data_7HAI
# 
_entry.id   7HAI 
# 
_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   7HAI         pdb_00007hai 10.2210/pdb7hai/pdb 
WWPDB D_1001407229 ?            ?                   
# 
_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                        7HAI 
_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-(3-bromophenyl)-5-methyl-1,3,4-oxadiazole' 239.069   1   ?        ? ? ? 
3 water       nat water                                         18.015    349 ?        ? ? ? 
# 
_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-(3-bromophenyl)-5-methyl-1,3,4-oxadiazole' A1AXQ 
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 
A1AXQ non-polymer         . '2-(3-bromophenyl)-5-methyl-1,3,4-oxadiazole' ? 'C9 H7 Br N2 O'  239.069 
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        A1AXQ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AXQ 
_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 A1AXQ 1   301 301 A1AXQ E5B A . 
C 3 HOH   1   401 172 HOH   HOH A . 
C 3 HOH   2   402 128 HOH   HOH A . 
C 3 HOH   3   403 257 HOH   HOH A . 
C 3 HOH   4   404 309 HOH   HOH A . 
C 3 HOH   5   405 285 HOH   HOH A . 
C 3 HOH   6   406 251 HOH   HOH A . 
C 3 HOH   7   407 265 HOH   HOH A . 
C 3 HOH   8   408 157 HOH   HOH A . 
C 3 HOH   9   409 141 HOH   HOH A . 
C 3 HOH   10  410 127 HOH   HOH A . 
C 3 HOH   11  411 30  HOH   HOH A . 
C 3 HOH   12  412 120 HOH   HOH A . 
C 3 HOH   13  413 140 HOH   HOH A . 
C 3 HOH   14  414 124 HOH   HOH A . 
C 3 HOH   15  415 63  HOH   HOH A . 
C 3 HOH   16  416 100 HOH   HOH A . 
C 3 HOH   17  417 179 HOH   HOH A . 
C 3 HOH   18  418 92  HOH   HOH A . 
C 3 HOH   19  419 61  HOH   HOH A . 
C 3 HOH   20  420 26  HOH   HOH A . 
C 3 HOH   21  421 129 HOH   HOH A . 
C 3 HOH   22  422 147 HOH   HOH A . 
C 3 HOH   23  423 90  HOH   HOH A . 
C 3 HOH   24  424 277 HOH   HOH A . 
C 3 HOH   25  425 266 HOH   HOH A . 
C 3 HOH   26  426 166 HOH   HOH A . 
C 3 HOH   27  427 59  HOH   HOH A . 
C 3 HOH   28  428 234 HOH   HOH A . 
C 3 HOH   29  429 295 HOH   HOH A . 
C 3 HOH   30  430 57  HOH   HOH A . 
C 3 HOH   31  431 37  HOH   HOH A . 
C 3 HOH   32  432 139 HOH   HOH A . 
C 3 HOH   33  433 122 HOH   HOH A . 
C 3 HOH   34  434 22  HOH   HOH A . 
C 3 HOH   35  435 71  HOH   HOH A . 
C 3 HOH   36  436 21  HOH   HOH A . 
C 3 HOH   37  437 70  HOH   HOH A . 
C 3 HOH   38  438 203 HOH   HOH A . 
C 3 HOH   39  439 232 HOH   HOH A . 
C 3 HOH   40  440 118 HOH   HOH A . 
C 3 HOH   41  441 169 HOH   HOH A . 
C 3 HOH   42  442 79  HOH   HOH A . 
C 3 HOH   43  443 239 HOH   HOH A . 
C 3 HOH   44  444 332 HOH   HOH A . 
C 3 HOH   45  445 151 HOH   HOH A . 
C 3 HOH   46  446 64  HOH   HOH A . 
C 3 HOH   47  447 287 HOH   HOH A . 
C 3 HOH   48  448 171 HOH   HOH A . 
C 3 HOH   49  449 98  HOH   HOH A . 
C 3 HOH   50  450 77  HOH   HOH A . 
C 3 HOH   51  451 75  HOH   HOH A . 
C 3 HOH   52  452 36  HOH   HOH A . 
C 3 HOH   53  453 249 HOH   HOH A . 
C 3 HOH   54  454 323 HOH   HOH A . 
C 3 HOH   55  455 2   HOH   HOH A . 
C 3 HOH   56  456 11  HOH   HOH A . 
C 3 HOH   57  457 7   HOH   HOH A . 
C 3 HOH   58  458 108 HOH   HOH A . 
C 3 HOH   59  459 3   HOH   HOH A . 
C 3 HOH   60  460 99  HOH   HOH A . 
C 3 HOH   61  461 67  HOH   HOH A . 
C 3 HOH   62  462 34  HOH   HOH A . 
C 3 HOH   63  463 113 HOH   HOH A . 
C 3 HOH   64  464 101 HOH   HOH A . 
C 3 HOH   65  465 231 HOH   HOH A . 
C 3 HOH   66  466 10  HOH   HOH A . 
C 3 HOH   67  467 39  HOH   HOH A . 
C 3 HOH   68  468 9   HOH   HOH A . 
C 3 HOH   69  469 334 HOH   HOH A . 
C 3 HOH   70  470 13  HOH   HOH A . 
C 3 HOH   71  471 31  HOH   HOH A . 
C 3 HOH   72  472 214 HOH   HOH A . 
C 3 HOH   73  473 125 HOH   HOH A . 
C 3 HOH   74  474 14  HOH   HOH A . 
C 3 HOH   75  475 153 HOH   HOH A . 
C 3 HOH   76  476 134 HOH   HOH A . 
C 3 HOH   77  477 35  HOH   HOH A . 
C 3 HOH   78  478 189 HOH   HOH A . 
C 3 HOH   79  479 54  HOH   HOH A . 
C 3 HOH   80  480 27  HOH   HOH A . 
C 3 HOH   81  481 246 HOH   HOH A . 
C 3 HOH   82  482 93  HOH   HOH A . 
C 3 HOH   83  483 259 HOH   HOH A . 
C 3 HOH   84  484 102 HOH   HOH A . 
C 3 HOH   85  485 142 HOH   HOH A . 
C 3 HOH   86  486 65  HOH   HOH A . 
C 3 HOH   87  487 274 HOH   HOH A . 
C 3 HOH   88  488 105 HOH   HOH A . 
C 3 HOH   89  489 314 HOH   HOH A . 
C 3 HOH   90  490 66  HOH   HOH A . 
C 3 HOH   91  491 16  HOH   HOH A . 
C 3 HOH   92  492 121 HOH   HOH A . 
C 3 HOH   93  493 51  HOH   HOH A . 
C 3 HOH   94  494 258 HOH   HOH A . 
C 3 HOH   95  495 307 HOH   HOH A . 
C 3 HOH   96  496 23  HOH   HOH A . 
C 3 HOH   97  497 86  HOH   HOH A . 
C 3 HOH   98  498 211 HOH   HOH A . 
C 3 HOH   99  499 95  HOH   HOH A . 
C 3 HOH   100 500 97  HOH   HOH A . 
C 3 HOH   101 501 115 HOH   HOH A . 
C 3 HOH   102 502 300 HOH   HOH A . 
C 3 HOH   103 503 78  HOH   HOH A . 
C 3 HOH   104 504 49  HOH   HOH A . 
C 3 HOH   105 505 280 HOH   HOH A . 
C 3 HOH   106 506 74  HOH   HOH A . 
C 3 HOH   107 507 69  HOH   HOH A . 
C 3 HOH   108 508 123 HOH   HOH A . 
C 3 HOH   109 509 216 HOH   HOH A . 
C 3 HOH   110 510 15  HOH   HOH A . 
C 3 HOH   111 511 168 HOH   HOH A . 
C 3 HOH   112 512 32  HOH   HOH A . 
C 3 HOH   113 513 242 HOH   HOH A . 
C 3 HOH   114 514 40  HOH   HOH A . 
C 3 HOH   115 515 87  HOH   HOH A . 
C 3 HOH   116 516 55  HOH   HOH A . 
C 3 HOH   117 517 18  HOH   HOH A . 
C 3 HOH   118 518 104 HOH   HOH A . 
C 3 HOH   119 519 223 HOH   HOH A . 
C 3 HOH   120 520 8   HOH   HOH A . 
C 3 HOH   121 521 282 HOH   HOH A . 
C 3 HOH   122 522 286 HOH   HOH A . 
C 3 HOH   123 523 186 HOH   HOH A . 
C 3 HOH   124 524 4   HOH   HOH A . 
C 3 HOH   125 525 46  HOH   HOH A . 
C 3 HOH   126 526 44  HOH   HOH A . 
C 3 HOH   127 527 24  HOH   HOH A . 
C 3 HOH   128 528 131 HOH   HOH A . 
C 3 HOH   129 529 175 HOH   HOH A . 
C 3 HOH   130 530 41  HOH   HOH A . 
C 3 HOH   131 531 68  HOH   HOH A . 
C 3 HOH   132 532 110 HOH   HOH A . 
C 3 HOH   133 533 82  HOH   HOH A . 
C 3 HOH   134 534 19  HOH   HOH A . 
C 3 HOH   135 535 43  HOH   HOH A . 
C 3 HOH   136 536 85  HOH   HOH A . 
C 3 HOH   137 537 170 HOH   HOH A . 
C 3 HOH   138 538 12  HOH   HOH A . 
C 3 HOH   139 539 199 HOH   HOH A . 
C 3 HOH   140 540 48  HOH   HOH A . 
C 3 HOH   141 541 329 HOH   HOH A . 
C 3 HOH   142 542 273 HOH   HOH A . 
C 3 HOH   143 543 29  HOH   HOH A . 
C 3 HOH   144 544 146 HOH   HOH A . 
C 3 HOH   145 545 28  HOH   HOH A . 
C 3 HOH   146 546 180 HOH   HOH A . 
C 3 HOH   147 547 138 HOH   HOH A . 
C 3 HOH   148 548 6   HOH   HOH A . 
C 3 HOH   149 549 84  HOH   HOH A . 
C 3 HOH   150 550 221 HOH   HOH A . 
C 3 HOH   151 551 94  HOH   HOH A . 
C 3 HOH   152 552 326 HOH   HOH A . 
C 3 HOH   153 553 264 HOH   HOH A . 
C 3 HOH   154 554 109 HOH   HOH A . 
C 3 HOH   155 555 161 HOH   HOH A . 
C 3 HOH   156 556 150 HOH   HOH A . 
C 3 HOH   157 557 240 HOH   HOH A . 
C 3 HOH   158 558 135 HOH   HOH A . 
C 3 HOH   159 559 91  HOH   HOH A . 
C 3 HOH   160 560 194 HOH   HOH A . 
C 3 HOH   161 561 56  HOH   HOH A . 
C 3 HOH   162 562 89  HOH   HOH A . 
C 3 HOH   163 563 250 HOH   HOH A . 
C 3 HOH   164 564 243 HOH   HOH A . 
C 3 HOH   165 565 133 HOH   HOH A . 
C 3 HOH   166 566 144 HOH   HOH A . 
C 3 HOH   167 567 17  HOH   HOH A . 
C 3 HOH   168 568 306 HOH   HOH A . 
C 3 HOH   169 569 294 HOH   HOH A . 
C 3 HOH   170 570 184 HOH   HOH A . 
C 3 HOH   171 571 339 HOH   HOH A . 
C 3 HOH   172 572 204 HOH   HOH A . 
C 3 HOH   173 573 42  HOH   HOH A . 
C 3 HOH   174 574 190 HOH   HOH A . 
C 3 HOH   175 575 178 HOH   HOH A . 
C 3 HOH   176 576 283 HOH   HOH A . 
C 3 HOH   177 577 164 HOH   HOH A . 
C 3 HOH   178 578 1   HOH   HOH A . 
C 3 HOH   179 579 193 HOH   HOH A . 
C 3 HOH   180 580 165 HOH   HOH A . 
C 3 HOH   181 581 145 HOH   HOH A . 
C 3 HOH   182 582 47  HOH   HOH A . 
C 3 HOH   183 583 279 HOH   HOH A . 
C 3 HOH   184 584 176 HOH   HOH A . 
C 3 HOH   185 585 96  HOH   HOH A . 
C 3 HOH   186 586 195 HOH   HOH A . 
C 3 HOH   187 587 330 HOH   HOH A . 
C 3 HOH   188 588 206 HOH   HOH A . 
C 3 HOH   189 589 20  HOH   HOH A . 
C 3 HOH   190 590 263 HOH   HOH A . 
C 3 HOH   191 591 212 HOH   HOH A . 
C 3 HOH   192 592 163 HOH   HOH A . 
C 3 HOH   193 593 76  HOH   HOH A . 
C 3 HOH   194 594 130 HOH   HOH A . 
C 3 HOH   195 595 348 HOH   HOH A . 
C 3 HOH   196 596 149 HOH   HOH A . 
C 3 HOH   197 597 52  HOH   HOH A . 
C 3 HOH   198 598 245 HOH   HOH A . 
C 3 HOH   199 599 162 HOH   HOH A . 
C 3 HOH   200 600 33  HOH   HOH A . 
C 3 HOH   201 601 185 HOH   HOH A . 
C 3 HOH   202 602 88  HOH   HOH A . 
C 3 HOH   203 603 38  HOH   HOH A . 
C 3 HOH   204 604 53  HOH   HOH A . 
C 3 HOH   205 605 336 HOH   HOH A . 
C 3 HOH   206 606 45  HOH   HOH A . 
C 3 HOH   207 607 80  HOH   HOH A . 
C 3 HOH   208 608 159 HOH   HOH A . 
C 3 HOH   209 609 349 HOH   HOH A . 
C 3 HOH   210 610 5   HOH   HOH A . 
C 3 HOH   211 611 269 HOH   HOH A . 
C 3 HOH   212 612 158 HOH   HOH A . 
C 3 HOH   213 613 50  HOH   HOH A . 
C 3 HOH   214 614 107 HOH   HOH A . 
C 3 HOH   215 615 304 HOH   HOH A . 
C 3 HOH   216 616 73  HOH   HOH A . 
C 3 HOH   217 617 213 HOH   HOH A . 
C 3 HOH   218 618 342 HOH   HOH A . 
C 3 HOH   219 619 219 HOH   HOH A . 
C 3 HOH   220 620 346 HOH   HOH A . 
C 3 HOH   221 621 328 HOH   HOH A . 
C 3 HOH   222 622 324 HOH   HOH A . 
C 3 HOH   223 623 253 HOH   HOH A . 
C 3 HOH   224 624 315 HOH   HOH A . 
C 3 HOH   225 625 136 HOH   HOH A . 
C 3 HOH   226 626 262 HOH   HOH A . 
C 3 HOH   227 627 276 HOH   HOH A . 
C 3 HOH   228 628 297 HOH   HOH A . 
C 3 HOH   229 629 313 HOH   HOH A . 
C 3 HOH   230 630 228 HOH   HOH A . 
C 3 HOH   231 631 290 HOH   HOH A . 
C 3 HOH   232 632 196 HOH   HOH A . 
C 3 HOH   233 633 132 HOH   HOH A . 
C 3 HOH   234 634 25  HOH   HOH A . 
C 3 HOH   235 635 236 HOH   HOH A . 
C 3 HOH   236 636 301 HOH   HOH A . 
C 3 HOH   237 637 174 HOH   HOH A . 
C 3 HOH   238 638 260 HOH   HOH A . 
C 3 HOH   239 639 248 HOH   HOH A . 
C 3 HOH   240 640 200 HOH   HOH A . 
C 3 HOH   241 641 112 HOH   HOH A . 
C 3 HOH   242 642 312 HOH   HOH A . 
C 3 HOH   243 643 148 HOH   HOH A . 
C 3 HOH   244 644 261 HOH   HOH A . 
C 3 HOH   245 645 72  HOH   HOH A . 
C 3 HOH   246 646 155 HOH   HOH A . 
C 3 HOH   247 647 103 HOH   HOH A . 
C 3 HOH   248 648 156 HOH   HOH A . 
C 3 HOH   249 649 247 HOH   HOH A . 
C 3 HOH   250 650 284 HOH   HOH A . 
C 3 HOH   251 651 183 HOH   HOH A . 
C 3 HOH   252 652 222 HOH   HOH A . 
C 3 HOH   253 653 305 HOH   HOH A . 
C 3 HOH   254 654 137 HOH   HOH A . 
C 3 HOH   255 655 255 HOH   HOH A . 
C 3 HOH   256 656 152 HOH   HOH A . 
C 3 HOH   257 657 241 HOH   HOH A . 
C 3 HOH   258 658 60  HOH   HOH A . 
C 3 HOH   259 659 119 HOH   HOH A . 
C 3 HOH   260 660 198 HOH   HOH A . 
C 3 HOH   261 661 208 HOH   HOH A . 
C 3 HOH   262 662 111 HOH   HOH A . 
C 3 HOH   263 663 288 HOH   HOH A . 
C 3 HOH   264 664 320 HOH   HOH A . 
C 3 HOH   265 665 235 HOH   HOH A . 
C 3 HOH   266 666 181 HOH   HOH A . 
C 3 HOH   267 667 62  HOH   HOH A . 
C 3 HOH   268 668 230 HOH   HOH A . 
C 3 HOH   269 669 341 HOH   HOH A . 
C 3 HOH   270 670 106 HOH   HOH A . 
C 3 HOH   271 671 182 HOH   HOH A . 
C 3 HOH   272 672 293 HOH   HOH A . 
C 3 HOH   273 673 298 HOH   HOH A . 
C 3 HOH   274 674 267 HOH   HOH A . 
C 3 HOH   275 675 308 HOH   HOH A . 
C 3 HOH   276 676 272 HOH   HOH A . 
C 3 HOH   277 677 205 HOH   HOH A . 
C 3 HOH   278 678 217 HOH   HOH A . 
C 3 HOH   279 679 335 HOH   HOH A . 
C 3 HOH   280 680 338 HOH   HOH A . 
C 3 HOH   281 681 302 HOH   HOH A . 
C 3 HOH   282 682 292 HOH   HOH A . 
C 3 HOH   283 683 81  HOH   HOH A . 
C 3 HOH   284 684 116 HOH   HOH A . 
C 3 HOH   285 685 318 HOH   HOH A . 
C 3 HOH   286 686 322 HOH   HOH A . 
C 3 HOH   287 687 226 HOH   HOH A . 
C 3 HOH   288 688 311 HOH   HOH A . 
C 3 HOH   289 689 218 HOH   HOH A . 
C 3 HOH   290 690 114 HOH   HOH A . 
C 3 HOH   291 691 224 HOH   HOH A . 
C 3 HOH   292 692 210 HOH   HOH A . 
C 3 HOH   293 693 227 HOH   HOH A . 
C 3 HOH   294 694 271 HOH   HOH A . 
C 3 HOH   295 695 275 HOH   HOH A . 
C 3 HOH   296 696 154 HOH   HOH A . 
C 3 HOH   297 697 117 HOH   HOH A . 
C 3 HOH   298 698 58  HOH   HOH A . 
C 3 HOH   299 699 319 HOH   HOH A . 
C 3 HOH   300 700 187 HOH   HOH A . 
C 3 HOH   301 701 201 HOH   HOH A . 
C 3 HOH   302 702 220 HOH   HOH A . 
C 3 HOH   303 703 192 HOH   HOH A . 
C 3 HOH   304 704 244 HOH   HOH A . 
C 3 HOH   305 705 202 HOH   HOH A . 
C 3 HOH   306 706 256 HOH   HOH A . 
C 3 HOH   307 707 325 HOH   HOH A . 
C 3 HOH   308 708 233 HOH   HOH A . 
C 3 HOH   309 709 281 HOH   HOH A . 
C 3 HOH   310 710 270 HOH   HOH A . 
C 3 HOH   311 711 337 HOH   HOH A . 
C 3 HOH   312 712 344 HOH   HOH A . 
C 3 HOH   313 713 289 HOH   HOH A . 
C 3 HOH   314 714 278 HOH   HOH A . 
C 3 HOH   315 715 225 HOH   HOH A . 
C 3 HOH   316 716 321 HOH   HOH A . 
C 3 HOH   317 717 268 HOH   HOH A . 
C 3 HOH   318 718 173 HOH   HOH A . 
C 3 HOH   319 719 229 HOH   HOH A . 
C 3 HOH   320 720 160 HOH   HOH A . 
C 3 HOH   321 721 177 HOH   HOH A . 
C 3 HOH   322 722 207 HOH   HOH A . 
C 3 HOH   323 723 197 HOH   HOH A . 
C 3 HOH   324 724 126 HOH   HOH A . 
C 3 HOH   325 725 296 HOH   HOH A . 
C 3 HOH   326 726 188 HOH   HOH A . 
C 3 HOH   327 727 237 HOH   HOH A . 
C 3 HOH   328 728 191 HOH   HOH A . 
C 3 HOH   329 729 317 HOH   HOH A . 
C 3 HOH   330 730 83  HOH   HOH A . 
C 3 HOH   331 731 238 HOH   HOH A . 
C 3 HOH   332 732 333 HOH   HOH A . 
C 3 HOH   333 733 303 HOH   HOH A . 
C 3 HOH   334 734 345 HOH   HOH A . 
C 3 HOH   335 735 209 HOH   HOH A . 
C 3 HOH   336 736 252 HOH   HOH A . 
C 3 HOH   337 737 340 HOH   HOH A . 
C 3 HOH   338 738 143 HOH   HOH A . 
C 3 HOH   339 739 343 HOH   HOH A . 
C 3 HOH   340 740 327 HOH   HOH A . 
C 3 HOH   341 741 310 HOH   HOH A . 
C 3 HOH   342 742 167 HOH   HOH A . 
C 3 HOH   343 743 291 HOH   HOH A . 
C 3 HOH   344 744 254 HOH   HOH A . 
C 3 HOH   345 745 316 HOH   HOH A . 
C 3 HOH   346 746 299 HOH   HOH A . 
C 3 HOH   347 747 347 HOH   HOH A . 
C 3 HOH   348 748 215 HOH   HOH A . 
C 3 HOH   349 749 331 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             594523.637 
_cell.length_a           66.136 
_cell.length_b           89.577 
_cell.length_c           100.354 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HAI 
_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                         7HAI 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HAI 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 S 9M' 
_diffrn_detector.pdbx_collection_date   2023-07-04 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HAI 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             55.220 
_reflns.d_resolution_high            1.650 
_reflns.number_obs                   36235 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.500 
_reflns.pdbx_Rmerge_I_obs            0.079 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        17.500 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              9.800 
_reflns.pdbx_Rrim_I_all              0.084 
_reflns.pdbx_Rpim_I_all              0.027 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     355820 
_reflns.pdbx_scaling_rejects         100 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.650 1.730  ? 42660 5250 ? 0.778 ? ? ? 8.100 ? 2.500  ? ? ? ? ? ? 99.600 0.832 0.287 0.792 
1 2 5.200 55.220 ? 11754 1202 ? 0.035 ? ? ? 9.800 ? 45.400 ? ? ? ? ? ? 96.400 0.037 0.012 0.999 
# 
_refine.entry_id                                 7HAI 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.86 
_refine.pdbx_overall_phase_error                 19.2634 
_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                          0.1703 
_refine.B_iso_mean                               25.68 
_refine.ls_number_reflns_R_free                  1761 
_refine.ls_percent_reflns_obs                    99.27 
_refine.ls_R_factor_R_work                       0.1690 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.65 
_refine.ls_number_reflns_obs                     36222 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.ls_number_reflns_R_work                  34461 
_refine.ls_d_res_low                             34.79 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1944 
_refine.overall_SU_ML                            0.1729 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         13 
_refine_hist.number_atoms_solvent             349 
_refine_hist.number_atoms_total               2006 
_refine_hist.d_res_high                       1.65 
_refine_hist.d_res_low                        34.79 
# 
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           1867 0.0111 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2526 1.2707 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     285  0.0729 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      326  0.0083 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 253  6.2957 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' 1.65 1.69  2626 0.2401 99.42  0.2671 138 . . . . . 
'X-RAY DIFFRACTION' 1.69 1.74  2634 0.2170 99.24  0.2507 118 . . . . . 
'X-RAY DIFFRACTION' 1.74 1.80  2640 0.1914 99.93  0.2548 130 . . . . . 
'X-RAY DIFFRACTION' 1.80 1.86  2621 0.1729 100.00 0.2048 141 . . . . . 
'X-RAY DIFFRACTION' 1.86 1.93  2675 0.1857 100.00 0.2040 110 . . . . . 
'X-RAY DIFFRACTION' 1.94 2.02  2647 0.1759 99.82  0.2189 132 . . . . . 
'X-RAY DIFFRACTION' 2.02 2.13  2625 0.1646 99.96  0.1901 147 . . . . . 
'X-RAY DIFFRACTION' 2.13 2.26  2660 0.1641 99.71  0.2081 136 . . . . . 
'X-RAY DIFFRACTION' 2.26 2.44  2650 0.1748 99.71  0.2408 127 . . . . . 
'X-RAY DIFFRACTION' 2.44 2.68  2636 0.1792 98.69  0.1849 144 . . . . . 
'X-RAY DIFFRACTION' 2.68 3.07  2649 0.1695 99.11  0.1930 145 . . . . . 
'X-RAY DIFFRACTION' 3.07 3.87  2658 0.1588 98.60  0.1652 164 . . . . . 
'X-RAY DIFFRACTION' 3.87 34.79 2740 0.1527 96.63  0.1814 129 . . . . . 
# 
_struct.entry_id                  7HAI 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with PS-5525' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HAI 
_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              7HAI 
_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 7HAI MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HAI LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HAI GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HAI HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HAI HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HAI HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HAI HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HAI HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HAI 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 GLN A 187 ? LEU A 191 ? GLN A 194 LEU A 198 5 ? 5  
HELX_P HELX_P10 AB1 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 11  ? ALA A 14  ? GLU A 18  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O THR A 83  ? O THR A 90  N ILE A 74  ? N ILE A 81  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HAI 
_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 443 ? ? O A HOH 636 ? ? 1.82 
2  1 O A HOH 623 ? ? O A HOH 675 ? ? 1.85 
3  1 O A HOH 599 ? ? O A HOH 628 ? ? 1.88 
4  1 O A HOH 632 ? ? O A HOH 682 ? ? 1.96 
5  1 O A HOH 453 ? ? O A HOH 476 ? ? 1.97 
6  1 O A HOH 628 ? ? O A HOH 636 ? ? 2.07 
7  1 O A HOH 553 ? ? O A HOH 691 ? ? 2.10 
8  1 O A HOH 673 ? ? O A HOH 720 ? ? 2.10 
9  1 O A HOH 615 ? ? O A HOH 719 ? ? 2.13 
10 1 O A GLY 125 ? B O A HOH 401 ? ? 2.14 
11 1 O A HOH 591 ? ? O A HOH 636 ? ? 2.15 
12 1 O A HOH 591 ? ? O A HOH 628 ? ? 2.19 
# 
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 439 ? ? 1_555 O A HOH 638 ? ? 3_555 1.95 
2 1 O A HOH 405 ? ? 1_555 O A HOH 424 ? ? 8_544 2.03 
3 1 O A HOH 588 ? ? 1_555 O A HOH 681 ? ? 8_544 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 TYR A 38  ? ? -163.45 107.10  
2  1 PHE A 118 ? B -55.72  -79.37  
3  1 MET A 119 ? B -16.23  -70.62  
4  1 GLU A 120 ? B -54.68  -75.39  
5  1 ALA A 121 ? B -29.88  -63.28  
6  1 GLN A 123 ? B -55.66  -72.95  
7  1 ALA A 124 ? A -99.13  37.54   
8  1 ALA A 124 ? B -7.32   -37.34  
9  1 ALA A 166 ? ? 65.16   -141.83 
10 1 ARG A 182 ? ? -170.07 137.72  
# 
_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     698 
_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 12.4743191661  -17.8459471987 -18.4684559488 0.160976962571 0.221974903094 0.173177074613 
0.00188530996154 -0.020625925501  -0.0348602131932 0.388239135946 0.298493916488 0.106242622163 -0.25420702641  -0.169378266965  
-0.0408883107751 0.0509334412381  -0.0840000875824 -0.0854133782927 0.00319470914144  -0.0187995165394  -0.0758409231616 
0.0402162622469  0.0258474073366   0.00299903240766  
2 ? 'X-RAY DIFFRACTION' refined -5.78646347021 -11.1773472537 -24.2272245685 0.156370707912 0.136568540561 0.165634746565 
0.00191563441568 -0.0226724890305 -0.0142371700515 0.636431725134 0.688905424718 0.37718136992  -0.21115261781  -0.0163890398787 
0.203333681755   0.0337117007794  0.0522134274111  0.0342347249081  -0.0516434135026  -0.0515621287257  0.0613146569591  
-0.0260566639196 -0.00538586677685 2.35321848919e-05 
3 ? 'X-RAY DIFFRACTION' refined 12.5053499573  -5.51994316677 -11.8434138424 0.186286589318 0.223837252799 0.236003402043 
-0.113341963038  0.0451907493316  -0.132889537293  0.996760323957 0.549575473149 0.183383074425 -0.527978224217 0.277801997952   
-0.009182090008  0.408438666937   -0.134476931146  0.720496795363   -0.0327859249142  -0.130043873418   0.00343398208947 
-0.478381017329  0.282548028123    0.0772214154389   
4 ? 'X-RAY DIFFRACTION' refined -3.53322231911 -18.7823288298 -19.9741666564 0.1514842947   0.124508596503 0.146198104812 
0.00113043488218 -0.0166485759044 -0.0190445042991 1.16327596685  0.615776724573 0.66912473327  -0.161782614694 -0.0364268910329 
-0.0452369169479 0.00633733891014 -0.0217790093007 -0.152826175972  -0.00303683697072 -0.00726400973214 0.0396438840971  
0.0663782481295  -0.00692211725965 0.000133919114908 
# 
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 110 A 95  . 
;chain 'A' and (resid 41 through 110 )
;
3 3 'X-RAY DIFFRACTION' A 111 A 96  A 136 A 121 . 
;chain 'A' and (resid 111 through 136 )
;
4 4 'X-RAY DIFFRACTION' A 137 A 122 A 224 A 209 . 
;chain 'A' and (resid 137 through 224 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       749 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.91 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AXQ C4   C  Y N 1   
A1AXQ C6   C  Y N 2   
A1AXQ C2   C  Y N 3   
A1AXQ C9   C  Y N 4   
A1AXQ C7   C  Y N 5   
A1AXQ O1   O  Y N 6   
A1AXQ C1   C  N N 7   
A1AXQ C3   C  Y N 8   
A1AXQ C5   C  Y N 9   
A1AXQ C8   C  Y N 10  
A1AXQ N1   N  Y N 11  
A1AXQ N2   N  Y N 12  
A1AXQ BR1  BR N N 13  
A1AXQ H6   H  N N 14  
A1AXQ H9   H  N N 15  
A1AXQ H7   H  N N 16  
A1AXQ H12  H  N N 17  
A1AXQ H11  H  N N 18  
A1AXQ H13  H  N N 19  
A1AXQ H5   H  N N 20  
ALA   N    N  N N 21  
ALA   CA   C  N S 22  
ALA   C    C  N N 23  
ALA   O    O  N N 24  
ALA   CB   C  N N 25  
ALA   OXT  O  N N 26  
ALA   H    H  N N 27  
ALA   H2   H  N N 28  
ALA   HA   H  N N 29  
ALA   HB1  H  N N 30  
ALA   HB2  H  N N 31  
ALA   HB3  H  N N 32  
ALA   HXT  H  N N 33  
ARG   N    N  N N 34  
ARG   CA   C  N S 35  
ARG   C    C  N N 36  
ARG   O    O  N N 37  
ARG   CB   C  N N 38  
ARG   CG   C  N N 39  
ARG   CD   C  N N 40  
ARG   NE   N  N N 41  
ARG   CZ   C  N N 42  
ARG   NH1  N  N N 43  
ARG   NH2  N  N N 44  
ARG   OXT  O  N N 45  
ARG   H    H  N N 46  
ARG   H2   H  N N 47  
ARG   HA   H  N N 48  
ARG   HB2  H  N N 49  
ARG   HB3  H  N N 50  
ARG   HG2  H  N N 51  
ARG   HG3  H  N N 52  
ARG   HD2  H  N N 53  
ARG   HD3  H  N N 54  
ARG   HE   H  N N 55  
ARG   HH11 H  N N 56  
ARG   HH12 H  N N 57  
ARG   HH21 H  N N 58  
ARG   HH22 H  N N 59  
ARG   HXT  H  N N 60  
ASN   N    N  N N 61  
ASN   CA   C  N S 62  
ASN   C    C  N N 63  
ASN   O    O  N N 64  
ASN   CB   C  N N 65  
ASN   CG   C  N N 66  
ASN   OD1  O  N N 67  
ASN   ND2  N  N N 68  
ASN   OXT  O  N N 69  
ASN   H    H  N N 70  
ASN   H2   H  N N 71  
ASN   HA   H  N N 72  
ASN   HB2  H  N N 73  
ASN   HB3  H  N N 74  
ASN   HD21 H  N N 75  
ASN   HD22 H  N N 76  
ASN   HXT  H  N N 77  
ASP   N    N  N N 78  
ASP   CA   C  N S 79  
ASP   C    C  N N 80  
ASP   O    O  N N 81  
ASP   CB   C  N N 82  
ASP   CG   C  N N 83  
ASP   OD1  O  N N 84  
ASP   OD2  O  N N 85  
ASP   OXT  O  N N 86  
ASP   H    H  N N 87  
ASP   H2   H  N N 88  
ASP   HA   H  N N 89  
ASP   HB2  H  N N 90  
ASP   HB3  H  N N 91  
ASP   HD2  H  N N 92  
ASP   HXT  H  N N 93  
GLN   N    N  N N 94  
GLN   CA   C  N S 95  
GLN   C    C  N N 96  
GLN   O    O  N N 97  
GLN   CB   C  N N 98  
GLN   CG   C  N N 99  
GLN   CD   C  N N 100 
GLN   OE1  O  N N 101 
GLN   NE2  N  N N 102 
GLN   OXT  O  N N 103 
GLN   H    H  N N 104 
GLN   H2   H  N N 105 
GLN   HA   H  N N 106 
GLN   HB2  H  N N 107 
GLN   HB3  H  N N 108 
GLN   HG2  H  N N 109 
GLN   HG3  H  N N 110 
GLN   HE21 H  N N 111 
GLN   HE22 H  N N 112 
GLN   HXT  H  N N 113 
GLU   N    N  N N 114 
GLU   CA   C  N S 115 
GLU   C    C  N N 116 
GLU   O    O  N N 117 
GLU   CB   C  N N 118 
GLU   CG   C  N N 119 
GLU   CD   C  N N 120 
GLU   OE1  O  N N 121 
GLU   OE2  O  N N 122 
GLU   OXT  O  N N 123 
GLU   H    H  N N 124 
GLU   H2   H  N N 125 
GLU   HA   H  N N 126 
GLU   HB2  H  N N 127 
GLU   HB3  H  N N 128 
GLU   HG2  H  N N 129 
GLU   HG3  H  N N 130 
GLU   HE2  H  N N 131 
GLU   HXT  H  N N 132 
GLY   N    N  N N 133 
GLY   CA   C  N N 134 
GLY   C    C  N N 135 
GLY   O    O  N N 136 
GLY   OXT  O  N N 137 
GLY   H    H  N N 138 
GLY   H2   H  N N 139 
GLY   HA2  H  N N 140 
GLY   HA3  H  N N 141 
GLY   HXT  H  N N 142 
HIS   N    N  N N 143 
HIS   CA   C  N S 144 
HIS   C    C  N N 145 
HIS   O    O  N N 146 
HIS   CB   C  N N 147 
HIS   CG   C  Y N 148 
HIS   ND1  N  Y N 149 
HIS   CD2  C  Y N 150 
HIS   CE1  C  Y N 151 
HIS   NE2  N  Y N 152 
HIS   OXT  O  N N 153 
HIS   H    H  N N 154 
HIS   H2   H  N N 155 
HIS   HA   H  N N 156 
HIS   HB2  H  N N 157 
HIS   HB3  H  N N 158 
HIS   HD1  H  N N 159 
HIS   HD2  H  N N 160 
HIS   HE1  H  N N 161 
HIS   HE2  H  N N 162 
HIS   HXT  H  N N 163 
HOH   O    O  N N 164 
HOH   H1   H  N N 165 
HOH   H2   H  N N 166 
ILE   N    N  N N 167 
ILE   CA   C  N S 168 
ILE   C    C  N N 169 
ILE   O    O  N N 170 
ILE   CB   C  N S 171 
ILE   CG1  C  N N 172 
ILE   CG2  C  N N 173 
ILE   CD1  C  N N 174 
ILE   OXT  O  N N 175 
ILE   H    H  N N 176 
ILE   H2   H  N N 177 
ILE   HA   H  N N 178 
ILE   HB   H  N N 179 
ILE   HG12 H  N N 180 
ILE   HG13 H  N N 181 
ILE   HG21 H  N N 182 
ILE   HG22 H  N N 183 
ILE   HG23 H  N N 184 
ILE   HD11 H  N N 185 
ILE   HD12 H  N N 186 
ILE   HD13 H  N N 187 
ILE   HXT  H  N N 188 
LEU   N    N  N N 189 
LEU   CA   C  N S 190 
LEU   C    C  N N 191 
LEU   O    O  N N 192 
LEU   CB   C  N N 193 
LEU   CG   C  N N 194 
LEU   CD1  C  N N 195 
LEU   CD2  C  N N 196 
LEU   OXT  O  N N 197 
LEU   H    H  N N 198 
LEU   H2   H  N N 199 
LEU   HA   H  N N 200 
LEU   HB2  H  N N 201 
LEU   HB3  H  N N 202 
LEU   HG   H  N N 203 
LEU   HD11 H  N N 204 
LEU   HD12 H  N N 205 
LEU   HD13 H  N N 206 
LEU   HD21 H  N N 207 
LEU   HD22 H  N N 208 
LEU   HD23 H  N N 209 
LEU   HXT  H  N N 210 
LYS   N    N  N N 211 
LYS   CA   C  N S 212 
LYS   C    C  N N 213 
LYS   O    O  N N 214 
LYS   CB   C  N N 215 
LYS   CG   C  N N 216 
LYS   CD   C  N N 217 
LYS   CE   C  N N 218 
LYS   NZ   N  N N 219 
LYS   OXT  O  N N 220 
LYS   H    H  N N 221 
LYS   H2   H  N N 222 
LYS   HA   H  N N 223 
LYS   HB2  H  N N 224 
LYS   HB3  H  N N 225 
LYS   HG2  H  N N 226 
LYS   HG3  H  N N 227 
LYS   HD2  H  N N 228 
LYS   HD3  H  N N 229 
LYS   HE2  H  N N 230 
LYS   HE3  H  N N 231 
LYS   HZ1  H  N N 232 
LYS   HZ2  H  N N 233 
LYS   HZ3  H  N N 234 
LYS   HXT  H  N N 235 
MET   N    N  N N 236 
MET   CA   C  N S 237 
MET   C    C  N N 238 
MET   O    O  N N 239 
MET   CB   C  N N 240 
MET   CG   C  N N 241 
MET   SD   S  N N 242 
MET   CE   C  N N 243 
MET   OXT  O  N N 244 
MET   H    H  N N 245 
MET   H2   H  N N 246 
MET   HA   H  N N 247 
MET   HB2  H  N N 248 
MET   HB3  H  N N 249 
MET   HG2  H  N N 250 
MET   HG3  H  N N 251 
MET   HE1  H  N N 252 
MET   HE2  H  N N 253 
MET   HE3  H  N N 254 
MET   HXT  H  N N 255 
PHE   N    N  N N 256 
PHE   CA   C  N S 257 
PHE   C    C  N N 258 
PHE   O    O  N N 259 
PHE   CB   C  N N 260 
PHE   CG   C  Y N 261 
PHE   CD1  C  Y N 262 
PHE   CD2  C  Y N 263 
PHE   CE1  C  Y N 264 
PHE   CE2  C  Y N 265 
PHE   CZ   C  Y N 266 
PHE   OXT  O  N N 267 
PHE   H    H  N N 268 
PHE   H2   H  N N 269 
PHE   HA   H  N N 270 
PHE   HB2  H  N N 271 
PHE   HB3  H  N N 272 
PHE   HD1  H  N N 273 
PHE   HD2  H  N N 274 
PHE   HE1  H  N N 275 
PHE   HE2  H  N N 276 
PHE   HZ   H  N N 277 
PHE   HXT  H  N N 278 
PRO   N    N  N N 279 
PRO   CA   C  N S 280 
PRO   C    C  N N 281 
PRO   O    O  N N 282 
PRO   CB   C  N N 283 
PRO   CG   C  N N 284 
PRO   CD   C  N N 285 
PRO   OXT  O  N N 286 
PRO   H    H  N N 287 
PRO   HA   H  N N 288 
PRO   HB2  H  N N 289 
PRO   HB3  H  N N 290 
PRO   HG2  H  N N 291 
PRO   HG3  H  N N 292 
PRO   HD2  H  N N 293 
PRO   HD3  H  N N 294 
PRO   HXT  H  N N 295 
SER   N    N  N N 296 
SER   CA   C  N S 297 
SER   C    C  N N 298 
SER   O    O  N N 299 
SER   CB   C  N N 300 
SER   OG   O  N N 301 
SER   OXT  O  N N 302 
SER   H    H  N N 303 
SER   H2   H  N N 304 
SER   HA   H  N N 305 
SER   HB2  H  N N 306 
SER   HB3  H  N N 307 
SER   HG   H  N N 308 
SER   HXT  H  N N 309 
THR   N    N  N N 310 
THR   CA   C  N S 311 
THR   C    C  N N 312 
THR   O    O  N N 313 
THR   CB   C  N R 314 
THR   OG1  O  N N 315 
THR   CG2  C  N N 316 
THR   OXT  O  N N 317 
THR   H    H  N N 318 
THR   H2   H  N N 319 
THR   HA   H  N N 320 
THR   HB   H  N N 321 
THR   HG1  H  N N 322 
THR   HG21 H  N N 323 
THR   HG22 H  N N 324 
THR   HG23 H  N N 325 
THR   HXT  H  N N 326 
TRP   N    N  N N 327 
TRP   CA   C  N S 328 
TRP   C    C  N N 329 
TRP   O    O  N N 330 
TRP   CB   C  N N 331 
TRP   CG   C  Y N 332 
TRP   CD1  C  Y N 333 
TRP   CD2  C  Y N 334 
TRP   NE1  N  Y N 335 
TRP   CE2  C  Y N 336 
TRP   CE3  C  Y N 337 
TRP   CZ2  C  Y N 338 
TRP   CZ3  C  Y N 339 
TRP   CH2  C  Y N 340 
TRP   OXT  O  N N 341 
TRP   H    H  N N 342 
TRP   H2   H  N N 343 
TRP   HA   H  N N 344 
TRP   HB2  H  N N 345 
TRP   HB3  H  N N 346 
TRP   HD1  H  N N 347 
TRP   HE1  H  N N 348 
TRP   HE3  H  N N 349 
TRP   HZ2  H  N N 350 
TRP   HZ3  H  N N 351 
TRP   HH2  H  N N 352 
TRP   HXT  H  N N 353 
TYR   N    N  N N 354 
TYR   CA   C  N S 355 
TYR   C    C  N N 356 
TYR   O    O  N N 357 
TYR   CB   C  N N 358 
TYR   CG   C  Y N 359 
TYR   CD1  C  Y N 360 
TYR   CD2  C  Y N 361 
TYR   CE1  C  Y N 362 
TYR   CE2  C  Y N 363 
TYR   CZ   C  Y N 364 
TYR   OH   O  N N 365 
TYR   OXT  O  N N 366 
TYR   H    H  N N 367 
TYR   H2   H  N N 368 
TYR   HA   H  N N 369 
TYR   HB2  H  N N 370 
TYR   HB3  H  N N 371 
TYR   HD1  H  N N 372 
TYR   HD2  H  N N 373 
TYR   HE1  H  N N 374 
TYR   HE2  H  N N 375 
TYR   HH   H  N N 376 
TYR   HXT  H  N N 377 
VAL   N    N  N N 378 
VAL   CA   C  N S 379 
VAL   C    C  N N 380 
VAL   O    O  N N 381 
VAL   CB   C  N N 382 
VAL   CG1  C  N N 383 
VAL   CG2  C  N N 384 
VAL   OXT  O  N N 385 
VAL   H    H  N N 386 
VAL   H2   H  N N 387 
VAL   HA   H  N N 388 
VAL   HB   H  N N 389 
VAL   HG11 H  N N 390 
VAL   HG12 H  N N 391 
VAL   HG13 H  N N 392 
VAL   HG21 H  N N 393 
VAL   HG22 H  N N 394 
VAL   HG23 H  N N 395 
VAL   HXT  H  N N 396 
# 
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 
A1AXQ C1  C2   sing N N 1   
A1AXQ C2  N1   doub Y N 2   
A1AXQ C2  O1   sing Y N 3   
A1AXQ N1  N2   sing Y N 4   
A1AXQ N2  C3   doub Y N 5   
A1AXQ C3  O1   sing Y N 6   
A1AXQ C3  C4   sing N N 7   
A1AXQ C4  C5   doub Y N 8   
A1AXQ C4  C9   sing Y N 9   
A1AXQ C5  C6   sing Y N 10  
A1AXQ C6  C7   doub Y N 11  
A1AXQ C7  C8   sing Y N 12  
A1AXQ C8  BR1  sing N N 13  
A1AXQ C8  C9   doub Y N 14  
A1AXQ C6  H6   sing N N 15  
A1AXQ C9  H9   sing N N 16  
A1AXQ C7  H7   sing N N 17  
A1AXQ C1  H12  sing N N 18  
A1AXQ C1  H11  sing N N 19  
A1AXQ C1  H13  sing N N 20  
A1AXQ C5  H5   sing N N 21  
ALA   N   CA   sing N N 22  
ALA   N   H    sing N N 23  
ALA   N   H2   sing N N 24  
ALA   CA  C    sing N N 25  
ALA   CA  CB   sing N N 26  
ALA   CA  HA   sing N N 27  
ALA   C   O    doub N N 28  
ALA   C   OXT  sing N N 29  
ALA   CB  HB1  sing N N 30  
ALA   CB  HB2  sing N N 31  
ALA   CB  HB3  sing N N 32  
ALA   OXT HXT  sing N N 33  
ARG   N   CA   sing N N 34  
ARG   N   H    sing N N 35  
ARG   N   H2   sing N N 36  
ARG   CA  C    sing N N 37  
ARG   CA  CB   sing N N 38  
ARG   CA  HA   sing N N 39  
ARG   C   O    doub N N 40  
ARG   C   OXT  sing N N 41  
ARG   CB  CG   sing N N 42  
ARG   CB  HB2  sing N N 43  
ARG   CB  HB3  sing N N 44  
ARG   CG  CD   sing N N 45  
ARG   CG  HG2  sing N N 46  
ARG   CG  HG3  sing N N 47  
ARG   CD  NE   sing N N 48  
ARG   CD  HD2  sing N N 49  
ARG   CD  HD3  sing N N 50  
ARG   NE  CZ   sing N N 51  
ARG   NE  HE   sing N N 52  
ARG   CZ  NH1  sing N N 53  
ARG   CZ  NH2  doub N N 54  
ARG   NH1 HH11 sing N N 55  
ARG   NH1 HH12 sing N N 56  
ARG   NH2 HH21 sing N N 57  
ARG   NH2 HH22 sing N N 58  
ARG   OXT HXT  sing N N 59  
ASN   N   CA   sing N N 60  
ASN   N   H    sing N N 61  
ASN   N   H2   sing N N 62  
ASN   CA  C    sing N N 63  
ASN   CA  CB   sing N N 64  
ASN   CA  HA   sing N N 65  
ASN   C   O    doub N N 66  
ASN   C   OXT  sing N N 67  
ASN   CB  CG   sing N N 68  
ASN   CB  HB2  sing N N 69  
ASN   CB  HB3  sing N N 70  
ASN   CG  OD1  doub N N 71  
ASN   CG  ND2  sing N N 72  
ASN   ND2 HD21 sing N N 73  
ASN   ND2 HD22 sing N N 74  
ASN   OXT HXT  sing N N 75  
ASP   N   CA   sing N N 76  
ASP   N   H    sing N N 77  
ASP   N   H2   sing N N 78  
ASP   CA  C    sing N N 79  
ASP   CA  CB   sing N N 80  
ASP   CA  HA   sing N N 81  
ASP   C   O    doub N N 82  
ASP   C   OXT  sing N N 83  
ASP   CB  CG   sing N N 84  
ASP   CB  HB2  sing N N 85  
ASP   CB  HB3  sing N N 86  
ASP   CG  OD1  doub N N 87  
ASP   CG  OD2  sing N N 88  
ASP   OD2 HD2  sing N N 89  
ASP   OXT HXT  sing N N 90  
GLN   N   CA   sing N N 91  
GLN   N   H    sing N N 92  
GLN   N   H2   sing N N 93  
GLN   CA  C    sing N N 94  
GLN   CA  CB   sing N N 95  
GLN   CA  HA   sing N N 96  
GLN   C   O    doub N N 97  
GLN   C   OXT  sing N N 98  
GLN   CB  CG   sing N N 99  
GLN   CB  HB2  sing N N 100 
GLN   CB  HB3  sing N N 101 
GLN   CG  CD   sing N N 102 
GLN   CG  HG2  sing N N 103 
GLN   CG  HG3  sing N N 104 
GLN   CD  OE1  doub N N 105 
GLN   CD  NE2  sing N N 106 
GLN   NE2 HE21 sing N N 107 
GLN   NE2 HE22 sing N N 108 
GLN   OXT HXT  sing N N 109 
GLU   N   CA   sing N N 110 
GLU   N   H    sing N N 111 
GLU   N   H2   sing N N 112 
GLU   CA  C    sing N N 113 
GLU   CA  CB   sing N N 114 
GLU   CA  HA   sing N N 115 
GLU   C   O    doub N N 116 
GLU   C   OXT  sing N N 117 
GLU   CB  CG   sing N N 118 
GLU   CB  HB2  sing N N 119 
GLU   CB  HB3  sing N N 120 
GLU   CG  CD   sing N N 121 
GLU   CG  HG2  sing N N 122 
GLU   CG  HG3  sing N N 123 
GLU   CD  OE1  doub N N 124 
GLU   CD  OE2  sing N N 125 
GLU   OE2 HE2  sing N N 126 
GLU   OXT HXT  sing N N 127 
GLY   N   CA   sing N N 128 
GLY   N   H    sing N N 129 
GLY   N   H2   sing N N 130 
GLY   CA  C    sing N N 131 
GLY   CA  HA2  sing N N 132 
GLY   CA  HA3  sing N N 133 
GLY   C   O    doub N N 134 
GLY   C   OXT  sing N N 135 
GLY   OXT HXT  sing N N 136 
HIS   N   CA   sing N N 137 
HIS   N   H    sing N N 138 
HIS   N   H2   sing N N 139 
HIS   CA  C    sing N N 140 
HIS   CA  CB   sing N N 141 
HIS   CA  HA   sing N N 142 
HIS   C   O    doub N N 143 
HIS   C   OXT  sing N N 144 
HIS   CB  CG   sing N N 145 
HIS   CB  HB2  sing N N 146 
HIS   CB  HB3  sing N N 147 
HIS   CG  ND1  sing Y N 148 
HIS   CG  CD2  doub Y N 149 
HIS   ND1 CE1  doub Y N 150 
HIS   ND1 HD1  sing N N 151 
HIS   CD2 NE2  sing Y N 152 
HIS   CD2 HD2  sing N N 153 
HIS   CE1 NE2  sing Y N 154 
HIS   CE1 HE1  sing N N 155 
HIS   NE2 HE2  sing N N 156 
HIS   OXT HXT  sing N N 157 
HOH   O   H1   sing N N 158 
HOH   O   H2   sing N N 159 
ILE   N   CA   sing N N 160 
ILE   N   H    sing N N 161 
ILE   N   H2   sing N N 162 
ILE   CA  C    sing N N 163 
ILE   CA  CB   sing N N 164 
ILE   CA  HA   sing N N 165 
ILE   C   O    doub N N 166 
ILE   C   OXT  sing N N 167 
ILE   CB  CG1  sing N N 168 
ILE   CB  CG2  sing N N 169 
ILE   CB  HB   sing N N 170 
ILE   CG1 CD1  sing N N 171 
ILE   CG1 HG12 sing N N 172 
ILE   CG1 HG13 sing N N 173 
ILE   CG2 HG21 sing N N 174 
ILE   CG2 HG22 sing N N 175 
ILE   CG2 HG23 sing N N 176 
ILE   CD1 HD11 sing N N 177 
ILE   CD1 HD12 sing N N 178 
ILE   CD1 HD13 sing N N 179 
ILE   OXT HXT  sing N N 180 
LEU   N   CA   sing N N 181 
LEU   N   H    sing N N 182 
LEU   N   H2   sing N N 183 
LEU   CA  C    sing N N 184 
LEU   CA  CB   sing N N 185 
LEU   CA  HA   sing N N 186 
LEU   C   O    doub N N 187 
LEU   C   OXT  sing N N 188 
LEU   CB  CG   sing N N 189 
LEU   CB  HB2  sing N N 190 
LEU   CB  HB3  sing N N 191 
LEU   CG  CD1  sing N N 192 
LEU   CG  CD2  sing N N 193 
LEU   CG  HG   sing N N 194 
LEU   CD1 HD11 sing N N 195 
LEU   CD1 HD12 sing N N 196 
LEU   CD1 HD13 sing N N 197 
LEU   CD2 HD21 sing N N 198 
LEU   CD2 HD22 sing N N 199 
LEU   CD2 HD23 sing N N 200 
LEU   OXT HXT  sing N N 201 
LYS   N   CA   sing N N 202 
LYS   N   H    sing N N 203 
LYS   N   H2   sing N N 204 
LYS   CA  C    sing N N 205 
LYS   CA  CB   sing N N 206 
LYS   CA  HA   sing N N 207 
LYS   C   O    doub N N 208 
LYS   C   OXT  sing N N 209 
LYS   CB  CG   sing N N 210 
LYS   CB  HB2  sing N N 211 
LYS   CB  HB3  sing N N 212 
LYS   CG  CD   sing N N 213 
LYS   CG  HG2  sing N N 214 
LYS   CG  HG3  sing N N 215 
LYS   CD  CE   sing N N 216 
LYS   CD  HD2  sing N N 217 
LYS   CD  HD3  sing N N 218 
LYS   CE  NZ   sing N N 219 
LYS   CE  HE2  sing N N 220 
LYS   CE  HE3  sing N N 221 
LYS   NZ  HZ1  sing N N 222 
LYS   NZ  HZ2  sing N N 223 
LYS   NZ  HZ3  sing N N 224 
LYS   OXT HXT  sing N N 225 
MET   N   CA   sing N N 226 
MET   N   H    sing N N 227 
MET   N   H2   sing N N 228 
MET   CA  C    sing N N 229 
MET   CA  CB   sing N N 230 
MET   CA  HA   sing N N 231 
MET   C   O    doub N N 232 
MET   C   OXT  sing N N 233 
MET   CB  CG   sing N N 234 
MET   CB  HB2  sing N N 235 
MET   CB  HB3  sing N N 236 
MET   CG  SD   sing N N 237 
MET   CG  HG2  sing N N 238 
MET   CG  HG3  sing N N 239 
MET   SD  CE   sing N N 240 
MET   CE  HE1  sing N N 241 
MET   CE  HE2  sing N N 242 
MET   CE  HE3  sing N N 243 
MET   OXT HXT  sing N N 244 
PHE   N   CA   sing N N 245 
PHE   N   H    sing N N 246 
PHE   N   H2   sing N N 247 
PHE   CA  C    sing N N 248 
PHE   CA  CB   sing N N 249 
PHE   CA  HA   sing N N 250 
PHE   C   O    doub N N 251 
PHE   C   OXT  sing N N 252 
PHE   CB  CG   sing N N 253 
PHE   CB  HB2  sing N N 254 
PHE   CB  HB3  sing N N 255 
PHE   CG  CD1  doub Y N 256 
PHE   CG  CD2  sing Y N 257 
PHE   CD1 CE1  sing Y N 258 
PHE   CD1 HD1  sing N N 259 
PHE   CD2 CE2  doub Y N 260 
PHE   CD2 HD2  sing N N 261 
PHE   CE1 CZ   doub Y N 262 
PHE   CE1 HE1  sing N N 263 
PHE   CE2 CZ   sing Y N 264 
PHE   CE2 HE2  sing N N 265 
PHE   CZ  HZ   sing N N 266 
PHE   OXT HXT  sing N N 267 
PRO   N   CA   sing N N 268 
PRO   N   CD   sing N N 269 
PRO   N   H    sing N N 270 
PRO   CA  C    sing N N 271 
PRO   CA  CB   sing N N 272 
PRO   CA  HA   sing N N 273 
PRO   C   O    doub N N 274 
PRO   C   OXT  sing N N 275 
PRO   CB  CG   sing N N 276 
PRO   CB  HB2  sing N N 277 
PRO   CB  HB3  sing N N 278 
PRO   CG  CD   sing N N 279 
PRO   CG  HG2  sing N N 280 
PRO   CG  HG3  sing N N 281 
PRO   CD  HD2  sing N N 282 
PRO   CD  HD3  sing N N 283 
PRO   OXT HXT  sing N N 284 
SER   N   CA   sing N N 285 
SER   N   H    sing N N 286 
SER   N   H2   sing N N 287 
SER   CA  C    sing N N 288 
SER   CA  CB   sing N N 289 
SER   CA  HA   sing N N 290 
SER   C   O    doub N N 291 
SER   C   OXT  sing N N 292 
SER   CB  OG   sing N N 293 
SER   CB  HB2  sing N N 294 
SER   CB  HB3  sing N N 295 
SER   OG  HG   sing N N 296 
SER   OXT HXT  sing N N 297 
THR   N   CA   sing N N 298 
THR   N   H    sing N N 299 
THR   N   H2   sing N N 300 
THR   CA  C    sing N N 301 
THR   CA  CB   sing N N 302 
THR   CA  HA   sing N N 303 
THR   C   O    doub N N 304 
THR   C   OXT  sing N N 305 
THR   CB  OG1  sing N N 306 
THR   CB  CG2  sing N N 307 
THR   CB  HB   sing N N 308 
THR   OG1 HG1  sing N N 309 
THR   CG2 HG21 sing N N 310 
THR   CG2 HG22 sing N N 311 
THR   CG2 HG23 sing N N 312 
THR   OXT HXT  sing N N 313 
TRP   N   CA   sing N N 314 
TRP   N   H    sing N N 315 
TRP   N   H2   sing N N 316 
TRP   CA  C    sing N N 317 
TRP   CA  CB   sing N N 318 
TRP   CA  HA   sing N N 319 
TRP   C   O    doub N N 320 
TRP   C   OXT  sing N N 321 
TRP   CB  CG   sing N N 322 
TRP   CB  HB2  sing N N 323 
TRP   CB  HB3  sing N N 324 
TRP   CG  CD1  doub Y N 325 
TRP   CG  CD2  sing Y N 326 
TRP   CD1 NE1  sing Y N 327 
TRP   CD1 HD1  sing N N 328 
TRP   CD2 CE2  doub Y N 329 
TRP   CD2 CE3  sing Y N 330 
TRP   NE1 CE2  sing Y N 331 
TRP   NE1 HE1  sing N N 332 
TRP   CE2 CZ2  sing Y N 333 
TRP   CE3 CZ3  doub Y N 334 
TRP   CE3 HE3  sing N N 335 
TRP   CZ2 CH2  doub Y N 336 
TRP   CZ2 HZ2  sing N N 337 
TRP   CZ3 CH2  sing Y N 338 
TRP   CZ3 HZ3  sing N N 339 
TRP   CH2 HH2  sing N N 340 
TRP   OXT HXT  sing N N 341 
TYR   N   CA   sing N N 342 
TYR   N   H    sing N N 343 
TYR   N   H2   sing N N 344 
TYR   CA  C    sing N N 345 
TYR   CA  CB   sing N N 346 
TYR   CA  HA   sing N N 347 
TYR   C   O    doub N N 348 
TYR   C   OXT  sing N N 349 
TYR   CB  CG   sing N N 350 
TYR   CB  HB2  sing N N 351 
TYR   CB  HB3  sing N N 352 
TYR   CG  CD1  doub Y N 353 
TYR   CG  CD2  sing Y N 354 
TYR   CD1 CE1  sing Y N 355 
TYR   CD1 HD1  sing N N 356 
TYR   CD2 CE2  doub Y N 357 
TYR   CD2 HD2  sing N N 358 
TYR   CE1 CZ   doub Y N 359 
TYR   CE1 HE1  sing N N 360 
TYR   CE2 CZ   sing Y N 361 
TYR   CE2 HE2  sing N N 362 
TYR   CZ  OH   sing N N 363 
TYR   OH  HH   sing N N 364 
TYR   OXT HXT  sing N N 365 
VAL   N   CA   sing N N 366 
VAL   N   H    sing N N 367 
VAL   N   H2   sing N N 368 
VAL   CA  C    sing N N 369 
VAL   CA  CB   sing N N 370 
VAL   CA  HA   sing N N 371 
VAL   C   O    doub N N 372 
VAL   C   OXT  sing N N 373 
VAL   CB  CG1  sing N N 374 
VAL   CB  CG2  sing N N 375 
VAL   CB  HB   sing N N 376 
VAL   CG1 HG11 sing N N 377 
VAL   CG1 HG12 sing N N 378 
VAL   CG1 HG13 sing N N 379 
VAL   CG2 HG21 sing N N 380 
VAL   CG2 HG22 sing N N 381 
VAL   CG2 HG23 sing N N 382 
VAL   OXT HXT  sing N N 383 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2021YFC2301405 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         'Crystallographic fragment screening of Human heat shock protein 90' 
_pdbx_deposit_group.group_description   
;Heat shock protein 90 (HSP90) is one of the most active molecular chaperones in cells. It plays a vital role in the cell maturation process and serves as a molecular chaperone involved in many oncogenic proteins folding, assembly and stabilization. Many HSP90 client proteins are kinases or transcription factors involved in signal transduction pathways and are key regulatory factors in tumor growth and maintenance. Therefore, HSP90 inhibitors can be used as drugs for cancer treatment.
;
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002298 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    7HAI 
_atom_sites.fract_transf_matrix[1][1]   0.015120 
_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]   0.011164 
_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]   0.009965 
_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 
BR ? ? 25.79822 9.11301 ? ? 1.35700  25.34896 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLU   A 1 9   ? 4.33906   -28.49589 -38.99611 1.000 46.06161 ? 16  GLU   A N   1 
ATOM   2    C  CA  . GLU   A 1 9   ? 5.61090   -27.81805 -39.23166 1.000 51.01500 ? 16  GLU   A CA  1 
ATOM   3    C  C   . GLU   A 1 9   ? 5.91957   -26.87585 -38.05758 1.000 41.21626 ? 16  GLU   A C   1 
ATOM   4    O  O   . GLU   A 1 9   ? 5.31732   -25.80617 -37.93584 1.000 37.96566 ? 16  GLU   A O   1 
ATOM   5    C  CB  . GLU   A 1 9   ? 5.56726   -27.03922 -40.55008 1.000 57.85861 ? 16  GLU   A CB  1 
ATOM   6    C  CG  . GLU   A 1 9   ? 6.89712   -26.99268 -41.30471 1.000 70.65425 ? 16  GLU   A CG  1 
ATOM   7    C  CD  . GLU   A 1 9   ? 7.91955   -26.03984 -40.70614 1.000 72.72248 ? 16  GLU   A CD  1 
ATOM   8    O  OE1 . GLU   A 1 9   ? 7.62900   -25.39453 -39.68016 1.000 78.87221 ? 16  GLU   A OE1 1 
ATOM   9    O  OE2 . GLU   A 1 9   ? 9.04240   -25.94560 -41.25375 1.000 78.74709 ? 16  GLU   A OE2 1 
ATOM   10   N  N   . VAL   A 1 10  ? 6.87483   -27.25267 -37.20897 1.000 30.67085 ? 17  VAL   A N   1 
ATOM   11   C  CA  . VAL   A 1 10  ? 7.10689   -26.57609 -35.93452 1.000 23.58915 ? 17  VAL   A CA  1 
ATOM   12   C  C   . VAL   A 1 10  ? 8.47218   -25.90686 -35.98556 1.000 23.67149 ? 17  VAL   A C   1 
ATOM   13   O  O   . VAL   A 1 10  ? 9.45535   -26.55535 -36.35760 1.000 25.62077 ? 17  VAL   A O   1 
ATOM   14   C  CB  . VAL   A 1 10  ? 7.05154   -27.57682 -34.77385 1.000 26.33491 ? 17  VAL   A CB  1 
ATOM   15   C  CG1 . VAL   A 1 10  ? 7.36384   -26.86068 -33.44658 1.000 27.07674 ? 17  VAL   A CG1 1 
ATOM   16   C  CG2 . VAL   A 1 10  ? 5.71901   -28.31416 -34.76001 1.000 31.31523 ? 17  VAL   A CG2 1 
ATOM   17   N  N   . GLU   A 1 11  ? 8.53488   -24.61875 -35.62727 1.000 19.90019 ? 18  GLU   A N   1 
ATOM   18   C  CA  . GLU   A 1 11  ? 9.78571   -23.86362 -35.58090 1.000 18.16118 ? 18  GLU   A CA  1 
ATOM   19   C  C   . GLU   A 1 11  ? 10.21268  -23.72109 -34.12669 1.000 18.27511 ? 18  GLU   A C   1 
ATOM   20   O  O   . GLU   A 1 11  ? 9.38734   -23.37557 -33.27676 1.000 17.15448 ? 18  GLU   A O   1 
ATOM   21   C  CB  . GLU   A 1 11  ? 9.61082   -22.48299 -36.21649 1.000 17.95768 ? 18  GLU   A CB  1 
ATOM   22   C  CG  . GLU   A 1 11  ? 9.45140   -22.55830 -37.74093 1.000 19.61886 ? 18  GLU   A CG  1 
ATOM   23   C  CD  . GLU   A 1 11  ? 9.24672   -21.18495 -38.33077 1.000 27.20500 ? 18  GLU   A CD  1 
ATOM   24   O  OE1 . GLU   A 1 11  ? 8.18514   -20.57029 -38.06729 1.000 28.39834 ? 18  GLU   A OE1 1 
ATOM   25   O  OE2 . GLU   A 1 11  ? 10.12631  -20.71900 -39.08273 1.000 33.84701 ? 18  GLU   A OE2 1 
ATOM   26   N  N   . THR   A 1 12  ? 11.49046  -24.00533 -33.84220 1.000 16.76088 ? 19  THR   A N   1 
ATOM   27   C  CA  . THR   A 1 12  ? 12.02488  -23.91612 -32.49043 1.000 15.88456 ? 19  THR   A CA  1 
ATOM   28   C  C   . THR   A 1 12  ? 13.02102  -22.77590 -32.45355 1.000 17.47848 ? 19  THR   A C   1 
ATOM   29   O  O   . THR   A 1 12  ? 13.90941  -22.70353 -33.30755 1.000 16.48266 ? 19  THR   A O   1 
ATOM   30   C  CB  . THR   A 1 12  ? 12.70846  -25.22163 -32.07886 1.000 15.70553 ? 19  THR   A CB  1 
ATOM   31   O  OG1 . THR   A 1 12  ? 11.81520  -26.33113 -32.23105 1.000 18.51550 ? 19  THR   A OG1 1 
ATOM   32   C  CG2 . THR   A 1 12  ? 13.13207  -25.14088 -30.61237 1.000 18.08179 ? 19  THR   A CG2 1 
ATOM   33   N  N   . PHE   A 1 13  ? 12.89079  -21.91206 -31.44995 1.000 15.72440 ? 20  PHE   A N   1 
ATOM   34   C  CA  . PHE   A 1 13  ? 13.68041  -20.69812 -31.27151 1.000 16.24451 ? 20  PHE   A CA  1 
ATOM   35   C  C   . PHE   A 1 13  ? 14.36300  -20.71571 -29.91920 1.000 16.43663 ? 20  PHE   A C   1 
ATOM   36   O  O   . PHE   A 1 13  ? 13.81023  -21.21596 -28.93968 1.000 16.11547 ? 20  PHE   A O   1 
ATOM   37   C  CB  . PHE   A 1 13  ? 12.78796  -19.44897 -31.27343 1.000 16.95825 ? 20  PHE   A CB  1 
ATOM   38   C  CG  . PHE   A 1 13  ? 12.04486  -19.23442 -32.56654 1.000 16.93759 ? 20  PHE   A CG  1 
ATOM   39   C  CD1 . PHE   A 1 13  ? 10.84359  -19.89664 -32.80915 1.000 17.67533 ? 20  PHE   A CD1 1 
ATOM   40   C  CD2 . PHE   A 1 13  ? 12.57689  -18.39497 -33.54756 1.000 20.08476 ? 20  PHE   A CD2 1 
ATOM   41   C  CE1 . PHE   A 1 13  ? 10.16846  -19.72181 -34.01506 1.000 18.98134 ? 20  PHE   A CE1 1 
ATOM   42   C  CE2 . PHE   A 1 13  ? 11.90083  -18.20812 -34.75473 1.000 23.77141 ? 20  PHE   A CE2 1 
ATOM   43   C  CZ  . PHE   A 1 13  ? 10.70391  -18.88304 -34.97728 1.000 19.75376 ? 20  PHE   A CZ  1 
ATOM   44   N  N   . ALA   A 1 14  ? 15.52315  -20.08457 -29.83674 1.000 16.85851 ? 21  ALA   A N   1 
ATOM   45   C  CA  . ALA   A 1 14  ? 16.13990  -19.84098 -28.54529 1.000 16.01902 ? 21  ALA   A CA  1 
ATOM   46   C  C   . ALA   A 1 14  ? 15.62173  -18.52790 -27.96828 1.000 16.36177 ? 21  ALA   A C   1 
ATOM   47   O  O   . ALA   A 1 14  ? 15.55660  -17.51962 -28.67917 1.000 17.65714 ? 21  ALA   A O   1 
ATOM   48   C  CB  . ALA   A 1 14  ? 17.65736  -19.78562 -28.69870 1.000 15.83737 ? 21  ALA   A CB  1 
ATOM   49   N  N   . PHE   A 1 15  ? 15.26765  -18.53082 -26.67811 1.000 15.32400 ? 22  PHE   A N   1 
ATOM   50   C  CA  . PHE   A 1 15  ? 15.10461  -17.24717 -25.99656 1.000 15.94789 ? 22  PHE   A CA  1 
ATOM   51   C  C   . PHE   A 1 15  ? 16.39366  -16.43287 -26.03618 1.000 16.61217 ? 22  PHE   A C   1 
ATOM   52   O  O   . PHE   A 1 15  ? 17.51132  -16.96122 -25.93192 1.000 18.35349 ? 22  PHE   A O   1 
ATOM   53   C  CB  . PHE   A 1 15  ? 14.73158  -17.40266 -24.51976 1.000 16.92224 ? 22  PHE   A CB  1 
ATOM   54   C  CG  . PHE   A 1 15  ? 13.33409  -17.95409 -24.28506 1.000 14.43883 ? 22  PHE   A CG  1 
ATOM   55   C  CD1 . PHE   A 1 15  ? 12.17915  -17.20333 -24.57828 1.000 15.45894 ? 22  PHE   A CD1 1 
ATOM   56   C  CD2 . PHE   A 1 15  ? 13.16955  -19.24439 -23.78824 1.000 15.24916 ? 22  PHE   A CD2 1 
ATOM   57   C  CE1 . PHE   A 1 15  ? 10.89916  -17.74534 -24.35353 1.000 14.37627 ? 22  PHE   A CE1 1 
ATOM   58   C  CE2 . PHE   A 1 15  ? 11.91960  -19.78512 -23.57730 1.000 15.20832 ? 22  PHE   A CE2 1 
ATOM   59   C  CZ  . PHE   A 1 15  ? 10.75987  -19.03850 -23.85270 1.000 14.78897 ? 22  PHE   A CZ  1 
ATOM   60   N  N   . GLN   A 1 16  ? 16.22715  -15.12291 -26.15255 1.000 17.29562 ? 23  GLN   A N   1 
ATOM   61   C  CA  . GLN   A 1 16  ? 17.34453  -14.24033 -25.85695 1.000 18.83501 ? 23  GLN   A CA  1 
ATOM   62   C  C   . GLN   A 1 16  ? 17.86712  -14.53849 -24.46233 1.000 19.56575 ? 23  GLN   A C   1 
ATOM   63   O  O   . GLN   A 1 16  ? 17.09531  -14.89801 -23.56529 1.000 18.34538 ? 23  GLN   A O   1 
ATOM   64   C  CB  . GLN   A 1 16  ? 16.89592  -12.78590 -25.95530 1.000 19.39831 ? 23  GLN   A CB  1 
ATOM   65   C  CG  . GLN   A 1 16  ? 16.48230  -12.34783 -27.32651 1.000 22.04112 ? 23  GLN   A CG  1 
ATOM   66   C  CD  . GLN   A 1 16  ? 15.97886  -10.90447 -27.26864 1.000 31.51619 ? 23  GLN   A CD  1 
ATOM   67   O  OE1 . GLN   A 1 16  ? 14.78926  -10.66414 -27.15491 1.000 34.28048 ? 23  GLN   A OE1 1 
ATOM   68   N  NE2 . GLN   A 1 16  ? 16.90693  -9.94120  -27.33452 1.000 35.72107 ? 23  GLN   A NE2 1 
ATOM   69   N  N   . ALA   A 1 17  ? 19.18175  -14.38403 -24.27233 1.000 20.09093 ? 24  ALA   A N   1 
ATOM   70   C  CA  . ALA   A 1 17  ? 19.79288  -14.79331 -23.00831 1.000 19.49794 ? 24  ALA   A CA  1 
ATOM   71   C  C   . ALA   A 1 17  ? 19.14852  -14.09345 -21.82550 1.000 20.30523 ? 24  ALA   A C   1 
ATOM   72   O  O   . ALA   A 1 17  ? 18.91680  -14.71465 -20.77747 1.000 21.34631 ? 24  ALA   A O   1 
ATOM   73   C  CB  . ALA   A 1 17  ? 21.30962  -14.52328 -23.02985 1.000 23.13651 ? 24  ALA   A CB  1 
ATOM   74   N  N   . GLU   A 1 18  ? 18.80922  -12.81339 -21.98214 1.000 21.04646 ? 25  GLU   A N   1 
ATOM   75   C  CA  . GLU   A 1 18  ? 18.24013  -12.07507 -20.86132 1.000 21.63967 ? 25  GLU   A CA  1 
ATOM   76   C  C   . GLU   A 1 18  ? 16.86847  -12.62028 -20.47409 1.000 18.79792 ? 25  GLU   A C   1 
ATOM   77   O  O   . GLU   A 1 18  ? 16.51315  -12.59943 -19.28272 1.000 19.96420 ? 25  GLU   A O   1 
ATOM   78   C  CB  . GLU   A 1 18  ? 18.13244  -10.59270 -21.21036 1.000 23.91257 ? 25  GLU   A CB  1 
ATOM   79   C  CG  . GLU   A 1 18  ? 19.46851  -9.90263  -21.46955 1.000 27.30429 ? 25  GLU   A CG  1 
ATOM   80   C  CD  . GLU   A 1 18  ? 20.03620  -10.12437 -22.86862 1.000 38.11782 ? 25  GLU   A CD  1 
ATOM   81   O  OE1 . GLU   A 1 18  ? 19.42050  -10.82277 -23.68855 1.000 29.89010 ? 25  GLU   A OE1 1 
ATOM   82   O  OE2 . GLU   A 1 18  ? 21.13308  -9.60565  -23.16411 1.000 37.44210 ? 25  GLU   A OE2 1 
ATOM   83   N  N   . ILE   A 1 19  ? 16.10725  -13.10437 -21.45172 1.000 19.07479 ? 26  ILE   A N   1 
ATOM   84   C  CA  . ILE   A 1 19  ? 14.77205  -13.64191 -21.15164 1.000 14.99285 ? 26  ILE   A CA  1 
ATOM   85   C  C   . ILE   A 1 19  ? 14.88909  -15.02899 -20.52803 1.000 16.71949 ? 26  ILE   A C   1 
ATOM   86   O  O   . ILE   A 1 19  ? 14.15675  -15.36111 -19.58788 1.000 18.16249 ? 26  ILE   A O   1 
ATOM   87   C  CB  . ILE   A 1 19  ? 13.87134  -13.64635 -22.40491 1.000 17.82547 ? 26  ILE   A CB  1 
ATOM   88   C  CG1 . ILE   A 1 19  ? 13.33745  -12.23188 -22.72974 1.000 18.29365 ? 26  ILE   A CG1 1 
ATOM   89   C  CG2 . ILE   A 1 19  ? 12.65187  -14.56759 -22.20260 1.000 17.93573 ? 26  ILE   A CG2 1 
ATOM   90   C  CD1 . ILE   A 1 19  ? 14.42465  -11.16188 -23.01715 1.000 25.92293 ? 26  ILE   A CD1 1 
ATOM   91   N  N   . ALA   A 1 20  ? 15.84587  -15.83951 -21.00308 1.000 16.50420 ? 27  ALA   A N   1 
ATOM   92   C  CA  . ALA   A 1 20  ? 16.09555  -17.11212 -20.34568 1.000 16.63916 ? 27  ALA   A CA  1 
ATOM   93   C  C   . ALA   A 1 20  ? 16.46422  -16.89090 -18.88065 1.000 18.38212 ? 27  ALA   A C   1 
ATOM   94   O  O   . ALA   A 1 20  ? 16.07269  -17.66795 -17.99953 1.000 19.55400 ? 27  ALA   A O   1 
ATOM   95   C  CB  . ALA   A 1 20  ? 17.20923  -17.86666 -21.08108 1.000 20.17208 ? 27  ALA   A CB  1 
ATOM   96   N  N   . GLN   A 1 21  ? 17.22490  -15.82799 -18.60564 1.000 18.71007 ? 28  GLN   A N   1 
ATOM   97   C  CA  . GLN   A 1 21  ? 17.60685  -15.53046 -17.23737 1.000 19.33449 ? 28  GLN   A CA  1 
ATOM   98   C  C   . GLN   A 1 21  ? 16.40596  -15.10916 -16.41462 1.000 22.47400 ? 28  GLN   A C   1 
ATOM   99   O  O   . GLN   A 1 21  ? 16.26560  -15.53640 -15.26215 1.000 21.90371 ? 28  GLN   A O   1 
ATOM   100  C  CB  . GLN   A 1 21  ? 18.68591  -14.44469 -17.21329 1.000 22.04532 ? 28  GLN   A CB  1 
ATOM   101  C  CG  . GLN   A 1 21  ? 19.36186  -14.27600 -15.85877 1.000 32.59571 ? 28  GLN   A CG  1 
ATOM   102  C  CD  . GLN   A 1 21  ? 20.38392  -13.12785 -15.88182 1.000 42.15594 ? 28  GLN   A CD  1 
ATOM   103  O  OE1 . GLN   A 1 21  ? 21.15031  -12.93352 -14.92758 1.000 50.36009 ? 28  GLN   A OE1 1 
ATOM   104  N  NE2 . GLN   A 1 21  ? 20.42633  -12.39392 -17.00725 1.000 39.90367 ? 28  GLN   A NE2 1 
ATOM   105  N  N   . LEU   A 1 22  ? 15.53365  -14.27466 -16.98599 1.000 18.20764 ? 29  LEU   A N   1 
ATOM   106  C  CA  . LEU   A 1 22  ? 14.31596  -13.88983 -16.26466 1.000 19.54065 ? 29  LEU   A CA  1 
ATOM   107  C  C   . LEU   A 1 22  ? 13.49959  -15.12028 -15.92012 1.000 19.70798 ? 29  LEU   A C   1 
ATOM   108  O  O   . LEU   A 1 22  ? 13.02751  -15.28946 -14.78465 1.000 18.97586 ? 29  LEU   A O   1 
ATOM   109  C  CB  . LEU   A 1 22  ? 13.48509  -12.92268 -17.10719 1.000 21.71003 ? 29  LEU   A CB  1 
ATOM   110  C  CG  . LEU   A 1 22  ? 12.04268  -12.66184 -16.62078 1.000 20.82491 ? 29  LEU   A CG  1 
ATOM   111  C  CD1 . LEU   A 1 22  ? 12.12545  -11.85539 -15.33748 1.000 24.53442 ? 29  LEU   A CD1 1 
ATOM   112  C  CD2 . LEU   A 1 22  ? 11.19817  -11.94752 -17.66234 1.000 21.86445 ? 29  LEU   A CD2 1 
ATOM   113  N  N   . MET   A 1 23  ? 13.34150  -16.01318 -16.89018 1.000 16.20510 ? 30  MET   A N   1 
ATOM   114  C  CA  . MET   A 1 23  ? 12.53088  -17.19486 -16.62755 1.000 17.82570 ? 30  MET   A CA  1 
ATOM   115  C  C   . MET   A 1 23  ? 13.16054  -18.09772 -15.58168 1.000 17.67022 ? 30  MET   A C   1 
ATOM   116  O  O   . MET   A 1 23  ? 12.45503  -18.60378 -14.69221 1.000 18.06226 ? 30  MET   A O   1 
ATOM   117  C  CB  . MET   A 1 23  ? 12.21863  -17.97539 -17.91359 1.000 19.36309 ? 30  MET   A CB  1 
ATOM   118  C  CG  . MET   A 1 23  ? 11.36269  -17.19465 -18.93437 1.000 16.60573 ? 30  MET   A CG  1 
ATOM   119  S  SD  . MET   A 1 23  ? 11.29505  -17.99773 -20.55192 1.000 18.12492 ? 30  MET   A SD  1 
ATOM   120  C  CE  . MET   A 1 23  ? 10.13790  -19.32188 -20.20721 1.000 20.24053 ? 30  MET   A CE  1 
ATOM   121  N  N   . SER   A 1 24  ? 14.48074  -18.29592 -15.63961 1.000 19.18070 ? 31  SER   A N   1 
ATOM   122  C  CA  . SER   A 1 24  ? 15.07577  -19.12397 -14.59116 1.000 17.58909 ? 31  SER   A CA  1 
ATOM   123  C  C   . SER   A 1 24  ? 14.95744  -18.47242 -13.20615 1.000 23.42278 ? 31  SER   A C   1 
ATOM   124  O  O   . SER   A 1 24  ? 14.72677  -19.18120 -12.21040 1.000 22.68526 ? 31  SER   A O   1 
ATOM   125  C  CB  . SER   A 1 24  ? 16.50003  -19.51312 -15.00792 1.000 24.41317 ? 31  SER   A CB  1 
ATOM   126  O  OG  . SER   A 1 24  ? 17.31851  -18.38834 -14.97709 1.000 35.76290 ? 31  SER   A OG  1 
ATOM   127  N  N   A LEU   A 1 25  ? 15.03967  -17.13669 -13.11871 0.735 18.84456 ? 32  LEU   A N   1 
ATOM   128  N  N   B LEU   A 1 25  ? 15.04394  -17.14131 -13.11931 0.265 19.01853 ? 32  LEU   A N   1 
ATOM   129  C  CA  A LEU   A 1 25  ? 14.84615  -16.48925 -11.81995 0.735 20.75478 ? 32  LEU   A CA  1 
ATOM   130  C  CA  B LEU   A 1 25  ? 14.85485  -16.48859 -11.82542 0.265 20.78648 ? 32  LEU   A CA  1 
ATOM   131  C  C   A LEU   A 1 25  ? 13.43103  -16.72663 -11.30310 0.735 22.98063 ? 32  LEU   A C   1 
ATOM   132  C  C   B LEU   A 1 25  ? 13.43593  -16.69439 -11.30385 0.265 22.88191 ? 32  LEU   A C   1 
ATOM   133  O  O   A LEU   A 1 25  ? 13.22137  -16.99479 -10.10797 0.735 20.60202 ? 32  LEU   A O   1 
ATOM   134  O  O   B LEU   A 1 25  ? 13.23195  -16.93481 -10.10536 0.265 20.81414 ? 32  LEU   A O   1 
ATOM   135  C  CB  A LEU   A 1 25  ? 15.12353  -14.98853 -11.93974 0.735 21.54882 ? 32  LEU   A CB  1 
ATOM   136  C  CB  B LEU   A 1 25  ? 15.17731  -14.99875 -11.93704 0.265 21.63802 ? 32  LEU   A CB  1 
ATOM   137  C  CG  A LEU   A 1 25  ? 14.97155  -14.10029 -10.69598 0.735 25.09424 ? 32  LEU   A CG  1 
ATOM   138  C  CG  B LEU   A 1 25  ? 16.62911  -14.62448 -12.25455 0.265 23.40320 ? 32  LEU   A CG  1 
ATOM   139  C  CD1 A LEU   A 1 25  ? 15.86396  -12.88611 -10.82348 0.735 29.55467 ? 32  LEU   A CD1 1 
ATOM   140  C  CD1 B LEU   A 1 25  ? 16.74200  -13.12341 -12.46809 0.265 27.54425 ? 32  LEU   A CD1 1 
ATOM   141  C  CD2 A LEU   A 1 25  ? 13.53450  -13.65884 -10.46521 0.735 25.67655 ? 32  LEU   A CD2 1 
ATOM   142  C  CD2 B LEU   A 1 25  ? 17.57621  -15.08546 -11.14922 0.265 22.97535 ? 32  LEU   A CD2 1 
ATOM   143  N  N   . ILE   A 1 26  ? 12.44275  -16.62325 -12.19093 1.000 17.38834 ? 33  ILE   A N   1 
ATOM   144  C  CA  . ILE   A 1 26  ? 11.05873  -16.81486 -11.76128 1.000 20.55990 ? 33  ILE   A CA  1 
ATOM   145  C  C   . ILE   A 1 26  ? 10.84684  -18.24653 -11.29031 1.000 20.45076 ? 33  ILE   A C   1 
ATOM   146  O  O   . ILE   A 1 26  ? 10.13510  -18.50428 -10.30477 1.000 20.09758 ? 33  ILE   A O   1 
ATOM   147  C  CB  . ILE   A 1 26  ? 10.12691  -16.45685 -12.92371 1.000 15.69469 ? 33  ILE   A CB  1 
ATOM   148  C  CG1 . ILE   A 1 26  ? 10.15292  -14.94460 -13.12761 1.000 17.59648 ? 33  ILE   A CG1 1 
ATOM   149  C  CG2 . ILE   A 1 26  ? 8.68962   -16.98681 -12.65856 1.000 16.55493 ? 33  ILE   A CG2 1 
ATOM   150  C  CD1 . ILE   A 1 26  ? 9.50468   -14.47959 -14.45475 1.000 18.53155 ? 33  ILE   A CD1 1 
ATOM   151  N  N   . ILE   A 1 27  ? 11.49322  -19.20076 -11.96381 1.000 19.74786 ? 34  ILE   A N   1 
ATOM   152  C  CA  . ILE   A 1 27  ? 11.29268  -20.60872 -11.64973 1.000 22.58479 ? 34  ILE   A CA  1 
ATOM   153  C  C   . ILE   A 1 27  ? 12.06332  -21.01437 -10.40037 1.000 24.23729 ? 34  ILE   A C   1 
ATOM   154  O  O   . ILE   A 1 27  ? 11.56840  -21.80401 -9.59162  1.000 26.44141 ? 34  ILE   A O   1 
ATOM   155  C  CB  . ILE   A 1 27  ? 11.69207  -21.46419 -12.86917 1.000 22.37732 ? 34  ILE   A CB  1 
ATOM   156  C  CG1 . ILE   A 1 27  ? 10.67163  -21.28547 -13.99273 1.000 21.48793 ? 34  ILE   A CG1 1 
ATOM   157  C  CG2 . ILE   A 1 27  ? 11.86353  -22.91877 -12.45137 1.000 23.67880 ? 34  ILE   A CG2 1 
ATOM   158  C  CD1 . ILE   A 1 27  ? 11.20340  -21.67610 -15.38941 1.000 20.97071 ? 34  ILE   A CD1 1 
ATOM   159  N  N   . ASN   A 1 28  ? 13.26247  -20.46491 -10.19519 1.000 21.79293 ? 35  ASN   A N   1 
ATOM   160  C  CA  . ASN   A 1 28  ? 14.15299  -20.96113 -9.14336  1.000 22.86867 ? 35  ASN   A CA  1 
ATOM   161  C  C   . ASN   A 1 28  ? 14.10328  -20.18319 -7.84429  1.000 28.85059 ? 35  ASN   A C   1 
ATOM   162  O  O   . ASN   A 1 28  ? 14.54877  -20.71688 -6.81759  1.000 31.44507 ? 35  ASN   A O   1 
ATOM   163  C  CB  . ASN   A 1 28  ? 15.59549  -20.95508 -9.63614  1.000 24.72366 ? 35  ASN   A CB  1 
ATOM   164  C  CG  . ASN   A 1 28  ? 15.81039  -21.92948 -10.73403 1.000 31.34795 ? 35  ASN   A CG  1 
ATOM   165  O  OD1 . ASN   A 1 28  ? 15.17664  -22.98680 -10.77015 1.000 32.39059 ? 35  ASN   A OD1 1 
ATOM   166  N  ND2 . ASN   A 1 28  ? 16.71498  -21.59566 -11.65250 1.000 36.92062 ? 35  ASN   A ND2 1 
ATOM   167  N  N   . THR   A 1 29  ? 13.64064  -18.93627 -7.84705  1.000 22.44862 ? 36  THR   A N   1 
ATOM   168  C  CA  . THR   A 1 29  ? 13.69686  -18.14815 -6.61687  1.000 21.46887 ? 36  THR   A CA  1 
ATOM   169  C  C   . THR   A 1 29  ? 12.62387  -18.62731 -5.64830  1.000 23.61226 ? 36  THR   A C   1 
ATOM   170  O  O   . THR   A 1 29  ? 11.47240  -18.83221 -6.04165  1.000 24.64349 ? 36  THR   A O   1 
ATOM   171  C  CB  . THR   A 1 29  ? 13.49232  -16.66360 -6.93451  1.000 23.63359 ? 36  THR   A CB  1 
ATOM   172  O  OG1 . THR   A 1 29  ? 14.53369  -16.22210 -7.80715  1.000 24.78767 ? 36  THR   A OG1 1 
ATOM   173  C  CG2 . THR   A 1 29  ? 13.52231  -15.80925 -5.68329  1.000 26.08982 ? 36  THR   A CG2 1 
ATOM   174  N  N   . PHE   A 1 30  ? 12.98220  -18.78989 -4.37435  1.000 21.16774 ? 37  PHE   A N   1 
ATOM   175  C  CA  . PHE   A 1 30  ? 11.93059  -19.03649 -3.39270  1.000 23.43882 ? 37  PHE   A CA  1 
ATOM   176  C  C   . PHE   A 1 30  ? 11.08574  -17.77710 -3.21375  1.000 22.90772 ? 37  PHE   A C   1 
ATOM   177  O  O   . PHE   A 1 30  ? 11.60473  -16.71448 -2.83030  1.000 20.57471 ? 37  PHE   A O   1 
ATOM   178  C  CB  . PHE   A 1 30  ? 12.52595  -19.47081 -2.06425  1.000 23.89085 ? 37  PHE   A CB  1 
ATOM   179  C  CG  . PHE   A 1 30  ? 11.49055  -19.76913 -1.03168  1.000 22.50900 ? 37  PHE   A CG  1 
ATOM   180  C  CD1 . PHE   A 1 30  ? 10.73166  -20.92387 -1.10156  1.000 27.22990 ? 37  PHE   A CD1 1 
ATOM   181  C  CD2 . PHE   A 1 30  ? 11.24538  -18.88044 0.00199   1.000 25.67531 ? 37  PHE   A CD2 1 
ATOM   182  C  CE1 . PHE   A 1 30  ? 9.75198   -21.19765 -0.14027  1.000 30.26947 ? 37  PHE   A CE1 1 
ATOM   183  C  CE2 . PHE   A 1 30  ? 10.25427  -19.14993 0.94798   1.000 23.40853 ? 37  PHE   A CE2 1 
ATOM   184  C  CZ  . PHE   A 1 30  ? 9.52370   -20.31016 0.88409   1.000 24.44941 ? 37  PHE   A CZ  1 
ATOM   185  N  N   . TYR   A 1 31  ? 9.77202   -17.90683 -3.44331  1.000 18.87414 ? 38  TYR   A N   1 
ATOM   186  C  CA  . TYR   A 1 31  ? 8.89420   -16.74445 -3.42876  1.000 20.00296 ? 38  TYR   A CA  1 
ATOM   187  C  C   . TYR   A 1 31  ? 7.45357   -17.24511 -3.30489  1.000 19.53611 ? 38  TYR   A C   1 
ATOM   188  O  O   . TYR   A 1 31  ? 6.89969   -17.80264 -4.25288  1.000 18.91704 ? 38  TYR   A O   1 
ATOM   189  C  CB  . TYR   A 1 31  ? 9.11278   -15.90459 -4.68377  1.000 19.78416 ? 38  TYR   A CB  1 
ATOM   190  C  CG  . TYR   A 1 31  ? 8.10541   -14.80919 -4.81861  1.000 21.53913 ? 38  TYR   A CG  1 
ATOM   191  C  CD1 . TYR   A 1 31  ? 8.23155   -13.63505 -4.05701  1.000 26.00584 ? 38  TYR   A CD1 1 
ATOM   192  C  CD2 . TYR   A 1 31  ? 7.05319   -14.92532 -5.70931  1.000 24.14398 ? 38  TYR   A CD2 1 
ATOM   193  C  CE1 . TYR   A 1 31  ? 7.29019   -12.61803 -4.17383  1.000 31.34960 ? 38  TYR   A CE1 1 
ATOM   194  C  CE2 . TYR   A 1 31  ? 6.12410   -13.91941 -5.82854  1.000 26.42211 ? 38  TYR   A CE2 1 
ATOM   195  C  CZ  . TYR   A 1 31  ? 6.25895   -12.78153 -5.06399  1.000 30.08923 ? 38  TYR   A CZ  1 
ATOM   196  O  OH  . TYR   A 1 31  ? 5.30215   -11.82074 -5.22569  1.000 41.26971 ? 38  TYR   A OH  1 
ATOM   197  N  N   . SER   A 1 32  ? 6.85334   -17.06400 -2.12698  1.000 17.84373 ? 39  SER   A N   1 
ATOM   198  C  CA  . SER   A 1 32  ? 5.60341   -17.74830 -1.80618  1.000 16.68758 ? 39  SER   A CA  1 
ATOM   199  C  C   . SER   A 1 32  ? 4.36976   -17.11602 -2.47365  1.000 19.49579 ? 39  SER   A C   1 
ATOM   200  O  O   . SER   A 1 32  ? 3.35718   -17.80530 -2.67652  1.000 20.70092 ? 39  SER   A O   1 
ATOM   201  C  CB  . SER   A 1 32  ? 5.43455   -17.75308 -0.28849  1.000 18.95502 ? 39  SER   A CB  1 
ATOM   202  O  OG  . SER   A 1 32  ? 6.40523   -18.61872 0.26633   1.000 20.80894 ? 39  SER   A OG  1 
ATOM   203  N  N   . ASN   A 1 33  ? 4.43621   -15.83502 -2.83163  1.000 19.53321 ? 40  ASN   A N   1 
ATOM   204  C  CA  . ASN   A 1 33  ? 3.26349   -15.07384 -3.26809  1.000 18.75264 ? 40  ASN   A CA  1 
ATOM   205  C  C   . ASN   A 1 33  ? 2.98970   -15.30654 -4.76199  1.000 19.08065 ? 40  ASN   A C   1 
ATOM   206  O  O   . ASN   A 1 33  ? 2.95463   -14.37740 -5.57530  1.000 19.62517 ? 40  ASN   A O   1 
ATOM   207  C  CB  . ASN   A 1 33  ? 3.50255   -13.60414 -2.94012  1.000 23.67855 ? 40  ASN   A CB  1 
ATOM   208  C  CG  . ASN   A 1 33  ? 2.33713   -12.69603 -3.32523  1.000 22.85930 ? 40  ASN   A CG  1 
ATOM   209  O  OD1 . ASN   A 1 33  ? 1.19369   -13.07273 -3.20653  1.000 24.05607 ? 40  ASN   A OD1 1 
ATOM   210  N  ND2 . ASN   A 1 33  ? 2.65124   -11.47355 -3.70538  1.000 26.02112 ? 40  ASN   A ND2 1 
ATOM   211  N  N   . LYS   A 1 34  ? 2.73060   -16.58035 -5.09959  1.000 16.00377 ? 41  LYS   A N   1 
ATOM   212  C  CA  . LYS   A 1 34  ? 2.67150   -16.94672 -6.51677  1.000 15.63031 ? 41  LYS   A CA  1 
ATOM   213  C  C   . LYS   A 1 34  ? 1.38422   -16.46257 -7.18267  1.000 15.42854 ? 41  LYS   A C   1 
ATOM   214  O  O   . LYS   A 1 34  ? 1.33613   -16.39702 -8.41417  1.000 15.51637 ? 41  LYS   A O   1 
ATOM   215  C  CB  . LYS   A 1 34  ? 2.75629   -18.45590 -6.65728  1.000 16.40308 ? 41  LYS   A CB  1 
ATOM   216  C  CG  . LYS   A 1 34  ? 4.13132   -19.08468 -6.31166  1.000 17.16262 ? 41  LYS   A CG  1 
ATOM   217  C  CD  . LYS   A 1 34  ? 4.06897   -20.58282 -6.50448  1.000 19.42620 ? 41  LYS   A CD  1 
ATOM   218  C  CE  . LYS   A 1 34  ? 5.41652   -21.28561 -6.29764  1.000 20.14100 ? 41  LYS   A CE  1 
ATOM   219  N  NZ  . LYS   A 1 34  ? 6.39366   -21.05429 -7.41431  1.000 19.66884 ? 41  LYS   A NZ  1 
ATOM   220  N  N   . GLU   A 1 35  ? 0.35294   -16.13644 -6.40552  1.000 14.81174 ? 42  GLU   A N   1 
ATOM   221  C  CA  . GLU   A 1 35  ? -0.97473  -15.87211 -6.95635  1.000 14.53400 ? 42  GLU   A CA  1 
ATOM   222  C  C   . GLU   A 1 35  ? -0.98937  -14.66421 -7.88339  1.000 16.41068 ? 42  GLU   A C   1 
ATOM   223  O  O   . GLU   A 1 35  ? -1.95005  -14.50509 -8.65421  1.000 16.90831 ? 42  GLU   A O   1 
ATOM   224  C  CB  . GLU   A 1 35  ? -1.97222  -15.67988 -5.78177  1.000 16.56961 ? 42  GLU   A CB  1 
ATOM   225  C  CG  . GLU   A 1 35  ? -1.80794  -14.37398 -5.03360  1.000 17.47051 ? 42  GLU   A CG  1 
ATOM   226  C  CD  . GLU   A 1 35  ? -2.75638  -14.22218 -3.81780  1.000 24.36285 ? 42  GLU   A CD  1 
ATOM   227  O  OE1 . GLU   A 1 35  ? -2.94332  -15.21206 -3.09273  1.000 29.33420 ? 42  GLU   A OE1 1 
ATOM   228  O  OE2 . GLU   A 1 35  ? -3.25515  -13.11780 -3.56953  1.000 32.04660 ? 42  GLU   A OE2 1 
ATOM   229  N  N   . ILE   A 1 36  ? 0.03435   -13.79920 -7.80949  1.000 16.59077 ? 43  ILE   A N   1 
ATOM   230  C  CA  . ILE   A 1 36  ? 0.05143   -12.61108 -8.64492  1.000 14.71776 ? 43  ILE   A CA  1 
ATOM   231  C  C   . ILE   A 1 36  ? 0.14501   -12.94422 -10.12430 1.000 15.85363 ? 43  ILE   A C   1 
ATOM   232  O  O   . ILE   A 1 36  ? -0.13705  -12.05884 -10.94502 1.000 15.66795 ? 43  ILE   A O   1 
ATOM   233  C  CB  . ILE   A 1 36  ? 1.18060   -11.65452 -8.23399  1.000 18.76820 ? 43  ILE   A CB  1 
ATOM   234  C  CG1 . ILE   A 1 36  ? 2.53792   -12.33365 -8.35280  1.000 19.14702 ? 43  ILE   A CG1 1 
ATOM   235  C  CG2 . ILE   A 1 36  ? 0.87803   -11.17987 -6.79071  1.000 22.71430 ? 43  ILE   A CG2 1 
ATOM   236  C  CD1 . ILE   A 1 36  ? 3.21568   -12.17175 -9.66148  1.000 25.28678 ? 43  ILE   A CD1 1 
ATOM   237  N  N   . PHE   A 1 37  ? 0.44615   -14.20140 -10.48753 1.000 14.83235 ? 44  PHE   A N   1 
ATOM   238  C  CA  . PHE   A 1 37  ? 0.46696   -14.52713 -11.91661 1.000 16.17920 ? 44  PHE   A CA  1 
ATOM   239  C  C   . PHE   A 1 37  ? -0.87829  -14.19749 -12.55459 1.000 15.93233 ? 44  PHE   A C   1 
ATOM   240  O  O   . PHE   A 1 37  ? -0.94044  -13.76408 -13.71204 1.000 14.09568 ? 44  PHE   A O   1 
ATOM   241  C  CB  . PHE   A 1 37  ? 0.79801   -16.00795 -12.16187 1.000 14.36496 ? 44  PHE   A CB  1 
ATOM   242  C  CG  . PHE   A 1 37  ? -0.38290  -16.92085 -11.94843 1.000 14.16382 ? 44  PHE   A CG  1 
ATOM   243  C  CD1 . PHE   A 1 37  ? -0.72267  -17.37908 -10.67580 1.000 16.24972 ? 44  PHE   A CD1 1 
ATOM   244  C  CD2 . PHE   A 1 37  ? -1.21117  -17.25580 -13.02355 1.000 16.77612 ? 44  PHE   A CD2 1 
ATOM   245  C  CE1 . PHE   A 1 37  ? -1.84033  -18.19657 -10.48231 1.000 15.18723 ? 44  PHE   A CE1 1 
ATOM   246  C  CE2 . PHE   A 1 37  ? -2.33735  -18.06217 -12.82461 1.000 14.56027 ? 44  PHE   A CE2 1 
ATOM   247  C  CZ  . PHE   A 1 37  ? -2.65965  -18.52356 -11.55639 1.000 16.43145 ? 44  PHE   A CZ  1 
ATOM   248  N  N   . LEU   A 1 38  ? -1.98460  -14.41195 -11.82137 1.000 13.12217 ? 45  LEU   A N   1 
ATOM   249  C  CA  . LEU   A 1 38  ? -3.27932  -14.27658 -12.47686 1.000 12.32184 ? 45  LEU   A CA  1 
ATOM   250  C  C   . LEU   A 1 38  ? -3.58504  -12.80346 -12.69714 1.000 12.85826 ? 45  LEU   A C   1 
ATOM   251  O  O   . LEU   A 1 38  ? -4.12634  -12.40414 -13.74597 1.000 14.49903 ? 45  LEU   A O   1 
ATOM   252  C  CB  . LEU   A 1 38  ? -4.35344  -14.92677 -11.60475 1.000 14.30994 ? 45  LEU   A CB  1 
ATOM   253  C  CG  . LEU   A 1 38  ? -5.76028  -14.96525 -12.23543 1.000 15.49613 ? 45  LEU   A CG  1 
ATOM   254  C  CD1 . LEU   A 1 38  ? -5.70851  -15.63561 -13.59741 1.000 14.76439 ? 45  LEU   A CD1 1 
ATOM   255  C  CD2 . LEU   A 1 38  ? -6.77122  -15.66539 -11.28566 1.000 18.94777 ? 45  LEU   A CD2 1 
ATOM   256  N  N   . ARG   A 1 39  ? -3.19039  -11.96721 -11.71931 1.000 15.63893 ? 46  ARG   A N   1 
ATOM   257  C  CA  . ARG   A 1 39  ? -3.31092  -10.52050 -11.87950 1.000 14.00310 ? 46  ARG   A CA  1 
ATOM   258  C  C   . ARG   A 1 39  ? -2.55025  -10.03998 -13.09225 1.000 17.06157 ? 46  ARG   A C   1 
ATOM   259  O  O   . ARG   A 1 39  ? -3.04819  -9.20871  -13.86261 1.000 16.56803 ? 46  ARG   A O   1 
ATOM   260  C  CB  . ARG   A 1 39  ? -2.77023  -9.80011  -10.62769 1.000 17.99139 ? 46  ARG   A CB  1 
ATOM   261  C  CG  . ARG   A 1 39  ? -2.68097  -8.30209  -10.78949 1.000 20.82338 ? 46  ARG   A CG  1 
ATOM   262  C  CD  . ARG   A 1 39  ? -1.99451  -7.63413  -9.56747  1.000 21.74011 ? 46  ARG   A CD  1 
ATOM   263  N  NE  . ARG   A 1 39  ? -0.54661  -7.85790  -9.53815  1.000 25.82621 ? 46  ARG   A NE  1 
ATOM   264  C  CZ  . ARG   A 1 39  ? 0.20321   -7.78841  -8.45020  1.000 25.05086 ? 46  ARG   A CZ  1 
ATOM   265  N  NH1 . ARG   A 1 39  ? -0.30126  -7.43582  -7.28097  1.000 25.69805 ? 46  ARG   A NH1 1 
ATOM   266  N  NH2 . ARG   A 1 39  ? 1.50719   -8.04970  -8.54239  1.000 25.76703 ? 46  ARG   A NH2 1 
ATOM   267  N  N   . GLU   A 1 40  ? -1.35944  -10.58656 -13.30678 1.000 15.41847 ? 47  GLU   A N   1 
ATOM   268  C  CA  . GLU   A 1 40  ? -0.52815  -10.09543 -14.39145 1.000 15.38338 ? 47  GLU   A CA  1 
ATOM   269  C  C   . GLU   A 1 40  ? -1.12258  -10.48340 -15.73676 1.000 16.04972 ? 47  GLU   A C   1 
ATOM   270  O  O   . GLU   A 1 40  ? -1.10338  -9.69183  -16.69295 1.000 14.64976 ? 47  GLU   A O   1 
ATOM   271  C  CB  . GLU   A 1 40  ? 0.87966   -10.67297 -14.24611 1.000 14.14958 ? 47  GLU   A CB  1 
ATOM   272  C  CG  . GLU   A 1 40  ? 1.57470   -10.14917 -12.98764 1.000 15.91106 ? 47  GLU   A CG  1 
ATOM   273  C  CD  . GLU   A 1 40  ? 1.56292   -8.63949  -12.85431 1.000 21.83622 ? 47  GLU   A CD  1 
ATOM   274  O  OE1 . GLU   A 1 40  ? 1.66436   -7.94273  -13.88638 1.000 21.74589 ? 47  GLU   A OE1 1 
ATOM   275  O  OE2 . GLU   A 1 40  ? 1.41276   -8.12703  -11.71486 1.000 26.12482 ? 47  GLU   A OE2 1 
ATOM   276  N  N   . LEU   A 1 41  ? -1.64249  -11.69888 -15.82810 1.000 13.71386 ? 48  LEU   A N   1 
ATOM   277  C  CA  . LEU   A 1 41  ? -2.18910  -12.15595 -17.10339 1.000 13.62572 ? 48  LEU   A CA  1 
ATOM   278  C  C   . LEU   A 1 41  ? -3.50280  -11.45196 -17.41809 1.000 14.32628 ? 48  LEU   A C   1 
ATOM   279  O  O   . LEU   A 1 41  ? -3.77417  -11.10369 -18.57711 1.000 13.18119 ? 48  LEU   A O   1 
ATOM   280  C  CB  . LEU   A 1 41  ? -2.39828  -13.67808 -17.10435 1.000 14.17716 ? 48  LEU   A CB  1 
ATOM   281  C  CG  . LEU   A 1 41  ? -1.09479  -14.47644 -17.02284 1.000 15.13101 ? 48  LEU   A CG  1 
ATOM   282  C  CD1 . LEU   A 1 41  ? -1.39785  -15.98690 -16.87839 1.000 13.38769 ? 48  LEU   A CD1 1 
ATOM   283  C  CD2 . LEU   A 1 41  ? -0.18087  -14.18453 -18.24062 1.000 15.28201 ? 48  LEU   A CD2 1 
ATOM   284  N  N   . ILE   A 1 42  ? -4.32401  -11.21340 -16.39451 1.000 13.66851 ? 49  ILE   A N   1 
ATOM   285  C  CA  . ILE   A 1 42  ? -5.55213  -10.46238 -16.60885 1.000 14.73660 ? 49  ILE   A CA  1 
ATOM   286  C  C   . ILE   A 1 42  ? -5.23877  -9.03304  -17.01290 1.000 14.08002 ? 49  ILE   A C   1 
ATOM   287  O  O   . ILE   A 1 42  ? -5.90979  -8.45861  -17.87943 1.000 16.12513 ? 49  ILE   A O   1 
ATOM   288  C  CB  . ILE   A 1 42  ? -6.45430  -10.53962 -15.35504 1.000 14.32198 ? 49  ILE   A CB  1 
ATOM   289  C  CG1 . ILE   A 1 42  ? -7.01529  -11.94933 -15.25105 1.000 12.27408 ? 49  ILE   A CG1 1 
ATOM   290  C  CG2 . ILE   A 1 42  ? -7.58930  -9.48496  -15.39439 1.000 16.82563 ? 49  ILE   A CG2 1 
ATOM   291  C  CD1 . ILE   A 1 42  ? -7.78184  -12.20037 -13.89202 1.000 20.40748 ? 49  ILE   A CD1 1 
ATOM   292  N  N   . SER   A 1 43  ? -4.17535  -8.44703  -16.43996 1.000 13.98510 ? 50  SER   A N   1 
ATOM   293  C  CA  . SER   A 1 43  ? -3.83919  -7.08718  -16.82053 1.000 14.51907 ? 50  SER   A CA  1 
ATOM   294  C  C   . SER   A 1 43  ? -3.34827  -7.05139  -18.26864 1.000 15.61910 ? 50  SER   A C   1 
ATOM   295  O  O   . SER   A 1 43  ? -3.73840  -6.16110  -19.03015 1.000 15.74771 ? 50  SER   A O   1 
ATOM   296  C  CB  . SER   A 1 43  ? -2.80221  -6.53685  -15.83128 1.000 19.45917 ? 50  SER   A CB  1 
ATOM   297  O  OG  . SER   A 1 43  ? -2.12597  -5.39363  -16.31882 1.000 24.30095 ? 50  SER   A OG  1 
ATOM   298  N  N   . ASN   A 1 44  ? -2.57138  -8.05391  -18.68539 1.000 15.50035 ? 51  ASN   A N   1 
ATOM   299  C  CA  . ASN   A 1 44  ? -2.18615  -8.14140  -20.09593 1.000 15.18769 ? 51  ASN   A CA  1 
ATOM   300  C  C   . ASN   A 1 44  ? -3.41206  -8.25097  -20.98850 1.000 14.74483 ? 51  ASN   A C   1 
ATOM   301  O  O   . ASN   A 1 44  ? -3.47114  -7.62971  -22.05932 1.000 14.70563 ? 51  ASN   A O   1 
ATOM   302  C  CB  . ASN   A 1 44  ? -1.29693  -9.35051  -20.34281 1.000 16.55892 ? 51  ASN   A CB  1 
ATOM   303  C  CG  . ASN   A 1 44  ? 0.08964   -9.15571  -19.82131 1.000 19.87988 ? 51  ASN   A CG  1 
ATOM   304  O  OD1 . ASN   A 1 44  ? 0.43515   -8.10448  -19.28491 1.000 19.26398 ? 51  ASN   A OD1 1 
ATOM   305  N  ND2 . ASN   A 1 44  ? 0.89155   -10.18797 -19.95480 1.000 20.58752 ? 51  ASN   A ND2 1 
ATOM   306  N  N   . SER   A 1 45  ? -4.38699  -9.05908  -20.57436 1.000 12.34678 ? 52  SER   A N   1 
ATOM   307  C  CA  . SER   A 1 45  ? -5.60455  -9.17235  -21.38435 1.000 13.52869 ? 52  SER   A CA  1 
ATOM   308  C  C   . SER   A 1 45  ? -6.31215  -7.82725  -21.48572 1.000 14.21794 ? 52  SER   A C   1 
ATOM   309  O  O   . SER   A 1 45  ? -6.78236  -7.43713  -22.56615 1.000 14.29109 ? 52  SER   A O   1 
ATOM   310  C  CB  . SER   A 1 45  ? -6.54686  -10.22070 -20.78570 1.000 14.08711 ? 52  SER   A CB  1 
ATOM   311  O  OG  . SER   A 1 45  ? -6.01801  -11.54776 -20.92891 1.000 16.34967 ? 52  SER   A OG  1 
ATOM   312  N  N   . SER   A 1 46  ? -6.41443  -7.11176  -20.35563 1.000 12.79392 ? 53  SER   A N   1 
ATOM   313  C  CA  . SER   A 1 46  ? -7.05462  -5.80125  -20.37122 1.000 15.74607 ? 53  SER   A CA  1 
ATOM   314  C  C   . SER   A 1 46  ? -6.31821  -4.84366  -21.30861 1.000 14.63237 ? 53  SER   A C   1 
ATOM   315  O  O   . SER   A 1 46  ? -6.96170  -4.14324  -22.09027 1.000 14.82827 ? 53  SER   A O   1 
ATOM   316  C  CB  . SER   A 1 46  ? -7.15122  -5.24199  -18.93734 1.000 18.61487 ? 53  SER   A CB  1 
ATOM   317  O  OG  . SER   A 1 46  ? -7.67282  -3.91407  -18.95323 1.000 17.68277 ? 53  SER   A OG  1 
ATOM   318  N  N   . ASP   A 1 47  ? -4.97475  -4.87585  -21.31274 1.000 14.53042 ? 54  ASP   A N   1 
ATOM   319  C  CA  . ASP   A 1 47  ? -4.20221  -4.03038  -22.22539 1.000 13.46265 ? 54  ASP   A CA  1 
ATOM   320  C  C   . ASP   A 1 47  ? -4.48753  -4.38036  -23.68665 1.000 17.07648 ? 54  ASP   A C   1 
ATOM   321  O  O   . ASP   A 1 47  ? -4.60416  -3.48258  -24.53880 1.000 17.58094 ? 54  ASP   A O   1 
ATOM   322  C  CB  . ASP   A 1 47  ? -2.70283  -4.17420  -21.93584 1.000 16.90439 ? 54  ASP   A CB  1 
ATOM   323  C  CG  . ASP   A 1 47  ? -2.28933  -3.46505  -20.64734 1.000 20.80942 ? 54  ASP   A CG  1 
ATOM   324  O  OD1 . ASP   A 1 47  ? -3.10050  -2.72100  -20.04377 1.000 19.72121 ? 54  ASP   A OD1 1 
ATOM   325  O  OD2 . ASP   A 1 47  ? -1.14862  -3.70208  -20.19860 1.000 20.16736 ? 54  ASP   A OD2 1 
ATOM   326  N  N   . ALA   A 1 48  ? -4.64521  -5.68267  -23.98617 1.000 15.03030 ? 55  ALA   A N   1 
ATOM   327  C  CA  . ALA   A 1 48  ? -4.92072  -6.12221  -25.35365 1.000 14.81762 ? 55  ALA   A CA  1 
ATOM   328  C  C   . ALA   A 1 48  ? -6.32420  -5.72225  -25.79195 1.000 14.01121 ? 55  ALA   A C   1 
ATOM   329  O  O   . ALA   A 1 48  ? -6.57162  -5.43419  -26.96640 1.000 14.05186 ? 55  ALA   A O   1 
ATOM   330  C  CB  . ALA   A 1 48  ? -4.75243  -7.64848  -25.45973 1.000 13.28136 ? 55  ALA   A CB  1 
ATOM   331  N  N   . LEU   A 1 49  ? -7.27229  -5.79067  -24.86678 1.000 13.18613 ? 56  LEU   A N   1 
ATOM   332  C  CA  . LEU   A 1 49  ? -8.62923  -5.35043  -25.15746 1.000 14.48021 ? 56  LEU   A CA  1 
ATOM   333  C  C   . LEU   A 1 49  ? -8.66680  -3.84458  -25.38542 1.000 15.03749 ? 56  LEU   A C   1 
ATOM   334  O  O   . LEU   A 1 49  ? -9.35581  -3.38247  -26.29043 1.000 16.46707 ? 56  LEU   A O   1 
ATOM   335  C  CB  . LEU   A 1 49  ? -9.54757  -5.77060  -24.01552 1.000 15.87174 ? 56  LEU   A CB  1 
ATOM   336  C  CG  . LEU   A 1 49  ? -9.77388  -7.29085  -23.96349 1.000 15.30866 ? 56  LEU   A CG  1 
ATOM   337  C  CD1 . LEU   A 1 49  ? -10.21614 -7.74703  -22.57830 1.000 16.48846 ? 56  LEU   A CD1 1 
ATOM   338  C  CD2 . LEU   A 1 49  ? -10.85507 -7.68725  -25.01711 1.000 14.89621 ? 56  LEU   A CD2 1 
ATOM   339  N  N   . ASP   A 1 50  ? -7.91242  -3.07658  -24.58864 1.000 15.03008 ? 57  ASP   A N   1 
ATOM   340  C  CA  . ASP   A 1 50  ? -7.86656  -1.63696  -24.82165 1.000 15.19111 ? 57  ASP   A CA  1 
ATOM   341  C  C   . ASP   A 1 50  ? -7.38541  -1.33794  -26.23351 1.000 14.71808 ? 57  ASP   A C   1 
ATOM   342  O  O   . ASP   A 1 50  ? -7.87540  -0.39699  -26.87133 1.000 16.31355 ? 57  ASP   A O   1 
ATOM   343  C  CB  . ASP   A 1 50  ? -6.93614  -0.93368  -23.82822 1.000 15.81741 ? 57  ASP   A CB  1 
ATOM   344  C  CG  . ASP   A 1 50  ? -7.43743  -0.93237  -22.39471 1.000 19.18605 ? 57  ASP   A CG  1 
ATOM   345  O  OD1 . ASP   A 1 50  ? -8.59276  -1.28706  -22.10522 1.000 19.48003 ? 57  ASP   A OD1 1 
ATOM   346  O  OD2 . ASP   A 1 50  ? -6.62286  -0.52337  -21.53921 1.000 21.04863 ? 57  ASP   A OD2 1 
ATOM   347  N  N   . LYS   A 1 51  ? -6.36980  -2.08243  -26.70397 1.000 15.66133 ? 58  LYS   A N   1 
ATOM   348  C  CA  . LYS   A 1 51  ? -5.80070  -1.79944  -28.02180 1.000 15.85543 ? 58  LYS   A CA  1 
ATOM   349  C  C   . LYS   A 1 51  ? -6.82598  -2.00481  -29.13222 1.000 16.85694 ? 58  LYS   A C   1 
ATOM   350  O  O   . LYS   A 1 51  ? -6.95608  -1.15944  -30.03119 1.000 17.44163 ? 58  LYS   A O   1 
ATOM   351  C  CB  . LYS   A 1 51  ? -4.54799  -2.65786  -28.25169 1.000 17.46854 ? 58  LYS   A CB  1 
ATOM   352  C  CG  . LYS   A 1 51  ? -3.39578  -2.23268  -27.37794 1.000 15.45451 ? 58  LYS   A CG  1 
ATOM   353  C  CD  . LYS   A 1 51  ? -2.22723  -3.24518  -27.58522 1.000 17.18120 ? 58  LYS   A CD  1 
ATOM   354  C  CE  . LYS   A 1 51  ? -1.17545  -3.06462  -26.49981 1.000 22.24390 ? 58  LYS   A CE  1 
ATOM   355  N  NZ  . LYS   A 1 51  ? -0.10719  -4.11521  -26.66835 1.000 27.36725 ? 58  LYS   A NZ  1 
ATOM   356  N  N   . ILE   A 1 52  ? -7.54439  -3.13105  -29.12199 1.000 15.16114 ? 59  ILE   A N   1 
ATOM   357  C  CA  . ILE   A 1 52  ? -8.52472  -3.31445  -30.19818 1.000 15.09034 ? 59  ILE   A CA  1 
ATOM   358  C  C   . ILE   A 1 52  ? -9.68945  -2.36368  -30.04435 1.000 16.37234 ? 59  ILE   A C   1 
ATOM   359  O  O   . ILE   A 1 52  ? -10.26599 -1.93557  -31.05001 1.000 18.78356 ? 59  ILE   A O   1 
ATOM   360  C  CB  . ILE   A 1 52  ? -8.97879  -4.79363  -30.29389 1.000 15.93394 ? 59  ILE   A CB  1 
ATOM   361  C  CG1 . ILE   A 1 52  ? -9.76453  -5.07097  -31.59787 1.000 19.24878 ? 59  ILE   A CG1 1 
ATOM   362  C  CG2 . ILE   A 1 52  ? -9.76409  -5.23664  -29.07510 1.000 16.51390 ? 59  ILE   A CG2 1 
ATOM   363  C  CD1 . ILE   A 1 52  ? -9.03206  -4.79554  -32.88853 1.000 20.07585 ? 59  ILE   A CD1 1 
ATOM   364  N  N   . ARG   A 1 53  ? -10.07081 -2.01273  -28.80622 1.000 16.30007 ? 60  ARG   A N   1 
ATOM   365  C  CA  . ARG   A 1 53  ? -11.11481 -1.01024  -28.65875 1.000 17.77988 ? 60  ARG   A CA  1 
ATOM   366  C  C   . ARG   A 1 53  ? -10.68653 0.32565   -29.25499 1.000 17.12519 ? 60  ARG   A C   1 
ATOM   367  O  O   . ARG   A 1 53  ? -11.44965 0.94674   -30.00491 1.000 18.78472 ? 60  ARG   A O   1 
ATOM   368  C  CB  . ARG   A 1 53  ? -11.51363 -0.84734  -27.18931 1.000 18.65496 ? 60  ARG   A CB  1 
ATOM   369  C  CG  . ARG   A 1 53  ? -12.57198 0.23231   -27.10692 1.000 23.32891 ? 60  ARG   A CG  1 
ATOM   370  C  CD  . ARG   A 1 53  ? -13.13923 0.48087   -25.73979 1.000 35.22251 ? 60  ARG   A CD  1 
ATOM   371  N  NE  . ARG   A 1 53  ? -14.16065 -0.48109  -25.32700 1.000 40.21210 ? 60  ARG   A NE  1 
ATOM   372  C  CZ  . ARG   A 1 53  ? -14.25985 -0.95140  -24.08884 1.000 36.84078 ? 60  ARG   A CZ  1 
ATOM   373  N  NH1 . ARG   A 1 53  ? -13.34791 -0.66499  -23.16968 1.000 32.74799 ? 60  ARG   A NH1 1 
ATOM   374  N  NH2 . ARG   A 1 53  ? -15.30256 -1.70888  -23.76087 1.000 35.07612 ? 60  ARG   A NH2 1 
ATOM   375  N  N   . TYR   A 1 54  ? -9.43775  0.75487   -29.00178 1.000 14.96549 ? 61  TYR   A N   1 
ATOM   376  C  CA  . TYR   A 1 54  ? -8.99122  2.03284   -29.55835 1.000 17.81787 ? 61  TYR   A CA  1 
ATOM   377  C  C   . TYR   A 1 54  ? -9.04603  1.98886   -31.07848 1.000 21.08999 ? 61  TYR   A C   1 
ATOM   378  O  O   . TYR   A 1 54  ? -9.53602  2.93069   -31.72273 1.000 20.58981 ? 61  TYR   A O   1 
ATOM   379  C  CB  . TYR   A 1 54  ? -7.57680  2.38169   -29.08019 1.000 19.34637 ? 61  TYR   A CB  1 
ATOM   380  C  CG  . TYR   A 1 54  ? -7.13246  3.75476   -29.57665 1.000 18.69557 ? 61  TYR   A CG  1 
ATOM   381  C  CD1 . TYR   A 1 54  ? -7.70356  4.92065   -29.07730 1.000 18.42758 ? 61  TYR   A CD1 1 
ATOM   382  C  CD2 . TYR   A 1 54  ? -6.20247  3.85745   -30.59459 1.000 21.76065 ? 61  TYR   A CD2 1 
ATOM   383  C  CE1 . TYR   A 1 54  ? -7.32458  6.16015   -29.55259 1.000 19.87497 ? 61  TYR   A CE1 1 
ATOM   384  C  CE2 . TYR   A 1 54  ? -5.80433  5.10697   -31.08854 1.000 23.16218 ? 61  TYR   A CE2 1 
ATOM   385  C  CZ  . TYR   A 1 54  ? -6.36953  6.23641   -30.56210 1.000 21.16638 ? 61  TYR   A CZ  1 
ATOM   386  O  OH  . TYR   A 1 54  ? -5.99906  7.48063   -31.03437 1.000 24.31977 ? 61  TYR   A OH  1 
ATOM   387  N  N   . GLU   A 1 55  ? -8.55808  0.89518   -31.66805 1.000 20.79436 ? 62  GLU   A N   1 
ATOM   388  C  CA  . GLU   A 1 55  ? -8.53819  0.79475   -33.13256 1.000 21.59701 ? 62  GLU   A CA  1 
ATOM   389  C  C   . GLU   A 1 55  ? -9.94868  0.82639   -33.69910 1.000 23.11622 ? 62  GLU   A C   1 
ATOM   390  O  O   . GLU   A 1 55  ? -10.17598 1.42901   -34.76043 1.000 24.09310 ? 62  GLU   A O   1 
ATOM   391  C  CB  . GLU   A 1 55  ? -7.81188  -0.48487  -33.56160 1.000 23.19784 ? 62  GLU   A CB  1 
ATOM   392  C  CG  . GLU   A 1 55  ? -6.30786  -0.36585  -33.43464 1.000 22.95818 ? 62  GLU   A CG  1 
ATOM   393  C  CD  . GLU   A 1 55  ? -5.55278  -1.46646  -34.14309 1.000 30.04913 ? 62  GLU   A CD  1 
ATOM   394  O  OE1 . GLU   A 1 55  ? -4.29892  -1.40770  -34.16579 1.000 34.89674 ? 62  GLU   A OE1 1 
ATOM   395  O  OE2 . GLU   A 1 55  ? -6.20795  -2.40083  -34.65842 1.000 27.39634 ? 62  GLU   A OE2 1 
ATOM   396  N  N   . SER   A 1 56  ? -10.92584 0.26204   -32.97575 1.000 19.88207 ? 63  SER   A N   1 
ATOM   397  C  CA  . SER   A 1 56  ? -12.29601 0.23173   -33.49563 1.000 22.82732 ? 63  SER   A CA  1 
ATOM   398  C  C   . SER   A 1 56  ? -12.93987 1.60921   -33.47767 1.000 23.01679 ? 63  SER   A C   1 
ATOM   399  O  O   . SER   A 1 56  ? -13.95807 1.82060   -34.15847 1.000 23.99236 ? 63  SER   A O   1 
ATOM   400  C  CB  . SER   A 1 56  ? -13.17000 -0.73043  -32.68018 1.000 22.24872 ? 63  SER   A CB  1 
ATOM   401  O  OG  . SER   A 1 56  ? -13.50020 -0.21198  -31.38804 1.000 23.23790 ? 63  SER   A OG  1 
ATOM   402  N  N   . LEU   A 1 57  ? -12.41386 2.54019   -32.68233 1.000 20.06365 ? 64  LEU   A N   1 
ATOM   403  C  CA  . LEU   A 1 57  ? -13.05680 3.84312   -32.57548 1.000 22.71079 ? 64  LEU   A CA  1 
ATOM   404  C  C   . LEU   A 1 57  ? -13.02641 4.58035   -33.89460 1.000 28.65649 ? 64  LEU   A C   1 
ATOM   405  O  O   . LEU   A 1 57  ? -13.89897 5.41257   -34.16079 1.000 32.22456 ? 64  LEU   A O   1 
ATOM   406  C  CB  . LEU   A 1 57  ? -12.38162 4.69546   -31.50048 1.000 21.66947 ? 64  LEU   A CB  1 
ATOM   407  C  CG  . LEU   A 1 57  ? -12.57081 4.16874   -30.08802 1.000 23.91045 ? 64  LEU   A CG  1 
ATOM   408  C  CD1 . LEU   A 1 57  ? -11.94939 5.18318   -29.14574 1.000 25.98036 ? 64  LEU   A CD1 1 
ATOM   409  C  CD2 . LEU   A 1 57  ? -14.01802 3.86721   -29.72287 1.000 26.43882 ? 64  LEU   A CD2 1 
ATOM   410  N  N   . THR   A 1 58  ? -12.03115 4.31965   -34.71855 1.000 24.35368 ? 65  THR   A N   1 
ATOM   411  C  CA  . THR   A 1 58  ? -11.96444 4.95990   -36.02859 1.000 27.29208 ? 65  THR   A CA  1 
ATOM   412  C  C   . THR   A 1 58  ? -12.20203 3.99006   -37.16822 1.000 29.98924 ? 65  THR   A C   1 
ATOM   413  O  O   . THR   A 1 58  ? -12.31525 4.42674   -38.31533 1.000 31.66111 ? 65  THR   A O   1 
ATOM   414  C  CB  . THR   A 1 58  ? -10.59901 5.63242   -36.23454 1.000 31.33887 ? 65  THR   A CB  1 
ATOM   415  O  OG1 . THR   A 1 58  ? -9.55865  4.65287   -36.12754 1.000 34.57916 ? 65  THR   A OG1 1 
ATOM   416  C  CG2 . THR   A 1 58  ? -10.38174 6.73309   -35.19784 1.000 32.37097 ? 65  THR   A CG2 1 
ATOM   417  N  N   . ASP   A 1 59  ? -12.28264 2.69200   -36.89097 1.000 27.96542 ? 66  ASP   A N   1 
ATOM   418  C  CA  . ASP   A 1 59  ? -12.48350 1.69825   -37.94209 1.000 27.42440 ? 66  ASP   A CA  1 
ATOM   419  C  C   . ASP   A 1 59  ? -13.32608 0.57497   -37.35372 1.000 25.35820 ? 66  ASP   A C   1 
ATOM   420  O  O   . ASP   A 1 59  ? -12.79831 -0.39590  -36.78597 1.000 27.46837 ? 66  ASP   A O   1 
ATOM   421  C  CB  . ASP   A 1 59  ? -11.14682 1.18964   -38.47589 1.000 28.29234 ? 66  ASP   A CB  1 
ATOM   422  C  CG  . ASP   A 1 59  ? -11.30565 0.18745   -39.59807 1.000 32.94458 ? 66  ASP   A CG  1 
ATOM   423  O  OD1 . ASP   A 1 59  ? -12.46211 -0.10473  -39.97066 1.000 33.81155 ? 66  ASP   A OD1 1 
ATOM   424  O  OD2 . ASP   A 1 59  ? -10.26714 -0.29294  -40.10701 1.000 32.68505 ? 66  ASP   A OD2 1 
ATOM   425  N  N   . PRO   A 1 60  ? -14.65286 0.67579   -37.46492 1.000 30.70356 ? 67  PRO   A N   1 
ATOM   426  C  CA  . PRO   A 1 60  ? -15.51874 -0.34315  -36.85672 1.000 25.97567 ? 67  PRO   A CA  1 
ATOM   427  C  C   . PRO   A 1 60  ? -15.26729 -1.73294  -37.39503 1.000 27.05034 ? 67  PRO   A C   1 
ATOM   428  O  O   . PRO   A 1 60  ? -15.54142 -2.71310  -36.68765 1.000 27.34649 ? 67  PRO   A O   1 
ATOM   429  C  CB  . PRO   A 1 60  ? -16.92417 0.14893   -37.22636 1.000 31.97154 ? 67  PRO   A CB  1 
ATOM   430  C  CG  . PRO   A 1 60  ? -16.75850 1.61281   -37.28723 1.000 39.70902 ? 67  PRO   A CG  1 
ATOM   431  C  CD  . PRO   A 1 60  ? -15.45250 1.77406   -38.02762 1.000 36.02663 ? 67  PRO   A CD  1 
ATOM   432  N  N   . SER   A 1 61  ? -14.76082 -1.85180  -38.63400 1.000 28.71585 ? 68  SER   A N   1 
ATOM   433  C  CA  . SER   A 1 61  ? -14.55291 -3.17164  -39.20678 1.000 27.61251 ? 68  SER   A CA  1 
ATOM   434  C  C   . SER   A 1 61  ? -13.47159 -3.94603  -38.46555 1.000 28.07058 ? 68  SER   A C   1 
ATOM   435  O  O   . SER   A 1 61  ? -13.33480 -5.15876  -38.67199 1.000 26.55863 ? 68  SER   A O   1 
ATOM   436  C  CB  . SER   A 1 61  ? -14.19292 -3.07751  -40.69178 1.000 27.59403 ? 68  SER   A CB  1 
ATOM   437  O  OG  . SER   A 1 61  ? -12.85992 -2.62614  -40.88842 1.000 29.69930 ? 68  SER   A OG  1 
ATOM   438  N  N   . LYS   A 1 62  ? -12.71311 -3.28099  -37.59329 1.000 24.92447 ? 69  LYS   A N   1 
ATOM   439  C  CA  . LYS   A 1 62  ? -11.74979 -4.00262  -36.77373 1.000 24.37612 ? 69  LYS   A CA  1 
ATOM   440  C  C   . LYS   A 1 62  ? -12.42103 -5.01643  -35.85668 1.000 24.54070 ? 69  LYS   A C   1 
ATOM   441  O  O   . LYS   A 1 62  ? -11.74359 -5.92005  -35.34866 1.000 21.43076 ? 69  LYS   A O   1 
ATOM   442  C  CB  . LYS   A 1 62  ? -10.95149 -3.01774  -35.92593 1.000 24.87691 ? 69  LYS   A CB  1 
ATOM   443  C  CG  . LYS   A 1 62  ? -10.12134 -2.05732  -36.78094 1.000 27.97338 ? 69  LYS   A CG  1 
ATOM   444  C  CD  . LYS   A 1 62  ? -8.68538  -2.51504  -36.79742 1.000 26.80022 ? 69  LYS   A CD  1 
ATOM   445  C  CE  . LYS   A 1 62  ? -7.82947  -1.71033  -37.75241 1.000 29.59993 ? 69  LYS   A CE  1 
ATOM   446  N  NZ  . LYS   A 1 62  ? -6.42226  -2.25111  -37.66804 1.000 34.71172 ? 69  LYS   A NZ  1 
ATOM   447  N  N   . LEU   A 1 63  ? -13.71224 -4.84650  -35.56928 1.000 21.52899 ? 70  LEU   A N   1 
ATOM   448  C  CA  . LEU   A 1 63  ? -14.45586 -5.78384  -34.73539 1.000 20.91094 ? 70  LEU   A CA  1 
ATOM   449  C  C   . LEU   A 1 63  ? -15.23205 -6.80082  -35.56799 1.000 20.04565 ? 70  LEU   A C   1 
ATOM   450  O  O   . LEU   A 1 63  ? -16.07236 -7.52184  -35.01871 1.000 22.19629 ? 70  LEU   A O   1 
ATOM   451  C  CB  . LEU   A 1 63  ? -15.40940 -5.02430  -33.78546 1.000 23.79077 ? 70  LEU   A CB  1 
ATOM   452  C  CG  . LEU   A 1 63  ? -14.69294 -4.07804  -32.81339 1.000 22.52898 ? 70  LEU   A CG  1 
ATOM   453  C  CD1 . LEU   A 1 63  ? -15.66484 -3.40535  -31.84120 1.000 26.07672 ? 70  LEU   A CD1 1 
ATOM   454  C  CD2 . LEU   A 1 63  ? -13.63805 -4.89308  -32.05162 1.000 22.85222 ? 70  LEU   A CD2 1 
ATOM   455  N  N   . ASP   A 1 64  ? -14.97373 -6.88573  -36.88343 1.000 21.46364 ? 71  ASP   A N   1 
ATOM   456  C  CA  . ASP   A 1 64  ? -15.70301 -7.88452  -37.66702 1.000 24.55859 ? 71  ASP   A CA  1 
ATOM   457  C  C   . ASP   A 1 64  ? -15.37947 -9.29660  -37.18800 1.000 24.87633 ? 71  ASP   A C   1 
ATOM   458  O  O   . ASP   A 1 64  ? -16.18849 -10.22044 -37.35464 1.000 25.10960 ? 71  ASP   A O   1 
ATOM   459  C  CB  . ASP   A 1 64  ? -15.36786 -7.75229  -39.15237 1.000 27.19473 ? 71  ASP   A CB  1 
ATOM   460  C  CG  . ASP   A 1 64  ? -16.01896 -6.53392  -39.79680 1.000 35.21962 ? 71  ASP   A CG  1 
ATOM   461  O  OD1 . ASP   A 1 64  ? -16.86825 -5.88219  -39.15744 1.000 30.56254 ? 71  ASP   A OD1 1 
ATOM   462  O  OD2 . ASP   A 1 64  ? -15.68245 -6.23885  -40.95906 1.000 35.03352 ? 71  ASP   A OD2 1 
ATOM   463  N  N   . SER   A 1 65  ? -14.19652 -9.47526  -36.58723 1.000 23.22639 ? 72  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 65  ? -13.70852 -10.72623 -36.02598 1.000 19.66356 ? 72  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 65  ? -14.25024 -10.99784 -34.63374 1.000 25.00398 ? 72  SER   A C   1 
ATOM   466  O  O   . SER   A 1 65  ? -13.83521 -11.97642 -34.00633 1.000 27.52918 ? 72  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 65  ? -12.16265 -10.70886 -35.98453 1.000 21.08128 ? 72  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 65  ? -11.68734 -9.47119  -35.46333 1.000 21.90237 ? 72  SER   A OG  1 
ATOM   469  N  N   . GLY   A 1 66  ? -15.16421 -10.15908 -34.14532 1.000 21.36590 ? 73  GLY   A N   1 
ATOM   470  C  CA  . GLY   A 1 66  ? -15.80831 -10.37856 -32.87419 1.000 25.94853 ? 73  GLY   A CA  1 
ATOM   471  C  C   . GLY   A 1 66  ? -16.03782 -9.06162  -32.16507 1.000 24.78034 ? 73  GLY   A C   1 
ATOM   472  O  O   . GLY   A 1 66  ? -15.08305 -8.32867  -31.88576 1.000 21.39210 ? 73  GLY   A O   1 
ATOM   473  N  N   . LYS   A 1 67  ? -17.29900 -8.75941  -31.84435 1.000 23.26015 ? 74  LYS   A N   1 
ATOM   474  C  CA  . LYS   A 1 67  ? -17.63598 -7.49741  -31.21058 1.000 21.88895 ? 74  LYS   A CA  1 
ATOM   475  C  C   . LYS   A 1 67  ? -17.45654 -7.53358  -29.69401 1.000 22.79471 ? 74  LYS   A C   1 
ATOM   476  O  O   . LYS   A 1 67  ? -17.28199 -6.48066  -29.07775 1.000 26.88097 ? 74  LYS   A O   1 
ATOM   477  C  CB  . LYS   A 1 67  ? -19.10038 -7.13009  -31.51353 1.000 28.19639 ? 74  LYS   A CB  1 
ATOM   478  C  CG  . LYS   A 1 67  ? -19.37358 -6.69781  -32.95721 1.000 38.48205 ? 74  LYS   A CG  1 
ATOM   479  C  CD  . LYS   A 1 67  ? -20.59046 -5.77588  -33.02037 1.000 45.94812 ? 74  LYS   A CD  1 
ATOM   480  C  CE  . LYS   A 1 67  ? -20.89937 -5.35900  -34.44619 1.000 52.18246 ? 74  LYS   A CE  1 
ATOM   481  N  NZ  . LYS   A 1 67  ? -19.74053 -5.60109  -35.34715 1.000 54.35911 ? 74  LYS   A NZ  1 
ATOM   482  N  N   . GLU   A 1 68  ? -17.53120 -8.70927  -29.06955 1.000 22.44746 ? 75  GLU   A N   1 
ATOM   483  C  CA  . GLU   A 1 68  ? -17.53766 -8.75260  -27.61112 1.000 24.71147 ? 75  GLU   A CA  1 
ATOM   484  C  C   . GLU   A 1 68  ? -16.11449 -8.61839  -27.08353 1.000 21.50845 ? 75  GLU   A C   1 
ATOM   485  O  O   . GLU   A 1 68  ? -15.19737 -9.25007  -27.60489 1.000 21.84921 ? 75  GLU   A O   1 
ATOM   486  C  CB  . GLU   A 1 68  ? -18.16027 -10.04915 -27.08899 1.000 24.40094 ? 75  GLU   A CB  1 
ATOM   487  C  CG  . GLU   A 1 68  ? -19.64716 -10.31600 -27.44653 1.000 31.54456 ? 75  GLU   A CG  1 
ATOM   488  C  CD  . GLU   A 1 68  ? -19.95462 -10.44065 -28.93563 1.000 49.53648 ? 75  GLU   A CD  1 
ATOM   489  O  OE1 . GLU   A 1 68  ? -19.24203 -11.21299 -29.62024 1.000 44.65304 ? 75  GLU   A OE1 1 
ATOM   490  O  OE2 . GLU   A 1 68  ? -20.92506 -9.78547  -29.41540 1.000 54.25669 ? 75  GLU   A OE2 1 
ATOM   491  N  N   . LEU   A 1 69  ? -15.93691 -7.80110  -26.06411 1.000 18.73416 ? 76  LEU   A N   1 
ATOM   492  C  CA  . LEU   A 1 69  ? -14.62382 -7.56742  -25.45222 1.000 16.66651 ? 76  LEU   A CA  1 
ATOM   493  C  C   . LEU   A 1 69  ? -14.68829 -8.11137  -24.02875 1.000 17.64676 ? 76  LEU   A C   1 
ATOM   494  O  O   . LEU   A 1 69  ? -15.33819 -7.51427  -23.16468 1.000 19.43746 ? 76  LEU   A O   1 
ATOM   495  C  CB  . LEU   A 1 69  ? -14.32323 -6.06688  -25.46464 1.000 17.98839 ? 76  LEU   A CB  1 
ATOM   496  C  CG  . LEU   A 1 69  ? -14.18353 -5.41460  -26.85268 1.000 22.04459 ? 76  LEU   A CG  1 
ATOM   497  C  CD1 . LEU   A 1 69  ? -13.70162 -3.99646  -26.68797 1.000 26.94296 ? 76  LEU   A CD1 1 
ATOM   498  C  CD2 . LEU   A 1 69  ? -13.20633 -6.17628  -27.70667 1.000 20.03135 ? 76  LEU   A CD2 1 
ATOM   499  N  N   . HIS   A 1 70  ? -14.05034 -9.25952  -23.78291 1.000 15.32603 ? 77  HIS   A N   1 
ATOM   500  C  CA  . HIS   A 1 70  ? -14.19474 -9.91227  -22.48476 1.000 15.61820 ? 77  HIS   A CA  1 
ATOM   501  C  C   . HIS   A 1 70  ? -12.99564 -10.80086 -22.18306 1.000 16.04200 ? 77  HIS   A C   1 
ATOM   502  O  O   . HIS   A 1 70  ? -12.13882 -11.04073 -23.03635 1.000 15.66231 ? 77  HIS   A O   1 
ATOM   503  C  CB  . HIS   A 1 70  ? -15.47261 -10.75012 -22.45465 1.000 17.93446 ? 77  HIS   A CB  1 
ATOM   504  C  CG  . HIS   A 1 70  ? -15.47923 -11.84678 -23.47091 1.000 18.46156 ? 77  HIS   A CG  1 
ATOM   505  N  ND1 . HIS   A 1 70  ? -16.48333 -11.98992 -24.40044 1.000 25.54030 ? 77  HIS   A ND1 1 
ATOM   506  C  CD2 . HIS   A 1 70  ? -14.62380 -12.87731 -23.68551 1.000 20.08038 ? 77  HIS   A CD2 1 
ATOM   507  C  CE1 . HIS   A 1 70  ? -16.23881 -13.04245 -25.15640 1.000 21.93776 ? 77  HIS   A CE1 1 
ATOM   508  N  NE2 . HIS   A 1 70  ? -15.12490 -13.60741 -24.73980 1.000 23.22714 ? 77  HIS   A NE2 1 
ATOM   509  N  N   . ILE   A 1 71  ? -12.98966 -11.30086 -20.94804 1.000 15.16953 ? 78  ILE   A N   1 
ATOM   510  C  CA  . ILE   A 1 71  ? -11.97599 -12.18915 -20.39293 1.000 13.75336 ? 78  ILE   A CA  1 
ATOM   511  C  C   . ILE   A 1 71  ? -12.68993 -13.38360 -19.76648 1.000 16.15616 ? 78  ILE   A C   1 
ATOM   512  O  O   . ILE   A 1 71  ? -13.58782 -13.20637 -18.92873 1.000 16.16310 ? 78  ILE   A O   1 
ATOM   513  C  CB  . ILE   A 1 71  ? -11.11839 -11.46980 -19.33490 1.000 14.62872 ? 78  ILE   A CB  1 
ATOM   514  C  CG1 . ILE   A 1 71  ? -10.53379 -10.15762 -19.89276 1.000 14.56211 ? 78  ILE   A CG1 1 
ATOM   515  C  CG2 . ILE   A 1 71  ? -10.08223 -12.46150 -18.76002 1.000 14.62140 ? 78  ILE   A CG2 1 
ATOM   516  C  CD1 . ILE   A 1 71  ? -9.71765  -9.36259  -18.82203 1.000 15.51801 ? 78  ILE   A CD1 1 
ATOM   517  N  N   . ASN   A 1 72  ? -12.30727 -14.59274 -20.17636 1.000 14.19758 ? 79  ASN   A N   1 
ATOM   518  C  CA  . ASN   A 1 72  ? -12.81126 -15.82092 -19.57871 1.000 12.79783 ? 79  ASN   A CA  1 
ATOM   519  C  C   . ASN   A 1 72  ? -11.70215 -16.55826 -18.85680 1.000 16.71048 ? 79  ASN   A C   1 
ATOM   520  O  O   . ASN   A 1 72  ? -10.58357 -16.68701 -19.37107 1.000 14.45410 ? 79  ASN   A O   1 
ATOM   521  C  CB  . ASN   A 1 72  ? -13.44157 -16.73769 -20.62767 1.000 15.17328 ? 79  ASN   A CB  1 
ATOM   522  C  CG  . ASN   A 1 72  ? -14.63695 -16.10879 -21.30271 1.000 15.76890 ? 79  ASN   A CG  1 
ATOM   523  O  OD1 . ASN   A 1 72  ? -15.35634 -15.30320 -20.69338 1.000 18.20410 ? 79  ASN   A OD1 1 
ATOM   524  N  ND2 . ASN   A 1 72  ? -14.88042 -16.48936 -22.57023 1.000 19.50271 ? 79  ASN   A ND2 1 
ATOM   525  N  N   . LEU   A 1 73  ? -12.03450 -17.11323 -17.70089 1.000 15.09583 ? 80  LEU   A N   1 
ATOM   526  C  CA  . LEU   A 1 73  ? -11.09809 -17.94467 -16.95173 1.000 12.77353 ? 80  LEU   A CA  1 
ATOM   527  C  C   . LEU   A 1 73  ? -11.67947 -19.34733 -16.94302 1.000 14.04631 ? 80  LEU   A C   1 
ATOM   528  O  O   . LEU   A 1 73  ? -12.79558 -19.56179 -16.44217 1.000 15.33073 ? 80  LEU   A O   1 
ATOM   529  C  CB  . LEU   A 1 73  ? -10.92737 -17.44733 -15.51067 1.000 12.83352 ? 80  LEU   A CB  1 
ATOM   530  C  CG  . LEU   A 1 73  ? -10.56327 -15.95809 -15.39233 1.000 13.51489 ? 80  LEU   A CG  1 
ATOM   531  C  CD1 . LEU   A 1 73  ? -10.51664 -15.59864 -13.90719 1.000 14.15424 ? 80  LEU   A CD1 1 
ATOM   532  C  CD2 . LEU   A 1 73  ? -9.23107  -15.66512 -16.08389 1.000 15.00410 ? 80  LEU   A CD2 1 
ATOM   533  N  N   . ILE   A 1 74  ? -10.94146 -20.29699 -17.49803 1.000 14.18264 ? 81  ILE   A N   1 
ATOM   534  C  CA  . ILE   A 1 74  ? -11.43138 -21.65400 -17.72225 1.000 13.76356 ? 81  ILE   A CA  1 
ATOM   535  C  C   . ILE   A 1 74  ? -10.51824 -22.66076 -17.02320 1.000 15.88484 ? 81  ILE   A C   1 
ATOM   536  O  O   . ILE   A 1 74  ? -9.48843  -23.07370 -17.56946 1.000 15.81693 ? 81  ILE   A O   1 
ATOM   537  C  CB  . ILE   A 1 74  ? -11.55080 -21.97642 -19.22274 1.000 14.87597 ? 81  ILE   A CB  1 
ATOM   538  C  CG1 . ILE   A 1 74  ? -12.25425 -20.82428 -19.93869 1.000 16.00735 ? 81  ILE   A CG1 1 
ATOM   539  C  CG2 . ILE   A 1 74  ? -12.26300 -23.33774 -19.35384 1.000 17.78139 ? 81  ILE   A CG2 1 
ATOM   540  C  CD1 . ILE   A 1 74  ? -12.40415 -20.98523 -21.42471 1.000 18.03930 ? 81  ILE   A CD1 1 
ATOM   541  N  N   . PRO   A 1 75  ? -10.90174 -23.13427 -15.83905 1.000 17.21157 ? 82  PRO   A N   1 
ATOM   542  C  CA  . PRO   A 1 75  ? -10.13958 -24.19851 -15.17514 1.000 16.33582 ? 82  PRO   A CA  1 
ATOM   543  C  C   . PRO   A 1 75  ? -10.58952 -25.55182 -15.69885 1.000 19.10429 ? 82  PRO   A C   1 
ATOM   544  O  O   . PRO   A 1 75  ? -11.76371 -25.75341 -16.00783 1.000 20.81628 ? 82  PRO   A O   1 
ATOM   545  C  CB  . PRO   A 1 75  ? -10.51671 -24.02518 -13.69653 1.000 17.66465 ? 82  PRO   A CB  1 
ATOM   546  C  CG  . PRO   A 1 75  ? -11.90535 -23.44657 -13.72515 1.000 22.87515 ? 82  PRO   A CG  1 
ATOM   547  C  CD  . PRO   A 1 75  ? -12.09989 -22.74530 -15.06242 1.000 19.63876 ? 82  PRO   A CD  1 
ATOM   548  N  N   . ASN   A 1 76  ? -9.62284  -26.47208 -15.81985 1.000 17.86033 ? 83  ASN   A N   1 
ATOM   549  C  CA  . ASN   A 1 76  ? -9.90731  -27.85389 -16.23648 1.000 18.46295 ? 83  ASN   A CA  1 
ATOM   550  C  C   . ASN   A 1 76  ? -9.08285  -28.78155 -15.35162 1.000 20.60523 ? 83  ASN   A C   1 
ATOM   551  O  O   . ASN   A 1 76  ? -7.88045  -28.93527 -15.56692 1.000 22.67887 ? 83  ASN   A O   1 
ATOM   552  C  CB  . ASN   A 1 76  ? -9.58547  -28.08706 -17.70413 1.000 21.64321 ? 83  ASN   A CB  1 
ATOM   553  C  CG  . ASN   A 1 76  ? -10.11688 -29.42970 -18.18886 1.000 31.99307 ? 83  ASN   A CG  1 
ATOM   554  O  OD1 . ASN   A 1 76  ? -9.81205  -30.46635 -17.60605 1.000 27.86199 ? 83  ASN   A OD1 1 
ATOM   555  N  ND2 . ASN   A 1 76  ? -10.95570 -29.40579 -19.21160 1.000 31.44746 ? 83  ASN   A ND2 1 
ATOM   556  N  N   . LYS   A 1 77  ? -9.74466  -29.44004 -14.39642 1.000 22.04264 ? 84  LYS   A N   1 
ATOM   557  C  CA  . LYS   A 1 77  ? -9.00579  -30.27301 -13.45117 1.000 20.22066 ? 84  LYS   A CA  1 
ATOM   558  C  C   . LYS   A 1 77  ? -8.56267  -31.58527 -14.07146 1.000 24.80429 ? 84  LYS   A C   1 
ATOM   559  O  O   . LYS   A 1 77  ? -7.59660  -32.17543 -13.58964 1.000 28.46230 ? 84  LYS   A O   1 
ATOM   560  C  CB  . LYS   A 1 77  ? -9.83759  -30.58255 -12.20121 1.000 27.02316 ? 84  LYS   A CB  1 
ATOM   561  C  CG  . LYS   A 1 77  ? -10.05081 -29.39648 -11.27673 1.000 28.15800 ? 84  LYS   A CG  1 
ATOM   562  C  CD  . LYS   A 1 77  ? -10.85104 -29.79399 -10.04403 1.000 30.15111 ? 84  LYS   A CD  1 
ATOM   563  C  CE  . LYS   A 1 77  ? -11.13724 -28.61388 -9.12597  1.000 33.78149 ? 84  LYS   A CE  1 
ATOM   564  N  NZ  . LYS   A 1 77  ? -12.09640 -27.68780 -9.78581  1.000 34.70811 ? 84  LYS   A NZ  1 
ATOM   565  N  N   . GLN   A 1 78  ? -9.22753  -32.05264 -15.13194 1.000 28.26453 ? 85  GLN   A N   1 
ATOM   566  C  CA  . GLN   A 1 78  ? -8.80268  -33.30828 -15.75079 1.000 28.51409 ? 85  GLN   A CA  1 
ATOM   567  C  C   . GLN   A 1 78  ? -7.51022  -33.12481 -16.53841 1.000 29.57826 ? 85  GLN   A C   1 
ATOM   568  O  O   . GLN   A 1 78  ? -6.64884  -34.00721 -16.53956 1.000 32.42999 ? 85  GLN   A O   1 
ATOM   569  C  CB  . GLN   A 1 78  ? -9.89514  -33.89182 -16.65681 1.000 32.47444 ? 85  GLN   A CB  1 
ATOM   570  C  CG  . GLN   A 1 78  ? -11.24828 -34.23867 -16.00246 1.000 43.49305 ? 85  GLN   A CG  1 
ATOM   571  C  CD  . GLN   A 1 78  ? -11.75873 -33.20447 -15.00270 1.000 52.50316 ? 85  GLN   A CD  1 
ATOM   572  O  OE1 . GLN   A 1 78  ? -11.91398 -33.49060 -13.80416 1.000 52.40844 ? 85  GLN   A OE1 1 
ATOM   573  N  NE2 . GLN   A 1 78  ? -12.04873 -31.98973 -15.50278 1.000 47.33762 ? 85  GLN   A NE2 1 
ATOM   574  N  N   . ASP   A 1 79  ? -7.35639  -31.97986 -17.19586 1.000 23.49271 ? 86  ASP   A N   1 
ATOM   575  C  CA  . ASP   A 1 79  ? -6.18511  -31.60712 -17.97341 1.000 23.15063 ? 86  ASP   A CA  1 
ATOM   576  C  C   . ASP   A 1 79  ? -5.13734  -30.90993 -17.11700 1.000 21.23318 ? 86  ASP   A C   1 
ATOM   577  O  O   . ASP   A 1 79  ? -4.00954  -30.73311 -17.57825 1.000 22.97498 ? 86  ASP   A O   1 
ATOM   578  C  CB  . ASP   A 1 79  ? -6.57923  -30.65073 -19.11086 1.000 28.86045 ? 86  ASP   A CB  1 
ATOM   579  C  CG  . ASP   A 1 79  ? -7.44252  -31.32230 -20.16933 1.000 38.05355 ? 86  ASP   A CG  1 
ATOM   580  O  OD1 . ASP   A 1 79  ? -7.60296  -32.56261 -20.10944 1.000 39.37737 ? 86  ASP   A OD1 1 
ATOM   581  O  OD2 . ASP   A 1 79  ? -7.97545  -30.60659 -21.04202 1.000 36.11222 ? 86  ASP   A OD2 1 
ATOM   582  N  N   . ARG   A 1 80  ? -5.49372  -30.55737 -15.88195 1.000 22.56706 ? 87  ARG   A N   1 
ATOM   583  C  CA  . ARG   A 1 80  ? -4.68127  -29.72008 -14.99494 1.000 18.03398 ? 87  ARG   A CA  1 
ATOM   584  C  C   . ARG   A 1 80  ? -4.23375  -28.44173 -15.69621 1.000 19.76930 ? 87  ARG   A C   1 
ATOM   585  O  O   . ARG   A 1 80  ? -3.05678  -28.05944 -15.66283 1.000 20.05863 ? 87  ARG   A O   1 
ATOM   586  C  CB  . ARG   A 1 80  ? -3.48891  -30.47916 -14.40387 1.000 19.80066 ? 87  ARG   A CB  1 
ATOM   587  C  CG  . ARG   A 1 80  ? -3.06757  -29.87082 -13.09114 1.000 20.07962 ? 87  ARG   A CG  1 
ATOM   588  C  CD  . ARG   A 1 80  ? -1.67579  -30.15944 -12.67052 1.000 31.47128 ? 87  ARG   A CD  1 
ATOM   589  N  NE  . ARG   A 1 80  ? -1.43243  -31.57482 -12.51206 1.000 37.31729 ? 87  ARG   A NE  1 
ATOM   590  C  CZ  . ARG   A 1 80  ? -0.25030  -32.15084 -12.67499 1.000 42.37454 ? 87  ARG   A CZ  1 
ATOM   591  N  NH1 . ARG   A 1 80  ? 0.83600   -31.44411 -12.97162 1.000 31.99525 ? 87  ARG   A NH1 1 
ATOM   592  N  NH2 . ARG   A 1 80  ? -0.14508  -33.46074 -12.49325 1.000 37.51955 ? 87  ARG   A NH2 1 
ATOM   593  N  N   . THR   A 1 81  ? -5.20657  -27.74061 -16.28675 1.000 17.87095 ? 88  THR   A N   1 
ATOM   594  C  CA  . THR   A 1 81  ? -4.93848  -26.48729 -16.98569 1.000 17.21854 ? 88  THR   A CA  1 
ATOM   595  C  C   . THR   A 1 81  ? -5.83892  -25.36325 -16.49939 1.000 15.88255 ? 88  THR   A C   1 
ATOM   596  O  O   . THR   A 1 81  ? -7.00604  -25.57559 -16.17749 1.000 17.14448 ? 88  THR   A O   1 
ATOM   597  C  CB  . THR   A 1 81  ? -5.07070  -26.61485 -18.50711 1.000 18.57420 ? 88  THR   A CB  1 
ATOM   598  O  OG1 . THR   A 1 81  ? -6.40728  -27.00749 -18.89624 1.000 20.00145 ? 88  THR   A OG1 1 
ATOM   599  C  CG2 . THR   A 1 81  ? -3.97952  -27.54445 -19.09200 1.000 19.35660 ? 88  THR   A CG2 1 
ATOM   600  N  N   . LEU   A 1 82  ? -5.26949  -24.16268 -16.44925 1.000 14.66993 ? 89  LEU   A N   1 
ATOM   601  C  CA  . LEU   A 1 82  ? -6.03972  -22.93555 -16.26367 1.000 16.49312 ? 89  LEU   A CA  1 
ATOM   602  C  C   . LEU   A 1 82  ? -5.82653  -22.10313 -17.51519 1.000 15.94775 ? 89  LEU   A C   1 
ATOM   603  O  O   . LEU   A 1 82  ? -4.68124  -21.81132 -17.86378 1.000 15.61109 ? 89  LEU   A O   1 
ATOM   604  C  CB  . LEU   A 1 82  ? -5.58880  -22.16948 -15.01009 1.000 15.11350 ? 89  LEU   A CB  1 
ATOM   605  C  CG  . LEU   A 1 82  ? -6.33270  -20.81914 -14.84479 1.000 14.03690 ? 89  LEU   A CG  1 
ATOM   606  C  CD1 . LEU   A 1 82  ? -7.84651  -20.99814 -14.62169 1.000 17.77227 ? 89  LEU   A CD1 1 
ATOM   607  C  CD2 . LEU   A 1 82  ? -5.74714  -20.10669 -13.62313 1.000 16.80213 ? 89  LEU   A CD2 1 
ATOM   608  N  N   . THR   A 1 83  ? -6.91088  -21.78876 -18.22907 1.000 13.98530 ? 90  THR   A N   1 
ATOM   609  C  CA  . THR   A 1 83  ? -6.82284  -21.03460 -19.47776 1.000 13.69605 ? 90  THR   A CA  1 
ATOM   610  C  C   . THR   A 1 83  ? -7.39974  -19.64114 -19.27792 1.000 17.45239 ? 90  THR   A C   1 
ATOM   611  O  O   . THR   A 1 83  ? -8.50149  -19.48545 -18.72212 1.000 16.40953 ? 90  THR   A O   1 
ATOM   612  C  CB  . THR   A 1 83  ? -7.55943  -21.76161 -20.61708 1.000 17.70529 ? 90  THR   A CB  1 
ATOM   613  O  OG1 . THR   A 1 83  ? -6.99258  -23.07769 -20.79017 1.000 17.21103 ? 90  THR   A OG1 1 
ATOM   614  C  CG2 . THR   A 1 83  ? -7.46555  -20.96516 -21.92494 1.000 19.71515 ? 90  THR   A CG2 1 
ATOM   615  N  N   . ILE   A 1 84  ? -6.65281  -18.63177 -19.69465 1.000 14.22960 ? 91  ILE   A N   1 
ATOM   616  C  CA  . ILE   A 1 84  ? -7.11287  -17.24195 -19.65265 1.000 15.67564 ? 91  ILE   A CA  1 
ATOM   617  C  C   . ILE   A 1 84  ? -7.35888  -16.81304 -21.09240 1.000 16.99160 ? 91  ILE   A C   1 
ATOM   618  O  O   . ILE   A 1 84  ? -6.41086  -16.75267 -21.87915 1.000 16.12826 ? 91  ILE   A O   1 
ATOM   619  C  CB  . ILE   A 1 84  ? -6.09671  -16.31006 -18.96934 1.000 16.96983 ? 91  ILE   A CB  1 
ATOM   620  C  CG1 . ILE   A 1 84  ? -5.83463  -16.70219 -17.49966 1.000 19.64611 ? 91  ILE   A CG1 1 
ATOM   621  C  CG2 . ILE   A 1 84  ? -6.56028  -14.83514 -19.05289 1.000 15.75724 ? 91  ILE   A CG2 1 
ATOM   622  C  CD1 . ILE   A 1 84  ? -4.68615  -17.66393 -17.23915 1.000 23.81173 ? 91  ILE   A CD1 1 
ATOM   623  N  N   . VAL   A 1 85  ? -8.61630  -16.51923 -21.44291 1.000 13.46018 ? 92  VAL   A N   1 
ATOM   624  C  CA  . VAL   A 1 85  ? -8.99813  -16.19698 -22.81731 1.000 13.23665 ? 92  VAL   A CA  1 
ATOM   625  C  C   . VAL   A 1 85  ? -9.40719  -14.74306 -22.85214 1.000 18.90101 ? 92  VAL   A C   1 
ATOM   626  O  O   . VAL   A 1 85  ? -10.21134 -14.31121 -22.01802 1.000 17.51305 ? 92  VAL   A O   1 
ATOM   627  C  CB  . VAL   A 1 85  ? -10.20156 -17.04134 -23.30605 1.000 17.01395 ? 92  VAL   A CB  1 
ATOM   628  C  CG1 . VAL   A 1 85  ? -10.48266 -16.73521 -24.78734 1.000 19.34049 ? 92  VAL   A CG1 1 
ATOM   629  C  CG2 . VAL   A 1 85  ? -10.01481 -18.54198 -23.05334 1.000 19.71599 ? 92  VAL   A CG2 1 
ATOM   630  N  N   A ASP   A 1 86  ? -8.89558  -13.99076 -23.82531 0.500 16.05498 ? 93  ASP   A N   1 
ATOM   631  N  N   B ASP   A 1 86  ? -8.89558  -13.99076 -23.82531 0.500 16.05498 ? 93  ASP   A N   1 
ATOM   632  C  CA  A ASP   A 1 86  ? -9.42028  -12.64846 -24.05459 0.500 15.76719 ? 93  ASP   A CA  1 
ATOM   633  C  CA  B ASP   A 1 86  ? -9.42028  -12.64846 -24.05459 0.500 15.76719 ? 93  ASP   A CA  1 
ATOM   634  C  C   A ASP   A 1 86  ? -9.67720  -12.46517 -25.54002 0.500 17.03305 ? 93  ASP   A C   1 
ATOM   635  C  C   B ASP   A 1 86  ? -9.67720  -12.46517 -25.54002 0.500 17.03305 ? 93  ASP   A C   1 
ATOM   636  O  O   A ASP   A 1 86  ? -9.13605  -13.18965 -26.38031 0.500 16.46352 ? 93  ASP   A O   1 
ATOM   637  O  O   B ASP   A 1 86  ? -9.13605  -13.18965 -26.38031 0.500 16.46352 ? 93  ASP   A O   1 
ATOM   638  C  CB  A ASP   A 1 86  ? -8.47550  -11.55839 -23.50552 0.500 15.76762 ? 93  ASP   A CB  1 
ATOM   639  C  CB  B ASP   A 1 86  ? -8.47550  -11.55839 -23.50552 0.500 15.76762 ? 93  ASP   A CB  1 
ATOM   640  C  CG  A ASP   A 1 86  ? -7.17306  -11.43864 -24.28893 0.500 17.54413 ? 93  ASP   A CG  1 
ATOM   641  C  CG  B ASP   A 1 86  ? -7.17306  -11.43864 -24.28893 0.500 17.54413 ? 93  ASP   A CG  1 
ATOM   642  O  OD1 A ASP   A 1 86  ? -7.20156  -11.02552 -25.47243 0.500 17.49160 ? 93  ASP   A OD1 1 
ATOM   643  O  OD1 B ASP   A 1 86  ? -7.20156  -11.02552 -25.47243 0.500 17.49160 ? 93  ASP   A OD1 1 
ATOM   644  O  OD2 A ASP   A 1 86  ? -6.12025  -11.76102 -23.70978 0.500 16.33158 ? 93  ASP   A OD2 1 
ATOM   645  O  OD2 B ASP   A 1 86  ? -6.12025  -11.76102 -23.70978 0.500 16.33158 ? 93  ASP   A OD2 1 
ATOM   646  N  N   . THR   A 1 87  ? -10.53299 -11.50047 -25.85734 1.000 15.04896 ? 94  THR   A N   1 
ATOM   647  C  CA  . THR   A 1 87  ? -10.83722 -11.15054 -27.23780 1.000 13.37460 ? 94  THR   A CA  1 
ATOM   648  C  C   . THR   A 1 87  ? -10.17160 -9.81843  -27.59888 1.000 16.35873 ? 94  THR   A C   1 
ATOM   649  O  O   . THR   A 1 87  ? -10.73348 -8.98804  -28.32261 1.000 16.07589 ? 94  THR   A O   1 
ATOM   650  C  CB  . THR   A 1 87  ? -12.35112 -11.13274 -27.46738 1.000 18.20991 ? 94  THR   A CB  1 
ATOM   651  O  OG1 . THR   A 1 87  ? -12.99530 -10.28594 -26.50567 1.000 15.93543 ? 94  THR   A OG1 1 
ATOM   652  C  CG2 . THR   A 1 87  ? -12.91478 -12.54059 -27.31260 1.000 18.86365 ? 94  THR   A CG2 1 
ATOM   653  N  N   . GLY   A 1 88  ? -8.94455  -9.61836  -27.12021 1.000 14.83212 ? 95  GLY   A N   1 
ATOM   654  C  CA  . GLY   A 1 88  ? -8.22199  -8.40453  -27.44419 1.000 16.17106 ? 95  GLY   A CA  1 
ATOM   655  C  C   . GLY   A 1 88  ? -7.64815  -8.42307  -28.84933 1.000 15.26773 ? 95  GLY   A C   1 
ATOM   656  O  O   . GLY   A 1 88  ? -8.05419  -9.19776  -29.72303 1.000 15.20178 ? 95  GLY   A O   1 
ATOM   657  N  N   . ILE   A 1 89  ? -6.62117  -7.58132  -29.04672 1.000 14.40738 ? 96  ILE   A N   1 
ATOM   658  C  CA  . ILE   A 1 89  ? -6.08528  -7.37627  -30.40067 1.000 13.48342 ? 96  ILE   A CA  1 
ATOM   659  C  C   . ILE   A 1 89  ? -5.32212  -8.59305  -30.90695 1.000 16.49653 ? 96  ILE   A C   1 
ATOM   660  O  O   . ILE   A 1 89  ? -5.16340  -8.75366  -32.12820 1.000 16.29200 ? 96  ILE   A O   1 
ATOM   661  C  CB  . ILE   A 1 89  ? -5.22924  -6.08660  -30.39646 1.000 15.74877 ? 96  ILE   A CB  1 
ATOM   662  C  CG1 . ILE   A 1 89  ? -4.94555  -5.59696  -31.83296 1.000 20.66510 ? 96  ILE   A CG1 1 
ATOM   663  C  CG2 . ILE   A 1 89  ? -3.96400  -6.26774  -29.56516 1.000 15.96301 ? 96  ILE   A CG2 1 
ATOM   664  C  CD1 . ILE   A 1 89  ? -4.57637  -4.13585  -31.84448 1.000 21.00171 ? 96  ILE   A CD1 1 
ATOM   665  N  N   . GLY   A 1 90  ? -4.84407  -9.47221  -30.01623 1.000 15.82567 ? 97  GLY   A N   1 
ATOM   666  C  CA  . GLY   A 1 90  ? -4.11262  -10.63186 -30.48213 1.000 17.00665 ? 97  GLY   A CA  1 
ATOM   667  C  C   . GLY   A 1 90  ? -2.68981  -10.25323 -30.83566 1.000 15.45880 ? 97  GLY   A C   1 
ATOM   668  O  O   . GLY   A 1 90  ? -2.23751  -9.11888  -30.65289 1.000 16.81681 ? 97  GLY   A O   1 
ATOM   669  N  N   . MET   A 1 91  ? -1.96977  -11.24312 -31.34195 1.000 15.41199 ? 98  MET   A N   1 
ATOM   670  C  CA  . MET   A 1 91  ? -0.56542  -11.08224 -31.71865 1.000 15.17500 ? 98  MET   A CA  1 
ATOM   671  C  C   . MET   A 1 91  ? -0.28993  -11.70186 -33.07534 1.000 15.01888 ? 98  MET   A C   1 
ATOM   672  O  O   . MET   A 1 91  ? -0.79102  -12.78760 -33.37994 1.000 19.05135 ? 98  MET   A O   1 
ATOM   673  C  CB  . MET   A 1 91  ? 0.39766   -11.72945 -30.70721 1.000 16.68317 ? 98  MET   A CB  1 
ATOM   674  C  CG  . MET   A 1 91  ? 0.42483   -11.04517 -29.33012 1.000 17.49809 ? 98  MET   A CG  1 
ATOM   675  S  SD  . MET   A 1 91  ? 1.40510   -11.90450 -28.07568 1.000 17.64889 ? 98  MET   A SD  1 
ATOM   676  C  CE  . MET   A 1 91  ? 0.29722   -13.25282 -27.62680 1.000 18.56354 ? 98  MET   A CE  1 
ATOM   677  N  N   . THR   A 1 92  ? 0.53594   -11.01252 -33.86146 1.000 17.03408 ? 99  THR   A N   1 
ATOM   678  C  CA  . THR   A 1 92  ? 1.04506   -11.58571 -35.11182 1.000 17.65674 ? 99  THR   A CA  1 
ATOM   679  C  C   . THR   A 1 92  ? 2.11272   -12.62943 -34.80331 1.000 16.67844 ? 99  THR   A C   1 
ATOM   680  O  O   . THR   A 1 92  ? 2.59196   -12.75155 -33.67117 1.000 16.54234 ? 99  THR   A O   1 
ATOM   681  C  CB  . THR   A 1 92  ? 1.66297   -10.49834 -35.99690 1.000 18.05621 ? 99  THR   A CB  1 
ATOM   682  O  OG1 . THR   A 1 92  ? 2.79728   -9.91686  -35.32649 1.000 19.85254 ? 99  THR   A OG1 1 
ATOM   683  C  CG2 . THR   A 1 92  ? 0.65468   -9.41177  -36.28958 1.000 21.33595 ? 99  THR   A CG2 1 
ATOM   684  N  N   . LYS   A 1 93  ? 2.50856   -13.39073 -35.83167 1.000 17.06257 ? 100 LYS   A N   1 
ATOM   685  C  CA  . LYS   A 1 93  ? 3.63550   -14.30895 -35.64333 1.000 18.90426 ? 100 LYS   A CA  1 
ATOM   686  C  C   . LYS   A 1 93  ? 4.87501   -13.55093 -35.20149 1.000 17.17312 ? 100 LYS   A C   1 
ATOM   687  O  O   . LYS   A 1 93  ? 5.61100   -13.99263 -34.30880 1.000 16.73941 ? 100 LYS   A O   1 
ATOM   688  C  CB  . LYS   A 1 93  ? 3.92208   -15.05281 -36.95064 1.000 20.22236 ? 100 LYS   A CB  1 
ATOM   689  C  CG  . LYS   A 1 93  ? 4.88615   -16.20935 -36.75383 1.000 20.63484 ? 100 LYS   A CG  1 
ATOM   690  C  CD  . LYS   A 1 93  ? 5.24332   -16.86561 -38.10667 1.000 20.83986 ? 100 LYS   A CD  1 
ATOM   691  C  CE  . LYS   A 1 93  ? 6.17155   -18.05528 -37.85102 1.000 25.80021 ? 100 LYS   A CE  1 
ATOM   692  N  NZ  . LYS   A 1 93  ? 6.88679   -18.37779 -39.10724 1.000 23.38763 ? 100 LYS   A NZ  1 
ATOM   693  N  N   . ALA   A 1 94  ? 5.11885   -12.39329 -35.81930 1.000 20.02542 ? 101 ALA   A N   1 
ATOM   694  C  CA  . ALA   A 1 94  ? 6.28770   -11.60675 -35.45708 1.000 22.00866 ? 101 ALA   A CA  1 
ATOM   695  C  C   . ALA   A 1 94  ? 6.21657   -11.15963 -34.00969 1.000 20.18358 ? 101 ALA   A C   1 
ATOM   696  O  O   . ALA   A 1 94  ? 7.23547   -11.16043 -33.30461 1.000 21.95535 ? 101 ALA   A O   1 
ATOM   697  C  CB  . ALA   A 1 94  ? 6.40419   -10.40256 -36.38419 1.000 22.76504 ? 101 ALA   A CB  1 
ATOM   698  N  N   . ASP   A 1 95  ? 5.02310   -10.76769 -33.54578 1.000 19.04138 ? 102 ASP   A N   1 
ATOM   699  C  CA  . ASP   A 1 95  ? 4.87157   -10.40956 -32.13557 1.000 18.59219 ? 102 ASP   A CA  1 
ATOM   700  C  C   . ASP   A 1 95  ? 5.21302   -11.58264 -31.23826 1.000 17.61863 ? 102 ASP   A C   1 
ATOM   701  O  O   . ASP   A 1 95  ? 5.88619   -11.42641 -30.20528 1.000 18.82346 ? 102 ASP   A O   1 
ATOM   702  C  CB  . ASP   A 1 95  ? 3.43269   -9.97138  -31.81010 1.000 20.40333 ? 102 ASP   A CB  1 
ATOM   703  C  CG  . ASP   A 1 95  ? 3.02412   -8.65365  -32.44058 1.000 25.85623 ? 102 ASP   A CG  1 
ATOM   704  O  OD1 . ASP   A 1 95  ? 3.86668   -7.74855  -32.59807 1.000 24.63833 ? 102 ASP   A OD1 1 
ATOM   705  O  OD2 . ASP   A 1 95  ? 1.80482   -8.48815  -32.71176 1.000 25.02547 ? 102 ASP   A OD2 1 
ATOM   706  N  N   . LEU   A 1 96  ? 4.70751   -12.76986 -31.57471 1.000 18.18024 ? 103 LEU   A N   1 
ATOM   707  C  CA  . LEU   A 1 96  ? 4.97754   -13.91492 -30.71752 1.000 18.95061 ? 103 LEU   A CA  1 
ATOM   708  C  C   . LEU   A 1 96  ? 6.46718   -14.14575 -30.59041 1.000 18.46095 ? 103 LEU   A C   1 
ATOM   709  O  O   . LEU   A 1 96  ? 6.99155   -14.36984 -29.48961 1.000 18.60933 ? 103 LEU   A O   1 
ATOM   710  C  CB  . LEU   A 1 96  ? 4.34104   -15.17952 -31.27035 1.000 17.53812 ? 103 LEU   A CB  1 
ATOM   711  C  CG  . LEU   A 1 96  ? 2.87076   -15.33837 -31.12540 1.000 18.13229 ? 103 LEU   A CG  1 
ATOM   712  C  CD1 . LEU   A 1 96  ? 2.45688   -16.59984 -31.87746 1.000 18.06528 ? 103 LEU   A CD1 1 
ATOM   713  C  CD2 . LEU   A 1 96  ? 2.51318   -15.39610 -29.63093 1.000 16.68461 ? 103 LEU   A CD2 1 
ATOM   714  N  N   . ILE   A 1 97  ? 7.17147   -14.10194 -31.71998 1.000 17.89402 ? 104 ILE   A N   1 
ATOM   715  C  CA  . ILE   A 1 97  ? 8.60682   -14.38801 -31.69295 1.000 17.21381 ? 104 ILE   A CA  1 
ATOM   716  C  C   . ILE   A 1 97  ? 9.35556   -13.30354 -30.93122 1.000 18.78908 ? 104 ILE   A C   1 
ATOM   717  O  O   . ILE   A 1 97  ? 10.29930  -13.58336 -30.17978 1.000 19.48594 ? 104 ILE   A O   1 
ATOM   718  C  CB  . ILE   A 1 97  ? 9.13553   -14.54143 -33.13049 1.000 17.28538 ? 104 ILE   A CB  1 
ATOM   719  C  CG1 . ILE   A 1 97  ? 8.52732   -15.79669 -33.74392 1.000 19.05894 ? 104 ILE   A CG1 1 
ATOM   720  C  CG2 . ILE   A 1 97  ? 10.68222  -14.58644 -33.17595 1.000 19.04096 ? 104 ILE   A CG2 1 
ATOM   721  C  CD1 . ILE   A 1 97  ? 8.66097   -15.81816 -35.26342 1.000 21.37706 ? 104 ILE   A CD1 1 
ATOM   722  N  N   . ASN   A 1 98  ? 8.92726   -12.06048 -31.08756 1.000 16.99491 ? 105 ASN   A N   1 
ATOM   723  C  CA  . ASN   A 1 98  ? 9.50349   -10.93106 -30.38835 1.000 19.71822 ? 105 ASN   A CA  1 
ATOM   724  C  C   . ASN   A 1 98  ? 8.94522   -10.81526 -28.96358 1.000 18.47342 ? 105 ASN   A C   1 
ATOM   725  O  O   . ASN   A 1 98  ? 8.35924   -9.80341  -28.58176 1.000 19.81001 ? 105 ASN   A O   1 
ATOM   726  C  CB  . ASN   A 1 98  ? 9.22013   -9.67462  -31.19812 1.000 22.82743 ? 105 ASN   A CB  1 
ATOM   727  C  CG  . ASN   A 1 98  ? 10.19144  -8.56307  -30.92652 1.000 37.35655 ? 105 ASN   A CG  1 
ATOM   728  O  OD1 . ASN   A 1 98  ? 11.21976  -8.72289  -30.21753 1.000 40.91382 ? 105 ASN   A OD1 1 
ATOM   729  N  ND2 . ASN   A 1 98  ? 9.84879   -7.38383  -31.45758 1.000 37.47719 ? 105 ASN   A ND2 1 
ATOM   730  N  N   . ASN   A 1 99  ? 9.13972   -11.88272 -28.17918 1.000 17.41378 ? 106 ASN   A N   1 
ATOM   731  C  CA  . ASN   A 1 99  ? 8.78827   -11.89289 -26.75689 1.000 14.79659 ? 106 ASN   A CA  1 
ATOM   732  C  C   . ASN   A 1 99  ? 7.33409   -11.49540 -26.50463 1.000 18.19103 ? 106 ASN   A C   1 
ATOM   733  O  O   . ASN   A 1 99  ? 7.03778   -10.75953 -25.56382 1.000 16.97612 ? 106 ASN   A O   1 
ATOM   734  C  CB  . ASN   A 1 99  ? 9.74688   -11.00676 -25.95181 1.000 15.23902 ? 106 ASN   A CB  1 
ATOM   735  C  CG  . ASN   A 1 99  ? 11.18584  -11.47256 -26.12124 1.000 17.20840 ? 106 ASN   A CG  1 
ATOM   736  O  OD1 . ASN   A 1 99  ? 11.44674  -12.66073 -25.93511 1.000 19.42435 ? 106 ASN   A OD1 1 
ATOM   737  N  ND2 . ASN   A 1 99  ? 12.10093  -10.57869 -26.45296 1.000 21.42139 ? 106 ASN   A ND2 1 
ATOM   738  N  N   . LEU   A 1 100 ? 6.42705   -12.07636 -27.29866 1.000 17.95864 ? 107 LEU   A N   1 
ATOM   739  C  CA  . LEU   A 1 100 ? 4.97536   -11.91709 -27.09019 1.000 18.65462 ? 107 LEU   A CA  1 
ATOM   740  C  C   . LEU   A 1 100 ? 4.58440   -10.44238 -27.00525 1.000 20.52373 ? 107 LEU   A C   1 
ATOM   741  O  O   . LEU   A 1 100 ? 3.79640   -10.01013 -26.16015 1.000 18.27571 ? 107 LEU   A O   1 
ATOM   742  C  CB  . LEU   A 1 100 ? 4.48667   -12.71624 -25.87869 1.000 17.99149 ? 107 LEU   A CB  1 
ATOM   743  C  CG  . LEU   A 1 100 ? 4.92024   -14.19960 -26.00279 1.000 21.25466 ? 107 LEU   A CG  1 
ATOM   744  C  CD1 . LEU   A 1 100 ? 6.07612   -14.61414 -25.11155 1.000 20.75433 ? 107 LEU   A CD1 1 
ATOM   745  C  CD2 . LEU   A 1 100 ? 3.75931   -15.13263 -25.82967 1.000 26.58606 ? 107 LEU   A CD2 1 
ATOM   746  N  N   . GLY   A 1 101 ? 5.17333   -9.65548  -27.89887 1.000 19.04594 ? 108 GLY   A N   1 
ATOM   747  C  CA  . GLY   A 1 101 ? 4.75548   -8.26862  -28.01289 1.000 21.40201 ? 108 GLY   A CA  1 
ATOM   748  C  C   . GLY   A 1 101 ? 5.28326   -7.34339  -26.94579 1.000 23.38230 ? 108 GLY   A C   1 
ATOM   749  O  O   . GLY   A 1 101 ? 4.74819   -6.22828  -26.79511 1.000 24.00920 ? 108 GLY   A O   1 
ATOM   750  N  N   . THR   A 1 102 ? 6.32256   -7.75352  -26.20622 1.000 18.93360 ? 109 THR   A N   1 
ATOM   751  C  CA  . THR   A 1 102 ? 6.88647   -6.99874  -25.09318 1.000 19.87884 ? 109 THR   A CA  1 
ATOM   752  C  C   . THR   A 1 102 ? 8.25959   -6.47050  -25.46971 1.000 21.49310 ? 109 THR   A C   1 
ATOM   753  O  O   . THR   A 1 102 ? 8.89789   -6.95514  -26.42084 1.000 22.07567 ? 109 THR   A O   1 
ATOM   754  C  CB  . THR   A 1 102 ? 7.02599   -7.84616  -23.81577 1.000 20.25481 ? 109 THR   A CB  1 
ATOM   755  O  OG1 . THR   A 1 102 ? 8.06633   -8.81898  -23.99166 1.000 21.16280 ? 109 THR   A OG1 1 
ATOM   756  C  CG2 . THR   A 1 102 ? 5.72437   -8.57326  -23.47548 1.000 23.07543 ? 109 THR   A CG2 1 
ATOM   757  N  N   . ILE   A 1 103 ? 8.71503   -5.47630  -24.70877 1.000 19.14843 ? 110 ILE   A N   1 
ATOM   758  C  CA  . ILE   A 1 103 ? 10.11033  -5.05319  -24.82890 1.000 18.65174 ? 110 ILE   A CA  1 
ATOM   759  C  C   . ILE   A 1 103 ? 10.89591  -5.76076  -23.74022 1.000 19.48588 ? 110 ILE   A C   1 
ATOM   760  O  O   . ILE   A 1 103 ? 11.48163  -5.16161  -22.83420 1.000 18.27787 ? 110 ILE   A O   1 
ATOM   761  C  CB  . ILE   A 1 103 ? 10.23730  -3.52016  -24.83235 1.000 23.42637 ? 110 ILE   A CB  1 
ATOM   762  C  CG1 . ILE   A 1 103 ? 9.54504   -2.87443  -23.64370 1.000 22.16240 ? 110 ILE   A CG1 1 
ATOM   763  C  CG2 . ILE   A 1 103 ? 9.72788   -2.94563  -26.17665 1.000 21.82573 ? 110 ILE   A CG2 1 
ATOM   764  C  CD1 . ILE   A 1 103 ? 9.99488   -1.42059  -23.41286 1.000 23.97147 ? 110 ILE   A CD1 1 
ATOM   765  N  N   . ALA   A 1 104 ? 10.93604  -7.08674  -23.83123 1.000 18.59762 ? 111 ALA   A N   1 
ATOM   766  C  CA  . ALA   A 1 104 ? 11.34870  -7.84505  -22.66895 1.000 20.10442 ? 111 ALA   A CA  1 
ATOM   767  C  C   . ALA   A 1 104 ? 12.83618  -7.70156  -22.34899 1.000 19.21089 ? 111 ALA   A C   1 
ATOM   768  O  O   . ALA   A 1 104 ? 13.20458  -7.85641  -21.18238 1.000 19.29231 ? 111 ALA   A O   1 
ATOM   769  C  CB  . ALA   A 1 104 ? 10.95572  -9.31491  -22.86395 1.000 21.83275 ? 111 ALA   A CB  1 
ATOM   770  N  N   . LYS   A 1 105 ? 13.70486  -7.43077  -23.34016 1.000 18.45814 ? 112 LYS   A N   1 
ATOM   771  C  CA  . LYS   A 1 105 ? 15.12258  -7.24624  -23.01324 1.000 22.87182 ? 112 LYS   A CA  1 
ATOM   772  C  C   . LYS   A 1 105 ? 15.31467  -6.04385  -22.09747 1.000 24.29812 ? 112 LYS   A C   1 
ATOM   773  O  O   . LYS   A 1 105 ? 15.88729  -6.16990  -21.01268 1.000 22.43528 ? 112 LYS   A O   1 
ATOM   774  C  CB  . LYS   A 1 105 ? 15.96885  -7.12699  -24.29177 1.000 20.03402 ? 112 LYS   A CB  1 
ATOM   775  C  CG  . LYS   A 1 105 ? 17.45578  -7.34745  -24.05059 1.000 29.37669 ? 112 LYS   A CG  1 
ATOM   776  C  CD  . LYS   A 1 105 ? 18.25753  -6.78520  -25.22979 1.000 29.13957 ? 112 LYS   A CD  1 
ATOM   777  C  CE  . LYS   A 1 105 ? 19.68045  -6.39731  -24.81047 1.000 39.53533 ? 112 LYS   A CE  1 
ATOM   778  N  NZ  . LYS   A 1 105 ? 20.68002  -7.13396  -25.65932 1.000 43.45993 ? 112 LYS   A NZ  1 
ATOM   779  N  N   . SER   A 1 106 ? 14.72900  -4.88899  -22.45013 1.000 21.92821 ? 113 SER   A N   1 
ATOM   780  C  CA  . SER   A 1 106 ? 14.92878  -3.74581  -21.56687 1.000 24.24380 ? 113 SER   A CA  1 
ATOM   781  C  C   . SER   A 1 106 ? 14.09853  -3.86297  -20.28938 1.000 22.29463 ? 113 SER   A C   1 
ATOM   782  O  O   . SER   A 1 106 ? 14.55286  -3.44871  -19.21954 1.000 25.68920 ? 113 SER   A O   1 
ATOM   783  C  CB  . SER   A 1 106 ? 14.62638  -2.42047  -22.26693 1.000 29.83381 ? 113 SER   A CB  1 
ATOM   784  O  OG  . SER   A 1 106 ? 13.34131  -2.41195  -22.85728 1.000 28.83181 ? 113 SER   A OG  1 
ATOM   785  N  N   A GLY   A 1 107 ? 12.90550  -4.46863  -20.38709 0.735 20.38401 ? 114 GLY   A N   1 
ATOM   786  N  N   B GLY   A 1 107 ? 12.85171  -4.33725  -20.36225 0.265 20.70502 ? 114 GLY   A N   1 
ATOM   787  C  CA  A GLY   A 1 107 ? 12.12165  -4.70824  -19.18572 0.735 20.72052 ? 114 GLY   A CA  1 
ATOM   788  C  CA  B GLY   A 1 107 ? 12.04482  -4.44451  -19.15153 0.265 21.83917 ? 114 GLY   A CA  1 
ATOM   789  C  C   A GLY   A 1 107 ? 12.81271  -5.61588  -18.18627 0.735 22.88594 ? 114 GLY   A C   1 
ATOM   790  C  C   B GLY   A 1 107 ? 12.70155  -5.29563  -18.07999 0.265 23.01997 ? 114 GLY   A C   1 
ATOM   791  O  O   A GLY   A 1 107 ? 12.74777  -5.38186  -16.97614 0.735 21.65897 ? 114 GLY   A O   1 
ATOM   792  O  O   B GLY   A 1 107 ? 12.73678  -4.91931  -16.90019 0.265 23.51790 ? 114 GLY   A O   1 
ATOM   793  N  N   A THR   A 1 108 ? 13.44269  -6.69224  -18.66412 0.735 19.77178 ? 115 THR   A N   1 
ATOM   794  N  N   B THR   A 1 108 ? 13.17791  -6.48580  -18.46789 0.265 21.18695 ? 115 THR   A N   1 
ATOM   795  C  CA  A THR   A 1 108 ? 14.16986  -7.56558  -17.74262 0.735 22.30567 ? 115 THR   A CA  1 
ATOM   796  C  CA  B THR   A 1 108 ? 13.98820  -7.30783  -17.57358 0.265 22.88220 ? 115 THR   A CA  1 
ATOM   797  C  C   A THR   A 1 108 ? 15.31361  -6.83279  -17.07285 0.735 24.44752 ? 115 THR   A C   1 
ATOM   798  C  C   B THR   A 1 108 ? 15.15396  -6.50061  -17.01910 0.265 24.98011 ? 115 THR   A C   1 
ATOM   799  O  O   A THR   A 1 108 ? 15.53073  -6.98612  -15.86766 0.735 24.15347 ? 115 THR   A O   1 
ATOM   800  O  O   B THR   A 1 108 ? 15.45430  -6.55636  -15.82113 0.265 25.48229 ? 115 THR   A O   1 
ATOM   801  C  CB  A THR   A 1 108 ? 14.72173  -8.79954  -18.45564 0.735 21.64368 ? 115 THR   A CB  1 
ATOM   802  C  CB  B THR   A 1 108 ? 14.51270  -8.53937  -18.31717 0.265 22.49117 ? 115 THR   A CB  1 
ATOM   803  O  OG1 A THR   A 1 108 ? 13.63740  -9.57977  -18.95407 0.735 20.67493 ? 115 THR   A OG1 1 
ATOM   804  O  OG1 B THR   A 1 108 ? 13.41904  -9.24769  -18.91533 0.265 21.70923 ? 115 THR   A OG1 1 
ATOM   805  C  CG2 A THR   A 1 108 ? 15.50897  -9.64935  -17.48869 0.735 22.91034 ? 115 THR   A CG2 1 
ATOM   806  C  CG2 B THR   A 1 108 ? 15.22868  -9.46971  -17.34742 0.265 23.35638 ? 115 THR   A CG2 1 
ATOM   807  N  N   A LYS   A 1 109 ? 16.06364  -6.04458  -17.84171 0.735 23.25034 ? 116 LYS   A N   1 
ATOM   808  N  N   B LYS   A 1 109 ? 15.83056  -5.74973  -17.89346 0.265 24.03693 ? 116 LYS   A N   1 
ATOM   809  C  CA  A LYS   A 1 109 ? 17.16622  -5.29200  -17.25624 0.735 24.24518 ? 116 LYS   A CA  1 
ATOM   810  C  CA  B LYS   A 1 109 ? 16.85229  -4.80529  -17.44786 0.265 25.48243 ? 116 LYS   A CA  1 
ATOM   811  C  C   A LYS   A 1 109 ? 16.67979  -4.46235  -16.07809 0.735 31.37955 ? 116 LYS   A C   1 
ATOM   812  C  C   B LYS   A 1 109 ? 16.26741  -3.80852  -16.45308 0.265 29.46788 ? 116 LYS   A C   1 
ATOM   813  O  O   A LYS   A 1 109 ? 17.22748  -4.55072  -14.97413 0.735 30.96564 ? 116 LYS   A O   1 
ATOM   814  O  O   B LYS   A 1 109 ? 16.66604  -3.75437  -15.28189 0.265 31.05912 ? 116 LYS   A O   1 
ATOM   815  C  CB  A LYS   A 1 109 ? 17.82892  -4.42934  -18.33609 0.735 26.56527 ? 116 LYS   A CB  1 
ATOM   816  C  CB  B LYS   A 1 109 ? 17.43313  -4.07647  -18.66198 0.265 28.12186 ? 116 LYS   A CB  1 
ATOM   817  C  CG  A LYS   A 1 109 ? 18.98017  -3.50336  -17.89699 0.735 35.69617 ? 116 LYS   A CG  1 
ATOM   818  C  CG  B LYS   A 1 109 ? 18.89781  -3.68309  -18.54267 0.265 36.94012 ? 116 LYS   A CG  1 
ATOM   819  C  CD  A LYS   A 1 109 ? 19.37191  -2.62644  -19.09276 0.735 37.61682 ? 116 LYS   A CD  1 
ATOM   820  C  CD  B LYS   A 1 109 ? 19.22811  -2.54791  -19.50143 0.265 38.30430 ? 116 LYS   A CD  1 
ATOM   821  C  CE  A LYS   A 1 109 ? 19.95347  -1.28162  -18.70343 0.735 48.46807 ? 116 LYS   A CE  1 
ATOM   822  C  CE  B LYS   A 1 109 ? 20.31502  -1.64475  -18.94609 0.265 45.87879 ? 116 LYS   A CE  1 
ATOM   823  N  NZ  A LYS   A 1 109 ? 20.99150  -1.46961  -17.65564 0.735 47.56624 ? 116 LYS   A NZ  1 
ATOM   824  N  NZ  B LYS   A 1 109 ? 21.12891  -2.35117  -17.92098 0.265 44.43127 ? 116 LYS   A NZ  1 
ATOM   825  N  N   A ALA   A 1 110 ? 15.62247  -3.67537  -16.28354 0.735 25.65302 ? 117 ALA   A N   1 
ATOM   826  N  N   B ALA   A 1 110 ? 15.31853  -2.99795  -16.92172 0.265 26.50475 ? 117 ALA   A N   1 
ATOM   827  C  CA  A ALA   A 1 110 ? 15.10782  -2.84317  -15.20162 0.735 30.94669 ? 117 ALA   A CA  1 
ATOM   828  C  CA  B ALA   A 1 110 ? 14.60536  -2.06299  -16.06340 0.265 27.08188 ? 117 ALA   A CA  1 
ATOM   829  C  C   A ALA   A 1 110 ? 14.65068  -3.69535  -14.02488 0.735 29.10292 ? 117 ALA   A C   1 
ATOM   830  C  C   B ALA   A 1 110 ? 14.16248  -2.71924  -14.75940 0.265 27.77301 ? 117 ALA   A C   1 
ATOM   831  O  O   A ALA   A 1 110 ? 14.95792  -3.39444  -12.86414 0.735 31.05361 ? 117 ALA   A O   1 
ATOM   832  O  O   B ALA   A 1 110 ? 14.31124  -2.13701  -13.67712 0.265 28.78044 ? 117 ALA   A O   1 
ATOM   833  C  CB  A ALA   A 1 110 ? 13.97060  -1.96285  -15.71920 0.735 26.40806 ? 117 ALA   A CB  1 
ATOM   834  C  CB  B ALA   A 1 110 ? 13.40953  -1.49751  -16.82902 0.265 25.96557 ? 117 ALA   A CB  1 
ATOM   835  N  N   A PHE   A 1 111 ? 13.88460  -4.74887  -14.29926 0.735 27.91906 ? 118 PHE   A N   1 
ATOM   836  N  N   B PHE   A 1 111 ? 13.63457  -3.94621  -14.83723 0.265 27.24851 ? 118 PHE   A N   1 
ATOM   837  C  CA  A PHE   A 1 111 ? 13.32237  -5.55145  -13.21848 0.735 24.61291 ? 118 PHE   A CA  1 
ATOM   838  C  CA  B PHE   A 1 111 ? 13.28551  -4.69815  -13.63054 0.265 26.93718 ? 118 PHE   A CA  1 
ATOM   839  C  C   A PHE   A 1 111 ? 14.42384  -6.12891  -12.33939 0.735 29.91532 ? 118 PHE   A C   1 
ATOM   840  C  C   B PHE   A 1 111 ? 14.51614  -4.81164  -12.73219 0.265 31.05670 ? 118 PHE   A C   1 
ATOM   841  O  O   A PHE   A 1 111 ? 14.34151  -6.08763  -11.10905 0.735 28.98109 ? 118 PHE   A O   1 
ATOM   842  O  O   B PHE   A 1 111 ? 14.64989  -4.04732  -11.77523 0.265 32.44672 ? 118 PHE   A O   1 
ATOM   843  C  CB  A PHE   A 1 111 ? 12.44219  -6.63373  -13.84470 0.735 25.05844 ? 118 PHE   A CB  1 
ATOM   844  C  CB  B PHE   A 1 111 ? 12.70415  -6.06808  -14.01005 0.265 26.02471 ? 118 PHE   A CB  1 
ATOM   845  C  CG  A PHE   A 1 111 ? 11.78623  -7.56224  -12.87747 0.735 22.01623 ? 118 PHE   A CG  1 
ATOM   846  C  CG  B PHE   A 1 111 ? 11.95541  -6.76565  -12.89589 0.265 24.81493 ? 118 PHE   A CG  1 
ATOM   847  C  CD1 A PHE   A 1 111 ? 11.14314  -7.09818  -11.72924 0.735 22.76137 ? 118 PHE   A CD1 1 
ATOM   848  C  CD1 B PHE   A 1 111 ? 11.31738  -6.04776  -11.89468 0.265 24.02226 ? 118 PHE   A CD1 1 
ATOM   849  C  CD2 A PHE   A 1 111 ? 11.73009  -8.91851  -13.17031 0.735 20.97518 ? 118 PHE   A CD2 1 
ATOM   850  C  CD2 B PHE   A 1 111 ? 11.81484  -8.14100  -12.90487 0.265 23.25527 ? 118 PHE   A CD2 1 
ATOM   851  C  CE1 A PHE   A 1 111 ? 10.50519  -7.98465  -10.88056 0.735 20.69080 ? 118 PHE   A CE1 1 
ATOM   852  C  CE1 B PHE   A 1 111 ? 10.60766  -6.68861  -10.89465 0.265 22.53729 ? 118 PHE   A CE1 1 
ATOM   853  C  CE2 A PHE   A 1 111 ? 11.07850  -9.79963  -12.32959 0.735 22.50308 ? 118 PHE   A CE2 1 
ATOM   854  C  CE2 B PHE   A 1 111 ? 11.10157  -8.78991  -11.90485 0.265 24.17468 ? 118 PHE   A CE2 1 
ATOM   855  C  CZ  A PHE   A 1 111 ? 10.47435  -9.32247  -11.16495 0.735 23.95745 ? 118 PHE   A CZ  1 
ATOM   856  C  CZ  B PHE   A 1 111 ? 10.49913  -8.06517  -10.89978 0.265 20.95777 ? 118 PHE   A CZ  1 
ATOM   857  N  N   A MET   A 1 112 ? 15.48845  -6.62467  -12.94704 0.735 29.27810 ? 119 MET   A N   1 
ATOM   858  N  N   B MET   A 1 112 ? 15.43283  -5.73171  -13.03724 0.265 29.66647 ? 119 MET   A N   1 
ATOM   859  C  CA  A MET   A 1 112 ? 16.48188  -7.32645  -12.15349 0.735 34.18282 ? 119 MET   A CA  1 
ATOM   860  C  CA  B MET   A 1 112 ? 16.73249  -5.76536  -12.37247 0.265 34.33823 ? 119 MET   A CA  1 
ATOM   861  C  C   A MET   A 1 112 ? 17.31778  -6.36838  -11.31180 0.735 38.18236 ? 119 MET   A C   1 
ATOM   862  C  C   B MET   A 1 112 ? 17.07493  -4.47815  -11.63369 0.265 36.58516 ? 119 MET   A C   1 
ATOM   863  O  O   A MET   A 1 112 ? 17.81962  -6.75991  -10.24819 0.735 35.66669 ? 119 MET   A O   1 
ATOM   864  O  O   B MET   A 1 112 ? 17.11494  -4.46281  -10.39928 0.265 39.01212 ? 119 MET   A O   1 
ATOM   865  C  CB  A MET   A 1 112 ? 17.33875  -8.17913  -13.08823 0.735 36.45993 ? 119 MET   A CB  1 
ATOM   866  C  CB  B MET   A 1 112 ? 17.83072  -6.05483  -13.39202 0.265 33.69818 ? 119 MET   A CB  1 
ATOM   867  C  CG  A MET   A 1 112 ? 16.89277  -9.63295  -13.07768 0.735 29.98309 ? 119 MET   A CG  1 
ATOM   868  C  CG  B MET   A 1 112 ? 18.80318  -7.13335  -12.98540 0.265 38.34274 ? 119 MET   A CG  1 
ATOM   869  S  SD  A MET   A 1 112 ? 17.90987  -10.48412 -14.25973 0.735 47.29431 ? 119 MET   A SD  1 
ATOM   870  S  SD  B MET   A 1 112 ? 18.66383  -8.56900  -14.05354 0.265 44.69208 ? 119 MET   A SD  1 
ATOM   871  C  CE  A MET   A 1 112 ? 16.78348  -11.75230 -14.77241 0.735 29.80280 ? 119 MET   A CE  1 
ATOM   872  C  CE  B MET   A 1 112 ? 17.85771  -9.71120  -12.95082 0.265 36.62798 ? 119 MET   A CE  1 
ATOM   873  N  N   A GLU   A 1 113 ? 17.45314  -5.11876  -11.75427 0.735 34.46486 ? 120 GLU   A N   1 
ATOM   874  N  N   B GLU   A 1 113 ? 17.35284  -3.40188  -12.37513 0.265 38.76353 ? 120 GLU   A N   1 
ATOM   875  C  CA  A GLU   A 1 113 ? 18.09560  -4.10333  -10.93611 0.735 39.57838 ? 120 GLU   A CA  1 
ATOM   876  C  CA  B GLU   A 1 113 ? 17.80786  -2.16815  -11.73917 0.265 40.60461 ? 120 GLU   A CA  1 
ATOM   877  C  C   A GLU   A 1 113 ? 17.21658  -3.74337  -9.74785  0.735 44.04447 ? 120 GLU   A C   1 
ATOM   878  C  C   B GLU   A 1 113 ? 16.81799  -1.73937  -10.67475 0.265 42.69061 ? 120 GLU   A C   1 
ATOM   879  O  O   A GLU   A 1 113 ? 17.71002  -3.56492  -8.62385  0.735 43.83683 ? 120 GLU   A O   1 
ATOM   880  O  O   B GLU   A 1 113 ? 17.07246  -1.84226  -9.47050  0.265 43.27239 ? 120 GLU   A O   1 
ATOM   881  C  CB  A GLU   A 1 113 ? 18.38613  -2.87263  -11.79157 0.735 38.40929 ? 120 GLU   A CB  1 
ATOM   882  C  CB  B GLU   A 1 113 ? 17.97593  -1.03569  -12.75930 0.265 44.23654 ? 120 GLU   A CB  1 
ATOM   883  C  CG  A GLU   A 1 113 ? 19.45980  -3.09184  -12.85975 0.735 43.45328 ? 120 GLU   A CG  1 
ATOM   884  C  CG  B GLU   A 1 113 ? 18.92002  -1.30350  -13.91488 0.265 46.57527 ? 120 GLU   A CG  1 
ATOM   885  C  CD  A GLU   A 1 113 ? 19.61807  -1.89798  -13.79173 0.735 48.99164 ? 120 GLU   A CD  1 
ATOM   886  C  CD  B GLU   A 1 113 ? 20.36283  -0.96899  -13.55964 0.265 52.50803 ? 120 GLU   A CD  1 
ATOM   887  O  OE1 A GLU   A 1 113 ? 18.93751  -0.87643  -13.55866 0.735 48.91863 ? 120 GLU   A OE1 1 
ATOM   888  O  OE1 B GLU   A 1 113 ? 20.76666  0.19966   -13.75395 0.265 55.15141 ? 120 GLU   A OE1 1 
ATOM   889  O  OE2 A GLU   A 1 113 ? 20.42015  -1.98013  -14.75688 0.735 54.12499 ? 120 GLU   A OE2 1 
ATOM   890  O  OE2 B GLU   A 1 113 ? 21.08924  -1.86184  -13.07547 0.265 53.68015 ? 120 GLU   A OE2 1 
ATOM   891  N  N   A ALA   A 1 114 ? 15.90655  -3.63582  -9.98151  0.735 37.11039 ? 121 ALA   A N   1 
ATOM   892  N  N   B ALA   A 1 114 ? 15.70559  -1.20282  -11.14499 0.265 39.59541 ? 121 ALA   A N   1 
ATOM   893  C  CA  A ALA   A 1 114 ? 14.97446  -3.35658  -8.89781  0.735 38.36134 ? 121 ALA   A CA  1 
ATOM   894  C  CA  B ALA   A 1 114 ? 14.50816  -1.00944  -10.35381 0.265 41.11421 ? 121 ALA   A CA  1 
ATOM   895  C  C   A ALA   A 1 114 ? 15.01946  -4.44363  -7.83340  0.735 41.52644 ? 121 ALA   A C   1 
ATOM   896  C  C   B ALA   A 1 114 ? 14.34162  -2.04585  -9.24907  0.265 42.69167 ? 121 ALA   A C   1 
ATOM   897  O  O   A ALA   A 1 114 ? 14.93676  -4.14933  -6.63663  0.735 48.09979 ? 121 ALA   A O   1 
ATOM   898  O  O   B ALA   A 1 114 ? 14.29820  -1.72624  -8.04823  0.265 46.61653 ? 121 ALA   A O   1 
ATOM   899  C  CB  A ALA   A 1 114 ? 13.56204  -3.19543  -9.45751  0.735 37.08143 ? 121 ALA   A CB  1 
ATOM   900  C  CB  B ALA   A 1 114 ? 13.32501  -1.08372  -11.30348 0.265 35.56925 ? 121 ALA   A CB  1 
ATOM   901  N  N   A LEU   A 1 115 ? 15.16313  -5.70356  -8.24752  0.735 36.44282 ? 122 LEU   A N   1 
ATOM   902  N  N   B LEU   A 1 115 ? 14.19303  -3.30145  -9.66742  0.265 39.30648 ? 122 LEU   A N   1 
ATOM   903  C  CA  A LEU   A 1 115 ? 15.16725  -6.81024  -7.29817  0.735 41.31785 ? 122 LEU   A CA  1 
ATOM   904  C  CA  B LEU   A 1 115 ? 13.99348  -4.38513  -8.71991  0.265 42.86050 ? 122 LEU   A CA  1 
ATOM   905  C  C   A LEU   A 1 115 ? 16.35763  -6.71960  -6.34752  0.735 53.49249 ? 122 LEU   A C   1 
ATOM   906  C  C   B LEU   A 1 115 ? 14.87150  -4.20522  -7.49682  0.265 45.16426 ? 122 LEU   A C   1 
ATOM   907  O  O   A LEU   A 1 115 ? 16.21684  -6.95363  -5.14143  0.735 48.29096 ? 122 LEU   A O   1 
ATOM   908  O  O   B LEU   A 1 115 ? 14.37362  -4.03050  -6.38076  0.265 48.84312 ? 122 LEU   A O   1 
ATOM   909  C  CB  A LEU   A 1 115 ? 15.19067  -8.13619  -8.05060  0.735 39.90200 ? 122 LEU   A CB  1 
ATOM   910  C  CB  B LEU   A 1 115 ? 14.21284  -5.73257  -9.42898  0.265 39.11935 ? 122 LEU   A CB  1 
ATOM   911  C  CG  A LEU   A 1 115 ? 13.87218  -8.46720  -8.74664  0.735 29.53569 ? 122 LEU   A CG  1 
ATOM   912  C  CG  B LEU   A 1 115 ? 14.35412  -7.11627  -8.77273  0.265 40.03682 ? 122 LEU   A CG  1 
ATOM   913  C  CD1 A LEU   A 1 115 ? 14.03665  -9.69343  -9.59558  0.735 32.92221 ? 122 LEU   A CD1 1 
ATOM   914  C  CD1 B LEU   A 1 115 ? 15.80973  -7.38579  -8.65558  0.265 44.38629 ? 122 LEU   A CD1 1 
ATOM   915  C  CD2 A LEU   A 1 115 ? 12.75267  -8.65916  -7.72423  0.735 29.83920 ? 122 LEU   A CD2 1 
ATOM   916  C  CD2 B LEU   A 1 115 ? 13.82500  -7.18565  -7.35774  0.265 41.46959 ? 122 LEU   A CD2 1 
ATOM   917  N  N   A GLN   A 1 116 ? 17.54191  -6.39980  -6.87261  0.735 56.99000 ? 123 GLN   A N   1 
ATOM   918  N  N   B GLN   A 1 116 ? 16.17719  -4.22691  -7.68070  0.265 48.70395 ? 123 GLN   A N   1 
ATOM   919  C  CA  A GLN   A 1 116 ? 18.69821  -6.22397  -6.00190  0.735 62.84433 ? 123 GLN   A CA  1 
ATOM   920  C  CA  B GLN   A 1 116 ? 17.01518  -4.05281  -6.51599  0.265 54.64700 ? 123 GLN   A CA  1 
ATOM   921  C  C   A GLN   A 1 116 ? 18.58320  -4.94984  -5.16990  0.735 61.60894 ? 123 GLN   A C   1 
ATOM   922  C  C   B GLN   A 1 116 ? 16.61052  -2.74398  -5.84694  0.265 56.31103 ? 123 GLN   A C   1 
ATOM   923  O  O   A GLN   A 1 116 ? 19.16424  -4.86662  -4.08130  0.735 64.51277 ? 123 GLN   A O   1 
ATOM   924  O  O   B GLN   A 1 116 ? 15.92130  -2.75758  -4.82247  0.265 57.90585 ? 123 GLN   A O   1 
ATOM   925  C  CB  A GLN   A 1 116 ? 19.98235  -6.22468  -6.83237  0.735 62.81015 ? 123 GLN   A CB  1 
ATOM   926  C  CB  B GLN   A 1 116 ? 18.48107  -4.11280  -6.93586  0.265 57.04017 ? 123 GLN   A CB  1 
ATOM   927  C  CG  A GLN   A 1 116 ? 20.41976  -7.61713  -7.24887  0.735 67.31852 ? 123 GLN   A CG  1 
ATOM   928  C  CG  B GLN   A 1 116 ? 18.75636  -5.53675  -7.38400  0.265 61.24742 ? 123 GLN   A CG  1 
ATOM   929  C  CD  A GLN   A 1 116 ? 21.92075  -7.82111  -7.15397  0.735 76.97863 ? 123 GLN   A CD  1 
ATOM   930  C  CD  B GLN   A 1 116 ? 18.11894  -6.55057  -6.44087  0.265 66.39347 ? 123 GLN   A CD  1 
ATOM   931  O  OE1 A GLN   A 1 116 ? 22.66317  -6.90385  -6.79656  0.735 79.72838 ? 123 GLN   A OE1 1 
ATOM   932  O  OE1 B GLN   A 1 116 ? 17.35985  -7.43150  -6.87141  0.265 68.79195 ? 123 GLN   A OE1 1 
ATOM   933  N  NE2 A GLN   A 1 116 ? 22.37613  -9.03364  -7.47077  0.735 75.34584 ? 123 GLN   A NE2 1 
ATOM   934  N  NE2 B GLN   A 1 116 ? 18.48001  -6.47670  -5.16380  0.265 67.49490 ? 123 GLN   A NE2 1 
ATOM   935  N  N   A ALA   A 1 117 ? 17.83436  -3.95941  -5.65305  0.735 57.77148 ? 124 ALA   A N   1 
ATOM   936  N  N   B ALA   A 1 117 ? 16.96713  -1.61162  -6.45372  0.265 58.28148 ? 124 ALA   A N   1 
ATOM   937  C  CA  A ALA   A 1 117 ? 17.60468  -2.70229  -4.94090  0.735 58.32017 ? 124 ALA   A CA  1 
ATOM   938  C  CA  B ALA   A 1 117 ? 16.61968  -0.29227  -5.92515  0.265 57.59054 ? 124 ALA   A CA  1 
ATOM   939  C  C   A ALA   A 1 117 ? 16.25621  -2.68029  -4.21218  0.735 60.50312 ? 124 ALA   A C   1 
ATOM   940  C  C   B ALA   A 1 117 ? 15.67321  -0.35835  -4.73104  0.265 58.53821 ? 124 ALA   A C   1 
ATOM   941  O  O   A ALA   A 1 117 ? 15.57304  -1.64842  -4.18218  0.735 56.99828 ? 124 ALA   A O   1 
ATOM   942  O  O   B ALA   A 1 117 ? 15.78878  0.44420   -3.79961  0.265 60.70297 ? 124 ALA   A O   1 
ATOM   943  C  CB  A ALA   A 1 117 ? 17.71754  -1.52878  -5.91097  0.735 55.40536 ? 124 ALA   A CB  1 
ATOM   944  C  CB  B ALA   A 1 117 ? 15.99871  0.57347   -7.02192  0.265 55.94353 ? 124 ALA   A CB  1 
ATOM   945  N  N   A GLY   A 1 118 ? 15.83068  -3.81029  -3.63419  0.735 54.78359 ? 125 GLY   A N   1 
ATOM   946  N  N   B GLY   A 1 118 ? 14.72948  -1.28596  -4.74672  0.265 55.20695 ? 125 GLY   A N   1 
ATOM   947  C  CA  A GLY   A 1 118 ? 14.68402  -3.81733  -2.73937  0.735 54.50791 ? 125 GLY   A CA  1 
ATOM   948  C  CA  B GLY   A 1 118 ? 13.83686  -1.40623  -3.61454  0.265 52.98013 ? 125 GLY   A CA  1 
ATOM   949  C  C   A GLY   A 1 118 ? 13.40947  -4.51119  -3.19173  0.735 49.80946 ? 125 GLY   A C   1 
ATOM   950  C  C   B GLY   A 1 118 ? 12.46974  -1.82656  -4.08074  0.265 47.53924 ? 125 GLY   A C   1 
ATOM   951  O  O   A GLY   A 1 118 ? 12.69344  -5.09256  -2.36619  0.735 37.85824 ? 125 GLY   A O   1 
ATOM   952  O  O   B GLY   A 1 118 ? 11.53597  -1.95047  -3.28695  0.265 44.21638 ? 125 GLY   A O   1 
ATOM   953  N  N   A ALA   A 1 119 ? 13.09966  -4.45115  -4.48630  0.735 43.79550 ? 126 ALA   A N   1 
ATOM   954  N  N   B ALA   A 1 119 ? 12.34883  -2.03106  -5.38882  0.265 46.55641 ? 126 ALA   A N   1 
ATOM   955  C  CA  A ALA   A 1 119 ? 11.78612  -4.87947  -4.95250  0.735 35.41998 ? 126 ALA   A CA  1 
ATOM   956  C  CA  B ALA   A 1 119 ? 11.12255  -2.58602  -5.94273  0.265 41.29355 ? 126 ALA   A CA  1 
ATOM   957  C  C   A ALA   A 1 119 ? 11.62963  -6.39517  -4.82981  0.735 30.73678 ? 126 ALA   A C   1 
ATOM   958  C  C   B ALA   A 1 119 ? 10.80426  -3.91476  -5.28764  0.265 38.30305 ? 126 ALA   A C   1 
ATOM   959  O  O   A ALA   A 1 119 ? 12.56532  -7.12186  -4.50946  0.735 30.72444 ? 126 ALA   A O   1 
ATOM   960  O  O   B ALA   A 1 119 ? 11.70146  -4.67569  -4.91384  0.265 36.16703 ? 126 ALA   A O   1 
ATOM   961  C  CB  A ALA   A 1 119 ? 11.55665  -4.43439  -6.39342  0.735 38.61447 ? 126 ALA   A CB  1 
ATOM   962  C  CB  B ALA   A 1 119 ? 11.26133  -2.79350  -7.44985  0.265 38.97163 ? 126 ALA   A CB  1 
ATOM   963  N  N   A ASP   A 1 120 ? 10.41819  -6.88424  -5.09101  0.735 29.73673 ? 127 ASP   A N   1 
ATOM   964  N  N   B ASP   A 1 120 ? 9.51565   -4.20768  -5.16585  0.265 33.97277 ? 127 ASP   A N   1 
ATOM   965  C  CA  A ASP   A 1 120 ? 10.15889  -8.31563  -5.07290  0.735 28.93199 ? 127 ASP   A CA  1 
ATOM   966  C  CA  B ASP   A 1 120 ? 9.15059   -5.59333  -4.94804  0.265 31.91702 ? 127 ASP   A CA  1 
ATOM   967  C  C   A ASP   A 1 120 ? 9.44405   -8.70762  -6.35736  0.735 27.55411 ? 127 ASP   A C   1 
ATOM   968  C  C   B ASP   A 1 120 ? 9.27407   -6.39769  -6.22547  0.265 29.28728 ? 127 ASP   A C   1 
ATOM   969  O  O   A ASP   A 1 120 ? 9.07788   -7.85344  -7.16430  0.735 23.49929 ? 127 ASP   A O   1 
ATOM   970  O  O   B ASP   A 1 120 ? 9.17017   -5.88012  -7.33860  0.265 28.41191 ? 127 ASP   A O   1 
ATOM   971  C  CB  A ASP   A 1 120 ? 9.34732   -8.73687  -3.84101  0.735 30.08851 ? 127 ASP   A CB  1 
ATOM   972  C  CB  B ASP   A 1 120 ? 7.72499   -5.76774  -4.44276  0.265 32.37111 ? 127 ASP   A CB  1 
ATOM   973  C  CG  A ASP   A 1 120 ? 7.95121   -8.17433  -3.85304  0.735 31.53291 ? 127 ASP   A CG  1 
ATOM   974  C  CG  B ASP   A 1 120 ? 7.44352   -7.22653  -4.07176  0.265 33.48716 ? 127 ASP   A CG  1 
ATOM   975  O  OD1 A ASP   A 1 120 ? 7.82455   -6.92998  -3.70693  0.735 39.80868 ? 127 ASP   A OD1 1 
ATOM   976  O  OD1 B ASP   A 1 120 ? 7.18192   -8.04429  -4.92573  0.265 28.39948 ? 127 ASP   A OD1 1 
ATOM   977  O  OD2 A ASP   A 1 120 ? 6.97743   -8.95580  -4.00151  0.735 27.61014 ? 127 ASP   A OD2 1 
ATOM   978  O  OD2 B ASP   A 1 120 ? 7.51165   -7.64047  -2.95245  0.265 34.67952 ? 127 ASP   A OD2 1 
ATOM   979  N  N   A ILE   A 1 121 ? 9.30275   -10.02214 -6.55500  0.735 24.63977 ? 128 ILE   A N   1 
ATOM   980  N  N   B ILE   A 1 121 ? 9.48262   -7.68876  -6.03415  0.265 28.09859 ? 128 ILE   A N   1 
ATOM   981  C  CA  A ILE   A 1 121 ? 8.78086   -10.55618 -7.81548  0.735 23.60575 ? 128 ILE   A CA  1 
ATOM   982  C  CA  B ILE   A 1 121 ? 9.22195   -8.70229  -7.03731  0.265 26.66274 ? 128 ILE   A CA  1 
ATOM   983  C  C   A ILE   A 1 121 ? 7.37779   -10.06011 -8.11577  0.735 23.95616 ? 128 ILE   A C   1 
ATOM   984  C  C   B ILE   A 1 121 ? 7.84534   -8.46868  -7.65073  0.265 25.87555 ? 128 ILE   A C   1 
ATOM   985  O  O   A ILE   A 1 121 ? 7.00015   -9.92138  -9.28249  0.735 24.10017 ? 128 ILE   A O   1 
ATOM   986  O  O   B ILE   A 1 121 ? 7.67437   -8.53259  -8.87703  0.265 25.76159 ? 128 ILE   A O   1 
ATOM   987  C  CB  A ILE   A 1 121 ? 8.86756   -12.09647 -7.80134  0.735 25.39602 ? 128 ILE   A CB  1 
ATOM   988  C  CB  B ILE   A 1 121 ? 9.30067   -10.09024 -6.39228  0.265 24.70244 ? 128 ILE   A CB  1 
ATOM   989  C  CG1 A ILE   A 1 121 ? 10.34528  -12.52169 -7.93231  0.735 29.10986 ? 128 ILE   A CG1 1 
ATOM   990  C  CG1 B ILE   A 1 121 ? 10.76931  -10.46461 -6.16880  0.265 31.54384 ? 128 ILE   A CG1 1 
ATOM   991  C  CG2 A ILE   A 1 121 ? 7.91731   -12.74079 -8.80326  0.735 25.78330 ? 128 ILE   A CG2 1 
ATOM   992  C  CG2 B ILE   A 1 121 ? 8.66013   -11.12041 -7.31673  0.265 27.05179 ? 128 ILE   A CG2 1 
ATOM   993  C  CD1 A ILE   A 1 121 ? 10.59891  -13.99738 -7.73008  0.735 27.77635 ? 128 ILE   A CD1 1 
ATOM   994  C  CD1 B ILE   A 1 121 ? 11.67119  -10.09195 -7.32328  0.265 30.62980 ? 128 ILE   A CD1 1 
ATOM   995  N  N   A SER   A 1 122 ? 6.58784   -9.74781  -7.09548  0.735 23.58065 ? 129 SER   A N   1 
ATOM   996  N  N   B SER   A 1 122 ? 6.85106   -8.21400  -6.78865  0.265 25.66802 ? 129 SER   A N   1 
ATOM   997  C  CA  A SER   A 1 122 ? 5.22670   -9.29138  -7.36809  0.735 24.29245 ? 129 SER   A CA  1 
ATOM   998  C  CA  B SER   A 1 122 ? 5.46995   -8.05051  -7.24817  0.265 25.53811 ? 129 SER   A CA  1 
ATOM   999  C  C   A SER   A 1 122 ? 5.18193   -8.00110  -8.17909  0.735 22.50015 ? 129 SER   A C   1 
ATOM   1000 C  C   B SER   A 1 122 ? 5.29909   -6.91699  -8.24970  0.265 24.48418 ? 129 SER   A C   1 
ATOM   1001 O  O   A SER   A 1 122 ? 4.10479   -7.62580  -8.66865  0.735 25.22136 ? 129 SER   A O   1 
ATOM   1002 O  O   B SER   A 1 122 ? 4.25055   -6.82821  -8.89948  0.265 24.45110 ? 129 SER   A O   1 
ATOM   1003 C  CB  A SER   A 1 122 ? 4.46405   -9.06803  -6.06407  0.735 24.02533 ? 129 SER   A CB  1 
ATOM   1004 C  CB  B SER   A 1 122 ? 4.56422   -7.85135  -6.02416  0.265 25.61396 ? 129 SER   A CB  1 
ATOM   1005 O  OG  A SER   A 1 122 ? 4.78119   -7.80201  -5.54273  0.735 25.71028 ? 129 SER   A OG  1 
ATOM   1006 O  OG  B SER   A 1 122 ? 5.10889   -6.84651  -5.16540  0.265 26.01117 ? 129 SER   A OG  1 
ATOM   1007 N  N   A MET   A 1 123 ? 6.29409   -7.29104  -8.29461  0.735 23.45223 ? 130 MET   A N   1 
ATOM   1008 N  N   B MET   A 1 123 ? 6.28329   -6.04787  -8.38339  0.265 23.01433 ? 130 MET   A N   1 
ATOM   1009 C  CA  A MET   A 1 123 ? 6.34293   -6.01233  -8.99151  0.735 22.45679 ? 130 MET   A CA  1 
ATOM   1010 C  CA  B MET   A 1 123 ? 6.22975   -4.98197  -9.35927  0.265 24.95383 ? 130 MET   A CA  1 
ATOM   1011 C  C   A MET   A 1 123 ? 6.62597   -6.16103  -10.49586 0.735 21.98466 ? 130 MET   A C   1 
ATOM   1012 C  C   B MET   A 1 123 ? 6.53673   -5.48039  -10.76985 0.265 23.66477 ? 130 MET   A C   1 
ATOM   1013 O  O   A MET   A 1 123 ? 6.76659   -5.15677  -11.19543 0.735 23.24859 ? 130 MET   A O   1 
ATOM   1014 O  O   B MET   A 1 123 ? 6.63642   -4.66697  -11.69598 0.265 24.37174 ? 130 MET   A O   1 
ATOM   1015 C  CB  A MET   A 1 123 ? 7.39431   -5.13096  -8.31942  0.735 25.89637 ? 130 MET   A CB  1 
ATOM   1016 C  CB  B MET   A 1 123 ? 7.23184   -3.89727  -8.97326  0.265 25.11164 ? 130 MET   A CB  1 
ATOM   1017 C  CG  A MET   A 1 123 ? 6.97503   -4.84981  -6.88690  0.735 27.51785 ? 130 MET   A CG  1 
ATOM   1018 C  CG  B MET   A 1 123 ? 7.42895   -3.72417  -7.46863  0.265 29.83814 ? 130 MET   A CG  1 
ATOM   1019 S  SD  A MET   A 1 123 ? 8.21300   -4.05855  -5.87431  0.735 30.84793 ? 130 MET   A SD  1 
ATOM   1020 S  SD  B MET   A 1 123 ? 7.19668   -2.04068  -6.91651  0.265 41.20328 ? 130 MET   A SD  1 
ATOM   1021 C  CE  A MET   A 1 123 ? 8.20180   -2.43274  -6.65233  0.735 33.63794 ? 130 MET   A CE  1 
ATOM   1022 C  CE  B MET   A 1 123 ? 8.18067   -1.30735  -8.18751  0.265 36.18535 ? 130 MET   A CE  1 
ATOM   1023 N  N   A ILE   A 1 124 ? 6.64021   -7.39019  -11.00549 0.735 19.74314 ? 131 ILE   A N   1 
ATOM   1024 N  N   B ILE   A 1 124 ? 6.70007   -6.79474  -10.95095 0.265 20.96473 ? 131 ILE   A N   1 
ATOM   1025 C  CA  A ILE   A 1 124 ? 7.11552   -7.65445  -12.36617 0.735 20.88882 ? 131 ILE   A CA  1 
ATOM   1026 C  CA  B ILE   A 1 124 ? 7.18257   -7.30537  -12.23561 0.265 21.43633 ? 131 ILE   A CA  1 
ATOM   1027 C  C   A ILE   A 1 124 ? 6.32502   -6.88078  -13.42986 0.735 20.68713 ? 131 ILE   A C   1 
ATOM   1028 C  C   B ILE   A 1 124 ? 6.35758   -6.73072  -13.38197 0.265 20.91209 ? 131 ILE   A C   1 
ATOM   1029 O  O   A ILE   A 1 124 ? 6.88064   -6.49556  -14.46673 0.735 18.91935 ? 131 ILE   A O   1 
ATOM   1030 O  O   B ILE   A 1 124 ? 6.89879   -6.35939  -14.43188 0.265 19.02829 ? 131 ILE   A O   1 
ATOM   1031 C  CB  A ILE   A 1 124 ? 7.07899   -9.17909  -12.59728 0.735 21.23649 ? 131 ILE   A CB  1 
ATOM   1032 C  CB  B ILE   A 1 124 ? 7.18718   -8.85020  -12.23730 0.265 21.50165 ? 131 ILE   A CB  1 
ATOM   1033 C  CG1 A ILE   A 1 124 ? 7.73231   -9.54126  -13.94471 0.735 21.00168 ? 131 ILE   A CG1 1 
ATOM   1034 C  CG1 B ILE   A 1 124 ? 7.74945   -9.40653  -13.55209 0.265 22.03567 ? 131 ILE   A CG1 1 
ATOM   1035 C  CG2 A ILE   A 1 124 ? 5.63218   -9.71394  -12.47875 0.735 20.24440 ? 131 ILE   A CG2 1 
ATOM   1036 C  CG2 B ILE   A 1 124 ? 5.78102   -9.40904  -11.99658 0.265 21.59505 ? 131 ILE   A CG2 1 
ATOM   1037 C  CD1 A ILE   A 1 124 ? 7.83747   -11.04366 -14.13037 0.735 19.20347 ? 131 ILE   A CD1 1 
ATOM   1038 C  CD1 B ILE   A 1 124 ? 7.37397   -10.85892 -13.77051 0.265 19.71602 ? 131 ILE   A CD1 1 
ATOM   1039 N  N   . GLY   A 1 125 ? 5.04136   -6.62863  -13.19787 1.000 22.60714 ? 132 GLY   A N   1 
ATOM   1040 C  CA  . GLY   A 1 125 ? 4.22584   -6.01409  -14.23338 1.000 22.22973 ? 132 GLY   A CA  1 
ATOM   1041 C  C   . GLY   A 1 125 ? 4.61586   -4.56642  -14.50417 1.000 26.79001 ? 132 GLY   A C   1 
ATOM   1042 O  O   . GLY   A 1 125 ? 4.32949   -4.03795  -15.58440 1.000 25.65099 ? 132 GLY   A O   1 
ATOM   1043 N  N   . GLN   A 1 126 ? 5.22814   -3.89365  -13.52468 1.000 23.28646 ? 133 GLN   A N   1 
ATOM   1044 C  CA  . GLN   A 1 126 ? 5.66426   -2.52295  -13.75206 1.000 24.56966 ? 133 GLN   A CA  1 
ATOM   1045 C  C   . GLN   A 1 126 ? 6.79638   -2.44625  -14.75621 1.000 26.08272 ? 133 GLN   A C   1 
ATOM   1046 O  O   . GLN   A 1 126 ? 7.16283   -1.34557  -15.17014 1.000 28.34669 ? 133 GLN   A O   1 
ATOM   1047 C  CB  . GLN   A 1 126 ? 6.08638   -1.86350  -12.44554 1.000 28.34097 ? 133 GLN   A CB  1 
ATOM   1048 C  CG  . GLN   A 1 126 ? 5.03264   -2.01715  -11.34327 1.000 28.97059 ? 133 GLN   A CG  1 
ATOM   1049 C  CD  . GLN   A 1 126 ? 5.46974   -1.31422  -10.07730 1.000 36.78767 ? 133 GLN   A CD  1 
ATOM   1050 O  OE1 . GLN   A 1 126 ? 6.18484   -0.30169  -10.13259 1.000 37.62488 ? 133 GLN   A OE1 1 
ATOM   1051 N  NE2 . GLN   A 1 126 ? 5.11171   -1.88171  -8.93084  1.000 40.26265 ? 133 GLN   A NE2 1 
ATOM   1052 N  N   A PHE   A 1 127 ? 7.38016   -3.59496  -15.11297 0.735 23.22928 ? 134 PHE   A N   1 
ATOM   1053 N  N   B PHE   A 1 127 ? 7.32858   -3.56655  -15.21295 0.265 23.56039 ? 134 PHE   A N   1 
ATOM   1054 C  CA  A PHE   A 1 127 ? 8.50938   -3.69142  -16.03467 0.735 24.94117 ? 134 PHE   A CA  1 
ATOM   1055 C  CA  B PHE   A 1 127 ? 8.43060   -3.48264  -16.15475 0.265 25.06179 ? 134 PHE   A CA  1 
ATOM   1056 C  C   A PHE   A 1 127 ? 8.11387   -4.31652  -17.37368 0.735 24.25422 ? 134 PHE   A C   1 
ATOM   1057 C  C   B PHE   A 1 127 ? 8.09180   -4.19663  -17.44040 0.265 24.45805 ? 134 PHE   A C   1 
ATOM   1058 O  O   A PHE   A 1 127 ? 8.98866   -4.63684  -18.18629 0.735 22.13606 ? 134 PHE   A O   1 
ATOM   1059 O  O   B PHE   A 1 127 ? 8.97192   -4.42087  -18.28149 0.265 23.11990 ? 134 PHE   A O   1 
ATOM   1060 C  CB  A PHE   A 1 127 ? 9.64470   -4.48266  -15.35968 0.735 21.79908 ? 134 PHE   A CB  1 
ATOM   1061 C  CB  B PHE   A 1 127 ? 9.68419   -3.99354  -15.46594 0.265 22.98093 ? 134 PHE   A CB  1 
ATOM   1062 C  CG  A PHE   A 1 127 ? 10.08241  -3.89928  -14.03237 0.735 22.56413 ? 134 PHE   A CG  1 
ATOM   1063 C  CG  B PHE   A 1 127 ? 9.91600   -3.25665  -14.20355 0.265 23.50502 ? 134 PHE   A CG  1 
ATOM   1064 C  CD1 A PHE   A 1 127 ? 10.94875  -2.82013  -13.98286 0.735 28.17903 ? 134 PHE   A CD1 1 
ATOM   1065 C  CD1 B PHE   A 1 127 ? 10.39987  -1.96519  -14.23354 0.265 27.03776 ? 134 PHE   A CD1 1 
ATOM   1066 C  CD2 A PHE   A 1 127 ? 9.56778   -4.39052  -12.84572 0.735 24.00347 ? 134 PHE   A CD2 1 
ATOM   1067 C  CD2 B PHE   A 1 127 ? 9.49277   -3.78248  -13.00019 0.265 23.30496 ? 134 PHE   A CD2 1 
ATOM   1068 C  CE1 A PHE   A 1 127 ? 11.32544  -2.26367  -12.75892 0.735 26.09785 ? 134 PHE   A CE1 1 
ATOM   1069 C  CE1 B PHE   A 1 127 ? 10.53412  -1.24998  -13.07243 0.265 24.45172 ? 134 PHE   A CE1 1 
ATOM   1070 C  CE2 A PHE   A 1 127 ? 9.94450   -3.85185  -11.61655 0.735 23.97889 ? 134 PHE   A CE2 1 
ATOM   1071 C  CE2 B PHE   A 1 127 ? 9.64663   -3.08154  -11.83096 0.265 25.77457 ? 134 PHE   A CE2 1 
ATOM   1072 C  CZ  A PHE   A 1 127 ? 10.82072  -2.78300  -11.57620 0.735 25.94608 ? 134 PHE   A CZ  1 
ATOM   1073 C  CZ  B PHE   A 1 127 ? 10.16337  -1.81283  -11.86802 0.265 26.43754 ? 134 PHE   A CZ  1 
ATOM   1074 N  N   . GLY   A 1 128 ? 6.81431   -4.52054  -17.61873 1.000 21.15101 ? 135 GLY   A N   1 
ATOM   1075 C  CA  . GLY   A 1 128 ? 6.33361   -4.93285  -18.90543 1.000 21.11475 ? 135 GLY   A CA  1 
ATOM   1076 C  C   . GLY   A 1 128 ? 6.55350   -6.38536  -19.24144 1.000 19.58697 ? 135 GLY   A C   1 
ATOM   1077 O  O   . GLY   A 1 128 ? 6.34845   -6.75873  -20.39946 1.000 21.53234 ? 135 GLY   A O   1 
ATOM   1078 N  N   . VAL   A 1 129 ? 6.97864   -7.20363  -18.27382 1.000 17.73391 ? 136 VAL   A N   1 
ATOM   1079 C  CA  . VAL   A 1 129 ? 7.30148   -8.60682  -18.51349 1.000 14.11483 ? 136 VAL   A CA  1 
ATOM   1080 C  C   . VAL   A 1 129 ? 6.44516   -9.49861  -17.60929 1.000 15.73209 ? 136 VAL   A C   1 
ATOM   1081 O  O   . VAL   A 1 129 ? 6.82905   -10.63868 -17.30177 1.000 15.85850 ? 136 VAL   A O   1 
ATOM   1082 C  CB  . VAL   A 1 129 ? 8.81802   -8.86249  -18.32923 1.000 15.50014 ? 136 VAL   A CB  1 
ATOM   1083 C  CG1 . VAL   A 1 129 ? 9.53984   -8.17614  -19.48251 1.000 19.12883 ? 136 VAL   A CG1 1 
ATOM   1084 C  CG2 . VAL   A 1 129 ? 9.33996   -8.29573  -17.01763 1.000 16.63943 ? 136 VAL   A CG2 1 
ATOM   1085 N  N   . GLY   A 1 130 ? 5.23699   -9.02854  -17.26191 1.000 16.72734 ? 137 GLY   A N   1 
ATOM   1086 C  CA  . GLY   A 1 130 ? 4.38953   -9.80421  -16.36860 1.000 16.35852 ? 137 GLY   A CA  1 
ATOM   1087 C  C   . GLY   A 1 130 ? 3.92977   -11.13561 -16.93322 1.000 14.50845 ? 137 GLY   A C   1 
ATOM   1088 O  O   . GLY   A 1 130 ? 3.62281   -12.04113 -16.14173 1.000 15.23768 ? 137 GLY   A O   1 
ATOM   1089 N  N   . PHE   A 1 131 ? 3.87840   -11.28203 -18.26595 1.000 13.64529 ? 138 PHE   A N   1 
ATOM   1090 C  CA  . PHE   A 1 131 ? 3.55048   -12.58012 -18.84630 1.000 14.53353 ? 138 PHE   A CA  1 
ATOM   1091 C  C   . PHE   A 1 131 ? 4.39113   -13.69390 -18.22583 1.000 14.80699 ? 138 PHE   A C   1 
ATOM   1092 O  O   . PHE   A 1 131 ? 3.88477   -14.78669 -17.96444 1.000 14.32726 ? 138 PHE   A O   1 
ATOM   1093 C  CB  . PHE   A 1 131 ? 3.73039   -12.56882 -20.37923 1.000 14.86633 ? 138 PHE   A CB  1 
ATOM   1094 C  CG  . PHE   A 1 131 ? 3.72382   -13.95107 -20.97550 1.000 16.03301 ? 138 PHE   A CG  1 
ATOM   1095 C  CD1 . PHE   A 1 131 ? 2.52729   -14.60538 -21.16165 1.000 14.56877 ? 138 PHE   A CD1 1 
ATOM   1096 C  CD2 . PHE   A 1 131 ? 4.91115   -14.59622 -21.29284 1.000 16.02016 ? 138 PHE   A CD2 1 
ATOM   1097 C  CE1 . PHE   A 1 131 ? 2.47121   -15.90495 -21.66564 1.000 14.93665 ? 138 PHE   A CE1 1 
ATOM   1098 C  CE2 . PHE   A 1 131 ? 4.90761   -15.88855 -21.79818 1.000 14.97705 ? 138 PHE   A CE2 1 
ATOM   1099 C  CZ  . PHE   A 1 131 ? 3.68411   -16.55869 -21.99497 1.000 17.52728 ? 138 PHE   A CZ  1 
ATOM   1100 N  N   . TYR   A 1 132 ? 5.69682   -13.45691 -18.02465 1.000 14.09027 ? 139 TYR   A N   1 
ATOM   1101 C  CA  . TYR   A 1 132 ? 6.54425   -14.57090 -17.62092 1.000 13.61122 ? 139 TYR   A CA  1 
ATOM   1102 C  C   . TYR   A 1 132 ? 6.27481   -15.03293 -16.19346 1.000 14.31727 ? 139 TYR   A C   1 
ATOM   1103 O  O   . TYR   A 1 132 ? 6.75522   -16.10872 -15.80348 1.000 14.81422 ? 139 TYR   A O   1 
ATOM   1104 C  CB  . TYR   A 1 132 ? 8.01838   -14.18044 -17.81158 1.000 13.68754 ? 139 TYR   A CB  1 
ATOM   1105 C  CG  . TYR   A 1 132 ? 8.30003   -13.88532 -19.26539 1.000 14.91523 ? 139 TYR   A CG  1 
ATOM   1106 C  CD1 . TYR   A 1 132 ? 8.54299   -14.91376 -20.15757 1.000 15.83183 ? 139 TYR   A CD1 1 
ATOM   1107 C  CD2 . TYR   A 1 132 ? 8.21607   -12.57472 -19.76729 1.000 16.89587 ? 139 TYR   A CD2 1 
ATOM   1108 C  CE1 . TYR   A 1 132 ? 8.78636   -14.65718 -21.52815 1.000 15.49049 ? 139 TYR   A CE1 1 
ATOM   1109 C  CE2 . TYR   A 1 132 ? 8.42438   -12.30055 -21.11571 1.000 18.59529 ? 139 TYR   A CE2 1 
ATOM   1110 C  CZ  . TYR   A 1 132 ? 8.71801   -13.34814 -21.99724 1.000 17.98041 ? 139 TYR   A CZ  1 
ATOM   1111 O  OH  . TYR   A 1 132 ? 8.90968   -13.09140 -23.34015 1.000 17.11946 ? 139 TYR   A OH  1 
ATOM   1112 N  N   . SER   A 1 133 ? 5.51477   -14.26904 -15.40491 1.000 14.36681 ? 140 SER   A N   1 
ATOM   1113 C  CA  . SER   A 1 133 ? 5.08258   -14.75379 -14.09184 1.000 15.55880 ? 140 SER   A CA  1 
ATOM   1114 C  C   . SER   A 1 133 ? 4.20294   -15.98462 -14.20582 1.000 13.91572 ? 140 SER   A C   1 
ATOM   1115 O  O   . SER   A 1 133 ? 3.98608   -16.65774 -13.18694 1.000 15.10347 ? 140 SER   A O   1 
ATOM   1116 C  CB  . SER   A 1 133 ? 4.29116   -13.69286 -13.27762 1.000 16.65493 ? 140 SER   A CB  1 
ATOM   1117 O  OG  . SER   A 1 133 ? 3.04996   -13.38897 -13.92472 1.000 15.42254 ? 140 SER   A OG  1 
ATOM   1118 N  N   . ALA   A 1 134 ? 3.69626   -16.30428 -15.40436 1.000 13.65286 ? 141 ALA   A N   1 
ATOM   1119 C  CA  . ALA   A 1 134 ? 3.03360   -17.59773 -15.58646 1.000 12.59505 ? 141 ALA   A CA  1 
ATOM   1120 C  C   . ALA   A 1 134 ? 3.86551   -18.75456 -15.04868 1.000 14.23458 ? 141 ALA   A C   1 
ATOM   1121 O  O   . ALA   A 1 134 ? 3.31030   -19.75539 -14.56414 1.000 14.15163 ? 141 ALA   A O   1 
ATOM   1122 C  CB  . ALA   A 1 134 ? 2.75616   -17.82137 -17.07895 1.000 12.34983 ? 141 ALA   A CB  1 
ATOM   1123 N  N   . TYR   A 1 135 ? 5.21376   -18.66177 -15.15105 1.000 14.19427 ? 142 TYR   A N   1 
ATOM   1124 C  CA  . TYR   A 1 135 ? 6.06413   -19.77912 -14.78158 1.000 15.50771 ? 142 TYR   A CA  1 
ATOM   1125 C  C   . TYR   A 1 135 ? 6.21941   -19.90900 -13.26790 1.000 15.74287 ? 142 TYR   A C   1 
ATOM   1126 O  O   . TYR   A 1 135 ? 6.89776   -20.82303 -12.80227 1.000 17.72465 ? 142 TYR   A O   1 
ATOM   1127 C  CB  . TYR   A 1 135 ? 7.44080   -19.66094 -15.50138 1.000 14.63333 ? 142 TYR   A CB  1 
ATOM   1128 C  CG  . TYR   A 1 135 ? 7.25762   -19.95977 -16.96944 1.000 14.91590 ? 142 TYR   A CG  1 
ATOM   1129 C  CD1 . TYR   A 1 135 ? 7.24931   -21.28646 -17.43167 1.000 16.10587 ? 142 TYR   A CD1 1 
ATOM   1130 C  CD2 . TYR   A 1 135 ? 6.97906   -18.93687 -17.87121 1.000 13.52676 ? 142 TYR   A CD2 1 
ATOM   1131 C  CE1 . TYR   A 1 135 ? 7.01078   -21.58317 -18.79423 1.000 15.03825 ? 142 TYR   A CE1 1 
ATOM   1132 C  CE2 . TYR   A 1 135 ? 6.74274   -19.21234 -19.22604 1.000 14.46387 ? 142 TYR   A CE2 1 
ATOM   1133 C  CZ  . TYR   A 1 135 ? 6.74071   -20.53936 -19.67045 1.000 15.25132 ? 142 TYR   A CZ  1 
ATOM   1134 O  OH  . TYR   A 1 135 ? 6.50478   -20.78398 -21.01068 1.000 15.59221 ? 142 TYR   A OH  1 
ATOM   1135 N  N   . LEU   A 1 136 ? 5.57198   -19.02848 -12.48805 1.000 14.45473 ? 143 LEU   A N   1 
ATOM   1136 C  CA  . LEU   A 1 136 ? 5.44332   -19.26654 -11.05518 1.000 15.12050 ? 143 LEU   A CA  1 
ATOM   1137 C  C   . LEU   A 1 136 ? 4.59560   -20.49912 -10.78439 1.000 15.90606 ? 143 LEU   A C   1 
ATOM   1138 O  O   . LEU   A 1 136 ? 4.80779   -21.19106 -9.78328  1.000 17.98793 ? 143 LEU   A O   1 
ATOM   1139 C  CB  . LEU   A 1 136 ? 4.77755   -18.05367 -10.38771 1.000 16.61345 ? 143 LEU   A CB  1 
ATOM   1140 C  CG  . LEU   A 1 136 ? 5.60534   -16.74441 -10.31647 1.000 15.86277 ? 143 LEU   A CG  1 
ATOM   1141 C  CD1 . LEU   A 1 136 ? 4.72081   -15.57776 -9.84747  1.000 18.22988 ? 143 LEU   A CD1 1 
ATOM   1142 C  CD2 . LEU   A 1 136 ? 6.84936   -16.92757 -9.43243  1.000 16.11155 ? 143 LEU   A CD2 1 
ATOM   1143 N  N   . VAL   A 1 137 ? 3.63343   -20.79749 -11.67408 1.000 16.42182 ? 144 VAL   A N   1 
ATOM   1144 C  CA  . VAL   A 1 137 ? 2.65961   -21.85496 -11.39017 1.000 15.51923 ? 144 VAL   A CA  1 
ATOM   1145 C  C   . VAL   A 1 137 ? 2.60249   -22.90788 -12.48703 1.000 16.30125 ? 144 VAL   A C   1 
ATOM   1146 O  O   . VAL   A 1 137 ? 2.07565   -23.99794 -12.25718 1.000 19.30872 ? 144 VAL   A O   1 
ATOM   1147 C  CB  . VAL   A 1 137 ? 1.24403   -21.29167 -11.12389 1.000 15.64809 ? 144 VAL   A CB  1 
ATOM   1148 C  CG1 . VAL   A 1 137 ? 1.27013   -20.39712 -9.88008  1.000 17.95531 ? 144 VAL   A CG1 1 
ATOM   1149 C  CG2 . VAL   A 1 137 ? 0.67918   -20.52497 -12.31282 1.000 14.55358 ? 144 VAL   A CG2 1 
ATOM   1150 N  N   . ALA   A 1 138 ? 3.15657   -22.61903 -13.67021 1.000 15.61486 ? 145 ALA   A N   1 
ATOM   1151 C  CA  . ALA   A 1 138 ? 3.00048   -23.51340 -14.81511 1.000 15.84529 ? 145 ALA   A CA  1 
ATOM   1152 C  C   . ALA   A 1 138 ? 4.31723   -24.16459 -15.17987 1.000 16.56241 ? 145 ALA   A C   1 
ATOM   1153 O  O   . ALA   A 1 138 ? 5.34253   -23.47210 -15.28257 1.000 19.18190 ? 145 ALA   A O   1 
ATOM   1154 C  CB  . ALA   A 1 138 ? 2.46667   -22.76483 -16.03621 1.000 16.99146 ? 145 ALA   A CB  1 
ATOM   1155 N  N   . GLU   A 1 139 ? 4.27469   -25.47057 -15.44204 1.000 15.77799 ? 146 GLU   A N   1 
ATOM   1156 C  CA  . GLU   A 1 139 ? 5.44704   -26.14395 -16.00029 1.000 17.88349 ? 146 GLU   A CA  1 
ATOM   1157 C  C   . GLU   A 1 139 ? 5.56319   -25.91592 -17.49801 1.000 18.72659 ? 146 GLU   A C   1 
ATOM   1158 O  O   . GLU   A 1 139 ? 6.65524   -26.01913 -18.06044 1.000 20.05390 ? 146 GLU   A O   1 
ATOM   1159 C  CB  . GLU   A 1 139 ? 5.38732   -27.65018 -15.71902 1.000 20.37432 ? 146 GLU   A CB  1 
ATOM   1160 C  CG  . GLU   A 1 139 ? 4.13359   -28.31689 -16.12974 1.000 27.70595 ? 146 GLU   A CG  1 
ATOM   1161 C  CD  . GLU   A 1 139 ? 4.08993   -29.78124 -15.72897 1.000 40.62150 ? 146 GLU   A CD  1 
ATOM   1162 O  OE1 . GLU   A 1 139 ? 4.86100   -30.17213 -14.81483 1.000 38.06195 ? 146 GLU   A OE1 1 
ATOM   1163 O  OE2 . GLU   A 1 139 ? 3.30393   -30.53657 -16.36518 1.000 42.26032 ? 146 GLU   A OE2 1 
ATOM   1164 N  N   . LYS   A 1 140 ? 4.44556   -25.64994 -18.16524 1.000 16.36225 ? 147 LYS   A N   1 
ATOM   1165 C  CA  . LYS   A 1 140 ? 4.42247   -25.39992 -19.59587 1.000 18.17002 ? 147 LYS   A CA  1 
ATOM   1166 C  C   . LYS   A 1 140 ? 3.36744   -24.34768 -19.84279 1.000 15.86044 ? 147 LYS   A C   1 
ATOM   1167 O  O   . LYS   A 1 140 ? 2.32805   -24.34741 -19.17122 1.000 15.56331 ? 147 LYS   A O   1 
ATOM   1168 C  CB  . LYS   A 1 140 ? 4.12309   -26.68046 -20.38004 1.000 18.46622 ? 147 LYS   A CB  1 
ATOM   1169 C  CG  . LYS   A 1 140 ? 4.16809   -26.50074 -21.89697 1.000 17.48695 ? 147 LYS   A CG  1 
ATOM   1170 C  CD  . LYS   A 1 140 ? 4.05847   -27.88028 -22.54835 1.000 24.32991 ? 147 LYS   A CD  1 
ATOM   1171 C  CE  . LYS   A 1 140 ? 2.66563   -28.29315 -22.85790 1.000 29.54591 ? 147 LYS   A CE  1 
ATOM   1172 N  NZ  . LYS   A 1 140 ? 2.63745   -29.77938 -23.17101 1.000 34.54452 ? 147 LYS   A NZ  1 
ATOM   1173 N  N   . VAL   A 1 141 ? 3.63384   -23.44491 -20.79015 1.000 13.65596 ? 148 VAL   A N   1 
ATOM   1174 C  CA  . VAL   A 1 141 ? 2.62066   -22.45639 -21.15164 1.000 13.71778 ? 148 VAL   A CA  1 
ATOM   1175 C  C   . VAL   A 1 141 ? 2.42617   -22.52817 -22.65699 1.000 16.15915 ? 148 VAL   A C   1 
ATOM   1176 O  O   . VAL   A 1 141 ? 3.41416   -22.54971 -23.40845 1.000 13.95478 ? 148 VAL   A O   1 
ATOM   1177 C  CB  . VAL   A 1 141 ? 3.04180   -21.03507 -20.74358 1.000 15.43819 ? 148 VAL   A CB  1 
ATOM   1178 C  CG1 . VAL   A 1 141 ? 1.99029   -20.02571 -21.23012 1.000 15.40941 ? 148 VAL   A CG1 1 
ATOM   1179 C  CG2 . VAL   A 1 141 ? 3.27285   -20.92017 -19.20717 1.000 15.81605 ? 148 VAL   A CG2 1 
ATOM   1180 N  N   . THR   A 1 142 ? 1.16689   -22.60392 -23.09143 1.000 15.29413 ? 149 THR   A N   1 
ATOM   1181 C  CA  . THR   A 1 142 ? 0.79178   -22.57244 -24.49825 1.000 15.74818 ? 149 THR   A CA  1 
ATOM   1182 C  C   . THR   A 1 142 ? -0.01205  -21.30045 -24.74698 1.000 16.44284 ? 149 THR   A C   1 
ATOM   1183 O  O   . THR   A 1 142 ? -0.96196  -21.00483 -24.00160 1.000 17.88387 ? 149 THR   A O   1 
ATOM   1184 C  CB  . THR   A 1 142 ? -0.04563  -23.79881 -24.88958 1.000 15.63299 ? 149 THR   A CB  1 
ATOM   1185 O  OG1 . THR   A 1 142 ? 0.62054   -25.00320 -24.47871 1.000 19.12288 ? 149 THR   A OG1 1 
ATOM   1186 C  CG2 . THR   A 1 142 ? -0.25553  -23.81171 -26.40164 1.000 17.17446 ? 149 THR   A CG2 1 
ATOM   1187 N  N   . VAL   A 1 143 ? 0.36632   -20.53529 -25.76954 1.000 13.62933 ? 150 VAL   A N   1 
ATOM   1188 C  CA  . VAL   A 1 143 ? -0.32613  -19.29478 -26.11576 1.000 14.32891 ? 150 VAL   A CA  1 
ATOM   1189 C  C   . VAL   A 1 143 ? -0.89569  -19.44589 -27.52034 1.000 18.21446 ? 150 VAL   A C   1 
ATOM   1190 O  O   . VAL   A 1 143 ? -0.13537  -19.60071 -28.48630 1.000 16.50770 ? 150 VAL   A O   1 
ATOM   1191 C  CB  . VAL   A 1 143 ? 0.59644   -18.07168 -26.03686 1.000 14.24486 ? 150 VAL   A CB  1 
ATOM   1192 C  CG1 . VAL   A 1 143 ? -0.21618  -16.81672 -26.44489 1.000 17.07525 ? 150 VAL   A CG1 1 
ATOM   1193 C  CG2 . VAL   A 1 143 ? 1.20700   -17.93871 -24.61348 1.000 15.14836 ? 150 VAL   A CG2 1 
ATOM   1194 N  N   . ILE   A 1 144 ? -2.22265  -19.43293 -27.63749 1.000 14.35940 ? 151 ILE   A N   1 
ATOM   1195 C  CA  . ILE   A 1 144 ? -2.89292  -19.46174 -28.93594 1.000 14.00237 ? 151 ILE   A CA  1 
ATOM   1196 C  C   . ILE   A 1 144 ? -3.36579  -18.04607 -29.23209 1.000 16.28557 ? 151 ILE   A C   1 
ATOM   1197 O  O   . ILE   A 1 144 ? -3.97876  -17.39598 -28.35975 1.000 16.85434 ? 151 ILE   A O   1 
ATOM   1198 C  CB  . ILE   A 1 144 ? -4.11494  -20.39744 -28.94194 1.000 16.68346 ? 151 ILE   A CB  1 
ATOM   1199 C  CG1 . ILE   A 1 144 ? -3.86250  -21.73260 -28.22635 1.000 23.63560 ? 151 ILE   A CG1 1 
ATOM   1200 C  CG2 . ILE   A 1 144 ? -4.62012  -20.49129 -30.38384 1.000 18.06433 ? 151 ILE   A CG2 1 
ATOM   1201 C  CD1 . ILE   A 1 144 ? -2.94813  -22.65403 -28.95003 1.000 23.51853 ? 151 ILE   A CD1 1 
ATOM   1202 N  N   . THR   A 1 145 ? -3.09292  -17.55315 -30.44271 1.000 15.57525 ? 152 THR   A N   1 
ATOM   1203 C  CA  . THR   A 1 145 ? -3.43182  -16.14715 -30.70917 1.000 14.95858 ? 152 THR   A CA  1 
ATOM   1204 C  C   . THR   A 1 145 ? -3.85300  -15.92375 -32.14931 1.000 17.97732 ? 152 THR   A C   1 
ATOM   1205 O  O   . THR   A 1 145 ? -3.42359  -16.62789 -33.05736 1.000 17.90807 ? 152 THR   A O   1 
ATOM   1206 C  CB  . THR   A 1 145 ? -2.24937  -15.22100 -30.32121 1.000 16.92209 ? 152 THR   A CB  1 
ATOM   1207 O  OG1 . THR   A 1 145 ? -2.69836  -13.85733 -30.20409 1.000 16.69769 ? 152 THR   A OG1 1 
ATOM   1208 C  CG2 . THR   A 1 145 ? -1.06166  -15.35520 -31.27834 1.000 18.52323 ? 152 THR   A CG2 1 
ATOM   1209 N  N   . LYS   A 1 146 ? -4.72540  -14.92770 -32.33672 1.000 16.37129 ? 153 LYS   A N   1 
ATOM   1210 C  CA  . LYS   A 1 146 ? -5.21612  -14.53405 -33.65612 1.000 16.23213 ? 153 LYS   A CA  1 
ATOM   1211 C  C   . LYS   A 1 146 ? -5.31179  -13.02611 -33.67154 1.000 17.80816 ? 153 LYS   A C   1 
ATOM   1212 O  O   . LYS   A 1 146 ? -6.10764  -12.45116 -32.92134 1.000 17.11064 ? 153 LYS   A O   1 
ATOM   1213 C  CB  . LYS   A 1 146 ? -6.59052  -15.14772 -33.94737 1.000 17.84393 ? 153 LYS   A CB  1 
ATOM   1214 C  CG  . LYS   A 1 146 ? -7.20081  -14.78669 -35.34631 1.000 17.96713 ? 153 LYS   A CG  1 
ATOM   1215 C  CD  . LYS   A 1 146 ? -6.40365  -15.26446 -36.50359 1.000 22.13014 ? 153 LYS   A CD  1 
ATOM   1216 C  CE  . LYS   A 1 146 ? -7.10573  -14.92016 -37.84791 1.000 20.35000 ? 153 LYS   A CE  1 
ATOM   1217 N  NZ  . LYS   A 1 146 ? -7.11662  -13.46065 -38.14755 1.000 20.96181 ? 153 LYS   A NZ  1 
ATOM   1218 N  N   . HIS   A 1 147 ? -4.53695  -12.40934 -34.54809 1.000 18.69153 ? 154 HIS   A N   1 
ATOM   1219 C  CA  . HIS   A 1 147 ? -4.56345  -10.97562 -34.81775 1.000 17.69474 ? 154 HIS   A CA  1 
ATOM   1220 C  C   . HIS   A 1 147 ? -5.25708  -10.74137 -36.16384 1.000 20.49016 ? 154 HIS   A C   1 
ATOM   1221 O  O   . HIS   A 1 147 ? -5.16467  -11.57101 -37.07712 1.000 21.03836 ? 154 HIS   A O   1 
ATOM   1222 C  CB  . HIS   A 1 147 ? -3.11089  -10.45471 -34.84835 1.000 17.72665 ? 154 HIS   A CB  1 
ATOM   1223 C  CG  . HIS   A 1 147 ? -2.97568  -8.96193  -34.97098 1.000 18.84144 ? 154 HIS   A CG  1 
ATOM   1224 N  ND1 . HIS   A 1 147 ? -3.15384  -8.29482  -36.16093 1.000 21.77969 ? 154 HIS   A ND1 1 
ATOM   1225 C  CD2 . HIS   A 1 147 ? -2.58038  -8.02884  -34.07250 1.000 19.54609 ? 154 HIS   A CD2 1 
ATOM   1226 C  CE1 . HIS   A 1 147 ? -2.94327  -7.00519  -35.97402 1.000 22.91239 ? 154 HIS   A CE1 1 
ATOM   1227 N  NE2 . HIS   A 1 147 ? -2.57504  -6.81969  -34.72189 1.000 23.30576 ? 154 HIS   A NE2 1 
ATOM   1228 N  N   . ASN   A 1 148 ? -5.96648  -9.61435  -36.29767 1.000 19.50033 ? 155 ASN   A N   1 
ATOM   1229 C  CA  . ASN   A 1 148 ? -6.67252  -9.36074  -37.56094 1.000 19.36196 ? 155 ASN   A CA  1 
ATOM   1230 C  C   . ASN   A 1 148 ? -5.74637  -9.43963  -38.77835 1.000 18.51461 ? 155 ASN   A C   1 
ATOM   1231 O  O   . ASN   A 1 148 ? -6.20611  -9.78504  -39.88736 1.000 23.59422 ? 155 ASN   A O   1 
ATOM   1232 C  CB  . ASN   A 1 148 ? -7.37554  -7.99299  -37.52605 1.000 23.35841 ? 155 ASN   A CB  1 
ATOM   1233 C  CG  . ASN   A 1 148 ? -8.63943  -7.98926  -36.70451 1.000 22.88881 ? 155 ASN   A CG  1 
ATOM   1234 O  OD1 . ASN   A 1 148 ? -9.28957  -9.01259  -36.53238 1.000 22.72862 ? 155 ASN   A OD1 1 
ATOM   1235 N  ND2 . ASN   A 1 148 ? -9.00678  -6.82040  -36.18366 1.000 20.32342 ? 155 ASN   A ND2 1 
ATOM   1236 N  N   . ASP   A 1 149 ? -4.46252  -9.12177  -38.61640 1.000 21.88444 ? 156 ASP   A N   1 
ATOM   1237 C  CA  . ASP   A 1 149 ? -3.55651  -9.03505  -39.75531 1.000 22.77810 ? 156 ASP   A CA  1 
ATOM   1238 C  C   . ASP   A 1 149 ? -2.73691  -10.29556 -39.97643 1.000 28.32154 ? 156 ASP   A C   1 
ATOM   1239 O  O   . ASP   A 1 149 ? -1.82771  -10.27523 -40.82090 1.000 29.43656 ? 156 ASP   A O   1 
ATOM   1240 C  CB  . ASP   A 1 149 ? -2.61272  -7.84807  -39.59374 1.000 26.81359 ? 156 ASP   A CB  1 
ATOM   1241 C  CG  . ASP   A 1 149 ? -3.33858  -6.51932  -39.58841 1.000 28.92524 ? 156 ASP   A CG  1 
ATOM   1242 O  OD1 . ASP   A 1 149 ? -4.45546  -6.45043  -40.12014 1.000 29.19749 ? 156 ASP   A OD1 1 
ATOM   1243 O  OD2 . ASP   A 1 149 ? -2.77409  -5.55109  -39.04767 1.000 33.06344 ? 156 ASP   A OD2 1 
ATOM   1244 N  N   . ASP   A 1 150 ? -3.03173  -11.39496 -39.27242 1.000 23.25134 ? 157 ASP   A N   1 
ATOM   1245 C  CA  . ASP   A 1 150 ? -2.24193  -12.61394 -39.43927 1.000 19.49678 ? 157 ASP   A CA  1 
ATOM   1246 C  C   . ASP   A 1 150 ? -3.13867  -13.83443 -39.21537 1.000 24.91802 ? 157 ASP   A C   1 
ATOM   1247 O  O   . ASP   A 1 150 ? -4.34319  -13.72076 -38.95455 1.000 23.32776 ? 157 ASP   A O   1 
ATOM   1248 C  CB  . ASP   A 1 150 ? -1.04216  -12.59107 -38.47651 1.000 22.66247 ? 157 ASP   A CB  1 
ATOM   1249 C  CG  . ASP   A 1 150 ? 0.16978   -13.35487 -38.99771 1.000 24.20324 ? 157 ASP   A CG  1 
ATOM   1250 O  OD1 . ASP   A 1 150 ? 0.03378   -14.16185 -39.94414 1.000 25.42842 ? 157 ASP   A OD1 1 
ATOM   1251 O  OD2 . ASP   A 1 150 ? 1.27517   -13.12082 -38.43296 1.000 24.09861 ? 157 ASP   A OD2 1 
ATOM   1252 N  N   . GLU   A 1 151 ? -2.54465  -15.01516 -39.34708 1.000 22.73017 ? 158 GLU   A N   1 
ATOM   1253 C  CA  . GLU   A 1 151 ? -3.21758  -16.29080 -39.15404 1.000 19.92561 ? 158 GLU   A CA  1 
ATOM   1254 C  C   . GLU   A 1 151 ? -3.12880  -16.68947 -37.67736 1.000 18.39465 ? 158 GLU   A C   1 
ATOM   1255 O  O   . GLU   A 1 151 ? -2.43665  -16.05775 -36.88363 1.000 21.58439 ? 158 GLU   A O   1 
ATOM   1256 C  CB  . GLU   A 1 151 ? -2.58350  -17.36462 -40.03892 1.000 27.81369 ? 158 GLU   A CB  1 
ATOM   1257 C  CG  . GLU   A 1 151 ? -2.84475  -17.23061 -41.56250 1.000 32.45375 ? 158 GLU   A CG  1 
ATOM   1258 C  CD  . GLU   A 1 151 ? -4.23131  -16.67369 -41.93320 1.000 50.54332 ? 158 GLU   A CD  1 
ATOM   1259 O  OE1 . GLU   A 1 151 ? -4.30155  -15.81191 -42.84228 1.000 55.98543 ? 158 GLU   A OE1 1 
ATOM   1260 O  OE2 . GLU   A 1 151 ? -5.26163  -17.11506 -41.35973 1.000 57.08894 ? 158 GLU   A OE2 1 
ATOM   1261 N  N   . GLN   A 1 152 ? -3.83149  -17.74912 -37.31054 1.000 20.59949 ? 159 GLN   A N   1 
ATOM   1262 C  CA  . GLN   A 1 152 ? -3.81191  -18.20816 -35.91789 1.000 17.98582 ? 159 GLN   A CA  1 
ATOM   1263 C  C   . GLN   A 1 152 ? -2.55502  -19.03548 -35.65780 1.000 19.66345 ? 159 GLN   A C   1 
ATOM   1264 O  O   . GLN   A 1 152 ? -2.25815  -19.96472 -36.41264 1.000 20.31001 ? 159 GLN   A O   1 
ATOM   1265 C  CB  . GLN   A 1 152 ? -5.05746  -19.04831 -35.63346 1.000 21.50415 ? 159 GLN   A CB  1 
ATOM   1266 C  CG  . GLN   A 1 152 ? -5.29043  -19.39977 -34.14505 1.000 19.46971 ? 159 GLN   A CG  1 
ATOM   1267 C  CD  . GLN   A 1 152 ? -6.72865  -19.84654 -33.87982 1.000 23.22992 ? 159 GLN   A CD  1 
ATOM   1268 O  OE1 . GLN   A 1 152 ? -7.66654  -19.14401 -34.23959 1.000 26.57075 ? 159 GLN   A OE1 1 
ATOM   1269 N  NE2 . GLN   A 1 152 ? -6.89881  -21.01550 -33.28697 1.000 22.88924 ? 159 GLN   A NE2 1 
ATOM   1270 N  N   A TYR   A 1 153 ? -1.83759  -18.71206 -34.57777 0.500 16.80951 ? 160 TYR   A N   1 
ATOM   1271 N  N   B TYR   A 1 153 ? -1.83759  -18.71206 -34.57777 0.500 16.80951 ? 160 TYR   A N   1 
ATOM   1272 C  CA  A TYR   A 1 153 ? -0.58749  -19.36959 -34.24009 0.500 18.80587 ? 160 TYR   A CA  1 
ATOM   1273 C  CA  B TYR   A 1 153 ? -0.58749  -19.36959 -34.24009 0.500 18.80587 ? 160 TYR   A CA  1 
ATOM   1274 C  C   A TYR   A 1 153 ? -0.65138  -19.90803 -32.81816 0.500 18.79656 ? 160 TYR   A C   1 
ATOM   1275 C  C   B TYR   A 1 153 ? -0.65138  -19.90803 -32.81816 0.500 18.79656 ? 160 TYR   A C   1 
ATOM   1276 O  O   A TYR   A 1 153 ? -1.40061  -19.39689 -31.97676 0.500 17.51576 ? 160 TYR   A O   1 
ATOM   1277 O  O   B TYR   A 1 153 ? -1.40061  -19.39689 -31.97676 0.500 17.51576 ? 160 TYR   A O   1 
ATOM   1278 C  CB  A TYR   A 1 153 ? 0.57731   -18.39005 -34.36297 0.500 16.74265 ? 160 TYR   A CB  1 
ATOM   1279 C  CB  B TYR   A 1 153 ? 0.57731   -18.39005 -34.36297 0.500 16.74265 ? 160 TYR   A CB  1 
ATOM   1280 C  CG  A TYR   A 1 153 ? 0.99620   -18.18907 -35.78615 0.500 21.60580 ? 160 TYR   A CG  1 
ATOM   1281 C  CG  B TYR   A 1 153 ? 0.99620   -18.18907 -35.78615 0.500 21.60580 ? 160 TYR   A CG  1 
ATOM   1282 C  CD1 A TYR   A 1 153 ? 1.86005   -19.08789 -36.38419 0.500 21.38458 ? 160 TYR   A CD1 1 
ATOM   1283 C  CD1 B TYR   A 1 153 ? 1.86005   -19.08789 -36.38419 0.500 21.38458 ? 160 TYR   A CD1 1 
ATOM   1284 C  CD2 A TYR   A 1 153 ? 0.50668   -17.12984 -36.54175 0.500 22.84100 ? 160 TYR   A CD2 1 
ATOM   1285 C  CD2 B TYR   A 1 153 ? 0.50668   -17.12984 -36.54175 0.500 22.84100 ? 160 TYR   A CD2 1 
ATOM   1286 C  CE1 A TYR   A 1 153 ? 2.25644   -18.94194 -37.68124 0.500 24.52680 ? 160 TYR   A CE1 1 
ATOM   1287 C  CE1 B TYR   A 1 153 ? 2.25644   -18.94194 -37.68124 0.500 24.52680 ? 160 TYR   A CE1 1 
ATOM   1288 C  CE2 A TYR   A 1 153 ? 0.89465   -16.98051 -37.87517 0.500 24.33576 ? 160 TYR   A CE2 1 
ATOM   1289 C  CE2 B TYR   A 1 153 ? 0.89465   -16.98051 -37.87517 0.500 24.33576 ? 160 TYR   A CE2 1 
ATOM   1290 C  CZ  A TYR   A 1 153 ? 1.77320   -17.90178 -38.42415 0.500 26.98575 ? 160 TYR   A CZ  1 
ATOM   1291 C  CZ  B TYR   A 1 153 ? 1.77320   -17.90178 -38.42415 0.500 26.98575 ? 160 TYR   A CZ  1 
ATOM   1292 O  OH  A TYR   A 1 153 ? 2.21176   -17.81883 -39.73355 0.500 32.32179 ? 160 TYR   A OH  1 
ATOM   1293 O  OH  B TYR   A 1 153 ? 2.21176   -17.81883 -39.73355 0.500 32.32179 ? 160 TYR   A OH  1 
ATOM   1294 N  N   . ALA   A 1 154 ? 0.17656   -20.91985 -32.54548 1.000 16.86123 ? 161 ALA   A N   1 
ATOM   1295 C  CA  . ALA   A 1 154 ? 0.39101   -21.42594 -31.18954 1.000 16.97289 ? 161 ALA   A CA  1 
ATOM   1296 C  C   . ALA   A 1 154 ? 1.86719   -21.27004 -30.82875 1.000 16.91280 ? 161 ALA   A C   1 
ATOM   1297 O  O   . ALA   A 1 154 ? 2.73740   -21.75936 -31.56481 1.000 17.75052 ? 161 ALA   A O   1 
ATOM   1298 C  CB  . ALA   A 1 154 ? -0.01076  -22.90033 -31.07255 1.000 20.30042 ? 161 ALA   A CB  1 
ATOM   1299 N  N   . TRP   A 1 155 ? 2.13409   -20.60160 -29.71130 1.000 14.96817 ? 162 TRP   A N   1 
ATOM   1300 C  CA  . TRP   A 1 155 ? 3.46467   -20.49937 -29.11279 1.000 15.02407 ? 162 TRP   A CA  1 
ATOM   1301 C  C   . TRP   A 1 155 ? 3.50061   -21.43415 -27.92164 1.000 16.25431 ? 162 TRP   A C   1 
ATOM   1302 O  O   . TRP   A 1 155 ? 2.48439   -21.62210 -27.24774 1.000 15.32338 ? 162 TRP   A O   1 
ATOM   1303 C  CB  . TRP   A 1 155 ? 3.68930   -19.04013 -28.67683 1.000 14.96976 ? 162 TRP   A CB  1 
ATOM   1304 C  CG  . TRP   A 1 155 ? 4.93409   -18.68644 -27.88786 1.000 14.15213 ? 162 TRP   A CG  1 
ATOM   1305 C  CD1 . TRP   A 1 155 ? 5.96962   -17.92959 -28.35778 1.000 14.23239 ? 162 TRP   A CD1 1 
ATOM   1306 C  CD2 . TRP   A 1 155 ? 5.18672   -18.87543 -26.46904 1.000 13.55475 ? 162 TRP   A CD2 1 
ATOM   1307 N  NE1 . TRP   A 1 155 ? 6.88363   -17.71446 -27.36096 1.000 14.97286 ? 162 TRP   A NE1 1 
ATOM   1308 C  CE2 . TRP   A 1 155 ? 6.41252   -18.24916 -26.18639 1.000 14.23288 ? 162 TRP   A CE2 1 
ATOM   1309 C  CE3 . TRP   A 1 155 ? 4.48858   -19.49459 -25.41446 1.000 14.28609 ? 162 TRP   A CE3 1 
ATOM   1310 C  CZ2 . TRP   A 1 155 ? 6.99658   -18.27577 -24.90382 1.000 14.49809 ? 162 TRP   A CZ2 1 
ATOM   1311 C  CZ3 . TRP   A 1 155 ? 5.07427   -19.50236 -24.12400 1.000 13.41018 ? 162 TRP   A CZ3 1 
ATOM   1312 C  CH2 . TRP   A 1 155 ? 6.31725   -18.89123 -23.89651 1.000 16.45970 ? 162 TRP   A CH2 1 
ATOM   1313 N  N   . GLU   A 1 156 ? 4.66612   -22.03878 -27.65018 1.000 13.36145 ? 163 GLU   A N   1 
ATOM   1314 C  CA  . GLU   A 1 156 ? 4.70253   -22.89680 -26.47776 1.000 14.83352 ? 163 GLU   A CA  1 
ATOM   1315 C  C   . GLU   A 1 156 ? 6.09742   -22.94534 -25.89360 1.000 15.24582 ? 163 GLU   A C   1 
ATOM   1316 O  O   . GLU   A 1 156 ? 7.08906   -22.94223 -26.64595 1.000 15.33879 ? 163 GLU   A O   1 
ATOM   1317 C  CB  . GLU   A 1 156 ? 4.22051   -24.30343 -26.84617 1.000 18.69505 ? 163 GLU   A CB  1 
ATOM   1318 C  CG  . GLU   A 1 156 ? 4.03322   -25.25534 -25.69053 1.000 20.50831 ? 163 GLU   A CG  1 
ATOM   1319 C  CD  . GLU   A 1 156 ? 3.29128   -26.50184 -26.15928 1.000 28.00622 ? 163 GLU   A CD  1 
ATOM   1320 O  OE1 . GLU   A 1 156 ? 3.95699   -27.34715 -26.81444 1.000 28.61177 ? 163 GLU   A OE1 1 
ATOM   1321 O  OE2 . GLU   A 1 156 ? 2.04320   -26.62544 -25.92444 1.000 26.26268 ? 163 GLU   A OE2 1 
ATOM   1322 N  N   . SER   A 1 157 ? 6.18062   -23.00388 -24.55348 1.000 15.44683 ? 164 SER   A N   1 
ATOM   1323 C  CA  . SER   A 1 157 ? 7.49168   -23.17235 -23.91654 1.000 14.16794 ? 164 SER   A CA  1 
ATOM   1324 C  C   . SER   A 1 157 ? 7.35490   -23.85263 -22.55742 1.000 14.54740 ? 164 SER   A C   1 
ATOM   1325 O  O   . SER   A 1 157 ? 6.43336   -23.54527 -21.76987 1.000 14.70005 ? 164 SER   A O   1 
ATOM   1326 C  CB  . SER   A 1 157 ? 8.24960   -21.85207 -23.74173 1.000 15.55810 ? 164 SER   A CB  1 
ATOM   1327 O  OG  . SER   A 1 157 ? 9.54403   -22.11895 -23.17255 1.000 14.98664 ? 164 SER   A OG  1 
ATOM   1328 N  N   . SER   A 1 158 ? 8.27934   -24.77983 -22.29587 1.000 16.05380 ? 165 SER   A N   1 
ATOM   1329 C  CA  . SER   A 1 158 ? 8.49019   -25.34370 -20.96283 1.000 17.13072 ? 165 SER   A CA  1 
ATOM   1330 C  C   . SER   A 1 158 ? 9.75538   -24.77779 -20.33484 1.000 19.42581 ? 165 SER   A C   1 
ATOM   1331 O  O   . SER   A 1 158 ? 10.36645  -25.40976 -19.45603 1.000 21.39275 ? 165 SER   A O   1 
ATOM   1332 C  CB  . SER   A 1 158 ? 8.56319   -26.87136 -21.03700 1.000 16.91044 ? 165 SER   A CB  1 
ATOM   1333 O  OG  . SER   A 1 158 ? 7.31686   -27.40986 -21.50567 1.000 21.36816 ? 165 SER   A OG  1 
ATOM   1334 N  N   . ALA   A 1 159 ? 10.13847  -23.57278 -20.76125 1.000 16.21537 ? 166 ALA   A N   1 
ATOM   1335 C  CA  . ALA   A 1 159 ? 11.36358  -22.88825 -20.33009 1.000 17.76810 ? 166 ALA   A CA  1 
ATOM   1336 C  C   . ALA   A 1 159 ? 12.54793  -23.71705 -20.83191 1.000 17.92771 ? 166 ALA   A C   1 
ATOM   1337 O  O   . ALA   A 1 159 ? 12.47309  -24.22452 -21.95068 1.000 22.18818 ? 166 ALA   A O   1 
ATOM   1338 C  CB  . ALA   A 1 159 ? 11.34422  -22.62869 -18.82317 1.000 22.16907 ? 166 ALA   A CB  1 
ATOM   1339 N  N   . GLY   A 1 160 ? 13.63157  -23.86084 -20.08256 1.000 20.83216 ? 167 GLY   A N   1 
ATOM   1340 C  CA  . GLY   A 1 160 ? 14.71591  -24.61483 -20.69227 1.000 21.48895 ? 167 GLY   A CA  1 
ATOM   1341 C  C   . GLY   A 1 160 ? 15.37716  -23.95242 -21.88906 1.000 21.98149 ? 167 GLY   A C   1 
ATOM   1342 O  O   . GLY   A 1 160 ? 16.16801  -24.60398 -22.59425 1.000 24.71863 ? 167 GLY   A O   1 
ATOM   1343 N  N   . GLY   A 1 161 ? 15.11210  -22.66980 -22.13167 1.000 17.55048 ? 168 GLY   A N   1 
ATOM   1344 C  CA  . GLY   A 1 161 ? 15.89159  -21.93652 -23.10473 1.000 16.97860 ? 168 GLY   A CA  1 
ATOM   1345 C  C   . GLY   A 1 161 ? 15.27775  -21.81742 -24.48205 1.000 17.04559 ? 168 GLY   A C   1 
ATOM   1346 O  O   . GLY   A 1 161 ? 15.86137  -21.13034 -25.34006 1.000 17.66708 ? 168 GLY   A O   1 
ATOM   1347 N  N   . SER   A 1 162 ? 14.12923  -22.44844 -24.73453 1.000 16.04197 ? 169 SER   A N   1 
ATOM   1348 C  CA  . SER   A 1 162 ? 13.62035  -22.49753 -26.09897 1.000 14.57935 ? 169 SER   A CA  1 
ATOM   1349 C  C   . SER   A 1 162 ? 12.09674  -22.38911 -26.07488 1.000 16.52575 ? 169 SER   A C   1 
ATOM   1350 O  O   . SER   A 1 162 ? 11.43531  -22.68395 -25.05948 1.000 17.38621 ? 169 SER   A O   1 
ATOM   1351 C  CB  . SER   A 1 162 ? 14.02895  -23.78264 -26.85641 1.000 17.56153 ? 169 SER   A CB  1 
ATOM   1352 O  OG  . SER   A 1 162 ? 13.37128  -24.94288 -26.32956 1.000 18.37328 ? 169 SER   A OG  1 
ATOM   1353 N  N   . PHE   A 1 163 ? 11.54885  -21.95024 -27.21041 1.000 15.83153 ? 170 PHE   A N   1 
ATOM   1354 C  CA  . PHE   A 1 163 ? 10.10245  -21.90355 -27.41164 1.000 13.72350 ? 170 PHE   A CA  1 
ATOM   1355 C  C   . PHE   A 1 163 ? 9.81367   -22.37181 -28.82923 1.000 16.49832 ? 170 PHE   A C   1 
ATOM   1356 O  O   . PHE   A 1 163 ? 10.69850  -22.37760 -29.67763 1.000 16.64923 ? 170 PHE   A O   1 
ATOM   1357 C  CB  . PHE   A 1 163 ? 9.47996   -20.49541 -27.17186 1.000 14.99372 ? 170 PHE   A CB  1 
ATOM   1358 C  CG  . PHE   A 1 163 ? 9.97889   -19.39443 -28.09902 1.000 13.89392 ? 170 PHE   A CG  1 
ATOM   1359 C  CD1 . PHE   A 1 163 ? 11.11288  -18.66314 -27.76156 1.000 14.94213 ? 170 PHE   A CD1 1 
ATOM   1360 C  CD2 . PHE   A 1 163 ? 9.30227   -19.04868 -29.25508 1.000 14.86304 ? 170 PHE   A CD2 1 
ATOM   1361 C  CE1 . PHE   A 1 163 ? 11.55100  -17.61920 -28.57104 1.000 16.84345 ? 170 PHE   A CE1 1 
ATOM   1362 C  CE2 . PHE   A 1 163 ? 9.74090   -18.04161 -30.06210 1.000 14.51189 ? 170 PHE   A CE2 1 
ATOM   1363 C  CZ  . PHE   A 1 163 ? 10.86575  -17.29266 -29.71079 1.000 16.38174 ? 170 PHE   A CZ  1 
ATOM   1364 N  N   . THR   A 1 164 ? 8.58392   -22.80997 -29.07039 1.000 15.17195 ? 171 THR   A N   1 
ATOM   1365 C  CA  . THR   A 1 164 ? 8.16382   -23.20384 -30.41902 1.000 15.06138 ? 171 THR   A CA  1 
ATOM   1366 C  C   . THR   A 1 164 ? 7.03144   -22.32230 -30.90593 1.000 14.78424 ? 171 THR   A C   1 
ATOM   1367 O  O   . THR   A 1 164 ? 6.25911   -21.79137 -30.10716 1.000 16.52211 ? 171 THR   A O   1 
ATOM   1368 C  CB  . THR   A 1 164 ? 7.76065   -24.68554 -30.48607 1.000 18.10399 ? 171 THR   A CB  1 
ATOM   1369 O  OG1 . THR   A 1 164 ? 6.62293   -24.92378 -29.66762 1.000 18.00968 ? 171 THR   A OG1 1 
ATOM   1370 C  CG2 . THR   A 1 164 ? 8.91559   -25.62134 -30.09467 1.000 18.21015 ? 171 THR   A CG2 1 
ATOM   1371 N  N   . VAL   A 1 165 ? 6.96109   -22.17849 -32.22739 1.000 16.57697 ? 172 VAL   A N   1 
ATOM   1372 C  CA  . VAL   A 1 165 ? 5.83070   -21.53187 -32.88603 1.000 18.62028 ? 172 VAL   A CA  1 
ATOM   1373 C  C   . VAL   A 1 165 ? 5.36733   -22.42410 -34.02144 1.000 19.46815 ? 172 VAL   A C   1 
ATOM   1374 O  O   . VAL   A 1 165 ? 6.18135   -22.91527 -34.80700 1.000 17.69289 ? 172 VAL   A O   1 
ATOM   1375 C  CB  . VAL   A 1 165 ? 6.18371   -20.12842 -33.40542 1.000 16.80656 ? 172 VAL   A CB  1 
ATOM   1376 C  CG1 . VAL   A 1 165 ? 4.97791   -19.49288 -34.13872 1.000 18.32975 ? 172 VAL   A CG1 1 
ATOM   1377 C  CG2 . VAL   A 1 165 ? 6.60103   -19.22251 -32.26209 1.000 16.66627 ? 172 VAL   A CG2 1 
ATOM   1378 N  N   . ARG   A 1 166 ? 4.05437   -22.58891 -34.13805 1.000 17.55856 ? 173 ARG   A N   1 
ATOM   1379 C  CA  . ARG   A 1 166 ? 3.48367   -23.32532 -35.25248 1.000 18.81195 ? 173 ARG   A CA  1 
ATOM   1380 C  C   . ARG   A 1 166 ? 2.14685   -22.71646 -35.62763 1.000 19.30253 ? 173 ARG   A C   1 
ATOM   1381 O  O   . ARG   A 1 166 ? 1.51100   -22.05038 -34.80488 1.000 18.15532 ? 173 ARG   A O   1 
ATOM   1382 C  CB  . ARG   A 1 166 ? 3.34821   -24.79581 -34.88788 1.000 22.83687 ? 173 ARG   A CB  1 
ATOM   1383 C  CG  . ARG   A 1 166 ? 2.24327   -25.07931 -33.88744 1.000 23.56831 ? 173 ARG   A CG  1 
ATOM   1384 C  CD  . ARG   A 1 166 ? 2.39465   -26.45685 -33.25312 1.000 31.94485 ? 173 ARG   A CD  1 
ATOM   1385 N  NE  . ARG   A 1 166 ? 3.52240   -26.49595 -32.32481 1.000 33.45368 ? 173 ARG   A NE  1 
ATOM   1386 C  CZ  . ARG   A 1 166 ? 4.04978   -27.61018 -31.83145 1.000 38.34364 ? 173 ARG   A CZ  1 
ATOM   1387 N  NH1 . ARG   A 1 166 ? 3.59182   -28.80454 -32.17801 1.000 36.01899 ? 173 ARG   A NH1 1 
ATOM   1388 N  NH2 . ARG   A 1 166 ? 5.06675   -27.52360 -30.97356 1.000 35.10205 ? 173 ARG   A NH2 1 
ATOM   1389 N  N   . THR   A 1 167 ? 1.72690   -22.92628 -36.88780 1.000 20.49312 ? 174 THR   A N   1 
ATOM   1390 C  CA  . THR   A 1 167 ? 0.35386   -22.57333 -37.22576 1.000 20.78836 ? 174 THR   A CA  1 
ATOM   1391 C  C   . THR   A 1 167 ? -0.58772  -23.46944 -36.44772 1.000 24.21976 ? 174 THR   A C   1 
ATOM   1392 O  O   . THR   A 1 167 ? -0.32338  -24.65937 -36.25778 1.000 30.22159 ? 174 THR   A O   1 
ATOM   1393 C  CB  . THR   A 1 167 ? 0.11131   -22.69750 -38.72616 1.000 27.25314 ? 174 THR   A CB  1 
ATOM   1394 O  OG1 . THR   A 1 167 ? 1.08234   -21.89925 -39.41026 1.000 28.19151 ? 174 THR   A OG1 1 
ATOM   1395 C  CG2 . THR   A 1 167 ? -1.28854  -22.22632 -39.07954 1.000 32.85140 ? 174 THR   A CG2 1 
ATOM   1396 N  N   . ASP   A 1 168 ? -1.67483  -22.88920 -35.94515 1.000 20.92374 ? 175 ASP   A N   1 
ATOM   1397 C  CA  . ASP   A 1 168 ? -2.58563  -23.63724 -35.09700 1.000 23.26543 ? 175 ASP   A CA  1 
ATOM   1398 C  C   . ASP   A 1 168 ? -3.72092  -24.17648 -35.95060 1.000 33.32747 ? 175 ASP   A C   1 
ATOM   1399 O  O   . ASP   A 1 168 ? -4.40600  -23.41137 -36.62818 1.000 37.71357 ? 175 ASP   A O   1 
ATOM   1400 C  CB  . ASP   A 1 168 ? -3.11661  -22.76304 -33.97430 1.000 23.06194 ? 175 ASP   A CB  1 
ATOM   1401 C  CG  . ASP   A 1 168 ? -3.93971  -23.53246 -32.98080 1.000 36.92499 ? 175 ASP   A CG  1 
ATOM   1402 O  OD1 . ASP   A 1 168 ? -3.52150  -24.64153 -32.57348 1.000 39.99704 ? 175 ASP   A OD1 1 
ATOM   1403 O  OD2 . ASP   A 1 168 ? -5.01187  -23.01541 -32.59315 1.000 29.84412 ? 175 ASP   A OD2 1 
ATOM   1404 N  N   . THR   A 1 169 ? -3.89068  -25.48569 -35.92729 1.000 39.52418 ? 176 THR   A N   1 
ATOM   1405 C  CA  . THR   A 1 169 ? -5.00749  -26.15636 -36.57349 1.000 47.98107 ? 176 THR   A CA  1 
ATOM   1406 C  C   . THR   A 1 169 ? -6.17737  -26.37787 -35.62638 1.000 47.18621 ? 176 THR   A C   1 
ATOM   1407 O  O   . THR   A 1 169 ? -7.18581  -26.96419 -36.03601 1.000 49.25666 ? 176 THR   A O   1 
ATOM   1408 C  CB  . THR   A 1 169 ? -4.53884  -27.50244 -37.14152 1.000 47.93670 ? 176 THR   A CB  1 
ATOM   1409 O  OG1 . THR   A 1 169 ? -3.70765  -28.15926 -36.16607 1.000 52.98558 ? 176 THR   A OG1 1 
ATOM   1410 C  CG2 . THR   A 1 169 ? -3.75121  -27.27377 -38.42253 1.000 43.88334 ? 176 THR   A CG2 1 
ATOM   1411 N  N   . GLY   A 1 170 ? -6.05854  -25.93606 -34.37781 1.000 46.04185 ? 177 GLY   A N   1 
ATOM   1412 C  CA  . GLY   A 1 170 ? -7.10757  -26.09411 -33.39521 1.000 46.29221 ? 177 GLY   A CA  1 
ATOM   1413 C  C   . GLY   A 1 170 ? -8.35210  -25.26872 -33.71676 1.000 36.32068 ? 177 GLY   A C   1 
ATOM   1414 O  O   . GLY   A 1 170 ? -8.52924  -24.70658 -34.79855 1.000 36.04142 ? 177 GLY   A O   1 
ATOM   1415 N  N   . GLU   A 1 171 ? -9.23127  -25.21299 -32.72787 1.000 36.04501 ? 178 GLU   A N   1 
ATOM   1416 C  CA  . GLU   A 1 171 ? -10.50215 -24.51383 -32.84738 1.000 31.92268 ? 178 GLU   A CA  1 
ATOM   1417 C  C   . GLU   A 1 171 ? -10.24439 -23.05126 -33.19728 1.000 32.07957 ? 178 GLU   A C   1 
ATOM   1418 O  O   . GLU   A 1 171 ? -9.51698  -22.37303 -32.45976 1.000 24.47559 ? 178 GLU   A O   1 
ATOM   1419 C  CB  . GLU   A 1 171 ? -11.24049 -24.63082 -31.51485 1.000 32.87144 ? 178 GLU   A CB  1 
ATOM   1420 C  CG  . GLU   A 1 171 ? -12.74185 -24.39081 -31.50360 1.000 36.69178 ? 178 GLU   A CG  1 
ATOM   1421 C  CD  . GLU   A 1 171 ? -13.49349 -25.28790 -32.47737 1.000 33.70887 ? 178 GLU   A CD  1 
ATOM   1422 O  OE1 . GLU   A 1 171 ? -14.08928 -24.76197 -33.43045 1.000 41.42104 ? 178 GLU   A OE1 1 
ATOM   1423 O  OE2 . GLU   A 1 171 ? -13.42342 -26.52086 -32.32319 1.000 38.77060 ? 178 GLU   A OE2 1 
ATOM   1424 N  N   . PRO   A 1 172 ? -10.79475 -22.53476 -34.29719 1.000 31.85547 ? 179 PRO   A N   1 
ATOM   1425 C  CA  . PRO   A 1 172 ? -10.55601 -21.12880 -34.65673 1.000 29.43535 ? 179 PRO   A CA  1 
ATOM   1426 C  C   . PRO   A 1 172 ? -11.05017 -20.17622 -33.56970 1.000 29.75491 ? 179 PRO   A C   1 
ATOM   1427 O  O   . PRO   A 1 172 ? -12.09052 -20.40612 -32.94179 1.000 37.26312 ? 179 PRO   A O   1 
ATOM   1428 C  CB  . PRO   A 1 172 ? -11.35931 -20.95305 -35.94925 1.000 37.09096 ? 179 PRO   A CB  1 
ATOM   1429 C  CG  . PRO   A 1 172 ? -11.39270 -22.33591 -36.56162 1.000 39.54357 ? 179 PRO   A CG  1 
ATOM   1430 C  CD  . PRO   A 1 172 ? -11.47154 -23.28498 -35.37413 1.000 37.40631 ? 179 PRO   A CD  1 
ATOM   1431 N  N   . MET   A 1 173 ? -10.32808 -19.06047 -33.39091 1.000 25.42279 ? 180 MET   A N   1 
ATOM   1432 C  CA  . MET   A 1 173 ? -10.57219 -18.13519 -32.28736 1.000 23.64512 ? 180 MET   A CA  1 
ATOM   1433 C  C   . MET   A 1 173 ? -11.25049 -16.81832 -32.64219 1.000 31.13047 ? 180 MET   A C   1 
ATOM   1434 O  O   . MET   A 1 173 ? -11.66601 -16.09673 -31.73032 1.000 33.80168 ? 180 MET   A O   1 
ATOM   1435 C  CB  . MET   A 1 173 ? -9.24406  -17.76956 -31.62973 1.000 26.76249 ? 180 MET   A CB  1 
ATOM   1436 C  CG  . MET   A 1 173 ? -8.71237  -18.79114 -30.71362 1.000 37.67292 ? 180 MET   A CG  1 
ATOM   1437 S  SD  . MET   A 1 173 ? -7.16039  -18.02875 -30.25606 1.000 36.85018 ? 180 MET   A SD  1 
ATOM   1438 C  CE  . MET   A 1 173 ? -7.71665  -16.69873 -29.22218 1.000 26.30129 ? 180 MET   A CE  1 
ATOM   1439 N  N   . GLY   A 1 174 ? -11.28083 -16.42951 -33.89324 1.000 27.34998 ? 181 GLY   A N   1 
ATOM   1440 C  CA  . GLY   A 1 174 ? -11.87654 -15.13886 -34.20107 1.000 24.04461 ? 181 GLY   A CA  1 
ATOM   1441 C  C   . GLY   A 1 174 ? -10.84417 -14.03530 -34.13380 1.000 21.98623 ? 181 GLY   A C   1 
ATOM   1442 O  O   . GLY   A 1 174 ? -10.38704 -13.51062 -35.15987 1.000 22.09586 ? 181 GLY   A O   1 
ATOM   1443 N  N   . ARG   A 1 175 ? -10.49436 -13.68884 -32.89370 1.000 16.28783 ? 182 ARG   A N   1 
ATOM   1444 C  CA  . ARG   A 1 175 ? -9.50850  -12.66904 -32.56369 1.000 17.81323 ? 182 ARG   A CA  1 
ATOM   1445 C  C   . ARG   A 1 175 ? -9.22070  -12.74843 -31.07727 1.000 18.09638 ? 182 ARG   A C   1 
ATOM   1446 O  O   . ARG   A 1 175 ? -10.15870 -12.84376 -30.27864 1.000 18.39277 ? 182 ARG   A O   1 
ATOM   1447 C  CB  . ARG   A 1 175 ? -10.01204 -11.26208 -32.88671 1.000 17.31639 ? 182 ARG   A CB  1 
ATOM   1448 C  CG  . ARG   A 1 175 ? -8.90886  -10.18941 -32.77051 1.000 16.67348 ? 182 ARG   A CG  1 
ATOM   1449 C  CD  . ARG   A 1 175 ? -9.50944  -8.75914  -32.70078 1.000 14.80286 ? 182 ARG   A CD  1 
ATOM   1450 N  NE  . ARG   A 1 175 ? -10.39437 -8.62699  -31.53503 1.000 17.52301 ? 182 ARG   A NE  1 
ATOM   1451 C  CZ  . ARG   A 1 175 ? -11.72216 -8.52977  -31.61362 1.000 17.73175 ? 182 ARG   A CZ  1 
ATOM   1452 N  NH1 . ARG   A 1 175 ? -12.34667 -8.51472  -32.77809 1.000 17.59999 ? 182 ARG   A NH1 1 
ATOM   1453 N  NH2 . ARG   A 1 175 ? -12.44857 -8.47075  -30.49300 1.000 17.58572 ? 182 ARG   A NH2 1 
ATOM   1454 N  N   . GLY   A 1 176 ? -7.94596  -12.63825 -30.71179 1.000 16.02845 ? 183 GLY   A N   1 
ATOM   1455 C  CA  . GLY   A 1 176 ? -7.62427  -12.53224 -29.30074 1.000 14.96606 ? 183 GLY   A CA  1 
ATOM   1456 C  C   . GLY   A 1 176 ? -6.49264  -13.46861 -28.94288 1.000 16.72119 ? 183 GLY   A C   1 
ATOM   1457 O  O   . GLY   A 1 176 ? -5.73373  -13.92260 -29.80682 1.000 16.63021 ? 183 GLY   A O   1 
ATOM   1458 N  N   . THR   A 1 177 ? -6.37245  -13.73269 -27.64319 1.000 14.53421 ? 184 THR   A N   1 
ATOM   1459 C  CA  . THR   A 1 177 ? -5.29648  -14.58895 -27.14310 1.000 14.11578 ? 184 THR   A CA  1 
ATOM   1460 C  C   . THR   A 1 177 ? -5.81368  -15.53224 -26.08027 1.000 19.33431 ? 184 THR   A C   1 
ATOM   1461 O  O   . THR   A 1 177 ? -6.64212  -15.13480 -25.23924 1.000 16.58295 ? 184 THR   A O   1 
ATOM   1462 C  CB  . THR   A 1 177 ? -4.16564  -13.73320 -26.56083 1.000 17.32600 ? 184 THR   A CB  1 
ATOM   1463 O  OG1 . THR   A 1 177 ? -3.63187  -12.87005 -27.58288 1.000 19.00903 ? 184 THR   A OG1 1 
ATOM   1464 C  CG2 . THR   A 1 177 ? -3.05480  -14.54641 -25.87396 1.000 17.38934 ? 184 THR   A CG2 1 
ATOM   1465 N  N   . LYS   A 1 178 ? -5.28156  -16.75712 -26.09150 1.000 15.53954 ? 185 LYS   A N   1 
ATOM   1466 C  CA  . LYS   A 1 178 ? -5.62558  -17.75659 -25.08475 1.000 15.86819 ? 185 LYS   A CA  1 
ATOM   1467 C  C   . LYS   A 1 178 ? -4.31774  -18.18439 -24.43708 1.000 18.93483 ? 185 LYS   A C   1 
ATOM   1468 O  O   . LYS   A 1 178 ? -3.44328  -18.67592 -25.14495 1.000 18.25958 ? 185 LYS   A O   1 
ATOM   1469 C  CB  . LYS   A 1 178 ? -6.26366  -18.96365 -25.77728 1.000 22.02903 ? 185 LYS   A CB  1 
ATOM   1470 C  CG  . LYS   A 1 178 ? -7.69320  -19.01432 -25.56417 1.000 42.52903 ? 185 LYS   A CG  1 
ATOM   1471 C  CD  . LYS   A 1 178 ? -8.43498  -19.84647 -26.60955 1.000 37.69088 ? 185 LYS   A CD  1 
ATOM   1472 C  CE  . LYS   A 1 178 ? -7.63876  -21.05495 -27.00750 1.000 35.74910 ? 185 LYS   A CE  1 
ATOM   1473 N  NZ  . LYS   A 1 178 ? -8.53134  -21.88916 -27.89966 1.000 43.16885 ? 185 LYS   A NZ  1 
ATOM   1474 N  N   . VAL   A 1 179 ? -4.17015  -18.00350 -23.11669 1.000 14.60996 ? 186 VAL   A N   1 
ATOM   1475 C  CA  . VAL   A 1 179 ? -2.97575  -18.47680 -22.40643 1.000 13.55489 ? 186 VAL   A CA  1 
ATOM   1476 C  C   . VAL   A 1 179 ? -3.36227  -19.72122 -21.63828 1.000 16.79894 ? 186 VAL   A C   1 
ATOM   1477 O  O   . VAL   A 1 179 ? -4.20795  -19.64949 -20.73181 1.000 16.68112 ? 186 VAL   A O   1 
ATOM   1478 C  CB  . VAL   A 1 179 ? -2.40935  -17.40944 -21.45760 1.000 13.43122 ? 186 VAL   A CB  1 
ATOM   1479 C  CG1 . VAL   A 1 179 ? -1.20464  -17.98222 -20.61791 1.000 14.57518 ? 186 VAL   A CG1 1 
ATOM   1480 C  CG2 . VAL   A 1 179 ? -1.99376  -16.19001 -22.25284 1.000 14.32777 ? 186 VAL   A CG2 1 
ATOM   1481 N  N   . ILE   A 1 180 ? -2.76463  -20.85879 -22.00367 1.000 15.43151 ? 187 ILE   A N   1 
ATOM   1482 C  CA  . ILE   A 1 180 ? -3.06844  -22.14923 -21.38503 1.000 13.96346 ? 187 ILE   A CA  1 
ATOM   1483 C  C   . ILE   A 1 180 ? -1.95291  -22.46489 -20.41701 1.000 15.65903 ? 187 ILE   A C   1 
ATOM   1484 O  O   . ILE   A 1 180 ? -0.81895  -22.67694 -20.84332 1.000 15.49672 ? 187 ILE   A O   1 
ATOM   1485 C  CB  . ILE   A 1 180 ? -3.23333  -23.26031 -22.43199 1.000 12.68929 ? 187 ILE   A CB  1 
ATOM   1486 C  CG1 . ILE   A 1 180 ? -4.25718  -22.81504 -23.48975 1.000 17.74720 ? 187 ILE   A CG1 1 
ATOM   1487 C  CG2 . ILE   A 1 180 ? -3.59918  -24.61686 -21.75818 1.000 17.17896 ? 187 ILE   A CG2 1 
ATOM   1488 C  CD1 . ILE   A 1 180 ? -4.19659  -23.65068 -24.73525 1.000 22.54933 ? 187 ILE   A CD1 1 
ATOM   1489 N  N   . LEU   A 1 181 ? -2.25438  -22.46937 -19.11680 1.000 14.45540 ? 188 LEU   A N   1 
ATOM   1490 C  CA  . LEU   A 1 181 ? -1.23802  -22.74823 -18.10849 1.000 13.20126 ? 188 LEU   A CA  1 
ATOM   1491 C  C   . LEU   A 1 181 ? -1.33043  -24.22292 -17.75305 1.000 15.55929 ? 188 LEU   A C   1 
ATOM   1492 O  O   . LEU   A 1 181 ? -2.34668  -24.66426 -17.20113 1.000 15.55586 ? 188 LEU   A O   1 
ATOM   1493 C  CB  . LEU   A 1 181 ? -1.46154  -21.88182 -16.86769 1.000 12.98719 ? 188 LEU   A CB  1 
ATOM   1494 C  CG  . LEU   A 1 181 ? -1.53018  -20.38223 -17.12271 1.000 14.65695 ? 188 LEU   A CG  1 
ATOM   1495 C  CD1 . LEU   A 1 181 ? -1.91689  -19.71873 -15.78940 1.000 17.09092 ? 188 LEU   A CD1 1 
ATOM   1496 C  CD2 . LEU   A 1 181 ? -0.21262  -19.83551 -17.66528 1.000 16.96274 ? 188 LEU   A CD2 1 
ATOM   1497 N  N   . HIS   A 1 182 ? -0.28286  -24.99502 -18.06662 1.000 15.24358 ? 189 HIS   A N   1 
ATOM   1498 C  CA  . HIS   A 1 182 ? -0.23371  -26.40333 -17.66443 1.000 18.52119 ? 189 HIS   A CA  1 
ATOM   1499 C  C   . HIS   A 1 182 ? 0.37219   -26.41639 -16.27398 1.000 17.90303 ? 189 HIS   A C   1 
ATOM   1500 O  O   . HIS   A 1 182 ? 1.56850   -26.19957 -16.11913 1.000 18.00891 ? 189 HIS   A O   1 
ATOM   1501 C  CB  . HIS   A 1 182 ? 0.58390   -27.22487 -18.66739 1.000 18.37272 ? 189 HIS   A CB  1 
ATOM   1502 C  CG  . HIS   A 1 182 ? 0.09921   -27.08640 -20.08372 1.000 22.80492 ? 189 HIS   A CG  1 
ATOM   1503 N  ND1 . HIS   A 1 182 ? -0.71527  -28.02917 -20.67617 1.000 26.02328 ? 189 HIS   A ND1 1 
ATOM   1504 C  CD2 . HIS   A 1 182 ? 0.28913   -26.11354 -21.01078 1.000 21.82332 ? 189 HIS   A CD2 1 
ATOM   1505 C  CE1 . HIS   A 1 182 ? -1.00227  -27.64617 -21.91145 1.000 23.25065 ? 189 HIS   A CE1 1 
ATOM   1506 N  NE2 . HIS   A 1 182 ? -0.38609  -26.49645 -22.14708 1.000 23.34860 ? 189 HIS   A NE2 1 
ATOM   1507 N  N   . LEU   A 1 183 ? -0.46327  -26.55758 -15.25280 1.000 15.21914 ? 190 LEU   A N   1 
ATOM   1508 C  CA  . LEU   A 1 183 ? -0.00963  -26.23572 -13.89791 1.000 15.85673 ? 190 LEU   A CA  1 
ATOM   1509 C  C   . LEU   A 1 183 ? 0.93628   -27.29194 -13.34394 1.000 18.66938 ? 190 LEU   A C   1 
ATOM   1510 O  O   . LEU   A 1 183 ? 0.82270   -28.48782 -13.64054 1.000 21.97595 ? 190 LEU   A O   1 
ATOM   1511 C  CB  . LEU   A 1 183 ? -1.20472  -26.10757 -12.95821 1.000 18.38227 ? 190 LEU   A CB  1 
ATOM   1512 C  CG  . LEU   A 1 183 ? -2.15926  -24.95172 -13.26075 1.000 16.22439 ? 190 LEU   A CG  1 
ATOM   1513 C  CD1 . LEU   A 1 183 ? -3.30774  -24.88240 -12.20093 1.000 17.98029 ? 190 LEU   A CD1 1 
ATOM   1514 C  CD2 . LEU   A 1 183 ? -1.40100  -23.63092 -13.25815 1.000 18.15348 ? 190 LEU   A CD2 1 
ATOM   1515 N  N   . LYS   A 1 184 ? 1.85840   -26.82849 -12.49713 1.000 18.49512 ? 191 LYS   A N   1 
ATOM   1516 C  CA  . LYS   A 1 184 ? 2.71153   -27.71423 -11.70219 1.000 18.61105 ? 191 LYS   A CA  1 
ATOM   1517 C  C   . LYS   A 1 184 ? 1.84704   -28.54625 -10.75764 1.000 21.87906 ? 191 LYS   A C   1 
ATOM   1518 O  O   . LYS   A 1 184 ? 0.78574   -28.10754 -10.32660 1.000 23.32582 ? 191 LYS   A O   1 
ATOM   1519 C  CB  . LYS   A 1 184 ? 3.72248   -26.87198 -10.91725 1.000 19.60636 ? 191 LYS   A CB  1 
ATOM   1520 C  CG  . LYS   A 1 184 ? 4.73575   -26.08914 -11.79132 1.000 21.72478 ? 191 LYS   A CG  1 
ATOM   1521 C  CD  . LYS   A 1 184 ? 5.62944   -25.15108 -10.90461 1.000 25.22028 ? 191 LYS   A CD  1 
ATOM   1522 C  CE  . LYS   A 1 184 ? 6.33751   -24.00195 -11.67517 1.000 32.02390 ? 191 LYS   A CE  1 
ATOM   1523 N  NZ  . LYS   A 1 184 ? 7.29866   -23.08878 -10.82789 1.000 30.69437 ? 191 LYS   A NZ  1 
ATOM   1524 N  N   . GLU   A 1 185 ? 2.30622   -29.76807 -10.44205 1.000 25.12093 ? 192 GLU   A N   1 
ATOM   1525 C  CA  . GLU   A 1 185 ? 1.48790   -30.69150 -9.65343  1.000 26.59673 ? 192 GLU   A CA  1 
ATOM   1526 C  C   . GLU   A 1 185 ? 1.09229   -30.11663 -8.30376  1.000 25.79761 ? 192 GLU   A C   1 
ATOM   1527 O  O   . GLU   A 1 185 ? 0.02508   -30.46386 -7.77979  1.000 27.85465 ? 192 GLU   A O   1 
ATOM   1528 C  CB  . GLU   A 1 185 ? 2.21336   -32.03572 -9.45192  1.000 30.21350 ? 192 GLU   A CB  1 
ATOM   1529 C  CG  . GLU   A 1 185 ? 3.58555   -31.92600 -8.75673  1.000 42.89973 ? 192 GLU   A CG  1 
ATOM   1530 C  CD  . GLU   A 1 185 ? 3.56583   -32.21048 -7.23739  1.000 53.28990 ? 192 GLU   A CD  1 
ATOM   1531 O  OE1 . GLU   A 1 185 ? 2.53169   -32.69629 -6.72233  1.000 58.76870 ? 192 GLU   A OE1 1 
ATOM   1532 O  OE2 . GLU   A 1 185 ? 4.58815   -31.92915 -6.55586  1.000 55.14830 ? 192 GLU   A OE2 1 
ATOM   1533 N  N   A ASP   A 1 186 ? 1.91932   -29.25259 -7.72086  0.500 24.59534 ? 193 ASP   A N   1 
ATOM   1534 N  N   B ASP   A 1 186 ? 1.91932   -29.25259 -7.72086  0.500 24.59534 ? 193 ASP   A N   1 
ATOM   1535 C  CA  A ASP   A 1 186 ? 1.62945   -28.70440 -6.40378  0.500 25.96476 ? 193 ASP   A CA  1 
ATOM   1536 C  CA  B ASP   A 1 186 ? 1.62945   -28.70440 -6.40378  0.500 25.96476 ? 193 ASP   A CA  1 
ATOM   1537 C  C   A ASP   A 1 186 ? 0.94614   -27.34236 -6.45611  0.500 24.11260 ? 193 ASP   A C   1 
ATOM   1538 C  C   B ASP   A 1 186 ? 0.94614   -27.34236 -6.45611  0.500 24.11260 ? 193 ASP   A C   1 
ATOM   1539 O  O   A ASP   A 1 186 ? 0.84426   -26.67833 -5.41901  0.500 22.65004 ? 193 ASP   A O   1 
ATOM   1540 O  O   B ASP   A 1 186 ? 0.84426   -26.67833 -5.41901  0.500 22.65004 ? 193 ASP   A O   1 
ATOM   1541 C  CB  A ASP   A 1 186 ? 2.90546   -28.62643 -5.56099  0.500 27.59831 ? 193 ASP   A CB  1 
ATOM   1542 C  CB  B ASP   A 1 186 ? 2.90546   -28.62643 -5.56099  0.500 27.59831 ? 193 ASP   A CB  1 
ATOM   1543 C  CG  A ASP   A 1 186 ? 3.94287   -27.67329 -6.12782  0.500 31.22640 ? 193 ASP   A CG  1 
ATOM   1544 C  CG  B ASP   A 1 186 ? 3.94287   -27.67329 -6.12782  0.500 31.22640 ? 193 ASP   A CG  1 
ATOM   1545 O  OD1 A ASP   A 1 186 ? 3.84081   -27.26692 -7.30801  0.500 33.72139 ? 193 ASP   A OD1 1 
ATOM   1546 O  OD1 B ASP   A 1 186 ? 3.84081   -27.26692 -7.30801  0.500 33.72139 ? 193 ASP   A OD1 1 
ATOM   1547 O  OD2 A ASP   A 1 186 ? 4.86365   -27.30216 -5.36919  0.500 34.56638 ? 193 ASP   A OD2 1 
ATOM   1548 O  OD2 B ASP   A 1 186 ? 4.86365   -27.30216 -5.36919  0.500 34.56638 ? 193 ASP   A OD2 1 
ATOM   1549 N  N   . GLN   A 1 187 ? 0.44447   -26.93439 -7.62367  1.000 21.19616 ? 194 GLN   A N   1 
ATOM   1550 C  CA  . GLN   A 1 187 ? -0.17816  -25.62913 -7.80733  1.000 19.67426 ? 194 GLN   A CA  1 
ATOM   1551 C  C   . GLN   A 1 187 ? -1.63213  -25.78689 -8.25249  1.000 17.46691 ? 194 GLN   A C   1 
ATOM   1552 O  O   . GLN   A 1 187 ? -2.19816  -24.89978 -8.90063  1.000 18.73340 ? 194 GLN   A O   1 
ATOM   1553 C  CB  . GLN   A 1 187 ? 0.62504   -24.79989 -8.81945  1.000 18.20272 ? 194 GLN   A CB  1 
ATOM   1554 C  CG  . GLN   A 1 187 ? 2.06135   -24.52074 -8.34136  1.000 18.54907 ? 194 GLN   A CG  1 
ATOM   1555 C  CD  . GLN   A 1 187 ? 2.13285   -23.87539 -6.97771  1.000 21.56979 ? 194 GLN   A CD  1 
ATOM   1556 O  OE1 . GLN   A 1 187 ? 1.34391   -22.98465 -6.65121  1.000 21.94275 ? 194 GLN   A OE1 1 
ATOM   1557 N  NE2 . GLN   A 1 187 ? 3.15055   -24.24526 -6.19902  1.000 24.55306 ? 194 GLN   A NE2 1 
ATOM   1558 N  N   . THR   A 1 188 ? -2.27047  -26.90547 -7.91087  1.000 20.99168 ? 195 THR   A N   1 
ATOM   1559 C  CA  . THR   A 1 188 ? -3.64427  -27.10429 -8.37748  1.000 21.47421 ? 195 THR   A CA  1 
ATOM   1560 C  C   . THR   A 1 188 ? -4.68980  -26.31354 -7.59048  1.000 18.83753 ? 195 THR   A C   1 
ATOM   1561 O  O   . THR   A 1 188 ? -5.87713  -26.32427 -7.98066  1.000 21.88788 ? 195 THR   A O   1 
ATOM   1562 C  CB  . THR   A 1 188 ? -4.00756  -28.59748 -8.38104  1.000 23.15861 ? 195 THR   A CB  1 
ATOM   1563 O  OG1 . THR   A 1 188 ? -3.95447  -29.12417 -7.04301  1.000 26.37669 ? 195 THR   A OG1 1 
ATOM   1564 C  CG2 . THR   A 1 188 ? -3.05102  -29.36420 -9.29851  1.000 21.38079 ? 195 THR   A CG2 1 
ATOM   1565 N  N   . GLU   A 1 189 ? -4.29776  -25.58947 -6.53316  1.000 19.05541 ? 196 GLU   A N   1 
ATOM   1566 C  CA  . GLU   A 1 189 ? -5.25717  -24.67517 -5.89988  1.000 22.09795 ? 196 GLU   A CA  1 
ATOM   1567 C  C   . GLU   A 1 189 ? -5.82087  -23.65229 -6.87549  1.000 19.89810 ? 196 GLU   A C   1 
ATOM   1568 O  O   . GLU   A 1 189 ? -6.93715  -23.15740 -6.66707  1.000 18.88667 ? 196 GLU   A O   1 
ATOM   1569 C  CB  . GLU   A 1 189 ? -4.60464  -23.99026 -4.69840  1.000 19.92703 ? 196 GLU   A CB  1 
ATOM   1570 C  CG  . GLU   A 1 189 ? -3.61134  -22.88712 -5.07407  1.000 20.23509 ? 196 GLU   A CG  1 
ATOM   1571 C  CD  . GLU   A 1 189 ? -2.80946  -22.45592 -3.85090  1.000 25.25588 ? 196 GLU   A CD  1 
ATOM   1572 O  OE1 . GLU   A 1 189 ? -1.94118  -23.24805 -3.38867  1.000 24.73971 ? 196 GLU   A OE1 1 
ATOM   1573 O  OE2 . GLU   A 1 189 ? -3.06901  -21.35215 -3.32661  1.000 24.98043 ? 196 GLU   A OE2 1 
ATOM   1574 N  N   . TYR   A 1 190 ? -5.08580  -23.33115 -7.94079  1.000 17.50978 ? 197 TYR   A N   1 
ATOM   1575 C  CA  . TYR   A 1 190 ? -5.53627  -22.30289 -8.88301  1.000 15.51792 ? 197 TYR   A CA  1 
ATOM   1576 C  C   . TYR   A 1 190 ? -6.52929  -22.84127 -9.88161  1.000 17.15808 ? 197 TYR   A C   1 
ATOM   1577 O  O   . TYR   A 1 190 ? -6.90371  -22.10732 -10.81146 1.000 17.82811 ? 197 TYR   A O   1 
ATOM   1578 C  CB  . TYR   A 1 190 ? -4.31646  -21.66834 -9.58459  1.000 16.94961 ? 197 TYR   A CB  1 
ATOM   1579 C  CG  . TYR   A 1 190 ? -3.38556  -21.04152 -8.55824  1.000 15.86170 ? 197 TYR   A CG  1 
ATOM   1580 C  CD1 . TYR   A 1 190 ? -3.79631  -19.93009 -7.82863  1.000 17.93689 ? 197 TYR   A CD1 1 
ATOM   1581 C  CD2 . TYR   A 1 190 ? -2.13344  -21.61536 -8.24576  1.000 17.68011 ? 197 TYR   A CD2 1 
ATOM   1582 C  CE1 . TYR   A 1 190 ? -2.99143  -19.37683 -6.82422  1.000 18.61140 ? 197 TYR   A CE1 1 
ATOM   1583 C  CE2 . TYR   A 1 190 ? -1.29559  -21.04291 -7.24591  1.000 19.06971 ? 197 TYR   A CE2 1 
ATOM   1584 C  CZ  . TYR   A 1 190 ? -1.75308  -19.90996 -6.55419  1.000 17.97078 ? 197 TYR   A CZ  1 
ATOM   1585 O  OH  . TYR   A 1 190 ? -0.98896  -19.35787 -5.53223  1.000 19.19998 ? 197 TYR   A OH  1 
ATOM   1586 N  N   . LEU   A 1 191 ? -6.96773  -24.10242 -9.70618  1.000 17.93781 ? 198 LEU   A N   1 
ATOM   1587 C  CA  . LEU   A 1 191 ? -8.12085  -24.60431 -10.44056 1.000 17.99891 ? 198 LEU   A CA  1 
ATOM   1588 C  C   . LEU   A 1 191 ? -9.38868  -24.57703 -9.59659  1.000 21.26563 ? 198 LEU   A C   1 
ATOM   1589 O  O   . LEU   A 1 191 ? -10.46290 -24.91200 -10.11152 1.000 22.88721 ? 198 LEU   A O   1 
ATOM   1590 C  CB  . LEU   A 1 191 ? -7.86805  -26.04124 -10.89433 1.000 17.74546 ? 198 LEU   A CB  1 
ATOM   1591 C  CG  . LEU   A 1 191 ? -6.64959  -26.22828 -11.77911 1.000 19.42882 ? 198 LEU   A CG  1 
ATOM   1592 C  CD1 . LEU   A 1 191 ? -6.42949  -27.71284 -12.07836 1.000 23.03318 ? 198 LEU   A CD1 1 
ATOM   1593 C  CD2 . LEU   A 1 191 ? -6.83883  -25.40135 -13.05565 1.000 20.87295 ? 198 LEU   A CD2 1 
ATOM   1594 N  N   . GLU   A 1 192 ? -9.28595  -24.25591 -8.30771  1.000 18.50176 ? 199 GLU   A N   1 
ATOM   1595 C  CA  . GLU   A 1 192 ? -10.46108 -24.27661 -7.43920  1.000 20.64808 ? 199 GLU   A CA  1 
ATOM   1596 C  C   . GLU   A 1 192 ? -11.23238 -22.96798 -7.54436  1.000 21.87577 ? 199 GLU   A C   1 
ATOM   1597 O  O   . GLU   A 1 192 ? -10.64142 -21.87694 -7.49787  1.000 20.22606 ? 199 GLU   A O   1 
ATOM   1598 C  CB  . GLU   A 1 192 ? -10.06026 -24.53339 -5.99367  1.000 24.81313 ? 199 GLU   A CB  1 
ATOM   1599 C  CG  . GLU   A 1 192 ? -9.08728  -25.68121 -5.84467  1.000 28.62915 ? 199 GLU   A CG  1 
ATOM   1600 C  CD  . GLU   A 1 192 ? -8.87844  -26.10410 -4.40530  1.000 45.56600 ? 199 GLU   A CD  1 
ATOM   1601 O  OE1 . GLU   A 1 192 ? -7.79282  -26.66319 -4.10688  1.000 49.66469 ? 199 GLU   A OE1 1 
ATOM   1602 O  OE2 . GLU   A 1 192 ? -9.78489  -25.88123 -3.57121  1.000 50.92914 ? 199 GLU   A OE2 1 
ATOM   1603 N  N   . GLU   A 1 193 ? -12.56113 -23.07902 -7.67377  1.000 22.47768 ? 200 GLU   A N   1 
ATOM   1604 C  CA  . GLU   A 1 193 ? -13.39148 -21.89937 -7.87514  1.000 18.74661 ? 200 GLU   A CA  1 
ATOM   1605 C  C   . GLU   A 1 193 ? -13.17244 -20.85165 -6.78385  1.000 20.77829 ? 200 GLU   A C   1 
ATOM   1606 O  O   . GLU   A 1 193 ? -13.04988 -19.65238 -7.07246  1.000 21.52841 ? 200 GLU   A O   1 
ATOM   1607 C  CB  . GLU   A 1 193 ? -14.87704 -22.29721 -7.92161  1.000 20.10798 ? 200 GLU   A CB  1 
ATOM   1608 C  CG  . GLU   A 1 193 ? -15.73054 -21.19511 -8.49739  1.000 25.85330 ? 200 GLU   A CG  1 
ATOM   1609 C  CD  . GLU   A 1 193 ? -17.24665 -21.45297 -8.38354  1.000 43.25449 ? 200 GLU   A CD  1 
ATOM   1610 O  OE1 . GLU   A 1 193 ? -17.63993 -22.45997 -7.75643  1.000 38.89034 ? 200 GLU   A OE1 1 
ATOM   1611 O  OE2 . GLU   A 1 193 ? -18.03437 -20.63551 -8.92910  1.000 42.35204 ? 200 GLU   A OE2 1 
ATOM   1612 N  N   . ARG   A 1 194 ? -13.19963 -21.27218 -5.51779  1.000 21.47276 ? 201 ARG   A N   1 
ATOM   1613 C  CA  . ARG   A 1 194 ? -13.15103 -20.27048 -4.45459  1.000 18.93097 ? 201 ARG   A CA  1 
ATOM   1614 C  C   . ARG   A 1 194 ? -11.81204 -19.54843 -4.43527  1.000 21.12853 ? 201 ARG   A C   1 
ATOM   1615 O  O   . ARG   A 1 194 ? -11.75909 -18.35217 -4.11778  1.000 20.45935 ? 201 ARG   A O   1 
ATOM   1616 C  CB  . ARG   A 1 194 ? -13.45298 -20.91009 -3.09286  1.000 22.78063 ? 201 ARG   A CB  1 
ATOM   1617 C  CG  . ARG   A 1 194 ? -12.54841 -22.02780 -2.72744  1.000 28.29163 ? 201 ARG   A CG  1 
ATOM   1618 C  CD  . ARG   A 1 194 ? -12.95298 -22.49087 -1.31222  1.000 32.31584 ? 201 ARG   A CD  1 
ATOM   1619 N  NE  . ARG   A 1 194 ? -11.97573 -23.41361 -0.75900  1.000 42.03114 ? 201 ARG   A NE  1 
ATOM   1620 C  CZ  . ARG   A 1 194 ? -12.09548 -23.96686 0.43954   1.000 34.29182 ? 201 ARG   A CZ  1 
ATOM   1621 N  NH1 . ARG   A 1 194 ? -13.15635 -23.73425 1.20113   1.000 43.05074 ? 201 ARG   A NH1 1 
ATOM   1622 N  NH2 . ARG   A 1 194 ? -11.12868 -24.76703 0.88333   1.000 45.67067 ? 201 ARG   A NH2 1 
ATOM   1623 N  N   . ARG   A 1 195 ? -10.72854 -20.24763 -4.80975  1.000 16.91745 ? 202 ARG   A N   1 
ATOM   1624 C  CA  . ARG   A 1 195 ? -9.40677  -19.62846 -4.84351  1.000 19.19702 ? 202 ARG   A CA  1 
ATOM   1625 C  C   . ARG   A 1 195 ? -9.31468  -18.62862 -5.98599  1.000 18.04404 ? 202 ARG   A C   1 
ATOM   1626 O  O   . ARG   A 1 195 ? -8.80516  -17.51363 -5.81119  1.000 15.95628 ? 202 ARG   A O   1 
ATOM   1627 C  CB  . ARG   A 1 195 ? -8.36185  -20.72319 -4.98686  1.000 17.92625 ? 202 ARG   A CB  1 
ATOM   1628 C  CG  . ARG   A 1 195 ? -6.91882  -20.23486 -4.97692  1.000 17.73466 ? 202 ARG   A CG  1 
ATOM   1629 C  CD  . ARG   A 1 195 ? -6.54007  -19.63255 -3.59506  1.000 19.83622 ? 202 ARG   A CD  1 
ATOM   1630 N  NE  . ARG   A 1 195 ? -5.10002  -19.40801 -3.53701  1.000 18.87161 ? 202 ARG   A NE  1 
ATOM   1631 C  CZ  . ARG   A 1 195 ? -4.49949  -18.24003 -3.32197  1.000 20.98070 ? 202 ARG   A CZ  1 
ATOM   1632 N  NH1 . ARG   A 1 195 ? -5.18960  -17.13896 -3.08335  1.000 21.27444 ? 202 ARG   A NH1 1 
ATOM   1633 N  NH2 . ARG   A 1 195 ? -3.16259  -18.18304 -3.34613  1.000 20.05165 ? 202 ARG   A NH2 1 
ATOM   1634 N  N   . ILE   A 1 196 ? -9.81056  -18.99981 -7.17157  1.000 16.90020 ? 203 ILE   A N   1 
ATOM   1635 C  CA  . ILE   A 1 196 ? -9.74256  -18.07940 -8.30092  1.000 17.17381 ? 203 ILE   A CA  1 
ATOM   1636 C  C   . ILE   A 1 196 ? -10.57163 -16.84072 -8.01992  1.000 17.31090 ? 203 ILE   A C   1 
ATOM   1637 O  O   . ILE   A 1 196 ? -10.12325 -15.71445 -8.28224  1.000 16.33033 ? 203 ILE   A O   1 
ATOM   1638 C  CB  . ILE   A 1 196 ? -10.19296 -18.75959 -9.60726  1.000 17.96526 ? 203 ILE   A CB  1 
ATOM   1639 C  CG1 . ILE   A 1 196 ? -9.28597  -19.94069 -9.95819  1.000 16.30595 ? 203 ILE   A CG1 1 
ATOM   1640 C  CG2 . ILE   A 1 196 ? -10.23473 -17.71048 -10.75549 1.000 17.18996 ? 203 ILE   A CG2 1 
ATOM   1641 C  CD1 . ILE   A 1 196 ? -9.90105  -20.88693 -11.01995 1.000 21.15029 ? 203 ILE   A CD1 1 
ATOM   1642 N  N   . LYS   A 1 197 ? -11.79178 -17.02863 -7.47547  1.000 16.42075 ? 204 LYS   A N   1 
ATOM   1643 C  CA  . LYS   A 1 197 ? -12.64322 -15.88542 -7.12859  1.000 16.31598 ? 204 LYS   A CA  1 
ATOM   1644 C  C   . LYS   A 1 197 ? -11.92661 -14.94760 -6.16249  1.000 18.64529 ? 204 LYS   A C   1 
ATOM   1645 O  O   . LYS   A 1 197 ? -11.98296 -13.72187 -6.31131  1.000 19.04764 ? 204 LYS   A O   1 
ATOM   1646 C  CB  . LYS   A 1 197 ? -13.95440 -16.36580 -6.48433  1.000 20.34210 ? 204 LYS   A CB  1 
ATOM   1647 C  CG  . LYS   A 1 197 ? -14.87552 -17.10926 -7.41364  1.000 24.45898 ? 204 LYS   A CG  1 
ATOM   1648 C  CD  . LYS   A 1 197 ? -16.19763 -17.49604 -6.64766  1.000 24.27155 ? 204 LYS   A CD  1 
ATOM   1649 C  CE  . LYS   A 1 197 ? -17.40503 -17.52410 -7.56684  1.000 42.88904 ? 204 LYS   A CE  1 
ATOM   1650 N  NZ  . LYS   A 1 197 ? -18.47461 -18.45452 -7.00387  1.000 47.68283 ? 204 LYS   A NZ  1 
ATOM   1651 N  N   . GLU   A 1 198 ? -11.29670 -15.51789 -5.12947  1.000 15.21833 ? 205 GLU   A N   1 
ATOM   1652 C  CA  . GLU   A 1 198 ? -10.57569 -14.71577 -4.14406  1.000 17.08437 ? 205 GLU   A CA  1 
ATOM   1653 C  C   . GLU   A 1 198 ? -9.50648  -13.86540 -4.80737  1.000 16.30478 ? 205 GLU   A C   1 
ATOM   1654 O  O   . GLU   A 1 198 ? -9.36149  -12.67469 -4.50381  1.000 18.20409 ? 205 GLU   A O   1 
ATOM   1655 C  CB  . GLU   A 1 198 ? -9.94143  -15.63351 -3.08588  1.000 17.90519 ? 205 GLU   A CB  1 
ATOM   1656 C  CG  . GLU   A 1 198 ? -9.06571  -14.91581 -2.07002  1.000 18.05265 ? 205 GLU   A CG  1 
ATOM   1657 C  CD  . GLU   A 1 198 ? -8.32757  -15.87819 -1.14905  1.000 21.34295 ? 205 GLU   A CD  1 
ATOM   1658 O  OE1 . GLU   A 1 198 ? -7.72664  -16.82784 -1.67598  1.000 20.51051 ? 205 GLU   A OE1 1 
ATOM   1659 O  OE2 . GLU   A 1 198 ? -8.30396  -15.64916 0.07428   1.000 20.82162 ? 205 GLU   A OE2 1 
ATOM   1660 N  N   . ILE   A 1 199 ? -8.74667  -14.45888 -5.72353  1.000 14.73122 ? 206 ILE   A N   1 
ATOM   1661 C  CA  . ILE   A 1 199 ? -7.64687  -13.72831 -6.35352  1.000 15.77990 ? 206 ILE   A CA  1 
ATOM   1662 C  C   . ILE   A 1 199 ? -8.15822  -12.62431 -7.26346  1.000 17.15243 ? 206 ILE   A C   1 
ATOM   1663 O  O   . ILE   A 1 199 ? -7.60563  -11.51786 -7.27124  1.000 18.84814 ? 206 ILE   A O   1 
ATOM   1664 C  CB  . ILE   A 1 199 ? -6.72222  -14.69318 -7.11118  1.000 17.30020 ? 206 ILE   A CB  1 
ATOM   1665 C  CG1 . ILE   A 1 199 ? -6.11878  -15.70844 -6.13052  1.000 16.49992 ? 206 ILE   A CG1 1 
ATOM   1666 C  CG2 . ILE   A 1 199 ? -5.69429  -13.92318 -7.92641  1.000 19.17650 ? 206 ILE   A CG2 1 
ATOM   1667 C  CD1 . ILE   A 1 199 ? -5.55352  -16.94411 -6.86164  1.000 16.45466 ? 206 ILE   A CD1 1 
ATOM   1668 N  N   . VAL   A 1 200 ? -9.19592  -12.90487 -8.06291  1.000 16.22256 ? 207 VAL   A N   1 
ATOM   1669 C  CA  . VAL   A 1 200 ? -9.76015  -11.87695 -8.92517  1.000 15.66491 ? 207 VAL   A CA  1 
ATOM   1670 C  C   . VAL   A 1 200 ? -10.30190 -10.71903 -8.10229  1.000 17.69027 ? 207 VAL   A C   1 
ATOM   1671 O  O   . VAL   A 1 200 ? -10.07360 -9.55116  -8.43365  1.000 20.26251 ? 207 VAL   A O   1 
ATOM   1672 C  CB  . VAL   A 1 200 ? -10.84346 -12.51275 -9.81030  1.000 16.57238 ? 207 VAL   A CB  1 
ATOM   1673 C  CG1 . VAL   A 1 200 ? -11.61832 -11.44795 -10.54941 1.000 17.80997 ? 207 VAL   A CG1 1 
ATOM   1674 C  CG2 . VAL   A 1 200 ? -10.18171 -13.51882 -10.77739 1.000 17.67794 ? 207 VAL   A CG2 1 
ATOM   1675 N  N   . LYS   A 1 201 ? -10.98409 -11.01752 -6.98828  1.000 16.13650 ? 208 LYS   A N   1 
ATOM   1676 C  CA  . LYS   A 1 201 ? -11.53343 -9.93600  -6.16331  1.000 18.14232 ? 208 LYS   A CA  1 
ATOM   1677 C  C   . LYS   A 1 201 ? -10.41827 -9.13400  -5.49945  1.000 18.62471 ? 208 LYS   A C   1 
ATOM   1678 O  O   . LYS   A 1 201 ? -10.52968 -7.90722  -5.36057  1.000 23.95497 ? 208 LYS   A O   1 
ATOM   1679 C  CB  . LYS   A 1 201 ? -12.49321 -10.51097 -5.11539  1.000 20.44054 ? 208 LYS   A CB  1 
ATOM   1680 C  CG  . LYS   A 1 201 ? -13.07923 -9.46586  -4.16304  1.000 23.50858 ? 208 LYS   A CG  1 
ATOM   1681 C  CD  . LYS   A 1 201 ? -13.85226 -10.13779 -3.06056  1.000 30.82573 ? 208 LYS   A CD  1 
ATOM   1682 C  CE  . LYS   A 1 201 ? -14.52190 -9.13173  -2.13454  1.000 34.64203 ? 208 LYS   A CE  1 
ATOM   1683 N  NZ  . LYS   A 1 201 ? -15.49217 -9.84131  -1.26668  1.000 46.01946 ? 208 LYS   A NZ  1 
ATOM   1684 N  N   . LYS   A 1 202 ? -9.32738  -9.80484  -5.08514  1.000 20.41932 ? 209 LYS   A N   1 
ATOM   1685 C  CA  . LYS   A 1 202 ? -8.22768  -9.11059  -4.40842  1.000 20.97038 ? 209 LYS   A CA  1 
ATOM   1686 C  C   . LYS   A 1 202 ? -7.45104  -8.20200  -5.35628  1.000 21.31972 ? 209 LYS   A C   1 
ATOM   1687 O  O   . LYS   A 1 202 ? -7.11162  -7.06418  -4.99973  1.000 22.06254 ? 209 LYS   A O   1 
ATOM   1688 C  CB  . LYS   A 1 202 ? -7.28997  -10.13720 -3.78560  1.000 21.54698 ? 209 LYS   A CB  1 
ATOM   1689 C  CG  . LYS   A 1 202 ? -6.08088  -9.52045  -3.07951  1.000 24.75828 ? 209 LYS   A CG  1 
ATOM   1690 C  CD  . LYS   A 1 202 ? -5.30286  -10.62790 -2.40334  1.000 30.21105 ? 209 LYS   A CD  1 
ATOM   1691 C  CE  . LYS   A 1 202 ? -4.08264  -10.08897 -1.65957  1.000 37.61307 ? 209 LYS   A CE  1 
ATOM   1692 N  NZ  . LYS   A 1 202 ? -3.33466  -11.19004 -0.95351  1.000 40.17448 ? 209 LYS   A NZ  1 
ATOM   1693 N  N   . HIS   A 1 203 ? -7.15351  -8.68569  -6.57719  1.000 20.46366 ? 210 HIS   A N   1 
ATOM   1694 C  CA  . HIS   A 1 203 ? -6.15497  -8.03879  -7.42196  1.000 22.57417 ? 210 HIS   A CA  1 
ATOM   1695 C  C   . HIS   A 1 203 ? -6.67718  -7.45387  -8.72282  1.000 23.46166 ? 210 HIS   A C   1 
ATOM   1696 O  O   . HIS   A 1 203 ? -5.93027  -6.69561  -9.36186  1.000 22.81249 ? 210 HIS   A O   1 
ATOM   1697 C  CB  . HIS   A 1 203 ? -5.04553  -9.03141  -7.81392  1.000 21.94631 ? 210 HIS   A CB  1 
ATOM   1698 C  CG  . HIS   A 1 203 ? -4.20464  -9.48598  -6.66940  1.000 23.49262 ? 210 HIS   A CG  1 
ATOM   1699 N  ND1 . HIS   A 1 203 ? -3.40980  -8.62712  -5.93809  1.000 26.65738 ? 210 HIS   A ND1 1 
ATOM   1700 C  CD2 . HIS   A 1 203 ? -4.07891  -10.70682 -6.09100  1.000 26.99748 ? 210 HIS   A CD2 1 
ATOM   1701 C  CE1 . HIS   A 1 203 ? -2.80053  -9.30954  -4.98329  1.000 27.15234 ? 210 HIS   A CE1 1 
ATOM   1702 N  NE2 . HIS   A 1 203 ? -3.20123  -10.56935 -5.04131  1.000 26.18833 ? 210 HIS   A NE2 1 
ATOM   1703 N  N   . SER   A 1 204 ? -7.89498  -7.79806  -9.15302  1.000 21.17017 ? 211 SER   A N   1 
ATOM   1704 C  CA  . SER   A 1 204 ? -8.41020  -7.42298  -10.46674 1.000 20.28040 ? 211 SER   A CA  1 
ATOM   1705 C  C   . SER   A 1 204 ? -9.77920  -6.76152  -10.37401 1.000 21.46790 ? 211 SER   A C   1 
ATOM   1706 O  O   . SER   A 1 204 ? -10.57411 -6.79385  -11.32472 1.000 21.99755 ? 211 SER   A O   1 
ATOM   1707 C  CB  . SER   A 1 204 ? -8.43441  -8.64685  -11.40029 1.000 20.13619 ? 211 SER   A CB  1 
ATOM   1708 O  OG  . SER   A 1 204 ? -7.12160  -9.21788  -11.46716 1.000 21.82784 ? 211 SER   A OG  1 
ATOM   1709 N  N   . GLN   A 1 205 ? -10.05271 -6.09302  -9.25799  1.000 22.39128 ? 212 GLN   A N   1 
ATOM   1710 C  CA  . GLN   A 1 205 ? -11.40466 -5.62095  -9.04126  1.000 23.82970 ? 212 GLN   A CA  1 
ATOM   1711 C  C   . GLN   A 1 205 ? -11.74382 -4.43300  -9.93245  1.000 24.79854 ? 212 GLN   A C   1 
ATOM   1712 O  O   . GLN   A 1 205 ? -12.93535 -4.12995  -10.10802 1.000 33.95843 ? 212 GLN   A O   1 
ATOM   1713 C  CB  . GLN   A 1 205 ? -11.60971 -5.27568  -7.56459  1.000 31.49561 ? 212 GLN   A CB  1 
ATOM   1714 C  CG  . GLN   A 1 205 ? -10.64406 -4.26361  -7.05539  1.000 37.76407 ? 212 GLN   A CG  1 
ATOM   1715 C  CD  . GLN   A 1 205 ? -9.36076  -4.81886  -6.39275  1.000 42.40274 ? 212 GLN   A CD  1 
ATOM   1716 O  OE1 . GLN   A 1 205 ? -8.37024  -5.21082  -7.06290  1.000 32.97544 ? 212 GLN   A OE1 1 
ATOM   1717 N  NE2 . GLN   A 1 205 ? -9.35438  -4.78397  -5.04426  1.000 47.38421 ? 212 GLN   A NE2 1 
ATOM   1718 N  N   . PHE   A 1 206 ? -10.74300 -3.78252  -10.53386 1.000 23.11916 ? 213 PHE   A N   1 
ATOM   1719 C  CA  . PHE   A 1 206 ? -10.99318 -2.57310  -11.30643 1.000 28.03658 ? 213 PHE   A CA  1 
ATOM   1720 C  C   . PHE   A 1 206 ? -10.64382 -2.78383  -12.78299 1.000 31.44035 ? 213 PHE   A C   1 
ATOM   1721 O  O   . PHE   A 1 206 ? -10.27071 -1.83578  -13.49402 1.000 35.86048 ? 213 PHE   A O   1 
ATOM   1722 C  CB  . PHE   A 1 206 ? -10.17698 -1.43677  -10.71722 1.000 33.53898 ? 213 PHE   A CB  1 
ATOM   1723 C  CG  . PHE   A 1 206 ? -10.63553 -1.07890  -9.32988  1.000 37.27547 ? 213 PHE   A CG  1 
ATOM   1724 C  CD1 . PHE   A 1 206 ? -11.84091 -0.48788  -9.08063  1.000 36.54075 ? 213 PHE   A CD1 1 
ATOM   1725 C  CD2 . PHE   A 1 206 ? -9.81262  -1.36826  -8.25558  1.000 36.34712 ? 213 PHE   A CD2 1 
ATOM   1726 C  CE1 . PHE   A 1 206 ? -12.23762 -0.22362  -7.78280  1.000 44.28682 ? 213 PHE   A CE1 1 
ATOM   1727 C  CE2 . PHE   A 1 206 ? -10.19302 -1.07040  -6.95756  1.000 40.11673 ? 213 PHE   A CE2 1 
ATOM   1728 C  CZ  . PHE   A 1 206 ? -11.40790 -0.51352  -6.72917  1.000 42.23584 ? 213 PHE   A CZ  1 
ATOM   1729 N  N   . ILE   A 1 207 ? -10.67424 -4.02683  -13.24809 1.000 18.02720 ? 214 ILE   A N   1 
ATOM   1730 C  CA  . ILE   A 1 207 ? -10.51728 -4.31171  -14.66701 1.000 17.25513 ? 214 ILE   A CA  1 
ATOM   1731 C  C   . ILE   A 1 207 ? -11.83261 -4.02631  -15.38002 1.000 23.84912 ? 214 ILE   A C   1 
ATOM   1732 O  O   . ILE   A 1 207 ? -12.90161 -4.47777  -14.94004 1.000 20.74519 ? 214 ILE   A O   1 
ATOM   1733 C  CB  . ILE   A 1 207 ? -10.06246 -5.76630  -14.84103 1.000 18.01758 ? 214 ILE   A CB  1 
ATOM   1734 C  CG1 . ILE   A 1 207 ? -8.64386  -5.93251  -14.25516 1.000 18.17496 ? 214 ILE   A CG1 1 
ATOM   1735 C  CG2 . ILE   A 1 207 ? -10.05380 -6.21565  -16.31568 1.000 17.66864 ? 214 ILE   A CG2 1 
ATOM   1736 C  CD1 . ILE   A 1 207 ? -7.50662  -5.18839  -14.99367 1.000 19.62383 ? 214 ILE   A CD1 1 
ATOM   1737 N  N   . GLY   A 1 208 ? -11.76361 -3.26194  -16.46895 1.000 18.13110 ? 215 GLY   A N   1 
ATOM   1738 C  CA  . GLY   A 1 208 ? -12.92415 -2.68813  -17.11509 1.000 20.17374 ? 215 GLY   A CA  1 
ATOM   1739 C  C   . GLY   A 1 208 ? -13.53098 -3.55439  -18.19660 1.000 20.52612 ? 215 GLY   A C   1 
ATOM   1740 O  O   . GLY   A 1 208 ? -14.10467 -3.04977  -19.17407 1.000 21.42895 ? 215 GLY   A O   1 
ATOM   1741 N  N   . TYR   A 1 209 ? -13.45132 -4.86428  -18.01102 1.000 17.39334 ? 216 TYR   A N   1 
ATOM   1742 C  CA  . TYR   A 1 209 ? -14.04179 -5.82431  -18.93172 1.000 20.15936 ? 216 TYR   A CA  1 
ATOM   1743 C  C   . TYR   A 1 209 ? -14.64511 -6.93324  -18.08684 1.000 17.97484 ? 216 TYR   A C   1 
ATOM   1744 O  O   . TYR   A 1 209 ? -14.13011 -7.21848  -16.99944 1.000 19.04787 ? 216 TYR   A O   1 
ATOM   1745 C  CB  . TYR   A 1 209 ? -13.00012 -6.42379  -19.89355 1.000 18.41023 ? 216 TYR   A CB  1 
ATOM   1746 C  CG  . TYR   A 1 209 ? -12.38381 -5.36057  -20.76442 1.000 17.78491 ? 216 TYR   A CG  1 
ATOM   1747 C  CD1 . TYR   A 1 209 ? -13.03145 -4.92451  -21.92878 1.000 18.84505 ? 216 TYR   A CD1 1 
ATOM   1748 C  CD2 . TYR   A 1 209 ? -11.18276 -4.75236  -20.40718 1.000 19.28240 ? 216 TYR   A CD2 1 
ATOM   1749 C  CE1 . TYR   A 1 209 ? -12.50406 -3.91909  -22.69901 1.000 18.48644 ? 216 TYR   A CE1 1 
ATOM   1750 C  CE2 . TYR   A 1 209 ? -10.63633 -3.71212  -21.18745 1.000 18.18278 ? 216 TYR   A CE2 1 
ATOM   1751 C  CZ  . TYR   A 1 209 ? -11.30782 -3.32769  -22.33766 1.000 17.77065 ? 216 TYR   A CZ  1 
ATOM   1752 O  OH  . TYR   A 1 209 ? -10.84980 -2.30817  -23.12442 1.000 19.89431 ? 216 TYR   A OH  1 
ATOM   1753 N  N   . PRO   A 1 210 ? -15.69835 -7.60065  -18.56938 1.000 18.64791 ? 217 PRO   A N   1 
ATOM   1754 C  CA  . PRO   A 1 210 ? -16.26449 -8.72776  -17.81389 1.000 16.75823 ? 217 PRO   A CA  1 
ATOM   1755 C  C   . PRO   A 1 210 ? -15.30490 -9.90060  -17.73204 1.000 19.06088 ? 217 PRO   A C   1 
ATOM   1756 O  O   . PRO   A 1 210 ? -14.72586 -10.30592 -18.74038 1.000 20.51633 ? 217 PRO   A O   1 
ATOM   1757 C  CB  . PRO   A 1 210 ? -17.53618 -9.10120  -18.59247 1.000 21.82398 ? 217 PRO   A CB  1 
ATOM   1758 C  CG  . PRO   A 1 210 ? -17.44477 -8.46422  -19.91084 1.000 24.77718 ? 217 PRO   A CG  1 
ATOM   1759 C  CD  . PRO   A 1 210 ? -16.46670 -7.29655  -19.80155 1.000 18.31534 ? 217 PRO   A CD  1 
ATOM   1760 N  N   . ILE   A 1 211 ? -15.13680 -10.43110 -16.51950 1.000 17.43470 ? 218 ILE   A N   1 
ATOM   1761 C  CA  . ILE   A 1 211 ? -14.27979 -11.58924 -16.26429 1.000 15.29648 ? 218 ILE   A CA  1 
ATOM   1762 C  C   . ILE   A 1 211 ? -15.20767 -12.70484 -15.81777 1.000 16.67072 ? 218 ILE   A C   1 
ATOM   1763 O  O   . ILE   A 1 211 ? -15.84886 -12.60438 -14.75053 1.000 18.11352 ? 218 ILE   A O   1 
ATOM   1764 C  CB  . ILE   A 1 211 ? -13.21529 -11.30747 -15.20010 1.000 16.03915 ? 218 ILE   A CB  1 
ATOM   1765 C  CG1 . ILE   A 1 211 ? -12.34040 -10.10252 -15.61767 1.000 15.91753 ? 218 ILE   A CG1 1 
ATOM   1766 C  CG2 . ILE   A 1 211 ? -12.39773 -12.59414 -14.89114 1.000 14.81123 ? 218 ILE   A CG2 1 
ATOM   1767 C  CD1 . ILE   A 1 211 ? -11.46375 -9.59704  -14.40307 1.000 16.73677 ? 218 ILE   A CD1 1 
ATOM   1768 N  N   . THR   A 1 212 ? -15.32225 -13.74243 -16.64315 1.000 15.50235 ? 219 THR   A N   1 
ATOM   1769 C  CA  . THR   A 1 212 ? -16.26259 -14.83705 -16.37576 1.000 14.80235 ? 219 THR   A CA  1 
ATOM   1770 C  C   . THR   A 1 212 ? -15.45279 -16.04985 -15.97345 1.000 15.54079 ? 219 THR   A C   1 
ATOM   1771 O  O   . THR   A 1 212 ? -14.60125 -16.51486 -16.73711 1.000 15.93903 ? 219 THR   A O   1 
ATOM   1772 C  CB  . THR   A 1 212 ? -17.12930 -15.13978 -17.59335 1.000 15.11293 ? 219 THR   A CB  1 
ATOM   1773 O  OG1 . THR   A 1 212 ? -17.83610 -13.94675 -17.97026 1.000 16.57180 ? 219 THR   A OG1 1 
ATOM   1774 C  CG2 . THR   A 1 212 ? -18.10845 -16.28070 -17.26634 1.000 17.67177 ? 219 THR   A CG2 1 
ATOM   1775 N  N   . LEU   A 1 213 ? -15.66849 -16.51242 -14.75192 1.000 15.73091 ? 220 LEU   A N   1 
ATOM   1776 C  CA  . LEU   A 1 213 ? -15.06537 -17.74048 -14.25445 1.000 16.12541 ? 220 LEU   A CA  1 
ATOM   1777 C  C   . LEU   A 1 213 ? -15.97924 -18.90901 -14.62507 1.000 15.93080 ? 220 LEU   A C   1 
ATOM   1778 O  O   . LEU   A 1 213 ? -17.10186 -19.02658 -14.08620 1.000 15.87369 ? 220 LEU   A O   1 
ATOM   1779 C  CB  . LEU   A 1 213 ? -14.85609 -17.64100 -12.74105 1.000 16.60235 ? 220 LEU   A CB  1 
ATOM   1780 C  CG  . LEU   A 1 213 ? -14.31199 -18.89881 -12.08179 1.000 19.34445 ? 220 LEU   A CG  1 
ATOM   1781 C  CD1 . LEU   A 1 213 ? -13.02702 -19.44466 -12.77015 1.000 17.51161 ? 220 LEU   A CD1 1 
ATOM   1782 C  CD2 . LEU   A 1 213 ? -14.03233 -18.54506 -10.60078 1.000 19.69183 ? 220 LEU   A CD2 1 
ATOM   1783 N  N   . PHE   A 1 214 ? -15.51799 -19.75120 -15.55584 1.000 15.85266 ? 221 PHE   A N   1 
ATOM   1784 C  CA  . PHE   A 1 214 ? -16.30386 -20.92865 -15.92585 1.000 16.26715 ? 221 PHE   A CA  1 
ATOM   1785 C  C   . PHE   A 1 214 ? -16.28164 -21.93310 -14.78463 1.000 17.91689 ? 221 PHE   A C   1 
ATOM   1786 O  O   . PHE   A 1 214 ? -15.30637 -22.02551 -14.02864 1.000 17.88654 ? 221 PHE   A O   1 
ATOM   1787 C  CB  . PHE   A 1 214 ? -15.71396 -21.59757 -17.18190 1.000 14.75618 ? 221 PHE   A CB  1 
ATOM   1788 C  CG  . PHE   A 1 214 ? -15.98339 -20.86672 -18.47206 1.000 14.48169 ? 221 PHE   A CG  1 
ATOM   1789 C  CD1 . PHE   A 1 214 ? -16.03434 -19.47233 -18.54280 1.000 15.36561 ? 221 PHE   A CD1 1 
ATOM   1790 C  CD2 . PHE   A 1 214 ? -16.07902 -21.60236 -19.65298 1.000 16.68343 ? 221 PHE   A CD2 1 
ATOM   1791 C  CE1 . PHE   A 1 214 ? -16.22689 -18.81120 -19.75392 1.000 16.66397 ? 221 PHE   A CE1 1 
ATOM   1792 C  CE2 . PHE   A 1 214 ? -16.28730 -20.96066 -20.88283 1.000 15.53078 ? 221 PHE   A CE2 1 
ATOM   1793 C  CZ  . PHE   A 1 214 ? -16.36326 -19.55384 -20.94738 1.000 14.15019 ? 221 PHE   A CZ  1 
ATOM   1794 N  N   . VAL   A 1 215 ? -17.35888 -22.70310 -14.65447 1.000 19.05918 ? 222 VAL   A N   1 
ATOM   1795 C  CA  . VAL   A 1 215 ? -17.37427 -23.80668 -13.69662 1.000 22.81532 ? 222 VAL   A CA  1 
ATOM   1796 C  C   . VAL   A 1 215 ? -17.21932 -25.13431 -14.43204 1.000 22.62887 ? 222 VAL   A C   1 
ATOM   1797 O  O   . VAL   A 1 215 ? -17.30542 -25.21775 -15.66132 1.000 22.01118 ? 222 VAL   A O   1 
ATOM   1798 C  CB  . VAL   A 1 215 ? -18.60997 -23.79591 -12.79959 1.000 32.85819 ? 222 VAL   A CB  1 
ATOM   1799 C  CG1 . VAL   A 1 215 ? -18.47467 -22.68362 -11.72216 1.000 35.54623 ? 222 VAL   A CG1 1 
ATOM   1800 C  CG2 . VAL   A 1 215 ? -19.78629 -23.58140 -13.62342 1.000 21.29063 ? 222 VAL   A CG2 1 
ATOM   1801 N  N   . GLU   A 1 216 ? -16.92468 -26.16864 -13.66402 1.000 23.30122 ? 223 GLU   A N   1 
ATOM   1802 C  CA  . GLU   A 1 216 ? -16.71332 -27.49065 -14.22919 1.000 23.07092 ? 223 GLU   A CA  1 
ATOM   1803 C  C   . GLU   A 1 216 ? -17.83518 -28.44129 -13.84312 1.000 29.40240 ? 223 GLU   A C   1 
ATOM   1804 O  O   . GLU   A 1 216 ? -18.41550 -28.32685 -12.76439 1.000 30.22885 ? 223 GLU   A O   1 
ATOM   1805 C  CB  . GLU   A 1 216 ? -15.36636 -28.05695 -13.79729 1.000 28.31359 ? 223 GLU   A CB  1 
ATOM   1806 C  CG  . GLU   A 1 216 ? -14.23058 -27.10366 -14.09543 1.000 28.02623 ? 223 GLU   A CG  1 
ATOM   1807 C  CD  . GLU   A 1 216 ? -12.89847 -27.67203 -13.62317 1.000 32.49490 ? 223 GLU   A CD  1 
ATOM   1808 O  OE1 . GLU   A 1 216 ? -12.48549 -28.71829 -14.18274 1.000 29.19143 ? 223 GLU   A OE1 1 
ATOM   1809 O  OE2 . GLU   A 1 216 ? -12.28542 -27.06275 -12.70720 1.000 29.70756 ? 223 GLU   A OE2 1 
ATOM   1810 N  N   . LYS   A 1 217 ? -18.12947 -29.37725 -14.75239 1.000 29.21434 ? 224 LYS   A N   1 
ATOM   1811 C  CA  . LYS   A 1 217 ? -19.02876 -30.49764 -14.48394 1.000 38.68372 ? 224 LYS   A CA  1 
ATOM   1812 C  C   . LYS   A 1 217 ? -18.83415 -31.09034 -13.08763 1.000 47.69322 ? 224 LYS   A C   1 
ATOM   1813 O  O   . LYS   A 1 217 ? -17.73392 -31.51677 -12.74494 1.000 45.07247 ? 224 LYS   A O   1 
ATOM   1814 C  CB  . LYS   A 1 217 ? -18.82417 -31.60080 -15.52675 1.000 40.41033 ? 224 LYS   A CB  1 
ATOM   1815 C  CG  . LYS   A 1 217 ? -19.77486 -32.76755 -15.36726 1.000 57.08622 ? 224 LYS   A CG  1 
ATOM   1816 C  CD  . LYS   A 1 217 ? -19.77996 -33.68621 -16.59211 1.000 57.75148 ? 224 LYS   A CD  1 
ATOM   1817 C  CE  . LYS   A 1 217 ? -20.40738 -35.03303 -16.23589 1.000 60.78130 ? 224 LYS   A CE  1 
ATOM   1818 N  NZ  . LYS   A 1 217 ? -19.54693 -36.19442 -16.58818 1.000 58.79023 ? 224 LYS   A NZ  1 
HETATM 1819 C  C4  B A1AXQ B 2 .   ? 11.82186  -12.83448 -9.45633  0.265 34.67587 ? 301 A1AXQ A C4  1 
HETATM 1820 C  C6  B A1AXQ B 2 .   ? 10.77846  -14.48806 -8.05974  0.265 27.91819 ? 301 A1AXQ A C6  1 
HETATM 1821 C  C2  B A1AXQ B 2 .   ? 14.16996  -10.78255 -11.09001 0.265 37.63067 ? 301 A1AXQ A C2  1 
HETATM 1822 C  C9  B A1AXQ B 2 .   ? 10.60148  -12.62743 -10.08390 0.265 35.86136 ? 301 A1AXQ A C9  1 
HETATM 1823 C  C7  B A1AXQ B 2 .   ? 9.56392   -14.28536 -8.68722  0.265 30.36383 ? 301 A1AXQ A C7  1 
HETATM 1824 O  O1  B A1AXQ B 2 .   ? 12.93551  -11.35918 -11.03081 0.265 40.52514 ? 301 A1AXQ A O1  1 
HETATM 1825 C  C1  B A1AXQ B 2 .   ? 14.47971  -9.92085  -12.24401 0.265 35.50725 ? 301 A1AXQ A C1  1 
HETATM 1826 C  C3  B A1AXQ B 2 .   ? 12.99130  -12.06906 -9.86638  0.265 36.64079 ? 301 A1AXQ A C3  1 
HETATM 1827 C  C5  B A1AXQ B 2 .   ? 11.90342  -13.77423 -8.43500  0.265 29.67121 ? 301 A1AXQ A C5  1 
HETATM 1828 C  C8  B A1AXQ B 2 .   ? 9.49928   -13.34873 -9.69539  0.265 45.02393 ? 301 A1AXQ A C8  1 
HETATM 1829 N  N1  B A1AXQ B 2 .   ? 14.90646  -11.09423 -10.08584 0.265 39.60351 ? 301 A1AXQ A N1  1 
HETATM 1830 N  N2  B A1AXQ B 2 .   ? 14.12877  -11.94736 -9.27228  0.265 42.74766 ? 301 A1AXQ A N2  1 
HETATM 1831 BR BR1 B A1AXQ B 2 .   ? 7.84617   -13.03720 -10.57618 0.265 67.12135 ? 301 A1AXQ A BR1 1 
HETATM 1832 O  O   . HOH   C 3 .   ? 9.62654   -1.03745  -3.59444  1.000 44.87146 ? 401 HOH   A O   1 
HETATM 1833 O  O   . HOH   C 3 .   ? 9.12700   -3.29107  -20.28065 1.000 29.21168 ? 402 HOH   A O   1 
HETATM 1834 O  O   . HOH   C 3 .   ? -18.15424 -5.16819  -37.35536 1.000 50.72079 ? 403 HOH   A O   1 
HETATM 1835 O  O   . HOH   C 3 .   ? -12.15799 -25.95013 -3.59045  1.000 42.52110 ? 404 HOH   A O   1 
HETATM 1836 O  O   . HOH   C 3 .   ? 11.62565  -22.05125 -40.44830 1.000 42.86552 ? 405 HOH   A O   1 
HETATM 1837 O  O   . HOH   C 3 .   ? -8.13147  -22.63975 -30.18758 1.000 36.28637 ? 406 HOH   A O   1 
HETATM 1838 O  O   . HOH   C 3 .   ? 5.74899   -25.67579 -7.22204  1.000 34.45789 ? 407 HOH   A O   1 
HETATM 1839 O  O   . HOH   C 3 .   ? 2.14836   -15.75036 -41.14394 1.000 37.62006 ? 408 HOH   A O   1 
HETATM 1840 O  O   . HOH   C 3 .   ? 0.25912   -1.63013  -19.79915 1.000 34.86239 ? 409 HOH   A O   1 
HETATM 1841 O  O   . HOH   C 3 .   ? -12.99381 -7.28203  -11.94949 1.000 29.33302 ? 410 HOH   A O   1 
HETATM 1842 O  O   . HOH   C 3 .   ? 3.15380   -6.20309  -11.11460 1.000 21.84122 ? 411 HOH   A O   1 
HETATM 1843 O  O   . HOH   C 3 .   ? -2.88566  -3.18609  -35.32687 1.000 36.78723 ? 412 HOH   A O   1 
HETATM 1844 O  O   . HOH   C 3 .   ? 13.84900  -11.32865 -29.43416 1.000 37.00312 ? 413 HOH   A O   1 
HETATM 1845 O  O   . HOH   C 3 .   ? -4.38216  0.51356   -22.21335 1.000 30.00534 ? 414 HOH   A O   1 
HETATM 1846 O  O   . HOH   C 3 .   ? -16.27143 -25.56045 -17.98717 1.000 23.40380 ? 415 HOH   A O   1 
HETATM 1847 O  O   . HOH   C 3 .   ? 7.68817   -27.81486 -24.02756 1.000 30.38830 ? 416 HOH   A O   1 
HETATM 1848 O  O   . HOH   C 3 .   ? 0.87416   -29.69426 -16.10094 1.000 33.69717 ? 417 HOH   A O   1 
HETATM 1849 O  O   . HOH   C 3 .   ? 6.75559   -26.55003 -27.65942 1.000 27.56704 ? 418 HOH   A O   1 
HETATM 1850 O  O   . HOH   C 3 .   ? -1.61396  -29.07613 -5.91499  1.000 30.32609 ? 419 HOH   A O   1 
HETATM 1851 O  O   . HOH   C 3 .   ? 1.45541   -7.83673  -16.48157 1.000 18.38003 ? 420 HOH   A O   1 
HETATM 1852 O  O   . HOH   C 3 .   ? -2.79447  -6.13018  -6.36261  1.000 33.54875 ? 421 HOH   A O   1 
HETATM 1853 O  O   . HOH   C 3 .   ? -15.85590 0.31729   -30.40569 1.000 35.62270 ? 422 HOH   A O   1 
HETATM 1854 O  O   . HOH   C 3 .   ? 3.29397   -24.34641 -38.69754 1.000 34.02330 ? 423 HOH   A O   1 
HETATM 1855 O  O   . HOH   C 3 .   ? -20.57916 -20.92764 -9.42460  1.000 43.09114 ? 424 HOH   A O   1 
HETATM 1856 O  O   . HOH   C 3 .   ? -3.74886  -13.26037 -42.75059 1.000 40.73469 ? 425 HOH   A O   1 
HETATM 1857 O  O   . HOH   C 3 .   ? 15.44791  -12.32649 -7.04916  1.000 38.69040 ? 426 HOH   A O   1 
HETATM 1858 O  O   . HOH   C 3 .   ? 6.01395   -21.18488 -0.08598  1.000 23.93508 ? 427 HOH   A O   1 
HETATM 1859 O  O   . HOH   C 3 .   ? 1.21909   -26.61157 -2.82074  1.000 38.34297 ? 428 HOH   A O   1 
HETATM 1860 O  O   . HOH   C 3 .   ? -6.57902  -3.61650  -8.15522  1.000 40.83050 ? 429 HOH   A O   1 
HETATM 1861 O  O   . HOH   C 3 .   ? -2.51014  -10.70288 -26.58520 1.000 28.04127 ? 430 HOH   A O   1 
HETATM 1862 O  O   . HOH   C 3 .   ? 9.83720   -14.74722 -25.17412 1.000 19.11054 ? 431 HOH   A O   1 
HETATM 1863 O  O   . HOH   C 3 .   ? 3.60018   -7.72259  -36.55560 1.000 31.49382 ? 432 HOH   A O   1 
HETATM 1864 O  O   . HOH   C 3 .   ? -10.95769 -14.20935 -37.64130 1.000 30.13048 ? 433 HOH   A O   1 
HETATM 1865 O  O   . HOH   C 3 .   ? 7.71037   -18.88646 -6.52177  1.000 20.74163 ? 434 HOH   A O   1 
HETATM 1866 O  O   . HOH   C 3 .   ? -0.35479  -5.42445  -18.28166 1.000 26.98437 ? 435 HOH   A O   1 
HETATM 1867 O  O   . HOH   C 3 .   ? -16.29920 -12.75719 -19.77000 1.000 18.74923 ? 436 HOH   A O   1 
HETATM 1868 O  O   . HOH   C 3 .   ? -8.67503  -11.87038 -36.34253 1.000 25.23926 ? 437 HOH   A O   1 
HETATM 1869 O  O   . HOH   C 3 .   ? 9.94997   -23.88329 -9.23655  1.000 39.59391 ? 438 HOH   A O   1 
HETATM 1870 O  O   . HOH   C 3 .   ? 5.04749   -9.96469  -2.47048  1.000 38.42166 ? 439 HOH   A O   1 
HETATM 1871 O  O   . HOH   C 3 .   ? -14.52005 -7.11454  -14.36203 1.000 32.55342 ? 440 HOH   A O   1 
HETATM 1872 O  O   . HOH   C 3 .   ? -8.16627  1.94805   -36.43793 1.000 34.05237 ? 441 HOH   A O   1 
HETATM 1873 O  O   . HOH   C 3 .   ? 7.81778   -23.27340 -14.30307 1.000 26.67248 ? 442 HOH   A O   1 
HETATM 1874 O  O   . HOH   C 3 .   ? -19.86992 -13.00999 -16.51023 1.000 39.15432 ? 443 HOH   A O   1 
HETATM 1875 O  O   . HOH   C 3 .   ? -6.14031  -24.26308 -30.51397 1.000 52.69677 ? 444 HOH   A O   1 
HETATM 1876 O  O   . HOH   C 3 .   ? -0.89047  -11.39380 -3.06603  1.000 35.04228 ? 445 HOH   A O   1 
HETATM 1877 O  O   . HOH   C 3 .   ? 11.39054  -28.34147 -30.50923 1.000 30.61686 ? 446 HOH   A O   1 
HETATM 1878 O  O   . HOH   C 3 .   ? -0.15283  -5.71101  -38.48595 1.000 40.81832 ? 447 HOH   A O   1 
HETATM 1879 O  O   . HOH   C 3 .   ? 0.15024   -22.15628 -2.10521  1.000 35.64729 ? 448 HOH   A O   1 
HETATM 1880 O  O   . HOH   C 3 .   ? 3.03369   -20.46675 -2.85526  1.000 30.37497 ? 449 HOH   A O   1 
HETATM 1881 O  O   . HOH   C 3 .   ? -6.33585  -14.00073 0.87105   1.000 27.28086 ? 450 HOH   A O   1 
HETATM 1882 O  O   . HOH   C 3 .   ? 5.87577   -21.75065 -37.33389 1.000 31.09334 ? 451 HOH   A O   1 
HETATM 1883 O  O   . HOH   C 3 .   ? 0.91001   -21.10149 -4.73539  1.000 23.71990 ? 452 HOH   A O   1 
HETATM 1884 O  O   . HOH   C 3 .   ? 0.51337   -4.86340  -16.13205 1.000 36.60083 ? 453 HOH   A O   1 
HETATM 1885 O  O   . HOH   C 3 .   ? 0.70682   -26.78887 -37.56307 1.000 42.91927 ? 454 HOH   A O   1 
HETATM 1886 O  O   . HOH   C 3 .   ? -5.34151  -10.42875 -27.34018 1.000 17.44836 ? 455 HOH   A O   1 
HETATM 1887 O  O   . HOH   C 3 .   ? -9.27238  -2.24752  -17.54595 1.000 18.19216 ? 456 HOH   A O   1 
HETATM 1888 O  O   . HOH   C 3 .   ? -2.18671  -13.66780 -35.62596 1.000 19.46769 ? 457 HOH   A O   1 
HETATM 1889 O  O   . HOH   C 3 .   ? 6.66421   -29.72080 -20.24433 1.000 32.41026 ? 458 HOH   A O   1 
HETATM 1890 O  O   . HOH   C 3 .   ? -8.14457  -24.91380 -19.15912 1.000 18.14338 ? 459 HOH   A O   1 
HETATM 1891 O  O   . HOH   C 3 .   ? -13.19305 -0.80343  -20.39255 1.000 28.38533 ? 460 HOH   A O   1 
HETATM 1892 O  O   . HOH   C 3 .   ? -17.09994 -5.48169  -22.78449 1.000 25.23046 ? 461 HOH   A O   1 
HETATM 1893 O  O   . HOH   C 3 .   ? 9.14651   -26.47166 -17.07621 1.000 26.83947 ? 462 HOH   A O   1 
HETATM 1894 O  O   . HOH   C 3 .   ? 7.68509   1.29036   -14.77087 1.000 31.38563 ? 463 HOH   A O   1 
HETATM 1895 O  O   . HOH   C 3 .   ? 3.68275   -29.86554 -25.83103 1.000 37.57375 ? 464 HOH   A O   1 
HETATM 1896 O  O   . HOH   C 3 .   ? -6.94610  -28.00725 -21.36612 1.000 40.06072 ? 465 HOH   A O   1 
HETATM 1897 O  O   . HOH   C 3 .   ? -5.73285  -2.06823  -19.43513 1.000 20.19628 ? 466 HOH   A O   1 
HETATM 1898 O  O   . HOH   C 3 .   ? 11.58616  -27.38011 -34.73218 1.000 23.25498 ? 467 HOH   A O   1 
HETATM 1899 O  O   . HOH   C 3 .   ? -6.41632  -7.68715  -34.30104 1.000 20.44332 ? 468 HOH   A O   1 
HETATM 1900 O  O   . HOH   C 3 .   ? -13.80988 -14.98458 -30.46272 1.000 42.95176 ? 469 HOH   A O   1 
HETATM 1901 O  O   . HOH   C 3 .   ? 9.74828   -17.54297 -7.78000  1.000 19.90095 ? 470 HOH   A O   1 
HETATM 1902 O  O   . HOH   C 3 .   ? -3.56311  -10.86055 -24.02671 1.000 24.17927 ? 471 HOH   A O   1 
HETATM 1903 O  O   . HOH   C 3 .   ? -4.12341  -4.86406  -8.44946  1.000 33.93842 ? 472 HOH   A O   1 
HETATM 1904 O  O   . HOH   C 3 .   ? 14.09143  -15.86159 -2.08357  1.000 32.43150 ? 473 HOH   A O   1 
HETATM 1905 O  O   . HOH   C 3 .   ? 11.23884  -8.00363  -27.36560 1.000 20.48924 ? 474 HOH   A O   1 
HETATM 1906 O  O   . HOH   C 3 .   ? 18.26738  -7.27573  -20.24660 1.000 28.08829 ? 475 HOH   A O   1 
HETATM 1907 O  O   . HOH   C 3 .   ? 2.00380   -3.92594  -17.01840 1.000 36.96879 ? 476 HOH   A O   1 
HETATM 1908 O  O   . HOH   C 3 .   ? -5.80191  -31.31471 -11.71413 1.000 32.94964 ? 477 HOH   A O   1 
HETATM 1909 O  O   . HOH   C 3 .   ? -4.41207  -26.52106 -30.79553 1.000 51.25833 ? 478 HOH   A O   1 
HETATM 1910 O  O   . HOH   C 3 .   ? -8.02224  -3.98362  -10.75942 1.000 28.10741 ? 479 HOH   A O   1 
HETATM 1911 O  O   . HOH   C 3 .   ? -1.56757  -6.36317  -26.08810 1.000 21.48154 ? 480 HOH   A O   1 
HETATM 1912 O  O   . HOH   C 3 .   ? -4.26854  -4.30232  -37.11292 1.000 37.53566 ? 481 HOH   A O   1 
HETATM 1913 O  O   . HOH   C 3 .   ? -1.17474  -26.06677 -32.47313 1.000 38.15242 ? 482 HOH   A O   1 
HETATM 1914 O  O   . HOH   C 3 .   ? -14.36103 -22.04157 -33.74113 1.000 39.26445 ? 483 HOH   A O   1 
HETATM 1915 O  O   . HOH   C 3 .   ? -6.28392  -11.40728 -10.02427 1.000 22.22186 ? 484 HOH   A O   1 
HETATM 1916 O  O   . HOH   C 3 .   ? 0.32725   -14.95390 -1.39274  1.000 33.25539 ? 485 HOH   A O   1 
HETATM 1917 O  O   . HOH   C 3 .   ? -8.41402  4.70665   -33.50638 1.000 28.28154 ? 486 HOH   A O   1 
HETATM 1918 O  O   . HOH   C 3 .   ? -19.49290 -9.94524  -33.01761 1.000 38.90137 ? 487 HOH   A O   1 
HETATM 1919 O  O   . HOH   C 3 .   ? -12.43784 -27.90784 -30.15390 1.000 28.30202 ? 488 HOH   A O   1 
HETATM 1920 O  O   . HOH   C 3 .   ? -5.69702  -28.30750 -4.83208  1.000 40.45638 ? 489 HOH   A O   1 
HETATM 1921 O  O   . HOH   C 3 .   ? 10.72068  -25.59587 -26.74365 1.000 27.49685 ? 490 HOH   A O   1 
HETATM 1922 O  O   . HOH   C 3 .   ? 13.55623  -14.22834 -26.79060 1.000 18.72209 ? 491 HOH   A O   1 
HETATM 1923 O  O   . HOH   C 3 .   ? -3.33443  -21.11043 -0.58526  1.000 28.79299 ? 492 HOH   A O   1 
HETATM 1924 O  O   . HOH   C 3 .   ? -1.18256  -7.44683  -23.60140 1.000 21.52830 ? 493 HOH   A O   1 
HETATM 1925 O  O   . HOH   C 3 .   ? 8.550     -0.371    -17.358   1.000 33.78859 ? 494 HOH   A O   1 
HETATM 1926 O  O   . HOH   C 3 .   ? -2.31112  -24.83818 -1.15268  1.000 42.65564 ? 495 HOH   A O   1 
HETATM 1927 O  O   . HOH   C 3 .   ? -19.831   -19.442   -14.326   1.000 18.91883 ? 496 HOH   A O   1 
HETATM 1928 O  O   . HOH   C 3 .   ? -18.96292 -10.95234 -23.72335 1.000 29.15179 ? 497 HOH   A O   1 
HETATM 1929 O  O   . HOH   C 3 .   ? -7.12069  -22.84568 -36.49487 1.000 38.88453 ? 498 HOH   A O   1 
HETATM 1930 O  O   . HOH   C 3 .   ? 0.56908   -5.38932  -13.99825 1.000 33.69530 ? 499 HOH   A O   1 
HETATM 1931 O  O   . HOH   C 3 .   ? 18.04344  -19.35512 -24.62030 1.000 28.23929 ? 500 HOH   A O   1 
HETATM 1932 O  O   . HOH   C 3 .   ? -13.14017 -25.05305 -10.85094 1.000 29.50827 ? 501 HOH   A O   1 
HETATM 1933 O  O   . HOH   C 3 .   ? -12.70328 -27.11565 -34.94357 1.000 43.58128 ? 502 HOH   A O   1 
HETATM 1934 O  O   . HOH   C 3 .   ? 13.00683  -13.89506 -29.61749 1.000 25.95721 ? 503 HOH   A O   1 
HETATM 1935 O  O   . HOH   C 3 .   ? -14.67197 -22.80155 -11.43020 1.000 26.73136 ? 504 HOH   A O   1 
HETATM 1936 O  O   . HOH   C 3 .   ? 20.05096  -10.47101 -26.38213 1.000 37.29624 ? 505 HOH   A O   1 
HETATM 1937 O  O   . HOH   C 3 .   ? -7.77773  -28.36973 -7.97416  1.000 30.14169 ? 506 HOH   A O   1 
HETATM 1938 O  O   . HOH   C 3 .   ? 8.47061   -20.45150 -9.19211  1.000 27.23648 ? 507 HOH   A O   1 
HETATM 1939 O  O   . HOH   C 3 .   ? -2.15706  -0.52545  -18.59361 1.000 31.73731 ? 508 HOH   A O   1 
HETATM 1940 O  O   . HOH   C 3 .   ? 19.61225  -16.59559 -27.73939 1.000 33.33626 ? 509 HOH   A O   1 
HETATM 1941 O  O   . HOH   C 3 .   ? 15.40250  -20.30451 -18.65393 1.000 22.73155 ? 510 HOH   A O   1 
HETATM 1942 O  O   . HOH   C 3 .   ? -20.60560 -14.20854 -18.29532 1.000 37.51442 ? 511 HOH   A O   1 
HETATM 1943 O  O   . HOH   C 3 .   ? -13.82076 -17.09555 -2.69224  1.000 23.89618 ? 512 HOH   A O   1 
HETATM 1944 O  O   . HOH   C 3 .   ? -6.11807  -7.24762  -42.23414 1.000 45.55459 ? 513 HOH   A O   1 
HETATM 1945 O  O   . HOH   C 3 .   ? -14.15500 -12.73108 -7.78752  1.000 22.79851 ? 514 HOH   A O   1 
HETATM 1946 O  O   . HOH   C 3 .   ? 8.06493   -23.29667 -7.17301  1.000 33.64158 ? 515 HOH   A O   1 
HETATM 1947 O  O   . HOH   C 3 .   ? 14.36053  -16.01117 -30.72405 1.000 28.38942 ? 516 HOH   A O   1 
HETATM 1948 O  O   . HOH   C 3 .   ? -10.34317 -11.60909 -2.09775  1.000 20.91864 ? 517 HOH   A O   1 
HETATM 1949 O  O   . HOH   C 3 .   ? 8.58720   -16.19038 -39.57918 1.000 33.85356 ? 518 HOH   A O   1 
HETATM 1950 O  O   . HOH   C 3 .   ? -5.68982  -18.80658 -39.13473 1.000 32.93381 ? 519 HOH   A O   1 
HETATM 1951 O  O   . HOH   C 3 .   ? -5.39765  -7.73141  -13.11903 1.000 19.30173 ? 520 HOH   A O   1 
HETATM 1952 O  O   . HOH   C 3 .   ? -14.48734 -3.80336  -12.71572 1.000 40.76245 ? 521 HOH   A O   1 
HETATM 1953 O  O   . HOH   C 3 .   ? 5.48148   -29.25346 -8.44127  1.000 40.78156 ? 522 HOH   A O   1 
HETATM 1954 O  O   . HOH   C 3 .   ? -1.32049  -4.56084  -33.60109 1.000 36.89892 ? 523 HOH   A O   1 
HETATM 1955 O  O   . HOH   C 3 .   ? 4.10303   -24.17825 -30.69502 1.000 18.93852 ? 524 HOH   A O   1 
HETATM 1956 O  O   . HOH   C 3 .   ? -6.30416  -5.06659  -35.58097 1.000 22.11533 ? 525 HOH   A O   1 
HETATM 1957 O  O   . HOH   C 3 .   ? -13.52897 -26.50278 -18.08244 1.000 25.93187 ? 526 HOH   A O   1 
HETATM 1958 O  O   . HOH   C 3 .   ? 10.63876  -25.38132 -23.76177 1.000 21.24433 ? 527 HOH   A O   1 
HETATM 1959 O  O   . HOH   C 3 .   ? 10.35918  -21.26822 -6.95198  1.000 32.63754 ? 528 HOH   A O   1 
HETATM 1960 O  O   . HOH   C 3 .   ? -0.29947  -7.07672  -30.93024 1.000 30.34000 ? 529 HOH   A O   1 
HETATM 1961 O  O   . HOH   C 3 .   ? -10.809   -14.688   0.971     1.000 22.74516 ? 530 HOH   A O   1 
HETATM 1962 O  O   . HOH   C 3 .   ? 3.78758   -11.82180 -38.54781 1.000 23.19530 ? 531 HOH   A O   1 
HETATM 1963 O  O   . HOH   C 3 .   ? -14.28603 -11.81879 0.36187   1.000 36.95725 ? 532 HOH   A O   1 
HETATM 1964 O  O   . HOH   C 3 .   ? -10.27314 -0.62164  -19.92473 1.000 28.18325 ? 533 HOH   A O   1 
HETATM 1965 O  O   . HOH   C 3 .   ? 3.60272   -6.76378  -17.75879 1.000 22.47034 ? 534 HOH   A O   1 
HETATM 1966 O  O   . HOH   C 3 .   ? -16.11395 -3.06396  -21.17728 1.000 26.38376 ? 535 HOH   A O   1 
HETATM 1967 O  O   . HOH   C 3 .   ? -7.66510  -24.39089 -23.21568 1.000 26.65711 ? 536 HOH   A O   1 
HETATM 1968 O  O   . HOH   C 3 .   ? -4.24488  -13.94820 -0.90830  1.000 40.59281 ? 537 HOH   A O   1 
HETATM 1969 O  O   . HOH   C 3 .   ? 8.89213   -15.55786 -27.74097 1.000 17.75496 ? 538 HOH   A O   1 
HETATM 1970 O  O   . HOH   C 3 .   ? -17.19455 -28.72049 -17.35608 1.000 38.21984 ? 539 HOH   A O   1 
HETATM 1971 O  O   . HOH   C 3 .   ? -15.20230 -11.13412 -29.73464 1.000 26.03887 ? 540 HOH   A O   1 
HETATM 1972 O  O   . HOH   C 3 .   ? -3.39593  -3.17567  -40.48409 1.000 47.84491 ? 541 HOH   A O   1 
HETATM 1973 O  O   . HOH   C 3 .   ? -10.59721 -6.28350  -2.96332  1.000 40.47864 ? 542 HOH   A O   1 
HETATM 1974 O  O   . HOH   C 3 .   ? 4.03090   -9.25892  -20.27518 1.000 20.51393 ? 543 HOH   A O   1 
HETATM 1975 O  O   . HOH   C 3 .   ? -5.16667  -5.36010  -11.77244 1.000 33.97114 ? 544 HOH   A O   1 
HETATM 1976 O  O   . HOH   C 3 .   ? -1.86634  -25.78556 -4.70720  1.000 20.76206 ? 545 HOH   A O   1 
HETATM 1977 O  O   . HOH   C 3 .   ? -11.84099 -0.22913  -15.27052 1.000 32.84993 ? 546 HOH   A O   1 
HETATM 1978 O  O   . HOH   C 3 .   ? -11.79161 -7.55535  -38.36534 1.000 34.28356 ? 547 HOH   A O   1 
HETATM 1979 O  O   . HOH   C 3 .   ? -5.11265  -14.30452 -22.61526 1.000 16.60761 ? 548 HOH   A O   1 
HETATM 1980 O  O   . HOH   C 3 .   ? -10.21298 -15.01994 -28.30781 1.000 23.16431 ? 549 HOH   A O   1 
HETATM 1981 O  O   . HOH   C 3 .   ? -18.14491 -2.98327  -35.50578 1.000 44.45650 ? 550 HOH   A O   1 
HETATM 1982 O  O   . HOH   C 3 .   ? 4.42081   -19.43765 -40.60873 1.000 32.38362 ? 551 HOH   A O   1 
HETATM 1983 O  O   . HOH   C 3 .   ? -1.78212  -32.68749 -8.03136  1.000 46.57235 ? 552 HOH   A O   1 
HETATM 1984 O  O   . HOH   C 3 .   ? 6.84202   -29.57437 -30.00201 1.000 46.74000 ? 553 HOH   A O   1 
HETATM 1985 O  O   . HOH   C 3 .   ? 15.72610  -18.39487 -3.58599  1.000 28.29492 ? 554 HOH   A O   1 
HETATM 1986 O  O   . HOH   C 3 .   ? -17.85119 -3.66623  -28.82500 1.000 37.73351 ? 555 HOH   A O   1 
HETATM 1987 O  O   . HOH   C 3 .   ? 2.02691   -6.07138  -25.84989 1.000 31.90229 ? 556 HOH   A O   1 
HETATM 1988 O  O   . HOH   C 3 .   ? -6.67258  -4.95114  -39.03739 1.000 38.38813 ? 557 HOH   A O   1 
HETATM 1989 O  O   . HOH   C 3 .   ? -7.37532  1.24677   -19.38588 1.000 29.13812 ? 558 HOH   A O   1 
HETATM 1990 O  O   . HOH   C 3 .   ? -4.62743  0.51942   -30.37512 1.000 27.70736 ? 559 HOH   A O   1 
HETATM 1991 O  O   . HOH   C 3 .   ? -8.97690  -10.34059 -40.49907 1.000 41.01270 ? 560 HOH   A O   1 
HETATM 1992 O  O   . HOH   C 3 .   ? -17.68274 -15.28936 -13.06566 1.000 24.36175 ? 561 HOH   A O   1 
HETATM 1993 O  O   . HOH   C 3 .   ? -15.13047 -12.19151 -11.97358 1.000 31.35493 ? 562 HOH   A O   1 
HETATM 1994 O  O   . HOH   C 3 .   ? 7.45865   -4.65264  -22.22830 1.000 32.52644 ? 563 HOH   A O   1 
HETATM 1995 O  O   . HOH   C 3 .   ? -5.25535  -31.71658 -7.09401  1.000 43.86980 ? 564 HOH   A O   1 
HETATM 1996 O  O   . HOH   C 3 .   ? -17.80094 -18.83420 -11.27117 1.000 31.77926 ? 565 HOH   A O   1 
HETATM 1997 O  O   . HOH   C 3 .   ? -2.46491  -15.64956 -0.25592  1.000 33.15450 ? 566 HOH   A O   1 
HETATM 1998 O  O   . HOH   C 3 .   ? 13.67150  -20.55003 -20.74233 1.000 19.44739 ? 567 HOH   A O   1 
HETATM 1999 O  O   . HOH   C 3 .   ? 3.18629   -30.19336 -19.26131 1.000 41.67699 ? 568 HOH   A O   1 
HETATM 2000 O  O   . HOH   C 3 .   ? -1.18812  -27.32057 -34.95409 1.000 52.18493 ? 569 HOH   A O   1 
HETATM 2001 O  O   . HOH   C 3 .   ? 0.42099   -5.42302  -21.96106 1.000 32.85178 ? 570 HOH   A O   1 
HETATM 2002 O  O   . HOH   C 3 .   ? -15.85645 6.35236   -32.20477 1.000 42.90575 ? 571 HOH   A O   1 
HETATM 2003 O  O   . HOH   C 3 .   ? -7.66965  -13.61036 -41.01432 1.000 48.33682 ? 572 HOH   A O   1 
HETATM 2004 O  O   . HOH   C 3 .   ? -3.10979  -1.02195  -24.00410 1.000 22.76993 ? 573 HOH   A O   1 
HETATM 2005 O  O   . HOH   C 3 .   ? -1.21858  -29.92483 -17.94125 1.000 38.60145 ? 574 HOH   A O   1 
HETATM 2006 O  O   . HOH   C 3 .   ? 4.92241   -30.51006 -11.56513 1.000 37.72086 ? 575 HOH   A O   1 
HETATM 2007 O  O   . HOH   C 3 .   ? 12.46314  -27.48122 -19.48987 1.000 38.87692 ? 576 HOH   A O   1 
HETATM 2008 O  O   . HOH   C 3 .   ? -4.04071  -3.39822  -15.29233 1.000 35.30501 ? 577 HOH   A O   1 
HETATM 2009 O  O   . HOH   C 3 .   ? 13.76651  -3.98185  -25.32671 1.000 18.89438 ? 578 HOH   A O   1 
HETATM 2010 O  O   . HOH   C 3 .   ? 15.48507  -0.65684  -19.53853 1.000 36.50299 ? 579 HOH   A O   1 
HETATM 2011 O  O   . HOH   C 3 .   ? -16.16577 -25.57979 -10.86229 1.000 32.50638 ? 580 HOH   A O   1 
HETATM 2012 O  O   . HOH   C 3 .   ? 17.09130  -24.82237 -25.40236 1.000 30.50324 ? 581 HOH   A O   1 
HETATM 2013 O  O   . HOH   C 3 .   ? 13.33442  -6.79901  -26.21455 1.000 21.73113 ? 582 HOH   A O   1 
HETATM 2014 O  O   . HOH   C 3 .   ? 16.52028  -27.54931 -22.62709 1.000 36.27303 ? 583 HOH   A O   1 
HETATM 2015 O  O   . HOH   C 3 .   ? 1.19174   -8.72221  -26.78248 1.000 26.98605 ? 584 HOH   A O   1 
HETATM 2016 O  O   . HOH   C 3 .   ? 11.45093  -1.71598  -20.37671 1.000 30.22233 ? 585 HOH   A O   1 
HETATM 2017 O  O   . HOH   C 3 .   ? -8.91856  -17.83689 -36.59715 1.000 36.37602 ? 586 HOH   A O   1 
HETATM 2018 O  O   . HOH   C 3 .   ? -13.67119 -31.09753 -12.85181 1.000 44.87129 ? 587 HOH   A O   1 
HETATM 2019 O  O   . HOH   C 3 .   ? 9.80884   -11.00862 -34.78632 1.000 35.32789 ? 588 HOH   A O   1 
HETATM 2020 O  O   . HOH   C 3 .   ? -3.52179  -13.21556 -20.65569 1.000 19.86182 ? 589 HOH   A O   1 
HETATM 2021 O  O   . HOH   C 3 .   ? 0.99958   -5.99095  -34.12232 1.000 36.90368 ? 590 HOH   A O   1 
HETATM 2022 O  O   . HOH   C 3 .   ? -18.68518 -12.33812 -13.86693 1.000 53.13717 ? 591 HOH   A O   1 
HETATM 2023 O  O   . HOH   C 3 .   ? 3.15933   -4.88208  -28.93423 1.000 38.56190 ? 592 HOH   A O   1 
HETATM 2024 O  O   . HOH   C 3 .   ? 20.84643  -14.16379 -26.74542 1.000 31.43606 ? 593 HOH   A O   1 
HETATM 2025 O  O   . HOH   C 3 .   ? -18.12334 -5.84662  -25.48093 1.000 35.18457 ? 594 HOH   A O   1 
HETATM 2026 O  O   . HOH   C 3 .   ? -12.27262 -32.09134 -19.20629 1.000 50.22353 ? 595 HOH   A O   1 
HETATM 2027 O  O   . HOH   C 3 .   ? 1.45192   -3.11675  -24.31117 1.000 33.61998 ? 596 HOH   A O   1 
HETATM 2028 O  O   . HOH   C 3 .   ? 8.69946   -20.57832 -4.29775  1.000 23.25222 ? 597 HOH   A O   1 
HETATM 2029 O  O   . HOH   C 3 .   ? 13.921    0.841     -13.576   1.000 29.10500 ? 598 HOH   A O   1 
HETATM 2030 O  O   . HOH   C 3 .   ? -16.63442 -9.17869  -14.23420 1.000 34.36759 ? 599 HOH   A O   1 
HETATM 2031 O  O   . HOH   C 3 .   ? 0.06509   -16.77317 -3.47875  1.000 20.83099 ? 600 HOH   A O   1 
HETATM 2032 O  O   . HOH   C 3 .   ? 8.52120   -19.89893 -41.50949 1.000 42.30045 ? 601 HOH   A O   1 
HETATM 2033 O  O   . HOH   C 3 .   ? -14.12985 -24.07503 -4.79684  1.000 27.44511 ? 602 HOH   A O   1 
HETATM 2034 O  O   . HOH   C 3 .   ? -13.67787 -25.97245 -7.83303  1.000 25.59742 ? 603 HOH   A O   1 
HETATM 2035 O  O   . HOH   C 3 .   ? -1.43815  -8.61664  -27.75299 1.000 25.19133 ? 604 HOH   A O   1 
HETATM 2036 O  O   . HOH   C 3 .   ? -9.56525  -13.20162 -39.95315 1.000 46.79394 ? 605 HOH   A O   1 
HETATM 2037 O  O   . HOH   C 3 .   ? -13.08314 -12.30380 -30.98804 1.000 25.21413 ? 606 HOH   A O   1 
HETATM 2038 O  O   . HOH   C 3 .   ? -0.44315  -12.49287 -21.46060 1.000 28.99290 ? 607 HOH   A O   1 
HETATM 2039 O  O   . HOH   C 3 .   ? -7.48267  7.50110   -33.71245 1.000 36.43966 ? 608 HOH   A O   1 
HETATM 2040 O  O   . HOH   C 3 .   ? -14.59611 -29.45488 -9.62390  1.000 43.81106 ? 609 HOH   A O   1 
HETATM 2041 O  O   . HOH   C 3 .   ? -13.81294 -18.64110 -24.47994 1.000 19.90183 ? 610 HOH   A O   1 
HETATM 2042 O  O   . HOH   C 3 .   ? 8.073     -8.536    -0.071    1.000 41.92953 ? 611 HOH   A O   1 
HETATM 2043 O  O   . HOH   C 3 .   ? -7.334    -1.908    -12.602   1.000 35.46154 ? 612 HOH   A O   1 
HETATM 2044 O  O   . HOH   C 3 .   ? -12.40572 -26.96978 -20.39261 1.000 25.77306 ? 613 HOH   A O   1 
HETATM 2045 O  O   . HOH   C 3 .   ? -14.25553 -16.20911 -26.12377 1.000 25.79904 ? 614 HOH   A O   1 
HETATM 2046 O  O   . HOH   C 3 .   ? 20.15812  -5.46991  -14.85870 1.000 48.93891 ? 615 HOH   A O   1 
HETATM 2047 O  O   . HOH   C 3 .   ? 15.43513  -7.28050  -27.83197 1.000 32.19684 ? 616 HOH   A O   1 
HETATM 2048 O  O   . HOH   C 3 .   ? 5.61653   -3.34533  -26.13525 1.000 35.85091 ? 617 HOH   A O   1 
HETATM 2049 O  O   . HOH   C 3 .   ? 8.04693   -30.10633 -37.37126 1.000 51.52323 ? 618 HOH   A O   1 
HETATM 2050 O  O   . HOH   C 3 .   ? -7.92192  -24.20056 -25.91400 1.000 43.88955 ? 619 HOH   A O   1 
HETATM 2051 O  O   . HOH   C 3 .   ? -9.231    -24.520   3.333     1.000 51.86936 ? 620 HOH   A O   1 
HETATM 2052 O  O   . HOH   C 3 .   ? 19.16049  0.49150   -9.47010  1.000 49.69543 ? 621 HOH   A O   1 
HETATM 2053 O  O   . HOH   C 3 .   ? -18.59401 -33.89299 -10.88962 1.000 57.78413 ? 622 HOH   A O   1 
HETATM 2054 O  O   . HOH   C 3 .   ? 2.99984   -6.67731  -20.40766 1.000 33.64964 ? 623 HOH   A O   1 
HETATM 2055 O  O   . HOH   C 3 .   ? -16.00679 -3.96892  -15.31309 1.000 52.00831 ? 624 HOH   A O   1 
HETATM 2056 O  O   . HOH   C 3 .   ? 3.91708   -23.10970 -3.33297  1.000 36.01619 ? 625 HOH   A O   1 
HETATM 2057 O  O   . HOH   C 3 .   ? -3.86658  -33.00950 -11.02528 1.000 42.42407 ? 626 HOH   A O   1 
HETATM 2058 O  O   . HOH   C 3 .   ? -5.50620  -12.01213 -42.07486 1.000 43.66472 ? 627 HOH   A O   1 
HETATM 2059 O  O   . HOH   C 3 .   ? -18.11112 -10.30977 -14.47336 1.000 62.02657 ? 628 HOH   A O   1 
HETATM 2060 O  O   . HOH   C 3 .   ? 10.62093  -17.52034 -38.80616 1.000 41.60552 ? 629 HOH   A O   1 
HETATM 2061 O  O   . HOH   C 3 .   ? -2.06962  -26.88589 -24.90610 1.000 35.33651 ? 630 HOH   A O   1 
HETATM 2062 O  O   . HOH   C 3 .   ? 22.248    -13.294   -19.572   1.000 43.12746 ? 631 HOH   A O   1 
HETATM 2063 O  O   . HOH   C 3 .   ? -12.37958 -20.48078 -29.67332 1.000 40.88984 ? 632 HOH   A O   1 
HETATM 2064 O  O   . HOH   C 3 .   ? 1.862     -18.555   0.150     1.000 28.62127 ? 633 HOH   A O   1 
HETATM 2065 O  O   . HOH   C 3 .   ? 2.59752   -10.05288 -23.09958 1.000 25.81283 ? 634 HOH   A O   1 
HETATM 2066 O  O   . HOH   C 3 .   ? 4.38323   -21.82828 -39.32023 1.000 41.30184 ? 635 HOH   A O   1 
HETATM 2067 O  O   . HOH   C 3 .   ? -18.88372 -11.61010 -15.88314 1.000 53.41534 ? 636 HOH   A O   1 
HETATM 2068 O  O   . HOH   C 3 .   ? 8.16384   -25.98104 -25.89185 1.000 30.33069 ? 637 HOH   A O   1 
HETATM 2069 O  O   . HOH   C 3 .   ? -5.865    -11.174   1.184     1.000 52.46637 ? 638 HOH   A O   1 
HETATM 2070 O  O   . HOH   C 3 .   ? -17.18424 -4.78846  -17.45838 1.000 34.56427 ? 639 HOH   A O   1 
HETATM 2071 O  O   . HOH   C 3 .   ? 17.92894  -15.21650 -29.57859 1.000 52.17140 ? 640 HOH   A O   1 
HETATM 2072 O  O   . HOH   C 3 .   ? 4.65182   -1.89065  -18.24547 1.000 31.48128 ? 641 HOH   A O   1 
HETATM 2073 O  O   . HOH   C 3 .   ? 4.04359   -4.82619  -22.07909 1.000 44.07248 ? 642 HOH   A O   1 
HETATM 2074 O  O   . HOH   C 3 .   ? 1.85448   -25.87993 -29.31975 1.000 34.32988 ? 643 HOH   A O   1 
HETATM 2075 O  O   . HOH   C 3 .   ? -14.15759 -29.12641 -17.25075 1.000 44.49601 ? 644 HOH   A O   1 
HETATM 2076 O  O   . HOH   C 3 .   ? -12.31630 -16.36465 -28.26002 1.000 31.75984 ? 645 HOH   A O   1 
HETATM 2077 O  O   . HOH   C 3 .   ? 14.46779  -22.14512 -17.09294 1.000 33.66173 ? 646 HOH   A O   1 
HETATM 2078 O  O   . HOH   C 3 .   ? -14.01752 -14.32901 -3.08821  1.000 30.34556 ? 647 HOH   A O   1 
HETATM 2079 O  O   . HOH   C 3 .   ? 0.01469   -19.20500 -1.97895  1.000 31.57852 ? 648 HOH   A O   1 
HETATM 2080 O  O   . HOH   C 3 .   ? 17.66772  -21.58923 -19.80348 1.000 34.61163 ? 649 HOH   A O   1 
HETATM 2081 O  O   . HOH   C 3 .   ? -9.33024  -5.77824  -39.64307 1.000 35.79647 ? 650 HOH   A O   1 
HETATM 2082 O  O   . HOH   C 3 .   ? -1.60087  -5.53244  -12.13224 1.000 40.18643 ? 651 HOH   A O   1 
HETATM 2083 O  O   . HOH   C 3 .   ? 1.72378   -3.46551  -12.56263 1.000 42.00524 ? 652 HOH   A O   1 
HETATM 2084 O  O   . HOH   C 3 .   ? 3.42027   -7.92396  -2.07619  1.000 45.37473 ? 653 HOH   A O   1 
HETATM 2085 O  O   . HOH   C 3 .   ? -14.22229 -9.88337  -8.33158  1.000 33.59907 ? 654 HOH   A O   1 
HETATM 2086 O  O   . HOH   C 3 .   ? 14.86833  -7.99414  -30.13273 1.000 36.65310 ? 655 HOH   A O   1 
HETATM 2087 O  O   . HOH   C 3 .   ? -0.47672  -1.27772  -22.99954 1.000 34.26620 ? 656 HOH   A O   1 
HETATM 2088 O  O   . HOH   C 3 .   ? -6.21412  3.85667   -34.57944 1.000 38.95257 ? 657 HOH   A O   1 
HETATM 2089 O  O   . HOH   C 3 .   ? 3.80740   -0.26717  -16.51006 1.000 33.49640 ? 658 HOH   A O   1 
HETATM 2090 O  O   . HOH   C 3 .   ? 12.31021  -25.20410 -38.45669 1.000 30.30333 ? 659 HOH   A O   1 
HETATM 2091 O  O   . HOH   C 3 .   ? 5.507     1.790     -16.558   1.000 31.77711 ? 660 HOH   A O   1 
HETATM 2092 O  O   . HOH   C 3 .   ? -3.48748  -27.13538 -3.13491  1.000 40.37458 ? 661 HOH   A O   1 
HETATM 2093 O  O   . HOH   C 3 .   ? 19.01555  -8.49650  -17.78416 1.000 32.74508 ? 662 HOH   A O   1 
HETATM 2094 O  O   . HOH   C 3 .   ? -7.89324  -21.06654 -37.55718 1.000 43.96019 ? 663 HOH   A O   1 
HETATM 2095 O  O   . HOH   C 3 .   ? -11.62482 -9.60286  -39.53621 1.000 45.04908 ? 664 HOH   A O   1 
HETATM 2096 O  O   . HOH   C 3 .   ? 3.52046   -9.02233  -39.01956 1.000 39.57153 ? 665 HOH   A O   1 
HETATM 2097 O  O   . HOH   C 3 .   ? 7.81267   -13.79776 -38.21453 1.000 31.04219 ? 666 HOH   A O   1 
HETATM 2098 O  O   . HOH   C 3 .   ? -9.89632  -26.08151 -20.93608 1.000 28.72172 ? 667 HOH   A O   1 
HETATM 2099 O  O   . HOH   C 3 .   ? 6.11171   -30.04150 -24.98738 1.000 40.96406 ? 668 HOH   A O   1 
HETATM 2100 O  O   . HOH   C 3 .   ? -16.31955 -34.29675 -10.37347 1.000 58.33191 ? 669 HOH   A O   1 
HETATM 2101 O  O   . HOH   C 3 .   ? -18.65145 -11.67679 -21.14582 1.000 31.33322 ? 670 HOH   A O   1 
HETATM 2102 O  O   . HOH   C 3 .   ? -6.256    6.754     -35.724   1.000 39.43102 ? 671 HOH   A O   1 
HETATM 2103 O  O   . HOH   C 3 .   ? -10.54599 -8.81992  -1.47185  1.000 35.29909 ? 672 HOH   A O   1 
HETATM 2104 O  O   . HOH   C 3 .   ? -4.26693  -29.91365 -22.33477 1.000 44.08724 ? 673 HOH   A O   1 
HETATM 2105 O  O   . HOH   C 3 .   ? 10.44920  -21.18656 -43.04788 1.000 46.75258 ? 674 HOH   A O   1 
HETATM 2106 O  O   . HOH   C 3 .   ? 2.819     -4.859    -20.146   1.000 40.31732 ? 675 HOH   A O   1 
HETATM 2107 O  O   . HOH   C 3 .   ? 16.95855  0.57653   -17.74285 1.000 42.29150 ? 676 HOH   A O   1 
HETATM 2108 O  O   . HOH   C 3 .   ? 1.59233   -7.57716  -23.12465 1.000 36.62676 ? 677 HOH   A O   1 
HETATM 2109 O  O   . HOH   C 3 .   ? 5.55925   -3.24691  -23.49649 1.000 37.29817 ? 678 HOH   A O   1 
HETATM 2110 O  O   . HOH   C 3 .   ? -19.43405 -2.33373  -37.80703 1.000 47.53320 ? 679 HOH   A O   1 
HETATM 2111 O  O   . HOH   C 3 .   ? -16.51630 -5.59598  -13.43935 1.000 47.27700 ? 680 HOH   A O   1 
HETATM 2112 O  O   . HOH   C 3 .   ? -22.105   -34.714   -13.781   1.000 46.32859 ? 681 HOH   A O   1 
HETATM 2113 O  O   . HOH   C 3 .   ? -11.78794 -19.43769 -28.12218 1.000 45.50256 ? 682 HOH   A O   1 
HETATM 2114 O  O   . HOH   C 3 .   ? 5.74982   -12.96560 -39.81495 1.000 31.30125 ? 683 HOH   A O   1 
HETATM 2115 O  O   . HOH   C 3 .   ? 6.53229   -21.59978 -2.73119  1.000 29.28808 ? 684 HOH   A O   1 
HETATM 2116 O  O   . HOH   C 3 .   ? 2.25598   -0.72370  -14.30318 1.000 45.55745 ? 685 HOH   A O   1 
HETATM 2117 O  O   . HOH   C 3 .   ? 12.11328  -9.98394  -1.57196  1.000 52.38456 ? 686 HOH   A O   1 
HETATM 2118 O  O   . HOH   C 3 .   ? 9.95226   -29.41564 -23.97113 1.000 40.57162 ? 687 HOH   A O   1 
HETATM 2119 O  O   . HOH   C 3 .   ? 17.34524  -16.99510 -4.84643  1.000 45.49784 ? 688 HOH   A O   1 
HETATM 2120 O  O   . HOH   C 3 .   ? 2.368     -0.857    -25.892   1.000 34.22481 ? 689 HOH   A O   1 
HETATM 2121 O  O   . HOH   C 3 .   ? -7.06593  -30.87324 -9.22151  1.000 32.08307 ? 690 HOH   A O   1 
HETATM 2122 O  O   . HOH   C 3 .   ? 7.86778   -29.03290 -28.24835 1.000 39.42972 ? 691 HOH   A O   1 
HETATM 2123 O  O   . HOH   C 3 .   ? -10.53497 -22.88741 -24.34771 1.000 41.94990 ? 692 HOH   A O   1 
HETATM 2124 O  O   . HOH   C 3 .   ? 10.54556  -22.62192 -4.47750  1.000 39.73723 ? 693 HOH   A O   1 
HETATM 2125 O  O   . HOH   C 3 .   ? 16.028    1.643     -15.254   1.000 39.01957 ? 694 HOH   A O   1 
HETATM 2126 O  O   . HOH   C 3 .   ? -4.99857  -25.30197 -1.24894  1.000 43.39133 ? 695 HOH   A O   1 
HETATM 2127 O  O   . HOH   C 3 .   ? 10.85827  -28.01323 -27.84497 1.000 36.34050 ? 696 HOH   A O   1 
HETATM 2128 O  O   . HOH   C 3 .   ? 13.72472  -11.73100 -5.03305  1.000 34.47012 ? 697 HOH   A O   1 
HETATM 2129 O  O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.39406 0.50  25.82200 ? 698 HOH   A O   1 
HETATM 2130 O  O   . HOH   C 3 .   ? 0.62835   -16.56205 -43.50436 1.000 45.32613 ? 699 HOH   A O   1 
HETATM 2131 O  O   . HOH   C 3 .   ? -1.99076  -23.12521 0.89196   1.000 40.84909 ? 700 HOH   A O   1 
HETATM 2132 O  O   . HOH   C 3 .   ? 4.76630   -14.87243 -41.51690 1.000 35.49170 ? 701 HOH   A O   1 
HETATM 2133 O  O   . HOH   C 3 .   ? 11.485    -30.068   -34.346   1.000 33.94668 ? 702 HOH   A O   1 
HETATM 2134 O  O   . HOH   C 3 .   ? -0.52182  -26.53982 -30.11621 1.000 40.72199 ? 703 HOH   A O   1 
HETATM 2135 O  O   . HOH   C 3 .   ? -6.711    -23.210   -1.751    1.000 37.20657 ? 704 HOH   A O   1 
HETATM 2136 O  O   . HOH   C 3 .   ? 20.50078  -5.91552  -21.00908 1.000 33.40331 ? 705 HOH   A O   1 
HETATM 2137 O  O   . HOH   C 3 .   ? -16.297   3.140     -26.336   1.000 33.97161 ? 706 HOH   A O   1 
HETATM 2138 O  O   . HOH   C 3 .   ? -17.10533 4.08634   -31.57277 1.000 45.09124 ? 707 HOH   A O   1 
HETATM 2139 O  O   . HOH   C 3 .   ? -10.14037 -29.04737 -30.92712 1.000 43.14134 ? 708 HOH   A O   1 
HETATM 2140 O  O   . HOH   C 3 .   ? 20.950    -18.323   -22.057   1.000 39.63557 ? 709 HOH   A O   1 
HETATM 2141 O  O   . HOH   C 3 .   ? -16.20711 -12.60316 -6.09899  1.000 38.75667 ? 710 HOH   A O   1 
HETATM 2142 O  O   . HOH   C 3 .   ? -6.90699  -31.47155 -4.78498  1.000 55.61217 ? 711 HOH   A O   1 
HETATM 2143 O  O   . HOH   C 3 .   ? -0.27053  -27.00894 -1.17628  1.000 48.35295 ? 712 HOH   A O   1 
HETATM 2144 O  O   . HOH   C 3 .   ? -13.78708 -13.82581 -38.12958 1.000 41.55341 ? 713 HOH   A O   1 
HETATM 2145 O  O   . HOH   C 3 .   ? -6.71812  -26.78734 -23.28290 1.000 52.45589 ? 714 HOH   A O   1 
HETATM 2146 O  O   . HOH   C 3 .   ? 1.95243   -32.26037 -26.76040 1.000 53.75749 ? 715 HOH   A O   1 
HETATM 2147 O  O   . HOH   C 3 .   ? 1.81779   -5.76963  -36.48914 1.000 40.63132 ? 716 HOH   A O   1 
HETATM 2148 O  O   . HOH   C 3 .   ? 14.29978  -13.20163 -2.94908  1.000 40.96520 ? 717 HOH   A O   1 
HETATM 2149 O  O   . HOH   C 3 .   ? 9.62832   -25.27388 -14.84808 1.000 37.52306 ? 718 HOH   A O   1 
HETATM 2150 O  O   . HOH   C 3 .   ? 20.58213  -7.35335  -15.75549 1.000 44.97968 ? 719 HOH   A O   1 
HETATM 2151 O  O   . HOH   C 3 .   ? -4.32900  -28.13785 -23.46022 1.000 37.99475 ? 720 HOH   A O   1 
HETATM 2152 O  O   . HOH   C 3 .   ? 8.719     -10.809   -0.041    1.000 42.78005 ? 721 HOH   A O   1 
HETATM 2153 O  O   . HOH   C 3 .   ? -11.99474 -20.52189 -25.41848 1.000 36.35889 ? 722 HOH   A O   1 
HETATM 2154 O  O   . HOH   C 3 .   ? -3.16459  2.13255   -20.49206 1.000 39.41636 ? 723 HOH   A O   1 
HETATM 2155 O  O   . HOH   C 3 .   ? 0.60965   -1.34022  -16.78973 1.000 32.74973 ? 724 HOH   A O   1 
HETATM 2156 O  O   . HOH   C 3 .   ? -16.24827 -13.47351 -3.82896  1.000 37.75745 ? 725 HOH   A O   1 
HETATM 2157 O  O   . HOH   C 3 .   ? 4.064     -1.947    -28.075   1.000 33.42465 ? 726 HOH   A O   1 
HETATM 2158 O  O   . HOH   C 3 .   ? 14.90173  -17.13532 0.29220   1.000 35.10078 ? 727 HOH   A O   1 
HETATM 2159 O  O   . HOH   C 3 .   ? -16.93800 -15.75833 -10.35332 1.000 33.97568 ? 728 HOH   A O   1 
HETATM 2160 O  O   . HOH   C 3 .   ? -20.71838 -10.77709 -19.61290 1.000 42.43663 ? 729 HOH   A O   1 
HETATM 2161 O  O   . HOH   C 3 .   ? -12.40409 -13.24091 -0.99555  1.000 27.87323 ? 730 HOH   A O   1 
HETATM 2162 O  O   . HOH   C 3 .   ? 4.568     2.994     -12.933   1.000 45.66938 ? 731 HOH   A O   1 
HETATM 2163 O  O   . HOH   C 3 .   ? -20.48674 -10.35542 -16.74837 1.000 50.78153 ? 732 HOH   A O   1 
HETATM 2164 O  O   . HOH   C 3 .   ? 3.958     -3.293    -33.852   1.000 44.33691 ? 733 HOH   A O   1 
HETATM 2165 O  O   . HOH   C 3 .   ? 20.635    -20.338   -26.627   1.000 39.82034 ? 734 HOH   A O   1 
HETATM 2166 O  O   . HOH   C 3 .   ? -10.489   -11.996   2.013     1.000 33.69141 ? 735 HOH   A O   1 
HETATM 2167 O  O   . HOH   C 3 .   ? 19.34562  -20.41579 -22.25985 1.000 32.99399 ? 736 HOH   A O   1 
HETATM 2168 O  O   . HOH   C 3 .   ? -16.88718 -9.65538  -5.78660  1.000 50.59841 ? 737 HOH   A O   1 
HETATM 2169 O  O   . HOH   C 3 .   ? -14.53430 -14.08988 -10.28904 1.000 28.08701 ? 738 HOH   A O   1 
HETATM 2170 O  O   . HOH   C 3 .   ? 17.21465  -4.87644  -28.06445 1.000 42.63562 ? 739 HOH   A O   1 
HETATM 2171 O  O   . HOH   C 3 .   ? -19.15098 -8.21126  -15.13186 1.000 57.71205 ? 740 HOH   A O   1 
HETATM 2172 O  O   . HOH   C 3 .   ? -2.89604  -26.40121 -27.45771 1.000 42.68613 ? 741 HOH   A O   1 
HETATM 2173 O  O   . HOH   C 3 .   ? -14.61375 -9.44680  -11.30867 1.000 33.67528 ? 742 HOH   A O   1 
HETATM 2174 O  O   . HOH   C 3 .   ? -19.62797 -5.94751  -21.57347 1.000 38.80239 ? 743 HOH   A O   1 
HETATM 2175 O  O   . HOH   C 3 .   ? 9.98094   -12.70451 -36.98320 1.000 42.62798 ? 744 HOH   A O   1 
HETATM 2176 O  O   . HOH   C 3 .   ? -9.692    9.183     -38.330   1.000 38.78819 ? 745 HOH   A O   1 
HETATM 2177 O  O   . HOH   C 3 .   ? -9.04628  -32.78372 -8.77041  1.000 44.97214 ? 746 HOH   A O   1 
HETATM 2178 O  O   . HOH   C 3 .   ? -6.454    7.956     -39.243   1.000 48.51091 ? 747 HOH   A O   1 
HETATM 2179 O  O   . HOH   C 3 .   ? -9.89935  -20.74661 -39.54825 1.000 46.23310 ? 748 HOH   A O   1 
HETATM 2180 O  O   . HOH   C 3 .   ? -22.97068 -12.15111 -20.28714 1.000 49.60345 ? 749 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   ? 0.58412 0.58671 0.57930 0.04243  -0.03578 -0.09039 16  GLU A N   
2    C CA  . GLU A 9   ? 0.64844 0.65032 0.63958 0.04555  -0.03193 -0.08806 16  GLU A CA  
3    C C   . GLU A 9   ? 0.52291 0.52815 0.51497 0.04227  -0.02933 -0.08268 16  GLU A C   
4    O O   . GLU A 9   ? 0.48166 0.49061 0.47025 0.04192  -0.02811 -0.08196 16  GLU A O   
5    C CB  . GLU A 9   ? 0.73768 0.74008 0.72060 0.05139  -0.03036 -0.09119 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.90187 0.90108 0.88158 0.05626  -0.02742 -0.09101 16  GLU A CG  
7    C CD  . GLU A 9   ? 0.92768 0.92828 0.90716 0.05587  -0.02314 -0.08600 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.00377 1.00780 0.98521 0.05182  -0.02248 -0.08278 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.00540 1.00359 0.98304 0.05967  -0.02038 -0.08532 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.38823 0.39230 0.38482 0.04010  -0.02843 -0.07900 17  VAL A N   
11   C CA  . VAL A 10  ? 0.29679 0.30410 0.29539 0.03639  -0.02685 -0.07420 17  VAL A CA  
12   C C   . VAL A 10  ? 0.29844 0.30563 0.29534 0.03859  -0.02326 -0.07182 17  VAL A C   
13   O O   . VAL A 10  ? 0.32374 0.32761 0.32212 0.04069  -0.02279 -0.07191 17  VAL A O   
14   C CB  . VAL A 10  ? 0.32932 0.33610 0.33519 0.03191  -0.02895 -0.07161 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.33704 0.34741 0.34434 0.02856  -0.02738 -0.06673 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.39150 0.39805 0.40028 0.02979  -0.03230 -0.07400 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.25041 0.26110 0.24460 0.03816  -0.02062 -0.06975 18  GLU A N   
18   C CA  . GLU A 11  ? 0.22846 0.23956 0.22202 0.03981  -0.01704 -0.06741 18  GLU A CA  
19   C C   . GLU A 11  ? 0.22753 0.24118 0.22566 0.03537  -0.01702 -0.06331 18  GLU A C   
20   O O   . GLU A 11  ? 0.21219 0.22886 0.21075 0.03187  -0.01800 -0.06210 18  GLU A O   
21   C CB  . GLU A 11  ? 0.22707 0.24029 0.21495 0.04265  -0.01375 -0.06810 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.25065 0.26143 0.23334 0.04823  -0.01314 -0.07185 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.34779 0.36089 0.32498 0.05128  -0.00952 -0.07206 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.36253 0.37875 0.33772 0.04952  -0.00993 -0.07228 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.43311 0.44486 0.40807 0.05565  -0.00602 -0.07186 18  GLU A OE2 
26   N N   . THR A 12  ? 0.20760 0.22017 0.20907 0.03572  -0.01598 -0.06119 19  THR A N   
27   C CA  . THR A 12  ? 0.19418 0.20942 0.19994 0.03204  -0.01614 -0.05745 19  THR A CA  
28   C C   . THR A 12  ? 0.21391 0.23110 0.21909 0.03328  -0.01265 -0.05603 19  THR A C   
29   O O   . THR A 12  ? 0.20223 0.21718 0.20686 0.03697  -0.01045 -0.05668 19  THR A O   
30   C CB  . THR A 12  ? 0.19092 0.20386 0.20196 0.03120  -0.01797 -0.05593 19  THR A CB  
31   O OG1 . THR A 12  ? 0.22687 0.23743 0.23921 0.03035  -0.02090 -0.05758 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.21853 0.23492 0.23358 0.02752  -0.01849 -0.05203 19  THR A CG2 
33   N N   . PHE A 13  ? 0.19017 0.21142 0.19587 0.03026  -0.01208 -0.05408 20  PHE A N   
34   C CA  . PHE A 13  ? 0.19589 0.21963 0.20170 0.03071  -0.00884 -0.05297 20  PHE A CA  
35   C C   . PHE A 13  ? 0.19577 0.22253 0.20622 0.02734  -0.00982 -0.05005 20  PHE A C   
36   O O   . PHE A 13  ? 0.19073 0.21904 0.20255 0.02408  -0.01254 -0.04868 20  PHE A O   
37   C CB  . PHE A 13  ? 0.20541 0.23180 0.20713 0.03012  -0.00710 -0.05376 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.20753 0.23194 0.20407 0.03365  -0.00593 -0.05655 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.21791 0.24136 0.21231 0.03313  -0.00875 -0.05828 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.24845 0.27208 0.24260 0.03776  -0.00195 -0.05741 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.23653 0.25860 0.22607 0.03666  -0.00803 -0.06113 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.29741 0.31951 0.28628 0.04158  -0.00086 -0.05990 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.24754 0.26903 0.23399 0.04100  -0.00413 -0.06188 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.19988 0.22788 0.21278 0.02822  -0.00747 -0.04909 21  ALA A N   
45   C CA  . ALA A 14  ? 0.18664 0.21849 0.20351 0.02514  -0.00829 -0.04678 21  ALA A CA  
46   C C   . ALA A 14  ? 0.19038 0.22600 0.20529 0.02306  -0.00695 -0.04697 21  ALA A C   
47   O O   . ALA A 14  ? 0.20762 0.24304 0.22023 0.02493  -0.00370 -0.04838 21  ALA A O   
48   C CB  . ALA A 14  ? 0.18290 0.21463 0.20422 0.02692  -0.00658 -0.04586 21  ALA A CB  
49   N N   . PHE A 15  ? 0.17583 0.21480 0.19161 0.01942  -0.00921 -0.04544 22  PHE A N   
50   C CA  . PHE A 15  ? 0.18274 0.22555 0.19766 0.01744  -0.00779 -0.04550 22  PHE A CA  
51   C C   . PHE A 15  ? 0.18938 0.23375 0.20805 0.01839  -0.00522 -0.04566 22  PHE A C   
52   O O   . PHE A 15  ? 0.20996 0.25430 0.23309 0.01908  -0.00583 -0.04468 22  PHE A O   
53   C CB  . PHE A 15  ? 0.19368 0.24008 0.20920 0.01375  -0.01065 -0.04367 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.16357 0.20921 0.17583 0.01227  -0.01272 -0.04325 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.17796 0.22365 0.18576 0.01190  -0.01143 -0.04451 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.17348 0.21830 0.18762 0.01136  -0.01578 -0.04144 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.16517 0.21029 0.17077 0.01050  -0.01340 -0.04402 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.17386 0.21787 0.18612 0.01003  -0.01749 -0.04095 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.16988 0.21410 0.17793 0.00951  -0.01642 -0.04228 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.19797 0.24387 0.21531 0.01832  -0.00222 -0.04683 23  GLN A N   
61   C CA  . GLN A 16  ? 0.21511 0.26351 0.23703 0.01815  -0.00010 -0.04697 23  GLN A CA  
62   C C   . GLN A 16  ? 0.22186 0.27419 0.24736 0.01510  -0.00338 -0.04561 23  GLN A C   
63   O O   . GLN A 16  ? 0.20663 0.26062 0.22979 0.01264  -0.00628 -0.04469 23  GLN A O   
64   C CB  . GLN A 16  ? 0.22239 0.27223 0.24243 0.01780  0.00336  -0.04834 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.25807 0.30465 0.27474 0.02132  0.00713  -0.04949 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.37803 0.42640 0.39304 0.02067  0.01061  -0.05046 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.41455 0.46326 0.42470 0.01962  0.01027  -0.05073 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.42936 0.47889 0.44899 0.02128  0.01411  -0.05093 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.22602 0.28003 0.25732 0.01547  -0.00287 -0.04540 24  ALA A N   
70   C CA  . ALA A 17  ? 0.21599 0.27398 0.25086 0.01317  -0.00630 -0.04408 24  ALA A CA  
71   C C   . ALA A 17  ? 0.22555 0.28766 0.25830 0.00995  -0.00769 -0.04443 24  ALA A C   
72   O O   . ALA A 17  ? 0.23818 0.30269 0.27019 0.00812  -0.01122 -0.04291 24  ALA A O   
73   C CB  . ALA A 17  ? 0.25914 0.31887 0.30108 0.01408  -0.00522 -0.04422 24  ALA A CB  
74   N N   . GLU A 18  ? 0.23511 0.29794 0.26662 0.00945  -0.00473 -0.04628 25  GLU A N   
75   C CA  . GLU A 18  ? 0.24203 0.30866 0.27152 0.00649  -0.00579 -0.04683 25  GLU A CA  
76   C C   . GLU A 18  ? 0.20834 0.27419 0.23171 0.00527  -0.00790 -0.04556 25  GLU A C   
77   O O   . GLU A 18  ? 0.22251 0.29164 0.24439 0.00297  -0.01038 -0.04484 25  GLU A O   
78   C CB  . GLU A 18  ? 0.27065 0.33763 0.30029 0.00640  -0.00164 -0.04906 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.31082 0.37903 0.34759 0.00725  0.00079  -0.05042 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.44840 0.51252 0.48738 0.01084  0.00398  -0.05021 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.34690 0.40718 0.38161 0.01282  0.00415  -0.04933 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.43753 0.50226 0.48284 0.01186  0.00636  -0.05098 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.21435 0.27604 0.23436 0.00692  -0.00698 -0.04532 26  ILE A N   
84   C CA  . ILE A 19  ? 0.16458 0.22543 0.17965 0.00577  -0.00888 -0.04418 26  ILE A CA  
85   C C   . ILE A 19  ? 0.18595 0.24695 0.20236 0.00529  -0.01272 -0.04183 26  ILE A C   
86   O O   . ILE A 19  ? 0.20440 0.26705 0.21865 0.00344  -0.01498 -0.04027 26  ILE A O   
87   C CB  . ILE A 19  ? 0.20305 0.25986 0.21437 0.00769  -0.00679 -0.04511 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.20972 0.26707 0.21829 0.00767  -0.00314 -0.04677 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.20600 0.26150 0.21397 0.00678  -0.00938 -0.04381 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.30472 0.36311 0.31712 0.00863  0.00028  -0.04824 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.18250 0.24187 0.20271 0.00708  -0.01326 -0.04131 27  ALA A N   
92   C CA  . ALA A 20  ? 0.18339 0.24323 0.20559 0.00672  -0.01656 -0.03886 27  ALA A CA  
93   C C   . ALA A 20  ? 0.20331 0.26841 0.22672 0.00469  -0.01874 -0.03763 27  ALA A C   
94   O O   . ALA A 20  ? 0.21797 0.28438 0.24062 0.00373  -0.02136 -0.03527 27  ALA A O   
95   C CB  . ALA A 20  ? 0.22749 0.28500 0.25395 0.00908  -0.01634 -0.03859 27  ALA A CB  
96   N N   . GLN A 21  ? 0.20571 0.27398 0.23121 0.00419  -0.01761 -0.03926 28  GLN A N   
97   C CA  . GLN A 21  ? 0.21149 0.28515 0.23798 0.00245  -0.01985 -0.03873 28  GLN A CA  
98   C C   . GLN A 21  ? 0.25247 0.32772 0.27372 0.00050  -0.02051 -0.03838 28  GLN A C   
99   O O   . GLN A 21  ? 0.24455 0.32290 0.26479 -0.00042 -0.02325 -0.03644 28  GLN A O   
100  C CB  . GLN A 21  ? 0.24348 0.32001 0.27414 0.00230  -0.01841 -0.04114 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.37437 0.45688 0.40724 0.00096  -0.02129 -0.04098 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.49284 0.57818 0.53071 0.00059  -0.01977 -0.04394 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.59401 0.68446 0.63498 -0.00024 -0.02210 -0.04450 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.46498 0.54708 0.50410 0.00144  -0.01578 -0.04582 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.20025 0.27349 0.21806 0.00010  -0.01788 -0.04002 29  LEU A N   
106  C CA  . LEU A 22  ? 0.21846 0.29283 0.23117 -0.00165 -0.01824 -0.03948 29  LEU A CA  
107  C C   . LEU A 22  ? 0.22169 0.29470 0.23242 -0.00170 -0.02053 -0.03645 29  LEU A C   
108  O O   . LEU A 22  ? 0.21227 0.28789 0.22083 -0.00287 -0.02242 -0.03459 29  LEU A O   
109  C CB  . LEU A 22  ? 0.24779 0.31973 0.25736 -0.00166 -0.01480 -0.04143 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.23838 0.31039 0.24248 -0.00315 -0.01479 -0.04056 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.28428 0.36074 0.28717 -0.00500 -0.01554 -0.04092 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.25347 0.32259 0.25469 -0.00259 -0.01146 -0.04208 29  LEU A CD2 
113  N N   . MET A 23  ? 0.17838 0.24723 0.19011 -0.00028 -0.02030 -0.03592 30  MET A N   
114  C CA  . MET A 23  ? 0.19975 0.26697 0.21057 -0.00041 -0.02220 -0.03324 30  MET A CA  
115  C C   . MET A 23  ? 0.19605 0.26592 0.20942 -0.00037 -0.02497 -0.03040 30  MET A C   
116  O O   . MET A 23  ? 0.20118 0.27218 0.21293 -0.00113 -0.02646 -0.02777 30  MET A O   
117  C CB  . MET A 23  ? 0.22064 0.28278 0.23229 0.00112  -0.02151 -0.03377 30  MET A CB  
118  C CG  . MET A 23  ? 0.18765 0.24734 0.19596 0.00143  -0.01900 -0.03620 30  MET A CG  
119  S SD  . MET A 23  ? 0.20837 0.26262 0.21767 0.00395  -0.01827 -0.03769 30  MET A SD  
120  C CE  . MET A 23  ? 0.23572 0.28818 0.24514 0.00297  -0.02083 -0.03547 30  MET A CE  
121  N N   . SER A 24  ? 0.21340 0.28452 0.23086 0.00070  -0.02553 -0.03064 31  SER A N   
122  C CA  . SER A 24  ? 0.19147 0.26570 0.21114 0.00097  -0.02816 -0.02775 31  SER A CA  
123  C C   . SER A 24  ? 0.26443 0.34401 0.28152 -0.00029 -0.02953 -0.02714 31  SER A C   
124  O O   . SER A 24  ? 0.25464 0.33629 0.27101 -0.00016 -0.03148 -0.02398 31  SER A O   
125  C CB  . SER A 24  ? 0.27612 0.35052 0.30095 0.00252  -0.02844 -0.02804 31  SER A CB  
126  O OG  . SER A 24  ? 0.41844 0.49577 0.44462 0.00220  -0.02765 -0.03065 31  SER A OG  
127  N N   A LEU A 25  ? 0.20627 0.28797 0.22177 -0.00135 -0.02836 -0.03005 32  LEU A N   
128  N N   B LEU A 25  ? 0.20847 0.29016 0.22399 -0.00135 -0.02837 -0.03004 32  LEU A N   
129  C CA  A LEU A 25  ? 0.22985 0.31637 0.24237 -0.00250 -0.02967 -0.02987 32  LEU A CA  
130  C CA  B LEU A 25  ? 0.23024 0.31676 0.24279 -0.00249 -0.02967 -0.02989 32  LEU A CA  
131  C C   A LEU A 25  ? 0.25999 0.34553 0.26764 -0.00323 -0.02973 -0.02757 32  LEU A C   
132  C C   B LEU A 25  ? 0.25873 0.34432 0.26636 -0.00325 -0.02970 -0.02765 32  LEU A C   
133  O O   A LEU A 25  ? 0.22946 0.31828 0.23504 -0.00320 -0.03159 -0.02517 32  LEU A O   
134  O O   B LEU A 25  ? 0.23214 0.32105 0.23765 -0.00325 -0.03155 -0.02533 32  LEU A O   
135  C CB  A LEU A 25  ? 0.23945 0.32771 0.25160 -0.00361 -0.02796 -0.03378 32  LEU A CB  
136  C CB  B LEU A 25  ? 0.24048 0.32884 0.25283 -0.00358 -0.02802 -0.03380 32  LEU A CB  
137  C CG  A LEU A 25  ? 0.28377 0.37688 0.29281 -0.00488 -0.02903 -0.03470 32  LEU A CG  
138  C CG  B LEU A 25  ? 0.26034 0.35058 0.27829 -0.00301 -0.02794 -0.03613 32  LEU A CG  
139  C CD1 A LEU A 25  ? 0.33849 0.43397 0.35049 -0.00557 -0.02798 -0.03874 32  LEU A CD1 
140  C CD1 B LEU A 25  ? 0.31242 0.40362 0.33052 -0.00420 -0.02558 -0.03998 32  LEU A CD1 
141  C CD2 A LEU A 25  ? 0.29359 0.38526 0.29674 -0.00602 -0.02773 -0.03415 32  LEU A CD2 
142  C CD2 B LEU A 25  ? 0.25235 0.34789 0.27272 -0.00250 -0.03134 -0.03487 32  LEU A CD2 
143  N N   . ILE A 26  ? 0.19121 0.27242 0.19705 -0.00367 -0.02766 -0.02818 33  ILE A N   
144  C CA  . ILE A 26  ? 0.23304 0.31324 0.23490 -0.00444 -0.02753 -0.02603 33  ILE A CA  
145  C C   . ILE A 26  ? 0.23133 0.31090 0.23480 -0.00355 -0.02933 -0.02195 33  ILE A C   
146  O O   . ILE A 26  ? 0.22717 0.30830 0.22815 -0.00377 -0.03010 -0.01908 33  ILE A O   
147  C CB  . ILE A 26  ? 0.17336 0.24925 0.17371 -0.00489 -0.02509 -0.02775 33  ILE A CB  
148  C CG1 . ILE A 26  ? 0.19782 0.27488 0.19589 -0.00577 -0.02291 -0.03107 33  ILE A CG1 
149  C CG2 . ILE A 26  ? 0.18567 0.25982 0.18352 -0.00549 -0.02517 -0.02512 33  ILE A CG2 
150  C CD1 . ILE A 26  ? 0.21132 0.28448 0.20832 -0.00558 -0.02015 -0.03317 33  ILE A CD1 
151  N N   . ILE A 27  ? 0.22175 0.29900 0.22959 -0.00234 -0.02980 -0.02147 34  ILE A N   
152  C CA  . ILE A 27  ? 0.25731 0.33330 0.26751 -0.00143 -0.03105 -0.01767 34  ILE A CA  
153  C C   . ILE A 27  ? 0.27640 0.35709 0.28741 -0.00043 -0.03309 -0.01488 34  ILE A C   
154  O O   . ILE A 27  ? 0.30418 0.38556 0.31492 0.00013  -0.03385 -0.01101 34  ILE A O   
155  C CB  . ILE A 27  ? 0.25475 0.32626 0.26923 -0.00041 -0.03063 -0.01843 34  ILE A CB  
156  C CG1 . ILE A 27  ? 0.24542 0.31241 0.25861 -0.00103 -0.02898 -0.02056 34  ILE A CG1 
157  C CG2 . ILE A 27  ? 0.27024 0.34109 0.28835 0.00075  -0.03192 -0.01457 34  ILE A CG2 
158  C CD1 . ILE A 27  ? 0.23926 0.30215 0.25539 0.00021  -0.02822 -0.02289 34  ILE A CD1 
159  N N   . ASN A 28  ? 0.24388 0.32813 0.25602 -0.00005 -0.03395 -0.01670 35  ASN A N   
160  C CA  . ASN A 28  ? 0.25545 0.34439 0.26907 0.00133  -0.03619 -0.01425 35  ASN A CA  
161  C C   . ASN A 28  ? 0.33072 0.42527 0.34021 0.00108  -0.03749 -0.01415 35  ASN A C   
162  O O   . ASN A 28  ? 0.36219 0.46080 0.37178 0.00259  -0.03943 -0.01132 35  ASN A O   
163  C CB  . ASN A 28  ? 0.27706 0.36708 0.29525 0.00216  -0.03676 -0.01613 35  ASN A CB  
164  C CG  . ASN A 28  ? 0.36126 0.44626 0.38356 0.00304  -0.03584 -0.01554 35  ASN A CG  
165  O OD1 . ASN A 28  ? 0.37521 0.45728 0.39820 0.00355  -0.03571 -0.01260 35  ASN A OD1 
166  N ND2 . ASN A 28  ? 0.43121 0.51501 0.45659 0.00333  -0.03505 -0.01836 35  ASN A ND2 
167  N N   . THR A 29  ? 0.25064 0.34578 0.25653 -0.00051 -0.03648 -0.01721 36  THR A N   
168  C CA  . THR A 29  ? 0.23772 0.33829 0.23971 -0.00065 -0.03785 -0.01769 36  THR A CA  
169  C C   . THR A 29  ? 0.26610 0.36722 0.26384 -0.00004 -0.03810 -0.01360 36  THR A C   
170  O O   . THR A 29  ? 0.28101 0.37801 0.27732 -0.00078 -0.03633 -0.01228 36  THR A O   
171  C CB  . THR A 29  ? 0.26588 0.36649 0.26559 -0.00256 -0.03630 -0.02221 36  THR A CB  
172  O OG1 . THR A 29  ? 0.27912 0.37932 0.28338 -0.00285 -0.03574 -0.02569 36  THR A OG1 
173  C CG2 . THR A 29  ? 0.29657 0.40254 0.29218 -0.00278 -0.03770 -0.02324 36  THR A CG2 
174  N N   . PHE A 30  ? 0.23405 0.34042 0.22981 0.00151  -0.04025 -0.01154 37  PHE A N   
175  C CA  . PHE A 30  ? 0.26415 0.37129 0.25514 0.00230  -0.04008 -0.00779 37  PHE A CA  
176  C C   . PHE A 30  ? 0.25921 0.36629 0.24490 0.00055  -0.03879 -0.01035 37  PHE A C   
177  O O   . PHE A 30  ? 0.22910 0.33983 0.21282 -0.00004 -0.03969 -0.01398 37  PHE A O   
178  C CB  . PHE A 30  ? 0.26840 0.38146 0.25788 0.00489  -0.04257 -0.00494 37  PHE A CB  
179  C CG  . PHE A 30  ? 0.25226 0.36614 0.23684 0.00627  -0.04212 -0.00061 37  PHE A CG  
180  C CD1 . PHE A 30  ? 0.31265 0.42298 0.29898 0.00723  -0.04067 0.00437  37  PHE A CD1 
181  C CD2 . PHE A 30  ? 0.29304 0.41105 0.27145 0.00665  -0.04292 -0.00155 37  PHE A CD2 
182  C CE1 . PHE A 30  ? 0.35228 0.46326 0.33456 0.00869  -0.03983 0.00876  37  PHE A CE1 
183  C CE2 . PHE A 30  ? 0.26576 0.38429 0.23937 0.00823  -0.04216 0.00276  37  PHE A CE2 
184  C CZ  . PHE A 30  ? 0.27940 0.39448 0.25509 0.00931  -0.04054 0.00808  37  PHE A CZ  
185  N N   . TYR A 31  ? 0.21013 0.31322 0.19378 -0.00024 -0.03669 -0.00841 38  TYR A N   
186  C CA  . TYR A 31  ? 0.22624 0.32856 0.20522 -0.00197 -0.03501 -0.01065 38  TYR A CA  
187  C C   . TYR A 31  ? 0.22207 0.32116 0.19906 -0.00198 -0.03327 -0.00668 38  TYR A C   
188  O O   . TYR A 31  ? 0.21470 0.30917 0.19489 -0.00274 -0.03191 -0.00597 38  TYR A O   
189  C CB  . TYR A 31  ? 0.22368 0.32325 0.20478 -0.00401 -0.03345 -0.01547 38  TYR A CB  
190  C CG  . TYR A 31  ? 0.24784 0.34589 0.22466 -0.00570 -0.03119 -0.01731 38  TYR A CG  
191  C CD1 . TYR A 31  ? 0.30460 0.40619 0.27731 -0.00624 -0.03136 -0.01986 38  TYR A CD1 
192  C CD2 . TYR A 31  ? 0.28236 0.37561 0.25940 -0.00671 -0.02894 -0.01673 38  TYR A CD2 
193  C CE1 . TYR A 31  ? 0.37410 0.47415 0.34289 -0.00774 -0.02898 -0.02138 38  TYR A CE1 
194  C CE2 . TYR A 31  ? 0.31289 0.40498 0.28604 -0.00811 -0.02675 -0.01816 38  TYR A CE2 
195  C CZ  . TYR A 31  ? 0.35961 0.45496 0.32868 -0.00861 -0.02665 -0.02033 38  TYR A CZ  
196  O OH  . TYR A 31  ? 0.50294 0.59678 0.46834 -0.00994 -0.02415 -0.02149 38  TYR A OH  
197  N N   . SER A 32  ? 0.20148 0.30311 0.17339 -0.00100 -0.03336 -0.00412 39  SER A N   
198  C CA  . SER A 32  ? 0.18798 0.28718 0.15889 -0.00040 -0.03186 0.00073  39  SER A CA  
199  C C   . SER A 32  ? 0.22538 0.32064 0.19474 -0.00259 -0.02930 -0.00042 39  SER A C   
200  O O   . SER A 32  ? 0.24116 0.33317 0.21221 -0.00267 -0.02792 0.00287  39  SER A O   
201  C CB  . SER A 32  ? 0.21702 0.32047 0.18272 0.00190  -0.03265 0.00411  39  SER A CB  
202  O OG  . SER A 32  ? 0.23871 0.34539 0.20655 0.00436  -0.03477 0.00635  39  SER A OG  
203  N N   . ASN A 33  ? 0.22663 0.32220 0.19334 -0.00429 -0.02856 -0.00497 40  ASN A N   
204  C CA  . ASN A 33  ? 0.21855 0.31132 0.18265 -0.00604 -0.02603 -0.00589 40  ASN A CA  
205  C C   . ASN A 33  ? 0.22271 0.31094 0.19133 -0.00745 -0.02480 -0.00763 40  ASN A C   
206  O O   . ASN A 33  ? 0.23023 0.31719 0.19825 -0.00889 -0.02340 -0.01146 40  ASN A O   
207  C CB  . ASN A 33  ? 0.28166 0.37692 0.24109 -0.00698 -0.02556 -0.00988 40  ASN A CB  
208  C CG  . ASN A 33  ? 0.27317 0.36592 0.22946 -0.00865 -0.02270 -0.01084 40  ASN A CG  
209  O OD1 . ASN A 33  ? 0.28933 0.38007 0.24463 -0.00860 -0.02142 -0.00740 40  ASN A OD1 
210  N ND2 . ASN A 33  ? 0.31353 0.40671 0.26844 -0.01000 -0.02160 -0.01537 40  ASN A ND2 
211  N N   . LYS A 34  ? 0.23033 0.20141 0.17633 0.00849  -0.02627 -0.01498 41  LYS A N   
212  C CA  . LYS A 34  ? 0.22261 0.19433 0.17694 0.00674  -0.02541 -0.01384 41  LYS A CA  
213  C C   . LYS A 34  ? 0.21855 0.18998 0.17768 0.00385  -0.02149 -0.01394 41  LYS A C   
214  O O   . LYS A 34  ? 0.21677 0.18966 0.18312 0.00239  -0.02127 -0.01401 41  LYS A O   
215  C CB  . LYS A 34  ? 0.23464 0.20252 0.18609 0.00813  -0.02504 -0.01009 41  LYS A CB  
216  C CG  . LYS A 34  ? 0.24502 0.21340 0.19368 0.01137  -0.02947 -0.00980 41  LYS A CG  
217  C CD  . LYS A 34  ? 0.27606 0.23968 0.22237 0.01268  -0.02866 -0.00593 41  LYS A CD  
218  C CE  . LYS A 34  ? 0.28553 0.24956 0.23018 0.01622  -0.03318 -0.00558 41  LYS A CE  
219  N NZ  . LYS A 34  ? 0.27461 0.24396 0.22876 0.01594  -0.03569 -0.00809 41  LYS A NZ  
220  N N   . GLU A 35  ? 0.21261 0.18238 0.16778 0.00328  -0.01848 -0.01405 42  GLU A N   
221  C CA  . GLU A 35  ? 0.20768 0.17705 0.16750 0.00092  -0.01467 -0.01395 42  GLU A CA  
222  C C   . GLU A 35  ? 0.22757 0.20041 0.19555 -0.00067 -0.01559 -0.01671 42  GLU A C   
223  O O   . GLU A 35  ? 0.23211 0.20503 0.20530 -0.00229 -0.01341 -0.01657 42  GLU A O   
224  C CB  . GLU A 35  ? 0.23607 0.20360 0.18990 0.00093  -0.01113 -0.01398 42  GLU A CB  
225  C CG  . GLU A 35  ? 0.24730 0.21719 0.19932 0.00143  -0.01225 -0.01773 42  GLU A CG  
226  C CD  . GLU A 35  ? 0.33746 0.30570 0.28252 0.00187  -0.00845 -0.01799 42  GLU A CD  
227  O OE1 . GLU A 35  ? 0.40412 0.36899 0.34146 0.00298  -0.00636 -0.01487 42  GLU A OE1 
228  O OE2 . GLU A 35  ? 0.43350 0.40361 0.38052 0.00129  -0.00750 -0.02125 42  GLU A OE2 
229  N N   . ILE A 36  ? 0.22845 0.20403 0.19790 -0.00019 -0.01878 -0.01921 43  ILE A N   
230  C CA  . ILE A 36  ? 0.20140 0.17944 0.17837 -0.00174 -0.01929 -0.02137 43  ILE A CA  
231  C C   . ILE A 36  ? 0.21359 0.19225 0.19653 -0.00263 -0.01931 -0.01976 43  ILE A C   
232  O O   . ILE A 36  ? 0.20902 0.18875 0.19753 -0.00388 -0.01891 -0.02064 43  ILE A O   
233  C CB  . ILE A 36  ? 0.25142 0.23206 0.22963 -0.00133 -0.02251 -0.02447 43  ILE A CB  
234  C CG1 . ILE A 36  ? 0.25577 0.23797 0.23376 -0.00001 -0.02564 -0.02388 43  ILE A CG1 
235  C CG2 . ILE A 36  ? 0.30370 0.28370 0.27564 -0.00031 -0.02239 -0.02680 43  ILE A CG2 
236  C CD1 . ILE A 36  ? 0.33025 0.31469 0.31584 -0.00108 -0.02638 -0.02354 43  ILE A CD1 
237  N N   . PHE A 37  ? 0.20148 0.17909 0.18300 -0.00183 -0.01961 -0.01742 44  PHE A N   
238  C CA  . PHE A 37  ? 0.21662 0.19489 0.20322 -0.00244 -0.01953 -0.01634 44  PHE A CA  
239  C C   . PHE A 37  ? 0.21266 0.19019 0.20251 -0.00378 -0.01722 -0.01629 44  PHE A C   
240  O O   . PHE A 37  ? 0.18749 0.16622 0.18187 -0.00434 -0.01745 -0.01640 44  PHE A O   
241  C CB  . PHE A 37  ? 0.19484 0.17150 0.17946 -0.00126 -0.01994 -0.01421 44  PHE A CB  
242  C CG  . PHE A 37  ? 0.19412 0.16736 0.17668 -0.00163 -0.01740 -0.01251 44  PHE A CG  
243  C CD1 . PHE A 37  ? 0.22347 0.19396 0.19999 -0.00105 -0.01607 -0.01140 44  PHE A CD1 
244  C CD2 . PHE A 37  ? 0.22588 0.19876 0.21277 -0.00263 -0.01616 -0.01218 44  PHE A CD2 
245  C CE1 . PHE A 37  ? 0.21140 0.17866 0.18699 -0.00182 -0.01300 -0.00968 44  PHE A CE1 
246  C CE2 . PHE A 37  ? 0.19883 0.16892 0.18547 -0.00335 -0.01371 -0.01107 44  PHE A CE2 
247  C CZ  . PHE A 37  ? 0.22520 0.19246 0.20665 -0.00317 -0.01181 -0.00971 44  PHE A CZ  
248  N N   . LEU A 38  ? 0.17844 0.15412 0.16602 -0.00415 -0.01489 -0.01608 45  LEU A N   
249  C CA  . LEU A 38  ? 0.16696 0.14247 0.15875 -0.00522 -0.01297 -0.01623 45  LEU A CA  
250  C C   . LEU A 38  ? 0.17202 0.14911 0.16743 -0.00577 -0.01313 -0.01822 45  LEU A C   
251  O O   . LEU A 38  ? 0.19103 0.16879 0.19107 -0.00611 -0.01324 -0.01839 45  LEU A O   
252  C CB  . LEU A 38  ? 0.19360 0.16708 0.18303 -0.00565 -0.00993 -0.01555 45  LEU A CB  
253  C CG  . LEU A 38  ? 0.20663 0.18046 0.20169 -0.00679 -0.00794 -0.01604 45  LEU A CG  
254  C CD1 . LEU A 38  ? 0.19599 0.17007 0.19492 -0.00676 -0.00951 -0.01542 45  LEU A CD1 
255  C CD2 . LEU A 38  ? 0.25149 0.22350 0.24494 -0.00755 -0.00417 -0.01525 45  LEU A CD2 
256  N N   . ARG A 39  ? 0.20785 0.18533 0.20103 -0.00560 -0.01347 -0.01987 46  ARG A N   
257  C CA  . ARG A 39  ? 0.18556 0.16398 0.18251 -0.00605 -0.01388 -0.02194 46  ARG A CA  
258  C C   . ARG A 39  ? 0.22262 0.20196 0.22368 -0.00630 -0.01567 -0.02137 46  ARG A C   
259  O O   . ARG A 39  ? 0.21504 0.19423 0.22024 -0.00662 -0.01548 -0.02159 46  ARG A O   
260  C CB  . ARG A 39  ? 0.23702 0.21573 0.23084 -0.00570 -0.01457 -0.02431 46  ARG A CB  
261  C CG  . ARG A 39  ? 0.27120 0.25041 0.26958 -0.00625 -0.01535 -0.02670 46  ARG A CG  
262  C CD  . ARG A 39  ? 0.28354 0.26328 0.27920 -0.00583 -0.01670 -0.02978 46  ARG A CD  
263  N NE  . ARG A 39  ? 0.33501 0.31616 0.33011 -0.00561 -0.01947 -0.02983 46  ARG A NE  
264  C CZ  . ARG A 39  ? 0.32615 0.30822 0.31744 -0.00471 -0.02141 -0.03209 46  ARG A CZ  
265  N NH1 . ARG A 39  ? 0.33605 0.31752 0.32284 -0.00389 -0.02080 -0.03454 46  ARG A NH1 
266  N NH2 . ARG A 39  ? 0.33431 0.31826 0.32646 -0.00441 -0.02415 -0.03220 46  ARG A NH2 
267  N N   . GLU A 40  ? 0.20191 0.18211 0.20181 -0.00596 -0.01723 -0.02045 47  GLU A N   
268  C CA  . GLU A 40  ? 0.19982 0.18118 0.20351 -0.00629 -0.01829 -0.01989 47  GLU A CA  
269  C C   . GLU A 40  ? 0.20782 0.18876 0.21323 -0.00609 -0.01768 -0.01808 47  GLU A C   
270  O O   . GLU A 40  ? 0.18911 0.17002 0.19750 -0.00631 -0.01766 -0.01754 47  GLU A O   
271  C CB  . GLU A 40  ? 0.18398 0.16704 0.18661 -0.00581 -0.01992 -0.01969 47  GLU A CB  
272  C CG  . GLU A 40  ? 0.20638 0.19038 0.20779 -0.00574 -0.02136 -0.02205 47  GLU A CG  
273  C CD  . GLU A 40  ? 0.28005 0.26414 0.28549 -0.00691 -0.02138 -0.02423 47  GLU A CD  
274  O OE1 . GLU A 40  ? 0.27735 0.26138 0.28751 -0.00784 -0.02077 -0.02344 47  GLU A OE1 
275  O OE2 . GLU A 40  ? 0.33507 0.31890 0.33866 -0.00676 -0.02190 -0.02673 47  GLU A OE2 
276  N N   . LEU A 41  ? 0.17911 0.15946 0.18250 -0.00555 -0.01725 -0.01715 48  LEU A N   
277  C CA  . LEU A 41  ? 0.17751 0.15774 0.18246 -0.00512 -0.01722 -0.01611 48  LEU A CA  
278  C C   . LEU A 41  ? 0.18568 0.16534 0.19331 -0.00526 -0.01658 -0.01675 48  LEU A C   
279  O O   . LEU A 41  ? 0.17056 0.15032 0.17995 -0.00466 -0.01720 -0.01617 48  LEU A O   
280  C CB  . LEU A 41  ? 0.18535 0.16487 0.18845 -0.00464 -0.01710 -0.01544 48  LEU A CB  
281  C CG  . LEU A 41  ? 0.19799 0.17801 0.19891 -0.00392 -0.01812 -0.01472 48  LEU A CG  
282  C CD1 . LEU A 41  ? 0.17708 0.15532 0.17627 -0.00340 -0.01787 -0.01400 48  LEU A CD1 
283  C CD2 . LEU A 41  ? 0.19873 0.18059 0.20132 -0.00342 -0.01893 -0.01429 48  LEU A CD2 
284  N N   . ILE A 42  ? 0.17747 0.15662 0.18525 -0.00575 -0.01537 -0.01799 49  ILE A N   
285  C CA  . ILE A 42  ? 0.18986 0.16893 0.20113 -0.00566 -0.01482 -0.01903 49  ILE A CA  
286  C C   . ILE A 42  ? 0.18102 0.15965 0.19430 -0.00549 -0.01559 -0.01921 49  ILE A C   
287  O O   . ILE A 42  ? 0.20615 0.18441 0.22212 -0.00472 -0.01617 -0.01900 49  ILE A O   
288  C CB  . ILE A 42  ? 0.18470 0.16365 0.19582 -0.00621 -0.01275 -0.02051 49  ILE A CB  
289  C CG1 . ILE A 42  ? 0.15899 0.13780 0.16957 -0.00653 -0.01157 -0.01984 49  ILE A CG1 
290  C CG2 . ILE A 42  ? 0.21482 0.19413 0.23034 -0.00594 -0.01217 -0.02222 49  ILE A CG2 
291  C CD1 . ILE A 42  ? 0.26255 0.24096 0.27188 -0.00724 -0.00855 -0.02064 49  ILE A CD1 
292  N N   . SER A 43  ? 0.18021 0.15870 0.19245 -0.00608 -0.01582 -0.01956 50  SER A N   
293  C CA  . SER A 43  ? 0.18639 0.16389 0.20139 -0.00625 -0.01626 -0.01965 50  SER A CA  
294  C C   . SER A 43  ? 0.20026 0.17748 0.21571 -0.00577 -0.01688 -0.01720 50  SER A C   
295  O O   . SER A 43  ? 0.20176 0.17740 0.21919 -0.00519 -0.01702 -0.01634 50  SER A O   
296  C CB  . SER A 43  ? 0.24896 0.22671 0.26368 -0.00720 -0.01651 -0.02120 50  SER A CB  
297  O OG  . SER A 43  ? 0.30951 0.28625 0.32756 -0.00782 -0.01685 -0.02092 50  SER A OG  
298  N N   . ASN A 44  ? 0.19907 0.17761 0.21226 -0.00566 -0.01716 -0.01600 51  ASN A N   
299  C CA  . ASN A 44  ? 0.19528 0.17381 0.20797 -0.00488 -0.01737 -0.01382 51  ASN A CA  
300  C C   . ASN A 44  ? 0.18996 0.16773 0.20254 -0.00340 -0.01801 -0.01334 51  ASN A C   
301  O O   . ASN A 44  ? 0.18993 0.16652 0.20230 -0.00240 -0.01826 -0.01168 51  ASN A O   
302  C CB  . ASN A 44  ? 0.21279 0.19315 0.22323 -0.00466 -0.01755 -0.01324 51  ASN A CB  
303  C CG  . ASN A 44  ? 0.25410 0.23581 0.26543 -0.00568 -0.01735 -0.01350 51  ASN A CG  
304  O OD1 . ASN A 44  ? 0.24561 0.22691 0.25943 -0.00678 -0.01712 -0.01427 51  ASN A OD1 
305  N ND2 . ASN A 44  ? 0.26294 0.24642 0.27287 -0.00523 -0.01765 -0.01325 51  ASN A ND2 
306  N N   . SER A 45  ? 0.15931 0.13775 0.17207 -0.00316 -0.01828 -0.01476 52  SER A N   
307  C CA  . SER A 45  ? 0.17389 0.15230 0.18784 -0.00173 -0.01934 -0.01503 52  SER A CA  
308  C C   . SER A 45  ? 0.18224 0.15918 0.19880 -0.00106 -0.01963 -0.01516 52  SER A C   
309  O O   . SER A 45  ? 0.18345 0.15962 0.19993 0.00072  -0.02097 -0.01417 52  SER A O   
310  C CB  . SER A 45  ? 0.18010 0.15966 0.19549 -0.00210 -0.01911 -0.01685 52  SER A CB  
311  O OG  . SER A 45  ? 0.20928 0.18945 0.22248 -0.00227 -0.01921 -0.01654 52  SER A OG  
312  N N   . SER A 46  ? 0.16371 0.14008 0.18232 -0.00215 -0.01855 -0.01651 53  SER A N   
313  C CA  . SER A 46  ? 0.20067 0.17528 0.22232 -0.00141 -0.01879 -0.01695 53  SER A CA  
314  C C   . SER A 46  ? 0.18772 0.15976 0.20849 -0.00084 -0.01915 -0.01434 53  SER A C   
315  O O   . SER A 46  ? 0.19050 0.16072 0.21218 0.00094  -0.02020 -0.01332 53  SER A O   
316  C CB  . SER A 46  ? 0.23641 0.21090 0.25997 -0.00265 -0.01743 -0.01934 53  SER A CB  
317  O OG  . SER A 46  ? 0.22418 0.19657 0.25112 -0.00184 -0.01768 -0.01999 53  SER A OG  
318  N N   . ASP A 47  ? 0.18705 0.15898 0.20606 -0.00219 -0.01824 -0.01303 54  ASP A N   
319  C CA  . ASP A 47  ? 0.17451 0.14403 0.19298 -0.00203 -0.01775 -0.01019 54  ASP A CA  
320  C C   . ASP A 47  ? 0.22160 0.19070 0.23653 0.00019  -0.01865 -0.00770 54  ASP A C   
321  O O   . ASP A 47  ? 0.22926 0.19529 0.24345 0.00152  -0.01872 -0.00525 54  ASP A O   
322  C CB  . ASP A 47  ? 0.21778 0.18841 0.23610 -0.00402 -0.01643 -0.00975 54  ASP A CB  
323  C CG  . ASP A 47  ? 0.26613 0.23650 0.28803 -0.00591 -0.01599 -0.01216 54  ASP A CG  
324  O OD1 . ASP A 47  ? 0.25210 0.22085 0.27637 -0.00570 -0.01630 -0.01392 54  ASP A OD1 
325  O OD2 . ASP A 47  ? 0.25722 0.22938 0.27967 -0.00742 -0.01554 -0.01276 54  ASP A OD2 
326  N N   . ALA A 48  ? 0.19560 0.16743 0.20805 0.00085  -0.01947 -0.00838 55  ALA A N   
327  C CA  . ALA A 48  ? 0.19418 0.16605 0.20277 0.00322  -0.02073 -0.00681 55  ALA A CA  
328  C C   . ALA A 48  ? 0.18395 0.15485 0.19357 0.00559  -0.02298 -0.00739 55  ALA A C   
329  O O   . ALA A 48  ? 0.18607 0.15548 0.19235 0.00810  -0.02428 -0.00542 55  ALA A O   
330  C CB  . ALA A 48  ? 0.17435 0.14928 0.18100 0.00323  -0.02125 -0.00819 55  ALA A CB  
331  N N   . LEU A 49  ? 0.17163 0.14371 0.18567 0.00507  -0.02353 -0.01024 56  LEU A N   
332  C CA  . LEU A 49  ? 0.18721 0.15903 0.20394 0.00729  -0.02568 -0.01135 56  LEU A CA  
333  C C   . LEU A 49  ? 0.19539 0.16321 0.21276 0.00840  -0.02567 -0.00933 56  LEU A C   
334  O O   . LEU A 49  ? 0.21431 0.18063 0.23073 0.01135  -0.02787 -0.00823 56  LEU A O   
335  C CB  . LEU A 49  ? 0.20221 0.17660 0.22425 0.00610  -0.02536 -0.01494 56  LEU A CB  
336  C CG  . LEU A 49  ? 0.19400 0.17162 0.21604 0.00542  -0.02564 -0.01672 56  LEU A CG  
337  C CD1 . LEU A 49  ? 0.20707 0.18643 0.23299 0.00324  -0.02366 -0.01923 56  LEU A CD1 
338  C CD2 . LEU A 49  ? 0.18782 0.16705 0.21111 0.00806  -0.02882 -0.01795 56  LEU A CD2 
339  N N   . ASP A 50  ? 0.19540 0.16126 0.21441 0.00623  -0.02344 -0.00889 57  ASP A N   
340  C CA  . ASP A 50  ? 0.19860 0.15986 0.21873 0.00705  -0.02321 -0.00686 57  ASP A CA  
341  C C   . ASP A 50  ? 0.19540 0.15368 0.21014 0.00892  -0.02343 -0.00247 57  ASP A C   
342  O O   . ASP A 50  ? 0.21707 0.17146 0.23131 0.01134  -0.02454 -0.00035 57  ASP A O   
343  C CB  . ASP A 50  ? 0.20614 0.16582 0.22903 0.00412  -0.02082 -0.00732 57  ASP A CB  
344  C CG  . ASP A 50  ? 0.24667 0.20832 0.27400 0.00278  -0.02046 -0.01153 57  ASP A CG  
345  O OD1 . ASP A 50  ? 0.24898 0.21281 0.27836 0.00397  -0.02152 -0.01393 57  ASP A OD1 
346  O OD2 . ASP A 50  ? 0.26992 0.23098 0.29886 0.00050  -0.01896 -0.01255 57  ASP A OD2 
347  N N   . LYS A 51  ? 0.20828 0.16802 0.21876 0.00793  -0.02210 -0.00090 58  LYS A N   
348  C CA  . LYS A 51  ? 0.21360 0.17060 0.21823 0.00957  -0.02144 0.00345  58  LYS A CA  
349  C C   . LYS A 51  ? 0.22783 0.18453 0.22812 0.01373  -0.02467 0.00417  58  LYS A C   
350  O O   . LYS A 51  ? 0.23791 0.19028 0.23451 0.01625  -0.02507 0.00775  58  LYS A O   
351  C CB  . LYS A 51  ? 0.23420 0.19377 0.23575 0.00783  -0.01924 0.00425  58  LYS A CB  
352  C CG  . LYS A 51  ? 0.20736 0.16677 0.21307 0.00421  -0.01630 0.00418  58  LYS A CG  
353  C CD  . LYS A 51  ? 0.22878 0.19179 0.23223 0.00291  -0.01458 0.00432  58  LYS A CD  
354  C CE  . LYS A 51  ? 0.29068 0.25509 0.29940 -0.00056 -0.01267 0.00284  58  LYS A CE  
355  N NZ  . LYS A 51  ? 0.35475 0.32312 0.36196 -0.00137 -0.01146 0.00257  58  LYS A NZ  
356  N N   . ILE A 52  ? 0.20482 0.16587 0.20536 0.01465  -0.02709 0.00085  59  ILE A N   
357  C CA  . ILE A 52  ? 0.20505 0.16627 0.20205 0.01880  -0.03079 0.00087  59  ILE A CA  
358  C C   . ILE A 52  ? 0.22059 0.17978 0.22170 0.02097  -0.03319 0.00025  59  ILE A C   
359  O O   . ILE A 52  ? 0.25315 0.21016 0.25039 0.02493  -0.03595 0.00206  59  ILE A O   
360  C CB  . ILE A 52  ? 0.21394 0.18035 0.21113 0.01910  -0.03291 -0.00293 59  ILE A CB  
361  C CG1 . ILE A 52  ? 0.25735 0.22427 0.24975 0.02359  -0.03703 -0.00311 59  ILE A CG1 
362  C CG2 . ILE A 52  ? 0.21750 0.18715 0.22280 0.01706  -0.03328 -0.00726 59  ILE A CG2 
363  C CD1 . ILE A 52  ? 0.27209 0.23603 0.25468 0.02610  -0.03652 0.00118  59  ILE A CD1 
364  N N   . ARG A 53  ? 0.21694 0.17682 0.22557 0.01883  -0.03233 -0.00241 60  ARG A N   
365  C CA  . ARG A 53  ? 0.23492 0.19268 0.24795 0.02107  -0.03430 -0.00305 60  ARG A CA  
366  C C   . ARG A 53  ? 0.22998 0.18097 0.23972 0.02262  -0.03357 0.00174  60  ARG A C   
367  O O   . ARG A 53  ? 0.25241 0.20067 0.26066 0.02664  -0.03648 0.00323  60  ARG A O   
368  C CB  . ARG A 53  ? 0.24264 0.20232 0.26384 0.01847  -0.03287 -0.00689 60  ARG A CB  
369  C CG  . ARG A 53  ? 0.30096 0.25844 0.32699 0.02116  -0.03484 -0.00769 60  ARG A CG  
370  C CD  . ARG A 53  ? 0.44827 0.40776 0.48226 0.01938  -0.03352 -0.01183 60  ARG A CD  
371  N NE  . ARG A 53  ? 0.50784 0.47343 0.54661 0.01936  -0.03459 -0.01619 60  ARG A NE  
372  C CZ  . ARG A 53  ? 0.46266 0.43154 0.50558 0.01640  -0.03202 -0.01948 60  ARG A CZ  
373  N NH1 . ARG A 53  ? 0.41170 0.37888 0.45369 0.01342  -0.02885 -0.01924 60  ARG A NH1 
374  N NH2 . ARG A 53  ? 0.43687 0.41083 0.48503 0.01651  -0.03262 -0.02315 60  ARG A NH2 
375  N N   . TYR A 54  ? 0.20403 0.15208 0.21251 0.01964  -0.02975 0.00438  61  TYR A N   
376  C CA  . TYR A 54  ? 0.24330 0.18431 0.24939 0.02065  -0.02842 0.00923  61  TYR A CA  
377  C C   . TYR A 54  ? 0.28858 0.22715 0.28560 0.02462  -0.02997 0.01351  61  TYR A C   
378  O O   . TYR A 54  ? 0.28476 0.21801 0.27954 0.02806  -0.03155 0.01664  61  TYR A O   
379  C CB  . TYR A 54  ? 0.26293 0.20203 0.27012 0.01640  -0.02390 0.01097  61  TYR A CB  
380  C CG  . TYR A 54  ? 0.25760 0.18888 0.26386 0.01689  -0.02198 0.01595  61  TYR A CG  
381  C CD1 . TYR A 54  ? 0.25386 0.18057 0.26574 0.01754  -0.02268 0.01547  61  TYR A CD1 
382  C CD2 . TYR A 54  ? 0.29961 0.22790 0.29929 0.01696  -0.01936 0.02117  61  TYR A CD2 
383  C CE1 . TYR A 54  ? 0.27503 0.19378 0.28635 0.01803  -0.02089 0.02024  61  TYR A CE1 
384  C CE2 . TYR A 54  ? 0.32028 0.24074 0.31904 0.01729  -0.01706 0.02634  61  TYR A CE2 
385  C CZ  . TYR A 54  ? 0.29467 0.21019 0.29936 0.01777  -0.01795 0.02589  61  TYR A CZ  
386  O OH  . TYR A 54  ? 0.33759 0.24454 0.34190 0.01806  -0.01563 0.03112  61  TYR A OH  
387  N N   . GLU A 55  ? 0.28552 0.22774 0.27682 0.02452  -0.02969 0.01363  62  GLU A N   
388  C CA  . GLU A 55  ? 0.29969 0.23987 0.28103 0.02848  -0.03098 0.01745  62  GLU A CA  
389  C C   . GLU A 55  ? 0.31918 0.25974 0.29938 0.03355  -0.03657 0.01600  62  GLU A C   
390  O O   . GLU A 55  ? 0.33549 0.27145 0.30850 0.03779  -0.03821 0.02008  62  GLU A O   
391  C CB  . GLU A 55  ? 0.32011 0.26492 0.29639 0.02750  -0.02985 0.01662  62  GLU A CB  
392  C CG  . GLU A 55  ? 0.31780 0.26140 0.29311 0.02377  -0.02437 0.01949  62  GLU A CG  
393  C CD  . GLU A 55  ? 0.40857 0.35574 0.37742 0.02388  -0.02309 0.01962  62  GLU A CD  
394  O OE1 . GLU A 55  ? 0.47036 0.41713 0.43843 0.02120  -0.01854 0.02197  62  GLU A OE1 
395  O OE2 . GLU A 55  ? 0.37499 0.32562 0.34032 0.02661  -0.02666 0.01696  62  GLU A OE2 
396  N N   . SER A 56  ? 0.27402 0.21978 0.26163 0.03331  -0.03949 0.01036  63  SER A N   
397  C CA  . SER A 56  ? 0.31061 0.25788 0.29885 0.03807  -0.04511 0.00818  63  SER A CA  
398  C C   . SER A 56  ? 0.31396 0.25579 0.30478 0.04084  -0.04661 0.01024  63  SER A C   
399  O O   . SER A 56  ? 0.32681 0.26842 0.31637 0.04585  -0.05153 0.00984  63  SER A O   
400  C CB  . SER A 56  ? 0.29794 0.25246 0.29495 0.03660  -0.04713 0.00150  63  SER A CB  
401  O OG  . SER A 56  ? 0.30716 0.26200 0.31377 0.03394  -0.04543 -0.00090 63  SER A OG  
402  N N   . LEU A 57  ? 0.27653 0.21414 0.27166 0.03790  -0.04289 0.01190  64  LEU A N   
403  C CA  . LEU A 57  ? 0.31065 0.24283 0.30942 0.04047  -0.04431 0.01331  64  LEU A CA  
404  C C   . LEU A 57  ? 0.39143 0.31668 0.38071 0.04529  -0.04590 0.01948  64  LEU A C   
405  O O   . LEU A 57  ? 0.43741 0.35900 0.42798 0.04957  -0.04930 0.02035  64  LEU A O   
406  C CB  . LEU A 57  ? 0.29662 0.22515 0.30157 0.03621  -0.03987 0.01371  64  LEU A CB  
407  C CG  . LEU A 57  ? 0.31994 0.25450 0.33405 0.03225  -0.03864 0.00758  64  LEU A CG  
408  C CD1 . LEU A 57  ? 0.34588 0.27602 0.36524 0.02900  -0.03506 0.00795  64  LEU A CD1 
409  C CD2 . LEU A 57  ? 0.34801 0.28769 0.36886 0.03464  -0.04252 0.00232  64  LEU A CD2 
410  N N   . THR A 58  ? 0.34087 0.26399 0.32047 0.04489  -0.04332 0.02396  65  THR A N   
411  C CA  . THR A 58  ? 0.38398 0.30027 0.35273 0.04969  -0.04433 0.03040  65  THR A CA  
412  C C   . THR A 58  ? 0.42021 0.34021 0.37903 0.05359  -0.04778 0.03019  65  THR A C   
413  O O   . THR A 58  ? 0.44652 0.36146 0.39500 0.05858  -0.04957 0.03506  65  THR A O   
414  C CB  . THR A 58  ? 0.43900 0.34851 0.40322 0.04671  -0.03795 0.03681  65  THR A CB  
415  O OG1 . THR A 58  ? 0.47899 0.39343 0.44143 0.04252  -0.03418 0.03578  65  THR A OG1 
416  C CG2 . THR A 58  ? 0.45038 0.35518 0.42439 0.04332  -0.03503 0.03703  65  THR A CG2 
417  N N   . ASP A 59  ? 0.39097 0.31927 0.35231 0.05166  -0.04883 0.02469  66  ASP A N   
418  C CA  . ASP A 59  ? 0.38574 0.31790 0.33836 0.05516  -0.05225 0.02356  66  ASP A CA  
419  C C   . ASP A 59  ? 0.35375 0.29473 0.31502 0.05415  -0.05591 0.01564  66  ASP A C   
420  O O   . ASP A 59  ? 0.37774 0.32358 0.34235 0.04977  -0.05332 0.01252  66  ASP A O   
421  C CB  . ASP A 59  ? 0.39986 0.33152 0.34359 0.05301  -0.04737 0.02685  66  ASP A CB  
422  C CG  . ASP A 59  ? 0.46084 0.39614 0.39476 0.05690  -0.05076 0.02545  66  ASP A CG  
423  O OD1 . ASP A 59  ? 0.47074 0.40896 0.40499 0.06124  -0.05728 0.02182  66  ASP A OD1 
424  O OD2 . ASP A 59  ? 0.46005 0.39547 0.38635 0.05570  -0.04694 0.02767  66  ASP A OD2 
425  N N   . PRO A 60  ? 0.41927 0.36244 0.38489 0.05816  -0.06190 0.01226  67  PRO A N   
426  C CA  . PRO A 60  ? 0.35328 0.30482 0.32886 0.05683  -0.06490 0.00467  67  PRO A CA  
427  C C   . PRO A 60  ? 0.36663 0.32343 0.33774 0.05651  -0.06599 0.00171  67  PRO A C   
428  O O   . PRO A 60  ? 0.36555 0.32850 0.34500 0.05322  -0.06594 -0.00375 67  PRO A O   
429  C CB  . PRO A 60  ? 0.42779 0.38006 0.40693 0.06246  -0.07157 0.00254  67  PRO A CB  
430  C CG  . PRO A 60  ? 0.52944 0.47338 0.50594 0.06435  -0.07020 0.00834  67  PRO A CG  
431  C CD  . PRO A 60  ? 0.48911 0.42722 0.45252 0.06386  -0.06598 0.01501  67  PRO A CD  
432  N N   . SER A 61  ? 0.39294 0.34722 0.35091 0.05996  -0.06684 0.00516  68  SER A N   
433  C CA  . SER A 61  ? 0.37881 0.33801 0.33233 0.06018  -0.06826 0.00178  68  SER A CA  
434  C C   . SER A 61  ? 0.38305 0.34427 0.33923 0.05400  -0.06236 0.00109  68  SER A C   
435  O O   . SER A 61  ? 0.36260 0.32840 0.31811 0.05324  -0.06319 -0.00273 68  SER A O   
436  C CB  . SER A 61  ? 0.38496 0.34080 0.32269 0.06550  -0.06998 0.00571  68  SER A CB  
437  O OG  . SER A 61  ? 0.41617 0.36669 0.34557 0.06355  -0.06346 0.01218  68  SER A OG  
438  N N   . LYS A 62  ? 0.34315 0.30108 0.30279 0.04974  -0.05675 0.00436  69  LYS A N   
439  C CA  . LYS A 62  ? 0.33420 0.29449 0.29749 0.04410  -0.05179 0.00322  69  LYS A CA  
440  C C   . LYS A 62  ? 0.33065 0.29715 0.30463 0.04135  -0.05332 -0.00331 69  LYS A C   
441  O O   . LYS A 62  ? 0.28977 0.25887 0.26564 0.03762  -0.05043 -0.00499 69  LYS A O   
442  C CB  . LYS A 62  ? 0.34093 0.29691 0.30737 0.04031  -0.04641 0.00711  69  LYS A CB  
443  C CG  . LYS A 62  ? 0.38559 0.33500 0.34227 0.04205  -0.04358 0.01405  69  LYS A CG  
444  C CD  . LYS A 62  ? 0.37180 0.32160 0.32489 0.03861  -0.03816 0.01603  69  LYS A CD  
445  C CE  . LYS A 62  ? 0.41253 0.35644 0.35570 0.04020  -0.03468 0.02288  69  LYS A CE  
446  N NZ  . LYS A 62  ? 0.47713 0.42282 0.41894 0.03645  -0.02919 0.02387  69  LYS A NZ  
447  N N   . LEU A 63  ? 0.28923 0.25795 0.27082 0.04296  -0.05736 -0.00679 70  LEU A N   
448  C CA  . LEU A 63  ? 0.27590 0.25045 0.26818 0.04040  -0.05846 -0.01284 70  LEU A CA  
449  C C   . LEU A 63  ? 0.26348 0.24262 0.25555 0.04341  -0.06386 -0.01750 70  LEU A C   
450  O O   . LEU A 63  ? 0.28580 0.26980 0.28776 0.04188  -0.06550 -0.02278 70  LEU A O   
451  C CB  . LEU A 63  ? 0.30871 0.28378 0.31145 0.03977  -0.05887 -0.01453 70  LEU A CB  
452  C CG  . LEU A 63  ? 0.29357 0.26451 0.29792 0.03646  -0.05372 -0.01113 70  LEU A CG  
453  C CD1 . LEU A 63  ? 0.33471 0.30661 0.34948 0.03597  -0.05400 -0.01360 70  LEU A CD1 
454  C CD2 . LEU A 63  ? 0.29718 0.26939 0.30171 0.03138  -0.04897 -0.01134 70  LEU A CD2 
455  N N   . ASP A 64  ? 0.28557 0.26330 0.26666 0.04764  -0.06657 -0.01587 71  ASP A N   
456  C CA  . ASP A 64  ? 0.32322 0.30557 0.30433 0.05058  -0.07217 -0.02114 71  ASP A CA  
457  C C   . ASP A 64  ? 0.32432 0.31057 0.31029 0.04645  -0.07029 -0.02528 71  ASP A C   
458  O O   . ASP A 64  ? 0.32374 0.31466 0.31565 0.04702  -0.07429 -0.03112 71  ASP A O   
459  C CB  . ASP A 64  ? 0.36221 0.34212 0.32894 0.05602  -0.07503 -0.01862 71  ASP A CB  
460  C CG  . ASP A 64  ? 0.46650 0.44302 0.42866 0.06146  -0.07889 -0.01558 71  ASP A CG  
461  O OD1 . ASP A 64  ? 0.40428 0.38123 0.37573 0.06140  -0.08030 -0.01654 71  ASP A OD1 
462  O OD2 . ASP A 64  ? 0.46964 0.44293 0.41854 0.06607  -0.08047 -0.01218 71  ASP A OD2 
463  N N   . SER A 65  ? 0.30473 0.28899 0.28877 0.04231  -0.06434 -0.02241 72  SER A N   
464  C CA  . SER A 65  ? 0.25748 0.24423 0.24541 0.03830  -0.06181 -0.02522 72  SER A CA  
465  C C   . SER A 65  ? 0.32017 0.30915 0.32072 0.03387  -0.05985 -0.02784 72  SER A C   
466  O O   . SER A 65  ? 0.35058 0.34081 0.35459 0.03030  -0.05723 -0.02950 72  SER A O   
467  C CB  . SER A 65  ? 0.27899 0.26269 0.25931 0.03626  -0.05643 -0.02077 72  SER A CB  
468  O OG  . SER A 65  ? 0.29093 0.27084 0.27042 0.03496  -0.05283 -0.01577 72  SER A OG  
469  N N   . GLY A 66  ? 0.27177 0.26110 0.27894 0.03427  -0.06091 -0.02817 73  GLY A N   
470  C CA  . GLY A 66  ? 0.32507 0.31688 0.34398 0.03055  -0.05897 -0.03090 73  GLY A CA  
471  C C   . GLY A 66  ? 0.31003 0.29967 0.33184 0.03026  -0.05714 -0.02836 73  GLY A C   
472  O O   . GLY A 66  ? 0.27023 0.25581 0.28676 0.02914  -0.05360 -0.02390 73  GLY A O   
473  N N   . LYS A 67  ? 0.28671 0.27925 0.31781 0.03117  -0.05944 -0.03157 74  LYS A N   
474  C CA  . LYS A 67  ? 0.26881 0.25947 0.30340 0.03144  -0.05815 -0.02989 74  LYS A CA  
475  C C   . LYS A 67  ? 0.27808 0.26908 0.31893 0.02656  -0.05271 -0.03025 74  LYS A C   
476  O O   . LYS A 67  ? 0.33064 0.31883 0.37188 0.02609  -0.05039 -0.02807 74  LYS A O   
477  C CB  . LYS A 67  ? 0.34489 0.33901 0.38744 0.03496  -0.06307 -0.03356 74  LYS A CB  
478  C CG  . LYS A 67  ? 0.47791 0.47079 0.51345 0.04095  -0.06907 -0.03258 74  LYS A CG  
479  C CD  . LYS A 67  ? 0.56968 0.56393 0.61221 0.04470  -0.07300 -0.03434 74  LYS A CD  
480  C CE  . LYS A 67  ? 0.65167 0.64449 0.68654 0.05123  -0.07948 -0.03325 74  LYS A CE  
481  N NZ  . LYS A 67  ? 0.68546 0.67412 0.70581 0.05215  -0.07884 -0.02905 74  LYS A NZ  
482  N N   . GLU A 68  ? 0.27104 0.26515 0.31671 0.02312  -0.05069 -0.03306 75  GLU A N   
483  C CA  . GLU A 68  ? 0.29763 0.29229 0.34900 0.01904  -0.04577 -0.03362 75  GLU A CA  
484  C C   . GLU A 68  ? 0.26092 0.25155 0.30475 0.01653  -0.04165 -0.02967 75  GLU A C   
485  O O   . GLU A 68  ? 0.26787 0.25723 0.30508 0.01622  -0.04159 -0.02804 75  GLU A O   
486  C CB  . GLU A 68  ? 0.28969 0.28851 0.34892 0.01625  -0.04466 -0.03756 75  GLU A CB  
487  C CG  . GLU A 68  ? 0.37495 0.37896 0.44464 0.01791  -0.04829 -0.04249 75  GLU A CG  
488  C CD  . GLU A 68  ? 0.60331 0.60848 0.67037 0.02221  -0.05470 -0.04392 75  GLU A CD  
489  O OE1 . GLU A 68  ? 0.54412 0.54807 0.60442 0.02237  -0.05579 -0.04327 75  GLU A OE1 
490  O OE2 . GLU A 68  ? 0.66079 0.66823 0.73249 0.02571  -0.05880 -0.04595 75  GLU A OE2 
491  N N   . LEU A 69  ? 0.22586 0.21482 0.27113 0.01492  -0.03843 -0.02857 76  LEU A N   
492  C CA  . LEU A 69  ? 0.20273 0.18834 0.24218 0.01255  -0.03485 -0.02544 76  LEU A CA  
493  C C   . LEU A 69  ? 0.21329 0.20045 0.25676 0.00898  -0.03095 -0.02712 76  LEU A C   
494  O O   . LEU A 69  ? 0.23399 0.22194 0.28261 0.00847  -0.02935 -0.02868 76  LEU A O   
495  C CB  . LEU A 69  ? 0.22141 0.20326 0.25881 0.01392  -0.03466 -0.02293 76  LEU A CB  
496  C CG  . LEU A 69  ? 0.27549 0.25460 0.30751 0.01763  -0.03794 -0.02020 76  LEU A CG  
497  C CD1 . LEU A 69  ? 0.33969 0.31407 0.36995 0.01807  -0.03667 -0.01724 76  LEU A CD1 
498  C CD2 . LEU A 69  ? 0.25276 0.23123 0.27711 0.01767  -0.03817 -0.01810 76  LEU A CD2 
499  N N   . HIS A 70  ? 0.18463 0.17212 0.22557 0.00679  -0.02936 -0.02685 77  HIS A N   
500  C CA  . HIS A 70  ? 0.18694 0.17555 0.23093 0.00376  -0.02575 -0.02812 77  HIS A CA  
501  C C   . HIS A 70  ? 0.19475 0.18175 0.23302 0.00185  -0.02400 -0.02626 77  HIS A C   
502  O O   . HIS A 70  ? 0.19206 0.17786 0.22518 0.00277  -0.02556 -0.02456 77  HIS A O   
503  C CB  . HIS A 70  ? 0.21243 0.20465 0.26435 0.00333  -0.02609 -0.03147 77  HIS A CB  
504  C CG  . HIS A 70  ? 0.21889 0.21210 0.27047 0.00397  -0.02881 -0.03232 77  HIS A CG  
505  N ND1 . HIS A 70  ? 0.30585 0.30191 0.36266 0.00608  -0.03258 -0.03511 77  HIS A ND1 
506  C CD2 . HIS A 70  ? 0.24135 0.23322 0.28839 0.00297  -0.02852 -0.03124 77  HIS A CD2 
507  C CE1 . HIS A 70  ? 0.26068 0.25701 0.31585 0.00629  -0.03453 -0.03587 77  HIS A CE1 
508  N NE2 . HIS A 70  ? 0.27980 0.27351 0.32922 0.00440  -0.03196 -0.03352 77  HIS A NE2 
509  N N   . ILE A 71  ? 0.18334 0.17044 0.22259 -0.00057 -0.02065 -0.02666 78  ILE A N   
510  C CA  . ILE A 71  ? 0.16751 0.15305 0.20201 -0.00230 -0.01881 -0.02507 78  ILE A CA  
511  C C   . ILE A 71  ? 0.19632 0.18281 0.23473 -0.00412 -0.01667 -0.02642 78  ILE A C   
512  O O   . ILE A 71  ? 0.19452 0.18225 0.23736 -0.00513 -0.01423 -0.02781 78  ILE A O   
513  C CB  . ILE A 71  ? 0.18054 0.16435 0.21093 -0.00322 -0.01666 -0.02370 78  ILE A CB  
514  C CG1 . ILE A 71  ? 0.18079 0.16338 0.20912 -0.00181 -0.01829 -0.02255 78  ILE A CG1 
515  C CG2 . ILE A 71  ? 0.18254 0.16495 0.20806 -0.00452 -0.01532 -0.02218 78  ILE A CG2 
516  C CD1 . ILE A 71  ? 0.19430 0.17541 0.21991 -0.00284 -0.01653 -0.02203 78  ILE A CD1 
517  N N   . ASN A 72  ? 0.17220 0.15795 0.20930 -0.00454 -0.01729 -0.02603 79  ASN A N   
518  C CA  . ASN A 72  ? 0.15345 0.13895 0.19385 -0.00652 -0.01495 -0.02669 79  ASN A CA  
519  C C   . ASN A 72  ? 0.20611 0.18854 0.24027 -0.00752 -0.01311 -0.02420 79  ASN A C   
520  O O   . ASN A 72  ? 0.17962 0.16087 0.20870 -0.00648 -0.01493 -0.02284 79  ASN A O   
521  C CB  . ASN A 72  ? 0.18137 0.16821 0.22694 -0.00615 -0.01740 -0.02892 79  ASN A CB  
522  C CG  . ASN A 72  ? 0.18546 0.17577 0.23792 -0.00487 -0.01970 -0.03181 79  ASN A CG  
523  O OD1 . ASN A 72  ? 0.21454 0.20644 0.27069 -0.00513 -0.01809 -0.03257 79  ASN A OD1 
524  N ND2 . ASN A 72  ? 0.23167 0.22335 0.28600 -0.00318 -0.02371 -0.03377 79  ASN A ND2 
525  N N   . LEU A 73  ? 0.18589 0.16708 0.22060 -0.00937 -0.00944 -0.02359 80  LEU A N   
526  C CA  . LEU A 73  ? 0.15957 0.13743 0.18834 -0.01001 -0.00782 -0.02108 80  LEU A CA  
527  C C   . LEU A 73  ? 0.17484 0.15110 0.20776 -0.01149 -0.00630 -0.02127 80  LEU A C   
528  O O   . LEU A 73  ? 0.18901 0.16596 0.22753 -0.01318 -0.00334 -0.02219 80  LEU A O   
529  C CB  . LEU A 73  ? 0.16219 0.13897 0.18646 -0.01063 -0.00460 -0.01971 80  LEU A CB  
530  C CG  . LEU A 73  ? 0.17106 0.14942 0.19303 -0.00952 -0.00575 -0.02028 80  LEU A CG  
531  C CD1 . LEU A 73  ? 0.18092 0.15830 0.19857 -0.01006 -0.00254 -0.01967 80  LEU A CD1 
532  C CD2 . LEU A 73  ? 0.19149 0.16944 0.20915 -0.00813 -0.00901 -0.01929 80  LEU A CD2 
533  N N   . ILE A 74  ? 0.17794 0.15209 0.20885 -0.01094 -0.00809 -0.02057 81  ILE A N   
534  C CA  . ILE A 74  ? 0.17167 0.14389 0.20739 -0.01219 -0.00740 -0.02120 81  ILE A CA  
535  C C   . ILE A 74  ? 0.20203 0.16942 0.23210 -0.01234 -0.00591 -0.01817 81  ILE A C   
536  O O   . ILE A 74  ? 0.20281 0.16894 0.22921 -0.01077 -0.00848 -0.01767 81  ILE A O   
537  C CB  . ILE A 74  ? 0.18380 0.15784 0.22358 -0.01098 -0.01153 -0.02409 81  ILE A CB  
538  C CG1 . ILE A 74  ? 0.19548 0.17400 0.23873 -0.00993 -0.01377 -0.02652 81  ILE A CG1 
539  C CG2 . ILE A 74  ? 0.21890 0.19108 0.26563 -0.01272 -0.01061 -0.02555 81  ILE A CG2 
540  C CD1 . ILE A 74  ? 0.21969 0.20026 0.26546 -0.00813 -0.01819 -0.02938 81  ILE A CD1 
541  N N   . PRO A 75  ? 0.22004 0.18451 0.24942 -0.01402 -0.00166 -0.01606 82  PRO A N   
542  C CA  . PRO A 75  ? 0.21252 0.17160 0.23657 -0.01390 -0.00031 -0.01286 82  PRO A CA  
543  C C   . PRO A 75  ? 0.24644 0.20260 0.27684 -0.01512 -0.00007 -0.01362 82  PRO A C   
544  O O   . PRO A 75  ? 0.26468 0.22238 0.30386 -0.01708 0.00117  -0.01593 82  PRO A O   
545  C CB  . PRO A 75  ? 0.23127 0.18841 0.25149 -0.01507 0.00452  -0.01022 82  PRO A CB  
546  C CG  . PRO A 75  ? 0.29338 0.25431 0.32146 -0.01695 0.00683  -0.01269 82  PRO A CG  
547  C CD  . PRO A 75  ? 0.24891 0.21479 0.28248 -0.01598 0.00240  -0.01646 82  PRO A CD  
548  N N   . ASN A 76  ? 0.23330 0.18540 0.25991 -0.01384 -0.00153 -0.01205 83  ASN A N   
549  C CA  . ASN A 76  ? 0.24040 0.18852 0.27259 -0.01483 -0.00133 -0.01264 83  ASN A CA  
550  C C   . ASN A 76  ? 0.27196 0.21335 0.29759 -0.01408 0.00031  -0.00837 83  ASN A C   
551  O O   . ASN A 76  ? 0.30039 0.24080 0.32050 -0.01149 -0.00263 -0.00761 83  ASN A O   
552  C CB  . ASN A 76  ? 0.27879 0.22916 0.31439 -0.01328 -0.00610 -0.01638 83  ASN A CB  
553  C CG  . ASN A 76  ? 0.40847 0.35534 0.45178 -0.01462 -0.00603 -0.01823 83  ASN A CG  
554  O OD1 . ASN A 76  ? 0.35863 0.29932 0.40069 -0.01504 -0.00408 -0.01557 83  ASN A OD1 
555  N ND2 . ASN A 76  ? 0.39759 0.34815 0.44912 -0.01527 -0.00819 -0.02284 83  ASN A ND2 
556  N N   . LYS A 77  ? 0.29140 0.22807 0.31805 -0.01624 0.00508  -0.00557 84  LYS A N   
557  C CA  . LYS A 77  ? 0.27320 0.20275 0.29234 -0.01517 0.00682  -0.00080 84  LYS A CA  
558  C C   . LYS A 77  ? 0.33193 0.25643 0.35409 -0.01444 0.00488  -0.00103 84  LYS A C   
559  O O   . LYS A 77  ? 0.38222 0.30169 0.39752 -0.01223 0.00423  0.00223  84  LYS A O   
560  C CB  . LYS A 77  ? 0.36112 0.28640 0.37923 -0.01755 0.01316  0.00295  84  LYS A CB  
561  C CG  . LYS A 77  ? 0.37631 0.30512 0.38845 -0.01751 0.01553  0.00404  84  LYS A CG  
562  C CD  . LYS A 77  ? 0.40367 0.32795 0.41398 -0.01967 0.02241  0.00794  84  LYS A CD  
563  C CE  . LYS A 77  ? 0.45033 0.37838 0.45484 -0.01951 0.02503  0.00837  84  LYS A CE  
564  N NZ  . LYS A 77  ? 0.45636 0.39195 0.47043 -0.02127 0.02480  0.00354  84  LYS A NZ  
565  N N   . GLN A 78  ? 0.37194 0.29772 0.40426 -0.01594 0.00359  -0.00513 85  GLN A N   
566  C CA  . GLN A 78  ? 0.37567 0.29652 0.41121 -0.01510 0.00156  -0.00601 85  GLN A CA  
567  C C   . GLN A 78  ? 0.38991 0.31325 0.42068 -0.01133 -0.00369 -0.00773 85  GLN A C   
568  O O   . GLN A 78  ? 0.42854 0.34696 0.45669 -0.00927 -0.00504 -0.00637 85  GLN A O   
569  C CB  . GLN A 78  ? 0.42136 0.34297 0.46955 -0.01772 0.00138  -0.01061 85  GLN A CB  
570  C CG  . GLN A 78  ? 0.55908 0.47841 0.61505 -0.02197 0.00691  -0.00960 85  GLN A CG  
571  C CD  . GLN A 78  ? 0.67345 0.59589 0.72554 -0.02321 0.01092  -0.00699 85  GLN A CD  
572  O OE1 . GLN A 78  ? 0.67531 0.59268 0.72329 -0.02442 0.01610  -0.00203 85  GLN A OE1 
573  N NE2 . GLN A 78  ? 0.60494 0.53555 0.65813 -0.02273 0.00864  -0.01037 85  GLN A NE2 
574  N N   . ASP A 79  ? 0.31068 0.24150 0.34044 -0.01032 -0.00641 -0.01055 86  ASP A N   
575  C CA  . ASP A 79  ? 0.30658 0.24089 0.33215 -0.00707 -0.01067 -0.01220 86  ASP A CA  
576  C C   . ASP A 79  ? 0.28515 0.22020 0.30141 -0.00511 -0.01073 -0.00874 86  ASP A C   
577  O O   . ASP A 79  ? 0.30761 0.24485 0.32048 -0.00241 -0.01373 -0.00945 86  ASP A O   
578  C CB  . ASP A 79  ? 0.37535 0.31701 0.40421 -0.00701 -0.01319 -0.01654 86  ASP A CB  
579  C CG  . ASP A 79  ? 0.48872 0.43071 0.52643 -0.00805 -0.01464 -0.02108 86  ASP A CG  
580  O OD1 . ASP A 79  ? 0.50595 0.44244 0.54776 -0.00879 -0.01390 -0.02123 86  ASP A OD1 
581  O OD2 . ASP A 79  ? 0.46132 0.40882 0.50196 -0.00801 -0.01665 -0.02456 86  ASP A OD2 
582  N N   . ARG A 80  ? 0.30389 0.23722 0.31634 -0.00637 -0.00743 -0.00531 87  ARG A N   
583  C CA  . ARG A 80  ? 0.24881 0.18365 0.25274 -0.00475 -0.00761 -0.00275 87  ARG A CA  
584  C C   . ARG A 80  ? 0.26849 0.21069 0.27196 -0.00379 -0.01040 -0.00550 87  ARG A C   
585  O O   . ARG A 80  ? 0.27304 0.21717 0.27192 -0.00148 -0.01276 -0.00514 87  ARG A O   
586  C CB  . ARG A 80  ? 0.27486 0.20498 0.27249 -0.00192 -0.00886 0.00029  87  ARG A CB  
587  C CG  . ARG A 80  ? 0.28142 0.21112 0.27040 -0.00092 -0.00785 0.00357  87  ARG A CG  
588  C CD  . ARG A 80  ? 0.42832 0.35649 0.41096 0.00266  -0.01075 0.00536  87  ARG A CD  
589  N NE  . ARG A 80  ? 0.50495 0.42574 0.48720 0.00397  -0.01062 0.00776  87  ARG A NE  
590  C CZ  . ARG A 80  ? 0.57003 0.48951 0.55050 0.00733  -0.01396 0.00799  87  ARG A CZ  
591  N NH1 . ARG A 80  ? 0.43703 0.36250 0.41615 0.00957  -0.01750 0.00597  87  ARG A NH1 
592  N NH2 . ARG A 80  ? 0.51110 0.42295 0.49152 0.00850  -0.01358 0.01037  87  ARG A NH2 
593  N N   . THR A 81  ? 0.24139 0.18765 0.24998 -0.00562 -0.00997 -0.00814 88  THR A N   
594  C CA  . THR A 81  ? 0.23113 0.18359 0.23951 -0.00489 -0.01219 -0.01037 88  THR A CA  
595  C C   . THR A 81  ? 0.21301 0.16831 0.22215 -0.00662 -0.01019 -0.01057 88  THR A C   
596  O O   . THR A 81  ? 0.22798 0.18220 0.24124 -0.00874 -0.00751 -0.01072 88  THR A O   
597  C CB  . THR A 81  ? 0.24572 0.20096 0.25905 -0.00431 -0.01485 -0.01398 88  THR A CB  
598  O OG1 . THR A 81  ? 0.26155 0.21647 0.28195 -0.00631 -0.01393 -0.01610 88  THR A OG1 
599  C CG2 . THR A 81  ? 0.25663 0.21013 0.26870 -0.00200 -0.01711 -0.01439 88  THR A CG2 
600  N N   . LEU A 82  ? 0.19755 0.15652 0.20332 -0.00570 -0.01140 -0.01075 89  LEU A N   
601  C CA  . LEU A 82  ? 0.21906 0.18133 0.22627 -0.00685 -0.01031 -0.01175 89  LEU A CA  
602  C C   . LEU A 82  ? 0.21006 0.17655 0.21934 -0.00589 -0.01315 -0.01402 89  LEU A C   
603  O O   . LEU A 82  ? 0.20643 0.17416 0.21256 -0.00433 -0.01510 -0.01374 89  LEU A O   
604  C CB  . LEU A 82  ? 0.20361 0.16582 0.20482 -0.00659 -0.00907 -0.00999 89  LEU A CB  
605  C CG  . LEU A 82  ? 0.18826 0.15383 0.19125 -0.00752 -0.00811 -0.01147 89  LEU A CG  
606  C CD1 . LEU A 82  ? 0.23388 0.19926 0.24213 -0.00951 -0.00501 -0.01222 89  LEU A CD1 
607  C CD2 . LEU A 82  ? 0.22544 0.19086 0.22211 -0.00695 -0.00738 -0.01033 89  LEU A CD2 
608  N N   . THR A 83  ? 0.18268 0.15130 0.19739 -0.00665 -0.01339 -0.01622 90  THR A N   
609  C CA  . THR A 83  ? 0.17749 0.14950 0.19340 -0.00540 -0.01609 -0.01804 90  THR A CA  
610  C C   . THR A 83  ? 0.22392 0.19843 0.24077 -0.00579 -0.01560 -0.01846 90  THR A C   
611  O O   . THR A 83  ? 0.20940 0.18418 0.22991 -0.00716 -0.01371 -0.01913 90  THR A O   
612  C CB  . THR A 83  ? 0.22638 0.19895 0.24738 -0.00517 -0.01781 -0.02066 90  THR A CB  
613  O OG1 . THR A 83  ? 0.22124 0.19102 0.24168 -0.00471 -0.01828 -0.02056 90  THR A OG1 
614  C CG2 . THR A 83  ? 0.25091 0.22668 0.27149 -0.00334 -0.02067 -0.02221 90  THR A CG2 
615  N N   . ILE A 84  ? 0.18347 0.15967 0.19751 -0.00463 -0.01699 -0.01806 91  ILE A N   
616  C CA  . ILE A 84  ? 0.20083 0.17885 0.21593 -0.00468 -0.01691 -0.01848 91  ILE A CA  
617  C C   . ILE A 84  ? 0.21641 0.19620 0.23299 -0.00317 -0.01942 -0.01961 91  ILE A C   
618  O O   . ILE A 84  ? 0.20642 0.18651 0.21987 -0.00189 -0.02075 -0.01889 91  ILE A O   
619  C CB  . ILE A 84  ? 0.21856 0.19656 0.22966 -0.00462 -0.01644 -0.01711 91  ILE A CB  
620  C CG1 . ILE A 84  ? 0.25398 0.23024 0.26224 -0.00555 -0.01442 -0.01612 91  ILE A CG1 
621  C CG2 . ILE A 84  ? 0.20221 0.18150 0.21500 -0.00453 -0.01655 -0.01772 91  ILE A CG2 
622  C CD1 . ILE A 84  ? 0.30852 0.28325 0.31297 -0.00493 -0.01493 -0.01474 91  ILE A CD1 
623  N N   . VAL A 85  ? 0.16969 0.15082 0.19091 -0.00310 -0.02003 -0.02138 92  VAL A N   
624  C CA  . VAL A 85  ? 0.16603 0.14870 0.18821 -0.00116 -0.02292 -0.02260 92  VAL A CA  
625  C C   . VAL A 85  ? 0.23727 0.22072 0.26016 -0.00047 -0.02323 -0.02230 92  VAL A C   
626  O O   . VAL A 85  ? 0.21829 0.20222 0.24490 -0.00150 -0.02176 -0.02308 92  VAL A O   
627  C CB  . VAL A 85  ? 0.21152 0.19543 0.23951 -0.00114 -0.02431 -0.02551 92  VAL A CB  
628  C CG1 . VAL A 85  ? 0.24062 0.22615 0.26808 0.00153  -0.02802 -0.02693 92  VAL A CG1 
629  C CG2 . VAL A 85  ? 0.24592 0.22827 0.27493 -0.00235 -0.02347 -0.02604 92  VAL A CG2 
630  N N   A ASP A 86  ? 0.20240 0.18578 0.22184 0.00140  -0.02491 -0.02115 93  ASP A N   
631  N N   B ASP A 86  ? 0.20240 0.18578 0.22184 0.00140  -0.02491 -0.02115 93  ASP A N   
632  C CA  A ASP A 86  ? 0.19837 0.18182 0.21889 0.00252  -0.02568 -0.02084 93  ASP A CA  
633  C CA  B ASP A 86  ? 0.19837 0.18182 0.21889 0.00252  -0.02568 -0.02084 93  ASP A CA  
634  C C   A ASP A 86  ? 0.21487 0.19878 0.23353 0.00536  -0.02880 -0.02096 93  ASP A C   
635  C C   B ASP A 86  ? 0.21487 0.19878 0.23353 0.00536  -0.02880 -0.02096 93  ASP A C   
636  O O   A ASP A 86  ? 0.20880 0.19286 0.22388 0.00640  -0.02991 -0.02087 93  ASP A O   
637  O O   B ASP A 86  ? 0.20880 0.19286 0.22388 0.00640  -0.02991 -0.02087 93  ASP A O   
638  C CB  A ASP A 86  ? 0.19986 0.18165 0.21759 0.00183  -0.02394 -0.01855 93  ASP A CB  
639  C CB  B ASP A 86  ? 0.19986 0.18165 0.21759 0.00183  -0.02394 -0.01855 93  ASP A CB  
640  C CG  A ASP A 86  ? 0.22439 0.20531 0.23690 0.00258  -0.02406 -0.01625 93  ASP A CG  
641  C CG  B ASP A 86  ? 0.22439 0.20531 0.23690 0.00258  -0.02406 -0.01625 93  ASP A CG  
642  O OD1 A ASP A 86  ? 0.22464 0.20519 0.23478 0.00466  -0.02561 -0.01527 93  ASP A OD1 
643  O OD1 B ASP A 86  ? 0.22464 0.20519 0.23478 0.00466  -0.02561 -0.01527 93  ASP A OD1 
644  O OD2 A ASP A 86  ? 0.20970 0.19041 0.22042 0.00123  -0.02251 -0.01542 93  ASP A OD2 
645  O OD2 B ASP A 86  ? 0.20970 0.19041 0.22042 0.00123  -0.02251 -0.01542 93  ASP A OD2 
646  N N   . THR A 87  ? 0.18896 0.17305 0.20979 0.00694  -0.03035 -0.02131 94  THR A N   
647  C CA  . THR A 87  ? 0.16866 0.15277 0.18674 0.01024  -0.03363 -0.02107 94  THR A CA  
648  C C   . THR A 87  ? 0.20896 0.19021 0.22238 0.01141  -0.03302 -0.01752 94  THR A C   
649  O O   . THR A 87  ? 0.20597 0.18628 0.21856 0.01409  -0.03523 -0.01681 94  THR A O   
650  C CB  . THR A 87  ? 0.22706 0.21350 0.25133 0.01175  -0.03652 -0.02422 94  THR A CB  
651  O OG1 . THR A 87  ? 0.19645 0.18294 0.22609 0.01077  -0.03507 -0.02465 94  THR A OG1 
652  C CG2 . THR A 87  ? 0.23284 0.22189 0.26200 0.01046  -0.03705 -0.02770 94  THR A CG2 
653  N N   . GLY A 88  ? 0.19109 0.17079 0.20168 0.00950  -0.03010 -0.01522 95  GLY A N   
654  C CA  . GLY A 88  ? 0.21015 0.18695 0.21732 0.01004  -0.02899 -0.01185 95  GLY A CA  
655  C C   . GLY A 88  ? 0.20132 0.17715 0.20163 0.01246  -0.02980 -0.00950 95  GLY A C   
656  O O   . GLY A 88  ? 0.20078 0.17814 0.19868 0.01460  -0.03222 -0.01089 95  GLY A O   
657  N N   . ILE A 89  ? 0.19232 0.16562 0.18947 0.01198  -0.02744 -0.00602 96  ILE A N   
658  C CA  . ILE A 89  ? 0.18352 0.15529 0.17349 0.01441  -0.02737 -0.00302 96  ILE A CA  
659  C C   . ILE A 89  ? 0.22211 0.19638 0.20830 0.01451  -0.02682 -0.00380 96  ILE A C   
660  O O   . ILE A 89  ? 0.22180 0.19578 0.20144 0.01725  -0.02751 -0.00256 96  ILE A O   
661  C CB  . ILE A 89  ? 0.21376 0.18187 0.20276 0.01339  -0.02432 0.00104  96  ILE A CB  
662  C CG1 . ILE A 89  ? 0.27955 0.24492 0.26071 0.01637  -0.02399 0.00498  96  ILE A CG1 
663  C CG2 . ILE A 89  ? 0.21518 0.18449 0.20685 0.00983  -0.02098 0.00109  96  ILE A CG2 
664  C CD1 . ILE A 89  ? 0.28533 0.24586 0.26678 0.01581  -0.02162 0.00906  96  ILE A CD1 
665  N N   . GLY A 90  ? 0.21170 0.18824 0.20136 0.01195  -0.02565 -0.00588 97  GLY A N   
666  C CA  . GLY A 90  ? 0.22696 0.20560 0.21361 0.01230  -0.02523 -0.00682 97  GLY A CA  
667  C C   . GLY A 90  ? 0.20853 0.18678 0.19205 0.01167  -0.02183 -0.00380 97  GLY A C   
668  O O   . GLY A 90  ? 0.22615 0.20237 0.21044 0.01053  -0.01967 -0.00101 97  GLY A O   
669  N N   . MET A 91  ? 0.20818 0.18851 0.18889 0.01236  -0.02121 -0.00467 98  MET A N   
670  C CA  . MET A 91  ? 0.20567 0.18671 0.18420 0.01183  -0.01767 -0.00239 98  MET A CA  
671  C C   . MET A 91  ? 0.20567 0.18777 0.17721 0.01487  -0.01760 -0.00240 98  MET A C   
672  O O   . MET A 91  ? 0.25670 0.24020 0.22696 0.01652  -0.02025 -0.00561 98  MET A O   
673  C CB  . MET A 91  ? 0.22235 0.20575 0.20578 0.00929  -0.01622 -0.00384 98  MET A CB  
674  C CG  . MET A 91  ? 0.23092 0.21355 0.22038 0.00632  -0.01575 -0.00377 98  MET A CG  
675  S SD  . MET A 91  ? 0.23036 0.21566 0.22455 0.00413  -0.01520 -0.00583 98  MET A SD  
676  C CE  . MET A 91  ? 0.24188 0.22713 0.23633 0.00489  -0.01828 -0.00899 98  MET A CE  
677  N N   . THR A 92  ? 0.23287 0.21422 0.20013 0.01548  -0.01429 0.00107  99  THR A N   
678  C CA  . THR A 92  ? 0.24269 0.22545 0.20273 0.01828  -0.01313 0.00121  99  THR A CA  
679  C C   . THR A 92  ? 0.22805 0.21450 0.19115 0.01719  -0.01143 -0.00108 99  THR A C   
680  O O   . THR A 92  ? 0.22356 0.21121 0.19377 0.01429  -0.01082 -0.00195 99  THR A O   
681  C CB  . THR A 92  ? 0.25028 0.23093 0.20485 0.01905  -0.00914 0.00617  99  THR A CB  
682  O OG1 . THR A 92  ? 0.27079 0.25208 0.23143 0.01550  -0.00489 0.00817  99  THR A OG1 
683  C CG2 . THR A 92  ? 0.29430 0.27059 0.24578 0.02045  -0.01089 0.00888  99  THR A CG2 
684  N N   . LYS A 93  ? 0.23422 0.22251 0.19157 0.01989  -0.01079 -0.00223 100 LYS A N   
685  C CA  . LYS A 93  ? 0.25537 0.24722 0.21568 0.01926  -0.00877 -0.00422 100 LYS A CA  
686  C C   . LYS A 93  ? 0.23147 0.22458 0.19645 0.01645  -0.00413 -0.00137 100 LYS A C   
687  O O   . LYS A 93  ? 0.22287 0.21844 0.19471 0.01444  -0.00363 -0.00297 100 LYS A O   
688  C CB  . LYS A 93  ? 0.27404 0.26758 0.22674 0.02291  -0.00812 -0.00567 100 LYS A CB  
689  C CG  . LYS A 93  ? 0.27686 0.27402 0.23314 0.02290  -0.00705 -0.00882 100 LYS A CG  
690  C CD  . LYS A 93  ? 0.28148 0.28048 0.22986 0.02674  -0.00584 -0.01045 100 LYS A CD  
691  C CE  . LYS A 93  ? 0.34161 0.34410 0.29458 0.02694  -0.00507 -0.01401 100 LYS A CE  
692  N NZ  . LYS A 93  ? 0.31250 0.31750 0.25862 0.03013  -0.00188 -0.01469 100 LYS A NZ  
693  N N   . ALA A 94  ? 0.26932 0.26064 0.23092 0.01636  -0.00078 0.00289  101 ALA A N   
694  C CA  . ALA A 94  ? 0.29220 0.28470 0.25933 0.01338  0.00390  0.00549  101 ALA A CA  
695  C C   . ALA A 94  ? 0.26628 0.25823 0.24238 0.00988  0.00235  0.00483  101 ALA A C   
696  O O   . ALA A 94  ? 0.28533 0.28021 0.26867 0.00746  0.00418  0.00411  101 ALA A O   
697  C CB  . ALA A 94  ? 0.30459 0.29403 0.26634 0.01383  0.00781  0.01061  101 ALA A CB  
698  N N   . ASP A 95  ? 0.25304 0.24156 0.22889 0.00976  -0.00113 0.00476  102 ASP A N   
699  C CA  . ASP A 95  ? 0.24497 0.23301 0.22844 0.00680  -0.00273 0.00362  102 ASP A CA  
700  C C   . ASP A 95  ? 0.23009 0.22141 0.21793 0.00619  -0.00465 -0.00015 102 ASP A C   
701  O O   . ASP A 95  ? 0.24265 0.23556 0.23699 0.00378  -0.00425 -0.00098 102 ASP A O   
702  C CB  . ASP A 95  ? 0.26949 0.25386 0.25188 0.00726  -0.00619 0.00351  102 ASP A CB  
703  C CG  . ASP A 95  ? 0.34098 0.32121 0.32023 0.00778  -0.00489 0.00740  102 ASP A CG  
704  O OD1 . ASP A 95  ? 0.32529 0.30459 0.30626 0.00615  -0.00107 0.01041  102 ASP A OD1 
705  O OD2 . ASP A 95  ? 0.33245 0.31011 0.30829 0.00975  -0.00788 0.00737  102 ASP A OD2 
706  N N   . LEU A 96  ? 0.23813 0.23013 0.22251 0.00849  -0.00711 -0.00263 103 LEU A N   
707  C CA  . LEU A 96  ? 0.24591 0.23999 0.23413 0.00810  -0.00894 -0.00579 103 LEU A CA  
708  C C   . LEU A 96  ? 0.23716 0.23503 0.22925 0.00739  -0.00632 -0.00606 103 LEU A C   
709  O O   . LEU A 96  ? 0.23670 0.23606 0.23431 0.00586  -0.00712 -0.00736 103 LEU A O   
710  C CB  . LEU A 96  ? 0.22932 0.22332 0.21373 0.01070  -0.01146 -0.00843 103 LEU A CB  
711  C CG  . LEU A 96  ? 0.23816 0.22948 0.22131 0.01121  -0.01486 -0.00961 103 LEU A CG  
712  C CD1 . LEU A 96  ? 0.23823 0.22997 0.21820 0.01383  -0.01699 -0.01259 103 LEU A CD1 
713  C CD2 . LEU A 96  ? 0.21832 0.20868 0.20693 0.00880  -0.01628 -0.01042 103 LEU A CD2 
714  N N   . ILE A 97  ? 0.23034 0.23006 0.21949 0.00874  -0.00316 -0.00494 104 ILE A N   
715  C CA  . ILE A 97  ? 0.21872 0.22291 0.21242 0.00830  -0.00038 -0.00560 104 ILE A CA  
716  C C   . ILE A 97  ? 0.23593 0.24121 0.23676 0.00504  0.00163  -0.00410 104 ILE A C   
717  O O   . ILE A 97  ? 0.24135 0.25015 0.24888 0.00396  0.00159  -0.00584 104 ILE A O   
718  C CB  . ILE A 97  ? 0.22073 0.22676 0.20928 0.01055  0.00322  -0.00471 104 ILE A CB  
719  C CG1 . ILE A 97  ? 0.24525 0.25088 0.22802 0.01390  0.00054  -0.00754 104 ILE A CG1 
720  C CG2 . ILE A 97  ? 0.23925 0.25048 0.23374 0.00975  0.00720  -0.00500 104 ILE A CG2 
721  C CD1 . ILE A 97  ? 0.27707 0.28331 0.25186 0.01674  0.00337  -0.00664 104 ILE A CD1 
722  N N   . ASN A 98  ? 0.21458 0.21672 0.21443 0.00359  0.00300  -0.00114 105 ASN A N   
723  C CA  . ASN A 98  ? 0.24665 0.24899 0.25355 0.00034  0.00468  0.00005  105 ASN A CA  
724  C C   . ASN A 98  ? 0.23015 0.23099 0.24077 -0.00118 0.00072  -0.00188 105 ASN A C   
725  O O   . ASN A 98  ? 0.24792 0.24541 0.25937 -0.00271 0.00032  -0.00062 105 ASN A O   
726  C CB  . ASN A 98  ? 0.28828 0.28693 0.29213 -0.00029 0.00784  0.00418  105 ASN A CB  
727  C CG  . ASN A 98  ? 0.46940 0.46894 0.48104 -0.00359 0.01149  0.00576  105 ASN A CG  
728  O OD1 . ASN A 98  ? 0.51019 0.51420 0.53014 -0.00540 0.01186  0.00346  105 ASN A OD1 
729  N ND2 . ASN A 98  ? 0.47313 0.46815 0.48268 -0.00439 0.01397  0.00963  105 ASN A ND2 
730  N N   . ASN A 99  ? 0.21533 0.21849 0.22783 -0.00051 -0.00209 -0.00493 106 ASN A N   
731  C CA  . ASN A 99  ? 0.18149 0.18375 0.19696 -0.00170 -0.00546 -0.00681 106 ASN A CA  
732  C C   . ASN A 99  ? 0.22735 0.22489 0.23893 -0.00173 -0.00741 -0.00613 106 ASN A C   
733  O O   . ASN A 99  ? 0.21156 0.20760 0.22586 -0.00345 -0.00846 -0.00652 106 ASN A O   
734  C CB  . ASN A 99  ? 0.18374 0.18826 0.20701 -0.00434 -0.00467 -0.00741 106 ASN A CB  
735  C CG  . ASN A 99  ? 0.20506 0.21515 0.23363 -0.00420 -0.00308 -0.00867 106 ASN A CG  
736  O OD1 . ASN A 99  ? 0.23269 0.24487 0.26048 -0.00223 -0.00494 -0.01056 106 ASN A OD1 
737  N ND2 . ASN A 99  ? 0.25567 0.26809 0.29016 -0.00622 0.00034  -0.00774 106 ASN A ND2 
738  N N   . LEU A 100 ? 0.22702 0.22266 0.23267 0.00038  -0.00818 -0.00573 107 LEU A N   
739  C CA  . LEU A 100 ? 0.23803 0.23000 0.24076 0.00074  -0.01040 -0.00573 107 LEU A CA  
740  C C   . LEU A 100 ? 0.26218 0.25145 0.26617 -0.00075 -0.00944 -0.00379 107 LEU A C   
741  O O   . LEU A 100 ? 0.23393 0.22117 0.23929 -0.00164 -0.01105 -0.00452 107 LEU A O   
742  C CB  . LEU A 100 ? 0.22935 0.22100 0.23325 0.00049  -0.01318 -0.00807 107 LEU A CB  
743  C CG  . LEU A 100 ? 0.27039 0.26390 0.27329 0.00212  -0.01407 -0.00972 107 LEU A CG  
744  C CD1 . LEU A 100 ? 0.26189 0.25807 0.26862 0.00158  -0.01434 -0.01090 107 LEU A CD1 
745  C CD2 . LEU A 100 ? 0.33943 0.33073 0.33999 0.00311  -0.01634 -0.01102 107 LEU A CD2 
746  N N   . GLY A 101 ? 0.24366 0.23271 0.24729 -0.00097 -0.00645 -0.00123 108 GLY A N   
747  C CA  . GLY A 101 ? 0.27449 0.25994 0.27876 -0.00199 -0.00539 0.00111  108 GLY A CA  
748  C C   . GLY A 101 ? 0.29727 0.28263 0.30852 -0.00492 -0.00485 0.00045  108 GLY A C   
749  O O   . GLY A 101 ? 0.30600 0.28776 0.31848 -0.00577 -0.00471 0.00164  108 GLY A O   
750  N N   . THR A 102 ? 0.23802 0.22723 0.25415 -0.00629 -0.00484 -0.00170 109 THR A N   
751  C CA  . THR A 102 ? 0.24745 0.23735 0.27051 -0.00886 -0.00512 -0.00336 109 THR A CA  
752  C C   . THR A 102 ? 0.26508 0.25758 0.29399 -0.01073 -0.00179 -0.00248 109 THR A C   
753  O O   . THR A 102 ? 0.27213 0.26695 0.29969 -0.00986 0.00067  -0.00109 109 THR A O   
754  C CB  . THR A 102 ? 0.25085 0.24341 0.27533 -0.00878 -0.00826 -0.00691 109 THR A CB  
755  O OG1 . THR A 102 ? 0.26048 0.25744 0.28617 -0.00806 -0.00795 -0.00781 109 THR A OG1 
756  C CG2 . THR A 102 ? 0.28910 0.27951 0.30815 -0.00707 -0.01082 -0.00766 109 THR A CG2 
757  N N   . ILE A 103 ? 0.23310 0.22541 0.26903 -0.01333 -0.00161 -0.00364 110 ILE A N   
758  C CA  . ILE A 103 ? 0.22299 0.21881 0.26688 -0.01558 0.00117  -0.00385 110 ILE A CA  
759  C C   . ILE A 103 ? 0.23021 0.23135 0.27882 -0.01576 -0.00175 -0.00810 110 ILE A C   
760  O O   . ILE A 103 ? 0.21190 0.21471 0.26787 -0.01781 -0.00292 -0.01083 110 ILE A O   
761  C CB  . ILE A 103 ? 0.28269 0.27501 0.33240 -0.01840 0.00347  -0.00248 110 ILE A CB  
762  C CG1 . ILE A 103 ? 0.26700 0.25652 0.31855 -0.01922 0.00011  -0.00515 110 ILE A CG1 
763  C CG2 . ILE A 103 ? 0.26584 0.25319 0.31024 -0.01769 0.00713  0.00273  110 ILE A CG2 
764  C CD1 . ILE A 103 ? 0.28784 0.27496 0.34801 -0.02245 0.00193  -0.00528 110 ILE A CD1 
765  N N   . ALA A 104 ? 0.23717 0.23170 0.23776 0.04466  0.01841  0.01708  111 ALA A N   
766  C CA  . ALA A 104 ? 0.24938 0.26462 0.24987 0.03032  0.00940  0.00227  111 ALA A CA  
767  C C   . ALA A 104 ? 0.23240 0.26354 0.23398 0.01313  0.01509  -0.00298 111 ALA A C   
768  O O   . ALA A 104 ? 0.22870 0.27023 0.23409 -0.00390 0.01415  -0.01749 111 ALA A O   
769  C CB  . ALA A 104 ? 0.26833 0.30237 0.25884 0.04458  -0.01267 0.00367  111 ALA A CB  
770  N N   . LYS A 105 ? 0.22288 0.25714 0.22131 0.01740  0.02075  0.00842  112 LYS A N   
771  C CA  . LYS A 105 ? 0.27284 0.32187 0.27431 0.00033  0.02688  0.00333  112 LYS A CA  
772  C C   . LYS A 105 ? 0.29100 0.32473 0.30750 -0.02032 0.04384  -0.00709 112 LYS A C   
773  O O   . LYS A 105 ? 0.26213 0.30764 0.28266 -0.03796 0.04299  -0.02179 112 LYS A O   
774  C CB  . LYS A 105 ? 0.23675 0.29143 0.23302 0.00971  0.03096  0.01888  112 LYS A CB  
775  C CG  . LYS A 105 ? 0.34744 0.42464 0.34410 -0.00441 0.03166  0.01434  112 LYS A CG  
776  C CD  . LYS A 105 ? 0.34477 0.42113 0.34128 0.00156  0.04256  0.03024  112 LYS A CD  
777  C CE  . LYS A 105 ? 0.46944 0.55812 0.47461 -0.01844 0.05170  0.02477  112 LYS A CE  
778  N NZ  . LYS A 105 ? 0.51448 0.62752 0.50927 -0.01015 0.04483  0.03393  112 LYS A NZ  
779  N N   . SER A 106 ? 0.26711 0.27373 0.29233 -0.01782 0.05838  -0.00079 113 SER A N   
780  C CA  . SER A 106 ? 0.29609 0.28826 0.33680 -0.03737 0.07370  -0.01165 113 SER A CA  
781  C C   . SER A 106 ? 0.27160 0.25994 0.31555 -0.04526 0.06972  -0.02805 113 SER A C   
782  O O   . SER A 106 ? 0.31110 0.30124 0.36374 -0.06407 0.07536  -0.04286 113 SER A O   
783  C CB  . SER A 106 ? 0.37276 0.33705 0.42373 -0.03394 0.09100  -0.00065 113 SER A CB  
784  O OG  . SER A 106 ? 0.36720 0.31457 0.41371 -0.01564 0.08849  0.00825  113 SER A OG  
785  N N   A GLY A 107 ? 0.25096 0.23554 0.28800 -0.03061 0.05943  -0.02564 114 GLY A N   
786  N N   B GLY A 107 ? 0.25551 0.23736 0.29383 -0.03120 0.06105  -0.02587 114 GLY A N   
787  C CA  A GLY A 107 ? 0.25458 0.23880 0.29390 -0.03696 0.05469  -0.04014 114 GLY A CA  
788  C CA  B GLY A 107 ? 0.26965 0.24873 0.31141 -0.03817 0.05799  -0.04052 114 GLY A CA  
789  C C   A GLY A 107 ? 0.27457 0.28554 0.30945 -0.04929 0.04406  -0.05357 114 GLY A C   
790  C C   B GLY A 107 ? 0.27728 0.28212 0.31526 -0.05133 0.04804  -0.05487 114 GLY A C   
791  O O   A GLY A 107 ? 0.25696 0.26843 0.29756 -0.06363 0.04700  -0.06888 114 GLY A O   
792  O O   B GLY A 107 ? 0.28159 0.28555 0.32644 -0.06686 0.05287  -0.07019 114 GLY A O   
793  N N   A THR A 108 ? 0.23105 0.26495 0.25524 -0.04305 0.03094  -0.04828 115 THR A N   
794  N N   B THR A 108 ? 0.25003 0.27834 0.27664 -0.04429 0.03324  -0.05034 115 THR A N   
795  C CA  A THR A 108 ? 0.25586 0.31580 0.27585 -0.05487 0.02063  -0.06058 115 THR A CA  
796  C CA  B THR A 108 ? 0.26414 0.31851 0.28676 -0.05673 0.02378  -0.06244 115 THR A CA  
797  C C   A THR A 108 ? 0.27917 0.34232 0.30741 -0.07594 0.03197  -0.07133 115 THR A C   
798  C C   B THR A 108 ? 0.28726 0.34337 0.31851 -0.07706 0.03604  -0.07190 115 THR A C   
799  O O   A THR A 108 ? 0.27149 0.34449 0.30174 -0.09016 0.03002  -0.08686 115 THR A O   
800  O O   B THR A 108 ? 0.28961 0.35487 0.32373 -0.09237 0.03543  -0.08767 115 THR A O   
801  C CB  A THR A 108 ? 0.24364 0.32720 0.25152 -0.04422 0.00482  -0.05261 115 THR A CB  
802  C CB  B THR A 108 ? 0.25556 0.33304 0.26596 -0.04560 0.00803  -0.05394 115 THR A CB  
803  O OG1 A THR A 108 ? 0.23400 0.31623 0.23532 -0.02509 -0.00793 -0.04473 115 THR A OG1 
804  O OG1 B THR A 108 ? 0.24878 0.32332 0.25275 -0.02564 -0.00372 -0.04483 115 THR A OG1 
805  C CG2 A THR A 108 ? 0.25214 0.36194 0.25641 -0.05716 -0.00525 -0.06536 115 THR A CG2 
806  C CG2 B THR A 108 ? 0.25899 0.36330 0.26515 -0.05752 -0.00321 -0.06654 115 THR A CG2 
807  N N   A LYS A 109 ? 0.26477 0.32034 0.29830 -0.07787 0.04363  -0.06309 116 LYS A N   
808  N N   B LYS A 109 ? 0.27650 0.32436 0.31244 -0.07701 0.04712  -0.06210 116 LYS A N   
809  C CA  A LYS A 109 ? 0.27321 0.33080 0.31719 -0.09789 0.05468  -0.07284 116 LYS A CA  
810  C CA  B LYS A 109 ? 0.29171 0.33693 0.33958 -0.09588 0.06058  -0.06990 116 LYS A CA  
811  C C   A LYS A 109 ? 0.36488 0.40758 0.41982 -0.11130 0.06358  -0.08830 116 LYS A C   
812  C C   B LYS A 109 ? 0.34462 0.37029 0.40473 -0.10743 0.07149  -0.08291 116 LYS A C   
813  O O   A LYS A 109 ? 0.35670 0.40957 0.41029 -0.12116 0.06101  -0.10087 116 LYS A O   
814  O O   B LYS A 109 ? 0.36070 0.39455 0.42485 -0.12326 0.07156  -0.09965 116 LYS A O   
815  C CB  A LYS A 109 ? 0.30384 0.35092 0.35459 -0.09620 0.06773  -0.05931 116 LYS A CB  
816  C CB  B LYS A 109 ? 0.32676 0.36231 0.37943 -0.09118 0.07192  -0.05423 116 LYS A CB  
817  C CG  A LYS A 109 ? 0.41496 0.46116 0.48017 -0.11621 0.08085  -0.06703 116 LYS A CG  
818  C CG  B LYS A 109 ? 0.43213 0.47847 0.49295 -0.10717 0.07930  -0.05778 116 LYS A CG  
819  C CD  A LYS A 109 ? 0.44135 0.47384 0.51408 -0.11110 0.09431  -0.05011 116 LYS A CD  
820  C CD  B LYS A 109 ? 0.45175 0.48013 0.52351 -0.10562 0.09568  -0.04396 116 LYS A CD  
821  C CE  A LYS A 109 ? 0.57703 0.59453 0.67000 -0.12847 0.11147  -0.05598 116 LYS A CE  
822  C CE  B LYS A 109 ? 0.54234 0.56972 0.63112 -0.12666 0.10805  -0.05288 116 LYS A CE  
823  N NZ  A LYS A 109 ? 0.55854 0.59380 0.65495 -0.14603 0.10766  -0.07253 116 LYS A NZ  
824  N NZ  B LYS A 109 ? 0.51674 0.56855 0.60290 -0.14092 0.09869  -0.06943 116 LYS A NZ  
825  N N   A ALA A 110 ? 0.29893 0.31592 0.35984 -0.10454 0.07215  -0.08423 117 ALA A N   
826  N N   B ALA A 110 ? 0.31387 0.31349 0.37969 -0.09883 0.08062  -0.07542 117 ALA A N   
827  C CA  A ALA A 110 ? 0.36746 0.36942 0.43896 -0.11602 0.08085  -0.09894 117 ALA A CA  
828  C CA  B ALA A 110 ? 0.32417 0.30366 0.40116 -0.10701 0.09038  -0.08689 117 ALA A CA  
829  C C   A ALA A 110 ? 0.34257 0.35998 0.40323 -0.11336 0.06794  -0.10865 117 ALA A C   
830  C C   B ALA A 110 ? 0.33035 0.32219 0.40272 -0.11315 0.08098  -0.10343 117 ALA A C   
831  O O   A ALA A 110 ? 0.36632 0.38850 0.42508 -0.11581 0.06873  -0.11546 117 ALA A O   
832  O O   B ALA A 110 ? 0.34264 0.33406 0.41682 -0.11815 0.08421  -0.11275 117 ALA A O   
833  C CB  A ALA A 110 ? 0.31767 0.29014 0.39557 -0.10572 0.09052  -0.09075 117 ALA A CB  
834  C CB  B ALA A 110 ? 0.31794 0.27153 0.39710 -0.09176 0.09623  -0.07485 117 ALA A CB  
835  N N   A PHE A 111 ? 0.32758 0.35302 0.38020 -0.10402 0.05577  -0.10554 118 PHE A N   
836  N N   B PHE A 111 ? 0.32309 0.32977 0.38247 -0.10144 0.06563  -0.09973 118 PHE A N   
837  C CA  A PHE A 111 ? 0.28476 0.32296 0.32745 -0.09545 0.04460  -0.10674 118 PHE A CA  
838  C CA  B PHE A 111 ? 0.31656 0.33891 0.36801 -0.10081 0.05494  -0.10845 118 PHE A CA  
839  C C   A PHE A 111 ? 0.34793 0.40637 0.38234 -0.09586 0.03907  -0.10580 118 PHE A C   
840  C C   B PHE A 111 ? 0.36467 0.40462 0.41073 -0.10562 0.05320  -0.11123 118 PHE A C   
841  O O   A PHE A 111 ? 0.33543 0.39695 0.36877 -0.09550 0.03982  -0.10875 118 PHE A O   
842  O O   B PHE A 111 ? 0.38248 0.41768 0.43266 -0.11038 0.06035  -0.11779 118 PHE A O   
843  C CB  A PHE A 111 ? 0.29076 0.33449 0.32686 -0.08319 0.03119  -0.10077 118 PHE A CB  
844  C CB  B PHE A 111 ? 0.30375 0.34037 0.34469 -0.08889 0.03835  -0.10297 118 PHE A CB  
845  C CG  A PHE A 111 ? 0.25108 0.30521 0.28023 -0.07290 0.02057  -0.09635 118 PHE A CG  
846  C CG  B PHE A 111 ? 0.28765 0.33286 0.32234 -0.08002 0.02959  -0.10144 118 PHE A CG  
847  C CD1 A PHE A 111 ? 0.26133 0.30923 0.29427 -0.07460 0.02612  -0.10091 118 PHE A CD1 
848  C CD1 B PHE A 111 ? 0.27912 0.31436 0.31925 -0.08262 0.03737  -0.10709 118 PHE A CD1 
849  C CD2 A PHE A 111 ? 0.23652 0.30368 0.25676 -0.06042 0.00578  -0.08543 118 PHE A CD2 
850  C CD2 B PHE A 111 ? 0.26589 0.32668 0.29102 -0.06811 0.01439  -0.09201 118 PHE A CD2 
851  C CE1 A PHE A 111 ? 0.23399 0.28989 0.26228 -0.06628 0.01772  -0.09557 118 PHE A CE1 
852  C CE1 B PHE A 111 ? 0.25896 0.30218 0.29518 -0.07595 0.03062  -0.10480 118 PHE A CE1 
853  C CE2 A PHE A 111 ? 0.25643 0.32552 0.27307 -0.05143 -0.00129 -0.07839 118 PHE A CE2 
854  C CE2 B PHE A 111 ? 0.27751 0.34110 0.29992 -0.06088 0.00889  -0.08781 118 PHE A CE2 
855  C CZ  A PHE A 111 ? 0.27493 0.33968 0.29566 -0.05534 0.00486  -0.08413 118 PHE A CZ  
856  C CZ  B PHE A 111 ? 0.23732 0.29382 0.26515 -0.06563 0.01691  -0.09492 118 PHE A CZ  
857  N N   A MET A 112 ? 0.33735 0.40813 0.36696 -0.09662 0.03480  -0.10143 119 MET A N   
858  N N   B MET A 112 ? 0.34365 0.40258 0.38096 -0.10347 0.04407  -0.10614 119 MET A N   
859  C CA  A MET A 112 ? 0.39707 0.48259 0.41913 -0.09400 0.02978  -0.09842 119 MET A CA  
860  C CA  B MET A 112 ? 0.40021 0.47060 0.43388 -0.10776 0.04457  -0.10796 119 MET A CA  
861  C C   A MET A 112 ? 0.44709 0.52981 0.47385 -0.10442 0.03976  -0.10723 119 MET A C   
862  C C   B MET A 112 ? 0.42938 0.48847 0.47221 -0.11749 0.05682  -0.11716 119 MET A C   
863  O O   A MET A 112 ? 0.41381 0.50474 0.43663 -0.10251 0.03763  -0.10723 119 MET A O   
864  O O   B MET A 112 ? 0.45924 0.52305 0.49999 -0.11690 0.05646  -0.12154 119 MET A O   
865  C CB  A MET A 112 ? 0.42387 0.52192 0.43952 -0.08974 0.02230  -0.09027 119 MET A CB  
866  C CB  B MET A 112 ? 0.38952 0.46967 0.42119 -0.11072 0.04263  -0.10328 119 MET A CB  
867  C CG  A MET A 112 ? 0.34256 0.44552 0.35114 -0.07380 0.00957  -0.07825 119 MET A CG  
868  C CG  B MET A 112 ? 0.44605 0.54415 0.46665 -0.10459 0.03356  -0.09824 119 MET A CG  
869  S SD  A MET A 112 ? 0.56012 0.67369 0.56316 -0.06774 0.00284  -0.06875 119 MET A SD  
870  S SD  B MET A 112 ? 0.52523 0.63615 0.53672 -0.09109 0.01970  -0.08533 119 MET A SD  
871  C CE  A MET A 112 ? 0.34094 0.45079 0.34063 -0.05035 -0.00828 -0.05758 119 MET A CE  
872  C CE  B MET A 112 ? 0.42540 0.53383 0.43246 -0.07654 0.01118  -0.07808 119 MET A CE  
873  N N   A GLU A 113 ? 0.40115 0.47021 0.43815 -0.11463 0.05104  -0.11358 120 GLU A N   
874  N N   B GLU A 113 ? 0.45807 0.50212 0.51265 -0.12583 0.06801  -0.11847 120 GLU A N   
875  C CA  A GLU A 113 ? 0.46546 0.52923 0.50911 -0.12322 0.06012  -0.12204 120 GLU A CA  
876  C CA  B GLU A 113 ? 0.48157 0.51502 0.54619 -0.13396 0.07869  -0.12599 120 GLU A CA  
877  C C   A GLU A 113 ? 0.52292 0.58190 0.56867 -0.12157 0.06250  -0.12786 120 GLU A C   
878  C C   B GLU A 113 ? 0.50970 0.53617 0.57618 -0.13163 0.08108  -0.13269 120 GLU A C   
879  O O   A GLU A 113 ? 0.51837 0.58348 0.56375 -0.12403 0.06368  -0.13320 120 GLU A O   
880  O O   B GLU A 113 ? 0.51493 0.55167 0.57755 -0.13188 0.07857  -0.13835 120 GLU A O   
881  C CB  A GLU A 113 ? 0.45174 0.49860 0.50903 -0.13251 0.07213  -0.12361 120 GLU A CB  
882  C CB  B GLU A 113 ? 0.52906 0.54268 0.60905 -0.14027 0.09164  -0.12211 120 GLU A CB  
883  C CG  A GLU A 113 ? 0.51308 0.56691 0.57104 -0.13629 0.07168  -0.11723 120 GLU A CG  
884  C CG  B GLU A 113 ? 0.55586 0.57607 0.63772 -0.14326 0.09220  -0.11276 120 GLU A CG  
885  C CD  A GLU A 113 ? 0.58376 0.61913 0.65856 -0.14361 0.08558  -0.11314 120 GLU A CD  
886  C CD  B GLU A 113 ? 0.62726 0.65607 0.71173 -0.15079 0.09340  -0.11632 120 GLU A CD  
887  O OE1 A GLU A 113 ? 0.58606 0.60156 0.67107 -0.14511 0.09512  -0.11624 120 GLU A OE1 
888  O OE1 B GLU A 113 ? 0.66055 0.67525 0.75970 -0.15720 0.10467  -0.11575 120 GLU A OE1 
889  O OE2 A GLU A 113 ? 0.64573 0.68673 0.72405 -0.14649 0.08769  -0.10478 120 GLU A OE2 
890  O OE2 B GLU A 113 ? 0.63954 0.68809 0.71197 -0.14934 0.08324  -0.11891 120 GLU A OE2 
891  N N   A ALA A 114 ? 0.43772 0.48605 0.48625 -0.11737 0.06330  -0.12684 121 ALA A N   
892  N N   B ALA A 114 ? 0.47425 0.48225 0.54795 -0.12931 0.08705  -0.13115 121 ALA A N   
893  C CA  A ALA A 114 ? 0.45395 0.49913 0.50448 -0.11529 0.06508  -0.13158 121 ALA A CA  
894  C CA  B ALA A 114 ? 0.49518 0.49744 0.56953 -0.12482 0.08762  -0.13522 121 ALA A CA  
895  C C   A ALA A 114 ? 0.49118 0.55422 0.53241 -0.10906 0.05579  -0.12833 121 ALA A C   
896  C C   B ALA A 114 ? 0.51212 0.53498 0.57499 -0.11967 0.07682  -0.13635 121 ALA A C   
897  O O   A ALA A 114 ? 0.57287 0.63898 0.61572 -0.11092 0.05842  -0.13390 121 ALA A O   
898  O O   B ALA A 114 ? 0.56004 0.58727 0.62390 -0.12150 0.07856  -0.14291 121 ALA A O   
899  C CB  A ALA A 114 ? 0.44126 0.47184 0.49583 -0.11043 0.06649  -0.12947 121 ALA A CB  
900  C CB  B ALA A 114 ? 0.42937 0.41573 0.50636 -0.11817 0.08882  -0.12870 121 ALA A CB  
901  N N   A LEU A 115 ? 0.42610 0.49978 0.45879 -0.10123 0.04538  -0.11848 122 LEU A N   
902  N N   B LEU A 115 ? 0.46853 0.50330 0.52164 -0.11243 0.06579  -0.12862 122 LEU A N   
903  C CA  A LEU A 115 ? 0.48411 0.57458 0.51120 -0.09626 0.04072  -0.11570 122 LEU A CA  
904  C CA  B LEU A 115 ? 0.51096 0.56271 0.55483 -0.10553 0.05574  -0.12547 122 LEU A CA  
905  C C   A LEU A 115 ? 0.63389 0.73779 0.66079 -0.10354 0.04659  -0.12293 122 LEU A C   
906  C C   B LEU A 115 ? 0.53715 0.59878 0.58010 -0.11009 0.05776  -0.13084 122 LEU A C   
907  O O   A LEU A 115 ? 0.56407 0.67899 0.59178 -0.10486 0.04948  -0.12767 122 LEU A O   
908  O O   B LEU A 115 ? 0.58265 0.64614 0.62703 -0.10985 0.05926  -0.13513 122 LEU A O   
909  C CB  A LEU A 115 ? 0.46533 0.56468 0.48608 -0.08768 0.03167  -0.10514 122 LEU A CB  
910  C CB  B LEU A 115 ? 0.46271 0.52632 0.49733 -0.09753 0.04379  -0.11492 122 LEU A CB  
911  C CG  A LEU A 115 ? 0.33738 0.42679 0.35804 -0.07890 0.02449  -0.09837 122 LEU A CG  
912  C CG  B LEU A 115 ? 0.47230 0.55096 0.49795 -0.08835 0.03275  -0.10623 122 LEU A CG  
913  C CD1 A LEU A 115 ? 0.37944 0.47655 0.39490 -0.07031 0.01566  -0.08834 122 LEU A CD1 
914  C CD1 B LEU A 115 ? 0.52435 0.61540 0.54672 -0.09248 0.03403  -0.10683 122 LEU A CD1 
915  C CD2 A LEU A 115 ? 0.33972 0.43127 0.36277 -0.07641 0.02537  -0.10076 122 LEU A CD2 
916  C CD2 B LEU A 115 ? 0.48756 0.57326 0.51484 -0.08906 0.03620  -0.11156 122 LEU A CD2 
917  N N   A GLN A 116 ? 0.67853 0.78203 0.70480 -0.10834 0.04814  -0.12377 123 GLN A N   
918  N N   B GLN A 116 ? 0.58046 0.64846 0.62161 -0.11442 0.05798  -0.13101 123 GLN A N   
919  C CA  A GLN A 116 ? 0.74882 0.86351 0.77547 -0.11549 0.05358  -0.13137 123 GLN A CA  
920  C CA  B GLN A 116 ? 0.65300 0.72939 0.69394 -0.11838 0.05972  -0.13645 123 GLN A CA  
921  C C   A GLN A 116 ? 0.73324 0.83951 0.76811 -0.12288 0.06136  -0.14254 123 GLN A C   
922  C C   B GLN A 116 ? 0.67433 0.73987 0.72536 -0.12509 0.06946  -0.14739 123 GLN A C   
923  O O   A GLN A 116 ? 0.76592 0.88316 0.80211 -0.12770 0.06557  -0.15028 123 GLN A O   
924  O O   B GLN A 116 ? 0.69338 0.76206 0.74472 -0.12326 0.06962  -0.15070 123 GLN A O   
925  C CB  A GLN A 116 ? 0.74872 0.86478 0.77300 -0.11847 0.05270  -0.12909 123 GLN A CB  
926  C CB  B GLN A 116 ? 0.68185 0.76432 0.72110 -0.12290 0.05976  -0.13608 123 GLN A CB  
927  C CG  A GLN A 116 ? 0.80362 0.93447 0.81971 -0.11217 0.04668  -0.12019 123 GLN A CG  
928  C CG  B GLN A 116 ? 0.73348 0.83080 0.76285 -0.11612 0.05207  -0.12730 123 GLN A CG  
929  C CD  A GLN A 116 ? 0.92314 1.06532 0.93637 -0.11694 0.04879  -0.12226 123 GLN A CD  
930  C CD  B GLN A 116 ? 0.79525 0.90694 0.82046 -0.11075 0.04988  -0.12626 123 GLN A CD  
931  O OE1 A GLN A 116 ? 0.95766 1.09652 0.97514 -0.12511 0.05411  -0.13062 123 GLN A OE1 
932  O OE1 B GLN A 116 ? 0.82617 0.93975 0.84786 -0.10254 0.04341  -0.11802 123 GLN A OE1 
933  N NE2 A GLN A 116 ? 0.90012 1.05535 0.90732 -0.11171 0.04475  -0.11460 123 GLN A NE2 
934  N NE2 B GLN A 116 ? 0.80507 0.92760 0.83183 -0.11538 0.05497  -0.13411 123 GLN A NE2 
935  N N   A ALA A 117 ? 0.68895 0.77581 0.73030 -0.12362 0.06350  -0.14338 124 ALA A N   
936  N N   B ALA A 117 ? 0.70062 0.75258 0.76123 -0.13261 0.07813  -0.15250 124 ALA A N   
937  C CA  A ALA A 117 ? 0.69619 0.77287 0.74684 -0.12976 0.07112  -0.15330 124 ALA A CA  
938  C CA  B ALA A 117 ? 0.69231 0.73128 0.76458 -0.13836 0.08782  -0.16204 124 ALA A CA  
939  C C   A ALA A 117 ? 0.72389 0.79891 0.77604 -0.12614 0.07185  -0.15541 124 ALA A C   
940  C C   B ALA A 117 ? 0.70328 0.74648 0.77443 -0.13505 0.08683  -0.16612 124 ALA A C   
941  O O   A ALA A 117 ? 0.68189 0.74188 0.74191 -0.12834 0.07730  -0.16011 124 ALA A O   
942  O O   B ALA A 117 ? 0.72898 0.77086 0.80659 -0.13988 0.09190  -0.17536 124 ALA A O   
943  C CB  A ALA A 117 ? 0.66213 0.72047 0.72255 -0.13576 0.07830  -0.15590 124 ALA A CB  
944  C CB  B ALA A 117 ? 0.67532 0.69269 0.75759 -0.13969 0.09577  -0.16044 124 ALA A CB  
945  N N   A GLY A 118 ? 0.64822 0.73901 0.69430 -0.12102 0.06757  -0.15229 125 GLY A N   
946  N N   B GLY A 118 ? 0.66180 0.70999 0.72582 -0.12702 0.08027  -0.15941 125 GLY A N   
947  C CA  A GLY A 118 ? 0.64339 0.73586 0.69181 -0.11878 0.06860  -0.15528 125 GLY A CA  
948  C CA  B GLY A 118 ? 0.63215 0.68521 0.69564 -0.12413 0.07927  -0.16241 125 GLY A CA  
949  C C   A GLY A 118 ? 0.58602 0.67496 0.63155 -0.11011 0.06254  -0.14673 125 GLY A C   
950  C C   B GLY A 118 ? 0.56569 0.61275 0.62784 -0.11691 0.07638  -0.15652 125 GLY A C   
951  O O   A GLY A 118 ? 0.43152 0.53036 0.47656 -0.10715 0.06112  -0.14679 125 GLY A O   
952  O O   B GLY A 118 ? 0.52271 0.57227 0.58504 -0.11392 0.07554  -0.15803 125 GLY A O   
953  N N   A ALA A 119 ? 0.51498 0.58972 0.55933 -0.10599 0.05873  -0.13940 126 ALA A N   
954  N N   B ALA A 119 ? 0.55623 0.59505 0.61765 -0.11422 0.07492  -0.15000 126 ALA A N   
955  C CA  A ALA A 119 ? 0.41172 0.47917 0.45491 -0.09792 0.05329  -0.13261 126 ALA A CA  
956  C CA  B ALA A 119 ? 0.49190 0.52563 0.55144 -0.10631 0.07037  -0.14346 126 ALA A CA  
957  C C   A ALA A 119 ? 0.34879 0.43324 0.38583 -0.09106 0.04541  -0.12518 126 ALA A C   
958  C C   B ALA A 119 ? 0.45140 0.50189 0.50206 -0.09911 0.05963  -0.13706 126 ALA A C   
959  O O   A ALA A 119 ? 0.34446 0.44502 0.37791 -0.09218 0.04454  -0.12423 126 ALA A O   
960  O O   B ALA A 119 ? 0.42165 0.48659 0.46595 -0.09855 0.05441  -0.13370 126 ALA A O   
961  C CB  A ALA A 119 ? 0.45624 0.50842 0.50251 -0.09775 0.05503  -0.13054 126 ALA A CB  
962  C CB  B ALA A 119 ? 0.46549 0.49082 0.52444 -0.10424 0.06878  -0.13689 126 ALA A CB  
963  N N   A ASP A 120 ? 0.33779 0.41771 0.37436 -0.08350 0.03990  -0.11960 127 ASP A N   
964  N N   B ASP A 120 ? 0.39745 0.44468 0.44868 -0.09316 0.05697  -0.13472 127 ASP A N   
965  C CA  A ASP A 120 ? 0.32453 0.41782 0.35693 -0.07596 0.03220  -0.11170 127 ASP A CA  
966  C CA  B ASP A 120 ? 0.36985 0.42930 0.41355 -0.08477 0.04589  -0.12558 127 ASP A CA  
967  C C   A ASP A 120 ? 0.31167 0.39339 0.34187 -0.06743 0.02371  -0.10282 127 ASP A C   
968  C C   B ASP A 120 ? 0.33842 0.39697 0.37740 -0.07864 0.03777  -0.11622 127 ASP A C   
969  O O   A ASP A 120 ? 0.26589 0.32931 0.29766 -0.06764 0.02432  -0.10311 127 ASP A O   
970  O O   B ASP A 120 ? 0.33023 0.37662 0.37268 -0.07964 0.04070  -0.11708 127 ASP A O   
971  C CB  A ASP A 120 ? 0.33506 0.43834 0.36983 -0.07467 0.03328  -0.11414 127 ASP A CB  
972  C CB  B ASP A 120 ? 0.37559 0.43285 0.42151 -0.07992 0.04461  -0.12549 127 ASP A CB  
973  C CG  A ASP A 120 ? 0.35676 0.44600 0.39535 -0.07198 0.03328  -0.11547 127 ASP A CG  
974  C CG  B ASP A 120 ? 0.38547 0.45972 0.42717 -0.07354 0.03660  -0.11888 127 ASP A CG  
975  O OD1 A ASP A 120 ? 0.46430 0.54127 0.50698 -0.07740 0.04013  -0.12269 127 ASP A OD1 
976  O OD1 B ASP A 120 ? 0.32255 0.39573 0.36077 -0.06626 0.02851  -0.11026 127 ASP A OD1 
977  O OD2 A ASP A 120 ? 0.30716 0.39675 0.34515 -0.06427 0.02692  -0.10941 127 ASP A OD2 
978  O OD2 B ASP A 120 ? 0.39520 0.48482 0.43765 -0.07548 0.03847  -0.12211 127 ASP A OD2 
979  N N   A ILE A 121 ? 0.27252 0.36430 0.29938 -0.05967 0.01622  -0.09480 128 ILE A N   
980  N N   B ILE A 121 ? 0.31990 0.39412 0.35359 -0.07343 0.03042  -0.10968 128 ILE A N   
981  C CA  A ILE A 121 ? 0.26315 0.34634 0.28741 -0.05070 0.00700  -0.08595 128 ILE A CA  
982  C CA  B ILE A 121 ? 0.30309 0.37756 0.33241 -0.06448 0.02047  -0.09952 128 ILE A CA  
983  C C   A ILE A 121 ? 0.27218 0.33910 0.29894 -0.04687 0.00481  -0.08589 128 ILE A C   
984  C C   B ILE A 121 ? 0.29780 0.35627 0.32909 -0.05856 0.01701  -0.09720 128 ILE A C   
985  O O   A ILE A 121 ? 0.27816 0.33351 0.30403 -0.04254 0.00030  -0.08264 128 ILE A O   
986  O O   B ILE A 121 ? 0.29849 0.35039 0.32994 -0.05502 0.01358  -0.09462 128 ILE A O   
987  C CB  A ILE A 121 ? 0.28235 0.37866 0.30392 -0.04280 0.00110  -0.07808 128 ILE A CB  
988  C CB  B ILE A 121 ? 0.27262 0.36633 0.29963 -0.05984 0.01661  -0.09515 128 ILE A CB  
989  C CG1 A ILE A 121 ? 0.32669 0.43430 0.34505 -0.04575 0.00300  -0.07689 128 ILE A CG1 
990  C CG1 B ILE A 121 ? 0.35550 0.46337 0.37965 -0.06425 0.01941  -0.09577 128 ILE A CG1 
991  C CG2 A ILE A 121 ? 0.29059 0.37804 0.31102 -0.03198 -0.00815 -0.06970 128 ILE A CG2 
992  C CG2 B ILE A 121 ? 0.30410 0.39527 0.32848 -0.04893 0.00653  -0.08500 128 ILE A CG2 
993  C CD1 A ILE A 121 ? 0.30645 0.42585 0.32308 -0.03967 0.00053  -0.07081 128 ILE A CD1 
994  C CD1 B ILE A 121 ? 0.34697 0.44832 0.36851 -0.06596 0.01816  -0.09368 128 ILE A CD1 
995  N N   A SER A 122 ? 0.26596 0.33318 0.29682 -0.04882 0.00927  -0.09110 129 SER A N   
996  N N   B SER A 122 ? 0.29450 0.35108 0.32969 -0.05852 0.02018  -0.10124 129 SER A N   
997  C CA  A SER A 122 ? 0.27857 0.33133 0.31310 -0.04516 0.00885  -0.09221 129 SER A CA  
998  C CA  B SER A 122 ? 0.29495 0.34038 0.33500 -0.05343 0.01955  -0.10190 129 SER A CA  
999  C C   A SER A 122 ? 0.25876 0.29597 0.30017 -0.05005 0.01777  -0.10050 129 SER A C   
1000 C C   B SER A 122 ? 0.28572 0.31205 0.33252 -0.05608 0.02768  -0.10740 129 SER A C   
1001 O O   A SER A 122 ? 0.29606 0.31906 0.34318 -0.04560 0.01957  -0.10207 129 SER A O   
1002 O O   B SER A 122 ? 0.28848 0.30129 0.33927 -0.04933 0.02695  -0.10609 129 SER A O   
1003 C CB  A SER A 122 ? 0.27293 0.32874 0.31117 -0.04727 0.01356  -0.09722 129 SER A CB  
1004 C CB  B SER A 122 ? 0.29400 0.34141 0.33781 -0.05430 0.02343  -0.10639 129 SER A CB  
1005 O OG  A SER A 122 ? 0.29401 0.34551 0.33736 -0.05659 0.02502  -0.10790 129 SER A OG  
1006 O OG  B SER A 122 ? 0.29777 0.34566 0.34488 -0.06367 0.03371  -0.11561 129 SER A OG  
1007 N N   A MET A 123 ? 0.27097 0.30725 0.31285 -0.05834 0.02475  -0.10501 130 MET A N   
1008 N N   B MET A 123 ? 0.26774 0.29001 0.31669 -0.06466 0.03628  -0.11252 130 MET A N   
1009 C CA  A MET A 123 ? 0.26220 0.27955 0.31151 -0.06356 0.03600  -0.11131 130 MET A CA  
1010 C CA  B MET A 123 ? 0.29720 0.29775 0.35319 -0.06682 0.04591  -0.11529 130 MET A CA  
1011 C C   A MET A 123 ? 0.25930 0.26804 0.30798 -0.06007 0.03337  -0.10747 130 MET A C   
1012 C C   B MET A 123 ? 0.28322 0.27944 0.33649 -0.06197 0.04046  -0.10975 130 MET A C   
1013 O O   A MET A 123 ? 0.27960 0.26901 0.33474 -0.06344 0.04408  -0.11009 130 MET A O   
1014 O O   B MET A 123 ? 0.29706 0.27288 0.35608 -0.06281 0.04956  -0.10987 130 MET A O   
1015 C CB  A MET A 123 ? 0.30414 0.32407 0.35574 -0.07454 0.04567  -0.11840 130 MET A CB  
1016 C CB  B MET A 123 ? 0.29860 0.29662 0.35891 -0.07797 0.05723  -0.12226 130 MET A CB  
1017 C CG  A MET A 123 ? 0.32213 0.34777 0.37565 -0.07706 0.04918  -0.12384 130 MET A CG  
1018 C CG  B MET A 123 ? 0.35431 0.36526 0.41414 -0.08308 0.05921  -0.12841 130 MET A CG  
1019 S SD  A MET A 123 ? 0.36134 0.39427 0.41646 -0.08790 0.05733  -0.13255 130 MET A SD  
1020 S SD  B MET A 123 ? 0.49998 0.49449 0.57107 -0.09015 0.07427  -0.13825 130 MET A SD  
1021 C CE  A MET A 123 ? 0.40119 0.40939 0.46751 -0.09382 0.07110  -0.13873 130 MET A CE  
1022 C CE  B MET A 123 ? 0.43968 0.41967 0.51553 -0.09502 0.08160  -0.13701 130 MET A CE  
1023 N N   A ILE A 124 ? 0.22918 0.25015 0.27082 -0.05197 0.01973  -0.10019 131 ILE A N   
1024 N N   B ILE A 124 ? 0.24586 0.25986 0.29084 -0.05578 0.02625  -0.10357 131 ILE A N   
1025 C CA  A ILE A 124 ? 0.24512 0.26392 0.28464 -0.04846 0.01533  -0.09762 131 ILE A CA  
1026 C CA  B ILE A 124 ? 0.25264 0.26782 0.29403 -0.05144 0.01961  -0.09962 131 ILE A CA  
1027 C C   A ILE A 124 ? 0.24966 0.24042 0.29593 -0.04003 0.02308  -0.09516 131 ILE A C   
1028 C C   B ILE A 124 ? 0.25284 0.24174 0.29998 -0.04149 0.02504  -0.09613 131 ILE A C   
1029 O O   A ILE A 124 ? 0.23013 0.21332 0.27540 -0.03594 0.02714  -0.08565 131 ILE A O   
1030 O O   B ILE A 124 ? 0.23184 0.21316 0.27799 -0.03711 0.02891  -0.08636 131 ILE A O   
1031 C CB  A ILE A 124 ? 0.24616 0.28404 0.27669 -0.03728 -0.00232 -0.08687 131 ILE A CB  
1032 C CB  B ILE A 124 ? 0.24957 0.28585 0.28154 -0.04157 0.00225  -0.08945 131 ILE A CB  
1033 C CG1 A ILE A 124 ? 0.24274 0.28604 0.26919 -0.03205 -0.00961 -0.08355 131 ILE A CG1 
1034 C CG1 B ILE A 124 ? 0.25581 0.29847 0.28297 -0.03518 -0.00674 -0.08457 131 ILE A CG1 
1035 C CG2 A ILE A 124 ? 0.23403 0.26822 0.26695 -0.02604 -0.00937 -0.08348 131 ILE A CG2 
1036 C CG2 B ILE A 124 ? 0.25106 0.28477 0.28469 -0.03125 -0.00451 -0.08595 131 ILE A CG2 
1037 C CD1 A ILE A 124 ? 0.21878 0.27538 0.23548 -0.01992 -0.02386 -0.06673 131 ILE A CD1 
1038 C CD1 B ILE A 124 ? 0.22548 0.27857 0.24507 -0.02084 -0.02186 -0.06967 131 ILE A CD1 
1039 N N   . GLY A 125 ? 0.27706 0.25318 0.32873 -0.03289 0.02549  -0.09515 132 GLY A N   
1040 C CA  . GLY A 125 ? 0.27917 0.23060 0.33486 -0.01858 0.03085  -0.08324 132 GLY A CA  
1041 C C   . GLY A 125 ? 0.34201 0.27114 0.40474 -0.02588 0.04878  -0.08431 132 GLY A C   
1042 O O   . GLY A 125 ? 0.33315 0.24385 0.39762 -0.01486 0.05367  -0.07223 132 GLY A O   
1043 N N   . GLN A 126 ? 0.29572 0.22567 0.36339 -0.04395 0.05862  -0.09871 133 GLN A N   
1044 C CA  . GLN A 126 ? 0.31545 0.22668 0.39140 -0.05118 0.07443  -0.09875 133 GLN A CA  
1045 C C   . GLN A 126 ? 0.33487 0.24746 0.40869 -0.05192 0.07650  -0.09004 133 GLN A C   
1046 O O   . GLN A 126 ? 0.36671 0.26164 0.44869 -0.05625 0.08982  -0.08747 133 GLN A O   
1047 C CB  . GLN A 126 ? 0.35820 0.28127 0.43735 -0.06493 0.07957  -0.10878 133 GLN A CB  
1048 C CG  . GLN A 126 ? 0.36388 0.29459 0.44227 -0.06205 0.07542  -0.11233 133 GLN A CG  
1049 C CD  . GLN A 126 ? 0.45872 0.39877 0.54027 -0.07307 0.08146  -0.12197 133 GLN A CD  
1050 O OE1 . GLN A 126 ? 0.46987 0.40194 0.55776 -0.08062 0.09148  -0.12540 133 GLN A OE1 
1051 N NE2 . GLN A 126 ? 0.49837 0.45566 0.57576 -0.07342 0.07522  -0.12592 133 GLN A NE2 
1052 N N   A PHE A 127 ? 0.29456 0.23024 0.35781 -0.04762 0.06306  -0.08457 134 PHE A N   
1053 N N   B PHE A 127 ? 0.29926 0.23337 0.36256 -0.04630 0.06329  -0.08329 134 PHE A N   
1054 C CA  A PHE A 127 ? 0.31503 0.25848 0.37414 -0.04707 0.06274  -0.07507 134 PHE A CA  
1055 C CA  B PHE A 127 ? 0.31773 0.25621 0.37830 -0.04619 0.06517  -0.07372 134 PHE A CA  
1056 C C   A PHE A 127 ? 0.30924 0.25218 0.36013 -0.02605 0.05367  -0.05708 134 PHE A C   
1057 C C   B PHE A 127 ? 0.31243 0.25279 0.36407 -0.02575 0.05512  -0.05635 134 PHE A C   
1058 O O   A PHE A 127 ? 0.28090 0.23437 0.32580 -0.02261 0.05049  -0.04821 134 PHE A O   
1059 O O   B PHE A 127 ? 0.29431 0.24353 0.34061 -0.02253 0.05320  -0.04717 134 PHE A O   
1060 C CB  A PHE A 127 ? 0.26765 0.23953 0.32108 -0.05971 0.05460  -0.08444 134 PHE A CB  
1061 C CB  B PHE A 127 ? 0.28417 0.24766 0.34134 -0.06141 0.06065  -0.08392 134 PHE A CB  
1062 C CG  A PHE A 127 ? 0.27426 0.24803 0.33505 -0.07986 0.06257  -0.10299 134 PHE A CG  
1063 C CG  B PHE A 127 ? 0.28891 0.24920 0.35497 -0.07995 0.07012  -0.10166 134 PHE A CG  
1064 C CD1 A PHE A 127 ? 0.34528 0.30972 0.41568 -0.09308 0.07630  -0.10742 134 PHE A CD1 
1065 C CD1 B PHE A 127 ? 0.33550 0.27848 0.41333 -0.09023 0.08593  -0.10458 134 PHE A CD1 
1066 C CD2 A PHE A 127 ? 0.28937 0.27606 0.34660 -0.08065 0.05555  -0.11063 134 PHE A CD2 
1067 C CD2 B PHE A 127 ? 0.28285 0.25747 0.34516 -0.08240 0.06276  -0.11114 134 PHE A CD2 
1068 C CE1 A PHE A 127 ? 0.31574 0.28786 0.38799 -0.10094 0.07985  -0.11635 134 PHE A CE1 
1069 C CE1 B PHE A 127 ? 0.30031 0.24639 0.38235 -0.09825 0.09093  -0.11450 134 PHE A CE1 
1070 C CE2 A PHE A 127 ? 0.28600 0.28035 0.34474 -0.08778 0.06033  -0.11647 134 PHE A CE2 
1071 C CE2 B PHE A 127 ? 0.31184 0.29015 0.37732 -0.08887 0.06870  -0.11744 134 PHE A CE2 
1072 C CZ  A PHE A 127 ? 0.31104 0.29799 0.37681 -0.09755 0.07195  -0.12056 134 PHE A CZ  
1073 C CZ  B PHE A 127 ? 0.32175 0.28601 0.39674 -0.09673 0.08219  -0.12050 134 PHE A CZ  
1074 N N   . GLY A 128 ? 0.27378 0.20556 0.32430 -0.01137 0.04893  -0.05180 135 GLY A N   
1075 C CA  . GLY A 128 ? 0.27692 0.20411 0.32123 0.00941  0.04162  -0.03543 135 GLY A CA  
1076 C C   . GLY A 128 ? 0.25299 0.20500 0.28622 0.01908  0.02249  -0.03091 135 GLY A C   
1077 O O   . GLY A 128 ? 0.28016 0.23075 0.30722 0.03668  0.01563  -0.01739 135 GLY A O   
1078 N N   . VAL A 129 ? 0.22282 0.19754 0.25344 0.00849  0.01350  -0.04190 136 VAL A N   
1079 C CA  . VAL A 129 ? 0.17177 0.17165 0.19288 0.01592  -0.00516 -0.03869 136 VAL A CA  
1080 C C   . VAL A 129 ? 0.18840 0.19860 0.21075 0.01691  -0.01726 -0.04580 136 VAL A C   
1081 O O   . VAL A 129 ? 0.18380 0.21797 0.20078 0.01604  -0.03172 -0.04846 136 VAL A O   
1082 C CB  . VAL A 129 ? 0.18392 0.20475 0.20026 0.00273  -0.00585 -0.04329 136 VAL A CB  
1083 C CG1 . VAL A 129 ? 0.23330 0.24546 0.24805 0.00691  0.00352  -0.03203 136 VAL A CG1 
1084 C CG2 . VAL A 129 ? 0.19542 0.21882 0.21799 -0.01961 0.00407  -0.05934 136 VAL A CG2 
1085 N N   . GLY A 130 ? 0.21796 0.21113 0.20647 -0.00587 -0.01927 -0.02470 137 GLY A N   
1086 C CA  . GLY A 130 ? 0.21454 0.20785 0.19916 -0.00407 -0.01993 -0.02451 137 GLY A CA  
1087 C C   . GLY A 130 ? 0.19157 0.18398 0.17570 -0.00177 -0.01897 -0.02200 137 GLY A C   
1088 O O   . GLY A 130 ? 0.20087 0.19462 0.18347 -0.00045 -0.01956 -0.02070 137 GLY A O   
1089 N N   . PHE A 131 ? 0.18096 0.17119 0.16631 -0.00129 -0.01751 -0.02130 138 PHE A N   
1090 C CA  . PHE A 131 ? 0.19252 0.18176 0.17793 0.00074  -0.01693 -0.02005 138 PHE A CA  
1091 C C   . PHE A 131 ? 0.19423 0.18673 0.18164 0.00215  -0.01784 -0.01860 138 PHE A C   
1092 O O   . PHE A 131 ? 0.18871 0.17968 0.17598 0.00359  -0.01791 -0.01729 138 PHE A O   
1093 C CB  . PHE A 131 ? 0.19685 0.18508 0.18292 0.00127  -0.01547 -0.02019 138 PHE A CB  
1094 C CG  . PHE A 131 ? 0.21156 0.19928 0.19834 0.00342  -0.01512 -0.02011 138 PHE A CG  
1095 C CD1 . PHE A 131 ? 0.19457 0.17892 0.18005 0.00400  -0.01532 -0.02060 138 PHE A CD1 
1096 C CD2 . PHE A 131 ? 0.20947 0.20017 0.19905 0.00483  -0.01465 -0.01985 138 PHE A CD2 
1097 C CE1 . PHE A 131 ? 0.19928 0.18211 0.18614 0.00565  -0.01523 -0.02126 138 PHE A CE1 
1098 C CE2 . PHE A 131 ? 0.19637 0.18566 0.18703 0.00715  -0.01429 -0.02046 138 PHE A CE2 
1099 C CZ  . PHE A 131 ? 0.23064 0.21542 0.21990 0.00742  -0.01466 -0.02140 138 PHE A CZ  
1100 N N   . TYR A 132 ? 0.18268 0.17983 0.17285 0.00181  -0.01856 -0.01849 139 TYR A N   
1101 C CA  . TYR A 132 ? 0.17454 0.17519 0.16744 0.00394  -0.01941 -0.01668 139 TYR A CA  
1102 C C   . TYR A 132 ? 0.18362 0.18580 0.17457 0.00459  -0.02116 -0.01492 139 TYR A C   
1103 O O   . TYR A 132 ? 0.18865 0.19266 0.18157 0.00692  -0.02186 -0.01238 139 TYR A O   
1104 C CB  . TYR A 132 ? 0.17199 0.17870 0.16937 0.00350  -0.01978 -0.01688 139 TYR A CB  
1105 C CG  . TYR A 132 ? 0.18724 0.19319 0.18627 0.00332  -0.01735 -0.01768 139 TYR A CG  
1106 C CD1 . TYR A 132 ? 0.19848 0.20404 0.19902 0.00615  -0.01580 -0.01743 139 TYR A CD1 
1107 C CD2 . TYR A 132 ? 0.21277 0.21783 0.21136 0.00053  -0.01639 -0.01865 139 TYR A CD2 
1108 C CE1 . TYR A 132 ? 0.19396 0.19984 0.19477 0.00637  -0.01329 -0.01825 139 TYR A CE1 
1109 C CE2 . TYR A 132 ? 0.23415 0.23901 0.23338 0.00057  -0.01387 -0.01844 139 TYR A CE2 
1110 C CZ  . TYR A 132 ? 0.22581 0.23172 0.22565 0.00356  -0.01228 -0.01831 139 TYR A CZ  
1111 O OH  . TYR A 132 ? 0.21482 0.22155 0.21409 0.00395  -0.00960 -0.01821 139 TYR A OH  
1112 N N   . SER A 133 ? 0.18574 0.18736 0.17277 0.00298  -0.02169 -0.01595 140 SER A N   
1113 C CA  . SER A 133 ? 0.20127 0.20471 0.18518 0.00387  -0.02271 -0.01391 140 SER A CA  
1114 C C   . SER A 133 ? 0.18179 0.18112 0.16582 0.00550  -0.02136 -0.01095 140 SER A C   
1115 O O   . SER A 133 ? 0.19680 0.19783 0.17924 0.00664  -0.02181 -0.00770 140 SER A O   
1116 C CB  . SER A 133 ? 0.21666 0.22029 0.19586 0.00221  -0.02289 -0.01626 140 SER A CB  
1117 O OG  . SER A 133 ? 0.20320 0.20137 0.18142 0.00163  -0.02085 -0.01734 140 SER A OG  
1118 N N   . ALA A 134 ? 0.17949 0.17378 0.16547 0.00552  -0.01980 -0.01188 141 ALA A N   
1119 C CA  . ALA A 134 ? 0.16684 0.15704 0.15467 0.00675  -0.01891 -0.00961 141 ALA A CA  
1120 C C   . ALA A 134 ? 0.18621 0.17778 0.17686 0.00919  -0.01969 -0.00595 141 ALA A C   
1121 O O   . ALA A 134 ? 0.18567 0.17468 0.17735 0.01000  -0.01922 -0.00251 141 ALA A O   
1122 C CB  . ALA A 134 ? 0.16449 0.15033 0.15441 0.00675  -0.01785 -0.01219 141 ALA A CB  
1123 N N   . TYR A 135 ? 0.18357 0.17933 0.17641 0.01048  -0.02079 -0.00622 142 TYR A N   
1124 C CA  . TYR A 135 ? 0.19848 0.19569 0.19504 0.01355  -0.02159 -0.00269 142 TYR A CA  
1125 C C   . TYR A 135 ? 0.20065 0.20281 0.19470 0.01434  -0.02333 0.00155  142 TYR A C   
1126 O O   . TYR A 135 ? 0.22420 0.22816 0.22109 0.01727  -0.02430 0.00559  142 TYR A O   
1127 C CB  . TYR A 135 ? 0.18470 0.18584 0.18546 0.01499  -0.02193 -0.00447 142 TYR A CB  
1128 C CG  . TYR A 135 ? 0.18927 0.18534 0.19213 0.01540  -0.01983 -0.00764 142 TYR A CG  
1129 C CD1 . TYR A 135 ? 0.20473 0.19583 0.21140 0.01823  -0.01894 -0.00696 142 TYR A CD1 
1130 C CD2 . TYR A 135 ? 0.17255 0.16825 0.17316 0.01304  -0.01876 -0.01131 142 TYR A CD2 
1131 C CE1 . TYR A 135 ? 0.19235 0.17902 0.20001 0.01868  -0.01721 -0.01091 142 TYR A CE1 
1132 C CE2 . TYR A 135 ? 0.18548 0.17743 0.18665 0.01363  -0.01699 -0.01418 142 TYR A CE2 
1133 C CZ  . TYR A 135 ? 0.19582 0.18353 0.20013 0.01640  -0.01634 -0.01441 142 TYR A CZ  
1134 O OH  . TYR A 135 ? 0.20125 0.18592 0.20526 0.01703  -0.01485 -0.01822 142 TYR A OH  
1135 N N   . LEU A 136 ? 0.18538 0.18992 0.17391 0.01217  -0.02367 0.00078  143 LEU A N   
1136 C CA  . LEU A 136 ? 0.19363 0.20263 0.17825 0.01311  -0.02479 0.00496  143 LEU A CA  
1137 C C   . LEU A 136 ? 0.20486 0.20895 0.19054 0.01431  -0.02303 0.01026  143 LEU A C   
1138 O O   . LEU A 136 ? 0.23055 0.23769 0.21521 0.01640  -0.02378 0.01594  143 LEU A O   
1139 C CB  . LEU A 136 ? 0.21371 0.22559 0.19194 0.01069  -0.02487 0.00192  143 LEU A CB  
1140 C CG  . LEU A 136 ? 0.20288 0.21993 0.17991 0.00904  -0.02702 -0.00313 143 LEU A CG  
1141 C CD1 . LEU A 136 ? 0.23469 0.25177 0.20619 0.00683  -0.02643 -0.00704 143 LEU A CD1 
1142 C CD2 . LEU A 136 ? 0.20314 0.22878 0.18025 0.01071  -0.03035 -0.00120 143 LEU A CD2 
1143 N N   . VAL A 137 ? 0.21304 0.20976 0.20115 0.01292  -0.02081 0.00875  144 VAL A N   
1144 C CA  . VAL A 137 ? 0.20259 0.19452 0.19256 0.01297  -0.01898 0.01337  144 VAL A CA  
1145 C C   . VAL A 137 ? 0.21285 0.19674 0.20978 0.01359  -0.01809 0.01285  144 VAL A C   
1146 O O   . VAL A 137 ? 0.25131 0.23045 0.25187 0.01391  -0.01693 0.01721  144 VAL A O   
1147 C CB  . VAL A 137 ? 0.20542 0.19713 0.19200 0.01023  -0.01711 0.01243  144 VAL A CB  
1148 C CG1 . VAL A 137 ? 0.23445 0.23401 0.21376 0.01022  -0.01772 0.01297  144 VAL A CG1 
1149 C CG2 . VAL A 137 ? 0.19237 0.18085 0.17975 0.00807  -0.01655 0.00612  144 VAL A CG2 
1150 N N   . ALA A 138 ? 0.20399 0.18632 0.20298 0.01380  -0.01850 0.00758  145 ALA A N   
1151 C CA  . ALA A 138 ? 0.20753 0.18248 0.21204 0.01432  -0.01762 0.00537  145 ALA A CA  
1152 C C   . ALA A 138 ? 0.21523 0.19008 0.22399 0.01795  -0.01831 0.00552  145 ALA A C   
1153 O O   . ALA A 138 ? 0.24681 0.22766 0.25435 0.01897  -0.01928 0.00381  145 ALA A O   
1154 C CB  . ALA A 138 ? 0.22301 0.19642 0.22617 0.01215  -0.01714 -0.00102 145 ALA A CB  
1155 N N   . GLU A 139 ? 0.20566 0.17359 0.22024 0.01980  -0.01766 0.00712  146 GLU A N   
1156 C CA  . GLU A 139 ? 0.23103 0.19789 0.25057 0.02379  -0.01786 0.00609  146 GLU A CA  
1157 C C   . GLU A 139 ? 0.24218 0.20713 0.26222 0.02363  -0.01702 -0.00142 146 GLU A C   
1158 O O   . GLU A 139 ? 0.25739 0.22475 0.27982 0.02670  -0.01685 -0.00354 146 GLU A O   
1159 C CB  . GLU A 139 ? 0.26295 0.22205 0.28914 0.02630  -0.01737 0.01043  146 GLU A CB  
1160 C CG  . GLU A 139 ? 0.35789 0.30789 0.38692 0.02358  -0.01619 0.00909  146 GLU A CG  
1161 C CD  . GLU A 139 ? 0.52177 0.46334 0.55833 0.02568  -0.01562 0.01423  146 GLU A CD  
1162 O OE1 . GLU A 139 ? 0.48807 0.43208 0.52603 0.02911  -0.01618 0.02097  146 GLU A OE1 
1163 O OE2 . GLU A 139 ? 0.54390 0.47642 0.58538 0.02393  -0.01480 0.01138  146 GLU A OE2 
1164 N N   . LYS A 140 ? 0.21414 0.17546 0.23209 0.02038  -0.01644 -0.00529 147 LYS A N   
1165 C CA  . LYS A 140 ? 0.23771 0.19794 0.25474 0.02018  -0.01582 -0.01219 147 LYS A CA  
1166 C C   . LYS A 140 ? 0.20960 0.17162 0.22140 0.01625  -0.01598 -0.01430 147 LYS A C   
1167 O O   . LYS A 140 ? 0.20651 0.16694 0.21788 0.01372  -0.01618 -0.01176 147 LYS A O   
1168 C CB  . LYS A 140 ? 0.24260 0.19422 0.26481 0.02148  -0.01532 -0.01553 147 LYS A CB  
1169 C CG  . LYS A 140 ? 0.23090 0.18234 0.25118 0.02191  -0.01477 -0.02319 147 LYS A CG  
1170 C CD  . LYS A 140 ? 0.31856 0.26134 0.34452 0.02385  -0.01450 -0.02714 147 LYS A CD  
1171 C CE  . LYS A 140 ? 0.38625 0.32287 0.41348 0.02022  -0.01540 -0.02989 147 LYS A CE  
1172 N NZ  . LYS A 140 ? 0.45035 0.37704 0.48514 0.02193  -0.01533 -0.03272 147 LYS A NZ  
1173 N N   . VAL A 141 ? 0.18167 0.14737 0.18983 0.01595  -0.01566 -0.01841 148 VAL A N   
1174 C CA  . VAL A 141 ? 0.18353 0.15046 0.18722 0.01282  -0.01588 -0.02031 148 VAL A CA  
1175 C C   . VAL A 141 ? 0.21534 0.18087 0.21777 0.01323  -0.01558 -0.02596 148 VAL A C   
1176 O O   . VAL A 141 ? 0.18680 0.15447 0.18895 0.01564  -0.01466 -0.02823 148 VAL A O   
1177 C CB  . VAL A 141 ? 0.20458 0.17784 0.20416 0.01176  -0.01592 -0.01891 148 VAL A CB  
1178 C CG1 . VAL A 141 ? 0.20539 0.17908 0.20102 0.00923  -0.01601 -0.02085 148 VAL A CG1 
1179 C CG2 . VAL A 141 ? 0.20846 0.18432 0.20816 0.01152  -0.01661 -0.01409 148 VAL A CG2 
1180 N N   . THR A 142 ? 0.20548 0.16831 0.20731 0.01106  -0.01635 -0.02823 149 THR A N   
1181 C CA  . THR A 142 ? 0.21209 0.17476 0.21152 0.01119  -0.01670 -0.03372 149 THR A CA  
1182 C C   . THR A 142 ? 0.22116 0.18770 0.21590 0.00907  -0.01725 -0.03348 149 THR A C   
1183 O O   . THR A 142 ? 0.23920 0.20554 0.23477 0.00680  -0.01787 -0.03108 149 THR A O   
1184 C CB  . THR A 142 ? 0.21124 0.16786 0.21488 0.01045  -0.01782 -0.03728 149 THR A CB  
1185 O OG1 . THR A 142 ? 0.25529 0.20682 0.26448 0.01247  -0.01722 -0.03658 149 THR A OG1 
1186 C CG2 . THR A 142 ? 0.23158 0.18916 0.23181 0.01117  -0.01853 -0.04389 149 THR A CG2 
1187 N N   . VAL A 143 ? 0.18583 0.15613 0.17589 0.01006  -0.01675 -0.03548 150 VAL A N   
1188 C CA  . VAL A 143 ? 0.19502 0.16857 0.18084 0.00867  -0.01721 -0.03476 150 VAL A CA  
1189 C C   . VAL A 143 ? 0.24495 0.21951 0.22760 0.00928  -0.01828 -0.03922 150 VAL A C   
1190 O O   . VAL A 143 ? 0.22368 0.20008 0.20346 0.01145  -0.01731 -0.04181 150 VAL A O   
1191 C CB  . VAL A 143 ? 0.19358 0.17107 0.17658 0.00905  -0.01568 -0.03193 150 VAL A CB  
1192 C CG1 . VAL A 143 ? 0.23000 0.20949 0.20929 0.00792  -0.01616 -0.03093 150 VAL A CG1 
1193 C CG2 . VAL A 143 ? 0.20407 0.18153 0.18997 0.00842  -0.01526 -0.02833 150 VAL A CG2 
1194 N N   . ILE A 144 ? 0.19604 0.17030 0.17924 0.00754  -0.02029 -0.04029 151 ILE A N   
1195 C CA  . ILE A 144 ? 0.19187 0.16849 0.17167 0.00798  -0.02209 -0.04446 151 ILE A CA  
1196 C C   . ILE A 144 ? 0.22076 0.20177 0.19625 0.00791  -0.02234 -0.04150 151 ILE A C   
1197 O O   . ILE A 144 ? 0.22729 0.20815 0.20495 0.00644  -0.02244 -0.03806 151 ILE A O   
1198 C CB  . ILE A 144 ? 0.22502 0.19934 0.20953 0.00593  -0.02471 -0.04783 151 ILE A CB  
1199 C CG1 . ILE A 144 ? 0.31292 0.28103 0.30410 0.00520  -0.02428 -0.04875 151 ILE A CG1 
1200 C CG2 . ILE A 144 ? 0.24276 0.22055 0.22306 0.00674  -0.02706 -0.05318 151 ILE A CG2 
1201 C CD1 . ILE A 144 ? 0.31247 0.27799 0.30314 0.00759  -0.02372 -0.05346 151 ILE A CD1 
1202 N N   . THR A 145 ? 0.21248 0.19744 0.18188 0.00977  -0.02224 -0.04259 152 THR A N   
1203 C CA  . THR A 145 ? 0.20476 0.19312 0.17048 0.01007  -0.02215 -0.03859 152 THR A CA  
1204 C C   . THR A 145 ? 0.24340 0.23670 0.20295 0.01182  -0.02373 -0.04050 152 THR A C   
1205 O O   . THR A 145 ? 0.24312 0.23812 0.19919 0.01334  -0.02379 -0.04469 152 THR A O   
1206 C CB  . THR A 145 ? 0.22998 0.21831 0.19467 0.01044  -0.01902 -0.03413 152 THR A CB  
1207 O OG1 . THR A 145 ? 0.22722 0.21644 0.19078 0.01012  -0.01892 -0.02985 152 THR A OG1 
1208 C CG2 . THR A 145 ? 0.25067 0.24186 0.21127 0.01248  -0.01685 -0.03505 152 THR A CG2 
1209 N N   . LYS A 146 ? 0.22266 0.21859 0.18078 0.01194  -0.02509 -0.03742 153 LYS A N   
1210 C CA  . LYS A 146 ? 0.22110 0.22275 0.17290 0.01395  -0.02696 -0.03781 153 LYS A CA  
1211 C C   . LYS A 146 ? 0.24130 0.24412 0.19121 0.01489  -0.02585 -0.03113 153 LYS A C   
1212 O O   . LYS A 146 ? 0.23153 0.23277 0.18582 0.01402  -0.02669 -0.02868 153 LYS A O   
1213 C CB  . LYS A 146 ? 0.23996 0.24416 0.19387 0.01321  -0.03135 -0.04199 153 LYS A CB  
1214 C CG  . LYS A 146 ? 0.24134 0.25304 0.18829 0.01555  -0.03427 -0.04276 153 LYS A CG  
1215 C CD  . LYS A 146 ? 0.29561 0.31054 0.23469 0.01767  -0.03366 -0.04639 153 LYS A CD  
1216 C CE  . LYS A 146 ? 0.27278 0.29629 0.20414 0.02014  -0.03706 -0.04705 153 LYS A CE  
1217 N NZ  . LYS A 146 ? 0.28091 0.30743 0.20811 0.02228  -0.03578 -0.03860 153 LYS A NZ  
1218 N N   . HIS A 147 ? 0.25361 0.25925 0.19733 0.01680  -0.02381 -0.02821 154 HIS A N   
1219 C CA  . HIS A 147 ? 0.24143 0.24801 0.18288 0.01798  -0.02261 -0.02134 154 HIS A CA  
1220 C C   . HIS A 147 ? 0.27689 0.29029 0.21136 0.02075  -0.02509 -0.02058 154 HIS A C   
1221 O O   . HIS A 147 ? 0.28407 0.30213 0.21317 0.02197  -0.02630 -0.02514 154 HIS A O   
1222 C CB  . HIS A 147 ? 0.24266 0.24806 0.18281 0.01780  -0.01813 -0.01766 154 HIS A CB  
1223 C CG  . HIS A 147 ? 0.25725 0.26169 0.19695 0.01824  -0.01625 -0.01016 154 HIS A CG  
1224 N ND1 . HIS A 147 ? 0.29504 0.30411 0.22838 0.02075  -0.01615 -0.00574 154 HIS A ND1 
1225 C CD2 . HIS A 147 ? 0.26620 0.26534 0.21113 0.01645  -0.01420 -0.00632 154 HIS A CD2 
1226 C CE1 . HIS A 147 ? 0.30977 0.31556 0.24524 0.02046  -0.01408 0.00105  154 HIS A CE1 
1227 N NE2 . HIS A 147 ? 0.31443 0.31401 0.25707 0.01772  -0.01290 0.00031  154 HIS A NE2 
1228 N N   . ASN A 148 ? 0.26410 0.27833 0.19849 0.02209  -0.02604 -0.01502 155 ASN A N   
1229 C CA  . ASN A 148 ? 0.26213 0.28380 0.18974 0.02516  -0.02889 -0.01353 155 ASN A CA  
1230 C C   . ASN A 148 ? 0.25283 0.27969 0.17095 0.02718  -0.02679 -0.01257 155 ASN A C   
1231 O O   . ASN A 148 ? 0.31704 0.35152 0.22791 0.02955  -0.02964 -0.01473 155 ASN A O   
1232 C CB  . ASN A 148 ? 0.31238 0.33350 0.24163 0.02695  -0.02943 -0.00607 155 ASN A CB  
1233 C CG  . ASN A 148 ? 0.30429 0.32419 0.24119 0.02634  -0.03255 -0.00776 155 ASN A CG  
1234 O OD1 . ASN A 148 ? 0.30059 0.32290 0.24010 0.02503  -0.03556 -0.01404 155 ASN A OD1 
1235 N ND2 . ASN A 148 ? 0.27162 0.28772 0.21286 0.02731  -0.03162 -0.00213 155 ASN A ND2 
1236 N N   . ASP A 149 ? 0.29653 0.32048 0.21450 0.02636  -0.02190 -0.00950 156 ASP A N   
1237 C CA  . ASP A 149 ? 0.30878 0.33848 0.21821 0.02844  -0.01894 -0.00721 156 ASP A CA  
1238 C C   . ASP A 149 ? 0.37909 0.41076 0.28623 0.02827  -0.01759 -0.01464 156 ASP A C   
1239 O O   . ASP A 149 ? 0.39369 0.43037 0.29440 0.03000  -0.01417 -0.01317 156 ASP A O   
1240 C CB  . ASP A 149 ? 0.36031 0.38696 0.27153 0.02772  -0.01399 0.00141  156 ASP A CB  
1241 C CG  . ASP A 149 ? 0.38729 0.41175 0.29999 0.02869  -0.01485 0.00940  156 ASP A CG  
1242 O OD1 . ASP A 149 ? 0.39053 0.41902 0.29982 0.03115  -0.01887 0.00966  156 ASP A OD1 
1243 O OD2 . ASP A 149 ? 0.43989 0.45861 0.35777 0.02702  -0.01160 0.01520  156 ASP A OD2 
1244 N N   . ASP A 150 ? 0.31434 0.34239 0.22672 0.02650  -0.01988 -0.02230 157 ASP A N   
1245 C CA  . ASP A 150 ? 0.26694 0.29560 0.17825 0.02672  -0.01852 -0.02940 157 ASP A CA  
1246 C C   . ASP A 150 ? 0.33517 0.36214 0.24946 0.02576  -0.02311 -0.03810 157 ASP A C   
1247 O O   . ASP A 150 ? 0.31422 0.34071 0.23142 0.02475  -0.02715 -0.03837 157 ASP A O   
1248 C CB  . ASP A 150 ? 0.30654 0.32996 0.22456 0.02479  -0.01423 -0.02762 157 ASP A CB  
1249 C CG  . ASP A 150 ? 0.32594 0.35259 0.24108 0.02645  -0.01075 -0.03130 157 ASP A CG  
1250 O OD1 . ASP A 150 ? 0.34207 0.37335 0.25075 0.02886  -0.01192 -0.03736 157 ASP A OD1 
1251 O OD2 . ASP A 150 ? 0.32363 0.34854 0.24346 0.02539  -0.00685 -0.02832 157 ASP A OD2 
1252 N N   . GLU A 151 ? 0.30773 0.33395 0.22196 0.02614  -0.02235 -0.04523 158 GLU A N   
1253 C CA  . GLU A 151 ? 0.27187 0.29527 0.18994 0.02493  -0.02612 -0.05388 158 GLU A CA  
1254 C C   . GLU A 151 ? 0.25174 0.26646 0.18071 0.02184  -0.02547 -0.05353 158 GLU A C   
1255 O O   . GLU A 151 ? 0.29198 0.30369 0.22444 0.02099  -0.02224 -0.04780 158 GLU A O   
1256 C CB  . GLU A 151 ? 0.37265 0.39863 0.28552 0.02731  -0.02537 -0.06195 158 GLU A CB  
1257 C CG  . GLU A 151 ? 0.43219 0.46787 0.33304 0.03057  -0.02695 -0.06452 158 GLU A CG  
1258 C CD  . GLU A 151 ? 0.66057 0.70085 0.55900 0.03016  -0.03220 -0.06284 158 GLU A CD  
1259 O OE1 . GLU A 151 ? 0.72991 0.77799 0.61929 0.03278  -0.03205 -0.05804 158 GLU A OE1 
1260 O OE2 . GLU A 151 ? 0.74217 0.77907 0.64787 0.02742  -0.03649 -0.06608 158 GLU A OE2 
1261 N N   . GLN A 152 ? 0.27908 0.29009 0.21352 0.02003  -0.02863 -0.05962 159 GLN A N   
1262 C CA  . GLN A 152 ? 0.24526 0.24857 0.18955 0.01726  -0.02802 -0.05880 159 GLN A CA  
1263 C C   . GLN A 152 ? 0.26712 0.26650 0.21350 0.01830  -0.02479 -0.06128 159 GLN A C   
1264 O O   . GLN A 152 ? 0.27597 0.27582 0.21989 0.02006  -0.02506 -0.06807 159 GLN A O   
1265 C CB  . GLN A 152 ? 0.28858 0.28956 0.23892 0.01468  -0.03228 -0.06355 159 GLN A CB  
1266 C CG  . GLN A 152 ? 0.26177 0.25587 0.22211 0.01162  -0.03172 -0.06116 159 GLN A CG  
1267 C CD  . GLN A 152 ? 0.30735 0.30131 0.27397 0.00866  -0.03564 -0.06352 159 GLN A CD  
1268 O OE1 . GLN A 152 ? 0.34837 0.34776 0.31344 0.00854  -0.03811 -0.06206 159 GLN A OE1 
1269 N NE2 . GLN A 152 ? 0.30243 0.29058 0.27668 0.00638  -0.03617 -0.06686 159 GLN A NE2 
1270 N N   A TYR A 153 ? 0.23058 0.22634 0.18176 0.01741  -0.02196 -0.05616 160 TYR A N   
1271 N N   B TYR A 153 ? 0.23058 0.22634 0.18176 0.01741  -0.02196 -0.05616 160 TYR A N   
1272 C CA  A TYR A 153 ? 0.25582 0.24889 0.20982 0.01873  -0.01892 -0.05721 160 TYR A CA  
1273 C CA  B TYR A 153 ? 0.25582 0.24889 0.20982 0.01873  -0.01892 -0.05721 160 TYR A CA  
1274 C C   A TYR A 153 ? 0.25500 0.24133 0.21785 0.01652  -0.01920 -0.05561 160 TYR A C   
1275 C C   B TYR A 153 ? 0.25500 0.24133 0.21785 0.01652  -0.01920 -0.05561 160 TYR A C   
1276 O O   A TYR A 153 ? 0.23828 0.22307 0.20418 0.01401  -0.02044 -0.05180 160 TYR A O   
1277 O O   B TYR A 153 ? 0.23828 0.22307 0.20418 0.01401  -0.02044 -0.05180 160 TYR A O   
1278 C CB  A TYR A 153 ? 0.22930 0.22656 0.18029 0.02011  -0.01500 -0.05186 160 TYR A CB  
1279 C CB  B TYR A 153 ? 0.22930 0.22656 0.18029 0.02011  -0.01500 -0.05186 160 TYR A CB  
1280 C CG  A TYR A 153 ? 0.29144 0.29553 0.23395 0.02307  -0.01343 -0.05369 160 TYR A CG  
1281 C CG  B TYR A 153 ? 0.29144 0.29553 0.23395 0.02307  -0.01343 -0.05369 160 TYR A CG  
1282 C CD1 A TYR A 153 ? 0.28864 0.29415 0.22973 0.02601  -0.01137 -0.05892 160 TYR A CD1 
1283 C CD1 B TYR A 153 ? 0.28864 0.29415 0.22973 0.02601  -0.01137 -0.05892 160 TYR A CD1 
1284 C CD2 A TYR A 153 ? 0.30758 0.31692 0.24336 0.02334  -0.01390 -0.05014 160 TYR A CD2 
1285 C CD2 B TYR A 153 ? 0.30758 0.31692 0.24336 0.02334  -0.01390 -0.05014 160 TYR A CD2 
1286 C CE1 A TYR A 153 ? 0.32887 0.34155 0.26149 0.02904  -0.00950 -0.06086 160 TYR A CE1 
1287 C CE1 B TYR A 153 ? 0.32887 0.34155 0.26149 0.02904  -0.00950 -0.06086 160 TYR A CE1 
1288 C CE2 A TYR A 153 ? 0.32704 0.34357 0.25403 0.02634  -0.01225 -0.05133 160 TYR A CE2 
1289 C CE2 B TYR A 153 ? 0.32704 0.34357 0.25403 0.02634  -0.01225 -0.05133 160 TYR A CE2 
1290 C CZ  A TYR A 153 ? 0.36056 0.37899 0.28578 0.02912  -0.00994 -0.05691 160 TYR A CZ  
1291 C CZ  B TYR A 153 ? 0.36056 0.37899 0.28578 0.02912  -0.00994 -0.05691 160 TYR A CZ  
1292 O OH  A TYR A 153 ? 0.42858 0.45499 0.34451 0.03248  -0.00776 -0.05856 160 TYR A OH  
1293 O OH  B TYR A 153 ? 0.42858 0.45499 0.34451 0.03248  -0.00776 -0.05856 160 TYR A OH  
1294 N N   . ALA A 154 ? 0.23037 0.21311 0.19717 0.01790  -0.01777 -0.05818 161 ALA A N   
1295 C CA  . ALA A 154 ? 0.23106 0.20819 0.20564 0.01661  -0.01744 -0.05540 161 ALA A CA  
1296 C C   . ALA A 154 ? 0.22931 0.20815 0.20514 0.01872  -0.01419 -0.05241 161 ALA A C   
1297 O O   . ALA A 154 ? 0.23977 0.22039 0.21428 0.02183  -0.01233 -0.05583 161 ALA A O   
1298 C CB  . ALA A 154 ? 0.27355 0.24405 0.25372 0.01641  -0.01906 -0.06052 161 ALA A CB  
1299 N N   . TRP A 155 ? 0.20373 0.18270 0.18229 0.01713  -0.01360 -0.04652 162 TRP A N   
1300 C CA  . TRP A 155 ? 0.20279 0.18368 0.18438 0.01847  -0.01134 -0.04337 162 TRP A CA  
1301 C C   . TRP A 155 ? 0.21791 0.19357 0.20612 0.01830  -0.01224 -0.04205 162 TRP A C   
1302 O O   . TRP A 155 ? 0.20683 0.17854 0.19685 0.01595  -0.01411 -0.04098 162 TRP A O   
1303 C CB  . TRP A 155 ? 0.20131 0.18625 0.18123 0.01649  -0.01061 -0.03808 162 TRP A CB  
1304 C CG  . TRP A 155 ? 0.18870 0.17664 0.17237 0.01668  -0.00907 -0.03443 162 TRP A CG  
1305 C CD1 . TRP A 155 ? 0.18798 0.18184 0.17095 0.01722  -0.00667 -0.03276 162 TRP A CD1 
1306 C CD2 . TRP A 155 ? 0.18006 0.16640 0.16856 0.01578  -0.01008 -0.03145 162 TRP A CD2 
1307 N NE1 . TRP A 155 ? 0.19498 0.19105 0.18287 0.01665  -0.00643 -0.02971 162 TRP A NE1 
1308 C CE2 . TRP A 155 ? 0.18613 0.17787 0.17679 0.01590  -0.00869 -0.02887 162 TRP A CE2 
1309 C CE3 . TRP A 155 ? 0.19003 0.17163 0.18114 0.01481  -0.01198 -0.03041 162 TRP A CE3 
1310 C CZ2 . TRP A 155 ? 0.18767 0.18057 0.18263 0.01541  -0.00966 -0.02597 162 TRP A CZ2 
1311 C CZ3 . TRP A 155 ? 0.17742 0.16010 0.17201 0.01457  -0.01249 -0.02682 162 TRP A CZ3 
1312 C CH2 . TRP A 155 ? 0.21358 0.20204 0.20977 0.01496  -0.01161 -0.02496 162 TRP A CH2 
1313 N N   . GLU A 156 ? 0.17978 0.15591 0.17199 0.02099  -0.01077 -0.04164 163 GLU A N   
1314 C CA  . GLU A 156 ? 0.19798 0.16935 0.19628 0.02115  -0.01172 -0.03918 163 GLU A CA  
1315 C C   . GLU A 156 ? 0.20065 0.17585 0.20277 0.02360  -0.01040 -0.03607 163 GLU A C   
1316 O O   . GLU A 156 ? 0.20035 0.17995 0.20251 0.02639  -0.00837 -0.03804 163 GLU A O   
1317 C CB  . GLU A 156 ? 0.24819 0.21229 0.24985 0.02244  -0.01246 -0.04368 163 GLU A CB  
1318 C CG  . GLU A 156 ? 0.27105 0.22889 0.27929 0.02225  -0.01338 -0.04040 163 GLU A CG  
1319 C CD  . GLU A 156 ? 0.36752 0.31713 0.37945 0.02225  -0.01434 -0.04524 163 GLU A CD  
1320 O OE1 . GLU A 156 ? 0.37527 0.32225 0.38959 0.02583  -0.01337 -0.04971 163 GLU A OE1 
1321 O OE2 . GLU A 156 ? 0.34631 0.29235 0.35920 0.01865  -0.01600 -0.04513 163 GLU A OE2 
1322 N N   . SER A 157 ? 0.20233 0.17684 0.20773 0.02275  -0.01155 -0.03117 164 SER A N   
1323 C CA  . SER A 157 ? 0.18324 0.16201 0.19307 0.02535  -0.01103 -0.02809 164 SER A CA  
1324 C C   . SER A 157 ? 0.18785 0.16331 0.20158 0.02557  -0.01266 -0.02346 164 SER A C   
1325 O O   . SER A 157 ? 0.19112 0.16467 0.20275 0.02251  -0.01397 -0.02085 164 SER A O   
1326 C CB  . SER A 157 ? 0.19857 0.18581 0.20676 0.02386  -0.01056 -0.02584 164 SER A CB  
1327 O OG  . SER A 157 ? 0.18780 0.18024 0.20139 0.02649  -0.01044 -0.02332 164 SER A OG  
1328 N N   . SER A 158 ? 0.20509 0.18037 0.22452 0.02957  -0.01236 -0.02214 165 SER A N   
1329 C CA  . SER A 158 ? 0.21773 0.19220 0.24096 0.03072  -0.01384 -0.01631 165 SER A CA  
1330 C C   . SER A 158 ? 0.24299 0.22713 0.26797 0.03217  -0.01447 -0.01304 165 SER A C   
1331 O O   . SER A 158 ? 0.26600 0.25148 0.29535 0.03504  -0.01560 -0.00861 165 SER A O   
1332 C CB  . SER A 158 ? 0.21548 0.18208 0.24496 0.03450  -0.01344 -0.01639 165 SER A CB  
1333 O OG  . SER A 158 ? 0.27517 0.23273 0.30399 0.03230  -0.01337 -0.01950 165 SER A OG  
1334 N N   . ALA A 159 ? 0.20099 0.19212 0.22300 0.03006  -0.01393 -0.01487 166 ALA A N   
1335 C CA  . ALA A 159 ? 0.21644 0.21770 0.24096 0.03051  -0.01454 -0.01282 166 ALA A CA  
1336 C C   . ALA A 159 ? 0.21514 0.21954 0.24649 0.03572  -0.01311 -0.01353 166 ALA A C   
1337 O O   . ALA A 159 ? 0.27023 0.27091 0.30191 0.03775  -0.01075 -0.01772 166 ALA A O   
1338 C CB  . ALA A 159 ? 0.27138 0.27572 0.29522 0.02917  -0.01747 -0.00798 166 ALA A CB  
1339 N N   . GLY A 160 ? 0.24765 0.25941 0.28446 0.03822  -0.01448 -0.01003 167 GLY A N   
1340 C CA  . GLY A 160 ? 0.25250 0.26761 0.29637 0.04359  -0.01263 -0.01120 167 GLY A CA  
1341 C C   . GLY A 160 ? 0.25632 0.27811 0.30077 0.04337  -0.00951 -0.01519 167 GLY A C   
1342 O O   . GLY A 160 ? 0.28842 0.31271 0.33806 0.04813  -0.00708 -0.01724 167 GLY A O   
1343 N N   . GLY A 161 ? 0.20070 0.22578 0.24035 0.03824  -0.00922 -0.01605 168 GLY A N   
1344 C CA  . GLY A 161 ? 0.19025 0.22346 0.23140 0.03770  -0.00621 -0.01804 168 GLY A CA  
1345 C C   . GLY A 161 ? 0.19448 0.22339 0.22978 0.03728  -0.00294 -0.02239 168 GLY A C   
1346 O O   . GLY A 161 ? 0.19993 0.23587 0.23547 0.03658  0.00003  -0.02334 168 GLY A O   
1347 N N   . SER A 162 ? 0.18695 0.20537 0.21721 0.03756  -0.00340 -0.02485 169 SER A N   
1348 C CA  . SER A 162 ? 0.17122 0.18665 0.19608 0.03804  -0.00071 -0.02964 169 SER A CA  
1349 C C   . SER A 162 ? 0.20124 0.20747 0.21920 0.03465  -0.00266 -0.03082 169 SER A C   
1350 O O   . SER A 162 ? 0.21386 0.21447 0.23226 0.03321  -0.00547 -0.02853 169 SER A O   
1351 C CB  . SER A 162 ? 0.20870 0.22197 0.23659 0.04402  0.00151  -0.03400 169 SER A CB  
1352 O OG  . SER A 162 ? 0.22184 0.22479 0.25147 0.04574  -0.00065 -0.03472 169 SER A OG  
1353 N N   . PHE A 163 ? 0.19470 0.20047 0.20635 0.03351  -0.00104 -0.03407 170 PHE A N   
1354 C CA  . PHE A 163 ? 0.17251 0.17081 0.17811 0.03086  -0.00279 -0.03594 170 PHE A CA  
1355 C C   . PHE A 163 ? 0.20953 0.20661 0.21072 0.03317  -0.00100 -0.04184 170 PHE A C   
1356 O O   . PHE A 163 ? 0.20944 0.21261 0.21055 0.03607  0.00209  -0.04372 170 PHE A O   
1357 C CB  . PHE A 163 ? 0.18960 0.18942 0.19067 0.02596  -0.00380 -0.03290 170 PHE A CB  
1358 C CG  . PHE A 163 ? 0.17435 0.18123 0.17232 0.02504  -0.00115 -0.03230 170 PHE A CG  
1359 C CD1 . PHE A 163 ? 0.18369 0.19803 0.18601 0.02418  0.00017  -0.02888 170 PHE A CD1 
1360 C CD2 . PHE A 163 ? 0.18904 0.19553 0.18016 0.02473  -0.00014 -0.03456 170 PHE A CD2 
1361 C CE1 . PHE A 163 ? 0.20636 0.22681 0.20680 0.02275  0.00290  -0.02739 170 PHE A CE1 
1362 C CE2 . PHE A 163 ? 0.18344 0.19624 0.17170 0.02393  0.00250  -0.03277 170 PHE A CE2 
1363 C CZ  . PHE A 163 ? 0.20325 0.22272 0.19647 0.02270  0.00426  -0.02886 170 PHE A CZ  
1364 N N   . THR A 164 ? 0.19628 0.18613 0.19406 0.03198  -0.00296 -0.04503 171 THR A N   
1365 C CA  . THR A 164 ? 0.19690 0.18592 0.18944 0.03372  -0.00210 -0.05144 171 THR A CA  
1366 C C   . THR A 164 ? 0.19572 0.18502 0.18099 0.03021  -0.00358 -0.05142 171 THR A C   
1367 O O   . THR A 164 ? 0.21852 0.20521 0.20403 0.02661  -0.00581 -0.04779 171 THR A O   
1368 C CB  . THR A 164 ? 0.23714 0.21763 0.23309 0.03598  -0.00336 -0.05687 171 THR A CB  
1369 O OG1 . THR A 164 ? 0.23779 0.21092 0.23557 0.03250  -0.00659 -0.05524 171 THR A OG1 
1370 C CG2 . THR A 164 ? 0.23614 0.21598 0.23979 0.04050  -0.00172 -0.05690 171 THR A CG2 
1371 N N   . VAL A 165 ? 0.21933 0.21247 0.19804 0.03176  -0.00220 -0.05543 172 VAL A N   
1372 C CA  . VAL A 165 ? 0.24744 0.24112 0.21892 0.02945  -0.00398 -0.05623 172 VAL A CA  
1373 C C   . VAL A 165 ? 0.26004 0.25248 0.22718 0.03182  -0.00472 -0.06437 172 VAL A C   
1374 O O   . VAL A 165 ? 0.23697 0.23278 0.20250 0.03574  -0.00204 -0.06852 172 VAL A O   
1375 C CB  . VAL A 165 ? 0.22361 0.22510 0.18987 0.02857  -0.00176 -0.05150 172 VAL A CB  
1376 C CG1 . VAL A 165 ? 0.24516 0.24739 0.20390 0.02694  -0.00386 -0.05190 172 VAL A CG1 
1377 C CG2 . VAL A 165 ? 0.22002 0.22210 0.19112 0.02574  -0.00150 -0.04452 172 VAL A CG2 
1378 N N   . ARG A 166 ? 0.23782 0.22629 0.20304 0.02948  -0.00835 -0.06699 173 ARG A N   
1379 C CA  . ARG A 166 ? 0.25538 0.24341 0.21597 0.03105  -0.00992 -0.07535 173 ARG A CA  
1380 C C   . ARG A 166 ? 0.26274 0.25234 0.21833 0.02812  -0.01343 -0.07524 173 ARG A C   
1381 O O   . ARG A 166 ? 0.24785 0.23593 0.20604 0.02479  -0.01496 -0.06959 173 ARG A O   
1382 C CB  . ARG A 166 ? 0.30692 0.28605 0.27473 0.03173  -0.01137 -0.08116 173 ARG A CB  
1383 C CG  . ARG A 166 ? 0.31651 0.28830 0.29068 0.02745  -0.01486 -0.07916 173 ARG A CG  
1384 C CD  . ARG A 166 ? 0.42270 0.38501 0.40605 0.02814  -0.01522 -0.08194 173 ARG A CD  
1385 N NE  . ARG A 166 ? 0.44028 0.40192 0.42889 0.03006  -0.01249 -0.07622 173 ARG A NE  
1386 C CZ  . ARG A 166 ? 0.50192 0.45679 0.49818 0.03231  -0.01179 -0.07736 173 ARG A CZ  
1387 N NH1 . ARG A 166 ? 0.47385 0.42077 0.47395 0.03281  -0.01328 -0.08433 173 ARG A NH1 
1388 N NH2 . ARG A 166 ? 0.45899 0.41509 0.45964 0.03417  -0.00974 -0.07139 173 ARG A NH2 
1389 N N   . THR A 167 ? 0.27901 0.27245 0.22719 0.02973  -0.01474 -0.08166 174 THR A N   
1390 C CA  . THR A 167 ? 0.28338 0.27824 0.22824 0.02714  -0.01902 -0.08256 174 THR A CA  
1391 C C   . THR A 167 ? 0.32671 0.31324 0.28029 0.02389  -0.02260 -0.08548 174 THR A C   
1392 O O   . THR A 167 ? 0.40303 0.38304 0.36221 0.02458  -0.02257 -0.09077 174 THR A O   
1393 C CB  . THR A 167 ? 0.36636 0.36787 0.30126 0.02970  -0.02023 -0.08936 174 THR A CB  
1394 O OG1 . THR A 167 ? 0.37814 0.38769 0.30532 0.03283  -0.01600 -0.08564 174 THR A OG1 
1395 C CG2 . THR A 167 ? 0.43729 0.44196 0.36895 0.02728  -0.02503 -0.08942 174 THR A CG2 
1396 N N   . ASP A 168 ? 0.28427 0.27084 0.23990 0.02039  -0.02536 -0.08146 175 ASP A N   
1397 C CA  . ASP A 168 ? 0.31319 0.29281 0.27798 0.01682  -0.02813 -0.08265 175 ASP A CA  
1398 C C   . ASP A 168 ? 0.44048 0.42155 0.40427 0.01543  -0.03272 -0.09033 175 ASP A C   
1399 O O   . ASP A 168 ? 0.49563 0.48395 0.45337 0.01530  -0.03500 -0.08990 175 ASP A O   
1400 C CB  . ASP A 168 ? 0.30941 0.28881 0.27803 0.01392  -0.02814 -0.07425 175 ASP A CB  
1401 C CG  . ASP A 168 ? 0.48388 0.45680 0.46230 0.01036  -0.02993 -0.07416 175 ASP A CG  
1402 O OD1 . ASP A 168 ? 0.52311 0.48908 0.50751 0.01045  -0.02915 -0.07657 175 ASP A OD1 
1403 O OD2 . ASP A 168 ? 0.39281 0.36774 0.37339 0.00762  -0.03188 -0.07119 175 ASP A OD2 
1404 N N   . THR A 169 ? 0.51913 0.49339 0.48922 0.01448  -0.03421 -0.09730 176 THR A N   
1405 C CA  . THR A 169 ? 0.62560 0.60000 0.59746 0.01214  -0.03908 -0.10540 176 THR A CA  
1406 C C   . THR A 169 ? 0.61327 0.58394 0.59565 0.00696  -0.04159 -0.10258 176 THR A C   
1407 O O   . THR A 169 ? 0.63815 0.60896 0.62442 0.00408  -0.04588 -0.10891 176 THR A O   
1408 C CB  . THR A 169 ? 0.62646 0.59477 0.60015 0.01383  -0.03930 -0.11565 176 THR A CB  
1409 O OG1 . THR A 169 ? 0.69088 0.64988 0.67245 0.01450  -0.03581 -0.11265 176 THR A OG1 
1410 C CG2 . THR A 169 ? 0.57684 0.55211 0.53841 0.01883  -0.03793 -0.12078 176 THR A CG2 
1411 N N   . GLY A 170 ? 0.59806 0.56607 0.58525 0.00566  -0.03901 -0.09352 177 GLY A N   
1412 C CA  . GLY A 170 ? 0.59888 0.56431 0.59571 0.00109  -0.04042 -0.08983 177 GLY A CA  
1413 C C   . GLY A 170 ? 0.47024 0.44416 0.46562 -0.00094 -0.04380 -0.08880 177 GLY A C   
1414 O O   . GLY A 170 ? 0.46692 0.44839 0.45409 0.00095  -0.04597 -0.09180 177 GLY A O   
1415 N N   . GLU A 171 ? 0.46421 0.43733 0.46801 -0.00458 -0.04410 -0.08404 178 GLU A N   
1416 C CA  . GLU A 171 ? 0.40889 0.38997 0.41405 -0.00661 -0.04712 -0.08254 178 GLU A CA  
1417 C C   . GLU A 171 ? 0.41180 0.40014 0.40694 -0.00309 -0.04618 -0.07772 178 GLU A C   
1418 O O   . GLU A 171 ? 0.31691 0.30334 0.30971 -0.00150 -0.04232 -0.07115 178 GLU A O   
1419 C CB  . GLU A 171 ? 0.41816 0.39696 0.43385 -0.01036 -0.04585 -0.07669 178 GLU A CB  
1420 C CG  . GLU A 171 ? 0.46202 0.44790 0.48420 -0.01364 -0.04911 -0.07653 178 GLU A CG  
1421 C CD  . GLU A 171 ? 0.42215 0.40987 0.44876 -0.01635 -0.05423 -0.08566 178 GLU A CD  
1422 O OE1 . GLU A 171 ? 0.51831 0.51493 0.54057 -0.01542 -0.05817 -0.08885 178 GLU A OE1 
1423 O OE2 . GLU A 171 ? 0.48632 0.46635 0.52043 -0.01916 -0.05446 -0.08984 178 GLU A OE2 
1424 N N   . PRO A 172 ? 0.40816 0.40475 0.39746 -0.00181 -0.04968 -0.08061 179 PRO A N   
1425 C CA  . PRO A 172 ? 0.37845 0.38124 0.35872 0.00166  -0.04861 -0.07511 179 PRO A CA  
1426 C C   . PRO A 172 ? 0.38080 0.38433 0.36542 0.00084  -0.04681 -0.06694 179 PRO A C   
1427 O O   . PRO A 172 ? 0.47265 0.47706 0.46611 -0.00221 -0.04824 -0.06631 179 PRO A O   
1428 C CB  . PRO A 172 ? 0.47396 0.48591 0.44941 0.00260  -0.05366 -0.07974 179 PRO A CB  
1429 C CG  . PRO A 172 ? 0.50514 0.51463 0.48270 0.00095  -0.05648 -0.08983 179 PRO A CG  
1430 C CD  . PRO A 172 ? 0.47713 0.47736 0.46678 -0.00301 -0.05477 -0.08967 179 PRO A CD  
1431 N N   . MET A 173 ? 0.32790 0.33163 0.30642 0.00360  -0.04363 -0.06090 180 MET A N   
1432 C CA  . MET A 173 ? 0.30451 0.30751 0.28639 0.00327  -0.04128 -0.05385 180 MET A CA  
1433 C C   . MET A 173 ? 0.39814 0.40758 0.37710 0.00536  -0.04250 -0.04970 180 MET A C   
1434 O O   . MET A 173 ? 0.43077 0.43986 0.41368 0.00512  -0.04096 -0.04496 180 MET A O   
1435 C CB  . MET A 173 ? 0.34681 0.34436 0.32568 0.00449  -0.03673 -0.04992 180 MET A CB  
1436 C CG  . MET A 173 ? 0.48545 0.47634 0.46962 0.00259  -0.03479 -0.05083 180 MET A CG  
1437 S SD  . MET A 173 ? 0.47771 0.46569 0.45674 0.00480  -0.03045 -0.04616 180 MET A SD  
1438 C CE  . MET A 173 ? 0.34311 0.33230 0.32391 0.00440  -0.02921 -0.03984 180 MET A CE  
1439 N N   . GLY A 174 ? 0.35082 0.36582 0.32253 0.00788  -0.04477 -0.05085 181 GLY A N   
1440 C CA  . GLY A 174 ? 0.30795 0.32841 0.27723 0.01039  -0.04574 -0.04575 181 GLY A CA  
1441 C C   . GLY A 174 ? 0.28491 0.30232 0.24815 0.01287  -0.04176 -0.03982 181 GLY A C   
1442 O O   . GLY A 174 ? 0.28795 0.30858 0.24301 0.01562  -0.04179 -0.03825 181 GLY A O   
1443 N N   . ARG A 175 ? 0.21323 0.22479 0.18084 0.01169  -0.03833 -0.03649 182 ARG A N   
1444 C CA  . ARG A 175 ? 0.23497 0.24258 0.19928 0.01301  -0.03450 -0.03134 182 ARG A CA  
1445 C C   . ARG A 175 ? 0.23858 0.24033 0.20867 0.01085  -0.03173 -0.03031 182 ARG A C   
1446 O O   . ARG A 175 ? 0.24014 0.24227 0.21644 0.00961  -0.03243 -0.03037 182 ARG A O   
1447 C CB  . ARG A 175 ? 0.22838 0.23858 0.19098 0.01567  -0.03482 -0.02587 182 ARG A CB  
1448 C CG  . ARG A 175 ? 0.22283 0.22869 0.18200 0.01674  -0.03100 -0.02073 182 ARG A CG  
1449 C CD  . ARG A 175 ? 0.19877 0.20446 0.15921 0.01900  -0.03086 -0.01504 182 ARG A CD  
1450 N NE  . ARG A 175 ? 0.23125 0.23531 0.19924 0.01815  -0.03104 -0.01561 182 ARG A NE  
1451 C CZ  . ARG A 175 ? 0.23098 0.23989 0.20285 0.01945  -0.03384 -0.01571 182 ARG A CZ  
1452 N NH1 . ARG A 175 ? 0.22803 0.24370 0.19699 0.02163  -0.03728 -0.01526 182 ARG A NH1 
1453 N NH2 . ARG A 175 ? 0.22709 0.23510 0.20599 0.01865  -0.03322 -0.01637 182 ARG A NH2 
1454 N N   . GLY A 176 ? 0.21454 0.21194 0.18253 0.01060  -0.02858 -0.02904 183 GLY A N   
1455 C CA  . GLY A 176 ? 0.20117 0.19399 0.17348 0.00898  -0.02623 -0.02759 183 GLY A CA  
1456 C C   . GLY A 176 ? 0.22444 0.21407 0.19683 0.00781  -0.02461 -0.02954 183 GLY A C   
1457 O O   . GLY A 176 ? 0.22428 0.21467 0.19292 0.00868  -0.02440 -0.03138 183 GLY A O   
1458 N N   . THR A 177 ? 0.19637 0.18294 0.17293 0.00622  -0.02332 -0.02891 184 THR A N   
1459 C CA  . THR A 177 ? 0.19174 0.17543 0.16917 0.00550  -0.02190 -0.02986 184 THR A CA  
1460 C C   . THR A 177 ? 0.25667 0.23847 0.23947 0.00371  -0.02210 -0.03039 184 THR A C   
1461 O O   . THR A 177 ? 0.22072 0.20316 0.20620 0.00288  -0.02193 -0.02866 184 THR A O   
1462 C CB  . THR A 177 ? 0.23333 0.21563 0.20936 0.00567  -0.01958 -0.02700 184 THR A CB  
1463 O OG1 . THR A 177 ? 0.25551 0.23945 0.22730 0.00700  -0.01889 -0.02569 184 THR A OG1 
1464 C CG2 . THR A 177 ? 0.23418 0.21461 0.21193 0.00522  -0.01837 -0.02735 184 THR A CG2 
1465 N N   . LYS A 178 ? 0.20882 0.18826 0.19335 0.00336  -0.02208 -0.03244 185 LYS A N   
1466 C CA  . LYS A 178 ? 0.21201 0.18891 0.20200 0.00168  -0.02190 -0.03195 185 LYS A CA  
1467 C C   . LYS A 178 ? 0.25173 0.22599 0.24171 0.00241  -0.02024 -0.03050 185 LYS A C   
1468 O O   . LYS A 178 ? 0.24394 0.21717 0.23267 0.00380  -0.02010 -0.03265 185 LYS A O   
1469 C CB  . LYS A 178 ? 0.28926 0.26495 0.28279 0.00065  -0.02386 -0.03590 185 LYS A CB  
1470 C CG  . LYS A 178 ? 0.54667 0.52453 0.54470 -0.00138 -0.02520 -0.03584 185 LYS A CG  
1471 C CD  . LYS A 178 ? 0.48427 0.46280 0.48501 -0.00252 -0.02811 -0.04087 185 LYS A CD  
1472 C CE  . LYS A 178 ? 0.46105 0.43455 0.46270 -0.00227 -0.02822 -0.04449 185 LYS A CE  
1473 N NZ  . LYS A 178 ? 0.55363 0.52759 0.55900 -0.00404 -0.03144 -0.05022 185 LYS A NZ  
1474 N N   . VAL A 179 ? 0.19663 0.17061 0.18787 0.00182  -0.01902 -0.02703 186 VAL A N   
1475 C CA  . VAL A 179 ? 0.18358 0.15610 0.17535 0.00267  -0.01798 -0.02524 186 VAL A CA  
1476 C C   . VAL A 179 ? 0.22399 0.19360 0.22069 0.00177  -0.01789 -0.02364 186 VAL A C   
1477 O O   . VAL A 179 ? 0.22165 0.19220 0.21996 0.00032  -0.01742 -0.02109 186 VAL A O   
1478 C CB  . VAL A 179 ? 0.18208 0.15699 0.17126 0.00279  -0.01707 -0.02256 186 VAL A CB  
1479 C CG1 . VAL A 179 ? 0.19626 0.17104 0.18650 0.00374  -0.01661 -0.02042 186 VAL A CG1 
1480 C CG2 . VAL A 179 ? 0.19403 0.17078 0.17959 0.00332  -0.01693 -0.02363 186 VAL A CG2 
1481 N N   . ILE A 180 ? 0.20696 0.17300 0.20637 0.00275  -0.01805 -0.02495 187 ILE A N   
1482 C CA  . ILE A 180 ? 0.18786 0.14967 0.19303 0.00197  -0.01788 -0.02309 187 ILE A CA  
1483 C C   . ILE A 180 ? 0.20936 0.17080 0.21481 0.00381  -0.01694 -0.01904 187 ILE A C   
1484 O O   . ILE A 180 ? 0.20761 0.16859 0.21261 0.00620  -0.01688 -0.02036 187 ILE A O   
1485 C CB  . ILE A 180 ? 0.17202 0.12908 0.18103 0.00198  -0.01892 -0.02770 187 ILE A CB  
1486 C CG1 . ILE A 180 ? 0.23578 0.19511 0.24342 0.00046  -0.02054 -0.03217 187 ILE A CG1 
1487 C CG2 . ILE A 180 ? 0.22831 0.17960 0.24481 0.00073  -0.01860 -0.02529 187 ILE A CG2 
1488 C CD1 . ILE A 180 ? 0.29721 0.25346 0.30610 0.00106  -0.02195 -0.03839 187 ILE A CD1 
1489 N N   . LEU A 181 ? 0.19351 0.15622 0.19951 0.00298  -0.01617 -0.01403 188 LEU A N   
1490 C CA  . LEU A 181 ? 0.17741 0.14105 0.18312 0.00492  -0.01575 -0.00965 188 LEU A CA  
1491 C C   . LEU A 181 ? 0.20708 0.16511 0.21899 0.00525  -0.01534 -0.00650 188 LEU A C   
1492 O O   . LEU A 181 ? 0.20653 0.16308 0.22144 0.00307  -0.01456 -0.00353 188 LEU A O   
1493 C CB  . LEU A 181 ? 0.17429 0.14326 0.17590 0.00422  -0.01522 -0.00606 188 LEU A CB  
1494 C CG  . LEU A 181 ? 0.19573 0.16894 0.19223 0.00361  -0.01549 -0.00912 188 LEU A CG  
1495 C CD1 . LEU A 181 ? 0.22624 0.20386 0.21928 0.00302  -0.01480 -0.00619 188 LEU A CD1 
1496 C CD2 . LEU A 181 ? 0.22503 0.19996 0.21953 0.00520  -0.01623 -0.01134 188 LEU A CD2 
1497 N N   . HIS A 182 ? 0.20324 0.15809 0.21785 0.00803  -0.01562 -0.00687 189 HIS A N   
1498 C CA  . HIS A 182 ? 0.24468 0.19318 0.26586 0.00896  -0.01517 -0.00322 189 HIS A CA  
1499 C C   . HIS A 182 ? 0.23613 0.18834 0.25577 0.01072  -0.01486 0.00412  189 HIS A C   
1500 O O   . HIS A 182 ? 0.23688 0.19262 0.25476 0.01372  -0.01556 0.00473  189 HIS A O   
1501 C CB  . HIS A 182 ? 0.24325 0.18648 0.26835 0.01179  -0.01552 -0.00750 189 HIS A CB  
1502 C CG  . HIS A 182 ? 0.30016 0.24157 0.32475 0.01051  -0.01611 -0.01545 189 HIS A CG  
1503 N ND1 . HIS A 182 ? 0.34141 0.27577 0.37158 0.00874  -0.01650 -0.01880 189 HIS A ND1 
1504 C CD2 . HIS A 182 ? 0.28799 0.23411 0.30709 0.01065  -0.01650 -0.02046 189 HIS A CD2 
1505 C CE1 . HIS A 182 ? 0.30683 0.24236 0.33422 0.00809  -0.01744 -0.02599 189 HIS A CE1 
1506 N NE2 . HIS A 182 ? 0.30803 0.25060 0.32851 0.00945  -0.01726 -0.02666 189 HIS A NE2 
1507 N N   . LEU A 183 ? 0.20183 0.15483 0.22160 0.00880  -0.01386 0.00963  190 LEU A N   
1508 C CA  . LEU A 183 ? 0.20928 0.16853 0.22468 0.01025  -0.01377 0.01596  190 LEU A CA  
1509 C C   . LEU A 183 ? 0.24447 0.20130 0.26359 0.01384  -0.01408 0.02174  190 LEU A C   
1510 O O   . LEU A 183 ? 0.28666 0.23529 0.31304 0.01440  -0.01347 0.02331  190 LEU A O   
1511 C CB  . LEU A 183 ? 0.24093 0.20265 0.25486 0.00753  -0.01206 0.02046  190 LEU A CB  
1512 C CG  . LEU A 183 ? 0.21356 0.17926 0.22363 0.00466  -0.01166 0.01575  190 LEU A CG  
1513 C CD1 . LEU A 183 ? 0.23489 0.20431 0.24397 0.00257  -0.00939 0.02077  190 LEU A CD1 
1514 C CD2 . LEU A 183 ? 0.23829 0.21025 0.24121 0.00591  -0.01302 0.01203  190 LEU A CD2 
1515 N N   . LYS A 184 ? 0.24138 0.20554 0.25580 0.01634  -0.01523 0.02494  191 LYS A N   
1516 C CA  . LYS A 184 ? 0.24198 0.20625 0.25891 0.02017  -0.01583 0.03210  191 LYS A CA  
1517 C C   . LYS A 184 ? 0.28372 0.24502 0.30257 0.01921  -0.01399 0.04045  191 LYS A C   
1518 O O   . LYS A 184 ? 0.30233 0.26607 0.31787 0.01594  -0.01249 0.04138  191 LYS A O   
1519 C CB  . LYS A 184 ? 0.25314 0.22806 0.26376 0.02232  -0.01794 0.03333  191 LYS A CB  
1520 C CG  . LYS A 184 ? 0.27890 0.25746 0.28908 0.02323  -0.01956 0.02621  191 LYS A CG  
1521 C CD  . LYS A 184 ? 0.32129 0.31120 0.32577 0.02427  -0.02198 0.02705  191 LYS A CD  
1522 C CE  . LYS A 184 ? 0.40632 0.40086 0.40958 0.02321  -0.02309 0.01971  191 LYS A CE  
1523 N NZ  . LYS A 184 ? 0.38708 0.39280 0.38636 0.02369  -0.02595 0.01975  191 LYS A NZ  
1524 N N   . GLU A 185 ? 0.32452 0.28056 0.34940 0.02225  -0.01384 0.04694  192 GLU A N   
1525 C CA  . GLU A 185 ? 0.34349 0.29518 0.37188 0.02115  -0.01163 0.05574  192 GLU A CA  
1526 C C   . GLU A 185 ? 0.33289 0.29438 0.35292 0.02047  -0.01086 0.06214  192 GLU A C   
1527 O O   . GLU A 185 ? 0.35902 0.31913 0.38020 0.01773  -0.00816 0.06741  192 GLU A O   
1528 C CB  . GLU A 185 ? 0.38909 0.33371 0.42517 0.02538  -0.01179 0.06262  192 GLU A CB  
1529 C CG  . GLU A 185 ? 0.54834 0.50085 0.58080 0.03094  -0.01426 0.06694  192 GLU A CG  
1530 C CD  . GLU A 185 ? 0.67934 0.63786 0.70758 0.03279  -0.01394 0.07895  192 GLU A CD  
1531 O OE1 . GLU A 185 ? 0.74946 0.70445 0.77904 0.03012  -0.01115 0.08528  192 GLU A OE1 
1532 O OE2 . GLU A 185 ? 0.70137 0.66912 0.72489 0.03686  -0.01653 0.08214  192 GLU A OE2 
1533 N N   A ASP A 186 ? 0.31693 0.28876 0.32882 0.02281  -0.01308 0.06161  193 ASP A N   
1534 N N   B ASP A 186 ? 0.31693 0.28876 0.32882 0.02281  -0.01308 0.06161  193 ASP A N   
1535 C CA  A ASP A 186 ? 0.33392 0.31581 0.33681 0.02274  -0.01263 0.06686  193 ASP A CA  
1536 C CA  B ASP A 186 ? 0.33392 0.31581 0.33681 0.02274  -0.01263 0.06686  193 ASP A CA  
1537 C C   A ASP A 186 ? 0.31083 0.29881 0.30653 0.01935  -0.01218 0.05963  193 ASP A C   
1538 C C   B ASP A 186 ? 0.31083 0.29881 0.30653 0.01935  -0.01218 0.05963  193 ASP A C   
1539 O O   A ASP A 186 ? 0.29206 0.28945 0.27909 0.01968  -0.01221 0.06164  193 ASP A O   
1540 O O   B ASP A 186 ? 0.29206 0.28945 0.27909 0.01968  -0.01221 0.06164  193 ASP A O   
1541 C CB  A ASP A 186 ? 0.35335 0.34381 0.35145 0.02743  -0.01573 0.07104  193 ASP A CB  
1542 C CB  B ASP A 186 ? 0.35335 0.34381 0.35145 0.02743  -0.01573 0.07104  193 ASP A CB  
1543 C CG  A ASP A 186 ? 0.39833 0.39388 0.39425 0.02837  -0.01907 0.06237  193 ASP A CG  
1544 C CG  B ASP A 186 ? 0.39833 0.39388 0.39425 0.02837  -0.01907 0.06237  193 ASP A CG  
1545 O OD1 A ASP A 186 ? 0.43044 0.42119 0.42963 0.02621  -0.01886 0.05394  193 ASP A OD1 
1546 O OD1 B ASP A 186 ? 0.43044 0.42119 0.42963 0.02621  -0.01886 0.05394  193 ASP A OD1 
1547 O OD2 A ASP A 186 ? 0.43910 0.44430 0.42997 0.03115  -0.02198 0.06417  193 ASP A OD2 
1548 O OD2 B ASP A 186 ? 0.43910 0.44430 0.42997 0.03115  -0.02198 0.06417  193 ASP A OD2 
1549 N N   . GLN A 187 ? 0.27448 0.25734 0.27354 0.01639  -0.01173 0.05140  194 GLN A N   
1550 C CA  . GLN A 187 ? 0.25552 0.24304 0.24897 0.01364  -0.01141 0.04441  194 GLN A CA  
1551 C C   . GLN A 187 ? 0.22769 0.21058 0.22539 0.00979  -0.00850 0.04335  194 GLN A C   
1552 O O   . GLN A 187 ? 0.24392 0.22742 0.24045 0.00757  -0.00840 0.03640  194 GLN A O   
1553 C CB  . GLN A 187 ? 0.23702 0.22454 0.23006 0.01391  -0.01392 0.03561  194 GLN A CB  
1554 C CG  . GLN A 187 ? 0.24039 0.23436 0.23003 0.01721  -0.01696 0.03620  194 GLN A CG  
1555 C CD  . GLN A 187 ? 0.27824 0.28224 0.25908 0.01792  -0.01770 0.03896  194 GLN A CD  
1556 O OE1 . GLN A 187 ? 0.28361 0.29110 0.25902 0.01576  -0.01652 0.03598  194 GLN A OE1 
1557 N NE2 . GLN A 187 ? 0.31476 0.32423 0.29392 0.02130  -0.02001 0.04388  194 GLN A NE2 
1558 N N   . THR A 188 ? 0.27189 0.25042 0.27527 0.00889  -0.00616 0.05051  195 THR A N   
1559 C CA  . THR A 188 ? 0.27733 0.25209 0.28649 0.00477  -0.00366 0.04929  195 THR A CA  
1560 C C   . THR A 188 ? 0.24294 0.22606 0.24674 0.00296  -0.00106 0.05036  195 THR A C   
1561 O O   . THR A 188 ? 0.28031 0.26220 0.28914 -0.00047 0.00093  0.04880  195 THR A O   
1562 C CB  . THR A 188 ? 0.29817 0.26444 0.31731 0.00366  -0.00194 0.05608  195 THR A CB  
1563 O OG1 . THR A 188 ? 0.33846 0.30851 0.35522 0.00523  0.00004  0.06693  195 THR A OG1 
1564 C CG2 . THR A 188 ? 0.27668 0.23377 0.30192 0.00572  -0.00432 0.05336  195 THR A CG2 
1565 N N   . GLU A 189 ? 0.24596 0.23813 0.23993 0.00523  -0.00115 0.05216  196 GLU A N   
1566 C CA  . GLU A 189 ? 0.28368 0.28397 0.27197 0.00403  0.00133  0.05100  196 GLU A CA  
1567 C C   . GLU A 189 ? 0.25576 0.25534 0.24494 0.00209  0.00071  0.04145  196 GLU A C   
1568 O O   . GLU A 189 ? 0.24161 0.24544 0.23056 0.00046  0.00334  0.04048  196 GLU A O   
1569 C CB  . GLU A 189 ? 0.25681 0.26671 0.23361 0.00710  0.00059  0.05248  196 GLU A CB  
1570 C CG  . GLU A 189 ? 0.26192 0.27361 0.23332 0.00858  -0.00332 0.04397  196 GLU A CG  
1571 C CD  . GLU A 189 ? 0.32582 0.34673 0.28706 0.01155  -0.00488 0.04591  196 GLU A CD  
1572 O OE1 . GLU A 189 ? 0.31914 0.34075 0.28010 0.01396  -0.00649 0.05218  196 GLU A OE1 
1573 O OE2 . GLU A 189 ? 0.32260 0.35025 0.27630 0.01168  -0.00460 0.04120  196 GLU A OE2 
1574 N N   . TYR A 190 ? 0.22667 0.22147 0.21715 0.00249  -0.00250 0.03483  197 TYR A N   
1575 C CA  . TYR A 190 ? 0.20155 0.19590 0.19215 0.00112  -0.00328 0.02650  197 TYR A CA  
1576 C C   . TYR A 190 ? 0.22112 0.21012 0.22068 -0.00181 -0.00250 0.02499  197 TYR A C   
1577 O O   . TYR A 190 ? 0.22957 0.21786 0.22995 -0.00273 -0.00354 0.01853  197 TYR A O   
1578 C CB  . TYR A 190 ? 0.22121 0.21381 0.20899 0.00271  -0.00671 0.02066  197 TYR A CB  
1579 C CG  . TYR A 190 ? 0.20801 0.20710 0.18756 0.00507  -0.00794 0.02135  197 TYR A CG  
1580 C CD1 . TYR A 190 ? 0.23438 0.23999 0.20716 0.00521  -0.00707 0.01885  197 TYR A CD1 
1581 C CD2 . TYR A 190 ? 0.23121 0.23048 0.21008 0.00736  -0.01003 0.02455  197 TYR A CD2 
1582 C CE1 . TYR A 190 ? 0.24334 0.25545 0.20835 0.00714  -0.00852 0.01876  197 TYR A CE1 
1583 C CE2 . TYR A 190 ? 0.24882 0.25552 0.22022 0.00937  -0.01173 0.02500  197 TYR A CE2 
1584 C CZ  . TYR A 190 ? 0.23518 0.24815 0.19948 0.00899  -0.01107 0.02168  197 TYR A CZ  
1585 O OH  . TYR A 190 ? 0.25072 0.27139 0.20741 0.01074  -0.01303 0.02130  197 TYR A OH  
1586 N N   . LEU A 191 ? 0.22986 0.21522 0.23647 -0.00337 -0.00086 0.03093  198 LEU A N   
1587 C CA  . LEU A 191 ? 0.22869 0.21069 0.24450 -0.00690 0.00010  0.02976  198 LEU A CA  
1588 C C   . LEU A 191 ? 0.26730 0.25571 0.28499 -0.00892 0.00394  0.03440  198 LEU A C   
1589 O O   . LEU A 191 ? 0.28532 0.27286 0.31143 -0.01223 0.00486  0.03358  198 LEU A O   
1590 C CB  . LEU A 191 ? 0.22562 0.19852 0.25011 -0.00800 -0.00050 0.03252  198 LEU A CB  
1591 C CG  . LEU A 191 ? 0.24923 0.21585 0.27313 -0.00572 -0.00375 0.02796  198 LEU A CG  
1592 C CD1 . LEU A 191 ? 0.29504 0.25220 0.32792 -0.00628 -0.00389 0.03094  198 LEU A CD1 
1593 C CD2 . LEU A 191 ? 0.26783 0.23434 0.29091 -0.00642 -0.00593 0.01871  198 LEU A CD2 
1594 N N   . GLU A 192 ? 0.23235 0.22780 0.24283 -0.00704 0.00624  0.03937  199 GLU A N   
1595 C CA  . GLU A 192 ? 0.25666 0.25929 0.26859 -0.00859 0.01063  0.04441  199 GLU A CA  
1596 C C   . GLU A 192 ? 0.27098 0.28052 0.27968 -0.00830 0.01141  0.03821  199 GLU A C   
1597 O O   . GLU A 192 ? 0.25218 0.26397 0.25235 -0.00560 0.00966  0.03290  199 GLU A O   
1598 C CB  . GLU A 192 ? 0.30995 0.31807 0.31476 -0.00631 0.01306  0.05266  199 GLU A CB  
1599 C CG  . GLU A 192 ? 0.35988 0.36133 0.36656 -0.00530 0.01171  0.05888  199 GLU A CG  
1600 C CD  . GLU A 192 ? 0.57434 0.58180 0.57516 -0.00326 0.01443  0.06896  199 GLU A CD  
1601 O OE1 . GLU A 192 ? 0.62806 0.63257 0.62641 -0.00064 0.01243  0.07318  199 GLU A OE1 
1602 O OE2 . GLU A 192 ? 0.64024 0.65604 0.63880 -0.00394 0.01862  0.07287  199 GLU A OE2 
1603 N N   . GLU A 193 ? 0.27488 0.28786 0.29132 -0.01110 0.01408  0.03900  200 GLU A N   
1604 C CA  . GLU A 193 ? 0.22588 0.24518 0.24123 -0.01053 0.01482  0.03324  200 GLU A CA  
1605 C C   . GLU A 193 ? 0.25288 0.27987 0.25673 -0.00685 0.01674  0.03254  200 GLU A C   
1606 O O   . GLU A 193 ? 0.26366 0.29179 0.26254 -0.00473 0.01517  0.02552  200 GLU A O   
1607 C CB  . GLU A 193 ? 0.23791 0.26204 0.26405 -0.01391 0.01808  0.03590  200 GLU A CB  
1608 C CG  . GLU A 193 ? 0.30846 0.33755 0.33629 -0.01329 0.01770  0.02918  200 GLU A CG  
1609 C CD  . GLU A 193 ? 0.52269 0.55949 0.56129 -0.01614 0.02131  0.03191  200 GLU A CD  
1610 O OE1 . GLU A 193 ? 0.46490 0.50351 0.50924 -0.01890 0.02469  0.03951  200 GLU A OE1 
1611 O OE2 . GLU A 193 ? 0.50868 0.55000 0.55051 -0.01555 0.02077  0.02679  200 GLU A OE2 
1612 N N   . ARG A 194 ? 0.26116 0.29380 0.26092 -0.00608 0.02033  0.03974  201 ARG A N   
1613 C CA  . ARG A 194 ? 0.22978 0.27102 0.21849 -0.00261 0.02240  0.03820  201 ARG A CA  
1614 C C   . ARG A 194 ? 0.26192 0.30022 0.24065 0.00027  0.01823  0.03294  201 ARG A C   
1615 O O   . ARG A 194 ? 0.25450 0.29685 0.22601 0.00272  0.01811  0.02689  201 ARG A O   
1616 C CB  . ARG A 194 ? 0.27703 0.32608 0.26244 -0.00218 0.02725  0.04748  201 ARG A CB  
1617 C CG  . ARG A 194 ? 0.34865 0.39339 0.33292 -0.00234 0.02614  0.05520  201 ARG A CG  
1618 C CD  . ARG A 194 ? 0.39798 0.45223 0.37764 -0.00143 0.03147  0.06482  201 ARG A CD  
1619 N NE  . ARG A 194 ? 0.52312 0.57469 0.49918 -0.00032 0.03028  0.07284  201 ARG A NE  
1620 C CZ  . ARG A 194 ? 0.42429 0.48306 0.39559 0.00081  0.03422  0.08279  201 ARG A CZ  
1621 N NH1 . ARG A 194 ? 0.53224 0.60149 0.50200 0.00071  0.04003  0.08589  201 ARG A NH1 
1622 N NH2 . ARG A 194 ? 0.57042 0.62642 0.53844 0.00240  0.03245  0.09011  201 ARG A NH2 
1623 N N   . ARG A 195 ? 0.21079 0.24195 0.19004 -0.00005 0.01476  0.03478  202 ARG A N   
1624 C CA  . ARG A 195 ? 0.24296 0.27200 0.21444 0.00227  0.01067  0.03013  202 ARG A CA  
1625 C C   . ARG A 195 ? 0.22932 0.25380 0.20247 0.00205  0.00781  0.02108  202 ARG A C   
1626 O O   . ARG A 195 ? 0.20459 0.23073 0.17095 0.00389  0.00622  0.01527  202 ARG A O   
1627 C CB  . ARG A 195 ? 0.22814 0.25146 0.20152 0.00222  0.00820  0.03507  202 ARG A CB  
1628 C CG  . ARG A 195 ? 0.22825 0.25061 0.19498 0.00450  0.00396  0.03135  202 ARG A CG  
1629 C CD  . ARG A 195 ? 0.25556 0.28726 0.21086 0.00719  0.00434  0.03200  202 ARG A CD  
1630 N NE  . ARG A 195 ? 0.24497 0.27636 0.19571 0.00892  -0.00009 0.02975  202 ARG A NE  
1631 C CZ  . ARG A 195 ? 0.27279 0.30750 0.21688 0.01002  -0.00254 0.02264  202 ARG A CZ  
1632 N NH1 . ARG A 195 ? 0.27668 0.31475 0.21689 0.01009  -0.00095 0.01676  202 ARG A NH1 
1633 N NH2 . ARG A 195 ? 0.26170 0.29636 0.20382 0.01107  -0.00671 0.02130  202 ARG A NH2 
1634 N N   . ILE A 196 ? 0.21369 0.23247 0.19597 -0.00027 0.00705  0.01976  203 ILE A N   
1635 C CA  . ILE A 196 ? 0.21803 0.23295 0.20155 -0.00024 0.00442  0.01218  203 ILE A CA  
1636 C C   . ILE A 196 ? 0.21886 0.23909 0.19979 0.00110  0.00630  0.00785  203 ILE A C   
1637 O O   . ILE A 196 ? 0.20828 0.22717 0.18503 0.00261  0.00445  0.00194  203 ILE A O   
1638 C CB  . ILE A 196 ? 0.22680 0.23589 0.21990 -0.00277 0.00311  0.01158  203 ILE A CB  
1639 C CG1 . ILE A 196 ? 0.20703 0.20968 0.20283 -0.00354 0.00117  0.01462  203 ILE A CG1 
1640 C CG2 . ILE A 196 ? 0.21772 0.22429 0.21113 -0.00230 0.00069  0.00442  203 ILE A CG2 
1641 C CD1 . ILE A 196 ? 0.26676 0.26419 0.27266 -0.00641 0.00050  0.01463  203 ILE A CD1 
1642 N N   . LYS A 197 ? 0.20449 0.23083 0.18859 0.00064  0.01024  0.01087  204 LYS A N   
1643 C CA  . LYS A 197 ? 0.20186 0.23403 0.18405 0.00259  0.01260  0.00683  204 LYS A CA  
1644 C C   . LYS A 197 ? 0.23405 0.26910 0.20529 0.00556  0.01257  0.00341  204 LYS A C   
1645 O O   . LYS A 197 ? 0.24013 0.27476 0.20883 0.00745  0.01196  -0.00309 204 LYS A O   
1646 C CB  . LYS A 197 ? 0.24860 0.28870 0.23561 0.00182  0.01754  0.01168  204 LYS A CB  
1647 C CG  . LYS A 197 ? 0.29713 0.33587 0.29633 -0.00142 0.01758  0.01376  204 LYS A CG  
1648 C CD  . LYS A 197 ? 0.28971 0.33807 0.29442 -0.00234 0.02308  0.01884  204 LYS A CD  
1649 C CE  . LYS A 197 ? 0.52083 0.57119 0.53757 -0.00439 0.02309  0.01738  204 LYS A CE  
1650 N NZ  . LYS A 197 ? 0.57616 0.63391 0.60167 -0.00731 0.02778  0.02447  204 LYS A NZ  
1651 N N   . GLU A 198 ? 0.19167 0.22997 0.15659 0.00608  0.01322  0.00782  205 GLU A N   
1652 C CA  . GLU A 198 ? 0.21764 0.25979 0.17170 0.00871  0.01263  0.00431  205 GLU A CA  
1653 C C   . GLU A 198 ? 0.21063 0.24627 0.16261 0.00895  0.00798  -0.00246 205 GLU A C   
1654 O O   . GLU A 198 ? 0.23603 0.27264 0.18300 0.01069  0.00748  -0.00911 205 GLU A O   
1655 C CB  . GLU A 198 ? 0.22855 0.27510 0.17666 0.00915  0.01306  0.01117  205 GLU A CB  
1656 C CG  . GLU A 198 ? 0.23270 0.28408 0.16914 0.01169  0.01144  0.00746  205 GLU A CG  
1657 C CD  . GLU A 198 ? 0.27478 0.33056 0.20559 0.01240  0.01092  0.01493  205 GLU A CD  
1658 O OE1 . GLU A 198 ? 0.26437 0.31474 0.20020 0.01100  0.00876  0.01986  205 GLU A OE1 
1659 O OE2 . GLU A 198 ? 0.26846 0.33308 0.18959 0.01470  0.01243  0.01549  205 GLU A OE2 
1660 N N   . ILE A 199 ? 0.19151 0.22041 0.14780 0.00717  0.00476  -0.00097 206 ILE A N   
1661 C CA  . ILE A 199 ? 0.20704 0.23061 0.16191 0.00713  0.00072  -0.00639 206 ILE A CA  
1662 C C   . ILE A 199 ? 0.22462 0.24415 0.18295 0.00721  0.00047  -0.01237 206 ILE A C   
1663 O O   . ILE A 199 ? 0.24778 0.26547 0.20289 0.00795  -0.00124 -0.01810 206 ILE A O   
1664 C CB  . ILE A 199 ? 0.22674 0.24505 0.18554 0.00567  -0.00206 -0.00308 206 ILE A CB  
1665 C CG1 . ILE A 199 ? 0.21649 0.23869 0.17175 0.00631  -0.00209 0.00321  206 ILE A CG1 
1666 C CG2 . ILE A 199 ? 0.25212 0.26551 0.21099 0.00536  -0.00556 -0.00835 206 ILE A CG2 
1667 C CD1 . ILE A 199 ? 0.21572 0.23242 0.17707 0.00523  -0.00364 0.00781  206 ILE A CD1 
1668 N N   . VAL A 200 ? 0.21095 0.22901 0.17642 0.00638  0.00189  -0.01099 207 VAL A N   
1669 C CA  . VAL A 200 ? 0.20377 0.21878 0.17264 0.00701  0.00159  -0.01572 207 VAL A CA  
1670 C C   . VAL A 200 ? 0.22947 0.24827 0.19441 0.00956  0.00380  -0.02014 207 VAL A C   
1671 O O   . VAL A 200 ? 0.26361 0.27855 0.22772 0.01066  0.00255  -0.02548 207 VAL A O   
1672 C CB  . VAL A 200 ? 0.21252 0.22735 0.18980 0.00576  0.00245  -0.01304 207 VAL A CB  
1673 C CG1 . VAL A 200 ? 0.22742 0.24114 0.20814 0.00716  0.00244  -0.01703 207 VAL A CG1 
1674 C CG2 . VAL A 200 ? 0.22710 0.23667 0.20792 0.00349  -0.00027 -0.01061 207 VAL A CG2 
1675 N N   . LYS A 201 ? 0.20816 0.23445 0.17051 0.01067  0.00732  -0.01798 208 LYS A N   
1676 C CA  . LYS A 201 ? 0.23353 0.26404 0.19175 0.01364  0.00987  -0.02289 208 LYS A CA  
1677 C C   . LYS A 201 ? 0.24288 0.27203 0.19275 0.01457  0.00767  -0.02827 208 LYS A C   
1678 O O   . LYS A 201 ? 0.31153 0.33894 0.25971 0.01655  0.00783  -0.03496 208 LYS A O   
1679 C CB  . LYS A 201 ? 0.25985 0.29997 0.21683 0.01468  0.01464  -0.01890 208 LYS A CB  
1680 C CG  . LYS A 201 ? 0.29850 0.34428 0.25043 0.01834  0.01791  -0.02429 208 LYS A CG  
1681 C CD  . LYS A 201 ? 0.38844 0.44492 0.33788 0.01927  0.02291  -0.01944 208 LYS A CD  
1682 C CE  . LYS A 201 ? 0.43622 0.49933 0.38069 0.02342  0.02681  -0.02520 208 LYS A CE  
1683 N NZ  . LYS A 201 ? 0.57657 0.65106 0.52090 0.02418  0.03259  -0.01934 208 LYS A NZ  
1684 N N   . LYS A 202 ? 0.26689 0.29680 0.21215 0.01320  0.00540  -0.02565 209 LYS A N   
1685 C CA  . LYS A 202 ? 0.27628 0.30640 0.21410 0.01370  0.00274  -0.03081 209 LYS A CA  
1686 C C   . LYS A 202 ? 0.28248 0.30404 0.22353 0.01245  -0.00081 -0.03595 209 LYS A C   
1687 O O   . LYS A 202 ? 0.29345 0.31345 0.23138 0.01323  -0.00187 -0.04297 209 LYS A O   
1688 C CB  . LYS A 202 ? 0.28378 0.31791 0.21700 0.01280  0.00096  -0.02573 209 LYS A CB  
1689 C CG  . LYS A 202 ? 0.32625 0.36216 0.25229 0.01302  -0.00258 -0.03084 209 LYS A CG  
1690 C CD  . LYS A 202 ? 0.39488 0.43638 0.31662 0.01289  -0.00411 -0.02457 209 LYS A CD  
1691 C CE  . LYS A 202 ? 0.48971 0.53486 0.40455 0.01307  -0.00824 -0.02944 209 LYS A CE  
1692 N NZ  . LYS A 202 ? 0.52139 0.57313 0.43192 0.01363  -0.00997 -0.02254 209 LYS A NZ  
1693 N N   . HIS A 203 ? 0.27137 0.28729 0.21886 0.01044  -0.00255 -0.03262 210 HIS A N   
1694 C CA  . HIS A 203 ? 0.29957 0.30870 0.24944 0.00887  -0.00589 -0.03578 210 HIS A CA  
1695 C C   . HIS A 203 ? 0.31084 0.31329 0.26731 0.00876  -0.00569 -0.03668 210 HIS A C   
1696 O O   . HIS A 203 ? 0.30389 0.30076 0.26212 0.00768  -0.00782 -0.03947 210 HIS A O   
1697 C CB  . HIS A 203 ? 0.29144 0.30003 0.24239 0.00690  -0.00853 -0.03145 210 HIS A CB  
1698 C CG  . HIS A 203 ? 0.31103 0.32568 0.25590 0.00706  -0.00998 -0.03050 210 HIS A CG  
1699 N ND1 . HIS A 203 ? 0.35202 0.36866 0.29218 0.00702  -0.01219 -0.03606 210 HIS A ND1 
1700 C CD2 . HIS A 203 ? 0.35449 0.37404 0.29725 0.00744  -0.00963 -0.02446 210 HIS A CD2 
1701 C CE1 . HIS A 203 ? 0.35778 0.38119 0.29270 0.00750  -0.01350 -0.03349 210 HIS A CE1 
1702 N NE2 . HIS A 203 ? 0.34455 0.36965 0.28084 0.00797  -0.01179 -0.02602 210 HIS A NE2 
1703 N N   . SER A 204 ? 0.28015 0.28355 0.24067 0.00970  -0.00336 -0.03398 211 SER A N   
1704 C CA  . SER A 204 ? 0.26850 0.26688 0.23519 0.00978  -0.00369 -0.03374 211 SER A CA  
1705 C C   . SER A 204 ? 0.28211 0.28217 0.25141 0.01246  -0.00100 -0.03547 211 SER A C   
1706 O O   . SER A 204 ? 0.28727 0.28634 0.26219 0.01295  -0.00083 -0.03366 211 SER A O   
1707 C CB  . SER A 204 ? 0.26545 0.26346 0.23616 0.00800  -0.00459 -0.02857 211 SER A CB  
1708 O OG  . SER A 204 ? 0.28803 0.28458 0.25674 0.00619  -0.00685 -0.02727 211 SER A OG  
1709 N N   . GLN A 205 ? 0.29415 0.29713 0.25949 0.01454  0.00095  -0.03946 212 GLN A N   
1710 C CA  . GLN A 205 ? 0.31033 0.31661 0.27848 0.01760  0.00414  -0.04076 212 GLN A CA  
1711 C C   . GLN A 205 ? 0.32317 0.32291 0.29615 0.01949  0.00349  -0.04365 212 GLN A C   
1712 O O   . GLN A 205 ? 0.43680 0.43904 0.41443 0.02222  0.00562  -0.04355 212 GLN A O   
1713 C CB  . GLN A 205 ? 0.40761 0.41958 0.36950 0.01980  0.00685  -0.04458 212 GLN A CB  
1714 C CG  . GLN A 205 ? 0.49022 0.49776 0.44689 0.02003  0.00503  -0.05122 212 GLN A CG  
1715 C CD  . GLN A 205 ? 0.55055 0.56006 0.50050 0.01750  0.00254  -0.05089 212 GLN A CD  
1716 O OE1 . GLN A 205 ? 0.43197 0.43761 0.38334 0.01461  -0.00066 -0.04842 212 GLN A OE1 
1717 N NE2 . GLN A 205 ? 0.61392 0.63018 0.55628 0.01901  0.00399  -0.05378 212 GLN A NE2 
1718 N N   . PHE A 206 ? 0.30459 0.29647 0.27736 0.01815  0.00069  -0.04550 213 PHE A N   
1719 C CA  . PHE A 206 ? 0.36774 0.35264 0.34488 0.02007  0.00027  -0.04764 213 PHE A CA  
1720 C C   . PHE A 206 ? 0.41104 0.39154 0.39201 0.01828  -0.00221 -0.04325 213 PHE A C   
1721 O O   . PHE A 206 ? 0.46870 0.44196 0.45188 0.01856  -0.00338 -0.04403 213 PHE A O   
1722 C CB  . PHE A 206 ? 0.44035 0.41936 0.41461 0.02011  -0.00041 -0.05388 213 PHE A CB  
1723 C CG  . PHE A 206 ? 0.48761 0.47102 0.45766 0.02268  0.00212  -0.05936 213 PHE A CG  
1724 C CD1 . PHE A 206 ? 0.47688 0.46187 0.44963 0.02699  0.00514  -0.06165 213 PHE A CD1 
1725 C CD2 . PHE A 206 ? 0.47704 0.46396 0.44002 0.02098  0.00139  -0.06223 213 PHE A CD2 
1726 C CE1 . PHE A 206 ? 0.57483 0.56496 0.54290 0.02960  0.00788  -0.06693 213 PHE A CE1 
1727 C CE2 . PHE A 206 ? 0.52486 0.51689 0.48250 0.02349  0.00368  -0.06751 213 PHE A CE2 
1728 C CZ  . PHE A 206 ? 0.55038 0.54400 0.51039 0.02779  0.00715  -0.06994 213 PHE A CZ  
1729 N N   . ILE A 207 ? 0.23964 0.22416 0.22115 0.01631  -0.00299 -0.03866 214 ILE A N   
1730 C CA  . ILE A 207 ? 0.22973 0.21158 0.21431 0.01517  -0.00510 -0.03498 214 ILE A CA  
1731 C C   . ILE A 207 ? 0.31085 0.29451 0.30080 0.01798  -0.00460 -0.03342 214 ILE A C   
1732 O O   . ILE A 207 ? 0.26856 0.25873 0.26093 0.01922  -0.00290 -0.03289 214 ILE A O   
1733 C CB  . ILE A 207 ? 0.23869 0.22386 0.22204 0.01226  -0.00617 -0.03173 214 ILE A CB  
1734 C CG1 . ILE A 207 ? 0.24280 0.22623 0.22154 0.00999  -0.00715 -0.03292 214 ILE A CG1 
1735 C CG2 . ILE A 207 ? 0.23381 0.21761 0.21991 0.01141  -0.00819 -0.02862 214 ILE A CG2 
1736 C CD1 . ILE A 207 ? 0.26326 0.24044 0.24192 0.00874  -0.00896 -0.03369 214 ILE A CD1 
1737 N N   . GLY A 208 ? 0.23935 0.21798 0.23156 0.01907  -0.00603 -0.03228 215 GLY A N   
1738 C CA  . GLY A 208 ? 0.26316 0.24290 0.26044 0.02259  -0.00592 -0.03097 215 GLY A CA  
1739 C C   . GLY A 208 ? 0.26501 0.24977 0.26511 0.02210  -0.00784 -0.02717 215 GLY A C   
1740 O O   . GLY A 208 ? 0.27542 0.26005 0.27873 0.02450  -0.00917 -0.02506 215 GLY A O   
1741 N N   . TYR A 209 ? 0.22410 0.21349 0.22328 0.01915  -0.00814 -0.02635 216 TYR A N   
1742 C CA  . TYR A 209 ? 0.25646 0.25080 0.25871 0.01808  -0.01013 -0.02391 216 TYR A CA  
1743 C C   . TYR A 209 ? 0.22584 0.22671 0.23041 0.01629  -0.00861 -0.02383 216 TYR A C   
1744 O O   . TYR A 209 ? 0.24067 0.24109 0.24198 0.01501  -0.00667 -0.02475 216 TYR A O   
1745 C CB  . TYR A 209 ? 0.23654 0.22765 0.23531 0.01548  -0.01253 -0.02266 216 TYR A CB  
1746 C CG  . TYR A 209 ? 0.23124 0.21662 0.22789 0.01695  -0.01355 -0.02171 216 TYR A CG  
1747 C CD1 . TYR A 209 ? 0.24351 0.23029 0.24223 0.01933  -0.01540 -0.01950 216 TYR A CD1 
1748 C CD2 . TYR A 209 ? 0.25349 0.23258 0.24657 0.01597  -0.01269 -0.02264 216 TYR A CD2 
1749 C CE1 . TYR A 209 ? 0.24131 0.22286 0.23823 0.02084  -0.01591 -0.01751 216 TYR A CE1 
1750 C CE2 . TYR A 209 ? 0.24169 0.21523 0.23395 0.01699  -0.01316 -0.02109 216 TYR A CE2 
1751 C CZ  . TYR A 209 ? 0.23552 0.21017 0.22951 0.01947  -0.01458 -0.01813 216 TYR A CZ  
1752 O OH  . TYR A 209 ? 0.26436 0.23379 0.25774 0.02071  -0.01475 -0.01543 216 TYR A OH  
1753 N N   . PRO A 210 ? 0.23031 0.23759 0.24063 0.01594  -0.00957 -0.02246 217 PRO A N   
1754 C CA  . PRO A 210 ? 0.20324 0.21651 0.21699 0.01354  -0.00790 -0.02161 217 PRO A CA  
1755 C C   . PRO A 210 ? 0.23449 0.24475 0.24500 0.00973  -0.00860 -0.02081 217 PRO A C   
1756 O O   . PRO A 210 ? 0.25447 0.26145 0.26361 0.00838  -0.01141 -0.02082 217 PRO A O   
1757 C CB  . PRO A 210 ? 0.26232 0.28274 0.28415 0.01359  -0.00964 -0.02062 217 PRO A CB  
1758 C CG  . PRO A 210 ? 0.30079 0.31885 0.32179 0.01551  -0.01308 -0.02071 217 PRO A CG  
1759 C CD  . PRO A 210 ? 0.22379 0.23381 0.23830 0.01778  -0.01230 -0.02144 217 PRO A CD  
1760 N N   . ILE A 211 ? 0.21388 0.22558 0.22298 0.00845  -0.00588 -0.01998 218 ILE A N   
1761 C CA  . ILE A 211 ? 0.18841 0.19758 0.19520 0.00536  -0.00617 -0.01846 218 ILE A CA  
1762 C C   . ILE A 211 ? 0.20179 0.21667 0.21495 0.00305  -0.00457 -0.01583 218 ILE A C   
1763 O O   . ILE A 211 ? 0.21789 0.23810 0.23225 0.00375  -0.00115 -0.01455 218 ILE A O   
1764 C CB  . ILE A 211 ? 0.20114 0.20747 0.20080 0.00580  -0.00462 -0.01881 218 ILE A CB  
1765 C CG1 . ILE A 211 ? 0.20304 0.20380 0.19796 0.00757  -0.00606 -0.02157 218 ILE A CG1 
1766 C CG2 . ILE A 211 ? 0.18666 0.19122 0.18489 0.00313  -0.00493 -0.01634 218 ILE A CG2 
1767 C CD1 . ILE A 211 ? 0.21594 0.21540 0.20459 0.00815  -0.00464 -0.02309 218 ILE A CD1 
1768 N N   . THR A 212 ? 0.18575 0.19985 0.20342 0.00030  -0.00685 -0.01520 219 THR A N   
1769 C CA  . THR A 212 ? 0.17256 0.19153 0.19833 -0.00265 -0.00570 -0.01275 219 THR A CA  
1770 C C   . THR A 212 ? 0.18379 0.19824 0.20844 -0.00533 -0.00532 -0.01032 219 THR A C   
1771 O O   . THR A 212 ? 0.19151 0.19994 0.21416 -0.00614 -0.00802 -0.01172 219 THR A O   
1772 C CB  . THR A 212 ? 0.17306 0.19483 0.20633 -0.00402 -0.00890 -0.01440 219 THR A CB  
1773 O OG1 . THR A 212 ? 0.18978 0.21590 0.22397 -0.00075 -0.00945 -0.01602 219 THR A OG1 
1774 C CG2 . THR A 212 ? 0.20044 0.22731 0.24370 -0.00783 -0.00767 -0.01198 219 THR A CG2 
1775 N N   . LEU A 213 ? 0.18491 0.20243 0.21036 -0.00619 -0.00172 -0.00646 220 LEU A N   
1776 C CA  . LEU A 213 ? 0.19101 0.20491 0.21677 -0.00856 -0.00095 -0.00273 220 LEU A CA  
1777 C C   . LEU A 213 ? 0.18443 0.19969 0.22118 -0.01256 -0.00112 -0.00087 220 LEU A C   
1778 O O   . LEU A 213 ? 0.17916 0.20156 0.22241 -0.01387 0.00169  0.00176  220 LEU A O   
1779 C CB  . LEU A 213 ? 0.19765 0.21487 0.21829 -0.00732 0.00301  0.00122  220 LEU A CB  
1780 C CG  . LEU A 213 ? 0.23317 0.24757 0.25425 -0.00925 0.00422  0.00662  220 LEU A CG  
1781 C CD1 . LEU A 213 ? 0.21373 0.21930 0.23233 -0.00939 0.00075  0.00530  220 LEU A CD1 
1782 C CD2 . LEU A 213 ? 0.23856 0.25766 0.25198 -0.00706 0.00769  0.00997  220 LEU A CD2 
1783 N N   . PHE A 214 ? 0.18472 0.19351 0.22410 -0.01455 -0.00432 -0.00263 221 PHE A N   
1784 C CA  . PHE A 214 ? 0.18629 0.19506 0.23673 -0.01886 -0.00493 -0.00169 221 PHE A CA  
1785 C C   . PHE A 214 ? 0.20638 0.21425 0.26013 -0.02102 -0.00126 0.00502  221 PHE A C   
1786 O O   . PHE A 214 ? 0.20948 0.21397 0.25615 -0.01917 0.00021  0.00813  221 PHE A O   
1787 C CB  . PHE A 214 ? 0.16930 0.17055 0.22082 -0.02003 -0.00925 -0.00614 221 PHE A CB  
1788 C CG  . PHE A 214 ? 0.16555 0.16881 0.21589 -0.01879 -0.01311 -0.01215 221 PHE A CG  
1789 C CD1 . PHE A 214 ? 0.17743 0.18484 0.22155 -0.01518 -0.01309 -0.01346 221 PHE A CD1 
1790 C CD2 . PHE A 214 ? 0.19295 0.19316 0.24778 -0.02096 -0.01696 -0.01661 221 PHE A CD2 
1791 C CE1 . PHE A 214 ? 0.19384 0.20284 0.23648 -0.01366 -0.01665 -0.01790 221 PHE A CE1 
1792 C CE2 . PHE A 214 ? 0.17823 0.18103 0.23083 -0.01950 -0.02076 -0.02180 221 PHE A CE2 
1793 C CZ  . PHE A 214 ? 0.16129 0.16863 0.20773 -0.01575 -0.02058 -0.02190 221 PHE A CZ  
1794 N N   . VAL A 215 ? 0.21592 0.22730 0.28094 -0.02503 0.00018  0.00771  222 VAL A N   
1795 C CA  . VAL A 215 ? 0.26251 0.27209 0.33227 -0.02769 0.00366  0.01496  222 VAL A CA  
1796 C C   . VAL A 215 ? 0.26021 0.26099 0.33860 -0.03158 0.00107  0.01403  222 VAL A C   
1797 O O   . VAL A 215 ? 0.25230 0.25025 0.33378 -0.03265 -0.00325 0.00733  222 VAL A O   
1798 C CB  . VAL A 215 ? 0.38405 0.40370 0.46072 -0.02963 0.00834  0.02021  222 VAL A CB  
1799 C CG1 . VAL A 215 ? 0.41929 0.44595 0.48536 -0.02508 0.01198  0.02223  222 VAL A CG1 
1800 C CG2 . VAL A 215 ? 0.23228 0.25804 0.31862 -0.03194 0.00648  0.01606  222 VAL A CG2 
1801 N N   . GLU A 216 ? 0.26921 0.26530 0.35083 -0.03329 0.00370  0.02073  223 GLU A N   
1802 C CA  . GLU A 216 ? 0.26670 0.25286 0.35704 -0.03672 0.00173  0.02028  223 GLU A CA  
1803 C C   . GLU A 216 ? 0.34140 0.32944 0.44631 -0.04250 0.00442  0.02553  223 GLU A C   
1804 O O   . GLU A 216 ? 0.34892 0.34443 0.45520 -0.04312 0.00922  0.03283  223 GLU A O   
1805 C CB  . GLU A 216 ? 0.33818 0.31525 0.42236 -0.03401 0.00210  0.02388  223 GLU A CB  
1806 C CG  . GLU A 216 ? 0.33925 0.31560 0.41003 -0.02869 -0.00019 0.01929  223 GLU A CG  
1807 C CD  . GLU A 216 ? 0.40001 0.36893 0.46572 -0.02584 0.00008  0.02316  223 GLU A CD  
1808 O OE1 . GLU A 216 ? 0.35935 0.31878 0.43101 -0.02694 -0.00162 0.02196  223 GLU A OE1 
1809 O OE2 . GLU A 216 ? 0.36655 0.33949 0.42272 -0.02236 0.00179  0.02694  223 GLU A OE2 
1810 N N   . LYS A 217 ? 0.33754 0.31899 0.45349 -0.04681 0.00133  0.02140  224 LYS A N   
1811 C CA  . LYS A 217 ? 0.45258 0.43284 0.58438 -0.05317 0.00337  0.02612  224 LYS A CA  
1812 C C   . LYS A 217 ? 0.56691 0.54583 0.69939 -0.05337 0.00917  0.03818  224 LYS A C   
1813 O O   . LYS A 217 ? 0.53865 0.50889 0.66501 -0.05042 0.00950  0.04150  224 LYS A O   
1814 C CB  . LYS A 217 ? 0.47540 0.44380 0.61620 -0.05660 -0.00090 0.02010  224 LYS A CB  
1815 C CG  . LYS A 217 ? 0.68131 0.64741 0.84030 -0.06397 0.00061  0.02387  224 LYS A CG  
1816 C CD  . LYS A 217 ? 0.68992 0.64587 0.85851 -0.06777 -0.00466 0.01484  224 LYS A CD  
1817 C CE  . LYS A 217 ? 0.72439 0.67389 0.91113 -0.07493 -0.00251 0.02021  224 LYS A CE  
1818 N NZ  . LYS A 217 ? 0.70367 0.63596 0.89414 -0.07520 -0.00420 0.01832  224 LYS A NZ  
# 
