ARG   A 1 194 ? -11.72138 -18.22264 -4.06513  1.000 15.69164 ? 201 ARG   A O   1 
ATOM   1442 C  CB  . ARG   A 1 194 ? -13.50560 -20.65568 -3.12292  1.000 24.64538 ? 201 ARG   A CB  1 
ATOM   1443 C  CG  . ARG   A 1 194 ? -12.61361 -21.80039 -2.70904  1.000 32.05500 ? 201 ARG   A CG  1 
ATOM   1444 C  CD  . ARG   A 1 194 ? -13.19383 -22.51244 -1.50141  1.000 39.22887 ? 201 ARG   A CD  1 
ATOM   1445 N  NE  . ARG   A 1 194 ? -12.18095 -23.29234 -0.80179  1.000 40.97861 ? 201 ARG   A NE  1 
ATOM   1446 C  CZ  . ARG   A 1 194 ? -12.36508 -23.86552 0.37924   1.000 44.17537 ? 201 ARG   A CZ  1 
ATOM   1447 N  NH1 . ARG   A 1 194 ? -13.51595 -23.76379 1.02455   1.000 39.78311 ? 201 ARG   A NH1 1 
ATOM   1448 N  NH2 . ARG   A 1 194 ? -11.36828 -24.55331 0.92856   1.000 48.10335 ? 201 ARG   A NH2 1 
ATOM   1449 N  N   . ARG   A 1 195 ? -10.76294 -20.11493 -4.82857  1.000 15.62740 ? 202 ARG   A N   1 
ATOM   1450 C  CA  . ARG   A 1 195 ? -9.43387  -19.51419 -4.82015  1.000 17.76186 ? 202 ARG   A CA  1 
ATOM   1451 C  C   . ARG   A 1 195 ? -9.27612  -18.52912 -5.97040  1.000 14.33144 ? 202 ARG   A C   1 
ATOM   1452 O  O   . ARG   A 1 195 ? -8.71128  -17.44380 -5.79116  1.000 16.58314 ? 202 ARG   A O   1 
ATOM   1453 C  CB  . ARG   A 1 195 ? -8.36398  -20.60412 -4.88353  1.000 17.05221 ? 202 ARG   A CB  1 
ATOM   1454 C  CG  . ARG   A 1 195 ? -6.92928  -20.08138 -4.93230  1.000 16.79494 ? 202 ARG   A CG  1 
ATOM   1455 C  CD  . ARG   A 1 195 ? -6.47629  -19.56497 -3.57011  1.000 15.60186 ? 202 ARG   A CD  1 
ATOM   1456 N  NE  . ARG   A 1 195 ? -5.04317  -19.29181 -3.54056  1.000 17.14173 ? 202 ARG   A NE  1 
ATOM   1457 C  CZ  . ARG   A 1 195 ? -4.50514  -18.09856 -3.32456  1.000 20.53578 ? 202 ARG   A CZ  1 
ATOM   1458 N  NH1 . ARG   A 1 195 ? -5.25418  -17.03163 -3.10005  1.000 16.71928 ? 202 ARG   A NH1 1 
ATOM   1459 N  NH2 . ARG   A 1 195 ? -3.18094  -17.97237 -3.34109  1.000 19.96095 ? 202 ARG   A NH2 1 
ATOM   1460 N  N   . ILE   A 1 196 ? -9.77761  -18.88406 -7.15733  1.000 14.32778 ? 203 ILE   A N   1 
ATOM   1461 C  CA  . ILE   A 1 196 ? -9.73702  -17.95368 -8.28268  1.000 12.90587 ? 203 ILE   A CA  1 
ATOM   1462 C  C   . ILE   A 1 196 ? -10.58345 -16.72218 -7.98501  1.000 17.50209 ? 203 ILE   A C   1 
ATOM   1463 O  O   . ILE   A 1 196 ? -10.15468 -15.58836 -8.23273  1.000 13.88450 ? 203 ILE   A O   1 
ATOM   1464 C  CB  . ILE   A 1 196 ? -10.19147 -18.64248 -9.58434  1.000 16.83777 ? 203 ILE   A CB  1 
ATOM   1465 C  CG1 . ILE   A 1 196 ? -9.27263  -19.81636 -9.93366  1.000 14.62482 ? 203 ILE   A CG1 1 
ATOM   1466 C  CG2 . ILE   A 1 196 ? -10.23372 -17.63328 -10.73642 1.000 14.01284 ? 203 ILE   A CG2 1 
ATOM   1467 C  CD1 . ILE   A 1 196 ? -9.88439  -20.78691 -10.92852 1.000 20.52856 ? 203 ILE   A CD1 1 
ATOM   1468 N  N   . LYS   A 1 197 ? -11.79698 -16.92132 -7.44903  1.000 14.30806 ? 204 LYS   A N   1 
ATOM   1469 C  CA  . LYS   A 1 197 ? -12.64585 -15.78388 -7.09665  1.000 14.66543 ? 204 LYS   A CA  1 
ATOM   1470 C  C   . LYS   A 1 197 ? -11.94256 -14.84628 -6.12656  1.000 18.97071 ? 204 LYS   A C   1 
ATOM   1471 O  O   . LYS   A 1 197 ? -12.02874 -13.61954 -6.26281  1.000 17.72629 ? 204 LYS   A O   1 
ATOM   1472 C  CB  . LYS   A 1 197 ? -13.96852 -16.25402 -6.48186  1.000 16.22816 ? 204 LYS   A CB  1 
ATOM   1473 C  CG  . LYS   A 1 197 ? -15.04245 -16.66252 -7.46256  1.000 24.31894 ? 204 LYS   A CG  1 
ATOM   1474 C  CD  . LYS   A 1 197 ? -16.30574 -17.08573 -6.70993  1.000 29.45797 ? 204 LYS   A CD  1 
ATOM   1475 C  CE  . LYS   A 1 197 ? -17.24205 -17.89826 -7.58482  1.000 48.70298 ? 204 LYS   A CE  1 
ATOM   1476 N  NZ  . LYS   A 1 197 ? -18.12724 -18.78551 -6.77669  1.000 56.82088 ? 204 LYS   A NZ  1 
ATOM   1477 N  N   . GLU   A 1 198 ? -11.25947 -15.40792 -5.12764  1.000 16.06824 ? 205 GLU   A N   1 
ATOM   1478 C  CA  . GLU   A 1 198 ? -10.55556 -14.58343 -4.15248  1.000 15.50700 ? 205 GLU   A CA  1 
ATOM   1479 C  C   . GLU   A 1 198 ? -9.48251  -13.73605 -4.82157  1.000 16.40942 ? 205 GLU   A C   1 
ATOM   1480 O  O   . GLU   A 1 198 ? -9.34213  -12.54421 -4.51963  1.000 15.94320 ? 205 GLU   A O   1 
ATOM   1481 C  CB  . GLU   A 1 198 ? -9.94705  -15.47489 -3.06918  1.000 17.71613 ? 205 GLU   A CB  1 
ATOM   1482 C  CG  . GLU   A 1 198 ? -9.01731  -14.76751 -2.09621  1.000 21.74410 ? 205 GLU   A CG  1 
ATOM   1483 C  CD  . GLU   A 1 198 ? -8.30603  -15.74459 -1.18376  1.000 19.08413 ? 205 GLU   A CD  1 
ATOM   1484 O  OE1 . GLU   A 1 198 ? -7.73671  -16.72392 -1.70735  1.000 22.25316 ? 205 GLU   A OE1 1 
ATOM   1485 O  OE2 . GLU   A 1 198 ? -8.32306  -15.54377 0.04944   1.000 18.80849 ? 205 GLU   A OE2 1 
ATOM   1486 N  N   . ILE   A 1 199 ? -8.72475  -14.33191 -5.74332  1.000 17.02886 ? 206 ILE   A N   1 
ATOM   1487 C  CA  . ILE   A 1 199 ? -7.62065  -13.62116 -6.38059  1.000 16.60553 ? 206 ILE   A CA  1 
ATOM   1488 C  C   . ILE   A 1 199 ? -8.14387  -12.51200 -7.28494  1.000 18.77941 ? 206 ILE   A C   1 
ATOM   1489 O  O   . ILE   A 1 199 ? -7.59662  -11.40336 -7.31024  1.000 16.66072 ? 206 ILE   A O   1 
ATOM   1490 C  CB  . ILE   A 1 199 ? -6.73268  -14.61135 -7.15384  1.000 12.72630 ? 206 ILE   A CB  1 
ATOM   1491 C  CG1 . ILE   A 1 199 ? -6.06679  -15.59143 -6.18847  1.000 17.04833 ? 206 ILE   A CG1 1 
ATOM   1492 C  CG2 . ILE   A 1 199 ? -5.66774  -13.87019 -7.95189  1.000 13.49029 ? 206 ILE   A CG2 1 
ATOM   1493 C  CD1 . ILE   A 1 199 ? -5.56078  -16.83715 -6.86527  1.000 19.93894 ? 206 ILE   A CD1 1 
ATOM   1494 N  N   . VAL   A 1 200 ? -9.20773  -12.79014 -8.04124  1.000 15.65404 ? 207 VAL   A N   1 
ATOM   1495 C  CA  . VAL   A 1 200 ? -9.77261  -11.77850 -8.92964  1.000 12.31471 ? 207 VAL   A CA  1 
ATOM   1496 C  C   . VAL   A 1 200 ? -10.29743 -10.59777 -8.12325  1.000 14.66596 ? 207 VAL   A C   1 
ATOM   1497 O  O   . VAL   A 1 200 ? -10.04665 -9.43394  -8.46221  1.000 17.78508 ? 207 VAL   A O   1 
ATOM   1498 C  CB  . VAL   A 1 200 ? -10.87009 -12.40091 -9.81223  1.000 15.43761 ? 207 VAL   A CB  1 
ATOM   1499 C  CG1 . VAL   A 1 200 ? -11.65717 -11.31665 -10.53434 1.000 15.86065 ? 207 VAL   A CG1 1 
ATOM   1500 C  CG2 . VAL   A 1 200 ? -10.25734 -13.39119 -10.80833 1.000 14.17316 ? 207 VAL   A CG2 1 
ATOM   1501 N  N   . LYS   A 1 201 ? -11.01461 -10.87772 -7.03165  1.000 16.08490 ? 208 LYS   A N   1 
ATOM   1502 C  CA  . LYS   A 1 201 ? -11.55137 -9.80660  -6.19638  1.000 18.92229 ? 208 LYS   A CA  1 
ATOM   1503 C  C   . LYS   A 1 201 ? -10.43369 -9.00588  -5.53902  1.000 19.12181 ? 208 LYS   A C   1 
ATOM   1504 O  O   . LYS   A 1 201 ? -10.54148 -7.78381  -5.39283  1.000 20.45358 ? 208 LYS   A O   1 
ATOM   1505 C  CB  . LYS   A 1 201 ? -12.49183 -10.39663 -5.14497  1.000 19.26828 ? 208 LYS   A CB  1 
ATOM   1506 C  CG  . LYS   A 1 201 ? -13.10473 -9.39634  -4.18640  1.000 25.28865 ? 208 LYS   A CG  1 
ATOM   1507 C  CD  . LYS   A 1 201 ? -14.09248 -10.08977 -3.25169  1.000 24.47533 ? 208 LYS   A CD  1 
ATOM   1508 C  CE  . LYS   A 1 201 ? -14.67531 -9.13535  -2.22045  1.000 38.91458 ? 208 LYS   A CE  1 
ATOM   1509 N  NZ  . LYS   A 1 201 ? -13.68256 -8.75205  -1.18202  1.000 58.51461 ? 208 LYS   A NZ  1 
ATOM   1510 N  N   . LYS   A 1 202 ? -9.34526  -9.67640  -5.15362  1.000 17.53562 ? 209 LYS   A N   1 
ATOM   1511 C  CA  . LYS   A 1 202 ? -8.24977  -8.99761  -4.46550  1.000 20.09738 ? 209 LYS   A CA  1 
ATOM   1512 C  C   . LYS   A 1 202 ? -7.47043  -8.07898  -5.40256  1.000 19.37304 ? 209 LYS   A C   1 
ATOM   1513 O  O   . LYS   A 1 202 ? -7.14761  -6.94235  -5.03715  1.000 18.80970 ? 209 LYS   A O   1 
ATOM   1514 C  CB  . LYS   A 1 202 ? -7.31307  -10.03289 -3.83891  1.000 19.98509 ? 209 LYS   A CB  1 
ATOM   1515 C  CG  . LYS   A 1 202 ? -6.09760  -9.43952  -3.12890  1.000 27.95901 ? 209 LYS   A CG  1 
ATOM   1516 C  CD  . LYS   A 1 202 ? -5.54094  -10.41021 -2.09916  1.000 39.15923 ? 209 LYS   A CD  1 
ATOM   1517 C  CE  . LYS   A 1 202 ? -4.14605  -10.00363 -1.65220  1.000 47.72091 ? 209 LYS   A CE  1 
ATOM   1518 N  NZ  . LYS   A 1 202 ? -3.46611  -11.07946 -0.87342  1.000 47.50188 ? 209 LYS   A NZ  1 
ATOM   1519 N  N   . HIS   A 1 203 ? -7.16245  -8.54667  -6.61543  1.000 18.54171 ? 210 HIS   A N   1 
ATOM   1520 C  CA  . HIS   A 1 203 ? -6.17987  -7.88982  -7.46699  1.000 19.97945 ? 210 HIS   A CA  1 
ATOM   1521 C  C   . HIS   A 1 203 ? -6.73409  -7.28842  -8.74988  1.000 22.73751 ? 210 HIS   A C   1 
ATOM   1522 O  O   . HIS   A 1 203 ? -6.04920  -6.45863  -9.35724  1.000 22.65881 ? 210 HIS   A O   1 
ATOM   1523 C  CB  . HIS   A 1 203 ? -5.06497  -8.87648  -7.85258  1.000 20.25423 ? 210 HIS   A CB  1 
ATOM   1524 C  CG  . HIS   A 1 203 ? -4.25683  -9.36425  -6.69117  1.000 22.08319 ? 210 HIS   A CG  1 
ATOM   1525 N  ND1 . HIS   A 1 203 ? -3.40973  -8.54528  -5.97635  1.000 23.82068 ? 210 HIS   A ND1 1 
ATOM   1526 C  CD2 . HIS   A 1 203 ? -4.16861  -10.58885 -6.11870  1.000 24.19078 ? 210 HIS   A CD2 1 
ATOM   1527 C  CE1 . HIS   A 1 203 ? -2.83208  -9.24509  -5.01537  1.000 26.06312 ? 210 HIS   A CE1 1 
ATOM   1528 N  NE2 . HIS   A 1 203 ? -3.27707  -10.48738 -5.07851  1.000 25.91605 ? 210 HIS   A NE2 1 
ATOM   1529 N  N   . SER   A 1 204 ? -7.93327  -7.67496  -9.18563  1.000 18.96513 ? 211 SER   A N   1 
ATOM   1530 C  CA  . SER   A 1 204 ? -8.43340  -7.26574  -10.49240 1.000 17.43919 ? 211 SER   A CA  1 
ATOM   1531 C  C   . SER   A 1 204 ? -9.81319  -6.61993  -10.39232 1.000 17.50183 ? 211 SER   A C   1 
ATOM   1532 O  O   . SER   A 1 204 ? -10.59976 -6.68031  -11.33978 1.000 18.77809 ? 211 SER   A O   1 
ATOM   1533 C  CB  . SER   A 1 204 ? -8.46473  -8.45682  -11.45416 1.000 20.71018 ? 211 SER   A CB  1 
ATOM   1534 O  OG  . SER   A 1 204 ? -7.18705  -9.07078  -11.55098 1.000 23.55101 ? 211 SER   A OG  1 
ATOM   1535 N  N   . GLN   A 1 205 ? -10.11583 -5.97242  -9.26551  1.000 19.54738 ? 212 GLN   A N   1 
ATOM   1536 C  CA  . GLN   A 1 205 ? -11.47051 -5.47077  -9.05960  1.000 29.23465 ? 212 GLN   A CA  1 
ATOM   1537 C  C   . GLN   A 1 205 ? -11.81929 -4.30184  -9.97768  1.000 29.66673 ? 212 GLN   A C   1 
ATOM   1538 O  O   . GLN   A 1 205 ? -13.00617 -4.05357  -10.21202 1.000 29.37280 ? 212 GLN   A O   1 
ATOM   1539 C  CB  . GLN   A 1 205 ? -11.67554 -5.06897  -7.59427  1.000 27.31646 ? 212 GLN   A CB  1 
ATOM   1540 C  CG  . GLN   A 1 205 ? -10.79654 -3.93209  -7.10300  1.000 42.79264 ? 212 GLN   A CG  1 
ATOM   1541 C  CD  . GLN   A 1 205 ? -9.50956  -4.40745  -6.44575  1.000 58.88799 ? 212 GLN   A CD  1 
ATOM   1542 O  OE1 . GLN   A 1 205 ? -8.71391  -5.13258  -7.04773  1.000 38.95987 ? 212 GLN   A OE1 1 
ATOM   1543 N  NE2 . GLN   A 1 205 ? -9.29677  -3.98896  -5.20113  1.000 46.71977 ? 212 GLN   A NE2 1 
ATOM   1544 N  N   . PHE   A 1 206 ? -10.82912 -3.58761  -10.51541 1.000 24.02190 ? 213 PHE   A N   1 
ATOM   1545 C  CA  . PHE   A 1 206 ? -11.09195 -2.43143  -11.36518 1.000 27.88099 ? 213 PHE   A CA  1 
ATOM   1546 C  C   . PHE   A 1 206 ? -10.74940 -2.67792  -12.83193 1.000 22.78226 ? 213 PHE   A C   1 
ATOM   1547 O  O   . PHE   A 1 206 ? -10.54263 -1.72158  -13.58514 1.000 30.74080 ? 213 PHE   A O   1 
ATOM   1548 C  CB  . PHE   A 1 206 ? -10.34111 -1.20604  -10.84610 1.000 29.88708 ? 213 PHE   A CB  1 
ATOM   1549 C  CG  . PHE   A 1 206 ? -10.69898 -0.82909  -9.43539  1.000 36.58423 ? 213 PHE   A CG  1 
ATOM   1550 C  CD1 . PHE   A 1 206 ? -11.97952 -0.40269  -9.12544  1.000 34.36770 ? 213 PHE   A CD1 1 
ATOM   1551 C  CD2 . PHE   A 1 206 ? -9.75274  -0.88263  -8.42425  1.000 38.27253 ? 213 PHE   A CD2 1 
ATOM   1552 C  CE1 . PHE   A 1 206 ? -12.31465 -0.04896  -7.83133  1.000 37.46176 ? 213 PHE   A CE1 1 
ATOM   1553 C  CE2 . PHE   A 1 206 ? -10.08220 -0.53014  -7.12670  1.000 42.58363 ? 213 PHE   A CE2 1 
ATOM   1554 C  CZ  . PHE   A 1 206 ? -11.36482 -0.11312  -6.83111  1.000 36.56117 ? 213 PHE   A CZ  1 
ATOM   1555 N  N   . ILE   A 1 207 ? -10.68090 -3.93792  -13.25493 1.000 18.08712 ? 214 ILE   A N   1 
ATOM   1556 C  CA  . ILE   A 1 207 ? -10.51953 -4.23870  -14.67152 1.000 16.46253 ? 214 ILE   A CA  1 
ATOM   1557 C  C   . ILE   A 1 207 ? -11.82326 -3.92524  -15.39328 1.000 25.15212 ? 214 ILE   A C   1 
ATOM   1558 O  O   . ILE   A 1 207 ? -12.89864 -4.38628  -14.99007 1.000 21.89646 ? 214 ILE   A O   1 
ATOM   1559 C  CB  . ILE   A 1 207 ? -10.10401 -5.70458  -14.86266 1.000 15.35051 ? 214 ILE   A CB  1 
ATOM   1560 C  CG1 . ILE   A 1 207 ? -8.69724  -5.93236  -14.29959 1.000 16.06348 ? 214 ILE   A CG1 1 
ATOM   1561 C  CG2 . ILE   A 1 207 ? -10.15991 -6.08740  -16.32820 1.000 16.91993 ? 214 ILE   A CG2 1 
ATOM   1562 C  CD1 . ILE   A 1 207 ? -7.61635  -5.16543  -15.02975 1.000 21.50559 ? 214 ILE   A CD1 1 
ATOM   1563 N  N   . GLY   A 1 208 ? -11.73507 -3.13925  -16.46525 1.000 16.65312 ? 215 GLY   A N   1 
ATOM   1564 C  CA  . GLY   A 1 208 ? -12.91762 -2.60593  -17.11776 1.000 21.45459 ? 215 GLY   A CA  1 
ATOM   1565 C  C   . GLY   A 1 208 ? -13.54603 -3.49327  -18.17361 1.000 15.11620 ? 215 GLY   A C   1 
ATOM   1566 O  O   . GLY   A 1 208 ? -14.16956 -2.99548  -19.11609 1.000 20.01391 ? 215 GLY   A O   1 
ATOM   1567 N  N   . TYR   A 1 209 ? -13.39340 -4.80494  -18.03152 1.000 16.44488 ? 216 TYR   A N   1 
ATOM   1568 C  CA  . TYR   A 1 209 ? -14.00043 -5.76802  -18.93578 1.000 19.20734 ? 216 TYR   A CA  1 
ATOM   1569 C  C   . TYR   A 1 209 ? -14.58623 -6.91235  -18.11053 1.000 19.42993 ? 216 TYR   A C   1 
ATOM   1570 O  O   . TYR   A 1 209 ? -14.06176 -7.23147  -17.04205 1.000 17.54997 ? 216 TYR   A O   1 
ATOM   1571 C  CB  . TYR   A 1 209 ? -12.98247 -6.31597  -19.94910 1.000 12.53540 ? 216 TYR   A CB  1 
ATOM   1572 C  CG  . TYR   A 1 209 ? -12.38218 -5.22872  -20.80569 1.000 14.97261 ? 216 TYR   A CG  1 
ATOM   1573 C  CD1 . TYR   A 1 209 ? -13.02669 -4.78492  -21.95238 1.000 14.99245 ? 216 TYR   A CD1 1 
ATOM   1574 C  CD2 . TYR   A 1 209 ? -11.17945 -4.62681  -20.45311 1.000 14.04673 ? 216 TYR   A CD2 1 
ATOM   1575 C  CE1 . TYR   A 1 209 ? -12.48829 -3.77302  -22.73157 1.000 19.40866 ? 216 TYR   A CE1 1 
ATOM   1576 C  CE2 . TYR   A 1 209 ? -10.63073 -3.61609  -21.22790 1.000 14.66054 ? 216 TYR   A CE2 1 
ATOM   1577 C  CZ  . TYR   A 1 209 ? -11.29258 -3.19394  -22.36483 1.000 15.68430 ? 216 TYR   A CZ  1 
ATOM   1578 O  OH  . TYR   A 1 209 ? -10.76087 -2.18738  -23.13719 1.000 18.21820 ? 216 TYR   A OH  1 
ATOM   1579 N  N   . PRO   A 1 210 ? -15.67330 -7.51583  -18.58153 1.000 17.78672 ? 217 PRO   A N   1 
ATOM   1580 C  CA  . PRO   A 1 210 ? -16.26111 -8.63516  -17.82677 1.000 18.26089 ? 217 PRO   A CA  1 
ATOM   1581 C  C   . PRO   A 1 210 ? -15.29557 -9.80904  -17.74389 1.000 19.88349 ? 217 PRO   A C   1 
ATOM   1582 O  O   . PRO   A 1 210 ? -14.71193 -10.23225 -18.74336 1.000 18.94255 ? 217 PRO   A O   1 
ATOM   1583 C  CB  . PRO   A 1 210 ? -17.52287 -8.98527  -18.62849 1.000 21.37576 ? 217 PRO   A CB  1 
ATOM   1584 C  CG  . PRO   A 1 210 ? -17.33729 -8.37564  -19.97033 1.000 24.46313 ? 217 PRO   A CG  1 
ATOM   1585 C  CD  . PRO   A 1 210 ? -16.42892 -7.19279  -19.80023 1.000 18.86319 ? 217 PRO   A CD  1 
ATOM   1586 N  N   . ILE   A 1 211 ? -15.11056 -10.31509 -16.52991 1.000 17.61034 ? 218 ILE   A N   1 
ATOM   1587 C  CA  . ILE   A 1 211 ? -14.27376 -11.47952 -16.26577 1.000 14.06558 ? 218 ILE   A CA  1 
ATOM   1588 C  C   . ILE   A 1 211 ? -15.21553 -12.59555 -15.84705 1.000 15.26316 ? 218 ILE   A C   1 
ATOM   1589 O  O   . ILE   A 1 211 ? -15.86707 -12.50553 -14.79810 1.000 17.50348 ? 218 ILE   A O   1 
ATOM   1590 C  CB  . ILE   A 1 211 ? -13.22785 -11.20623 -15.17706 1.000 14.17083 ? 218 ILE   A CB  1 
ATOM   1591 C  CG1 . ILE   A 1 211 ? -12.28694 -10.07198 -15.59292 1.000 14.63380 ? 218 ILE   A CG1 1 
ATOM   1592 C  CG2 . ILE   A 1 211 ? -12.44148 -12.47382 -14.86941 1.000 17.64702 ? 218 ILE   A CG2 1 
ATOM   1593 C  CD1 . ILE   A 1 211 ? -11.48313 -9.50617  -14.43335 1.000 13.94051 ? 218 ILE   A CD1 1 
ATOM   1594 N  N   . THR   A 1 212 ? -15.30885 -13.63761 -16.66379 1.000 11.51559 ? 219 THR   A N   1 
ATOM   1595 C  CA  . THR   A 1 212 ? -16.22749 -14.73975 -16.41075 1.000 13.75836 ? 219 THR   A CA  1 
ATOM   1596 C  C   . THR   A 1 212 ? -15.42281 -15.95594 -15.98741 1.000 12.18052 ? 219 THR   A C   1 
ATOM   1597 O  O   . THR   A 1 212 ? -14.58298 -16.44490 -16.74963 1.000 13.68285 ? 219 THR   A O   1 
ATOM   1598 C  CB  . THR   A 1 212 ? -17.07010 -15.06484 -17.64292 1.000 16.54500 ? 219 THR   A CB  1 
ATOM   1599 O  OG1 . THR   A 1 212 ? -17.80730 -13.90218 -18.04146 1.000 12.51341 ? 219 THR   A OG1 1 
ATOM   1600 C  CG2 . THR   A 1 212 ? -18.04595 -16.20571 -17.32903 1.000 19.10185 ? 219 THR   A CG2 1 
ATOM   1601 N  N   . LEU   A 1 213 ? -15.67460 -16.43371 -14.77526 1.000 14.48532 ? 220 LEU   A N   1 
ATOM   1602 C  CA  . LEU   A 1 213 ? -15.04173 -17.64578 -14.27166 1.000 14.44541 ? 220 LEU   A CA  1 
ATOM   1603 C  C   . LEU   A 1 213 ? -15.94030 -18.82618 -14.62390 1.000 16.71012 ? 220 LEU   A C   1 
ATOM   1604 O  O   . LEU   A 1 213 ? -17.03900 -18.96172 -14.07417 1.000 13.66288 ? 220 LEU   A O   1 
ATOM   1605 C  CB  . LEU   A 1 213 ? -14.81502 -17.54416 -12.76525 1.000 16.60805 ? 220 LEU   A CB  1 
ATOM   1606 C  CG  . LEU   A 1 213 ? -14.30180 -18.78175 -12.02981 1.000 20.97226 ? 220 LEU   A CG  1 
ATOM   1607 C  CD1 . LEU   A 1 213 ? -13.05470 -19.34401 -12.69994 1.000 17.34634 ? 220 LEU   A CD1 1 
ATOM   1608 C  CD2 . LEU   A 1 213 ? -14.02617 -18.43753 -10.57232 1.000 20.45742 ? 220 LEU   A CD2 1 
ATOM   1609 N  N   . PHE   A 1 214 ? -15.48562 -19.66249 -15.55486 1.000 15.12848 ? 221 PHE   A N   1 
ATOM   1610 C  CA  . PHE   A 1 214 ? -16.23587 -20.85295 -15.93446 1.000 13.88801 ? 221 PHE   A CA  1 
ATOM   1611 C  C   . PHE   A 1 214 ? -16.23865 -21.86177 -14.78935 1.000 18.98686 ? 221 PHE   A C   1 
ATOM   1612 O  O   . PHE   A 1 214 ? -15.28944 -21.95011 -14.00716 1.000 16.03242 ? 221 PHE   A O   1 
ATOM   1613 C  CB  . PHE   A 1 214 ? -15.62298 -21.51429 -17.17599 1.000 14.15047 ? 221 PHE   A CB  1 
ATOM   1614 C  CG  . PHE   A 1 214 ? -15.90148 -20.79792 -18.47523 1.000 14.45531 ? 221 PHE   A CG  1 
ATOM   1615 C  CD1 . PHE   A 1 214 ? -16.02573 -19.41672 -18.52584 1.000 13.28190 ? 221 PHE   A CD1 1 
ATOM   1616 C  CD2 . PHE   A 1 214 ? -16.01807 -21.51698 -19.65462 1.000 14.48773 ? 221 PHE   A CD2 1 
ATOM   1617 C  CE1 . PHE   A 1 214 ? -16.26919 -18.76655 -19.72563 1.000 14.07849 ? 221 PHE   A CE1 1 
ATOM   1618 C  CE2 . PHE   A 1 214 ? -16.26202 -20.87501 -20.85990 1.000 16.63265 ? 221 PHE   A CE2 1 
ATOM   1619 C  CZ  . PHE   A 1 214 ? -16.39187 -19.49650 -20.89493 1.000 15.52436 ? 221 PHE   A CZ  1 
ATOM   1620 N  N   . VAL   A 1 215 ? -17.30685 -22.64593 -14.70695 1.000 18.93337 ? 222 VAL   A N   1 
ATOM   1621 C  CA  . VAL   A 1 215 ? -17.39280 -23.73675 -13.74868 1.000 18.21133 ? 222 VAL   A CA  1 
ATOM   1622 C  C   . VAL   A 1 215 ? -17.22908 -25.05728 -14.49962 1.000 19.48428 ? 222 VAL   A C   1 
ATOM   1623 O  O   . VAL   A 1 215 ? -17.30744 -25.11588 -15.72566 1.000 18.28033 ? 222 VAL   A O   1 
ATOM   1624 C  CB  . VAL   A 1 215 ? -18.70547 -23.69744 -12.94065 1.000 32.95265 ? 222 VAL   A CB  1 
ATOM   1625 C  CG1 . VAL   A 1 215 ? -18.76466 -22.44541 -12.08393 1.000 40.00489 ? 222 VAL   A CG1 1 
ATOM   1626 C  CG2 . VAL   A 1 215 ? -19.88347 -23.71542 -13.86938 1.000 21.66422 ? 222 VAL   A CG2 1 
ATOM   1627 N  N   . GLU   A 1 216 ? -16.97762 -26.12402 -13.74982 1.000 21.46762 ? 223 GLU   A N   1 
ATOM   1628 C  CA  . GLU   A 1 216 ? -16.74350 -27.43575 -14.33604 1.000 28.12757 ? 223 GLU   A CA  1 
ATOM   1629 C  C   . GLU   A 1 216 ? -17.85776 -28.40382 -13.96428 1.000 34.24890 ? 223 GLU   A C   1 
ATOM   1630 O  O   . GLU   A 1 216 ? -18.52640 -28.24287 -12.93969 1.000 33.21874 ? 223 GLU   A O   1 
ATOM   1631 C  CB  . GLU   A 1 216 ? -15.39507 -28.01030 -13.89413 1.000 30.20015 ? 223 GLU   A CB  1 
ATOM   1632 C  CG  . GLU   A 1 216 ? -14.22003 -27.08830 -14.13105 1.000 30.04960 ? 223 GLU   A CG  1 
ATOM   1633 C  CD  . GLU   A 1 216 ? -12.92431 -27.64808 -13.57475 1.000 37.78627 ? 223 GLU   A CD  1 
ATOM   1634 O  OE1 . GLU   A 1 216 ? -12.49782 -28.72574 -14.04232 1.000 31.71305 ? 223 GLU   A OE1 1 
ATOM   1635 O  OE2 . GLU   A 1 216 ? -12.32750 -27.00501 -12.68275 1.000 31.22963 ? 223 GLU   A OE2 1 
ATOM   1636 N  N   . LYS   A 1 217 ? -18.04054 -29.41429 -14.81395 1.000 34.86990 ? 224 LYS   A N   1 
ATOM   1637 C  CA  . LYS   A 1 217 ? -19.04494 -30.45760 -14.61531 1.000 41.77076 ? 224 LYS   A CA  1 
ATOM   1638 C  C   . LYS   A 1 217 ? -18.91964 -31.12980 -13.24679 1.000 52.09012 ? 224 LYS   A C   1 
ATOM   1639 O  O   . LYS   A 1 217 ? -17.81982 -31.46820 -12.81242 1.000 51.19402 ? 224 LYS   A O   1 
ATOM   1640 C  CB  . LYS   A 1 217 ? -18.93371 -31.51391 -15.72313 1.000 45.06634 ? 224 LYS   A CB  1 
ATOM   1641 C  CG  . LYS   A 1 217 ? -19.90502 -32.67598 -15.57900 1.000 68.65922 ? 224 LYS   A CG  1 
ATOM   1642 C  CD  . LYS   A 1 217 ? -20.15968 -33.36723 -16.91219 1.000 63.82210 ? 224 LYS   A CD  1 
ATOM   1643 C  CE  . LYS   A 1 217 ? -19.78099 -34.84476 -16.85209 1.000 67.82304 ? 224 LYS   A CE  1 
ATOM   1644 N  NZ  . LYS   A 1 217 ? -18.30720 -35.05577 -16.80922 1.000 78.58942 ? 224 LYS   A NZ  1 
HETATM 1645 C  C1  . A1AYN B 2 .   ? -13.18874 -20.96719 -24.92268 0.562 31.31192 ? 301 A1AYN A C1  1 
HETATM 1646 C  C2  . A1AYN B 2 .   ? -13.51286 -22.14547 -24.20827 1.000 31.34949 ? 301 A1AYN A C2  1 
HETATM 1647 C  C3  . A1AYN B 2 .   ? -12.43578 -23.11406 -24.22467 1.000 29.16645 ? 301 A1AYN A C3  1 
HETATM 1648 C  C4  . A1AYN B 2 .   ? -11.84781 -21.02885 -25.48839 1.000 44.39976 ? 301 A1AYN A C4  1 
HETATM 1649 N  N1  . A1AYN B 2 .   ? -15.71985 -20.01749 -24.60478 0.881 23.88135 ? 301 A1AYN A N1  1 
HETATM 1650 O  O1  . A1AYN B 2 .   ? -13.79326 -18.57191 -24.20349 1.000 20.84877 ? 301 A1AYN A O1  1 
HETATM 1651 O  O2  . A1AYN B 2 .   ? -14.35423 -19.30067 -26.49139 0.371 26.65011 ? 301 A1AYN A O2  1 
HETATM 1652 S  S1  . A1AYN B 2 .   ? -14.25666 -19.59199 -25.08900 0.642 27.63526 ? 301 A1AYN A S1  1 
HETATM 1653 S  S2  . A1AYN B 2 .   ? -11.06721 -22.53006 -25.11335 0.521 38.20709 ? 301 A1AYN A S2  1 
HETATM 1654 CL CL1 . A1AYN B 2 .   ? -12.37047 -24.68034 -23.50427 0.427 34.57150 ? 301 A1AYN A CL1 1 
HETATM 1655 CL CL2 . A1AYN B 2 .   ? -11.03877 -19.84746 -26.42489 0.342 52.42129 ? 301 A1AYN A CL2 1 
HETATM 1656 O  O   . HOH   C 3 .   ? -14.85689 -22.00624 1.58627   1.000 49.00084 ? 401 HOH   A O   1 
HETATM 1657 O  O   . HOH   C 3 .   ? -12.762   -27.046   -35.298   1.000 35.31756 ? 402 HOH   A O   1 
HETATM 1658 O  O   . HOH   C 3 .   ? 1.99543   -15.70383 -40.99957 1.000 40.13802 ? 403 HOH   A O   1 
HETATM 1659 O  O   . HOH   C 3 .   ? 11.48247  -21.79801 -40.55131 1.000 43.20686 ? 404 HOH   A O   1 
HETATM 1660 O  O   . HOH   C 3 .   ? 9.14627   -3.37109  -20.33539 1.000 45.50678 ? 405 HOH   A O   1 
HETATM 1661 O  O   . HOH   C 3 .   ? -17.19189 -20.10447 -4.97583  1.000 43.46530 ? 406 HOH   A O   1 
HETATM 1662 O  O   . HOH   C 3 .   ? 15.05787  -0.97186  -12.08932 1.000 42.11260 ? 407 HOH   A O   1 
HETATM 1663 O  O   . HOH   C 3 .   ? 0.35389   -14.69512 -1.49264  1.000 37.26521 ? 408 HOH   A O   1 
HETATM 1664 O  O   . HOH   C 3 .   ? 22.29544  -7.63979  -22.17224 1.000 43.08573 ? 409 HOH   A O   1 
HETATM 1665 O  O   . HOH   C 3 .   ? 19.83562  -2.23432  -8.25211  1.000 46.38666 ? 410 HOH   A O   1 
HETATM 1666 O  O   . HOH   C 3 .   ? -1.62941  -29.03896 -5.90953  1.000 27.63044 ? 411 HOH   A O   1 
HETATM 1667 O  O   . HOH   C 3 .   ? 6.06334   -21.02217 0.06420   1.000 22.67560 ? 412 HOH   A O   1 
HETATM 1668 O  O   . HOH   C 3 .   ? -16.22161 -25.59236 -17.97345 1.000 20.21357 ? 413 HOH   A O   1 
HETATM 1669 O  O   . HOH   C 3 .   ? 7.57899   -18.65572 -6.53086  1.000 18.47580 ? 414 HOH   A O   1 
HETATM 1670 O  O   . HOH   C 3 .   ? -4.52534  -25.93038 -30.30907 1.000 36.32772 ? 415 HOH   A O   1 
HETATM 1671 O  O   . HOH   C 3 .   ? 18.23265  -7.24528  -20.32129 1.000 32.94171 ? 416 HOH   A O   1 
HETATM 1672 O  O   . HOH   C 3 .   ? 7.56521   1.21424   -14.81803 1.000 25.42109 ? 417 HOH   A O   1 
HETATM 1673 O  O   . HOH   C 3 .   ? -6.36038  -4.93244  -39.02918 1.000 39.99310 ? 418 HOH   A O   1 
HETATM 1674 O  O   . HOH   C 3 .   ? 0.52062   -26.83950 -37.31167 1.000 32.17022 ? 419 HOH   A O   1 
HETATM 1675 O  O   . HOH   C 3 .   ? -10.99383 -14.05544 -37.57511 1.000 29.96011 ? 420 HOH   A O   1 
HETATM 1676 O  O   . HOH   C 3 .   ? -8.73943  -11.87350 -36.42861 1.000 21.46368 ? 421 HOH   A O   1 
HETATM 1677 O  O   . HOH   C 3 .   ? -5.76025  -2.15053  -19.33889 1.000 19.26770 ? 422 HOH   A O   1 
HETATM 1678 O  O   . HOH   C 3 .   ? -8.50991  4.78152   -33.45483 1.000 24.22829 ? 423 HOH   A O   1 
HETATM 1679 O  O   . HOH   C 3 .   ? -16.31861 -12.63372 -19.80351 1.000 18.20342 ? 424 HOH   A O   1 
HETATM 1680 O  O   . HOH   C 3 .   ? -19.10865 -32.34490 -10.69028 1.000 54.85997 ? 425 HOH   A O   1 
HETATM 1681 O  O   . HOH   C 3 .   ? 9.77773   -14.82812 -25.22214 1.000 16.51380 ? 426 HOH   A O   1 
HETATM 1682 O  O   . HOH   C 3 .   ? 7.78361   -23.12609 -14.22658 1.000 23.25813 ? 427 HOH   A O   1 
HETATM 1683 O  O   . HOH   C 3 .   ? -2.80170  -3.19394  -35.50349 1.000 37.08272 ? 428 HOH   A O   1 
HETATM 1684 O  O   . HOH   C 3 .   ? 3.02013   -24.45763 -38.54424 1.000 33.37388 ? 429 HOH   A O   1 
HETATM 1685 O  O   . HOH   C 3 .   ? -6.44058  -7.72092  -34.25214 1.000 13.59761 ? 430 HOH   A O   1 
HETATM 1686 O  O   . HOH   C 3 .   ? 14.00113  -11.25990 -29.57031 1.000 38.39875 ? 431 HOH   A O   1 
HETATM 1687 O  O   . HOH   C 3 .   ? -4.18363  -4.78693  -8.50834  1.000 34.52109 ? 432 HOH   A O   1 
HETATM 1688 O  O   . HOH   C 3 .   ? -0.38852  -5.41041  -18.35822 1.000 25.04203 ? 433 HOH   A O   1 
HETATM 1689 O  O   . HOH   C 3 .   ? 3.00654   -5.84132  -5.99439  1.000 41.38867 ? 434 HOH   A O   1 
HETATM 1690 O  O   . HOH   C 3 .   ? 19.70602  -16.88212 -27.48355 1.000 31.68975 ? 435 HOH   A O   1 
HETATM 1691 O  O   . HOH   C 3 .   ? -10.10537 -24.70990 3.25764   1.000 51.41835 ? 436 HOH   A O   1 
HETATM 1692 O  O   . HOH   C 3 .   ? -4.41262  0.63556   -22.20403 1.000 29.37372 ? 437 HOH   A O   1 
HETATM 1693 O  O   . HOH   C 3 .   ? -11.75096 -0.29048  -15.46724 1.000 36.40386 ? 438 HOH   A O   1 
HETATM 1694 O  O   . HOH   C 3 .   ? -8.19624  1.97751   -36.47888 1.000 33.49468 ? 439 HOH   A O   1 
HETATM 1695 O  O   . HOH   C 3 .   ? -9.34245  -2.29587  -17.59979 1.000 18.00717 ? 440 HOH   A O   1 
HETATM 1696 O  O   . HOH   C 3 .   ? 5.78444   -21.89255 -37.35962 1.000 29.10365 ? 441 HOH   A O   1 
HETATM 1697 O  O   . HOH   C 3 .   ? 3.61533   -7.72638  -36.55991 1.000 28.43141 ? 442 HOH   A O   1 
HETATM 1698 O  O   . HOH   C 3 .   ? -7.32598  -27.95452 -21.09218 1.000 42.11597 ? 443 HOH   A O   1 
HETATM 1699 O  O   . HOH   C 3 .   ? 1.32732   -7.91231  -16.55329 1.000 19.15962 ? 444 HOH   A O   1 
HETATM 1700 O  O   . HOH   C 3 .   ? 18.49256  -16.07514 -13.50467 1.000 30.16388 ? 445 HOH   A O   1 
HETATM 1701 O  O   . HOH   C 3 .   ? 15.33785  -20.20632 -18.66707 1.000 20.39481 ? 446 HOH   A O   1 
HETATM 1702 O  O   . HOH   C 3 .   ? 14.78441  -26.21946 -24.44556 1.000 40.68644 ? 447 HOH   A O   1 
HETATM 1703 O  O   . HOH   C 3 .   ? 8.57394   -0.46168  -17.35321 1.000 42.41695 ? 448 HOH   A O   1 
HETATM 1704 O  O   . HOH   C 3 .   ? 11.44141  -27.50776 -34.64653 1.000 23.71706 ? 449 HOH   A O   1 
HETATM 1705 O  O   . HOH   C 3 .   ? -0.26792  -5.61732  -38.22328 1.000 38.66079 ? 450 HOH   A O   1 
HETATM 1706 O  O   . HOH   C 3 .   ? 4.54370   -30.59738 -11.57299 1.000 33.23071 ? 451 HOH   A O   1 
HETATM 1707 O  O   . HOH   C 3 .   ? 0.65888   -29.55038 -15.96759 1.000 31.89448 ? 452 HOH   A O   1 
HETATM 1708 O  O   . HOH   C 3 .   ? -3.94077  -21.07844 -38.16631 1.000 44.40264 ? 453 HOH   A O   1 
HETATM 1709 O  O   . HOH   C 3 .   ? 0.89468   -20.91825 -4.68368  1.000 27.26978 ? 454 HOH   A O   1 
HETATM 1710 O  O   . HOH   C 3 .   ? 6.59637   -26.69816 -27.62700 1.000 29.95196 ? 455 HOH   A O   1 
HETATM 1711 O  O   . HOH   C 3 .   ? -7.80013  -28.14859 -7.91301  1.000 27.43376 ? 456 HOH   A O   1 
HETATM 1712 O  O   . HOH   C 3 .   ? -13.13215 -7.31410  -11.99020 1.000 30.83667 ? 457 HOH   A O   1 
HETATM 1713 O  O   . HOH   C 3 .   ? -1.58325  -32.42130 -8.15525  1.000 41.18120 ? 458 HOH   A O   1 
HETATM 1714 O  O   . HOH   C 3 .   ? 3.25743   -6.15727  -11.14433 1.000 22.08331 ? 459 HOH   A O   1 
HETATM 1715 O  O   . HOH   C 3 .   ? 11.35679  -28.39939 -30.45256 1.000 23.38844 ? 460 HOH   A O   1 
HETATM 1716 O  O   . HOH   C 3 .   ? -2.90550  -5.95901  -6.55989  1.000 31.67338 ? 461 HOH   A O   1 
HETATM 1717 O  O   . HOH   C 3 .   ? -14.56347 -6.85805  -14.41553 1.000 30.09054 ? 462 HOH   A O   1 
HETATM 1718 O  O   . HOH   C 3 .   ? 9.98941   -23.88516 -9.03367  1.000 39.69160 ? 463 HOH   A O   1 
HETATM 1719 O  O   . HOH   C 3 .   ? -13.04009 -24.87829 -10.85995 1.000 27.91553 ? 464 HOH   A O   1 
HETATM 1720 O  O   . HOH   C 3 .   ? 9.65938   -17.32221 -7.74455  1.000 23.50006 ? 465 HOH   A O   1 
HETATM 1721 O  O   . HOH   C 3 .   ? -0.94969  -11.28587 -2.95674  1.000 36.50289 ? 466 HOH   A O   1 
HETATM 1722 O  O   . HOH   C 3 .   ? -3.90549  -14.04114 -0.83157  1.000 38.29468 ? 467 HOH   A O   1 
HETATM 1723 O  O   . HOH   C 3 .   ? 0.74400   -5.26359  -13.95896 1.000 32.41661 ? 468 HOH   A O   1 
HETATM 1724 O  O   . HOH   C 3 .   ? 6.66523   -29.66223 -20.05511 1.000 28.02374 ? 469 HOH   A O   1 
HETATM 1725 O  O   . HOH   C 3 .   ? 12.88140  -13.98671 -29.64037 1.000 21.54537 ? 470 HOH   A O   1 
HETATM 1726 O  O   . HOH   C 3 .   ? -5.35016  -10.34866 -27.30994 1.000 13.86493 ? 471 HOH   A O   1 
HETATM 1727 O  O   . HOH   C 3 .   ? 7.70157   -27.77282 -24.05297 1.000 23.36453 ? 472 HOH   A O   1 
HETATM 1728 O  O   . HOH   C 3 .   ? -5.84575  -7.14591  -42.33741 1.000 46.37595 ? 473 HOH   A O   1 
HETATM 1729 O  O   . HOH   C 3 .   ? -7.47441  -5.43430  -2.79918  1.000 48.47511 ? 474 HOH   A O   1 
HETATM 1730 O  O   . HOH   C 3 .   ? 20.79702  -16.55098 -19.95629 1.000 32.14130 ? 475 HOH   A O   1 
HETATM 1731 O  O   . HOH   C 3 .   ? -13.34986 -0.73044  -20.38427 1.000 23.97643 ? 476 HOH   A O   1 
HETATM 1732 O  O   . HOH   C 3 .   ? -14.72765 -22.65178 -11.43718 1.000 24.97286 ? 477 HOH   A O   1 
HETATM 1733 O  O   . HOH   C 3 .   ? -8.13319  -24.79589 -19.09552 1.000 13.55827 ? 478 HOH   A O   1 
HETATM 1734 O  O   . HOH   C 3 .   ? -13.73524 -16.98487 -2.71219  1.000 21.75809 ? 479 HOH   A O   1 
HETATM 1735 O  O   . HOH   C 3 .   ? 8.81657   -15.45879 -27.84677 1.000 15.32330 ? 480 HOH   A O   1 
HETATM 1736 O  O   . HOH   C 3 .   ? 9.17427   -26.32275 -17.01144 1.000 26.56704 ? 481 HOH   A O   1 
HETATM 1737 O  O   . HOH   C 3 .   ? -1.20862  -7.34784  -23.62112 1.000 21.30842 ? 482 HOH   A O   1 
HETATM 1738 O  O   . HOH   C 3 .   ? -15.87999 0.28545   -30.47642 1.000 34.39409 ? 483 HOH   A O   1 
HETATM 1739 O  O   . HOH   C 3 .   ? -3.89855  -3.46831  -15.34457 1.000 33.76059 ? 484 HOH   A O   1 
HETATM 1740 O  O   . HOH   C 3 .   ? -2.27722  -13.59023 -35.57633 1.000 15.41126 ? 485 HOH   A O   1 
HETATM 1741 O  O   . HOH   C 3 .   ? -17.12336 -5.40102  -22.76796 1.000 21.46292 ? 486 HOH   A O   1 
HETATM 1742 O  O   . HOH   C 3 .   ? 3.08376   -20.42021 -2.75874  1.000 33.55693 ? 487 HOH   A O   1 
HETATM 1743 O  O   . HOH   C 3 .   ? 13.60287  -14.27910 -26.73892 1.000 17.77380 ? 488 HOH   A O   1 
HETATM 1744 O  O   . HOH   C 3 .   ? 0.38023   -22.20352 -2.12914  1.000 44.50405 ? 489 HOH   A O   1 
HETATM 1745 O  O   . HOH   C 3 .   ? -6.33293  -5.00799  -35.53952 1.000 16.87215 ? 490 HOH   A O   1 
HETATM 1746 O  O   . HOH   C 3 .   ? 10.39294  -21.01506 -6.94287  1.000 36.62109 ? 491 HOH   A O   1 
HETATM 1747 O  O   . HOH   C 3 .   ? 0.83346   -6.16218  -34.11656 1.000 38.18568 ? 492 HOH   A O   1 
HETATM 1748 O  O   . HOH   C 3 .   ? -0.30407  -7.12587  -30.96276 1.000 26.81966 ? 493 HOH   A O   1 
HETATM 1749 O  O   . HOH   C 3 .   ? 17.95266  -19.36393 -24.55438 1.000 21.69647 ? 494 HOH   A O   1 
HETATM 1750 O  O   . HOH   C 3 .   ? -20.55773 -14.11070 -18.14199 1.000 41.40391 ? 495 HOH   A O   1 
HETATM 1751 O  O   . HOH   C 3 .   ? -5.43954  -7.62410  -13.12776 1.000 14.36218 ? 496 HOH   A O   1 
HETATM 1752 O  O   . HOH   C 3 .   ? 5.82641   -25.22580 -7.26952  1.000 40.56792 ? 497 HOH   A O   1 
HETATM 1753 O  O   . HOH   C 3 .   ? -8.94144  -10.27524 -40.30781 1.000 39.38229 ? 498 HOH   A O   1 
HETATM 1754 O  O   . HOH   C 3 .   ? -3.76815  -13.15974 -42.61925 1.000 42.38631 ? 499 HOH   A O   1 
HETATM 1755 O  O   . HOH   C 3 .   ? -15.27686 -10.99437 -29.73926 1.000 21.68735 ? 500 HOH   A O   1 
HETATM 1756 O  O   . HOH   C 3 .   ? 12.32593  -27.26614 -19.71617 1.000 32.41369 ? 501 HOH   A O   1 
HETATM 1757 O  O   . HOH   C 3 .   ? 10.55485  -25.37307 -23.70538 1.000 17.41556 ? 502 HOH   A O   1 
HETATM 1758 O  O   . HOH   C 3 .   ? 14.45104  -15.99020 -30.68678 1.000 34.01564 ? 503 HOH   A O   1 
HETATM 1759 O  O   . HOH   C 3 .   ? -2.12588  -0.62432  -18.49668 1.000 31.97482 ? 504 HOH   A O   1 
HETATM 1760 O  O   . HOH   C 3 .   ? -15.206   -23.251   -30.672   1.000 32.32730 ? 505 HOH   A O   1 
HETATM 1761 O  O   . HOH   C 3 .   ? -10.69504 -14.41075 0.94314   1.000 27.09263 ? 506 HOH   A O   1 
HETATM 1762 O  O   . HOH   C 3 .   ? 11.25488  -8.08371  -27.38196 1.000 18.20143 ? 507 HOH   A O   1 
HETATM 1763 O  O   . HOH   C 3 .   ? -14.14783 -12.65861 -7.78553  1.000 19.74231 ? 508 HOH   A O   1 
HETATM 1764 O  O   . HOH   C 3 .   ? -7.62291  -24.46365 -22.97076 1.000 31.23578 ? 509 HOH   A O   1 
HETATM 1765 O  O   . HOH   C 3 .   ? -5.86369  -31.13195 -11.55744 1.000 26.50556 ? 510 HOH   A O   1 
HETATM 1766 O  O   . HOH   C 3 .   ? -6.28218  -11.23900 -10.05544 1.000 23.16075 ? 511 HOH   A O   1 
HETATM 1767 O  O   . HOH   C 3 .   ? 7.99655   -23.13909 -7.20520  1.000 36.61654 ? 512 HOH   A O   1 
HETATM 1768 O  O   . HOH   C 3 .   ? -8.06524  -3.89865  -10.67895 1.000 25.31728 ? 513 HOH   A O   1 
HETATM 1769 O  O   . HOH   C 3 .   ? -3.48495  -10.82369 -23.98837 1.000 22.95923 ? 514 HOH   A O   1 
HETATM 1770 O  O   . HOH   C 3 .   ? 14.00970  -15.59371 -2.07361  1.000 34.63022 ? 515 HOH   A O   1 
HETATM 1771 O  O   . HOH   C 3 .   ? -2.40216  -10.64791 -26.34620 1.000 28.88374 ? 516 HOH   A O   1 
HETATM 1772 O  O   . HOH   C 3 .   ? 15.42493  -0.73174  -19.40508 1.000 31.91359 ? 517 HOH   A O   1 
HETATM 1773 O  O   . HOH   C 3 .   ? 8.46257   -16.30691 -39.52275 1.000 35.20169 ? 518 HOH   A O   1 
HETATM 1774 O  O   . HOH   C 3 .   ? 0.39107   -1.39090  -19.72991 1.000 30.71126 ? 519 HOH   A O   1 
HETATM 1775 O  O   . HOH   C 3 .   ? -5.92185  -18.62326 -38.93885 1.000 30.39185 ? 520 HOH   A O   1 
HETATM 1776 O  O   . HOH   C 3 .   ? -4.65103  0.48208   -30.27556 1.000 28.22392 ? 521 HOH   A O   1 
HETATM 1777 O  O   . HOH   C 3 .   ? 6.03581   1.02010   -7.66672  1.000 48.60973 ? 522 HOH   A O   1 
HETATM 1778 O  O   . HOH   C 3 .   ? -2.34235  -24.80726 -1.37885  1.000 49.66324 ? 523 HOH   A O   1 
HETATM 1779 O  O   . HOH   C 3 .   ? -17.29899 -28.69569 -17.41980 1.000 38.00479 ? 524 HOH   A O   1 
HETATM 1780 O  O   . HOH   C 3 .   ? -16.07979 -2.90567  -21.17477 1.000 24.90687 ? 525 HOH   A O   1 
HETATM 1781 O  O   . HOH   C 3 .   ? 3.68826   -11.89351 -38.56058 1.000 21.16219 ? 526 HOH   A O   1 
HETATM 1782 O  O   . HOH   C 3 .   ? 4.02925   -24.20584 -30.63433 1.000 14.82432 ? 527 HOH   A O   1 
HETATM 1783 O  O   . HOH   C 3 .   ? -3.12418  -1.08575  -24.13368 1.000 25.26593 ? 528 HOH   A O   1 
HETATM 1784 O  O   . HOH   C 3 .   ? 9.49863   -11.19511 -34.92165 1.000 40.86089 ? 529 HOH   A O   1 
HETATM 1785 O  O   . HOH   C 3 .   ? 20.35453  -10.78495 -26.34326 1.000 40.97577 ? 530 HOH   A O   1 
HETATM 1786 O  O   . HOH   C 3 .   ? -3.45376  -3.26879  -40.61120 1.000 43.57407 ? 531 HOH   A O   1 
HETATM 1787 O  O   . HOH   C 3 .   ? 10.62070  -25.61483 -26.67310 1.000 26.47346 ? 532 HOH   A O   1 
HETATM 1788 O  O   . HOH   C 3 .   ? -10.37903 -11.59991 -2.07019  1.000 22.31473 ? 533 HOH   A O   1 
HETATM 1789 O  O   . HOH   C 3 .   ? -7.59540  -23.01330 -30.44174 1.000 34.42574 ? 534 HOH   A O   1 
HETATM 1790 O  O   . HOH   C 3 .   ? 8.88157   -20.32954 -4.33028  1.000 24.02176 ? 535 HOH   A O   1 
HETATM 1791 O  O   . HOH   C 3 .   ? -5.13678  -14.17135 -22.66997 1.000 16.23819 ? 536 HOH   A O   1 
HETATM 1792 O  O   . HOH   C 3 .   ? 3.57066   -6.73713  -17.90350 1.000 22.23418 ? 537 HOH   A O   1 
HETATM 1793 O  O   . HOH   C 3 .   ? 7.25521   -4.72156  -22.45451 1.000 35.76679 ? 538 HOH   A O   1 
HETATM 1794 O  O   . HOH   C 3 .   ? -17.82081 -18.94369 -11.34743 1.000 31.45694 ? 539 HOH   A O   1 
HETATM 1795 O  O   . HOH   C 3 .   ? -5.09855  -31.54660 -6.99354  1.000 38.73498 ? 540 HOH   A O   1 
HETATM 1796 O  O   . HOH   C 3 .   ? -3.27552  -21.08372 -0.50989  1.000 38.59837 ? 541 HOH   A O   1 
HETATM 1797 O  O   . HOH   C 3 .   ? -1.37011  -26.01925 -32.20205 1.000 30.69838 ? 542 HOH   A O   1 
HETATM 1798 O  O   . HOH   C 3 .   ? 8.42794   -20.49430 -9.32047  1.000 24.64065 ? 543 HOH   A O   1 
HETATM 1799 O  O   . HOH   C 3 .   ? 4.15436   -19.35489 -40.67635 1.000 33.59571 ? 544 HOH   A O   1 
HETATM 1800 O  O   . HOH   C 3 .   ? -19.833   -19.495   -14.368   1.000 15.16232 ? 545 HOH   A O   1 
HETATM 1801 O  O   . HOH   C 3 .   ? -19.96810 -12.71739 -16.57981 1.000 42.67017 ? 546 HOH   A O   1 
HETATM 1802 O  O   . HOH   C 3 .   ? -17.89976 -3.64030  -28.81790 1.000 41.23917 ? 547 HOH   A O   1 
HETATM 1803 O  O   . HOH   C 3 .   ? -10.30541 -3.37424  -40.00566 1.000 49.22693 ? 548 HOH   A O   1 
HETATM 1804 O  O   . HOH   C 3 .   ? 1.41752   -3.16842  -24.30959 1.000 36.07699 ? 549 HOH   A O   1 
HETATM 1805 O  O   . HOH   C 3 .   ? 20.00707  -5.45087  -14.77029 1.000 44.15834 ? 550 HOH   A O   1 
HETATM 1806 O  O   . HOH   C 3 .   ? -1.79160  -25.60721 -4.72326  1.000 20.36575 ? 551 HOH   A O   1 
HETATM 1807 O  O   . HOH   C 3 .   ? 0.45492   -5.50969  -21.77351 1.000 33.37407 ? 552 HOH   A O   1 
HETATM 1808 O  O   . HOH   C 3 .   ? -11.81623 -7.51207  -38.32632 1.000 33.24667 ? 553 HOH   A O   1 
HETATM 1809 O  O   . HOH   C 3 .   ? -13.44854 -26.52067 -18.12032 1.000 19.41909 ? 554 HOH   A O   1 
HETATM 1810 O  O   . HOH   C 3 .   ? -1.96905  -33.79046 -10.56761 1.000 44.86718 ? 555 HOH   A O   1 
HETATM 1811 O  O   . HOH   C 3 .   ? -3.40524  -13.00670 -20.68531 1.000 18.81457 ? 556 HOH   A O   1 
HETATM 1812 O  O   . HOH   C 3 .   ? -1.61240  -6.26786  -26.25936 1.000 19.33466 ? 557 HOH   A O   1 
HETATM 1813 O  O   . HOH   C 3 .   ? 13.66466  -20.47677 -20.84600 1.000 16.25380 ? 558 HOH   A O   1 
HETATM 1814 O  O   . HOH   C 3 .   ? -17.75894 -15.23132 -13.17187 1.000 21.29025 ? 559 HOH   A O   1 
HETATM 1815 O  O   . HOH   C 3 .   ? 5.14446   -29.28063 -8.37607  1.000 41.32687 ? 560 HOH   A O   1 
HETATM 1816 O  O   . HOH   C 3 .   ? 4.88018   -9.68759  -2.40965  1.000 42.25941 ? 561 HOH   A O   1 
HETATM 1817 O  O   . HOH   C 3 .   ? -19.52456 -10.35099 -32.69635 1.000 37.25429 ? 562 HOH   A O   1 
HETATM 1818 O  O   . HOH   C 3 .   ? -6.00274  -13.97891 0.81224   1.000 24.28965 ? 563 HOH   A O   1 
HETATM 1819 O  O   . HOH   C 3 .   ? -10.24701 -14.97483 -28.29471 1.000 30.46503 ? 564 HOH   A O   1 
HETATM 1820 O  O   . HOH   C 3 .   ? -2.99295  -31.53738 -20.05784 1.000 42.79036 ? 565 HOH   A O   1 
HETATM 1821 O  O   . HOH   C 3 .   ? -10.14114 -0.47499  -19.81631 1.000 31.91384 ? 566 HOH   A O   1 
HETATM 1822 O  O   . HOH   C 3 .   ? -14.66132 -3.55301  -12.82638 1.000 40.39022 ? 567 HOH   A O   1 
HETATM 1823 O  O   . HOH   C 3 .   ? -8.79328  -18.08465 -36.68307 1.000 34.14898 ? 568 HOH   A O   1 
HETATM 1824 O  O   . HOH   C 3 .   ? 10.92283  -11.53803 -4.94499  1.000 30.77470 ? 569 HOH   A O   1 
HETATM 1825 O  O   . HOH   C 3 .   ? 10.27540  -17.86353 -38.98702 1.000 40.16899 ? 570 HOH   A O   1 
HETATM 1826 O  O   . HOH   C 3 .   ? 15.62303  -18.05589 -3.55059  1.000 33.42071 ? 571 HOH   A O   1 
HETATM 1827 O  O   . HOH   C 3 .   ? -12.285   -20.567   -29.735   1.000 44.71739 ? 572 HOH   A O   1 
HETATM 1828 O  O   . HOH   C 3 .   ? -13.07495 -12.02283 -31.12546 1.000 23.99441 ? 573 HOH   A O   1 
HETATM 1829 O  O   . HOH   C 3 .   ? -16.63122 -9.25209  -14.25204 1.000 31.52420 ? 574 HOH   A O   1 
HETATM 1830 O  O   . HOH   C 3 .   ? 1.19241   -8.83160  -26.90511 1.000 32.96915 ? 575 HOH   A O   1 
HETATM 1831 O  O   . HOH   C 3 .   ? -18.21073 -3.08881  -35.58819 1.000 46.26659 ? 576 HOH   A O   1 
HETATM 1832 O  O   . HOH   C 3 .   ? 13.33669  -6.88147  -26.19423 1.000 19.19251 ? 577 HOH   A O   1 
HETATM 1833 O  O   . HOH   C 3 .   ? -7.28886  1.44336   -19.30469 1.000 30.94354 ? 578 HOH   A O   1 
HETATM 1834 O  O   . HOH   C 3 .   ? 8.31887   -19.89515 -41.36499 1.000 44.52132 ? 579 HOH   A O   1 
HETATM 1835 O  O   . HOH   C 3 .   ? -7.26225  -36.48613 -15.32940 1.000 47.89108 ? 580 HOH   A O   1 
HETATM 1836 O  O   . HOH   C 3 .   ? 2.08050   -6.15585  -25.79181 1.000 39.80023 ? 581 HOH   A O   1 
HETATM 1837 O  O   . HOH   C 3 .   ? 4.03919   -9.17187  -20.36391 1.000 17.14856 ? 582 HOH   A O   1 
HETATM 1838 O  O   . HOH   C 3 .   ? -8.20677  -24.10690 -25.79143 1.000 40.72646 ? 583 HOH   A O   1 
HETATM 1839 O  O   . HOH   C 3 .   ? -1.66673  -8.49862  -27.80178 1.000 27.40063 ? 584 HOH   A O   1 
HETATM 1840 O  O   . HOH   C 3 .   ? -14.65789 -28.89451 -9.69168  1.000 42.96679 ? 585 HOH   A O   1 
HETATM 1841 O  O   . HOH   C 3 .   ? -3.65086  -32.84228 -11.18469 1.000 46.86651 ? 586 HOH   A O   1 
HETATM 1842 O  O   . HOH   C 3 .   ? 3.13008   -4.09527  -8.91744  1.000 38.73693 ? 587 HOH   A O   1 
HETATM 1843 O  O   . HOH   C 3 .   ? -9.01924  -25.86885 -29.51398 1.000 37.49862 ? 588 HOH   A O   1 
HETATM 1844 O  O   . HOH   C 3 .   ? 20.82081  -14.09898 -26.77609 1.000 26.73621 ? 589 HOH   A O   1 
HETATM 1845 O  O   . HOH   C 3 .   ? -0.02557  -16.54427 -3.43236  1.000 24.85059 ? 590 HOH   A O   1 
HETATM 1846 O  O   . HOH   C 3 .   ? -12.23839 -26.84641 -20.21516 1.000 18.31127 ? 591 HOH   A O   1 
HETATM 1847 O  O   . HOH   C 3 .   ? -15.11448 -11.99681 -11.94011 1.000 29.88644 ? 592 HOH   A O   1 
HETATM 1848 O  O   . HOH   C 3 .   ? -10.51825 -6.20804  -2.84110  1.000 41.06277 ? 593 HOH   A O   1 
HETATM 1849 O  O   . HOH   C 3 .   ? -18.01679 -5.71837  -25.39076 1.000 31.15783 ? 594 HOH   A O   1 
HETATM 1850 O  O   . HOH   C 3 .   ? 6.92581   -29.86203 -30.18720 1.000 45.49842 ? 595 HOH   A O   1 
HETATM 1851 O  O   . HOH   C 3 .   ? -13.56886 -25.78262 -7.79518  1.000 23.34098 ? 596 HOH   A O   1 
HETATM 1852 O  O   . HOH   C 3 .   ? -2.19316  -8.92978  -43.40531 1.000 47.63457 ? 597 HOH   A O   1 
HETATM 1853 O  O   . HOH   C 3 .   ? -0.46285  -12.44724 -21.33587 1.000 25.41618 ? 598 HOH   A O   1 
HETATM 1854 O  O   . HOH   C 3 .   ? -18.00519 -33.86667 -10.96619 1.000 49.31058 ? 599 HOH   A O   1 
HETATM 1855 O  O   . HOH   C 3 .   ? 3.80670   -23.12703 -3.40230  1.000 33.18933 ? 600 HOH   A O   1 
HETATM 1856 O  O   . HOH   C 3 .   ? -2.44409  -15.50383 -0.12796  1.000 37.69969 ? 601 HOH   A O   1 
HETATM 1857 O  O   . HOH   C 3 .   ? -7.62112  -13.69281 -41.07741 1.000 43.59163 ? 602 HOH   A O   1 
HETATM 1858 O  O   . HOH   C 3 .   ? 20.23766  -5.87599  -21.20666 1.000 37.33614 ? 603 HOH   A O   1 
HETATM 1859 O  O   . HOH   C 3 .   ? -15.75134 -1.15326  -27.75640 1.000 43.09154 ? 604 HOH   A O   1 
HETATM 1860 O  O   . HOH   C 3 .   ? -17.71051 -15.99771 -23.58503 1.000 34.68804 ? 605 HOH   A O   1 
HETATM 1861 O  O   . HOH   C 3 .   ? 17.36187  -15.40880 -29.80172 1.000 41.28623 ? 606 HOH   A O   1 
HETATM 1862 O  O   . HOH   C 3 .   ? -0.98271  -29.85919 -16.93984 1.000 36.37573 ? 607 HOH   A O   1 
HETATM 1863 O  O   . HOH   C 3 .   ? -7.63806  7.55233   -33.64721 1.000 30.31799 ? 608 HOH   A O   1 
HETATM 1864 O  O   . HOH   C 3 .   ? -12.300   -9.670    1.443     1.000 49.40863 ? 609 HOH   A O   1 
HETATM 1865 O  O   . HOH   C 3 .   ? -16.35455 -25.35390 -10.80064 1.000 36.99014 ? 610 HOH   A O   1 
HETATM 1866 O  O   . HOH   C 3 .   ? -13.99925 -24.03015 -4.80935  1.000 25.40862 ? 611 HOH   A O   1 
HETATM 1867 O  O   . HOH   C 3 .   ? -14.69473 -21.57917 -33.39803 1.000 43.80337 ? 612 HOH   A O   1 
HETATM 1868 O  O   . HOH   C 3 .   ? 21.56070  -13.53643 -19.55560 1.000 40.19560 ? 613 HOH   A O   1 
HETATM 1869 O  O   . HOH   C 3 .   ? -16.018   -4.166    -15.316   1.000 43.22681 ? 614 HOH   A O   1 
HETATM 1870 O  O   . HOH   C 3 .   ? -11.91140 -18.77100 -28.40723 1.000 41.99410 ? 615 HOH   A O   1 
HETATM 1871 O  O   . HOH   C 3 .   ? 11.55133  -1.69148  -20.24442 1.000 34.21125 ? 616 HOH   A O   1 
HETATM 1872 O  O   . HOH   C 3 .   ? 2.73946   -10.08758 -23.22255 1.000 27.34269 ? 617 HOH   A O   1 
HETATM 1873 O  O   . HOH   C 3 .   ? 13.75870  -4.07755  -25.41578 1.000 11.42454 ? 618 HOH   A O   1 
HETATM 1874 O  O   . HOH   C 3 .   ? -5.62527  -12.14265 -41.91242 1.000 40.41205 ? 619 HOH   A O   1 
HETATM 1875 O  O   . HOH   C 3 .   ? 8.11837   -25.82764 -25.76220 1.000 40.10725 ? 620 HOH   A O   1 
HETATM 1876 O  O   . HOH   C 3 .   ? 14.35424  -22.48141 -17.25835 1.000 31.95656 ? 621 HOH   A O   1 
HETATM 1877 O  O   . HOH   C 3 .   ? -1.82066  -26.98163 -24.99952 1.000 39.35095 ? 622 HOH   A O   1 
HETATM 1878 O  O   . HOH   C 3 .   ? -17.21766 -4.91480  -17.51691 1.000 32.07368 ? 623 HOH   A O   1 
HETATM 1879 O  O   . HOH   C 3 .   ? -10.47917 -8.71051  -1.39245  1.000 34.15712 ? 624 HOH   A O   1 
HETATM 1880 O  O   . HOH   C 3 .   ? 3.85608   -30.50555 -19.54335 1.000 40.80877 ? 625 HOH   A O   1 
HETATM 1881 O  O   . HOH   C 3 .   ? 1.859     -18.391   0.144     1.000 32.58560 ? 626 HOH   A O   1 
HETATM 1882 O  O   . HOH   C 3 .   ? 2.96206   -6.26043  -20.47837 1.000 42.03909 ? 627 HOH   A O   1 
HETATM 1883 O  O   . HOH   C 3 .   ? 4.19083   -21.92513 -39.34909 1.000 43.69871 ? 628 HOH   A O   1 
HETATM 1884 O  O   . HOH   C 3 .   ? -4.88702  -5.18900  -12.14399 1.000 37.33051 ? 629 HOH   A O   1 
HETATM 1885 O  O   . HOH   C 3 .   ? -14.24485 -15.98428 -26.16396 1.000 30.83211 ? 630 HOH   A O   1 
HETATM 1886 O  O   . HOH   C 3 .   ? 4.67845   -2.01794  -18.30437 1.000 31.24271 ? 631 HOH   A O   1 
HETATM 1887 O  O   . HOH   C 3 .   ? 1.95941   -25.98318 -29.25023 1.000 31.32917 ? 632 HOH   A O   1 
HETATM 1888 O  O   . HOH   C 3 .   ? 5.617     -3.063    -26.058   1.000 40.52892 ? 633 HOH   A O   1 
HETATM 1889 O  O   . HOH   C 3 .   ? 7.04631   1.94383   -12.63884 1.000 37.49441 ? 634 HOH   A O   1 
HETATM 1890 O  O   . HOH   C 3 .   ? -14.23451 -11.78870 0.43636   1.000 36.43146 ? 635 HOH   A O   1 
HETATM 1891 O  O   . HOH   C 3 .   ? -18.33491 -14.69834 -22.43822 1.000 38.74401 ? 636 HOH   A O   1 
HETATM 1892 O  O   . HOH   C 3 .   ? 18.62350  -22.30618 -21.36510 1.000 44.48374 ? 637 HOH   A O   1 
HETATM 1893 O  O   . HOH   C 3 .   ? -13.936   -0.724    -13.478   1.000 34.35642 ? 638 HOH   A O   1 
HETATM 1894 O  O   . HOH   C 3 .   ? -1.38214  -32.90713 -16.50495 1.000 44.87503 ? 639 HOH   A O   1 
HETATM 1895 O  O   . HOH   C 3 .   ? -9.21969  -5.69232  -39.59857 1.000 39.77482 ? 640 HOH   A O   1 
HETATM 1896 O  O   . HOH   C 3 .   ? -14.25535 -9.82212  -8.13289  1.000 35.67133 ? 641 HOH   A O   1 
HETATM 1897 O  O   . HOH   C 3 .   ? 1.82021   -2.98868  -13.01837 1.000 36.98612 ? 642 HOH   A O   1 
HETATM 1898 O  O   . HOH   C 3 .   ? -13.99648 -14.15667 -3.15887  1.000 31.28643 ? 643 HOH   A O   1 
HETATM 1899 O  O   . HOH   C 3 .   ? -0.03097  -19.16336 -2.06159  1.000 37.02220 ? 644 HOH   A O   1 
HETATM 1900 O  O   . HOH   C 3 .   ? 12.05660  -25.47117 -38.56033 1.000 32.09834 ? 645 HOH   A O   1 
HETATM 1901 O  O   . HOH   C 3 .   ? -12.44872 -16.33855 -28.17600 1.000 35.63210 ? 646 HOH   A O   1 
HETATM 1902 O  O   . HOH   C 3 .   ? 6.15626   -29.76903 -24.81460 1.000 41.55084 ? 647 HOH   A O   1 
HETATM 1903 O  O   . HOH   C 3 .   ? 1.44426   -7.44005  -22.83457 1.000 39.62631 ? 648 HOH   A O   1 
HETATM 1904 O  O   . HOH   C 3 .   ? 16.17459  0.18772   -9.87740  1.000 44.24232 ? 649 HOH   A O   1 
HETATM 1905 O  O   . HOH   C 3 .   ? -0.49967  -1.30043  -23.09323 1.000 38.89688 ? 650 HOH   A O   1 
HETATM 1906 O  O   . HOH   C 3 .   ? 18.27307  -3.38836  -22.91363 1.000 40.06402 ? 651 HOH   A O   1 
HETATM 1907 O  O   . HOH   C 3 .   ? -5.43921  -1.88283  -16.64898 1.000 34.21780 ? 652 HOH   A O   1 
HETATM 1908 O  O   . HOH   C 3 .   ? 19.13375  -8.37697  -17.87862 1.000 35.18212 ? 653 HOH   A O   1 
HETATM 1909 O  O   . HOH   C 3 .   ? -6.867    -22.959   -1.745    1.000 38.17186 ? 654 HOH   A O   1 
HETATM 1910 O  O   . HOH   C 3 .   ? 0.63081   -28.40282 -35.98962 1.000 46.12875 ? 655 HOH   A O   1 
HETATM 1911 O  O   . HOH   C 3 .   ? -11.45431 -9.61684  -39.62137 1.000 46.53538 ? 656 HOH   A O   1 
HETATM 1912 O  O   . HOH   C 3 .   ? 3.68767   -0.27385  -16.38858 1.000 35.81649 ? 657 HOH   A O   1 
HETATM 1913 O  O   . HOH   C 3 .   ? 15.37656  -12.36726 -7.13834  1.000 39.28825 ? 658 HOH   A O   1 
HETATM 1914 O  O   . HOH   C 3 .   ? 10.98338  -1.38710  -17.33221 1.000 35.47931 ? 659 HOH   A O   1 
HETATM 1915 O  O   . HOH   C 3 .   ? -9.80916  -25.92430 -20.88569 1.000 28.22475 ? 660 HOH   A O   1 
HETATM 1916 O  O   . HOH   C 3 .   ? 2.386     -0.905    -25.917   1.000 31.79036 ? 661 HOH   A O   1 
HETATM 1917 O  O   . HOH   C 3 .   ? 3.66997   -8.97529  -39.05494 1.000 37.44271 ? 662 HOH   A O   1 
HETATM 1918 O  O   . HOH   C 3 .   ? -12.25043 -26.76097 -5.70820  1.000 51.61630 ? 663 HOH   A O   1 
HETATM 1919 O  O   . HOH   C 3 .   ? -3.40784  -27.31656 -3.17772  1.000 46.53549 ? 664 HOH   A O   1 
HETATM 1920 O  O   . HOH   C 3 .   ? -18.51353 -11.54465 -21.15243 1.000 27.02348 ? 665 HOH   A O   1 
HETATM 1921 O  O   . HOH   C 3 .   ? -6.279    6.896     -36.048   1.000 43.49486 ? 666 HOH   A O   1 
HETATM 1922 O  O   . HOH   C 3 .   ? 7.84029   -13.94861 -38.23862 1.000 31.14350 ? 667 HOH   A O   1 
HETATM 1923 O  O   . HOH   C 3 .   ? -16.48169 -18.16811 -3.20018  1.000 43.05149 ? 668 HOH   A O   1 
HETATM 1924 O  O   . HOH   C 3 .   ? 5.76968   -12.93801 -39.73085 1.000 25.97611 ? 669 HOH   A O   1 
HETATM 1925 O  O   . HOH   C 3 .   ? -6.12234  3.82380   -34.42255 1.000 36.45862 ? 670 HOH   A O   1 
HETATM 1926 O  O   . HOH   C 3 .   ? -2.30084  -0.96108  -30.91423 1.000 40.91674 ? 671 HOH   A O   1 
HETATM 1927 O  O   . HOH   C 3 .   ? -17.029   -0.542    -17.648   1.000 35.69531 ? 672 HOH   A O   1 
HETATM 1928 O  O   . HOH   C 3 .   ? -0.90493  -29.45611 -3.16960  1.000 51.14110 ? 673 HOH   A O   1 
HETATM 1929 O  O   . HOH   C 3 .   ? -19.42153 -2.34460  -37.87030 1.000 48.90759 ? 674 HOH   A O   1 
HETATM 1930 O  O   . HOH   C 3 .   ? -17.805   0.904     -21.875   1.000 45.88092 ? 675 HOH   A O   1 
HETATM 1931 O  O   . HOH   C 3 .   ? 10.24124  -21.24014 -43.23191 1.000 49.48132 ? 676 HOH   A O   1 
HETATM 1932 O  O   . HOH   C 3 .   ? 2.27772   -0.68208  -14.33259 1.000 46.13107 ? 677 HOH   A O   1 
HETATM 1933 O  O   . HOH   C 3 .   ? 8.141     -8.125    0.124     1.000 46.11586 ? 678 HOH   A O   1 
HETATM 1934 O  O   . HOH   C 3 .   ? -10.593   -22.601   4.613     1.000 44.12346 ? 679 HOH   A O   1 
HETATM 1935 O  O   . HOH   C 3 .   ? 5.37997   -3.18291  -23.65396 1.000 45.73562 ? 680 HOH   A O   1 
HETATM 1936 O  O   . HOH   C 3 .   ? 7.89733   -29.08464 -28.08192 1.000 35.67784 ? 681 HOH   A O   1 
HETATM 1937 O  O   . HOH   C 3 .   ? 17.43785  -17.28006 -5.13348  1.000 44.62782 ? 682 HOH   A O   1 
HETATM 1938 O  O   . HOH   C 3 .   ? 0.73373   -12.08270 -23.68927 1.000 37.47500 ? 683 HOH   A O   1 
HETATM 1939 O  O   . HOH   C 3 .   ? -4.21941  -28.00029 -23.35924 1.000 41.57461 ? 684 HOH   A O   1 
HETATM 1940 O  O   . HOH   C 3 .   ? 4.73805   -14.93003 -41.48270 1.000 38.22631 ? 685 HOH   A O   1 
HETATM 1941 O  O   . HOH   C 3 .   ? -10.42924 -16.79888 -38.05980 1.000 43.70612 ? 686 HOH   A O   1 
HETATM 1942 O  O   . HOH   C 3 .   ? -7.06263  -30.76712 -9.30905  1.000 35.30519 ? 687 HOH   A O   1 
HETATM 1943 O  O   . HOH   C 3 .   ? 22.88725  -15.55980 -19.27620 1.000 37.63814 ? 688 HOH   A O   1 
HETATM 1944 O  O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.25890 0.50  25.57882 ? 689 HOH   A O   1 
HETATM 1945 O  O   . HOH   C 3 .   ? -16.287   3.228     -26.332   1.000 30.64267 ? 690 HOH   A O   1 
HETATM 1946 O  O   . HOH   C 3 .   ? 11.33920  -30.11673 -34.40581 1.000 33.33167 ? 691 HOH   A O   1 
HETATM 1947 O  O   . HOH   C 3 .   ? -1.29353  -6.64845  -43.05763 1.000 52.70573 ? 692 HOH   A O   1 
HETATM 1948 O  O   . HOH   C 3 .   ? 1.64967   -5.92112  -36.63241 1.000 40.61789 ? 693 HOH   A O   1 
HETATM 1949 O  O   . HOH   C 3 .   ? -4.867    -25.075   -1.018    1.000 53.10464 ? 694 HOH   A O   1 
HETATM 1950 O  O   . HOH   C 3 .   ? 6.484     -6.556    0.368     1.000 47.66621 ? 695 HOH   A O   1 
HETATM 1951 O  O   . HOH   C 3 .   ? -16.36622 -12.73025 -6.29922  1.000 36.55910 ? 696 HOH   A O   1 
HETATM 1952 O  O   . HOH   C 3 .   ? 10.85840  -28.32400 -27.82216 1.000 37.18958 ? 697 HOH   A O   1 
HETATM 1953 O  O   . HOH   C 3 .   ? 1.79994   -22.85547 -0.97135  1.000 48.39328 ? 698 HOH   A O   1 
HETATM 1954 O  O   . HOH   C 3 .   ? -0.49471  -26.71082 -30.09419 1.000 36.72674 ? 699 HOH   A O   1 
HETATM 1955 O  O   . HOH   C 3 .   ? -4.17412  2.00799   -28.05403 1.000 33.00651 ? 700 HOH   A O   1 
HETATM 1956 O  O   . HOH   C 3 .   ? 3.10047   -2.08459  -20.33202 1.000 35.92767 ? 701 HOH   A O   1 
HETATM 1957 O  O   . HOH   C 3 .   ? 9.63718   -25.13847 -14.68349 1.000 38.57056 ? 702 HOH   A O   1 
HETATM 1958 O  O   . HOH   C 3 .   ? 21.905    -18.044   -25.278   1.000 44.41779 ? 703 HOH   A O   1 
HETATM 1959 O  O   . HOH   C 3 .   ? 0.53962   -1.29093  -16.73139 1.000 34.84317 ? 704 HOH   A O   1 
HETATM 1960 O  O   . HOH   C 3 .   ? -12.31594 -13.11321 -1.02664  1.000 27.89438 ? 705 HOH   A O   1 
HETATM 1961 O  O   . HOH   C 3 .   ? -6.49593  -26.86270 -23.42350 1.000 44.48571 ? 706 HOH   A O   1 
HETATM 1962 O  O   . HOH   C 3 .   ? 20.62095  -7.58410  -15.97607 1.000 45.58839 ? 707 HOH   A O   1 
HETATM 1963 O  O   . HOH   C 3 .   ? -14.82752 -9.69836  -11.26220 1.000 37.65004 ? 708 HOH   A O   1 
HETATM 1964 O  O   . HOH   C 3 .   ? 19.38271  -20.44289 -22.42939 1.000 34.80435 ? 709 HOH   A O   1 
HETATM 1965 O  O   . HOH   C 3 .   ? 14.63363  -13.10702 -2.91161  1.000 36.22301 ? 710 HOH   A O   1 
HETATM 1966 O  O   . HOH   C 3 .   ? -19.78012 -5.21062  -18.61983 1.000 48.51324 ? 711 HOH   A O   1 
HETATM 1967 O  O   . HOH   C 3 .   ? -14.52743 -14.02641 -10.23636 1.000 29.84831 ? 712 HOH   A O   1 
HETATM 1968 O  O   . HOH   C 3 .   ? -2.39298  -26.66412 -28.22455 1.000 38.16472 ? 713 HOH   A O   1 
HETATM 1969 O  O   . HOH   C 3 .   ? 14.99590  -17.26598 0.30978   1.000 45.17930 ? 714 HOH   A O   1 
HETATM 1970 O  O   . HOH   C 3 .   ? -22.025   -34.438   -13.934   1.000 58.09295 ? 715 HOH   A O   1 
HETATM 1971 O  O   . HOH   C 3 .   ? -16.09579 -13.53906 -3.82152  1.000 36.89207 ? 716 HOH   A O   1 
HETATM 1972 O  O   . HOH   C 3 .   ? -16.88431 -15.22687 -10.34288 1.000 37.53990 ? 717 HOH   A O   1 
HETATM 1973 O  O   . HOH   C 3 .   ? 9.75670   -12.77507 -37.02397 1.000 40.86717 ? 718 HOH   A O   1 
HETATM 1974 O  O   . HOH   C 3 .   ? 13.59530  -11.63399 -5.11607  1.000 29.34227 ? 719 HOH   A O   1 
HETATM 1975 O  O   . HOH   C 3 .   ? -10.394   -11.648   1.943     1.000 42.07590 ? 720 HOH   A O   1 
HETATM 1976 O  O   . HOH   C 3 .   ? -8.70174  -10.75534 0.02908   1.000 46.19405 ? 721 HOH   A O   1 
HETATM 1977 O  O   . HOH   C 3 .   ? -18.68548 -2.07985  -30.62303 1.000 51.73213 ? 722 HOH   A O   1 
HETATM 1978 O  O   . HOH   C 3 .   ? -19.62537 -5.86831  -21.47225 1.000 40.95723 ? 723 HOH   A O   1 
HETATM 1979 O  O   . HOH   C 3 .   ? 17.35201  -4.94054  -28.30558 1.000 53.49628 ? 724 HOH   A O   1 
HETATM 1980 O  O   . HOH   C 3 .   ? -9.08915  -32.58689 -8.77947  1.000 46.16187 ? 725 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   ? 0.42328 0.64310 0.36315 -0.08259 -0.02473 -0.20778 16  GLU A N   
2    C CA  . GLU A 9   ? 0.55538 0.74575 0.48342 -0.05578 -0.02790 -0.19144 16  GLU A CA  
3    C C   . GLU A 9   ? 0.50953 0.69243 0.45096 -0.04255 -0.03111 -0.17301 16  GLU A C   
4    O O   . GLU A 9   ? 0.49615 0.72381 0.45229 -0.03031 -0.03888 -0.16305 16  GLU A O   
5    C CB  . GLU A 9   ? 0.62495 0.85862 0.54678 -0.03238 -0.03685 -0.18677 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.73813 0.97185 0.65832 0.00222  -0.04164 -0.16335 16  GLU A CG  
7    C CD  . GLU A 9   ? 0.93718 1.11098 0.84170 0.01110  -0.03442 -0.15696 16  GLU A CD  
8    O OE1 . GLU A 9   ? 0.80842 0.98189 0.70620 0.03804  -0.03518 -0.14160 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 0.98364 1.10979 0.88218 -0.00660 -0.02521 -0.16617 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.35274 0.47857 0.28803 -0.04348 -0.02329 -0.16847 17  VAL A N   
11   C CA  . VAL A 10  ? 0.27987 0.39419 0.22751 -0.03565 -0.02488 -0.15464 17  VAL A CA  
12   C C   . VAL A 10  ? 0.33878 0.42803 0.27924 -0.01008 -0.02470 -0.14066 17  VAL A C   
13   O O   . VAL A 10  ? 0.34016 0.38757 0.26802 -0.00727 -0.01508 -0.14050 17  VAL A O   
14   C CB  . VAL A 10  ? 0.32990 0.40131 0.27997 -0.05728 -0.01302 -0.15948 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.32176 0.38393 0.28455 -0.04862 -0.01530 -0.14575 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.41538 0.51118 0.37322 -0.08267 -0.00980 -0.17268 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.23381 0.34250 0.18535 0.00972  -0.03132 -0.12093 18  GLU A N   
18   C CA  . GLU A 11  ? 0.23049 0.31324 0.18244 0.03128  -0.02743 -0.09983 18  GLU A CA  
19   C C   . GLU A 11  ? 0.27461 0.33206 0.24147 0.02920  -0.02433 -0.08624 18  GLU A C   
20   O O   . GLU A 11  ? 0.18894 0.26308 0.16696 0.02388  -0.02857 -0.08398 18  GLU A O   
21   C CB  . GLU A 11  ? 0.22736 0.34111 0.17603 0.05416  -0.03173 -0.08797 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.26001 0.40395 0.19075 0.06228  -0.03506 -0.09853 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.44632 0.61797 0.36933 0.09003  -0.03588 -0.08309 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.40604 0.61189 0.33733 0.09468  -0.04001 -0.07841 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.44604 0.60069 0.35697 0.10758  -0.02872 -0.07283 18  GLU A OE2 
26   N N   . THR A 12  ? 0.21774 0.23992 0.18414 0.03469  -0.01691 -0.07740 19  THR A N   
27   C CA  . THR A 12  ? 0.19156 0.19625 0.17018 0.03502  -0.01445 -0.06489 19  THR A CA  
28   C C   . THR A 12  ? 0.17875 0.18684 0.16422 0.05002  -0.01370 -0.04991 19  THR A C   
29   O O   . THR A 12  ? 0.18038 0.18288 0.15999 0.06015  -0.00927 -0.04719 19  THR A O   
30   C CB  . THR A 12  ? 0.23409 0.20234 0.20623 0.03134  -0.00483 -0.06587 19  THR A CB  
31   O OG1 . THR A 12  ? 0.26241 0.21938 0.22440 0.01342  -0.00043 -0.08258 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.22133 0.18081 0.20440 0.03425  -0.00353 -0.05261 19  THR A CG2 
33   N N   . PHE A 13  ? 0.19389 0.20994 0.19078 0.04941  -0.01604 -0.04172 20  PHE A N   
34   C CA  . PHE A 13  ? 0.17682 0.19533 0.17951 0.05746  -0.01254 -0.03116 20  PHE A CA  
35   C C   . PHE A 13  ? 0.22909 0.24289 0.24378 0.05271  -0.01194 -0.02543 20  PHE A C   
36   O O   . PHE A 13  ? 0.19184 0.20330 0.20972 0.04561  -0.01530 -0.02658 20  PHE A O   
37   C CB  . PHE A 13  ? 0.16043 0.19261 0.16094 0.06162  -0.01280 -0.02782 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.18852 0.23606 0.17566 0.07154  -0.01386 -0.03112 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.20572 0.27482 0.19035 0.06628  -0.02177 -0.04115 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.21975 0.26449 0.19618 0.08614  -0.00590 -0.02449 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.19398 0.28939 0.16620 0.07660  -0.02437 -0.04531 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.24264 0.30632 0.20363 0.09954  -0.00693 -0.02590 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.22618 0.31927 0.18536 0.09541  -0.01751 -0.03664 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.14425 0.16061 0.16523 0.05611  -0.00691 -0.01992 21  ALA A N   
45   C CA  . ALA A 14  ? 0.13738 0.16189 0.17020 0.05090  -0.00730 -0.01637 21  ALA A CA  
46   C C   . ALA A 14  ? 0.19068 0.21849 0.22554 0.04397  -0.00542 -0.01618 21  ALA A C   
47   O O   . ALA A 14  ? 0.17309 0.19546 0.20172 0.04653  0.00193  -0.01534 21  ALA A O   
48   C CB  . ALA A 14  ? 0.17141 0.20675 0.21216 0.05483  -0.00223 -0.01349 21  ALA A CB  
49   N N   . PHE A 15  ? 0.16445 0.19725 0.20438 0.03702  -0.00965 -0.01616 22  PHE A N   
50   C CA  . PHE A 15  ? 0.16874 0.20187 0.20906 0.02938  -0.00524 -0.01706 22  PHE A CA  
51   C C   . PHE A 15  ? 0.17765 0.21726 0.22365 0.02278  0.00372  -0.01945 22  PHE A C   
52   O O   . PHE A 15  ? 0.13587 0.19312 0.19169 0.02259  0.00195  -0.01996 22  PHE A O   
53   C CB  . PHE A 15  ? 0.14563 0.18534 0.18959 0.02298  -0.01128 -0.01741 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.13620 0.16950 0.17518 0.02470  -0.01613 -0.01646 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.14914 0.17784 0.18128 0.02699  -0.01281 -0.01618 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.15393 0.18686 0.19403 0.02478  -0.02154 -0.01540 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.13985 0.17308 0.17066 0.02745  -0.01735 -0.01648 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.15678 0.18607 0.19406 0.02203  -0.02370 -0.01670 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.13860 0.17286 0.17344 0.02237  -0.02289 -0.01808 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.16537 0.19095 0.20409 0.01742  0.01582  -0.02111 23  GLN A N   
61   C CA  . GLN A 16  ? 0.20433 0.23516 0.24856 0.00281  0.02721  -0.02764 23  GLN A CA  
62   C C   . GLN A 16  ? 0.16222 0.22154 0.21884 -0.00885 0.01837  -0.03370 23  GLN A C   
63   O O   . GLN A 16  ? 0.13697 0.19790 0.19152 -0.00721 0.00918  -0.03217 23  GLN A O   
64   C CB  . GLN A 16  ? 0.23434 0.23498 0.26309 -0.00282 0.04589  -0.02921 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.24275 0.21803 0.25664 0.01013  0.06016  -0.02228 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.46363 0.40192 0.45556 0.01135  0.08166  -0.01992 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.36518 0.29437 0.34561 0.02344  0.07933  -0.01396 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.42222 0.33811 0.40707 -0.00117 0.10531  -0.02464 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.16698 0.25394 0.23648 -0.01993 0.02154  -0.04062 24  ALA A N   
70   C CA  . ALA A 17  ? 0.19682 0.32424 0.27824 -0.02746 0.01165  -0.04612 24  ALA A CA  
71   C C   . ALA A 17  ? 0.16304 0.28362 0.23664 -0.04012 0.01236  -0.05296 24  ALA A C   
72   O O   . ALA A 17  ? 0.18470 0.32424 0.25951 -0.03600 0.00014  -0.05110 24  ALA A O   
73   C CB  . ALA A 17  ? 0.15936 0.32626 0.25679 -0.04089 0.01731  -0.05567 24  ALA A CB  
74   N N   . GLU A 18  ? 0.20036 0.28953 0.26242 -0.05355 0.02910  -0.05983 25  GLU A N   
75   C CA  . GLU A 18  ? 0.22478 0.30233 0.27602 -0.06573 0.03316  -0.06731 25  GLU A CA  
76   C C   . GLU A 18  ? 0.19741 0.25778 0.23948 -0.04882 0.02307  -0.05601 25  GLU A C   
77   O O   . GLU A 18  ? 0.20063 0.26854 0.23910 -0.05366 0.01791  -0.05943 25  GLU A O   
78   C CB  . GLU A 18  ? 0.28717 0.32367 0.32246 -0.08084 0.05897  -0.07550 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.32267 0.37423 0.36645 -0.10554 0.07382  -0.09099 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.48817 0.53743 0.53889 -0.09656 0.07938  -0.08373 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.30062 0.33879 0.34895 -0.07087 0.07000  -0.06758 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.44176 0.50160 0.49988 -0.11708 0.09437  -0.09575 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.18808 0.22941 0.22637 -0.03037 0.02060  -0.04395 26  ILE A N   
84   C CA  . ILE A 19  ? 0.18265 0.21432 0.21494 -0.01774 0.01221  -0.03556 26  ILE A CA  
85   C C   . ILE A 19  ? 0.16665 0.22337 0.20881 -0.01218 -0.00427 -0.03174 26  ILE A C   
86   O O   . ILE A 19  ? 0.14328 0.20070 0.18215 -0.01067 -0.00981 -0.02942 26  ILE A O   
87   C CB  . ILE A 19  ? 0.17499 0.18684 0.19972 -0.00203 0.01541  -0.02692 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.24322 0.22440 0.25024 0.00043  0.03442  -0.02573 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.14502 0.16190 0.17038 0.00791  0.00372  -0.02090 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.30157 0.26640 0.30320 -0.01301 0.05337  -0.03316 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.12350 0.19822 0.17540 -0.00724 -0.00957 -0.02983 27  ALA A N   
92   C CA  . ALA A 20  ? 0.16913 0.26306 0.22546 0.00139  -0.02026 -0.02436 27  ALA A CA  
93   C C   . ALA A 20  ? 0.17348 0.29323 0.23060 -0.00569 -0.02418 -0.02872 27  ALA A C   
94   O O   . ALA A 20  ? 0.17291 0.29591 0.22544 0.00187  -0.03015 -0.02265 27  ALA A O   
95   C CB  . ALA A 20  ? 0.14352 0.25301 0.20761 0.01037  -0.02167 -0.02111 27  ALA A CB  
96   N N   . GLN A 21  ? 0.14768 0.28591 0.20885 -0.02153 -0.01924 -0.04042 28  GLN A N   
97   C CA  . GLN A 21  ? 0.15090 0.32126 0.21191 -0.03086 -0.02346 -0.04828 28  GLN A CA  
98   C C   . GLN A 21  ? 0.16596 0.31147 0.21335 -0.03578 -0.02107 -0.04974 28  GLN A C   
99   O O   . GLN A 21  ? 0.15460 0.31876 0.19743 -0.03354 -0.02793 -0.04913 28  GLN A O   
100  C CB  . GLN A 21  ? 0.24055 0.43973 0.31003 -0.05207 -0.01671 -0.06486 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.46675 0.68512 0.52812 -0.06610 -0.01531 -0.07627 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.65525 0.88084 0.71710 -0.08897 -0.00154 -0.09290 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.56397 0.76204 0.62693 -0.09993 0.01183  -0.09805 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.45750 0.72014 0.51713 -0.09623 -0.00266 -0.10173 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.16711 0.27191 0.20613 -0.03886 -0.01061 -0.04979 29  LEU A N   
106  C CA  . LEU A 22  ? 0.20924 0.29066 0.23516 -0.03892 -0.00720 -0.04852 29  LEU A CA  
107  C C   . LEU A 22  ? 0.23330 0.31489 0.25929 -0.02352 -0.01738 -0.03591 29  LEU A C   
108  O O   . LEU A 22  ? 0.17772 0.26305 0.19678 -0.02360 -0.01986 -0.03524 29  LEU A O   
109  C CB  . LEU A 22  ? 0.17952 0.22151 0.19520 -0.03829 0.00735  -0.04753 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.24187 0.26228 0.24494 -0.03182 0.01128  -0.04247 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.26263 0.27790 0.25286 -0.04610 0.01949  -0.05362 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.27967 0.27122 0.27404 -0.02021 0.02279  -0.03536 29  LEU A CD2 
113  N N   . MET A 23  ? 0.15294 0.22807 0.18487 -0.01179 -0.02115 -0.02697 30  MET A N   
114  C CA  . MET A 23  ? 0.16846 0.23825 0.19870 -0.00201 -0.02619 -0.01766 30  MET A CA  
115  C C   . MET A 23  ? 0.17984 0.27039 0.20904 0.00462  -0.03224 -0.01295 30  MET A C   
116  O O   . MET A 23  ? 0.17939 0.26469 0.20172 0.00944  -0.03272 -0.00678 30  MET A O   
117  C CB  . MET A 23  ? 0.15774 0.21341 0.19168 0.00497  -0.02623 -0.01287 30  MET A CB  
118  C CG  . MET A 23  ? 0.22908 0.27260 0.26246 0.00410  -0.02087 -0.01564 30  MET A CG  
119  S SD  . MET A 23  ? 0.19683 0.23548 0.23398 0.01107  -0.02241 -0.01408 30  MET A SD  
120  C CE  . MET A 23  ? 0.17287 0.20736 0.20970 0.01090  -0.02525 -0.01171 30  MET A CE  
121  N N   . SER A 24  ? 0.13897 0.25586 0.17377 0.00690  -0.03555 -0.01471 31  SER A N   
122  C CA  . SER A 24  ? 0.11626 0.26073 0.14727 0.01861  -0.04072 -0.00828 31  SER A CA  
123  C C   . SER A 24  ? 0.21006 0.37340 0.23355 0.01151  -0.04312 -0.01409 31  SER A C   
124  O O   . SER A 24  ? 0.21567 0.38681 0.22909 0.02354  -0.04527 -0.00536 31  SER A O   
125  C CB  . SER A 24  ? 0.14709 0.32711 0.18721 0.02460  -0.04393 -0.00904 31  SER A CB  
126  O OG  . SER A 24  ? 0.54142 0.75946 0.58586 0.01100  -0.04624 -0.02188 31  SER A OG  
127  N N   . LEU A 25  ? 0.17252 0.33886 0.19732 -0.00769 -0.04020 -0.02888 32  LEU A N   
128  C CA  . LEU A 25  ? 0.16871 0.34746 0.18313 -0.01730 -0.04038 -0.03743 32  LEU A CA  
129  C C   . LEU A 25  ? 0.21018 0.35721 0.21331 -0.01150 -0.03723 -0.02898 32  LEU A C   
130  O O   . LEU A 25  ? 0.20638 0.36606 0.19875 -0.00661 -0.03995 -0.02630 32  LEU A O   
131  C CB  . LEU A 25  ? 0.22810 0.40340 0.24219 -0.04128 -0.03210 -0.05641 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.35179 0.53887 0.35253 -0.05607 -0.02975 -0.07044 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.46425 0.66898 0.46894 -0.07467 -0.02142 -0.08614 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.46467 0.60228 0.45142 -0.05977 -0.01800 -0.07025 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.17091 0.28167 0.17618 -0.01151 -0.03114 -0.02501 33  ILE A N   
136  C CA  . ILE A 26  ? 0.21041 0.29843 0.20863 -0.00709 -0.02750 -0.01777 33  ILE A CA  
137  C C   . ILE A 26  ? 0.24253 0.33212 0.23817 0.00665  -0.03039 -0.00456 33  ILE A C   
138  O O   . ILE A 26  ? 0.25094 0.33603 0.23697 0.01012  -0.02807 0.00059  33  ILE A O   
139  C CB  . ILE A 26  ? 0.15472 0.21687 0.15789 -0.00792 -0.02142 -0.01655 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.21702 0.26681 0.21367 -0.01721 -0.01235 -0.02625 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.22453 0.27466 0.22615 -0.00271 -0.01892 -0.00846 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.23239 0.26384 0.23203 -0.01298 -0.00594 -0.02382 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.18193 0.27396 0.18320 0.01550  -0.03256 0.00162  34  ILE A N   
144  C CA  . ILE A 27  ? 0.24312 0.32378 0.23725 0.02934  -0.02924 0.01500  34  ILE A CA  
145  C C   . ILE A 27  ? 0.30765 0.41330 0.28895 0.04273  -0.03181 0.02185  34  ILE A C   
146  O O   . ILE A 27  ? 0.28208 0.37468 0.25007 0.05312  -0.02570 0.03302  34  ILE A O   
147  C CB  . ILE A 27  ? 0.26369 0.33230 0.26350 0.03553  -0.02724 0.01889  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.20424 0.24958 0.21263 0.02442  -0.02394 0.01344  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.31696 0.37122 0.30341 0.05286  -0.01970 0.03315  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.25447 0.29294 0.26876 0.02673  -0.02363 0.01213  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.22759 0.37293 0.21183 0.04265  -0.03980 0.01489  35  ASN A N   
152  C CA  . ASN A 28  ? 0.23672 0.41949 0.20963 0.06023  -0.04397 0.02222  35  ASN A CA  
153  C C   . ASN A 28  ? 0.32029 0.53178 0.28360 0.05338  -0.04877 0.01352  35  ASN A C   
154  O O   . ASN A 28  ? 0.31347 0.54254 0.26537 0.06828  -0.04709 0.02096  35  ASN A O   
155  C CB  . ASN A 28  ? 0.25612 0.47277 0.23964 0.06461  -0.04779 0.01888  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.33573 0.52937 0.32321 0.07728  -0.04333 0.02956  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.40555 0.56251 0.38130 0.09096  -0.03466 0.04377  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.36435 0.57189 0.36656 0.07011  -0.04531 0.02138  35  ASN A ND2 
159  N N   . THR A 29  ? 0.22254 0.42715 0.19024 0.03001  -0.04861 -0.00310 36  THR A N   
160  C CA  . THR A 29  ? 0.24436 0.47209 0.20017 0.02084  -0.05091 -0.01445 36  THR A CA  
161  C C   . THR A 29  ? 0.30768 0.51297 0.24626 0.03169  -0.04582 -0.00244 36  THR A C   
162  O O   . THR A 29  ? 0.29910 0.46088 0.23970 0.03023  -0.03767 0.00435  36  THR A O   
163  C CB  . THR A 29  ? 0.31637 0.53086 0.27635 -0.00629 -0.04664 -0.03494 36  THR A CB  
164  O OG1 . THR A 29  ? 0.25955 0.48865 0.23550 -0.01735 -0.04684 -0.04517 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.29729 0.52590 0.24322 -0.01800 -0.04479 -0.04848 36  THR A CG2 
166  N N   . PHE A 30  ? 0.22232 0.45583 0.14719 0.04174  -0.04796 -0.00021 37  PHE A N   
167  C CA  . PHE A 30  ? 0.27788 0.49470 0.18223 0.05089  -0.04291 0.00962  37  PHE A CA  
168  C C   . PHE A 30  ? 0.27435 0.47074 0.17558 0.02919  -0.03859 -0.00554 37  PHE A C   
169  O O   . PHE A 30  ? 0.26194 0.48136 0.15946 0.01275  -0.04186 -0.02511 37  PHE A O   
170  C CB  . PHE A 30  ? 0.26542 0.51211 0.16022 0.06620  -0.04313 0.01422  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.32351 0.55071 0.19685 0.07656  -0.03608 0.02518  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.39349 0.58482 0.25685 0.09466  -0.02525 0.04734  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.33067 0.57047 0.19308 0.06635  -0.03732 0.01268  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.35757 0.52806 0.20241 0.10253  -0.01544 0.05754  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.34763 0.56846 0.19015 0.07629  -0.02957 0.02315  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.31661 0.50376 0.15143 0.09447  -0.01850 0.04600  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.22704 0.37900 0.13006 0.02862  -0.02860 0.00279  38  TYR A N   
178  C CA  . TYR A 31  ? 0.22662 0.35479 0.12800 0.01273  -0.02149 -0.00840 38  TYR A CA  
179  C C   . TYR A 31  ? 0.22811 0.32422 0.12874 0.01987  -0.01137 0.00581  38  TYR A C   
180  O O   . TYR A 31  ? 0.22293 0.29934 0.13916 0.02014  -0.00785 0.01284  38  TYR A O   
181  C CB  . TYR A 31  ? 0.23815 0.35400 0.15507 -0.00233 -0.02031 -0.02011 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.32249 0.40785 0.23443 -0.01208 -0.00901 -0.02715 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.35154 0.43650 0.24532 -0.02376 -0.00349 -0.04265 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.27100 0.32996 0.19417 -0.00836 -0.00240 -0.01859 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.46912 0.52027 0.35369 -0.02847 0.01072  -0.04697 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.26937 0.30472 0.18593 -0.01113 0.00932  -0.02204 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.38268 0.41029 0.27877 -0.01963 0.01703  -0.03495 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.54376 0.54205 0.42895 -0.01846 0.03237  -0.03640 38  TYR A OH  
189  N N   . SER A 32  ? 0.24646 0.34146 0.12905 0.02411  -0.00632 0.00834  39  SER A N   
190  C CA  . SER A 32  ? 0.25219 0.32413 0.13346 0.03157  0.00440  0.02294  39  SER A CA  
191  C C   . SER A 32  ? 0.31071 0.36101 0.20421 0.02254  0.01272  0.01998  39  SER A C   
192  O O   . SER A 32  ? 0.32059 0.35831 0.22299 0.02475  0.02071  0.03024  39  SER A O   
193  C CB  . SER A 32  ? 0.27795 0.35743 0.13425 0.04097  0.00823  0.02762  39  SER A CB  
194  O OG  . SER A 32  ? 0.29213 0.39635 0.13505 0.05592  0.00180  0.03482  39  SER A OG  
195  N N   . ASN A 33  ? 0.23855 0.28549 0.13145 0.01302  0.01312  0.00630  40  ASN A N   
196  C CA  . ASN A 33  ? 0.27520 0.30446 0.17312 0.01119  0.02340  0.00578  40  ASN A CA  
197  C C   . ASN A 33  ? 0.24005 0.26664 0.16130 0.00987  0.02186  0.00839  40  ASN A C   
198  O O   . ASN A 33  ? 0.23413 0.25277 0.15828 0.00747  0.02476  0.00212  40  ASN A O   
199  C CB  . ASN A 33  ? 0.33180 0.35013 0.21168 0.00457  0.02969  -0.00860 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.45324 0.45131 0.33202 0.00929  0.04376  -0.00632 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.37133 0.37205 0.25690 0.01785  0.04909  0.00508  40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.38139 0.35983 0.25010 0.00459  0.05213  -0.01689 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.22937 0.26243 0.16255 0.01444  -0.02701 -0.00186 41  LYS A N   
204  C CA  . LYS A 34  ? 0.20057 0.25198 0.16061 0.01854  -0.01551 -0.00003 41  LYS A CA  
205  C C   . LYS A 34  ? 0.20608 0.23900 0.16428 0.01731  -0.00569 -0.01040 41  LYS A C   
206  O O   . LYS A 34  ? 0.17493 0.21759 0.15001 0.01716  -0.00146 -0.01026 41  LYS A O   
207  C CB  . LYS A 34  ? 0.21890 0.27633 0.18277 0.03388  -0.00507 0.00489  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.21105 0.29564 0.18352 0.04069  -0.01150 0.01883  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.25840 0.33526 0.22344 0.05948  -0.00122 0.02154  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.21419 0.32260 0.18965 0.07278  -0.00419 0.03797  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.20432 0.34648 0.20185 0.08245  0.00073  0.04952  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.21229 0.22075 0.14937 0.01907  -0.00118 -0.01700 42  GLU A N   
213  C CA  . GLU A 35  ? 0.23203 0.23080 0.17343 0.02070  0.01003  -0.02157 42  GLU A CA  
214  C C   . GLU A 35  ? 0.27256 0.27090 0.22126 0.01250  0.00485  -0.02636 42  GLU A C   
215  O O   . GLU A 35  ? 0.23867 0.23549 0.19816 0.01328  0.01258  -0.02836 42  GLU A O   
216  C CB  . GLU A 35  ? 0.23650 0.21643 0.15395 0.02936  0.01878  -0.02228 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.27493 0.22925 0.15679 0.03037  0.00932  -0.02956 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.47556 0.40802 0.32199 0.04803  0.02140  -0.02877 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.40695 0.34628 0.25063 0.05588  0.03016  -0.02076 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.50748 0.41453 0.32571 0.05685  0.02328  -0.03461 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.22464 0.22455 0.16935 0.00272  -0.01043 -0.02556 43  ILE A N   
222  C CA  . ILE A 36  ? 0.20780 0.20410 0.15792 -0.00711 -0.01734 -0.02764 43  ILE A CA  
223  C C   . ILE A 36  ? 0.19690 0.21757 0.17661 -0.00725 -0.01010 -0.02338 43  ILE A C   
224  O O   . ILE A 36  ? 0.16725 0.18494 0.15246 -0.01321 -0.01196 -0.02486 43  ILE A O   
225  C CB  . ILE A 36  ? 0.24656 0.23847 0.18827 -0.02254 -0.04084 -0.02241 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.26031 0.29251 0.22986 -0.02729 -0.04728 -0.00649 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.32652 0.27666 0.22231 -0.02022 -0.05172 -0.03028 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.30936 0.37693 0.31389 -0.03502 -0.04845 0.00739  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.15662 0.19530 0.14863 0.00167  -0.00250 -0.01826 44  PHE A N   
230  C CA  . PHE A 37  ? 0.15872 0.20870 0.16426 0.00736  0.00433  -0.01590 44  PHE A CA  
231  C C   . PHE A 37  ? 0.18216 0.21319 0.18588 0.00633  0.00902  -0.02438 44  PHE A C   
232  O O   . PHE A 37  ? 0.13191 0.16641 0.14220 0.00547  0.00963  -0.02406 44  PHE A O   
233  C CB  . PHE A 37  ? 0.15100 0.20472 0.15374 0.02240  0.01075  -0.01221 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.17994 0.20714 0.17190 0.02606  0.01456  -0.01884 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.17359 0.19286 0.15871 0.02524  0.01507  -0.01849 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.23582 0.24572 0.22459 0.02860  0.01533  -0.02248 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.20510 0.20631 0.18753 0.02549  0.01772  -0.01796 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.19703 0.18459 0.18178 0.02618  0.01341  -0.02314 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.16666 0.15323 0.15182 0.02390  0.01530  -0.01904 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.15731 0.17218 0.15401 0.00739  0.01281  -0.02865 45  LEU A N   
241  C CA  . LEU A 38  ? 0.13959 0.14495 0.14218 0.00667  0.01663  -0.03090 45  LEU A CA  
242  C C   . LEU A 38  ? 0.19677 0.19721 0.19750 0.00224  0.01501  -0.03461 45  LEU A C   
243  O O   . LEU A 38  ? 0.19073 0.19021 0.19988 0.00043  0.01495  -0.03542 45  LEU A O   
244  C CB  . LEU A 38  ? 0.14587 0.14598 0.14913 0.00979  0.02264  -0.02648 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.15251 0.15224 0.17146 0.00752  0.02491  -0.02120 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.15478 0.14673 0.17911 0.00299  0.01571  -0.02172 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.21709 0.22232 0.24391 0.00990  0.03182  -0.00875 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.17105 0.16168 0.15498 0.00099  0.01112  -0.03705 46  ARG A N   
249  C CA  . ARG A 39  ? 0.21220 0.18663 0.18483 -0.00309 0.00521  -0.04106 46  ARG A CA  
250  C C   . ARG A 39  ? 0.23679 0.22365 0.22480 -0.01342 -0.00202 -0.03766 46  ARG A C   
251  O O   . ARG A 39  ? 0.18911 0.16848 0.17901 -0.01531 -0.00240 -0.03924 46  ARG A O   
252  C CB  . ARG A 39  ? 0.24723 0.19735 0.18845 -0.00430 -0.00521 -0.04441 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.32268 0.24201 0.24161 -0.00960 -0.01728 -0.04891 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.38195 0.26665 0.26190 -0.01457 -0.03636 -0.05200 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.39884 0.30567 0.29796 -0.03416 -0.05385 -0.04205 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.47946 0.36938 0.35604 -0.04248 -0.07363 -0.04000 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.45368 0.29499 0.27752 -0.03135 -0.07914 -0.05052 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.41990 0.34287 0.32565 -0.06039 -0.08847 -0.02485 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.16627 0.17543 0.16605 -0.01776 -0.00619 -0.03000 47  GLU A N   
260  C CA  . GLU A 40  ? 0.15578 0.18472 0.17186 -0.02471 -0.01013 -0.02051 47  GLU A CA  
261  C C   . GLU A 40  ? 0.15953 0.19303 0.18277 -0.01598 -0.00003 -0.02190 47  GLU A C   
262  O O   . GLU A 40  ? 0.13557 0.17193 0.16418 -0.02012 -0.00140 -0.01818 47  GLU A O   
263  C CB  . GLU A 40  ? 0.14999 0.21051 0.18023 -0.02618 -0.01358 -0.00623 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.16059 0.21707 0.18496 -0.03977 -0.03087 -0.00122 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.28331 0.31238 0.29505 -0.05702 -0.04847 -0.00230 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.24132 0.27873 0.26676 -0.06427 -0.04985 0.00509  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.40169 0.39531 0.38385 -0.06174 -0.06187 -0.01029 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.12505 0.15446 0.14482 -0.00494 0.00722  -0.02624 48  LEU A N   
269  C CA  . LEU A 41  ? 0.14730 0.17010 0.16471 0.00237  0.01058  -0.02810 48  LEU A CA  
270  C C   . LEU A 41  ? 0.16934 0.17672 0.18871 -0.00262 0.00871  -0.03354 48  LEU A C   
271  O O   . LEU A 41  ? 0.17558 0.17924 0.19416 -0.00167 0.00747  -0.03334 48  LEU A O   
272  C CB  . LEU A 41  ? 0.13269 0.14446 0.13967 0.01275  0.01212  -0.03011 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.16300 0.18852 0.16374 0.02503  0.01617  -0.02344 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.16413 0.16539 0.14607 0.03588  0.01489  -0.02701 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.14550 0.18791 0.14445 0.03530  0.02144  -0.01464 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.13055 0.13030 0.15094 -0.00480 0.00973  -0.03634 49  ILE A N   
277  C CA  . ILE A 42  ? 0.15936 0.15097 0.18422 -0.00516 0.01052  -0.03727 49  ILE A CA  
278  C C   . ILE A 42  ? 0.16693 0.15266 0.18675 -0.00942 0.00709  -0.03854 49  ILE A C   
279  O O   . ILE A 42  ? 0.18554 0.16690 0.20932 -0.00921 0.00614  -0.03816 49  ILE A O   
280  C CB  . ILE A 42  ? 0.16583 0.15511 0.19027 0.00020  0.01698  -0.03546 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.14684 0.14321 0.18316 0.00056  0.01811  -0.02898 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.13944 0.12402 0.16613 0.00579  0.02100  -0.03333 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.19954 0.20189 0.23842 0.00735  0.02763  -0.02142 49  ILE A CD1 
284  N N   . SER A 43  ? 0.15689 0.14064 0.16796 -0.01532 0.00204  -0.03805 50  SER A N   
285  C CA  . SER A 43  ? 0.20199 0.17500 0.20739 -0.02374 -0.00613 -0.03623 50  SER A CA  
286  C C   . SER A 43  ? 0.20500 0.19570 0.22389 -0.02718 -0.00603 -0.02862 50  SER A C   
287  O O   . SER A 43  ? 0.15913 0.14093 0.17700 -0.03042 -0.00896 -0.02709 50  SER A O   
288  C CB  . SER A 43  ? 0.21886 0.18249 0.21189 -0.03416 -0.01839 -0.03376 50  SER A CB  
289  O OG  . SER A 43  ? 0.35430 0.31069 0.34703 -0.04821 -0.03119 -0.02647 50  SER A OG  
290  N N   . ASN A 44  ? 0.16312 0.17662 0.19006 -0.02286 -0.00141 -0.02282 51  ASN A N   
291  C CA  . ASN A 44  ? 0.18848 0.21610 0.21908 -0.01778 0.00279  -0.01496 51  ASN A CA  
292  C C   . ASN A 44  ? 0.17342 0.18337 0.19651 -0.01140 0.00378  -0.02257 51  ASN A C   
293  O O   . ASN A 44  ? 0.13644 0.14578 0.15775 -0.01129 0.00337  -0.01828 51  ASN A O   
294  C CB  . ASN A 44  ? 0.15751 0.20479 0.18714 -0.00524 0.01014  -0.00863 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.27197 0.35015 0.31729 -0.01115 0.00894  0.00736  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.19402 0.27552 0.25002 -0.02885 -0.00151 0.01445  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.18151 0.27995 0.22667 0.00370  0.01717  0.01498  51  ASN A ND2 
298  N N   . SER A 45  ? 0.13271 0.13011 0.15320 -0.00734 0.00338  -0.03071 52  SER A N   
299  C CA  . SER A 45  ? 0.16510 0.14850 0.18404 -0.00532 -0.00084 -0.03377 52  SER A CA  
300  C C   . SER A 45  ? 0.16520 0.14389 0.19076 -0.00991 -0.00240 -0.03333 52  SER A C   
301  O O   . SER A 45  ? 0.17290 0.14576 0.19636 -0.00903 -0.00617 -0.03185 52  SER A O   
302  C CB  . SER A 45  ? 0.13890 0.11600 0.16264 -0.00506 -0.00374 -0.03567 52  SER A CB  
303  O OG  . SER A 45  ? 0.19159 0.16090 0.20114 0.00064  -0.00598 -0.03682 52  SER A OG  
304  N N   . SER A 46  ? 0.14401 0.11952 0.17106 -0.01221 -0.00032 -0.03481 53  SER A N   
305  C CA  . SER A 46  ? 0.18490 0.14684 0.20865 -0.01160 -0.00161 -0.03496 53  SER A CA  
306  C C   . SER A 46  ? 0.21448 0.17227 0.23324 -0.01854 -0.00670 -0.03092 53  SER A C   
307  O O   . SER A 46  ? 0.18555 0.13425 0.20328 -0.01678 -0.00883 -0.02947 53  SER A O   
308  C CB  . SER A 46  ? 0.17472 0.12147 0.18509 -0.00821 0.00024  -0.03857 53  SER A CB  
309  O OG  . SER A 46  ? 0.25629 0.17993 0.25293 -0.00252 -0.00117 -0.03951 53  SER A OG  
310  N N   . ASP A 47  ? 0.18784 0.15624 0.20669 -0.02651 -0.00873 -0.02532 54  ASP A N   
311  C CA  . ASP A 47  ? 0.16189 0.13514 0.18247 -0.03457 -0.01269 -0.01442 54  ASP A CA  
312  C C   . ASP A 47  ? 0.18365 0.16489 0.20384 -0.02610 -0.00789 -0.01136 54  ASP A C   
313  O O   . ASP A 47  ? 0.18195 0.15709 0.19974 -0.02864 -0.01050 -0.00559 54  ASP A O   
314  C CB  . ASP A 47  ? 0.16637 0.16290 0.19655 -0.04398 -0.01472 -0.00149 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.29697 0.27673 0.32146 -0.05751 -0.02751 -0.00194 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.32382 0.26709 0.32892 -0.05679 -0.03359 -0.01271 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.24663 0.24768 0.28259 -0.06696 -0.03245 0.00984  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.15138 0.13961 0.16767 -0.01540 -0.00304 -0.01513 55  ALA A N   
319  C CA  . ALA A 48  ? 0.17824 0.16184 0.18083 -0.00498 -0.00233 -0.01405 55  ALA A CA  
320  C C   . ALA A 48  ? 0.18171 0.14663 0.18361 -0.00559 -0.01021 -0.01987 55  ALA A C   
321  O O   . ALA A 48  ? 0.17947 0.13678 0.17032 -0.00162 -0.01322 -0.01675 55  ALA A O   
322  C CB  . ALA A 48  ? 0.16888 0.14983 0.15611 0.00758  -0.00003 -0.01808 55  ALA A CB  
323  N N   . LEU A 49  ? 0.15803 0.11873 0.17227 -0.00860 -0.01287 -0.02539 56  LEU A N   
324  C CA  . LEU A 49  ? 0.16031 0.11350 0.18220 -0.00773 -0.01896 -0.02493 56  LEU A CA  
325  C C   . LEU A 49  ? 0.16825 0.11414 0.18902 -0.00891 -0.01830 -0.02170 56  LEU A C   
326  O O   . LEU A 49  ? 0.18449 0.12448 0.20501 -0.00636 -0.02355 -0.01846 56  LEU A O   
327  C CB  . LEU A 49  ? 0.17330 0.13297 0.21242 -0.00692 -0.01784 -0.02512 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.15023 0.11148 0.19188 -0.00889 -0.02422 -0.02507 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.18711 0.16053 0.24509 -0.00885 -0.01799 -0.02264 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.16293 0.11729 0.20847 -0.01183 -0.04004 -0.01948 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.17212 0.11342 0.18913 -0.01370 -0.01518 -0.02174 57  ASP A N   
332  C CA  . ASP A 50  ? 0.20884 0.13253 0.21754 -0.01707 -0.01892 -0.01793 57  ASP A CA  
333  C C   . ASP A 50  ? 0.23692 0.16513 0.24213 -0.02025 -0.02098 -0.00918 57  ASP A C   
334  O O   . ASP A 50  ? 0.21072 0.12509 0.21089 -0.01917 -0.02495 -0.00556 57  ASP A O   
335  C CB  . ASP A 50  ? 0.20503 0.11560 0.20460 -0.02665 -0.02253 -0.01759 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.31516 0.20841 0.30457 -0.01865 -0.02078 -0.02651 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.27996 0.17823 0.27564 -0.00469 -0.01373 -0.02926 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.30391 0.17894 0.27821 -0.02600 -0.02742 -0.02809 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.20836 0.15561 0.21314 -0.02069 -0.01670 -0.00406 58  LYS A N   
340  C CA  . LYS A 51  ? 0.20061 0.15537 0.19799 -0.01923 -0.01458 0.00809  58  LYS A CA  
341  C C   . LYS A 51  ? 0.21873 0.16125 0.20317 -0.00888 -0.01841 0.00446  58  LYS A C   
342  O O   . LYS A 51  ? 0.23553 0.17127 0.21313 -0.00877 -0.02052 0.01219  58  LYS A O   
343  C CB  . LYS A 51  ? 0.19865 0.17892 0.19471 -0.01415 -0.00518 0.01693  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.25029 0.25085 0.26445 -0.02805 -0.00448 0.03016  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.21972 0.25292 0.23706 -0.01806 0.00718  0.04100  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.34151 0.39754 0.38275 -0.03416 0.00354  0.05364  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.39448 0.49095 0.44380 -0.02144 0.01692  0.07009  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.21925 0.15665 0.19947 -0.00203 -0.02246 -0.00535 59  ILE A N   
349  C CA  . ILE A 52  ? 0.22426 0.14639 0.19079 0.00426  -0.03281 -0.00689 59  ILE A CA  
350  C C   . ILE A 52  ? 0.22364 0.14076 0.20670 0.00074  -0.03963 -0.00568 59  ILE A C   
351  O O   . ILE A 52  ? 0.23791 0.14530 0.21214 0.00392  -0.04745 -0.00162 59  ILE A O   
352  C CB  . ILE A 52  ? 0.23221 0.14378 0.18729 0.00849  -0.04197 -0.01452 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.29099 0.17860 0.22216 0.01318  -0.05892 -0.01449 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.21083 0.13088 0.19442 0.00074  -0.04538 -0.01798 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.33067 0.20656 0.22445 0.02621  -0.05394 -0.01009 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.21494 0.13708 0.21783 -0.00222 -0.03591 -0.00792 60  ARG A N   
357  C CA  . ARG A 53  ? 0.29230 0.20898 0.30568 0.00174  -0.03832 -0.00444 60  ARG A CA  
358  C C   . ARG A 53  ? 0.29189 0.19285 0.29182 0.00069  -0.03822 0.00074  60  ARG A C   
359  O O   . ARG A 53  ? 0.25231 0.14585 0.25131 0.00594  -0.04382 0.00579  60  ARG A O   
360  C CB  . ARG A 53  ? 0.26577 0.18518 0.29137 0.00595  -0.03100 -0.00709 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.39542 0.30534 0.42340 0.01782  -0.02995 -0.00186 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.54087 0.45010 0.57198 0.03117  -0.01985 -0.00235 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.53461 0.47627 0.59554 0.03654  -0.01705 0.00583  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.58305 0.53542 0.65008 0.04253  -0.00706 0.00584  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.43071 0.36021 0.47176 0.04417  -0.00061 -0.00500 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.37173 0.35854 0.47195 0.04585  -0.00545 0.01971  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.24112 0.13780 0.23284 -0.00770 -0.03394 0.00260  61  TYR A N   
368  C CA  . TYR A 54  ? 0.25711 0.13778 0.23821 -0.01317 -0.03694 0.01187  61  TYR A CA  
369  C C   . TYR A 54  ? 0.29666 0.18251 0.26884 -0.00979 -0.03838 0.02022  61  TYR A C   
370  O O   . TYR A 54  ? 0.28442 0.15511 0.24960 -0.00796 -0.04318 0.02641  61  TYR A O   
371  C CB  . TYR A 54  ? 0.26228 0.14335 0.24259 -0.02800 -0.03658 0.01870  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.29261 0.15421 0.26442 -0.03842 -0.04393 0.03242  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.32142 0.14234 0.27833 -0.03827 -0.05326 0.02900  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.32059 0.20219 0.29587 -0.04579 -0.04112 0.05100  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.35973 0.15484 0.30522 -0.04946 -0.06352 0.04225  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.32337 0.18882 0.29425 -0.05807 -0.04914 0.06789  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.40546 0.22494 0.36137 -0.06198 -0.06228 0.06269  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.42176 0.21736 0.36973 -0.07606 -0.07372 0.08018  61  TYR A OH  
379  N N   . GLU A 55  ? 0.25924 0.16121 0.22492 -0.00582 -0.03443 0.02040  62  GLU A N   
380  C CA  . GLU A 55  ? 0.29255 0.19217 0.23734 0.00253  -0.03552 0.02744  62  GLU A CA  
381  C C   . GLU A 55  ? 0.32757 0.21214 0.26825 0.00876  -0.04845 0.02278  62  GLU A C   
382  O O   . GLU A 55  ? 0.38571 0.25999 0.31189 0.01284  -0.05280 0.03033  62  GLU A O   
383  C CB  . GLU A 55  ? 0.29532 0.20451 0.22186 0.01235  -0.02916 0.02618  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.36871 0.30251 0.29920 0.01078  -0.01425 0.04052  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.50443 0.44474 0.40568 0.03070  -0.00422 0.04386  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.50494 0.42007 0.37720 0.04312  -0.01293 0.03037  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.55856 0.52740 0.46377 0.03500  0.01106  0.06210  62  GLU A OE2 
388  N N   . SER A 56  ? 0.29584 0.18267 0.25252 0.00886  -0.05539 0.01398  63  SER A N   
389  C CA  . SER A 56  ? 0.33443 0.21639 0.29706 0.01239  -0.07026 0.01547  63  SER A CA  
390  C C   . SER A 56  ? 0.35003 0.22794 0.32458 0.01547  -0.07023 0.02240  63  SER A C   
391  O O   . SER A 56  ? 0.30038 0.17688 0.27886 0.01998  -0.08226 0.02841  63  SER A O   
392  C CB  . SER A 56  ? 0.31753 0.21171 0.30313 0.00959  -0.07720 0.01165  63  SER A CB  
393  O OG  . SER A 56  ? 0.33365 0.24076 0.34530 0.01055  -0.06650 0.01191  63  SER A OG  
394  N N   . LEU A 57  ? 0.29616 0.16761 0.27291 0.01363  -0.05969 0.02250  64  LEU A N   
395  C CA  . LEU A 57  ? 0.39359 0.24937 0.37144 0.02052  -0.06057 0.02773  64  LEU A CA  
396  C C   . LEU A 57  ? 0.44241 0.28498 0.40378 0.02180  -0.06717 0.03702  64  LEU A C   
397  O O   . LEU A 57  ? 0.44315 0.27667 0.40681 0.03138  -0.07218 0.04278  64  LEU A O   
398  C CB  . LEU A 57  ? 0.36069 0.19627 0.33025 0.01683  -0.05376 0.02479  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.36890 0.21036 0.34817 0.02026  -0.04698 0.01591  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.40910 0.21681 0.36767 0.01646  -0.04644 0.01252  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.41912 0.27477 0.41689 0.03787  -0.04490 0.01836  64  LEU A CD2 
402  N N   . THR A 58  ? 0.38964 0.23262 0.33330 0.01538  -0.06555 0.04094  65  THR A N   
403  C CA  . THR A 58  ? 0.45172 0.28353 0.37587 0.01816  -0.06997 0.05184  65  THR A CA  
404  C C   . THR A 58  ? 0.51051 0.34559 0.41568 0.02492  -0.07786 0.05115  65  THR A C   
405  O O   . THR A 58  ? 0.56854 0.39183 0.45419 0.03061  -0.08452 0.05924  65  THR A O   
406  C CB  . THR A 58  ? 0.59614 0.42447 0.50987 0.00840  -0.06133 0.06395  65  THR A CB  
407  O OG1 . THR A 58  ? 0.56127 0.41098 0.47393 0.00521  -0.05156 0.06393  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.54767 0.35648 0.46943 -0.00103 -0.06217 0.06531  65  THR A CG2 
409  N N   . ASP A 59  ? 0.47663 0.35516 0.35088 0.05644  -0.03731 0.08506  66  ASP A N   
410  C CA  . ASP A 59  ? 0.46416 0.37705 0.34723 0.05923  -0.04385 0.08332  66  ASP A CA  
411  C C   . ASP A 59  ? 0.40364 0.34206 0.30889 0.06164  -0.05060 0.07416  66  ASP A C   
412  O O   . ASP A 59  ? 0.33947 0.28825 0.25593 0.05119  -0.05103 0.06392  66  ASP A O   
413  C CB  . ASP A 59  ? 0.43391 0.35447 0.31354 0.04707  -0.04072 0.08270  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.55750 0.49824 0.42998 0.05290  -0.04660 0.07981  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.51288 0.46303 0.38524 0.06142  -0.05765 0.07853  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.54497 0.49032 0.40931 0.04937  -0.04058 0.08073  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.43426 0.38575 0.34897 0.07537  -0.05582 0.08067  67  PRO A N   
418  C CA  . PRO A 60  ? 0.36863 0.34921 0.31013 0.07565  -0.06317 0.07706  67  PRO A CA  
419  C C   . PRO A 60  ? 0.37118 0.37023 0.31592 0.06300  -0.07541 0.06759  67  PRO A C   
420  O O   . PRO A 60  ? 0.34122 0.35529 0.30489 0.05655  -0.07927 0.06081  67  PRO A O   
421  C CB  . PRO A 60  ? 0.51732 0.51570 0.46997 0.09242  -0.06832 0.09347  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.55514 0.52025 0.48600 0.10580  -0.05505 0.10182  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.54585 0.48302 0.45052 0.09228  -0.05165 0.09466  67  PRO A CD  
424  N N   . SER A 61  ? 0.39799 0.39113 0.31934 0.06090  -0.08077 0.06745  68  SER A N   
425  C CA  . SER A 61  ? 0.33030 0.32799 0.24060 0.05253  -0.09184 0.05806  68  SER A CA  
426  C C   . SER A 61  ? 0.44343 0.43623 0.35613 0.04375  -0.08230 0.04591  68  SER A C   
427  O O   . SER A 61  ? 0.34222 0.33519 0.24653 0.03839  -0.09002 0.03707  68  SER A O   
428  C CB  . SER A 61  ? 0.38551 0.36891 0.25924 0.05698  -0.09555 0.06130  68  SER A CB  
429  O OG  . SER A 61  ? 0.39824 0.36655 0.25751 0.05836  -0.07757 0.06269  68  SER A OG  
430  N N   . LYS A 62  ? 0.31123 0.29662 0.23233 0.04162  -0.06749 0.04632  69  LYS A N   
431  C CA  . LYS A 62  ? 0.32301 0.30949 0.25211 0.03286  -0.06027 0.03784  69  LYS A CA  
432  C C   . LYS A 62  ? 0.33148 0.33080 0.28078 0.02880  -0.06704 0.02929  69  LYS A C   
433  O O   . LYS A 62  ? 0.29070 0.29204 0.24314 0.02277  -0.06410 0.02133  69  LYS A O   
434  C CB  . LYS A 62  ? 0.39447 0.36916 0.32898 0.02758  -0.04911 0.04230  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.44896 0.41221 0.36756 0.02736  -0.04236 0.05398  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.39011 0.36206 0.30997 0.02028  -0.03379 0.05766  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.39328 0.35987 0.30256 0.01944  -0.02590 0.07440  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.55686 0.54129 0.47362 0.01545  -0.01502 0.08416  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.26461 0.27530 0.22977 0.03303  -0.07489 0.03378  70  LEU A N   
440  C CA  . LEU A 63  ? 0.22621 0.25378 0.21499 0.02895  -0.08103 0.03045  70  LEU A CA  
441  C C   . LEU A 63  ? 0.24243 0.28157 0.23042 0.02329  -0.10077 0.03101  70  LEU A C   
442  O O   . LEU A 63  ? 0.24728 0.30462 0.25939 0.01792  -0.10927 0.03336  70  LEU A O   
443  C CB  . LEU A 63  ? 0.30182 0.33815 0.31221 0.03850  -0.07491 0.03988  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.29238 0.30492 0.29416 0.04248  -0.05883 0.03778  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.33156 0.34509 0.34416 0.05780  -0.05083 0.04754  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.29323 0.30015 0.29555 0.03083  -0.05490 0.02579  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.27267 0.29876 0.23051 0.02339  -0.10949 0.03028  71  ASP A N   
448  C CA  . ASP A 64  ? 0.30396 0.32883 0.24895 0.01479  -0.13276 0.02919  71  ASP A CA  
449  C C   . ASP A 64  ? 0.33101 0.34523 0.27021 0.00457  -0.13617 0.01662  71  ASP A C   
450  O O   . ASP A 64  ? 0.32501 0.34042 0.26608 -0.00682 -0.15129 0.01609  71  ASP A O   
451  C CB  . ASP A 64  ? 0.34223 0.34375 0.24242 0.01912  -0.14002 0.02888  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.61371 0.62585 0.51830 0.02831  -0.14146 0.04329  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.49135 0.48417 0.36033 0.03532  -0.14003 0.04433  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.48057 0.51945 0.42236 0.03109  -0.14204 0.05516  71  ASP A OD2 
455  N N   . SER A 65  ? 0.31018 0.31467 0.24510 0.00786  -0.11692 0.00768  72  SER A N   
456  C CA  . SER A 65  ? 0.29896 0.29354 0.22961 0.00159  -0.11607 -0.00302 72  SER A CA  
457  C C   . SER A 65  ? 0.36872 0.38622 0.34117 -0.00492 -0.11462 -0.00140 72  SER A C   
458  O O   . SER A 65  ? 0.32510 0.33649 0.29839 -0.00908 -0.11057 -0.00933 72  SER A O   
459  C CB  . SER A 65  ? 0.35374 0.33498 0.26617 0.00991  -0.09521 -0.00845 72  SER A CB  
460  O OG  . SER A 65  ? 0.27386 0.26915 0.20652 0.01398  -0.08002 -0.00150 72  SER A OG  
461  N N   . GLY A 66  ? 0.33189 0.37435 0.33641 -0.00295 -0.11568 0.01027  73  GLY A N   
462  C CA  . GLY A 66  ? 0.31082 0.37447 0.35164 -0.00477 -0.11109 0.01475  73  GLY A CA  
463  C C   . GLY A 66  ? 0.23673 0.31112 0.29528 0.00817  -0.09554 0.02366  73  GLY A C   
464  O O   . GLY A 66  ? 0.21261 0.26992 0.25678 0.01368  -0.08123 0.01827  73  GLY A O   
465  N N   . LYS A 67  ? 0.19674 0.29741 0.28455 0.01346  -0.09844 0.03958  74  LYS A N   
466  C CA  . LYS A 67  ? 0.24701 0.34929 0.34180 0.03126  -0.08175 0.04936  74  LYS A CA  
467  C C   . LYS A 67  ? 0.25862 0.35607 0.36116 0.03726  -0.06501 0.04664  74  LYS A C   
468  O O   . LYS A 67  ? 0.25021 0.32658 0.33760 0.05065  -0.04962 0.04705  74  LYS A O   
469  C CB  . LYS A 67  ? 0.26680 0.40134 0.38831 0.04054  -0.08840 0.07224  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.38991 0.52648 0.49912 0.03470  -0.10672 0.07569  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.60487 0.74730 0.71532 0.05336  -0.09975 0.09143  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.55025 0.70095 0.65464 0.04620  -0.11757 0.09617  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.77984 0.95763 0.91013 0.05681  -0.11367 0.11593  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.18083 0.29100 0.30049 0.02747  -0.06852 0.04376  75  GLU A N   
475  C CA  . GLU A 68  ? 0.21961 0.32710 0.34628 0.03465  -0.05296 0.04349  75  GLU A CA  
476  C C   . GLU A 68  ? 0.22469 0.29820 0.32191 0.03023  -0.04534 0.02530  75  GLU A C   
477  O O   . GLU A 68  ? 0.22082 0.28716 0.30779 0.01703  -0.05290 0.01361  75  GLU A O   
478  C CB  . GLU A 68  ? 0.20298 0.33755 0.36026 0.02488  -0.05968 0.04951  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.31233 0.47732 0.49505 0.02583  -0.06290 0.06867  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.73935 0.90790 0.91636 0.01430  -0.08172 0.06978  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.65149 0.84054 0.84405 0.01912  -0.08285 0.08653  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.70701 0.85572 0.86105 0.00150  -0.09434 0.05473  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.14590 0.19687 0.22705 0.04205  -0.03080 0.02502  76  LEU A N   
484  C CA  . LEU A 69  ? 0.15237 0.17128 0.20635 0.03543  -0.02699 0.01184  76  LEU A CA  
485  C C   . LEU A 69  ? 0.16270 0.17771 0.21832 0.03882  -0.01863 0.01003  76  LEU A C   
486  O O   . LEU A 69  ? 0.17198 0.17330 0.21724 0.05582  -0.00635 0.01697  76  LEU A O   
487  C CB  . LEU A 69  ? 0.23942 0.22253 0.26169 0.04278  -0.02174 0.01275  76  LEU A CB  
488  C CG  . LEU A 69  ? 0.25837 0.24148 0.27539 0.04143  -0.02783 0.01636  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.37818 0.31764 0.35965 0.04493  -0.02336 0.01676  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.20293 0.20073 0.22635 0.02500  -0.03800 0.00964  76  LEU A CD2 
491  N N   . HIS A 70  ? 0.14575 0.16977 0.21026 0.02570  -0.02350 0.00186  77  HIS A N   
492  C CA  . HIS A 70  ? 0.13538 0.15964 0.20414 0.02906  -0.01608 0.00169  77  HIS A CA  
493  C C   . HIS A 70  ? 0.13961 0.16104 0.20544 0.01460  -0.02123 -0.00928 77  HIS A C   
494  O O   . HIS A 70  ? 0.12145 0.14534 0.18565 0.00400  -0.02888 -0.01470 77  HIS A O   
495  C CB  . HIS A 70  ? 0.17363 0.23210 0.27673 0.03430  -0.01441 0.01451  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.14325 0.22590 0.26854 0.01889  -0.02987 0.01419  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.27313 0.34988 0.39280 0.00483  -0.03743 0.00213  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.21151 0.31878 0.35858 0.01579  -0.04047 0.02523  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.21215 0.30077 0.34198 -0.00538 -0.05139 0.00366  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.24299 0.35078 0.39012 -0.00131 -0.05569 0.01746  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.11902 0.13612 0.18346 0.01727  -0.01496 -0.01015 78  ILE A N   
502  C CA  . ILE A 71  ? 0.12347 0.13934 0.18618 0.00684  -0.01810 -0.01768 78  ILE A CA  
503  C C   . ILE A 71  ? 0.16927 0.20305 0.25299 0.00869  -0.01421 -0.01399 78  ILE A C   
504  O O   . ILE A 71  ? 0.13709 0.17154 0.22353 0.02058  -0.00424 -0.00602 78  ILE A O   
505  C CB  . ILE A 71  ? 0.15303 0.13823 0.18541 0.00583  -0.01702 -0.02166 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.16846 0.13322 0.18026 -0.00018 -0.02342 -0.02255 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.18735 0.17846 0.22331 -0.00372 -0.02062 -0.02567 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.18511 0.11001 0.15989 -0.00438 -0.02719 -0.02461 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.10931 0.15472 0.20498 -0.00140 -0.02058 -0.01798 79  ASN A N   
510  C CA  . ASN A 72  ? 0.12398 0.18107 0.23680 -0.00314 -0.01894 -0.01445 79  ASN A CA  
511  C C   . ASN A 72  ? 0.12322 0.17135 0.22607 -0.00682 -0.01770 -0.02122 79  ASN A C   
512  O O   . ASN A 72  ? 0.13707 0.18058 0.23020 -0.01156 -0.02193 -0.02714 79  ASN A O   
513  C CB  . ASN A 72  ? 0.10891 0.17943 0.23909 -0.01247 -0.02979 -0.01172 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.20194 0.28889 0.34847 -0.01047 -0.03389 -0.00074 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.11959 0.21565 0.27488 0.00142  -0.02392 0.00986  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.16650 0.25194 0.30660 -0.01943 -0.04585 -0.00159 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.10496 0.15366 0.21182 -0.00284 -0.01064 -0.01736 80  LEU A N   
518  C CA  . LEU A 73  ? 0.07530 0.11799 0.17514 -0.00505 -0.00934 -0.02120 80  LEU A CA  
519  C C   . LEU A 73  ? 0.12450 0.17578 0.24193 -0.00928 -0.00987 -0.01741 80  LEU A C   
520  O O   . LEU A 73  ? 0.07605 0.13757 0.20980 -0.00685 -0.00499 -0.00747 80  LEU A O   
521  C CB  . LEU A 73  ? 0.10555 0.13408 0.18720 0.00279  -0.00192 -0.01981 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.16351 0.17119 0.21876 0.00559  -0.00351 -0.02254 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.16907 0.15101 0.19451 0.01336  0.00178  -0.02205 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.14700 0.15452 0.19741 -0.00588 -0.01446 -0.02726 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.12053 0.16607 0.23329 -0.01472 -0.01504 -0.02289 81  ILE A N   
526  C CA  . ILE A 74  ? 0.13150 0.17316 0.25164 -0.02135 -0.01927 -0.02080 81  ILE A CA  
527  C C   . ILE A 74  ? 0.15498 0.18623 0.26487 -0.01816 -0.01435 -0.02312 81  ILE A C   
528  O O   . ILE A 74  ? 0.16405 0.18559 0.25852 -0.01506 -0.01482 -0.02849 81  ILE A O   
529  C CB  . ILE A 74  ? 0.11846 0.14987 0.23052 -0.02853 -0.03094 -0.02526 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.16575 0.20849 0.28253 -0.02892 -0.03465 -0.02158 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.12472 0.14295 0.23820 -0.03946 -0.03988 -0.02189 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.21601 0.24624 0.31653 -0.03443 -0.04557 -0.02491 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.16046 0.19454 0.27831 -0.01643 -0.00793 -0.01682 82  PRO A N   
534  C CA  . PRO A 75  ? 0.17459 0.19800 0.28321 -0.01329 -0.00391 -0.01736 82  PRO A CA  
535  C C   . PRO A 75  ? 0.18042 0.18663 0.28790 -0.02121 -0.00949 -0.01618 82  PRO A C   
536  O O   . PRO A 75  ? 0.15664 0.16561 0.27917 -0.03213 -0.01627 -0.00981 82  PRO A O   
537  C CB  . PRO A 75  ? 0.16252 0.19314 0.27599 -0.00757 0.00532  -0.01026 82  PRO A CB  
538  C CG  . PRO A 75  ? 0.17822 0.22198 0.31038 -0.00935 0.00719  -0.00167 82  PRO A CG  
539  C CD  . PRO A 75  ? 0.16324 0.21109 0.29799 -0.01412 -0.00158 -0.00628 82  PRO A CD  
540  N N   . ASN A 76  ? 0.19608 0.18268 0.28395 -0.01586 -0.00760 -0.02029 83  ASN A N   
541  C CA  . ASN A 76  ? 0.23431 0.18978 0.30782 -0.02206 -0.01319 -0.02057 83  ASN A CA  
542  C C   . ASN A 76  ? 0.21420 0.15800 0.27613 -0.01138 -0.00336 -0.01834 83  ASN A C   
543  O O   . ASN A 76  ? 0.22351 0.16205 0.26825 0.00264  0.00307  -0.02120 83  ASN A O   
544  C CB  . ASN A 76  ? 0.23115 0.15943 0.27689 -0.02221 -0.02120 -0.02927 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.33469 0.21695 0.35409 -0.03161 -0.03149 -0.03073 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.33670 0.19724 0.34379 -0.02784 -0.02646 -0.02845 83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.37893 0.24169 0.38569 -0.04505 -0.04793 -0.03401 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.30945 0.21277 0.36599 -0.03372 0.00728  0.09365  84  LYS A N   
549  C CA  . LYS A 77  ? 0.31158 0.19655 0.35081 -0.02158 0.01390  0.10137  84  LYS A CA  
550  C C   . LYS A 77  ? 0.38005 0.21659 0.40347 -0.02587 0.00664  0.09742  84  LYS A C   
551  O O   . LYS A 77  ? 0.38370 0.20270 0.38750 -0.00906 0.01069  0.09740  84  LYS A O   
552  C CB  . LYS A 77  ? 0.35368 0.25381 0.40548 -0.02368 0.02569  0.12629  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.36864 0.30678 0.42095 -0.00984 0.03791  0.13081  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.49495 0.44513 0.55358 -0.00708 0.05310  0.15761  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.43555 0.41387 0.48198 0.01163  0.06759  0.16086  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.52399 0.52780 0.58893 0.00870  0.06933  0.15702  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.37369 0.18565 0.40191 -0.04723 -0.00451 0.09486  85  GLN A N   
558  C CA  . GLN A 78  ? 0.54874 0.30148 0.55102 -0.05052 -0.01109 0.08949  85  GLN A CA  
559  C C   . GLN A 78  ? 0.45592 0.19221 0.43223 -0.03060 -0.01168 0.06869  85  GLN A C   
560  O O   . GLN A 78  ? 0.50038 0.19984 0.45129 -0.01455 -0.00710 0.06756  85  GLN A O   
561  C CB  . GLN A 78  ? 0.47974 0.21518 0.48635 -0.07819 -0.02316 0.08694  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.77553 0.52269 0.80256 -0.09576 -0.02042 0.10721  85  GLN A CG  
563  C CD  . GLN A 78  ? 0.88266 0.69133 0.94783 -0.09941 -0.01478 0.12415  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.85992 0.68779 0.93675 -0.09434 -0.00231 0.14362  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.68786 0.52804 0.77024 -0.10489 -0.02175 0.11724  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.37051 0.13477 0.35371 -0.02971 -0.01565 0.05472  86  ASP A N   
567  C CA  . ASP A 79  ? 0.41817 0.17794 0.38296 -0.01068 -0.01412 0.03869  86  ASP A CA  
568  C C   . ASP A 79  ? 0.33450 0.13263 0.30549 0.01074  -0.00498 0.04163  86  ASP A C   
569  O O   . ASP A 79  ? 0.36608 0.16505 0.32628 0.02818  -0.00222 0.03453  86  ASP A O   
570  C CB  . ASP A 79  ? 0.35254 0.12502 0.32155 -0.02043 -0.02275 0.02453  86  ASP A CB  
571  C CG  . ASP A 79  ? 0.59684 0.32864 0.55317 -0.04241 -0.03632 0.01980  86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.57202 0.27076 0.51570 -0.04744 -0.03616 0.02386  86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.53416 0.28020 0.49603 -0.05314 -0.04512 0.01137  86  ASP A OD2 
574  N N   . ARG A 80  ? 0.32752 0.15666 0.31381 0.00955  -0.00065 0.05342  87  ARG A N   
575  C CA  . ARG A 80  ? 0.28804 0.15301 0.27612 0.02430  0.00343  0.05506  87  ARG A CA  
576  C C   . ARG A 80  ? 0.29956 0.18864 0.29181 0.02551  -0.00099 0.04060  87  ARG A C   
577  O O   . ARG A 80  ? 0.24994 0.15316 0.23843 0.03806  -0.00156 0.03772  87  ARG A O   
578  C CB  . ARG A 80  ? 0.30827 0.16467 0.28326 0.04378  0.00763  0.06310  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.31189 0.19986 0.28661 0.05242  0.00948  0.07271  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.43025 0.33038 0.39878 0.07161  0.00833  0.07731  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.54899 0.41930 0.50756 0.08477  0.01456  0.08961  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.58950 0.45895 0.54403 0.10480  0.01678  0.09448  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.49314 0.39572 0.45739 0.11198  0.01256  0.08995  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.52162 0.35681 0.46302 0.11878  0.02439  0.10665  87  ARG A NH2 
585  N N   . THR A 81  ? 0.24197 0.13830 0.24457 0.01168  -0.00444 0.03420  88  THR A N   
586  C CA  . THR A 81  ? 0.21656 0.13225 0.22260 0.01141  -0.00799 0.02203  88  THR A CA  
587  C C   . THR A 81  ? 0.22390 0.16261 0.23972 0.00509  -0.00628 0.02361  88  THR A C   
588  O O   . THR A 81  ? 0.23049 0.17096 0.25665 -0.00277 -0.00326 0.03302  88  THR A O   
589  C CB  . THR A 81  ? 0.30489 0.20221 0.30789 0.00500  -0.01342 0.01140  88  THR A CB  
590  O OG1 . THR A 81  ? 0.28899 0.17385 0.29911 -0.01166 -0.01794 0.01510  88  THR A OG1 
591  C CG2 . THR A 81  ? 0.28963 0.15868 0.27465 0.01717  -0.01167 0.00861  88  THR A CG2 
592  N N   . LEU A 82  ? 0.18132 0.13686 0.19337 0.00920  -0.00749 0.01618  89  LEU A N   
593  C CA  . LEU A 82  ? 0.17026 0.13898 0.18471 0.00640  -0.00498 0.01452  89  LEU A CA  
594  C C   . LEU A 82  ? 0.17788 0.14934 0.19591 0.00243  -0.01018 0.00320  89  LEU A C   
595  O O   . LEU A 82  ? 0.18191 0.15544 0.19458 0.00529  -0.01425 -0.00335 89  LEU A O   
596  C CB  . LEU A 82  ? 0.17697 0.15194 0.17368 0.01400  -0.00247 0.01535  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.19361 0.17163 0.18262 0.01525  0.00210  0.01196  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.17879 0.16338 0.18184 0.01583  0.01269  0.02380  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.22665 0.19846 0.18572 0.02174  0.00178  0.00953  89  LEU A CD2 
600  N N   . THR A 83  ? 0.16405 0.13903 0.19337 -0.00404 -0.01001 0.00376  90  THR A N   
601  C CA  . THR A 83  ? 0.16105 0.13744 0.19274 -0.00756 -0.01489 -0.00503 90  THR A CA  
602  C C   . THR A 83  ? 0.18641 0.17318 0.21819 -0.00488 -0.01052 -0.00499 90  THR A C   
603  O O   . THR A 83  ? 0.16156 0.15686 0.20102 -0.00293 -0.00390 0.00460  90  THR A O   
604  C CB  . THR A 83  ? 0.18807 0.15683 0.22850 -0.01736 -0.02131 -0.00417 90  THR A CB  
605  O OG1 . THR A 83  ? 0.21546 0.16243 0.24611 -0.01761 -0.02436 -0.00615 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.22150 0.19214 0.26050 -0.01948 -0.02621 -0.01211 90  THR A CG2 
607  N N   . ILE A 84  ? 0.13925 0.12440 0.16212 -0.00356 -0.01279 -0.01363 91  ILE A N   
608  C CA  . ILE A 84  ? 0.18721 0.17232 0.20408 -0.00023 -0.00877 -0.01494 91  ILE A CA  
609  C C   . ILE A 84  ? 0.20606 0.19476 0.23206 -0.00416 -0.01282 -0.01758 91  ILE A C   
610  O O   . ILE A 84  ? 0.18472 0.17050 0.20734 -0.00718 -0.01777 -0.02405 91  ILE A O   
611  C CB  . ILE A 84  ? 0.16903 0.14315 0.16421 0.00113  -0.01020 -0.02162 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.28258 0.25132 0.26209 0.00560  -0.00777 -0.01876 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.18703 0.14951 0.16954 0.00454  -0.00612 -0.02430 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.35482 0.32985 0.33752 0.00287  -0.01447 -0.01773 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.13852 0.13688 0.17695 -0.00310 -0.01029 -0.01005 92  VAL A N   
616  C CA  . VAL A 85  ? 0.15003 0.15407 0.19632 -0.00654 -0.01568 -0.01009 92  VAL A CA  
617  C C   . VAL A 85  ? 0.20095 0.20427 0.24196 0.00237  -0.00863 -0.00782 92  VAL A C   
618  O O   . VAL A 85  ? 0.17810 0.18339 0.21802 0.01219  0.00152  -0.00041 92  VAL A O   
619  C CB  . VAL A 85  ? 0.17490 0.19340 0.24145 -0.01432 -0.02203 -0.00024 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.19996 0.22157 0.26823 -0.01965 -0.03182 -0.00170 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.22960 0.23892 0.29596 -0.02256 -0.02730 -0.00144 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.14965 0.14737 0.18453 0.00106  -0.01219 -0.01291 93  ASP A N   
623  C CA  . ASP A 86  ? 0.15002 0.14350 0.17964 0.00968  -0.00611 -0.00906 93  ASP A CA  
624  C C   . ASP A 86  ? 0.19932 0.20192 0.23636 0.00655  -0.01316 -0.00670 93  ASP A C   
625  O O   . ASP A 86  ? 0.18864 0.19193 0.22492 -0.00194 -0.02185 -0.01223 93  ASP A O   
626  C CB  . ASP A 86  ? 0.15493 0.12192 0.15961 0.01135  -0.00222 -0.01732 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.32745 0.29004 0.32827 0.00101  -0.00972 -0.02447 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.27532 0.24222 0.28014 0.00017  -0.01184 -0.02252 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.22397 0.18193 0.21862 -0.00542 -0.01308 -0.02975 93  ASP A OD2 
630  N N   . THR A 87  ? 0.14160 0.14948 0.18232 0.01599  -0.00839 0.00260  94  THR A N   
631  C CA  . THR A 87  ? 0.13453 0.15049 0.17865 0.01512  -0.01496 0.00675  94  THR A CA  
632  C C   . THR A 87  ? 0.24344 0.23701 0.26848 0.02044  -0.00908 0.00353  94  THR A C   
633  O O   . THR A 87  ? 0.16419 0.16034 0.18958 0.02841  -0.00722 0.01226  94  THR A O   
634  C CB  . THR A 87  ? 0.18254 0.22686 0.24921 0.02138  -0.01605 0.02408  94  THR A CB  
635  O OG1 . THR A 87  ? 0.14600 0.18900 0.21354 0.03863  -0.00008 0.03342  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.16045 0.22683 0.24768 0.00880  -0.02693 0.02866  94  THR A CG2 
637  N N   . GLY A 88  ? 0.17782 0.15015 0.18722 0.01482  -0.00721 -0.00696 95  GLY A N   
638  C CA  . GLY A 88  ? 0.18813 0.13728 0.18056 0.01430  -0.00384 -0.00884 95  GLY A CA  
639  C C   . GLY A 88  ? 0.16862 0.12514 0.16231 0.00868  -0.00895 -0.00785 95  GLY A C   
640  O O   . GLY A 88  ? 0.18918 0.16427 0.19095 0.00842  -0.01521 -0.00570 95  GLY A O   
641  N N   . ILE A 89  ? 0.19213 0.13160 0.17475 0.00309  -0.00676 -0.00869 96  ILE A N   
642  C CA  . ILE A 89  ? 0.19052 0.13567 0.17186 0.00094  -0.00753 -0.00403 96  ILE A CA  
643  C C   . ILE A 89  ? 0.20468 0.16804 0.19131 -0.00376 -0.01140 -0.00800 96  ILE A C   
644  O O   . ILE A 89  ? 0.21067 0.18066 0.19197 -0.00119 -0.01143 -0.00449 96  ILE A O   
645  C CB  . ILE A 89  ? 0.23635 0.15879 0.20722 -0.00574 -0.00342 -0.00033 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.22881 0.15672 0.19756 -0.00485 -0.00103 0.00877  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.20778 0.12901 0.18167 -0.02005 -0.00662 -0.00507 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.26023 0.16087 0.21802 -0.00978 0.00364  0.01647  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.17869 0.14733 0.17143 -0.00803 -0.01348 -0.01456 97  GLY A N   
650  C CA  . GLY A 90  ? 0.18828 0.16893 0.18253 -0.00836 -0.01451 -0.01741 97  GLY A CA  
651  C C   . GLY A 90  ? 0.17916 0.16635 0.17605 -0.01219 -0.00935 -0.01190 97  GLY A C   
652  O O   . GLY A 90  ? 0.19959 0.18109 0.19854 -0.01938 -0.00769 -0.00620 97  GLY A O   
653  N N   . MET A 91  ? 0.17948 0.17781 0.17576 -0.00705 -0.00630 -0.01186 98  MET A N   
654  C CA  . MET A 91  ? 0.18139 0.19571 0.18580 -0.00751 0.00118  -0.00201 98  MET A CA  
655  C C   . MET A 91  ? 0.17579 0.19256 0.16458 0.00623  0.00927  0.00046  98  MET A C   
656  O O   . MET A 91  ? 0.23001 0.23482 0.20134 0.01480  0.00706  -0.00858 98  MET A O   
657  C CB  . MET A 91  ? 0.18745 0.21733 0.20790 -0.01059 0.00042  -0.00038 98  MET A CB  
658  C CG  . MET A 91  ? 0.28032 0.30651 0.31021 -0.02547 -0.00814 -0.00127 98  MET A CG  
659  S SD  . MET A 91  ? 0.21758 0.26390 0.26282 -0.02726 -0.01205 0.00093  98  MET A SD  
660  C CE  . MET A 91  ? 0.15572 0.18404 0.18752 -0.01758 -0.01420 -0.01303 98  MET A CE  
661  N N   . THR A 92  ? 0.19308 0.22186 0.18465 0.00783  0.01864  0.01338  99  THR A N   
662  C CA  . THR A 92  ? 0.20427 0.23604 0.17732 0.02448  0.03041  0.01804  99  THR A CA  
663  C C   . THR A 92  ? 0.19844 0.24664 0.17985 0.03492  0.03929  0.02215  99  THR A C   
664  O O   . THR A 92  ? 0.20510 0.26918 0.21203 0.02655  0.03524  0.02465  99  THR A O   
665  C CB  . THR A 92  ? 0.20997 0.25336 0.18573 0.02436  0.04056  0.03459  99  THR A CB  
666  O OG1 . THR A 92  ? 0.19868 0.26958 0.20850 0.01267  0.04429  0.05007  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.21278 0.23850 0.18056 0.01608  0.03279  0.03292  99  THR A CG2 
668  N N   . LYS A 93  ? 0.20413 0.22241 0.20142 0.04611  -0.00893 -0.03765 100 LYS A N   
669  C CA  . LYS A 93  ? 0.22708 0.22903 0.21998 0.03478  0.00469  -0.02910 100 LYS A CA  
670  C C   . LYS A 93  ? 0.21944 0.20353 0.21581 0.03657  0.00580  -0.01505 100 LYS A C   
671  O O   . LYS A 93  ? 0.21208 0.19252 0.21461 0.03185  0.01264  -0.01274 100 LYS A O   
672  C CB  . LYS A 93  ? 0.25321 0.25199 0.23037 0.03184  0.01059  -0.02734 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.27649 0.25978 0.24768 0.02732  0.02194  -0.02467 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.30322 0.28569 0.25957 0.02738  0.02741  -0.02607 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.38687 0.35185 0.33503 0.02977  0.03550  -0.02968 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.38774 0.35974 0.32783 0.03467  0.04132  -0.03175 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.23621 0.20738 0.22368 0.04147  -0.00215 -0.00575 101 ALA A N   
678  C CA  . ALA A 94  ? 0.26923 0.22518 0.25440 0.03571  -0.00044 0.00618  101 ALA A CA  
679  C C   . ALA A 94  ? 0.30399 0.25938 0.30479 0.03645  -0.00282 0.00186  101 ALA A C   
680  O O   . ALA A 94  ? 0.27867 0.23635 0.28645 0.02865  0.00422  0.00669  101 ALA A O   
681  C CB  . ALA A 94  ? 0.28256 0.21252 0.24179 0.03446  -0.01045 0.01757  101 ALA A CB  
682  N N   . ASP A 95  ? 0.22993 0.18953 0.23737 0.04655  -0.01306 -0.00992 102 ASP A N   
683  C CA  . ASP A 95  ? 0.26371 0.23048 0.28723 0.04642  -0.01438 -0.01848 102 ASP A CA  
684  C C   . ASP A 95  ? 0.20343 0.18784 0.23851 0.03405  -0.00207 -0.02065 102 ASP A C   
685  O O   . ASP A 95  ? 0.21016 0.19369 0.25249 0.02762  0.00133  -0.01747 102 ASP A O   
686  C CB  . ASP A 95  ? 0.24160 0.22623 0.27342 0.06127  -0.02659 -0.03786 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.40447 0.35907 0.41971 0.08075  -0.04509 -0.03676 102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.37215 0.28489 0.36783 0.07582  -0.04766 -0.02100 102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.34941 0.32155 0.36715 0.10056  -0.05849 -0.05279 102 ASP A OD2 
690  N N   . LEU A 96  ? 0.21949 0.21495 0.25064 0.02967  0.00316  -0.02593 103 LEU A N   
691  C CA  . LEU A 96  ? 0.21909 0.21495 0.24767 0.01768  0.01114  -0.02679 103 LEU A CA  
692  C C   . LEU A 96  ? 0.21810 0.19975 0.24477 0.01914  0.01592  -0.01342 103 LEU A C   
693  O O   . LEU A 96  ? 0.22761 0.20900 0.25808 0.01469  0.01691  -0.01120 103 LEU A O   
694  C CB  . LEU A 96  ? 0.20801 0.20359 0.22100 0.01058  0.01490  -0.03341 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.18902 0.21142 0.20105 -0.00120 0.01365  -0.05160 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.22558 0.23802 0.21342 -0.01497 0.01931  -0.05578 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.17477 0.21176 0.19195 -0.01532 0.01451  -0.05972 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.20686 0.18385 0.22769 0.02532  0.01853  -0.00654 104 ILE A N   
699  C CA  . ILE A 97  ? 0.24535 0.22515 0.26776 0.02882  0.02307  0.00058  104 ILE A CA  
700  C C   . ILE A 97  ? 0.22740 0.21633 0.26121 0.02385  0.02204  0.00595  104 ILE A C   
701  O O   . ILE A 97  ? 0.24320 0.24296 0.28347 0.02448  0.02391  0.00789  104 ILE A O   
702  C CB  . ILE A 97  ? 0.29543 0.28074 0.31026 0.03314  0.02725  0.00236  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.21024 0.18400 0.21140 0.03655  0.02852  -0.00488 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.23432 0.23988 0.25489 0.03791  0.03216  0.00377  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.27611 0.25753 0.26884 0.03779  0.03177  -0.00511 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.19350 0.17513 0.22614 0.01972  0.01727  0.00744  105 ASN A N   
707  C CA  . ASN A 98  ? 0.22162 0.20156 0.25747 0.01146  0.01562  0.01138  105 ASN A CA  
708  C C   . ASN A 98  ? 0.23413 0.21692 0.28219 0.01057  0.01253  0.00397  105 ASN A C   
709  O O   . ASN A 98  ? 0.22634 0.19835 0.27470 0.01030  0.00605  -0.00083 105 ASN A O   
710  C CB  . ASN A 98  ? 0.28720 0.24196 0.30504 0.00803  0.00866  0.01616  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.54237 0.48867 0.55003 -0.00864 0.00981  0.02325  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.57448 0.54565 0.59475 -0.01690 0.01694  0.02307  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.61936 0.52763 0.59890 -0.01497 0.00137  0.02934  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.18129 0.17576 0.23498 0.01059  0.01598  0.00205  106 ASN A N   
715  C CA  . ASN A 99  ? 0.18442 0.18633 0.24559 0.00404  0.01470  -0.00313 106 ASN A CA  
716  C C   . ASN A 99  ? 0.19966 0.20447 0.26441 0.00273  0.01036  -0.01671 106 ASN A C   
717  O O   . ASN A 99  ? 0.15078 0.16355 0.22432 -0.00127 0.00783  -0.02456 106 ASN A O   
718  C CB  . ASN A 99  ? 0.14847 0.15904 0.21720 -0.00315 0.01544  0.00065  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.15494 0.18207 0.22464 -0.00172 0.01951  0.00855  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.16017 0.19052 0.22657 0.00674  0.01888  0.00975  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.15405 0.19135 0.22420 -0.01009 0.02247  0.01218  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.16275 0.16778 0.22143 0.00632  0.00953  -0.02275 107 LEU A N   
723  C CA  . LEU A 100 ? 0.18809 0.21256 0.25236 0.00561  0.00557  -0.04081 107 LEU A CA  
724  C C   . LEU A 100 ? 0.18568 0.21006 0.25935 0.01890  -0.00368 -0.04938 107 LEU A C   
725  O O   . LEU A 100 ? 0.14562 0.19277 0.23058 0.02017  -0.00757 -0.06758 107 LEU A O   
726  C CB  . LEU A 100 ? 0.17522 0.21842 0.23912 -0.01240 0.00933  -0.04978 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.29128 0.32189 0.33235 -0.02881 0.01445  -0.04396 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.29701 0.31950 0.32429 -0.02774 0.01579  -0.04565 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.21765 0.22214 0.24959 -0.02563 0.01498  -0.02579 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.23064 0.22653 0.29489 0.02809  -0.00818 -0.03752 108 GLY A N   
731  C CA  . GLY A 101 ? 0.25789 0.23359 0.31740 0.04190  -0.02083 -0.04345 108 GLY A CA  
732  C C   . GLY A 101 ? 0.29262 0.25879 0.35565 0.03644  -0.02185 -0.04629 108 GLY A C   
733  O O   . GLY A 101 ? 0.26028 0.20818 0.31840 0.05042  -0.03424 -0.05780 108 GLY A O   
734  N N   . THR A 102 ? 0.20177 0.17835 0.27087 0.01866  -0.01091 -0.03761 109 THR A N   
735  C CA  . THR A 102 ? 0.21233 0.18499 0.28449 0.00950  -0.01043 -0.04025 109 THR A CA  
736  C C   . THR A 102 ? 0.22663 0.17416 0.28259 -0.00320 -0.00729 -0.02275 109 THR A C   
737  O O   . THR A 102 ? 0.22769 0.17268 0.27497 -0.00648 -0.00293 -0.00933 109 THR A O   
738  C CB  . THR A 102 ? 0.17209 0.18027 0.25963 -0.00412 -0.00182 -0.04402 109 THR A CB  
739  O OG1 . THR A 102 ? 0.24347 0.25702 0.32770 -0.01145 0.00578  -0.02763 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.17587 0.21442 0.27320 -0.00169 -0.00260 -0.06231 109 THR A CG2 
741  N N   . ILE A 103 ? 0.21548 0.14911 0.26605 -0.01330 -0.00874 -0.02560 110 ILE A N   
742  C CA  . ILE A 103 ? 0.23020 0.15518 0.26652 -0.03487 -0.00262 -0.01214 110 ILE A CA  
743  C C   . ILE A 103 ? 0.19644 0.16782 0.25408 -0.04677 0.00738  -0.01147 110 ILE A C   
744  O O   . ILE A 103 ? 0.20361 0.17995 0.26088 -0.06216 0.00948  -0.01451 110 ILE A O   
745  C CB  . ILE A 103 ? 0.29931 0.17291 0.30661 -0.04399 -0.01087 -0.01457 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.33884 0.21104 0.35700 -0.03614 -0.01661 -0.03421 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.37904 0.19670 0.35347 -0.03212 -0.02390 -0.00974 110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.45671 0.27308 0.44223 -0.04750 -0.02426 -0.03789 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.24407 0.12142 0.27280 0.01485  0.01271  0.03857  111 ALA A N   
750  C CA  . ALA A 104 ? 0.25297 0.15899 0.30387 0.02379  0.00966  0.04104  111 ALA A CA  
751  C C   . ALA A 104 ? 0.20209 0.15474 0.29085 0.00877  0.02311  0.03088  111 ALA A C   
752  O O   . ALA A 104 ? 0.18714 0.20056 0.28650 0.00130  0.01651  0.01136  111 ALA A O   
753  C CB  . ALA A 104 ? 0.25886 0.18829 0.27758 0.03809  -0.01013 0.04228  111 ALA A CB  
754  N N   . LYS A 105 ? 0.19204 0.14305 0.28130 -0.00337 0.03717  0.03144  112 LYS A N   
755  C CA  . LYS A 105 ? 0.19009 0.21878 0.29793 -0.02638 0.04575  0.00748  112 LYS A CA  
756  C C   . LYS A 105 ? 0.29458 0.33690 0.41895 -0.06545 0.06230  -0.02437 112 LYS A C   
757  O O   . LYS A 105 ? 0.20440 0.31953 0.34360 -0.07588 0.05577  -0.04620 112 LYS A O   
758  C CB  . LYS A 105 ? 0.20871 0.23150 0.31288 -0.03496 0.06102  0.01438  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.35638 0.47130 0.48406 -0.05749 0.06990  -0.00965 112 LYS A CG  
760  C CD  . LYS A 105 ? 0.31844 0.44394 0.44087 -0.05300 0.07942  0.00134  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.63613 0.82308 0.78142 -0.09513 0.10274  -0.02424 112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.46465 0.74626 0.64041 -0.10928 0.09538  -0.05300 112 LYS A NZ  
763  N N   . SER A 106 ? 0.25993 0.22879 0.37869 -0.08717 0.08272  -0.02754 113 SER A N   
764  C CA  . SER A 106 ? 0.28088 0.25034 0.40971 -0.12468 0.09934  -0.05901 113 SER A CA  
765  C C   . SER A 106 ? 0.26732 0.24106 0.39835 -0.11462 0.08864  -0.06936 113 SER A C   
766  O O   . SER A 106 ? 0.27844 0.29054 0.41896 -0.14082 0.09426  -0.09921 113 SER A O   
767  C CB  . SER A 106 ? 0.40677 0.29978 0.50906 -0.12928 0.11024  -0.05296 113 SER A CB  
768  O OG  . SER A 106 ? 0.40116 0.23932 0.48357 -0.09509 0.09557  -0.02992 113 SER A OG  
769  N N   . GLY A 107 ? 0.24622 0.18384 0.36729 -0.07936 0.07369  -0.04593 114 GLY A N   
770  C CA  . GLY A 107 ? 0.26666 0.21469 0.38893 -0.07054 0.06459  -0.05493 114 GLY A CA  
771  C C   . GLY A 107 ? 0.24864 0.28660 0.37470 -0.06843 0.04640  -0.06517 114 GLY A C   
772  O O   . GLY A 107 ? 0.22530 0.29340 0.35452 -0.08352 0.04723  -0.08884 114 GLY A O   
773  N N   . THR A 108 ? 0.17590 0.25564 0.29901 -0.04860 0.02920  -0.04780 115 THR A N   
774  C CA  . THR A 108 ? 0.15616 0.32069 0.28142 -0.04344 0.00927  -0.05596 115 THR A CA  
775  C C   . THR A 108 ? 0.17702 0.40483 0.32085 -0.08034 0.02022  -0.08980 115 THR A C   
776  O O   . THR A 108 ? 0.19128 0.47400 0.33646 -0.08959 0.01009  -0.10799 115 THR A O   
777  C CB  . THR A 108 ? 0.13439 0.32294 0.25225 -0.01169 -0.00990 -0.03137 115 THR A CB  
778  O OG1 . THR A 108 ? 0.18413 0.31469 0.28056 0.01964  -0.02274 -0.00087 115 THR A OG1 
779  C CG2 . THR A 108 ? 0.16930 0.44406 0.28907 -0.00312 -0.03230 -0.03949 115 THR A CG2 
780  N N   . LYS A 109 ? 0.19009 0.41164 0.34589 -0.10422 0.04047  -0.09825 116 LYS A N   
781  C CA  . LYS A 109 ? 0.21898 0.48394 0.38285 -0.13995 0.05206  -0.12739 116 LYS A CA  
782  C C   . LYS A 109 ? 0.24901 0.49215 0.40077 -0.15857 0.05937  -0.14964 116 LYS A C   
783  O O   . LYS A 109 ? 0.29613 0.58864 0.44062 -0.16603 0.05264  -0.16575 116 LYS A O   
784  C CB  . LYS A 109 ? 0.25146 0.48189 0.41714 -0.16232 0.07517  -0.12806 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.36163 0.63770 0.52651 -0.18828 0.08203  -0.14893 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.44215 0.66046 0.59835 -0.21533 0.10683  -0.15175 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.59665 0.85719 0.75128 -0.24643 0.11547  -0.17496 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.49869 0.84667 0.66177 -0.24116 0.09789  -0.18828 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.26656 0.43171 0.41335 -0.16284 0.07421  -0.14952 117 ALA A N   
790  C CA  . ALA A 110 ? 0.33821 0.47947 0.47260 -0.17659 0.08459  -0.17101 117 ALA A CA  
791  C C   . ALA A 110 ? 0.27540 0.45476 0.40565 -0.16312 0.06732  -0.17448 117 ALA A C   
792  O O   . ALA A 110 ? 0.29830 0.50404 0.41809 -0.17633 0.06988  -0.19450 117 ALA A O   
793  C CB  . ALA A 110 ? 0.33242 0.37843 0.45896 -0.17291 0.10248  -0.16488 117 ALA A CB  
794  N N   . PHE A 111 ? 0.23196 0.41413 0.36756 -0.13717 0.04975  -0.15358 118 PHE A N   
795  C CA  . PHE A 111 ? 0.21251 0.42732 0.33608 -0.12214 0.03091  -0.15179 118 PHE A CA  
796  C C   . PHE A 111 ? 0.21700 0.50089 0.32600 -0.12108 0.01642  -0.15523 118 PHE A C   
797  O O   . PHE A 111 ? 0.23327 0.53576 0.32722 -0.12689 0.01556  -0.16667 118 PHE A O   
798  C CB  . PHE A 111 ? 0.18045 0.36970 0.29360 -0.08157 0.01274  -0.11419 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.20979 0.42314 0.30433 -0.06640 -0.00677 -0.10709 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.20118 0.41535 0.28967 -0.08270 0.00230  -0.12942 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.20038 0.42996 0.27936 -0.03625 -0.03337 -0.07758 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.18842 0.42468 0.25598 -0.07188 -0.01428 -0.12173 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.22948 0.45980 0.28126 -0.02356 -0.04710 -0.06482 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.24906 0.48797 0.29643 -0.04193 -0.03797 -0.08626 118 PHE A CZ  
805  N N   . MET A 112 ? 0.20809 0.52685 0.32219 -0.11322 0.00768  -0.14510 119 MET A N   
806  C CA  . MET A 112 ? 0.36180 0.73656 0.46396 -0.10662 -0.00531 -0.14496 119 MET A CA  
807  C C   . MET A 112 ? 0.34360 0.74558 0.44714 -0.13897 0.00977  -0.17386 119 MET A C   
808  O O   . MET A 112 ? 0.33489 0.77695 0.42807 -0.13919 0.00209  -0.17860 119 MET A O   
809  C CB  . MET A 112 ? 0.35248 0.75091 0.45984 -0.08497 -0.01706 -0.12659 119 MET A CB  
810  C CG  . MET A 112 ? 0.17801 0.55261 0.26808 -0.04668 -0.03674 -0.09503 119 MET A CG  
811  S SD  . MET A 112 ? 0.70713 1.09975 0.79323 -0.01847 -0.04823 -0.07646 119 MET A SD  
812  C CE  . MET A 112 ? 0.28771 0.60536 0.35499 0.01244  -0.05738 -0.04279 119 MET A CE  
813  N N   . GLU A 113 ? 0.28006 0.65495 0.39404 -0.16647 0.03183  -0.19131 120 GLU A N   
814  C CA  . GLU A 113 ? 0.37821 0.76727 0.48759 -0.19807 0.04734  -0.21848 120 GLU A CA  
815  C C   . GLU A 113 ? 0.46860 0.83942 0.56453 -0.20436 0.05316  -0.23077 120 GLU A C   
816  O O   . GLU A 113 ? 0.38555 0.79182 0.47284 -0.21916 0.05444  -0.24626 120 GLU A O   
817  C CB  . GLU A 113 ? 0.39999 0.74954 0.51643 -0.22451 0.07069  -0.23050 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.60491 0.98485 0.73364 -0.22769 0.06927  -0.22447 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.78641 1.10641 0.91832 -0.24537 0.09070  -0.22443 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.85670 1.18915 0.99894 -0.24331 0.09050  -0.21344 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.77147 1.02928 0.89326 -0.25933 0.10821  -0.23386 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.33228 0.65000 0.42755 -0.19345 0.05725  -0.22418 121 ALA A N   
823  C CA  . ALA A 114 ? 0.34201 0.64420 0.42618 -0.19755 0.06424  -0.23612 121 ALA A CA  
824  C C   . ALA A 114 ? 0.33353 0.68623 0.40385 -0.18415 0.04418  -0.22715 121 ALA A C   
825  O O   . ALA A 114 ? 0.42865 0.79791 0.48833 -0.19771 0.04970  -0.24217 121 ALA A O   
826  C CB  . ALA A 114 ? 0.32972 0.56753 0.41890 -0.18456 0.07166  -0.22904 121 ALA A CB  
827  N N   . LEU A 115 ? 0.29774 0.66980 0.36615 -0.15690 0.02138  -0.20050 122 LEU A N   
828  C CA  . LEU A 115 ? 0.33979 0.74331 0.39144 -0.14081 0.00266  -0.18564 122 LEU A CA  
829  C C   . LEU A 115 ? 0.50880 0.96367 0.55743 -0.15604 0.00123  -0.19856 122 LEU A C   
830  O O   . LEU A 115 ? 0.44171 0.91399 0.47661 -0.16043 -0.00264 -0.20162 122 LEU A O   
831  C CB  . LEU A 115 ? 0.25342 0.65275 0.30151 -0.10709 -0.01909 -0.15259 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.25387 0.60632 0.29841 -0.08873 -0.02348 -0.13435 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.27612 0.61529 0.31536 -0.05718 -0.04192 -0.10189 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.25608 0.59658 0.28355 -0.08888 -0.02377 -0.13348 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.47119 0.95235 0.53272 -0.16579 0.00422  -0.20661 123 GLN A N   
836  C CA  . GLN A 116 ? 0.54186 1.07536 0.60283 -0.18314 0.00336  -0.22149 123 GLN A CA  
837  C C   . GLN A 116 ? 0.52572 1.05430 0.58276 -0.21858 0.02435  -0.25167 123 GLN A C   
838  O O   . GLN A 116 ? 0.68457 1.25556 0.73803 -0.23619 0.02364  -0.26551 123 GLN A O   
839  C CB  . GLN A 116 ? 0.50863 1.07617 0.58536 -0.18342 0.00067  -0.22162 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.48942 1.07025 0.56828 -0.14729 -0.02067 -0.19389 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.92368 1.56572 1.01262 -0.14652 -0.02930 -0.19748 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.88719 1.56802 0.98055 -0.17401 -0.02176 -0.21974 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.83242 1.48189 0.92463 -0.11500 -0.04478 -0.17625 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.65770 1.13257 0.71507 -0.22848 0.04290  -0.26196 124 ALA A N   
845  C CA  . ALA A 117 ? 0.53587 0.99205 0.58800 -0.25920 0.06525  -0.28998 124 ALA A CA  
846  C C   . ALA A 117 ? 0.71414 1.14448 0.75506 -0.25576 0.07042  -0.29326 124 ALA A C   
847  O O   . ALA A 117 ? 0.60151 0.99216 0.64126 -0.27228 0.09175  -0.31267 124 ALA A O   
848  C CB  . ALA A 117 ? 0.50546 0.91218 0.56707 -0.27508 0.08637  -0.30145 124 ALA A CB  
849  N N   . GLY A 118 ? 0.57343 1.02256 0.60528 -0.23374 0.05154  -0.27360 125 GLY A N   
850  C CA  . GLY A 118 ? 0.65944 1.09752 0.67830 -0.23330 0.05471  -0.27663 125 GLY A CA  
851  C C   . GLY A 118 ? 0.49228 0.89349 0.51170 -0.20978 0.05113  -0.25923 125 GLY A C   
852  O O   . GLY A 118 ? 0.45558 0.85785 0.46227 -0.20525 0.04830  -0.25536 125 GLY A O   
853  N N   . ALA A 119 ? 0.36863 0.73816 0.40153 -0.19633 0.05109  -0.24881 126 ALA A N   
854  C CA  . ALA A 119 ? 0.33908 0.67248 0.37330 -0.17581 0.04794  -0.23404 126 ALA A CA  
855  C C   . ALA A 119 ? 0.31013 0.66470 0.32912 -0.15124 0.02176  -0.20310 126 ALA A C   
856  O O   . ALA A 119 ? 0.40358 0.79165 0.41507 -0.14526 0.00572  -0.19033 126 ALA A O   
857  C CB  . ALA A 119 ? 0.32207 0.61305 0.37441 -0.16887 0.05355  -0.22976 126 ALA A CB  
858  N N   . ASP A 120 ? 0.35481 0.68352 0.36882 -0.13620 0.01826  -0.19037 127 ASP A N   
859  C CA  . ASP A 120 ? 0.29841 0.62938 0.29520 -0.11205 -0.00488 -0.15688 127 ASP A CA  
860  C C   . ASP A 120 ? 0.26876 0.56453 0.27184 -0.09173 -0.01180 -0.13823 127 ASP A C   
861  O O   . ASP A 120 ? 0.25814 0.52873 0.28061 -0.09732 0.00139  -0.15369 127 ASP A O   
862  C CB  . ASP A 120 ? 0.37530 0.71354 0.35280 -0.11609 -0.00473 -0.15553 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.44534 0.76316 0.42900 -0.12328 0.01372  -0.17315 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.56883 0.87958 0.56702 -0.14165 0.03627  -0.20441 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.46884 0.77299 0.44319 -0.10972 0.00668  -0.15541 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.22378 0.50734 0.21055 -0.06836 -0.03167 -0.10419 128 ILE A N   
867  C CA  . ILE A 121 ? 0.21711 0.46574 0.20672 -0.04661 -0.04154 -0.08012 128 ILE A CA  
868  C C   . ILE A 121 ? 0.24629 0.47851 0.24343 -0.04912 -0.03283 -0.08963 128 ILE A C   
869  O O   . ILE A 121 ? 0.22548 0.43027 0.23858 -0.03658 -0.03453 -0.08029 128 ILE A O   
870  C CB  . ILE A 121 ? 0.23768 0.45553 0.20646 -0.02523 -0.05942 -0.04512 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.36858 0.59359 0.33934 -0.01918 -0.06759 -0.04030 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.20369 0.36963 0.16989 -0.00741 -0.06545 -0.02049 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.41000 0.62796 0.36417 -0.00562 -0.07899 -0.02153 128 ILE A CD1 
874  N N   . SER A 122 ? 0.28110 0.52472 0.27159 -0.06366 -0.02033 -0.10821 129 SER A N   
875  C CA  . SER A 122 ? 0.31872 0.53726 0.32111 -0.06161 -0.00555 -0.11712 129 SER A CA  
876  C C   . SER A 122 ? 0.28280 0.45430 0.32042 -0.05997 0.01928  -0.13189 129 SER A C   
877  O O   . SER A 122 ? 0.26830 0.39870 0.32404 -0.04436 0.03098  -0.12346 129 SER A O   
878  C CB  . SER A 122 ? 0.22501 0.46881 0.21310 -0.07970 0.00813  -0.14129 129 SER A CB  
879  O OG  . SER A 122 ? 0.30787 0.55420 0.30928 -0.09993 0.03167  -0.17699 129 SER A OG  
880  N N   . MET A 123 ? 0.22073 0.39692 0.26723 -0.07650 0.02667  -0.15307 130 MET A N   
881  C CA  . MET A 123 ? 0.24187 0.36691 0.31434 -0.07940 0.04998  -0.16725 130 MET A CA  
882  C C   . MET A 123 ? 0.23149 0.32349 0.31576 -0.06202 0.04150  -0.13874 130 MET A C   
883  O O   . MET A 123 ? 0.23742 0.28623 0.33774 -0.06742 0.05831  -0.14753 130 MET A O   
884  C CB  . MET A 123 ? 0.31219 0.45528 0.38437 -0.11267 0.06489  -0.20712 130 MET A CB  
885  C CG  . MET A 123 ? 0.43504 0.62707 0.48837 -0.12630 0.06469  -0.21908 130 MET A CG  
886  S SD  . MET A 123 ? 0.47433 0.68466 0.52846 -0.15604 0.08210  -0.24610 130 MET A SD  
887  C CE  . MET A 123 ? 0.48133 0.62078 0.55824 -0.15832 0.10557  -0.25563 130 MET A CE  
888  N N   . ILE A 124 ? 0.18600 0.29211 0.25843 -0.04177 0.01633  -0.10480 131 ILE A N   
889  C CA  . ILE A 124 ? 0.20251 0.28236 0.28081 -0.02512 0.00711  -0.07822 131 ILE A CA  
890  C C   . ILE A 124 ? 0.18457 0.19439 0.28083 -0.01278 0.02272  -0.06884 131 ILE A C   
891  O O   . ILE A 124 ? 0.18188 0.16110 0.28574 -0.01167 0.02725  -0.06145 131 ILE A O   
892  C CB  . ILE A 124 ? 0.18714 0.28530 0.24377 -0.00267 -0.02253 -0.04414 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.21866 0.29294 0.27765 0.01468  -0.03166 -0.01943 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.13417 0.21289 0.18261 0.01105  -0.02691 -0.02709 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.22718 0.31734 0.26016 0.03344  -0.05939 0.00894  131 ILE A CD1 
896  N N   . GLY A 125 ? 0.21216 0.19756 0.31507 -0.00322 0.03090  -0.06879 132 GLY A N   
897  C CA  . GLY A 125 ? 0.28776 0.20881 0.40811 0.01301  0.04178  -0.05765 132 GLY A CA  
898  C C   . GLY A 125 ? 0.32968 0.22253 0.45260 -0.00189 0.06002  -0.07301 132 GLY A C   
899  O O   . GLY A 125 ? 0.31900 0.18689 0.42698 0.00734  0.05348  -0.04968 132 GLY A O   
900  N N   . GLN A 126 ? 0.25760 0.16591 0.38548 -0.02753 0.07708  -0.11147 133 GLN A N   
901  C CA  . GLN A 126 ? 0.29904 0.18334 0.42463 -0.04172 0.09174  -0.12089 133 GLN A CA  
902  C C   . GLN A 126 ? 0.33598 0.21142 0.45673 -0.04991 0.08899  -0.11055 133 GLN A C   
903  O O   . GLN A 126 ? 0.33649 0.18659 0.45158 -0.05969 0.09913  -0.11399 133 GLN A O   
904  C CB  . GLN A 126 ? 0.33318 0.24393 0.45796 -0.06909 0.10753  -0.16033 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.38646 0.31159 0.51353 -0.06420 0.11308  -0.17482 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.37727 0.33332 0.49675 -0.09184 0.12606  -0.20994 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.50628 0.44933 0.62243 -0.10989 0.13700  -0.22220 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.55392 0.55259 0.66653 -0.09591 0.12405  -0.22420 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.26856 0.16362 0.39133 -0.04655 0.07552  -0.09958 134 PHE A N   
910  C CA  . PHE A 127 ? 0.30863 0.20210 0.43016 -0.05508 0.07420  -0.09118 134 PHE A CA  
911  C C   . PHE A 127 ? 0.29445 0.16547 0.40363 -0.02603 0.05758  -0.04989 134 PHE A C   
912  O O   . PHE A 127 ? 0.31272 0.18617 0.42144 -0.02849 0.05490  -0.04038 134 PHE A O   
913  C CB  . PHE A 127 ? 0.24025 0.20867 0.36297 -0.07255 0.06396  -0.10549 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.26116 0.26940 0.38424 -0.10174 0.07307  -0.14327 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.35208 0.35170 0.47450 -0.12852 0.09188  -0.16477 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.27424 0.32633 0.38869 -0.09733 0.06175  -0.14987 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.38430 0.41839 0.49956 -0.14892 0.09914  -0.19203 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.28194 0.36888 0.39237 -0.12532 0.07015  -0.18529 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.34053 0.41733 0.45008 -0.14652 0.08900  -0.20159 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.24354 0.10492 0.33542 -0.00339 0.04409  -0.02867 135 GLY A N   
921  C CA  . GLY A 128 ? 0.24774 0.10493 0.31016 0.01234  0.02567  -0.00230 135 GLY A CA  
922  C C   . GLY A 128 ? 0.26629 0.14763 0.31656 0.02234  0.01113  0.01270  135 GLY A C   
923  O O   . GLY A 128 ? 0.30864 0.19334 0.35096 0.02675  0.00636  0.02453  135 GLY A O   
924  N N   . VAL A 129 ? 0.20422 0.10541 0.26443 0.02556  0.00664  0.01073  136 VAL A N   
925  C CA  . VAL A 129 ? 0.20891 0.13527 0.24172 0.03676  -0.00860 0.02356  136 VAL A CA  
926  C C   . VAL A 129 ? 0.24449 0.19117 0.27015 0.04238  -0.01551 0.02668  136 VAL A C   
927  O O   . VAL A 129 ? 0.18393 0.16043 0.20004 0.04599  -0.02347 0.03121  136 VAL A O   
928  C CB  . VAL A 129 ? 0.21542 0.16875 0.28467 0.03942  -0.01598 0.02691  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.25074 0.18101 0.32721 0.03120  -0.00282 0.02714  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.19237 0.19522 0.27841 0.01718  -0.00992 -0.00432 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.21867 0.18549 0.23557 -0.01342 -0.01653 -0.03609 137 GLY A N   
932  C CA  . GLY A 130 ? 0.18192 0.15533 0.19082 -0.00371 -0.01468 -0.03587 137 GLY A CA  
933  C C   . GLY A 130 ? 0.20867 0.18994 0.21913 -0.00251 -0.00922 -0.02753 137 GLY A C   
934  O O   . GLY A 130 ? 0.17945 0.16877 0.18608 0.00339  -0.00744 -0.02531 137 GLY A O   
935  N N   . PHE A 131 ? 0.16740 0.14595 0.18293 -0.00787 -0.00681 -0.02276 138 PHE A N   
936  C CA  . PHE A 131 ? 0.20780 0.19116 0.22476 -0.00711 -0.00325 -0.01702 138 PHE A CA  
937  C C   . PHE A 131 ? 0.17196 0.16384 0.18970 -0.00509 -0.00318 -0.01647 138 PHE A C   
938  O O   . PHE A 131 ? 0.14102 0.13502 0.15778 -0.00179 -0.00109 -0.01226 138 PHE A O   
939  C CB  . PHE A 131 ? 0.21820 0.19851 0.23831 -0.01208 -0.00183 -0.01418 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.23399 0.21829 0.25540 -0.01158 -0.00001 -0.01150 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.17818 0.16100 0.19943 -0.01011 0.00075  -0.00878 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.18259 0.17230 0.20628 -0.01231 0.00042  -0.01230 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.18903 0.17180 0.21173 -0.01024 0.00100  -0.00782 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.19816 0.18826 0.22168 -0.01020 0.00137  -0.01141 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.21701 0.20166 0.23970 -0.00959 0.00120  -0.00962 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.14203 0.13916 0.16267 -0.00713 -0.00569 -0.02000 139 TYR A N   
947  C CA  . TYR A 132 ? 0.15896 0.16533 0.18084 -0.00381 -0.00593 -0.01909 139 TYR A CA  
948  C C   . TYR A 132 ? 0.17995 0.19088 0.19547 0.00347  -0.00703 -0.01865 139 TYR A C   
949  O O   . TYR A 132 ? 0.14885 0.16550 0.16375 0.00809  -0.00681 -0.01569 139 TYR A O   
950  C CB  . TYR A 132 ? 0.11658 0.13193 0.14553 -0.00780 -0.00844 -0.02267 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.15411 0.16813 0.18855 -0.01395 -0.00559 -0.02064 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.19480 0.21251 0.23020 -0.01162 -0.00232 -0.01785 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.17044 0.17836 0.20762 -0.02099 -0.00608 -0.02119 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.14523 0.16410 0.18305 -0.01547 0.00079  -0.01593 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.19305 0.20112 0.23366 -0.02580 -0.00259 -0.01722 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.19711 0.21231 0.23740 -0.02266 0.00106  -0.01470 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.19999 0.21773 0.24125 -0.02576 0.00495  -0.01078 139 TYR A OH  
958  N N   . SER A 133 ? 0.16608 0.17477 0.17571 0.00605  -0.00790 -0.02099 140 SER A N   
959  C CA  . SER A 133 ? 0.19657 0.21140 0.19800 0.01441  -0.00721 -0.01865 140 SER A CA  
960  C C   . SER A 133 ? 0.20536 0.21899 0.20716 0.01634  -0.00169 -0.00854 140 SER A C   
961  O O   . SER A 133 ? 0.14930 0.16893 0.14536 0.02285  0.00020  -0.00313 140 SER A O   
962  C CB  . SER A 133 ? 0.17537 0.18882 0.16939 0.01837  -0.00849 -0.02390 140 SER A CB  
963  O OG  . SER A 133 ? 0.19865 0.20588 0.19405 0.01738  -0.00442 -0.02038 140 SER A OG  
964  N N   . ALA A 134 ? 0.15009 0.15626 0.15851 0.01062  0.00056  -0.00561 141 ALA A N   
965  C CA  . ALA A 134 ? 0.17062 0.17380 0.18200 0.01036  0.00411  0.00282  141 ALA A CA  
966  C C   . ALA A 134 ? 0.16205 0.16607 0.17209 0.01453  0.00397  0.00712  141 ALA A C   
967  O O   . ALA A 134 ? 0.15460 0.15689 0.16451 0.01655  0.00691  0.01591  141 ALA A O   
968  C CB  . ALA A 134 ? 0.16036 0.15549 0.17834 0.00378  0.00415  0.00219  141 ALA A CB  
969  N N   . TYR A 135 ? 0.15884 0.16628 0.16878 0.01610  0.00067  0.00201  142 TYR A N   
970  C CA  . TYR A 135 ? 0.16844 0.17736 0.17713 0.02208  -0.00000 0.00580  142 TYR A CA  
971  C C   . TYR A 135 ? 0.19822 0.21671 0.19861 0.03029  -0.00066 0.00941  142 TYR A C   
972  O O   . TYR A 135 ? 0.17925 0.20018 0.17725 0.03709  -0.00169 0.01347  142 TYR A O   
973  C CB  . TYR A 135 ? 0.16579 0.17929 0.17901 0.02180  -0.00293 -0.00064 142 TYR A CB  
974  C CG  . TYR A 135 ? 0.19985 0.20416 0.21818 0.01679  -0.00138 -0.00224 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.17364 0.16817 0.19262 0.01994  -0.00056 0.00073  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.17102 0.17494 0.19210 0.00975  -0.00113 -0.00671 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.18226 0.16863 0.20367 0.01661  -0.00012 -0.00262 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.15262 0.15004 0.17587 0.00658  0.00005  -0.00809 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.16095 0.15043 0.18390 0.01022  0.00029  -0.00692 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.18347 0.16698 0.20650 0.00833  0.00046  -0.01024 142 TYR A OH  
981  N N   . LEU A 136 ? 0.18965 0.21393 0.18426 0.03145  -0.00021 0.00796  143 LEU A N   
982  C CA  . LEU A 136 ? 0.18716 0.22096 0.17117 0.04070  0.00050  0.01312  143 LEU A CA  
983  C C   . LEU A 136 ? 0.21043 0.23924 0.19397 0.04271  0.00667  0.02784  143 LEU A C   
984  O O   . LEU A 136 ? 0.18667 0.22124 0.16220 0.05117  0.00775  0.03604  143 LEU A O   
985  C CB  . LEU A 136 ? 0.17879 0.21943 0.15553 0.04283  -0.00001 0.00701  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.16951 0.21399 0.14492 0.04175  -0.00737 -0.00748 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.21711 0.26179 0.18557 0.04403  -0.00735 -0.01372 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.20264 0.25964 0.17191 0.04901  -0.01340 -0.01089 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.15988 0.17829 0.15239 0.03473  0.01032  0.03195  144 VAL A N   
990  C CA  . VAL A 137 ? 0.19442 0.20851 0.18965 0.03383  0.01607  0.04628  144 VAL A CA  
991  C C   . VAL A 137 ? 0.17049 0.16704 0.17649 0.02654  0.01559  0.04903  144 VAL A C   
992  O O   . VAL A 137 ? 0.21906 0.20756 0.22915 0.02476  0.01888  0.06109  144 VAL A O   
993  C CB  . VAL A 137 ? 0.20065 0.22326 0.19748 0.03143  0.02108  0.04976  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.20671 0.24579 0.19001 0.04143  0.02185  0.04726  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.13607 0.15413 0.14145 0.02319  0.01912  0.04049  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.20465 0.19476 0.21509 0.02237  0.01144  0.03812  145 ALA A N   
997  C CA  . ALA A 138 ? 0.17878 0.15271 0.19743 0.01645  0.01007  0.03753  145 ALA A CA  
998  C C   . ALA A 138 ? 0.18758 0.15488 0.20395 0.02218  0.00658  0.03305  145 ALA A C   
999  O O   . ALA A 138 ? 0.24559 0.22313 0.25863 0.02607  0.00422  0.02528  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.16681 0.14008 0.19116 0.00852  0.00861  0.02904  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.16326 0.11348 0.18257 0.02271  0.00604  0.03784  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.21434 0.15695 0.23191 0.02953  0.00275  0.03223  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.23608 0.17402 0.25708 0.02517  0.00026  0.02046  146 GLU A C   
1004 O O   . GLU A 139 ? 0.22667 0.16705 0.24563 0.03148  -0.00154 0.01332  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.24570 0.16818 0.26344 0.03390  0.00252  0.04137  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.39560 0.30100 0.42128 0.02370  0.00357  0.04845  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.69598 0.57755 0.72261 0.02724  0.00294  0.05847  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.59673 0.48067 0.61669 0.03682  0.00485  0.06846  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.68944 0.54891 0.72308 0.02078  -0.00017 0.05616  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.22768 0.16150 0.25365 0.01548  0.00027  0.01874  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.20413 0.13493 0.23131 0.01192  -0.00229 0.00826  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.18042 0.11947 0.21112 0.00316  -0.00146 0.00771  147 LYS A C   
1013 O O   . LYS A 140 ? 0.16603 0.10582 0.20138 -0.00164 0.00031  0.01530  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.21730 0.12620 0.24659 0.01146  -0.00591 0.00560  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.24777 0.15394 0.27586 0.00913  -0.00930 -0.00609 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.30530 0.18800 0.33319 0.01139  -0.01423 -0.01127 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.42877 0.29968 0.46462 -0.00002 -0.01847 -0.01175 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.50682 0.35018 0.54439 0.00058  -0.02399 -0.01486 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.14542 0.09221 0.17400 0.00199  -0.00219 -0.00010 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.15865 0.11218 0.18950 -0.00442 -0.00198 -0.00091 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.21924 0.16827 0.24912 -0.00665 -0.00522 -0.00845 148 VAL A C   
1022 O O   . VAL A 141 ? 0.14273 0.09273 0.16735 -0.00221 -0.00558 -0.01436 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.16523 0.13223 0.19296 -0.00331 0.00014  -0.00163 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.18708 0.15816 0.21635 -0.00808 0.00008  -0.00226 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.12803 0.10067 0.15434 0.00035  0.00216  0.00391  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.19277 0.13942 0.22775 -0.01282 -0.00762 -0.00815 149 THR A N   
1027 C CA  . THR A 142 ? 0.22825 0.17356 0.26117 -0.01466 -0.01175 -0.01551 149 THR A CA  
1028 C C   . THR A 142 ? 0.21501 0.17220 0.24860 -0.01742 -0.01098 -0.01385 149 THR A C   
1029 O O   . THR A 142 ? 0.23834 0.20090 0.27869 -0.02062 -0.00959 -0.00794 149 THR A O   
1030 C CB  . THR A 142 ? 0.22165 0.15456 0.26098 -0.01956 -0.01738 -0.01796 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.27329 0.19107 0.31219 -0.01632 -0.01809 -0.01823 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.29435 0.22653 0.32866 -0.01951 -0.02312 -0.02797 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.18234 0.14417 0.20856 -0.01511 -0.01138 -0.01819 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.18013 0.15039 0.20549 -0.01628 -0.01118 -0.01621 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.19878 0.16973 0.22042 -0.01644 -0.01637 -0.02153 150 VAL A C   
1036 O O   . VAL A 143 ? 0.22943 0.19951 0.24197 -0.01260 -0.01692 -0.02652 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.19144 0.16638 0.21108 -0.01369 -0.00689 -0.01429 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.19187 0.17113 0.20992 -0.01401 -0.00717 -0.01162 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.17729 0.15274 0.19991 -0.01313 -0.00359 -0.01111 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.14471 0.11975 0.17329 -0.02007 -0.02027 -0.02057 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.17206 0.15117 0.19747 -0.01988 -0.02660 -0.02560 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.19380 0.18254 0.21594 -0.01706 -0.02509 -0.02068 151 ILE A C   
1043 O O   . ILE A 144 ? 0.17048 0.16368 0.19972 -0.01781 -0.02240 -0.01477 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.18155 0.16072 0.21955 -0.02645 -0.03342 -0.02809 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.31728 0.28313 0.36166 -0.03030 -0.03355 -0.02918 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.21194 0.19455 0.24498 -0.02568 -0.04216 -0.03656 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.26980 0.22306 0.30481 -0.02699 -0.03777 -0.03929 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.16015 0.15184 0.17057 -0.01261 -0.02662 -0.02268 152 THR A N   
1049 C CA  . THR A 145 ? 0.22713 0.22437 0.23311 -0.00903 -0.02468 -0.01631 152 THR A CA  
1050 C C   . THR A 145 ? 0.21844 0.22239 0.21433 -0.00465 -0.03003 -0.01866 152 THR A C   
1051 O O   . THR A 145 ? 0.17768 0.18131 0.16482 -0.00272 -0.03285 -0.02536 152 THR A O   
1052 C CB  . THR A 145 ? 0.22237 0.21459 0.22266 -0.00751 -0.01716 -0.01110 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.23286 0.22553 0.23155 -0.00496 -0.01564 -0.00434 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.22078 0.21335 0.20953 -0.00479 -0.01506 -0.01295 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.15492 0.16554 0.15107 -0.00154 -0.03176 -0.01346 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.18745 0.20626 0.17274 0.00435  -0.03697 -0.01365 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.20944 0.22746 0.18923 0.00986  -0.03306 -0.00309 153 LYS A C   
1058 O O   . LYS A 146 ? 0.18826 0.20776 0.17713 0.01076  -0.03317 0.00084  153 LYS A O   
1059 C CB  . LYS A 146 ? 0.17337 0.20363 0.16752 0.00291  -0.04705 -0.01962 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.17120 0.21296 0.15400 0.01041  -0.05393 -0.01983 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.21874 0.25997 0.18404 0.01414  -0.05662 -0.02705 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.24250 0.29760 0.19485 0.02265  -0.06470 -0.02792 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.20496 0.26163 0.14696 0.03068  -0.05921 -0.01398 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.19021 0.20577 0.15523 0.01407  -0.02939 0.00192  154 HIS A N   
1065 C CA  . HIS A 147 ? 0.21482 0.22640 0.17280 0.01926  -0.02604 0.01332  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.25627 0.27878 0.20181 0.02764  -0.03204 0.01541  154 HIS A C   
1067 O O   . HIS A 147 ? 0.21685 0.24855 0.15414 0.02939  -0.03657 0.00824  154 HIS A O   
1068 C CB  . HIS A 147 ? 0.19086 0.19329 0.14255 0.01685  -0.01715 0.01995  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.19070 0.18332 0.13817 0.01947  -0.01310 0.03262  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.23039 0.22577 0.16414 0.02658  -0.01339 0.04188  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.23508 0.21323 0.18960 0.01603  -0.00905 0.03755  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.25658 0.23765 0.19018 0.02691  -0.00940 0.05309  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.22086 0.19066 0.16719 0.02031  -0.00718 0.04964  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.24576 0.26701 0.18902 0.03412  -0.03284 0.02460  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.25420 0.28736 0.18494 0.04377  -0.03921 0.02777  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.26893 0.30539 0.17994 0.04736  -0.03640 0.03100  155 ASN A C   
1077 O O   . ASN A 148 ? 0.27128 0.32194 0.17024 0.05444  -0.04342 0.02762  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.26796 0.29570 0.19723 0.05197  -0.03899 0.03967  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.30771 0.34241 0.25333 0.05371  -0.04444 0.03552  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.30356 0.35305 0.26023 0.04982  -0.05076 0.02513  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.29525 0.31965 0.24285 0.06001  -0.04208 0.04397  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.26631 0.29241 0.17393 0.04300  -0.02643 0.03727  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.27282 0.30452 0.16235 0.04704  -0.02127 0.04348  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.34446 0.38352 0.23135 0.04419  -0.02015 0.03154  156 ASP A C   
1085 O O   . ASP A 149 ? 0.32257 0.36764 0.19632 0.04718  -0.01349 0.03653  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.31232 0.33086 0.20101 0.04388  -0.01045 0.05988  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.43166 0.43894 0.31966 0.04875  -0.01150 0.07261  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.36843 0.38372 0.25104 0.05786  -0.01970 0.07151  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.44556 0.43562 0.33905 0.04371  -0.00482 0.08319  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.28126 0.32016 0.18019 0.03921  -0.02605 0.01675  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.26392 0.30579 0.16061 0.03762  -0.02546 0.00502  157 ASP A CA  
1092 C C   . ASP A 150 ? 0.33077 0.37391 0.23610 0.03518  -0.03663 -0.01100 157 ASP A C   
1093 O O   . ASP A 150 ? 0.26556 0.31069 0.18031 0.03382  -0.04392 -0.01207 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.23827 0.27108 0.14563 0.02997  -0.01581 0.00796  157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.27312 0.31276 0.17153 0.03282  -0.01089 0.00296  157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.27765 0.32600 0.16230 0.04040  -0.01615 -0.00650 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.30172 0.33911 0.20694 0.02821  -0.00223 0.00771  157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.24569 0.28798 0.14861 0.03478  -0.03796 -0.02315 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.28928 0.32869 0.20135 0.03086  -0.04841 -0.03840 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.23529 0.26249 0.16821 0.02069  -0.04537 -0.03856 158 GLU A C   
1101 O O   . GLU A 151 ? 0.23730 0.25917 0.17572 0.01773  -0.03595 -0.02921 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.33604 0.37691 0.23353 0.03703  -0.05222 -0.05234 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.51060 0.56583 0.38373 0.04914  -0.05477 -0.05296 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.81894 0.88401 0.69086 0.05116  -0.06595 -0.05355 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.85690 0.91924 0.74558 0.04368  -0.07590 -0.06174 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 0.87373 0.95074 0.72862 0.06038  -0.06473 -0.04490 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.22015 0.24315 0.16478 0.01510  -0.05391 -0.04919 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.23405 0.24651 0.19736 0.00612  -0.05130 -0.04847 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.23291 0.23473 0.19287 0.00690  -0.04643 -0.05330 159 GLN A C   
1110 O O   . GLN A 152 ? 0.24183 0.24029 0.19266 0.01103  -0.05144 -0.06489 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.24483 0.25744 0.22379 -0.00124 -0.06164 -0.05559 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.19635 0.20245 0.19537 -0.01023 -0.05783 -0.05030 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.27610 0.28949 0.29361 -0.01807 -0.06612 -0.05194 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.27463 0.30284 0.29495 -0.01635 -0.06979 -0.04876 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.26380 0.26762 0.29518 -0.02668 -0.06885 -0.05577 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.17338 0.17019 0.14060 0.00394  -0.03746 -0.04538 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.20613 0.19594 0.17133 0.00585  -0.03229 -0.04825 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.23882 0.21884 0.21979 -0.00091 -0.03062 -0.04597 160 TYR A C   
1119 O O   . TYR A 153 ? 0.21884 0.20006 0.21088 -0.00643 -0.02979 -0.03911 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.19255 0.18984 0.14944 0.01017  -0.02240 -0.04014 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.25623 0.26376 0.19494 0.01882  -0.02193 -0.04217 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.27409 0.28309 0.20227 0.02648  -0.02140 -0.05116 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.24829 0.26452 0.17905 0.02095  -0.02181 -0.03474 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.30793 0.32898 0.21751 0.03603  -0.02020 -0.05293 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.28544 0.31276 0.19761 0.02989  -0.02078 -0.03507 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.37128 0.40206 0.27260 0.03740  -0.01971 -0.04431 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.46914 0.51356 0.35005 0.04792  -0.01790 -0.04461 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.18226 0.15333 0.16288 0.00120  -0.02984 -0.05144 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.17442 0.13611 0.16709 -0.00310 -0.02761 -0.04826 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.21884 0.18287 0.20804 0.00194  -0.01990 -0.04542 161 ALA A C   
1131 O O   . ALA A 154 ? 0.20658 0.17103 0.18659 0.00945  -0.01915 -0.05166 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.22037 0.16692 0.21795 -0.00521 -0.03497 -0.05653 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.16579 0.13314 0.16242 -0.00147 -0.01463 -0.03678 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.15417 0.12531 0.15156 0.00160  -0.00873 -0.03392 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.21352 0.17482 0.21867 0.00075  -0.00964 -0.03299 162 TRP A C   
1136 O O   . TRP A 155 ? 0.21159 0.16717 0.22389 -0.00470 -0.01193 -0.02983 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.16296 0.14362 0.16278 -0.00181 -0.00385 -0.02600 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.16774 0.15504 0.17161 -0.00119 0.00096  -0.02275 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.14165 0.14071 0.14405 -0.00003 0.00558  -0.02061 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.16396 0.14909 0.17487 -0.00222 0.00122  -0.02064 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.15812 0.16279 0.16793 -0.00103 0.00767  -0.01853 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.17327 0.16931 0.18690 -0.00150 0.00474  -0.01895 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.17817 0.15504 0.19344 -0.00354 -0.00103 -0.01926 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.15388 0.15263 0.17313 -0.00122 0.00472  -0.01758 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.16693 0.14608 0.18596 -0.00239 0.00023  -0.01653 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.18978 0.17968 0.21013 -0.00083 0.00243  -0.01651 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.14885 0.10964 0.15273 0.00688  -0.00755 -0.03477 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.14615 0.09665 0.15567 0.00767  -0.00846 -0.03251 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.16429 0.12273 0.17374 0.01452  -0.00465 -0.03115 163 GLU A C   
1150 O O   . GLU A 156 ? 0.16295 0.13029 0.16777 0.02090  -0.00258 -0.03534 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.24048 0.17268 0.24900 0.00931  -0.01417 -0.03876 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.25834 0.17660 0.27344 0.00870  -0.01510 -0.03365 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.44843 0.34529 0.46582 0.00622  -0.02177 -0.03855 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.43065 0.31453 0.44238 0.01427  -0.02457 -0.04608 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.40890 0.30221 0.43456 -0.00368 -0.02457 -0.03528 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.17542 0.13332 0.19005 0.01390  -0.00371 -0.02502 164 SER A N   
1157 C CA  . SER A 157 ? 0.17430 0.14105 0.18979 0.02104  -0.00162 -0.02386 164 SER A CA  
1158 C C   . SER A 157 ? 0.17699 0.13624 0.19519 0.02260  -0.00250 -0.01757 164 SER A C   
1159 O O   . SER A 157 ? 0.19131 0.14923 0.21201 0.01650  -0.00226 -0.01201 164 SER A O   
1160 C CB  . SER A 157 ? 0.13292 0.11955 0.15126 0.01827  0.00153  -0.02217 164 SER A CB  
1161 O OG  . SER A 157 ? 0.15244 0.15102 0.17373 0.02488  0.00248  -0.02179 164 SER A OG  
1162 N N   . SER A 158 ? 0.19425 0.14979 0.21116 0.03216  -0.00311 -0.01786 165 SER A N   
1163 C CA  . SER A 158 ? 0.17375 0.12707 0.19162 0.03642  -0.00332 -0.01043 165 SER A CA  
1164 C C   . SER A 158 ? 0.21537 0.19053 0.23467 0.04193  -0.00231 -0.01005 165 SER A C   
1165 O O   . SER A 158 ? 0.24201 0.21828 0.26040 0.05080  -0.00329 -0.00634 165 SER A O   
1166 C CB  . SER A 158 ? 0.23284 0.16510 0.24846 0.04424  -0.00560 -0.00970 165 SER A CB  
1167 O OG  . SER A 158 ? 0.29342 0.20524 0.31026 0.03689  -0.00783 -0.01013 165 SER A OG  
1168 N N   . ALA A 159 ? 0.16390 0.15636 0.18616 0.03664  -0.00092 -0.01349 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.18047 0.19602 0.20752 0.03908  -0.00082 -0.01452 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.23236 0.25517 0.26037 0.05063  -0.00035 -0.01770 166 ALA A C   
1171 O O   . ALA A 159 ? 0.30213 0.31585 0.32656 0.05416  0.00086  -0.02186 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.22563 0.24655 0.25249 0.03964  -0.00306 -0.01000 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.25815 0.29851 0.29048 0.05786  -0.00172 -0.01672 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.20113 0.25152 0.23527 0.07060  -0.00095 -0.01970 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.26995 0.34020 0.30981 0.06882  0.00305  -0.02434 167 GLY A C   
1176 O O   . GLY A 160 ? 0.23387 0.31187 0.27362 0.08057  0.00496  -0.02773 167 GLY A O   
1177 N N   . GLY A 161 ? 0.16710 0.24535 0.21135 0.05527  0.00482  -0.02394 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.15255 0.25337 0.20411 0.05194  0.00939  -0.02519 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.14365 0.23547 0.18750 0.05012  0.01354  -0.02727 168 GLY A C   
1180 O O   . GLY A 161 ? 0.12624 0.23772 0.17491 0.04750  0.01853  -0.02641 168 GLY A O   
1181 N N   . SER A 162 ? 0.16388 0.22848 0.19646 0.05113  0.01151  -0.02947 169 SER A N   
1182 C CA  . SER A 162 ? 0.13666 0.19404 0.16056 0.05095  0.01389  -0.03297 169 SER A CA  
1183 C C   . SER A 162 ? 0.18966 0.22255 0.20736 0.04249  0.01044  -0.03266 169 SER A C   
1184 O O   . SER A 162 ? 0.16846 0.18666 0.18701 0.03992  0.00674  -0.03035 169 SER A O   
1185 C CB  . SER A 162 ? 0.16281 0.21615 0.17865 0.06655  0.01428  -0.04009 169 SER A CB  
1186 O OG  . SER A 162 ? 0.21356 0.23896 0.22361 0.07138  0.00880  -0.04284 169 SER A OG  
1187 N N   . PHE A 163 ? 0.18156 0.21295 0.19316 0.03882  0.01199  -0.03424 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.19018 0.20184 0.19618 0.03252  0.00827  -0.03515 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.19821 0.20644 0.19311 0.03797  0.00793  -0.04198 170 PHE A C   
1190 O O   . PHE A 163 ? 0.17568 0.19959 0.16650 0.04533  0.01224  -0.04424 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.15809 0.17270 0.16838 0.02047  0.00902  -0.02884 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.12249 0.15344 0.13274 0.01708  0.01390  -0.02556 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.19957 0.24932 0.21912 0.01457  0.01777  -0.02127 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.16604 0.19410 0.16775 0.01579  0.01427  -0.02579 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.19779 0.26178 0.21919 0.00975  0.02286  -0.01599 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.14982 0.19213 0.15071 0.01290  0.01950  -0.02024 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.16841 0.22791 0.17975 0.00921  0.02425  -0.01462 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.17631 0.16586 0.16645 0.03479  0.00255  -0.04556 171 THR A N   
1199 C CA  . THR A 164 ? 0.17267 0.15801 0.15116 0.03957  0.00003  -0.05376 171 THR A CA  
1200 C C   . THR A 164 ? 0.16715 0.15192 0.14367 0.03059  -0.00194 -0.05103 171 THR A C   
1201 O O   . THR A 164 ? 0.15501 0.13532 0.13955 0.02130  -0.00310 -0.04481 171 THR A O   
1202 C CB  . THR A 164 ? 0.20750 0.16995 0.18201 0.04522  -0.00703 -0.06338 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.24540 0.19104 0.22784 0.03506  -0.01205 -0.06002 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.20386 0.16447 0.17938 0.05645  -0.00548 -0.06571 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.18226 0.17333 0.14701 0.03511  -0.00215 -0.05564 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.20787 0.19887 0.16827 0.02950  -0.00529 -0.05419 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.20617 0.19057 0.15348 0.03658  -0.01215 -0.06666 172 VAL A C   
1208 O O   . VAL A 165 ? 0.21883 0.20861 0.15509 0.04788  -0.01047 -0.07393 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.18680 0.19600 0.14456 0.02754  0.00186  -0.04431 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.23214 0.24094 0.18279 0.02481  -0.00203 -0.04294 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.18586 0.19849 0.15723 0.01932  0.00649  -0.03408 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.20144 0.17546 0.15038 0.03049  -0.02037 -0.06998 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.22324 0.19111 0.16060 0.03565  -0.02921 -0.08322 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.22015 0.19108 0.15910 0.02832  -0.03520 -0.08113 173 ARG A C   
1215 O O   . ARG A 166 ? 0.20263 0.17459 0.15423 0.01904  -0.03366 -0.07111 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.24173 0.18693 0.18337 0.03624  -0.03703 -0.09434 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.29061 0.22230 0.25056 0.02310  -0.04123 -0.08905 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.40669 0.31550 0.37275 0.02348  -0.04536 -0.09448 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.43202 0.34037 0.40146 0.02808  -0.03744 -0.08778 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.59073 0.48280 0.56231 0.03251  -0.03822 -0.08978 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.45033 0.32641 0.42213 0.03098  -0.04446 -0.09518 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.50648 0.40152 0.48075 0.03805  -0.03167 -0.08381 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.23902 0.21301 0.16415 0.03406  -0.04234 -0.09126 174 THR A N   
1224 C CA  . THR A 167 ? 0.26724 0.24403 0.19489 0.02804  -0.05092 -0.09203 174 THR A CA  
1225 C C   . THR A 167 ? 0.29252 0.25315 0.23843 0.01713  -0.05933 -0.09608 174 THR A C   
1226 O O   . THR A 167 ? 0.30058 0.24528 0.24906 0.01736  -0.06338 -0.10459 174 THR A O   
1227 C CB  . THR A 167 ? 0.34629 0.33025 0.25387 0.03775  -0.05845 -0.10416 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.39269 0.39381 0.28336 0.04798  -0.04875 -0.09758 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.44024 0.43058 0.35148 0.03212  -0.06808 -0.10448 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.28494 0.25072 0.24513 0.00750  -0.06009 -0.08692 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.30357 0.25853 0.28390 -0.00397 -0.06553 -0.08680 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.46490 0.41987 0.44824 -0.00799 -0.07747 -0.09608 175 ASP A C   
1233 O O   . ASP A 168 ? 0.39018 0.35985 0.36679 -0.00541 -0.08247 -0.09806 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.32187 0.28597 0.31664 -0.01116 -0.05937 -0.07190 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.44307 0.40012 0.45912 -0.02262 -0.06289 -0.06927 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.47721 0.41787 0.49850 -0.02506 -0.06246 -0.07096 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.37608 0.34504 0.40397 -0.02864 -0.06574 -0.06452 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.50074 0.44062 0.49403 -0.01405 -0.08027 -0.09899 176 THR A N   
1239 C CA  . THR A 169 ? 0.66488 0.60425 0.66424 -0.02016 -0.08985 -0.10554 176 THR A CA  
1240 C C   . THR A 169 ? 0.66023 0.60157 0.68352 -0.03447 -0.09117 -0.09730 176 THR A C   
1241 O O   . THR A 169 ? 0.67690 0.61769 0.70859 -0.04179 -0.09890 -0.10205 176 THR A O   
1242 C CB  . THR A 169 ? 0.76666 0.68740 0.75897 -0.01662 -0.09331 -0.11617 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.63736 0.54166 0.63376 -0.01644 -0.08641 -0.11138 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.61160 0.53738 0.58025 -0.00216 -0.09459 -0.12636 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.56916 0.51414 0.60365 -0.03848 -0.08364 -0.08512 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.59357 0.54474 0.65009 -0.05049 -0.08293 -0.07563 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.43859 0.41277 0.50269 -0.05363 -0.08872 -0.07496 177 GLY A C   
1248 O O   . GLY A 170 ? 0.38699 0.36986 0.43923 -0.04768 -0.09544 -0.08312 177 GLY A O   
1249 N N   . GLU A 171 ? 0.49188 0.47789 0.57577 -0.06205 -0.08568 -0.06433 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.42164 0.43290 0.51600 -0.06434 -0.09027 -0.06187 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.23607 0.25906 0.31777 -0.05313 -0.09015 -0.06157 178 GLU A C   
1252 O O   . GLU A 171 ? 0.25163 0.26947 0.32828 -0.04834 -0.08241 -0.05587 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.35144 0.37526 0.46873 -0.07294 -0.08416 -0.04888 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.45430 0.48020 0.58909 -0.08559 -0.08737 -0.04847 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.35062 0.38526 0.48500 -0.08821 -0.09963 -0.05967 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.41957 0.47983 0.56036 -0.08684 -0.10370 -0.05848 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.42749 0.44385 0.55513 -0.09095 -0.10553 -0.06964 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.37628 0.41418 0.45090 -0.04811 -0.09832 -0.06717 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.37854 0.42944 0.44156 -0.03678 -0.09718 -0.06354 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.39381 0.45434 0.46824 -0.03652 -0.08648 -0.04859 179 PRO A C   
1261 O O   . PRO A 172 ? 0.38130 0.45387 0.47854 -0.04464 -0.08725 -0.04379 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.43967 0.50879 0.49991 -0.03384 -0.10795 -0.06902 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.53621 0.59211 0.59137 -0.03893 -0.11396 -0.08057 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.45529 0.48964 0.52001 -0.04786 -0.10760 -0.07931 179 PRO A CD  
1265 N N   . MET A 173 ? 0.23373 0.28970 0.29238 -0.02694 -0.07655 -0.04135 180 MET A N   
1266 C CA  . MET A 173 ? 0.26713 0.32942 0.33304 -0.02456 -0.06714 -0.02936 180 MET A CA  
1267 C C   . MET A 173 ? 0.35235 0.43173 0.41583 -0.01560 -0.06899 -0.02442 180 MET A C   
1268 O O   . MET A 173 ? 0.46426 0.55442 0.53910 -0.01378 -0.06458 -0.01669 180 MET A O   
1269 C CB  . MET A 173 ? 0.31903 0.36460 0.37169 -0.02029 -0.05598 -0.02459 180 MET A CB  
1270 C CG  . MET A 173 ? 0.57105 0.59992 0.62381 -0.02606 -0.05317 -0.02819 180 MET A CG  
1271 S SD  . MET A 173 ? 0.58418 0.60273 0.63176 -0.02291 -0.04034 -0.01992 180 MET A SD  
1272 C CE  . MET A 173 ? 0.45212 0.48503 0.51656 -0.02408 -0.03667 -0.01107 180 MET A CE  
1273 N N   . GLY A 174 ? 0.26063 0.34286 0.30814 -0.00832 -0.07499 -0.02824 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.26294 0.35795 0.30479 0.00236  -0.07600 -0.02175 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.21609 0.29626 0.24113 0.01056  -0.06576 -0.01320 181 GLY A C   
1276 O O   . GLY A 174 ? 0.20717 0.28356 0.21323 0.01803  -0.06622 -0.01156 181 GLY A O   
1277 N N   . ARG A 175 ? 0.14762 0.21962 0.17963 0.00888  -0.05666 -0.00755 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.16710 0.22214 0.18626 0.01364  -0.04758 -0.00107 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.19365 0.24142 0.22275 0.00932  -0.03997 0.00083  182 ARG A C   
1280 O O   . ARG A 175 ? 0.16681 0.22611 0.21051 0.00894  -0.03981 0.00232  182 ARG A O   
1281 C CB  . ARG A 175 ? 0.15426 0.21093 0.16545 0.02502  -0.04742 0.00691  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.16856 0.20459 0.16733 0.02810  -0.03912 0.01366  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.16730 0.19970 0.16352 0.03866  -0.03803 0.02167  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.15928 0.19989 0.17032 0.04086  -0.03737 0.02059  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.16108 0.22108 0.18112 0.04769  -0.04245 0.02132  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.17062 0.24349 0.18644 0.05288  -0.04997 0.02243  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.15684 0.22616 0.19035 0.05020  -0.03998 0.02099  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.26958 0.28590 0.15491 0.08042  -0.02340 0.06049  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.23164 0.24213 0.15417 0.06775  -0.01367 0.05408  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.21805 0.21562 0.14016 0.05469  -0.00687 0.04041  183 GLY A C   
1291 O O   . GLY A 176 ? 0.25846 0.24595 0.15263 0.05900  -0.00153 0.03947  183 GLY A O   
1292 N N   . THR A 177 ? 0.20488 0.20335 0.15618 0.04173  -0.00588 0.03121  184 THR A N   
1293 C CA  . THR A 177 ? 0.18794 0.17755 0.14466 0.03160  0.00056  0.02134  184 THR A CA  
1294 C C   . THR A 177 ? 0.27357 0.27115 0.24705 0.01926  -0.01058 0.00828  184 THR A C   
1295 O O   . THR A 177 ? 0.17825 0.18642 0.17112 0.01649  -0.01474 0.00903  184 THR A O   
1296 C CB  . THR A 177 ? 0.18760 0.16676 0.16319 0.02818  0.01762  0.02872  184 THR A CB  
1297 O OG1 . THR A 177 ? 0.22842 0.19911 0.18966 0.03784  0.03103  0.04384  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.20414 0.18427 0.19220 0.01897  0.02149  0.02081  184 THR A CG2 
1299 N N   . LYS A 178 ? 0.15883 0.14901 0.12274 0.01419  -0.01276 -0.00193 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.18178 0.17324 0.15780 0.00254  -0.02094 -0.01197 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.21162 0.19323 0.19366 0.00136  -0.01080 -0.01443 185 LYS A C   
1302 O O   . LYS A 178 ? 0.22628 0.19654 0.19070 0.00848  -0.00437 -0.01602 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.26165 0.24830 0.21686 -0.00245 -0.03643 -0.02165 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.37703 0.35601 0.34045 -0.01583 -0.04281 -0.03060 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.48728 0.46336 0.43679 -0.02722 -0.06236 -0.03952 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.52412 0.49345 0.43659 -0.01827 -0.07011 -0.04307 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.67103 0.62427 0.56101 -0.02930 -0.08419 -0.05657 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.15862 0.14611 0.16348 -0.00508 -0.00902 -0.01382 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.16485 0.15046 0.17910 -0.00603 -0.00325 -0.01423 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.23318 0.21298 0.24665 -0.01143 -0.00984 -0.02006 186 VAL A C   
1311 O O   . VAL A 179 ? 0.16310 0.14888 0.18605 -0.01839 -0.01441 -0.02035 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.16495 0.15834 0.19920 -0.01047 0.00051  -0.01003 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.15042 0.15033 0.19706 -0.01219 0.00156  -0.00942 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.14747 0.13991 0.18359 -0.00769 0.00863  -0.00220 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.18268 0.14814 0.18319 -0.00643 -0.00778 -0.02316 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.17148 0.12190 0.16733 -0.01084 -0.01218 -0.02699 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.17856 0.13330 0.18582 -0.00468 -0.00655 -0.02120 187 ILE A C   
1318 O O   . ILE A 180 ? 0.19094 0.14571 0.19696 0.00747  0.00137  -0.01813 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.18728 0.10851 0.15447 -0.00827 -0.01453 -0.03567 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.21862 0.14175 0.17318 -0.01479 -0.02481 -0.04121 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.22851 0.12582 0.19123 -0.01514 -0.01801 -0.03837 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.33826 0.22918 0.25440 -0.01179 -0.02942 -0.05309 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.16547 0.12720 0.18351 -0.01116 -0.01023 -0.01810 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.15573 0.12511 0.18201 -0.00544 -0.00913 -0.01161 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.21622 0.16175 0.23024 -0.00180 -0.00817 -0.00918 188 LEU A C   
1326 O O   . LEU A 181 ? 0.17703 0.11334 0.18754 -0.01120 -0.01070 -0.00824 188 LEU A O   
1327 C CB  . LEU A 181 ? 0.14569 0.13191 0.18105 -0.01255 -0.01381 -0.01004 188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.18091 0.17899 0.22439 -0.01754 -0.01420 -0.01334 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.23729 0.24026 0.27922 -0.02262 -0.01808 -0.01506 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.13294 0.14328 0.18947 -0.01409 -0.01161 -0.01017 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.21304 0.14786 0.22161 0.01302  -0.00229 -0.00610 189 HIS A N   
1332 C CA  . HIS A 182 ? 0.19163 0.09766 0.18699 0.02066  0.00065  -0.00139 189 HIS A CA  
1333 C C   . HIS A 182 ? 0.20669 0.13445 0.21422 0.02666  -0.00217 0.01113  189 HIS A C   
1334 O O   . HIS A 182 ? 0.18887 0.13943 0.20948 0.04075  -0.00116 0.01867  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.21201 0.09315 0.19171 0.03920  0.01040  -0.00332 189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.29967 0.16211 0.26001 0.03528  0.01151  -0.01687 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.39267 0.20894 0.32396 0.02829  0.00875  -0.02818 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.31482 0.19745 0.27794 0.03647  0.01369  -0.02035 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.40721 0.22230 0.32358 0.02601  0.00693  -0.03874 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.39191 0.24282 0.32423 0.03306  0.01161  -0.03340 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.19808 0.12255 0.20161 0.01632  -0.00598 0.01469  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.18411 0.13255 0.19194 0.01958  -0.01151 0.02398  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.26497 0.20786 0.26818 0.03866  -0.01000 0.03816  190 LEU A C   
1344 O O   . LEU A 183 ? 0.27030 0.17694 0.26060 0.04689  -0.00191 0.04256  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.23933 0.18358 0.23822 0.00702  -0.01164 0.02560  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.24112 0.19886 0.24677 -0.00687 -0.01289 0.01517  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.21623 0.17416 0.21440 -0.01382 -0.00872 0.02055  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.20764 0.19102 0.22204 -0.00577 -0.01962 0.00896  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.20644 0.18404 0.21907 0.04576  -0.01919 0.04545  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.25750 0.23851 0.26621 0.06568  -0.02086 0.06259  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.30582 0.25545 0.28852 0.06535  -0.01641 0.07243  191 LYS A C   
1352 O O   . LYS A 184 ? 0.27141 0.21415 0.24408 0.04879  -0.01537 0.06722  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.27031 0.30105 0.29410 0.06845  -0.03732 0.06747  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.26284 0.33069 0.32062 0.06927  -0.04070 0.06446  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.34956 0.46517 0.42324 0.06128  -0.06179 0.06559  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.45400 0.60855 0.56799 0.05483  -0.06461 0.06365  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.49961 0.68369 0.62260 0.03799  -0.08442 0.05626  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.31154 0.24323 0.28462 0.08590  -0.01169 0.08953  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.40004 0.29408 0.34819 0.08666  -0.00361 0.10312  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.40574 0.32117 0.33943 0.07926  -0.01052 0.10866  192 GLU A C   
1361 O O   . GLU A 185 ? 0.44474 0.33604 0.36290 0.06852  -0.00090 0.11404  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.48178 0.36217 0.42554 0.10658  0.00054  0.11522  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.66943 0.49969 0.59433 0.10124  0.01248  0.12192  192 GLU A CG  
1364 C CD  . GLU A 185 ? 0.94717 0.76566 0.86628 0.12266  0.01638  0.13462  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 0.81632 0.66661 0.74884 0.14153  0.01117  0.13712  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 0.94487 0.72435 0.84850 0.12014  0.02505  0.14337  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.30024 0.26047 0.23757 0.08440  -0.02683 0.10763  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.35464 0.33056 0.26727 0.08116  -0.03474 0.11081  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.28638 0.27606 0.20046 0.06035  -0.03846 0.08940  193 ASP A C   
1370 O O   . ASP A 186 ? 0.31908 0.32329 0.20987 0.05894  -0.04740 0.08640  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.37547 0.38613 0.28553 0.09507  -0.05342 0.11815  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.42565 0.47780 0.36925 0.09222  -0.06964 0.10683  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.47687 0.53025 0.44212 0.08103  -0.06529 0.09369  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.63320 0.71496 0.58449 0.09736  -0.08548 0.10955  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.25010 0.23182 0.18604 0.04637  -0.03150 0.07467  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.22844 0.22032 0.16775 0.03024  -0.03329 0.05640  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.24462 0.21529 0.18657 0.01820  -0.01738 0.05366  194 GLN A C   
1378 O O   . GLN A 187 ? 0.26830 0.24470 0.22259 0.00734  -0.01645 0.03986  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.19515 0.20718 0.16185 0.02481  -0.04243 0.04294  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.20684 0.25111 0.18264 0.03226  -0.06020 0.04646  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.32180 0.37913 0.27106 0.02979  -0.07545 0.04308  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.29419 0.33977 0.22394 0.01978  -0.07317 0.03053  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.30834 0.38957 0.25380 0.04102  -0.09143 0.05429  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.30513 0.25293 0.23793 0.01940  -0.00526 0.06864  195 THR A N   
1385 C CA  . THR A 188 ? 0.35249 0.28656 0.29601 0.00435  0.00761  0.06846  195 THR A CA  
1386 C C   . THR A 188 ? 0.29589 0.24503 0.23106 -0.00028 0.01563  0.06857  195 THR A C   
1387 O O   . THR A 188 ? 0.31450 0.26403 0.26606 -0.01261 0.02595  0.07024  195 THR A O   
1388 C CB  . THR A 188 ? 0.37222 0.27320 0.31270 0.00292  0.01819  0.08550  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.42379 0.32105 0.33895 0.01444  0.02417  0.10516  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.36471 0.24230 0.30934 0.01093  0.01374  0.08356  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.28426 0.24646 0.19364 0.00997  0.01092  0.06674  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.36632 0.33822 0.26159 0.01004  0.02081  0.06362  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.25143 0.23335 0.17006 0.00125  0.02086  0.04712  196 GLU A C   
1394 O O   . GLU A 189 ? 0.24241 0.23225 0.16192 0.00126  0.03445  0.04824  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.31666 0.29297 0.17099 0.02269  0.01184  0.05883  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.27088 0.25542 0.12787 0.01985  -0.00831 0.03743  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.45999 0.44742 0.27605 0.02828  -0.02381 0.03199  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.37197 0.36667 0.18143 0.03510  -0.03667 0.04224  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.37399 0.35505 0.16240 0.02906  -0.02409 0.01715  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.25289 0.23612 0.19048 -0.00367 0.00792  0.03447  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.26730 0.25767 0.22414 -0.00997 0.00758  0.02138  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.24567 0.23798 0.23097 -0.02029 0.01415  0.02614  197 TYR A C   
1403 O O   . TYR A 190 ? 0.24030 0.24036 0.24237 -0.02432 0.01224  0.01776  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.21105 0.20301 0.17451 -0.01102 -0.00726 0.00876  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.20571 0.19962 0.14468 -0.00599 -0.01811 0.00276  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.22360 0.21199 0.13892 -0.00369 -0.01610 -0.00714 197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.22745 0.22809 0.16449 -0.00242 -0.03101 0.00726  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.23163 0.21680 0.11813 -0.00192 -0.02963 -0.01585 197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.25805 0.26549 0.17360 -0.00054 -0.04587 0.00160  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.23095 0.22835 0.11900 -0.00221 -0.04649 -0.01153 197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.26543 0.26431 0.12580 -0.00310 -0.06463 -0.02062 197 TYR A OH  
1412 N N   . LEU A 191 ? 0.21293 0.19690 0.20258 -0.02558 0.02062  0.04003  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.21274 0.20038 0.22890 -0.04003 0.02563  0.04554  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.29149 0.29798 0.31579 -0.04202 0.04199  0.05979  198 LEU A C   
1415 O O   . LEU A 191 ? 0.21809 0.23912 0.27265 -0.05599 0.04515  0.06582  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.21012 0.17036 0.22848 -0.04890 0.02289  0.05165  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.23420 0.17513 0.24500 -0.04337 0.01128  0.04024  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.30983 0.21414 0.31532 -0.04790 0.01232  0.04664  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.25253 0.20401 0.27673 -0.04822 0.00309  0.02510  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.21188 0.22069 0.20980 -0.02832 0.05232  0.06614  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.21743 0.24448 0.21893 -0.02590 0.07311  0.08271  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.28668 0.33826 0.29708 -0.01707 0.08008  0.07540  199 GLU A C   
1423 O O   . GLU A 192 ? 0.22713 0.27071 0.21575 -0.00542 0.07302  0.05838  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.30869 0.32388 0.26819 -0.01119 0.08319  0.09352  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.46999 0.45924 0.41670 -0.01398 0.07716  0.10379  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.81143 0.79189 0.71186 0.00352  0.08473  0.11597  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.97061 0.96376 0.85260 0.01387  0.09893  0.11873  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.86097 0.82208 0.74273 0.00887  0.07494  0.12115  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.23838 0.24788 0.28565 -0.08105 -0.02313 0.02384  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.20328 0.26514 0.28417 -0.08163 -0.03179 0.01878  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.17198 0.26850 0.25422 -0.06249 -0.01309 0.02657  200 GLU A C   
1432 O O   . GLU A 193 ? 0.15125 0.26632 0.23021 -0.04800 -0.01843 0.01814  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.21699 0.30541 0.35333 -0.11017 -0.03908 0.02341  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.28027 0.43491 0.46687 -0.10507 -0.03958 0.02728  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.51073 0.70044 0.76155 -0.13148 -0.05324 0.03014  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.57052 0.78869 0.83766 -0.12177 -0.07148 0.02054  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.34501 0.52336 0.61640 -0.15462 -0.04114 0.03892  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.20905 0.30605 0.28737 -0.06200 0.00959  0.04242  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.23190 0.35309 0.29850 -0.04476 0.02667  0.04588  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.20723 0.31403 0.23132 -0.02634 0.01772  0.03566  201 ARG A C   
1441 O O   . ARG A 194 ? 0.15365 0.27487 0.16769 -0.01478 0.02147  0.02831  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.25416 0.37215 0.31010 -0.04674 0.05389  0.06609  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.37536 0.44983 0.39275 -0.04601 0.05418  0.07806  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.47156 0.53832 0.48065 -0.05176 0.08335  0.10348  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.52501 0.55105 0.48094 -0.03949 0.08405  0.11856  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.58186 0.59028 0.50632 -0.03688 0.10822  0.14423  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.51378 0.54206 0.45573 -0.04695 0.13956  0.15748  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.66045 0.63210 0.53516 -0.02112 0.10267  0.15975  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.17114 0.24902 0.17360 -0.02360 0.00731  0.03535  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.20656 0.28295 0.18536 -0.00883 -0.00137 0.02861  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.15715 0.24121 0.14617 -0.00702 -0.01171 0.01327  202 ARG A C   
1452 O O   . ARG A 195 ? 0.18456 0.27899 0.16653 -0.00063 -0.01380 0.00635  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.21135 0.26202 0.17454 -0.00115 -0.00506 0.03701  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.20645 0.26867 0.16301 0.01306  -0.01456 0.03360  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.19129 0.27237 0.12914 0.01831  -0.01880 0.03899  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.20296 0.30209 0.14626 0.02791  -0.03311 0.03926  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.23740 0.35909 0.18378 0.02314  -0.04420 0.02784  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.19359 0.31320 0.12846 0.01351  -0.04059 0.01395  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.21630 0.35936 0.18276 0.02746  -0.05725 0.03028  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.15679 0.23053 0.15708 -0.01406 -0.01930 0.00806  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.13786 0.21428 0.13822 -0.01024 -0.02836 -0.00249 203 ILE A CA  
1462 C C   . ILE A 196 ? 0.18160 0.28400 0.19940 -0.00752 -0.02592 -0.00399 203 ILE A C   
1463 O O   . ILE A 196 ? 0.13865 0.24041 0.14849 0.00077  -0.02589 -0.00918 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.19639 0.25157 0.19181 -0.01798 -0.04135 -0.00850 203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.19012 0.20627 0.15929 -0.01501 -0.03822 -0.00967 203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.16399 0.21952 0.14891 -0.01118 -0.05106 -0.01544 203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.28171 0.26238 0.23590 -0.02774 -0.05089 -0.01882 203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.12507 0.24869 0.16988 -0.01355 -0.02037 0.00212  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.11445 0.26333 0.17944 -0.00426 -0.01202 0.00239  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.18209 0.32067 0.21804 0.00699  0.00111  -0.00299 204 LYS A C   
1471 O O   . LYS A 197 ? 0.16847 0.30361 0.20143 0.01801  0.00367  -0.00940 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.11000 0.29051 0.21609 -0.01109 0.00015  0.01346  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.18833 0.39447 0.34121 -0.02323 -0.01799 0.01695  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.22085 0.46887 0.42956 -0.03268 -0.00068 0.03142  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.44144 0.71039 0.69866 -0.05621 -0.02441 0.03378  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.52523 0.81147 0.82223 -0.07444 -0.00402 0.04610  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.15705 0.28588 0.16759 0.00420  0.00738  -0.00039 205 GLU A N   
1478 C CA  . GLU A 198 ? 0.16545 0.28259 0.14116 0.01071  0.01226  -0.00834 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.18404 0.28784 0.15160 0.01017  -0.00127 -0.01912 205 GLU A C   
1480 O O   . GLU A 198 ? 0.18761 0.27806 0.14009 0.01350  0.00157  -0.03019 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.20504 0.31639 0.15170 0.00840  0.01345  -0.00035 205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.27424 0.37373 0.17820 0.01124  0.00696  -0.01016 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.25096 0.34827 0.12588 0.01190  -0.00009 0.00196  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.28378 0.38469 0.17705 0.01096  -0.00929 0.01315  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.26646 0.35364 0.09454 0.01625  0.00425  0.00101  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.18933 0.29186 0.16583 0.00581  -0.01242 -0.01574 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.18695 0.28177 0.16222 0.00387  -0.01915 -0.02129 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.21684 0.29982 0.19688 0.00782  -0.01624 -0.02528 206 ILE A C   
1489 O O   . ILE A 199 ? 0.19701 0.26530 0.17072 0.00533  -0.01489 -0.03151 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.13489 0.23113 0.11751 0.00385  -0.02350 -0.01434 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.18792 0.29346 0.16638 0.00521  -0.02725 -0.00690 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.14300 0.23689 0.13268 0.00215  -0.02283 -0.01602 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.22502 0.32356 0.20901 0.01173  -0.02578 0.00164  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.17187 0.25937 0.16354 0.01305  -0.01749 -0.02045 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.13206 0.20976 0.12608 0.02190  -0.01835 -0.01960 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.16470 0.23474 0.15780 0.03098  -0.00715 -0.02472 207 VAL A C   
1497 O O   . VAL A 200 ? 0.21666 0.26015 0.19895 0.03604  -0.00335 -0.02709 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.16163 0.25390 0.17103 0.02485  -0.02998 -0.01308 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.16604 0.25572 0.18087 0.03971  -0.03419 -0.00807 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.15572 0.23517 0.14763 0.01788  -0.03983 -0.01294 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.17522 0.26115 0.17478 0.03416  0.00237  -0.02597 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.21914 0.29086 0.20896 0.04747  0.01908  -0.03305 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.24691 0.28127 0.19836 0.03913  0.01991  -0.04839 208 LYS A C   
1504 O O   . LYS A 201 ? 0.28100 0.28032 0.21582 0.04752  0.02912  -0.05760 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.21180 0.30868 0.21162 0.05302  0.03538  -0.02919 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.29990 0.37900 0.28195 0.07188  0.06043  -0.03735 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.27436 0.38464 0.27095 0.07846  0.08363  -0.02817 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.47442 0.56150 0.44265 0.10196  0.11636  -0.03745 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.76516 0.80022 0.65791 0.09261  0.11465  -0.05754 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.22893 0.26901 0.16834 0.02228  0.00837  -0.05099 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.27920 0.29431 0.19009 0.00901  0.00126  -0.06575 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.27413 0.26702 0.19493 -0.00087 -0.00346 -0.06760 209 LYS A C   
1513 O O   . LYS A 202 ? 0.28665 0.24103 0.18700 -0.00820 -0.00200 -0.08179 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.27149 0.31052 0.17733 -0.00305 -0.01381 -0.06283 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.38336 0.41012 0.26883 -0.02072 -0.03102 -0.07689 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.52376 0.57105 0.39307 -0.02306 -0.04579 -0.07128 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.63116 0.67769 0.50433 -0.04009 -0.07096 -0.07615 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.62188 0.68931 0.49367 -0.03592 -0.08729 -0.06216 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.24945 0.25903 0.19602 -0.00195 -0.00664 -0.05353 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.26951 0.26382 0.22580 -0.01409 -0.00682 -0.05035 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.31220 0.28371 0.26801 -0.00136 0.00288  -0.03889 210 HIS A C   
1522 O O   . HIS A 203 ? 0.31991 0.26520 0.27582 -0.01059 0.00931  -0.03486 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.25400 0.28243 0.23315 -0.02374 -0.01344 -0.04122 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.26739 0.32064 0.25103 -0.03559 -0.02779 -0.04768 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.29142 0.33789 0.27577 -0.05601 -0.03885 -0.05954 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.28407 0.36620 0.26887 -0.02991 -0.03588 -0.04269 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.30962 0.38601 0.29465 -0.06084 -0.05689 -0.06125 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.30135 0.39781 0.28553 -0.04304 -0.05321 -0.04932 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.30150 0.26707 0.15202 -0.02587 -0.04453 -0.09098 211 SER A N   
1530 C CA  . SER A 204 ? 0.28438 0.23041 0.14782 -0.02291 -0.04186 -0.08764 211 SER A CA  
1531 C C   . SER A 204 ? 0.30018 0.21549 0.14932 -0.00926 -0.02993 -0.09277 211 SER A C   
1532 O O   . SER A 204 ? 0.31606 0.22370 0.17372 0.00018  -0.02381 -0.08577 211 SER A O   
1533 C CB  . SER A 204 ? 0.31275 0.27934 0.19481 -0.01977 -0.04242 -0.07164 211 SER A CB  
1534 O OG  . SER A 204 ? 0.33417 0.32953 0.23113 -0.02860 -0.04985 -0.06341 211 SER A OG  
1535 N N   . GLN A 205 ? 0.33712 0.23956 0.16603 -0.00622 -0.02583 -0.10542 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.47018 0.35273 0.28787 0.01096  -0.01249 -0.10812 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.48521 0.33326 0.30872 0.01458  -0.00820 -0.11056 212 GLN A C   
1538 O O   . GLN A 205 ? 0.48459 0.32415 0.30729 0.03186  0.00422  -0.10603 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.45454 0.33494 0.24842 0.01402  -0.00928 -0.12183 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.65961 0.52121 0.44510 0.00083  -0.01675 -0.14178 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.85397 0.74532 0.63818 -0.01603 -0.02898 -0.14602 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.58789 0.50224 0.39016 -0.02393 -0.03728 -0.13436 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.70583 0.60045 0.46885 -0.02038 -0.02972 -0.16279 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.41683 0.24777 0.24812 -0.00110 -0.01762 -0.11465 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.47663 0.26964 0.31309 0.00083  -0.01335 -0.11410 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.40430 0.20076 0.26056 -0.00565 -0.01727 -0.09908 213 PHE A C   
1547 O O   . PHE A 206 ? 0.51231 0.27934 0.37636 -0.01158 -0.01742 -0.09563 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.51405 0.27712 0.34441 -0.01305 -0.01982 -0.12978 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.60798 0.36511 0.41694 -0.00601 -0.01615 -0.14852 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.58916 0.32989 0.38677 0.01583  -0.00208 -0.15133 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.62686 0.39965 0.42767 -0.02029 -0.02669 -0.16317 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.63644 0.37391 0.41303 0.02241  0.00156  -0.16930 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.68963 0.45955 0.46880 -0.01426 -0.02306 -0.18234 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.62409 0.37486 0.39020 0.00665  -0.00869 -0.18576 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.32985 0.16185 0.19552 -0.00483 -0.02073 -0.08957 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.28892 0.14822 0.18836 -0.00748 -0.02120 -0.07118 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.39607 0.25347 0.30613 0.01219  -0.00531 -0.06052 214 ILE A C   
1558 O O   . ILE A 207 ? 0.35454 0.22060 0.25683 0.02877  0.00500  -0.06071 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.25432 0.16054 0.16839 -0.01017 -0.02776 -0.06404 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.26277 0.17763 0.16994 -0.02828 -0.04365 -0.07049 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.25272 0.19082 0.19934 -0.00823 -0.02616 -0.04819 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.32706 0.24123 0.24882 -0.04669 -0.05337 -0.06615 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.28418 0.13536 0.21320 0.01046  -0.00307 -0.04874 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.34344 0.19092 0.28082 0.03032  0.01228  -0.03728 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.23648 0.13747 0.20040 0.03920  0.01726  -0.02154 215 GLY A C   
1566 O O   . GLY A 208 ? 0.28970 0.20098 0.26976 0.05046  0.02642  -0.00672 215 GLY A O   
1567 N N   . TYR A 209 ? 0.24034 0.17561 0.20887 0.03441  0.01128  -0.02462 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.25178 0.23493 0.24308 0.04034  0.01459  -0.01482 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.25372 0.24881 0.23571 0.04363  0.01627  -0.02154 216 TYR A C   
1570 O O   . TYR A 209 ? 0.24166 0.21991 0.20525 0.03735  0.01025  -0.03156 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.14868 0.16484 0.16276 0.02801  0.00347  -0.00960 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.17687 0.18868 0.20334 0.02323  0.00191  0.00154  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.16286 0.19831 0.20847 0.03372  0.01043  0.01725  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.17559 0.16265 0.19548 0.00726  -0.00807 -0.00168 216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.21558 0.24782 0.27405 0.02965  0.00995  0.03180  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.18038 0.16275 0.21391 0.00020  -0.00937 0.01155  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.17973 0.18345 0.23275 0.01209  0.00015  0.02940  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.20794 0.20816 0.27612 0.00548  -0.00024 0.04673  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.21804 0.24459 0.21318 0.05245  0.02429  -0.01468 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.22191 0.26031 0.21161 0.05278  0.02607  -0.01782 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.23788 0.28440 0.23319 0.03931  0.01364  -0.02275 217 PRO A C   
1582 O O   . PRO A 210 ? 0.21277 0.27976 0.22720 0.03310  0.00663  -0.02166 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.24514 0.31402 0.25302 0.05459  0.03181  -0.00745 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.27539 0.35529 0.29881 0.05303  0.02967  -0.00084 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.21486 0.27092 0.23094 0.06143  0.03197  -0.00232 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.21983 0.25195 0.19733 0.03710  0.01148  -0.02750 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.17209 0.20962 0.15272 0.02810  0.00150  -0.02954 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.18179 0.23164 0.16650 0.02960  0.00727  -0.02431 218 ILE A C   
1589 O O   . ILE A 211 ? 0.21798 0.26109 0.18598 0.03505  0.01435  -0.02189 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.18810 0.20417 0.14616 0.02366  -0.00624 -0.03585 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.19879 0.20228 0.15494 0.01761  -0.01284 -0.04040 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.22768 0.25324 0.18958 0.01841  -0.01487 -0.03423 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.20610 0.18716 0.13642 0.01178  -0.01943 -0.04947 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.12069 0.18934 0.12751 0.02439  0.00439  -0.02272 219 THR A N   
1595 C CA  . THR A 212 ? 0.14279 0.22173 0.15824 0.02153  0.00912  -0.01707 219 THR A CA  
1596 C C   . THR A 212 ? 0.12590 0.19414 0.14276 0.01581  0.00121  -0.01685 219 THR A C   
1597 O O   . THR A 212 ? 0.14041 0.21048 0.16900 0.01304  -0.00718 -0.02264 219 THR A O   
1598 C CB  . THR A 212 ? 0.16080 0.26728 0.20055 0.01837  0.01192  -0.01705 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.10970 0.22054 0.14521 0.02481  0.01842  -0.01283 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.18663 0.30256 0.23659 0.01088  0.01604  -0.01104 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.16208 0.22153 0.16676 0.01629  0.00459  -0.00878 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.16448 0.21328 0.17111 0.01307  -0.00085 -0.00372 220 LEU A CA  
1603 C C   . LEU A 213 ? 0.18473 0.23769 0.21249 0.00494  0.00268  0.00211  220 LEU A C   
1604 O O   . LEU A 213 ? 0.14324 0.20471 0.17117 0.00235  0.01133  0.01250  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.20228 0.24376 0.18499 0.01789  0.00093  0.00456  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.26003 0.29356 0.24326 0.01734  -0.00223 0.01617  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.21330 0.23928 0.20650 0.01780  -0.01277 0.01034  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.26163 0.29761 0.21806 0.02375  -0.00087 0.02339  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.16026 0.20871 0.20584 0.00051  -0.00406 -0.00531 221 PHE A N   
1610 C CA  . PHE A 214 ? 0.13860 0.18446 0.20461 -0.01015 -0.00262 -0.00350 221 PHE A CA  
1611 C C   . PHE A 214 ? 0.21086 0.23654 0.27401 -0.01247 -0.00050 0.01269  221 PHE A C   
1612 O O   . PHE A 214 ? 0.18242 0.19536 0.23139 -0.00391 -0.00357 0.01883  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.13797 0.17960 0.22009 -0.01190 -0.01100 -0.01922 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.12941 0.19894 0.22088 -0.01242 -0.01213 -0.03265 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.11166 0.19968 0.19331 -0.00612 -0.00853 -0.03077 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.12130 0.19821 0.23096 -0.01833 -0.01680 -0.04724 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.11274 0.22270 0.19948 -0.00474 -0.00831 -0.03707 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.14071 0.24197 0.24928 -0.01593 -0.01617 -0.05391 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.12981 0.23912 0.22093 -0.00858 -0.01092 -0.04411 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.20501 0.23118 0.28320 -0.02498 0.00460  0.02145  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.20160 0.20776 0.28259 -0.02957 0.00712  0.04021  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.21974 0.19812 0.32245 -0.03938 0.00159  0.03314  222 VAL A C   
1623 O O   . VAL A 215 ? 0.19901 0.18113 0.31444 -0.04469 -0.00321 0.01301  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.38112 0.40748 0.46345 -0.03777 0.01759  0.05959  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.47176 0.51999 0.52826 -0.02385 0.02334  0.06436  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.22414 0.27208 0.32692 -0.05274 0.01996  0.05279  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.25329 0.20308 0.35930 -0.04046 0.00242  0.04970  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.34393 0.25632 0.46848 -0.04745 -0.00228 0.04334  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.41954 0.31852 0.56325 -0.06870 0.00310  0.06041  223 GLU A C   
1630 O O   . GLU A 216 ? 0.40191 0.31831 0.54195 -0.07292 0.01105  0.08504  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.38304 0.26570 0.49872 -0.02943 -0.00610 0.04940  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.38118 0.28164 0.47893 -0.01045 -0.01184 0.03666  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.48853 0.36954 0.57764 0.00801  -0.01505 0.04678  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.41889 0.26630 0.51976 0.01235  -0.01786 0.04195  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.40535 0.30585 0.47538 0.01897  -0.01489 0.05859  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.43060 0.29957 0.59473 -0.08253 -0.00151 0.04655  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.51709 0.36639 0.70362 -0.10772 0.00170  0.06010  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.65655 0.48523 0.83740 -0.10337 0.00837  0.09444  224 LYS A C   
1639 O O   . LYS A 217 ? 0.65770 0.45881 0.82863 -0.08391 0.00705  0.10157  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.56856 0.38293 0.76083 -0.11522 -0.00546 0.03294  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.87172 0.66562 1.07140 -0.13884 -0.00267 0.04121  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.81501 0.59283 1.01710 -0.15223 -0.01010 0.00925  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.88759 0.60239 1.08699 -0.15401 -0.01107 0.00913  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 1.03862 0.72038 1.22704 -0.12384 -0.01316 0.00474  224 LYS A NZ  
# 
