data_7HBA
# 
_entry.id   7HBA 
# 
_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   7HBA         pdb_00007hba 10.2210/pdb7hba/pdb 
WWPDB D_1001407257 ?            ?                   
# 
_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                        7HBA 
_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 '4-(4,5-dichloro-1H-imidazol-1-yl)aniline' 228.078   2   ?        ? ? ? 
3 water       nat water                                      18.015    108 ?        ? ? ? 
# 
_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 '4-(4,5-dichloro-1H-imidazol-1-yl)aniline' A1AYO 
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 
A1AYO non-polymer         . '4-(4,5-dichloro-1H-imidazol-1-yl)aniline' ? 'C9 H7 Cl2 N3'   228.078 
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        A1AYO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AYO 
_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 A1AYO 1   301 301 A1AYO BF1 A . 
C 2 A1AYO 1   302 302 A1AYO BF1 A . 
D 3 HOH   1   401 44  HOH   HOH A . 
D 3 HOH   2   402 60  HOH   HOH A . 
D 3 HOH   3   403 50  HOH   HOH A . 
D 3 HOH   4   404 14  HOH   HOH A . 
D 3 HOH   5   405 45  HOH   HOH A . 
D 3 HOH   6   406 97  HOH   HOH A . 
D 3 HOH   7   407 88  HOH   HOH A . 
D 3 HOH   8   408 108 HOH   HOH A . 
D 3 HOH   9   409 22  HOH   HOH A . 
D 3 HOH   10  410 30  HOH   HOH A . 
D 3 HOH   11  411 23  HOH   HOH A . 
D 3 HOH   12  412 24  HOH   HOH A . 
D 3 HOH   13  413 2   HOH   HOH A . 
D 3 HOH   14  414 16  HOH   HOH A . 
D 3 HOH   15  415 105 HOH   HOH A . 
D 3 HOH   16  416 39  HOH   HOH A . 
D 3 HOH   17  417 91  HOH   HOH A . 
D 3 HOH   18  418 7   HOH   HOH A . 
D 3 HOH   19  419 75  HOH   HOH A . 
D 3 HOH   20  420 4   HOH   HOH A . 
D 3 HOH   21  421 20  HOH   HOH A . 
D 3 HOH   22  422 5   HOH   HOH A . 
D 3 HOH   23  423 3   HOH   HOH A . 
D 3 HOH   24  424 6   HOH   HOH A . 
D 3 HOH   25  425 11  HOH   HOH A . 
D 3 HOH   26  426 33  HOH   HOH A . 
D 3 HOH   27  427 93  HOH   HOH A . 
D 3 HOH   28  428 61  HOH   HOH A . 
D 3 HOH   29  429 17  HOH   HOH A . 
D 3 HOH   30  430 13  HOH   HOH A . 
D 3 HOH   31  431 77  HOH   HOH A . 
D 3 HOH   32  432 35  HOH   HOH A . 
D 3 HOH   33  433 9   HOH   HOH A . 
D 3 HOH   34  434 27  HOH   HOH A . 
D 3 HOH   35  435 34  HOH   HOH A . 
D 3 HOH   36  436 15  HOH   HOH A . 
D 3 HOH   37  437 21  HOH   HOH A . 
D 3 HOH   38  438 31  HOH   HOH A . 
D 3 HOH   39  439 36  HOH   HOH A . 
D 3 HOH   40  440 38  HOH   HOH A . 
D 3 HOH   41  441 18  HOH   HOH A . 
D 3 HOH   42  442 79  HOH   HOH A . 
D 3 HOH   43  443 107 HOH   HOH A . 
D 3 HOH   44  444 56  HOH   HOH A . 
D 3 HOH   45  445 86  HOH   HOH A . 
D 3 HOH   46  446 10  HOH   HOH A . 
D 3 HOH   47  447 78  HOH   HOH A . 
D 3 HOH   48  448 47  HOH   HOH A . 
D 3 HOH   49  449 43  HOH   HOH A . 
D 3 HOH   50  450 66  HOH   HOH A . 
D 3 HOH   51  451 103 HOH   HOH A . 
D 3 HOH   52  452 19  HOH   HOH A . 
D 3 HOH   53  453 54  HOH   HOH A . 
D 3 HOH   54  454 8   HOH   HOH A . 
D 3 HOH   55  455 87  HOH   HOH A . 
D 3 HOH   56  456 55  HOH   HOH A . 
D 3 HOH   57  457 48  HOH   HOH A . 
D 3 HOH   58  458 58  HOH   HOH A . 
D 3 HOH   59  459 25  HOH   HOH A . 
D 3 HOH   60  460 64  HOH   HOH A . 
D 3 HOH   61  461 68  HOH   HOH A . 
D 3 HOH   62  462 52  HOH   HOH A . 
D 3 HOH   63  463 81  HOH   HOH A . 
D 3 HOH   64  464 94  HOH   HOH A . 
D 3 HOH   65  465 12  HOH   HOH A . 
D 3 HOH   66  466 42  HOH   HOH A . 
D 3 HOH   67  467 62  HOH   HOH A . 
D 3 HOH   68  468 102 HOH   HOH A . 
D 3 HOH   69  469 26  HOH   HOH A . 
D 3 HOH   70  470 29  HOH   HOH A . 
D 3 HOH   71  471 106 HOH   HOH A . 
D 3 HOH   72  472 28  HOH   HOH A . 
D 3 HOH   73  473 59  HOH   HOH A . 
D 3 HOH   74  474 46  HOH   HOH A . 
D 3 HOH   75  475 90  HOH   HOH A . 
D 3 HOH   76  476 89  HOH   HOH A . 
D 3 HOH   77  477 57  HOH   HOH A . 
D 3 HOH   78  478 53  HOH   HOH A . 
D 3 HOH   79  479 1   HOH   HOH A . 
D 3 HOH   80  480 32  HOH   HOH A . 
D 3 HOH   81  481 37  HOH   HOH A . 
D 3 HOH   82  482 82  HOH   HOH A . 
D 3 HOH   83  483 96  HOH   HOH A . 
D 3 HOH   84  484 100 HOH   HOH A . 
D 3 HOH   85  485 99  HOH   HOH A . 
D 3 HOH   86  486 83  HOH   HOH A . 
D 3 HOH   87  487 84  HOH   HOH A . 
D 3 HOH   88  488 98  HOH   HOH A . 
D 3 HOH   89  489 49  HOH   HOH A . 
D 3 HOH   90  490 41  HOH   HOH A . 
D 3 HOH   91  491 65  HOH   HOH A . 
D 3 HOH   92  492 70  HOH   HOH A . 
D 3 HOH   93  493 80  HOH   HOH A . 
D 3 HOH   94  494 85  HOH   HOH A . 
D 3 HOH   95  495 69  HOH   HOH A . 
D 3 HOH   96  496 104 HOH   HOH A . 
D 3 HOH   97  497 72  HOH   HOH A . 
D 3 HOH   98  498 73  HOH   HOH A . 
D 3 HOH   99  499 92  HOH   HOH A . 
D 3 HOH   100 500 74  HOH   HOH A . 
D 3 HOH   101 501 71  HOH   HOH A . 
D 3 HOH   102 502 67  HOH   HOH A . 
D 3 HOH   103 503 76  HOH   HOH A . 
D 3 HOH   104 504 101 HOH   HOH A . 
D 3 HOH   105 505 51  HOH   HOH A . 
D 3 HOH   106 506 40  HOH   HOH A . 
D 3 HOH   107 507 95  HOH   HOH A . 
D 3 HOH   108 508 63  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             606610.158 
_cell.length_a           70.000 
_cell.length_b           89.210 
_cell.length_c           97.140 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HBA 
_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                         7HBA 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HBA 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2024-01-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HBA 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             30.890 
_reflns.d_resolution_high            2.150 
_reflns.number_obs                   16893 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.900 
_reflns.pdbx_Rmerge_I_obs            0.106 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.700 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.900 
_reflns.pdbx_Rrim_I_all              0.111 
_reflns.pdbx_Rpim_I_all              0.031 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     217117 
_reflns.pdbx_scaling_rejects         12 
_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 2.150 2.210  ? 16290 1226 ? 1.510 ? ? ? 13.300 ? 1.900  ? ? ? ? ? ? 100.000 1.570 0.427 0.720 
1 2 9.620 30.890 ? 1747  207  ? 0.043 ? ? ? 8.400  ? 40.600 ? ? ? ? ? ? 93.900  0.045 0.015 0.997 
# 
_refine.entry_id                                 7HBA 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.ls_percent_reflns_R_free                 4.81 
_refine.pdbx_overall_phase_error                 25.0969 
_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                          0.2009 
_refine.B_iso_mean                               51.64 
_refine.ls_number_reflns_R_free                  812 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_R_factor_R_work                       0.2003 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            2.15 
_refine.ls_number_reflns_obs                     16887 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.ls_number_reflns_R_work                  16075 
_refine.ls_d_res_low                             30.44 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2134 
_refine.overall_SU_ML                            0.2486 
_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         28 
_refine_hist.number_atoms_solvent             108 
_refine_hist.number_atoms_total               1780 
_refine_hist.d_res_high                       2.15 
_refine_hist.d_res_low                        30.44 
# 
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           1700 0.0017 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2293 0.4685 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0380 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      291  0.0038 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 224  6.7080 ? ? ? 
# 
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' 2.15 2.28  2616 0.2801 100.00 0.3241 146 . . . . . 
'X-RAY DIFFRACTION' 2.28 2.46  2636 0.2647 100.00 0.2876 133 . . . . . 
'X-RAY DIFFRACTION' 2.46 2.71  2664 0.2449 100.00 0.2557 132 . . . . . 
'X-RAY DIFFRACTION' 2.71 3.10  2666 0.2283 100.00 0.2446 132 . . . . . 
'X-RAY DIFFRACTION' 3.10 3.90  2710 0.1971 100.00 0.2200 124 . . . . . 
'X-RAY DIFFRACTION' 3.91 30.44 2783 0.1643 99.46  0.1680 145 . . . . . 
# 
_struct.entry_id                  7HBA 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13425' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HBA 
_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 2 ? 
D 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              7HBA 
_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 7HBA MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HBA LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HBA GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HBA HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HBA HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HBA HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HBA HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HBA HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HBA 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,D 
# 
_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 98  ? ALA A 117 ? ASN A 105 ALA A 124 1 ? 20 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N ILE A 144 ? N ILE A 151 O LYS A 178 ? O LYS A 185 
AA1 5 6 O VAL A 179 ? O VAL A 186 N ILE A 84  ? N ILE A 91  
AA1 6 7 O VAL A 85  ? O VAL A 92  N ASN A 72  ? N ASN A 79  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HBA 
_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 459 ? ? O A HOH 490 ? ? 1.99 
2 1 O A HOH 485 ? ? O A HOH 491 ? ? 2.05 
3 1 O A VAL 222 ? ? O A HOH 401 ? ? 2.14 
4 1 O A HOH 475 ? ? O A HOH 488 ? ? 2.15 
5 1 O A HOH 501 ? ? O A HOH 502 ? ? 2.17 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ALA 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     166 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             59.21 
_pdbx_validate_torsion.psi             -146.08 
# 
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 14.2523347191  27.3862350606 31.1379621443 0.420011442286 0.427924431351 0.503832083916 
0.0625250587882  -0.0310463480195 -0.0476359971857  3.40733130919 2.45672385438 5.09339360159 -0.994924667138 -1.36540186157  
-0.00463201376069 0.0570468672898  -0.14190360437  -0.169363631321 0.112559587796  0.131038369548    -0.139098312466  
-0.236971745108 0.0748686883031   -0.170208086446  
2 ? 'X-RAY DIFFRACTION' refined -6.0997590717  37.6079737461 22.8414132897 0.377102178205 0.386578105207 0.388136128168 
0.00439305971913 -0.043242569541  -0.00816806537432 2.93146723911 4.24821145239 7.03352505062 -1.72573375864  1.58254008353   
-2.77877121008    -0.123648663312  0.227722582237  0.154888347793  -0.144969977523 -0.062012071803   0.139787315102   
-0.290490174202 -0.00529867385127 0.173179511906   
3 ? 'X-RAY DIFFRACTION' refined -2.29094594742 25.997327965  24.8554574947 0.447263456256 0.376871287943 0.454893540122 
-0.0079195438243 -0.0727173089683 -0.0143868373759  3.28812068865 3.48722949506 3.65107502549 -0.454927026402 -1.06125374925  
-1.19874947485    -0.116169538593  -0.194796822458 -0.282929030694 -0.130776284459 0.022343176963    -0.0663498366505 
0.426301500584  -0.0841415132311  0.0865488428526  
4 ? 'X-RAY DIFFRACTION' refined 12.8741420936  39.2351566483 33.6048539017 0.479045826565 0.494473907475 0.552036188255 
0.0160177069295  -0.0613303636577 -0.0879603053458  6.12134864833 4.0548796019  7.09626286384 0.266013971116  0.0785596065997 
-1.01907450849    -0.0243045222845 -0.707786145646 0.419127124383  0.391286973057  -0.0429723649974  -0.410348362447  
-0.472768504347 0.612283876896    0.136332185747   
5 ? 'X-RAY DIFFRACTION' refined 3.83272504686  24.98578306   20.9970602199 0.43674922244  0.403375002528 0.483366870269 
0.00572342556216 -0.0223275861255 -0.0439718444567  3.3387763268  2.59687828182 3.45340436353 -1.2117931264   0.35555315247   
-0.824941159204   0.0869380013128  0.163614122519  -0.470850678768 -0.34658205944  0.00914755619834  0.138074352509   
0.402418588985  0.0732346014719   -0.166620621905  
6 ? 'X-RAY DIFFRACTION' refined -4.18662008046 24.395634119  37.9540368228 0.533698871335 0.570878367391 0.454713669688 
0.0180884037243  -0.0272006046722 0.0880020771428   3.94012110191 2.88636577746 3.3501662279  -1.03545962874  -0.809166478454 
0.395708738902    -0.336319353746  -0.814693267005 -0.398628992421 0.475154584882  0.222286686893    0.175013407895   
0.410737808108  -0.19576567481    0.00350298019512 
7 ? 'X-RAY DIFFRACTION' refined -12.5909426821 30.4545410637 32.5881883679 0.494863871759 0.590971940721 0.407378509632 
0.0418893158585  -0.0293025700486 0.091644661925    4.20832702667 4.22634440113 3.37853324961 -0.364222443706 -0.458199070212 
-0.165169280817   0.0582617176321  -0.120470315645 -0.427782233509 0.343021654755  -0.00801176935261 0.0297270423162  
0.172871615101  -0.0998656004192  -0.0250666453764 
# 
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 76  A 61  . 
;chain 'A' and (resid 41 through 76 )
;
3 3 'X-RAY DIFFRACTION' A 77  A 62  A 105 A 90  . 
;chain 'A' and (resid 77 through 105 )
;
4 4 'X-RAY DIFFRACTION' A 106 A 91  A 136 A 121 . 
;chain 'A' and (resid 106 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
6 6 'X-RAY DIFFRACTION' A 183 A 168 A 210 A 195 . 
;chain 'A' and (resid 183 through 210 )
;
7 7 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AYO C2   C  Y N 1   
A1AYO C3   C  Y N 2   
A1AYO C5   C  Y N 3   
A1AYO N1   N  N N 4   
A1AYO C6   C  Y N 5   
A1AYO C4   C  Y N 6   
A1AYO C1   C  Y N 7   
A1AYO C7   C  Y N 8   
A1AYO C8   C  Y N 9   
A1AYO C9   C  Y N 10  
A1AYO N2   N  Y N 11  
A1AYO N3   N  Y N 12  
A1AYO CL1  CL N N 13  
A1AYO CL2  CL N N 14  
A1AYO H3   H  N N 15  
A1AYO H4   H  N N 16  
A1AYO H5   H  N N 17  
A1AYO H2   H  N N 18  
A1AYO H1   H  N N 19  
A1AYO H6   H  N N 20  
A1AYO H7   H  N N 21  
ALA   N    N  N N 22  
ALA   CA   C  N S 23  
ALA   C    C  N N 24  
ALA   O    O  N N 25  
ALA   CB   C  N N 26  
ALA   OXT  O  N N 27  
ALA   H    H  N N 28  
ALA   H2   H  N N 29  
ALA   HA   H  N N 30  
ALA   HB1  H  N N 31  
ALA   HB2  H  N N 32  
ALA   HB3  H  N N 33  
ALA   HXT  H  N N 34  
ARG   N    N  N N 35  
ARG   CA   C  N S 36  
ARG   C    C  N N 37  
ARG   O    O  N N 38  
ARG   CB   C  N N 39  
ARG   CG   C  N N 40  
ARG   CD   C  N N 41  
ARG   NE   N  N N 42  
ARG   CZ   C  N N 43  
ARG   NH1  N  N N 44  
ARG   NH2  N  N N 45  
ARG   OXT  O  N N 46  
ARG   H    H  N N 47  
ARG   H2   H  N N 48  
ARG   HA   H  N N 49  
ARG   HB2  H  N N 50  
ARG   HB3  H  N N 51  
ARG   HG2  H  N N 52  
ARG   HG3  H  N N 53  
ARG   HD2  H  N N 54  
ARG   HD3  H  N N 55  
ARG   HE   H  N N 56  
ARG   HH11 H  N N 57  
ARG   HH12 H  N N 58  
ARG   HH21 H  N N 59  
ARG   HH22 H  N N 60  
ARG   HXT  H  N N 61  
ASN   N    N  N N 62  
ASN   CA   C  N S 63  
ASN   C    C  N N 64  
ASN   O    O  N N 65  
ASN   CB   C  N N 66  
ASN   CG   C  N N 67  
ASN   OD1  O  N N 68  
ASN   ND2  N  N N 69  
ASN   OXT  O  N N 70  
ASN   H    H  N N 71  
ASN   H2   H  N N 72  
ASN   HA   H  N N 73  
ASN   HB2  H  N N 74  
ASN   HB3  H  N N 75  
ASN   HD21 H  N N 76  
ASN   HD22 H  N N 77  
ASN   HXT  H  N N 78  
ASP   N    N  N N 79  
ASP   CA   C  N S 80  
ASP   C    C  N N 81  
ASP   O    O  N N 82  
ASP   CB   C  N N 83  
ASP   CG   C  N N 84  
ASP   OD1  O  N N 85  
ASP   OD2  O  N N 86  
ASP   OXT  O  N N 87  
ASP   H    H  N N 88  
ASP   H2   H  N N 89  
ASP   HA   H  N N 90  
ASP   HB2  H  N N 91  
ASP   HB3  H  N N 92  
ASP   HD2  H  N N 93  
ASP   HXT  H  N N 94  
GLN   N    N  N N 95  
GLN   CA   C  N S 96  
GLN   C    C  N N 97  
GLN   O    O  N N 98  
GLN   CB   C  N N 99  
GLN   CG   C  N N 100 
GLN   CD   C  N N 101 
GLN   OE1  O  N N 102 
GLN   NE2  N  N N 103 
GLN   OXT  O  N N 104 
GLN   H    H  N N 105 
GLN   H2   H  N N 106 
GLN   HA   H  N N 107 
GLN   HB2  H  N N 108 
GLN   HB3  H  N N 109 
GLN   HG2  H  N N 110 
GLN   HG3  H  N N 111 
GLN   HE21 H  N N 112 
GLN   HE22 H  N N 113 
GLN   HXT  H  N N 114 
GLU   N    N  N N 115 
GLU   CA   C  N S 116 
GLU   C    C  N N 117 
GLU   O    O  N N 118 
GLU   CB   C  N N 119 
GLU   CG   C  N N 120 
GLU   CD   C  N N 121 
GLU   OE1  O  N N 122 
GLU   OE2  O  N N 123 
GLU   OXT  O  N N 124 
GLU   H    H  N N 125 
GLU   H2   H  N N 126 
GLU   HA   H  N N 127 
GLU   HB2  H  N N 128 
GLU   HB3  H  N N 129 
GLU   HG2  H  N N 130 
GLU   HG3  H  N N 131 
GLU   HE2  H  N N 132 
GLU   HXT  H  N N 133 
GLY   N    N  N N 134 
GLY   CA   C  N N 135 
GLY   C    C  N N 136 
GLY   O    O  N N 137 
GLY   OXT  O  N N 138 
GLY   H    H  N N 139 
GLY   H2   H  N N 140 
GLY   HA2  H  N N 141 
GLY   HA3  H  N N 142 
GLY   HXT  H  N N 143 
HIS   N    N  N N 144 
HIS   CA   C  N S 145 
HIS   C    C  N N 146 
HIS   O    O  N N 147 
HIS   CB   C  N N 148 
HIS   CG   C  Y N 149 
HIS   ND1  N  Y N 150 
HIS   CD2  C  Y N 151 
HIS   CE1  C  Y N 152 
HIS   NE2  N  Y N 153 
HIS   OXT  O  N N 154 
HIS   H    H  N N 155 
HIS   H2   H  N N 156 
HIS   HA   H  N N 157 
HIS   HB2  H  N N 158 
HIS   HB3  H  N N 159 
HIS   HD1  H  N N 160 
HIS   HD2  H  N N 161 
HIS   HE1  H  N N 162 
HIS   HE2  H  N N 163 
HIS   HXT  H  N N 164 
HOH   O    O  N N 165 
HOH   H1   H  N N 166 
HOH   H2   H  N N 167 
ILE   N    N  N N 168 
ILE   CA   C  N S 169 
ILE   C    C  N N 170 
ILE   O    O  N N 171 
ILE   CB   C  N S 172 
ILE   CG1  C  N N 173 
ILE   CG2  C  N N 174 
ILE   CD1  C  N N 175 
ILE   OXT  O  N N 176 
ILE   H    H  N N 177 
ILE   H2   H  N N 178 
ILE   HA   H  N N 179 
ILE   HB   H  N N 180 
ILE   HG12 H  N N 181 
ILE   HG13 H  N N 182 
ILE   HG21 H  N N 183 
ILE   HG22 H  N N 184 
ILE   HG23 H  N N 185 
ILE   HD11 H  N N 186 
ILE   HD12 H  N N 187 
ILE   HD13 H  N N 188 
ILE   HXT  H  N N 189 
LEU   N    N  N N 190 
LEU   CA   C  N S 191 
LEU   C    C  N N 192 
LEU   O    O  N N 193 
LEU   CB   C  N N 194 
LEU   CG   C  N N 195 
LEU   CD1  C  N N 196 
LEU   CD2  C  N N 197 
LEU   OXT  O  N N 198 
LEU   H    H  N N 199 
LEU   H2   H  N N 200 
LEU   HA   H  N N 201 
LEU   HB2  H  N N 202 
LEU   HB3  H  N N 203 
LEU   HG   H  N N 204 
LEU   HD11 H  N N 205 
LEU   HD12 H  N N 206 
LEU   HD13 H  N N 207 
LEU   HD21 H  N N 208 
LEU   HD22 H  N N 209 
LEU   HD23 H  N N 210 
LEU   HXT  H  N N 211 
LYS   N    N  N N 212 
LYS   CA   C  N S 213 
LYS   C    C  N N 214 
LYS   O    O  N N 215 
LYS   CB   C  N N 216 
LYS   CG   C  N N 217 
LYS   CD   C  N N 218 
LYS   CE   C  N N 219 
LYS   NZ   N  N N 220 
LYS   OXT  O  N N 221 
LYS   H    H  N N 222 
LYS   H2   H  N N 223 
LYS   HA   H  N N 224 
LYS   HB2  H  N N 225 
LYS   HB3  H  N N 226 
LYS   HG2  H  N N 227 
LYS   HG3  H  N N 228 
LYS   HD2  H  N N 229 
LYS   HD3  H  N N 230 
LYS   HE2  H  N N 231 
LYS   HE3  H  N N 232 
LYS   HZ1  H  N N 233 
LYS   HZ2  H  N N 234 
LYS   HZ3  H  N N 235 
LYS   HXT  H  N N 236 
MET   N    N  N N 237 
MET   CA   C  N S 238 
MET   C    C  N N 239 
MET   O    O  N N 240 
MET   CB   C  N N 241 
MET   CG   C  N N 242 
MET   SD   S  N N 243 
MET   CE   C  N N 244 
MET   OXT  O  N N 245 
MET   H    H  N N 246 
MET   H2   H  N N 247 
MET   HA   H  N N 248 
MET   HB2  H  N N 249 
MET   HB3  H  N N 250 
MET   HG2  H  N N 251 
MET   HG3  H  N N 252 
MET   HE1  H  N N 253 
MET   HE2  H  N N 254 
MET   HE3  H  N N 255 
MET   HXT  H  N N 256 
PHE   N    N  N N 257 
PHE   CA   C  N S 258 
PHE   C    C  N N 259 
PHE   O    O  N N 260 
PHE   CB   C  N N 261 
PHE   CG   C  Y N 262 
PHE   CD1  C  Y N 263 
PHE   CD2  C  Y N 264 
PHE   CE1  C  Y N 265 
PHE   CE2  C  Y N 266 
PHE   CZ   C  Y N 267 
PHE   OXT  O  N N 268 
PHE   H    H  N N 269 
PHE   H2   H  N N 270 
PHE   HA   H  N N 271 
PHE   HB2  H  N N 272 
PHE   HB3  H  N N 273 
PHE   HD1  H  N N 274 
PHE   HD2  H  N N 275 
PHE   HE1  H  N N 276 
PHE   HE2  H  N N 277 
PHE   HZ   H  N N 278 
PHE   HXT  H  N N 279 
PRO   N    N  N N 280 
PRO   CA   C  N S 281 
PRO   C    C  N N 282 
PRO   O    O  N N 283 
PRO   CB   C  N N 284 
PRO   CG   C  N N 285 
PRO   CD   C  N N 286 
PRO   OXT  O  N N 287 
PRO   H    H  N N 288 
PRO   HA   H  N N 289 
PRO   HB2  H  N N 290 
PRO   HB3  H  N N 291 
PRO   HG2  H  N N 292 
PRO   HG3  H  N N 293 
PRO   HD2  H  N N 294 
PRO   HD3  H  N N 295 
PRO   HXT  H  N N 296 
SER   N    N  N N 297 
SER   CA   C  N S 298 
SER   C    C  N N 299 
SER   O    O  N N 300 
SER   CB   C  N N 301 
SER   OG   O  N N 302 
SER   OXT  O  N N 303 
SER   H    H  N N 304 
SER   H2   H  N N 305 
SER   HA   H  N N 306 
SER   HB2  H  N N 307 
SER   HB3  H  N N 308 
SER   HG   H  N N 309 
SER   HXT  H  N N 310 
THR   N    N  N N 311 
THR   CA   C  N S 312 
THR   C    C  N N 313 
THR   O    O  N N 314 
THR   CB   C  N R 315 
THR   OG1  O  N N 316 
THR   CG2  C  N N 317 
THR   OXT  O  N N 318 
THR   H    H  N N 319 
THR   H2   H  N N 320 
THR   HA   H  N N 321 
THR   HB   H  N N 322 
THR   HG1  H  N N 323 
THR   HG21 H  N N 324 
THR   HG22 H  N N 325 
THR   HG23 H  N N 326 
THR   HXT  H  N N 327 
TRP   N    N  N N 328 
TRP   CA   C  N S 329 
TRP   C    C  N N 330 
TRP   O    O  N N 331 
TRP   CB   C  N N 332 
TRP   CG   C  Y N 333 
TRP   CD1  C  Y N 334 
TRP   CD2  C  Y N 335 
TRP   NE1  N  Y N 336 
TRP   CE2  C  Y N 337 
TRP   CE3  C  Y N 338 
TRP   CZ2  C  Y N 339 
TRP   CZ3  C  Y N 340 
TRP   CH2  C  Y N 341 
TRP   OXT  O  N N 342 
TRP   H    H  N N 343 
TRP   H2   H  N N 344 
TRP   HA   H  N N 345 
TRP   HB2  H  N N 346 
TRP   HB3  H  N N 347 
TRP   HD1  H  N N 348 
TRP   HE1  H  N N 349 
TRP   HE3  H  N N 350 
TRP   HZ2  H  N N 351 
TRP   HZ3  H  N N 352 
TRP   HH2  H  N N 353 
TRP   HXT  H  N N 354 
TYR   N    N  N N 355 
TYR   CA   C  N S 356 
TYR   C    C  N N 357 
TYR   O    O  N N 358 
TYR   CB   C  N N 359 
TYR   CG   C  Y N 360 
TYR   CD1  C  Y N 361 
TYR   CD2  C  Y N 362 
TYR   CE1  C  Y N 363 
TYR   CE2  C  Y N 364 
TYR   CZ   C  Y N 365 
TYR   OH   O  N N 366 
TYR   OXT  O  N N 367 
TYR   H    H  N N 368 
TYR   H2   H  N N 369 
TYR   HA   H  N N 370 
TYR   HB2  H  N N 371 
TYR   HB3  H  N N 372 
TYR   HD1  H  N N 373 
TYR   HD2  H  N N 374 
TYR   HE1  H  N N 375 
TYR   HE2  H  N N 376 
TYR   HH   H  N N 377 
TYR   HXT  H  N N 378 
VAL   N    N  N N 379 
VAL   CA   C  N S 380 
VAL   C    C  N N 381 
VAL   O    O  N N 382 
VAL   CB   C  N N 383 
VAL   CG1  C  N N 384 
VAL   CG2  C  N N 385 
VAL   OXT  O  N N 386 
VAL   H    H  N N 387 
VAL   H2   H  N N 388 
VAL   HA   H  N N 389 
VAL   HB   H  N N 390 
VAL   HG11 H  N N 391 
VAL   HG12 H  N N 392 
VAL   HG13 H  N N 393 
VAL   HG21 H  N N 394 
VAL   HG22 H  N N 395 
VAL   HG23 H  N N 396 
VAL   HXT  H  N N 397 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1AYO N1  C1   sing N N 1   
A1AYO C1  C2   doub Y N 2   
A1AYO C2  C3   sing Y N 3   
A1AYO C3  C4   doub Y N 4   
A1AYO C4  N2   sing N N 5   
A1AYO N2  C5   sing Y N 6   
A1AYO C5  N3   doub Y N 7   
A1AYO N3  C6   sing Y N 8   
A1AYO C6  CL1  sing N N 9   
A1AYO C6  C7   doub Y N 10  
A1AYO C7  CL2  sing N N 11  
A1AYO C4  C8   sing Y N 12  
A1AYO C8  C9   doub Y N 13  
A1AYO C1  C9   sing Y N 14  
A1AYO N2  C7   sing Y N 15  
A1AYO C2  H3   sing N N 16  
A1AYO C3  H4   sing N N 17  
A1AYO C5  H5   sing N N 18  
A1AYO N1  H2   sing N N 19  
A1AYO N1  H1   sing N N 20  
A1AYO C8  H6   sing N N 21  
A1AYO C9  H7   sing N N 22  
ALA   N   CA   sing N N 23  
ALA   N   H    sing N N 24  
ALA   N   H2   sing N N 25  
ALA   CA  C    sing N N 26  
ALA   CA  CB   sing N N 27  
ALA   CA  HA   sing N N 28  
ALA   C   O    doub N N 29  
ALA   C   OXT  sing N N 30  
ALA   CB  HB1  sing N N 31  
ALA   CB  HB2  sing N N 32  
ALA   CB  HB3  sing N N 33  
ALA   OXT HXT  sing N N 34  
ARG   N   CA   sing N N 35  
ARG   N   H    sing N N 36  
ARG   N   H2   sing N N 37  
ARG   CA  C    sing N N 38  
ARG   CA  CB   sing N N 39  
ARG   CA  HA   sing N N 40  
ARG   C   O    doub N N 41  
ARG   C   OXT  sing N N 42  
ARG   CB  CG   sing N N 43  
ARG   CB  HB2  sing N N 44  
ARG   CB  HB3  sing N N 45  
ARG   CG  CD   sing N N 46  
ARG   CG  HG2  sing N N 47  
ARG   CG  HG3  sing N N 48  
ARG   CD  NE   sing N N 49  
ARG   CD  HD2  sing N N 50  
ARG   CD  HD3  sing N N 51  
ARG   NE  CZ   sing N N 52  
ARG   NE  HE   sing N N 53  
ARG   CZ  NH1  sing N N 54  
ARG   CZ  NH2  doub N N 55  
ARG   NH1 HH11 sing N N 56  
ARG   NH1 HH12 sing N N 57  
ARG   NH2 HH21 sing N N 58  
ARG   NH2 HH22 sing N N 59  
ARG   OXT HXT  sing N N 60  
ASN   N   CA   sing N N 61  
ASN   N   H    sing N N 62  
ASN   N   H2   sing N N 63  
ASN   CA  C    sing N N 64  
ASN   CA  CB   sing N N 65  
ASN   CA  HA   sing N N 66  
ASN   C   O    doub N N 67  
ASN   C   OXT  sing N N 68  
ASN   CB  CG   sing N N 69  
ASN   CB  HB2  sing N N 70  
ASN   CB  HB3  sing N N 71  
ASN   CG  OD1  doub N N 72  
ASN   CG  ND2  sing N N 73  
ASN   ND2 HD21 sing N N 74  
ASN   ND2 HD22 sing N N 75  
ASN   OXT HXT  sing N N 76  
ASP   N   CA   sing N N 77  
ASP   N   H    sing N N 78  
ASP   N   H2   sing N N 79  
ASP   CA  C    sing N N 80  
ASP   CA  CB   sing N N 81  
ASP   CA  HA   sing N N 82  
ASP   C   O    doub N N 83  
ASP   C   OXT  sing N N 84  
ASP   CB  CG   sing N N 85  
ASP   CB  HB2  sing N N 86  
ASP   CB  HB3  sing N N 87  
ASP   CG  OD1  doub N N 88  
ASP   CG  OD2  sing N N 89  
ASP   OD2 HD2  sing N N 90  
ASP   OXT HXT  sing N N 91  
GLN   N   CA   sing N N 92  
GLN   N   H    sing N N 93  
GLN   N   H2   sing N N 94  
GLN   CA  C    sing N N 95  
GLN   CA  CB   sing N N 96  
GLN   CA  HA   sing N N 97  
GLN   C   O    doub N N 98  
GLN   C   OXT  sing N N 99  
GLN   CB  CG   sing N N 100 
GLN   CB  HB2  sing N N 101 
GLN   CB  HB3  sing N N 102 
GLN   CG  CD   sing N N 103 
GLN   CG  HG2  sing N N 104 
GLN   CG  HG3  sing N N 105 
GLN   CD  OE1  doub N N 106 
GLN   CD  NE2  sing N N 107 
GLN   NE2 HE21 sing N N 108 
GLN   NE2 HE22 sing N N 109 
GLN   OXT HXT  sing N N 110 
GLU   N   CA   sing N N 111 
GLU   N   H    sing N N 112 
GLU   N   H2   sing N N 113 
GLU   CA  C    sing N N 114 
GLU   CA  CB   sing N N 115 
GLU   CA  HA   sing N N 116 
GLU   C   O    doub N N 117 
GLU   C   OXT  sing N N 118 
GLU   CB  CG   sing N N 119 
GLU   CB  HB2  sing N N 120 
GLU   CB  HB3  sing N N 121 
GLU   CG  CD   sing N N 122 
GLU   CG  HG2  sing N N 123 
GLU   CG  HG3  sing N N 124 
GLU   CD  OE1  doub N N 125 
GLU   CD  OE2  sing N N 126 
GLU   OE2 HE2  sing N N 127 
GLU   OXT HXT  sing N N 128 
GLY   N   CA   sing N N 129 
GLY   N   H    sing N N 130 
GLY   N   H2   sing N N 131 
GLY   CA  C    sing N N 132 
GLY   CA  HA2  sing N N 133 
GLY   CA  HA3  sing N N 134 
GLY   C   O    doub N N 135 
GLY   C   OXT  sing N N 136 
GLY   OXT HXT  sing N N 137 
HIS   N   CA   sing N N 138 
HIS   N   H    sing N N 139 
HIS   N   H2   sing N N 140 
HIS   CA  C    sing N N 141 
HIS   CA  CB   sing N N 142 
HIS   CA  HA   sing N N 143 
HIS   C   O    doub N N 144 
HIS   C   OXT  sing N N 145 
HIS   CB  CG   sing N N 146 
HIS   CB  HB2  sing N N 147 
HIS   CB  HB3  sing N N 148 
HIS   CG  ND1  sing Y N 149 
HIS   CG  CD2  doub Y N 150 
HIS   ND1 CE1  doub Y N 151 
HIS   ND1 HD1  sing N N 152 
HIS   CD2 NE2  sing Y N 153 
HIS   CD2 HD2  sing N N 154 
HIS   CE1 NE2  sing Y N 155 
HIS   CE1 HE1  sing N N 156 
HIS   NE2 HE2  sing N N 157 
HIS   OXT HXT  sing N N 158 
HOH   O   H1   sing N N 159 
HOH   O   H2   sing N N 160 
ILE   N   CA   sing N N 161 
ILE   N   H    sing N N 162 
ILE   N   H2   sing N N 163 
ILE   CA  C    sing N N 164 
ILE   CA  CB   sing N N 165 
ILE   CA  HA   sing N N 166 
ILE   C   O    doub N N 167 
ILE   C   OXT  sing N N 168 
ILE   CB  CG1  sing N N 169 
ILE   CB  CG2  sing N N 170 
ILE   CB  HB   sing N N 171 
ILE   CG1 CD1  sing N N 172 
ILE   CG1 HG12 sing N N 173 
ILE   CG1 HG13 sing N N 174 
ILE   CG2 HG21 sing N N 175 
ILE   CG2 HG22 sing N N 176 
ILE   CG2 HG23 sing N N 177 
ILE   CD1 HD11 sing N N 178 
ILE   CD1 HD12 sing N N 179 
ILE   CD1 HD13 sing N N 180 
ILE   OXT HXT  sing N N 181 
LEU   N   CA   sing N N 182 
LEU   N   H    sing N N 183 
LEU   N   H2   sing N N 184 
LEU   CA  C    sing N N 185 
LEU   CA  CB   sing N N 186 
LEU   CA  HA   sing N N 187 
LEU   C   O    doub N N 188 
LEU   C   OXT  sing N N 189 
LEU   CB  CG   sing N N 190 
LEU   CB  HB2  sing N N 191 
LEU   CB  HB3  sing N N 192 
LEU   CG  CD1  sing N N 193 
LEU   CG  CD2  sing N N 194 
LEU   CG  HG   sing N N 195 
LEU   CD1 HD11 sing N N 196 
LEU   CD1 HD12 sing N N 197 
LEU   CD1 HD13 sing N N 198 
LEU   CD2 HD21 sing N N 199 
LEU   CD2 HD22 sing N N 200 
LEU   CD2 HD23 sing N N 201 
LEU   OXT HXT  sing N N 202 
LYS   N   CA   sing N N 203 
LYS   N   H    sing N N 204 
LYS   N   H2   sing N N 205 
LYS   CA  C    sing N N 206 
LYS   CA  CB   sing N N 207 
LYS   CA  HA   sing N N 208 
LYS   C   O    doub N N 209 
LYS   C   OXT  sing N N 210 
LYS   CB  CG   sing N N 211 
LYS   CB  HB2  sing N N 212 
LYS   CB  HB3  sing N N 213 
LYS   CG  CD   sing N N 214 
LYS   CG  HG2  sing N N 215 
LYS   CG  HG3  sing N N 216 
LYS   CD  CE   sing N N 217 
LYS   CD  HD2  sing N N 218 
LYS   CD  HD3  sing N N 219 
LYS   CE  NZ   sing N N 220 
LYS   CE  HE2  sing N N 221 
LYS   CE  HE3  sing N N 222 
LYS   NZ  HZ1  sing N N 223 
LYS   NZ  HZ2  sing N N 224 
LYS   NZ  HZ3  sing N N 225 
LYS   OXT HXT  sing N N 226 
MET   N   CA   sing N N 227 
MET   N   H    sing N N 228 
MET   N   H2   sing N N 229 
MET   CA  C    sing N N 230 
MET   CA  CB   sing N N 231 
MET   CA  HA   sing N N 232 
MET   C   O    doub N N 233 
MET   C   OXT  sing N N 234 
MET   CB  CG   sing N N 235 
MET   CB  HB2  sing N N 236 
MET   CB  HB3  sing N N 237 
MET   CG  SD   sing N N 238 
MET   CG  HG2  sing N N 239 
MET   CG  HG3  sing N N 240 
MET   SD  CE   sing N N 241 
MET   CE  HE1  sing N N 242 
MET   CE  HE2  sing N N 243 
MET   CE  HE3  sing N N 244 
MET   OXT HXT  sing N N 245 
PHE   N   CA   sing N N 246 
PHE   N   H    sing N N 247 
PHE   N   H2   sing N N 248 
PHE   CA  C    sing N N 249 
PHE   CA  CB   sing N N 250 
PHE   CA  HA   sing N N 251 
PHE   C   O    doub N N 252 
PHE   C   OXT  sing N N 253 
PHE   CB  CG   sing N N 254 
PHE   CB  HB2  sing N N 255 
PHE   CB  HB3  sing N N 256 
PHE   CG  CD1  doub Y N 257 
PHE   CG  CD2  sing Y N 258 
PHE   CD1 CE1  sing Y N 259 
PHE   CD1 HD1  sing N N 260 
PHE   CD2 CE2  doub Y N 261 
PHE   CD2 HD2  sing N N 262 
PHE   CE1 CZ   doub Y N 263 
PHE   CE1 HE1  sing N N 264 
PHE   CE2 CZ   sing Y N 265 
PHE   CE2 HE2  sing N N 266 
PHE   CZ  HZ   sing N N 267 
PHE   OXT HXT  sing N N 268 
PRO   N   CA   sing N N 269 
PRO   N   CD   sing N N 270 
PRO   N   H    sing N N 271 
PRO   CA  C    sing N N 272 
PRO   CA  CB   sing N N 273 
PRO   CA  HA   sing N N 274 
PRO   C   O    doub N N 275 
PRO   C   OXT  sing N N 276 
PRO   CB  CG   sing N N 277 
PRO   CB  HB2  sing N N 278 
PRO   CB  HB3  sing N N 279 
PRO   CG  CD   sing N N 280 
PRO   CG  HG2  sing N N 281 
PRO   CG  HG3  sing N N 282 
PRO   CD  HD2  sing N N 283 
PRO   CD  HD3  sing N N 284 
PRO   OXT HXT  sing N N 285 
SER   N   CA   sing N N 286 
SER   N   H    sing N N 287 
SER   N   H2   sing N N 288 
SER   CA  C    sing N N 289 
SER   CA  CB   sing N N 290 
SER   CA  HA   sing N N 291 
SER   C   O    doub N N 292 
SER   C   OXT  sing N N 293 
SER   CB  OG   sing N N 294 
SER   CB  HB2  sing N N 295 
SER   CB  HB3  sing N N 296 
SER   OG  HG   sing N N 297 
SER   OXT HXT  sing N N 298 
THR   N   CA   sing N N 299 
THR   N   H    sing N N 300 
THR   N   H2   sing N N 301 
THR   CA  C    sing N N 302 
THR   CA  CB   sing N N 303 
THR   CA  HA   sing N N 304 
THR   C   O    doub N N 305 
THR   C   OXT  sing N N 306 
THR   CB  OG1  sing N N 307 
THR   CB  CG2  sing N N 308 
THR   CB  HB   sing N N 309 
THR   OG1 HG1  sing N N 310 
THR   CG2 HG21 sing N N 311 
THR   CG2 HG22 sing N N 312 
THR   CG2 HG23 sing N N 313 
THR   OXT HXT  sing N N 314 
TRP   N   CA   sing N N 315 
TRP   N   H    sing N N 316 
TRP   N   H2   sing N N 317 
TRP   CA  C    sing N N 318 
TRP   CA  CB   sing N N 319 
TRP   CA  HA   sing N N 320 
TRP   C   O    doub N N 321 
TRP   C   OXT  sing N N 322 
TRP   CB  CG   sing N N 323 
TRP   CB  HB2  sing N N 324 
TRP   CB  HB3  sing N N 325 
TRP   CG  CD1  doub Y N 326 
TRP   CG  CD2  sing Y N 327 
TRP   CD1 NE1  sing Y N 328 
TRP   CD1 HD1  sing N N 329 
TRP   CD2 CE2  doub Y N 330 
TRP   CD2 CE3  sing Y N 331 
TRP   NE1 CE2  sing Y N 332 
TRP   NE1 HE1  sing N N 333 
TRP   CE2 CZ2  sing Y N 334 
TRP   CE3 CZ3  doub Y N 335 
TRP   CE3 HE3  sing N N 336 
TRP   CZ2 CH2  doub Y N 337 
TRP   CZ2 HZ2  sing N N 338 
TRP   CZ3 CH2  sing Y N 339 
TRP   CZ3 HZ3  sing N N 340 
TRP   CH2 HH2  sing N N 341 
TRP   OXT HXT  sing N N 342 
TYR   N   CA   sing N N 343 
TYR   N   H    sing N N 344 
TYR   N   H2   sing N N 345 
TYR   CA  C    sing N N 346 
TYR   CA  CB   sing N N 347 
TYR   CA  HA   sing N N 348 
TYR   C   O    doub N N 349 
TYR   C   OXT  sing N N 350 
TYR   CB  CG   sing N N 351 
TYR   CB  HB2  sing N N 352 
TYR   CB  HB3  sing N N 353 
TYR   CG  CD1  doub Y N 354 
TYR   CG  CD2  sing Y N 355 
TYR   CD1 CE1  sing Y N 356 
TYR   CD1 HD1  sing N N 357 
TYR   CD2 CE2  doub Y N 358 
TYR   CD2 HD2  sing N N 359 
TYR   CE1 CZ   doub Y N 360 
TYR   CE1 HE1  sing N N 361 
TYR   CE2 CZ   sing Y N 362 
TYR   CE2 HE2  sing N N 363 
TYR   CZ  OH   sing N N 364 
TYR   OH  HH   sing N N 365 
TYR   OXT HXT  sing N N 366 
VAL   N   CA   sing N N 367 
VAL   N   H    sing N N 368 
VAL   N   H2   sing N N 369 
VAL   CA  C    sing N N 370 
VAL   CA  CB   sing N N 371 
VAL   CA  HA   sing N N 372 
VAL   C   O    doub N N 373 
VAL   C   OXT  sing N N 374 
VAL   CB  CG1  sing N N 375 
VAL   CB  CG2  sing N N 376 
VAL   CB  HB   sing N N 377 
VAL   CG1 HG11 sing N N 378 
VAL   CG1 HG12 sing N N 379 
VAL   CG1 HG13 sing N N 380 
VAL   CG2 HG21 sing N N 381 
VAL   CG2 HG22 sing N N 382 
VAL   CG2 HG23 sing N N 383 
VAL   OXT HXT  sing N N 384 
# 
_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                    7HBA 
_atom_sites.fract_transf_matrix[1][1]   0.014286 
_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]   0.011210 
_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]   0.010294 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLU   A 1 9   ? 9.20734   15.48131 10.68083 1.000 82.24775  ? 16  GLU   A N   1 
ATOM   2    C  CA  . GLU   A 1 9   ? 10.31794  16.41685 10.54868 1.000 85.06092  ? 16  GLU   A CA  1 
ATOM   3    C  C   . GLU   A 1 9   ? 10.29438  17.43024 11.68979 1.000 77.03996  ? 16  GLU   A C   1 
ATOM   4    O  O   . GLU   A 1 9   ? 9.48494   18.35756 11.69078 1.000 77.07352  ? 16  GLU   A O   1 
ATOM   5    C  CB  . GLU   A 1 9   ? 10.26012  17.12887 9.19531  1.000 96.32536  ? 16  GLU   A CB  1 
ATOM   6    C  CG  . GLU   A 1 9   ? 11.62266  17.40986 8.58007  1.000 99.88302  ? 16  GLU   A CG  1 
ATOM   7    C  CD  . GLU   A 1 9   ? 12.14887  18.79356 8.91043  1.000 114.91091 ? 16  GLU   A CD  1 
ATOM   8    O  OE1 . GLU   A 1 9   ? 11.57458  19.46234 9.79549  1.000 104.73093 ? 16  GLU   A OE1 1 
ATOM   9    O  OE2 . GLU   A 1 9   ? 13.14350  19.21380 8.28241  1.000 114.81894 ? 16  GLU   A OE2 1 
ATOM   10   N  N   . VAL   A 1 10  ? 11.18635  17.24705 12.66094 1.000 70.33015  ? 17  VAL   A N   1 
ATOM   11   C  CA  . VAL   A 1 10  ? 11.23202  18.06679 13.86618 1.000 59.55753  ? 17  VAL   A CA  1 
ATOM   12   C  C   . VAL   A 1 10  ? 12.59542  18.73666 13.95131 1.000 51.99544  ? 17  VAL   A C   1 
ATOM   13   O  O   . VAL   A 1 10  ? 13.62954  18.06272 13.87960 1.000 58.16057  ? 17  VAL   A O   1 
ATOM   14   C  CB  . VAL   A 1 10  ? 10.96043  17.23202 15.13135 1.000 59.17089  ? 17  VAL   A CB  1 
ATOM   15   C  CG1 . VAL   A 1 10  ? 10.88160  18.13166 16.35302 1.000 51.24583  ? 17  VAL   A CG1 1 
ATOM   16   C  CG2 . VAL   A 1 10  ? 9.68072   16.42707 14.97460 1.000 65.90718  ? 17  VAL   A CG2 1 
ATOM   17   N  N   . GLU   A 1 11  ? 12.59456  20.05635 14.11397 1.000 53.45934  ? 18  GLU   A N   1 
ATOM   18   C  CA  . GLU   A 1 11  ? 13.81637  20.82855 14.29245 1.000 54.90307  ? 18  GLU   A CA  1 
ATOM   19   C  C   . GLU   A 1 11  ? 14.02795  21.10514 15.77434 1.000 49.86375  ? 18  GLU   A C   1 
ATOM   20   O  O   . GLU   A 1 11  ? 13.09928  21.52939 16.46991 1.000 48.63657  ? 18  GLU   A O   1 
ATOM   21   C  CB  . GLU   A 1 11  ? 13.75300  22.14570 13.51879 1.000 52.64453  ? 18  GLU   A CB  1 
ATOM   22   C  CG  . GLU   A 1 11  ? 13.68512  21.98544 12.01318 1.000 59.71037  ? 18  GLU   A CG  1 
ATOM   23   C  CD  . GLU   A 1 11  ? 13.53561  23.31422 11.29930 1.000 65.93051  ? 18  GLU   A CD  1 
ATOM   24   O  OE1 . GLU   A 1 11  ? 12.58107  24.05538 11.61498 1.000 65.92565  ? 18  GLU   A OE1 1 
ATOM   25   O  OE2 . GLU   A 1 11  ? 14.37345  23.61775 10.42526 1.000 70.28678  ? 18  GLU   A OE2 1 
ATOM   26   N  N   . THR   A 1 12  ? 15.24604  20.86748 16.25036 1.000 44.84315  ? 19  THR   A N   1 
ATOM   27   C  CA  . THR   A 1 12  ? 15.61314  21.10765 17.63856 1.000 45.48446  ? 19  THR   A CA  1 
ATOM   28   C  C   . THR   A 1 12  ? 16.47863  22.35663 17.72077 1.000 45.46066  ? 19  THR   A C   1 
ATOM   29   O  O   . THR   A 1 12  ? 17.46432  22.48399 16.98670 1.000 46.16693  ? 19  THR   A O   1 
ATOM   30   C  CB  . THR   A 1 12  ? 16.35872  19.90915 18.22990 1.000 45.68074  ? 19  THR   A CB  1 
ATOM   31   O  OG1 . THR   A 1 12  ? 15.60177  18.71273 18.00591 1.000 45.01230  ? 19  THR   A OG1 1 
ATOM   32   C  CG2 . THR   A 1 12  ? 16.56636  20.09965 19.72489 1.000 43.98877  ? 19  THR   A CG2 1 
ATOM   33   N  N   . PHE   A 1 13  ? 16.10594  23.27196 18.61036 1.000 45.64079  ? 20  PHE   A N   1 
ATOM   34   C  CA  . PHE   A 1 13  ? 16.81986  24.52243 18.80948 1.000 44.16857  ? 20  PHE   A CA  1 
ATOM   35   C  C   . PHE   A 1 13  ? 17.34852  24.58644 20.23440 1.000 48.05725  ? 20  PHE   A C   1 
ATOM   36   O  O   . PHE   A 1 13  ? 16.79111  23.97395 21.14898 1.000 49.28165  ? 20  PHE   A O   1 
ATOM   37   C  CB  . PHE   A 1 13  ? 15.92061  25.74190 18.55276 1.000 42.90986  ? 20  PHE   A CB  1 
ATOM   38   C  CG  . PHE   A 1 13  ? 15.23166  25.73208 17.21634 1.000 48.14643  ? 20  PHE   A CG  1 
ATOM   39   C  CD1 . PHE   A 1 13  ? 14.11779  24.93649 16.99661 1.000 48.78715  ? 20  PHE   A CD1 1 
ATOM   40   C  CD2 . PHE   A 1 13  ? 15.68070  26.54338 16.18871 1.000 46.93572  ? 20  PHE   A CD2 1 
ATOM   41   C  CE1 . PHE   A 1 13  ? 13.48037  24.93376 15.77219 1.000 49.59911  ? 20  PHE   A CE1 1 
ATOM   42   C  CE2 . PHE   A 1 13  ? 15.04333  26.54948 14.96306 1.000 53.47628  ? 20  PHE   A CE2 1 
ATOM   43   C  CZ  . PHE   A 1 13  ? 13.94444  25.74049 14.75369 1.000 54.92683  ? 20  PHE   A CZ  1 
ATOM   44   N  N   . ALA   A 1 14  ? 18.42614  25.34044 20.41771 1.000 45.89513  ? 21  ALA   A N   1 
ATOM   45   C  CA  . ALA   A 1 14  ? 18.98562  25.57167 21.74062 1.000 48.33029  ? 21  ALA   A CA  1 
ATOM   46   C  C   . ALA   A 1 14  ? 18.44253  26.87894 22.30099 1.000 49.11078  ? 21  ALA   A C   1 
ATOM   47   O  O   . ALA   A 1 14  ? 18.39015  27.89102 21.59372 1.000 48.28240  ? 21  ALA   A O   1 
ATOM   48   C  CB  . ALA   A 1 14  ? 20.51295  25.61350 21.68776 1.000 49.36073  ? 21  ALA   A CB  1 
ATOM   49   N  N   . PHE   A 1 15  ? 18.02599  26.84987 23.56429 1.000 44.66250  ? 22  PHE   A N   1 
ATOM   50   C  CA  . PHE   A 1 15  ? 17.62283  28.07568 24.23549 1.000 47.78739  ? 22  PHE   A CA  1 
ATOM   51   C  C   . PHE   A 1 15  ? 18.80834  29.02482 24.34419 1.000 52.37576  ? 22  PHE   A C   1 
ATOM   52   O  O   . PHE   A 1 15  ? 19.96485  28.60250 24.43049 1.000 45.92395  ? 22  PHE   A O   1 
ATOM   53   C  CB  . PHE   A 1 15  ? 17.07786  27.77455 25.63250 1.000 46.83142  ? 22  PHE   A CB  1 
ATOM   54   C  CG  . PHE   A 1 15  ? 15.65982  27.28470 25.64265 1.000 46.11541  ? 22  PHE   A CG  1 
ATOM   55   C  CD1 . PHE   A 1 15  ? 14.61845  28.13042 25.30064 1.000 42.49955  ? 22  PHE   A CD1 1 
ATOM   56   C  CD2 . PHE   A 1 15  ? 15.36628  25.98322 26.01297 1.000 45.67039  ? 22  PHE   A CD2 1 
ATOM   57   C  CE1 . PHE   A 1 15  ? 13.31083  27.68474 25.31590 1.000 43.89186  ? 22  PHE   A CE1 1 
ATOM   58   C  CE2 . PHE   A 1 15  ? 14.06123  25.53106 26.03082 1.000 46.33147  ? 22  PHE   A CE2 1 
ATOM   59   C  CZ  . PHE   A 1 15  ? 13.03161  26.38356 25.68161 1.000 44.23723  ? 22  PHE   A CZ  1 
ATOM   60   N  N   . GLN   A 1 16  ? 18.51555  30.32170 24.32767 1.000 49.08835  ? 23  GLN   A N   1 
ATOM   61   C  CA  . GLN   A 1 16  ? 19.54996  31.29796 24.62762 1.000 51.15980  ? 23  GLN   A CA  1 
ATOM   62   C  C   . GLN   A 1 16  ? 20.03299  31.10363 26.05965 1.000 49.16846  ? 23  GLN   A C   1 
ATOM   63   O  O   . GLN   A 1 16  ? 19.26715  30.71920 26.94837 1.000 48.72011  ? 23  GLN   A O   1 
ATOM   64   C  CB  . GLN   A 1 16  ? 19.02646  32.71883 24.42013 1.000 47.72135  ? 23  GLN   A CB  1 
ATOM   65   C  CG  . GLN   A 1 16  ? 18.84217  33.09309 22.95750 1.000 46.39303  ? 23  GLN   A CG  1 
ATOM   66   C  CD  . GLN   A 1 16  ? 17.98946  34.33164 22.77319 1.000 51.48690  ? 23  GLN   A CD  1 
ATOM   67   O  OE1 . GLN   A 1 16  ? 18.50718  35.43907 22.62802 1.000 54.31621  ? 23  GLN   A OE1 1 
ATOM   68   N  NE2 . GLN   A 1 16  ? 16.67363  34.15066 22.77537 1.000 47.34329  ? 23  GLN   A NE2 1 
ATOM   69   N  N   . ALA   A 1 17  ? 21.32790  31.35701 26.27178 1.000 53.50875  ? 24  ALA   A N   1 
ATOM   70   C  CA  . ALA   A 1 17  ? 21.94683  31.06773 27.56256 1.000 50.81495  ? 24  ALA   A CA  1 
ATOM   71   C  C   . ALA   A 1 17  ? 21.21912  31.76418 28.70486 1.000 48.56103  ? 24  ALA   A C   1 
ATOM   72   O  O   . ALA   A 1 17  ? 21.05547  31.19173 29.78830 1.000 50.71966  ? 24  ALA   A O   1 
ATOM   73   C  CB  . ALA   A 1 17  ? 23.42028  31.47563 27.53847 1.000 45.99631  ? 24  ALA   A CB  1 
ATOM   74   N  N   . GLU   A 1 18  ? 20.76387  32.99744 28.47709 1.000 49.74280  ? 25  GLU   A N   1 
ATOM   75   C  CA  . GLU   A 1 18  ? 20.04210  33.72193 29.51750 1.000 53.12960  ? 25  GLU   A CA  1 
ATOM   76   C  C   . GLU   A 1 18  ? 18.69425  33.07388 29.81159 1.000 51.61321  ? 25  GLU   A C   1 
ATOM   77   O  O   . GLU   A 1 18  ? 18.28299  32.98591 30.97479 1.000 48.64123  ? 25  GLU   A O   1 
ATOM   78   C  CB  . GLU   A 1 18  ? 19.85613  35.18259 29.10573 1.000 61.94381  ? 25  GLU   A CB  1 
ATOM   79   C  CG  . GLU   A 1 18  ? 21.15608  35.95083 28.90750 1.000 64.78121  ? 25  GLU   A CG  1 
ATOM   80   C  CD  . GLU   A 1 18  ? 21.75386  35.75639 27.52498 1.000 65.98724  ? 25  GLU   A CD  1 
ATOM   81   O  OE1 . GLU   A 1 18  ? 21.19460  34.96687 26.73422 1.000 63.53858  ? 25  GLU   A OE1 1 
ATOM   82   O  OE2 . GLU   A 1 18  ? 22.78727  36.39251 27.23049 1.000 69.02849  ? 25  GLU   A OE2 1 
ATOM   83   N  N   . ILE   A 1 19  ? 17.99410  32.61297 28.77228 1.000 48.86780  ? 26  ILE   A N   1 
ATOM   84   C  CA  . ILE   A 1 19  ? 16.67847  32.00943 28.96904 1.000 47.03096  ? 26  ILE   A CA  1 
ATOM   85   C  C   . ILE   A 1 19  ? 16.81241  30.65461 29.65353 1.000 48.28601  ? 26  ILE   A C   1 
ATOM   86   O  O   . ILE   A 1 19  ? 16.09210  30.35089 30.61210 1.000 49.66258  ? 26  ILE   A O   1 
ATOM   87   C  CB  . ILE   A 1 19  ? 15.92873  31.89127 27.62844 1.000 47.58666  ? 26  ILE   A CB  1 
ATOM   88   C  CG1 . ILE   A 1 19  ? 15.23569  33.20973 27.27505 1.000 50.19321  ? 26  ILE   A CG1 1 
ATOM   89   C  CG2 . ILE   A 1 19  ? 14.90677  30.76201 27.68164 1.000 43.47857  ? 26  ILE   A CG2 1 
ATOM   90   C  CD1 . ILE   A 1 19  ? 16.15855  34.26129 26.70034 1.000 50.87550  ? 26  ILE   A CD1 1 
ATOM   91   N  N   . ALA   A 1 20  ? 17.73672  29.82014 29.17169 1.000 44.75750  ? 27  ALA   A N   1 
ATOM   92   C  CA  . ALA   A 1 20  ? 17.91745  28.49879 29.76367 1.000 49.27214  ? 27  ALA   A CA  1 
ATOM   93   C  C   . ALA   A 1 20  ? 18.32949  28.60241 31.22613 1.000 47.95193  ? 27  ALA   A C   1 
ATOM   94   O  O   . ALA   A 1 20  ? 17.92167  27.77982 32.05570 1.000 42.81755  ? 27  ALA   A O   1 
ATOM   95   C  CB  . ALA   A 1 20  ? 18.95177  27.70449 28.96668 1.000 43.76043  ? 27  ALA   A CB  1 
ATOM   96   N  N   . GLN   A 1 21  ? 19.13307  29.61240 31.56218 1.000 45.91074  ? 28  GLN   A N   1 
ATOM   97   C  CA  . GLN   A 1 21  ? 19.55049  29.81778 32.94152 1.000 48.87971  ? 28  GLN   A CA  1 
ATOM   98   C  C   . GLN   A 1 21  ? 18.43369  30.41780 33.79189 1.000 50.44871  ? 28  GLN   A C   1 
ATOM   99   O  O   . GLN   A 1 21  ? 18.43844  30.24486 35.01603 1.000 52.40134  ? 28  GLN   A O   1 
ATOM   100  C  CB  . GLN   A 1 21  ? 20.82273  30.67886 32.94753 1.000 55.47206  ? 28  GLN   A CB  1 
ATOM   101  C  CG  . GLN   A 1 21  ? 21.04701  31.61546 34.12052 1.000 61.05053  ? 28  GLN   A CG  1 
ATOM   102  C  CD  . GLN   A 1 21  ? 21.98272  32.76337 33.76905 1.000 66.96529  ? 28  GLN   A CD  1 
ATOM   103  O  OE1 . GLN   A 1 21  ? 22.81409  32.64685 32.86561 1.000 62.48406  ? 28  GLN   A OE1 1 
ATOM   104  N  NE2 . GLN   A 1 21  ? 21.87366  33.86557 34.50444 1.000 59.73506  ? 28  GLN   A NE2 1 
ATOM   105  N  N   . LEU   A 1 22  ? 17.46196  31.09062 33.16654 1.000 48.66770  ? 29  LEU   A N   1 
ATOM   106  C  CA  . LEU   A 1 22  ? 16.25261  31.49134 33.88161 1.000 51.52930  ? 29  LEU   A CA  1 
ATOM   107  C  C   . LEU   A 1 22  ? 15.34457  30.29513 34.13065 1.000 48.09482  ? 29  LEU   A C   1 
ATOM   108  O  O   . LEU   A 1 22  ? 14.77826  30.15301 35.22069 1.000 45.16048  ? 29  LEU   A O   1 
ATOM   109  C  CB  . LEU   A 1 22  ? 15.50099  32.57073 33.09714 1.000 49.11884  ? 29  LEU   A CB  1 
ATOM   110  C  CG  . LEU   A 1 22  ? 14.15687  33.03467 33.67545 1.000 52.85712  ? 29  LEU   A CG  1 
ATOM   111  C  CD1 . LEU   A 1 22  ? 14.24470  33.37895 35.16672 1.000 50.85406  ? 29  LEU   A CD1 1 
ATOM   112  C  CD2 . LEU   A 1 22  ? 13.57986  34.20279 32.88283 1.000 51.20351  ? 29  LEU   A CD2 1 
ATOM   113  N  N   . MET   A 1 23  ? 15.18940  29.42996 33.12635 1.000 48.24374  ? 30  MET   A N   1 
ATOM   114  C  CA  . MET   A 1 23  ? 14.31091  28.27430 33.26719 1.000 48.40026  ? 30  MET   A CA  1 
ATOM   115  C  C   . MET   A 1 23  ? 14.81387  27.32659 34.34667 1.000 47.82739  ? 30  MET   A C   1 
ATOM   116  O  O   . MET   A 1 23  ? 14.01766  26.74711 35.09447 1.000 51.53972  ? 30  MET   A O   1 
ATOM   117  C  CB  . MET   A 1 23  ? 14.18735  27.55104 31.92758 1.000 41.77424  ? 30  MET   A CB  1 
ATOM   118  C  CG  . MET   A 1 23  ? 13.47386  28.35814 30.85711 1.000 43.05122  ? 30  MET   A CG  1 
ATOM   119  S  SD  . MET   A 1 23  ? 13.49503  27.53888 29.25170 1.000 51.28652  ? 30  MET   A SD  1 
ATOM   120  C  CE  . MET   A 1 23  ? 12.27163  26.25692 29.50243 1.000 49.44017  ? 30  MET   A CE  1 
ATOM   121  N  N   . SER   A 1 24  ? 16.13343  27.15783 34.44643 1.000 44.92974  ? 31  SER   A N   1 
ATOM   122  C  CA  . SER   A 1 24  ? 16.68409  26.31953 35.50465 1.000 50.19184  ? 31  SER   A CA  1 
ATOM   123  C  C   . SER   A 1 24  ? 16.43724  26.93710 36.87620 1.000 46.78533  ? 31  SER   A C   1 
ATOM   124  O  O   . SER   A 1 24  ? 16.21714  26.21659 37.85611 1.000 47.72169  ? 31  SER   A O   1 
ATOM   125  C  CB  . SER   A 1 24  ? 18.17704  26.08870 35.26822 1.000 46.64378  ? 31  SER   A CB  1 
ATOM   126  O  OG  . SER   A 1 24  ? 18.87882  25.95940 36.49239 1.000 59.86176  ? 31  SER   A OG  1 
ATOM   127  N  N   . LEU   A 1 25  ? 16.45995  28.26939 36.96527 1.000 47.07363  ? 32  LEU   A N   1 
ATOM   128  C  CA  . LEU   A 1 25  ? 16.13362  28.92660 38.22707 1.000 50.54142  ? 32  LEU   A CA  1 
ATOM   129  C  C   . LEU   A 1 25  ? 14.67754  28.68238 38.60488 1.000 49.38897  ? 32  LEU   A C   1 
ATOM   130  O  O   . LEU   A 1 25  ? 14.37093  28.38999 39.76582 1.000 48.88971  ? 32  LEU   A O   1 
ATOM   131  C  CB  . LEU   A 1 25  ? 16.43674  30.42625 38.12757 1.000 47.65253  ? 32  LEU   A CB  1 
ATOM   132  C  CG  . LEU   A 1 25  ? 16.46513  31.34553 39.36003 1.000 58.23771  ? 32  LEU   A CG  1 
ATOM   133  C  CD1 . LEU   A 1 25  ? 17.19175  32.63613 39.00817 1.000 59.55815  ? 32  LEU   A CD1 1 
ATOM   134  C  CD2 . LEU   A 1 25  ? 15.07361  31.67449 39.89446 1.000 52.23683  ? 32  LEU   A CD2 1 
ATOM   135  N  N   . ILE   A 1 26  ? 13.76816  28.78320 37.63319 1.000 43.55255  ? 33  ILE   A N   1 
ATOM   136  C  CA  . ILE   A 1 26  ? 12.34808  28.59299 37.91401 1.000 47.34910  ? 33  ILE   A CA  1 
ATOM   137  C  C   . ILE   A 1 26  ? 12.06819  27.15255 38.33056 1.000 47.69225  ? 33  ILE   A C   1 
ATOM   138  O  O   . ILE   A 1 26  ? 11.24319  26.89571 39.21613 1.000 50.44713  ? 33  ILE   A O   1 
ATOM   139  C  CB  . ILE   A 1 26  ? 11.51246  29.00972 36.68887 1.000 44.78844  ? 33  ILE   A CB  1 
ATOM   140  C  CG1 . ILE   A 1 26  ? 11.45078  30.53381 36.58479 1.000 42.98663  ? 33  ILE   A CG1 1 
ATOM   141  C  CG2 . ILE   A 1 26  ? 10.10875  28.42363 36.75533 1.000 44.17457  ? 33  ILE   A CG2 1 
ATOM   142  C  CD1 . ILE   A 1 26  ? 11.00925  31.03454 35.22927 1.000 41.76871  ? 33  ILE   A CD1 1 
ATOM   143  N  N   . ILE   A 1 27  ? 12.76241  26.19336 37.71920 1.000 52.39992  ? 34  ILE   A N   1 
ATOM   144  C  CA  . ILE   A 1 27  ? 12.48156  24.78786 37.99207 1.000 53.30626  ? 34  ILE   A CA  1 
ATOM   145  C  C   . ILE   A 1 27  ? 13.06718  24.34383 39.33253 1.000 54.40682  ? 34  ILE   A C   1 
ATOM   146  O  O   . ILE   A 1 27  ? 12.46111  23.52664 40.03699 1.000 59.30638  ? 34  ILE   A O   1 
ATOM   147  C  CB  . ILE   A 1 27  ? 12.99766  23.92657 36.82438 1.000 56.11466  ? 34  ILE   A CB  1 
ATOM   148  C  CG1 . ILE   A 1 27  ? 11.91118  23.77816 35.75925 1.000 52.72776  ? 34  ILE   A CG1 1 
ATOM   149  C  CG2 . ILE   A 1 27  ? 13.46740  22.55727 37.30120 1.000 54.01843  ? 34  ILE   A CG2 1 
ATOM   150  C  CD1 . ILE   A 1 27  ? 12.42822  23.28238 34.43770 1.000 59.29856  ? 34  ILE   A CD1 1 
ATOM   151  N  N   . ASN   A 1 28  ? 14.22086  24.88467 39.72658 1.000 55.45198  ? 35  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 28  ? 14.95440  24.36111 40.87210 1.000 56.41457  ? 35  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 28  ? 14.78374  25.17103 42.15128 1.000 60.69854  ? 35  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 28  ? 15.05846  24.64272 43.23421 1.000 58.01250  ? 35  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 28  ? 16.44717  24.26849 40.53815 1.000 56.66047  ? 35  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 28  ? 16.71672  23.38749 39.33758 1.000 55.93359  ? 35  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 28  ? 16.17509  22.28817 39.22796 1.000 53.25360  ? 35  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 28  ? 17.54947  23.87015 38.42313 1.000 57.25337  ? 35  ASN   A ND2 1 
ATOM   159  N  N   . THR   A 1 29  ? 14.34917  26.42499 42.06547 1.000 59.11445  ? 36  THR   A N   1 
ATOM   160  C  CA  . THR   A 1 29  ? 14.20974  27.25394 43.25591 1.000 61.53257  ? 36  THR   A CA  1 
ATOM   161  C  C   . THR   A 1 29  ? 12.97029  26.84138 44.04161 1.000 55.55347  ? 36  THR   A C   1 
ATOM   162  O  O   . THR   A 1 29  ? 11.89121  26.66347 43.46777 1.000 55.90117  ? 36  THR   A O   1 
ATOM   163  C  CB  . THR   A 1 29  ? 14.13166  28.73304 42.87243 1.000 65.20172  ? 36  THR   A CB  1 
ATOM   164  O  OG1 . THR   A 1 29  ? 15.41152  29.17271 42.39890 1.000 63.79769  ? 36  THR   A OG1 1 
ATOM   165  C  CG2 . THR   A 1 29  ? 13.72031  29.58458 44.06540 1.000 55.57459  ? 36  THR   A CG2 1 
ATOM   166  N  N   . PHE   A 1 30  ? 13.13120  26.67459 45.35392 1.000 53.51767  ? 37  PHE   A N   1 
ATOM   167  C  CA  . PHE   A 1 30  ? 12.00445  26.36549 46.22910 1.000 60.60409  ? 37  PHE   A CA  1 
ATOM   168  C  C   . PHE   A 1 30  ? 11.09174  27.58130 46.31756 1.000 60.12820  ? 37  PHE   A C   1 
ATOM   169  O  O   . PHE   A 1 30  ? 11.47318  28.61545 46.87513 1.000 65.86192  ? 37  PHE   A O   1 
ATOM   170  C  CB  . PHE   A 1 30  ? 12.49904  25.95257 47.61222 1.000 61.51465  ? 37  PHE   A CB  1 
ATOM   171  C  CG  . PHE   A 1 30  ? 11.39705  25.55620 48.55698 1.000 67.98127  ? 37  PHE   A CG  1 
ATOM   172  C  CD1 . PHE   A 1 30  ? 10.81561  24.30151 48.47808 1.000 68.96457  ? 37  PHE   A CD1 1 
ATOM   173  C  CD2 . PHE   A 1 30  ? 10.94306  26.43883 49.52409 1.000 63.94828  ? 37  PHE   A CD2 1 
ATOM   174  C  CE1 . PHE   A 1 30  ? 9.80128   23.93450 49.34514 1.000 64.64356  ? 37  PHE   A CE1 1 
ATOM   175  C  CE2 . PHE   A 1 30  ? 9.92957   26.07740 50.39381 1.000 60.35861  ? 37  PHE   A CE2 1 
ATOM   176  C  CZ  . PHE   A 1 30  ? 9.35910   24.82334 50.30403 1.000 61.43445  ? 37  PHE   A CZ  1 
ATOM   177  N  N   . TYR   A 1 31  ? 9.88593   27.45997 45.76846 1.000 55.16835  ? 38  TYR   A N   1 
ATOM   178  C  CA  . TYR   A 1 31  ? 8.93901   28.57095 45.73605 1.000 54.81212  ? 38  TYR   A CA  1 
ATOM   179  C  C   . TYR   A 1 31  ? 7.54058   27.97467 45.79573 1.000 56.22395  ? 38  TYR   A C   1 
ATOM   180  O  O   . TYR   A 1 31  ? 7.09905   27.33302 44.83850 1.000 56.55217  ? 38  TYR   A O   1 
ATOM   181  C  CB  . TYR   A 1 31  ? 9.13988   29.41982 44.48161 1.000 62.11223  ? 38  TYR   A CB  1 
ATOM   182  C  CG  . TYR   A 1 31  ? 8.37886   30.72668 44.47241 1.000 59.30350  ? 38  TYR   A CG  1 
ATOM   183  C  CD1 . TYR   A 1 31  ? 7.13073   30.82143 43.87293 1.000 58.93223  ? 38  TYR   A CD1 1 
ATOM   184  C  CD2 . TYR   A 1 31  ? 8.90739   31.86522 45.06848 1.000 59.37666  ? 38  TYR   A CD2 1 
ATOM   185  C  CE1 . TYR   A 1 31  ? 6.43437   32.01589 43.85933 1.000 62.27170  ? 38  TYR   A CE1 1 
ATOM   186  C  CE2 . TYR   A 1 31  ? 8.21600   33.06220 45.06368 1.000 62.58481  ? 38  TYR   A CE2 1 
ATOM   187  C  CZ  . TYR   A 1 31  ? 6.97926   33.13154 44.45869 1.000 62.98086  ? 38  TYR   A CZ  1 
ATOM   188  O  OH  . TYR   A 1 31  ? 6.28841   34.32216 44.45191 1.000 65.41566  ? 38  TYR   A OH  1 
ATOM   189  N  N   . SER   A 1 32  ? 6.85117   28.17837 46.91983 1.000 58.64311  ? 39  SER   A N   1 
ATOM   190  C  CA  . SER   A 1 32  ? 5.57135   27.51300 47.13664 1.000 60.08196  ? 39  SER   A CA  1 
ATOM   191  C  C   . SER   A 1 32  ? 4.42041   28.20820 46.42053 1.000 56.56907  ? 39  SER   A C   1 
ATOM   192  O  O   . SER   A 1 32  ? 3.42341   27.55576 46.08950 1.000 57.11179  ? 39  SER   A O   1 
ATOM   193  C  CB  . SER   A 1 32  ? 5.27674   27.41931 48.63436 1.000 58.42917  ? 39  SER   A CB  1 
ATOM   194  O  OG  . SER   A 1 32  ? 6.31853   26.73651 49.31072 1.000 54.51543  ? 39  SER   A OG  1 
ATOM   195  N  N   . ASN   A 1 33  ? 4.53288   29.51331 46.16641 1.000 57.52585  ? 40  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 33  ? 3.47118   30.26820 45.49845 1.000 55.33639  ? 40  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 33  ? 3.49365   30.01041 43.98819 1.000 52.25521  ? 40  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 33  ? 3.61897   30.91584 43.16428 1.000 49.17396  ? 40  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 33  ? 3.60393   31.75300 45.81254 1.000 53.96710  ? 40  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 33  ? 2.37434   32.54624 45.41643 1.000 60.52799  ? 40  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 33  ? 1.25082   32.04913 45.48843 1.000 60.39389  ? 40  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 33  ? 2.58293   33.78748 44.99011 1.000 60.46366  ? 40  ASN   A ND2 1 
ATOM   203  N  N   . LYS   A 1 34  ? 3.35576   28.73090 43.63406 1.000 43.81243  ? 41  LYS   A N   1 
ATOM   204  C  CA  . LYS   A 1 34  ? 3.39453   28.32930 42.23321 1.000 47.99622  ? 41  LYS   A CA  1 
ATOM   205  C  C   . LYS   A 1 34  ? 2.12679   28.70654 41.47850 1.000 47.59190  ? 41  LYS   A C   1 
ATOM   206  O  O   . LYS   A 1 34  ? 2.13003   28.68189 40.24421 1.000 47.48626  ? 41  LYS   A O   1 
ATOM   207  C  CB  . LYS   A 1 34  ? 3.61830   26.82003 42.12494 1.000 50.15591  ? 41  LYS   A CB  1 
ATOM   208  C  CG  . LYS   A 1 34  ? 5.01548   26.36442 42.50777 1.000 47.92334  ? 41  LYS   A CG  1 
ATOM   209  C  CD  . LYS   A 1 34  ? 5.10542   24.84749 42.54090 1.000 49.72868  ? 41  LYS   A CD  1 
ATOM   210  C  CE  . LYS   A 1 34  ? 6.43674   24.38359 43.11059 1.000 57.32837  ? 41  LYS   A CE  1 
ATOM   211  N  NZ  . LYS   A 1 34  ? 7.58682   24.83991 42.28130 1.000 51.81936  ? 41  LYS   A NZ  1 
ATOM   212  N  N   . GLU   A 1 35  ? 1.05153   29.06442 42.18567 1.000 45.99868  ? 42  GLU   A N   1 
ATOM   213  C  CA  . GLU   A 1 35  ? -0.23776  29.28663 41.53773 1.000 50.04408  ? 42  GLU   A CA  1 
ATOM   214  C  C   . GLU   A 1 35  ? -0.22402  30.47364 40.58241 1.000 49.15794  ? 42  GLU   A C   1 
ATOM   215  O  O   . GLU   A 1 35  ? -1.14412  30.60630 39.76726 1.000 50.08691  ? 42  GLU   A O   1 
ATOM   216  C  CB  . GLU   A 1 35  ? -1.32549  29.48903 42.59413 1.000 51.21905  ? 42  GLU   A CB  1 
ATOM   217  C  CG  . GLU   A 1 35  ? -1.20262  30.79580 43.35800 1.000 50.46952  ? 42  GLU   A CG  1 
ATOM   218  C  CD  . GLU   A 1 35  ? -2.20435  30.90863 44.48985 1.000 56.70221  ? 42  GLU   A CD  1 
ATOM   219  O  OE1 . GLU   A 1 35  ? -2.53841  29.86973 45.09760 1.000 57.09765  ? 42  GLU   A OE1 1 
ATOM   220  O  OE2 . GLU   A 1 35  ? -2.65560  32.03817 44.77364 1.000 60.28325  ? 42  GLU   A OE2 1 
ATOM   221  N  N   . ILE   A 1 36  ? 0.79635   31.33367 40.65562 1.000 45.95757  ? 43  ILE   A N   1 
ATOM   222  C  CA  . ILE   A 1 36  ? 0.86588   32.49907 39.78106 1.000 44.63329  ? 43  ILE   A CA  1 
ATOM   223  C  C   . ILE   A 1 36  ? 1.13037   32.13262 38.32950 1.000 43.56634  ? 43  ILE   A C   1 
ATOM   224  O  O   . ILE   A 1 36  ? 1.03467   33.00320 37.45793 1.000 44.80166  ? 43  ILE   A O   1 
ATOM   225  C  CB  . ILE   A 1 36  ? 1.93774   33.49073 40.28431 1.000 48.34379  ? 43  ILE   A CB  1 
ATOM   226  C  CG1 . ILE   A 1 36  ? 3.32919   32.85064 40.28750 1.000 47.32775  ? 43  ILE   A CG1 1 
ATOM   227  C  CG2 . ILE   A 1 36  ? 1.58533   33.99352 41.67698 1.000 52.35316  ? 43  ILE   A CG2 1 
ATOM   228  C  CD1 . ILE   A 1 36  ? 4.20163   33.24871 39.10846 1.000 49.64634  ? 43  ILE   A CD1 1 
ATOM   229  N  N   . PHE   A 1 37  ? 1.46371   30.86985 38.04509 1.000 42.49600  ? 44  PHE   A N   1 
ATOM   230  C  CA  . PHE   A 1 37  ? 1.65652   30.45194 36.65936 1.000 45.72926  ? 44  PHE   A CA  1 
ATOM   231  C  C   . PHE   A 1 37  ? 0.38151   30.64045 35.84646 1.000 44.64563  ? 44  PHE   A C   1 
ATOM   232  O  O   . PHE   A 1 37  ? 0.43591   31.01751 34.66977 1.000 39.39177  ? 44  PHE   A O   1 
ATOM   233  C  CB  . PHE   A 1 37  ? 2.11734   28.99275 36.60661 1.000 42.28840  ? 44  PHE   A CB  1 
ATOM   234  C  CG  . PHE   A 1 37  ? 0.99290   27.99600 36.69870 1.000 42.36848  ? 44  PHE   A CG  1 
ATOM   235  C  CD1 . PHE   A 1 37  ? 0.50633   27.59703 37.93124 1.000 44.76334  ? 44  PHE   A CD1 1 
ATOM   236  C  CD2 . PHE   A 1 37  ? 0.42091   27.46078 35.55496 1.000 41.97799  ? 44  PHE   A CD2 1 
ATOM   237  C  CE1 . PHE   A 1 37  ? -0.52794  26.68680 38.02479 1.000 48.64523  ? 44  PHE   A CE1 1 
ATOM   238  C  CE2 . PHE   A 1 37  ? -0.61712  26.55267 35.64343 1.000 43.46105  ? 44  PHE   A CE2 1 
ATOM   239  C  CZ  . PHE   A 1 37  ? -1.08936  26.16317 36.87852 1.000 42.95668  ? 44  PHE   A CZ  1 
ATOM   240  N  N   . LEU   A 1 38  ? -0.77726  30.38168 36.45883 1.000 41.47255  ? 45  LEU   A N   1 
ATOM   241  C  CA  . LEU   A 1 38  ? -2.04001  30.51772 35.74214 1.000 44.14777  ? 45  LEU   A CA  1 
ATOM   242  C  C   . LEU   A 1 38  ? -2.33234  31.97634 35.42055 1.000 42.91779  ? 45  LEU   A C   1 
ATOM   243  O  O   . LEU   A 1 38  ? -2.83034  32.29027 34.33363 1.000 45.57599  ? 45  LEU   A O   1 
ATOM   244  C  CB  . LEU   A 1 38  ? -3.17585  29.90681 36.56199 1.000 40.36450  ? 45  LEU   A CB  1 
ATOM   245  C  CG  . LEU   A 1 38  ? -4.48888  29.65634 35.81854 1.000 44.97969  ? 45  LEU   A CG  1 
ATOM   246  C  CD1 . LEU   A 1 38  ? -4.25644  28.76739 34.60716 1.000 38.82683  ? 45  LEU   A CD1 1 
ATOM   247  C  CD2 . LEU   A 1 38  ? -5.52172  29.04286 36.75170 1.000 42.58944  ? 45  LEU   A CD2 1 
ATOM   248  N  N   . ARG   A 1 39  ? -2.02607  32.88061 36.35325 1.000 44.73154  ? 46  ARG   A N   1 
ATOM   249  C  CA  . ARG   A 1 39  ? -2.20322  34.30451 36.09156 1.000 43.28213  ? 46  ARG   A CA  1 
ATOM   250  C  C   . ARG   A 1 39  ? -1.33826  34.75911 34.92417 1.000 45.51346  ? 46  ARG   A C   1 
ATOM   251  O  O   . ARG   A 1 39  ? -1.78915  35.53201 34.07081 1.000 41.55728  ? 46  ARG   A O   1 
ATOM   252  C  CB  . ARG   A 1 39  ? -1.87366  35.10913 37.34853 1.000 42.59680  ? 46  ARG   A CB  1 
ATOM   253  C  CG  . ARG   A 1 39  ? -1.83084  36.61254 37.14076 1.000 47.40479  ? 46  ARG   A CG  1 
ATOM   254  C  CD  . ARG   A 1 39  ? -1.27481  37.31411 38.36910 1.000 50.57115  ? 46  ARG   A CD  1 
ATOM   255  N  NE  . ARG   A 1 39  ? 0.15972   37.09486 38.51030 1.000 51.58370  ? 46  ARG   A NE  1 
ATOM   256  C  CZ  . ARG   A 1 39  ? 0.84033   37.27458 39.63408 1.000 52.95069  ? 46  ARG   A CZ  1 
ATOM   257  N  NH1 . ARG   A 1 39  ? 0.24741   37.68364 40.74422 1.000 50.21455  ? 46  ARG   A NH1 1 
ATOM   258  N  NH2 . ARG   A 1 39  ? 2.14899   37.03739 39.64457 1.000 53.09330  ? 46  ARG   A NH2 1 
ATOM   259  N  N   . GLU   A 1 40  ? -0.09509  34.27671 34.86278 1.000 39.60120  ? 47  GLU   A N   1 
ATOM   260  C  CA  . GLU   A 1 40  ? 0.81675   34.70797 33.80883 1.000 43.30773  ? 47  GLU   A CA  1 
ATOM   261  C  C   . GLU   A 1 40  ? 0.40698   34.14590 32.45376 1.000 38.89350  ? 47  GLU   A C   1 
ATOM   262  O  O   . GLU   A 1 40  ? 0.51017   34.83613 31.43324 1.000 39.69531  ? 47  GLU   A O   1 
ATOM   263  C  CB  . GLU   A 1 40  ? 2.24815   34.29335 34.15209 1.000 39.93469  ? 47  GLU   A CB  1 
ATOM   264  C  CG  . GLU   A 1 40  ? 2.77109   34.86783 35.46208 1.000 43.66743  ? 47  GLU   A CG  1 
ATOM   265  C  CD  . GLU   A 1 40  ? 2.63550   36.37776 35.54034 1.000 50.94261  ? 47  GLU   A CD  1 
ATOM   266  O  OE1 . GLU   A 1 40  ? 2.81258   37.05061 34.50261 1.000 47.05792  ? 47  GLU   A OE1 1 
ATOM   267  O  OE2 . GLU   A 1 40  ? 2.35432   36.89275 36.64343 1.000 50.25267  ? 47  GLU   A OE2 1 
ATOM   268  N  N   . LEU   A 1 41  ? -0.05655  32.89515 32.42106 1.000 40.20213  ? 48  LEU   A N   1 
ATOM   269  C  CA  . LEU   A 1 41  ? -0.48015  32.30357 31.15662 1.000 41.27043  ? 48  LEU   A CA  1 
ATOM   270  C  C   . LEU   A 1 41  ? -1.78116  32.92542 30.66546 1.000 38.87377  ? 48  LEU   A C   1 
ATOM   271  O  O   . LEU   A 1 41  ? -1.93854  33.17988 29.46569 1.000 42.12380  ? 48  LEU   A O   1 
ATOM   272  C  CB  . LEU   A 1 41  ? -0.62593  30.78947 31.30768 1.000 43.72670  ? 48  LEU   A CB  1 
ATOM   273  C  CG  . LEU   A 1 41  ? 0.67448   30.01116 31.51821 1.000 38.15811  ? 48  LEU   A CG  1 
ATOM   274  C  CD1 . LEU   A 1 41  ? 0.40943   28.51416 31.53012 1.000 36.85572  ? 48  LEU   A CD1 1 
ATOM   275  C  CD2 . LEU   A 1 41  ? 1.69126   30.37034 30.44484 1.000 34.61398  ? 48  LEU   A CD2 1 
ATOM   276  N  N   . ILE   A 1 42  ? -2.72432  33.17742 31.57650 1.000 42.39462  ? 49  ILE   A N   1 
ATOM   277  C  CA  . ILE   A 1 42  ? -3.97138  33.83448 31.19327 1.000 40.26533  ? 49  ILE   A CA  1 
ATOM   278  C  C   . ILE   A 1 42  ? -3.69762  35.25823 30.72547 1.000 41.00093  ? 49  ILE   A C   1 
ATOM   279  O  O   . ILE   A 1 42  ? -4.29058  35.73183 29.74772 1.000 40.04180  ? 49  ILE   A O   1 
ATOM   280  C  CB  . ILE   A 1 42  ? -4.97450  33.79935 32.36235 1.000 47.20619  ? 49  ILE   A CB  1 
ATOM   281  C  CG1 . ILE   A 1 42  ? -5.50965  32.37979 32.56275 1.000 40.75459  ? 49  ILE   A CG1 1 
ATOM   282  C  CG2 . ILE   A 1 42  ? -6.12079  34.77748 32.12741 1.000 43.41396  ? 49  ILE   A CG2 1 
ATOM   283  C  CD1 . ILE   A 1 42  ? -6.47605  32.24981 33.71847 1.000 38.06347  ? 49  ILE   A CD1 1 
ATOM   284  N  N   . SER   A 1 43  ? -2.78759  35.95939 31.40871 1.000 41.94759  ? 50  SER   A N   1 
ATOM   285  C  CA  . SER   A 1 43  ? -2.42610  37.31092 30.99116 1.000 37.41546  ? 50  SER   A CA  1 
ATOM   286  C  C   . SER   A 1 43  ? -1.81242  37.31119 29.59666 1.000 40.13446  ? 50  SER   A C   1 
ATOM   287  O  O   . SER   A 1 43  ? -2.08846  38.20641 28.78948 1.000 41.05228  ? 50  SER   A O   1 
ATOM   288  C  CB  . SER   A 1 43  ? -1.46330  37.93432 32.00230 1.000 41.42995  ? 50  SER   A CB  1 
ATOM   289  O  OG  . SER   A 1 43  ? -0.78589  39.04805 31.44613 1.000 45.99403  ? 50  SER   A OG  1 
ATOM   290  N  N   . ASN   A 1 44  ? -0.97560  36.31467 29.29469 1.000 39.75367  ? 51  ASN   A N   1 
ATOM   291  C  CA  . ASN   A 1 44  ? -0.43044  36.19500 27.94647 1.000 39.49357  ? 51  ASN   A CA  1 
ATOM   292  C  C   . ASN   A 1 44  ? -1.53596  35.93097 26.93216 1.000 36.67717  ? 51  ASN   A C   1 
ATOM   293  O  O   . ASN   A 1 44  ? -1.51149  36.47051 25.81947 1.000 40.04644  ? 51  ASN   A O   1 
ATOM   294  C  CB  . ASN   A 1 44  ? 0.61890   35.08422 27.89994 1.000 38.14879  ? 51  ASN   A CB  1 
ATOM   295  C  CG  . ASN   A 1 44  ? 1.92148   35.48469 28.56206 1.000 43.02146  ? 51  ASN   A CG  1 
ATOM   296  O  OD1 . ASN   A 1 44  ? 2.18530   36.66826 28.77319 1.000 45.43589  ? 51  ASN   A OD1 1 
ATOM   297  N  ND2 . ASN   A 1 44  ? 2.74504   34.49654 28.89461 1.000 39.91195  ? 51  ASN   A ND2 1 
ATOM   298  N  N   . SER   A 1 45  ? -2.51724  35.10366 27.30084 1.000 37.47763  ? 52  SER   A N   1 
ATOM   299  C  CA  . SER   A 1 45  ? -3.65106  34.85833 26.41590 1.000 38.06182  ? 52  SER   A CA  1 
ATOM   300  C  C   . SER   A 1 45  ? -4.47821  36.12217 26.22006 1.000 40.61910  ? 52  SER   A C   1 
ATOM   301  O  O   . SER   A 1 45  ? -4.96691  36.38862 25.11570 1.000 40.28276  ? 52  SER   A O   1 
ATOM   302  C  CB  . SER   A 1 45  ? -4.51806  33.73111 26.97574 1.000 37.96188  ? 52  SER   A CB  1 
ATOM   303  O  OG  . SER   A 1 45  ? -3.84325  32.48718 26.91147 1.000 40.23363  ? 52  SER   A OG  1 
ATOM   304  N  N   . SER   A 1 46  ? -4.64454  36.91366 27.28323 1.000 40.87234  ? 53  SER   A N   1 
ATOM   305  C  CA  . SER   A 1 46  ? -5.38557  38.16578 27.16929 1.000 37.94453  ? 53  SER   A CA  1 
ATOM   306  C  C   . SER   A 1 46  ? -4.69873  39.12832 26.20839 1.000 39.56485  ? 53  SER   A C   1 
ATOM   307  O  O   . SER   A 1 46  ? -5.36504  39.81737 25.42722 1.000 41.32067  ? 53  SER   A O   1 
ATOM   308  C  CB  . SER   A 1 46  ? -5.54665  38.80598 28.54852 1.000 38.25749  ? 53  SER   A CB  1 
ATOM   309  O  OG  . SER   A 1 46  ? -6.24483  40.03687 28.46253 1.000 42.01369  ? 53  SER   A OG  1 
ATOM   310  N  N   . ASP   A 1 47  ? -3.36486  39.19045 26.25128 1.000 42.28327  ? 54  ASP   A N   1 
ATOM   311  C  CA  . ASP   A 1 47  ? -2.63638  40.05186 25.32513 1.000 41.76042  ? 54  ASP   A CA  1 
ATOM   312  C  C   . ASP   A 1 47  ? -2.82071  39.58981 23.88526 1.000 40.37186  ? 54  ASP   A C   1 
ATOM   313  O  O   . ASP   A 1 47  ? -2.99619  40.41241 22.97824 1.000 40.73381  ? 54  ASP   A O   1 
ATOM   314  C  CB  . ASP   A 1 47  ? -1.15187  40.08398 25.69177 1.000 43.60016  ? 54  ASP   A CB  1 
ATOM   315  C  CG  . ASP   A 1 47  ? -0.89760  40.70548 27.05366 1.000 48.35518  ? 54  ASP   A CG  1 
ATOM   316  O  OD1 . ASP   A 1 47  ? -1.79020  41.41389 27.56423 1.000 47.91933  ? 54  ASP   A OD1 1 
ATOM   317  O  OD2 . ASP   A 1 47  ? 0.19824   40.48740 27.61263 1.000 45.95228  ? 54  ASP   A OD2 1 
ATOM   318  N  N   . ALA   A 1 48  ? -2.78546  38.27379 23.65685 1.000 39.70213  ? 55  ALA   A N   1 
ATOM   319  C  CA  . ALA   A 1 48  ? -2.98363  37.74858 22.31014 1.000 39.37331  ? 55  ALA   A CA  1 
ATOM   320  C  C   . ALA   A 1 48  ? -4.39371  38.01866 21.80343 1.000 38.39261  ? 55  ALA   A C   1 
ATOM   321  O  O   . ALA   A 1 48  ? -4.58640  38.24236 20.60313 1.000 39.34225  ? 55  ALA   A O   1 
ATOM   322  C  CB  . ALA   A 1 48  ? -2.68704  36.24898 22.27864 1.000 34.11563  ? 55  ALA   A CB  1 
ATOM   323  N  N   . LEU   A 1 49  ? -5.38733  38.00065 22.69468 1.000 35.66812  ? 56  LEU   A N   1 
ATOM   324  C  CA  . LEU   A 1 49  ? -6.75260  38.30650 22.28206 1.000 36.41519  ? 56  LEU   A CA  1 
ATOM   325  C  C   . LEU   A 1 49  ? -6.92476  39.79596 22.01173 1.000 37.70759  ? 56  LEU   A C   1 
ATOM   326  O  O   . LEU   A 1 49  ? -7.68497  40.18485 21.11796 1.000 40.20620  ? 56  LEU   A O   1 
ATOM   327  C  CB  . LEU   A 1 49  ? -7.74095  37.82983 23.34602 1.000 40.42604  ? 56  LEU   A CB  1 
ATOM   328  C  CG  . LEU   A 1 49  ? -7.87960  36.31302 23.49198 1.000 42.05802  ? 56  LEU   A CG  1 
ATOM   329  C  CD1 . LEU   A 1 49  ? -8.36445  35.95609 24.88561 1.000 39.81830  ? 56  LEU   A CD1 1 
ATOM   330  C  CD2 . LEU   A 1 49  ? -8.81942  35.75676 22.43619 1.000 38.06646  ? 56  LEU   A CD2 1 
ATOM   331  N  N   . ASP   A 1 50  ? -6.22902  40.64359 22.77524 1.000 39.52361  ? 57  ASP   A N   1 
ATOM   332  C  CA  . ASP   A 1 50  ? -6.26655  42.07989 22.51495 1.000 42.08457  ? 57  ASP   A CA  1 
ATOM   333  C  C   . ASP   A 1 50  ? -5.74664  42.40077 21.11934 1.000 41.46392  ? 57  ASP   A C   1 
ATOM   334  O  O   . ASP   A 1 50  ? -6.28350  43.27879 20.43348 1.000 39.86678  ? 57  ASP   A O   1 
ATOM   335  C  CB  . ASP   A 1 50  ? -5.44588  42.82792 23.56732 1.000 40.63695  ? 57  ASP   A CB  1 
ATOM   336  C  CG  . ASP   A 1 50  ? -6.14301  42.90547 24.91143 1.000 45.54400  ? 57  ASP   A CG  1 
ATOM   337  O  OD1 . ASP   A 1 50  ? -7.37682  42.72285 24.95969 1.000 42.50704  ? 57  ASP   A OD1 1 
ATOM   338  O  OD2 . ASP   A 1 50  ? -5.45279  43.15491 25.92225 1.000 48.68893  ? 57  ASP   A OD2 1 
ATOM   339  N  N   . LYS   A 1 51  ? -4.70616  41.69049 20.67902 1.000 41.91852  ? 58  LYS   A N   1 
ATOM   340  C  CA  . LYS   A 1 51  ? -4.06698  42.01142 19.40708 1.000 43.13929  ? 58  LYS   A CA  1 
ATOM   341  C  C   . LYS   A 1 51  ? -4.95786  41.64374 18.22678 1.000 42.32117  ? 58  LYS   A C   1 
ATOM   342  O  O   . LYS   A 1 51  ? -5.10057  42.42532 17.27939 1.000 40.65714  ? 58  LYS   A O   1 
ATOM   343  C  CB  . LYS   A 1 51  ? -2.71751  41.30184 19.31235 1.000 40.61312  ? 58  LYS   A CB  1 
ATOM   344  C  CG  . LYS   A 1 51  ? -1.62068  41.98936 20.10154 1.000 48.88931  ? 58  LYS   A CG  1 
ATOM   345  C  CD  . LYS   A 1 51  ? -0.42543  41.08008 20.30221 1.000 52.56447  ? 58  LYS   A CD  1 
ATOM   346  C  CE  . LYS   A 1 51  ? 0.37342   41.50655 21.52225 1.000 57.40896  ? 58  LYS   A CE  1 
ATOM   347  N  NZ  . LYS   A 1 51  ? 1.48757   40.56857 21.81137 1.000 51.06828  ? 58  LYS   A NZ  1 
ATOM   348  N  N   . ILE   A 1 52  ? -5.56411  40.45455 18.26041 1.000 41.04202  ? 59  ILE   A N   1 
ATOM   349  C  CA  . ILE   A 1 52  ? -6.43704  40.06133 17.15944 1.000 41.75544  ? 59  ILE   A CA  1 
ATOM   350  C  C   . ILE   A 1 52  ? -7.71692  40.88900 17.16723 1.000 41.71866  ? 59  ILE   A C   1 
ATOM   351  O  O   . ILE   A 1 52  ? -8.29373  41.16128 16.10681 1.000 45.10299  ? 59  ILE   A O   1 
ATOM   352  C  CB  . ILE   A 1 52  ? -6.72784  38.54780 17.21174 1.000 42.25381  ? 59  ILE   A CB  1 
ATOM   353  C  CG1 . ILE   A 1 52  ? -7.49903  38.10478 15.96456 1.000 41.23356  ? 59  ILE   A CG1 1 
ATOM   354  C  CG2 . ILE   A 1 52  ? -7.48353  38.17703 18.48065 1.000 38.52838  ? 59  ILE   A CG2 1 
ATOM   355  C  CD1 . ILE   A 1 52  ? -6.68445  38.17004 14.69175 1.000 43.72334  ? 59  ILE   A CD1 1 
ATOM   356  N  N   . ARG   A 1 53  ? -8.17467  41.31845 18.34678 1.000 40.37538  ? 60  ARG   A N   1 
ATOM   357  C  CA  . ARG   A 1 53  ? -9.35400  42.17569 18.40477 1.000 44.39239  ? 60  ARG   A CA  1 
ATOM   358  C  C   . ARG   A 1 53  ? -9.06705  43.54379 17.80226 1.000 46.14257  ? 60  ARG   A C   1 
ATOM   359  O  O   . ARG   A 1 53  ? -9.89032  44.08379 17.05434 1.000 47.89050  ? 60  ARG   A O   1 
ATOM   360  C  CB  . ARG   A 1 53  ? -9.83883  42.32192 19.84684 1.000 44.32123  ? 60  ARG   A CB  1 
ATOM   361  C  CG  . ARG   A 1 53  ? -11.03212 43.25895 19.99161 1.000 49.42661  ? 60  ARG   A CG  1 
ATOM   362  C  CD  . ARG   A 1 53  ? -11.67459 43.15126 21.36238 1.000 54.69670  ? 60  ARG   A CD  1 
ATOM   363  N  NE  . ARG   A 1 53  ? -10.80763 43.67199 22.41219 1.000 57.81506  ? 60  ARG   A NE  1 
ATOM   364  C  CZ  . ARG   A 1 53  ? -11.18208 44.56332 23.31983 1.000 60.39132  ? 60  ARG   A CZ  1 
ATOM   365  N  NH1 . ARG   A 1 53  ? -12.40416 45.07153 23.32750 1.000 64.65129  ? 60  ARG   A NH1 1 
ATOM   366  N  NH2 . ARG   A 1 53  ? -10.30775 44.95676 24.24158 1.000 62.46719  ? 60  ARG   A NH2 1 
ATOM   367  N  N   . TYR   A 1 54  ? -7.90302  44.11805 18.11500 1.000 44.59010  ? 61  TYR   A N   1 
ATOM   368  C  CA  . TYR   A 1 54  ? -7.55025  45.41927 17.55871 1.000 48.50607  ? 61  TYR   A CA  1 
ATOM   369  C  C   . TYR   A 1 54  ? -7.41618  45.35173 16.04232 1.000 44.39387  ? 61  TYR   A C   1 
ATOM   370  O  O   . TYR   A 1 54  ? -7.86648  46.25788 15.33112 1.000 46.75514  ? 61  TYR   A O   1 
ATOM   371  C  CB  . TYR   A 1 54  ? -6.25558  45.92830 18.19337 1.000 43.02217  ? 61  TYR   A CB  1 
ATOM   372  C  CG  . TYR   A 1 54  ? -5.75443  47.21564 17.58437 1.000 46.47297  ? 61  TYR   A CG  1 
ATOM   373  C  CD1 . TYR   A 1 54  ? -6.25609  48.44210 17.99914 1.000 49.09596  ? 61  TYR   A CD1 1 
ATOM   374  C  CD2 . TYR   A 1 54  ? -4.78334  47.20573 16.59132 1.000 48.52699  ? 61  TYR   A CD2 1 
ATOM   375  C  CE1 . TYR   A 1 54  ? -5.80522  49.62301 17.44241 1.000 48.07907  ? 61  TYR   A CE1 1 
ATOM   376  C  CE2 . TYR   A 1 54  ? -4.32709  48.38068 16.02791 1.000 50.41191  ? 61  TYR   A CE2 1 
ATOM   377  C  CZ  . TYR   A 1 54  ? -4.84052  49.58641 16.45752 1.000 51.84226  ? 61  TYR   A CZ  1 
ATOM   378  O  OH  . TYR   A 1 54  ? -4.38909  50.76083 15.90080 1.000 53.78645  ? 61  TYR   A OH  1 
ATOM   379  N  N   . GLU   A 1 55  ? -6.80021  44.28305 15.52861 1.000 43.42288  ? 62  GLU   A N   1 
ATOM   380  C  CA  . GLU   A 1 55  ? -6.65867  44.13448 14.08376 1.000 42.97640  ? 62  GLU   A CA  1 
ATOM   381  C  C   . GLU   A 1 55  ? -8.01028  43.97743 13.40045 1.000 48.33815  ? 62  GLU   A C   1 
ATOM   382  O  O   . GLU   A 1 55  ? -8.18638  44.42785 12.26236 1.000 50.64505  ? 62  GLU   A O   1 
ATOM   383  C  CB  . GLU   A 1 55  ? -5.76252  42.93727 13.76226 1.000 45.57722  ? 62  GLU   A CB  1 
ATOM   384  C  CG  . GLU   A 1 55  ? -4.30627  43.12094 14.16163 1.000 53.01884  ? 62  GLU   A CG  1 
ATOM   385  C  CD  . GLU   A 1 55  ? -3.39537  42.06196 13.56591 1.000 61.57477  ? 62  GLU   A CD  1 
ATOM   386  O  OE1 . GLU   A 1 55  ? -3.90742  41.13397 12.90507 1.000 58.25211  ? 62  GLU   A OE1 1 
ATOM   387  O  OE2 . GLU   A 1 55  ? -2.16509  42.15762 13.76022 1.000 64.33702  ? 62  GLU   A OE2 1 
ATOM   388  N  N   . SER   A 1 56  ? -8.97530  43.34850 14.07568 1.000 45.82401  ? 63  SER   A N   1 
ATOM   389  C  CA  . SER   A 1 56  ? -10.28699 43.13142 13.47815 1.000 44.81171  ? 63  SER   A CA  1 
ATOM   390  C  C   . SER   A 1 56  ? -11.10929 44.40978 13.39591 1.000 49.20546  ? 63  SER   A C   1 
ATOM   391  O  O   . SER   A 1 56  ? -12.10708 44.44240 12.66802 1.000 53.10183  ? 63  SER   A O   1 
ATOM   392  C  CB  . SER   A 1 56  ? -11.05623 42.07442 14.26990 1.000 42.68049  ? 63  SER   A CB  1 
ATOM   393  O  OG  . SER   A 1 56  ? -11.54910 42.60861 15.48616 1.000 46.05116  ? 63  SER   A OG  1 
ATOM   394  N  N   . LEU   A 1 57  ? -10.71934 45.45808 14.12449 1.000 47.22726  ? 64  LEU   A N   1 
ATOM   395  C  CA  . LEU   A 1 57  ? -11.47588 46.70444 14.08326 1.000 51.70308  ? 64  LEU   A CA  1 
ATOM   396  C  C   . LEU   A 1 57  ? -11.34902 47.39408 12.73178 1.000 52.83713  ? 64  LEU   A C   1 
ATOM   397  O  O   . LEU   A 1 57  ? -12.28519 48.07131 12.29294 1.000 54.68070  ? 64  LEU   A O   1 
ATOM   398  C  CB  . LEU   A 1 57  ? -11.01459 47.63565 15.20372 1.000 49.82389  ? 64  LEU   A CB  1 
ATOM   399  C  CG  . LEU   A 1 57  ? -11.14010 47.07369 16.62143 1.000 49.68436  ? 64  LEU   A CG  1 
ATOM   400  C  CD1 . LEU   A 1 57  ? -10.66758 48.09015 17.65069 1.000 48.43183  ? 64  LEU   A CD1 1 
ATOM   401  C  CD2 . LEU   A 1 57  ? -12.57102 46.63440 16.90531 1.000 50.71943  ? 64  LEU   A CD2 1 
ATOM   402  N  N   . THR   A 1 58  ? -10.20816 47.23743 12.06112 1.000 52.71021  ? 65  THR   A N   1 
ATOM   403  C  CA  . THR   A 1 58  ? -10.01096 47.78582 10.72829 1.000 55.13574  ? 65  THR   A CA  1 
ATOM   404  C  C   . THR   A 1 58  ? -10.07332 46.73347 9.63072  1.000 57.68385  ? 65  THR   A C   1 
ATOM   405  O  O   . THR   A 1 58  ? -10.15256 47.09743 8.45297  1.000 58.43723  ? 65  THR   A O   1 
ATOM   406  C  CB  . THR   A 1 58  ? -8.66363  48.52118 10.64377 1.000 56.19823  ? 65  THR   A CB  1 
ATOM   407  O  OG1 . THR   A 1 58  ? -7.61015  47.64425 11.06308 1.000 56.65746  ? 65  THR   A OG1 1 
ATOM   408  C  CG2 . THR   A 1 58  ? -8.67253  49.76103 11.52981 1.000 57.25904  ? 65  THR   A CG2 1 
ATOM   409  N  N   . ASP   A 1 59  ? -10.04147 45.44791 9.97915  1.000 56.40015  ? 66  ASP   A N   1 
ATOM   410  C  CA  . ASP   A 1 59  ? -10.11190 44.36625 8.99909  1.000 57.90411  ? 66  ASP   A CA  1 
ATOM   411  C  C   . ASP   A 1 59  ? -10.95153 43.24197 9.58939  1.000 58.44119  ? 66  ASP   A C   1 
ATOM   412  O  O   . ASP   A 1 59  ? -10.42449 42.32699 10.23505 1.000 53.53785  ? 66  ASP   A O   1 
ATOM   413  C  CB  . ASP   A 1 59  ? -8.71557  43.87229 8.61857  1.000 58.80166  ? 66  ASP   A CB  1 
ATOM   414  C  CG  . ASP   A 1 59  ? -8.72352  42.96073 7.40253  1.000 61.02797  ? 66  ASP   A CG  1 
ATOM   415  O  OD1 . ASP   A 1 59  ? -9.81890  42.57737 6.93974  1.000 60.68122  ? 66  ASP   A OD1 1 
ATOM   416  O  OD2 . ASP   A 1 59  ? -7.62567  42.62553 6.91164  1.000 65.44557  ? 66  ASP   A OD2 1 
ATOM   417  N  N   . PRO   A 1 60  ? -12.27460 43.29164 9.40360  1.000 56.91652  ? 67  PRO   A N   1 
ATOM   418  C  CA  . PRO   A 1 60  ? -13.12997 42.21063 9.92548  1.000 58.04901  ? 67  PRO   A CA  1 
ATOM   419  C  C   . PRO   A 1 60  ? -12.75093 40.82893 9.42211  1.000 58.24318  ? 67  PRO   A C   1 
ATOM   420  O  O   . PRO   A 1 60  ? -13.07963 39.83635 10.08365 1.000 60.44802  ? 67  PRO   A O   1 
ATOM   421  C  CB  . PRO   A 1 60  ? -14.53564 42.59996 9.44663  1.000 55.82418  ? 67  PRO   A CB  1 
ATOM   422  C  CG  . PRO   A 1 60  ? -14.46484 44.03073 9.04404  1.000 64.59379  ? 67  PRO   A CG  1 
ATOM   423  C  CD  . PRO   A 1 60  ? -13.04154 44.49621 9.04466  1.000 60.45952  ? 67  PRO   A CD  1 
ATOM   424  N  N   . SER   A 1 61  ? -12.07229 40.72866 8.27667  1.000 60.03560  ? 68  SER   A N   1 
ATOM   425  C  CA  . SER   A 1 61  ? -11.69444 39.43068 7.73144  1.000 59.13694  ? 68  SER   A CA  1 
ATOM   426  C  C   . SER   A 1 61  ? -10.64214 38.71930 8.57122  1.000 60.65393  ? 68  SER   A C   1 
ATOM   427  O  O   . SER   A 1 61  ? -10.36782 37.54175 8.31702  1.000 60.83962  ? 68  SER   A O   1 
ATOM   428  C  CB  . SER   A 1 61  ? -11.18811 39.58986 6.29604  1.000 58.63461  ? 68  SER   A CB  1 
ATOM   429  O  OG  . SER   A 1 61  ? -9.91573  40.21208 6.26752  1.000 64.33975  ? 68  SER   A OG  1 
ATOM   430  N  N   . LYS   A 1 62  ? -10.04611 39.39752 9.55503  1.000 52.26131  ? 69  LYS   A N   1 
ATOM   431  C  CA  . LYS   A 1 62  ? -9.09637  38.73738 10.44142 1.000 51.35584  ? 69  LYS   A CA  1 
ATOM   432  C  C   . LYS   A 1 62  ? -9.77224  37.72474 11.35473 1.000 51.77193  ? 69  LYS   A C   1 
ATOM   433  O  O   . LYS   A 1 62  ? -9.09258  36.84546 11.89444 1.000 50.09961  ? 69  LYS   A O   1 
ATOM   434  C  CB  . LYS   A 1 62  ? -8.34733  39.77270 11.28192 1.000 52.15203  ? 69  LYS   A CB  1 
ATOM   435  C  CG  . LYS   A 1 62  ? -7.61258  40.82308 10.46738 1.000 51.54438  ? 69  LYS   A CG  1 
ATOM   436  C  CD  . LYS   A 1 62  ? -6.10821  40.65415 10.57030 1.000 50.64371  ? 69  LYS   A CD  1 
ATOM   437  C  CE  . LYS   A 1 62  ? -5.38449  41.60922 9.63527  1.000 59.95652  ? 69  LYS   A CE  1 
ATOM   438  N  NZ  . LYS   A 1 62  ? -3.93526  41.28645 9.52539  1.000 60.97227  ? 69  LYS   A NZ  1 
ATOM   439  N  N   . LEU   A 1 63  ? -11.08732 37.82783 11.53964 1.000 51.27554  ? 70  LEU   A N   1 
ATOM   440  C  CA  . LEU   A 1 63  ? -11.84085 36.89965 12.36967 1.000 49.97588  ? 70  LEU   A CA  1 
ATOM   441  C  C   . LEU   A 1 63  ? -12.47966 35.77709 11.56380 1.000 53.05678  ? 70  LEU   A C   1 
ATOM   442  O  O   . LEU   A 1 63  ? -13.27109 35.00620 12.11641 1.000 51.09557  ? 70  LEU   A O   1 
ATOM   443  C  CB  . LEU   A 1 63  ? -12.91517 37.64866 13.15897 1.000 50.97725  ? 70  LEU   A CB  1 
ATOM   444  C  CG  . LEU   A 1 63  ? -12.40709 38.71491 14.12943 1.000 53.88904  ? 70  LEU   A CG  1 
ATOM   445  C  CD1 . LEU   A 1 63  ? -13.57075 39.38629 14.84107 1.000 53.39686  ? 70  LEU   A CD1 1 
ATOM   446  C  CD2 . LEU   A 1 63  ? -11.43204 38.11169 15.12986 1.000 50.04957  ? 70  LEU   A CD2 1 
ATOM   447  N  N   . ASP   A 1 64  ? -12.15914 35.66995 10.27074 1.000 51.82103  ? 71  ASP   A N   1 
ATOM   448  C  CA  . ASP   A 1 64  ? -12.67764 34.56474 9.47146  1.000 52.76325  ? 71  ASP   A CA  1 
ATOM   449  C  C   . ASP   A 1 64  ? -12.20286 33.22125 10.00636 1.000 53.11287  ? 71  ASP   A C   1 
ATOM   450  O  O   . ASP   A 1 64  ? -12.86626 32.19924 9.79703  1.000 51.65911  ? 71  ASP   A O   1 
ATOM   451  C  CB  . ASP   A 1 64  ? -12.26404 34.73173 8.00945  1.000 52.80214  ? 71  ASP   A CB  1 
ATOM   452  C  CG  . ASP   A 1 64  ? -12.96987 35.89060 7.33356  1.000 61.57110  ? 71  ASP   A CG  1 
ATOM   453  O  OD1 . ASP   A 1 64  ? -13.82459 36.52760 7.98458  1.000 61.16230  ? 71  ASP   A OD1 1 
ATOM   454  O  OD2 . ASP   A 1 64  ? -12.67122 36.16390 6.15170  1.000 61.28621  ? 71  ASP   A OD2 1 
ATOM   455  N  N   . SER   A 1 65  ? -11.06390 33.20267 10.69552 1.000 49.30765  ? 72  SER   A N   1 
ATOM   456  C  CA  . SER   A 1 65  ? -10.55776 32.00494 11.35053 1.000 49.06618  ? 72  SER   A CA  1 
ATOM   457  C  C   . SER   A 1 65  ? -11.14828 31.80034 12.74069 1.000 54.44020  ? 72  SER   A C   1 
ATOM   458  O  O   . SER   A 1 65  ? -10.63885 30.96753 13.49839 1.000 57.25153  ? 72  SER   A O   1 
ATOM   459  C  CB  . SER   A 1 65  ? -9.03026  32.06347 11.43936 1.000 52.51565  ? 72  SER   A CB  1 
ATOM   460  O  OG  . SER   A 1 65  ? -8.59446  33.34776 11.85413 1.000 48.76697  ? 72  SER   A OG  1 
ATOM   461  N  N   . GLY   A 1 66  ? -12.19950 32.53762 13.09140 1.000 50.15080  ? 73  GLY   A N   1 
ATOM   462  C  CA  . GLY   A 1 66  ? -12.81747 32.41185 14.39638 1.000 49.42063  ? 73  GLY   A CA  1 
ATOM   463  C  C   . GLY   A 1 66  ? -13.22184 33.74793 14.98333 1.000 51.70537  ? 73  GLY   A C   1 
ATOM   464  O  O   . GLY   A 1 66  ? -12.36897 34.60138 15.24360 1.000 50.52646  ? 73  GLY   A O   1 
ATOM   465  N  N   . LYS   A 1 67  ? -14.52212 33.94258 15.19848 1.000 53.51663  ? 74  LYS   A N   1 
ATOM   466  C  CA  . LYS   A 1 67  ? -15.02532 35.21237 15.70653 1.000 56.31209  ? 74  LYS   A CA  1 
ATOM   467  C  C   . LYS   A 1 67  ? -14.98495 35.30299 17.22513 1.000 57.22352  ? 74  LYS   A C   1 
ATOM   468  O  O   . LYS   A 1 67  ? -14.85370 36.40588 17.76883 1.000 55.64874  ? 74  LYS   A O   1 
ATOM   469  C  CB  . LYS   A 1 67  ? -16.46076 35.43965 15.22443 1.000 53.96109  ? 74  LYS   A CB  1 
ATOM   470  C  CG  . LYS   A 1 67  ? -16.55988 36.16198 13.89216 1.000 60.20420  ? 74  LYS   A CG  1 
ATOM   471  C  CD  . LYS   A 1 67  ? -17.56015 35.48366 12.97074 1.000 71.76083  ? 74  LYS   A CD  1 
ATOM   472  C  CE  . LYS   A 1 67  ? -16.90159 34.38858 12.14720 1.000 67.83637  ? 74  LYS   A CE  1 
ATOM   473  N  NZ  . LYS   A 1 67  ? -17.88104 33.70141 11.26119 1.000 71.46364  ? 74  LYS   A NZ  1 
ATOM   474  N  N   . GLU   A 1 68  ? -15.09210 34.17475 17.91928 1.000 50.62972  ? 75  GLU   A N   1 
ATOM   475  C  CA  . GLU   A 1 68  ? -15.16612 34.17800 19.37233 1.000 49.67266  ? 75  GLU   A CA  1 
ATOM   476  C  C   . GLU   A 1 68  ? -13.78579 34.38975 19.98368 1.000 52.36113  ? 75  GLU   A C   1 
ATOM   477  O  O   . GLU   A 1 68  ? -12.79795 33.78582 19.55495 1.000 51.89814  ? 75  GLU   A O   1 
ATOM   478  C  CB  . GLU   A 1 68  ? -15.77502 32.87001 19.88666 1.000 57.29855  ? 75  GLU   A CB  1 
ATOM   479  C  CG  . GLU   A 1 68  ? -16.83453 32.22223 18.98406 1.000 63.23892  ? 75  GLU   A CG  1 
ATOM   480  C  CD  . GLU   A 1 68  ? -16.25777 31.54178 17.74939 1.000 80.97223  ? 75  GLU   A CD  1 
ATOM   481  O  OE1 . GLU   A 1 68  ? -16.84101 31.69960 16.65423 1.000 79.89401  ? 75  GLU   A OE1 1 
ATOM   482  O  OE2 . GLU   A 1 68  ? -15.21791 30.86072 17.86674 1.000 75.29209  ? 75  GLU   A OE2 1 
ATOM   483  N  N   . LEU   A 1 69  ? -13.72592 35.26157 20.98974 1.000 47.48921  ? 76  LEU   A N   1 
ATOM   484  C  CA  . LEU   A 1 69  ? -12.49259 35.59910 21.69461 1.000 43.12814  ? 76  LEU   A CA  1 
ATOM   485  C  C   . LEU   A 1 69  ? -12.66753 35.20832 23.15625 1.000 44.56368  ? 76  LEU   A C   1 
ATOM   486  O  O   . LEU   A 1 69  ? -13.37734 35.88977 23.90400 1.000 43.41259  ? 76  LEU   A O   1 
ATOM   487  C  CB  . LEU   A 1 69  ? -12.17355 37.08730 21.55667 1.000 48.67110  ? 76  LEU   A CB  1 
ATOM   488  C  CG  . LEU   A 1 69  ? -12.12545 37.64360 20.13297 1.000 46.01147  ? 76  LEU   A CG  1 
ATOM   489  C  CD1 . LEU   A 1 69  ? -11.98495 39.15690 20.15830 1.000 49.71504  ? 76  LEU   A CD1 1 
ATOM   490  C  CD2 . LEU   A 1 69  ? -10.99222 37.00825 19.34221 1.000 41.55504  ? 76  LEU   A CD2 1 
ATOM   491  N  N   . HIS   A 1 70  ? -12.02600 34.11710 23.56524 1.000 42.64189  ? 77  HIS   A N   1 
ATOM   492  C  CA  . HIS   A 1 70  ? -12.22621 33.59285 24.90909 1.000 42.04891  ? 77  HIS   A CA  1 
ATOM   493  C  C   . HIS   A 1 70  ? -11.00587 32.78348 25.32392 1.000 41.73362  ? 77  HIS   A C   1 
ATOM   494  O  O   . HIS   A 1 70  ? -10.11343 32.50387 24.51978 1.000 38.66863  ? 77  HIS   A O   1 
ATOM   495  C  CB  . HIS   A 1 70  ? -13.49750 32.74098 24.98338 1.000 44.57931  ? 77  HIS   A CB  1 
ATOM   496  C  CG  . HIS   A 1 70  ? -13.57225 31.67555 23.93339 1.000 45.35054  ? 77  HIS   A CG  1 
ATOM   497  N  ND1 . HIS   A 1 70  ? -12.63582 30.67068 23.82363 1.000 50.63370  ? 77  HIS   A ND1 1 
ATOM   498  C  CD2 . HIS   A 1 70  ? -14.47072 31.46228 22.94301 1.000 50.54746  ? 77  HIS   A CD2 1 
ATOM   499  C  CE1 . HIS   A 1 70  ? -12.95481 29.88234 22.81222 1.000 45.00622  ? 77  HIS   A CE1 1 
ATOM   500  N  NE2 . HIS   A 1 70  ? -14.06367 30.34085 22.26130 1.000 48.52765  ? 77  HIS   A NE2 1 
ATOM   501  N  N   . ILE   A 1 71  ? -10.98544 32.40940 26.60154 1.000 44.15372  ? 78  ILE   A N   1 
ATOM   502  C  CA  . ILE   A 1 71  ? -9.95894  31.54677 27.17350 1.000 41.05453  ? 78  ILE   A CA  1 
ATOM   503  C  C   . ILE   A 1 71  ? -10.64837 30.33312 27.78119 1.000 43.01430  ? 78  ILE   A C   1 
ATOM   504  O  O   . ILE   A 1 71  ? -11.65025 30.47443 28.49226 1.000 40.59001  ? 78  ILE   A O   1 
ATOM   505  C  CB  . ILE   A 1 71  ? -9.11645  32.28324 28.23168 1.000 44.03319  ? 78  ILE   A CB  1 
ATOM   506  C  CG1 . ILE   A 1 71  ? -8.45292  33.51992 27.62466 1.000 42.16028  ? 78  ILE   A CG1 1 
ATOM   507  C  CG2 . ILE   A 1 71  ? -8.06417  31.35511 28.82114 1.000 38.93372  ? 78  ILE   A CG2 1 
ATOM   508  C  CD1 . ILE   A 1 71  ? -7.83464  34.44451 28.65051 1.000 40.67411  ? 78  ILE   A CD1 1 
ATOM   509  N  N   . ASN   A 1 72  ? -10.11680 29.14605 27.49859 1.000 42.75169  ? 79  ASN   A N   1 
ATOM   510  C  CA  . ASN   A 1 72  ? -10.65756 27.89407 28.01119 1.000 42.98416  ? 79  ASN   A CA  1 
ATOM   511  C  C   . ASN   A 1 72  ? -9.59321  27.18191 28.83339 1.000 41.62478  ? 79  ASN   A C   1 
ATOM   512  O  O   . ASN   A 1 72  ? -8.43939  27.07614 28.40428 1.000 46.71156  ? 79  ASN   A O   1 
ATOM   513  C  CB  . ASN   A 1 72  ? -11.13835 26.99103 26.87077 1.000 38.88777  ? 79  ASN   A CB  1 
ATOM   514  C  CG  . ASN   A 1 72  ? -12.38630 27.52220 26.19174 1.000 47.66946  ? 79  ASN   A CG  1 
ATOM   515  O  OD1 . ASN   A 1 72  ? -13.10329 28.35599 26.74678 1.000 43.41211  ? 79  ASN   A OD1 1 
ATOM   516  N  ND2 . ASN   A 1 72  ? -12.65423 27.03775 24.98469 1.000 44.14438  ? 79  ASN   A ND2 1 
ATOM   517  N  N   . LEU   A 1 73  ? -9.98276  26.69876 30.01050 1.000 43.00602  ? 80  LEU   A N   1 
ATOM   518  C  CA  . LEU   A 1 73  ? -9.09975  25.95638 30.90236 1.000 43.50777  ? 80  LEU   A CA  1 
ATOM   519  C  C   . LEU   A 1 73  ? -9.57285  24.51011 30.95602 1.000 46.04893  ? 80  LEU   A C   1 
ATOM   520  O  O   . LEU   A 1 73  ? -10.69748 24.23786 31.39013 1.000 47.39243  ? 80  LEU   A O   1 
ATOM   521  C  CB  . LEU   A 1 73  ? -9.08618  26.57539 32.29973 1.000 40.52019  ? 80  LEU   A CB  1 
ATOM   522  C  CG  . LEU   A 1 73  ? -8.81465  28.07928 32.36288 1.000 39.81548  ? 80  LEU   A CG  1 
ATOM   523  C  CD1 . LEU   A 1 73  ? -8.83970  28.56821 33.80138 1.000 41.84443  ? 80  LEU   A CD1 1 
ATOM   524  C  CD2 . LEU   A 1 73  ? -7.48738  28.41506 31.70087 1.000 36.61210  ? 80  LEU   A CD2 1 
ATOM   525  N  N   . ILE   A 1 74  ? -8.71860  23.59013 30.51825 1.000 44.18747  ? 81  ILE   A N   1 
ATOM   526  C  CA  . ILE   A 1 74  ? -9.10682  22.18980 30.36612 1.000 44.24469  ? 81  ILE   A CA  1 
ATOM   527  C  C   . ILE   A 1 74  ? -8.20207  21.29515 31.20579 1.000 46.68873  ? 81  ILE   A C   1 
ATOM   528  O  O   . ILE   A 1 74  ? -7.13681  20.87555 30.73049 1.000 46.85972  ? 81  ILE   A O   1 
ATOM   529  C  CB  . ILE   A 1 74  ? -9.06742  21.76503 28.88955 1.000 40.69280  ? 81  ILE   A CB  1 
ATOM   530  C  CG1 . ILE   A 1 74  ? -9.69060  22.84675 28.00411 1.000 43.95608  ? 81  ILE   A CG1 1 
ATOM   531  C  CG2 . ILE   A 1 74  ? -9.77714  20.43448 28.69932 1.000 42.77038  ? 81  ILE   A CG2 1 
ATOM   532  C  CD1 . ILE   A 1 74  ? -9.58911  22.55971 26.52498 1.000 50.03872  ? 81  ILE   A CD1 1 
ATOM   533  N  N   . PRO   A 1 75  ? -8.57344  20.97694 32.44260 1.000 45.09662  ? 82  PRO   A N   1 
ATOM   534  C  CA  . PRO   A 1 75  ? -7.79758  20.00674 33.21878 1.000 44.36708  ? 82  PRO   A CA  1 
ATOM   535  C  C   . PRO   A 1 75  ? -8.10513  18.57728 32.80262 1.000 51.79656  ? 82  PRO   A C   1 
ATOM   536  O  O   . PRO   A 1 75  ? -9.21803  18.24516 32.38707 1.000 53.38324  ? 82  PRO   A O   1 
ATOM   537  C  CB  . PRO   A 1 75  ? -8.25118  20.27147 34.65892 1.000 51.68099  ? 82  PRO   A CB  1 
ATOM   538  C  CG  . PRO   A 1 75  ? -9.65367  20.75410 34.50364 1.000 45.56992  ? 82  PRO   A CG  1 
ATOM   539  C  CD  . PRO   A 1 75  ? -9.65214  21.58430 33.24224 1.000 45.46134  ? 82  PRO   A CD  1 
ATOM   540  N  N   . ASN   A 1 76  ? -7.08892  17.72365 32.92345 1.000 52.18864  ? 83  ASN   A N   1 
ATOM   541  C  CA  . ASN   A 1 76  ? -7.20748  16.31255 32.55466 1.000 50.91468  ? 83  ASN   A CA  1 
ATOM   542  C  C   . ASN   A 1 76  ? -6.45655  15.49816 33.60316 1.000 57.05412  ? 83  ASN   A C   1 
ATOM   543  O  O   . ASN   A 1 76  ? -5.22314  15.46526 33.60324 1.000 56.55548  ? 83  ASN   A O   1 
ATOM   544  C  CB  . ASN   A 1 76  ? -6.66210  16.06047 31.15336 1.000 52.10702  ? 83  ASN   A CB  1 
ATOM   545  C  CG  . ASN   A 1 76  ? -7.03894  14.69212 30.61307 1.000 59.13493  ? 83  ASN   A CG  1 
ATOM   546  O  OD1 . ASN   A 1 76  ? -7.22784  13.73853 31.36866 1.000 66.67827  ? 83  ASN   A OD1 1 
ATOM   547  N  ND2 . ASN   A 1 76  ? -7.15116  14.59161 29.29387 1.000 62.50778  ? 83  ASN   A ND2 1 
ATOM   548  N  N   . LYS   A 1 77  ? -7.20523  14.83978 34.49083 1.000 56.83140  ? 84  LYS   A N   1 
ATOM   549  C  CA  . LYS   A 1 77  ? -6.57560  14.04600 35.54011 1.000 61.11178  ? 84  LYS   A CA  1 
ATOM   550  C  C   . LYS   A 1 77  ? -5.91956  12.78929 34.98332 1.000 63.23536  ? 84  LYS   A C   1 
ATOM   551  O  O   . LYS   A 1 77  ? -4.88624  12.35193 35.50240 1.000 64.28623  ? 84  LYS   A O   1 
ATOM   552  C  CB  . LYS   A 1 77  ? -7.60357  13.67453 36.60884 1.000 63.11711  ? 84  LYS   A CB  1 
ATOM   553  C  CG  . LYS   A 1 77  ? -7.96130  14.80796 37.55669 1.000 63.12347  ? 84  LYS   A CG  1 
ATOM   554  C  CD  . LYS   A 1 77  ? -8.81361  14.30366 38.70942 1.000 68.38033  ? 84  LYS   A CD  1 
ATOM   555  C  CE  . LYS   A 1 77  ? -8.98446  15.36823 39.77954 1.000 68.41060  ? 84  LYS   A CE  1 
ATOM   556  N  NZ  . LYS   A 1 77  ? -10.14682 16.25468 39.49750 1.000 69.08843  ? 84  LYS   A NZ  1 
ATOM   557  N  N   . GLN   A 1 78  ? -6.49734  12.19636 33.93608 1.000 63.76143  ? 85  GLN   A N   1 
ATOM   558  C  CA  . GLN   A 1 78  ? -5.93311  10.97081 33.37869 1.000 69.06133  ? 85  GLN   A CA  1 
ATOM   559  C  C   . GLN   A 1 78  ? -4.58140  11.23538 32.72696 1.000 64.39654  ? 85  GLN   A C   1 
ATOM   560  O  O   . GLN   A 1 78  ? -3.60331  10.52687 32.99217 1.000 68.33276  ? 85  GLN   A O   1 
ATOM   561  C  CB  . GLN   A 1 78  ? -6.90633  10.35151 32.37526 1.000 73.20071  ? 85  GLN   A CB  1 
ATOM   562  C  CG  . GLN   A 1 78  ? -6.40201  9.06486  31.73925 1.000 68.11998  ? 85  GLN   A CG  1 
ATOM   563  C  CD  . GLN   A 1 78  ? -6.25788  7.93562  32.74177 1.000 87.38923  ? 85  GLN   A CD  1 
ATOM   564  O  OE1 . GLN   A 1 78  ? -5.15761  7.43463  32.97680 1.000 89.26885  ? 85  GLN   A OE1 1 
ATOM   565  N  NE2 . GLN   A 1 78  ? -7.37224  7.52883  33.33922 1.000 87.04827  ? 85  GLN   A NE2 1 
ATOM   566  N  N   . ASP   A 1 79  ? -4.50750  12.25337 31.87011 1.000 61.19898  ? 86  ASP   A N   1 
ATOM   567  C  CA  . ASP   A 1 79  ? -3.25389  12.62438 31.22789 1.000 61.64631  ? 86  ASP   A CA  1 
ATOM   568  C  C   . ASP   A 1 79  ? -2.35184  13.45885 32.12724 1.000 59.36459  ? 86  ASP   A C   1 
ATOM   569  O  O   . ASP   A 1 79  ? -1.19206  13.68855 31.76591 1.000 59.18725  ? 86  ASP   A O   1 
ATOM   570  C  CB  . ASP   A 1 79  ? -3.53594  13.39464 29.93462 1.000 59.76994  ? 86  ASP   A CB  1 
ATOM   571  C  CG  . ASP   A 1 79  ? -4.15164  12.52255 28.85873 1.000 73.11252  ? 86  ASP   A CG  1 
ATOM   572  O  OD1 . ASP   A 1 79  ? -4.13789  12.93321 27.67922 1.000 73.93938  ? 86  ASP   A OD1 1 
ATOM   573  O  OD2 . ASP   A 1 79  ? -4.64881  11.42609 29.19195 1.000 76.41970  ? 86  ASP   A OD2 1 
ATOM   574  N  N   . ARG   A 1 80  ? -2.85248  13.90369 33.28078 1.000 56.80581  ? 87  ARG   A N   1 
ATOM   575  C  CA  . ARG   A 1 80  ? -2.12706  14.80350 34.17834 1.000 59.56939  ? 87  ARG   A CA  1 
ATOM   576  C  C   . ARG   A 1 80  ? -1.64671  16.04644 33.43132 1.000 55.44418  ? 87  ARG   A C   1 
ATOM   577  O  O   . ARG   A 1 80  ? -0.49058  16.46346 33.53389 1.000 52.20296  ? 87  ARG   A O   1 
ATOM   578  C  CB  . ARG   A 1 80  ? -0.96291  14.08552 34.86380 1.000 59.04881  ? 87  ARG   A CB  1 
ATOM   579  C  CG  . ARG   A 1 80  ? -0.66175  14.61309 36.25824 1.000 59.70527  ? 87  ARG   A CG  1 
ATOM   580  C  CD  . ARG   A 1 80  ? 0.83079   14.65656 36.53266 1.000 57.14282  ? 87  ARG   A CD  1 
ATOM   581  N  NE  . ARG   A 1 80  ? 1.34777   13.36636 36.97166 1.000 62.99171  ? 87  ARG   A NE  1 
ATOM   582  C  CZ  . ARG   A 1 80  ? 2.62787   13.02254 36.93691 1.000 64.87421  ? 87  ARG   A CZ  1 
ATOM   583  N  NH1 . ARG   A 1 80  ? 3.55357   13.85077 36.48189 1.000 64.81167  ? 87  ARG   A NH1 1 
ATOM   584  N  NH2 . ARG   A 1 80  ? 2.98841   11.81820 37.37099 1.000 66.37736  ? 87  ARG   A NH2 1 
ATOM   585  N  N   . THR   A 1 81  ? -2.55700  16.63984 32.66320 1.000 48.50010  ? 88  THR   A N   1 
ATOM   586  C  CA  . THR   A 1 81  ? -2.26337  17.82827 31.87793 1.000 52.36853  ? 88  THR   A CA  1 
ATOM   587  C  C   . THR   A 1 81  ? -3.29324  18.90766 32.17008 1.000 48.25579  ? 88  THR   A C   1 
ATOM   588  O  O   . THR   A 1 81  ? -4.47685  18.61565 32.36656 1.000 49.13510  ? 88  THR   A O   1 
ATOM   589  C  CB  . THR   A 1 81  ? -2.25208  17.52809 30.37013 1.000 48.53189  ? 88  THR   A CB  1 
ATOM   590  O  OG1 . THR   A 1 81  ? -3.54649  17.06852 29.96088 1.000 53.65527  ? 88  THR   A OG1 1 
ATOM   591  C  CG2 . THR   A 1 81  ? -1.20801  16.47142 30.03575 1.000 51.35120  ? 88  THR   A CG2 1 
ATOM   592  N  N   . LEU   A 1 82  ? -2.83085  20.15429 32.20475 1.000 48.70855  ? 89  LEU   A N   1 
ATOM   593  C  CA  . LEU   A 1 82  ? -3.69656  21.32290 32.29018 1.000 43.93143  ? 89  LEU   A CA  1 
ATOM   594  C  C   . LEU   A 1 82  ? -3.48773  22.14855 31.03103 1.000 47.65399  ? 89  LEU   A C   1 
ATOM   595  O  O   . LEU   A 1 82  ? -2.36860  22.59612 30.75772 1.000 43.17392  ? 89  LEU   A O   1 
ATOM   596  C  CB  . LEU   A 1 82  ? -3.39801  22.15226 33.53984 1.000 42.90111  ? 89  LEU   A CB  1 
ATOM   597  C  CG  . LEU   A 1 82  ? -4.21570  23.43895 33.67394 1.000 44.19993  ? 89  LEU   A CG  1 
ATOM   598  C  CD1 . LEU   A 1 82  ? -5.70342  23.12743 33.77733 1.000 40.93796  ? 89  LEU   A CD1 1 
ATOM   599  C  CD2 . LEU   A 1 82  ? -3.74895  24.25035 34.87150 1.000 42.44129  ? 89  LEU   A CD2 1 
ATOM   600  N  N   . THR   A 1 83  ? -4.55639  22.33965 30.26544 1.000 42.47962  ? 90  THR   A N   1 
ATOM   601  C  CA  . THR   A 1 83  ? -4.49107  23.00710 28.97402 1.000 42.03807  ? 90  THR   A CA  1 
ATOM   602  C  C   . THR   A 1 83  ? -5.15764  24.37257 29.06438 1.000 45.64679  ? 90  THR   A C   1 
ATOM   603  O  O   . THR   A 1 83  ? -6.28141  24.48826 29.56612 1.000 42.43434  ? 90  THR   A O   1 
ATOM   604  C  CB  . THR   A 1 83  ? -5.16267  22.16148 27.88942 1.000 40.76496  ? 90  THR   A CB  1 
ATOM   605  O  OG1 . THR   A 1 83  ? -4.53937  20.87213 27.83139 1.000 42.87326  ? 90  THR   A OG1 1 
ATOM   606  C  CG2 . THR   A 1 83  ? -5.03061  22.83346 26.53853 1.000 43.12639  ? 90  THR   A CG2 1 
ATOM   607  N  N   . ILE   A 1 84  ? -4.46074  25.39882 28.58370 1.000 43.25809  ? 91  ILE   A N   1 
ATOM   608  C  CA  . ILE   A 1 84  ? -4.98908  26.75551 28.49285 1.000 42.36152  ? 91  ILE   A CA  1 
ATOM   609  C  C   . ILE   A 1 84  ? -5.13319  27.08474 27.01303 1.000 43.64743  ? 91  ILE   A C   1 
ATOM   610  O  O   . ILE   A 1 84  ? -4.13446  27.17233 26.28755 1.000 41.53331  ? 91  ILE   A O   1 
ATOM   611  C  CB  . ILE   A 1 84  ? -4.08728  27.77349 29.20515 1.000 40.93414  ? 91  ILE   A CB  1 
ATOM   612  C  CG1 . ILE   A 1 84  ? -4.02480  27.48306 30.70771 1.000 44.20776  ? 91  ILE   A CG1 1 
ATOM   613  C  CG2 . ILE   A 1 84  ? -4.58166  29.19121 28.95671 1.000 40.19873  ? 91  ILE   A CG2 1 
ATOM   614  C  CD1 . ILE   A 1 84  ? -2.80742  26.68914 31.13490 1.000 48.09112  ? 91  ILE   A CD1 1 
ATOM   615  N  N   . VAL   A 1 85  ? -6.37216  27.26608 26.56123 1.000 40.70328  ? 92  VAL   A N   1 
ATOM   616  C  CA  . VAL   A 1 85  ? -6.68072  27.52114 25.15852 1.000 47.16524  ? 92  VAL   A CA  1 
ATOM   617  C  C   . VAL   A 1 85  ? -7.20143  28.94438 25.02445 1.000 48.78321  ? 92  VAL   A C   1 
ATOM   618  O  O   . VAL   A 1 85  ? -8.08465  29.36378 25.78187 1.000 48.67201  ? 92  VAL   A O   1 
ATOM   619  C  CB  . VAL   A 1 85  ? -7.70824  26.51315 24.61330 1.000 46.34830  ? 92  VAL   A CB  1 
ATOM   620  C  CG1 . VAL   A 1 85  ? -8.06115  26.83752 23.16880 1.000 41.37716  ? 92  VAL   A CG1 1 
ATOM   621  C  CG2 . VAL   A 1 85  ? -7.17830  25.09349 24.72798 1.000 49.05523  ? 92  VAL   A CG2 1 
ATOM   622  N  N   . ASP   A 1 86  ? -6.65576  29.68368 24.06249 1.000 41.14156  ? 93  ASP   A N   1 
ATOM   623  C  CA  . ASP   A 1 86  ? -7.15896  31.00109 23.70852 1.000 44.19381  ? 93  ASP   A CA  1 
ATOM   624  C  C   . ASP   A 1 86  ? -7.30340  31.09048 22.19538 1.000 45.48312  ? 93  ASP   A C   1 
ATOM   625  O  O   . ASP   A 1 86  ? -6.66492  30.34753 21.44511 1.000 44.23533  ? 93  ASP   A O   1 
ATOM   626  C  CB  . ASP   A 1 86  ? -6.24678  32.11841 24.26680 1.000 41.61536  ? 93  ASP   A CB  1 
ATOM   627  C  CG  . ASP   A 1 86  ? -4.96801  32.32366 23.45316 1.000 47.14686  ? 93  ASP   A CG  1 
ATOM   628  O  OD1 . ASP   A 1 86  ? -5.04299  32.72139 22.27044 1.000 44.05549  ? 93  ASP   A OD1 1 
ATOM   629  O  OD2 . ASP   A 1 86  ? -3.87607  32.07578 24.00938 1.000 44.58082  ? 93  ASP   A OD2 1 
ATOM   630  N  N   . THR   A 1 87  ? -8.17578  31.99513 21.75530 1.000 40.09256  ? 94  THR   A N   1 
ATOM   631  C  CA  . THR   A 1 87  ? -8.37974  32.27083 20.33513 1.000 37.21729  ? 94  THR   A CA  1 
ATOM   632  C  C   . THR   A 1 87  ? -7.72985  33.58604 19.92738 1.000 41.97964  ? 94  THR   A C   1 
ATOM   633  O  O   . THR   A 1 87  ? -8.27956  34.34615 19.12170 1.000 40.37367  ? 94  THR   A O   1 
ATOM   634  C  CB  . THR   A 1 87  ? -9.86792  32.27628 20.00193 1.000 41.97994  ? 94  THR   A CB  1 
ATOM   635  O  OG1 . THR   A 1 87  ? -10.56722 33.10127 20.94115 1.000 41.69520  ? 94  THR   A OG1 1 
ATOM   636  C  CG2 . THR   A 1 87  ? -10.42932 30.86399 20.05921 1.000 44.98088  ? 94  THR   A CG2 1 
ATOM   637  N  N   . GLY   A 1 88  ? -6.55154  33.87275 20.47975 1.000 39.87637  ? 95  GLY   A N   1 
ATOM   638  C  CA  . GLY   A 1 88  ? -5.83835  35.09850 20.19212 1.000 41.38032  ? 95  GLY   A CA  1 
ATOM   639  C  C   . GLY   A 1 88  ? -5.19641  35.08365 18.82592 1.000 37.48072  ? 95  GLY   A C   1 
ATOM   640  O  O   . GLY   A 1 88  ? -5.50841  34.25679 17.96647 1.000 39.51835  ? 95  GLY   A O   1 
ATOM   641  N  N   . ILE   A 1 89  ? -4.26510  36.02237 18.63176 1.000 37.76891  ? 96  ILE   A N   1 
ATOM   642  C  CA  . ILE   A 1 89  ? -3.64112  36.20333 17.33035 1.000 39.66421  ? 96  ILE   A CA  1 
ATOM   643  C  C   . ILE   A 1 89  ? -2.75120  35.02871 16.94687 1.000 40.80850  ? 96  ILE   A C   1 
ATOM   644  O  O   . ILE   A 1 89  ? -2.45160  34.84790 15.76067 1.000 43.79402  ? 96  ILE   A O   1 
ATOM   645  C  CB  . ILE   A 1 89  ? -2.84649  37.52205 17.30994 1.000 39.96931  ? 96  ILE   A CB  1 
ATOM   646  C  CG1 . ILE   A 1 89  ? -2.60531  37.98463 15.86793 1.000 43.49795  ? 96  ILE   A CG1 1 
ATOM   647  C  CG2 . ILE   A 1 89  ? -1.52775  37.37008 18.06102 1.000 37.32763  ? 96  ILE   A CG2 1 
ATOM   648  C  CD1 . ILE   A 1 89  ? -2.06773  39.39388 15.76804 1.000 46.64550  ? 96  ILE   A CD1 1 
ATOM   649  N  N   . GLY   A 1 90  ? -2.32439  34.21975 17.91106 1.000 39.96236  ? 97  GLY   A N   1 
ATOM   650  C  CA  . GLY   A 1 90  ? -1.46461  33.09620 17.61232 1.000 41.42697  ? 97  GLY   A CA  1 
ATOM   651  C  C   . GLY   A 1 90  ? -0.02092  33.51357 17.39817 1.000 42.36586  ? 97  GLY   A C   1 
ATOM   652  O  O   . GLY   A 1 90  ? 0.37263   34.66577 17.60216 1.000 43.72081  ? 97  GLY   A O   1 
ATOM   653  N  N   . MET   A 1 91  ? 0.78031   32.54230 16.96448 1.000 43.20955  ? 98  MET   A N   1 
ATOM   654  C  CA  . MET   A 1 91  ? 2.21270   32.73975 16.79046 1.000 40.30568  ? 98  MET   A CA  1 
ATOM   655  C  C   . MET   A 1 91  ? 2.65809   32.11118 15.47916 1.000 44.86069  ? 98  MET   A C   1 
ATOM   656  O  O   . MET   A 1 91  ? 2.29643   30.96898 15.18114 1.000 44.46383  ? 98  MET   A O   1 
ATOM   657  C  CB  . MET   A 1 91  ? 2.99374   32.13157 17.96238 1.000 40.08613  ? 98  MET   A CB  1 
ATOM   658  C  CG  . MET   A 1 91  ? 3.08748   33.03289 19.18634 1.000 41.47632  ? 98  MET   A CG  1 
ATOM   659  S  SD  . MET   A 1 91  ? 3.62274   32.15402 20.67032 1.000 41.95055  ? 98  MET   A SD  1 
ATOM   660  C  CE  . MET   A 1 91  ? 2.53993   30.72895 20.64147 1.000 38.95853  ? 98  MET   A CE  1 
ATOM   661  N  N   . THR   A 1 92  ? 3.43790   32.85822 14.70137 1.000 46.45594  ? 99  THR   A N   1 
ATOM   662  C  CA  . THR   A 1 92  ? 4.01316   32.34508 13.46862 1.000 40.96389  ? 99  THR   A CA  1 
ATOM   663  C  C   . THR   A 1 92  ? 5.26699   31.52639 13.76967 1.000 44.07023  ? 99  THR   A C   1 
ATOM   664  O  O   . THR   A 1 92  ? 5.72559   31.43610 14.91143 1.000 41.66977  ? 99  THR   A O   1 
ATOM   665  C  CB  . THR   A 1 92  ? 4.35684   33.48813 12.51374 1.000 47.32201  ? 99  THR   A CB  1 
ATOM   666  O  OG1 . THR   A 1 92  ? 5.44098   34.25300 13.05670 1.000 48.33412  ? 99  THR   A OG1 1 
ATOM   667  C  CG2 . THR   A 1 92  ? 3.15760   34.39632 12.30790 1.000 40.87862  ? 99  THR   A CG2 1 
ATOM   668  N  N   . LYS   A 1 93  ? 5.82962   30.92245 12.71966 1.000 44.97926  ? 100 LYS   A N   1 
ATOM   669  C  CA  . LYS   A 1 93  ? 7.07372   30.17855 12.88969 1.000 51.45823  ? 100 LYS   A CA  1 
ATOM   670  C  C   . LYS   A 1 93  ? 8.21738   31.10757 13.27468 1.000 45.19272  ? 100 LYS   A C   1 
ATOM   671  O  O   . LYS   A 1 93  ? 9.04958   30.76262 14.12190 1.000 42.52662  ? 100 LYS   A O   1 
ATOM   672  C  CB  . LYS   A 1 93  ? 7.41622   29.40984 11.61346 1.000 51.61205  ? 100 LYS   A CB  1 
ATOM   673  C  CG  . LYS   A 1 93  ? 8.51956   28.38211 11.80679 1.000 50.60587  ? 100 LYS   A CG  1 
ATOM   674  C  CD  . LYS   A 1 93  ? 8.85511   27.65294 10.51789 1.000 53.45339  ? 100 LYS   A CD  1 
ATOM   675  C  CE  . LYS   A 1 93  ? 9.88114   26.55809 10.76557 1.000 52.62026  ? 100 LYS   A CE  1 
ATOM   676  N  NZ  . LYS   A 1 93  ? 10.55323  26.13224 9.50754  1.000 51.31823  ? 100 LYS   A NZ  1 
ATOM   677  N  N   . ALA   A 1 94  ? 8.27302   32.29404 12.66352 1.000 44.52565  ? 101 ALA   A N   1 
ATOM   678  C  CA  . ALA   A 1 94  ? 9.29909   33.26495 13.02673 1.000 49.21224  ? 101 ALA   A CA  1 
ATOM   679  C  C   . ALA   A 1 94  ? 9.13956   33.73356 14.46661 1.000 48.33949  ? 101 ALA   A C   1 
ATOM   680  O  O   . ALA   A 1 94  ? 10.12830  34.09858 15.11303 1.000 50.50465  ? 101 ALA   A O   1 
ATOM   681  C  CB  . ALA   A 1 94  ? 9.25882   34.45622 12.06953 1.000 43.82630  ? 101 ALA   A CB  1 
ATOM   682  N  N   . ASP   A 1 95  ? 7.90869   33.73280 14.98423 1.000 46.31205  ? 102 ASP   A N   1 
ATOM   683  C  CA  . ASP   A 1 95  ? 7.69236   34.07437 16.38658 1.000 42.82161  ? 102 ASP   A CA  1 
ATOM   684  C  C   . ASP   A 1 95  ? 8.33966   33.04485 17.30407 1.000 45.73478  ? 102 ASP   A C   1 
ATOM   685  O  O   . ASP   A 1 95  ? 9.02448   33.39787 18.27088 1.000 45.35010  ? 102 ASP   A O   1 
ATOM   686  C  CB  . ASP   A 1 95  ? 6.19427   34.17706 16.67906 1.000 45.05716  ? 102 ASP   A CB  1 
ATOM   687  C  CG  . ASP   A 1 95  ? 5.57973   35.45881 16.15464 1.000 48.47383  ? 102 ASP   A CG  1 
ATOM   688  O  OD1 . ASP   A 1 95  ? 6.28917   36.48511 16.09833 1.000 51.22510  ? 102 ASP   A OD1 1 
ATOM   689  O  OD2 . ASP   A 1 95  ? 4.38151   35.43915 15.80257 1.000 47.28804  ? 102 ASP   A OD2 1 
ATOM   690  N  N   . LEU   A 1 96  ? 8.13807   31.75890 17.00729 1.000 42.81221  ? 103 LEU   A N   1 
ATOM   691  C  CA  . LEU   A 1 96  ? 8.59684   30.69665 17.89397 1.000 45.25892  ? 103 LEU   A CA  1 
ATOM   692  C  C   . LEU   A 1 96  ? 10.10812  30.50790 17.86342 1.000 45.15068  ? 103 LEU   A C   1 
ATOM   693  O  O   . LEU   A 1 96  ? 10.66920  29.97197 18.82485 1.000 49.03520  ? 103 LEU   A O   1 
ATOM   694  C  CB  . LEU   A 1 96  ? 7.91083   29.37922 17.52922 1.000 42.47015  ? 103 LEU   A CB  1 
ATOM   695  C  CG  . LEU   A 1 96  ? 6.38413   29.34715 17.62404 1.000 45.82368  ? 103 LEU   A CG  1 
ATOM   696  C  CD1 . LEU   A 1 96  ? 5.82649   28.16526 16.84442 1.000 43.36042  ? 103 LEU   A CD1 1 
ATOM   697  C  CD2 . LEU   A 1 96  ? 5.93519   29.29885 19.07593 1.000 44.73538  ? 103 LEU   A CD2 1 
ATOM   698  N  N   . ILE   A 1 97  ? 10.77898  30.92589 16.79292 1.000 43.05141  ? 104 ILE   A N   1 
ATOM   699  C  CA  . ILE   A 1 97  ? 12.20499  30.69380 16.62796 1.000 51.78094  ? 104 ILE   A CA  1 
ATOM   700  C  C   . ILE   A 1 97  ? 13.01510  31.97507 16.80903 1.000 57.11561  ? 104 ILE   A C   1 
ATOM   701  O  O   . ILE   A 1 97  ? 14.07841  31.95221 17.43229 1.000 67.19435  ? 104 ILE   A O   1 
ATOM   702  C  CB  . ILE   A 1 97  ? 12.50045  30.04250 15.25782 1.000 51.38903  ? 104 ILE   A CB  1 
ATOM   703  C  CG1 . ILE   A 1 97  ? 11.94364  28.61838 15.20994 1.000 52.25117  ? 104 ILE   A CG1 1 
ATOM   704  C  CG2 . ILE   A 1 97  ? 13.99347  30.03198 14.96699 1.000 60.23973  ? 104 ILE   A CG2 1 
ATOM   705  C  CD1 . ILE   A 1 97  ? 11.44633  28.20273 13.84486 1.000 58.09493  ? 104 ILE   A CD1 1 
ATOM   706  N  N   . ASN   A 1 98  ? 12.52296  33.10062 16.29323 1.000 52.41314  ? 105 ASN   A N   1 
ATOM   707  C  CA  . ASN   A 1 98  ? 13.31891  34.32309 16.22698 1.000 55.87030  ? 105 ASN   A CA  1 
ATOM   708  C  C   . ASN   A 1 98  ? 12.73747  35.45784 17.06008 1.000 53.17865  ? 105 ASN   A C   1 
ATOM   709  O  O   . ASN   A 1 98  ? 13.40633  35.94450 17.97842 1.000 49.94061  ? 105 ASN   A O   1 
ATOM   710  C  CB  . ASN   A 1 98  ? 13.46746  34.75827 14.76324 1.000 56.61794  ? 105 ASN   A CB  1 
ATOM   711  C  CG  . ASN   A 1 98  ? 14.66001  34.11741 14.08378 1.000 67.97661  ? 105 ASN   A CG  1 
ATOM   712  O  OD1 . ASN   A 1 98  ? 14.51175  33.19606 13.28068 1.000 68.02054  ? 105 ASN   A OD1 1 
ATOM   713  N  ND2 . ASN   A 1 98  ? 15.85218  34.61757 14.38796 1.000 71.74058  ? 105 ASN   A ND2 1 
ATOM   714  N  N   . ASN   A 1 99  ? 11.51019  35.89422 16.76891 1.000 44.47754  ? 106 ASN   A N   1 
ATOM   715  C  CA  . ASN   A 1 99  ? 11.02391  37.16708 17.29761 1.000 49.12551  ? 106 ASN   A CA  1 
ATOM   716  C  C   . ASN   A 1 99  ? 10.85142  37.12681 18.81210 1.000 47.65705  ? 106 ASN   A C   1 
ATOM   717  O  O   . ASN   A 1 99  ? 11.38113  37.98569 19.52743 1.000 48.74867  ? 106 ASN   A O   1 
ATOM   718  C  CB  . ASN   A 1 99  ? 9.70976   37.54749 16.61551 1.000 47.42350  ? 106 ASN   A CB  1 
ATOM   719  C  CG  . ASN   A 1 99  ? 9.81450   37.53033 15.10288 1.000 49.74407  ? 106 ASN   A CG  1 
ATOM   720  O  OD1 . ASN   A 1 99  ? 10.84798  37.88940 14.53669 1.000 51.30634  ? 106 ASN   A OD1 1 
ATOM   721  N  ND2 . ASN   A 1 99  ? 8.74234   37.11443 14.43977 1.000 52.53143  ? 106 ASN   A ND2 1 
ATOM   722  N  N   . LEU   A 1 100 ? 10.10601  36.14324 19.32197 1.000 43.53290  ? 107 LEU   A N   1 
ATOM   723  C  CA  . LEU   A 1 100 ? 9.81681   36.11892 20.75260 1.000 45.97955  ? 107 LEU   A CA  1 
ATOM   724  C  C   . LEU   A 1 100 ? 11.07026  35.87151 21.58155 1.000 44.00780  ? 107 LEU   A C   1 
ATOM   725  O  O   . LEU   A 1 100 ? 11.14243  36.30973 22.73512 1.000 49.38292  ? 107 LEU   A O   1 
ATOM   726  C  CB  . LEU   A 1 100 ? 8.75660   35.06363 21.06060 1.000 40.53160  ? 107 LEU   A CB  1 
ATOM   727  C  CG  . LEU   A 1 100 ? 7.36707   35.35141 20.48751 1.000 44.95529  ? 107 LEU   A CG  1 
ATOM   728  C  CD1 . LEU   A 1 100 ? 6.35664   34.34250 21.00300 1.000 44.86471  ? 107 LEU   A CD1 1 
ATOM   729  C  CD2 . LEU   A 1 100 ? 6.93124   36.77326 20.81389 1.000 43.07096  ? 107 LEU   A CD2 1 
ATOM   730  N  N   . GLY   A 1 101 ? 12.06176  35.17746 21.01974 1.000 44.26075  ? 108 GLY   A N   1 
ATOM   731  C  CA  . GLY   A 1 101 ? 13.31883  35.00378 21.72504 1.000 48.61216  ? 108 GLY   A CA  1 
ATOM   732  C  C   . GLY   A 1 101 ? 14.06996  36.30422 21.91947 1.000 44.98184  ? 108 GLY   A C   1 
ATOM   733  O  O   . GLY   A 1 101 ? 14.76248  36.48018 22.92617 1.000 47.26818  ? 108 GLY   A O   1 
ATOM   734  N  N   . THR   A 1 102 ? 13.94626  37.23106 20.96652 1.000 48.03352  ? 109 THR   A N   1 
ATOM   735  C  CA  . THR   A 1 102 ? 14.57855  38.53706 21.11855 1.000 48.84751  ? 109 THR   A CA  1 
ATOM   736  C  C   . THR   A 1 102 ? 13.93924  39.32553 22.25440 1.000 46.78819  ? 109 THR   A C   1 
ATOM   737  O  O   . THR   A 1 102 ? 14.64242  39.95161 23.05604 1.000 47.66128  ? 109 THR   A O   1 
ATOM   738  C  CB  . THR   A 1 102 ? 14.49468  39.31747 19.80625 1.000 50.70260  ? 109 THR   A CB  1 
ATOM   739  O  OG1 . THR   A 1 102 ? 15.03016  38.52089 18.74194 1.000 50.05042  ? 109 THR   A OG1 1 
ATOM   740  C  CG2 . THR   A 1 102 ? 15.28177  40.61653 19.90431 1.000 56.43374  ? 109 THR   A CG2 1 
ATOM   741  N  N   . ILE   A 1 103 ? 12.60764  39.30351 22.34119 1.000 44.73165  ? 110 ILE   A N   1 
ATOM   742  C  CA  . ILE   A 1 103 ? 11.92609  39.95277 23.45619 1.000 43.70129  ? 110 ILE   A CA  1 
ATOM   743  C  C   . ILE   A 1 103 ? 12.21306  39.21172 24.75647 1.000 46.52121  ? 110 ILE   A C   1 
ATOM   744  O  O   . ILE   A 1 103 ? 12.36702  39.82767 25.81877 1.000 45.34867  ? 110 ILE   A O   1 
ATOM   745  C  CB  . ILE   A 1 103 ? 10.41481  40.04850 23.17224 1.000 48.36591  ? 110 ILE   A CB  1 
ATOM   746  C  CG1 . ILE   A 1 103 ? 10.15312  40.97091 21.97962 1.000 52.55658  ? 110 ILE   A CG1 1 
ATOM   747  C  CG2 . ILE   A 1 103 ? 9.66138   40.54645 24.39620 1.000 48.55121  ? 110 ILE   A CG2 1 
ATOM   748  C  CD1 . ILE   A 1 103 ? 9.08161   40.46450 21.03862 1.000 52.04719  ? 110 ILE   A CD1 1 
ATOM   749  N  N   . ALA   A 1 104 ? 12.30731  37.88072 24.69243 1.000 42.64232  ? 111 ALA   A N   1 
ATOM   750  C  CA  . ALA   A 1 104 ? 12.58880  37.10180 25.89378 1.000 44.76395  ? 111 ALA   A CA  1 
ATOM   751  C  C   . ALA   A 1 104 ? 13.99180  37.37713 26.42026 1.000 48.21998  ? 111 ALA   A C   1 
ATOM   752  O  O   . ALA   A 1 104 ? 14.20592  37.40806 27.63672 1.000 47.26437  ? 111 ALA   A O   1 
ATOM   753  C  CB  . ALA   A 1 104 ? 12.40667  35.61092 25.61174 1.000 41.13034  ? 111 ALA   A CB  1 
ATOM   754  N  N   . LYS   A 1 105 ? 14.95911  37.58359 25.52348 1.000 46.48234  ? 112 LYS   A N   1 
ATOM   755  C  CA  . LYS   A 1 105 ? 16.33501  37.80872 25.95799 1.000 49.43446  ? 112 LYS   A CA  1 
ATOM   756  C  C   . LYS   A 1 105 ? 16.45772  39.10375 26.75172 1.000 46.17083  ? 112 LYS   A C   1 
ATOM   757  O  O   . LYS   A 1 105 ? 17.05111  39.12722 27.83679 1.000 50.76806  ? 112 LYS   A O   1 
ATOM   758  C  CB  . LYS   A 1 105 ? 17.27171  37.82393 24.74954 1.000 49.00414  ? 112 LYS   A CB  1 
ATOM   759  C  CG  . LYS   A 1 105 ? 18.72314  38.10808 25.09998 1.000 49.15017  ? 112 LYS   A CG  1 
ATOM   760  C  CD  . LYS   A 1 105 ? 19.57109  38.28459 23.85232 1.000 49.78029  ? 112 LYS   A CD  1 
ATOM   761  C  CE  . LYS   A 1 105 ? 20.93846  37.64604 24.02141 1.000 55.73342  ? 112 LYS   A CE  1 
ATOM   762  N  NZ  . LYS   A 1 105 ? 22.02594  38.57936 23.62238 1.000 57.03673  ? 112 LYS   A NZ  1 
ATOM   763  N  N   . SER   A 1 106 ? 15.89947  40.19623 26.22404 1.000 46.93230  ? 113 SER   A N   1 
ATOM   764  C  CA  . SER   A 1 106 ? 15.96527  41.47274 26.92709 1.000 49.79246  ? 113 SER   A CA  1 
ATOM   765  C  C   . SER   A 1 106 ? 15.14227  41.43855 28.20915 1.000 48.63471  ? 113 SER   A C   1 
ATOM   766  O  O   . SER   A 1 106 ? 15.52940  42.03771 29.21896 1.000 49.26892  ? 113 SER   A O   1 
ATOM   767  C  CB  . SER   A 1 106 ? 15.49236  42.59974 26.00847 1.000 52.12676  ? 113 SER   A CB  1 
ATOM   768  O  OG  . SER   A 1 106 ? 14.08012  42.71992 26.03232 1.000 54.86458  ? 113 SER   A OG  1 
ATOM   769  N  N   . GLY   A 1 107 ? 14.01035  40.73239 28.19146 1.000 48.07491  ? 114 GLY   A N   1 
ATOM   770  C  CA  . GLY   A 1 107 ? 13.18508  40.65105 29.38448 1.000 47.23039  ? 114 GLY   A CA  1 
ATOM   771  C  C   . GLY   A 1 107 ? 13.77211  39.74416 30.44994 1.000 48.39892  ? 114 GLY   A C   1 
ATOM   772  O  O   . GLY   A 1 107 ? 13.63669  40.01436 31.64578 1.000 45.88017  ? 114 GLY   A O   1 
ATOM   773  N  N   . THR   A 1 108 ? 14.41735  38.65307 30.03228 1.000 45.75259  ? 115 THR   A N   1 
ATOM   774  C  CA  . THR   A 1 108 ? 15.04516  37.75339 30.99598 1.000 47.87104  ? 115 THR   A CA  1 
ATOM   775  C  C   . THR   A 1 108 ? 16.20244  38.44035 31.71138 1.000 47.50391  ? 115 THR   A C   1 
ATOM   776  O  O   . THR   A 1 108 ? 16.32782  38.34998 32.93830 1.000 53.60979  ? 115 THR   A O   1 
ATOM   777  C  CB  . THR   A 1 108 ? 15.52534  36.48231 30.29260 1.000 47.27318  ? 115 THR   A CB  1 
ATOM   778  O  OG1 . THR   A 1 108 ? 14.39830  35.67101 29.94397 1.000 46.78189  ? 115 THR   A OG1 1 
ATOM   779  C  CG2 . THR   A 1 108 ? 16.45779  35.68238 31.19174 1.000 49.48955  ? 115 THR   A CG2 1 
ATOM   780  N  N   . LYS   A 1 109 ? 17.06054  39.13354 30.95806 1.000 45.57541  ? 116 LYS   A N   1 
ATOM   781  C  CA  . LYS   A 1 109 ? 18.19909  39.81938 31.56135 1.000 48.70103  ? 116 LYS   A CA  1 
ATOM   782  C  C   . LYS   A 1 109 ? 17.74553  40.83560 32.60255 1.000 52.57289  ? 116 LYS   A C   1 
ATOM   783  O  O   . LYS   A 1 109 ? 18.35294  40.95256 33.67326 1.000 55.83574  ? 116 LYS   A O   1 
ATOM   784  C  CB  . LYS   A 1 109 ? 19.03193  40.49655 30.47306 1.000 48.09300  ? 116 LYS   A CB  1 
ATOM   785  C  CG  . LYS   A 1 109 ? 20.33526  41.09660 30.96475 1.000 64.39621  ? 116 LYS   A CG  1 
ATOM   786  C  CD  . LYS   A 1 109 ? 20.77622  42.24848 30.07730 1.000 70.05384  ? 116 LYS   A CD  1 
ATOM   787  C  CE  . LYS   A 1 109 ? 21.83842  43.09462 30.75861 1.000 73.33410  ? 116 LYS   A CE  1 
ATOM   788  N  NZ  . LYS   A 1 109 ? 21.34104  44.46020 31.08750 1.000 80.91413  ? 116 LYS   A NZ  1 
ATOM   789  N  N   . ALA   A 1 110 ? 16.67223  41.57333 32.31021 1.000 48.85201  ? 117 ALA   A N   1 
ATOM   790  C  CA  . ALA   A 1 110 ? 16.16562  42.54979 33.26858 1.000 51.41023  ? 117 ALA   A CA  1 
ATOM   791  C  C   . ALA   A 1 110 ? 15.52279  41.86470 34.46829 1.000 48.75089  ? 117 ALA   A C   1 
ATOM   792  O  O   . ALA   A 1 110 ? 15.64957  42.33963 35.60271 1.000 56.65042  ? 117 ALA   A O   1 
ATOM   793  C  CB  . ALA   A 1 110 ? 15.16948  43.48692 32.58615 1.000 48.63717  ? 117 ALA   A CB  1 
ATOM   794  N  N   . PHE   A 1 111 ? 14.82890  40.74715 34.23847 1.000 46.94209  ? 118 PHE   A N   1 
ATOM   795  C  CA  . PHE   A 1 111 ? 14.19199  40.02974 35.33893 1.000 49.99606  ? 118 PHE   A CA  1 
ATOM   796  C  C   . PHE   A 1 111 ? 15.22724  39.48154 36.31061 1.000 49.75810  ? 118 PHE   A C   1 
ATOM   797  O  O   . PHE   A 1 111 ? 15.00055  39.45639 37.52600 1.000 49.58066  ? 118 PHE   A O   1 
ATOM   798  C  CB  . PHE   A 1 111 ? 13.31914  38.89965 34.78930 1.000 45.00764  ? 118 PHE   A CB  1 
ATOM   799  C  CG  . PHE   A 1 111 ? 12.55543  38.14670 35.84375 1.000 48.53725  ? 118 PHE   A CG  1 
ATOM   800  C  CD1 . PHE   A 1 111 ? 12.02576  38.80193 36.94327 1.000 49.44262  ? 118 PHE   A CD1 1 
ATOM   801  C  CD2 . PHE   A 1 111 ? 12.37148  36.77774 35.73479 1.000 49.17942  ? 118 PHE   A CD2 1 
ATOM   802  C  CE1 . PHE   A 1 111 ? 11.32502  38.10790 37.91414 1.000 49.38061  ? 118 PHE   A CE1 1 
ATOM   803  C  CE2 . PHE   A 1 111 ? 11.67237  36.07815 36.70303 1.000 48.23162  ? 118 PHE   A CE2 1 
ATOM   804  C  CZ  . PHE   A 1 111 ? 11.14854  36.74447 37.79316 1.000 49.26412  ? 118 PHE   A CZ  1 
ATOM   805  N  N   . MET   A 1 112 ? 16.37859  39.05478 35.79729 1.000 49.20257  ? 119 MET   A N   1 
ATOM   806  C  CA  . MET   A 1 112 ? 17.36731  38.42624 36.66099 1.000 54.72445  ? 119 MET   A CA  1 
ATOM   807  C  C   . MET   A 1 112 ? 18.17062  39.45124 37.44690 1.000 53.47278  ? 119 MET   A C   1 
ATOM   808  O  O   . MET   A 1 112 ? 18.62929  39.15286 38.55506 1.000 63.57465  ? 119 MET   A O   1 
ATOM   809  C  CB  . MET   A 1 112 ? 18.28299  37.53485 35.82837 1.000 54.74568  ? 119 MET   A CB  1 
ATOM   810  C  CG  . MET   A 1 112 ? 17.49898  36.46753 35.09274 1.000 55.17434  ? 119 MET   A CG  1 
ATOM   811  S  SD  . MET   A 1 112 ? 17.47805  34.90200 35.96949 1.000 69.34565  ? 119 MET   A SD  1 
ATOM   812  C  CE  . MET   A 1 112 ? 18.59671  33.95635 34.95479 1.000 59.02658  ? 119 MET   A CE  1 
ATOM   813  N  N   . GLU   A 1 113 ? 18.35569  40.65263 36.89662 1.000 58.52937  ? 120 GLU   A N   1 
ATOM   814  C  CA  . GLU   A 1 113 ? 18.92088  41.73752 37.68995 1.000 61.16457  ? 120 GLU   A CA  1 
ATOM   815  C  C   . GLU   A 1 113 ? 18.00030  42.09408 38.84823 1.000 62.91144  ? 120 GLU   A C   1 
ATOM   816  O  O   . GLU   A 1 113 ? 18.46355  42.34986 39.96596 1.000 66.98592  ? 120 GLU   A O   1 
ATOM   817  C  CB  . GLU   A 1 113 ? 19.16854  42.96442 36.81302 1.000 63.66091  ? 120 GLU   A CB  1 
ATOM   818  C  CG  . GLU   A 1 113 ? 20.26441  42.79762 35.78066 1.000 74.31469  ? 120 GLU   A CG  1 
ATOM   819  C  CD  . GLU   A 1 113 ? 20.25032  43.90679 34.74912 1.000 90.28167  ? 120 GLU   A CD  1 
ATOM   820  O  OE1 . GLU   A 1 113 ? 21.04985  43.84376 33.79326 1.000 93.86832  ? 120 GLU   A OE1 1 
ATOM   821  O  OE2 . GLU   A 1 113 ? 19.43709  44.84430 34.89598 1.000 99.41897  ? 120 GLU   A OE2 1 
ATOM   822  N  N   . ALA   A 1 114 ? 16.68815  42.10772 38.59939 1.000 57.73442  ? 121 ALA   A N   1 
ATOM   823  C  CA  . ALA   A 1 114 ? 15.73664  42.44990 39.65060 1.000 62.59594  ? 121 ALA   A CA  1 
ATOM   824  C  C   . ALA   A 1 114 ? 15.67779  41.36722 40.72093 1.000 60.74865  ? 121 ALA   A C   1 
ATOM   825  O  O   . ALA   A 1 114 ? 15.53225  41.67265 41.91037 1.000 67.27039  ? 121 ALA   A O   1 
ATOM   826  C  CB  . ALA   A 1 114 ? 14.35261  42.68715 39.04749 1.000 56.15094  ? 121 ALA   A CB  1 
ATOM   827  N  N   . LEU   A 1 115 ? 15.79131  40.09708 40.31970 1.000 57.64553  ? 122 LEU   A N   1 
ATOM   828  C  CA  . LEU   A 1 115 ? 15.74876  39.00782 41.29070 1.000 57.29747  ? 122 LEU   A CA  1 
ATOM   829  C  C   . LEU   A 1 115 ? 16.88669  39.10760 42.29728 1.000 67.90866  ? 122 LEU   A C   1 
ATOM   830  O  O   . LEU   A 1 115 ? 16.73190  38.69493 43.45231 1.000 73.49137  ? 122 LEU   A O   1 
ATOM   831  C  CB  . LEU   A 1 115 ? 15.79210  37.65917 40.57261 1.000 56.40395  ? 122 LEU   A CB  1 
ATOM   832  C  CG  . LEU   A 1 115 ? 14.48168  37.19030 39.93657 1.000 52.84136  ? 122 LEU   A CG  1 
ATOM   833  C  CD1 . LEU   A 1 115 ? 14.73391  36.05304 38.95905 1.000 52.27189  ? 122 LEU   A CD1 1 
ATOM   834  C  CD2 . LEU   A 1 115 ? 13.48589  36.77190 41.00649 1.000 52.27456  ? 122 LEU   A CD2 1 
ATOM   835  N  N   . GLN   A 1 116 ? 18.03227  39.64959 41.88390 1.000 67.33815  ? 123 GLN   A N   1 
ATOM   836  C  CA  . GLN   A 1 116 ? 19.12952  39.87673 42.81381 1.000 73.34312  ? 123 GLN   A CA  1 
ATOM   837  C  C   . GLN   A 1 116 ? 18.94389  41.14404 43.63571 1.000 75.70846  ? 123 GLN   A C   1 
ATOM   838  O  O   . GLN   A 1 116 ? 19.62209  41.30949 44.65564 1.000 78.52369  ? 123 GLN   A O   1 
ATOM   839  C  CB  . GLN   A 1 116 ? 20.45796  39.94525 42.05822 1.000 75.23476  ? 123 GLN   A CB  1 
ATOM   840  C  CG  . GLN   A 1 116 ? 20.79514  38.68264 41.28742 1.000 76.68821  ? 123 GLN   A CG  1 
ATOM   841  C  CD  . GLN   A 1 116 ? 22.05649  38.01354 41.79504 1.000 89.92884  ? 123 GLN   A CD  1 
ATOM   842  O  OE1 . GLN   A 1 116 ? 22.86770  38.63224 42.48475 1.000 89.49835  ? 123 GLN   A OE1 1 
ATOM   843  N  NE2 . GLN   A 1 116 ? 22.22665  36.74074 41.45855 1.000 96.54020  ? 123 GLN   A NE2 1 
ATOM   844  N  N   . ALA   A 1 117 ? 18.04388  42.03630 43.21881 1.000 75.05612  ? 124 ALA   A N   1 
ATOM   845  C  CA  . ALA   A 1 117 ? 17.78288  43.28628 43.92120 1.000 74.84777  ? 124 ALA   A CA  1 
ATOM   846  C  C   . ALA   A 1 117 ? 16.53592  43.21064 44.79719 1.000 79.10441  ? 124 ALA   A C   1 
ATOM   847  O  O   . ALA   A 1 117 ? 15.92726  44.24282 45.10133 1.000 85.66774  ? 124 ALA   A O   1 
ATOM   848  C  CB  . ALA   A 1 117 ? 17.66525  44.43942 42.92473 1.000 75.37002  ? 124 ALA   A CB  1 
ATOM   849  N  N   . GLY   A 1 118 ? 16.13772  42.00451 45.20310 1.000 77.84340  ? 125 GLY   A N   1 
ATOM   850  C  CA  . GLY   A 1 118 ? 15.03997  41.80545 46.12556 1.000 82.39668  ? 125 GLY   A CA  1 
ATOM   851  C  C   . GLY   A 1 118 ? 13.77772  41.24808 45.50089 1.000 70.84383  ? 125 GLY   A C   1 
ATOM   852  O  O   . GLY   A 1 118 ? 12.95567  40.66358 46.21983 1.000 75.55314  ? 125 GLY   A O   1 
ATOM   853  N  N   . ALA   A 1 119 ? 13.59596  41.41076 44.19211 1.000 70.25807  ? 126 ALA   A N   1 
ATOM   854  C  CA  . ALA   A 1 119 ? 12.37666  40.95349 43.54250 1.000 68.39239  ? 126 ALA   A CA  1 
ATOM   855  C  C   . ALA   A 1 119 ? 12.26420  39.43291 43.61256 1.000 69.52904  ? 126 ALA   A C   1 
ATOM   856  O  O   . ALA   A 1 119 ? 13.25673  38.71034 43.73838 1.000 71.96934  ? 126 ALA   A O   1 
ATOM   857  C  CB  . ALA   A 1 119 ? 12.33698  41.41767 42.08647 1.000 59.76724  ? 126 ALA   A CB  1 
ATOM   858  N  N   . ASP   A 1 120 ? 11.03015  38.94994 43.53467 1.000 65.21910  ? 127 ASP   A N   1 
ATOM   859  C  CA  . ASP   A 1 120 ? 10.73826  37.52627 43.58792 1.000 67.38989  ? 127 ASP   A CA  1 
ATOM   860  C  C   . ASP   A 1 120 ? 10.17749  37.05721 42.24741 1.000 62.57947  ? 127 ASP   A C   1 
ATOM   861  O  O   . ASP   A 1 120 ? 9.97213   37.84293 41.31711 1.000 60.35522  ? 127 ASP   A O   1 
ATOM   862  C  CB  . ASP   A 1 120 ? 9.77594   37.21521 44.73730 1.000 72.57551  ? 127 ASP   A CB  1 
ATOM   863  C  CG  . ASP   A 1 120 ? 8.41927   37.86219 44.55420 1.000 72.63314  ? 127 ASP   A CG  1 
ATOM   864  O  OD1 . ASP   A 1 120 ? 8.37313   39.07826 44.27676 1.000 73.81207  ? 127 ASP   A OD1 1 
ATOM   865  O  OD2 . ASP   A 1 120 ? 7.39842   37.15620 44.69094 1.000 74.00795  ? 127 ASP   A OD2 1 
ATOM   866  N  N   . ILE   A 1 121 ? 9.92651   35.74849 42.16290 1.000 61.51558  ? 128 ILE   A N   1 
ATOM   867  C  CA  . ILE   A 1 121 ? 9.53297   35.13271 40.89966 1.000 58.34149  ? 128 ILE   A CA  1 
ATOM   868  C  C   . ILE   A 1 121 ? 8.15491   35.61357 40.45579 1.000 61.33280  ? 128 ILE   A C   1 
ATOM   869  O  O   . ILE   A 1 121 ? 7.88087   35.70548 39.25222 1.000 60.71708  ? 128 ILE   A O   1 
ATOM   870  C  CB  . ILE   A 1 121 ? 9.59788   33.59799 41.03664 1.000 56.39151  ? 128 ILE   A CB  1 
ATOM   871  C  CG1 . ILE   A 1 121 ? 11.05225  33.12515 40.99484 1.000 61.73901  ? 128 ILE   A CG1 1 
ATOM   872  C  CG2 . ILE   A 1 121 ? 8.79104   32.90280 39.94708 1.000 54.05994  ? 128 ILE   A CG2 1 
ATOM   873  C  CD1 . ILE   A 1 121 ? 11.36620  32.02439 41.98445 1.000 63.51483  ? 128 ILE   A CD1 1 
ATOM   874  N  N   . SER   A 1 122 ? 7.27952   35.95986 41.40390 1.000 55.70056  ? 129 SER   A N   1 
ATOM   875  C  CA  . SER   A 1 122 ? 5.91012   36.33093 41.05984 1.000 58.08822  ? 129 SER   A CA  1 
ATOM   876  C  C   . SER   A 1 122 ? 5.83404   37.59457 40.21082 1.000 54.67239  ? 129 SER   A C   1 
ATOM   877  O  O   . SER   A 1 122 ? 4.79252   37.85107 39.59736 1.000 55.12112  ? 129 SER   A O   1 
ATOM   878  C  CB  . SER   A 1 122 ? 5.08039   36.51306 42.33154 1.000 57.28619  ? 129 SER   A CB  1 
ATOM   879  O  OG  . SER   A 1 122 ? 5.53294   37.62638 43.08080 1.000 64.35008  ? 129 SER   A OG  1 
ATOM   880  N  N   . MET   A 1 123 ? 6.90222   38.38891 40.15940 1.000 53.90239  ? 130 MET   A N   1 
ATOM   881  C  CA  . MET   A 1 123 ? 6.93455   39.59995 39.35210 1.000 53.19605  ? 130 MET   A CA  1 
ATOM   882  C  C   . MET   A 1 123 ? 7.42914   39.34289 37.93325 1.000 52.86005  ? 130 MET   A C   1 
ATOM   883  O  O   . MET   A 1 123 ? 7.81187   40.29080 37.23743 1.000 49.78623  ? 130 MET   A O   1 
ATOM   884  C  CB  . MET   A 1 123 ? 7.80487   40.65897 40.03124 1.000 50.89598  ? 130 MET   A CB  1 
ATOM   885  C  CG  . MET   A 1 123 ? 7.39388   40.95692 41.46255 1.000 64.07577  ? 130 MET   A CG  1 
ATOM   886  S  SD  . MET   A 1 123 ? 8.73957   41.63308 42.45065 1.000 66.35227  ? 130 MET   A SD  1 
ATOM   887  C  CE  . MET   A 1 123 ? 8.75208   43.32857 41.88382 1.000 63.02941  ? 130 MET   A CE  1 
ATOM   888  N  N   . ILE   A 1 124 ? 7.41749   38.08300 37.49038 1.000 45.80794  ? 131 ILE   A N   1 
ATOM   889  C  CA  . ILE   A 1 124 ? 7.96132   37.73118 36.18196 1.000 48.17984  ? 131 ILE   A CA  1 
ATOM   890  C  C   . ILE   A 1 124 ? 7.16892   38.38918 35.05906 1.000 44.57016  ? 131 ILE   A C   1 
ATOM   891  O  O   . ILE   A 1 124 ? 7.71657   38.67366 33.98656 1.000 44.06017  ? 131 ILE   A O   1 
ATOM   892  C  CB  . ILE   A 1 124 ? 8.00152   36.19534 36.03314 1.000 50.26488  ? 131 ILE   A CB  1 
ATOM   893  C  CG1 . ILE   A 1 124 ? 8.71794   35.78682 34.74414 1.000 45.96501  ? 131 ILE   A CG1 1 
ATOM   894  C  CG2 . ILE   A 1 124 ? 6.59556   35.60676 36.09497 1.000 45.84217  ? 131 ILE   A CG2 1 
ATOM   895  C  CD1 . ILE   A 1 124 ? 8.91551   34.29272 34.61071 1.000 45.58154  ? 131 ILE   A CD1 1 
ATOM   896  N  N   . GLY   A 1 125 ? 5.88129   38.65976 35.28510 1.000 48.96904  ? 132 GLY   A N   1 
ATOM   897  C  CA  . GLY   A 1 125 ? 5.05941   39.24000 34.23706 1.000 48.24293  ? 132 GLY   A CA  1 
ATOM   898  C  C   . GLY   A 1 125 ? 5.42044   40.67221 33.90242 1.000 45.54306  ? 132 GLY   A C   1 
ATOM   899  O  O   . GLY   A 1 125 ? 5.21299   41.11749 32.76985 1.000 50.54343  ? 132 GLY   A O   1 
ATOM   900  N  N   . GLN   A 1 126 ? 5.96526   41.41244 34.86979 1.000 47.94018  ? 133 GLN   A N   1 
ATOM   901  C  CA  . GLN   A 1 126 ? 6.36182   42.79381 34.62413 1.000 46.06916  ? 133 GLN   A CA  1 
ATOM   902  C  C   . GLN   A 1 126 ? 7.52551   42.90999 33.64980 1.000 46.12068  ? 133 GLN   A C   1 
ATOM   903  O  O   . GLN   A 1 126 ? 7.86850   44.02898 33.25419 1.000 51.25220  ? 133 GLN   A O   1 
ATOM   904  C  CB  . GLN   A 1 126 ? 6.72688   43.47808 35.94183 1.000 46.52373  ? 133 GLN   A CB  1 
ATOM   905  C  CG  . GLN   A 1 126 ? 5.74510   43.21465 37.06903 1.000 53.03906  ? 133 GLN   A CG  1 
ATOM   906  C  CD  . GLN   A 1 126 ? 6.03798   44.04922 38.29887 1.000 63.31156  ? 133 GLN   A CD  1 
ATOM   907  O  OE1 . GLN   A 1 126 ? 6.46709   45.19922 38.19581 1.000 64.65287  ? 133 GLN   A OE1 1 
ATOM   908  N  NE2 . GLN   A 1 126 ? 5.80886   43.47256 39.47303 1.000 60.57108  ? 133 GLN   A NE2 1 
ATOM   909  N  N   . PHE   A 1 127 ? 8.13544   41.79292 33.25671 1.000 46.18582  ? 134 PHE   A N   1 
ATOM   910  C  CA  . PHE   A 1 127 ? 9.25867   41.79007 32.33032 1.000 45.04209  ? 134 PHE   A CA  1 
ATOM   911  C  C   . PHE   A 1 127 ? 8.92052   41.11082 31.00945 1.000 44.64192  ? 134 PHE   A C   1 
ATOM   912  O  O   . PHE   A 1 127 ? 9.80607   40.94326 30.16400 1.000 46.37802  ? 134 PHE   A O   1 
ATOM   913  C  CB  . PHE   A 1 127 ? 10.47217  41.12168 32.98115 1.000 44.35872  ? 134 PHE   A CB  1 
ATOM   914  C  CG  . PHE   A 1 127 ? 10.87453  41.74584 34.28829 1.000 46.66866  ? 134 PHE   A CG  1 
ATOM   915  C  CD1 . PHE   A 1 127 ? 10.28947  41.33913 35.47634 1.000 44.38899  ? 134 PHE   A CD1 1 
ATOM   916  C  CD2 . PHE   A 1 127 ? 11.83129  42.74684 34.32746 1.000 44.28307  ? 134 PHE   A CD2 1 
ATOM   917  C  CE1 . PHE   A 1 127 ? 10.65328  41.91547 36.67862 1.000 46.57112  ? 134 PHE   A CE1 1 
ATOM   918  C  CE2 . PHE   A 1 127 ? 12.20070  43.32632 35.52717 1.000 47.47436  ? 134 PHE   A CE2 1 
ATOM   919  C  CZ  . PHE   A 1 127 ? 11.61061  42.90971 36.70400 1.000 49.48408  ? 134 PHE   A CZ  1 
ATOM   920  N  N   . GLY   A 1 128 ? 7.66382   40.71584 30.81369 1.000 42.71562  ? 135 GLY   A N   1 
ATOM   921  C  CA  . GLY   A 1 128 ? 7.22324   40.14825 29.55680 1.000 42.05857  ? 135 GLY   A CA  1 
ATOM   922  C  C   . GLY   A 1 128 ? 7.64947   38.72322 29.29311 1.000 45.16624  ? 135 GLY   A C   1 
ATOM   923  O  O   . GLY   A 1 128 ? 7.53906   38.26588 28.15018 1.000 46.67512  ? 135 GLY   A O   1 
ATOM   924  N  N   . VAL   A 1 129 ? 8.12774   38.00151 30.30413 1.000 44.33669  ? 136 VAL   A N   1 
ATOM   925  C  CA  . VAL   A 1 129 ? 8.58648   36.63112 30.10621 1.000 40.46039  ? 136 VAL   A CA  1 
ATOM   926  C  C   . VAL   A 1 129 ? 7.79486   35.68898 31.00411 1.000 42.84154  ? 136 VAL   A C   1 
ATOM   927  O  O   . VAL   A 1 129 ? 8.32179   34.67943 31.48440 1.000 40.79873  ? 136 VAL   A O   1 
ATOM   928  C  CB  . VAL   A 1 129 ? 10.09974  36.51073 30.36437 1.000 44.26561  ? 136 VAL   A CB  1 
ATOM   929  C  CG1 . VAL   A 1 129 ? 10.87490  37.24134 29.28016 1.000 40.11043  ? 136 VAL   A CG1 1 
ATOM   930  C  CG2 . VAL   A 1 129 ? 10.45355  37.06951 31.73245 1.000 42.73077  ? 136 VAL   A CG2 1 
ATOM   931  N  N   . GLY   A 1 130 ? 6.51293   35.99903 31.21168 1.000 44.00263  ? 137 GLY   A N   1 
ATOM   932  C  CA  . GLY   A 1 130 ? 5.68281   35.22583 32.11999 1.000 42.47301  ? 137 GLY   A CA  1 
ATOM   933  C  C   . GLY   A 1 130 ? 5.40802   33.80284 31.67626 1.000 42.28313  ? 137 GLY   A C   1 
ATOM   934  O  O   . GLY   A 1 130 ? 4.96134   32.99104 32.49334 1.000 39.69595  ? 137 GLY   A O   1 
ATOM   935  N  N   . PHE   A 1 131 ? 5.66041   33.47970 30.40452 1.000 37.64344  ? 138 PHE   A N   1 
ATOM   936  C  CA  . PHE   A 1 131 ? 5.39678   32.12495 29.92476 1.000 41.69636  ? 138 PHE   A CA  1 
ATOM   937  C  C   . PHE   A 1 131 ? 6.28066   31.10335 30.62942 1.000 41.63416  ? 138 PHE   A C   1 
ATOM   938  O  O   . PHE   A 1 131 ? 5.84730   29.97539 30.89417 1.000 39.26954  ? 138 PHE   A O   1 
ATOM   939  C  CB  . PHE   A 1 131 ? 5.59961   32.04721 28.41108 1.000 39.27087  ? 138 PHE   A CB  1 
ATOM   940  C  CG  . PHE   A 1 131 ? 5.68013   30.64099 27.88187 1.000 41.20536  ? 138 PHE   A CG  1 
ATOM   941  C  CD1 . PHE   A 1 131 ? 4.53888   29.86399 27.76069 1.000 38.67184  ? 138 PHE   A CD1 1 
ATOM   942  C  CD2 . PHE   A 1 131 ? 6.89918   30.09412 27.51245 1.000 40.37790  ? 138 PHE   A CD2 1 
ATOM   943  C  CE1 . PHE   A 1 131 ? 4.61215   28.56910 27.27642 1.000 41.11366  ? 138 PHE   A CE1 1 
ATOM   944  C  CE2 . PHE   A 1 131 ? 6.97899   28.80064 27.02949 1.000 42.85710  ? 138 PHE   A CE2 1 
ATOM   945  C  CZ  . PHE   A 1 131 ? 5.83431   28.03747 26.91059 1.000 43.62203  ? 138 PHE   A CZ  1 
ATOM   946  N  N   . TYR   A 1 132 ? 7.52341   31.47959 30.94324 1.000 38.62579  ? 139 TYR   A N   1 
ATOM   947  C  CA  . TYR   A 1 132 ? 8.44889   30.56397 31.60101 1.000 40.35532  ? 139 TYR   A CA  1 
ATOM   948  C  C   . TYR   A 1 132 ? 7.98879   30.15960 32.99442 1.000 39.05936  ? 139 TYR   A C   1 
ATOM   949  O  O   . TYR   A 1 132 ? 8.52755   29.19546 33.54973 1.000 39.08099  ? 139 TYR   A O   1 
ATOM   950  C  CB  . TYR   A 1 132 ? 9.84282   31.19099 31.67696 1.000 41.09783  ? 139 TYR   A CB  1 
ATOM   951  C  CG  . TYR   A 1 132 ? 10.45681  31.47385 30.32466 1.000 44.08480  ? 139 TYR   A CG  1 
ATOM   952  C  CD1 . TYR   A 1 132 ? 10.45068  30.51054 29.32446 1.000 42.82307  ? 139 TYR   A CD1 1 
ATOM   953  C  CD2 . TYR   A 1 132 ? 11.04793  32.70041 30.04950 1.000 42.82163  ? 139 TYR   A CD2 1 
ATOM   954  C  CE1 . TYR   A 1 132 ? 11.01054  30.76116 28.08621 1.000 38.86707  ? 139 TYR   A CE1 1 
ATOM   955  C  CE2 . TYR   A 1 132 ? 11.61433  32.95919 28.81392 1.000 46.24860  ? 139 TYR   A CE2 1 
ATOM   956  C  CZ  . TYR   A 1 132 ? 11.58959  31.98656 27.83603 1.000 44.57899  ? 139 TYR   A CZ  1 
ATOM   957  O  OH  . TYR   A 1 132 ? 12.14849  32.23769 26.60410 1.000 50.40334  ? 139 TYR   A OH  1 
ATOM   958  N  N   . SER   A 1 133 ? 7.01353   30.86540 33.57029 1.000 38.52530  ? 140 SER   A N   1 
ATOM   959  C  CA  . SER   A 1 133 ? 6.44631   30.47041 34.85257 1.000 40.24153  ? 140 SER   A CA  1 
ATOM   960  C  C   . SER   A 1 133 ? 5.66624   29.16655 34.77019 1.000 40.81798  ? 140 SER   A C   1 
ATOM   961  O  O   . SER   A 1 133 ? 5.32192   28.60510 35.81563 1.000 45.78840  ? 140 SER   A O   1 
ATOM   962  C  CB  . SER   A 1 133 ? 5.53890   31.57812 35.38762 1.000 42.07478  ? 140 SER   A CB  1 
ATOM   963  O  OG  . SER   A 1 133 ? 4.35680   31.67862 34.61274 1.000 42.75521  ? 140 SER   A OG  1 
ATOM   964  N  N   . ALA   A 1 134 ? 5.37618   28.67888 33.56080 1.000 43.04195  ? 141 ALA   A N   1 
ATOM   965  C  CA  . ALA   A 1 134 ? 4.69006   27.39988 33.41961 1.000 39.84619  ? 141 ALA   A CA  1 
ATOM   966  C  C   . ALA   A 1 134 ? 5.51747   26.25646 33.98807 1.000 44.08687  ? 141 ALA   A C   1 
ATOM   967  O  O   . ALA   A 1 134 ? 4.95933   25.24496 34.42840 1.000 46.37597  ? 141 ALA   A O   1 
ATOM   968  C  CB  . ALA   A 1 134 ? 4.36550   27.13864 31.94901 1.000 41.54389  ? 141 ALA   A CB  1 
ATOM   969  N  N   . TYR   A 1 135 ? 6.84168   26.39841 33.99453 1.000 39.42076  ? 142 TYR   A N   1 
ATOM   970  C  CA  . TYR   A 1 135 ? 7.72569   25.36201 34.50863 1.000 42.83497  ? 142 TYR   A CA  1 
ATOM   971  C  C   . TYR   A 1 135 ? 7.80704   25.35332 36.02824 1.000 45.23445  ? 142 TYR   A C   1 
ATOM   972  O  O   . TYR   A 1 135 ? 8.54297   24.53399 36.58828 1.000 43.41573  ? 142 TYR   A O   1 
ATOM   973  C  CB  . TYR   A 1 135 ? 9.11708   25.52277 33.89528 1.000 42.15886  ? 142 TYR   A CB  1 
ATOM   974  C  CG  . TYR   A 1 135 ? 9.13034   25.17724 32.42610 1.000 43.40197  ? 142 TYR   A CG  1 
ATOM   975  C  CD1 . TYR   A 1 135 ? 9.37281   23.87778 32.00047 1.000 40.07831  ? 142 TYR   A CD1 1 
ATOM   976  C  CD2 . TYR   A 1 135 ? 8.85645   26.14178 31.46581 1.000 39.16378  ? 142 TYR   A CD2 1 
ATOM   977  C  CE1 . TYR   A 1 135 ? 9.37040   23.55482 30.65751 1.000 42.66901  ? 142 TYR   A CE1 1 
ATOM   978  C  CE2 . TYR   A 1 135 ? 8.84791   25.82834 30.12128 1.000 43.05676  ? 142 TYR   A CE2 1 
ATOM   979  C  CZ  . TYR   A 1 135 ? 9.10666   24.53390 29.72232 1.000 46.32946  ? 142 TYR   A CZ  1 
ATOM   980  O  OH  . TYR   A 1 135 ? 9.09961   24.21795 28.38314 1.000 46.77165  ? 142 TYR   A OH  1 
ATOM   981  N  N   . LEU   A 1 136 ? 7.07860   26.24369 36.70528 1.000 44.51610  ? 143 LEU   A N   1 
ATOM   982  C  CA  . LEU   A 1 136 ? 6.88925   26.09243 38.14304 1.000 49.86730  ? 143 LEU   A CA  1 
ATOM   983  C  C   . LEU   A 1 136 ? 6.09744   24.82963 38.45011 1.000 49.97049  ? 143 LEU   A C   1 
ATOM   984  O  O   . LEU   A 1 136 ? 6.33914   24.16383 39.46378 1.000 44.67345  ? 143 LEU   A O   1 
ATOM   985  C  CB  . LEU   A 1 136 ? 6.17459   27.31730 38.71547 1.000 42.82305  ? 143 LEU   A CB  1 
ATOM   986  C  CG  . LEU   A 1 136 ? 6.91716   28.65379 38.72746 1.000 44.40686  ? 143 LEU   A CG  1 
ATOM   987  C  CD1 . LEU   A 1 136 ? 5.94163   29.79067 38.98175 1.000 45.72002  ? 143 LEU   A CD1 1 
ATOM   988  C  CD2 . LEU   A 1 136 ? 8.01035   28.64361 39.78245 1.000 44.76794  ? 143 LEU   A CD2 1 
ATOM   989  N  N   . VAL   A 1 137 ? 5.15443   24.48046 37.57795 1.000 48.22427  ? 144 VAL   A N   1 
ATOM   990  C  CA  . VAL   A 1 137 ? 4.28083   23.33785 37.80305 1.000 52.77146  ? 144 VAL   A CA  1 
ATOM   991  C  C   . VAL   A 1 137 ? 4.41063   22.26250 36.73359 1.000 45.70806  ? 144 VAL   A C   1 
ATOM   992  O  O   . VAL   A 1 137 ? 3.93639   21.13591 36.95289 1.000 50.43746  ? 144 VAL   A O   1 
ATOM   993  C  CB  . VAL   A 1 137 ? 2.80894   23.78660 37.91988 1.000 46.68465  ? 144 VAL   A CB  1 
ATOM   994  C  CG1 . VAL   A 1 137 ? 2.63150   24.72659 39.10056 1.000 47.49855  ? 144 VAL   A CG1 1 
ATOM   995  C  CG2 . VAL   A 1 137 ? 2.35671   24.45224 36.62754 1.000 48.32939  ? 144 VAL   A CG2 1 
ATOM   996  N  N   . ALA   A 1 138 ? 5.02611   22.54690 35.59050 1.000 48.44921  ? 145 ALA   A N   1 
ATOM   997  C  CA  . ALA   A 1 138 ? 5.07609   21.61314 34.47591 1.000 45.47116  ? 145 ALA   A CA  1 
ATOM   998  C  C   . ALA   A 1 138 ? 6.49893   21.12249 34.25058 1.000 49.34255  ? 145 ALA   A C   1 
ATOM   999  O  O   . ALA   A 1 138 ? 7.45252   21.90694 34.28635 1.000 48.49422  ? 145 ALA   A O   1 
ATOM   1000 C  CB  . ALA   A 1 138 ? 4.54354   22.25978 33.19401 1.000 40.18129  ? 145 ALA   A CB  1 
ATOM   1001 N  N   . GLU   A 1 139 ? 6.63421   19.81711 34.02264 1.000 49.16215  ? 146 GLU   A N   1 
ATOM   1002 C  CA  . GLU   A 1 139 ? 7.90764   19.24222 33.61514 1.000 46.24219  ? 146 GLU   A CA  1 
ATOM   1003 C  C   . GLU   A 1 139 ? 8.10446   19.27379 32.10698 1.000 48.41948  ? 146 GLU   A C   1 
ATOM   1004 O  O   . GLU   A 1 139 ? 9.23741   19.11856 31.63839 1.000 47.52898  ? 146 GLU   A O   1 
ATOM   1005 C  CB  . GLU   A 1 139 ? 8.02309   17.79955 34.11615 1.000 47.83412  ? 146 GLU   A CB  1 
ATOM   1006 C  CG  . GLU   A 1 139 ? 7.18318   16.80493 33.33557 1.000 53.88491  ? 146 GLU   A CG  1 
ATOM   1007 C  CD  . GLU   A 1 139 ? 6.95556   15.51405 34.09499 1.000 68.82307  ? 146 GLU   A CD  1 
ATOM   1008 O  OE1 . GLU   A 1 139 ? 7.28742   15.46398 35.29873 1.000 71.68844  ? 146 GLU   A OE1 1 
ATOM   1009 O  OE2 . GLU   A 1 139 ? 6.44194   14.55015 33.48913 1.000 70.01018  ? 146 GLU   A OE2 1 
ATOM   1010 N  N   . LYS   A 1 140 ? 7.03214   19.47495 31.34360 1.000 46.45726  ? 147 LYS   A N   1 
ATOM   1011 C  CA  . LYS   A 1 140 ? 7.11472   19.58668 29.89331 1.000 46.35582  ? 147 LYS   A CA  1 
ATOM   1012 C  C   . LYS   A 1 140 ? 5.93258   20.41625 29.41774 1.000 44.87215  ? 147 LYS   A C   1 
ATOM   1013 O  O   . LYS   A 1 140 ? 4.80705   20.21059 29.88031 1.000 46.79604  ? 147 LYS   A O   1 
ATOM   1014 C  CB  . LYS   A 1 140 ? 7.10842   18.20550 29.22790 1.000 46.31409  ? 147 LYS   A CB  1 
ATOM   1015 C  CG  . LYS   A 1 140 ? 6.60455   18.20835 27.79393 1.000 47.38881  ? 147 LYS   A CG  1 
ATOM   1016 C  CD  . LYS   A 1 140 ? 7.18347   17.05423 26.99535 1.000 47.33322  ? 147 LYS   A CD  1 
ATOM   1017 C  CE  . LYS   A 1 140 ? 6.09025   16.10493 26.54175 1.000 53.85037  ? 147 LYS   A CE  1 
ATOM   1018 N  NZ  . LYS   A 1 140 ? 6.61468   15.06741 25.61426 1.000 64.02275  ? 147 LYS   A NZ  1 
ATOM   1019 N  N   . VAL   A 1 141 ? 6.18625   21.35326 28.50873 1.000 42.84358  ? 148 VAL   A N   1 
ATOM   1020 C  CA  . VAL   A 1 141 ? 5.15107   22.22308 27.96380 1.000 41.54884  ? 148 VAL   A CA  1 
ATOM   1021 C  C   . VAL   A 1 141 ? 5.09018   22.01913 26.45760 1.000 45.52205  ? 148 VAL   A C   1 
ATOM   1022 O  O   . VAL   A 1 141 ? 6.11444   22.11187 25.77080 1.000 43.94872  ? 148 VAL   A O   1 
ATOM   1023 C  CB  . VAL   A 1 141 ? 5.40679   23.70373 28.29992 1.000 42.63364  ? 148 VAL   A CB  1 
ATOM   1024 C  CG1 . VAL   A 1 141 ? 4.24343   24.55709 27.81969 1.000 41.29860  ? 148 VAL   A CG1 1 
ATOM   1025 C  CG2 . VAL   A 1 141 ? 5.62153   23.88177 29.79519 1.000 39.93051  ? 148 VAL   A CG2 1 
ATOM   1026 N  N   . THR   A 1 142 ? 3.89401   21.73555 25.95165 1.000 41.18765  ? 149 THR   A N   1 
ATOM   1027 C  CA  . THR   A 1 142 ? 3.63349   21.64088 24.52250 1.000 44.70644  ? 149 THR   A CA  1 
ATOM   1028 C  C   . THR   A 1 142 ? 2.70042   22.77331 24.12001 1.000 43.16594  ? 149 THR   A C   1 
ATOM   1029 O  O   . THR   A 1 142 ? 1.67089   22.99351 24.76740 1.000 46.32759  ? 149 THR   A O   1 
ATOM   1030 C  CB  . THR   A 1 142 ? 3.01461   20.28994 24.15971 1.000 50.48707  ? 149 THR   A CB  1 
ATOM   1031 O  OG1 . THR   A 1 142 ? 3.81990   19.23488 24.69955 1.000 48.34378  ? 149 THR   A OG1 1 
ATOM   1032 C  CG2 . THR   A 1 142 ? 2.92791   20.13541 22.64913 1.000 47.86446  ? 149 THR   A CG2 1 
ATOM   1033 N  N   . VAL   A 1 143 ? 3.06227   23.49036 23.06007 1.000 39.62620  ? 150 VAL   A N   1 
ATOM   1034 C  CA  . VAL   A 1 143 ? 2.31745   24.65927 22.60717 1.000 43.82558  ? 150 VAL   A CA  1 
ATOM   1035 C  C   . VAL   A 1 143 ? 1.89856   24.43837 21.16110 1.000 45.64486  ? 150 VAL   A C   1 
ATOM   1036 O  O   . VAL   A 1 143 ? 2.75067   24.33759 20.26916 1.000 45.21536  ? 150 VAL   A O   1 
ATOM   1037 C  CB  . VAL   A 1 143 ? 3.13959   25.94996 22.74481 1.000 44.12905  ? 150 VAL   A CB  1 
ATOM   1038 C  CG1 . VAL   A 1 143 ? 2.35927   27.13265 22.19595 1.000 40.32564  ? 150 VAL   A CG1 1 
ATOM   1039 C  CG2 . VAL   A 1 143 ? 3.51879   26.18418 24.19895 1.000 41.59346  ? 150 VAL   A CG2 1 
ATOM   1040 N  N   . ILE   A 1 144 ? 0.59126   24.36329 20.93297 1.000 44.80617  ? 151 ILE   A N   1 
ATOM   1041 C  CA  . ILE   A 1 144 ? 0.01551   24.33961 19.59411 1.000 40.53532  ? 151 ILE   A CA  1 
ATOM   1042 C  C   . ILE   A 1 144 ? -0.49172  25.74238 19.29083 1.000 43.47320  ? 151 ILE   A C   1 
ATOM   1043 O  O   . ILE   A 1 144 ? -1.30427  26.29160 20.04474 1.000 40.42963  ? 151 ILE   A O   1 
ATOM   1044 C  CB  . ILE   A 1 144 ? -1.11495  23.30409 19.48423 1.000 46.14612  ? 151 ILE   A CB  1 
ATOM   1045 C  CG1 . ILE   A 1 144 ? -0.69859  21.97895 20.12811 1.000 45.39415  ? 151 ILE   A CG1 1 
ATOM   1046 C  CG2 . ILE   A 1 144 ? -1.50432  23.09123 18.03053 1.000 44.98474  ? 151 ILE   A CG2 1 
ATOM   1047 C  CD1 . ILE   A 1 144 ? 0.53601   21.35688 19.51044 1.000 54.43742  ? 151 ILE   A CD1 1 
ATOM   1048 N  N   . THR   A 1 145 ? -0.01082  26.33094 18.19726 1.000 45.76982  ? 152 THR   A N   1 
ATOM   1049 C  CA  . THR   A 1 145 ? -0.36846  27.69809 17.84986 1.000 47.14993  ? 152 THR   A CA  1 
ATOM   1050 C  C   . THR   A 1 145 ? -0.70762  27.78730 16.36897 1.000 46.09410  ? 152 THR   A C   1 
ATOM   1051 O  O   . THR   A 1 145 ? -0.21276  27.00747 15.55052 1.000 46.43558  ? 152 THR   A O   1 
ATOM   1052 C  CB  . THR   A 1 145 ? 0.75720   28.68454 18.19584 1.000 42.68710  ? 152 THR   A CB  1 
ATOM   1053 O  OG1 . THR   A 1 145 ? 0.28929   30.02793 18.02237 1.000 43.78443  ? 152 THR   A OG1 1 
ATOM   1054 C  CG2 . THR   A 1 145 ? 1.97578   28.45144 17.31301 1.000 45.98065  ? 152 THR   A CG2 1 
ATOM   1055 N  N   . LYS   A 1 146 ? -1.56865  28.74820 16.03710 1.000 43.29734  ? 153 LYS   A N   1 
ATOM   1056 C  CA  . LYS   A 1 146 ? -1.99802  28.97869 14.66232 1.000 43.62031  ? 153 LYS   A CA  1 
ATOM   1057 C  C   . LYS   A 1 146 ? -2.18367  30.47270 14.45165 1.000 45.73324  ? 153 LYS   A C   1 
ATOM   1058 O  O   . LYS   A 1 146 ? -2.97128  31.10907 15.15906 1.000 42.65141  ? 153 LYS   A O   1 
ATOM   1059 C  CB  . LYS   A 1 146 ? -3.29590  28.22666 14.34957 1.000 46.70482  ? 153 LYS   A CB  1 
ATOM   1060 C  CG  . LYS   A 1 146 ? -3.86621  28.52365 12.97012 1.000 45.58925  ? 153 LYS   A CG  1 
ATOM   1061 C  CD  . LYS   A 1 146 ? -2.88691  28.14616 11.86998 1.000 42.53028  ? 153 LYS   A CD  1 
ATOM   1062 C  CE  . LYS   A 1 146 ? -3.52920  28.25942 10.49387 1.000 47.15794  ? 153 LYS   A CE  1 
ATOM   1063 N  NZ  . LYS   A 1 146 ? -3.56987  29.66476 10.00082 1.000 45.65837  ? 153 LYS   A NZ  1 
ATOM   1064 N  N   . HIS   A 1 147 ? -1.46072  31.02447 13.48290 1.000 43.14854  ? 154 HIS   A N   1 
ATOM   1065 C  CA  . HIS   A 1 147 ? -1.54968  32.42942 13.12086 1.000 42.56215  ? 154 HIS   A CA  1 
ATOM   1066 C  C   . HIS   A 1 147 ? -2.18290  32.55372 11.74131 1.000 45.06991  ? 154 HIS   A C   1 
ATOM   1067 O  O   . HIS   A 1 147 ? -2.02454  31.67431 10.89027 1.000 45.63076  ? 154 HIS   A O   1 
ATOM   1068 C  CB  . HIS   A 1 147 ? -0.16154  33.08058 13.13714 1.000 44.21916  ? 154 HIS   A CB  1 
ATOM   1069 C  CG  . HIS   A 1 147 ? -0.18405  34.57562 13.04567 1.000 43.42964  ? 154 HIS   A CG  1 
ATOM   1070 N  ND1 . HIS   A 1 147 ? -0.39055  35.24639 11.86062 1.000 42.74152  ? 154 HIS   A ND1 1 
ATOM   1071 C  CD2 . HIS   A 1 147 ? -0.01104  35.52843 13.99239 1.000 41.89859  ? 154 HIS   A CD2 1 
ATOM   1072 C  CE1 . HIS   A 1 147 ? -0.35138  36.54901 12.08089 1.000 42.35210  ? 154 HIS   A CE1 1 
ATOM   1073 N  NE2 . HIS   A 1 147 ? -0.12294  36.74649 13.36606 1.000 44.87181  ? 154 HIS   A NE2 1 
ATOM   1074 N  N   . ASN   A 1 148 ? -2.91388  33.65299 11.52933 1.000 44.25262  ? 155 ASN   A N   1 
ATOM   1075 C  CA  . ASN   A 1 148 ? -3.60103  33.85146 10.25523 1.000 43.94948  ? 155 ASN   A CA  1 
ATOM   1076 C  C   . ASN   A 1 148 ? -2.63252  33.85288 9.07861  1.000 44.08868  ? 155 ASN   A C   1 
ATOM   1077 O  O   . ASN   A 1 148 ? -3.02365  33.52268 7.95309  1.000 46.21454  ? 155 ASN   A O   1 
ATOM   1078 C  CB  . ASN   A 1 148 ? -4.39372  35.16010 10.27985 1.000 45.09564  ? 155 ASN   A CB  1 
ATOM   1079 C  CG  . ASN   A 1 148 ? -5.72934  35.02348 10.98529 1.000 45.60295  ? 155 ASN   A CG  1 
ATOM   1080 O  OD1 . ASN   A 1 148 ? -6.25067  33.92001 11.14658 1.000 49.07628  ? 155 ASN   A OD1 1 
ATOM   1081 N  ND2 . ASN   A 1 148 ? -6.29357  36.15009 11.40541 1.000 46.39449  ? 155 ASN   A ND2 1 
ATOM   1082 N  N   . ASP   A 1 149 ? -1.37192  34.20735 9.31600  1.000 44.58153  ? 156 ASP   A N   1 
ATOM   1083 C  CA  . ASP   A 1 149 ? -0.38568  34.36412 8.25703  1.000 48.95536  ? 156 ASP   A CA  1 
ATOM   1084 C  C   . ASP   A 1 149 ? 0.55444   33.17219 8.12582  1.000 46.46969  ? 156 ASP   A C   1 
ATOM   1085 O  O   . ASP   A 1 149 ? 1.49225   33.23008 7.32509  1.000 52.74774  ? 156 ASP   A O   1 
ATOM   1086 C  CB  . ASP   A 1 149 ? 0.43433   35.63757 8.49438  1.000 46.76584  ? 156 ASP   A CB  1 
ATOM   1087 C  CG  . ASP   A 1 149 ? -0.40696  36.89783 8.41336  1.000 54.33084  ? 156 ASP   A CG  1 
ATOM   1088 O  OD1 . ASP   A 1 149 ? -1.59698  36.79998 8.04694  1.000 51.82777  ? 156 ASP   A OD1 1 
ATOM   1089 O  OD2 . ASP   A 1 149 ? 0.12066   37.98669 8.72398  1.000 59.02548  ? 156 ASP   A OD2 1 
ATOM   1090 N  N   . ASP   A 1 150 ? 0.33433   32.09895 8.88207  1.000 44.81235  ? 157 ASP   A N   1 
ATOM   1091 C  CA  . ASP   A 1 150 ? 1.23339   30.95348 8.85896  1.000 46.76828  ? 157 ASP   A CA  1 
ATOM   1092 C  C   . ASP   A 1 150 ? 0.42558   29.67910 9.07201  1.000 47.81533  ? 157 ASP   A C   1 
ATOM   1093 O  O   . ASP   A 1 150 ? -0.79761  29.71099 9.23493  1.000 44.19964  ? 157 ASP   A O   1 
ATOM   1094 C  CB  . ASP   A 1 150 ? 2.33340   31.09717 9.91648  1.000 47.07920  ? 157 ASP   A CB  1 
ATOM   1095 C  CG  . ASP   A 1 150 ? 3.64979   30.48642 9.47614  1.000 47.22334  ? 157 ASP   A CG  1 
ATOM   1096 O  OD1 . ASP   A 1 150 ? 3.62704   29.57322 8.62389  1.000 52.24311  ? 157 ASP   A OD1 1 
ATOM   1097 O  OD2 . ASP   A 1 150 ? 4.70666   30.91598 9.98554  1.000 46.28927  ? 157 ASP   A OD2 1 
ATOM   1098 N  N   . GLU   A 1 151 ? 1.12565   28.54907 9.06412  1.000 47.87444  ? 158 GLU   A N   1 
ATOM   1099 C  CA  . GLU   A 1 151 ? 0.51531   27.25407 9.31259  1.000 47.92697  ? 158 GLU   A CA  1 
ATOM   1100 C  C   . GLU   A 1 151 ? 0.51091   26.94895 10.80844 1.000 48.58825  ? 158 GLU   A C   1 
ATOM   1101 O  O   . GLU   A 1 151 ? 1.06520   27.68759 11.62510 1.000 47.01124  ? 158 GLU   A O   1 
ATOM   1102 C  CB  . GLU   A 1 151 ? 1.25341   26.15521 8.54597  1.000 53.33226  ? 158 GLU   A CB  1 
ATOM   1103 C  CG  . GLU   A 1 151 ? 1.19032   26.28944 7.03168  1.000 57.86229  ? 158 GLU   A CG  1 
ATOM   1104 C  CD  . GLU   A 1 151 ? 2.11617   25.31710 6.32256  1.000 74.66338  ? 158 GLU   A CD  1 
ATOM   1105 O  OE1 . GLU   A 1 151 ? 2.49974   24.30118 6.94013  1.000 72.17473  ? 158 GLU   A OE1 1 
ATOM   1106 O  OE2 . GLU   A 1 151 ? 2.45738   25.56591 5.14694  1.000 85.20445  ? 158 GLU   A OE2 1 
ATOM   1107 N  N   . GLN   A 1 152 ? -0.12844  25.83884 11.16390 1.000 43.99687  ? 159 GLN   A N   1 
ATOM   1108 C  CA  . GLN   A 1 152 ? -0.19063  25.41407 12.55459 1.000 43.77049  ? 159 GLN   A CA  1 
ATOM   1109 C  C   . GLN   A 1 152 ? 1.11392   24.73209 12.94449 1.000 47.00949  ? 159 GLN   A C   1 
ATOM   1110 O  O   . GLN   A 1 152 ? 1.59955   23.84845 12.23164 1.000 47.59522  ? 159 GLN   A O   1 
ATOM   1111 C  CB  . GLN   A 1 152 ? -1.37219  24.47110 12.77009 1.000 47.07645  ? 159 GLN   A CB  1 
ATOM   1112 C  CG  . GLN   A 1 152 ? -1.64671  24.14043 14.22453 1.000 50.74236  ? 159 GLN   A CG  1 
ATOM   1113 C  CD  . GLN   A 1 152 ? -3.02539  23.54877 14.42598 1.000 53.71372  ? 159 GLN   A CD  1 
ATOM   1114 O  OE1 . GLN   A 1 152 ? -4.03286  24.16432 14.07792 1.000 55.02753  ? 159 GLN   A OE1 1 
ATOM   1115 N  NE2 . GLN   A 1 152 ? -3.07848  22.34653 14.98638 1.000 57.05761  ? 159 GLN   A NE2 1 
ATOM   1116 N  N   . TYR   A 1 153 ? 1.68085   25.14294 14.07569 1.000 43.60121  ? 160 TYR   A N   1 
ATOM   1117 C  CA  . TYR   A 1 153 ? 2.96678   24.63515 14.52548 1.000 47.11421  ? 160 TYR   A CA  1 
ATOM   1118 C  C   . TYR   A 1 153 ? 2.84850   24.10061 15.94528 1.000 46.69905  ? 160 TYR   A C   1 
ATOM   1119 O  O   . TYR   A 1 153 ? 1.90985   24.41990 16.67973 1.000 46.59318  ? 160 TYR   A O   1 
ATOM   1120 C  CB  . TYR   A 1 153 ? 4.05353   25.71790 14.45872 1.000 48.57362  ? 160 TYR   A CB  1 
ATOM   1121 C  CG  . TYR   A 1 153 ? 4.55725   25.98950 13.05881 1.000 50.17874  ? 160 TYR   A CG  1 
ATOM   1122 C  CD1 . TYR   A 1 153 ? 5.47736   25.14319 12.45460 1.000 45.68913  ? 160 TYR   A CD1 1 
ATOM   1123 C  CD2 . TYR   A 1 153 ? 4.10995   27.09045 12.34043 1.000 52.14990  ? 160 TYR   A CD2 1 
ATOM   1124 C  CE1 . TYR   A 1 153 ? 5.93958   25.38672 11.17428 1.000 56.12725  ? 160 TYR   A CE1 1 
ATOM   1125 C  CE2 . TYR   A 1 153 ? 4.56557   27.34190 11.05966 1.000 52.75714  ? 160 TYR   A CE2 1 
ATOM   1126 C  CZ  . TYR   A 1 153 ? 5.48026   26.48755 10.48171 1.000 55.78733  ? 160 TYR   A CZ  1 
ATOM   1127 O  OH  . TYR   A 1 153 ? 5.93668   26.73476 9.20669  1.000 63.22385  ? 160 TYR   A OH  1 
ATOM   1128 N  N   . ALA   A 1 154 ? 3.82343   23.27639 16.32146 1.000 48.19379  ? 161 ALA   A N   1 
ATOM   1129 C  CA  . ALA   A 1 154 ? 3.87777   22.65512 17.63827 1.000 47.28354  ? 161 ALA   A CA  1 
ATOM   1130 C  C   . ALA   A 1 154 ? 5.20692   22.99840 18.29420 1.000 47.21379  ? 161 ALA   A C   1 
ATOM   1131 O  O   . ALA   A 1 154 ? 6.26728   22.58315 17.81384 1.000 44.66037  ? 161 ALA   A O   1 
ATOM   1132 C  CB  . ALA   A 1 154 ? 3.70169   21.13873 17.54053 1.000 41.91031  ? 161 ALA   A CB  1 
ATOM   1133 N  N   . TRP   A 1 155 ? 5.14521   23.75719 19.38263 1.000 44.34609  ? 162 TRP   A N   1 
ATOM   1134 C  CA  . TRP   A 1 155 ? 6.30765   24.08908 20.19251 1.000 42.11237  ? 162 TRP   A CA  1 
ATOM   1135 C  C   . TRP   A 1 155 ? 6.33672   23.17540 21.41027 1.000 45.51548  ? 162 TRP   A C   1 
ATOM   1136 O  O   . TRP   A 1 155 ? 5.29636   22.90444 22.01684 1.000 45.73425  ? 162 TRP   A O   1 
ATOM   1137 C  CB  . TRP   A 1 155 ? 6.25662   25.55773 20.62228 1.000 41.87250  ? 162 TRP   A CB  1 
ATOM   1138 C  CG  . TRP   A 1 155 ? 7.45896   26.05166 21.37229 1.000 41.41141  ? 162 TRP   A CG  1 
ATOM   1139 C  CD1 . TRP   A 1 155 ? 8.50623   26.76098 20.85994 1.000 42.79859  ? 162 TRP   A CD1 1 
ATOM   1140 C  CD2 . TRP   A 1 155 ? 7.71934   25.91132 22.77538 1.000 42.05821  ? 162 TRP   A CD2 1 
ATOM   1141 N  NE1 . TRP   A 1 155 ? 9.41003   27.05532 21.85090 1.000 39.88585  ? 162 TRP   A NE1 1 
ATOM   1142 C  CE2 . TRP   A 1 155 ? 8.95049   26.54562 23.03648 1.000 42.64676  ? 162 TRP   A CE2 1 
ATOM   1143 C  CE3 . TRP   A 1 155 ? 7.03611   25.30421 23.83373 1.000 42.41120  ? 162 TRP   A CE3 1 
ATOM   1144 C  CZ2 . TRP   A 1 155 ? 9.51264   26.58938 24.31075 1.000 40.70843  ? 162 TRP   A CZ2 1 
ATOM   1145 C  CZ3 . TRP   A 1 155 ? 7.59622   25.34799 25.09774 1.000 41.80299  ? 162 TRP   A CZ3 1 
ATOM   1146 C  CH2 . TRP   A 1 155 ? 8.82119   25.98727 25.32567 1.000 44.51006  ? 162 TRP   A CH2 1 
ATOM   1147 N  N   . GLU   A 1 156 ? 7.52628   22.69269 21.76252 1.000 39.42361  ? 163 GLU   A N   1 
ATOM   1148 C  CA  . GLU   A 1 156 ? 7.64420   21.75108 22.86619 1.000 43.26621  ? 163 GLU   A CA  1 
ATOM   1149 C  C   . GLU   A 1 156 ? 9.02255   21.85535 23.49874 1.000 46.11465  ? 163 GLU   A C   1 
ATOM   1150 O  O   . GLU   A 1 156 ? 10.02798  22.00003 22.79801 1.000 42.05820  ? 163 GLU   A O   1 
ATOM   1151 C  CB  . GLU   A 1 156 ? 7.39337   20.31281 22.40168 1.000 41.37000  ? 163 GLU   A CB  1 
ATOM   1152 C  CG  . GLU   A 1 156 ? 7.25786   19.31584 23.53891 1.000 48.75670  ? 163 GLU   A CG  1 
ATOM   1153 C  CD  . GLU   A 1 156 ? 6.63714   18.00916 23.09326 1.000 57.91150  ? 163 GLU   A CD  1 
ATOM   1154 O  OE1 . GLU   A 1 156 ? 5.41273   17.83881 23.27310 1.000 58.36235  ? 163 GLU   A OE1 1 
ATOM   1155 O  OE2 . GLU   A 1 156 ? 7.37471   17.15305 22.56163 1.000 58.69101  ? 163 GLU   A OE2 1 
ATOM   1156 N  N   . SER   A 1 157 ? 9.05777   21.76978 24.82761 1.000 44.44381  ? 164 SER   A N   1 
ATOM   1157 C  CA  . SER   A 1 157 ? 10.31622  21.77228 25.56069 1.000 45.51872  ? 164 SER   A CA  1 
ATOM   1158 C  C   . SER   A 1 157 ? 10.08964  21.17737 26.93999 1.000 42.83178  ? 164 SER   A C   1 
ATOM   1159 O  O   . SER   A 1 157 ? 9.12366   21.53503 27.62149 1.000 43.16659  ? 164 SER   A O   1 
ATOM   1160 C  CB  . SER   A 1 157 ? 10.88547  23.18774 25.68915 1.000 43.48148  ? 164 SER   A CB  1 
ATOM   1161 O  OG  . SER   A 1 157 ? 11.96722  23.21632 26.60430 1.000 46.33967  ? 164 SER   A OG  1 
ATOM   1162 N  N   . SER   A 1 158 ? 10.97671  20.26690 27.33961 1.000 41.89970  ? 165 SER   A N   1 
ATOM   1163 C  CA  . SER   A 1 158 ? 11.06693  19.79852 28.71565 1.000 44.13648  ? 165 SER   A CA  1 
ATOM   1164 C  C   . SER   A 1 158 ? 12.14363  20.54831 29.49011 1.000 47.25074  ? 165 SER   A C   1 
ATOM   1165 O  O   . SER   A 1 158 ? 12.70813  20.01121 30.44988 1.000 48.21050  ? 165 SER   A O   1 
ATOM   1166 C  CB  . SER   A 1 158 ? 11.33791  18.29490 28.74889 1.000 44.18440  ? 165 SER   A CB  1 
ATOM   1167 O  OG  . SER   A 1 158 ? 10.20492  17.56292 28.31812 1.000 53.71677  ? 165 SER   A OG  1 
ATOM   1168 N  N   . ALA   A 1 159 ? 12.43087  21.78106 29.08284 1.000 46.50984  ? 166 ALA   A N   1 
ATOM   1169 C  CA  . ALA   A 1 159 ? 13.57407  22.56863 29.56070 1.000 45.95579  ? 166 ALA   A CA  1 
ATOM   1170 C  C   . ALA   A 1 159 ? 14.84403  21.77890 29.23236 1.000 49.76764  ? 166 ALA   A C   1 
ATOM   1171 O  O   . ALA   A 1 159 ? 14.91057  21.08616 28.20842 1.000 51.40595  ? 166 ALA   A O   1 
ATOM   1172 C  CB  . ALA   A 1 159 ? 13.40290  22.92750 31.02524 1.000 46.68494  ? 166 ALA   A CB  1 
ATOM   1173 N  N   . GLY   A 1 160 ? 15.86219  21.86769 30.08254 1.000 46.55175  ? 167 GLY   A N   1 
ATOM   1174 C  CA  . GLY   A 1 160 ? 17.09821  21.17297 29.79499 1.000 49.12730  ? 167 GLY   A CA  1 
ATOM   1175 C  C   . GLY   A 1 160 ? 17.94413  21.79616 28.71016 1.000 51.19721  ? 167 GLY   A C   1 
ATOM   1176 O  O   . GLY   A 1 160 ? 18.91362  21.17263 28.26804 1.000 51.25490  ? 167 GLY   A O   1 
ATOM   1177 N  N   . GLY   A 1 161 ? 17.60059  23.00009 28.25376 1.000 49.07643  ? 168 GLY   A N   1 
ATOM   1178 C  CA  . GLY   A 1 161 ? 18.43303  23.74527 27.33369 1.000 50.46811  ? 168 GLY   A CA  1 
ATOM   1179 C  C   . GLY   A 1 161 ? 18.01656  23.70706 25.87943 1.000 47.42304  ? 168 GLY   A C   1 
ATOM   1180 O  O   . GLY   A 1 161 ? 18.67413  24.35223 25.05349 1.000 47.42922  ? 168 GLY   A O   1 
ATOM   1181 N  N   . SER   A 1 162 ? 16.95183  22.98528 25.53446 1.000 43.13347  ? 169 SER   A N   1 
ATOM   1182 C  CA  . SER   A 1 162 ? 16.54741  22.85338 24.14319 1.000 46.85617  ? 169 SER   A CA  1 
ATOM   1183 C  C   . SER   A 1 162 ? 15.02983  22.83705 24.03728 1.000 45.55426  ? 169 SER   A C   1 
ATOM   1184 O  O   . SER   A 1 162 ? 14.31950  22.48508 24.98216 1.000 44.69135  ? 169 SER   A O   1 
ATOM   1185 C  CB  . SER   A 1 162 ? 17.12615  21.58338 23.50478 1.000 44.13832  ? 169 SER   A CB  1 
ATOM   1186 O  OG  . SER   A 1 162 ? 16.59900  20.42196 24.12213 1.000 50.34989  ? 169 SER   A OG  1 
ATOM   1187 N  N   . PHE   A 1 163 ? 14.54397  23.22720 22.86090 1.000 41.63916  ? 170 PHE   A N   1 
ATOM   1188 C  CA  . PHE   A 1 163 ? 13.13341  23.12990 22.52102 1.000 42.24194  ? 170 PHE   A CA  1 
ATOM   1189 C  C   . PHE   A 1 163 ? 13.01015  22.69634 21.06740 1.000 46.80148  ? 170 PHE   A C   1 
ATOM   1190 O  O   . PHE   A 1 163 ? 13.95673  22.80492 20.28360 1.000 44.17600  ? 170 PHE   A O   1 
ATOM   1191 C  CB  . PHE   A 1 163 ? 12.39122  24.45443 22.75503 1.000 42.99092  ? 170 PHE   A CB  1 
ATOM   1192 C  CG  . PHE   A 1 163 ? 12.85335  25.58200 21.87535 1.000 40.48004  ? 170 PHE   A CG  1 
ATOM   1193 C  CD1 . PHE   A 1 163 ? 13.96109  26.33914 22.21911 1.000 43.66339  ? 170 PHE   A CD1 1 
ATOM   1194 C  CD2 . PHE   A 1 163 ? 12.16879  25.89608 20.71283 1.000 39.82106  ? 170 PHE   A CD2 1 
ATOM   1195 C  CE1 . PHE   A 1 163 ? 14.38241  27.38285 21.41522 1.000 42.20951  ? 170 PHE   A CE1 1 
ATOM   1196 C  CE2 . PHE   A 1 163 ? 12.58445  26.93720 19.90530 1.000 39.99486  ? 170 PHE   A CE2 1 
ATOM   1197 C  CZ  . PHE   A 1 163 ? 13.69096  27.68335 20.25821 1.000 46.52047  ? 170 PHE   A CZ  1 
ATOM   1198 N  N   . THR   A 1 164 ? 11.82861  22.19694 20.71393 1.000 42.28094  ? 171 THR   A N   1 
ATOM   1199 C  CA  . THR   A 1 164 ? 11.56100  21.70095 19.37305 1.000 46.70060  ? 171 THR   A CA  1 
ATOM   1200 C  C   . THR   A 1 164 ? 10.41630  22.47889 18.73872 1.000 45.08441  ? 171 THR   A C   1 
ATOM   1201 O  O   . THR   A 1 164 ? 9.49274   22.93035 19.42258 1.000 43.30837  ? 171 THR   A O   1 
ATOM   1202 C  CB  . THR   A 1 164 ? 11.21368  20.20515 19.38227 1.000 43.65150  ? 171 THR   A CB  1 
ATOM   1203 O  OG1 . THR   A 1 164 ? 10.02490  19.99198 20.15385 1.000 46.34492  ? 171 THR   A OG1 1 
ATOM   1204 C  CG2 . THR   A 1 164 ? 12.35364  19.39272 19.97644 1.000 44.12066  ? 171 THR   A CG2 1 
ATOM   1205 N  N   . VAL   A 1 165 ? 10.49096  22.63081 17.41854 1.000 45.71697  ? 172 VAL   A N   1 
ATOM   1206 C  CA  . VAL   A 1 165 ? 9.44161   23.25622 16.62353 1.000 45.67666  ? 172 VAL   A CA  1 
ATOM   1207 C  C   . VAL   A 1 165 ? 9.14635   22.34669 15.44054 1.000 49.88879  ? 172 VAL   A C   1 
ATOM   1208 O  O   . VAL   A 1 165 ? 10.07113  21.87259 14.77133 1.000 51.67779  ? 172 VAL   A O   1 
ATOM   1209 C  CB  . VAL   A 1 165 ? 9.84247   24.66308 16.13831 1.000 48.34180  ? 172 VAL   A CB  1 
ATOM   1210 C  CG1 . VAL   A 1 165 ? 8.79924   25.21260 15.17663 1.000 45.81711  ? 172 VAL   A CG1 1 
ATOM   1211 C  CG2 . VAL   A 1 165 ? 10.02499  25.60273 17.31963 1.000 44.45476  ? 172 VAL   A CG2 1 
ATOM   1212 N  N   . ARG   A 1 166 ? 7.86379   22.09862 15.18809 1.000 46.94569  ? 173 ARG   A N   1 
ATOM   1213 C  CA  . ARG   A 1 166 ? 7.45894   21.23485 14.09076 1.000 51.57265  ? 173 ARG   A CA  1 
ATOM   1214 C  C   . ARG   A 1 166 ? 6.08492   21.66164 13.60040 1.000 52.62751  ? 173 ARG   A C   1 
ATOM   1215 O  O   . ARG   A 1 166 ? 5.34176   22.35774 14.29734 1.000 47.65705  ? 173 ARG   A O   1 
ATOM   1216 C  CB  . ARG   A 1 166 ? 7.42962   19.76194 14.51303 1.000 55.66995  ? 173 ARG   A CB  1 
ATOM   1217 C  CG  . ARG   A 1 166 ? 6.15116   19.37176 15.23472 1.000 58.55859  ? 173 ARG   A CG  1 
ATOM   1218 C  CD  . ARG   A 1 166 ? 6.17343   17.92474 15.69474 1.000 61.15653  ? 173 ARG   A CD  1 
ATOM   1219 N  NE  . ARG   A 1 166 ? 5.26194   17.69870 16.81089 1.000 80.65145  ? 173 ARG   A NE  1 
ATOM   1220 C  CZ  . ARG   A 1 166 ? 3.93996   17.65340 16.70721 1.000 75.94727  ? 173 ARG   A CZ  1 
ATOM   1221 N  NH1 . ARG   A 1 166 ? 3.33075   17.79862 15.54118 1.000 66.49708  ? 173 ARG   A NH1 1 
ATOM   1222 N  NH2 . ARG   A 1 166 ? 3.21013   17.45506 17.80132 1.000 71.71642  ? 173 ARG   A NH2 1 
ATOM   1223 N  N   . THR   A 1 167 ? 5.75678   21.23494 12.38461 1.000 55.65006  ? 174 THR   A N   1 
ATOM   1224 C  CA  . THR   A 1 167 ? 4.41107   21.43061 11.86646 1.000 59.55281  ? 174 THR   A CA  1 
ATOM   1225 C  C   . THR   A 1 167 ? 3.45652   20.46749 12.56033 1.000 59.55189  ? 174 THR   A C   1 
ATOM   1226 O  O   . THR   A 1 167 ? 3.71321   19.26171 12.62456 1.000 61.82099  ? 174 THR   A O   1 
ATOM   1227 C  CB  . THR   A 1 167 ? 4.38154   21.21363 10.35390 1.000 61.01905  ? 174 THR   A CB  1 
ATOM   1228 O  OG1 . THR   A 1 167 ? 5.20698   22.19367 9.71254  1.000 65.75795  ? 174 THR   A OG1 1 
ATOM   1229 C  CG2 . THR   A 1 167 ? 2.95888   21.33538 9.82523  1.000 63.44519  ? 174 THR   A CG2 1 
ATOM   1230 N  N   . ASP   A 1 168 ? 2.36115   21.00002 13.09357 1.000 54.44282  ? 175 ASP   A N   1 
ATOM   1231 C  CA  . ASP   A 1 168 ? 1.40128   20.17740 13.81536 1.000 61.87431  ? 175 ASP   A CA  1 
ATOM   1232 C  C   . ASP   A 1 168 ? 0.46458   19.48317 12.83610 1.000 67.29329  ? 175 ASP   A C   1 
ATOM   1233 O  O   . ASP   A 1 168 ? -0.16520  20.13332 11.99546 1.000 65.59520  ? 175 ASP   A O   1 
ATOM   1234 C  CB  . ASP   A 1 168 ? 0.59834   21.02143 14.80359 1.000 60.51733  ? 175 ASP   A CB  1 
ATOM   1235 C  CG  . ASP   A 1 168 ? -0.35380  20.18578 15.63635 1.000 64.98729  ? 175 ASP   A CG  1 
ATOM   1236 O  OD1 . ASP   A 1 168 ? 0.03770   19.07239 16.04699 1.000 70.05947  ? 175 ASP   A OD1 1 
ATOM   1237 O  OD2 . ASP   A 1 168 ? -1.49300  20.63581 15.87606 1.000 66.98140  ? 175 ASP   A OD2 1 
ATOM   1238 N  N   . THR   A 1 169 ? 0.37390   18.15989 12.95000 1.000 74.46882  ? 176 THR   A N   1 
ATOM   1239 C  CA  . THR   A 1 169 ? -0.48895  17.36320 12.09015 1.000 81.39622  ? 176 THR   A CA  1 
ATOM   1240 C  C   . THR   A 1 169 ? -1.85611  17.09351 12.70334 1.000 79.42708  ? 176 THR   A C   1 
ATOM   1241 O  O   . THR   A 1 169 ? -2.73579  16.57278 12.00905 1.000 77.77889  ? 176 THR   A O   1 
ATOM   1242 C  CB  . THR   A 1 169 ? 0.18207   16.02446 11.76059 1.000 82.89963  ? 176 THR   A CB  1 
ATOM   1243 O  OG1 . THR   A 1 169 ? 0.09294   15.15248 12.89490 1.000 91.07904  ? 176 THR   A OG1 1 
ATOM   1244 C  CG2 . THR   A 1 169 ? 1.64716   16.23448 11.40888 1.000 77.60053  ? 176 THR   A CG2 1 
ATOM   1245 N  N   . GLY   A 1 170 ? -2.05659  17.43884 13.97349 1.000 79.48178  ? 177 GLY   A N   1 
ATOM   1246 C  CA  . GLY   A 1 170 ? -3.27491  17.09533 14.68037 1.000 79.71016  ? 177 GLY   A CA  1 
ATOM   1247 C  C   . GLY   A 1 170 ? -4.49077  17.91249 14.29745 1.000 79.20368  ? 177 GLY   A C   1 
ATOM   1248 O  O   . GLY   A 1 170 ? -4.59860  18.39492 13.16672 1.000 74.44298  ? 177 GLY   A O   1 
ATOM   1249 N  N   . GLU   A 1 171 ? -5.41075  18.06924 15.24284 1.000 76.94902  ? 178 GLU   A N   1 
ATOM   1250 C  CA  . GLU   A 1 171 ? -6.66342  18.76248 14.97651 1.000 77.14723  ? 178 GLU   A CA  1 
ATOM   1251 C  C   . GLU   A 1 171 ? -6.39704  20.21379 14.59596 1.000 70.96829  ? 178 GLU   A C   1 
ATOM   1252 O  O   . GLU   A 1 171 ? -5.68015  20.92170 15.32189 1.000 65.22465  ? 178 GLU   A O   1 
ATOM   1253 C  CB  . GLU   A 1 171 ? -7.57706  18.69514 16.20255 1.000 76.60744  ? 178 GLU   A CB  1 
ATOM   1254 C  CG  . GLU   A 1 171 ? -8.53820  17.50914 16.21093 1.000 86.89211  ? 178 GLU   A CG  1 
ATOM   1255 C  CD  . GLU   A 1 171 ? -9.56498  17.56847 15.09327 1.000 94.49089  ? 178 GLU   A CD  1 
ATOM   1256 O  OE1 . GLU   A 1 171 ? -9.91132  18.68744 14.66012 1.000 89.97509  ? 178 GLU   A OE1 1 
ATOM   1257 O  OE2 . GLU   A 1 171 ? -10.02683 16.49599 14.64647 1.000 92.55095  ? 178 GLU   A OE2 1 
ATOM   1258 N  N   . PRO   A 1 172 ? -6.92270  20.69195 13.46787 1.000 72.96024  ? 179 PRO   A N   1 
ATOM   1259 C  CA  . PRO   A 1 172 ? -6.78995  22.11415 13.13404 1.000 68.24527  ? 179 PRO   A CA  1 
ATOM   1260 C  C   . PRO   A 1 172 ? -7.45058  22.98211 14.19558 1.000 65.88005  ? 179 PRO   A C   1 
ATOM   1261 O  O   . PRO   A 1 172 ? -8.50559  22.64253 14.73593 1.000 72.04135  ? 179 PRO   A O   1 
ATOM   1262 C  CB  . PRO   A 1 172 ? -7.49445  22.24766 11.77791 1.000 57.67096  ? 179 PRO   A CB  1 
ATOM   1263 C  CG  . PRO   A 1 172 ? -7.86924  20.88273 11.34169 1.000 69.14907  ? 179 PRO   A CG  1 
ATOM   1264 C  CD  . PRO   A 1 172 ? -7.53779  19.88846 12.39618 1.000 71.85177  ? 179 PRO   A CD  1 
ATOM   1265 N  N   . MET   A 1 173 ? -6.81254  24.11234 14.49452 1.000 59.31882  ? 180 MET   A N   1 
ATOM   1266 C  CA  . MET   A 1 173 ? -7.26679  24.98645 15.56584 1.000 59.54126  ? 180 MET   A CA  1 
ATOM   1267 C  C   . MET   A 1 173 ? -8.00169  26.22428 15.07383 1.000 56.81907  ? 180 MET   A C   1 
ATOM   1268 O  O   . MET   A 1 173 ? -8.68989  26.87104 15.87100 1.000 68.35515  ? 180 MET   A O   1 
ATOM   1269 C  CB  . MET   A 1 173 ? -6.07738  25.42715 16.42439 1.000 60.84726  ? 180 MET   A CB  1 
ATOM   1270 C  CG  . MET   A 1 173 ? -5.78298  24.51750 17.60151 1.000 61.97695  ? 180 MET   A CG  1 
ATOM   1271 S  SD  . MET   A 1 173 ? -4.68830  25.33000 18.77576 1.000 72.13673  ? 180 MET   A SD  1 
ATOM   1272 C  CE  . MET   A 1 173 ? -3.64419  26.24838 17.64969 1.000 49.72789  ? 180 MET   A CE  1 
ATOM   1273 N  N   . GLY   A 1 174 ? -7.87803  26.56790 13.79506 1.000 54.75193  ? 181 GLY   A N   1 
ATOM   1274 C  CA  . GLY   A 1 174 ? -8.47597  27.78608 13.28664 1.000 50.65960  ? 181 GLY   A CA  1 
ATOM   1275 C  C   . GLY   A 1 174 ? -7.59404  28.99167 13.53336 1.000 52.77638  ? 181 GLY   A C   1 
ATOM   1276 O  O   . GLY   A 1 174 ? -7.03163  29.56006 12.59234 1.000 53.85499  ? 181 GLY   A O   1 
ATOM   1277 N  N   . ARG   A 1 175 ? -7.46047  29.38239 14.79986 1.000 48.16307  ? 182 ARG   A N   1 
ATOM   1278 C  CA  . ARG   A 1 175 ? -6.59201  30.48074 15.19964 1.000 43.63167  ? 182 ARG   A CA  1 
ATOM   1279 C  C   . ARG   A 1 175 ? -6.48955  30.48869 16.71582 1.000 42.46343  ? 182 ARG   A C   1 
ATOM   1280 O  O   . ARG   A 1 175 ? -7.48304  30.25181 17.40673 1.000 48.59986  ? 182 ARG   A O   1 
ATOM   1281 C  CB  . ARG   A 1 175 ? -7.12182  31.83254 14.70044 1.000 42.55319  ? 182 ARG   A CB  1 
ATOM   1282 C  CG  . ARG   A 1 175 ? -6.12073  32.96866 14.82990 1.000 41.48642  ? 182 ARG   A CG  1 
ATOM   1283 C  CD  . ARG   A 1 175 ? -6.79486  34.33367 14.78556 1.000 43.46632  ? 182 ARG   A CD  1 
ATOM   1284 N  NE  . ARG   A 1 175 ? -7.72478  34.52974 15.89165 1.000 42.81258  ? 182 ARG   A NE  1 
ATOM   1285 C  CZ  . ARG   A 1 175 ? -9.04545  34.50760 15.77450 1.000 45.16848  ? 182 ARG   A CZ  1 
ATOM   1286 N  NH1 . ARG   A 1 175 ? -9.63201  34.30875 14.60591 1.000 42.90422  ? 182 ARG   A NH1 1 
ATOM   1287 N  NH2 . ARG   A 1 175 ? -9.79613  34.69241 16.85687 1.000 41.54692  ? 182 ARG   A NH2 1 
ATOM   1288 N  N   . GLY   A 1 176 ? -5.28901  30.75810 17.22552 1.000 40.81981  ? 183 GLY   A N   1 
ATOM   1289 C  CA  . GLY   A 1 176 ? -5.09022  30.87583 18.65033 1.000 39.33940  ? 183 GLY   A CA  1 
ATOM   1290 C  C   . GLY   A 1 176 ? -3.88809  30.08206 19.10110 1.000 43.86003  ? 183 GLY   A C   1 
ATOM   1291 O  O   . GLY   A 1 176 ? -3.05484  29.65938 18.29170 1.000 44.28009  ? 183 GLY   A O   1 
ATOM   1292 N  N   . THR   A 1 177 ? -3.80417  29.87858 20.41292 1.000 39.74707  ? 184 THR   A N   1 
ATOM   1293 C  CA  . THR   A 1 177 ? -2.68868  29.17908 21.02998 1.000 40.12068  ? 184 THR   A CA  1 
ATOM   1294 C  C   . THR   A 1 177 ? -3.22296  28.23124 22.09169 1.000 44.99536  ? 184 THR   A C   1 
ATOM   1295 O  O   . THR   A 1 177 ? -4.10685  28.59543 22.87257 1.000 41.64971  ? 184 THR   A O   1 
ATOM   1296 C  CB  . THR   A 1 177 ? -1.68736  30.16318 21.65463 1.000 40.33635  ? 184 THR   A CB  1 
ATOM   1297 O  OG1 . THR   A 1 177 ? -1.11961  30.98342 20.62636 1.000 40.03881  ? 184 THR   A OG1 1 
ATOM   1298 C  CG2 . THR   A 1 177 ? -0.57391  29.41791 22.37372 1.000 41.75165  ? 184 THR   A CG2 1 
ATOM   1299 N  N   . LYS   A 1 178 ? -2.69196  27.01162 22.10534 1.000 43.23468  ? 185 LYS   A N   1 
ATOM   1300 C  CA  . LYS   A 1 178 ? -3.05272  25.99913 23.08867 1.000 43.96615  ? 185 LYS   A CA  1 
ATOM   1301 C  C   . LYS   A 1 178 ? -1.79853  25.60050 23.85213 1.000 44.87636  ? 185 LYS   A C   1 
ATOM   1302 O  O   . LYS   A 1 178 ? -0.85973  25.05095 23.26577 1.000 42.11513  ? 185 LYS   A O   1 
ATOM   1303 C  CB  . LYS   A 1 178 ? -3.69333  24.78426 22.41435 1.000 47.10176  ? 185 LYS   A CB  1 
ATOM   1304 C  CG  . LYS   A 1 178 ? -3.70621  23.53018 23.27053 1.000 54.34290  ? 185 LYS   A CG  1 
ATOM   1305 C  CD  . LYS   A 1 178 ? -4.68765  22.49255 22.74031 1.000 52.61203  ? 185 LYS   A CD  1 
ATOM   1306 C  CE  . LYS   A 1 178 ? -4.70449  22.44918 21.22088 1.000 51.54784  ? 185 LYS   A CE  1 
ATOM   1307 N  NZ  . LYS   A 1 178 ? -5.75512  21.52581 20.70997 1.000 65.76285  ? 185 LYS   A NZ  1 
ATOM   1308 N  N   . VAL   A 1 179 ? -1.78248  25.88268 25.15046 1.000 41.68732  ? 186 VAL   A N   1 
ATOM   1309 C  CA  . VAL   A 1 179 ? -0.63986  25.59566 26.00905 1.000 42.22782  ? 186 VAL   A CA  1 
ATOM   1310 C  C   . VAL   A 1 179 ? -0.98600  24.37139 26.84624 1.000 44.55038  ? 186 VAL   A C   1 
ATOM   1311 O  O   . VAL   A 1 179 ? -1.89642  24.41357 27.68022 1.000 38.66683  ? 186 VAL   A O   1 
ATOM   1312 C  CB  . VAL   A 1 179 ? -0.28157  26.79716 26.89337 1.000 41.80654  ? 186 VAL   A CB  1 
ATOM   1313 C  CG1 . VAL   A 1 179 ? 0.90589   26.46499 27.78137 1.000 35.94280  ? 186 VAL   A CG1 1 
ATOM   1314 C  CG2 . VAL   A 1 179 ? 0.01204   28.01875 26.03400 1.000 39.13051  ? 186 VAL   A CG2 1 
ATOM   1315 N  N   . ILE   A 1 180 ? -0.26234  23.27810 26.62590 1.000 41.57586  ? 187 ILE   A N   1 
ATOM   1316 C  CA  . ILE   A 1 180 ? -0.48517  22.02411 27.33587 1.000 41.57448  ? 187 ILE   A CA  1 
ATOM   1317 C  C   . ILE   A 1 180 ? 0.60865   21.86842 28.38280 1.000 44.68979  ? 187 ILE   A C   1 
ATOM   1318 O  O   . ILE   A 1 180 ? 1.79222   21.74550 28.04462 1.000 44.89069  ? 187 ILE   A O   1 
ATOM   1319 C  CB  . ILE   A 1 180 ? -0.50055  20.82711 26.37304 1.000 44.10034  ? 187 ILE   A CB  1 
ATOM   1320 C  CG1 . ILE   A 1 180 ? -1.49865  21.06277 25.24070 1.000 45.92053  ? 187 ILE   A CG1 1 
ATOM   1321 C  CG2 . ILE   A 1 180 ? -0.83155  19.54441 27.12371 1.000 44.16459  ? 187 ILE   A CG2 1 
ATOM   1322 C  CD1 . ILE   A 1 180 ? -1.30744  20.13244 24.05795 1.000 47.17683  ? 187 ILE   A CD1 1 
ATOM   1323 N  N   . LEU   A 1 181 ? 0.21624   21.86664 29.65302 1.000 40.83420  ? 188 LEU   A N   1 
ATOM   1324 C  CA  . LEU   A 1 181 ? 1.14925   21.75037 30.76782 1.000 41.54258  ? 188 LEU   A CA  1 
ATOM   1325 C  C   . LEU   A 1 181 ? 1.13108   20.31599 31.28162 1.000 46.38567  ? 188 LEU   A C   1 
ATOM   1326 O  O   . LEU   A 1 181 ? 0.14606   19.87779 31.88387 1.000 41.79950  ? 188 LEU   A O   1 
ATOM   1327 C  CB  . LEU   A 1 181 ? 0.78791   22.72760 31.88292 1.000 40.37678  ? 188 LEU   A CB  1 
ATOM   1328 C  CG  . LEU   A 1 181 ? 0.53017   24.17278 31.46902 1.000 41.33931  ? 188 LEU   A CG  1 
ATOM   1329 C  CD1 . LEU   A 1 181 ? 0.08542   24.97184 32.66959 1.000 42.25465  ? 188 LEU   A CD1 1 
ATOM   1330 C  CD2 . LEU   A 1 181 ? 1.78701   24.77179 30.87153 1.000 43.77302  ? 188 LEU   A CD2 1 
ATOM   1331 N  N   . HIS   A 1 182 ? 2.21901   19.58877 31.04560 1.000 43.98504  ? 189 HIS   A N   1 
ATOM   1332 C  CA  . HIS   A 1 182 ? 2.40040   18.26073 31.62639 1.000 45.89821  ? 189 HIS   A CA  1 
ATOM   1333 C  C   . HIS   A 1 182 ? 2.88899   18.45086 33.05697 1.000 48.34024  ? 189 HIS   A C   1 
ATOM   1334 O  O   . HIS   A 1 182 ? 4.08499   18.62532 33.30310 1.000 46.22189  ? 189 HIS   A O   1 
ATOM   1335 C  CB  . HIS   A 1 182 ? 3.37462   17.43789 30.79184 1.000 50.75647  ? 189 HIS   A CB  1 
ATOM   1336 C  CG  . HIS   A 1 182 ? 2.98041   17.32181 29.35179 1.000 48.39536  ? 189 HIS   A CG  1 
ATOM   1337 N  ND1 . HIS   A 1 182 ? 2.31279   16.22665 28.84847 1.000 50.08508  ? 189 HIS   A ND1 1 
ATOM   1338 C  CD2 . HIS   A 1 182 ? 3.14420   18.17357 28.31192 1.000 45.79790  ? 189 HIS   A CD2 1 
ATOM   1339 C  CE1 . HIS   A 1 182 ? 2.09062   16.40402 27.55787 1.000 44.63364  ? 189 HIS   A CE1 1 
ATOM   1340 N  NE2 . HIS   A 1 182 ? 2.58488   17.57735 27.20783 1.000 46.78285  ? 189 HIS   A NE2 1 
ATOM   1341 N  N   . LEU   A 1 183 ? 1.95503   18.42246 34.00430 1.000 45.84521  ? 190 LEU   A N   1 
ATOM   1342 C  CA  . LEU   A 1 183 ? 2.25274   18.79692 35.37888 1.000 47.56498  ? 190 LEU   A CA  1 
ATOM   1343 C  C   . LEU   A 1 183 ? 3.20684   17.80570 36.03417 1.000 54.97197  ? 190 LEU   A C   1 
ATOM   1344 O  O   . LEU   A 1 183 ? 3.26972   16.62852 35.66934 1.000 56.69094  ? 190 LEU   A O   1 
ATOM   1345 C  CB  . LEU   A 1 183 ? 0.96495   18.88203 36.19772 1.000 46.56689  ? 190 LEU   A CB  1 
ATOM   1346 C  CG  . LEU   A 1 183 ? -0.04593  19.95070 35.78177 1.000 46.05171  ? 190 LEU   A CG  1 
ATOM   1347 C  CD1 . LEU   A 1 183 ? -1.24083  19.94341 36.72117 1.000 47.95572  ? 190 LEU   A CD1 1 
ATOM   1348 C  CD2 . LEU   A 1 183 ? 0.60561   21.32317 35.74325 1.000 40.61388  ? 190 LEU   A CD2 1 
ATOM   1349 N  N   . LYS   A 1 184 ? 3.95445   18.30021 37.01759 1.000 54.38538  ? 191 LYS   A N   1 
ATOM   1350 C  CA  . LYS   A 1 184 ? 4.78099   17.43376 37.83876 1.000 54.19258  ? 191 LYS   A CA  1 
ATOM   1351 C  C   . LYS   A 1 184 ? 3.89764   16.56646 38.73501 1.000 60.70801  ? 191 LYS   A C   1 
ATOM   1352 O  O   . LYS   A 1 184 ? 2.68212   16.75951 38.83481 1.000 58.39438  ? 191 LYS   A O   1 
ATOM   1353 C  CB  . LYS   A 1 184 ? 5.75662   18.26094 38.67508 1.000 51.62442  ? 191 LYS   A CB  1 
ATOM   1354 C  CG  . LYS   A 1 184 ? 6.71006   19.11094 37.84877 1.000 52.46860  ? 191 LYS   A CG  1 
ATOM   1355 C  CD  . LYS   A 1 184 ? 7.50822   20.06440 38.72336 1.000 54.85948  ? 191 LYS   A CD  1 
ATOM   1356 C  CE  . LYS   A 1 184 ? 8.12870   21.17980 37.89682 1.000 54.92880  ? 191 LYS   A CE  1 
ATOM   1357 N  NZ  . LYS   A 1 184 ? 8.89634   22.13787 38.74056 1.000 59.22614  ? 191 LYS   A NZ  1 
ATOM   1358 N  N   . GLU   A 1 185 ? 4.53046   15.59740 39.40003 1.000 59.23358  ? 192 GLU   A N   1 
ATOM   1359 C  CA  . GLU   A 1 185 ? 3.77553   14.62866 40.18910 1.000 59.70661  ? 192 GLU   A CA  1 
ATOM   1360 C  C   . GLU   A 1 185 ? 3.07762   15.28999 41.37246 1.000 61.12248  ? 192 GLU   A C   1 
ATOM   1361 O  O   . GLU   A 1 185 ? 1.94408   14.93117 41.71328 1.000 60.57620  ? 192 GLU   A O   1 
ATOM   1362 C  CB  . GLU   A 1 185 ? 4.70280   13.51098 40.66734 1.000 63.85627  ? 192 GLU   A CB  1 
ATOM   1363 C  CG  . GLU   A 1 185 ? 4.06271   12.54225 41.64839 1.000 73.53870  ? 192 GLU   A CG  1 
ATOM   1364 C  CD  . GLU   A 1 185 ? 4.62195   11.13782 41.52987 1.000 93.19770  ? 192 GLU   A CD  1 
ATOM   1365 O  OE1 . GLU   A 1 185 ? 3.82229   10.17903 41.49308 1.000 100.05799 ? 192 GLU   A OE1 1 
ATOM   1366 O  OE2 . GLU   A 1 185 ? 5.86127   10.99252 41.47402 1.000 91.15073  ? 192 GLU   A OE2 1 
ATOM   1367 N  N   . ASP   A 1 186 ? 3.73100   16.26051 42.00633 1.000 58.17586  ? 193 ASP   A N   1 
ATOM   1368 C  CA  . ASP   A 1 186 ? 3.21095   16.88710 43.21419 1.000 61.59907  ? 193 ASP   A CA  1 
ATOM   1369 C  C   . ASP   A 1 186 ? 2.43414   18.17023 42.93943 1.000 59.72294  ? 193 ASP   A C   1 
ATOM   1370 O  O   . ASP   A 1 186 ? 2.14867   18.91832 43.88000 1.000 60.63793  ? 193 ASP   A O   1 
ATOM   1371 C  CB  . ASP   A 1 186 ? 4.35569   17.17300 44.19087 1.000 59.73367  ? 193 ASP   A CB  1 
ATOM   1372 C  CG  . ASP   A 1 186 ? 5.39314   18.12080 43.61643 1.000 70.09785  ? 193 ASP   A CG  1 
ATOM   1373 O  OD1 . ASP   A 1 186 ? 5.41747   18.30817 42.38111 1.000 61.64182  ? 193 ASP   A OD1 1 
ATOM   1374 O  OD2 . ASP   A 1 186 ? 6.18809   18.67737 44.40325 1.000 75.10177  ? 193 ASP   A OD2 1 
ATOM   1375 N  N   . GLN   A 1 187 ? 2.08172   18.44061 41.68230 1.000 54.22402  ? 194 GLN   A N   1 
ATOM   1376 C  CA  . GLN   A 1 187 ? 1.35935   19.65324 41.31846 1.000 54.88050  ? 194 GLN   A CA  1 
ATOM   1377 C  C   . GLN   A 1 187 ? -0.03445  19.35906 40.77221 1.000 53.29239  ? 194 GLN   A C   1 
ATOM   1378 O  O   . GLN   A 1 187 ? -0.59507  20.18131 40.04059 1.000 56.44619  ? 194 GLN   A O   1 
ATOM   1379 C  CB  . GLN   A 1 187 ? 2.16567   20.46438 40.30264 1.000 54.99355  ? 194 GLN   A CB  1 
ATOM   1380 C  CG  . GLN   A 1 187 ? 3.55655   20.85937 40.77950 1.000 52.63291  ? 194 GLN   A CG  1 
ATOM   1381 C  CD  . GLN   A 1 187 ? 3.53183   21.65180 42.07241 1.000 52.63266  ? 194 GLN   A CD  1 
ATOM   1382 O  OE1 . GLN   A 1 187 ? 2.67619   22.51465 42.26969 1.000 56.45670  ? 194 GLN   A OE1 1 
ATOM   1383 N  NE2 . GLN   A 1 187 ? 4.47484   21.36262 42.96141 1.000 56.69097  ? 194 GLN   A NE2 1 
ATOM   1384 N  N   . THR   A 1 188 ? -0.60958  18.20630 41.11971 1.000 56.37615  ? 195 THR   A N   1 
ATOM   1385 C  CA  . THR   A 1 188 ? -1.91807  17.82185 40.60236 1.000 56.46076  ? 195 THR   A CA  1 
ATOM   1386 C  C   . THR   A 1 188 ? -3.06352  18.60257 41.23350 1.000 55.72911  ? 195 THR   A C   1 
ATOM   1387 O  O   . THR   A 1 188 ? -4.21070  18.43060 40.80474 1.000 57.19040  ? 195 THR   A O   1 
ATOM   1388 C  CB  . THR   A 1 188 ? -2.14332  16.32099 40.80376 1.000 57.53448  ? 195 THR   A CB  1 
ATOM   1389 O  OG1 . THR   A 1 188 ? -2.32147  16.04429 42.19856 1.000 60.55842  ? 195 THR   A OG1 1 
ATOM   1390 C  CG2 . THR   A 1 188 ? -0.95479  15.52809 40.27793 1.000 55.59842  ? 195 THR   A CG2 1 
ATOM   1391 N  N   . GLU   A 1 189 ? -2.79119  19.44921 42.23043 1.000 55.82999  ? 196 GLU   A N   1 
ATOM   1392 C  CA  . GLU   A 1 189 ? -3.84496  20.27535 42.80769 1.000 54.29713  ? 196 GLU   A CA  1 
ATOM   1393 C  C   . GLU   A 1 189 ? -4.43193  21.23820 41.78726 1.000 53.87151  ? 196 GLU   A C   1 
ATOM   1394 O  O   . GLU   A 1 189 ? -5.57962  21.66776 41.94289 1.000 53.59186  ? 196 GLU   A O   1 
ATOM   1395 C  CB  . GLU   A 1 189 ? -3.31186  21.05860 44.01164 1.000 55.90074  ? 196 GLU   A CB  1 
ATOM   1396 C  CG  . GLU   A 1 189 ? -2.47437  22.27335 43.64094 1.000 51.98430  ? 196 GLU   A CG  1 
ATOM   1397 C  CD  . GLU   A 1 189 ? -1.75362  22.87423 44.83025 1.000 55.54395  ? 196 GLU   A CD  1 
ATOM   1398 O  OE1 . GLU   A 1 189 ? -0.77566  22.26102 45.30659 1.000 62.86612  ? 196 GLU   A OE1 1 
ATOM   1399 O  OE2 . GLU   A 1 189 ? -2.16235  23.96308 45.28478 1.000 58.57232  ? 196 GLU   A OE2 1 
ATOM   1400 N  N   . TYR   A 1 190 ? -3.67491  21.58119 40.74799 1.000 52.15896  ? 197 TYR   A N   1 
ATOM   1401 C  CA  . TYR   A 1 190 ? -4.13485  22.49100 39.70970 1.000 51.17593  ? 197 TYR   A CA  1 
ATOM   1402 C  C   . TYR   A 1 190 ? -4.98046  21.79510 38.65107 1.000 50.83841  ? 197 TYR   A C   1 
ATOM   1403 O  O   . TYR   A 1 190 ? -5.32442  22.41695 37.63995 1.000 45.94104  ? 197 TYR   A O   1 
ATOM   1404 C  CB  . TYR   A 1 190 ? -2.93213  23.19081 39.07405 1.000 46.52636  ? 197 TYR   A CB  1 
ATOM   1405 C  CG  . TYR   A 1 190 ? -2.10277  23.93886 40.09216 1.000 49.94065  ? 197 TYR   A CG  1 
ATOM   1406 C  CD1 . TYR   A 1 190 ? -2.59123  25.08605 40.70274 1.000 47.94462  ? 197 TYR   A CD1 1 
ATOM   1407 C  CD2 . TYR   A 1 190 ? -0.84723  23.48069 40.46880 1.000 51.39324  ? 197 TYR   A CD2 1 
ATOM   1408 C  CE1 . TYR   A 1 190 ? -1.84406  25.76988 41.64380 1.000 49.75039  ? 197 TYR   A CE1 1 
ATOM   1409 C  CE2 . TYR   A 1 190 ? -0.09222  24.15761 41.41120 1.000 48.32040  ? 197 TYR   A CE2 1 
ATOM   1410 C  CZ  . TYR   A 1 190 ? -0.59646  25.30152 41.99468 1.000 49.97901  ? 197 TYR   A CZ  1 
ATOM   1411 O  OH  . TYR   A 1 190 ? 0.14781   25.98079 42.93195 1.000 51.54302  ? 197 TYR   A OH  1 
ATOM   1412 N  N   . LEU   A 1 191 ? -5.30983  20.52263 38.86076 1.000 52.05570  ? 198 LEU   A N   1 
ATOM   1413 C  CA  . LEU   A 1 191 ? -6.31476  19.82412 38.07465 1.000 54.78971  ? 198 LEU   A CA  1 
ATOM   1414 C  C   . LEU   A 1 191 ? -7.66310  19.77784 38.77763 1.000 54.52309  ? 198 LEU   A C   1 
ATOM   1415 O  O   . LEU   A 1 191 ? -8.62599  19.25108 38.21283 1.000 56.86112  ? 198 LEU   A O   1 
ATOM   1416 C  CB  . LEU   A 1 191 ? -5.84873  18.39903 37.75996 1.000 52.89081  ? 198 LEU   A CB  1 
ATOM   1417 C  CG  . LEU   A 1 191 ? -4.55062  18.26648 36.96250 1.000 56.43582  ? 198 LEU   A CG  1 
ATOM   1418 C  CD1 . LEU   A 1 191 ? -4.20553  16.80156 36.73842 1.000 57.69043  ? 198 LEU   A CD1 1 
ATOM   1419 C  CD2 . LEU   A 1 191 ? -4.66075  19.00596 35.63970 1.000 51.77962  ? 198 LEU   A CD2 1 
ATOM   1420 N  N   . GLU   A 1 192 ? -7.75123  20.31348 39.99244 1.000 54.33857  ? 199 GLU   A N   1 
ATOM   1421 C  CA  . GLU   A 1 192 ? -8.98986  20.32046 40.75505 1.000 56.13160  ? 199 GLU   A CA  1 
ATOM   1422 C  C   . GLU   A 1 192 ? -9.84699  21.51466 40.36090 1.000 56.88718  ? 199 GLU   A C   1 
ATOM   1423 O  O   . GLU   A 1 192 ? -9.33214  22.59892 40.07254 1.000 54.40056  ? 199 GLU   A O   1 
ATOM   1424 C  CB  . GLU   A 1 192 ? -8.69975  20.35669 42.25606 1.000 62.15412  ? 199 GLU   A CB  1 
ATOM   1425 C  CG  . GLU   A 1 192 ? -7.98247  19.12384 42.76903 1.000 61.56443  ? 199 GLU   A CG  1 
ATOM   1426 C  CD  . GLU   A 1 192 ? -8.94083  18.00012 43.10348 1.000 71.38155  ? 199 GLU   A CD  1 
ATOM   1427 O  OE1 . GLU   A 1 192 ? -10.08164 18.29371 43.52097 1.000 79.03450  ? 199 GLU   A OE1 1 
ATOM   1428 O  OE2 . GLU   A 1 192 ? -8.55550  16.82339 42.94433 1.000 80.44964  ? 199 GLU   A OE2 1 
ATOM   1429 N  N   . GLU   A 1 193 ? -11.16416 21.30597 40.36265 1.000 59.97264  ? 200 GLU   A N   1 
ATOM   1430 C  CA  . GLU   A 1 193 ? -12.08819 22.34165 39.91345 1.000 57.84122  ? 200 GLU   A CA  1 
ATOM   1431 C  C   . GLU   A 1 193 ? -12.09164 23.53423 40.86245 1.000 56.47151  ? 200 GLU   A C   1 
ATOM   1432 O  O   . GLU   A 1 193 ? -11.93023 24.68251 40.43324 1.000 51.86855  ? 200 GLU   A O   1 
ATOM   1433 C  CB  . GLU   A 1 193 ? -13.49263 21.75548 39.78071 1.000 58.96245  ? 200 GLU   A CB  1 
ATOM   1434 C  CG  . GLU   A 1 193 ? -14.56086 22.77753 39.45215 1.000 65.33887  ? 200 GLU   A CG  1 
ATOM   1435 C  CD  . GLU   A 1 193 ? -15.95546 22.18543 39.46374 1.000 75.47268  ? 200 GLU   A CD  1 
ATOM   1436 O  OE1 . GLU   A 1 193 ? -16.88783 22.84136 38.95328 1.000 77.04076  ? 200 GLU   A OE1 1 
ATOM   1437 O  OE2 . GLU   A 1 193 ? -16.11982 21.06391 39.98773 1.000 73.37393  ? 200 GLU   A OE2 1 
ATOM   1438 N  N   . ARG   A 1 194 ? -12.28199 23.28100 42.15949 1.000 57.32869  ? 201 ARG   A N   1 
ATOM   1439 C  CA  . ARG   A 1 194 ? -12.35761 24.37295 43.12459 1.000 56.80762  ? 201 ARG   A CA  1 
ATOM   1440 C  C   . ARG   A 1 194 ? -11.03235 25.11383 43.24562 1.000 56.57158  ? 201 ARG   A C   1 
ATOM   1441 O  O   . ARG   A 1 194 ? -11.01814 26.31125 43.55353 1.000 54.05075  ? 201 ARG   A O   1 
ATOM   1442 C  CB  . ARG   A 1 194 ? -12.79519 23.83503 44.48691 1.000 58.05602  ? 201 ARG   A CB  1 
ATOM   1443 C  CG  . ARG   A 1 194 ? -11.91512 22.71699 45.01478 1.000 72.58365  ? 201 ARG   A CG  1 
ATOM   1444 C  CD  . ARG   A 1 194 ? -12.46066 22.13806 46.30788 1.000 75.45324  ? 201 ARG   A CD  1 
ATOM   1445 N  NE  . ARG   A 1 194 ? -11.51963 21.20468 46.91517 1.000 94.46407  ? 201 ARG   A NE  1 
ATOM   1446 C  CZ  . ARG   A 1 194 ? -11.71442 20.59121 48.07422 1.000 88.95152  ? 201 ARG   A CZ  1 
ATOM   1447 N  NH1 . ARG   A 1 194 ? -12.81379 20.78710 48.78355 1.000 91.73194  ? 201 ARG   A NH1 1 
ATOM   1448 N  NH2 . ARG   A 1 194 ? -10.78187 19.76161 48.53404 1.000 89.30351  ? 201 ARG   A NH2 1 
ATOM   1449 N  N   . ARG   A 1 195 ? -9.91270  24.42618 43.00765 1.000 56.97168  ? 202 ARG   A N   1 
ATOM   1450 C  CA  . ARG   A 1 195 ? -8.61392  25.08872 43.06965 1.000 53.47845  ? 202 ARG   A CA  1 
ATOM   1451 C  C   . ARG   A 1 195 ? -8.42668  26.04507 41.89936 1.000 50.79094  ? 202 ARG   A C   1 
ATOM   1452 O  O   . ARG   A 1 195 ? -7.93336  27.16467 42.07816 1.000 48.39396  ? 202 ARG   A O   1 
ATOM   1453 C  CB  . ARG   A 1 195 ? -7.49443  24.04899 43.09611 1.000 54.51805  ? 202 ARG   A CB  1 
ATOM   1454 C  CG  . ARG   A 1 195 ? -6.09775  24.63780 43.21471 1.000 55.31796  ? 202 ARG   A CG  1 
ATOM   1455 C  CD  . ARG   A 1 195 ? -5.86278  25.24409 44.58770 1.000 53.37061  ? 202 ARG   A CD  1 
ATOM   1456 N  NE  . ARG   A 1 195 ? -4.46387  25.60427 44.78586 1.000 57.40119  ? 202 ARG   A NE  1 
ATOM   1457 C  CZ  . ARG   A 1 195 ? -4.02598  26.84347 44.96281 1.000 55.18710  ? 202 ARG   A CZ  1 
ATOM   1458 N  NH1 . ARG   A 1 195 ? -4.85632  27.87343 44.98804 1.000 50.19853  ? 202 ARG   A NH1 1 
ATOM   1459 N  NH2 . ARG   A 1 195 ? -2.72164  27.05510 45.11527 1.000 53.48610  ? 202 ARG   A NH2 1 
ATOM   1460 N  N   . ILE   A 1 196 ? -8.81289  25.62132 40.69415 1.000 49.75431  ? 203 ILE   A N   1 
ATOM   1461 C  CA  . ILE   A 1 196 ? -8.69462  26.49236 39.52863 1.000 52.31249  ? 203 ILE   A CA  1 
ATOM   1462 C  C   . ILE   A 1 196 ? -9.61122  27.70135 39.67154 1.000 51.99900  ? 203 ILE   A C   1 
ATOM   1463 O  O   . ILE   A 1 196 ? -9.22720  28.83028 39.34146 1.000 52.32617  ? 203 ILE   A O   1 
ATOM   1464 C  CB  . ILE   A 1 196 ? -8.98775  25.70349 38.23824 1.000 51.87583  ? 203 ILE   A CB  1 
ATOM   1465 C  CG1 . ILE   A 1 196 ? -7.89744  24.65987 37.98837 1.000 48.44360  ? 203 ILE   A CG1 1 
ATOM   1466 C  CG2 . ILE   A 1 196 ? -9.09822  26.64144 37.04720 1.000 51.27123  ? 203 ILE   A CG2 1 
ATOM   1467 C  CD1 . ILE   A 1 196 ? -8.33922  23.52314 37.09110 1.000 47.31655  ? 203 ILE   A CD1 1 
ATOM   1468 N  N   . LYS   A 1 197 ? -10.83200 27.48999 40.17529 1.000 50.11322  ? 204 LYS   A N   1 
ATOM   1469 C  CA  . LYS   A 1 197 ? -11.76165 28.60452 40.34188 1.000 49.86852  ? 204 LYS   A CA  1 
ATOM   1470 C  C   . LYS   A 1 197 ? -11.21381 29.63935 41.31534 1.000 52.65761  ? 204 LYS   A C   1 
ATOM   1471 O  O   . LYS   A 1 197 ? -11.35874 30.84834 41.09768 1.000 50.87427  ? 204 LYS   A O   1 
ATOM   1472 C  CB  . LYS   A 1 197 ? -13.12145 28.10275 40.82748 1.000 49.49545  ? 204 LYS   A CB  1 
ATOM   1473 C  CG  . LYS   A 1 197 ? -13.92775 27.33722 39.79775 1.000 59.70467  ? 204 LYS   A CG  1 
ATOM   1474 C  CD  . LYS   A 1 197 ? -15.40130 27.32906 40.17635 1.000 64.41250  ? 204 LYS   A CD  1 
ATOM   1475 C  CE  . LYS   A 1 197 ? -15.99813 25.93705 40.07312 1.000 71.72179  ? 204 LYS   A CE  1 
ATOM   1476 N  NZ  . LYS   A 1 197 ? -16.69038 25.71529 38.77565 1.000 80.65045  ? 204 LYS   A NZ  1 
ATOM   1477 N  N   . GLU   A 1 198 ? -10.58536 29.18182 42.39917 1.000 49.66824  ? 205 GLU   A N   1 
ATOM   1478 C  CA  . GLU   A 1 198 ? -10.04346 30.10764 43.38668 1.000 49.29657  ? 205 GLU   A CA  1 
ATOM   1479 C  C   . GLU   A 1 198 ? -8.89932  30.92914 42.80449 1.000 50.49925  ? 205 GLU   A C   1 
ATOM   1480 O  O   . GLU   A 1 198 ? -8.78343  32.12776 43.08529 1.000 47.77990  ? 205 GLU   A O   1 
ATOM   1481 C  CB  . GLU   A 1 198 ? -9.58781  29.33282 44.62305 1.000 51.30884  ? 205 GLU   A CB  1 
ATOM   1482 C  CG  . GLU   A 1 198 ? -8.69274  30.11173 45.57032 1.000 54.24417  ? 205 GLU   A CG  1 
ATOM   1483 C  CD  . GLU   A 1 198 ? -8.00400  29.21260 46.57680 1.000 57.90145  ? 205 GLU   A CD  1 
ATOM   1484 O  OE1 . GLU   A 1 198 ? -7.38541  28.21395 46.15228 1.000 61.69738  ? 205 GLU   A OE1 1 
ATOM   1485 O  OE2 . GLU   A 1 198 ? -8.08339  29.50057 47.78966 1.000 62.31288  ? 205 GLU   A OE2 1 
ATOM   1486 N  N   . ILE   A 1 199 ? -8.05545  30.30767 41.97798 1.000 45.67392  ? 206 ILE   A N   1 
ATOM   1487 C  CA  . ILE   A 1 199 ? -6.91974  31.02111 41.40130 1.000 52.10447  ? 206 ILE   A CA  1 
ATOM   1488 C  C   . ILE   A 1 199 ? -7.39008  32.02880 40.35938 1.000 48.17765  ? 206 ILE   A C   1 
ATOM   1489 O  O   . ILE   A 1 199 ? -6.87260  33.15017 40.28312 1.000 46.10075  ? 206 ILE   A O   1 
ATOM   1490 C  CB  . ILE   A 1 199 ? -5.90855  30.02188 40.81062 1.000 49.50699  ? 206 ILE   A CB  1 
ATOM   1491 C  CG1 . ILE   A 1 199 ? -5.35429  29.11639 41.91133 1.000 48.06829  ? 206 ILE   A CG1 1 
ATOM   1492 C  CG2 . ILE   A 1 199 ? -4.77792  30.75498 40.10316 1.000 48.10197  ? 206 ILE   A CG2 1 
ATOM   1493 C  CD1 . ILE   A 1 199 ? -4.76824  27.82473 41.39748 1.000 46.95673  ? 206 ILE   A CD1 1 
ATOM   1494 N  N   . VAL   A 1 200 ? -8.37550  31.64954 39.54212 1.000 46.08899  ? 207 VAL   A N   1 
ATOM   1495 C  CA  . VAL   A 1 200 ? -8.89572  32.56295 38.52746 1.000 49.90930  ? 207 VAL   A CA  1 
ATOM   1496 C  C   . VAL   A 1 200 ? -9.54537  33.77454 39.18418 1.000 52.15192  ? 207 VAL   A C   1 
ATOM   1497 O  O   . VAL   A 1 200 ? -9.32414  34.91917 38.76962 1.000 50.90964  ? 207 VAL   A O   1 
ATOM   1498 C  CB  . VAL   A 1 200 ? -9.87795  31.82402 37.59857 1.000 48.70471  ? 207 VAL   A CB  1 
ATOM   1499 C  CG1 . VAL   A 1 200 ? -10.62094 32.81068 36.70991 1.000 47.52000  ? 207 VAL   A CG1 1 
ATOM   1500 C  CG2 . VAL   A 1 200 ? -9.13925  30.79671 36.75573 1.000 42.62726  ? 207 VAL   A CG2 1 
ATOM   1501 N  N   . LYS   A 1 201 ? -10.34891 33.54347 40.22465 1.000 50.56361  ? 208 LYS   A N   1 
ATOM   1502 C  CA  . LYS   A 1 201 ? -11.00204 34.64548 40.92254 1.000 50.17002  ? 208 LYS   A CA  1 
ATOM   1503 C  C   . LYS   A 1 201 ? -9.99453  35.53318 41.64374 1.000 53.86500  ? 208 LYS   A C   1 
ATOM   1504 O  O   . LYS   A 1 201 ? -10.19694 36.74918 41.73997 1.000 55.70312  ? 208 LYS   A O   1 
ATOM   1505 C  CB  . LYS   A 1 201 ? -12.03121 34.09156 41.90895 1.000 52.44209  ? 208 LYS   A CB  1 
ATOM   1506 C  CG  . LYS   A 1 201 ? -12.66306 35.12768 42.82195 1.000 55.36368  ? 208 LYS   A CG  1 
ATOM   1507 C  CD  . LYS   A 1 201 ? -13.90977 34.57305 43.48931 1.000 59.87376  ? 208 LYS   A CD  1 
ATOM   1508 C  CE  . LYS   A 1 201 ? -14.50830 35.57152 44.46487 1.000 67.01735  ? 208 LYS   A CE  1 
ATOM   1509 N  NZ  . LYS   A 1 201 ? -15.79523 35.08096 45.03089 1.000 78.03145  ? 208 LYS   A NZ  1 
ATOM   1510 N  N   . LYS   A 1 202 ? -8.90125  34.95209 42.13911 1.000 52.58460  ? 209 LYS   A N   1 
ATOM   1511 C  CA  . LYS   A 1 202 ? -7.92946  35.71971 42.90971 1.000 53.44064  ? 209 LYS   A CA  1 
ATOM   1512 C  C   . LYS   A 1 202 ? -7.02478  36.56092 42.01559 1.000 52.24198  ? 209 LYS   A C   1 
ATOM   1513 O  O   . LYS   A 1 202 ? -6.72341  37.71303 42.34612 1.000 49.93606  ? 209 LYS   A O   1 
ATOM   1514 C  CB  . LYS   A 1 202 ? -7.09159  34.77634 43.77450 1.000 51.74155  ? 209 LYS   A CB  1 
ATOM   1515 C  CG  . LYS   A 1 202 ? -6.06911  35.46842 44.66153 1.000 53.52113  ? 209 LYS   A CG  1 
ATOM   1516 C  CD  . LYS   A 1 202 ? -5.39158  34.46980 45.58899 1.000 60.92770  ? 209 LYS   A CD  1 
ATOM   1517 C  CE  . LYS   A 1 202 ? -4.35828  35.14153 46.47837 1.000 63.80621  ? 209 LYS   A CE  1 
ATOM   1518 N  NZ  . LYS   A 1 202 ? -3.95079  34.26294 47.61120 1.000 69.39120  ? 209 LYS   A NZ  1 
ATOM   1519 N  N   . HIS   A 1 203 ? -6.58816  36.01365 40.88176 1.000 50.18388  ? 210 HIS   A N   1 
ATOM   1520 C  CA  . HIS   A 1 203 ? -5.56237  36.65278 40.06738 1.000 54.18968  ? 210 HIS   A CA  1 
ATOM   1521 C  C   . HIS   A 1 203 ? -6.05607  37.17071 38.72616 1.000 54.65811  ? 210 HIS   A C   1 
ATOM   1522 O  O   . HIS   A 1 203 ? -5.49885  38.14508 38.21673 1.000 56.77587  ? 210 HIS   A O   1 
ATOM   1523 C  CB  . HIS   A 1 203 ? -4.40510  35.67813 39.81851 1.000 48.48752  ? 210 HIS   A CB  1 
ATOM   1524 C  CG  . HIS   A 1 203 ? -3.70044  35.24816 41.06625 1.000 51.10860  ? 210 HIS   A CG  1 
ATOM   1525 N  ND1 . HIS   A 1 203 ? -2.99742  36.12557 41.86390 1.000 55.61633  ? 210 HIS   A ND1 1 
ATOM   1526 C  CD2 . HIS   A 1 203 ? -3.59242  34.03455 41.65674 1.000 55.30912  ? 210 HIS   A CD2 1 
ATOM   1527 C  CE1 . HIS   A 1 203 ? -2.48584  35.47084 42.89048 1.000 55.06623  ? 210 HIS   A CE1 1 
ATOM   1528 N  NE2 . HIS   A 1 203 ? -2.83197  34.19992 42.78865 1.000 56.51834  ? 210 HIS   A NE2 1 
ATOM   1529 N  N   . SER   A 1 204 ? -7.07636  36.54961 38.13826 1.000 51.40145  ? 211 SER   A N   1 
ATOM   1530 C  CA  . SER   A 1 204 ? -7.53975  36.90383 36.80224 1.000 47.83371  ? 211 SER   A CA  1 
ATOM   1531 C  C   . SER   A 1 204 ? -8.99829  37.34701 36.81595 1.000 50.59634  ? 211 SER   A C   1 
ATOM   1532 O  O   . SER   A 1 204 ? -9.75249  37.05877 35.88510 1.000 46.15596  ? 211 SER   A O   1 
ATOM   1533 C  CB  . SER   A 1 204 ? -7.34321  35.73214 35.84188 1.000 51.82576  ? 211 SER   A CB  1 
ATOM   1534 O  OG  . SER   A 1 204 ? -5.98848  35.31514 35.82208 1.000 47.27949  ? 211 SER   A OG  1 
ATOM   1535 N  N   . GLN   A 1 205 ? -9.40190  38.06057 37.86821 1.000 53.65061  ? 212 GLN   A N   1 
ATOM   1536 C  CA  . GLN   A 1 205 ? -10.80488 38.42573 38.02761 1.000 54.54380  ? 212 GLN   A CA  1 
ATOM   1537 C  C   . GLN   A 1 205 ? -11.26732 39.41570 36.96630 1.000 54.48826  ? 212 GLN   A C   1 
ATOM   1538 O  O   . GLN   A 1 205 ? -12.43650 39.38780 36.56586 1.000 52.83999  ? 212 GLN   A O   1 
ATOM   1539 C  CB  . GLN   A 1 205 ? -11.03285 39.00781 39.42141 1.000 56.56794  ? 212 GLN   A CB  1 
ATOM   1540 C  CG  . GLN   A 1 205 ? -12.48782 39.10257 39.82919 1.000 59.22750  ? 212 GLN   A CG  1 
ATOM   1541 C  CD  . GLN   A 1 205 ? -12.66477 39.83412 41.14171 1.000 71.04085  ? 212 GLN   A CD  1 
ATOM   1542 O  OE1 . GLN   A 1 205 ? -11.69127 40.12811 41.83576 1.000 69.22960  ? 212 GLN   A OE1 1 
ATOM   1543 N  NE2 . GLN   A 1 205 ? -13.90964 40.14037 41.48695 1.000 72.97491  ? 212 GLN   A NE2 1 
ATOM   1544 N  N   . PHE   A 1 206 ? -10.37574 40.28721 36.49434 1.000 51.74669  ? 213 PHE   A N   1 
ATOM   1545 C  CA  . PHE   A 1 206 ? -10.75671 41.39820 35.63161 1.000 49.00755  ? 213 PHE   A CA  1 
ATOM   1546 C  C   . PHE   A 1 206 ? -10.27199 41.22933 34.19567 1.000 50.10779  ? 213 PHE   A C   1 
ATOM   1547 O  O   . PHE   A 1 206 ? -10.17778 42.21701 33.45962 1.000 49.69163  ? 213 PHE   A O   1 
ATOM   1548 C  CB  . PHE   A 1 206 ? -10.23829 42.71129 36.21583 1.000 50.18294  ? 213 PHE   A CB  1 
ATOM   1549 C  CG  . PHE   A 1 206 ? -10.76474 43.00691 37.58833 1.000 53.50565  ? 213 PHE   A CG  1 
ATOM   1550 C  CD1 . PHE   A 1 206 ? -12.12639 42.98619 37.84066 1.000 52.77984  ? 213 PHE   A CD1 1 
ATOM   1551 C  CD2 . PHE   A 1 206 ? -9.89923  43.29038 38.62968 1.000 53.08825  ? 213 PHE   A CD2 1 
ATOM   1552 C  CE1 . PHE   A 1 206 ? -12.61528 43.25450 39.10393 1.000 55.38040  ? 213 PHE   A CE1 1 
ATOM   1553 C  CE2 . PHE   A 1 206 ? -10.38190 43.55655 39.89479 1.000 58.21351  ? 213 PHE   A CE2 1 
ATOM   1554 C  CZ  . PHE   A 1 206 ? -11.74130 43.53980 40.13255 1.000 57.26273  ? 213 PHE   A CZ  1 
ATOM   1555 N  N   . ILE   A 1 207 ? -9.96206  39.99934 33.78018 1.000 48.06826  ? 214 ILE   A N   1 
ATOM   1556 C  CA  . ILE   A 1 207 ? -9.61462  39.75650 32.38585 1.000 43.30642  ? 214 ILE   A CA  1 
ATOM   1557 C  C   . ILE   A 1 207 ? -10.83498 40.02263 31.51758 1.000 47.92363  ? 214 ILE   A C   1 
ATOM   1558 O  O   . ILE   A 1 207 ? -11.93767 39.53729 31.80016 1.000 50.13670  ? 214 ILE   A O   1 
ATOM   1559 C  CB  . ILE   A 1 207 ? -9.08935  38.32439 32.20683 1.000 46.11758  ? 214 ILE   A CB  1 
ATOM   1560 C  CG1 . ILE   A 1 207 ? -7.84481  38.10431 33.06921 1.000 41.56193  ? 214 ILE   A CG1 1 
ATOM   1561 C  CG2 . ILE   A 1 207 ? -8.78336  38.04239 30.74252 1.000 43.68656  ? 214 ILE   A CG2 1 
ATOM   1562 C  CD1 . ILE   A 1 207 ? -6.62984  38.86905 32.59385 1.000 40.71583  ? 214 ILE   A CD1 1 
ATOM   1563 N  N   . GLY   A 1 208 ? -10.64436 40.80229 30.45527 1.000 46.49034  ? 215 GLY   A N   1 
ATOM   1564 C  CA  . GLY   A 1 208 ? -11.75308 41.23537 29.62625 1.000 45.50321  ? 215 GLY   A CA  1 
ATOM   1565 C  C   . GLY   A 1 208 ? -12.21058 40.23340 28.58561 1.000 46.60532  ? 215 GLY   A C   1 
ATOM   1566 O  O   . GLY   A 1 208 ? -12.63653 40.62131 27.49352 1.000 42.87819  ? 215 GLY   A O   1 
ATOM   1567 N  N   . TYR   A 1 209 ? -12.13182 38.94422 28.90764 1.000 42.81654  ? 216 TYR   A N   1 
ATOM   1568 C  CA  . TYR   A 1 209 ? -12.57373 37.88411 28.01304 1.000 42.38203  ? 216 TYR   A CA  1 
ATOM   1569 C  C   . TYR   A 1 209 ? -13.12130 36.73901 28.85724 1.000 41.96622  ? 216 TYR   A C   1 
ATOM   1570 O  O   . TYR   A 1 209 ? -12.64657 36.52358 29.97517 1.000 43.87611  ? 216 TYR   A O   1 
ATOM   1571 C  CB  . TYR   A 1 209 ? -11.43302 37.38426 27.11295 1.000 46.30772  ? 216 TYR   A CB  1 
ATOM   1572 C  CG  . TYR   A 1 209 ? -10.83726 38.46287 26.23716 1.000 43.94187  ? 216 TYR   A CG  1 
ATOM   1573 C  CD1 . TYR   A 1 209 ? -11.44144 38.82360 25.03927 1.000 41.44600  ? 216 TYR   A CD1 1 
ATOM   1574 C  CD2 . TYR   A 1 209 ? -9.67381  39.12338 26.60946 1.000 44.18825  ? 216 TYR   A CD2 1 
ATOM   1575 C  CE1 . TYR   A 1 209 ? -10.90408 39.81223 24.23656 1.000 40.37717  ? 216 TYR   A CE1 1 
ATOM   1576 C  CE2 . TYR   A 1 209 ? -9.12808  40.11314 25.81279 1.000 43.47795  ? 216 TYR   A CE2 1 
ATOM   1577 C  CZ  . TYR   A 1 209 ? -9.74731  40.45303 24.62833 1.000 44.82223  ? 216 TYR   A CZ  1 
ATOM   1578 O  OH  . TYR   A 1 209 ? -9.20935  41.43643 23.83157 1.000 47.94353  ? 216 TYR   A OH  1 
ATOM   1579 N  N   . PRO   A 1 210 ? -14.11564 36.00945 28.35254 1.000 41.19575  ? 217 PRO   A N   1 
ATOM   1580 C  CA  . PRO   A 1 210 ? -14.68927 34.91033 29.14975 1.000 44.94589  ? 217 PRO   A CA  1 
ATOM   1581 C  C   . PRO   A 1 210 ? -13.67407 33.79725 29.36093 1.000 44.57093  ? 217 PRO   A C   1 
ATOM   1582 O  O   . PRO   A 1 210 ? -13.06191 33.30424 28.41104 1.000 42.72324  ? 217 PRO   A O   1 
ATOM   1583 C  CB  . PRO   A 1 210 ? -15.88252 34.43165 28.31031 1.000 44.35353  ? 217 PRO   A CB  1 
ATOM   1584 C  CG  . PRO   A 1 210 ? -15.74390 35.06165 26.97594 1.000 48.15287  ? 217 PRO   A CG  1 
ATOM   1585 C  CD  . PRO   A 1 210 ? -14.80698 36.21695 27.07176 1.000 45.74266  ? 217 PRO   A CD  1 
ATOM   1586 N  N   . ILE   A 1 211 ? -13.49739 33.40859 30.62005 1.000 40.24941  ? 218 ILE   A N   1 
ATOM   1587 C  CA  . ILE   A 1 211 ? -12.64059 32.29119 30.99807 1.000 40.78717  ? 218 ILE   A CA  1 
ATOM   1588 C  C   . ILE   A 1 211 ? -13.55256 31.15879 31.44881 1.000 44.22334  ? 218 ILE   A C   1 
ATOM   1589 O  O   . ILE   A 1 211 ? -14.20842 31.25642 32.49339 1.000 44.54675  ? 218 ILE   A O   1 
ATOM   1590 C  CB  . ILE   A 1 211 ? -11.64346 32.67716 32.09871 1.000 42.10662  ? 218 ILE   A CB  1 
ATOM   1591 C  CG1 . ILE   A 1 211 ? -10.82219 33.89693 31.67405 1.000 39.70338  ? 218 ILE   A CG1 1 
ATOM   1592 C  CG2 . ILE   A 1 211 ? -10.73020 31.50549 32.42255 1.000 39.85526  ? 218 ILE   A CG2 1 
ATOM   1593 C  CD1 . ILE   A 1 211 ? -10.05883 34.54188 32.80888 1.000 39.29318  ? 218 ILE   A CD1 1 
ATOM   1594 N  N   . THR   A 1 212 ? -13.59920 30.08484 30.66527 1.000 43.76671  ? 219 THR   A N   1 
ATOM   1595 C  CA  . THR   A 1 212 ? -14.49342 28.96189 30.91423 1.000 45.11417  ? 219 THR   A CA  1 
ATOM   1596 C  C   . THR   A 1 212 ? -13.69603 27.76301 31.40798 1.000 43.03064  ? 219 THR   A C   1 
ATOM   1597 O  O   . THR   A 1 212 ? -12.72475 27.35028 30.76609 1.000 44.90470  ? 219 THR   A O   1 
ATOM   1598 C  CB  . THR   A 1 212 ? -15.26895 28.58650 29.64903 1.000 45.22640  ? 219 THR   A CB  1 
ATOM   1599 O  OG1 . THR   A 1 212 ? -15.86008 29.76161 29.08096 1.000 41.08686  ? 219 THR   A OG1 1 
ATOM   1600 C  CG2 . THR   A 1 212 ? -16.36521 27.58513 29.97596 1.000 42.25794  ? 219 THR   A CG2 1 
ATOM   1601 N  N   . LEU   A 1 213 ? -14.11125 27.20520 32.54148 1.000 49.61740  ? 220 LEU   A N   1 
ATOM   1602 C  CA  . LEU   A 1 213 ? -13.49422 26.00389 33.08857 1.000 48.74565  ? 220 LEU   A CA  1 
ATOM   1603 C  C   . LEU   A 1 213 ? -14.23105 24.78782 32.53933 1.000 47.79607  ? 220 LEU   A C   1 
ATOM   1604 O  O   . LEU   A 1 213 ? -15.43918 24.63703 32.75466 1.000 48.97631  ? 220 LEU   A O   1 
ATOM   1605 C  CB  . LEU   A 1 213 ? -13.53418 26.02152 34.61832 1.000 49.48091  ? 220 LEU   A CB  1 
ATOM   1606 C  CG  . LEU   A 1 213 ? -13.23776 24.75135 35.43058 1.000 57.91223  ? 220 LEU   A CG  1 
ATOM   1607 C  CD1 . LEU   A 1 213 ? -12.05770 23.94552 34.86618 1.000 55.77176  ? 220 LEU   A CD1 1 
ATOM   1608 C  CD2 . LEU   A 1 213 ? -13.02090 25.09810 36.90460 1.000 58.95837  ? 220 LEU   A CD2 1 
ATOM   1609 N  N   . PHE   A 1 214 ? -13.50710 23.92941 31.82691 1.000 45.64788  ? 221 PHE   A N   1 
ATOM   1610 C  CA  . PHE   A 1 214 ? -14.05816 22.67561 31.32616 1.000 48.28024  ? 221 PHE   A CA  1 
ATOM   1611 C  C   . PHE   A 1 214 ? -13.91411 21.62819 32.42398 1.000 55.53984  ? 221 PHE   A C   1 
ATOM   1612 O  O   . PHE   A 1 214 ? -12.81053 21.13630 32.67905 1.000 62.64617  ? 221 PHE   A O   1 
ATOM   1613 C  CB  . PHE   A 1 214 ? -13.34221 22.23651 30.05113 1.000 49.10070  ? 221 PHE   A CB  1 
ATOM   1614 C  CG  . PHE   A 1 214 ? -13.80167 22.95155 28.80904 1.000 46.61626  ? 221 PHE   A CG  1 
ATOM   1615 C  CD1 . PHE   A 1 214 ? -14.33863 24.22689 28.87483 1.000 52.73745  ? 221 PHE   A CD1 1 
ATOM   1616 C  CD2 . PHE   A 1 214 ? -13.68624 22.34423 27.57021 1.000 50.86888  ? 221 PHE   A CD2 1 
ATOM   1617 C  CE1 . PHE   A 1 214 ? -14.75675 24.87974 27.73031 1.000 48.59707  ? 221 PHE   A CE1 1 
ATOM   1618 C  CE2 . PHE   A 1 214 ? -14.10168 22.99124 26.42190 1.000 56.14600  ? 221 PHE   A CE2 1 
ATOM   1619 C  CZ  . PHE   A 1 214 ? -14.63752 24.26078 26.50248 1.000 52.50320  ? 221 PHE   A CZ  1 
ATOM   1620 N  N   . VAL   A 1 215 ? -15.01642 21.29525 33.08078 1.000 51.49426  ? 222 VAL   A N   1 
ATOM   1621 C  CA  . VAL   A 1 215 ? -14.98630 20.32193 34.16562 1.000 58.64667  ? 222 VAL   A CA  1 
ATOM   1622 C  C   . VAL   A 1 215 ? -15.04753 18.91933 33.57505 1.000 55.68797  ? 222 VAL   A C   1 
ATOM   1623 O  O   . VAL   A 1 215 ? -15.65367 18.68257 32.52408 1.000 55.34864  ? 222 VAL   A O   1 
ATOM   1624 C  CB  . VAL   A 1 215 ? -16.12056 20.58293 35.18007 1.000 58.13288  ? 222 VAL   A CB  1 
ATOM   1625 C  CG1 . VAL   A 1 215 ? -16.22073 22.06891 35.47851 1.000 58.95796  ? 222 VAL   A CG1 1 
ATOM   1626 C  CG2 . VAL   A 1 215 ? -17.44092 20.06820 34.66129 1.000 55.56116  ? 222 VAL   A CG2 1 
ATOM   1627 N  N   . GLU   A 1 216 ? -14.39473 17.97859 34.25170 1.000 57.01489  ? 223 GLU   A N   1 
ATOM   1628 C  CA  . GLU   A 1 216 ? -14.17759 16.65541 33.69019 1.000 62.59380  ? 223 GLU   A CA  1 
ATOM   1629 C  C   . GLU   A 1 216 ? -15.41170 15.77030 33.86016 1.000 62.15666  ? 223 GLU   A C   1 
ATOM   1630 O  O   . GLU   A 1 216 ? -16.35182 16.08805 34.59406 1.000 62.40194  ? 223 GLU   A O   1 
ATOM   1631 C  CB  . GLU   A 1 216 ? -12.95648 15.99670 34.33201 1.000 65.69198  ? 223 GLU   A CB  1 
ATOM   1632 C  CG  . GLU   A 1 216 ? -11.64729 16.71348 34.03699 1.000 61.10597  ? 223 GLU   A CG  1 
ATOM   1633 C  CD  . GLU   A 1 216 ? -10.43845 15.80632 34.16094 1.000 63.50168  ? 223 GLU   A CD  1 
ATOM   1634 O  OE1 . GLU   A 1 216 ? -10.24913 14.94104 33.28006 1.000 65.26712  ? 223 GLU   A OE1 1 
ATOM   1635 O  OE2 . GLU   A 1 216 ? -9.67233  15.96461 35.13414 1.000 64.80147  ? 223 GLU   A OE2 1 
ATOM   1636 N  N   . LYS   A 1 217 ? -15.38801 14.63891 33.15996 1.000 68.62184  ? 224 LYS   A N   1 
ATOM   1637 C  CA  . LYS   A 1 217 ? -16.47902 13.66939 33.15892 1.000 72.11610  ? 224 LYS   A CA  1 
ATOM   1638 C  C   . LYS   A 1 217 ? -16.77933 13.15084 34.56115 1.000 70.00442  ? 224 LYS   A C   1 
ATOM   1639 O  O   . LYS   A 1 217 ? -16.14188 12.20989 35.03290 1.000 76.57592  ? 224 LYS   A O   1 
ATOM   1640 C  CB  . LYS   A 1 217 ? -16.13607 12.49956 32.23132 1.000 81.24280  ? 224 LYS   A CB  1 
ATOM   1641 C  CG  . LYS   A 1 217 ? -17.26975 11.51225 32.00826 1.000 86.73901  ? 224 LYS   A CG  1 
ATOM   1642 C  CD  . LYS   A 1 217 ? -16.89503 10.44154 30.98874 1.000 86.26843  ? 224 LYS   A CD  1 
ATOM   1643 C  CE  . LYS   A 1 217 ? -16.13816 9.27682  31.62358 1.000 83.33468  ? 224 LYS   A CE  1 
ATOM   1644 N  NZ  . LYS   A 1 217 ? -14.76486 9.61753  32.09403 1.000 92.38199  ? 224 LYS   A NZ  1 
HETATM 1645 C  C2  . A1AYO B 2 .   ? 9.57888   32.57551 24.24695 0.832 42.58166  ? 301 A1AYO A C2  1 
HETATM 1646 C  C3  . A1AYO B 2 .   ? 8.24731   32.44274 24.59258 0.832 43.98435  ? 301 A1AYO A C3  1 
HETATM 1647 C  C5  . A1AYO B 2 .   ? 5.19716   32.62965 24.65684 0.832 43.21191  ? 301 A1AYO A C5  1 
HETATM 1648 N  N1  . A1AYO B 2 .   ? 11.37627  32.22691 22.68093 0.832 47.66164  ? 301 A1AYO A N1  1 
HETATM 1649 C  C6  . A1AYO B 2 .   ? 3.94166   30.91525 24.43247 0.832 40.76694  ? 301 A1AYO A C6  1 
HETATM 1650 C  C4  . A1AYO B 2 .   ? 7.36921   31.81581 23.73094 0.832 44.72942  ? 301 A1AYO A C4  1 
HETATM 1651 C  C1  . A1AYO B 2 .   ? 10.05094  32.09297 23.02693 0.832 45.39709  ? 301 A1AYO A C1  1 
HETATM 1652 C  C7  . A1AYO B 2 .   ? 5.20204   30.57183 23.94094 0.832 42.91810  ? 301 A1AYO A C7  1 
HETATM 1653 C  C8  . A1AYO B 2 .   ? 7.81577   31.34002 22.51384 0.832 45.24611  ? 301 A1AYO A C8  1 
HETATM 1654 C  C9  . A1AYO B 2 .   ? 9.14696   31.47107 22.16644 0.832 43.66921  ? 301 A1AYO A C9  1 
HETATM 1655 N  N2  . A1AYO B 2 .   ? 5.99275   31.68903 24.08945 0.832 44.56054  ? 301 A1AYO A N2  1 
HETATM 1656 N  N3  . A1AYO B 2 .   ? 3.97991   32.18260 24.85977 0.832 44.11262  ? 301 A1AYO A N3  1 
HETATM 1657 CL CL1 . A1AYO B 2 .   ? 2.52515   29.95530 24.51940 0.832 42.48814  ? 301 A1AYO A CL1 1 
HETATM 1658 CL CL2 . A1AYO B 2 .   ? 5.70012   29.09031 23.28156 0.832 46.97281  ? 301 A1AYO A CL2 1 
HETATM 1659 C  C2  . A1AYO C 2 .   ? 5.77490   39.19278 23.57386 0.864 39.22249  ? 302 A1AYO A C2  1 
HETATM 1660 C  C3  . A1AYO C 2 .   ? 6.24907   38.39351 24.59690 0.864 40.13442  ? 302 A1AYO A C3  1 
HETATM 1661 C  C5  . A1AYO C 2 .   ? 5.49855   35.90083 27.00327 0.864 37.86859  ? 302 A1AYO A C5  1 
HETATM 1662 N  N1  . A1AYO C 2 .   ? 4.23184   39.57155 21.76340 0.864 43.40766  ? 302 A1AYO A N1  1 
HETATM 1663 C  C6  . A1AYO C 2 .   ? 7.45433   35.03372 27.11199 0.864 38.31143  ? 302 A1AYO A C6  1 
HETATM 1664 C  C4  . A1AYO C 2 .   ? 5.65418   37.17326 24.84940 0.864 40.81688  ? 302 A1AYO A C4  1 
HETATM 1665 C  C1  . A1AYO C 2 .   ? 4.70323   38.77873 22.78314 0.864 44.72474  ? 302 A1AYO A C1  1 
HETATM 1666 C  C7  . A1AYO C 2 .   ? 7.40281   35.78537 25.94023 0.864 36.90883  ? 302 A1AYO A C7  1 
HETATM 1667 C  C8  . A1AYO C 2 .   ? 4.59669   36.74279 24.07372 0.864 39.07852  ? 302 A1AYO A C8  1 
HETATM 1668 C  C9  . A1AYO C 2 .   ? 4.12173   37.53993 23.05003 0.864 43.64731  ? 302 A1AYO A C9  1 
HETATM 1669 N  N2  . A1AYO C 2 .   ? 6.14639   36.33871 25.89636 0.864 39.42087  ? 302 A1AYO A N2  1 
HETATM 1670 N  N3  . A1AYO C 2 .   ? 6.27202   35.13265 27.73502 0.864 37.17000  ? 302 A1AYO A N3  1 
HETATM 1671 CL CL1 . A1AYO C 2 .   ? 8.75488   34.10914 27.73526 0.864 41.52519  ? 302 A1AYO A CL1 1 
HETATM 1672 CL CL2 . A1AYO C 2 .   ? 8.61160   36.01995 24.77371 0.864 42.50470  ? 302 A1AYO A CL2 1 
HETATM 1673 O  O   . HOH   D 3 .   ? -15.00938 17.99237 30.60611 1.000 53.17740  ? 401 HOH   A O   1 
HETATM 1674 O  O   . HOH   D 3 .   ? 0.91250   39.16573 29.80904 1.000 47.95796  ? 402 HOH   A O   1 
HETATM 1675 O  O   . HOH   D 3 .   ? -3.67460  13.18246 37.39010 1.000 60.12587  ? 403 HOH   A O   1 
HETATM 1676 O  O   . HOH   D 3 .   ? 13.59539  19.97615 26.44182 1.000 40.67468  ? 404 HOH   A O   1 
HETATM 1677 O  O   . HOH   D 3 .   ? 10.72738  27.71538 41.55816 1.000 51.78712  ? 405 HOH   A O   1 
HETATM 1678 O  O   . HOH   D 3 .   ? -5.45206  16.30507 41.08282 1.000 60.57698  ? 406 HOH   A O   1 
HETATM 1679 O  O   . HOH   D 3 .   ? 14.12830  26.10440 10.39768 1.000 66.01672  ? 407 HOH   A O   1 
HETATM 1680 O  O   . HOH   D 3 .   ? 15.51606  25.17759 8.84200  1.000 72.58097  ? 408 HOH   A O   1 
HETATM 1681 O  O   . HOH   D 3 .   ? -0.49276  19.91726 44.42603 1.000 56.77936  ? 409 HOH   A O   1 
HETATM 1682 O  O   . HOH   D 3 .   ? 14.51124  19.30538 23.20860 1.000 49.64533  ? 410 HOH   A O   1 
HETATM 1683 O  O   . HOH   D 3 .   ? 2.74873   36.93562 31.95819 1.000 44.94862  ? 411 HOH   A O   1 
HETATM 1684 O  O   . HOH   D 3 .   ? -4.21857  41.88033 28.19561 1.000 44.91096  ? 412 HOH   A O   1 
HETATM 1685 O  O   . HOH   D 3 .   ? -14.13638 30.85228 27.50831 1.000 41.17073  ? 413 HOH   A O   1 
HETATM 1686 O  O   . HOH   D 3 .   ? 17.38935  25.28040 31.71047 1.000 47.85543  ? 414 HOH   A O   1 
HETATM 1687 O  O   . HOH   D 3 .   ? 11.82082  37.42049 12.18848 1.000 65.00979  ? 415 HOH   A O   1 
HETATM 1688 O  O   . HOH   D 3 .   ? 6.63468   32.64271 10.01349 1.000 47.68936  ? 416 HOH   A O   1 
HETATM 1689 O  O   . HOH   D 3 .   ? -6.52209  47.75926 13.41458 1.000 53.32109  ? 417 HOH   A O   1 
HETATM 1690 O  O   . HOH   D 3 .   ? -4.35572  36.79964 34.45594 1.000 43.74341  ? 418 HOH   A O   1 
HETATM 1691 O  O   . HOH   D 3 .   ? -10.53586 35.35362 4.90962  1.000 64.55646  ? 419 HOH   A O   1 
HETATM 1692 O  O   . HOH   D 3 .   ? -5.47335  19.14329 29.53520 1.000 44.58623  ? 420 HOH   A O   1 
HETATM 1693 O  O   . HOH   D 3 .   ? 6.29803   36.54184 12.14196 1.000 51.54448  ? 421 HOH   A O   1 
HETATM 1694 O  O   . HOH   D 3 .   ? -3.61323  35.64758 13.56483 1.000 39.95339  ? 422 HOH   A O   1 
HETATM 1695 O  O   . HOH   D 3 .   ? -2.84729  33.19914 20.92653 1.000 33.12671  ? 423 HOH   A O   1 
HETATM 1696 O  O   . HOH   D 3 .   ? -7.94380  41.56016 29.74706 1.000 41.39469  ? 424 HOH   A O   1 
HETATM 1697 O  O   . HOH   D 3 .   ? -17.69347 24.89089 34.08040 1.000 44.80102  ? 425 HOH   A O   1 
HETATM 1698 O  O   . HOH   D 3 .   ? 1.60748   24.11479 44.06850 1.000 53.17095  ? 426 HOH   A O   1 
HETATM 1699 O  O   . HOH   D 3 .   ? 8.22449   20.38250 10.57161 1.000 63.39489  ? 427 HOH   A O   1 
HETATM 1700 O  O   . HOH   D 3 .   ? 0.92013   30.17157 12.69447 1.000 46.51917  ? 428 HOH   A O   1 
HETATM 1701 O  O   . HOH   D 3 .   ? 4.02996   38.90483 37.27868 1.000 43.64829  ? 429 HOH   A O   1 
HETATM 1702 O  O   . HOH   D 3 .   ? 1.53758   39.36867 34.02425 1.000 43.21881  ? 430 HOH   A O   1 
HETATM 1703 O  O   . HOH   D 3 .   ? 11.70577  33.05347 19.36763 1.000 48.54655  ? 431 HOH   A O   1 
HETATM 1704 O  O   . HOH   D 3 .   ? 10.08741  18.06824 22.07111 1.000 52.85378  ? 432 HOH   A O   1 
HETATM 1705 O  O   . HOH   D 3 .   ? 7.71528   20.42697 18.61060 1.000 43.12160  ? 433 HOH   A O   1 
HETATM 1706 O  O   . HOH   D 3 .   ? -7.66099  45.42429 21.41082 1.000 42.64900  ? 434 HOH   A O   1 
HETATM 1707 O  O   . HOH   D 3 .   ? 15.82591  17.31866 15.65967 1.000 55.38525  ? 435 HOH   A O   1 
HETATM 1708 O  O   . HOH   D 3 .   ? -12.43785 31.90497 17.58146 1.000 46.49065  ? 436 HOH   A O   1 
HETATM 1709 O  O   . HOH   D 3 .   ? 0.53302   37.98272 21.97039 1.000 42.06936  ? 437 HOH   A O   1 
HETATM 1710 O  O   . HOH   D 3 .   ? -5.99668  44.91155 10.64966 1.000 46.83665  ? 438 HOH   A O   1 
HETATM 1711 O  O   . HOH   D 3 .   ? 9.72380   24.87171 40.33791 1.000 57.63572  ? 439 HOH   A O   1 
HETATM 1712 O  O   . HOH   D 3 .   ? -2.57264  38.82927 41.39081 1.000 55.69733  ? 440 HOH   A O   1 
HETATM 1713 O  O   . HOH   D 3 .   ? 17.42009  44.11694 29.54284 1.000 54.15802  ? 441 HOH   A O   1 
HETATM 1714 O  O   . HOH   D 3 .   ? 6.89112   14.48540 38.30278 1.000 59.63270  ? 442 HOH   A O   1 
HETATM 1715 O  O   . HOH   D 3 .   ? -13.87564 14.79688 30.77035 1.000 66.85133  ? 443 HOH   A O   1 
HETATM 1716 O  O   . HOH   D 3 .   ? -8.69555  43.29868 27.40226 1.000 52.97321  ? 444 HOH   A O   1 
HETATM 1717 O  O   . HOH   D 3 .   ? 9.59508   15.49060 30.15410 1.000 57.69918  ? 445 HOH   A O   1 
HETATM 1718 O  O   . HOH   D 3 .   ? 15.90174  25.08026 29.16624 1.000 42.62042  ? 446 HOH   A O   1 
HETATM 1719 O  O   . HOH   D 3 .   ? 2.19663   36.78033 17.08012 1.000 48.29526  ? 447 HOH   A O   1 
HETATM 1720 O  O   . HOH   D 3 .   ? 2.64327   41.45575 24.26264 1.000 51.89826  ? 448 HOH   A O   1 
HETATM 1721 O  O   . HOH   D 3 .   ? -15.39341 37.91022 23.96144 1.000 50.83055  ? 449 HOH   A O   1 
HETATM 1722 O  O   . HOH   D 3 .   ? 5.87303   23.93340 48.95354 1.000 58.86335  ? 450 HOH   A O   1 
HETATM 1723 O  O   . HOH   D 3 .   ? 8.40753   24.41512 8.71174  1.000 62.04786  ? 451 HOH   A O   1 
HETATM 1724 O  O   . HOH   D 3 .   ? 2.79040   40.62297 31.31073 1.000 43.84562  ? 452 HOH   A O   1 
HETATM 1725 O  O   . HOH   D 3 .   ? -10.03948 33.47536 45.28801 1.000 52.45466  ? 453 HOH   A O   1 
HETATM 1726 O  O   . HOH   D 3 .   ? 4.66674   38.08700 30.51515 1.000 40.86286  ? 454 HOH   A O   1 
HETATM 1727 O  O   . HOH   D 3 .   ? 19.24797  27.12180 39.10626 1.000 57.78141  ? 455 HOH   A O   1 
HETATM 1728 O  O   . HOH   D 3 .   ? 16.13689  45.10913 36.32037 1.000 59.65433  ? 456 HOH   A O   1 
HETATM 1729 O  O   . HOH   D 3 .   ? 17.13758  41.34694 22.53677 1.000 52.29305  ? 457 HOH   A O   1 
HETATM 1730 O  O   . HOH   D 3 .   ? -13.42790 31.77285 39.25602 1.000 54.35274  ? 458 HOH   A O   1 
HETATM 1731 O  O   . HOH   D 3 .   ? -2.77263  44.22949 25.35284 1.000 51.95236  ? 459 HOH   A O   1 
HETATM 1732 O  O   . HOH   D 3 .   ? -16.43419 28.35209 33.94350 1.000 49.12296  ? 460 HOH   A O   1 
HETATM 1733 O  O   . HOH   D 3 .   ? -10.32230 30.85583 16.42926 1.000 51.69968  ? 461 HOH   A O   1 
HETATM 1734 O  O   . HOH   D 3 .   ? -11.38436 43.18647 26.74718 1.000 47.71345  ? 462 HOH   A O   1 
HETATM 1735 O  O   . HOH   D 3 .   ? -8.86617  46.20292 26.49692 1.000 53.63048  ? 463 HOH   A O   1 
HETATM 1736 O  O   . HOH   D 3 .   ? -13.20777 18.84126 36.83440 1.000 57.11132  ? 464 HOH   A O   1 
HETATM 1737 O  O   . HOH   D 3 .   ? -2.80239  29.73143 25.54005 1.000 40.27202  ? 465 HOH   A O   1 
HETATM 1738 O  O   . HOH   D 3 .   ? 14.93525  17.36994 20.60969 1.000 48.70494  ? 466 HOH   A O   1 
HETATM 1739 O  O   . HOH   D 3 .   ? 12.985    44.270   28.363   1.000 54.87049  ? 467 HOH   A O   1 
HETATM 1740 O  O   . HOH   D 3 .   ? -13.85368 36.07051 32.69203 1.000 58.96338  ? 468 HOH   A O   1 
HETATM 1741 O  O   . HOH   D 3 .   ? -1.06520  31.21906 27.33259 1.000 41.98076  ? 469 HOH   A O   1 
HETATM 1742 O  O   . HOH   D 3 .   ? -3.84352  38.21009 12.10674 1.000 44.87060  ? 470 HOH   A O   1 
HETATM 1743 O  O   . HOH   D 3 .   ? -7.97373  39.61850 40.33313 1.000 61.54990  ? 471 HOH   A O   1 
HETATM 1744 O  O   . HOH   D 3 .   ? -12.98510 43.02437 32.59634 1.000 50.91215  ? 472 HOH   A O   1 
HETATM 1745 O  O   . HOH   D 3 .   ? 5.300     42.349   22.424   1.000 47.76279  ? 473 HOH   A O   1 
HETATM 1746 O  O   . HOH   D 3 .   ? 2.39576   39.17385 25.94598 1.000 49.33479  ? 474 HOH   A O   1 
HETATM 1747 O  O   . HOH   D 3 .   ? -14.47627 40.74528 25.04132 1.000 52.04143  ? 475 HOH   A O   1 
HETATM 1748 O  O   . HOH   D 3 .   ? 14.54233  44.70549 42.39876 1.000 67.15410  ? 476 HOH   A O   1 
HETATM 1749 O  O   . HOH   D 3 .   ? 2.79244   24.62472 46.83871 1.000 55.47834  ? 477 HOH   A O   1 
HETATM 1750 O  O   . HOH   D 3 .   ? 4.55356   22.78065 45.73259 1.000 56.09444  ? 478 HOH   A O   1 
HETATM 1751 O  O   . HOH   D 3 .   ? 15.65541  31.32994 23.61776 1.000 30.38656  ? 479 HOH   A O   1 
HETATM 1752 O  O   . HOH   D 3 .   ? 4.59892   39.11088 27.55551 1.000 40.66533  ? 480 HOH   A O   1 
HETATM 1753 O  O   . HOH   D 3 .   ? -11.05446 24.85992 23.40272 1.000 46.65367  ? 481 HOH   A O   1 
HETATM 1754 O  O   . HOH   D 3 .   ? -18.63336 16.15552 36.75559 1.000 58.43627  ? 482 HOH   A O   1 
HETATM 1755 O  O   . HOH   D 3 .   ? -2.424    44.059   16.995   1.000 60.61044  ? 483 HOH   A O   1 
HETATM 1756 O  O   . HOH   D 3 .   ? 2.13198   14.89984 32.72686 1.000 59.13141  ? 484 HOH   A O   1 
HETATM 1757 O  O   . HOH   D 3 .   ? 9.324     45.119   30.644   1.000 55.49536  ? 485 HOH   A O   1 
HETATM 1758 O  O   . HOH   D 3 .   ? -6.75299  17.31389 27.47449 1.000 54.79275  ? 486 HOH   A O   1 
HETATM 1759 O  O   . HOH   D 3 .   ? -14.47653 39.62877 33.91502 1.000 61.46523  ? 487 HOH   A O   1 
HETATM 1760 O  O   . HOH   D 3 .   ? -14.04529 42.11800 23.44307 1.000 58.20317  ? 488 HOH   A O   1 
HETATM 1761 O  O   . HOH   D 3 .   ? 16.64480  23.15114 33.24489 1.000 52.49410  ? 489 HOH   A O   1 
HETATM 1762 O  O   . HOH   D 3 .   ? -1.66187  43.53912 23.85293 1.000 57.05205  ? 490 HOH   A O   1 
HETATM 1763 O  O   . HOH   D 3 .   ? 7.938     44.035   29.588   1.000 55.44356  ? 491 HOH   A O   1 
HETATM 1764 O  O   . HOH   D 3 .   ? 3.07325   41.44584 38.46276 1.000 58.08686  ? 492 HOH   A O   1 
HETATM 1765 O  O   . HOH   D 3 .   ? -3.304    45.154   21.092   1.000 53.15435  ? 493 HOH   A O   1 
HETATM 1766 O  O   . HOH   D 3 .   ? -14.14531 42.19595 34.91168 1.000 59.31971  ? 494 HOH   A O   1 
HETATM 1767 O  O   . HOH   D 3 .   ? 19.08714  41.81256 24.96899 1.000 54.55952  ? 495 HOH   A O   1 
HETATM 1768 O  O   . HOH   D 3 .   ? -13.63641 34.54223 38.38952 1.000 57.93374  ? 496 HOH   A O   1 
HETATM 1769 O  O   . HOH   D 3 .   ? 11.879    44.196   30.771   1.000 52.76580  ? 497 HOH   A O   1 
HETATM 1770 O  O   . HOH   D 3 .   ? -12.25965 17.78242 29.72107 1.000 58.98124  ? 498 HOH   A O   1 
HETATM 1771 O  O   . HOH   D 3 .   ? -5.10992  13.87151 40.17644 1.000 58.43229  ? 499 HOH   A O   1 
HETATM 1772 O  O   . HOH   D 3 .   ? 2.18704   43.32348 18.88812 1.000 55.27500  ? 500 HOH   A O   1 
HETATM 1773 O  O   . HOH   D 3 .   ? -15.549   42.770   29.403   1.000 52.06409  ? 501 HOH   A O   1 
HETATM 1774 O  O   . HOH   D 3 .   ? -15.28543 41.96811 31.40462 1.000 57.11105  ? 502 HOH   A O   1 
HETATM 1775 O  O   . HOH   D 3 .   ? -10.36063 35.99609 45.91189 1.000 55.01527  ? 503 HOH   A O   1 
HETATM 1776 O  O   . HOH   D 3 .   ? 4.04854   42.07896 28.11200 1.000 57.94134  ? 504 HOH   A O   1 
HETATM 1777 O  O   . HOH   D 3 .   ? -13.57229 29.98797 36.64800 1.000 56.71604  ? 505 HOH   A O   1 
HETATM 1778 O  O   . HOH   D 3 .   ? 18.97093  44.01372 27.01723 1.000 51.36568  ? 506 HOH   A O   1 
HETATM 1779 O  O   . HOH   D 3 .   ? -17.80020 37.42270 24.81200 1.000 54.40807  ? 507 HOH   A O   1 
HETATM 1780 O  O   . HOH   D 3 .   ? -11.16672 17.48176 27.43362 1.000 48.48812  ? 508 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   ? 1.01650 1.11469 0.99385 0.00474  -0.11459 -0.35952 16  GLU A N   
2    C CA  . GLU A 9   ? 1.05952 1.15363 1.01878 0.03401  -0.09935 -0.33631 16  GLU A CA  
3    C C   . GLU A 9   ? 0.94677 1.05030 0.93010 0.03964  -0.09377 -0.29909 16  GLU A C   
4    O O   . GLU A 9   ? 0.93348 1.07863 0.91634 0.04360  -0.10185 -0.28442 16  GLU A O   
5    C CB  . GLU A 9   ? 1.20301 1.33601 1.12091 0.05275  -0.10388 -0.34203 16  GLU A CB  
6    C CG  . GLU A 9   ? 1.26419 1.37702 1.15389 0.07714  -0.08504 -0.33742 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.45092 1.57537 1.33980 0.09594  -0.07190 -0.30026 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.31011 1.44738 1.22180 0.09110  -0.07581 -0.27785 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.45949 1.57880 1.32430 0.11481  -0.05615 -0.29410 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.86815 0.93353 0.87055 0.04183  -0.08000 -0.28460 17  VAL A N   
11   C CA  . VAL A 10  ? 0.72333 0.79147 0.74811 0.04461  -0.07479 -0.25336 17  VAL A CA  
12   C C   . VAL A 10  ? 0.63475 0.68926 0.65158 0.06390  -0.05834 -0.23667 17  VAL A C   
13   O O   . VAL A 10  ? 0.72233 0.74852 0.73899 0.06932  -0.04848 -0.24477 17  VAL A O   
14   C CB  . VAL A 10  ? 0.71631 0.75763 0.77428 0.02685  -0.07502 -0.25002 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.60707 0.65670 0.68333 0.03034  -0.07131 -0.21973 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.79417 0.84694 0.86306 0.00255  -0.08881 -0.26987 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.64842 0.72315 0.65964 0.07402  -0.05443 -0.21369 18  GLU A N   
18   C CA  . GLU A 11  ? 0.67091 0.73622 0.67893 0.08675  -0.03844 -0.19683 18  GLU A CA  
19   C C   . GLU A 11  ? 0.60178 0.65514 0.63768 0.08103  -0.03560 -0.17804 18  GLU A C   
20   O O   . GLU A 11  ? 0.57984 0.64314 0.62499 0.07498  -0.04266 -0.16717 18  GLU A O   
21   C CB  . GLU A 11  ? 0.64452 0.73116 0.62457 0.10029  -0.03286 -0.18355 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.74047 0.84187 0.68639 0.11035  -0.03390 -0.19940 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.82337 0.94341 0.73829 0.12632  -0.02713 -0.18157 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.81844 0.95399 0.73245 0.12836  -0.03414 -0.16748 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.88736 1.00546 0.77776 0.13847  -0.01299 -0.18027 18  GLU A OE2 
26   N N   . THR A 12  ? 0.53967 0.57605 0.58811 0.08459  -0.02540 -0.17458 19  THR A N   
27   C CA  . THR A 12  ? 0.54260 0.57114 0.61447 0.08093  -0.02334 -0.15842 19  THR A CA  
28   C C   . THR A 12  ? 0.54082 0.57795 0.60853 0.08647  -0.01193 -0.14357 19  THR A C   
29   O O   . THR A 12  ? 0.55091 0.59198 0.61124 0.09370  -0.00097 -0.14688 19  THR A O   
30   C CB  . THR A 12  ? 0.54573 0.55328 0.63665 0.08174  -0.02146 -0.16438 19  THR A CB  
31   O OG1 . THR A 12  ? 0.54277 0.53348 0.63401 0.07439  -0.02888 -0.18047 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.51844 0.52243 0.63050 0.07882  -0.02239 -0.14751 19  THR A CG2 
33   N N   . PHE A 13  ? 0.54102 0.58003 0.61308 0.08205  -0.01307 -0.12808 20  PHE A N   
34   C CA  . PHE A 13  ? 0.52322 0.56399 0.59099 0.08256  -0.00200 -0.11527 20  PHE A CA  
35   C C   . PHE A 13  ? 0.56625 0.60321 0.65649 0.07613  -0.00335 -0.10801 20  PHE A C   
36   O O   . PHE A 13  ? 0.57923 0.61141 0.68185 0.07312  -0.01288 -0.10693 20  PHE A O   
37   C CB  . PHE A 13  ? 0.51460 0.55605 0.55973 0.08520  -0.00024 -0.10403 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.58584 0.63770 0.60580 0.09435  -0.00189 -0.10924 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.58980 0.65325 0.61065 0.09371  -0.01636 -0.11929 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.57882 0.63110 0.57342 0.10280  0.01129  -0.10380 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.60248 0.68265 0.59942 0.10201  -0.02052 -0.12618 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.66653 0.73183 0.63349 0.11417  0.00885  -0.10768 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.67906 0.76079 0.64712 0.11414  -0.00853 -0.12000 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.53588 0.57717 0.63075 0.07311  0.00662  -0.10313 21  ALA A N   
45   C CA  . ALA A 14  ? 0.55976 0.60361 0.67296 0.06624  0.00421  -0.09790 21  ALA A CA  
46   C C   . ALA A 14  ? 0.57800 0.61065 0.67734 0.05960  0.00647  -0.08836 21  ALA A C   
47   O O   . ALA A 14  ? 0.57666 0.60115 0.65670 0.05885  0.01727  -0.08402 21  ALA A O   
48   C CB  . ALA A 14  ? 0.56103 0.62282 0.69163 0.06415  0.01253  -0.10084 21  ALA A CB  
49   N N   . PHE A 15  ? 0.52073 0.54966 0.62658 0.05671  -0.00209 -0.08441 22  PHE A N   
50   C CA  . PHE A 15  ? 0.56962 0.58491 0.66117 0.05162  0.00109  -0.07748 22  PHE A CA  
51   C C   . PHE A 15  ? 0.62716 0.64216 0.72072 0.03985  0.01115  -0.07929 22  PHE A C   
52   O O   . PHE A 15  ? 0.53153 0.56695 0.64642 0.03495  0.01097  -0.08506 22  PHE A O   
53   C CB  . PHE A 15  ? 0.55580 0.57024 0.65335 0.05162  -0.00922 -0.07412 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.54918 0.56135 0.64165 0.05889  -0.01528 -0.06964 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.51271 0.51690 0.58518 0.06421  -0.01126 -0.06373 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.53594 0.55483 0.64450 0.06054  -0.02388 -0.07060 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.52736 0.54000 0.60034 0.06993  -0.01732 -0.06008 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.54387 0.56445 0.65207 0.06256  -0.02838 -0.06735 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.52196 0.54429 0.61456 0.06668  -0.02592 -0.06269 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.60047 0.59244 0.67222 0.03526  0.02102  -0.07441 23  GLN A N   
61   C CA  . GLN A 16  ? 0.62798 0.61417 0.70168 0.01843  0.03095  -0.07777 23  GLN A CA  
62   C C   . GLN A 16  ? 0.59227 0.59284 0.68307 0.00957  0.01924  -0.08445 23  GLN A C   
63   O O   . GLN A 16  ? 0.58835 0.58694 0.67586 0.01724  0.00808  -0.08226 23  GLN A O   
64   C CB  . GLN A 16  ? 0.60803 0.55516 0.65000 0.01626  0.04535  -0.07095 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.60190 0.53665 0.62417 0.02463  0.05997  -0.06255 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.69261 0.58552 0.67814 0.03233  0.07266  -0.05138 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.74361 0.60584 0.71432 0.02076  0.09050  -0.04856 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.64544 0.53683 0.61657 0.05221  0.06475  -0.04455 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.63444 0.65450 0.74415 -0.00654 0.02200  -0.09239 24  ALA A N   
70   C CA  . ALA A 17  ? 0.58572 0.63131 0.71371 -0.01329 0.00844  -0.09988 24  ALA A CA  
71   C C   . ALA A 17  ? 0.57293 0.59356 0.67861 -0.01623 0.00375  -0.10090 24  ALA A C   
72   O O   . ALA A 17  ? 0.59411 0.62918 0.70383 -0.00979 -0.01044 -0.10153 24  ALA A O   
73   C CB  . ALA A 17  ? 0.50688 0.58204 0.65873 -0.03346 0.01324  -0.10966 24  ALA A CB  
74   N N   . GLU A 18  ? 0.61028 0.59068 0.68903 -0.02348 0.01716  -0.10006 25  GLU A N   
75   C CA  . GLU A 18  ? 0.67126 0.62295 0.72447 -0.02363 0.01540  -0.10208 25  GLU A CA  
76   C C   . GLU A 18  ? 0.65727 0.60443 0.69936 -0.00051 0.00790  -0.09125 25  GLU A C   
77   O O   . GLU A 18  ? 0.62195 0.56993 0.65627 0.00370  -0.00083 -0.09265 25  GLU A O   
78   C CB  . GLU A 18  ? 0.80909 0.71126 0.83324 -0.03339 0.03478  -0.10239 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.84165 0.74330 0.87644 -0.06236 0.04519  -0.11392 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.84749 0.76200 0.89772 -0.06495 0.05730  -0.10726 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.81270 0.73743 0.86404 -0.04363 0.05526  -0.09600 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.88204 0.79770 0.94303 -0.08954 0.06946  -0.11426 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.62326 0.56893 0.66456 0.01367  0.01141  -0.08101 26  ILE A N   
84   C CA  . ILE A 19  ? 0.60164 0.54841 0.63692 0.03185  0.00508  -0.07166 26  ILE A CA  
85   C C   . ILE A 19  ? 0.59965 0.57678 0.65823 0.03546  -0.00974 -0.07166 26  ILE A C   
86   O O   . ILE A 19  ? 0.61817 0.59672 0.67206 0.04263  -0.01586 -0.06713 26  ILE A O   
87   C CB  . ILE A 19  ? 0.61204 0.55506 0.64097 0.04377  0.01108  -0.06345 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.66727 0.57573 0.66412 0.05086  0.02507  -0.05683 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.54988 0.51263 0.58948 0.05599  0.00047  -0.05798 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.68859 0.57112 0.67332 0.03826  0.04061  -0.05961 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.53946 0.53941 0.62171 0.03241  -0.01368 -0.07535 27  ALA A N   
92   C CA  . ALA A 20  ? 0.58275 0.60491 0.68446 0.03903  -0.02541 -0.07343 27  ALA A CA  
93   C C   . ALA A 20  ? 0.56295 0.59535 0.66365 0.03645  -0.03376 -0.07536 27  ALA A C   
94   O O   . ALA A 20  ? 0.49510 0.53398 0.59779 0.04588  -0.04137 -0.06831 27  ALA A O   
95   C CB  . ALA A 20  ? 0.49862 0.54095 0.62313 0.03928  -0.02576 -0.07780 27  ALA A CB  
96   N N   . GLN A 21  ? 0.53822 0.57195 0.63423 0.02278  -0.03193 -0.08517 28  GLN A N   
97   C CA  . GLN A 21  ? 0.57305 0.61980 0.66435 0.01892  -0.04147 -0.09060 28  GLN A CA  
98   C C   . GLN A 21  ? 0.61159 0.63219 0.67304 0.02380  -0.03967 -0.08755 28  GLN A C   
99   O O   . GLN A 21  ? 0.63542 0.66693 0.68866 0.02784  -0.04858 -0.08795 28  GLN A O   
100  C CB  . GLN A 21  ? 0.64924 0.70992 0.74853 -0.00168 -0.04048 -0.10576 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.72714 0.78416 0.80834 -0.01442 -0.04513 -0.11826 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.80224 0.85531 0.88683 -0.04138 -0.03716 -0.13429 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.73065 0.80313 0.84033 -0.05031 -0.03193 -0.13579 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.72781 0.75504 0.78680 -0.05541 -0.03489 -0.14705 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.60549 0.59451 0.64915 0.02669  -0.02789 -0.08339 29  LEU A N   
106  C CA  . LEU A 22  ? 0.65698 0.62575 0.67516 0.03728  -0.02460 -0.07760 29  LEU A CA  
107  C C   . LEU A 22  ? 0.60525 0.58903 0.63310 0.05223  -0.02958 -0.06342 29  LEU A C   
108  O O   . LEU A 22  ? 0.57148 0.55719 0.58722 0.06010  -0.03200 -0.05833 29  LEU A O   
109  C CB  . LEU A 22  ? 0.64504 0.57917 0.64208 0.04001  -0.00981 -0.07561 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.70698 0.62266 0.67869 0.05564  -0.00374 -0.06817 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.68954 0.60088 0.64181 0.05488  -0.00753 -0.07556 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.70569 0.58573 0.65409 0.06174  0.01181  -0.06570 29  LEU A CD2 
113  N N   . MET A 23  ? 0.59724 0.59030 0.64551 0.05508  -0.02986 -0.05762 30  MET A N   
114  C CA  . MET A 23  ? 0.59217 0.59527 0.65155 0.06438  -0.03287 -0.04589 30  MET A CA  
115  C C   . MET A 23  ? 0.57727 0.59539 0.64456 0.06767  -0.04148 -0.04146 30  MET A C   
116  O O   . MET A 23  ? 0.62467 0.64453 0.68908 0.07500  -0.04129 -0.03021 30  MET A O   
117  C CB  . MET A 23  ? 0.50079 0.50808 0.57837 0.06375  -0.03212 -0.04546 30  MET A CB  
118  C CG  . MET A 23  ? 0.52390 0.52113 0.59071 0.06542  -0.02436 -0.04600 30  MET A CG  
119  S SD  . MET A 23  ? 0.61992 0.62573 0.70300 0.06440  -0.02530 -0.04946 30  MET A SD  
120  C CE  . MET A 23  ? 0.58742 0.60539 0.68569 0.06665  -0.03047 -0.04247 30  MET A CE  
121  N N   . SER A 24  ? 0.53263 0.56450 0.61000 0.06361  -0.04816 -0.04869 31  SER A N   
122  C CA  . SER A 24  ? 0.59204 0.64138 0.67365 0.07123  -0.05705 -0.04293 31  SER A CA  
123  C C   . SER A 24  ? 0.55695 0.60723 0.61345 0.07404  -0.05971 -0.04244 31  SER A C   
124  O O   . SER A 24  ? 0.56836 0.62590 0.61895 0.08510  -0.06314 -0.03071 31  SER A O   
125  C CB  . SER A 24  ? 0.53317 0.60603 0.63305 0.06860  -0.06413 -0.05128 31  SER A CB  
126  O OG  . SER A 24  ? 0.69439 0.79067 0.78942 0.07424  -0.07461 -0.05085 31  SER A OG  
127  N N   . LEU A 25  ? 0.57042 0.60963 0.60853 0.06487  -0.05662 -0.05494 32  LEU A N   
128  C CA  . LEU A 25  ? 0.62559 0.66036 0.63439 0.06806  -0.05767 -0.05755 32  LEU A CA  
129  C C   . LEU A 25  ? 0.61938 0.64177 0.61540 0.08073  -0.04908 -0.04238 32  LEU A C   
130  O O   . LEU A 25  ? 0.61596 0.64556 0.59606 0.09064  -0.05090 -0.03463 32  LEU A O   
131  C CB  . LEU A 25  ? 0.60167 0.61716 0.59175 0.05419  -0.05333 -0.07611 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.74972 0.75698 0.70606 0.05215  -0.05539 -0.08840 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.77570 0.76364 0.72360 0.03128  -0.05186 -0.11005 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.69077 0.67493 0.61906 0.06698  -0.04469 -0.07956 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.54761 0.55627 0.55091 0.08116  -0.03947 -0.03738 33  ILE A N   
136  C CA  . ILE A 26  ? 0.59874 0.60454 0.59577 0.09167  -0.03081 -0.02360 33  ILE A CA  
137  C C   . ILE A 26  ? 0.59265 0.61339 0.60606 0.09676  -0.03293 -0.00733 33  ILE A C   
138  O O   . ILE A 26  ? 0.62962 0.65437 0.63277 0.10521  -0.02735 0.00510  33  ILE A O   
139  C CB  . ILE A 26  ? 0.56693 0.56374 0.57109 0.09142  -0.02244 -0.02287 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.56105 0.53384 0.53841 0.09260  -0.01494 -0.03322 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.55216 0.56114 0.56513 0.09940  -0.01600 -0.00770 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.54753 0.51041 0.52908 0.09370  -0.00804 -0.03305 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.64247 0.66875 0.67974 0.09239  -0.03889 -0.00655 34  ILE A N   
144  C CA  . ILE A 27  ? 0.64798 0.67773 0.69969 0.09662  -0.03804 0.00918  34  ILE A CA  
145  C C   . ILE A 27  ? 0.66409 0.70172 0.70141 0.10713  -0.04296 0.01805  34  ILE A C   
146  O O   . ILE A 27  ? 0.72760 0.76350 0.76227 0.11405  -0.03712 0.03581  34  ILE A O   
147  C CB  . ILE A 27  ? 0.67590 0.70233 0.75387 0.09084  -0.04091 0.00551  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.62981 0.65172 0.72188 0.08321  -0.03455 0.00508  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.64726 0.67121 0.73398 0.09806  -0.04279 0.01770  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.70830 0.72599 0.81878 0.07702  -0.03743 -0.00479 34  ILE A CD1 
151  N N   . ASN A 28  ? 0.67701 0.72581 0.70410 0.10819  -0.05322 0.00647  35  ASN A N   
152  C CA  . ASN A 28  ? 0.68785 0.75236 0.70329 0.12040  -0.06138 0.01410  35  ASN A CA  
153  C C   . ASN A 28  ? 0.75122 0.82301 0.73204 0.12617  -0.06325 0.01148  35  ASN A C   
154  O O   . ASN A 28  ? 0.71807 0.80308 0.68306 0.13996  -0.06784 0.02284  35  ASN A O   
155  C CB  . ASN A 28  ? 0.67945 0.76375 0.70964 0.11922  -0.07402 0.00267  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.66266 0.73948 0.72308 0.11742  -0.07142 0.00479  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.63143 0.69224 0.69972 0.12386  -0.06459 0.02037  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.67100 0.75718 0.74719 0.10758  -0.07531 -0.01161 35  ASN A ND2 
159  N N   . THR A 29  ? 0.73986 0.80123 0.70499 0.11819  -0.05910 -0.00287 36  THR A N   
160  C CA  . THR A 29  ? 0.78220 0.84558 0.71018 0.12369  -0.06007 -0.00943 36  THR A CA  
161  C C   . THR A 29  ? 0.71346 0.77231 0.62500 0.13753  -0.04755 0.01102  36  THR A C   
162  O O   . THR A 29  ? 0.71687 0.76489 0.64223 0.13633  -0.03473 0.02112  36  THR A O   
163  C CB  . THR A 29  ? 0.83971 0.88404 0.75362 0.11183  -0.05651 -0.03152 36  THR A CB  
164  O OG1 . THR A 29  ? 0.81538 0.86773 0.74091 0.09677  -0.06756 -0.05093 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.73444 0.77156 0.60558 0.11920  -0.05343 -0.03883 36  THR A CG2 
166  N N   . PHE A 30  ? 0.69299 0.76488 0.57556 0.15069  -0.05120 0.01739  37  PHE A N   
167  C CA  . PHE A 30  ? 0.79014 0.86007 0.65247 0.16456  -0.03715 0.03734  37  PHE A CA  
168  C C   . PHE A 30  ? 0.79602 0.85185 0.63672 0.16457  -0.02583 0.02609  37  PHE A C   
169  O O   . PHE A 30  ? 0.88078 0.93230 0.68938 0.16511  -0.03103 0.00593  37  PHE A O   
170  C CB  . PHE A 30  ? 0.80612 0.89439 0.63676 0.18114  -0.04411 0.04660  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.89582 0.98329 0.70387 0.19640  -0.02729 0.07029  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.90288 0.98630 0.73115 0.20017  -0.01484 0.09959  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.85841 0.94727 0.62406 0.20611  -0.02205 0.06272  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.85397 0.93847 0.66372 0.21184  0.00336  0.12295  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.81893 0.91063 0.56379 0.22118  -0.00427 0.08566  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.82478 0.91619 0.59327 0.22330  0.00886  0.11684  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.72963 0.77892 0.58760 0.16440  -0.01019 0.03815  38  TYR A N   
178  C CA  . TYR A 31  ? 0.73458 0.77252 0.57551 0.16907  0.00242  0.03039  38  TYR A CA  
179  C C   . TYR A 31  ? 0.74347 0.79369 0.59909 0.17624  0.02023  0.05419  38  TYR A C   
180  O O   . TYR A 31  ? 0.73292 0.78883 0.62698 0.16661  0.02308  0.06321  38  TYR A O   
181  C CB  . TYR A 31  ? 0.82806 0.84833 0.68359 0.15715  -0.00013 0.01212  38  TYR A CB  
182  C CG  . TYR A 31  ? 0.80724 0.80825 0.63777 0.16559  0.01219  0.00193  38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.79580 0.80151 0.64185 0.17298  0.02628  0.01349  38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.82894 0.80739 0.61971 0.16688  0.00999  -0.01998 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.85219 0.83994 0.67391 0.18609  0.03878  0.00620  38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.88735 0.83935 0.65124 0.17723  0.02369  -0.02917 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.88585 0.84231 0.66483 0.18922  0.03858  -0.01460 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.93489 0.86489 0.68571 0.20476  0.05340  -0.02175 38  TYR A OH  
189  N N   . SER A 32  ? 0.78191 0.83903 0.60724 0.19203  0.03246  0.06322  39  SER A N   
190  C CA  . SER A 32  ? 0.78854 0.86458 0.62972 0.19756  0.05104  0.08824  39  SER A CA  
191  C C   . SER A 32  ? 0.73670 0.81931 0.59335 0.20016  0.06362  0.08626  39  SER A C   
192  O O   . SER A 32  ? 0.72504 0.83050 0.61445 0.19617  0.07507  0.10382  39  SER A O   
193  C CB  . SER A 32  ? 0.77763 0.86274 0.57967 0.21542  0.06160  0.10122  39  SER A CB  
194  O OG  . SER A 32  ? 0.73381 0.81771 0.51982 0.21686  0.04929  0.10578  39  SER A OG  
195  N N   . ASN A 33  ? 0.76264 0.82630 0.59678 0.20679  0.06220  0.06548  40  ASN A N   
196  C CA  . ASN A 33  ? 0.73002 0.79889 0.57363 0.21561  0.07442  0.06478  40  ASN A CA  
197  C C   . ASN A 33  ? 0.67547 0.74834 0.56164 0.20021  0.06627  0.06258  40  ASN A C   
198  O O   . ASN A 33  ? 0.64389 0.69862 0.52588 0.20201  0.06382  0.04887  40  ASN A O   
199  C CB  . ASN A 33  ? 0.73830 0.77583 0.53637 0.23079  0.07844  0.04458  40  ASN A CB  
200  C CG  . ASN A 33  ? 0.81893 0.86308 0.61777 0.24983  0.09545  0.04857  40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.79647 0.87930 0.61892 0.25764  0.10808  0.06820  40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.83882 0.84603 0.61250 0.25771  0.09688  0.03067  40  ASN A ND2 
203  N N   . LYS A 34  ? 0.62022 0.63013 0.41433 0.12971  -0.04500 0.03790  41  LYS A N   
204  C CA  . LYS A 34  ? 0.65057 0.68130 0.49176 0.12010  -0.03242 0.04129  41  LYS A CA  
205  C C   . LYS A 34  ? 0.64822 0.66155 0.49850 0.11164  -0.01631 0.03116  41  LYS A C   
206  O O   . LYS A 34  ? 0.63171 0.65773 0.51482 0.10105  -0.01168 0.03023  41  LYS A O   
207  C CB  . LYS A 34  ? 0.67306 0.70977 0.52286 0.13606  -0.01388 0.05549  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.63335 0.70028 0.48724 0.14761  -0.02824 0.06890  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.66128 0.71840 0.50978 0.16992  -0.00891 0.08208  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.74726 0.83600 0.59496 0.18829  -0.02258 0.09756  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.64510 0.78951 0.53429 0.18294  -0.03675 0.10379  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.64619 0.63460 0.46694 0.11900  -0.00744 0.02519  42  GLU A N   
213  C CA  . GLU A 35  ? 0.69526 0.67680 0.52938 0.11451  0.00999  0.02044  42  GLU A CA  
214  C C   . GLU A 35  ? 0.67866 0.66058 0.52854 0.09905  -0.00399 0.00816  42  GLU A C   
215  O O   . GLU A 35  ? 0.68347 0.66656 0.55305 0.09364  0.00788  0.00546  42  GLU A O   
216  C CB  . GLU A 35  ? 0.72715 0.69270 0.52624 0.13171  0.02416  0.02104  42  GLU A CB  
217  C CG  . GLU A 35  ? 0.74110 0.68234 0.49417 0.14134  0.00530  0.00667  42  GLU A CG  
218  C CD  . GLU A 35  ? 0.83974 0.76649 0.54820 0.16830  0.02316  0.00896  42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.84168 0.78001 0.54776 0.17889  0.04427  0.02588  42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.90541 0.80735 0.57773 0.18115  0.01680  -0.00454 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.64071 0.62211 0.48335 0.08967  -0.03103 0.00317  43  ILE A N   
222  C CA  . ILE A 36  ? 0.62141 0.59816 0.47629 0.07232  -0.04637 -0.00499 43  ILE A CA  
223  C C   . ILE A 36  ? 0.58250 0.58857 0.48425 0.05914  -0.03888 0.00148  43  ILE A C   
224  O O   . ILE A 36  ? 0.59467 0.59863 0.50896 0.04550  -0.04665 -0.00261 43  ILE A O   
225  C CB  . ILE A 36  ? 0.67866 0.64448 0.51371 0.05958  -0.08196 -0.00778 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.64292 0.65032 0.50500 0.05177  -0.09332 0.00779  43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.76465 0.68688 0.53765 0.07603  -0.09265 -0.01893 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.64495 0.68873 0.55265 0.02855  -0.10468 0.01847  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.55535 0.58297 0.47633 0.06576  -0.02434 0.01153  44  PHE A N   
230  C CA  . PHE A 37  ? 0.57912 0.62647 0.53192 0.06018  -0.01569 0.01569  44  PHE A CA  
231  C C   . PHE A 37  ? 0.56858 0.60022 0.52753 0.05551  -0.00412 0.00739  44  PHE A C   
232  O O   . PHE A 37  ? 0.49306 0.53376 0.46989 0.04619  -0.00581 0.00628  44  PHE A O   
233  C CB  . PHE A 37  ? 0.53091 0.58781 0.48805 0.07511  -0.00225 0.02536  44  PHE A CB  
234  C CG  . PHE A 37  ? 0.54455 0.57369 0.49157 0.08206  0.01640  0.02382  44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.58741 0.60066 0.51274 0.09040  0.02241  0.02736  44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.53960 0.55817 0.49721 0.07844  0.02596  0.02103  44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.64446 0.63745 0.56639 0.09149  0.03856  0.03201  44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.56922 0.56153 0.52057 0.07773  0.03750  0.02269  44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.57084 0.55317 0.50814 0.08250  0.04430  0.03015  44  PHE A CZ  
240  N N   . LEU A 38  ? 0.53881 0.55238 0.48458 0.06249  0.00778  0.00452  45  LEU A N   
241  C CA  . LEU A 38  ? 0.57035 0.57891 0.52815 0.05777  0.01722  0.00055  45  LEU A CA  
242  C C   . LEU A 38  ? 0.55778 0.56056 0.51234 0.05268  0.00596  -0.00814 45  LEU A C   
243  O O   . LEU A 38  ? 0.58478 0.59095 0.55595 0.04510  0.00636  -0.01075 45  LEU A O   
244  C CB  . LEU A 38  ? 0.52638 0.52971 0.47758 0.06593  0.03331  0.00642  45  LEU A CB  
245  C CG  . LEU A 38  ? 0.57517 0.58457 0.54929 0.05798  0.04298  0.00929  45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.49366 0.49794 0.48364 0.04607  0.04058  0.00936  45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.54276 0.55867 0.51677 0.06372  0.05945  0.02275  45  LEU A CD2 
248  N N   . ARG A 39  ? 0.59512 0.58226 0.52221 0.05769  -0.00657 -0.01301 46  ARG A N   
249  C CA  . ARG A 39  ? 0.58780 0.55483 0.50189 0.05365  -0.02139 -0.02168 46  ARG A CA  
250  C C   . ARG A 39  ? 0.60486 0.58287 0.54157 0.03350  -0.03512 -0.01843 46  ARG A C   
251  O O   . ARG A 39  ? 0.55557 0.52566 0.49776 0.02768  -0.03862 -0.02136 46  ARG A O   
252  C CB  . ARG A 39  ? 0.60491 0.53977 0.47380 0.06223  -0.03802 -0.02888 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.68630 0.58392 0.53095 0.05610  -0.06057 -0.03833 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.75820 0.61338 0.54989 0.06078  -0.08496 -0.04674 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.76088 0.63309 0.56598 0.03852  -0.10651 -0.03827 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.79794 0.64797 0.56598 0.03909  -0.12888 -0.04150 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.80011 0.60183 0.50598 0.06341  -0.13208 -0.05544 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.78187 0.66150 0.57393 0.01716  -0.14879 -0.02918 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.51755 0.51868 0.46843 0.02499  -0.04151 -0.00926 47  GLU A N   
260  C CA  . GLU A 40  ? 0.54921 0.57207 0.52422 0.00752  -0.05185 -0.00010 47  GLU A CA  
261  C C   . GLU A 40  ? 0.48032 0.51993 0.47753 0.00928  -0.03479 0.00203  47  GLU A C   
262  O O   . GLU A 40  ? 0.48525 0.52989 0.49310 -0.00162 -0.03976 0.00572  47  GLU A O   
263  C CB  . GLU A 40  ? 0.49102 0.54678 0.47953 0.00247  -0.06099 0.01366  47  GLU A CB  
264  C CG  . GLU A 40  ? 0.55229 0.59068 0.51619 -0.00288 -0.08496 0.01209  47  GLU A CG  
265  C CD  . GLU A 40  ? 0.66502 0.66373 0.60683 -0.01998 -0.11049 0.00542  47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.60701 0.61257 0.56841 -0.03728 -0.11625 0.01263  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.68518 0.64031 0.58388 -0.01412 -0.12525 -0.00672 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.49500 0.53794 0.49456 0.02212  -0.01692 0.00039  48  LEU A N   
269  C CA  . LEU A 41  ? 0.50342 0.55089 0.51378 0.02375  -0.00572 -0.00025 48  LEU A CA  
270  C C   . LEU A 41  ? 0.47853 0.50996 0.48853 0.01973  -0.00587 -0.00827 48  LEU A C   
271  O O   . LEU A 41  ? 0.51628 0.55133 0.53290 0.01509  -0.00675 -0.00821 48  LEU A O   
272  C CB  . LEU A 41  ? 0.53784 0.57987 0.54370 0.03571  0.00763  0.00006  48  LEU A CB  
273  C CG  . LEU A 41  ? 0.46169 0.52128 0.46687 0.04699  0.01041  0.00946  48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.45693 0.49487 0.44855 0.06044  0.02210  0.00849  48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.40237 0.49251 0.42029 0.04694  0.00884  0.01839  48  LEU A CD2 
276  N N   . ILE A 42  ? 0.53080 0.54819 0.53181 0.02480  -0.00409 -0.01331 49  ILE A N   
277  C CA  . ILE A 42  ? 0.50525 0.51591 0.50874 0.02587  -0.00361 -0.01778 49  ILE A CA  
278  C C   . ILE A 42  ? 0.52106 0.51985 0.51695 0.02029  -0.01790 -0.01969 49  ILE A C   
279  O O   . ILE A 42  ? 0.50682 0.50526 0.50933 0.01800  -0.01987 -0.02034 49  ILE A O   
280  C CB  . ILE A 42  ? 0.59735 0.60407 0.59219 0.03886  0.00523  -0.01842 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.50684 0.52592 0.51573 0.03831  0.01892  -0.01150 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.55025 0.55454 0.54474 0.04692  0.00480  -0.02101 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.47152 0.49793 0.47679 0.05075  0.03166  -0.00521 49  ILE A CD1 
284  N N   . SER A 43  ? 0.54273 0.52835 0.52274 0.01612  -0.03104 -0.01921 50  SER A N   
285  C CA  . SER A 43  ? 0.49531 0.46089 0.46542 0.00525  -0.04905 -0.01818 50  SER A CA  
286  C C   . SER A 43  ? 0.51467 0.50321 0.50705 -0.00887 -0.04970 -0.00757 50  SER A C   
287  O O   . SER A 43  ? 0.53134 0.50731 0.52115 -0.01451 -0.05676 -0.00547 50  SER A O   
288  C CB  . SER A 43  ? 0.56010 0.50511 0.50894 -0.00287 -0.06879 -0.01767 50  SER A CB  
289  O OG  . SER A 43  ? 0.62340 0.55373 0.57043 -0.02336 -0.08974 -0.01025 50  SER A OG  
290  N N   . ASN A 44  ? 0.49309 0.51431 0.50306 -0.01069 -0.04115 0.00050  51  ASN A N   
291  C CA  . ASN A 44  ? 0.47636 0.52281 0.50141 -0.01610 -0.03666 0.01149  51  ASN A CA  
292  C C   . ASN A 44  ? 0.44383 0.48315 0.46658 -0.00841 -0.02809 0.00409  51  ASN A C   
293  O O   . ASN A 44  ? 0.48506 0.52796 0.50856 -0.01313 -0.03033 0.01024  51  ASN A O   
294  C CB  . ASN A 44  ? 0.44390 0.52476 0.48082 -0.00960 -0.02626 0.02074  51  ASN A CB  
295  C CG  . ASN A 44  ? 0.49380 0.59819 0.54263 -0.02132 -0.03828 0.03558  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.52813 0.62158 0.57664 -0.04043 -0.05724 0.04137  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.44141 0.57575 0.49932 -0.01040 -0.03005 0.04296  51  ASN A ND2 
298  N N   . SER A 45  ? 0.45753 0.48844 0.47801 0.00156  -0.02001 -0.00658 52  SER A N   
299  C CA  . SER A 45  ? 0.46612 0.49242 0.48764 0.00456  -0.01759 -0.01217 52  SER A CA  
300  C C   . SER A 45  ? 0.50341 0.51743 0.52250 0.00377  -0.02635 -0.01353 52  SER A C   
301  O O   . SER A 45  ? 0.49889 0.51365 0.51803 0.00314  -0.02967 -0.01272 52  SER A O   
302  C CB  . SER A 45  ? 0.46436 0.48804 0.48997 0.00932  -0.01032 -0.01788 52  SER A CB  
303  O OG  . SER A 45  ? 0.49486 0.51860 0.51524 0.01250  -0.00375 -0.01725 52  SER A OG  
304  N N   . SER A 46  ? 0.51483 0.51283 0.52530 0.00731  -0.03110 -0.01598 53  SER A N   
305  C CA  . SER A 46  ? 0.48850 0.46554 0.48768 0.01302  -0.03964 -0.01772 53  SER A CA  
306  C C   . SER A 46  ? 0.51504 0.48061 0.50764 0.00092  -0.05140 -0.00953 53  SER A C   
307  O O   . SER A 46  ? 0.54199 0.49797 0.53004 0.00484  -0.05619 -0.00806 53  SER A O   
308  C CB  . SER A 46  ? 0.50862 0.45926 0.48574 0.02417  -0.04332 -0.02363 53  SER A CB  
309  O OG  . SER A 46  ? 0.57277 0.49381 0.52974 0.03604  -0.05168 -0.02625 53  SER A OG  
310  N N   . ASP A 47  ? 0.54708 0.51803 0.54146 -0.01411 -0.05632 -0.00058 54  ASP A N   
311  C CA  . ASP A 47  ? 0.54138 0.51012 0.53521 -0.02952 -0.06598 0.01409  54  ASP A CA  
312  C C   . ASP A 47  ? 0.51298 0.50612 0.51484 -0.02618 -0.05601 0.01965  54  ASP A C   
313  O O   . ASP A 47  ? 0.52350 0.50629 0.51792 -0.02975 -0.06211 0.02781  54  ASP A O   
314  C CB  . ASP A 47  ? 0.55561 0.54135 0.55965 -0.04791 -0.07242 0.02827  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.63267 0.58470 0.61990 -0.05462 -0.09001 0.02275  54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.65158 0.55778 0.61135 -0.04400 -0.09802 0.00970  54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.59222 0.56341 0.59035 -0.06784 -0.09667 0.03185  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.49330 0.51185 0.50334 -0.01788 -0.04233 0.01506  55  ALA A N   
319  C CA  . ALA A 48  ? 0.48646 0.51784 0.49170 -0.01139 -0.03561 0.01666  55  ALA A CA  
320  C C   . ALA A 48  ? 0.48125 0.49711 0.48038 -0.00498 -0.04183 0.00776  55  ALA A C   
321  O O   . ALA A 48  ? 0.49639 0.51333 0.48510 -0.00287 -0.04418 0.01240  55  ALA A O   
322  C CB  . ALA A 48  ? 0.41547 0.46115 0.41962 -0.00154 -0.02353 0.01065  55  ALA A CB  
323  N N   . LEU A 49  ? 0.44757 0.45430 0.45335 0.00013  -0.04406 -0.00246 56  LEU A N   
324  C CA  . LEU A 49  ? 0.45721 0.46139 0.46501 0.00781  -0.05015 -0.00640 56  LEU A CA  
325  C C   . LEU A 49  ? 0.48462 0.46779 0.48030 0.01066  -0.05988 0.00017  56  LEU A C   
326  O O   . LEU A 49  ? 0.51733 0.50080 0.50952 0.01667  -0.06631 0.00257  56  LEU A O   
327  C CB  . LEU A 49  ? 0.50023 0.51248 0.52330 0.01495  -0.04606 -0.01330 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.51231 0.53894 0.54676 0.00986  -0.03999 -0.01761 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.47694 0.51132 0.52465 0.01439  -0.03178 -0.01846 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.45674 0.49276 0.49685 0.00630  -0.04885 -0.01875 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.51893 0.47846 0.50432 0.00600  -0.06413 0.00352  57  ASP A N   
332  C CA  . ASP A 50  ? 0.56957 0.49426 0.53519 0.00621  -0.07691 0.01071  57  ASP A CA  
333  C C   . ASP A 50  ? 0.56132 0.49152 0.52260 -0.00434 -0.07980 0.02567  57  ASP A C   
334  O O   . ASP A 50  ? 0.55232 0.46283 0.49961 0.00158  -0.08821 0.03157  57  ASP A O   
335  C CB  . ASP A 50  ? 0.56814 0.45792 0.51795 -0.00327 -0.08663 0.01182  57  ASP A CB  
336  C CG  . ASP A 50  ? 0.64126 0.51072 0.57849 0.01543  -0.08588 -0.00275 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.59709 0.47872 0.53926 0.03749  -0.07820 -0.00911 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.69452 0.53905 0.61639 0.00879  -0.09347 -0.00588 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.55456 0.51306 0.52509 -0.01606 -0.07134 0.03378  58  LYS A N   
340  C CA  . LYS A 51  ? 0.56869 0.53797 0.53245 -0.02356 -0.07019 0.05239  58  LYS A CA  
341  C C   . LYS A 51  ? 0.55907 0.53671 0.51223 -0.00918 -0.06854 0.04801  58  LYS A C   
342  O O   . LYS A 51  ? 0.54655 0.51379 0.48444 -0.00847 -0.07428 0.06035  58  LYS A O   
343  C CB  . LYS A 51  ? 0.52055 0.52599 0.49658 -0.03261 -0.05809 0.06430  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.62222 0.62535 0.61001 -0.05436 -0.06592 0.07963  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.64644 0.69638 0.65440 -0.05766 -0.05303 0.08922  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.70424 0.75025 0.72678 -0.07789 -0.06606 0.09559  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.59892 0.69678 0.64466 -0.07733 -0.05406 0.10557  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.53595 0.52897 0.49448 0.00057  -0.06360 0.03176  59  ILE A N   
349  C CA  . ILE A 52  ? 0.54780 0.54502 0.49369 0.01062  -0.06856 0.02662  59  ILE A CA  
350  C C   . ILE A 52  ? 0.55035 0.53554 0.49923 0.01834  -0.08168 0.02468  59  ILE A C   
351  O O   . ILE A 52  ? 0.59805 0.58269 0.53297 0.02510  -0.09044 0.02859  59  ILE A O   
352  C CB  . ILE A 52  ? 0.54982 0.55793 0.49771 0.01399  -0.06536 0.01099  59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.54471 0.55048 0.47150 0.02069  -0.07643 0.00566  59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.49311 0.50383 0.46697 0.01215  -0.06645 0.00019  59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.58860 0.59260 0.48009 0.02802  -0.07127 0.01529  59  ILE A CD1 
356  N N   . ARG A 53  ? 0.53159 0.50768 0.49481 0.02160  -0.08291 0.01968  60  ARG A N   
357  C CA  . ARG A 53  ? 0.58532 0.55238 0.54901 0.03675  -0.09247 0.02022  60  ARG A CA  
358  C C   . ARG A 53  ? 0.62695 0.56076 0.56550 0.03857  -0.10079 0.03403  60  ARG A C   
359  O O   . ARG A 53  ? 0.65284 0.58386 0.58292 0.05155  -0.11004 0.03909  60  ARG A O   
360  C CB  . ARG A 53  ? 0.58175 0.54461 0.55765 0.04676  -0.08832 0.01256  60  ARG A CB  
361  C CG  . ARG A 53  ? 0.64985 0.60533 0.62281 0.07118  -0.09471 0.01482  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.70965 0.67403 0.69455 0.08801  -0.08590 0.00816  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.77184 0.69302 0.73185 0.08666  -0.08375 0.00300  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.82419 0.71101 0.75940 0.11084  -0.08448 -0.00066 60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.87518 0.77126 0.81002 0.14285  -0.08327 0.00226  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.87508 0.71648 0.78191 0.10515  -0.08779 -0.00695 60  ARG A NH2 
367  N N   . TYR A 54  ? 0.61950 0.52803 0.54669 0.02390  -0.09983 0.04278  61  TYR A N   
368  C CA  . TYR A 54  ? 0.68981 0.56067 0.59253 0.01935  -0.11002 0.06003  61  TYR A CA  
369  C C   . TYR A 54  ? 0.63548 0.52351 0.52778 0.01765  -0.10915 0.07416  61  TYR A C   
370  O O   . TYR A 54  ? 0.67986 0.54459 0.55203 0.02592  -0.11889 0.08519  61  TYR A O   
371  C CB  . TYR A 54  ? 0.62989 0.47629 0.52846 -0.00417 -0.11278 0.07034  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.69487 0.50070 0.57018 -0.01752 -0.12547 0.09348  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.75949 0.50037 0.60556 -0.00900 -0.14249 0.09296  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.71157 0.54170 0.59054 -0.03661 -0.11989 0.11801  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.77070 0.46443 0.59165 -0.02398 -0.15696 0.11600  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.75341 0.54838 0.61364 -0.05260 -0.13143 0.14449  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.80516 0.52822 0.63638 -0.04870 -0.15163 0.14327  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.85224 0.53037 0.66103 -0.06737 -0.16594 0.17135  61  TYR A OH  
379  N N   . GLU A 55  ? 0.60855 0.53343 0.50788 0.01096  -0.09738 0.07416  62  GLU A N   
380  C CA  . GLU A 55  ? 0.60471 0.54409 0.48411 0.01485  -0.09499 0.08600  62  GLU A CA  
381  C C   . GLU A 55  ? 0.67481 0.61688 0.54494 0.03318  -0.10648 0.07585  62  GLU A C   
382  O O   . GLU A 55  ? 0.71403 0.65095 0.55930 0.04008  -0.11216 0.08816  62  GLU A O   
383  C CB  . GLU A 55  ? 0.62631 0.59910 0.50632 0.01216  -0.07912 0.08479  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.71208 0.69796 0.60443 -0.00500 -0.06736 0.10336  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.81014 0.83352 0.69590 0.00185  -0.04865 0.10837  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.77440 0.80079 0.63812 0.01980  -0.04690 0.09272  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.83166 0.88064 0.73222 -0.00958 -0.03718 0.12888  62  GLU A OE2 
388  N N   . SER A 56  ? 0.63178 0.58608 0.52324 0.04024  -0.11097 0.05664  63  SER A N   
389  C CA  . SER A 56  ? 0.61409 0.58217 0.50638 0.05358  -0.12518 0.05026  63  SER A CA  
390  C C   . SER A 56  ? 0.67708 0.62780 0.56471 0.06914  -0.13660 0.06006  63  SER A C   
391  O O   . SER A 56  ? 0.72233 0.68752 0.60778 0.08166  -0.15046 0.06124  63  SER A O   
392  C CB  . SER A 56  ? 0.56783 0.56197 0.49186 0.05235  -0.12654 0.03331  63  SER A CB  
393  O OG  . SER A 56  ? 0.60307 0.59607 0.55060 0.05974  -0.12349 0.03181  63  SER A OG  
394  N N   . LEU A 57  ? 0.66532 0.58147 0.54763 0.06973  -0.13373 0.06715  64  LEU A N   
395  C CA  . LEU A 57  ? 0.73650 0.62338 0.60459 0.08991  -0.14486 0.07570  64  LEU A CA  
396  C C   . LEU A 57  ? 0.76720 0.63680 0.60357 0.09221  -0.15337 0.09437  64  LEU A C   
397  O O   . LEU A 57  ? 0.79669 0.65840 0.62252 0.11410  -0.16552 0.10064  64  LEU A O   
398  C CB  . LEU A 57  ? 0.73302 0.57017 0.58989 0.08959  -0.14352 0.07644  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.71976 0.56854 0.59947 0.09177  -0.13470 0.05908  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.73313 0.51989 0.58717 0.09339  -0.13857 0.05848  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.71006 0.60105 0.61599 0.11698  -0.13420 0.05072  64  LEU A CD2 
402  N N   . THR A 58  ? 0.77147 0.63912 0.59215 0.07284  -0.14588 0.10612  65  THR A N   
403  C CA  . THR A 58  ? 0.81664 0.67364 0.60462 0.07502  -0.15038 0.12707  65  THR A CA  
404  C C   . THR A 58  ? 0.84004 0.73477 0.61691 0.07806  -0.14880 0.12258  65  THR A C   
405  O O   . THR A 58  ? 0.86201 0.75172 0.60663 0.08639  -0.15437 0.13756  65  THR A O   
406  C CB  . THR A 58  ? 0.84436 0.67332 0.61760 0.05280  -0.14263 0.15160  65  THR A CB  
407  O OG1 . THR A 58  ? 0.83376 0.69217 0.62680 0.03367  -0.12659 0.14786  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.87933 0.64981 0.64644 0.04974  -0.15309 0.15758  65  THR A CG2 
409  N N   . ASP A 59  ? 0.80750 0.73244 0.60301 0.07292  -0.14299 0.10237  66  ASP A N   
410  C CA  . ASP A 59  ? 0.82653 0.77280 0.60076 0.07718  -0.14541 0.09367  66  ASP A CA  
411  C C   . ASP A 59  ? 0.81680 0.78472 0.61898 0.07573  -0.15438 0.06870  66  ASP A C   
412  O O   . ASP A 59  ? 0.74754 0.72314 0.56352 0.06564  -0.14316 0.05643  66  ASP A O   
413  C CB  . ASP A 59  ? 0.84281 0.79475 0.59663 0.06994  -0.12473 0.10177  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.88325 0.84213 0.59341 0.08285  -0.12735 0.09506  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.88283 0.84060 0.58218 0.09097  -0.14953 0.08077  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.94535 0.91139 0.62990 0.08615  -0.10815 0.10512  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.78915 0.77030 0.60311 0.08483  -0.17543 0.06399  67  PRO A N   
418  C CA  . PRO A 60  ? 0.78369 0.79179 0.63011 0.07807  -0.18647 0.04624  67  PRO A CA  
419  C C   . PRO A 60  ? 0.79550 0.79975 0.61773 0.06815  -0.18985 0.03095  67  PRO A C   
420  O O   . PRO A 60  ? 0.81101 0.82676 0.65898 0.05607  -0.19358 0.01732  67  PRO A O   
421  C CB  . PRO A 60  ? 0.74404 0.77451 0.60251 0.08988  -0.21166 0.05166  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.86892 0.87860 0.70674 0.10733  -0.20992 0.07029  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.83760 0.81215 0.64744 0.10101  -0.18803 0.07875  67  PRO A CD  
424  N N   . SER A 61  ? 0.84266 0.82722 0.61119 0.07520  -0.18833 0.03386  68  SER A N   
425  C CA  . SER A 61  ? 0.84924 0.81840 0.57929 0.07371  -0.19199 0.01747  68  SER A CA  
426  C C   . SER A 61  ? 0.86706 0.83156 0.60596 0.06753  -0.16742 0.01031  68  SER A C   
427  O O   . SER A 61  ? 0.88594 0.83184 0.59385 0.06868  -0.17009 -0.00551 68  SER A O   
428  C CB  . SER A 61  ? 0.87204 0.82175 0.53405 0.09102  -0.19225 0.02452  68  SER A CB  
429  O OG  . SER A 61  ? 0.94781 0.89804 0.59878 0.09750  -0.16141 0.04332  68  SER A OG  
430  N N   . LYS A 62  ? 0.74491 0.72075 0.52003 0.06236  -0.14622 0.02125  69  LYS A N   
431  C CA  . LYS A 62  ? 0.72847 0.70558 0.51723 0.05623  -0.12565 0.01583  69  LYS A CA  
432  C C   . LYS A 62  ? 0.72287 0.70257 0.54166 0.04459  -0.13472 -0.00230 69  LYS A C   
433  O O   . LYS A 62  ? 0.70404 0.67758 0.52194 0.04212  -0.12240 -0.01054 69  LYS A O   
434  C CB  . LYS A 62  ? 0.72581 0.71164 0.54408 0.05017  -0.10743 0.03259  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.72673 0.71027 0.52145 0.05494  -0.09879 0.05680  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.71198 0.70892 0.50333 0.05262  -0.07458 0.07039  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.83552 0.83784 0.60472 0.05500  -0.06539 0.10049  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.83971 0.87059 0.60637 0.05637  -0.04033 0.11850  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.70286 0.69549 0.54989 0.03813  -0.15536 -0.00519 70  LEU A N   
440  C CA  . LEU A 63  ? 0.67153 0.67454 0.55278 0.02379  -0.16488 -0.01586 70  LEU A CA  
441  C C   . LEU A 63  ? 0.72482 0.71130 0.57980 0.01532  -0.19248 -0.02871 70  LEU A C   
442  O O   . LEU A 63  ? 0.68647 0.68278 0.57215 -0.00219 -0.20676 -0.03334 70  LEU A O   
443  C CB  . LEU A 63  ? 0.65513 0.69238 0.58939 0.02236  -0.16928 -0.00645 70  LEU A CB  
444  C CG  . LEU A 63  ? 0.68475 0.72484 0.63795 0.03080  -0.14715 0.00255  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.65505 0.72458 0.64920 0.03849  -0.15141 0.01036  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.63722 0.66830 0.59614 0.02352  -0.12729 -0.00374 70  LEU A CD2 
447  N N   . ASP A 64  ? 0.73809 0.69720 0.53368 0.02659  -0.20191 -0.03314 71  ASP A N   
448  C CA  . ASP A 64  ? 0.77399 0.70165 0.52913 0.01933  -0.23268 -0.04884 71  ASP A CA  
449  C C   . ASP A 64  ? 0.79460 0.68842 0.53503 0.01120  -0.22922 -0.06431 71  ASP A C   
450  O O   . ASP A 64  ? 0.79058 0.65646 0.51576 -0.00550 -0.25938 -0.07666 71  ASP A O   
451  C CB  . ASP A 64  ? 0.80943 0.70714 0.48968 0.04026  -0.23924 -0.05160 71  ASP A CB  
452  C CG  . ASP A 64  ? 0.90941 0.83290 0.59711 0.04619  -0.25247 -0.03692 71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.86991 0.83368 0.62030 0.03622  -0.25778 -0.02582 71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.93260 0.83593 0.56007 0.06450  -0.25643 -0.03525 71  ASP A OD2 
455  N N   . SER A 65  ? 0.74540 0.63888 0.48919 0.02154  -0.19567 -0.06238 72  SER A N   
456  C CA  . SER A 65  ? 0.75532 0.61960 0.48937 0.01769  -0.18872 -0.07420 72  SER A CA  
457  C C   . SER A 65  ? 0.79156 0.68298 0.59393 -0.00549 -0.18721 -0.06925 72  SER A C   
458  O O   . SER A 65  ? 0.83311 0.70648 0.63570 -0.00794 -0.17594 -0.07465 72  SER A O   
459  C CB  . SER A 65  ? 0.80888 0.66920 0.51728 0.04220  -0.15359 -0.07097 72  SER A CB  
460  O OG  . SER A 65  ? 0.73295 0.63818 0.48180 0.04488  -0.13118 -0.05200 72  SER A OG  
461  N N   . GLY A 66  ? 0.70419 0.63984 0.56148 -0.01844 -0.19661 -0.05734 73  GLY A N   
462  C CA  . GLY A 66  ? 0.66275 0.63180 0.58321 -0.03528 -0.19184 -0.04901 73  GLY A CA  
463  C C   . GLY A 66  ? 0.65877 0.67808 0.62773 -0.02750 -0.17842 -0.03337 73  GLY A C   
464  O O   . GLY A 66  ? 0.64540 0.66556 0.60882 -0.01162 -0.15537 -0.02976 73  GLY A O   
465  N N   . LYS A 67  ? 0.65253 0.71308 0.66778 -0.03788 -0.19405 -0.02241 74  LYS A N   
466  C CA  . LYS A 67  ? 0.66084 0.76451 0.71425 -0.02297 -0.18256 -0.00798 74  LYS A CA  
467  C C   . LYS A 67  ? 0.65241 0.77821 0.74361 -0.02011 -0.15826 -0.00165 74  LYS A C   
468  O O   . LYS A 67  ? 0.62675 0.76232 0.72533 -0.00046 -0.14155 0.00408  74  LYS A O   
469  C CB  . LYS A 67  ? 0.60512 0.75311 0.69205 -0.02795 -0.20843 0.00448  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.69898 0.83656 0.75194 -0.01564 -0.22549 0.00420  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.84048 0.99022 0.89588 -0.03491 -0.26505 0.00525  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.83234 0.91960 0.82553 -0.04821 -0.28130 -0.01469 74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.88019 0.96768 0.86742 -0.07048 -0.32686 -0.01576 74  LYS A NZ  
474  N N   . GLU A 68  ? 0.56262 0.68979 0.67129 -0.03836 -0.15745 -0.00241 75  GLU A N   
475  C CA  . GLU A 68  ? 0.53106 0.68262 0.67366 -0.03488 -0.13508 0.00580  75  GLU A CA  
476  C C   . GLU A 68  ? 0.58689 0.70303 0.69957 -0.02287 -0.11148 -0.00429 75  GLU A C   
477  O O   . GLU A 68  ? 0.60609 0.68306 0.68275 -0.02729 -0.11138 -0.01590 75  GLU A O   
478  C CB  . GLU A 68  ? 0.61318 0.77872 0.78518 -0.06125 -0.14333 0.01297  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.67775 0.85866 0.86638 -0.08691 -0.17817 0.01954  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.94310 1.06035 1.07313 -0.09743 -0.20169 -0.00015 75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.93140 1.05173 1.05248 -0.10283 -0.22939 -0.00068 75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.90262 0.96668 0.99145 -0.09637 -0.19239 -0.01474 75  GLU A OE2 
483  N N   . LEU A 69  ? 0.51617 0.64666 0.64155 -0.00555 -0.09275 0.00110  76  LEU A N   
484  C CA  . LEU A 69  ? 0.47841 0.58017 0.58009 0.00347  -0.07489 -0.00581 76  LEU A CA  
485  C C   . LEU A 69  ? 0.48447 0.60190 0.60685 0.00548  -0.05918 -0.00108 76  LEU A C   
486  O O   . LEU A 69  ? 0.45579 0.59821 0.59547 0.02174  -0.05083 0.00723  76  LEU A O   
487  C CB  . LEU A 69  ? 0.55882 0.64755 0.64291 0.02157  -0.07219 -0.00497 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.53564 0.61296 0.59963 0.02249  -0.08618 -0.00461 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.59318 0.65378 0.64198 0.03943  -0.08473 0.00013  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.49751 0.54963 0.53176 0.01205  -0.08684 -0.01144 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.47030 0.58241 0.56749 0.01540  -0.08492 0.00840  77  HIS A N   
492  C CA  . HIS A 70  ? 0.46004 0.57744 0.56018 0.01343  -0.07658 0.00777  77  HIS A CA  
493  C C   . HIS A 70  ? 0.47190 0.56169 0.55209 0.00461  -0.07764 -0.00178 77  HIS A C   
494  O O   . HIS A 70  ? 0.44372 0.51356 0.51195 -0.00101 -0.08425 -0.00730 77  HIS A O   
495  C CB  . HIS A 70  ? 0.47305 0.62492 0.59584 0.00321  -0.07946 0.01896  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.48256 0.63550 0.60506 -0.01649 -0.09472 0.01866  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.56612 0.68901 0.66872 -0.02894 -0.09822 0.00978  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.53458 0.71379 0.67220 -0.02573 -0.10767 0.02532  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.49438 0.61922 0.59644 -0.04523 -0.11097 0.00886  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.52048 0.68055 0.64279 -0.04511 -0.11861 0.01754  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.50354 0.59412 0.57998 0.00538  -0.06986 -0.00190 78  ILE A N   
502  C CA  . ILE A 71  ? 0.47617 0.54716 0.53656 -0.00082 -0.07065 -0.00657 78  ILE A CA  
503  C C   . ILE A 71  ? 0.49473 0.57784 0.56178 -0.01035 -0.06755 0.00279  78  ILE A C   
504  O O   . ILE A 71  ? 0.45284 0.55832 0.53108 -0.00659 -0.05902 0.01061  78  ILE A O   
505  C CB  . ILE A 71  ? 0.52347 0.58181 0.56778 0.00954  -0.06527 -0.01478 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.50556 0.54926 0.54708 0.01609  -0.06710 -0.02363 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.46782 0.51305 0.49843 0.00465  -0.06817 -0.01616 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.49544 0.52709 0.52290 0.02381  -0.06265 -0.03412 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.49890 0.56560 0.55986 -0.02190 -0.07216 0.00306  79  ASN A N   
510  C CA  . ASN A 72  ? 0.49879 0.56886 0.56555 -0.03302 -0.06824 0.01266  79  ASN A CA  
511  C C   . ASN A 72  ? 0.49482 0.54327 0.54346 -0.03000 -0.06452 0.01369  79  ASN A C   
512  O O   . ASN A 72  ? 0.57023 0.59736 0.60723 -0.02765 -0.06937 0.00694  79  ASN A O   
513  C CB  . ASN A 72  ? 0.44514 0.51114 0.52128 -0.05121 -0.07669 0.01304  79  ASN A CB  
514  C CG  . ASN A 72  ? 0.53844 0.63602 0.63677 -0.05593 -0.08248 0.01645  79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.47063 0.59573 0.58310 -0.04545 -0.07602 0.02274  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.49424 0.58852 0.59453 -0.07075 -0.09464 0.01254  79  ASN A ND2 
517  N N   . LEU A 73  ? 0.51005 0.56664 0.55734 -0.02866 -0.05507 0.02431  80  LEU A N   
518  C CA  . LEU A 73  ? 0.52752 0.56814 0.55744 -0.02415 -0.05144 0.02991  80  LEU A CA  
519  C C   . LEU A 73  ? 0.56065 0.59101 0.59800 -0.03727 -0.04574 0.04282  80  LEU A C   
520  O O   . LEU A 73  ? 0.56727 0.61510 0.61832 -0.04401 -0.03748 0.05353  80  LEU A O   
521  C CB  . LEU A 73  ? 0.49012 0.54466 0.50480 -0.01050 -0.04428 0.03276  80  LEU A CB  
522  C CG  . LEU A 73  ? 0.48161 0.54269 0.48850 0.00050  -0.04771 0.01853  80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.51193 0.58152 0.49645 0.01253  -0.04012 0.01906  80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.44840 0.49265 0.45004 0.00162  -0.05940 0.00699  80  LEU A CD2 
525  N N   . ILE A 74  ? 0.54932 0.55032 0.57929 -0.04066 -0.04835 0.04252  81  ILE A N   
526  C CA  . ILE A 74  ? 0.55494 0.53527 0.59089 -0.05506 -0.04268 0.05206  81  ILE A CA  
527  C C   . ILE A 74  ? 0.59823 0.55676 0.61897 -0.04542 -0.03532 0.06447  81  ILE A C   
528  O O   . ILE A 74  ? 0.61194 0.54475 0.62377 -0.03999 -0.03798 0.06063  81  ILE A O   
529  C CB  . ILE A 74  ? 0.51657 0.47390 0.55567 -0.06894 -0.05062 0.03985  81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.54637 0.52805 0.59571 -0.07283 -0.06089 0.02826  81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.54699 0.48352 0.59457 -0.08934 -0.04554 0.04657  81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.63185 0.59295 0.67645 -0.08444 -0.07031 0.01522  81  ILE A CD1 
533  N N   . PRO A 75  ? 0.57579 0.54474 0.59293 -0.04108 -0.02490 0.08128  82  PRO A N   
534  C CA  . PRO A 75  ? 0.57831 0.52638 0.58106 -0.03145 -0.01759 0.09738  82  PRO A CA  
535  C C   . PRO A 75  ? 0.68155 0.59386 0.69262 -0.04616 -0.00870 0.10669  82  PRO A C   
536  O O   . PRO A 75  ? 0.69579 0.60798 0.72455 -0.06657 -0.00551 0.10639  82  PRO A O   
537  C CB  . PRO A 75  ? 0.66583 0.63959 0.65823 -0.02213 -0.00870 0.11231  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.57394 0.57188 0.58563 -0.03482 -0.00422 0.10973  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.56716 0.56949 0.59067 -0.04077 -0.01791 0.08776  82  PRO A CD  
540  N N   . ASN A 76  ? 0.70066 0.58218 0.70009 -0.03568 -0.00468 0.11539  83  ASN A N   
541  C CA  . ASN A 76  ? 0.69841 0.53479 0.70132 -0.04692 0.00612  0.12379  83  ASN A CA  
542  C C   . ASN A 76  ? 0.78589 0.60649 0.77542 -0.02822 0.01723  0.14855  83  ASN A C   
543  O O   . ASN A 76  ? 0.78540 0.59856 0.76489 -0.00865 0.01366  0.14995  83  ASN A O   
544  C CB  . ASN A 76  ? 0.72508 0.52816 0.72659 -0.05234 0.00041  0.10448  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.83066 0.58219 0.83401 -0.07001 0.01099  0.10642  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.93299 0.66362 0.93686 -0.07079 0.02511  0.12706  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.88177 0.60979 0.88345 -0.08478 0.00460  0.08464  83  ASN A ND2 
548  N N   . LYS A 77  ? 0.78326 0.60144 0.77463 -0.03365 0.03122  0.17033  84  LYS A N   
549  C CA  . LYS A 77  ? 0.84711 0.65118 0.82367 -0.01465 0.04274  0.19806  84  LYS A CA  
550  C C   . LYS A 77  ? 0.89314 0.64030 0.86922 -0.01226 0.05215  0.20440  84  LYS A C   
551  O O   . LYS A 77  ? 0.91388 0.65082 0.87788 0.01185  0.05579  0.22170  84  LYS A O   
552  C CB  . LYS A 77  ? 0.86851 0.68346 0.84619 -0.02117 0.05830  0.22178  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.85452 0.72257 0.82132 -0.01180 0.05415  0.22286  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.91986 0.79554 0.88275 -0.01299 0.07401  0.25131  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.91184 0.83448 0.85297 0.00224  0.07232  0.25319  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.90361 0.85759 0.86384 -0.01257 0.07280  0.23786  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.90838 0.61785 0.89641 -0.03621 0.05607  0.19064  85  GLN A N   
558  C CA  . GLN A 78  ? 0.99807 0.64432 0.98163 -0.03454 0.06791  0.19398  85  GLN A CA  
559  C C   . GLN A 78  ? 0.94449 0.58353 0.91876 -0.01248 0.06040  0.18168  85  GLN A C   
560  O O   . GLN A 78  ? 1.00565 0.61812 0.97256 0.01045  0.07031  0.19838  85  GLN A O   
561  C CB  . GLN A 78  ? 1.05987 0.66716 1.05427 -0.06882 0.07132  0.17727  85  GLN A CB  
562  C CG  . GLN A 78  ? 1.02376 0.55559 1.00889 -0.06957 0.08547  0.17638  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.28035 0.77717 1.26287 -0.05849 0.10756  0.21060  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.31672 0.78778 1.28731 -0.02968 0.11695  0.22527  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 1.27130 0.76898 1.26716 -0.08034 0.11705  0.22596  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.89485 0.55892 0.87151 -0.01786 0.04429  0.15488  86  ASP A N   
567  C CA  . ASP A 79  ? 0.90235 0.56614 0.87379 0.00178  0.03816  0.14373  86  ASP A CA  
568  C C   . ASP A 79  ? 0.85677 0.57086 0.82795 0.02691  0.02833  0.15522  86  ASP A C   
569  O O   . ASP A 79  ? 0.85261 0.57133 0.82490 0.04527  0.02454  0.15191  86  ASP A O   
570  C CB  . ASP A 79  ? 0.87624 0.54586 0.84888 -0.01428 0.02595  0.11247  86  ASP A CB  
571  C CG  . ASP A 79  ? 1.06510 0.68067 1.03218 -0.03738 0.03272  0.09709  86  ASP A CG  
572  O OD1 . ASP A 79  ? 1.07960 0.68938 1.04038 -0.04592 0.02469  0.07279  86  ASP A OD1 
573  O OD2 . ASP A 79  ? 1.11967 0.69709 1.08684 -0.04782 0.04600  0.10926  86  ASP A OD2 
574  N N   . ARG A 80  ? 0.81242 0.56420 0.78174 0.02746  0.02452  0.16827  87  ARG A N   
575  C CA  . ARG A 80  ? 0.83272 0.63383 0.79682 0.04666  0.01190  0.17483  87  ARG A CA  
576  C C   . ARG A 80  ? 0.76912 0.59799 0.73951 0.04588  -0.00440 0.14953  87  ARG A C   
577  O O   . ARG A 80  ? 0.72039 0.56994 0.69315 0.06302  -0.01319 0.15057  87  ARG A O   
578  C CB  . ARG A 80  ? 0.82947 0.62540 0.78871 0.07383  0.01643  0.20052  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.82642 0.66917 0.77294 0.08888  0.00645  0.21707  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.78579 0.64999 0.73539 0.11465  -0.00342 0.22832  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.86947 0.70679 0.81714 0.13473  0.01059  0.25980  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.88791 0.73103 0.84598 0.15901  0.00840  0.27376  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.87089 0.74748 0.84418 0.16436  -0.00732 0.25907  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.91687 0.73243 0.87274 0.17900  0.02354  0.30518  87  ARG A NH2 
585  N N   . THR A 81  ? 0.67880 0.50968 0.65431 0.02529  -0.00834 0.12834  88  THR A N   
586  C CA  . THR A 81  ? 0.71875 0.57133 0.69969 0.02283  -0.02145 0.10560  88  THR A CA  
587  C C   . THR A 81  ? 0.65549 0.54078 0.63723 0.01085  -0.02886 0.09561  88  THR A C   
588  O O   . THR A 81  ? 0.66673 0.54945 0.65073 -0.00307 -0.02250 0.09941  88  THR A O   
589  C CB  . THR A 81  ? 0.68031 0.49908 0.66460 0.01286  -0.01842 0.08855  88  THR A CB  
590  O OG1 . THR A 81  ? 0.75155 0.55065 0.73646 -0.00981 -0.01396 0.08311  88  THR A OG1 
591  C CG2 . THR A 81  ? 0.72905 0.51102 0.71105 0.02777  -0.00735 0.09734  88  THR A CG2 
592  N N   . LEU A 82  ? 0.65099 0.56663 0.63308 0.01656  -0.04099 0.08374  89  LEU A N   
593  C CA  . LEU A 82  ? 0.58142 0.52326 0.56451 0.00813  -0.04682 0.07132  89  LEU A CA  
594  C C   . LEU A 82  ? 0.62581 0.56723 0.61760 0.00300  -0.05424 0.05157  89  LEU A C   
595  O O   . LEU A 82  ? 0.56696 0.51266 0.56079 0.01197  -0.06035 0.04631  89  LEU A O   
596  C CB  . LEU A 82  ? 0.56220 0.53506 0.53279 0.01921  -0.05314 0.07404  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.57176 0.56680 0.54083 0.01411  -0.05647 0.06017  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.52825 0.52455 0.50266 0.00358  -0.04534 0.06612  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.54819 0.56613 0.49826 0.02494  -0.06325 0.05870  89  LEU A CD2 
600  N N   . THR A 83  ? 0.55891 0.49781 0.55732 -0.01136 -0.05369 0.04265  90  THR A N   
601  C CA  . THR A 83  ? 0.55267 0.48859 0.55599 -0.01640 -0.05973 0.02660  90  THR A CA  
602  C C   . THR A 83  ? 0.58746 0.55147 0.59544 -0.01757 -0.06526 0.01836  90  THR A C   
603  O O   . THR A 83  ? 0.54025 0.51952 0.55254 -0.02290 -0.06226 0.02262  90  THR A O   
604  C CB  . THR A 83  ? 0.54460 0.45515 0.54913 -0.03162 -0.05712 0.02237  90  THR A CB  
605  O OG1 . THR A 83  ? 0.58493 0.46138 0.58268 -0.02920 -0.04901 0.02925  90  THR A OG1 
606  C CG2 . THR A 83  ? 0.57589 0.48354 0.57917 -0.03472 -0.06362 0.00717  90  THR A CG2 
607  N N   . ILE A 84  ? 0.55499 0.52482 0.56380 -0.01177 -0.07125 0.00801  91  ILE A N   
608  C CA  . ILE A 84  ? 0.53609 0.52454 0.54891 -0.01129 -0.07489 -0.00045 91  ILE A CA  
609  C C   . ILE A 84  ? 0.55359 0.53395 0.57086 -0.01669 -0.07799 -0.00853 91  ILE A C   
610  O O   . ILE A 84  ? 0.53163 0.49959 0.54686 -0.01333 -0.07908 -0.01299 91  ILE A O   
611  C CB  . ILE A 84  ? 0.51589 0.51487 0.52455 -0.00164 -0.07895 -0.00563 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.55774 0.56695 0.55500 0.00402  -0.07767 0.00193  91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.50235 0.51065 0.51437 -0.00069 -0.08027 -0.01539 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.60957 0.61446 0.60321 0.01008  -0.08058 0.00994  91  ILE A CD1 
615  N N   . VAL A 85  ? 0.51083 0.50116 0.53455 -0.02429 -0.07915 -0.00882 92  VAL A N   
616  C CA  . VAL A 85  ? 0.59380 0.58007 0.61820 -0.02982 -0.08413 -0.01463 92  VAL A CA  
617  C C   . VAL A 85  ? 0.60515 0.61121 0.63718 -0.02348 -0.08602 -0.01660 92  VAL A C   
618  O O   . VAL A 85  ? 0.59401 0.62019 0.63511 -0.02108 -0.08330 -0.01230 92  VAL A O   
619  C CB  . VAL A 85  ? 0.58345 0.56717 0.61041 -0.04538 -0.08696 -0.01253 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.52204 0.50533 0.54477 -0.05101 -0.09516 -0.01898 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.63041 0.58545 0.64802 -0.05109 -0.08244 -0.01095 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.51214 0.51082 0.54023 -0.01924 -0.08828 -0.02167 93  ASP A N   
623  C CA  . ASP A 86  ? 0.54433 0.55589 0.57894 -0.01247 -0.08899 -0.02163 93  ASP A CA  
624  C C   . ASP A 86  ? 0.56420 0.57127 0.59269 -0.01528 -0.09432 -0.02194 93  ASP A C   
625  O O   . ASP A 86  ? 0.55905 0.54749 0.57419 -0.02020 -0.09542 -0.02554 93  ASP A O   
626  C CB  . ASP A 86  ? 0.51376 0.51923 0.54821 -0.00249 -0.08452 -0.02621 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.59129 0.57921 0.62086 -0.00133 -0.08403 -0.02970 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.55463 0.53803 0.58125 -0.00024 -0.08442 -0.02827 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.56102 0.54240 0.59045 -0.00084 -0.08288 -0.03221 93  ASP A OD2 
630  N N   . THR A 87  ? 0.48762 0.51183 0.52388 -0.01045 -0.09683 -0.01728 94  THR A N   
631  C CA  . THR A 87  ? 0.45405 0.47825 0.48179 -0.01051 -0.10301 -0.01516 94  THR A CA  
632  C C   . THR A 87  ? 0.51829 0.53281 0.54394 0.00242  -0.09684 -0.01342 94  THR A C   
633  O O   . THR A 87  ? 0.49476 0.51856 0.52070 0.00902  -0.09940 -0.00611 94  THR A O   
634  C CB  . THR A 87  ? 0.50009 0.55484 0.54012 -0.01421 -0.11213 -0.00738 94  THR A CB  
635  O OG1 . THR A 87  ? 0.48255 0.55807 0.54361 -0.00386 -0.10589 -0.00081 94  THR A OG1 
636  C CG2 . THR A 87  ? 0.53627 0.59591 0.57689 -0.03239 -0.11969 -0.00981 94  THR A CG2 
637  N N   . GLY A 88  ? 0.49770 0.49456 0.52286 0.00567  -0.08896 -0.01868 95  GLY A N   
638  C CA  . GLY A 88  ? 0.52024 0.50495 0.54707 0.01438  -0.08190 -0.01753 95  GLY A CA  
639  C C   . GLY A 88  ? 0.47993 0.45146 0.49270 0.01494  -0.08036 -0.01461 95  GLY A C   
640  O O   . GLY A 88  ? 0.51063 0.48296 0.50793 0.01005  -0.08626 -0.01421 95  GLY A O   
641  N N   . ILE A 89  ? 0.48690 0.44447 0.50368 0.02013  -0.07145 -0.01305 96  ILE A N   
642  C CA  . ILE A 89  ? 0.51932 0.46465 0.52309 0.02312  -0.06594 -0.00729 96  ILE A CA  
643  C C   . ILE A 89  ? 0.54113 0.47684 0.53257 0.01785  -0.06379 -0.01226 96  ILE A C   
644  O O   . ILE A 89  ? 0.58867 0.51471 0.56059 0.02043  -0.05955 -0.00870 96  ILE A O   
645  C CB  . ILE A 89  ? 0.52327 0.45564 0.53974 0.02822  -0.05461 -0.00282 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.57604 0.49872 0.57796 0.03480  -0.04720 0.00886  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.48680 0.41326 0.51822 0.02165  -0.04993 -0.01013 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.61610 0.52418 0.63204 0.03966  -0.03483 0.01674  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.52720 0.46407 0.52712 0.01248  -0.06527 -0.01943 97  GLY A N   
650  C CA  . GLY A 90  ? 0.55257 0.47829 0.54318 0.01070  -0.06083 -0.02257 97  GLY A CA  
651  C C   . GLY A 90  ? 0.56263 0.48218 0.56490 0.01501  -0.04867 -0.01908 97  GLY A C   
652  O O   . GLY A 90  ? 0.57285 0.49575 0.59258 0.01609  -0.04491 -0.01557 97  GLY A O   
653  N N   . MET A 91  ? 0.57948 0.48890 0.57338 0.01729  -0.04115 -0.01974 98  MET A N   
654  C CA  . MET A 91  ? 0.53718 0.44652 0.54773 0.02208  -0.02808 -0.01443 98  MET A CA  
655  C C   . MET A 91  ? 0.60906 0.50075 0.59469 0.02922  -0.01470 -0.01229 98  MET A C   
656  O O   . MET A 91  ? 0.61732 0.49416 0.57794 0.02948  -0.01579 -0.01870 98  MET A O   
657  C CB  . MET A 91  ? 0.52280 0.44349 0.55680 0.02125  -0.03027 -0.01557 98  MET A CB  
658  C CG  . MET A 91  ? 0.52570 0.46436 0.58585 0.01512  -0.03956 -0.01709 98  MET A CG  
659  S SD  . MET A 91  ? 0.52095 0.47573 0.59725 0.01431  -0.04812 -0.01837 98  MET A SD  
660  C CE  . MET A 91  ? 0.49777 0.43709 0.54538 0.01570  -0.05087 -0.02133 98  MET A CE  
661  N N   . THR A 92  ? 0.62789 0.51854 0.61868 0.03457  -0.00072 -0.00359 99  THR A N   
662  C CA  . THR A 92  ? 0.57216 0.44620 0.53808 0.04382  0.01628  -0.00041 99  THR A CA  
663  C C   . THR A 92  ? 0.60427 0.48064 0.58956 0.05060  0.02923  0.00186  99  THR A C   
664  O O   . THR A 92  ? 0.55639 0.45091 0.57595 0.04748  0.02298  0.00261  99  THR A O   
665  C CB  . THR A 92  ? 0.65344 0.52671 0.61787 0.04828  0.02921  0.01150  99  THR A CB  
666  O OG1 . THR A 92  ? 0.64550 0.53556 0.65541 0.04631  0.03747  0.02033  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.57610 0.44986 0.52724 0.04458  0.01679  0.01297  99  THR A CG2 
668  N N   . LYS A 93  ? 0.62972 0.48822 0.59107 0.06163  0.04803  0.00375  100 LYS A N   
669  C CA  . LYS A 93  ? 0.70373 0.56557 0.68588 0.07236  0.06451  0.00900  100 LYS A CA  
670  C C   . LYS A 93  ? 0.59635 0.48970 0.63108 0.07221  0.07226  0.02327  100 LYS A C   
671  O O   . LYS A 93  ? 0.54278 0.45745 0.61558 0.07435  0.07213  0.02815  100 LYS A O   
672  C CB  . LYS A 93  ? 0.72902 0.56151 0.67049 0.08631  0.08674  0.00751  100 LYS A CB  
673  C CG  . LYS A 93  ? 0.71178 0.54168 0.66933 0.10096  0.10491  0.01162  100 LYS A CG  
674  C CD  . LYS A 93  ? 0.77457 0.56981 0.68661 0.11677  0.13045  0.00841  100 LYS A CD  
675  C CE  . LYS A 93  ? 0.76052 0.54986 0.68895 0.13451  0.15021  0.01289  100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.76405 0.52675 0.65905 0.15411  0.18294  0.01446  100 LYS A NZ  
677  N N   . ALA A 94  ? 0.58518 0.48270 0.62390 0.06892  0.07842  0.03117  101 ALA A N   
678  C CA  . ALA A 94  ? 0.61768 0.54328 0.70888 0.06395  0.08466  0.04388  101 ALA A CA  
679  C C   . ALA A 94  ? 0.58778 0.53499 0.71391 0.04933  0.06139  0.03835  101 ALA A C   
680  O O   . ALA A 94  ? 0.59001 0.56518 0.76376 0.04378  0.06116  0.04507  101 ALA A O   
681  C CB  . ALA A 94  ? 0.55401 0.47264 0.63855 0.06241  0.09676  0.05405  101 ALA A CB  
682  N N   . ASP A 95  ? 0.57341 0.50990 0.67634 0.04267  0.04171  0.02621  102 ASP A N   
683  C CA  . ASP A 95  ? 0.51542 0.46889 0.64271 0.03099  0.02121  0.01935  102 ASP A CA  
684  C C   . ASP A 95  ? 0.53989 0.51128 0.68655 0.03437  0.01581  0.01910  102 ASP A C   
685  O O   . ASP A 95  ? 0.51388 0.51182 0.69739 0.02706  0.00664  0.02087  102 ASP A O   
686  C CB  . ASP A 95  ? 0.55861 0.49769 0.65566 0.02649  0.00539  0.00847  102 ASP A CB  
687  C CG  . ASP A 95  ? 0.60768 0.53668 0.69743 0.02279  0.00655  0.01079  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.63179 0.56613 0.74840 0.01782  0.01381  0.01761  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.60702 0.52341 0.66630 0.02469  0.00022  0.00701  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.51661 0.47254 0.63752 0.04538  0.02106  0.01721  103 LEU A N   
691  C CA  . LEU A 96  ? 0.53910 0.50677 0.67376 0.05123  0.01648  0.01886  103 LEU A CA  
692  C C   . LEU A 96  ? 0.51588 0.50910 0.69054 0.06048  0.02977  0.03288  103 LEU A C   
693  O O   . LEU A 96  ? 0.54904 0.56520 0.74888 0.06380  0.02192  0.03801  103 LEU A O   
694  C CB  . LEU A 96  ? 0.52758 0.46384 0.62225 0.05961  0.02058  0.01269  103 LEU A CB  
695  C CG  . LEU A 96  ? 0.58792 0.50489 0.64829 0.04973  0.00619  0.00038  103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.58205 0.46383 0.60162 0.05498  0.01372  -0.00641 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.56435 0.49755 0.63783 0.04212  -0.01259 -0.00226 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.48685 0.47970 0.66921 0.06576  0.05016  0.04131  104 ILE A N   
699  C CA  . ILE A 97  ? 0.57491 0.59451 0.79802 0.07665  0.06700  0.05706  104 ILE A CA  
700  C C   . ILE A 97  ? 0.61423 0.66878 0.88712 0.06302  0.06526  0.06587  104 ILE A C   
701  O O   . ILE A 97  ? 0.71180 0.80653 1.03474 0.06256  0.06249  0.07658  104 ILE A O   
702  C CB  . ILE A 97  ? 0.58772 0.58111 0.78372 0.09548  0.09696  0.06203  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.62407 0.58302 0.77821 0.10823  0.09929  0.05311  104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.67324 0.69859 0.91701 0.10744  0.11897  0.08125  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.73195 0.64595 0.82944 0.11710  0.11785  0.04528  104 ILE A CD1 
706  N N   . ASN A 98  ? 0.56313 0.60354 0.82478 0.05114  0.06603  0.06228  105 ASN A N   
707  C CA  . ASN A 98  ? 0.58394 0.64830 0.89057 0.03777  0.07037  0.07176  105 ASN A CA  
708  C C   . ASN A 98  ? 0.54796 0.61169 0.86089 0.01586  0.04762  0.06032  105 ASN A C   
709  O O   . ASN A 98  ? 0.48222 0.57689 0.83840 0.00128  0.03374  0.06040  105 ASN A O   
710  C CB  . ASN A 98  ? 0.60466 0.65005 0.89651 0.04502  0.09842  0.08230  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.73482 0.79809 1.04989 0.06203  0.12582  0.09930  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.75644 0.79562 1.03241 0.08168  0.14338  0.09935  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.74698 0.85254 1.12630 0.05419  0.13038  0.11359  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.60312 0.58083 0.50599 0.02986  0.04841  -0.02849 106 ASN A N   
715  C CA  . ASN A 99  ? 0.65583 0.62885 0.58186 0.02032  0.03558  -0.00597 106 ASN A CA  
716  C C   . ASN A 99  ? 0.62920 0.58895 0.59260 0.02457  0.02594  -0.01196 106 ASN A C   
717  O O   . ASN A 99  ? 0.63228 0.59516 0.62479 0.02008  0.02653  -0.00278 106 ASN A O   
718  C CB  . ASN A 99  ? 0.64597 0.61073 0.54518 0.01476  0.01885  0.00521  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.68555 0.66645 0.53805 0.00968  0.02574  0.01136  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.70123 0.70096 0.54722 0.00659  0.04469  0.02087  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.73242 0.71217 0.55137 0.00670  0.01019  0.00662  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.58317 0.52766 0.54322 0.03031  0.01667  -0.02717 107 LEU A N   
723  C CA  . LEU A 100 ? 0.60742 0.54338 0.59621 0.03351  0.00810  -0.02970 107 LEU A CA  
724  C C   . LEU A 100 ? 0.57048 0.51746 0.58416 0.04017  0.01681  -0.03443 107 LEU A C   
725  O O   . LEU A 100 ? 0.63041 0.57873 0.66719 0.03950  0.01057  -0.03236 107 LEU A O   
726  C CB  . LEU A 100 ? 0.54664 0.46744 0.52593 0.03400  -0.00201 -0.04030 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.60637 0.52945 0.57227 0.02585  -0.01567 -0.03384 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.60750 0.52298 0.57417 0.02037  -0.02567 -0.04224 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.57358 0.50435 0.55857 0.02780  -0.02123 -0.01666 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.57116 0.53049 0.58006 0.04827  0.03093  -0.04145 108 GLY A N   
731  C CA  . GLY A 101 ? 0.60823 0.59135 0.64747 0.05691  0.03823  -0.04208 108 GLY A CA  
732  C C   . GLY A 101 ? 0.54463 0.55477 0.60970 0.04295  0.03980  -0.02861 108 GLY A C   
733  O O   . GLY A 101 ? 0.55733 0.58639 0.65226 0.04233  0.03538  -0.02769 108 GLY A O   
734  N N   . THR A 102 ? 0.58724 0.59830 0.63952 0.02922  0.04443  -0.01671 109 THR A N   
735  C CA  . THR A 102 ? 0.58556 0.60996 0.66046 0.01024  0.04492  -0.00182 109 THR A CA  
736  C C   . THR A 102 ? 0.56523 0.56128 0.65123 0.00304  0.02736  -0.00271 109 THR A C   
737  O O   . THR A 102 ? 0.56432 0.57046 0.67613 -0.00894 0.02302  -0.00266 109 THR A O   
738  C CB  . THR A 102 ? 0.61655 0.64010 0.66981 -0.00254 0.05378  0.01620  109 THR A CB  
739  O OG1 . THR A 102 ? 0.60502 0.65705 0.63962 0.00633  0.07244  0.01275  109 THR A OG1 
740  C CG2 . THR A 102 ? 0.67788 0.71050 0.75585 -0.02676 0.05627  0.03433  109 THR A CG2 
741  N N   . ILE A 103 ? 0.55612 0.52062 0.62286 0.00996  0.01729  -0.00522 110 ILE A N   
742  C CA  . ILE A 103 ? 0.54816 0.48908 0.62321 0.00944  0.00441  -0.00979 110 ILE A CA  
743  C C   . ILE A 103 ? 0.57524 0.52899 0.66336 0.01642  -0.00062 -0.02399 110 ILE A C   
744  O O   . ILE A 103 ? 0.55814 0.50756 0.65735 0.01081  -0.00822 -0.03030 110 ILE A O   
745  C CB  . ILE A 103 ? 0.62071 0.53909 0.67788 0.01835  -0.00289 -0.00669 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.68233 0.58810 0.72649 0.01266  -0.00158 0.01278  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.62577 0.52721 0.69174 0.02428  -0.01179 -0.01496 110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.68238 0.59217 0.70300 0.02039  -0.00610 0.01850  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.52359 0.48978 0.60685 0.02870  0.00299  -0.02911 111 ALA A N   
750  C CA  . ALA A 104 ? 0.54361 0.52040 0.63682 0.03726  -0.00243 -0.03620 111 ALA A CA  
751  C C   . ALA A 104 ? 0.56743 0.57786 0.68685 0.03211  -0.00298 -0.03551 111 ALA A C   
752  O O   . ALA A 104 ? 0.54908 0.56984 0.67691 0.03160  -0.01338 -0.03965 111 ALA A O   
753  C CB  . ALA A 104 ? 0.50342 0.47449 0.58486 0.05190  0.00179  -0.03922 111 ALA A CB  
754  N N   . LYS A 105 ? 0.53284 0.56794 0.66533 0.02680  0.00785  -0.02942 112 LYS A N   
755  C CA  . LYS A 105 ? 0.54379 0.62504 0.70946 0.01961  0.00714  -0.02663 112 LYS A CA  
756  C C   . LYS A 105 ? 0.50079 0.57717 0.67632 -0.00506 -0.00596 -0.02900 112 LYS A C   
757  O O   . LYS A 105 ? 0.54495 0.64711 0.73690 -0.00964 -0.01842 -0.03410 112 LYS A O   
758  C CB  . LYS A 105 ? 0.52228 0.63812 0.70154 0.01715  0.02531  -0.01789 112 LYS A CB  
759  C CG  . LYS A 105 ? 0.48885 0.66709 0.71154 0.00663  0.02568  -0.01201 112 LYS A CG  
760  C CD  . LYS A 105 ? 0.47862 0.69736 0.71545 0.00064  0.04768  -0.00080 112 LYS A CD  
761  C CE  . LYS A 105 ? 0.51373 0.80903 0.79486 0.01420  0.05538  0.00251  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.49787 0.85259 0.81667 -0.01582 0.06394  0.01702  112 LYS A NZ  
763  N N   . SER A 106 ? 0.52665 0.56689 0.68967 -0.02075 -0.00458 -0.02569 113 SER A N   
764  C CA  . SER A 106 ? 0.56842 0.58738 0.73609 -0.04374 -0.01617 -0.03148 113 SER A CA  
765  C C   . SER A 106 ? 0.56749 0.56234 0.71806 -0.03413 -0.02921 -0.04845 113 SER A C   
766  O O   . SER A 106 ? 0.57375 0.56978 0.72847 -0.04874 -0.04164 -0.06105 113 SER A O   
767  C CB  . SER A 106 ? 0.61631 0.59174 0.77253 -0.05722 -0.01069 -0.02053 113 SER A CB  
768  O OG  . SER A 106 ? 0.67484 0.60469 0.80507 -0.04023 -0.01336 -0.02428 113 SER A OG  
769  N N   . GLY A 107 ? 0.57327 0.55019 0.70316 -0.01193 -0.02635 -0.04961 114 GLY A N   
770  C CA  . GLY A 107 ? 0.57267 0.53561 0.68627 -0.00243 -0.03454 -0.06290 114 GLY A CA  
771  C C   . GLY A 107 ? 0.57382 0.57376 0.69136 0.00324  -0.04246 -0.06642 114 GLY A C   
772  O O   . GLY A 107 ? 0.54559 0.54619 0.65145 0.00087  -0.05223 -0.07887 114 GLY A O   
773  N N   . THR A 108 ? 0.52584 0.55581 0.65675 0.01334  -0.03810 -0.05527 115 THR A N   
774  C CA  . THR A 108 ? 0.53882 0.60387 0.67619 0.02304  -0.04685 -0.05268 115 THR A CA  
775  C C   . THR A 108 ? 0.51513 0.61810 0.67171 0.00509  -0.06052 -0.05783 115 THR A C   
776  O O   . THR A 108 ? 0.58968 0.71028 0.73698 0.00450  -0.07491 -0.06316 115 THR A O   
777  C CB  . THR A 108 ? 0.52167 0.60307 0.67143 0.04247  -0.03764 -0.04033 115 THR A CB  
778  O OG1 . THR A 108 ? 0.53538 0.57992 0.66220 0.05542  -0.03049 -0.03841 115 THR A OG1 
779  C CG2 . THR A 108 ? 0.53052 0.65374 0.69612 0.05514  -0.04782 -0.03253 115 THR A CG2 
780  N N   . LYS A 109 ? 0.47650 0.59647 0.65869 -0.01278 -0.05696 -0.05526 116 LYS A N   
781  C CA  . LYS A 109 ? 0.49429 0.65576 0.70037 -0.03721 -0.07162 -0.05976 116 LYS A CA  
782  C C   . LYS A 109 ? 0.56245 0.69213 0.74295 -0.05641 -0.08656 -0.08088 116 LYS A C   
783  O O   . LYS A 109 ? 0.59208 0.75544 0.77399 -0.06802 -0.10543 -0.08978 116 LYS A O   
784  C CB  . LYS A 109 ? 0.47019 0.64989 0.70724 -0.05894 -0.06192 -0.05102 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.64606 0.88229 0.91842 -0.08917 -0.07681 -0.05210 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.71482 0.94156 1.00534 -0.12432 -0.06889 -0.04666 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.73358 1.00011 1.05267 -0.16605 -0.08881 -0.05338 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.86347 1.05495 1.15595 -0.19871 -0.09860 -0.07169 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.54488 0.61113 0.70014 -0.05777 -0.07879 -0.09013 117 ALA A N   
790  C CA  . ALA A 110 ? 0.59936 0.62721 0.72679 -0.06973 -0.08907 -0.11450 117 ALA A CA  
791  C C   . ALA A 110 ? 0.57253 0.60988 0.66990 -0.04999 -0.09477 -0.12337 117 ALA A C   
792  O O   . ALA A 110 ? 0.67885 0.71865 0.75497 -0.06123 -0.10881 -0.14410 117 ALA A O   
793  C CB  . ALA A 110 ? 0.59212 0.55096 0.70491 -0.06858 -0.07743 -0.11886 117 ALA A CB  
794  N N   . PHE A 111 ? 0.54981 0.59198 0.64179 -0.02326 -0.08406 -0.10794 118 PHE A N   
795  C CA  . PHE A 111 ? 0.59425 0.64721 0.65816 -0.00710 -0.08707 -0.10975 118 PHE A CA  
796  C C   . PHE A 111 ? 0.57225 0.67953 0.63880 -0.01072 -0.10516 -0.10526 118 PHE A C   
797  O O   . PHE A 111 ? 0.57648 0.69544 0.61192 -0.01000 -0.11466 -0.11481 118 PHE A O   
798  C CB  . PHE A 111 ? 0.53422 0.57907 0.59679 0.01558  -0.07296 -0.09078 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.58520 0.63887 0.62012 0.02856  -0.07290 -0.08698 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.60804 0.65856 0.61199 0.02571  -0.07549 -0.10596 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.58964 0.65206 0.62690 0.04290  -0.06885 -0.06437 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.61127 0.67726 0.58770 0.03612  -0.07253 -0.09924 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.58361 0.65356 0.59541 0.05060  -0.06788 -0.05546 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.60444 0.68125 0.58612 0.04679  -0.06896 -0.07126 118 PHE A CZ  
805  N N   . MET A 112 ? 0.53981 0.68671 0.64296 -0.01310 -0.11000 -0.08987 119 MET A N   
806  C CA  . MET A 112 ? 0.58642 0.79398 0.69888 -0.01063 -0.12866 -0.07978 119 MET A CA  
807  C C   . MET A 112 ? 0.56140 0.79725 0.67308 -0.04121 -0.15079 -0.09971 119 MET A C   
808  O O   . MET A 112 ? 0.67874 0.95912 0.77768 -0.04202 -0.17103 -0.09874 119 MET A O   
809  C CB  . MET A 112 ? 0.55942 0.80495 0.71571 0.00449  -0.12385 -0.05593 119 MET A CB  
810  C CG  . MET A 112 ? 0.57885 0.78853 0.72899 0.03220  -0.10419 -0.04119 119 MET A CG  
811  S SD  . MET A 112 ? 0.75691 0.98296 0.89495 0.06261  -0.11131 -0.01678 119 MET A SD  
812  C CE  . MET A 112 ? 0.60052 0.85604 0.78617 0.08735  -0.10305 0.00174  119 MET A CE  
813  N N   . GLU A 113 ? 0.63058 0.83981 0.75345 -0.06860 -0.14898 -0.11673 120 GLU A N   
814  C CA  . GLU A 113 ? 0.66466 0.88164 0.77767 -0.10343 -0.17041 -0.14247 120 GLU A CA  
815  C C   . GLU A 113 ? 0.71831 0.89989 0.77215 -0.10043 -0.17519 -0.16904 120 GLU A C   
816  O O   . GLU A 113 ? 0.76747 0.97927 0.79842 -0.11693 -0.19799 -0.18616 120 GLU A O   
817  C CB  . GLU A 113 ? 0.70270 0.88022 0.83591 -0.13437 -0.16485 -0.15320 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.80191 1.02857 0.99314 -0.14584 -0.16079 -0.12923 120 GLU A CG  
819  C CD  . GLU A 113 ? 1.01655 1.19271 1.22102 -0.17223 -0.14858 -0.13142 120 GLU A CD  
820  O OE1 . GLU A 113 ? 1.03464 1.24882 1.28310 -0.18266 -0.13992 -0.11038 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 1.16954 1.26818 1.33974 -0.18067 -0.14642 -0.15263 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.68046 0.80467 0.70851 -0.07905 -0.15370 -0.17307 121 ALA A N   
823  C CA  . ALA A 114 ? 0.76959 0.86543 0.74334 -0.07169 -0.15222 -0.19846 121 ALA A CA  
824  C C   . ALA A 114 ? 0.73778 0.88523 0.68516 -0.05507 -0.16023 -0.18505 121 ALA A C   
825  O O   . ALA A 114 ? 0.83292 0.98892 0.73412 -0.06063 -0.17064 -0.20732 121 ALA A O   
826  C CB  . ALA A 114 ? 0.71143 0.74718 0.67487 -0.05033 -0.12621 -0.20115 121 ALA A CB  
827  N N   . LEU A 115 ? 0.67995 0.85833 0.65199 -0.03448 -0.15525 -0.14862 122 LEU A N   
828  C CA  . LEU A 115 ? 0.66951 0.89000 0.61754 -0.01805 -0.16287 -0.12825 122 LEU A CA  
829  C C   . LEU A 115 ? 0.78675 1.06742 0.72605 -0.03443 -0.19380 -0.13237 122 LEU A C   
830  O O   . LEU A 115 ? 0.86192 1.17158 0.75884 -0.02852 -0.20405 -0.12833 122 LEU A O   
831  C CB  . LEU A 115 ? 0.64431 0.87453 0.62425 0.00594  -0.15328 -0.08919 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.61685 0.79967 0.59121 0.02293  -0.12709 -0.08023 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.59856 0.77913 0.60841 0.03990  -0.11938 -0.05073 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.62472 0.80893 0.55255 0.03186  -0.12133 -0.07605 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.75781 1.06423 0.73651 -0.05702 -0.20965 -0.13834 123 GLN A N   
836  C CA  . GLN A 116 ? 0.81368 1.18460 0.78843 -0.07874 -0.24296 -0.14532 123 GLN A CA  
837  C C   . GLN A 116 ? 0.86869 1.21346 0.79442 -0.10937 -0.25501 -0.19230 123 GLN A C   
838  O O   . GLN A 116 ? 0.89513 1.29083 0.79758 -0.12818 -0.28457 -0.20367 123 GLN A O   
839  C CB  . GLN A 116 ? 0.79837 1.21898 0.84123 -0.09409 -0.25518 -0.13199 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.79095 1.24151 0.88135 -0.06025 -0.24372 -0.08987 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.91562 1.46182 1.03944 -0.05414 -0.27100 -0.06446 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.89117 1.49205 1.01730 -0.08393 -0.30040 -0.07821 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.98381 1.55016 1.13412 -0.01490 -0.26268 -0.02752 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.89269 1.15849 0.80062 -0.11328 -0.23386 -0.22049 124 ALA A N   
845  C CA  . ALA A 117 ? 0.92070 1.14340 0.77978 -0.13747 -0.24094 -0.26990 124 ALA A CA  
846  C C   . ALA A 117 ? 1.00583 1.20166 0.79812 -0.11360 -0.22477 -0.28703 124 ALA A C   
847  O O   . ALA A 117 ? 1.12177 1.25854 0.87468 -0.11971 -0.21656 -0.32929 124 ALA A O   
848  C CB  . ALA A 117 ? 0.94396 1.09236 0.82740 -0.15580 -0.22873 -0.29031 124 ALA A CB  
849  N N   . GLY A 118 ? 0.98042 1.21740 0.75987 -0.08570 -0.21825 -0.25404 125 GLY A N   
850  C CA  . GLY A 118 ? 1.06077 1.29166 0.77827 -0.06578 -0.20268 -0.26336 125 GLY A CA  
851  C C   . GLY A 118 ? 0.92085 1.12051 0.65038 -0.03499 -0.16792 -0.24159 125 GLY A C   
852  O O   . GLY A 118 ? 0.98745 1.20496 0.67826 -0.01706 -0.15441 -0.23124 125 GLY A O   
853  N N   . ALA A 119 ? 0.90997 1.06867 0.69085 -0.03094 -0.15374 -0.23303 126 ALA A N   
854  C CA  . ALA A 119 ? 0.89084 1.02302 0.68474 -0.00569 -0.12417 -0.21503 126 ALA A CA  
855  C C   . ALA A 119 ? 0.88885 1.06137 0.69157 0.00976  -0.12142 -0.16886 126 ALA A C   
856  O O   . ALA A 119 ? 0.90172 1.11342 0.71936 0.00595  -0.14084 -0.14460 126 ALA A O   
857  C CB  . ALA A 119 ? 0.78026 0.86623 0.62440 -0.00707 -0.11452 -0.21282 126 ALA A CB  
858  N N   . ASP A 120 ? 0.84006 1.00236 0.63560 0.02754  -0.09718 -0.15576 127 ASP A N   
859  C CA  . ASP A 120 ? 0.85781 1.04398 0.65872 0.03890  -0.09176 -0.11240 127 ASP A CA  
860  C C   . ASP A 120 ? 0.79226 0.94677 0.63871 0.04676  -0.07601 -0.09386 127 ASP A C   
861  O O   . ASP A 120 ? 0.76713 0.88791 0.63819 0.04547  -0.06905 -0.11184 127 ASP A O   
862  C CB  . ASP A 120 ? 0.93186 1.14295 0.68272 0.04614  -0.07793 -0.10814 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.94117 1.13097 0.68758 0.05573  -0.05004 -0.12928 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.96591 1.12440 0.71422 0.05547  -0.04780 -0.16721 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.95443 1.15966 0.69787 0.06353  -0.03053 -0.10627 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.77351 0.93637 0.62743 0.05378  -0.07166 -0.05663 128 ILE A N   
867  C CA  . ILE A 121 ? 0.73027 0.86358 0.62287 0.05796  -0.06118 -0.03945 128 ILE A CA  
868  C C   . ILE A 121 ? 0.77240 0.88870 0.66927 0.06012  -0.04007 -0.05145 128 ILE A C   
869  O O   . ILE A 121 ? 0.76290 0.85301 0.69106 0.06069  -0.03459 -0.05223 128 ILE A O   
870  C CB  . ILE A 121 ? 0.70397 0.84096 0.59769 0.06303  -0.06299 0.00093  128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.76271 0.91120 0.67189 0.06855  -0.08343 0.01435  128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.67699 0.78057 0.59647 0.06324  -0.04900 0.01460  128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.78561 0.95522 0.67244 0.07607  -0.09343 0.04953  128 ILE A CD1 
874  N N   . SER A 122 ? 0.70463 0.84141 0.57033 0.06304  -0.02786 -0.06107 129 SER A N   
875  C CA  . SER A 122 ? 0.73231 0.86670 0.60808 0.06946  -0.00663 -0.06831 129 SER A CA  
876  C C   . SER A 122 ? 0.69272 0.79549 0.58909 0.07516  -0.00502 -0.09746 129 SER A C   
877  O O   . SER A 122 ? 0.69281 0.79167 0.60987 0.08329  0.00878  -0.09817 129 SER A O   
878  C CB  . SER A 122 ? 0.72262 0.89404 0.55995 0.07509  0.00907  -0.07502 129 SER A CB  
879  O OG  . SER A 122 ? 0.82372 0.99371 0.62758 0.07912  0.00447  -0.11173 129 SER A OG  
880  N N   . MET A 123 ? 0.69102 0.77310 0.58393 0.06981  -0.01982 -0.11858 130 MET A N   
881  C CA  . MET A 123 ? 0.68921 0.73227 0.59973 0.07191  -0.01951 -0.14171 130 MET A CA  
882  C C   . MET A 123 ? 0.67923 0.70102 0.62819 0.06546  -0.02599 -0.12502 130 MET A C   
883  O O   . MET A 123 ? 0.64651 0.63624 0.60890 0.06161  -0.02981 -0.13813 130 MET A O   
884  C CB  . MET A 123 ? 0.67354 0.70117 0.55910 0.06312  -0.03184 -0.17421 130 MET A CB  
885  C CG  . MET A 123 ? 0.84994 0.89768 0.68697 0.06936  -0.02579 -0.19687 130 MET A CG  
886  S SD  . MET A 123 ? 0.89129 0.93886 0.69094 0.04858  -0.05045 -0.22769 130 MET A SD  
887  C CE  . MET A 123 ? 0.87103 0.84652 0.67728 0.04591  -0.04928 -0.26811 130 MET A CE  
888  N N   . ILE A 124 ? 0.58051 0.61605 0.54393 0.06375  -0.02621 -0.09663 131 ILE A N   
889  C CA  . ILE A 124 ? 0.60668 0.62487 0.59906 0.05912  -0.03086 -0.08382 131 ILE A CA  
890  C C   . ILE A 124 ? 0.56276 0.55759 0.57311 0.06360  -0.02280 -0.08728 131 ILE A C   
891  O O   . ILE A 124 ? 0.55702 0.53284 0.58422 0.05878  -0.02644 -0.08517 131 ILE A O   
892  C CB  . ILE A 124 ? 0.62805 0.65654 0.62525 0.05892  -0.03139 -0.05702 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.57153 0.58274 0.59220 0.05708  -0.03480 -0.04905 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.57042 0.60607 0.56530 0.06068  -0.01929 -0.04507 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.56695 0.57543 0.58952 0.05991  -0.03574 -0.02760 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.61697 0.61893 0.62469 0.07402  -0.01151 -0.09047 132 GLY A N   
897  C CA  . GLY A 125 ? 0.60595 0.59376 0.63330 0.08183  -0.00638 -0.08913 132 GLY A CA  
898  C C   . GLY A 125 ? 0.58345 0.53468 0.61230 0.08591  -0.00881 -0.10622 132 GLY A C   
899  O O   . GLY A 125 ? 0.64789 0.57961 0.69292 0.08848  -0.00968 -0.09852 132 GLY A O   
900  N N   . GLN A 126 ? 0.62469 0.56315 0.63367 0.08451  -0.01111 -0.12879 133 GLN A N   
901  C CA  . GLN A 126 ? 0.61688 0.50868 0.62485 0.08355  -0.01446 -0.14660 133 GLN A CA  
902  C C   . GLN A 126 ? 0.61852 0.49204 0.64181 0.06343  -0.02491 -0.13589 133 GLN A C   
903  O O   . GLN A 126 ? 0.69679 0.52777 0.72280 0.05748  -0.02770 -0.14377 133 GLN A O   
904  C CB  . GLN A 126 ? 0.63646 0.51704 0.61419 0.08127  -0.01665 -0.17784 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.71613 0.62759 0.67152 0.09954  -0.00377 -0.18879 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.86488 0.75892 0.78175 0.09931  -0.00483 -0.22594 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.90185 0.74216 0.81250 0.09433  -0.01043 -0.24916 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.82596 0.76260 0.71287 0.10251  0.00021  -0.23177 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.60619 0.50923 0.63943 0.05356  -0.02907 -0.11765 134 PHE A N   
910  C CA  . PHE A 127 ? 0.58766 0.48654 0.63720 0.03729  -0.03484 -0.10687 134 PHE A CA  
911  C C   . PHE A 127 ? 0.57649 0.48075 0.63895 0.04162  -0.02959 -0.08517 134 PHE A C   
912  O O   . PHE A 127 ? 0.59346 0.50175 0.66694 0.03115  -0.03042 -0.07518 134 PHE A O   
913  C CB  . PHE A 127 ? 0.56768 0.49943 0.61831 0.02515  -0.04410 -0.10733 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.60251 0.53563 0.63506 0.01674  -0.05335 -0.13001 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.57602 0.52702 0.58353 0.02732  -0.05257 -0.13841 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.57575 0.49340 0.61341 -0.00497 -0.06302 -0.14318 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.61106 0.56504 0.59338 0.01912  -0.06169 -0.16236 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.62358 0.54064 0.63959 -0.01653 -0.07435 -0.16855 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.65309 0.58853 0.63855 -0.00309 -0.07389 -0.17962 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.55090 0.46042 0.61168 0.05553  -0.02408 -0.07873 135 GLY A N   
921  C CA  . GLY A 128 ? 0.53891 0.45251 0.60662 0.05684  -0.02218 -0.06197 135 GLY A CA  
922  C C   . GLY A 128 ? 0.57232 0.50459 0.63920 0.05178  -0.02243 -0.05390 135 GLY A C   
923  O O   . GLY A 128 ? 0.59195 0.52264 0.65885 0.04968  -0.02143 -0.04489 135 GLY A O   
924  N N   . VAL A 129 ? 0.55830 0.50516 0.62113 0.05113  -0.02418 -0.05690 136 VAL A N   
925  C CA  . VAL A 129 ? 0.50681 0.46134 0.56916 0.05080  -0.02425 -0.04825 136 VAL A CA  
926  C C   . VAL A 129 ? 0.53704 0.50018 0.59057 0.05331  -0.02381 -0.04259 136 VAL A C   
927  O O   . VAL A 129 ? 0.51139 0.47758 0.56119 0.05500  -0.02585 -0.03523 136 VAL A O   
928  C CB  . VAL A 129 ? 0.54836 0.51494 0.61859 0.04931  -0.02773 -0.04910 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.49278 0.45665 0.57459 0.04262  -0.02483 -0.04958 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.52558 0.50632 0.59167 0.04682  -0.03494 -0.05742 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.54076 0.57525 0.55589 0.00937  -0.03006 -0.05302 137 GLY A N   
932  C CA  . GLY A 130 ? 0.52076 0.56654 0.52648 0.02343  -0.02606 -0.04725 137 GLY A CA  
933  C C   . GLY A 130 ? 0.50970 0.56805 0.52882 0.02448  -0.01887 -0.03377 137 GLY A C   
934  O O   . GLY A 130 ? 0.47412 0.54424 0.48990 0.03380  -0.01567 -0.02580 137 GLY A O   
935  N N   . PHE A 131 ? 0.44770 0.50213 0.48045 0.01560  -0.01628 -0.03086 138 PHE A N   
936  C CA  . PHE A 131 ? 0.49369 0.55353 0.53704 0.01653  -0.01145 -0.02124 138 PHE A CA  
937  C C   . PHE A 131 ? 0.48673 0.56024 0.53494 0.02097  -0.01299 -0.01735 138 PHE A C   
938  O O   . PHE A 131 ? 0.45458 0.53073 0.50676 0.02598  -0.00958 -0.00757 138 PHE A O   
939  C CB  . PHE A 131 ? 0.46308 0.51487 0.51416 0.00859  -0.00944 -0.02207 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.48426 0.53736 0.54399 0.00965  -0.00702 -0.01694 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.45275 0.50112 0.51548 0.01090  -0.00557 -0.01058 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.46971 0.52852 0.53595 0.00966  -0.00661 -0.01864 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.48318 0.52591 0.55304 0.01092  -0.00530 -0.00780 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.50093 0.55536 0.57208 0.01328  -0.00467 -0.01591 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.51418 0.55724 0.58602 0.01332  -0.00479 -0.01139 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.44499 0.52770 0.49491 0.01892  -0.01876 -0.02369 139 TYR A N   
947  C CA  . TYR A 132 ? 0.45954 0.55881 0.51497 0.02514  -0.02143 -0.01946 139 TYR A CA  
948  C C   . TYR A 132 ? 0.44469 0.55178 0.48761 0.03672  -0.02241 -0.01310 139 TYR A C   
949  O O   . TYR A 132 ? 0.44005 0.55881 0.48605 0.04456  -0.02324 -0.00524 139 TYR A O   
950  C CB  . TYR A 132 ? 0.46161 0.57504 0.52488 0.01942  -0.02919 -0.02750 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.49508 0.60709 0.57285 0.00922  -0.02563 -0.02963 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.47777 0.58668 0.56263 0.01211  -0.01765 -0.02408 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.47705 0.58973 0.56025 -0.00291 -0.03010 -0.03683 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.42422 0.53447 0.51808 0.00572  -0.01277 -0.02539 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.51540 0.62998 0.61186 -0.01168 -0.02455 -0.03516 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.49280 0.60803 0.59296 -0.00604 -0.01515 -0.02930 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.56214 0.68169 0.67127 -0.01190 -0.00809 -0.02712 139 TYR A OH  
958  N N   . SER A 133 ? 0.44473 0.54657 0.47248 0.04012  -0.02137 -0.01508 140 SER A N   
959  C CA  . SER A 133 ? 0.46795 0.57968 0.48137 0.05317  -0.01917 -0.00663 140 SER A CA  
960  C C   . SER A 133 ? 0.47205 0.58367 0.49518 0.05641  -0.00974 0.01157  140 SER A C   
961  O O   . SER A 133 ? 0.53424 0.65660 0.54892 0.06709  -0.00608 0.02385  140 SER A O   
962  C CB  . SER A 133 ? 0.49922 0.60587 0.49356 0.05846  -0.01824 -0.01362 140 SER A CB  
963  O OG  . SER A 133 ? 0.50874 0.60540 0.51036 0.05518  -0.00998 -0.00880 140 SER A OG  
964  N N   . ALA A 134 ? 0.49887 0.59787 0.53865 0.04721  -0.00629 0.01385  141 ALA A N   
965  C CA  . ALA A 134 ? 0.45600 0.55021 0.50777 0.04715  -0.00014 0.02941  141 ALA A CA  
966  C C   . ALA A 134 ? 0.50745 0.60560 0.56205 0.05463  -0.00089 0.03940  141 ALA A C   
967  O O   . ALA A 134 ? 0.53544 0.63138 0.59526 0.05793  0.00435  0.05630  141 ALA A O   
968  C CB  . ALA A 134 ? 0.47844 0.55603 0.54402 0.03600  0.00006  0.02526  141 ALA A CB  
969  N N   . TYR A 135 ? 0.44646 0.55154 0.49981 0.05745  -0.00729 0.03097  142 TYR A N   
970  C CA  . TYR A 135 ? 0.48659 0.59785 0.54310 0.06742  -0.00889 0.04037  142 TYR A CA  
971  C C   . TYR A 135 ? 0.51615 0.64591 0.55664 0.08021  -0.01057 0.04976  142 TYR A C   
972  O O   . TYR A 135 ? 0.49039 0.62798 0.53123 0.09097  -0.01269 0.05961  142 TYR A O   
973  C CB  . TYR A 135 ? 0.47279 0.59127 0.53779 0.06669  -0.01478 0.02897  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.49034 0.59098 0.56775 0.05934  -0.01109 0.02335  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.45009 0.53687 0.53583 0.06562  -0.00815 0.03006  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.43844 0.53344 0.51616 0.04776  -0.01069 0.01138  142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.48687 0.55581 0.57855 0.06118  -0.00557 0.02232  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.49052 0.57083 0.57461 0.04310  -0.00749 0.00627  142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.53424 0.60199 0.62407 0.05012  -0.00521 0.01051  142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.54475 0.59655 0.63581 0.04767  -0.00285 0.00280  142 TYR A OH  
981  N N   . LEU A 136 ? 0.51004 0.64716 0.53421 0.08170  -0.00965 0.04692  143 LEU A N   
982  C CA  . LEU A 136 ? 0.57891 0.73249 0.58333 0.09634  -0.00843 0.05855  143 LEU A CA  
983  C C   . LEU A 136 ? 0.57951 0.72821 0.59093 0.10072  0.00276  0.08428  143 LEU A C   
984  O O   . LEU A 136 ? 0.51206 0.67206 0.51326 0.11408  0.00414  0.10054  143 LEU A O   
985  C CB  . LEU A 136 ? 0.49470 0.65448 0.47790 0.09932  -0.00805 0.04863  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.51803 0.67967 0.48956 0.09607  -0.02079 0.02383  143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.54249 0.69871 0.49595 0.09854  -0.01783 0.01400  143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.52129 0.70246 0.47723 0.10679  -0.03284 0.02036  143 LEU A CD2 
989  N N   . VAL A 137 ? 0.55689 0.68886 0.58655 0.08891  0.00991  0.08922  144 VAL A N   
990  C CA  . VAL A 137 ? 0.61264 0.73807 0.65436 0.08830  0.01978  0.11397  144 VAL A CA  
991  C C   . VAL A 137 ? 0.52435 0.62279 0.58956 0.07804  0.01861  0.11665  144 VAL A C   
992  O O   . VAL A 137 ? 0.58406 0.67125 0.66108 0.07704  0.02431  0.13779  144 VAL A O   
993  C CB  . VAL A 137 ? 0.53194 0.66544 0.57642 0.08367  0.02916  0.12099  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.54337 0.70149 0.55988 0.09865  0.03205  0.11946  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.55246 0.67404 0.60979 0.06907  0.02581  0.10330  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.56110 0.64721 0.63253 0.07085  0.01172  0.09661  145 ALA A N   
997  C CA  . ALA A 138 ? 0.52688 0.58533 0.61549 0.06281  0.01025  0.09486  145 ALA A CA  
998  C C   . ALA A 138 ? 0.57793 0.63131 0.66555 0.07264  0.00532  0.08872  145 ALA A C   
999  O O   . ALA A 138 ? 0.56374 0.63511 0.64371 0.07743  0.00058  0.07574  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.46083 0.51005 0.55583 0.04881  0.00775  0.07770  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.58063 0.60943 0.67788 0.07572  0.00623  0.09857  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.54583 0.56681 0.64436 0.08718  0.00277  0.09220  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.57782 0.58047 0.68144 0.08037  0.00052  0.07214  146 GLU A C   
1004 O O   . GLU A 139 ? 0.56575 0.57077 0.66937 0.09068  -0.00094 0.06297  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.57180 0.57049 0.67519 0.09771  0.00497  0.11236  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.65828 0.61494 0.77417 0.08667  0.00574  0.11516  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.85319 0.78655 0.97523 0.09271  0.00903  0.14121  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.88509 0.83928 0.99946 0.10568  0.01225  0.15972  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.87787 0.77068 1.01152 0.08437  0.00761  0.14341  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.55655 0.54453 0.66408 0.06476  0.00036  0.06588  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.56056 0.53292 0.66784 0.05891  -0.00235 0.04655  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.54031 0.51610 0.64852 0.04254  -0.00356 0.04100  147 LYS A C   
1013 O O   . LYS A 140 ? 0.56292 0.53598 0.67913 0.03386  -0.00277 0.05329  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.57180 0.50457 0.68335 0.06177  -0.00446 0.04539  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.59349 0.50468 0.70238 0.05172  -0.00898 0.02723  147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.60618 0.48159 0.71068 0.06229  -0.01141 0.01743  147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.70023 0.53467 0.81117 0.04936  -0.01891 0.01666  147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.84591 0.63952 0.94714 0.06038  -0.02303 0.00133  147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.51406 0.49823 0.61557 0.03912  -0.00479 0.02475  148 VAL A N   
1020 C CA  . VAL A 141 ? 0.49656 0.48470 0.59741 0.02641  -0.00646 0.01920  148 VAL A CA  
1021 C C   . VAL A 141 ? 0.55478 0.52362 0.65123 0.02238  -0.01051 0.00406  148 VAL A C   
1022 O O   . VAL A 141 ? 0.53757 0.50662 0.62566 0.03003  -0.00900 -0.00661 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.50403 0.51846 0.59740 0.02641  -0.00461 0.01517  148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.48657 0.50317 0.57942 0.01624  -0.00588 0.01208  148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.46416 0.49710 0.55592 0.03340  -0.00233 0.02655  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.50251 0.45774 0.60469 0.01103  -0.01579 0.00360  149 THR A N   
1027 C CA  . THR A 142 ? 0.55513 0.49394 0.64958 0.00660  -0.02219 -0.01185 149 THR A CA  
1028 C C   . THR A 142 ? 0.53043 0.48567 0.62402 -0.00254 -0.02453 -0.01362 149 THR A C   
1029 O O   . THR A 142 ? 0.56229 0.52898 0.66897 -0.01008 -0.02497 -0.00242 149 THR A O   
1030 C CB  . THR A 142 ? 0.63651 0.54307 0.73870 0.00038  -0.03048 -0.01324 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.61480 0.50328 0.71877 0.01065  -0.02756 -0.00826 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.61444 0.50226 0.70193 -0.00078 -0.03882 -0.03320 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.48979 0.44775 0.56808 -0.00015 -0.02493 -0.02588 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.53949 0.51162 0.61406 -0.00570 -0.02667 -0.02682 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.57084 0.52962 0.63383 -0.00842 -0.03540 -0.03937 150 VAL A C   
1036 O O   . VAL A 143 ? 0.57401 0.52461 0.61936 -0.00075 -0.03372 -0.05022 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.54071 0.52990 0.60610 -0.00043 -0.01883 -0.02680 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.49159 0.48912 0.55148 -0.00442 -0.02075 -0.02705 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.50145 0.50375 0.57516 0.00249  -0.01336 -0.01721 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.55665 0.51642 0.62937 -0.01833 -0.04481 -0.03758 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.50890 0.46145 0.56981 -0.02147 -0.05610 -0.04931 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.54066 0.51474 0.59638 -0.02078 -0.05478 -0.04496 151 ILE A C   
1043 O O   . ILE A 144 ? 0.49071 0.48221 0.56322 -0.02471 -0.05343 -0.03327 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.57792 0.51901 0.65642 -0.03434 -0.07053 -0.05042 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.57274 0.49009 0.66194 -0.03584 -0.06992 -0.04885 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.57294 0.50228 0.63400 -0.03607 -0.08534 -0.06727 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.70355 0.59558 0.76925 -0.02319 -0.06774 -0.06377 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.57824 0.55102 0.60979 -0.01397 -0.05405 -0.05307 152 THR A N   
1049 C CA  . THR A 145 ? 0.59301 0.58139 0.61707 -0.01158 -0.05190 -0.04737 152 THR A CA  
1050 C C   . THR A 145 ? 0.58809 0.57314 0.59013 -0.00886 -0.06149 -0.05643 152 THR A C   
1051 O O   . THR A 145 ? 0.60328 0.57356 0.58751 -0.00506 -0.06522 -0.06924 152 THR A O   
1052 C CB  . THR A 145 ? 0.53736 0.53087 0.55369 -0.00523 -0.03748 -0.04228 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.54948 0.55259 0.56154 -0.00378 -0.03589 -0.03493 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.58836 0.57438 0.58431 0.00193  -0.03175 -0.05031 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.54834 0.54727 0.54950 -0.00858 -0.06567 -0.04985 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.55953 0.55965 0.53819 -0.00445 -0.07587 -0.05581 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.58495 0.59707 0.55564 0.00210  -0.06983 -0.04353 153 LYS A C   
1058 O O   . LYS A 146 ? 0.53552 0.55980 0.52524 0.00059  -0.06981 -0.03315 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.59289 0.59732 0.58435 -0.01309 -0.09598 -0.06157 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.58479 0.59480 0.55260 -0.00814 -0.10986 -0.06768 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.56468 0.55726 0.49401 0.00143  -0.10849 -0.08187 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.63065 0.62856 0.53258 0.00701  -0.12529 -0.08998 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.61205 0.62541 0.49735 0.01772  -0.11773 -0.07508 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.56307 0.57107 0.50531 0.01059  -0.06380 -0.04371 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.55742 0.57104 0.48871 0.01714  -0.05792 -0.03064 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.59589 0.61466 0.50190 0.02430  -0.06980 -0.03252 154 HIS A C   
1067 O O   . HIS A 147 ? 0.61101 0.62533 0.49743 0.02648  -0.07762 -0.04589 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.58407 0.59098 0.50508 0.02003  -0.03989 -0.02448 154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.57588 0.58208 0.49217 0.02363  -0.03255 -0.00891 154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.57510 0.58234 0.46655 0.03190  -0.03355 -0.00111 154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.55313 0.55428 0.48454 0.02074  -0.02468 0.00012  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.57154 0.57242 0.46523 0.03336  -0.02596 0.01371  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.59725 0.59291 0.51476 0.02640  -0.02112 0.01319  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.58326 0.61044 0.48770 0.02978  -0.07195 -0.01965 155 ASN A N   
1075 C CA  . ASN A 148 ? 0.58467 0.62032 0.46489 0.03831  -0.08483 -0.01915 155 ASN A CA  
1076 C C   . ASN A 148 ? 0.60190 0.63022 0.44305 0.04710  -0.07789 -0.02139 155 ASN A C   
1077 O O   . ASN A 148 ? 0.63605 0.66958 0.45031 0.05421  -0.09079 -0.02848 155 ASN A O   
1078 C CB  . ASN A 148 ? 0.59501 0.63903 0.47939 0.04597  -0.08509 -0.00159 155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.58469 0.64655 0.50146 0.04235  -0.09766 -0.00057 155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.62010 0.69117 0.55341 0.03295  -0.11061 -0.01225 155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.58970 0.65633 0.51676 0.05024  -0.09343 0.01426  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.61241 0.63150 0.44999 0.04715  -0.05798 -0.01535 156 ASP A N   
1083 C CA  . ASP A 149 ? 0.67957 0.69707 0.48344 0.05649  -0.04658 -0.01227 156 ASP A CA  
1084 C C   . ASP A 149 ? 0.65238 0.66548 0.44778 0.05708  -0.04202 -0.02896 156 ASP A C   
1085 O O   . ASP A 149 ? 0.73984 0.75519 0.50914 0.06636  -0.02932 -0.02637 156 ASP A O   
1086 C CB  . ASP A 149 ? 0.65177 0.66533 0.45979 0.05590  -0.02663 0.00869  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.74799 0.75994 0.55640 0.05974  -0.02980 0.02623  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.71542 0.73516 0.51864 0.06522  -0.04679 0.02342  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.80830 0.81073 0.62368 0.05734  -0.01615 0.04281  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.62627 0.63345 0.44294 0.04888  -0.05091 -0.04441 157 ASP A N   
1091 C CA  . ASP A 150 ? 0.65588 0.65468 0.46643 0.05125  -0.04642 -0.05986 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.66959 0.65778 0.48939 0.04503  -0.06653 -0.07920 157 ASP A C   
1093 O O   . ASP A 150 ? 0.61767 0.61018 0.45154 0.03751  -0.08307 -0.07919 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.65129 0.65041 0.48710 0.04588  -0.02847 -0.05251 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.65826 0.65770 0.47832 0.05571  -0.01493 -0.05903 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.73334 0.72534 0.52632 0.06593  -0.02184 -0.07548 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.63857 0.64652 0.47369 0.05388  0.00197  -0.04841 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.67694 0.65139 0.49069 0.04834  -0.06489 -0.09477 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.67985 0.63718 0.50397 0.04109  -0.08285 -0.11283 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.67512 0.62950 0.54151 0.02822  -0.07887 -0.10608 158 GLU A C   
1101 O O   . GLU A 151 ? 0.64586 0.61084 0.52951 0.02658  -0.06311 -0.09090 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.76507 0.70296 0.55836 0.05377  -0.08362 -0.13392 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.83788 0.77766 0.58296 0.06883  -0.08959 -0.14389 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.06816 0.98997 0.77874 0.08640  -0.08502 -0.16414 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.03861 0.93957 0.76414 0.08463  -0.08511 -0.17516 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.21405 1.14239 0.88094 0.10394  -0.08068 -0.16835 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.61677 0.55582 0.49910 0.01871  -0.09421 -0.11734 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.60248 0.53832 0.52229 0.00758  -0.09076 -0.10972 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.64931 0.57059 0.56625 0.01582  -0.07724 -0.11411 159 GLN A C   
1110 O O   . GLN A 152 ? 0.67114 0.57209 0.56517 0.02524  -0.08054 -0.13099 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.64063 0.56629 0.58177 -0.00714 -0.11142 -0.11651 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.67304 0.60081 0.65413 -0.01913 -0.10720 -0.10345 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.70076 0.63025 0.70987 -0.03642 -0.12607 -0.10283 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.70791 0.65924 0.72365 -0.04126 -0.13605 -0.09836 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.74412 0.65173 0.77209 -0.04586 -0.13110 -0.10570 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.59520 0.52731 0.53414 0.01398  -0.06282 -0.09971 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.64144 0.56737 0.58132 0.02285  -0.04964 -0.10072 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.62700 0.54905 0.59830 0.01454  -0.04917 -0.09225 160 TYR A C   
1119 O O   . TYR A 153 ? 0.61555 0.54648 0.60830 0.00272  -0.05395 -0.08204 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.65485 0.60244 0.58829 0.03067  -0.03160 -0.09059 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.68531 0.63617 0.58508 0.04339  -0.02667 -0.09723 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.63807 0.57959 0.51832 0.05872  -0.02092 -0.10948 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.71069 0.67434 0.59643 0.04241  -0.02679 -0.09011 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.77948 0.72716 0.62594 0.07285  -0.01438 -0.11457 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.72788 0.69639 0.58027 0.05528  -0.02095 -0.09343 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.77516 0.73710 0.60740 0.07051  -0.01424 -0.10572 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.87873 0.84859 0.67490 0.08572  -0.00645 -0.10809 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.64927 0.55983 0.62205 0.02310  -0.04242 -0.09540 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.63095 0.53644 0.62916 0.01874  -0.04093 -0.08623 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.62282 0.54537 0.62572 0.02867  -0.02566 -0.07830 161 ALA A C   
1131 O O   . ALA A 154 ? 0.59580 0.51486 0.58623 0.04288  -0.01879 -0.08553 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.57450 0.44504 0.57286 0.01962  -0.05074 -0.09675 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.57384 0.51652 0.59459 0.02211  -0.02102 -0.06413 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.53655 0.49758 0.56595 0.02850  -0.01038 -0.05639 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.57673 0.53031 0.62234 0.02955  -0.01173 -0.04888 162 TRP A C   
1136 O O   . TRP A 155 ? 0.57832 0.52464 0.63473 0.02026  -0.01777 -0.04241 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.52388 0.50851 0.55857 0.02132  -0.00633 -0.04769 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.50799 0.51343 0.55203 0.02501  0.00160  -0.04169 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.52067 0.54323 0.56226 0.02788  0.00945  -0.04174 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.50843 0.52273 0.56686 0.02525  0.00135  -0.03389 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.47232 0.51419 0.52896 0.02821  0.01229  -0.03578 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.50638 0.54309 0.57091 0.02776  0.00683  -0.03180 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.51239 0.51988 0.57917 0.02368  -0.00289 -0.02722 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.47288 0.52468 0.54918 0.02939  0.00572  -0.02585 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.49698 0.51898 0.57236 0.02718  -0.00164 -0.01965 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.52290 0.56649 0.60179 0.03031  0.00143  -0.02029 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.49721 0.45517 0.54554 0.04178  -0.00550 -0.04776 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.54453 0.49396 0.60542 0.04590  -0.00654 -0.03901 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.57079 0.54325 0.63810 0.05807  0.00074  -0.03370 163 GLU A C   
1150 O O   . GLU A 156 ? 0.51726 0.50130 0.57947 0.06788  0.00679  -0.04008 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.53448 0.44657 0.59082 0.05106  -0.01205 -0.04610 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.62829 0.52560 0.69865 0.05264  -0.01376 -0.03328 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.75932 0.61265 0.82840 0.05063  -0.02221 -0.03926 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.76523 0.60750 0.84477 0.03399  -0.02965 -0.03396 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.78049 0.61030 0.83920 0.06586  -0.02169 -0.04942 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.54250 0.52479 0.62137 0.05806  0.00005  -0.02109 164 SER A N   
1157 C CA  . SER A 157 ? 0.54554 0.55177 0.63220 0.06975  0.00375  -0.01525 164 SER A CA  
1158 C C   . SER A 157 ? 0.50978 0.51409 0.60354 0.07278  0.00103  -0.00095 164 SER A C   
1159 O O   . SER A 157 ? 0.51363 0.51835 0.60815 0.06242  -0.00137 0.00626  164 SER A O   
1160 C CB  . SER A 157 ? 0.50713 0.54746 0.59751 0.06342  0.00567  -0.01601 164 SER A CB  
1161 O OG  . SER A 157 ? 0.53086 0.59777 0.63206 0.07172  0.00560  -0.00956 164 SER A OG  
1162 N N   . SER A 158 ? 0.49673 0.50042 0.59485 0.08900  0.00236  0.00444  165 SER A N   
1163 C CA  . SER A 158 ? 0.52131 0.53110 0.62458 0.09578  0.00059  0.02056  165 SER A CA  
1164 C C   . SER A 158 ? 0.54504 0.59672 0.65355 0.10184  -0.00055 0.02352  165 SER A C   
1165 O O   . SER A 158 ? 0.55253 0.61483 0.66442 0.11484  -0.00235 0.03507  165 SER A O   
1166 C CB  . SER A 158 ? 0.53120 0.51174 0.63586 0.11123  0.00127  0.02683  165 SER A CB  
1167 O OG  . SER A 158 ? 0.66637 0.60585 0.76877 0.10196  -0.00078 0.02642  165 SER A OG  
1168 N N   . ALA A 159 ? 0.52750 0.60243 0.63723 0.09207  -0.00069 0.01382  166 ALA A N   
1169 C CA  . ALA A 159 ? 0.50411 0.61897 0.62303 0.09424  -0.00355 0.01316  166 ALA A CA  
1170 C C   . ALA A 159 ? 0.54433 0.67234 0.67427 0.11251  -0.00034 0.01435  166 ALA A C   
1171 O O   . ALA A 159 ? 0.57262 0.68052 0.70005 0.12024  0.00600  0.00908  166 ALA A O   
1172 C CB  . ALA A 159 ? 0.50936 0.63979 0.62467 0.09345  -0.01065 0.02143  166 ALA A CB  
1173 N N   . GLY A 160 ? 0.48818 0.65101 0.62957 0.12126  -0.00525 0.02046  167 GLY A N   
1174 C CA  . GLY A 160 ? 0.50978 0.69184 0.66499 0.14064  -0.00187 0.02285  167 GLY A CA  
1175 C C   . GLY A 160 ? 0.52277 0.73094 0.69155 0.13773  0.00462  0.01440  167 GLY A C   
1176 O O   . GLY A 160 ? 0.51442 0.73855 0.69448 0.15610  0.01061  0.01584  167 GLY A O   
1177 N N   . GLY A 161 ? 0.49455 0.70758 0.66255 0.11664  0.00483  0.00715  168 GLY A N   
1178 C CA  . GLY A 161 ? 0.49723 0.73984 0.68049 0.11103  0.01140  0.00319  168 GLY A CA  
1179 C C   . GLY A 161 ? 0.47065 0.69020 0.64101 0.11015  0.02306  -0.00417 168 GLY A C   
1180 O O   . GLY A 161 ? 0.45867 0.70351 0.63991 0.10582  0.03084  -0.00498 168 GLY A O   
1181 N N   . SER A 162 ? 0.43890 0.61311 0.58687 0.11353  0.02400  -0.00883 169 SER A N   
1182 C CA  . SER A 162 ? 0.49903 0.65052 0.63077 0.11488  0.03251  -0.01781 169 SER A CA  
1183 C C   . SER A 162 ? 0.50318 0.61270 0.61497 0.10245  0.02689  -0.02271 169 SER A C   
1184 O O   . SER A 162 ? 0.49851 0.59092 0.60863 0.09903  0.01925  -0.01812 169 SER A O   
1185 C CB  . SER A 162 ? 0.46990 0.61094 0.59622 0.14063  0.04015  -0.02161 169 SER A CB  
1186 O OG  . SER A 162 ? 0.56309 0.66847 0.68151 0.15030  0.03394  -0.02035 169 SER A OG  
1187 N N   . PHE A 163 ? 0.46265 0.55941 0.56004 0.09640  0.03115  -0.03059 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.48829 0.54861 0.56810 0.08650  0.02547  -0.03632 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.55904 0.60045 0.61875 0.09494  0.03030  -0.04797 170 PHE A C   
1190 O O   . PHE A 163 ? 0.51988 0.58091 0.57770 0.10598  0.04040  -0.05021 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.49534 0.56227 0.57585 0.06617  0.02154  -0.03345 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.45706 0.54415 0.53685 0.05982  0.02841  -0.03405 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.47944 0.60159 0.57799 0.05667  0.03216  -0.02765 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.45993 0.53173 0.52136 0.05611  0.03029  -0.03960 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.45441 0.59397 0.55539 0.04865  0.03932  -0.02501 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.45682 0.54623 0.51658 0.05082  0.03785  -0.03665 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.52158 0.64386 0.60213 0.04636  0.04317  -0.02843 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.51884 0.52411 0.56354 0.08997  0.02271  -0.05526 171 THR A N   
1199 C CA  . THR A 164 ? 0.59050 0.57248 0.61143 0.09782  0.02318  -0.06943 171 THR A CA  
1200 C C   . THR A 164 ? 0.57670 0.55104 0.58526 0.08183  0.01718  -0.07295 171 THR A C   
1201 O O   . THR A 164 ? 0.55167 0.52396 0.56989 0.06598  0.00987  -0.06639 171 THR A O   
1202 C CB  . THR A 164 ? 0.56825 0.50883 0.58148 0.10778  0.01613  -0.07803 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.60608 0.52628 0.62853 0.09130  0.00479  -0.07260 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.56877 0.51482 0.59280 0.12743  0.02225  -0.07349 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.59297 0.56530 0.57876 0.08848  0.02088  -0.08267 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.60050 0.56502 0.56999 0.07752  0.01426  -0.08694 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.67316 0.60919 0.61320 0.08912  0.00871  -0.10537 172 VAL A C   
1208 O O   . VAL A 165 ? 0.70063 0.63789 0.62501 0.10857  0.01786  -0.11318 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.62476 0.61994 0.59207 0.07320  0.02428  -0.07781 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.60303 0.58884 0.54896 0.06666  0.01748  -0.08194 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.55933 0.57603 0.55372 0.05987  0.02609  -0.06304 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.64640 0.55827 0.57906 0.07801  -0.00681 -0.11295 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.72485 0.60616 0.62851 0.08638  -0.01687 -0.13337 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.74238 0.61816 0.63906 0.07075  -0.03236 -0.13678 173 ARG A C   
1215 O O   . ARG A 166 ? 0.66750 0.55690 0.58635 0.05397  -0.03599 -0.12334 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.78777 0.63123 0.69621 0.09128  -0.02517 -0.14340 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.82376 0.64729 0.75392 0.06982  -0.04164 -0.13964 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.86773 0.65082 0.80512 0.07333  -0.04875 -0.14592 173 ARG A CD  
1219 N NE  . ARG A 166 ? 1.10587 0.88327 1.07525 0.05299  -0.05671 -0.13124 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 1.04611 0.81452 1.02502 0.03282  -0.07231 -0.13226 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.93556 0.69745 0.89357 0.02954  -0.08461 -0.14885 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.98166 0.75103 0.99222 0.01626  -0.07563 -0.11520 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.79769 0.65475 0.66200 0.07836  -0.04195 -0.15558 174 THR A N   
1224 C CA  . THR A 167 ? 0.85142 0.70199 0.70932 0.06451  -0.06085 -0.16142 174 THR A CA  
1225 C C   . THR A 167 ? 0.85238 0.67560 0.73472 0.04813  -0.07859 -0.16524 174 THR A C   
1226 O O   . THR A 167 ? 0.89333 0.68285 0.77274 0.05366  -0.08371 -0.17794 174 THR A O   
1227 C CB  . THR A 167 ? 0.88890 0.72800 0.70155 0.07866  -0.06793 -0.18204 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.94587 0.81480 0.73783 0.09262  -0.04937 -0.17347 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.92294 0.75709 0.73060 0.06410  -0.09122 -0.18914 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.77433 0.61206 0.68219 0.02859  -0.08703 -0.15275 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.86475 0.68416 0.80203 0.01063  -0.10170 -0.15107 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.94601 0.74121 0.86962 0.00323  -0.12620 -0.17153 175 ASP A C   
1233 O O   . ASP A 168 ? 0.92410 0.73546 0.83277 0.00126  -0.13572 -0.17605 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.82618 0.67576 0.79744 -0.00522 -0.09932 -0.12860 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.87547 0.71263 0.88111 -0.02365 -0.11070 -0.12192 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.94759 0.75496 0.95939 -0.02277 -0.11119 -0.12522 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.88646 0.74441 0.91412 -0.03830 -0.11845 -0.11178 175 ASP A OD2 
1238 N N   . THR A 169 ? 1.04857 0.80365 0.97725 -0.00090 -0.13772 -0.18382 176 THR A N   
1239 C CA  . THR A 169 ? 1.14966 0.87527 1.06775 -0.01048 -0.16437 -0.20600 176 THR A CA  
1240 C C   . THR A 169 ? 1.10895 0.83815 1.07077 -0.03949 -0.18145 -0.19521 176 THR A C   
1241 O O   . THR A 169 ? 1.09414 0.80678 1.05432 -0.05241 -0.20676 -0.21167 176 THR A O   
1242 C CB  . THR A 169 ? 1.19360 0.86594 1.09028 0.00165  -0.16944 -0.22850 176 THR A CB  
1243 O OG1 . THR A 169 ? 1.29307 0.94148 1.22604 -0.01041 -0.16898 -0.21648 176 THR A OG1 
1244 C CG2 . THR A 169 ? 1.13689 0.81229 0.99928 0.03221  -0.14726 -0.23355 176 THR A CG2 
1245 N N   . GLY A 170 ? 1.08882 0.84164 1.08948 -0.04966 -0.16861 -0.16807 177 GLY A N   
1246 C CA  . GLY A 170 ? 1.07452 0.83369 1.12041 -0.07569 -0.18050 -0.15385 177 GLY A CA  
1247 C C   . GLY A 170 ? 1.05063 0.84833 1.11041 -0.08885 -0.19323 -0.14893 177 GLY A C   
1248 O O   . GLY A 170 ? 0.99791 0.80310 1.02748 -0.08126 -0.20320 -0.16463 177 GLY A O   
1249 N N   . GLU A 171 ? 0.99804 0.82264 1.10304 -0.10663 -0.19222 -0.12575 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.98025 0.84500 1.10600 -0.11902 -0.20464 -0.11862 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.89930 0.79772 0.99945 -0.10071 -0.19269 -0.11507 178 GLU A C   
1252 O O   . GLU A 171 ? 0.82382 0.73461 0.91982 -0.08804 -0.16925 -0.10120 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.94629 0.83827 1.12617 -0.13736 -0.19972 -0.09076 178 GLU A CB  
1254 C CG  . GLU A 171 ? 1.06935 0.94531 1.28684 -0.16496 -0.22192 -0.09171 178 GLU A CG  
1255 C CD  . GLU A 171 ? 1.15957 1.04974 1.38091 -0.17769 -0.25096 -0.10693 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 1.09253 1.02221 1.30390 -0.16796 -0.25053 -0.10469 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 1.14059 1.00117 1.37476 -0.19732 -0.27549 -0.12126 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.92621 0.83825 1.00770 -0.09861 -0.20884 -0.12705 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.86292 0.80639 0.92370 -0.08235 -0.19767 -0.11942 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.80765 0.79053 0.90497 -0.08625 -0.18523 -0.09261 179 PRO A C   
1261 O O   . PRO A 172 ? 0.86560 0.86691 1.00473 -0.10321 -0.19392 -0.08151 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.73316 0.68448 0.77359 -0.08258 -0.22234 -0.13537 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.88713 0.80756 0.93266 -0.09831 -0.24738 -0.15593 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.92123 0.81443 0.99438 -0.10944 -0.23904 -0.15025 179 PRO A CD  
1265 N N   . MET A 173 ? 0.72553 0.72126 0.80705 -0.07005 -0.16445 -0.08220 180 MET A N   
1266 C CA  . MET A 173 ? 0.70900 0.73578 0.81752 -0.06911 -0.15024 -0.05951 180 MET A CA  
1267 C C   . MET A 173 ? 0.66530 0.72339 0.77018 -0.06098 -0.15346 -0.05218 180 MET A C   
1268 O O   . MET A 173 ? 0.79323 0.87970 0.92425 -0.06032 -0.14607 -0.03473 180 MET A O   
1269 C CB  . MET A 173 ? 0.73255 0.74987 0.82949 -0.05752 -0.12591 -0.05256 180 MET A CB  
1270 C CG  . MET A 173 ? 0.74325 0.74880 0.86279 -0.06512 -0.11774 -0.04550 180 MET A CG  
1271 S SD  . MET A 173 ? 0.87333 0.88247 0.98507 -0.05148 -0.09209 -0.03387 180 MET A SD  
1272 C CE  . MET A 173 ? 0.60653 0.60677 0.67613 -0.03654 -0.08763 -0.04606 180 MET A CE  
1273 N N   . GLY A 174 ? 0.65168 0.70541 0.72324 -0.05256 -0.16360 -0.06422 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.59360 0.67371 0.65752 -0.04182 -0.16571 -0.05547 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.62930 0.70494 0.67102 -0.02547 -0.14330 -0.04610 181 GLY A C   
1276 O O   . GLY A 174 ? 0.65779 0.72489 0.66356 -0.01377 -0.14151 -0.05035 181 GLY A O   
1277 N N   . ARG A 175 ? 0.56219 0.64316 0.62463 -0.02493 -0.12645 -0.03305 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.51298 0.58619 0.55863 -0.01262 -0.10673 -0.02558 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.48884 0.56567 0.55890 -0.01513 -0.09277 -0.01621 182 ARG A C   
1280 O O   . ARG A 175 ? 0.54930 0.64719 0.65008 -0.02042 -0.09580 -0.00770 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.49818 0.58537 0.53328 0.00011  -0.10677 -0.01563 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.49736 0.56852 0.51042 0.01085  -0.08922 -0.00987 182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.51932 0.60091 0.53129 0.02344  -0.08701 0.00350  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.49439 0.59522 0.53707 0.02483  -0.08489 0.01195  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.50758 0.63736 0.57126 0.02697  -0.09625 0.01810  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.47691 0.61908 0.53418 0.02697  -0.11335 0.01566  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.44571 0.59553 0.53735 0.03018  -0.09050 0.02715  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.57160 0.53918 0.44019 0.00778  -0.10074 0.00807  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.54499 0.50850 0.44122 0.00200  -0.09584 0.00925  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.60593 0.55172 0.50883 -0.00803 -0.08502 0.00543  183 GLY A C   
1291 O O   . GLY A 176 ? 0.62064 0.55372 0.50808 -0.00882 -0.07826 0.00384  183 GLY A O   
1292 N N   . THR A 177 ? 0.54604 0.49306 0.47111 -0.01364 -0.08315 0.00429  184 THR A N   
1293 C CA  . THR A 177 ? 0.55225 0.48606 0.48609 -0.01990 -0.07459 0.00253  184 THR A CA  
1294 C C   . THR A 177 ? 0.60593 0.54801 0.55567 -0.02780 -0.07709 -0.00190 184 THR A C   
1295 O O   . THR A 177 ? 0.55489 0.51214 0.51547 -0.02716 -0.08152 -0.00048 184 THR A O   
1296 C CB  . THR A 177 ? 0.55506 0.47963 0.49790 -0.01585 -0.06764 0.00924  184 THR A CB  
1297 O OG1 . THR A 177 ? 0.55942 0.47269 0.48918 -0.01054 -0.06148 0.01564  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.57100 0.48973 0.52564 -0.02020 -0.06165 0.00699  184 THR A CG2 
1299 N N   . LYS A 178 ? 0.58706 0.51794 0.53773 -0.03417 -0.07251 -0.00628 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.59156 0.52336 0.55559 -0.04155 -0.07142 -0.00704 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.60588 0.52436 0.57486 -0.03824 -0.06388 -0.00214 185 LYS A C   
1302 O O   . LYS A 178 ? 0.57766 0.48111 0.54142 -0.03672 -0.05844 -0.00470 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.63319 0.56077 0.59569 -0.05202 -0.07311 -0.01698 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.72474 0.64047 0.69957 -0.06013 -0.06691 -0.01571 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.70129 0.61589 0.68184 -0.07452 -0.06938 -0.02726 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.69386 0.60675 0.65797 -0.07511 -0.07556 -0.04187 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.86971 0.78690 0.84207 -0.09082 -0.08113 -0.05754 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.55959 0.48641 0.53792 -0.03538 -0.06389 0.00422  186 VAL A N   
1309 C CA  . VAL A 179 ? 0.56666 0.48807 0.54973 -0.02976 -0.05989 0.00913  186 VAL A CA  
1310 C C   . VAL A 179 ? 0.59686 0.51277 0.58309 -0.03270 -0.05632 0.01469  186 VAL A C   
1311 O O   . VAL A 179 ? 0.51744 0.44505 0.50667 -0.03514 -0.05697 0.01894  186 VAL A O   
1312 C CB  . VAL A 179 ? 0.55512 0.49020 0.54314 -0.02319 -0.06334 0.01088  186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.47861 0.41479 0.47227 -0.01668 -0.06226 0.01406  186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.52193 0.45620 0.50865 -0.02174 -0.06421 0.00737  186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.56572 0.46257 0.55140 -0.03157 -0.05069 0.01572  187 ILE A N   
1316 C CA  . ILE A 180 ? 0.56950 0.45267 0.55747 -0.03343 -0.04475 0.02354  187 ILE A CA  
1317 C C   . ILE A 180 ? 0.60843 0.49273 0.59684 -0.01972 -0.04350 0.03395  187 ILE A C   
1318 O O   . ILE A 180 ? 0.61213 0.49097 0.60255 -0.01119 -0.04259 0.03221  187 ILE A O   
1319 C CB  . ILE A 180 ? 0.61072 0.46713 0.59777 -0.04019 -0.03904 0.01667  187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.63276 0.49440 0.61761 -0.05242 -0.04379 0.00312  187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.61678 0.45299 0.60828 -0.04375 -0.03076 0.02635  187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.65832 0.49645 0.63773 -0.05731 -0.04052 -0.00996 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.55676 0.45162 0.54313 -0.01640 -0.04344 0.04463  188 LEU A N   
1324 C CA  . LEU A 181 ? 0.56453 0.46632 0.54758 -0.00138 -0.04487 0.05486  188 LEU A CA  
1325 C C   . LEU A 181 ? 0.63496 0.51346 0.61402 0.00241  -0.03552 0.07000  188 LEU A C   
1326 O O   . LEU A 181 ? 0.57939 0.45405 0.55475 -0.00380 -0.02902 0.07977  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.54245 0.47156 0.52012 0.00282  -0.05084 0.05652  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.54748 0.49380 0.52943 -0.00179 -0.05805 0.04263  188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.55377 0.52277 0.52895 0.00349  -0.06211 0.04294  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.57476 0.52344 0.56498 0.00223  -0.06299 0.03378  188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.60918 0.47159 0.59046 0.01319  -0.03322 0.07293  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.64349 0.48024 0.62020 0.02193  -0.02413 0.09005  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.67074 0.52896 0.63701 0.03989  -0.02919 0.10541  189 HIS A C   
1334 O O   . HIS A 182 ? 0.63815 0.51125 0.60682 0.05660  -0.03683 0.10550  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.71119 0.52278 0.69455 0.02975  -0.01961 0.08617  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.68530 0.47951 0.67400 0.01408  -0.01608 0.06791  189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.71845 0.47655 0.70800 0.00286  -0.00608 0.06591  189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.64668 0.45507 0.63836 0.00794  -0.02127 0.05059  189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.65020 0.40428 0.64140 -0.00863 -0.00733 0.04593  189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.66762 0.45162 0.65830 -0.00472 -0.01583 0.03826  189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.64115 0.50473 0.59603 0.03682  -0.02499 0.11768  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.65937 0.54951 0.59838 0.05335  -0.03105 0.12934  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.76024 0.63836 0.69008 0.07591  -0.02926 0.14909  190 LEU A C   
1344 O O   . LEU A 183 ? 0.79351 0.63402 0.72646 0.07705  -0.01769 0.16011  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.64848 0.54552 0.57533 0.04554  -0.02298 0.13948  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.63285 0.54900 0.56791 0.02821  -0.02572 0.12199  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.65679 0.58404 0.58128 0.02405  -0.01563 0.13391  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.55338 0.49934 0.49042 0.03401  -0.04182 0.10330  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.74574 0.65642 0.66423 0.09509  -0.04159 0.15257  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.74888 0.65589 0.65430 0.12086  -0.04212 0.17431  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.84660 0.73152 0.72851 0.12396  -0.02646 0.20256  191 LYS A C   
1352 O O   . LYS A 184 ? 0.81983 0.70128 0.69761 0.10598  -0.01660 0.20314  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.70238 0.65733 0.60179 0.13981  -0.06222 0.16763  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.69615 0.67410 0.62332 0.13562  -0.07557 0.14140  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.71018 0.73872 0.63551 0.14841  -0.09613 0.13001  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.69375 0.74391 0.64939 0.13512  -0.10589 0.10154  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.73079 0.82984 0.68969 0.14385  -0.12634 0.08639  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.83738 0.70835 0.70487 0.14820  -0.02315 0.22773  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.86052 0.70220 0.70586 0.15205  -0.00426 0.25950  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.87642 0.75165 0.69430 0.15423  -0.00498 0.26700  192 GLU A C   
1361 O O   . GLU A 185 ? 0.87815 0.73656 0.68690 0.14157  0.01388  0.28235  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.92453 0.74394 0.75778 0.18233  -0.00143 0.28702  192 GLU A CB  
1363 C CG  . GLU A 185 ? 1.06647 0.85602 0.87164 0.19130  0.01870  0.32551  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.33268 1.06997 1.13844 0.20949  0.03139  0.35115  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.43700 1.12263 1.24213 0.19740  0.05598  0.37142  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.30203 1.04984 1.11144 0.23588  0.01740  0.35058  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.82680 0.75084 0.63278 0.16946  -0.02580 0.25468  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.86918 0.82736 0.64394 0.17659  -0.02802 0.25961  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.83335 0.81707 0.61877 0.15442  -0.03259 0.23041  193 ASP A C   
1370 O O   . ASP A 186 ? 0.84143 0.85932 0.60322 0.16158  -0.03814 0.22597  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.83981 0.83810 0.59169 0.20821  -0.04943 0.26163  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.95120 0.98200 0.73021 0.20728  -0.07406 0.22781  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.83827 0.85208 0.65176 0.18691  -0.07227 0.20944  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 1.00433 1.07898 0.77021 0.22662  -0.09488 0.21939  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.75814 0.72583 0.57630 0.12979  -0.03029 0.21051  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.75553 0.74412 0.58556 0.11104  -0.03464 0.18440  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.73846 0.70506 0.58135 0.08688  -0.01552 0.18780  194 GLN A C   
1378 O O   . GLN A 187 ? 0.76934 0.74430 0.63106 0.06967  -0.01875 0.16602  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.74498 0.74253 0.60200 0.10439  -0.05121 0.15591  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.70659 0.73301 0.56021 0.12462  -0.07129 0.14793  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.70242 0.76783 0.52955 0.13778  -0.08214 0.14266  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.74842 0.82596 0.57071 0.12755  -0.08031 0.12971  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.75270 0.83950 0.56180 0.16233  -0.09414 0.15158  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.78927 0.72883 0.62394 0.08540  0.00445  0.21513  195 THR A N   
1385 C CA  . THR A 188 ? 0.79043 0.71141 0.64340 0.06016  0.02281  0.21767  195 THR A CA  
1386 C C   . THR A 188 ? 0.77270 0.72574 0.61901 0.05348  0.02928  0.21416  195 THR A C   
1387 O O   . THR A 188 ? 0.78620 0.73397 0.65280 0.03193  0.04280  0.21309  195 THR A O   
1388 C CB  . THR A 188 ? 0.81901 0.69788 0.66915 0.05870  0.04425  0.24813  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.86512 0.75364 0.68219 0.07558  0.05547  0.27623  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.80387 0.65025 0.65837 0.07055  0.03862  0.25232  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.77103 0.75917 0.59108 0.07163  0.01979  0.21042  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.74333 0.76298 0.55674 0.06778  0.02604  0.20352  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.72418 0.75442 0.56828 0.04963  0.01856  0.17466  196 GLU A C   
1394 O O   . GLU A 189 ? 0.71207 0.76107 0.56311 0.04082  0.02859  0.17082  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.76413 0.81822 0.54162 0.09219  0.01439  0.19916  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.70565 0.77877 0.49074 0.09661  -0.01143 0.16647  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.75165 0.85647 0.50230 0.12066  -0.02570 0.16036  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.85087 0.95443 0.58333 0.13830  -0.03311 0.17438  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.78390 0.91573 0.52585 0.12301  -0.03030 0.14018  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.69984 0.71978 0.56218 0.04542  0.00221  0.15580  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.67658 0.70344 0.56443 0.03098  -0.00544 0.13121  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.66982 0.67658 0.58523 0.00873  0.00493  0.13309  197 TYR A C   
1403 O O   . TYR A 190 ? 0.59978 0.61033 0.53544 -0.00227 -0.00245 0.11453  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.61625 0.64176 0.50978 0.03632  -0.02535 0.11192  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.65884 0.70822 0.53047 0.05550  -0.03803 0.10491  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.62765 0.70356 0.49046 0.06000  -0.04167 0.09006  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.68170 0.72889 0.54213 0.07011  -0.04684 0.11172  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.64987 0.74801 0.49241 0.07635  -0.05450 0.07944  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.63985 0.71427 0.48183 0.08701  -0.06101 0.10245  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.65578 0.75490 0.48829 0.08899  -0.06507 0.08513  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.67265 0.79904 0.48671 0.10457  -0.08041 0.07167  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.69224 0.67721 0.60842 0.00221  0.02155  0.15481  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.72243 0.69308 0.66625 -0.02143 0.03347  0.15566  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.70965 0.70261 0.65937 -0.03016 0.05135  0.16602  198 LEU A C   
1415 O O   . LEU A 191 ? 0.73121 0.72027 0.70899 -0.05189 0.06155  0.16530  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.71183 0.63867 0.65911 -0.02662 0.04254  0.17077  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.76485 0.66864 0.71082 -0.01855 0.02826  0.16097  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.79488 0.65276 0.74434 -0.02180 0.04023  0.17644  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.69683 0.60839 0.66217 -0.03015 0.01459  0.13346  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.70693 0.72581 0.63188 -0.01390 0.05555  0.17412  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.72003 0.76454 0.64818 -0.01927 0.07510  0.18485  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.71101 0.79179 0.65865 -0.02361 0.06791  0.16115  199 GLU A C   
1423 O O   . GLU A 192 ? 0.67834 0.76891 0.61972 -0.01268 0.04876  0.14055  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.80558 0.86300 0.69299 0.00306  0.08388  0.20392  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.81667 0.83993 0.68257 0.01075  0.09376  0.23320  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.94208 0.95091 0.81918 -0.00514 0.12388  0.26078  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 1.02578 1.06478 0.91239 -0.01326 0.13974  0.26270  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 1.07044 1.03715 0.94913 -0.00967 0.13300  0.28042  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.73475 0.83558 0.70836 -0.03937 0.08438  0.16493  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.68775 0.82474 0.68521 -0.04270 0.07834  0.14396  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.66884 0.83595 0.64087 -0.01960 0.07602  0.13647  200 GLU A C   
1432 O O   . GLU A 193 ? 0.60665 0.78404 0.58008 -0.01056 0.05874  0.11432  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.68256 0.83993 0.71782 -0.06472 0.09745  0.15049  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.73944 0.94171 0.80143 -0.06490 0.09323  0.13173  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.84436 1.07570 0.94756 -0.08626 0.11340  0.13867  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.84099 1.11037 0.97584 -0.08951 0.10802  0.12261  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.82177 1.03855 0.92755 -0.09954 0.13516  0.16089  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.68380 0.86353 0.63090 -0.00933 0.09435  0.15465  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.67605 0.88588 0.59650 0.01303  0.09374  0.14511  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.68776 0.88408 0.57763 0.03160  0.07028  0.12997  201 ARG A C   
1441 O O   . ARG A 194 ? 0.65306 0.86843 0.53220 0.04624  0.06108  0.10942  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.69507 0.92086 0.58993 0.02081  0.11981  0.16970  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.89966 1.09360 0.76459 0.02462  0.12563  0.19664  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.93968 1.14849 0.77872 0.03177  0.15491  0.22544  201 ARG A CD  
1445 N NE  . ARG A 194 ? 1.20276 1.38148 1.00497 0.04256  0.15819  0.25237  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 1.14264 1.32576 0.91135 0.05318  0.18219  0.28308  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 1.16679 1.38437 0.93424 0.05309  0.20722  0.29068  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 1.16824 1.32163 0.90325 0.06592  0.18203  0.30804  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.70737 0.87144 0.58586 0.03112  0.06086  0.13858  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.67320 0.82880 0.52994 0.04638  0.03824  0.12339  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.63248 0.78293 0.51442 0.04022  0.01953  0.09703  202 ARG A C   
1452 O O   . ARG A 195 ? 0.60288 0.76134 0.47453 0.05217  0.00533  0.07643  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.70083 0.82730 0.54331 0.04888  0.03435  0.14086  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.71781 0.84177 0.54225 0.06418  0.01121  0.12609  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.69678 0.84833 0.48273 0.08625  0.00830  0.12202  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.75267 0.90467 0.52365 0.09964  -0.01415 0.10963  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.72038 0.88899 0.48749 0.10694  -0.03124 0.08061  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.65045 0.83301 0.42386 0.10513  -0.02837 0.06140  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.70044 0.87181 0.45997 0.11627  -0.05140 0.06986  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.61342 0.74954 0.52748 0.02163  0.01967  0.09716  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.64065 0.77170 0.57528 0.01705  0.00366  0.07582  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.62492 0.78352 0.56728 0.02395  0.00398  0.06019  203 ILE A C   
1463 O O   . ILE A 196 ? 0.62992 0.78608 0.57215 0.03169  -0.00966 0.04139  203 ILE A O   
1464 C CB  . ILE A 196 ? 0.63163 0.74496 0.59445 -0.00291 0.00395  0.07921  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.60175 0.68240 0.55648 -0.00629 0.00161  0.09011  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.61783 0.73146 0.59878 -0.00573 -0.01025 0.05989  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.58618 0.64801 0.56362 -0.02629 0.00870  0.09724  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.58952 0.77406 0.54049 0.02175  0.02106  0.06816  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.57366 0.78706 0.53406 0.03112  0.02309  0.05367  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.61737 0.83616 0.54721 0.05238  0.01767  0.03953  204 LYS A C   
1471 O O   . LYS A 197 ? 0.59165 0.81456 0.52678 0.06200  0.00927  0.01964  204 LYS A O   
1472 C CB  . LYS A 197 ? 0.55286 0.79831 0.52944 0.02540  0.04514  0.06602  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.66759 0.91691 0.68400 0.00310  0.04885  0.07219  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.70407 0.99672 0.74658 -0.00010 0.06755  0.07593  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.78768 1.08263 0.85480 -0.02448 0.08448  0.09479  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.88284 1.18731 0.99420 -0.04348 0.07576  0.08574  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.59072 0.80878 0.48767 0.06072  0.02207  0.04901  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.59368 0.82014 0.45923 0.08055  0.01526  0.03255  205 GLU A CA  
1479 C C   . GLU A 198 ? 0.61611 0.81968 0.48295 0.08219  -0.00774 0.01184  205 GLU A C   
1480 O O   . GLU A 198 ? 0.58255 0.78975 0.44312 0.09354  -0.01550 -0.01152 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.62957 0.86284 0.45710 0.09004  0.02323  0.04930  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.67655 0.91632 0.46816 0.10929  0.00990  0.03070  205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.73441 0.97779 0.48779 0.11926  0.01228  0.05002  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.78765 1.01036 0.54621 0.11092  0.00966  0.06927  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.79483 1.06157 0.51121 0.13731  0.01692  0.04611  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.55985 0.73879 0.43677 0.07049  -0.01725 0.01944  206 ILE A N   
1487 C CA  . ILE A 199 ? 0.64637 0.80557 0.52779 0.07020  -0.03636 0.00206  206 ILE A CA  
1488 C C   . ILE A 199 ? 0.59090 0.74141 0.49822 0.06598  -0.04089 -0.01256 206 ILE A C   
1489 O O   . ILE A 199 ? 0.56744 0.70882 0.47536 0.07138  -0.05150 -0.03277 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.61912 0.75738 0.50454 0.06072  -0.04253 0.01542  206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.60792 0.75357 0.46489 0.06983  -0.03954 0.03085  206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.60348 0.72459 0.49959 0.05830  -0.05940 -0.00147 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.59884 0.72398 0.46132 0.06183  -0.03812 0.05121  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.55614 0.70928 0.48575 0.05649  -0.03311 -0.00253 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.59894 0.74666 0.55073 0.05570  -0.03789 -0.01321 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.62367 0.78607 0.57179 0.07184  -0.03494 -0.02952 207 VAL A C   
1497 O O   . VAL A 200 ? 0.61119 0.75816 0.56499 0.07793  -0.04306 -0.04509 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.57308 0.72859 0.54888 0.04328  -0.03192 -0.00030 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.55033 0.70929 0.54593 0.04787  -0.03659 -0.00975 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.50221 0.63556 0.48188 0.02818  -0.03662 0.01020  207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.59750 0.78798 0.53571 0.07965  -0.02148 -0.02583 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.58899 0.79526 0.52198 0.09732  -0.01651 -0.04273 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.64857 0.84040 0.55766 0.10808  -0.02665 -0.06440 208 LYS A C   
1504 O O   . LYS A 201 ? 0.67309 0.85911 0.58427 0.12014  -0.02897 -0.08497 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.60803 0.85054 0.53399 0.10290  0.00291  -0.03244 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.64214 0.90445 0.55698 0.12391  0.01083  -0.05064 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.68442 0.98723 0.60328 0.12740  0.03350  -0.03747 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.77251 1.09691 0.67694 0.15081  0.04346  -0.05665 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.89414 1.26254 0.80816 0.15422  0.06827  -0.04328 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.64128 0.82713 0.52957 0.10421  -0.03341 -0.06129 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.66131 0.84086 0.52834 0.11320  -0.04493 -0.08421 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.65056 0.79840 0.53599 0.10578  -0.06001 -0.09948 209 LYS A C   
1513 O O   . LYS A 202 ? 0.62560 0.76349 0.50825 0.11303  -0.06643 -0.12515 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.64540 0.83599 0.48455 0.11401  -0.04819 -0.07439 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.67478 0.86770 0.49108 0.12346  -0.06275 -0.09967 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.77295 0.98392 0.55810 0.12902  -0.06569 -0.08645 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.81366 1.03399 0.57669 0.13873  -0.08357 -0.11419 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.88892 1.13515 0.61248 0.15147  -0.08500 -0.10123 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.62395 0.75443 0.52838 0.09106  -0.06430 -0.08471 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.67895 0.78117 0.59884 0.08259  -0.07629 -0.09523 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.68380 0.76494 0.62802 0.07782  -0.07425 -0.09066 210 HIS A C   
1522 O O   . HIS A 203 ? 0.71529 0.77124 0.67069 0.07572  -0.08000 -0.10318 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.60802 0.70668 0.52760 0.07163  -0.08357 -0.08356 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.64272 0.76111 0.53806 0.07852  -0.08935 -0.08792 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.70136 0.82421 0.58760 0.08465  -0.10028 -0.11395 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.69648 0.83132 0.57370 0.08133  -0.08618 -0.06940 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.69495 0.84072 0.55660 0.09225  -0.10540 -0.11160 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.71362 0.86535 0.56846 0.09136  -0.09615 -0.08278 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.69513 0.76372 0.49417 0.02530  -0.08756 0.06628  211 SER A N   
1530 C CA  . SER A 204 ? 0.64060 0.71184 0.46502 0.02708  -0.07140 0.06536  211 SER A CA  
1531 C C   . SER A 204 ? 0.68650 0.74443 0.49151 0.03152  -0.05297 0.06422  211 SER A C   
1532 O O   . SER A 204 ? 0.62293 0.68715 0.44363 0.03655  -0.04140 0.06912  211 SER A O   
1533 C CB  . SER A 204 ? 0.67589 0.76293 0.53032 0.03257  -0.07043 0.07458  211 SER A CB  
1534 O OG  . SER A 204 ? 0.60546 0.70763 0.48332 0.03141  -0.08550 0.07590  211 SER A OG  
1535 N N   . GLN A 205 ? 0.74190 0.78321 0.51337 0.03034  -0.05053 0.05650  212 GLN A N   
1536 C CA  . GLN A 205 ? 0.76171 0.79352 0.51719 0.03697  -0.03124 0.05569  212 GLN A CA  
1537 C C   . GLN A 205 ? 0.75549 0.78378 0.53104 0.04059  -0.01919 0.05201  212 GLN A C   
1538 O O   . GLN A 205 ? 0.73097 0.76395 0.51277 0.04867  -0.00491 0.05663  212 GLN A O   
1539 C CB  . GLN A 205 ? 0.80818 0.82142 0.51973 0.03637  -0.02954 0.04569  212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.84932 0.85766 0.54339 0.04502  -0.00730 0.04697  212 GLN A CG  
1541 C CD  . GLN A 205 ? 1.02179 1.00912 0.66833 0.04579  -0.00243 0.03316  212 GLN A CD  
1542 O OE1 . GLN A 205 ? 1.01041 0.98729 0.63271 0.03839  -0.01958 0.02291  212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 1.05206 1.03494 0.68571 0.05499  0.02083  0.03137  212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.71890 0.74030 0.50694 0.03467  -0.02492 0.04551  213 PHE A N   
1545 C CA  . PHE A 206 ? 0.68367 0.69414 0.48425 0.03842  -0.01315 0.04406  213 PHE A CA  
1546 C C   . PHE A 206 ? 0.68208 0.70797 0.51381 0.03777  -0.01372 0.05345  213 PHE A C   
1547 O O   . PHE A 206 ? 0.67711 0.69217 0.51878 0.03800  -0.00698 0.05460  213 PHE A O   
1548 C CB  . PHE A 206 ? 0.71215 0.69476 0.49981 0.03130  -0.01470 0.02953  213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.77306 0.73708 0.52283 0.03346  -0.01175 0.01673  213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.76894 0.73075 0.50570 0.04682  0.00556  0.01872  213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.77947 0.73115 0.50649 0.02224  -0.02626 0.00211  213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.81992 0.76545 0.51884 0.04999  0.01230  0.00654  213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.86477 0.79842 0.54866 0.02490  -0.02282 -0.01129 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.85927 0.78884 0.52761 0.03931  -0.00156 -0.00895 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.64431 0.69266 0.48941 0.03767  -0.02019 0.06045  214 ILE A N   
1556 C CA  . ILE A 207 ? 0.57110 0.63462 0.43973 0.03912  -0.01794 0.06744  214 ILE A CA  
1557 C C   . ILE A 207 ? 0.62887 0.69437 0.49764 0.04946  -0.00676 0.07339  214 ILE A C   
1558 O O   . ILE A 207 ? 0.65700 0.72787 0.52009 0.05559  -0.00375 0.07461  214 ILE A O   
1559 C CB  . ILE A 207 ? 0.59600 0.67916 0.47709 0.03875  -0.02625 0.07043  214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.53634 0.62155 0.42128 0.03102  -0.03999 0.06675  214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.55401 0.65207 0.45381 0.04169  -0.02150 0.07453  214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.51703 0.60680 0.42319 0.02290  -0.04174 0.06432  214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.60887 0.67194 0.48561 0.05133  -0.00074 0.07866  215 GLY A N   
1564 C CA  . GLY A 208 ? 0.59623 0.66106 0.47162 0.06289  0.00707  0.08623  215 GLY A CA  
1565 C C   . GLY A 208 ? 0.59974 0.68978 0.48127 0.06820  0.00433  0.09075  215 GLY A C   
1566 O O   . GLY A 208 ? 0.55077 0.64672 0.43169 0.07594  0.00748  0.09870  215 GLY A O   
1567 N N   . TYR A 209 ? 0.54608 0.64905 0.43171 0.06427  -0.00238 0.08569  216 TYR A N   
1568 C CA  . TYR A 209 ? 0.53193 0.65483 0.42356 0.06712  -0.00614 0.08542  216 TYR A CA  
1569 C C   . TYR A 209 ? 0.52377 0.65112 0.41964 0.06371  -0.01043 0.08128  216 TYR A C   
1570 O O   . TYR A 209 ? 0.55276 0.66968 0.44466 0.05863  -0.01210 0.07978  216 TYR A O   
1571 C CB  . TYR A 209 ? 0.57771 0.70798 0.47379 0.06448  -0.00728 0.08363  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.55034 0.67695 0.44230 0.06617  0.00030  0.09073  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.51961 0.65376 0.40139 0.07435  0.00322  0.09751  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.55466 0.67093 0.45336 0.05877  0.00397  0.09190  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.51045 0.63838 0.38532 0.07606  0.01222  0.10806  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.54762 0.65869 0.44565 0.05800  0.01355  0.10063  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.56785 0.68300 0.45219 0.06712  0.01897  0.11007  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.61128 0.71853 0.49182 0.06656  0.03046  0.12264  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.50638 0.64893 0.40994 0.06554  -0.01282 0.08021  217 PRO A N   
1580 C CA  . PRO A 210 ? 0.55066 0.69527 0.46181 0.06001  -0.01443 0.07852  217 PRO A CA  
1581 C C   . PRO A 210 ? 0.54764 0.68447 0.46138 0.05439  -0.01972 0.07533  217 PRO A C   
1582 O O   . PRO A 210 ? 0.52131 0.66223 0.43975 0.05515  -0.02326 0.07005  217 PRO A O   
1583 C CB  . PRO A 210 ? 0.53168 0.69691 0.45664 0.06101  -0.01766 0.07639  217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.57878 0.75304 0.49777 0.06806  -0.02083 0.07609  217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.55791 0.71670 0.46341 0.07197  -0.01492 0.08140  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.49833 0.62364 0.40733 0.05049  -0.01960 0.07908  218 ILE A N   
1587 C CA  . ILE A 211 ? 0.50668 0.62323 0.41982 0.04756  -0.02565 0.07970  218 ILE A CA  
1588 C C   . ILE A 211 ? 0.54881 0.66220 0.46928 0.04243  -0.02402 0.08341  218 ILE A C   
1589 O O   . ILE A 211 ? 0.55725 0.66665 0.46868 0.03986  -0.01818 0.09084  218 ILE A O   
1590 C CB  . ILE A 211 ? 0.53124 0.63708 0.43153 0.04722  -0.02972 0.08382  218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.50041 0.60911 0.39902 0.04863  -0.03007 0.07980  218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.50211 0.60172 0.41048 0.04756  -0.03807 0.08699  218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.50259 0.60229 0.38808 0.04560  -0.03561 0.08049  218 ILE A CD1 
1594 N N   . THR A 212 ? 0.53759 0.65128 0.47406 0.04026  -0.02754 0.07768  219 THR A N   
1595 C CA  . THR A 212 ? 0.55184 0.66064 0.50165 0.03236  -0.02582 0.07992  219 THR A CA  
1596 C C   . THR A 212 ? 0.53152 0.61824 0.48521 0.03181  -0.02957 0.08474  219 THR A C   
1597 O O   . THR A 212 ? 0.55493 0.63651 0.51473 0.03732  -0.03494 0.07733  219 THR A O   
1598 C CB  . THR A 212 ? 0.54312 0.66551 0.50977 0.02860  -0.02884 0.06735  219 THR A CB  
1599 O OG1 . THR A 212 ? 0.48493 0.62889 0.44730 0.03299  -0.02794 0.06516  219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.49956 0.61995 0.48609 0.01659  -0.02642 0.06946  219 THR A CG2 
1601 N N   . LEU A 213 ? 0.62042 0.69410 0.57071 0.02658  -0.02526 0.09847  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.61638 0.66544 0.57029 0.02705  -0.02867 0.10779  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.59982 0.63755 0.57866 0.01751  -0.02636 0.10288  220 LEU A C   
1604 O O   . LEU A 213 ? 0.60993 0.65305 0.59790 0.00607  -0.01857 0.10661  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.63695 0.67487 0.56823 0.02647  -0.02500 0.12803  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.75327 0.76316 0.68397 0.02616  -0.02624 0.14583  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.72520 0.72096 0.67291 0.03567  -0.03747 0.14132  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.78025 0.78437 0.67553 0.02928  -0.02579 0.16498  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.57309 0.59567 0.56565 0.02182  -0.03238 0.09312  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.60499 0.60853 0.62091 0.01233  -0.03151 0.08538  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.70708 0.67735 0.72583 0.01047  -0.02834 0.10653  221 PHE A C   
1612 O O   . PHE A 214 ? 0.80415 0.75486 0.82126 0.02289  -0.03345 0.11288  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.61390 0.61222 0.63948 0.01959  -0.03734 0.06276  221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.57407 0.60040 0.59674 0.01758  -0.03986 0.04205  221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.64580 0.70191 0.65608 0.01683  -0.03862 0.04657  221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.62748 0.64829 0.65701 0.01795  -0.04357 0.01808  221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.58660 0.66728 0.59260 0.01714  -0.04223 0.03136  221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.68867 0.73569 0.70893 0.01718  -0.04748 0.00092  221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.63613 0.71358 0.64517 0.01713  -0.04744 0.00948  221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.65559 0.62089 0.68007 -0.00411 -0.01924 0.11948  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.75769 0.68953 0.78109 -0.00711 -0.01359 0.14430  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.72176 0.61889 0.77523 -0.01411 -0.01440 0.13629  222 VAL A C   
1623 O O   . VAL A 215 ? 0.70784 0.61109 0.78407 -0.02502 -0.01610 0.11263  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.75075 0.69197 0.76606 -0.02005 0.00094  0.16393  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.75810 0.73446 0.74757 -0.01351 0.00253  0.16218  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.70460 0.65136 0.75511 -0.04110 0.00899  0.15541  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.75173 0.61031 0.80426 -0.00703 -0.01451 0.15559  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.82695 0.64442 0.90690 -0.00841 -0.01595 0.14681  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.82082 0.61542 0.92543 -0.03335 -0.00486 0.15306  223 GLU A C   
1630 O O   . GLU A 216 ? 0.82027 0.63013 0.92059 -0.04758 0.00604  0.17055  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.87953 0.66348 0.95299 0.01202  -0.02106 0.16699  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.81746 0.62507 0.87921 0.03540  -0.03277 0.15788  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.85449 0.62967 0.92862 0.05680  -0.03938 0.16639  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.87709 0.62553 0.97723 0.05997  -0.03782 0.14663  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.87568 0.65284 0.93364 0.07151  -0.04694 0.19177  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.90578 0.66285 1.03869 -0.03893 -0.00646 0.13722  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.94847 0.67836 1.11325 -0.06544 0.00244  0.13824  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.93263 0.63461 1.09261 -0.07217 0.01660  0.18129  224 LYS A C   
1639 O O   . LYS A 217 ? 1.03230 0.68413 1.19311 -0.06280 0.01800  0.20061  224 LYS A O   
1640 C CB  . LYS A 217 ? 1.07063 0.75438 1.26184 -0.06614 -0.00281 0.11274  224 LYS A CB  
1641 C CG  . LYS A 217 ? 1.13676 0.79229 1.36663 -0.09742 0.00344  0.10494  224 LYS A CG  
1642 C CD  . LYS A 217 ? 1.13920 0.74752 1.39109 -0.09731 -0.00311 0.07207  224 LYS A CD  
1643 C CE  . LYS A 217 ? 1.12291 0.66135 1.38208 -0.08484 0.00347  0.09517  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 1.24680 0.78587 1.47743 -0.04850 -0.00021 0.11397  224 LYS A NZ  
# 
