data_7HB7
# 
_entry.id   7HB7 
# 
_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   7HB7         pdb_00007hb7 10.2210/pdb7hb7/pdb 
WWPDB D_1001407254 ?            ?                   
# 
_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                        7HB7 
_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           Y 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, L.' 1  ? 
'Wang, W.'  2  ? 
'Zhu, Z.'   3  ? 
'Li, Q.'    4  ? 
'Li, M.'    5  ? 
'Zhou, H.'  6  ? 
'Xu, Q.'    7  ? 
'Wen, W.'   8  ? 
'Wang, Q.'  9  ? 
'Yu, F.'    10 ? 
# 
_citation.id                        primary 
_citation.title                     
;Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.
;
_citation.journal_abbrev            Iucrj 
_citation.journal_volume            12 
_citation.page_first                177 
_citation.page_last                 187 
_citation.year                      2025 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   39819741 
_citation.pdbx_database_id_DOI      10.1107/S2052252524012247 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Huang, L.' 0009-0001-8431-0182 1  
primary 'Wang, W.'  ?                   2  
primary 'Zhu, Z.'   ?                   3  
primary 'Li, Q.'    ?                   4  
primary 'Li, M.'    ?                   5  
primary 'Zhou, H.'  ?                   6  
primary 'Xu, Q.'    0000-0002-7137-0768 7  
primary 'Wen, W.'   ?                   8  
primary 'Wang, Q.'  ?                   9  
primary 'Yu, F.'    0000-0002-9502-3277 10 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Heat shock protein HSP 90-alpha'                   26859.117 1 3.6.4.10 ? ? ? 
2 non-polymer syn 2,2-dimethyl-2,3-dihydro-1-benzofuran-7-carboxamide 191.226   1 ?        ? ? ? 
# 
_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         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        2,2-dimethyl-2,3-dihydro-1-benzofuran-7-carboxamide 
_pdbx_entity_nonpoly.comp_id     WP1 
# 
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 
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 
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 
WP1 non-polymer         . 2,2-dimethyl-2,3-dihydro-1-benzofuran-7-carboxamide ? 'C11 H13 N O2'   191.226 
# 
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        WP1 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WP1 
_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        ? 
# 
_pdbx_nonpoly_scheme.asym_id         B 
_pdbx_nonpoly_scheme.entity_id       2 
_pdbx_nonpoly_scheme.mon_id          WP1 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     301 
_pdbx_nonpoly_scheme.auth_seq_num    301 
_pdbx_nonpoly_scheme.pdb_mon_id      WP1 
_pdbx_nonpoly_scheme.auth_mon_id     AWI 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
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             599927.826 
_cell.length_a           70.280 
_cell.length_b           88.230 
_cell.length_c           96.750 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HB7 
_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                         7HB7 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HB7 
# 
_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   2024-01-21 
_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                     7HB7 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             30.290 
_reflns.d_resolution_high            2.980 
_reflns.number_obs                   6399 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.900 
_reflns.pdbx_Rmerge_I_obs            0.197 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        10.100 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.300 
_reflns.pdbx_Rrim_I_all              0.206 
_reflns.pdbx_Rpim_I_all              0.059 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     78659 
_reflns.pdbx_scaling_rejects         7 
_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 2.980  3.060  ? 5854 452 ? 1.195 ? ? ? 13.000 ? 2.500  ? ? ? ? ? ? 100.000 1.244 0.343 0.787 
1 2 13.330 30.290 ? 534  82  ? 0.096 ? ? ? 6.500  ? 15.100 ? ? ? ? ? ? 90.300  0.103 0.036 0.989 
# 
_refine.entry_id                                 7HB7 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.ls_percent_reflns_R_free                 4.69 
_refine.pdbx_overall_phase_error                 29.5200 
_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                          0.2296 
_refine.B_iso_mean                               65.76 
_refine.ls_number_reflns_R_free                  300 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_R_factor_R_work                       0.2273 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            2.98 
_refine.ls_number_reflns_obs                     6396 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.ls_number_reflns_R_work                  6096 
_refine.ls_d_res_low                             30.29 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2795 
_refine.overall_SU_ML                            0.3568 
_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         14 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               1658 
_refine_hist.d_res_high                       2.98 
_refine_hist.d_res_low                        30.29 
# 
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           1685 0.0015 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2274 0.3895 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     260  0.0384 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0021 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 227  6.4497 ? ? ? 
# 
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' 2.98 3.75  2990 0.2702 99.97 0.3115 148 . . . . . 
'X-RAY DIFFRACTION' 3.75 30.29 3106 0.2094 99.88 0.2652 152 . . . . . 
# 
_struct.entry_id                  7HB7 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr12696' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HB7 
_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 ? 
# 
_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              7HB7 
_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 7HB7 MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HB7 LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HB7 GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HB7 HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HB7 HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HB7 HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HB7 HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HB7 HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HB7 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 
# 
_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  ? LEU A 57  ? GLU A 42  LEU A 64  1 ? 23 
HELX_P HELX_P3 AA3 THR A 58  ? GLY A 66  ? THR A 65  GLY A 73  5 ? 9  
HELX_P HELX_P4 AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5 AA5 ASN A 99  ? ALA A 117 ? ASN A 106 ALA A 124 1 ? 19 
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 GLN A 187 ? LEU A 191 ? GLN A 194 LEU A 198 5 ? 5  
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 GLN A 152 ? SER A 157 ? GLN A 159 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 ILE A 71  ? N ILE A 78  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HB7 
_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_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 66  ? ? -158.05 85.50   
2 1 THR A 94  ? ? -103.15 41.84   
3 1 ILE A 104 ? ? -80.03  -70.66  
4 1 ASN A 105 ? ? -105.53 -139.92 
5 1 ASN A 106 ? ? 53.73   -76.73  
6 1 SER A 165 ? ? -97.75  36.61   
7 1 ALA A 166 ? ? 58.86   -136.25 
8 1 ARG A 182 ? ? -170.36 140.29  
# 
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 13.8242366461  27.3885497225 31.0493971739 0.5420541931   0.664362744299 0.697040381911 
0.1056658598      -0.139509188247  0.0262958563152   3.39478704059 3.56337588919 4.82402057608 -0.559212597423 -3.62724233914   
0.396520084115  -0.2220760284     -0.216119655128  -0.374506552806  0.358163996788  0.00955431658466 -0.330042275029  
0.00333710729114 0.544602686784   0.267742509308  
2  ? 'X-RAY DIFFRACTION' refined -4.13211621732 37.0317996004 27.3399913318 0.508431092884 0.390391008985 0.54344302176  
-0.118910929929   -0.0336926841822 -0.064143951071   4.73249257375 6.58514446711 7.26500352111 -2.37052518453  3.35956044016    
-5.00319990457  -0.531622626236   0.31755176013    0.662475169458   0.797627303075  0.218211956021   0.252289492419   
-1.7052762358    0.212204362692   0.329273172508  
3  ? 'X-RAY DIFFRACTION' refined -12.2627353249 37.5074766502 12.2874488979 0.572504166106 0.734237881762 0.767562214901 
-0.0657959077731  -0.072321350955  0.0782734858207   4.62738900572 8.4765109586  9.1770209174  -2.2256574527   2.43044421655    
0.0599129450084 -0.00617041841734 1.63485521349    -0.604521279927  -2.04624734149  -0.275222671932  0.949473722095   
0.443065066821   -0.703812288567  -0.264633553716 
4  ? 'X-RAY DIFFRACTION' refined -2.22694911648 25.9924465574 24.4911212195 0.421109001556 0.31198561247  0.448232000148 
0.067906422343    -0.122553277496  -0.0423180460659  3.65827649427 3.15201377901 6.38609071514 -2.47172997742  -1.36960129381   
-1.69288463976  0.223442680826    -0.420231989805  -0.0956736617262 0.0473212152662 -0.260086746967  -0.237085378275  
0.178170318883   0.140553414327   -0.068745430383 
5  ? 'X-RAY DIFFRACTION' refined 14.8126929272  39.3041518735 31.9787100439 0.442377979804 0.423652653411 0.838516331068 
0.0105890087976   -0.111617416926  0.0118408309637   8.88206685717 7.81035641388 8.4159140574  -0.621486228864 0.905986423266   
-4.1935086322   -0.293143125104   0.403700147872   1.02152183006    0.733870133942  0.00670617593925 -1.52687655795   
-0.362968531169  2.43507375344    0.359789248337  
6  ? 'X-RAY DIFFRACTION' refined 8.20824122867  39.0924798926 38.6819241396 0.847482326418 0.864434728801 0.630124804161 
-0.0231636012639  0.0488018276228  -0.154140510924   8.21143950485 9.53524591397 6.62664121896 0.267841715972  -2.98363447467   
-2.78432035647  0.381365762596    -1.86195501109   1.78290876867    0.745218039625  -0.13373900029   1.11194038822    
-0.525312623963  0.737782974444   0.0433060805272 
7  ? 'X-RAY DIFFRACTION' refined 4.4880697849   25.3926269456 28.4520073761 0.441950054527 0.487260093521 0.539575620333 
-0.0739591559571  -0.042395980385  -0.00968847145252 4.99868391509 2.35348252864 4.97794745816 -1.59646232133  0.749127549793   
-1.61905350186  0.398150976871    -0.131094621434  -0.61787743013   0.0952141394502 -0.114923270052  0.157871250487   
0.593837694607   0.957149945125   -0.103039629264 
8  ? 'X-RAY DIFFRACTION' refined 2.16737601535  24.0934216096 18.6287123368 0.568634775781 0.394565047431 0.541501751622 
-0.00626994435598 -0.0218629901953 -0.103169032756   4.70065297308 3.44459650393 3.61624634614 -1.89520493524  0.743384432908   
-3.46789997983  -0.0536234110041  0.244595372757   -0.232586713293  -0.245399921078 0.100324440765   0.0641577234086  
0.118773699753   -0.0532272003362 -0.243313042044 
9  ? 'X-RAY DIFFRACTION' refined -5.77896323015 24.0371997102 41.2975369383 0.560282642473 0.677885411539 0.440583776774 
-0.00247658529039 0.0123209342889  0.120552080384    8.04514081926 7.47119533815 8.92463870172 -1.77387785516  -0.0748247495017 
0.724293864721  0.050310033926    -1.65487489581   -0.556131665142  1.04153210117   -0.229378302846  -0.0445794328026 
0.121444122442   -0.160705029124  0.0838858525301 
10 ? 'X-RAY DIFFRACTION' refined -13.0645822933 29.9485072725 32.3658328796 0.527472084831 0.447186285178 0.483304199294 
-0.00855617341807 -0.0594784373824 0.0376813059901   7.77327563079 7.04568070356 7.80102071433 0.630449915428  -0.814431920741  
-5.81569263363  -0.257056172321   -0.0674932685531 -0.14484603561   1.54689085362   -0.0298589915032 -1.97025139913   
-1.2529078525    -0.570552974867  0.214686247327  
# 
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 64  A 49  . 
;chain 'A' and (resid 41 through 64 )
;
3  3  'X-RAY DIFFRACTION' A 65  A 50  A 76  A 61  . 
;chain 'A' and (resid 65 through 76 )
;
4  4  'X-RAY DIFFRACTION' A 77  A 62  A 106 A 91  . 
;chain 'A' and (resid 77 through 106 )
;
5  5  'X-RAY DIFFRACTION' A 107 A 92  A 123 A 108 . 
;chain 'A' and (resid 107 through 123 )
;
6  6  'X-RAY DIFFRACTION' A 124 A 109 A 136 A 121 . 
;chain 'A' and (resid 124 through 136 )
;
7  7  'X-RAY DIFFRACTION' A 137 A 122 A 153 A 138 . 
;chain 'A' and (resid 137 through 153 )
;
8  8  'X-RAY DIFFRACTION' A 154 A 139 A 190 A 175 . 
;chain 'A' and (resid 154 through 190 )
;
9  9  'X-RAY DIFFRACTION' A 191 A 176 A 210 A 195 . 
;chain 'A' and (resid 191 through 210 )
;
10 10 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
ILE N    N N N 144 
ILE CA   C N S 145 
ILE C    C N N 146 
ILE O    O N N 147 
ILE CB   C N S 148 
ILE CG1  C N N 149 
ILE CG2  C N N 150 
ILE CD1  C N N 151 
ILE OXT  O N N 152 
ILE H    H N N 153 
ILE H2   H N N 154 
ILE HA   H N N 155 
ILE HB   H N N 156 
ILE HG12 H N N 157 
ILE HG13 H N N 158 
ILE HG21 H N N 159 
ILE HG22 H N N 160 
ILE HG23 H N N 161 
ILE HD11 H N N 162 
ILE HD12 H N N 163 
ILE HD13 H N N 164 
ILE HXT  H N N 165 
LEU N    N N N 166 
LEU CA   C N S 167 
LEU C    C N N 168 
LEU O    O N N 169 
LEU CB   C N N 170 
LEU CG   C N N 171 
LEU CD1  C N N 172 
LEU CD2  C N N 173 
LEU OXT  O N N 174 
LEU H    H N N 175 
LEU H2   H N N 176 
LEU HA   H N N 177 
LEU HB2  H N N 178 
LEU HB3  H N N 179 
LEU HG   H N N 180 
LEU HD11 H N N 181 
LEU HD12 H N N 182 
LEU HD13 H N N 183 
LEU HD21 H N N 184 
LEU HD22 H N N 185 
LEU HD23 H N N 186 
LEU HXT  H N N 187 
LYS N    N N N 188 
LYS CA   C N S 189 
LYS C    C N N 190 
LYS O    O N N 191 
LYS CB   C N N 192 
LYS CG   C N N 193 
LYS CD   C N N 194 
LYS CE   C N N 195 
LYS NZ   N N N 196 
LYS OXT  O N N 197 
LYS H    H N N 198 
LYS H2   H N N 199 
LYS HA   H N N 200 
LYS HB2  H N N 201 
LYS HB3  H N N 202 
LYS HG2  H N N 203 
LYS HG3  H N N 204 
LYS HD2  H N N 205 
LYS HD3  H N N 206 
LYS HE2  H N N 207 
LYS HE3  H N N 208 
LYS HZ1  H N N 209 
LYS HZ2  H N N 210 
LYS HZ3  H N N 211 
LYS HXT  H N N 212 
MET N    N N N 213 
MET CA   C N S 214 
MET C    C N N 215 
MET O    O N N 216 
MET CB   C N N 217 
MET CG   C N N 218 
MET SD   S N N 219 
MET CE   C N N 220 
MET OXT  O N N 221 
MET H    H N N 222 
MET H2   H N N 223 
MET HA   H N N 224 
MET HB2  H N N 225 
MET HB3  H N N 226 
MET HG2  H N N 227 
MET HG3  H N N 228 
MET HE1  H N N 229 
MET HE2  H N N 230 
MET HE3  H N N 231 
MET HXT  H N N 232 
PHE N    N N N 233 
PHE CA   C N S 234 
PHE C    C N N 235 
PHE O    O N N 236 
PHE CB   C N N 237 
PHE CG   C Y N 238 
PHE CD1  C Y N 239 
PHE CD2  C Y N 240 
PHE CE1  C Y N 241 
PHE CE2  C Y N 242 
PHE CZ   C Y N 243 
PHE OXT  O N N 244 
PHE H    H N N 245 
PHE H2   H N N 246 
PHE HA   H N N 247 
PHE HB2  H N N 248 
PHE HB3  H N N 249 
PHE HD1  H N N 250 
PHE HD2  H N N 251 
PHE HE1  H N N 252 
PHE HE2  H N N 253 
PHE HZ   H N N 254 
PHE HXT  H N N 255 
PRO N    N N N 256 
PRO CA   C N S 257 
PRO C    C N N 258 
PRO O    O N N 259 
PRO CB   C N N 260 
PRO CG   C N N 261 
PRO CD   C N N 262 
PRO OXT  O N N 263 
PRO H    H N N 264 
PRO HA   H N N 265 
PRO HB2  H N N 266 
PRO HB3  H N N 267 
PRO HG2  H N N 268 
PRO HG3  H N N 269 
PRO HD2  H N N 270 
PRO HD3  H N N 271 
PRO HXT  H N N 272 
SER N    N N N 273 
SER CA   C N S 274 
SER C    C N N 275 
SER O    O N N 276 
SER CB   C N N 277 
SER OG   O N N 278 
SER OXT  O N N 279 
SER H    H N N 280 
SER H2   H N N 281 
SER HA   H N N 282 
SER HB2  H N N 283 
SER HB3  H N N 284 
SER HG   H N N 285 
SER HXT  H N N 286 
THR N    N N N 287 
THR CA   C N S 288 
THR C    C N N 289 
THR O    O N N 290 
THR CB   C N R 291 
THR OG1  O N N 292 
THR CG2  C N N 293 
THR OXT  O N N 294 
THR H    H N N 295 
THR H2   H N N 296 
THR HA   H N N 297 
THR HB   H N N 298 
THR HG1  H N N 299 
THR HG21 H N N 300 
THR HG22 H N N 301 
THR HG23 H N N 302 
THR HXT  H N N 303 
TRP N    N N N 304 
TRP CA   C N S 305 
TRP C    C N N 306 
TRP O    O N N 307 
TRP CB   C N N 308 
TRP CG   C Y N 309 
TRP CD1  C Y N 310 
TRP CD2  C Y N 311 
TRP NE1  N Y N 312 
TRP CE2  C Y N 313 
TRP CE3  C Y N 314 
TRP CZ2  C Y N 315 
TRP CZ3  C Y N 316 
TRP CH2  C Y N 317 
TRP OXT  O N N 318 
TRP H    H N N 319 
TRP H2   H N N 320 
TRP HA   H N N 321 
TRP HB2  H N N 322 
TRP HB3  H N N 323 
TRP HD1  H N N 324 
TRP HE1  H N N 325 
TRP HE3  H N N 326 
TRP HZ2  H N N 327 
TRP HZ3  H N N 328 
TRP HH2  H N N 329 
TRP HXT  H N N 330 
TYR N    N N N 331 
TYR CA   C N S 332 
TYR C    C N N 333 
TYR O    O N N 334 
TYR CB   C N N 335 
TYR CG   C Y N 336 
TYR CD1  C Y N 337 
TYR CD2  C Y N 338 
TYR CE1  C Y N 339 
TYR CE2  C Y N 340 
TYR CZ   C Y N 341 
TYR OH   O N N 342 
TYR OXT  O N N 343 
TYR H    H N N 344 
TYR H2   H N N 345 
TYR HA   H N N 346 
TYR HB2  H N N 347 
TYR HB3  H N N 348 
TYR HD1  H N N 349 
TYR HD2  H N N 350 
TYR HE1  H N N 351 
TYR HE2  H N N 352 
TYR HH   H N N 353 
TYR HXT  H N N 354 
VAL N    N N N 355 
VAL CA   C N S 356 
VAL C    C N N 357 
VAL O    O N N 358 
VAL CB   C N N 359 
VAL CG1  C N N 360 
VAL CG2  C N N 361 
VAL OXT  O N N 362 
VAL H    H N N 363 
VAL H2   H N N 364 
VAL HA   H N N 365 
VAL HB   H N N 366 
VAL HG11 H N N 367 
VAL HG12 H N N 368 
VAL HG13 H N N 369 
VAL HG21 H N N 370 
VAL HG22 H N N 371 
VAL HG23 H N N 372 
VAL HXT  H N N 373 
WP1 CAG  C N N 374 
WP1 CAH  C N N 375 
WP1 CAJ  C N N 376 
WP1 CAK  C N N 377 
WP1 OAI  O N N 378 
WP1 CAC  C Y N 379 
WP1 CAB  C Y N 380 
WP1 CAA  C Y N 381 
WP1 CAF  C Y N 382 
WP1 CAE  C Y N 383 
WP1 CAD  C Y N 384 
WP1 CAL  C N N 385 
WP1 OAN  O N N 386 
WP1 NAM  N N N 387 
WP1 H1   H N N 388 
WP1 H2   H N N 389 
WP1 H3   H N N 390 
WP1 H4   H N N 391 
WP1 H5   H N N 392 
WP1 H6   H N N 393 
WP1 H7   H N N 394 
WP1 H8   H N N 395 
WP1 H9   H N N 396 
WP1 H10  H N N 397 
WP1 H11  H N N 398 
WP1 H12  H N N 399 
WP1 H13  H N N 400 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
ILE N   CA   sing N N 137 
ILE N   H    sing N N 138 
ILE N   H2   sing N N 139 
ILE CA  C    sing N N 140 
ILE CA  CB   sing N N 141 
ILE CA  HA   sing N N 142 
ILE C   O    doub N N 143 
ILE C   OXT  sing N N 144 
ILE CB  CG1  sing N N 145 
ILE CB  CG2  sing N N 146 
ILE CB  HB   sing N N 147 
ILE CG1 CD1  sing N N 148 
ILE CG1 HG12 sing N N 149 
ILE CG1 HG13 sing N N 150 
ILE CG2 HG21 sing N N 151 
ILE CG2 HG22 sing N N 152 
ILE CG2 HG23 sing N N 153 
ILE CD1 HD11 sing N N 154 
ILE CD1 HD12 sing N N 155 
ILE CD1 HD13 sing N N 156 
ILE OXT HXT  sing N N 157 
LEU N   CA   sing N N 158 
LEU N   H    sing N N 159 
LEU N   H2   sing N N 160 
LEU CA  C    sing N N 161 
LEU CA  CB   sing N N 162 
LEU CA  HA   sing N N 163 
LEU C   O    doub N N 164 
LEU C   OXT  sing N N 165 
LEU CB  CG   sing N N 166 
LEU CB  HB2  sing N N 167 
LEU CB  HB3  sing N N 168 
LEU CG  CD1  sing N N 169 
LEU CG  CD2  sing N N 170 
LEU CG  HG   sing N N 171 
LEU CD1 HD11 sing N N 172 
LEU CD1 HD12 sing N N 173 
LEU CD1 HD13 sing N N 174 
LEU CD2 HD21 sing N N 175 
LEU CD2 HD22 sing N N 176 
LEU CD2 HD23 sing N N 177 
LEU OXT HXT  sing N N 178 
LYS N   CA   sing N N 179 
LYS N   H    sing N N 180 
LYS N   H2   sing N N 181 
LYS CA  C    sing N N 182 
LYS CA  CB   sing N N 183 
LYS CA  HA   sing N N 184 
LYS C   O    doub N N 185 
LYS C   OXT  sing N N 186 
LYS CB  CG   sing N N 187 
LYS CB  HB2  sing N N 188 
LYS CB  HB3  sing N N 189 
LYS CG  CD   sing N N 190 
LYS CG  HG2  sing N N 191 
LYS CG  HG3  sing N N 192 
LYS CD  CE   sing N N 193 
LYS CD  HD2  sing N N 194 
LYS CD  HD3  sing N N 195 
LYS CE  NZ   sing N N 196 
LYS CE  HE2  sing N N 197 
LYS CE  HE3  sing N N 198 
LYS NZ  HZ1  sing N N 199 
LYS NZ  HZ2  sing N N 200 
LYS NZ  HZ3  sing N N 201 
LYS OXT HXT  sing N N 202 
MET N   CA   sing N N 203 
MET N   H    sing N N 204 
MET N   H2   sing N N 205 
MET CA  C    sing N N 206 
MET CA  CB   sing N N 207 
MET CA  HA   sing N N 208 
MET C   O    doub N N 209 
MET C   OXT  sing N N 210 
MET CB  CG   sing N N 211 
MET CB  HB2  sing N N 212 
MET CB  HB3  sing N N 213 
MET CG  SD   sing N N 214 
MET CG  HG2  sing N N 215 
MET CG  HG3  sing N N 216 
MET SD  CE   sing N N 217 
MET CE  HE1  sing N N 218 
MET CE  HE2  sing N N 219 
MET CE  HE3  sing N N 220 
MET OXT HXT  sing N N 221 
PHE N   CA   sing N N 222 
PHE N   H    sing N N 223 
PHE N   H2   sing N N 224 
PHE CA  C    sing N N 225 
PHE CA  CB   sing N N 226 
PHE CA  HA   sing N N 227 
PHE C   O    doub N N 228 
PHE C   OXT  sing N N 229 
PHE CB  CG   sing N N 230 
PHE CB  HB2  sing N N 231 
PHE CB  HB3  sing N N 232 
PHE CG  CD1  doub Y N 233 
PHE CG  CD2  sing Y N 234 
PHE CD1 CE1  sing Y N 235 
PHE CD1 HD1  sing N N 236 
PHE CD2 CE2  doub Y N 237 
PHE CD2 HD2  sing N N 238 
PHE CE1 CZ   doub Y N 239 
PHE CE1 HE1  sing N N 240 
PHE CE2 CZ   sing Y N 241 
PHE CE2 HE2  sing N N 242 
PHE CZ  HZ   sing N N 243 
PHE OXT HXT  sing N N 244 
PRO N   CA   sing N N 245 
PRO N   CD   sing N N 246 
PRO N   H    sing N N 247 
PRO CA  C    sing N N 248 
PRO CA  CB   sing N N 249 
PRO CA  HA   sing N N 250 
PRO C   O    doub N N 251 
PRO C   OXT  sing N N 252 
PRO CB  CG   sing N N 253 
PRO CB  HB2  sing N N 254 
PRO CB  HB3  sing N N 255 
PRO CG  CD   sing N N 256 
PRO CG  HG2  sing N N 257 
PRO CG  HG3  sing N N 258 
PRO CD  HD2  sing N N 259 
PRO CD  HD3  sing N N 260 
PRO OXT HXT  sing N N 261 
SER N   CA   sing N N 262 
SER N   H    sing N N 263 
SER N   H2   sing N N 264 
SER CA  C    sing N N 265 
SER CA  CB   sing N N 266 
SER CA  HA   sing N N 267 
SER C   O    doub N N 268 
SER C   OXT  sing N N 269 
SER CB  OG   sing N N 270 
SER CB  HB2  sing N N 271 
SER CB  HB3  sing N N 272 
SER OG  HG   sing N N 273 
SER OXT HXT  sing N N 274 
THR N   CA   sing N N 275 
THR N   H    sing N N 276 
THR N   H2   sing N N 277 
THR CA  C    sing N N 278 
THR CA  CB   sing N N 279 
THR CA  HA   sing N N 280 
THR C   O    doub N N 281 
THR C   OXT  sing N N 282 
THR CB  OG1  sing N N 283 
THR CB  CG2  sing N N 284 
THR CB  HB   sing N N 285 
THR OG1 HG1  sing N N 286 
THR CG2 HG21 sing N N 287 
THR CG2 HG22 sing N N 288 
THR CG2 HG23 sing N N 289 
THR OXT HXT  sing N N 290 
TRP N   CA   sing N N 291 
TRP N   H    sing N N 292 
TRP N   H2   sing N N 293 
TRP CA  C    sing N N 294 
TRP CA  CB   sing N N 295 
TRP CA  HA   sing N N 296 
TRP C   O    doub N N 297 
TRP C   OXT  sing N N 298 
TRP CB  CG   sing N N 299 
TRP CB  HB2  sing N N 300 
TRP CB  HB3  sing N N 301 
TRP CG  CD1  doub Y N 302 
TRP CG  CD2  sing Y N 303 
TRP CD1 NE1  sing Y N 304 
TRP CD1 HD1  sing N N 305 
TRP CD2 CE2  doub Y N 306 
TRP CD2 CE3  sing Y N 307 
TRP NE1 CE2  sing Y N 308 
TRP NE1 HE1  sing N N 309 
TRP CE2 CZ2  sing Y N 310 
TRP CE3 CZ3  doub Y N 311 
TRP CE3 HE3  sing N N 312 
TRP CZ2 CH2  doub Y N 313 
TRP CZ2 HZ2  sing N N 314 
TRP CZ3 CH2  sing Y N 315 
TRP CZ3 HZ3  sing N N 316 
TRP CH2 HH2  sing N N 317 
TRP OXT HXT  sing N N 318 
TYR N   CA   sing N N 319 
TYR N   H    sing N N 320 
TYR N   H2   sing N N 321 
TYR CA  C    sing N N 322 
TYR CA  CB   sing N N 323 
TYR CA  HA   sing N N 324 
TYR C   O    doub N N 325 
TYR C   OXT  sing N N 326 
TYR CB  CG   sing N N 327 
TYR CB  HB2  sing N N 328 
TYR CB  HB3  sing N N 329 
TYR CG  CD1  doub Y N 330 
TYR CG  CD2  sing Y N 331 
TYR CD1 CE1  sing Y N 332 
TYR CD1 HD1  sing N N 333 
TYR CD2 CE2  doub Y N 334 
TYR CD2 HD2  sing N N 335 
TYR CE1 CZ   doub Y N 336 
TYR CE1 HE1  sing N N 337 
TYR CE2 CZ   sing Y N 338 
TYR CE2 HE2  sing N N 339 
TYR CZ  OH   sing N N 340 
TYR OH  HH   sing N N 341 
TYR OXT HXT  sing N N 342 
VAL N   CA   sing N N 343 
VAL N   H    sing N N 344 
VAL N   H2   sing N N 345 
VAL CA  C    sing N N 346 
VAL CA  CB   sing N N 347 
VAL CA  HA   sing N N 348 
VAL C   O    doub N N 349 
VAL C   OXT  sing N N 350 
VAL CB  CG1  sing N N 351 
VAL CB  CG2  sing N N 352 
VAL CB  HB   sing N N 353 
VAL CG1 HG11 sing N N 354 
VAL CG1 HG12 sing N N 355 
VAL CG1 HG13 sing N N 356 
VAL CG2 HG21 sing N N 357 
VAL CG2 HG22 sing N N 358 
VAL CG2 HG23 sing N N 359 
VAL OXT HXT  sing N N 360 
WP1 CAE CAF  doub Y N 361 
WP1 CAE CAD  sing Y N 362 
WP1 OAN CAL  doub N N 363 
WP1 CAF CAA  sing Y N 364 
WP1 CAL CAD  sing N N 365 
WP1 CAL NAM  sing N N 366 
WP1 CAD CAC  doub Y N 367 
WP1 CAA CAB  doub Y N 368 
WP1 CAC CAB  sing Y N 369 
WP1 CAC OAI  sing N N 370 
WP1 CAB CAG  sing N N 371 
WP1 CAJ CAH  sing N N 372 
WP1 OAI CAH  sing N N 373 
WP1 CAG CAH  sing N N 374 
WP1 CAH CAK  sing N N 375 
WP1 CAG H1   sing N N 376 
WP1 CAG H2   sing N N 377 
WP1 CAJ H3   sing N N 378 
WP1 CAJ H4   sing N N 379 
WP1 CAJ H5   sing N N 380 
WP1 CAK H6   sing N N 381 
WP1 CAK H7   sing N N 382 
WP1 CAK H8   sing N N 383 
WP1 CAA H9   sing N N 384 
WP1 CAF H10  sing N N 385 
WP1 CAE H11  sing N N 386 
WP1 NAM H12  sing N N 387 
WP1 NAM H13  sing N N 388 
# 
_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                    7HB7 
_atom_sites.fract_transf_matrix[1][1]   0.014229 
_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]   0.011334 
_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]   0.010336 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 6.96715 ?       ? ? 11.43723 ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-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   ? 9.00438   15.68345 10.23893 1.000 86.65383  ? 16  GLU A N   1 
ATOM   2    C CA  . GLU A 1 9   ? 10.22403  16.47971 10.30478 1.000 93.98615  ? 16  GLU A CA  1 
ATOM   3    C C   . GLU A 1 9   ? 10.16293  17.45991 11.47190 1.000 86.00697  ? 16  GLU A C   1 
ATOM   4    O O   . GLU A 1 9   ? 9.32554   18.36242 11.49417 1.000 79.85873  ? 16  GLU A O   1 
ATOM   5    C CB  . GLU A 1 9   ? 10.44688  17.22911 8.98953  1.000 102.42015 ? 16  GLU A CB  1 
ATOM   6    C CG  . GLU A 1 9   ? 11.88683  17.65146 8.75021  1.000 104.65594 ? 16  GLU A CG  1 
ATOM   7    C CD  . GLU A 1 9   ? 12.14812  19.08924 9.15303  1.000 117.27985 ? 16  GLU A CD  1 
ATOM   8    O OE1 . GLU A 1 9   ? 11.18838  19.78089 9.55391  1.000 117.03439 ? 16  GLU A OE1 1 
ATOM   9    O OE2 . GLU A 1 9   ? 13.31430  19.52818 9.06849  1.000 118.33334 ? 16  GLU A OE2 1 
ATOM   10   N N   . VAL A 1 10  ? 11.05605  17.27577 12.44104 1.000 76.02954  ? 17  VAL A N   1 
ATOM   11   C CA  . VAL A 1 10  ? 11.09059  18.08051 13.65609 1.000 67.50036  ? 17  VAL A CA  1 
ATOM   12   C C   . VAL A 1 10  ? 12.44717  18.76481 13.74451 1.000 70.81742  ? 17  VAL A C   1 
ATOM   13   O O   . VAL A 1 10  ? 13.48767  18.11417 13.59244 1.000 68.66689  ? 17  VAL A O   1 
ATOM   14   C CB  . VAL A 1 10  ? 10.82796  17.22519 14.90965 1.000 66.68632  ? 17  VAL A CB  1 
ATOM   15   C CG1 . VAL A 1 10  ? 10.95987  18.06796 16.16907 1.000 63.64471  ? 17  VAL A CG1 1 
ATOM   16   C CG2 . VAL A 1 10  ? 9.45431   16.57705 14.83337 1.000 72.37447  ? 17  VAL A CG2 1 
ATOM   17   N N   . GLU A 1 11  ? 12.43330  20.07214 13.98816 1.000 66.88625  ? 18  GLU A N   1 
ATOM   18   C CA  . GLU A 1 11  ? 13.64842  20.85377 14.17167 1.000 61.50789  ? 18  GLU A CA  1 
ATOM   19   C C   . GLU A 1 11  ? 13.84856  21.13345 15.65496 1.000 59.32905  ? 18  GLU A C   1 
ATOM   20   O O   . GLU A 1 11  ? 12.90167  21.51084 16.35253 1.000 58.31311  ? 18  GLU A O   1 
ATOM   21   C CB  . GLU A 1 11  ? 13.57736  22.16946 13.39526 1.000 61.26070  ? 18  GLU A CB  1 
ATOM   22   C CG  . GLU A 1 11  ? 13.59297  22.01475 11.88593 1.000 63.67302  ? 18  GLU A CG  1 
ATOM   23   C CD  . GLU A 1 11  ? 13.31701  23.32221 11.16930 1.000 75.75145  ? 18  GLU A CD  1 
ATOM   24   O OE1 . GLU A 1 11  ? 12.33842  24.00710 11.53531 1.000 81.72306  ? 18  GLU A OE1 1 
ATOM   25   O OE2 . GLU A 1 11  ? 14.07930  23.66640 10.24173 1.000 74.29597  ? 18  GLU A OE2 1 
ATOM   26   N N   . THR A 1 12  ? 15.07625  20.94957 16.13116 1.000 58.95058  ? 19  THR A N   1 
ATOM   27   C CA  . THR A 1 12  ? 15.42945  21.19781 17.52250 1.000 57.42070  ? 19  THR A CA  1 
ATOM   28   C C   . THR A 1 12  ? 16.25218  22.47487 17.61401 1.000 56.29833  ? 19  THR A C   1 
ATOM   29   O O   . THR A 1 12  ? 17.22897  22.64395 16.87626 1.000 57.18444  ? 19  THR A O   1 
ATOM   30   C CB  . THR A 1 12  ? 16.21170  20.02325 18.11459 1.000 58.47947  ? 19  THR A CB  1 
ATOM   31   O OG1 . THR A 1 12  ? 15.43223  18.82487 18.01045 1.000 59.92009  ? 19  THR A OG1 1 
ATOM   32   C CG2 . THR A 1 12  ? 16.53598  20.28464 19.57839 1.000 57.35011  ? 19  THR A CG2 1 
ATOM   33   N N   . PHE A 1 13  ? 15.85588  23.36617 18.51743 1.000 54.74415  ? 20  PHE A N   1 
ATOM   34   C CA  . PHE A 1 13  ? 16.51180  24.64943 18.70302 1.000 53.96620  ? 20  PHE A CA  1 
ATOM   35   C C   . PHE A 1 13  ? 17.09487  24.72809 20.10689 1.000 54.09366  ? 20  PHE A C   1 
ATOM   36   O O   . PHE A 1 13  ? 16.65030  24.03702 21.02671 1.000 59.08918  ? 20  PHE A O   1 
ATOM   37   C CB  . PHE A 1 13  ? 15.53951  25.81865 18.48503 1.000 54.51683  ? 20  PHE A CB  1 
ATOM   38   C CG  . PHE A 1 13  ? 14.90081  25.84478 17.12222 1.000 55.64598  ? 20  PHE A CG  1 
ATOM   39   C CD1 . PHE A 1 13  ? 13.92508  24.92316 16.77550 1.000 54.96041  ? 20  PHE A CD1 1 
ATOM   40   C CD2 . PHE A 1 13  ? 15.26127  26.80737 16.19556 1.000 56.39181  ? 20  PHE A CD2 1 
ATOM   41   C CE1 . PHE A 1 13  ? 13.33626  24.95060 15.52746 1.000 57.03350  ? 20  PHE A CE1 1 
ATOM   42   C CE2 . PHE A 1 13  ? 14.67239  26.83982 14.94505 1.000 64.54049  ? 20  PHE A CE2 1 
ATOM   43   C CZ  . PHE A 1 13  ? 13.71183  25.90862 14.61077 1.000 64.61837  ? 20  PHE A CZ  1 
ATOM   44   N N   . ALA A 1 14  ? 18.09816  25.58575 20.26334 1.000 62.90421  ? 21  ALA A N   1 
ATOM   45   C CA  . ALA A 1 14  ? 18.73257  25.82704 21.55221 1.000 57.33506  ? 21  ALA A CA  1 
ATOM   46   C C   . ALA A 1 14  ? 18.20594  27.13771 22.12253 1.000 60.52256  ? 21  ALA A C   1 
ATOM   47   O O   . ALA A 1 14  ? 18.30622  28.18406 21.47349 1.000 63.63138  ? 21  ALA A O   1 
ATOM   48   C CB  . ALA A 1 14  ? 20.25394  25.87170 21.41386 1.000 62.30038  ? 21  ALA A CB  1 
ATOM   49   N N   . PHE A 1 15  ? 17.63810  27.07629 23.32504 1.000 66.24917  ? 22  PHE A N   1 
ATOM   50   C CA  . PHE A 1 15  ? 17.15842  28.28097 23.98845 1.000 58.28130  ? 22  PHE A CA  1 
ATOM   51   C C   . PHE A 1 15  ? 18.30225  29.26513 24.20119 1.000 64.16773  ? 22  PHE A C   1 
ATOM   52   O O   . PHE A 1 15  ? 19.45939  28.87743 24.38709 1.000 67.35816  ? 22  PHE A O   1 
ATOM   53   C CB  . PHE A 1 15  ? 16.52129  27.93170 25.33522 1.000 52.47182  ? 22  PHE A CB  1 
ATOM   54   C CG  . PHE A 1 15  ? 15.03674  27.70531 25.27161 1.000 65.04495  ? 22  PHE A CG  1 
ATOM   55   C CD1 . PHE A 1 15  ? 14.19774  28.64363 24.69034 1.000 77.15921  ? 22  PHE A CD1 1 
ATOM   56   C CD2 . PHE A 1 15  ? 14.48079  26.54933 25.79345 1.000 61.56249  ? 22  PHE A CD2 1 
ATOM   57   C CE1 . PHE A 1 15  ? 12.83080  28.43343 24.63861 1.000 74.48162  ? 22  PHE A CE1 1 
ATOM   58   C CE2 . PHE A 1 15  ? 13.11832  26.33212 25.74027 1.000 60.95904  ? 22  PHE A CE2 1 
ATOM   59   C CZ  . PHE A 1 15  ? 12.29280  27.27468 25.16219 1.000 69.01532  ? 22  PHE A CZ  1 
ATOM   60   N N   . GLN A 1 16  ? 17.97061  30.55362 24.15952 1.000 55.64416  ? 23  GLN A N   1 
ATOM   61   C CA  . GLN A 1 16  ? 18.94827  31.57383 24.50552 1.000 53.03389  ? 23  GLN A CA  1 
ATOM   62   C C   . GLN A 1 16  ? 19.42841  31.36136 25.93559 1.000 60.80336  ? 23  GLN A C   1 
ATOM   63   O O   . GLN A 1 16  ? 18.68099  30.89646 26.80095 1.000 66.64445  ? 23  GLN A O   1 
ATOM   64   C CB  . GLN A 1 16  ? 18.34933  32.97263 24.34594 1.000 52.89671  ? 23  GLN A CB  1 
ATOM   65   C CG  . GLN A 1 16  ? 18.41326  33.51797 22.92621 1.000 54.44078  ? 23  GLN A CG  1 
ATOM   66   C CD  . GLN A 1 16  ? 17.56100  34.75905 22.73421 1.000 65.15102  ? 23  GLN A CD  1 
ATOM   67   O OE1 . GLN A 1 16  ? 16.90568  35.22720 23.66477 1.000 67.47162  ? 23  GLN A OE1 1 
ATOM   68   N NE2 . GLN A 1 16  ? 17.56645  35.29831 21.52038 1.000 76.78418  ? 23  GLN A NE2 1 
ATOM   69   N N   . ALA A 1 17  ? 20.70114  31.69146 26.17269 1.000 65.13797  ? 24  ALA A N   1 
ATOM   70   C CA  . ALA A 1 17  ? 21.30177  31.44470 27.48019 1.000 57.18079  ? 24  ALA A CA  1 
ATOM   71   C C   . ALA A 1 17  ? 20.50175  32.10707 28.59380 1.000 57.65573  ? 24  ALA A C   1 
ATOM   72   O O   . ALA A 1 17  ? 20.25800  31.49547 29.63961 1.000 60.50995  ? 24  ALA A O   1 
ATOM   73   C CB  . ALA A 1 17  ? 22.74925  31.93464 27.49392 1.000 61.58974  ? 24  ALA A CB  1 
ATOM   74   N N   . GLU A 1 18  ? 20.06921  33.35137 28.37968 1.000 60.49821  ? 25  GLU A N   1 
ATOM   75   C CA  . GLU A 1 18  ? 19.30193  34.05675 29.40135 1.000 65.23300  ? 25  GLU A CA  1 
ATOM   76   C C   . GLU A 1 18  ? 17.98471  33.34880 29.69300 1.000 62.44041  ? 25  GLU A C   1 
ATOM   77   O O   . GLU A 1 18  ? 17.58483  33.22005 30.85623 1.000 58.18152  ? 25  GLU A O   1 
ATOM   78   C CB  . GLU A 1 18  ? 19.05148  35.49956 28.96184 1.000 65.95463  ? 25  GLU A CB  1 
ATOM   79   C CG  . GLU A 1 18  ? 20.31231  36.34326 28.85385 1.000 76.53909  ? 25  GLU A CG  1 
ATOM   80   C CD  . GLU A 1 18  ? 21.01534  36.18459 27.51763 1.000 78.42387  ? 25  GLU A CD  1 
ATOM   81   O OE1 . GLU A 1 18  ? 20.61346  35.30244 26.72971 1.000 70.01922  ? 25  GLU A OE1 1 
ATOM   82   O OE2 . GLU A 1 18  ? 21.97466  36.94067 27.25721 1.000 84.30772  ? 25  GLU A OE2 1 
ATOM   83   N N   . ILE A 1 19  ? 17.29700  32.88005 28.64987 1.000 62.27029  ? 26  ILE A N   1 
ATOM   84   C CA  . ILE A 1 19  ? 16.03892  32.17035 28.85550 1.000 60.39302  ? 26  ILE A CA  1 
ATOM   85   C C   . ILE A 1 19  ? 16.28610  30.83446 29.54546 1.000 63.25731  ? 26  ILE A C   1 
ATOM   86   O O   . ILE A 1 19  ? 15.52893  30.43290 30.43690 1.000 63.61404  ? 26  ILE A O   1 
ATOM   87   C CB  . ILE A 1 19  ? 15.29919  31.99420 27.51664 1.000 52.39845  ? 26  ILE A CB  1 
ATOM   88   C CG1 . ILE A 1 19  ? 14.78414  33.34354 27.01252 1.000 56.44601  ? 26  ILE A CG1 1 
ATOM   89   C CG2 . ILE A 1 19  ? 14.14610  31.01442 27.66330 1.000 55.43211  ? 26  ILE A CG2 1 
ATOM   90   C CD1 . ILE A 1 19  ? 14.80528  33.48133 25.50834 1.000 60.56278  ? 26  ILE A CD1 1 
ATOM   91   N N   . ALA A 1 20  ? 17.35680  30.13424 29.16030 1.000 63.44499  ? 27  ALA A N   1 
ATOM   92   C CA  . ALA A 1 20  ? 17.65198  28.83777 29.76385 1.000 56.37469  ? 27  ALA A CA  1 
ATOM   93   C C   . ALA A 1 20  ? 17.92160  28.96630 31.25927 1.000 63.33153  ? 27  ALA A C   1 
ATOM   94   O O   . ALA A 1 20  ? 17.51633  28.10190 32.04558 1.000 67.34105  ? 27  ALA A O   1 
ATOM   95   C CB  . ALA A 1 20  ? 18.84036  28.18703 29.05597 1.000 55.79545  ? 27  ALA A CB  1 
ATOM   96   N N   . GLN A 1 21  ? 18.60571  30.03766 31.67335 1.000 61.90868  ? 28  GLN A N   1 
ATOM   97   C CA  . GLN A 1 21  ? 18.82922  30.26043 33.09930 1.000 59.01755  ? 28  GLN A CA  1 
ATOM   98   C C   . GLN A 1 21  ? 17.54155  30.64172 33.81798 1.000 63.00512  ? 28  GLN A C   1 
ATOM   99   O O   . GLN A 1 21  ? 17.38968  30.35036 35.00985 1.000 64.63544  ? 28  GLN A O   1 
ATOM   100  C CB  . GLN A 1 21  ? 19.88724  31.34436 33.31138 1.000 65.87781  ? 28  GLN A CB  1 
ATOM   101  C CG  . GLN A 1 21  ? 21.18260  31.12239 32.55082 1.000 67.59620  ? 28  GLN A CG  1 
ATOM   102  C CD  . GLN A 1 21  ? 22.23786  32.15847 32.88423 1.000 75.80886  ? 28  GLN A CD  1 
ATOM   103  O OE1 . GLN A 1 21  ? 21.98990  33.09055 33.64977 1.000 75.53583  ? 28  GLN A OE1 1 
ATOM   104  N NE2 . GLN A 1 21  ? 23.42261  32.00358 32.30478 1.000 82.72968  ? 28  GLN A NE2 1 
ATOM   105  N N   . LEU A 1 22  ? 16.61122  31.29425 33.11842 1.000 61.85089  ? 29  LEU A N   1 
ATOM   106  C CA  . LEU A 1 22  ? 15.34409  31.66975 33.73705 1.000 58.97948  ? 29  LEU A CA  1 
ATOM   107  C C   . LEU A 1 22  ? 14.51566  30.43893 34.08124 1.000 56.13631  ? 29  LEU A C   1 
ATOM   108  O O   . LEU A 1 22  ? 13.98749  30.32266 35.19351 1.000 58.95049  ? 29  LEU A O   1 
ATOM   109  C CB  . LEU A 1 22  ? 14.56285  32.59703 32.80715 1.000 68.74448  ? 29  LEU A CB  1 
ATOM   110  C CG  . LEU A 1 22  ? 13.22307  33.08994 33.35222 1.000 59.88547  ? 29  LEU A CG  1 
ATOM   111  C CD1 . LEU A 1 22  ? 13.45392  33.97162 34.56300 1.000 55.49260  ? 29  LEU A CD1 1 
ATOM   112  C CD2 . LEU A 1 22  ? 12.44169  33.83366 32.28080 1.000 67.17567  ? 29  LEU A CD2 1 
ATOM   113  N N   . MET A 1 23  ? 14.39170  29.50896 33.13250 1.000 56.31470  ? 30  MET A N   1 
ATOM   114  C CA  . MET A 1 23  ? 13.59950  28.30480 33.36040 1.000 58.90811  ? 30  MET A CA  1 
ATOM   115  C C   . MET A 1 23  ? 14.20616  27.44326 34.45939 1.000 61.11186  ? 30  MET A C   1 
ATOM   116  O O   . MET A 1 23  ? 13.51359  27.04673 35.40280 1.000 65.03454  ? 30  MET A O   1 
ATOM   117  C CB  . MET A 1 23  ? 13.47580  27.51415 32.05993 1.000 54.46242  ? 30  MET A CB  1 
ATOM   118  C CG  . MET A 1 23  ? 13.17334  28.37473 30.85056 1.000 60.11353  ? 30  MET A CG  1 
ATOM   119  S SD  . MET A 1 23  ? 13.21243  27.42655 29.31984 1.000 58.84883  ? 30  MET A SD  1 
ATOM   120  C CE  . MET A 1 23  ? 11.75046  26.41102 29.50135 1.000 52.68461  ? 30  MET A CE  1 
ATOM   121  N N   . SER A 1 24  ? 15.50468  27.14455 34.35283 1.000 65.06996  ? 31  SER A N   1 
ATOM   122  C CA  . SER A 1 24  ? 16.17059  26.33168 35.36685 1.000 61.61998  ? 31  SER A CA  1 
ATOM   123  C C   . SER A 1 24  ? 15.98871  26.92217 36.75887 1.000 64.52436  ? 31  SER A C   1 
ATOM   124  O O   . SER A 1 24  ? 15.86384  26.18643 37.74442 1.000 65.75169  ? 31  SER A O   1 
ATOM   125  C CB  . SER A 1 24  ? 17.65610  26.19443 35.03540 1.000 61.46287  ? 31  SER A CB  1 
ATOM   126  O OG  . SER A 1 24  ? 18.38240  25.72666 36.15760 1.000 68.26132  ? 31  SER A OG  1 
ATOM   127  N N   . LEU A 1 25  ? 15.96640  28.25272 36.85792 1.000 67.03802  ? 32  LEU A N   1 
ATOM   128  C CA  . LEU A 1 25  ? 15.65001  28.89033 38.13059 1.000 65.00584  ? 32  LEU A CA  1 
ATOM   129  C C   . LEU A 1 25  ? 14.20485  28.62495 38.53347 1.000 68.08570  ? 32  LEU A C   1 
ATOM   130  O O   . LEU A 1 25  ? 13.90793  28.44995 39.71960 1.000 72.36815  ? 32  LEU A O   1 
ATOM   131  C CB  . LEU A 1 25  ? 15.91481  30.39311 38.04495 1.000 64.81032  ? 32  LEU A CB  1 
ATOM   132  C CG  . LEU A 1 25  ? 16.12902  31.11819 39.37470 1.000 67.56372  ? 32  LEU A CG  1 
ATOM   133  C CD1 . LEU A 1 25  ? 17.44740  30.70443 40.01247 1.000 71.14487  ? 32  LEU A CD1 1 
ATOM   134  C CD2 . LEU A 1 25  ? 16.06988  32.62444 39.17928 1.000 65.30229  ? 32  LEU A CD2 1 
ATOM   135  N N   . ILE A 1 26  ? 13.29458  28.57941 37.55895 1.000 65.21313  ? 33  ILE A N   1 
ATOM   136  C CA  . ILE A 1 26  ? 11.88024  28.39368 37.86862 1.000 59.97732  ? 33  ILE A CA  1 
ATOM   137  C C   . ILE A 1 26  ? 11.61931  26.98003 38.37902 1.000 64.29253  ? 33  ILE A C   1 
ATOM   138  O O   . ILE A 1 26  ? 10.85950  26.78200 39.33535 1.000 75.67326  ? 33  ILE A O   1 
ATOM   139  C CB  . ILE A 1 26  ? 11.02238  28.72757 36.63312 1.000 57.44331  ? 33  ILE A CB  1 
ATOM   140  C CG1 . ILE A 1 26  ? 10.77501  30.23572 36.54884 1.000 51.25387  ? 33  ILE A CG1 1 
ATOM   141  C CG2 . ILE A 1 26  ? 9.70560   27.96489 36.65889 1.000 63.11777  ? 33  ILE A CG2 1 
ATOM   142  C CD1 . ILE A 1 26  ? 10.25141  30.69579 35.20608 1.000 49.75701  ? 33  ILE A CD1 1 
ATOM   143  N N   . ILE A 1 27  ? 12.25230  25.97714 37.76587 1.000 64.78836  ? 34  ILE A N   1 
ATOM   144  C CA  . ILE A 1 27  ? 11.99894  24.59444 38.16324 1.000 69.26221  ? 34  ILE A CA  1 
ATOM   145  C C   . ILE A 1 27  ? 12.69342  24.26854 39.48060 1.000 81.40659  ? 34  ILE A C   1 
ATOM   146  O O   . ILE A 1 27  ? 12.16472  23.51029 40.30251 1.000 85.68008  ? 34  ILE A O   1 
ATOM   147  C CB  . ILE A 1 27  ? 12.43278  23.62168 37.05137 1.000 66.16600  ? 34  ILE A CB  1 
ATOM   148  C CG1 . ILE A 1 27  ? 12.28817  24.26815 35.67584 1.000 57.10057  ? 34  ILE A CG1 1 
ATOM   149  C CG2 . ILE A 1 27  ? 11.63022  22.33205 37.12938 1.000 74.80549  ? 34  ILE A CG2 1 
ATOM   150  C CD1 . ILE A 1 27  ? 12.69547  23.36543 34.54510 1.000 54.16542  ? 34  ILE A CD1 1 
ATOM   151  N N   . ASN A 1 28  ? 13.88501  24.82490 39.70445 1.000 78.76516  ? 35  ASN A N   1 
ATOM   152  C CA  . ASN A 1 28  ? 14.70872  24.41463 40.83551 1.000 82.57811  ? 35  ASN A CA  1 
ATOM   153  C C   . ASN A 1 28  ? 14.48851  25.24410 42.09497 1.000 90.87791  ? 35  ASN A C   1 
ATOM   154  O O   . ASN A 1 28  ? 14.77682  24.75430 43.19318 1.000 106.42036 ? 35  ASN A O   1 
ATOM   155  C CB  . ASN A 1 28  ? 16.19255  24.46019 40.45264 1.000 80.98282  ? 35  ASN A CB  1 
ATOM   156  C CG  . ASN A 1 28  ? 16.52893  23.51277 39.31569 1.000 79.52698  ? 35  ASN A CG  1 
ATOM   157  O OD1 . ASN A 1 28  ? 17.28346  23.85570 38.40548 1.000 95.68425  ? 35  ASN A OD1 1 
ATOM   158  N ND2 . ASN A 1 28  ? 15.96252  22.31290 39.36116 1.000 79.19416  ? 35  ASN A ND2 1 
ATOM   159  N N   . THR A 1 29  ? 13.99257  26.47390 41.97659 1.000 90.18525  ? 36  THR A N   1 
ATOM   160  C CA  . THR A 1 29  ? 13.78174  27.30027 43.15932 1.000 95.38779  ? 36  THR A CA  1 
ATOM   161  C C   . THR A 1 29  ? 12.58551  26.79270 43.95451 1.000 91.33582  ? 36  THR A C   1 
ATOM   162  O O   . THR A 1 29  ? 11.48733  26.63191 43.41313 1.000 87.00828  ? 36  THR A O   1 
ATOM   163  C CB  . THR A 1 29  ? 13.56717  28.76223 42.76961 1.000 96.58953  ? 36  THR A CB  1 
ATOM   164  O OG1 . THR A 1 29  ? 14.75387  29.27298 42.14958 1.000 89.70089  ? 36  THR A OG1 1 
ATOM   165  C CG2 . THR A 1 29  ? 13.24290  29.60022 43.99800 1.000 89.83245  ? 36  THR A CG2 1 
ATOM   166  N N   . PHE A 1 30  ? 12.80297  26.53894 45.24265 1.000 88.80231  ? 37  PHE A N   1 
ATOM   167  C CA  . PHE A 1 30  ? 11.73276  26.09994 46.13132 1.000 87.78051  ? 37  PHE A CA  1 
ATOM   168  C C   . PHE A 1 30  ? 10.75057  27.24720 46.33477 1.000 91.08344  ? 37  PHE A C   1 
ATOM   169  O O   . PHE A 1 30  ? 11.04019  28.20253 47.06247 1.000 99.82990  ? 37  PHE A O   1 
ATOM   170  C CB  . PHE A 1 30  ? 12.31620  25.62875 47.45982 1.000 95.33764  ? 37  PHE A CB  1 
ATOM   171  C CG  . PHE A 1 30  ? 11.31079  24.98648 48.37136 1.000 99.59111  ? 37  PHE A CG  1 
ATOM   172  C CD1 . PHE A 1 30  ? 10.67248  23.81330 48.00451 1.000 101.94647 ? 37  PHE A CD1 1 
ATOM   173  C CD2 . PHE A 1 30  ? 11.00859  25.55209 49.59848 1.000 93.69249  ? 37  PHE A CD2 1 
ATOM   174  C CE1 . PHE A 1 30  ? 9.74772   23.21901 48.84342 1.000 97.15596  ? 37  PHE A CE1 1 
ATOM   175  C CE2 . PHE A 1 30  ? 10.08486  24.96271 50.44107 1.000 86.26998  ? 37  PHE A CE2 1 
ATOM   176  C CZ  . PHE A 1 30  ? 9.45391   23.79511 50.06307 1.000 81.19031  ? 37  PHE A CZ  1 
ATOM   177  N N   . TYR A 1 31  ? 9.58953   27.15759 45.68888 1.000 83.85841  ? 38  TYR A N   1 
ATOM   178  C CA  . TYR A 1 31  ? 8.58920   28.21613 45.72324 1.000 84.98765  ? 38  TYR A CA  1 
ATOM   179  C C   . TYR A 1 31  ? 7.21032   27.58110 45.81268 1.000 81.64907  ? 38  TYR A C   1 
ATOM   180  O O   . TYR A 1 31  ? 6.85133   26.75605 44.96803 1.000 76.74860  ? 38  TYR A O   1 
ATOM   181  C CB  . TYR A 1 31  ? 8.70227   29.10977 44.48201 1.000 78.09824  ? 38  TYR A CB  1 
ATOM   182  C CG  . TYR A 1 31  ? 7.74102   30.27333 44.45618 1.000 75.56712  ? 38  TYR A CG  1 
ATOM   183  C CD1 . TYR A 1 31  ? 8.02164   31.44362 45.14823 1.000 78.89594  ? 38  TYR A CD1 1 
ATOM   184  C CD2 . TYR A 1 31  ? 6.56716   30.21366 43.71845 1.000 79.49211  ? 38  TYR A CD2 1 
ATOM   185  C CE1 . TYR A 1 31  ? 7.15018   32.51459 45.12377 1.000 79.38285  ? 38  TYR A CE1 1 
ATOM   186  C CE2 . TYR A 1 31  ? 5.69223   31.28066 43.68452 1.000 80.92293  ? 38  TYR A CE2 1 
ATOM   187  C CZ  . TYR A 1 31  ? 5.98707   32.42763 44.38980 1.000 79.68221  ? 38  TYR A CZ  1 
ATOM   188  O OH  . TYR A 1 31  ? 5.11611   33.49148 44.35970 1.000 73.08672  ? 38  TYR A OH  1 
ATOM   189  N N   . SER A 1 32  ? 6.44121   27.96801 46.83264 1.000 90.11450  ? 39  SER A N   1 
ATOM   190  C CA  . SER A 1 32  ? 5.19370   27.28438 47.15398 1.000 92.02256  ? 39  SER A CA  1 
ATOM   191  C C   . SER A 1 32  ? 3.96007   27.91920 46.52425 1.000 90.48883  ? 39  SER A C   1 
ATOM   192  O O   . SER A 1 32  ? 2.93769   27.23749 46.38669 1.000 100.39242 ? 39  SER A O   1 
ATOM   193  C CB  . SER A 1 32  ? 5.00299   27.22418 48.67329 1.000 104.38210 ? 39  SER A CB  1 
ATOM   194  O OG  . SER A 1 32  ? 5.80189   26.20380 49.24704 1.000 112.98948 ? 39  SER A OG  1 
ATOM   195  N N   . ASN A 1 33  ? 4.01893   29.19542 46.14497 1.000 78.23091  ? 40  ASN A N   1 
ATOM   196  C CA  . ASN A 1 33  ? 2.86351   29.85484 45.54530 1.000 73.54667  ? 40  ASN A CA  1 
ATOM   197  C C   . ASN A 1 33  ? 2.80248   29.58809 44.04613 1.000 72.98915  ? 40  ASN A C   1 
ATOM   198  O O   . ASN A 1 33  ? 2.72691   30.52448 43.24398 1.000 79.23045  ? 40  ASN A O   1 
ATOM   199  C CB  . ASN A 1 33  ? 2.90216   31.36054 45.81787 1.000 67.15438  ? 40  ASN A CB  1 
ATOM   200  C CG  . ASN A 1 33  ? 1.52071   31.98472 45.83995 1.000 75.17314  ? 40  ASN A CG  1 
ATOM   201  O OD1 . ASN A 1 33  ? 0.50940   31.28285 45.85098 1.000 82.01541  ? 40  ASN A OD1 1 
ATOM   202  N ND2 . ASN A 1 33  ? 1.47128   33.31196 45.84182 1.000 82.36910  ? 40  ASN A ND2 1 
ATOM   203  N N   . LYS A 1 34  ? 2.82036   28.31051 43.66110 1.000 71.01014  ? 41  LYS A N   1 
ATOM   204  C CA  . LYS A 1 34  ? 2.86911   27.93525 42.25342 1.000 67.05073  ? 41  LYS A CA  1 
ATOM   205  C C   . LYS A 1 34  ? 1.57014   28.21690 41.50944 1.000 66.60982  ? 41  LYS A C   1 
ATOM   206  O O   . LYS A 1 34  ? 1.55249   28.10886 40.27917 1.000 68.58519  ? 41  LYS A O   1 
ATOM   207  C CB  . LYS A 1 34  ? 3.21797   26.45132 42.12006 1.000 61.89644  ? 41  LYS A CB  1 
ATOM   208  C CG  . LYS A 1 34  ? 4.65745   26.11176 42.46822 1.000 67.00279  ? 41  LYS A CG  1 
ATOM   209  C CD  . LYS A 1 34  ? 4.89779   24.61155 42.40309 1.000 66.88814  ? 41  LYS A CD  1 
ATOM   210  C CE  . LYS A 1 34  ? 6.23032   24.23715 43.03033 1.000 65.39762  ? 41  LYS A CE  1 
ATOM   211  N NZ  . LYS A 1 34  ? 7.38026   24.67870 42.19376 1.000 60.93940  ? 41  LYS A NZ  1 
ATOM   212  N N   . GLU A 1 35  ? 0.49265   28.57628 42.21114 1.000 68.83618  ? 42  GLU A N   1 
ATOM   213  C CA  . GLU A 1 35  ? -0.79628  28.78533 41.56059 1.000 65.85150  ? 42  GLU A CA  1 
ATOM   214  C C   . GLU A 1 35  ? -0.81017  29.99378 40.63352 1.000 68.88433  ? 42  GLU A C   1 
ATOM   215  O O   . GLU A 1 35  ? -1.75569  30.13720 39.85068 1.000 70.44425  ? 42  GLU A O   1 
ATOM   216  C CB  . GLU A 1 35  ? -1.89792  28.93588 42.61200 1.000 65.90234  ? 42  GLU A CB  1 
ATOM   217  C CG  . GLU A 1 35  ? -1.88122  30.26688 43.34642 1.000 68.60690  ? 42  GLU A CG  1 
ATOM   218  C CD  . GLU A 1 35  ? -3.07225  30.43852 44.26980 1.000 82.14476  ? 42  GLU A CD  1 
ATOM   219  O OE1 . GLU A 1 35  ? -3.35010  29.51432 45.06238 1.000 81.65497  ? 42  GLU A OE1 1 
ATOM   220  O OE2 . GLU A 1 35  ? -3.73121  31.49765 44.20286 1.000 85.73619  ? 42  GLU A OE2 1 
ATOM   221  N N   . ILE A 1 36  ? 0.20715   30.85728 40.69451 1.000 67.33263  ? 43  ILE A N   1 
ATOM   222  C CA  . ILE A 1 36  ? 0.23529   32.05384 39.86073 1.000 67.09259  ? 43  ILE A CA  1 
ATOM   223  C C   . ILE A 1 36  ? 0.48474   31.75107 38.39234 1.000 59.99821  ? 43  ILE A C   1 
ATOM   224  O O   . ILE A 1 36  ? 0.36404   32.65451 37.55736 1.000 65.89726  ? 43  ILE A O   1 
ATOM   225  C CB  . ILE A 1 36  ? 1.30362   33.04322 40.36968 1.000 72.17729  ? 43  ILE A CB  1 
ATOM   226  C CG1 . ILE A 1 36  ? 2.69719   32.41610 40.29239 1.000 72.16666  ? 43  ILE A CG1 1 
ATOM   227  C CG2 . ILE A 1 36  ? 0.99096   33.47996 41.79182 1.000 73.54072  ? 43  ILE A CG2 1 
ATOM   228  C CD1 . ILE A 1 36  ? 3.60488   33.06506 39.26844 1.000 66.28157  ? 43  ILE A CD1 1 
ATOM   229  N N   . PHE A 1 37  ? 0.83102   30.50665 38.05297 1.000 62.82764  ? 44  PHE A N   1 
ATOM   230  C CA  . PHE A 1 37  ? 1.07721   30.16478 36.65540 1.000 61.55838  ? 44  PHE A CA  1 
ATOM   231  C C   . PHE A 1 37  ? -0.19448  30.28415 35.82451 1.000 59.41728  ? 44  PHE A C   1 
ATOM   232  O O   . PHE A 1 37  ? -0.14438  30.69343 34.65869 1.000 59.31046  ? 44  PHE A O   1 
ATOM   233  C CB  . PHE A 1 37  ? 1.65763   28.75277 36.55278 1.000 60.58886  ? 44  PHE A CB  1 
ATOM   234  C CG  . PHE A 1 37  ? 0.61893   27.66460 36.56784 1.000 52.97838  ? 44  PHE A CG  1 
ATOM   235  C CD1 . PHE A 1 37  ? 0.03278   27.26514 37.75642 1.000 54.51181  ? 44  PHE A CD1 1 
ATOM   236  C CD2 . PHE A 1 37  ? 0.22795   27.04287 35.39326 1.000 58.89338  ? 44  PHE A CD2 1 
ATOM   237  C CE1 . PHE A 1 37  ? -0.92258  26.26698 37.77531 1.000 59.54100  ? 44  PHE A CE1 1 
ATOM   238  C CE2 . PHE A 1 37  ? -0.72792  26.04461 35.40577 1.000 62.20866  ? 44  PHE A CE2 1 
ATOM   239  C CZ  . PHE A 1 37  ? -1.30337  25.65603 36.59855 1.000 53.71090  ? 44  PHE A CZ  1 
ATOM   240  N N   . LEU A 1 38  ? -1.34421  29.93365 36.40693 1.000 62.53539  ? 45  LEU A N   1 
ATOM   241  C CA  . LEU A 1 38  ? -2.59891  30.01431 35.66850 1.000 57.53416  ? 45  LEU A CA  1 
ATOM   242  C C   . LEU A 1 38  ? -2.99465  31.45754 35.39410 1.000 57.74705  ? 45  LEU A C   1 
ATOM   243  O O   . LEU A 1 38  ? -3.60274  31.74544 34.35757 1.000 56.17769  ? 45  LEU A O   1 
ATOM   244  C CB  . LEU A 1 38  ? -3.70823  29.29574 36.43548 1.000 54.72583  ? 45  LEU A CB  1 
ATOM   245  C CG  . LEU A 1 38  ? -4.85761  28.74965 35.58710 1.000 56.84154  ? 45  LEU A CG  1 
ATOM   246  C CD1 . LEU A 1 38  ? -4.32069  27.93399 34.42075 1.000 52.87676  ? 45  LEU A CD1 1 
ATOM   247  C CD2 . LEU A 1 38  ? -5.80573  27.91891 36.43698 1.000 56.63973  ? 45  LEU A CD2 1 
ATOM   248  N N   . ARG A 1 39  ? -2.66031  32.37292 36.30481 1.000 62.41259  ? 46  ARG A N   1 
ATOM   249  C CA  . ARG A 1 39  ? -2.96333  33.78207 36.08379 1.000 57.17418  ? 46  ARG A CA  1 
ATOM   250  C C   . ARG A 1 39  ? -2.17253  34.33791 34.90616 1.000 57.93997  ? 46  ARG A C   1 
ATOM   251  O O   . ARG A 1 39  ? -2.69400  35.14139 34.12406 1.000 63.88368  ? 46  ARG A O   1 
ATOM   252  C CB  . ARG A 1 39  ? -2.67590  34.57728 37.35700 1.000 67.71660  ? 46  ARG A CB  1 
ATOM   253  C CG  . ARG A 1 39  ? -2.23599  36.01165 37.12758 1.000 69.55689  ? 46  ARG A CG  1 
ATOM   254  C CD  . ARG A 1 39  ? -1.69956  36.62586 38.40943 1.000 69.31843  ? 46  ARG A CD  1 
ATOM   255  N NE  . ARG A 1 39  ? -0.24253  36.66363 38.42517 1.000 76.77890  ? 46  ARG A NE  1 
ATOM   256  C CZ  . ARG A 1 39  ? 0.49401   36.73311 39.52556 1.000 77.25980  ? 46  ARG A CZ  1 
ATOM   257  N NH1 . ARG A 1 39  ? -0.05932  36.77830 40.72651 1.000 78.47261  ? 46  ARG A NH1 1 
ATOM   258  N NH2 . ARG A 1 39  ? 1.81919   36.75596 39.41826 1.000 74.12681  ? 46  ARG A NH2 1 
ATOM   259  N N   . GLU A 1 40  ? -0.91658  33.91209 34.75587 1.000 53.22350  ? 47  GLU A N   1 
ATOM   260  C CA  . GLU A 1 40  ? -0.09154  34.41886 33.66462 1.000 55.06937  ? 47  GLU A CA  1 
ATOM   261  C C   . GLU A 1 40  ? -0.53250  33.84963 32.32193 1.000 57.95692  ? 47  GLU A C   1 
ATOM   262  O O   . GLU A 1 40  ? -0.60452  34.58021 31.32662 1.000 57.81836  ? 47  GLU A O   1 
ATOM   263  C CB  . GLU A 1 40  ? 1.37938   34.09875 33.92845 1.000 54.42876  ? 47  GLU A CB  1 
ATOM   264  C CG  . GLU A 1 40  ? 1.92296   34.69191 35.21899 1.000 59.55276  ? 47  GLU A CG  1 
ATOM   265  C CD  . GLU A 1 40  ? 1.50670   36.13733 35.42085 1.000 71.88670  ? 47  GLU A CD  1 
ATOM   266  O OE1 . GLU A 1 40  ? 1.63990   36.93756 34.47088 1.000 71.09725  ? 47  GLU A OE1 1 
ATOM   267  O OE2 . GLU A 1 40  ? 1.04747   36.47450 36.53153 1.000 74.11001  ? 47  GLU A OE2 1 
ATOM   268  N N   . LEU A 1 41  ? -0.82766  32.54833 32.27186 1.000 56.82161  ? 48  LEU A N   1 
ATOM   269  C CA  . LEU A 1 41  ? -1.25881  31.93966 31.01754 1.000 49.11065  ? 48  LEU A CA  1 
ATOM   270  C C   . LEU A 1 41  ? -2.60495  32.49451 30.56904 1.000 53.74784  ? 48  LEU A C   1 
ATOM   271  O O   . LEU A 1 41  ? -2.82846  32.70264 29.37075 1.000 59.51287  ? 48  LEU A O   1 
ATOM   272  C CB  . LEU A 1 41  ? -1.32366  30.41967 31.16504 1.000 44.87281  ? 48  LEU A CB  1 
ATOM   273  C CG  . LEU A 1 41  ? 0.01643   29.70485 31.35322 1.000 43.40327  ? 48  LEU A CG  1 
ATOM   274  C CD1 . LEU A 1 41  ? -0.15637  28.19496 31.26751 1.000 46.17543  ? 48  LEU A CD1 1 
ATOM   275  C CD2 . LEU A 1 41  ? 1.03545   30.19242 30.33428 1.000 52.39397  ? 48  LEU A CD2 1 
ATOM   276  N N   . ILE A 1 42  ? -3.51354  32.74077 31.51496 1.000 53.31254  ? 49  ILE A N   1 
ATOM   277  C CA  . ILE A 1 42  ? -4.79460  33.34700 31.16825 1.000 53.41880  ? 49  ILE A CA  1 
ATOM   278  C C   . ILE A 1 42  ? -4.59444  34.79340 30.73031 1.000 54.27962  ? 49  ILE A C   1 
ATOM   279  O O   . ILE A 1 42  ? -5.24703  35.26894 29.79272 1.000 53.01732  ? 49  ILE A O   1 
ATOM   280  C CB  . ILE A 1 42  ? -5.77489  33.23139 32.35067 1.000 58.42607  ? 49  ILE A CB  1 
ATOM   281  C CG1 . ILE A 1 42  ? -6.23975  31.78294 32.51349 1.000 53.26702  ? 49  ILE A CG1 1 
ATOM   282  C CG2 . ILE A 1 42  ? -6.97646  34.13957 32.15069 1.000 60.71097  ? 49  ILE A CG2 1 
ATOM   283  C CD1 . ILE A 1 42  ? -7.17296  31.56738 33.68516 1.000 51.49252  ? 49  ILE A CD1 1 
ATOM   284  N N   . SER A 1 43  ? -3.67930  35.51144 31.38829 1.000 50.20199  ? 50  SER A N   1 
ATOM   285  C CA  . SER A 1 43  ? -3.35643  36.86820 30.95675 1.000 49.68724  ? 50  SER A CA  1 
ATOM   286  C C   . SER A 1 43  ? -2.70772  36.86713 29.57789 1.000 55.12989  ? 50  SER A C   1 
ATOM   287  O O   . SER A 1 43  ? -2.95021  37.77246 28.77088 1.000 54.41347  ? 50  SER A O   1 
ATOM   288  C CB  . SER A 1 43  ? -2.44245  37.54430 31.97831 1.000 48.93706  ? 50  SER A CB  1 
ATOM   289  O OG  . SER A 1 43  ? -2.92131  37.35468 33.29804 1.000 68.93188  ? 50  SER A OG  1 
ATOM   290  N N   . ASN A 1 44  ? -1.87491  35.86222 29.29257 1.000 53.53888  ? 51  ASN A N   1 
ATOM   291  C CA  . ASN A 1 44  ? -1.30563  35.73173 27.95530 1.000 45.35346  ? 51  ASN A CA  1 
ATOM   292  C C   . ASN A 1 44  ? -2.39411  35.46554 26.92467 1.000 49.24301  ? 51  ASN A C   1 
ATOM   293  O O   . ASN A 1 44  ? -2.34054  35.98321 25.80281 1.000 52.00062  ? 51  ASN A O   1 
ATOM   294  C CB  . ASN A 1 44  ? -0.26409  34.61268 27.93301 1.000 45.63556  ? 51  ASN A CB  1 
ATOM   295  C CG  . ASN A 1 44  ? 1.06801   35.04191 28.51378 1.000 52.91203  ? 51  ASN A CG  1 
ATOM   296  O OD1 . ASN A 1 44  ? 1.36326   36.23291 28.60850 1.000 63.38362  ? 51  ASN A OD1 1 
ATOM   297  N ND2 . ASN A 1 44  ? 1.88232   34.06900 28.90612 1.000 59.25679  ? 51  ASN A ND2 1 
ATOM   298  N N   . SER A 1 45  ? -3.39116  34.65642 27.28895 1.000 50.88897  ? 52  SER A N   1 
ATOM   299  C CA  . SER A 1 45  ? -4.50959  34.40447 26.38753 1.000 48.20364  ? 52  SER A CA  1 
ATOM   300  C C   . SER A 1 45  ? -5.35065  35.65889 26.19057 1.000 50.21139  ? 52  SER A C   1 
ATOM   301  O O   . SER A 1 45  ? -5.86312  35.90369 25.09209 1.000 51.89275  ? 52  SER A O   1 
ATOM   302  C CB  . SER A 1 45  ? -5.36754  33.26139 26.92764 1.000 47.66001  ? 52  SER A CB  1 
ATOM   303  O OG  . SER A 1 45  ? -4.69719  32.01949 26.80358 1.000 54.61663  ? 52  SER A OG  1 
ATOM   304  N N   . SER A 1 46  ? -5.50555  36.46436 27.24457 1.000 47.88246  ? 53  SER A N   1 
ATOM   305  C CA  . SER A 1 46  ? -6.25229  37.71080 27.11869 1.000 49.70233  ? 53  SER A CA  1 
ATOM   306  C C   . SER A 1 46  ? -5.53952  38.70071 26.20713 1.000 53.99923  ? 53  SER A C   1 
ATOM   307  O O   . SER A 1 46  ? -6.19616  39.47503 25.50138 1.000 50.78401  ? 53  SER A O   1 
ATOM   308  C CB  . SER A 1 46  ? -6.48164  38.32789 28.49817 1.000 56.30688  ? 53  SER A CB  1 
ATOM   309  O OG  . SER A 1 46  ? -6.83443  39.69619 28.39139 1.000 68.05807  ? 53  SER A OG  1 
ATOM   310  N N   . ASP A 1 47  ? -4.20442  38.69266 26.20765 1.000 56.27449  ? 54  ASP A N   1 
ATOM   311  C CA  . ASP A 1 47  ? -3.46214  39.55994 25.29909 1.000 51.78120  ? 54  ASP A CA  1 
ATOM   312  C C   . ASP A 1 47  ? -3.60913  39.09697 23.85570 1.000 50.49188  ? 54  ASP A C   1 
ATOM   313  O O   . ASP A 1 47  ? -3.73194  39.92154 22.94240 1.000 51.09201  ? 54  ASP A O   1 
ATOM   314  C CB  . ASP A 1 47  ? -1.98809  39.60353 25.69988 1.000 61.56313  ? 54  ASP A CB  1 
ATOM   315  C CG  . ASP A 1 47  ? -1.75318  40.39321 26.97101 1.000 65.65277  ? 54  ASP A CG  1 
ATOM   316  O OD1 . ASP A 1 47  ? -2.66698  41.13536 27.38869 1.000 73.14674  ? 54  ASP A OD1 1 
ATOM   317  O OD2 . ASP A 1 47  ? -0.65452  40.27175 27.55256 1.000 64.56195  ? 54  ASP A OD2 1 
ATOM   318  N N   . ALA A 1 48  ? -3.59643  37.78059 23.63054 1.000 51.50067  ? 55  ALA A N   1 
ATOM   319  C CA  . ALA A 1 48  ? -3.77068  37.25987 22.27965 1.000 48.89663  ? 55  ALA A CA  1 
ATOM   320  C C   . ALA A 1 48  ? -5.16527  37.54922 21.74189 1.000 51.62354  ? 55  ALA A C   1 
ATOM   321  O O   . ALA A 1 48  ? -5.32787  37.78108 20.53852 1.000 56.31788  ? 55  ALA A O   1 
ATOM   322  C CB  . ALA A 1 48  ? -3.49258  35.75741 22.25465 1.000 49.97679  ? 55  ALA A CB  1 
ATOM   323  N N   . LEU A 1 49  ? -6.17913  37.54067 22.61016 1.000 47.77012  ? 56  LEU A N   1 
ATOM   324  C CA  . LEU A 1 49  ? -7.52985  37.86125 22.16417 1.000 44.09509  ? 56  LEU A CA  1 
ATOM   325  C C   . LEU A 1 49  ? -7.69873  39.35466 21.92137 1.000 47.08456  ? 56  LEU A C   1 
ATOM   326  O O   . LEU A 1 49  ? -8.45760  39.75340 21.03080 1.000 46.65758  ? 56  LEU A O   1 
ATOM   327  C CB  . LEU A 1 49  ? -8.55225  37.36845 23.18641 1.000 50.77667  ? 56  LEU A CB  1 
ATOM   328  C CG  . LEU A 1 49  ? -8.66137  35.85222 23.35137 1.000 48.77311  ? 56  LEU A CG  1 
ATOM   329  C CD1 . LEU A 1 49  ? -9.26138  35.50858 24.70279 1.000 46.00412  ? 56  LEU A CD1 1 
ATOM   330  C CD2 . LEU A 1 49  ? -9.48430  35.24649 22.22643 1.000 48.52676  ? 56  LEU A CD2 1 
ATOM   331  N N   . ASP A 1 50  ? -7.00720  40.19197 22.69927 1.000 52.72275  ? 57  ASP A N   1 
ATOM   332  C CA  . ASP A 1 50  ? -7.04996  41.62985 22.45550 1.000 52.44240  ? 57  ASP A CA  1 
ATOM   333  C C   . ASP A 1 50  ? -6.43085  41.98557 21.11129 1.000 52.78773  ? 57  ASP A C   1 
ATOM   334  O O   . ASP A 1 50  ? -6.88302  42.92662 20.44931 1.000 57.72837  ? 57  ASP A O   1 
ATOM   335  C CB  . ASP A 1 50  ? -6.33298  42.37933 23.57991 1.000 50.07901  ? 57  ASP A CB  1 
ATOM   336  C CG  . ASP A 1 50  ? -7.17600  42.49796 24.83381 1.000 56.65582  ? 57  ASP A CG  1 
ATOM   337  O OD1 . ASP A 1 50  ? -8.40929  42.32517 24.74083 1.000 63.98761  ? 57  ASP A OD1 1 
ATOM   338  O OD2 . ASP A 1 50  ? -6.60500  42.76516 25.91299 1.000 54.44352  ? 57  ASP A OD2 1 
ATOM   339  N N   . LYS A 1 51  ? -5.40431  41.24441 20.68904 1.000 52.26301  ? 58  LYS A N   1 
ATOM   340  C CA  . LYS A 1 51  ? -4.73805  41.54990 19.42735 1.000 57.53526  ? 58  LYS A CA  1 
ATOM   341  C C   . LYS A 1 51  ? -5.63216  41.22207 18.23733 1.000 57.78468  ? 58  LYS A C   1 
ATOM   342  O O   . LYS A 1 51  ? -5.83494  42.06104 17.35244 1.000 68.26284  ? 58  LYS A O   1 
ATOM   343  C CB  . LYS A 1 51  ? -3.41477  40.78860 19.33520 1.000 59.22597  ? 58  LYS A CB  1 
ATOM   344  C CG  . LYS A 1 51  ? -2.26330  41.46046 20.06693 1.000 62.44968  ? 58  LYS A CG  1 
ATOM   345  C CD  . LYS A 1 51  ? -0.92780  41.15428 19.40840 1.000 75.99173  ? 58  LYS A CD  1 
ATOM   346  C CE  . LYS A 1 51  ? -0.87053  41.70417 17.99200 1.000 74.46680  ? 58  LYS A CE  1 
ATOM   347  N NZ  . LYS A 1 51  ? 0.32760   41.21442 17.25550 1.000 63.18356  ? 58  LYS A NZ  1 
ATOM   348  N N   . ILE A 1 52  ? -6.18275  40.00575 18.20152 1.000 53.23042  ? 59  ILE A N   1 
ATOM   349  C CA  . ILE A 1 52  ? -6.98385  39.59394 17.05232 1.000 60.98769  ? 59  ILE A CA  1 
ATOM   350  C C   . ILE A 1 52  ? -8.27014  40.40721 16.96044 1.000 56.81180  ? 59  ILE A C   1 
ATOM   351  O O   . ILE A 1 52  ? -8.74724  40.70082 15.85717 1.000 56.22674  ? 59  ILE A O   1 
ATOM   352  C CB  . ILE A 1 52  ? -7.26602  38.07900 17.10805 1.000 56.80302  ? 59  ILE A CB  1 
ATOM   353  C CG1 . ILE A 1 52  ? -7.90569  37.60438 15.80080 1.000 50.20906  ? 59  ILE A CG1 1 
ATOM   354  C CG2 . ILE A 1 52  ? -8.13884  37.72219 18.30604 1.000 48.25384  ? 59  ILE A CG2 1 
ATOM   355  C CD1 . ILE A 1 52  ? -7.12269  37.98619 14.56231 1.000 47.25940  ? 59  ILE A CD1 1 
ATOM   356  N N   . ARG A 1 53  ? -8.84919  40.79310 18.10047 1.000 53.87787  ? 60  ARG A N   1 
ATOM   357  C CA  . ARG A 1 53  ? -10.02812 41.65074 18.06639 1.000 52.19399  ? 60  ARG A CA  1 
ATOM   358  C C   . ARG A 1 53  ? -9.67599  43.05432 17.59618 1.000 58.55819  ? 60  ARG A C   1 
ATOM   359  O O   . ARG A 1 53  ? -10.49517 43.71761 16.94998 1.000 62.60237  ? 60  ARG A O   1 
ATOM   360  C CB  . ARG A 1 53  ? -10.68649 41.70020 19.44574 1.000 51.15744  ? 60  ARG A CB  1 
ATOM   361  C CG  . ARG A 1 53  ? -12.00585 42.45688 19.47664 1.000 53.52597  ? 60  ARG A CG  1 
ATOM   362  C CD  . ARG A 1 53  ? -12.82940 42.09439 20.70110 1.000 62.73720  ? 60  ARG A CD  1 
ATOM   363  N NE  . ARG A 1 53  ? -12.56960 42.98806 21.82318 1.000 70.70311  ? 60  ARG A NE  1 
ATOM   364  C CZ  . ARG A 1 53  ? -13.24438 44.10420 22.06252 1.000 73.66758  ? 60  ARG A CZ  1 
ATOM   365  N NH1 . ARG A 1 53  ? -14.22553 44.50271 21.26903 1.000 62.12379  ? 60  ARG A NH1 1 
ATOM   366  N NH2 . ARG A 1 53  ? -12.92732 44.83876 23.12485 1.000 72.13478  ? 60  ARG A NH2 1 
ATOM   367  N N   . TYR A 1 54  ? -8.46381  43.51716 17.90058 1.000 58.50480  ? 61  TYR A N   1 
ATOM   368  C CA  . TYR A 1 54  ? -8.05134  44.84541 17.46581 1.000 59.27894  ? 61  TYR A CA  1 
ATOM   369  C C   . TYR A 1 54  ? -7.77326  44.87739 15.96726 1.000 58.79730  ? 61  TYR A C   1 
ATOM   370  O O   . TYR A 1 54  ? -8.09243  45.86328 15.29270 1.000 61.98001  ? 61  TYR A O   1 
ATOM   371  C CB  . TYR A 1 54  ? -6.82357  45.28666 18.25709 1.000 58.67661  ? 61  TYR A CB  1 
ATOM   372  C CG  . TYR A 1 54  ? -6.21167  46.57260 17.76736 1.000 62.96435  ? 61  TYR A CG  1 
ATOM   373  C CD1 . TYR A 1 54  ? -4.96174  46.57483 17.16852 1.000 63.94301  ? 61  TYR A CD1 1 
ATOM   374  C CD2 . TYR A 1 54  ? -6.87665  47.78429 17.90720 1.000 66.66678  ? 61  TYR A CD2 1 
ATOM   375  C CE1 . TYR A 1 54  ? -4.38912  47.74074 16.71747 1.000 68.47720  ? 61  TYR A CE1 1 
ATOM   376  C CE2 . TYR A 1 54  ? -6.30882  48.96276 17.45775 1.000 71.10817  ? 61  TYR A CE2 1 
ATOM   377  C CZ  . TYR A 1 54  ? -5.06294  48.93040 16.86316 1.000 71.98164  ? 61  TYR A CZ  1 
ATOM   378  O OH  . TYR A 1 54  ? -4.47557  50.08489 16.40779 1.000 76.96923  ? 61  TYR A OH  1 
ATOM   379  N N   . GLU A 1 55  ? -7.18272  43.80801 15.42693 1.000 61.86191  ? 62  GLU A N   1 
ATOM   380  C CA  . GLU A 1 55  ? -6.91544  43.76008 13.99312 1.000 62.56964  ? 62  GLU A CA  1 
ATOM   381  C C   . GLU A 1 55  ? -8.19942  43.62110 13.18555 1.000 65.34125  ? 62  GLU A C   1 
ATOM   382  O O   . GLU A 1 55  ? -8.27725  44.12088 12.05720 1.000 65.59137  ? 62  GLU A O   1 
ATOM   383  C CB  . GLU A 1 55  ? -5.96136  42.60900 13.67213 1.000 65.64166  ? 62  GLU A CB  1 
ATOM   384  C CG  . GLU A 1 55  ? -4.67498  42.61739 14.48175 1.000 70.92014  ? 62  GLU A CG  1 
ATOM   385  C CD  . GLU A 1 55  ? -3.43575  42.59000 13.61083 1.000 94.84171  ? 62  GLU A CD  1 
ATOM   386  O OE1 . GLU A 1 55  ? -2.97860  41.48094 13.26228 1.000 92.93057  ? 62  GLU A OE1 1 
ATOM   387  O OE2 . GLU A 1 55  ? -2.91719  43.67580 13.27683 1.000 120.61129 ? 62  GLU A OE2 1 
ATOM   388  N N   . SER A 1 56  ? -9.21307  42.95360 13.74180 1.000 63.06956  ? 63  SER A N   1 
ATOM   389  C CA  . SER A 1 56  ? -10.47409 42.78336 13.03046 1.000 59.99151  ? 63  SER A CA  1 
ATOM   390  C C   . SER A 1 56  ? -11.26147 44.08215 12.92500 1.000 64.13894  ? 63  SER A C   1 
ATOM   391  O O   . SER A 1 56  ? -12.18859 44.16477 12.11215 1.000 71.59185  ? 63  SER A O   1 
ATOM   392  C CB  . SER A 1 56  ? -11.32594 41.71483 13.71668 1.000 57.59643  ? 63  SER A CB  1 
ATOM   393  O OG  . SER A 1 56  ? -11.76049 42.14835 14.99355 1.000 55.11046  ? 63  SER A OG  1 
ATOM   394  N N   . LEU A 1 57  ? -10.91722 45.09346 13.72592 1.000 63.23671  ? 64  LEU A N   1 
ATOM   395  C CA  . LEU A 1 57  ? -11.61282 46.37229 13.65629 1.000 65.68905  ? 64  LEU A CA  1 
ATOM   396  C C   . LEU A 1 57  ? -11.34441 47.10257 12.34729 1.000 68.74714  ? 64  LEU A C   1 
ATOM   397  O O   . LEU A 1 57  ? -12.16575 47.92705 11.93198 1.000 71.82250  ? 64  LEU A O   1 
ATOM   398  C CB  . LEU A 1 57  ? -11.21240 47.24913 14.84359 1.000 67.32507  ? 64  LEU A CB  1 
ATOM   399  C CG  . LEU A 1 57  ? -11.71419 46.76729 16.20773 1.000 65.20322  ? 64  LEU A CG  1 
ATOM   400  C CD1 . LEU A 1 57  ? -10.91924 47.40323 17.33708 1.000 67.29633  ? 64  LEU A CD1 1 
ATOM   401  C CD2 . LEU A 1 57  ? -13.20070 47.04859 16.36872 1.000 71.34116  ? 64  LEU A CD2 1 
ATOM   402  N N   . THR A 1 58  ? -10.21851 46.82108 11.69299 1.000 66.03115  ? 65  THR A N   1 
ATOM   403  C CA  . THR A 1 58  ? -9.91439  47.36762 10.37850 1.000 66.66471  ? 65  THR A CA  1 
ATOM   404  C C   . THR A 1 58  ? -9.87925  46.29912 9.29518  1.000 68.11551  ? 65  THR A C   1 
ATOM   405  O O   . THR A 1 58  ? -9.59780  46.61927 8.13537  1.000 73.12204  ? 65  THR A O   1 
ATOM   406  C CB  . THR A 1 58  ? -8.57624  48.11743 10.40734 1.000 66.68908  ? 65  THR A CB  1 
ATOM   407  O OG1 . THR A 1 58  ? -7.51186  47.19287 10.66373 1.000 82.58420  ? 65  THR A OG1 1 
ATOM   408  C CG2 . THR A 1 58  ? -8.58623  49.18721 11.49091 1.000 68.94094  ? 65  THR A CG2 1 
ATOM   409  N N   . ASP A 1 59  ? -10.15552 45.04251 9.64146  1.000 75.72244  ? 66  ASP A N   1 
ATOM   410  C CA  . ASP A 1 59  ? -10.17831 43.94225 8.68680  1.000 73.38775  ? 66  ASP A CA  1 
ATOM   411  C C   . ASP A 1 59  ? -11.02438 42.80405 9.24545  1.000 74.54681  ? 66  ASP A C   1 
ATOM   412  O O   . ASP A 1 59  ? -10.48714 41.87870 9.86805  1.000 76.05454  ? 66  ASP A O   1 
ATOM   413  C CB  . ASP A 1 59  ? -8.75837  43.45939 8.38209  1.000 77.70333  ? 66  ASP A CB  1 
ATOM   414  C CG  . ASP A 1 59  ? -8.67422  42.65872 7.09384  1.000 82.89722  ? 66  ASP A CG  1 
ATOM   415  O OD1 . ASP A 1 59  ? -9.67066  42.00190 6.72588  1.000 84.07384  ? 66  ASP A OD1 1 
ATOM   416  O OD2 . ASP A 1 59  ? -7.60602  42.68650 6.44702  1.000 83.16571  ? 66  ASP A OD2 1 
ATOM   417  N N   . PRO A 1 60  ? -12.34517 42.83603 9.04938  1.000 74.13020  ? 67  PRO A N   1 
ATOM   418  C CA  . PRO A 1 60  ? -13.19204 41.75255 9.57724  1.000 71.08557  ? 67  PRO A CA  1 
ATOM   419  C C   . PRO A 1 60  ? -12.90116 40.39346 8.96461  1.000 67.68155  ? 67  PRO A C   1 
ATOM   420  O O   . PRO A 1 60  ? -13.34514 39.37786 9.51459  1.000 66.29519  ? 67  PRO A O   1 
ATOM   421  C CB  . PRO A 1 60  ? -14.61534 42.22260 9.24198  1.000 67.48522  ? 67  PRO A CB  1 
ATOM   422  C CG  . PRO A 1 60  ? -14.49589 43.70280 9.04253  1.000 68.73437  ? 67  PRO A CG  1 
ATOM   423  C CD  . PRO A 1 60  ? -13.14136 43.91350 8.44004  1.000 68.93521  ? 67  PRO A CD  1 
ATOM   424  N N   . SER A 1 61  ? -12.17371 40.33713 7.84574  1.000 69.75259  ? 68  SER A N   1 
ATOM   425  C CA  . SER A 1 61  ? -11.83901 39.05441 7.23893  1.000 72.61665  ? 68  SER A CA  1 
ATOM   426  C C   . SER A 1 61  ? -10.85044 38.25787 8.07919  1.000 68.43551  ? 68  SER A C   1 
ATOM   427  O O   . SER A 1 61  ? -10.70013 37.05161 7.85808  1.000 77.70011  ? 68  SER A O   1 
ATOM   428  C CB  . SER A 1 61  ? -11.27329 39.26558 5.83393  1.000 78.40133  ? 68  SER A CB  1 
ATOM   429  O OG  . SER A 1 61  ? -9.94201  39.74814 5.88648  1.000 77.63296  ? 68  SER A OG  1 
ATOM   430  N N   . LYS A 1 62  ? -10.17225 38.90191 9.03224  1.000 65.85334  ? 69  LYS A N   1 
ATOM   431  C CA  . LYS A 1 62  ? -9.26278  38.18198 9.91427  1.000 59.68054  ? 69  LYS A CA  1 
ATOM   432  C C   . LYS A 1 62  ? -10.00130 37.24988 10.86438 1.000 63.32566  ? 69  LYS A C   1 
ATOM   433  O O   . LYS A 1 62  ? -9.38367  36.33531 11.42008 1.000 68.82480  ? 69  LYS A O   1 
ATOM   434  C CB  . LYS A 1 62  ? -8.40851  39.16898 10.71174 1.000 55.60576  ? 69  LYS A CB  1 
ATOM   435  C CG  . LYS A 1 62  ? -7.63490  40.15572 9.85271  1.000 62.07148  ? 69  LYS A CG  1 
ATOM   436  C CD  . LYS A 1 62  ? -6.40814  40.67991 10.58079 1.000 55.74802  ? 69  LYS A CD  1 
ATOM   437  C CE  . LYS A 1 62  ? -5.48069  41.41905 9.63125  1.000 60.11397  ? 69  LYS A CE  1 
ATOM   438  N NZ  . LYS A 1 62  ? -4.07715  40.93466 9.73760  1.000 70.36020  ? 69  LYS A NZ  1 
ATOM   439  N N   . LEU A 1 63  ? -11.30086 37.45958 11.06234 1.000 59.76466  ? 70  LEU A N   1 
ATOM   440  C CA  . LEU A 1 63  ? -12.11382 36.60731 11.91700 1.000 56.59081  ? 70  LEU A CA  1 
ATOM   441  C C   . LEU A 1 63  ? -12.79949 35.48566 11.14845 1.000 61.84877  ? 70  LEU A C   1 
ATOM   442  O O   . LEU A 1 63  ? -13.64899 34.79209 11.71723 1.000 66.80444  ? 70  LEU A O   1 
ATOM   443  C CB  . LEU A 1 63  ? -13.16039 37.44555 12.65561 1.000 54.91514  ? 70  LEU A CB  1 
ATOM   444  C CG  . LEU A 1 63  ? -12.63966 38.31784 13.79940 1.000 52.18845  ? 70  LEU A CG  1 
ATOM   445  C CD1 . LEU A 1 63  ? -13.78915 38.84119 14.64602 1.000 53.51268  ? 70  LEU A CD1 1 
ATOM   446  C CD2 . LEU A 1 63  ? -11.64647 37.54804 14.65595 1.000 55.14653  ? 70  LEU A CD2 1 
ATOM   447  N N   . ASP A 1 64  ? -12.45550 35.29542 9.87145  1.000 66.33782  ? 71  ASP A N   1 
ATOM   448  C CA  . ASP A 1 64  ? -13.02929 34.19058 9.11077  1.000 72.03979  ? 71  ASP A CA  1 
ATOM   449  C C   . ASP A 1 64  ? -12.60531 32.84385 9.68039  1.000 71.56721  ? 71  ASP A C   1 
ATOM   450  O O   . ASP A 1 64  ? -13.31942 31.84778 9.51784  1.000 75.60526  ? 71  ASP A O   1 
ATOM   451  C CB  . ASP A 1 64  ? -12.62650 34.29690 7.63946  1.000 77.34538  ? 71  ASP A CB  1 
ATOM   452  C CG  . ASP A 1 64  ? -13.23968 35.50172 6.95260  1.000 79.47629  ? 71  ASP A CG  1 
ATOM   453  O OD1 . ASP A 1 64  ? -14.26072 36.01762 7.45406  1.000 78.39585  ? 71  ASP A OD1 1 
ATOM   454  O OD2 . ASP A 1 64  ? -12.70249 35.93114 5.90960  1.000 82.82907  ? 71  ASP A OD2 1 
ATOM   455  N N   . SER A 1 65  ? -11.45533 32.79325 10.34951 1.000 67.32088  ? 72  SER A N   1 
ATOM   456  C CA  . SER A 1 65  ? -10.98422 31.58355 11.00906 1.000 66.74932  ? 72  SER A CA  1 
ATOM   457  C C   . SER A 1 65  ? -11.59194 31.39163 12.39261 1.000 63.16097  ? 72  SER A C   1 
ATOM   458  O O   . SER A 1 65  ? -11.10414 30.55160 13.15609 1.000 64.01539  ? 72  SER A O   1 
ATOM   459  C CB  . SER A 1 65  ? -9.45689  31.60348 11.11353 1.000 64.63125  ? 72  SER A CB  1 
ATOM   460  O OG  . SER A 1 65  ? -8.98819  32.88628 11.49271 1.000 63.17356  ? 72  SER A OG  1 
ATOM   461  N N   . GLY A 1 66  ? -12.63550 32.14490 12.73078 1.000 62.12456  ? 73  GLY A N   1 
ATOM   462  C CA  . GLY A 1 66  ? -13.26456 32.03327 14.03126 1.000 59.53745  ? 73  GLY A CA  1 
ATOM   463  C C   . GLY A 1 66  ? -13.70236 33.36992 14.59252 1.000 56.87151  ? 73  GLY A C   1 
ATOM   464  O O   . GLY A 1 66  ? -12.88985 34.28914 14.73010 1.000 60.01075  ? 73  GLY A O   1 
ATOM   465  N N   . LYS A 1 67  ? -14.98835 33.49153 14.91944 1.000 68.49019  ? 74  LYS A N   1 
ATOM   466  C CA  . LYS A 1 67  ? -15.51563 34.72641 15.48540 1.000 64.71068  ? 74  LYS A CA  1 
ATOM   467  C C   . LYS A 1 67  ? -15.54301 34.71393 17.00667 1.000 67.50427  ? 74  LYS A C   1 
ATOM   468  O O   . LYS A 1 67  ? -15.44767 35.77901 17.62754 1.000 64.75018  ? 74  LYS A O   1 
ATOM   469  C CB  . LYS A 1 67  ? -16.92751 34.99096 14.95491 1.000 71.66351  ? 74  LYS A CB  1 
ATOM   470  C CG  . LYS A 1 67  ? -16.98388 35.99822 13.81994 1.000 66.92972  ? 74  LYS A CG  1 
ATOM   471  C CD  . LYS A 1 67  ? -17.87619 35.50900 12.69266 1.000 83.52534  ? 74  LYS A CD  1 
ATOM   472  C CE  . LYS A 1 67  ? -17.43725 36.08400 11.35649 1.000 85.58331  ? 74  LYS A CE  1 
ATOM   473  N NZ  . LYS A 1 67  ? -18.01160 35.32480 10.21194 1.000 97.94154  ? 74  LYS A NZ  1 
ATOM   474  N N   . GLU A 1 68  ? -15.67104 33.53961 17.62007 1.000 59.73078  ? 75  GLU A N   1 
ATOM   475  C CA  . GLU A 1 68  ? -15.73167 33.45639 19.07292 1.000 54.72489  ? 75  GLU A CA  1 
ATOM   476  C C   . GLU A 1 68  ? -14.36978 33.76633 19.68181 1.000 54.56772  ? 75  GLU A C   1 
ATOM   477  O O   . GLU A 1 68  ? -13.33934 33.26610 19.21953 1.000 48.64798  ? 75  GLU A O   1 
ATOM   478  C CB  . GLU A 1 68  ? -16.19834 32.06892 19.51081 1.000 55.98826  ? 75  GLU A CB  1 
ATOM   479  C CG  . GLU A 1 68  ? -16.98638 31.30453 18.46226 1.000 66.64911  ? 75  GLU A CG  1 
ATOM   480  C CD  . GLU A 1 68  ? -17.45458 29.95179 18.96500 1.000 82.72172  ? 75  GLU A CD  1 
ATOM   481  O OE1 . GLU A 1 68  ? -18.43198 29.91113 19.74149 1.000 83.82959  ? 75  GLU A OE1 1 
ATOM   482  O OE2 . GLU A 1 68  ? -16.84446 28.92946 18.58624 1.000 81.94021  ? 75  GLU A OE2 1 
ATOM   483  N N   . LEU A 1 69  ? -14.36990 34.59232 20.72393 1.000 50.56127  ? 76  LEU A N   1 
ATOM   484  C CA  . LEU A 1 69  ? -13.16229 34.95793 21.46014 1.000 47.56675  ? 76  LEU A CA  1 
ATOM   485  C C   . LEU A 1 69  ? -13.37240 34.53751 22.91117 1.000 49.41593  ? 76  LEU A C   1 
ATOM   486  O O   . LEU A 1 69  ? -14.07587 35.21705 23.66537 1.000 47.86871  ? 76  LEU A O   1 
ATOM   487  C CB  . LEU A 1 69  ? -12.87933 36.45223 21.33979 1.000 41.11361  ? 76  LEU A CB  1 
ATOM   488  C CG  . LEU A 1 69  ? -12.93247 37.02477 19.92177 1.000 36.91670  ? 76  LEU A CG  1 
ATOM   489  C CD1 . LEU A 1 69  ? -12.68491 38.52359 19.93628 1.000 38.65432  ? 76  LEU A CD1 1 
ATOM   490  C CD2 . LEU A 1 69  ? -11.92892 36.32161 19.02134 1.000 41.43496  ? 76  LEU A CD2 1 
ATOM   491  N N   . HIS A 1 70  ? -12.76915 33.41636 23.30048 1.000 48.04148  ? 77  HIS A N   1 
ATOM   492  C CA  . HIS A 1 70  ? -12.96880 32.86961 24.63380 1.000 48.34512  ? 77  HIS A CA  1 
ATOM   493  C C   . HIS A 1 70  ? -11.69057 32.18801 25.10060 1.000 47.37193  ? 77  HIS A C   1 
ATOM   494  O O   . HIS A 1 70  ? -10.71958 32.05279 24.35181 1.000 46.67996  ? 77  HIS A O   1 
ATOM   495  C CB  . HIS A 1 70  ? -14.15475 31.89442 24.66309 1.000 45.97212  ? 77  HIS A CB  1 
ATOM   496  C CG  . HIS A 1 70  ? -14.09596 30.82848 23.61128 1.000 40.36916  ? 77  HIS A CG  1 
ATOM   497  N ND1 . HIS A 1 70  ? -12.93028 30.17641 23.27140 1.000 46.02309  ? 77  HIS A ND1 1 
ATOM   498  C CD2 . HIS A 1 70  ? -15.06171 30.30774 22.81741 1.000 45.43903  ? 77  HIS A CD2 1 
ATOM   499  C CE1 . HIS A 1 70  ? -13.18077 29.29706 22.31813 1.000 47.19593  ? 77  HIS A CE1 1 
ATOM   500  N NE2 . HIS A 1 70  ? -14.46667 29.35754 22.02358 1.000 40.73921  ? 77  HIS A NE2 1 
ATOM   501  N N   . ILE A 1 71  ? -11.70575 31.76089 26.36096 1.000 48.93888  ? 78  ILE A N   1 
ATOM   502  C CA  . ILE A 1 71  ? -10.61858 31.00085 26.96436 1.000 47.17013  ? 78  ILE A CA  1 
ATOM   503  C C   . ILE A 1 71  ? -11.21746 29.75404 27.59750 1.000 50.51036  ? 78  ILE A C   1 
ATOM   504  O O   . ILE A 1 71  ? -12.19991 29.84415 28.34209 1.000 51.11983  ? 78  ILE A O   1 
ATOM   505  C CB  . ILE A 1 71  ? -9.85112  31.82585 28.01532 1.000 44.76993  ? 78  ILE A CB  1 
ATOM   506  C CG1 . ILE A 1 71  ? -9.26283  33.08727 27.38179 1.000 44.97974  ? 78  ILE A CG1 1 
ATOM   507  C CG2 . ILE A 1 71  ? -8.75422  30.98868 28.65353 1.000 45.86336  ? 78  ILE A CG2 1 
ATOM   508  C CD1 . ILE A 1 71  ? -8.77661  34.10568 28.38752 1.000 40.75570  ? 78  ILE A CD1 1 
ATOM   509  N N   . ASN A 1 72  ? -10.63418 28.59546 27.29975 1.000 45.96978  ? 79  ASN A N   1 
ATOM   510  C CA  . ASN A 1 72  ? -11.11596 27.31859 27.80877 1.000 48.73858  ? 79  ASN A CA  1 
ATOM   511  C C   . ASN A 1 72  ? -10.02035 26.64495 28.62208 1.000 48.29561  ? 79  ASN A C   1 
ATOM   512  O O   . ASN A 1 72  ? -8.86300  26.59287 28.19202 1.000 50.13156  ? 79  ASN A O   1 
ATOM   513  C CB  . ASN A 1 72  ? -11.56864 26.40386 26.66655 1.000 45.58877  ? 79  ASN A CB  1 
ATOM   514  C CG  . ASN A 1 72  ? -12.88586 26.84221 26.05611 1.000 50.33110  ? 79  ASN A CG  1 
ATOM   515  O OD1 . ASN A 1 72  ? -13.63493 27.61237 26.65715 1.000 52.48777  ? 79  ASN A OD1 1 
ATOM   516  N ND2 . ASN A 1 72  ? -13.17675 26.35005 24.85634 1.000 41.91905  ? 79  ASN A ND2 1 
ATOM   517  N N   . LEU A 1 73  ? -10.38954 26.13434 29.79356 1.000 45.89575  ? 80  LEU A N   1 
ATOM   518  C CA  . LEU A 1 73  ? -9.48603  25.39378 30.66462 1.000 45.81197  ? 80  LEU A CA  1 
ATOM   519  C C   . LEU A 1 73  ? -9.95163  23.94475 30.71277 1.000 51.06858  ? 80  LEU A C   1 
ATOM   520  O O   . LEU A 1 73  ? -11.04554 23.65942 31.21217 1.000 55.46931  ? 80  LEU A O   1 
ATOM   521  C CB  . LEU A 1 73  ? -9.45445  26.00076 32.06707 1.000 47.72341  ? 80  LEU A CB  1 
ATOM   522  C CG  . LEU A 1 73  ? -9.38901  27.52814 32.14106 1.000 46.61430  ? 80  LEU A CG  1 
ATOM   523  C CD1 . LEU A 1 73  ? -9.40061  27.99634 33.58774 1.000 53.70540  ? 80  LEU A CD1 1 
ATOM   524  C CD2 . LEU A 1 73  ? -8.16183  28.05071 31.41370 1.000 45.09670  ? 80  LEU A CD2 1 
ATOM   525  N N   . ILE A 1 74  ? -9.12952  23.04179 30.19963 1.000 55.74943  ? 81  ILE A N   1 
ATOM   526  C CA  . ILE A 1 74  ? -9.48914  21.63864 30.03725 1.000 51.60687  ? 81  ILE A CA  1 
ATOM   527  C C   . ILE A 1 74  ? -8.49971  20.79061 30.82536 1.000 51.84281  ? 81  ILE A C   1 
ATOM   528  O O   . ILE A 1 74  ? -7.41352  20.47048 30.33710 1.000 53.27710  ? 81  ILE A O   1 
ATOM   529  C CB  . ILE A 1 74  ? -9.51206  21.23201 28.55455 1.000 41.31144  ? 81  ILE A CB  1 
ATOM   530  C CG1 . ILE A 1 74  ? -10.37046 22.20807 27.74755 1.000 44.82413  ? 81  ILE A CG1 1 
ATOM   531  C CG2 . ILE A 1 74  ? -10.02300 19.80806 28.40220 1.000 47.31145  ? 81  ILE A CG2 1 
ATOM   532  C CD1 . ILE A 1 74  ? -10.09593 22.18097 26.26234 1.000 50.77762  ? 81  ILE A CD1 1 
ATOM   533  N N   . PRO A 1 75  ? -8.83682  20.40595 32.05126 1.000 52.78293  ? 82  PRO A N   1 
ATOM   534  C CA  . PRO A 1 75  ? -7.99457  19.46306 32.78880 1.000 48.22346  ? 82  PRO A CA  1 
ATOM   535  C C   . PRO A 1 75  ? -8.28615  18.02383 32.39442 1.000 54.89635  ? 82  PRO A C   1 
ATOM   536  O O   . PRO A 1 75  ? -9.41357  17.65798 32.05389 1.000 55.04649  ? 82  PRO A O   1 
ATOM   537  C CB  . PRO A 1 75  ? -8.37666  19.72241 34.24995 1.000 53.85483  ? 82  PRO A CB  1 
ATOM   538  C CG  . PRO A 1 75  ? -9.79979  20.16446 34.17695 1.000 60.08244  ? 82  PRO A CG  1 
ATOM   539  C CD  . PRO A 1 75  ? -9.95798  20.90555 32.86803 1.000 56.62890  ? 82  PRO A CD  1 
ATOM   540  N N   . ASN A 1 76  ? -7.23954  17.20233 32.44509 1.000 58.62266  ? 83  ASN A N   1 
ATOM   541  C CA  . ASN A 1 76  ? -7.33965  15.78433 32.10759 1.000 55.19868  ? 83  ASN A CA  1 
ATOM   542  C C   . ASN A 1 76  ? -6.56584  14.99862 33.15591 1.000 60.67343  ? 83  ASN A C   1 
ATOM   543  O O   . ASN A 1 76  ? -5.33385  15.06485 33.19780 1.000 67.16514  ? 83  ASN A O   1 
ATOM   544  C CB  . ASN A 1 76  ? -6.79902  15.50762 30.70403 1.000 54.26476  ? 83  ASN A CB  1 
ATOM   545  C CG  . ASN A 1 76  ? -7.23257  14.15644 30.16479 1.000 58.59609  ? 83  ASN A CG  1 
ATOM   546  O OD1 . ASN A 1 76  ? -7.15545  13.14168 30.85741 1.000 64.96612  ? 83  ASN A OD1 1 
ATOM   547  N ND2 . ASN A 1 76  ? -7.69184  14.13862 28.91920 1.000 65.23185  ? 83  ASN A ND2 1 
ATOM   548  N N   . LYS A 1 77  ? -7.28519  14.25578 33.99877 1.000 61.90255  ? 84  LYS A N   1 
ATOM   549  C CA  . LYS A 1 77  ? -6.63425  13.49998 35.06227 1.000 61.78608  ? 84  LYS A CA  1 
ATOM   550  C C   . LYS A 1 77  ? -5.98668  12.22118 34.54721 1.000 66.94494  ? 84  LYS A C   1 
ATOM   551  O O   . LYS A 1 77  ? -4.98911  11.76616 35.11802 1.000 72.71474  ? 84  LYS A O   1 
ATOM   552  C CB  . LYS A 1 77  ? -7.64119  13.17223 36.16583 1.000 58.42914  ? 84  LYS A CB  1 
ATOM   553  C CG  . LYS A 1 77  ? -7.93526  14.33830 37.09501 1.000 56.62871  ? 84  LYS A CG  1 
ATOM   554  C CD  . LYS A 1 77  ? -7.96440  13.89572 38.54801 1.000 67.13683  ? 84  LYS A CD  1 
ATOM   555  C CE  . LYS A 1 77  ? -8.84216  14.81080 39.38663 1.000 65.29661  ? 84  LYS A CE  1 
ATOM   556  N NZ  . LYS A 1 77  ? -10.26148 14.78372 38.93862 1.000 68.62201  ? 84  LYS A NZ  1 
ATOM   557  N N   . GLN A 1 78  ? -6.53121  11.63053 33.48133 1.000 70.66822  ? 85  GLN A N   1 
ATOM   558  C CA  . GLN A 1 78  ? -5.94488  10.41274 32.93017 1.000 69.62430  ? 85  GLN A CA  1 
ATOM   559  C C   . GLN A 1 78  ? -4.57875  10.69259 32.31559 1.000 69.36739  ? 85  GLN A C   1 
ATOM   560  O O   . GLN A 1 78  ? -3.59455  10.01152 32.62632 1.000 78.51344  ? 85  GLN A O   1 
ATOM   561  C CB  . GLN A 1 78  ? -6.88838  9.79767  31.89592 1.000 76.71923  ? 85  GLN A CB  1 
ATOM   562  C CG  . GLN A 1 78  ? -7.77396  8.68937  32.44389 1.000 86.58223  ? 85  GLN A CG  1 
ATOM   563  C CD  . GLN A 1 78  ? -6.97904  7.49093  32.92511 1.000 102.87695 ? 85  GLN A CD  1 
ATOM   564  O OE1 . GLN A 1 78  ? -6.68089  7.36528  34.11305 1.000 105.47909 ? 85  GLN A OE1 1 
ATOM   565  N NE2 . GLN A 1 78  ? -6.63084  6.60212  32.00160 1.000 105.35409 ? 85  GLN A NE2 1 
ATOM   566  N N   . ASP A 1 79  ? -4.49877  11.69487 31.44077 1.000 69.67237  ? 86  ASP A N   1 
ATOM   567  C CA  . ASP A 1 79  ? -3.23224  12.07367 30.82919 1.000 69.76769  ? 86  ASP A CA  1 
ATOM   568  C C   . ASP A 1 79  ? -2.38966  12.97538 31.72127 1.000 63.28915  ? 86  ASP A C   1 
ATOM   569  O O   . ASP A 1 79  ? -1.24113  13.26490 31.36701 1.000 63.27388  ? 86  ASP A O   1 
ATOM   570  C CB  . ASP A 1 79  ? -3.48347  12.77200 29.48994 1.000 73.57874  ? 86  ASP A CB  1 
ATOM   571  C CG  . ASP A 1 79  ? -4.39393  11.97356 28.57698 1.000 78.97722  ? 86  ASP A CG  1 
ATOM   572  O OD1 . ASP A 1 79  ? -4.94711  10.94983 29.03130 1.000 80.20920  ? 86  ASP A OD1 1 
ATOM   573  O OD2 . ASP A 1 79  ? -4.55853  12.37199 27.40475 1.000 93.91236  ? 86  ASP A OD2 1 
ATOM   574  N N   . ARG A 1 80  ? -2.92852  13.41412 32.86164 1.000 61.43253  ? 87  ARG A N   1 
ATOM   575  C CA  . ARG A 1 80  ? -2.24275  14.33459 33.77041 1.000 56.10506  ? 87  ARG A CA  1 
ATOM   576  C C   . ARG A 1 80  ? -1.80899  15.60279 33.03476 1.000 59.60861  ? 87  ARG A C   1 
ATOM   577  O O   . ARG A 1 80  ? -0.65173  16.02348 33.09344 1.000 59.86847  ? 87  ARG A O   1 
ATOM   578  C CB  . ARG A 1 80  ? -1.05357  13.65392 34.45445 1.000 56.04083  ? 87  ARG A CB  1 
ATOM   579  C CG  . ARG A 1 80  ? -0.58618  14.34713 35.72690 1.000 58.21547  ? 87  ARG A CG  1 
ATOM   580  C CD  . ARG A 1 80  ? 0.23841   13.41272 36.59502 1.000 61.19633  ? 87  ARG A CD  1 
ATOM   581  N NE  . ARG A 1 80  ? 1.61612   13.31432 36.12908 1.000 66.31738  ? 87  ARG A NE  1 
ATOM   582  C CZ  . ARG A 1 80  ? 2.50280   12.44376 36.59144 1.000 73.99216  ? 87  ARG A CZ  1 
ATOM   583  N NH1 . ARG A 1 80  ? 2.19185   11.58066 37.54475 1.000 69.21232  ? 87  ARG A NH1 1 
ATOM   584  N NH2 . ARG A 1 80  ? 3.73293   12.44006 36.08575 1.000 76.11123  ? 87  ARG A NH2 1 
ATOM   585  N N   . THR A 1 81  ? -2.75677  16.21070 32.32335 1.000 58.77515  ? 88  THR A N   1 
ATOM   586  C CA  . THR A 1 81  ? -2.50452  17.42262 31.55794 1.000 53.63600  ? 88  THR A CA  1 
ATOM   587  C C   . THR A 1 81  ? -3.55322  18.47423 31.88575 1.000 54.31232  ? 88  THR A C   1 
ATOM   588  O O   . THR A 1 81  ? -4.73155  18.15503 32.07002 1.000 56.68545  ? 88  THR A O   1 
ATOM   589  C CB  . THR A 1 81  ? -2.51313  17.15542 30.04333 1.000 54.07363  ? 88  THR A CB  1 
ATOM   590  O OG1 . THR A 1 81  ? -3.83479  16.78935 29.62689 1.000 62.35369  ? 88  THR A OG1 1 
ATOM   591  C CG2 . THR A 1 81  ? -1.53852  16.04385 29.67995 1.000 58.70502  ? 88  THR A CG2 1 
ATOM   592  N N   . LEU A 1 82  ? -3.11429  19.72842 31.95972 1.000 50.86388  ? 89  LEU A N   1 
ATOM   593  C CA  . LEU A 1 82  ? -4.00256  20.87946 32.05988 1.000 47.22771  ? 89  LEU A CA  1 
ATOM   594  C C   . LEU A 1 82  ? -3.82662  21.71150 30.79924 1.000 46.47626  ? 89  LEU A C   1 
ATOM   595  O O   . LEU A 1 82  ? -2.71297  22.15247 30.49507 1.000 47.21662  ? 89  LEU A O   1 
ATOM   596  C CB  . LEU A 1 82  ? -3.70367  21.71265 33.30788 1.000 51.32440  ? 89  LEU A CB  1 
ATOM   597  C CG  . LEU A 1 82  ? -4.55263  22.97644 33.47009 1.000 43.07815  ? 89  LEU A CG  1 
ATOM   598  C CD1 . LEU A 1 82  ? -6.03401  22.63197 33.46274 1.000 45.25649  ? 89  LEU A CD1 1 
ATOM   599  C CD2 . LEU A 1 82  ? -4.18046  23.72598 34.73990 1.000 52.08392  ? 89  LEU A CD2 1 
ATOM   600  N N   . THR A 1 83  ? -4.91729  21.91976 30.06851 1.000 46.51398  ? 90  THR A N   1 
ATOM   601  C CA  . THR A 1 83  ? -4.88102  22.57618 28.76920 1.000 50.14718  ? 90  THR A CA  1 
ATOM   602  C C   . THR A 1 83  ? -5.57630  23.92847 28.84501 1.000 48.21665  ? 90  THR A C   1 
ATOM   603  O O   . THR A 1 83  ? -6.68405  24.03396 29.38189 1.000 43.54758  ? 90  THR A O   1 
ATOM   604  C CB  . THR A 1 83  ? -5.54544  21.70556 27.70087 1.000 47.52747  ? 90  THR A CB  1 
ATOM   605  O OG1 . THR A 1 83  ? -4.94856  20.40326 27.70591 1.000 48.09113  ? 90  THR A OG1 1 
ATOM   606  C CG2 . THR A 1 83  ? -5.36998  22.32673 26.32719 1.000 47.96623  ? 90  THR A CG2 1 
ATOM   607  N N   . ILE A 1 84  ? -4.92417  24.95494 28.30511 1.000 51.96427  ? 91  ILE A N   1 
ATOM   608  C CA  . ILE A 1 84  ? -5.49125  26.29373 28.19211 1.000 50.87021  ? 91  ILE A CA  1 
ATOM   609  C C   . ILE A 1 84  ? -5.62998  26.60703 26.71009 1.000 50.80375  ? 91  ILE A C   1 
ATOM   610  O O   . ILE A 1 84  ? -4.62511  26.69935 25.99390 1.000 57.89664  ? 91  ILE A O   1 
ATOM   611  C CB  . ILE A 1 84  ? -4.62428  27.34860 28.89737 1.000 46.99374  ? 91  ILE A CB  1 
ATOM   612  C CG1 . ILE A 1 84  ? -4.74985  27.21642 30.41521 1.000 53.22424  ? 91  ILE A CG1 1 
ATOM   613  C CG2 . ILE A 1 84  ? -5.02209  28.74873 28.45529 1.000 49.45164  ? 91  ILE A CG2 1 
ATOM   614  C CD1 . ILE A 1 84  ? -3.59767  26.48387 31.05559 1.000 60.14628  ? 91  ILE A CD1 1 
ATOM   615  N N   . VAL A 1 85  ? -6.86782  26.76521 26.25050 1.000 41.77225  ? 92  VAL A N   1 
ATOM   616  C CA  . VAL A 1 85  ? -7.16854  27.01449 24.84572 1.000 45.28181  ? 92  VAL A CA  1 
ATOM   617  C C   . VAL A 1 85  ? -7.76441  28.40763 24.71658 1.000 53.00049  ? 92  VAL A C   1 
ATOM   618  O O   . VAL A 1 85  ? -8.73789  28.74037 25.40360 1.000 58.29369  ? 92  VAL A O   1 
ATOM   619  C CB  . VAL A 1 85  ? -8.12851  25.95600 24.27551 1.000 43.93649  ? 92  VAL A CB  1 
ATOM   620  C CG1 . VAL A 1 85  ? -8.48929  26.28798 22.83531 1.000 34.71781  ? 92  VAL A CG1 1 
ATOM   621  C CG2 . VAL A 1 85  ? -7.50687  24.57329 24.36627 1.000 50.42891  ? 92  VAL A CG2 1 
ATOM   622  N N   . ASP A 1 86  ? -7.17989  29.21908 23.83924 1.000 48.38783  ? 93  ASP A N   1 
ATOM   623  C CA  . ASP A 1 86  ? -7.71005  30.53238 23.51171 1.000 46.32224  ? 93  ASP A CA  1 
ATOM   624  C C   . ASP A 1 86  ? -7.78393  30.67499 21.99945 1.000 52.53012  ? 93  ASP A C   1 
ATOM   625  O O   . ASP A 1 86  ? -7.03175  30.03237 21.26173 1.000 45.14610  ? 93  ASP A O   1 
ATOM   626  C CB  . ASP A 1 86  ? -6.85483  31.66062 24.11752 1.000 45.87000  ? 93  ASP A CB  1 
ATOM   627  C CG  . ASP A 1 86  ? -5.55015  31.88170 23.36879 1.000 52.12217  ? 93  ASP A CG  1 
ATOM   628  O OD1 . ASP A 1 86  ? -5.56338  32.56000 22.31915 1.000 48.78869  ? 93  ASP A OD1 1 
ATOM   629  O OD2 . ASP A 1 86  ? -4.50616  31.37788 23.83473 1.000 61.90922  ? 93  ASP A OD2 1 
ATOM   630  N N   . THR A 1 87  ? -8.70539  31.52069 21.54444 1.000 51.27579  ? 94  THR A N   1 
ATOM   631  C CA  . THR A 1 87  ? -8.89576  31.79395 20.12155 1.000 50.77054  ? 94  THR A CA  1 
ATOM   632  C C   . THR A 1 87  ? -8.29777  33.13571 19.72139 1.000 51.93277  ? 94  THR A C   1 
ATOM   633  O O   . THR A 1 87  ? -8.89737  33.89200 18.95174 1.000 50.76457  ? 94  THR A O   1 
ATOM   634  C CB  . THR A 1 87  ? -10.37784 31.73952 19.76619 1.000 50.75343  ? 94  THR A CB  1 
ATOM   635  O OG1 . THR A 1 87  ? -11.13694 32.41688 20.77568 1.000 46.99267  ? 94  THR A OG1 1 
ATOM   636  C CG2 . THR A 1 87  ? -10.84630 30.29589 19.66981 1.000 37.19076  ? 94  THR A CG2 1 
ATOM   637  N N   . GLY A 1 88  ? -7.11108  33.45093 20.23209 1.000 51.64434  ? 95  GLY A N   1 
ATOM   638  C CA  . GLY A 1 88  ? -6.46696  34.71881 19.96408 1.000 52.25065  ? 95  GLY A CA  1 
ATOM   639  C C   . GLY A 1 88  ? -5.85086  34.78494 18.58128 1.000 55.27529  ? 95  GLY A C   1 
ATOM   640  O O   . GLY A 1 88  ? -6.21178  34.04091 17.66584 1.000 56.93614  ? 95  GLY A O   1 
ATOM   641  N N   . ILE A 1 89  ? -4.88844  35.70002 18.43816 1.000 55.40115  ? 96  ILE A N   1 
ATOM   642  C CA  . ILE A 1 89  ? -4.27479  35.94989 17.13943 1.000 54.33598  ? 96  ILE A CA  1 
ATOM   643  C C   . ILE A 1 89  ? -3.44367  34.76587 16.65944 1.000 48.58113  ? 96  ILE A C   1 
ATOM   644  O O   . ILE A 1 89  ? -3.24041  34.60736 15.45006 1.000 55.01142  ? 96  ILE A O   1 
ATOM   645  C CB  . ILE A 1 89  ? -3.42628  37.23638 17.20066 1.000 53.70893  ? 96  ILE A CB  1 
ATOM   646  C CG1 . ILE A 1 89  ? -3.02858  37.69620 15.79589 1.000 51.70989  ? 96  ILE A CG1 1 
ATOM   647  C CG2 . ILE A 1 89  ? -2.19517  37.03229 18.07168 1.000 54.21516  ? 96  ILE A CG2 1 
ATOM   648  C CD1 . ILE A 1 89  ? -2.78405  39.18530 15.68948 1.000 56.08458  ? 96  ILE A CD1 1 
ATOM   649  N N   . GLY A 1 90  ? -2.97286  33.91533 17.56831 1.000 46.48818  ? 97  GLY A N   1 
ATOM   650  C CA  . GLY A 1 90  ? -2.12007  32.80724 17.19083 1.000 46.66392  ? 97  GLY A CA  1 
ATOM   651  C C   . GLY A 1 90  ? -0.65902  33.20180 17.13369 1.000 44.13041  ? 97  GLY A C   1 
ATOM   652  O O   . GLY A 1 90  ? -0.26138  34.32772 17.44595 1.000 50.56723  ? 97  GLY A O   1 
ATOM   653  N N   . MET A 1 91  ? 0.16442   32.24303 16.71542 1.000 42.94499  ? 98  MET A N   1 
ATOM   654  C CA  . MET A 1 91  ? 1.60515   32.44124 16.66358 1.000 45.56233  ? 98  MET A CA  1 
ATOM   655  C C   . MET A 1 91  ? 2.16538   31.83835 15.38476 1.000 46.36681  ? 98  MET A C   1 
ATOM   656  O O   . MET A 1 91  ? 1.72206   30.77491 14.94322 1.000 49.94922  ? 98  MET A O   1 
ATOM   657  C CB  . MET A 1 91  ? 2.29425   31.81933 17.88420 1.000 52.03857  ? 98  MET A CB  1 
ATOM   658  C CG  . MET A 1 91  ? 2.18790   32.65840 19.14758 1.000 51.37650  ? 98  MET A CG  1 
ATOM   659  S SD  . MET A 1 91  ? 2.93378   31.86186 20.58043 1.000 49.16879  ? 98  MET A SD  1 
ATOM   660  C CE  . MET A 1 91  ? 1.49156   31.61383 21.61197 1.000 58.36780  ? 98  MET A CE  1 
ATOM   661  N N   . THR A 1 92  ? 3.13982   32.52458 14.79744 1.000 48.88802  ? 99  THR A N   1 
ATOM   662  C CA  . THR A 1 92  ? 3.81087   32.07402 13.58816 1.000 48.92277  ? 99  THR A CA  1 
ATOM   663  C C   . THR A 1 92  ? 5.09245   31.32470 13.94140 1.000 58.48364  ? 99  THR A C   1 
ATOM   664  O O   . THR A 1 92  ? 5.52887   31.29346 15.09449 1.000 64.93817  ? 99  THR A O   1 
ATOM   665  C CB  . THR A 1 92  ? 4.12195   33.26185 12.67236 1.000 49.42050  ? 99  THR A CB  1 
ATOM   666  O OG1 . THR A 1 92  ? 5.17602   34.04498 13.24553 1.000 54.67320  ? 99  THR A OG1 1 
ATOM   667  C CG2 . THR A 1 92  ? 2.89021   34.13502 12.49736 1.000 42.00547  ? 99  THR A CG2 1 
ATOM   668  N N   . LYS A 1 93  ? 5.69777   30.71096 12.92016 1.000 51.76524  ? 100 LYS A N   1 
ATOM   669  C CA  . LYS A 1 93  ? 6.94296   29.97941 13.13582 1.000 55.64479  ? 100 LYS A CA  1 
ATOM   670  C C   . LYS A 1 93  ? 8.06017   30.91410 13.57842 1.000 60.73529  ? 100 LYS A C   1 
ATOM   671  O O   . LYS A 1 93  ? 8.90654   30.53871 14.39850 1.000 63.23205  ? 100 LYS A O   1 
ATOM   672  C CB  . LYS A 1 93  ? 7.34721   29.23051 11.86586 1.000 57.54053  ? 100 LYS A CB  1 
ATOM   673  C CG  . LYS A 1 93  ? 8.11309   27.94279 12.13096 1.000 56.87349  ? 100 LYS A CG  1 
ATOM   674  C CD  . LYS A 1 93  ? 8.46795   27.22226 10.84036 1.000 63.69275  ? 100 LYS A CD  1 
ATOM   675  C CE  . LYS A 1 93  ? 9.96574   27.24732 10.58509 1.000 64.84200  ? 100 LYS A CE  1 
ATOM   676  N NZ  . LYS A 1 93  ? 10.32308  26.57868 9.30404  1.000 62.50143  ? 100 LYS A NZ  1 
ATOM   677  N N   . ALA A 1 94  ? 8.08132   32.13669 13.04334 1.000 54.58518  ? 101 ALA A N   1 
ATOM   678  C CA  . ALA A 1 94  ? 9.08087   33.10893 13.47008 1.000 57.48799  ? 101 ALA A CA  1 
ATOM   679  C C   . ALA A 1 94  ? 8.85722   33.52335 14.91819 1.000 63.46421  ? 101 ALA A C   1 
ATOM   680  O O   . ALA A 1 94  ? 9.81902   33.74908 15.66201 1.000 72.25559  ? 101 ALA A O   1 
ATOM   681  C CB  . ALA A 1 94  ? 9.05405   34.32772 12.54923 1.000 53.95292  ? 101 ALA A CB  1 
ATOM   682  N N   . ASP A 1 95  ? 7.59312   33.62347 15.33597 1.000 53.92290  ? 102 ASP A N   1 
ATOM   683  C CA  . ASP A 1 95  ? 7.29410   33.95799 16.72395 1.000 57.55045  ? 102 ASP A CA  1 
ATOM   684  C C   . ASP A 1 95  ? 7.73031   32.84343 17.66444 1.000 61.99328  ? 102 ASP A C   1 
ATOM   685  O O   . ASP A 1 95  ? 8.29508   33.10750 18.73228 1.000 66.49608  ? 102 ASP A O   1 
ATOM   686  C CB  . ASP A 1 95  ? 5.79997   34.23045 16.88455 1.000 55.19946  ? 102 ASP A CB  1 
ATOM   687  C CG  . ASP A 1 95  ? 5.32979   35.39762 16.04837 1.000 63.86960  ? 102 ASP A CG  1 
ATOM   688  O OD1 . ASP A 1 95  ? 6.16197   36.26966 15.72045 1.000 68.77115  ? 102 ASP A OD1 1 
ATOM   689  O OD2 . ASP A 1 95  ? 4.12643   35.44863 15.71973 1.000 63.06495  ? 102 ASP A OD2 1 
ATOM   690  N N   . LEU A 1 96  ? 7.47470   31.59056 17.28344 1.000 60.87474  ? 103 LEU A N   1 
ATOM   691  C CA  . LEU A 1 96  ? 7.81845   30.46749 18.14770 1.000 62.13677  ? 103 LEU A CA  1 
ATOM   692  C C   . LEU A 1 96  ? 9.32797   30.29473 18.25710 1.000 64.26325  ? 103 LEU A C   1 
ATOM   693  O O   . LEU A 1 96  ? 9.85025   30.02589 19.34516 1.000 75.73705  ? 103 LEU A O   1 
ATOM   694  C CB  . LEU A 1 96  ? 7.16603   29.18848 17.62259 1.000 56.83266  ? 103 LEU A CB  1 
ATOM   695  C CG  . LEU A 1 96  ? 5.65286   29.06720 17.81934 1.000 50.75640  ? 103 LEU A CG  1 
ATOM   696  C CD1 . LEU A 1 96  ? 5.11363   27.82725 17.12199 1.000 59.82489  ? 103 LEU A CD1 1 
ATOM   697  C CD2 . LEU A 1 96  ? 5.30095   29.04942 19.29825 1.000 50.21257  ? 103 LEU A CD2 1 
ATOM   698  N N   . ILE A 1 97  ? 10.04462  30.45200 17.14581 1.000 62.11242  ? 104 ILE A N   1 
ATOM   699  C CA  . ILE A 1 97  ? 11.48927  30.25307 17.12175 1.000 70.83724  ? 104 ILE A CA  1 
ATOM   700  C C   . ILE A 1 97  ? 12.18510  31.49002 17.67242 1.000 74.06720  ? 104 ILE A C   1 
ATOM   701  O O   . ILE A 1 97  ? 12.74965  31.46302 18.77173 1.000 78.26756  ? 104 ILE A O   1 
ATOM   702  C CB  . ILE A 1 97  ? 11.97961  29.93374 15.69849 1.000 71.69059  ? 104 ILE A CB  1 
ATOM   703  C CG1 . ILE A 1 97  ? 11.45894  28.56610 15.25317 1.000 65.24089  ? 104 ILE A CG1 1 
ATOM   704  C CG2 . ILE A 1 97  ? 13.49878  29.97447 15.63557 1.000 59.10198  ? 104 ILE A CG2 1 
ATOM   705  C CD1 . ILE A 1 97  ? 11.40258  28.39939 13.75312 1.000 60.63823  ? 104 ILE A CD1 1 
ATOM   706  N N   . ASN A 1 98  ? 12.14973  32.58199 16.91096 1.000 76.72912  ? 105 ASN A N   1 
ATOM   707  C CA  . ASN A 1 98  ? 12.80437  33.81843 17.31512 1.000 66.19632  ? 105 ASN A CA  1 
ATOM   708  C C   . ASN A 1 98  ? 11.76155  34.82939 17.76908 1.000 66.27862  ? 105 ASN A C   1 
ATOM   709  O O   . ASN A 1 98  ? 10.79313  34.46228 18.44210 1.000 76.51318  ? 105 ASN A O   1 
ATOM   710  C CB  . ASN A 1 98  ? 13.63656  34.38021 16.16206 1.000 69.82420  ? 105 ASN A CB  1 
ATOM   711  C CG  . ASN A 1 98  ? 15.10405  34.50673 16.50948 1.000 88.55705  ? 105 ASN A CG  1 
ATOM   712  O OD1 . ASN A 1 98  ? 15.47843  34.54035 17.68167 1.000 98.66079  ? 105 ASN A OD1 1 
ATOM   713  N ND2 . ASN A 1 98  ? 15.94711  34.57478 15.48647 1.000 90.12354  ? 105 ASN A ND2 1 
ATOM   714  N N   . ASN A 1 99  ? 11.95225  36.09816 17.40240 1.000 75.20938  ? 106 ASN A N   1 
ATOM   715  C CA  . ASN A 1 99  ? 10.97484  37.15512 17.64813 1.000 85.27024  ? 106 ASN A CA  1 
ATOM   716  C C   . ASN A 1 99  ? 10.56418  37.24247 19.11370 1.000 80.54070  ? 106 ASN A C   1 
ATOM   717  O O   . ASN A 1 99  ? 11.00873  38.13972 19.83761 1.000 88.39227  ? 106 ASN A O   1 
ATOM   718  C CB  . ASN A 1 99  ? 9.73533   36.94804 16.77127 1.000 75.13924  ? 106 ASN A CB  1 
ATOM   719  C CG  . ASN A 1 99  ? 10.01891  37.16998 15.29740 1.000 76.09809  ? 106 ASN A CG  1 
ATOM   720  O OD1 . ASN A 1 99  ? 11.17125  37.32143 14.89182 1.000 76.19927  ? 106 ASN A OD1 1 
ATOM   721  N ND2 . ASN A 1 99  ? 8.96529   37.19194 14.48732 1.000 70.45588  ? 106 ASN A ND2 1 
ATOM   722  N N   . LEU A 1 100 ? 9.70721   36.31577 19.55220 1.000 60.50798  ? 107 LEU A N   1 
ATOM   723  C CA  . LEU A 1 100 ? 9.20582   36.35244 20.92259 1.000 62.11661  ? 107 LEU A CA  1 
ATOM   724  C C   . LEU A 1 100 ? 10.33643  36.18367 21.93039 1.000 66.54430  ? 107 LEU A C   1 
ATOM   725  O O   . LEU A 1 100 ? 10.32603  36.81041 22.99632 1.000 63.22812  ? 107 LEU A O   1 
ATOM   726  C CB  . LEU A 1 100 ? 8.14076   35.27206 21.11781 1.000 62.78737  ? 107 LEU A CB  1 
ATOM   727  C CG  . LEU A 1 100 ? 6.72492   35.59667 20.62870 1.000 58.01350  ? 107 LEU A CG  1 
ATOM   728  C CD1 . LEU A 1 100 ? 5.68524   34.77861 21.38033 1.000 61.91082  ? 107 LEU A CD1 1 
ATOM   729  C CD2 . LEU A 1 100 ? 6.42970   37.08350 20.75785 1.000 60.96672  ? 107 LEU A CD2 1 
ATOM   730  N N   . GLY A 1 101 ? 11.32306  35.34397 21.61060 1.000 66.06712  ? 108 GLY A N   1 
ATOM   731  C CA  . GLY A 1 101 ? 12.47544  35.21012 22.48651 1.000 56.01086  ? 108 GLY A CA  1 
ATOM   732  C C   . GLY A 1 101 ? 13.32557  36.46559 22.52160 1.000 70.46088  ? 108 GLY A C   1 
ATOM   733  O O   . GLY A 1 101 ? 13.89047  36.81526 23.56189 1.000 70.02567  ? 108 GLY A O   1 
ATOM   734  N N   . THR A 1 102 ? 13.42822  37.16122 21.38621 1.000 70.73530  ? 109 THR A N   1 
ATOM   735  C CA  . THR A 1 102 ? 14.16213  38.42189 21.35317 1.000 67.00749  ? 109 THR A CA  1 
ATOM   736  C C   . THR A 1 102 ? 13.48750  39.47054 22.22808 1.000 68.55919  ? 109 THR A C   1 
ATOM   737  O O   . THR A 1 102 ? 14.16225  40.28579 22.86827 1.000 80.81353  ? 109 THR A O   1 
ATOM   738  C CB  . THR A 1 102 ? 14.28285  38.91991 19.91226 1.000 64.48954  ? 109 THR A CB  1 
ATOM   739  O OG1 . THR A 1 102 ? 14.70708  37.84249 19.06752 1.000 68.27881  ? 109 THR A OG1 1 
ATOM   740  C CG2 . THR A 1 102 ? 15.29084  40.05700 19.81945 1.000 77.50039  ? 109 THR A CG2 1 
ATOM   741  N N   . ILE A 1 103 ? 12.15421  39.46019 22.27280 1.000 62.48448  ? 110 ILE A N   1 
ATOM   742  C CA  . ILE A 1 103 ? 11.43125  40.39695 23.12580 1.000 64.30020  ? 110 ILE A CA  1 
ATOM   743  C C   . ILE A 1 103 ? 11.63283  40.04349 24.59480 1.000 65.70436  ? 110 ILE A C   1 
ATOM   744  O O   . ILE A 1 103 ? 11.74972  40.92785 25.45218 1.000 70.69429  ? 110 ILE A O   1 
ATOM   745  C CB  . ILE A 1 103 ? 9.93970   40.41604 22.74008 1.000 67.98742  ? 110 ILE A CB  1 
ATOM   746  C CG1 . ILE A 1 103 ? 9.74890   41.09462 21.37972 1.000 68.53893  ? 110 ILE A CG1 1 
ATOM   747  C CG2 . ILE A 1 103 ? 9.10315   41.10373 23.81481 1.000 64.28107  ? 110 ILE A CG2 1 
ATOM   748  C CD1 . ILE A 1 103 ? 9.57830   42.59774 21.45285 1.000 65.89458  ? 110 ILE A CD1 1 
ATOM   749  N N   . ALA A 1 104 ? 11.70087  38.74914 24.90605 1.000 67.59693  ? 111 ALA A N   1 
ATOM   750  C CA  . ALA A 1 104 ? 11.78764  38.29376 26.28693 1.000 60.10980  ? 111 ALA A CA  1 
ATOM   751  C C   . ALA A 1 104 ? 13.20290  38.32412 26.84940 1.000 71.21943  ? 111 ALA A C   1 
ATOM   752  O O   . ALA A 1 104 ? 13.36670  38.16837 28.06450 1.000 76.96991  ? 111 ALA A O   1 
ATOM   753  C CB  . ALA A 1 104 ? 11.22508  36.87523 26.40422 1.000 50.40773  ? 111 ALA A CB  1 
ATOM   754  N N   . LYS A 1 105 ? 14.22385  38.51898 26.01027 1.000 75.61552  ? 112 LYS A N   1 
ATOM   755  C CA  . LYS A 1 105 ? 15.59529  38.49105 26.50999 1.000 70.79504  ? 112 LYS A CA  1 
ATOM   756  C C   . LYS A 1 105 ? 15.87903  39.65834 27.44817 1.000 73.68122  ? 112 LYS A C   1 
ATOM   757  O O   . LYS A 1 105 ? 16.72113  39.53831 28.34543 1.000 81.90106  ? 112 LYS A O   1 
ATOM   758  C CB  . LYS A 1 105 ? 16.58527  38.48728 25.34309 1.000 71.90872  ? 112 LYS A CB  1 
ATOM   759  C CG  . LYS A 1 105 ? 16.82919  39.85017 24.71623 1.000 86.83600  ? 112 LYS A CG  1 
ATOM   760  C CD  . LYS A 1 105 ? 17.54242  39.73144 23.38133 1.000 87.05182  ? 112 LYS A CD  1 
ATOM   761  C CE  . LYS A 1 105 ? 17.57090  41.06644 22.65606 1.000 84.44801  ? 112 LYS A CE  1 
ATOM   762  N NZ  . LYS A 1 105 ? 18.32274  40.98480 21.37435 1.000 88.90540  ? 112 LYS A NZ  1 
ATOM   763  N N   . SER A 1 106 ? 15.18881  40.78629 27.26579 1.000 72.86060  ? 113 SER A N   1 
ATOM   764  C CA  . SER A 1 106 ? 15.36776  41.91768 28.16809 1.000 66.02845  ? 113 SER A CA  1 
ATOM   765  C C   . SER A 1 106 ? 14.51868  41.76239 29.42264 1.000 68.84131  ? 113 SER A C   1 
ATOM   766  O O   . SER A 1 106 ? 14.96514  42.10317 30.52403 1.000 68.53105  ? 113 SER A O   1 
ATOM   767  C CB  . SER A 1 106 ? 15.02827  43.22362 27.44963 1.000 68.97607  ? 113 SER A CB  1 
ATOM   768  O OG  . SER A 1 106 ? 13.91010  43.05932 26.59537 1.000 77.07050  ? 113 SER A OG  1 
ATOM   769  N N   . GLY A 1 107 ? 13.29457  41.25060 29.27389 1.000 73.18642  ? 114 GLY A N   1 
ATOM   770  C CA  . GLY A 1 107 ? 12.46656  40.98711 30.43699 1.000 70.92137  ? 114 GLY A CA  1 
ATOM   771  C C   . GLY A 1 107 ? 13.05378  39.93058 31.34928 1.000 68.21429  ? 114 GLY A C   1 
ATOM   772  O O   . GLY A 1 107 ? 12.84187  39.96637 32.56399 1.000 68.71130  ? 114 GLY A O   1 
ATOM   773  N N   . THR A 1 108 ? 13.79789  38.97851 30.78273 1.000 68.82235  ? 115 THR A N   1 
ATOM   774  C CA  . THR A 1 108 ? 14.47346  37.98088 31.60506 1.000 62.04683  ? 115 THR A CA  1 
ATOM   775  C C   . THR A 1 108 ? 15.60207  38.61276 32.40977 1.000 71.50681  ? 115 THR A C   1 
ATOM   776  O O   . THR A 1 108 ? 15.71859  38.38439 33.61918 1.000 74.95742  ? 115 THR A O   1 
ATOM   777  C CB  . THR A 1 108 ? 15.00924  36.84847 30.72864 1.000 68.86876  ? 115 THR A CB  1 
ATOM   778  O OG1 . THR A 1 108 ? 13.91938  36.19770 30.06353 1.000 62.87611  ? 115 THR A OG1 1 
ATOM   779  C CG2 . THR A 1 108 ? 15.76312  35.83396 31.57474 1.000 74.50400  ? 115 THR A CG2 1 
ATOM   780  N N   . LYS A 1 109 ? 16.44330  39.41505 31.75081 1.000 73.11870  ? 116 LYS A N   1 
ATOM   781  C CA  . LYS A 1 109 ? 17.54402  40.07567 32.44596 1.000 69.18310  ? 116 LYS A CA  1 
ATOM   782  C C   . LYS A 1 109 ? 17.03382  40.95606 33.57945 1.000 76.71032  ? 116 LYS A C   1 
ATOM   783  O O   . LYS A 1 109 ? 17.58953  40.94401 34.68416 1.000 79.07044  ? 116 LYS A O   1 
ATOM   784  C CB  . LYS A 1 109 ? 18.36534  40.90290 31.45684 1.000 74.82234  ? 116 LYS A CB  1 
ATOM   785  C CG  . LYS A 1 109 ? 19.48732  40.13828 30.77563 1.000 77.21077  ? 116 LYS A CG  1 
ATOM   786  C CD  . LYS A 1 109 ? 20.50447  41.09005 30.16379 1.000 83.87291  ? 116 LYS A CD  1 
ATOM   787  C CE  . LYS A 1 109 ? 21.22796  41.89202 31.23455 1.000 77.74060  ? 116 LYS A CE  1 
ATOM   788  N NZ  . LYS A 1 109 ? 21.96748  43.05053 30.65908 1.000 84.18003  ? 116 LYS A NZ  1 
ATOM   789  N N   . ALA A 1 110 ? 15.97286  41.72542 33.32508 1.000 74.45938  ? 117 ALA A N   1 
ATOM   790  C CA  . ALA A 1 110 ? 15.41254  42.58000 34.36525 1.000 77.95789  ? 117 ALA A CA  1 
ATOM   791  C C   . ALA A 1 110 ? 14.75001  41.76475 35.46764 1.000 80.43146  ? 117 ALA A C   1 
ATOM   792  O O   . ALA A 1 110 ? 14.78065  42.16739 36.63623 1.000 94.56709  ? 117 ALA A O   1 
ATOM   793  C CB  . ALA A 1 110 ? 14.41228  43.56214 33.75606 1.000 79.22614  ? 117 ALA A CB  1 
ATOM   794  N N   . PHE A 1 111 ? 14.14911  40.62421 35.12039 1.000 78.02432  ? 118 PHE A N   1 
ATOM   795  C CA  . PHE A 1 111 ? 13.51098  39.78511 36.12961 1.000 79.45028  ? 118 PHE A CA  1 
ATOM   796  C C   . PHE A 1 111 ? 14.53914  39.22202 37.10155 1.000 82.05920  ? 118 PHE A C   1 
ATOM   797  O O   . PHE A 1 111 ? 14.34901  39.27615 38.32182 1.000 88.78369  ? 118 PHE A O   1 
ATOM   798  C CB  . PHE A 1 111 ? 12.72990  38.65504 35.45812 1.000 73.03250  ? 118 PHE A CB  1 
ATOM   799  C CG  . PHE A 1 111 ? 11.88021  37.85762 36.40649 1.000 73.66323  ? 118 PHE A CG  1 
ATOM   800  C CD1 . PHE A 1 111 ? 11.16630  38.48498 37.41334 1.000 73.47446  ? 118 PHE A CD1 1 
ATOM   801  C CD2 . PHE A 1 111 ? 11.79316  36.48126 36.28959 1.000 62.89224  ? 118 PHE A CD2 1 
ATOM   802  C CE1 . PHE A 1 111 ? 10.38248  37.75384 38.28609 1.000 69.76478  ? 118 PHE A CE1 1 
ATOM   803  C CE2 . PHE A 1 111 ? 11.01236  35.74380 37.15912 1.000 57.85971  ? 118 PHE A CE2 1 
ATOM   804  C CZ  . PHE A 1 111 ? 10.30528  36.38100 38.15782 1.000 68.57443  ? 118 PHE A CZ  1 
ATOM   805  N N   . MET A 1 112 ? 15.64251  38.68247 36.57685 1.000 78.86330  ? 119 MET A N   1 
ATOM   806  C CA  . MET A 1 112 ? 16.66960  38.11537 37.44413 1.000 83.58456  ? 119 MET A CA  1 
ATOM   807  C C   . MET A 1 112 ? 17.32533  39.18215 38.31015 1.000 89.24890  ? 119 MET A C   1 
ATOM   808  O O   . MET A 1 112 ? 17.79439  38.88223 39.41315 1.000 91.49735  ? 119 MET A O   1 
ATOM   809  C CB  . MET A 1 112 ? 17.71836  37.38315 36.60744 1.000 76.41070  ? 119 MET A CB  1 
ATOM   810  C CG  . MET A 1 112 ? 17.12660  36.42108 35.58946 1.000 72.05436  ? 119 MET A CG  1 
ATOM   811  S SD  . MET A 1 112 ? 18.25370  35.10353 35.09852 1.000 96.68744  ? 119 MET A SD  1 
ATOM   812  C CE  . MET A 1 112 ? 17.55889  33.71313 35.98699 1.000 73.65625  ? 119 MET A CE  1 
ATOM   813  N N   . GLU A 1 113 ? 17.36849  40.42835 37.83511 1.000 97.19088  ? 120 GLU A N   1 
ATOM   814  C CA  . GLU A 1 113 ? 17.87263  41.50920 38.67374 1.000 101.21980 ? 120 GLU A CA  1 
ATOM   815  C C   . GLU A 1 113 ? 16.89503  41.84802 39.79083 1.000 111.45051 ? 120 GLU A C   1 
ATOM   816  O O   . GLU A 1 113 ? 17.31649  42.23658 40.88630 1.000 119.92163 ? 120 GLU A O   1 
ATOM   817  C CB  . GLU A 1 113 ? 18.15666  42.74877 37.82600 1.000 111.28684 ? 120 GLU A CB  1 
ATOM   818  C CG  . GLU A 1 113 ? 19.35912  42.61479 36.90866 1.000 105.56416 ? 120 GLU A CG  1 
ATOM   819  C CD  . GLU A 1 113 ? 19.38821  43.68179 35.83367 1.000 126.39054 ? 120 GLU A CD  1 
ATOM   820  O OE1 . GLU A 1 113 ? 18.42051  44.46718 35.74830 1.000 135.65311 ? 120 GLU A OE1 1 
ATOM   821  O OE2 . GLU A 1 113 ? 20.37801  43.73557 35.07447 1.000 130.68362 ? 120 GLU A OE2 1 
ATOM   822  N N   . ALA A 1 114 ? 15.59284  41.70005 39.53796 1.000 131.38299 ? 121 ALA A N   1 
ATOM   823  C CA  . ALA A 1 114 ? 14.59220  42.04295 40.54091 1.000 134.40980 ? 121 ALA A CA  1 
ATOM   824  C C   . ALA A 1 114 ? 14.47078  40.97981 41.62397 1.000 130.25571 ? 121 ALA A C   1 
ATOM   825  O O   . ALA A 1 114 ? 14.17818  41.31368 42.77756 1.000 133.27506 ? 121 ALA A O   1 
ATOM   826  C CB  . ALA A 1 114 ? 13.23441  42.26734 39.87503 1.000 133.83511 ? 121 ALA A CB  1 
ATOM   827  N N   . LEU A 1 115 ? 14.67858  39.70581 41.27851 1.000 104.10907 ? 122 LEU A N   1 
ATOM   828  C CA  . LEU A 1 115 ? 14.60904  38.65153 42.28565 1.000 103.00821 ? 122 LEU A CA  1 
ATOM   829  C C   . LEU A 1 115 ? 15.66224  38.85355 43.36640 1.000 107.62231 ? 122 LEU A C   1 
ATOM   830  O O   . LEU A 1 115 ? 15.40842  38.59434 44.54807 1.000 112.73237 ? 122 LEU A O   1 
ATOM   831  C CB  . LEU A 1 115 ? 14.76821  37.27825 41.63155 1.000 90.38788  ? 122 LEU A CB  1 
ATOM   832  C CG  . LEU A 1 115 ? 13.87427  36.95086 40.43373 1.000 85.47903  ? 122 LEU A CG  1 
ATOM   833  C CD1 . LEU A 1 115 ? 14.57158  35.98653 39.48329 1.000 77.10543  ? 122 LEU A CD1 1 
ATOM   834  C CD2 . LEU A 1 115 ? 12.54485  36.38103 40.89992 1.000 85.56196  ? 122 LEU A CD2 1 
ATOM   835  N N   . GLN A 1 116 ? 16.84956  39.31965 42.98389 1.000 105.54575 ? 123 GLN A N   1 
ATOM   836  C CA  . GLN A 1 116 ? 17.89130  39.59283 43.96459 1.000 106.41544 ? 123 GLN A CA  1 
ATOM   837  C C   . GLN A 1 116 ? 17.66487  40.90372 44.70520 1.000 106.29681 ? 123 GLN A C   1 
ATOM   838  O O   . GLN A 1 116 ? 18.29754  41.13226 45.74197 1.000 96.18492  ? 123 GLN A O   1 
ATOM   839  C CB  . GLN A 1 116 ? 19.26450  39.61191 43.28363 1.000 100.59493 ? 123 GLN A CB  1 
ATOM   840  C CG  . GLN A 1 116 ? 19.90580  38.23519 43.04714 1.000 95.39918  ? 123 GLN A CG  1 
ATOM   841  C CD  . GLN A 1 116 ? 18.93298  37.17818 42.54552 1.000 96.40472  ? 123 GLN A CD  1 
ATOM   842  O OE1 . GLN A 1 116 ? 18.03126  37.46374 41.75839 1.000 93.16354  ? 123 GLN A OE1 1 
ATOM   843  N NE2 . GLN A 1 116 ? 19.11962  35.94522 42.99926 1.000 95.09495  ? 123 GLN A NE2 1 
ATOM   844  N N   . ALA A 1 117 ? 16.78255  41.76387 44.20184 1.000 116.53988 ? 124 ALA A N   1 
ATOM   845  C CA  . ALA A 1 117 ? 16.49205  43.04307 44.83191 1.000 113.93979 ? 124 ALA A CA  1 
ATOM   846  C C   . ALA A 1 117 ? 15.28584  42.98126 45.76045 1.000 124.78358 ? 124 ALA A C   1 
ATOM   847  O O   . ALA A 1 117 ? 14.86916  44.01878 46.28547 1.000 126.18737 ? 124 ALA A O   1 
ATOM   848  C CB  . ALA A 1 117 ? 16.28014  44.12113 43.76595 1.000 113.45711 ? 124 ALA A CB  1 
ATOM   849  N N   . GLY A 1 118 ? 14.71767  41.79115 45.97511 1.000 136.43787 ? 125 GLY A N   1 
ATOM   850  C CA  . GLY A 1 118 ? 13.63417  41.58267 46.92156 1.000 138.35303 ? 125 GLY A CA  1 
ATOM   851  C C   . GLY A 1 118 ? 12.39810  40.94608 46.31195 1.000 132.87110 ? 125 GLY A C   1 
ATOM   852  O O   . GLY A 1 118 ? 11.62474  40.29998 47.02678 1.000 134.07793 ? 125 GLY A O   1 
ATOM   853  N N   . ALA A 1 119 ? 12.20190  41.11461 45.00622 1.000 130.64438 ? 126 ALA A N   1 
ATOM   854  C CA  . ALA A 1 119 ? 11.02973  40.56902 44.33752 1.000 128.21021 ? 126 ALA A CA  1 
ATOM   855  C C   . ALA A 1 119 ? 11.07874  39.04322 44.31315 1.000 109.19556 ? 126 ALA A C   1 
ATOM   856  O O   . ALA A 1 119 ? 12.14299  38.42339 44.39492 1.000 109.48693 ? 126 ALA A O   1 
ATOM   857  C CB  . ALA A 1 119 ? 10.92197  41.11011 42.91096 1.000 115.45187 ? 126 ALA A CB  1 
ATOM   858  N N   . ASP A 1 120 ? 9.90043   38.43763 44.20249 1.000 100.02392 ? 127 ASP A N   1 
ATOM   859  C CA  . ASP A 1 120 ? 9.76413   36.99203 44.14677 1.000 88.20574  ? 127 ASP A CA  1 
ATOM   860  C C   . ASP A 1 120 ? 9.31287   36.56143 42.75171 1.000 84.77014  ? 127 ASP A C   1 
ATOM   861  O O   . ASP A 1 120 ? 9.24931   37.36735 41.81661 1.000 86.13659  ? 127 ASP A O   1 
ATOM   862  C CB  . ASP A 1 120 ? 8.81068   36.50383 45.24590 1.000 80.73446  ? 127 ASP A CB  1 
ATOM   863  C CG  . ASP A 1 120 ? 7.42030   37.11464 45.14666 1.000 84.17968  ? 127 ASP A CG  1 
ATOM   864  O OD1 . ASP A 1 120 ? 7.10602   37.76909 44.13044 1.000 89.15441  ? 127 ASP A OD1 1 
ATOM   865  O OD2 . ASP A 1 120 ? 6.63332   36.93450 46.09942 1.000 82.78727  ? 127 ASP A OD2 1 
ATOM   866  N N   . ILE A 1 121 ? 8.99461   35.27264 42.61630 1.000 81.79667  ? 128 ILE A N   1 
ATOM   867  C CA  . ILE A 1 121 ? 8.62064   34.72799 41.31545 1.000 72.56593  ? 128 ILE A CA  1 
ATOM   868  C C   . ILE A 1 121 ? 7.23199   35.20944 40.90277 1.000 72.70579  ? 128 ILE A C   1 
ATOM   869  O O   . ILE A 1 121 ? 6.93776   35.32944 39.70582 1.000 71.14980  ? 128 ILE A O   1 
ATOM   870  C CB  . ILE A 1 121 ? 8.72444   33.18935 41.35774 1.000 74.78981  ? 128 ILE A CB  1 
ATOM   871  C CG1 . ILE A 1 121 ? 10.19410  32.75997 41.37146 1.000 66.87142  ? 128 ILE A CG1 1 
ATOM   872  C CG2 . ILE A 1 121 ? 8.01290   32.54461 40.17968 1.000 75.62288  ? 128 ILE A CG2 1 
ATOM   873  C CD1 . ILE A 1 121 ? 10.69547  32.31569 42.72922 1.000 81.81685  ? 128 ILE A CD1 1 
ATOM   874  N N   . SER A 1 122 ? 6.37401   35.53614 41.87457 1.000 70.47310  ? 129 SER A N   1 
ATOM   875  C CA  . SER A 1 122 ? 5.00392   35.94146 41.57127 1.000 75.57839  ? 129 SER A CA  1 
ATOM   876  C C   . SER A 1 122 ? 4.93401   37.18460 40.69247 1.000 72.69256  ? 129 SER A C   1 
ATOM   877  O O   . SER A 1 122 ? 3.89545   37.42955 40.06966 1.000 76.07402  ? 129 SER A O   1 
ATOM   878  C CB  . SER A 1 122 ? 4.22766   36.18661 42.86695 1.000 79.00046  ? 129 SER A CB  1 
ATOM   879  O OG  . SER A 1 122 ? 4.57189   37.43414 43.44473 1.000 84.99472  ? 129 SER A OG  1 
ATOM   880  N N   . MET A 1 123 ? 6.00633   37.97601 40.62822 1.000 73.60202  ? 130 MET A N   1 
ATOM   881  C CA  . MET A 1 123 ? 6.04950   39.17078 39.79380 1.000 73.06333  ? 130 MET A CA  1 
ATOM   882  C C   . MET A 1 123 ? 6.62660   38.89818 38.40986 1.000 66.64868  ? 130 MET A C   1 
ATOM   883  O O   . MET A 1 123 ? 7.18181   39.80948 37.78232 1.000 66.58462  ? 130 MET A O   1 
ATOM   884  C CB  . MET A 1 123 ? 6.84666   40.26968 40.49754 1.000 77.21347  ? 130 MET A CB  1 
ATOM   885  C CG  . MET A 1 123 ? 5.98622   41.28335 41.23453 1.000 76.44797  ? 130 MET A CG  1 
ATOM   886  S SD  . MET A 1 123 ? 6.95084   42.37799 42.29272 1.000 90.78272  ? 130 MET A SD  1 
ATOM   887  C CE  . MET A 1 123 ? 6.58441   41.69781 43.90960 1.000 92.49953  ? 130 MET A CE  1 
ATOM   888  N N   . ILE A 1 124 ? 6.51118   37.66324 37.91642 1.000 67.21661  ? 131 ILE A N   1 
ATOM   889  C CA  . ILE A 1 124 ? 7.07729   37.32856 36.61399 1.000 60.24790  ? 131 ILE A CA  1 
ATOM   890  C C   . ILE A 1 124 ? 6.27221   37.96665 35.48906 1.000 65.20778  ? 131 ILE A C   1 
ATOM   891  O O   . ILE A 1 124 ? 6.80778   38.22611 34.40428 1.000 68.77049  ? 131 ILE A O   1 
ATOM   892  C CB  . ILE A 1 124 ? 7.16816   35.79768 36.45702 1.000 58.57375  ? 131 ILE A CB  1 
ATOM   893  C CG1 . ILE A 1 124 ? 8.02531   35.42185 35.24523 1.000 65.04849  ? 131 ILE A CG1 1 
ATOM   894  C CG2 . ILE A 1 124 ? 5.77929   35.17739 36.35781 1.000 63.66296  ? 131 ILE A CG2 1 
ATOM   895  C CD1 . ILE A 1 124 ? 8.27446   33.93427 35.10964 1.000 50.65471  ? 131 ILE A CD1 1 
ATOM   896  N N   . GLY A 1 125 ? 4.98827   38.24679 35.72423 1.000 67.16374  ? 132 GLY A N   1 
ATOM   897  C CA  . GLY A 1 125 ? 4.16101   38.81966 34.67735 1.000 65.06914  ? 132 GLY A CA  1 
ATOM   898  C C   . GLY A 1 125 ? 4.51332   40.25404 34.34435 1.000 67.79453  ? 132 GLY A C   1 
ATOM   899  O O   . GLY A 1 125 ? 4.27779   40.70825 33.22065 1.000 64.48735  ? 132 GLY A O   1 
ATOM   900  N N   . GLN A 1 126 ? 5.07939   40.98543 35.30443 1.000 67.38850  ? 133 GLN A N   1 
ATOM   901  C CA  . GLN A 1 126 ? 5.45058   42.37873 35.08942 1.000 67.87199  ? 133 GLN A CA  1 
ATOM   902  C C   . GLN A 1 126 ? 6.64627   42.54082 34.16026 1.000 71.89675  ? 133 GLN A C   1 
ATOM   903  O O   . GLN A 1 126 ? 7.01059   43.67965 33.84729 1.000 76.05293  ? 133 GLN A O   1 
ATOM   904  C CB  . GLN A 1 126 ? 5.74235   43.05055 36.43277 1.000 68.77502  ? 133 GLN A CB  1 
ATOM   905  C CG  . GLN A 1 126 ? 5.01286   42.42121 37.61153 1.000 75.56874  ? 133 GLN A CG  1 
ATOM   906  C CD  . GLN A 1 126 ? 3.65167   43.04377 37.85673 1.000 89.08025  ? 133 GLN A CD  1 
ATOM   907  O OE1 . GLN A 1 126 ? 3.23814   43.96068 37.14671 1.000 107.50472 ? 133 GLN A OE1 1 
ATOM   908  N NE2 . GLN A 1 126 ? 2.94576   42.54476 38.86500 1.000 85.25744  ? 133 GLN A NE2 1 
ATOM   909  N N   . PHE A 1 127 ? 7.25896   41.44606 33.71187 1.000 71.33042  ? 134 PHE A N   1 
ATOM   910  C CA  . PHE A 1 127 ? 8.41662   41.49748 32.82986 1.000 69.90988  ? 134 PHE A CA  1 
ATOM   911  C C   . PHE A 1 127 ? 8.12987   40.90816 31.45386 1.000 71.30275  ? 134 PHE A C   1 
ATOM   912  O O   . PHE A 1 127 ? 9.04593   40.80459 30.63126 1.000 74.68296  ? 134 PHE A O   1 
ATOM   913  C CB  . PHE A 1 127 ? 9.60263   40.77867 33.47881 1.000 71.92208  ? 134 PHE A CB  1 
ATOM   914  C CG  . PHE A 1 127 ? 10.06897  41.41286 34.76144 1.000 72.34746  ? 134 PHE A CG  1 
ATOM   915  C CD1 . PHE A 1 127 ? 9.45388   41.11145 35.96589 1.000 72.68097  ? 134 PHE A CD1 1 
ATOM   916  C CD2 . PHE A 1 127 ? 11.12205  42.31198 34.76083 1.000 74.65017  ? 134 PHE A CD2 1 
ATOM   917  C CE1 . PHE A 1 127 ? 9.88130   41.69447 37.14538 1.000 76.24959  ? 134 PHE A CE1 1 
ATOM   918  C CE2 . PHE A 1 127 ? 11.55427  42.89767 35.93671 1.000 76.23147  ? 134 PHE A CE2 1 
ATOM   919  C CZ  . PHE A 1 127 ? 10.93264  42.58853 37.13030 1.000 78.66887  ? 134 PHE A CZ  1 
ATOM   920  N N   . GLY A 1 128 ? 6.88384   40.52410 31.18288 1.000 69.39977  ? 135 GLY A N   1 
ATOM   921  C CA  . GLY A 1 128 ? 6.53588   39.97083 29.88941 1.000 54.83609  ? 135 GLY A CA  1 
ATOM   922  C C   . GLY A 1 128 ? 7.05809   38.57807 29.62930 1.000 57.92625  ? 135 GLY A C   1 
ATOM   923  O O   . GLY A 1 128 ? 7.13535   38.16272 28.47030 1.000 70.50879  ? 135 GLY A O   1 
ATOM   924  N N   . VAL A 1 129 ? 7.42154   37.84025 30.67657 1.000 62.17279  ? 136 VAL A N   1 
ATOM   925  C CA  . VAL A 1 129 ? 7.93622   36.48351 30.52894 1.000 58.07659  ? 136 VAL A CA  1 
ATOM   926  C C   . VAL A 1 129 ? 7.09582   35.53478 31.37359 1.000 59.08986  ? 136 VAL A C   1 
ATOM   927  O O   . VAL A 1 129 ? 7.60396   34.54200 31.90687 1.000 59.52792  ? 136 VAL A O   1 
ATOM   928  C CB  . VAL A 1 129 ? 9.42420   36.40744 30.91897 1.000 57.76634  ? 136 VAL A CB  1 
ATOM   929  C CG1 . VAL A 1 129 ? 10.27350  37.16466 29.91329 1.000 57.15649  ? 136 VAL A CG1 1 
ATOM   930  C CG2 . VAL A 1 129 ? 9.63736   36.96757 32.31729 1.000 52.88211  ? 136 VAL A CG2 1 
ATOM   931  N N   . GLY A 1 130 ? 5.79807   35.82663 31.48657 1.000 57.90977  ? 137 GLY A N   1 
ATOM   932  C CA  . GLY A 1 130 ? 4.92858   35.05661 32.35893 1.000 61.32637  ? 137 GLY A CA  1 
ATOM   933  C C   . GLY A 1 130 ? 4.65363   33.64239 31.89080 1.000 55.32090  ? 137 GLY A C   1 
ATOM   934  O O   . GLY A 1 130 ? 4.22510   32.81006 32.69703 1.000 51.74664  ? 137 GLY A O   1 
ATOM   935  N N   . PHE A 1 131 ? 4.88512   33.34919 30.60892 1.000 55.44151  ? 138 PHE A N   1 
ATOM   936  C CA  . PHE A 1 131 ? 4.61160   32.00583 30.10651 1.000 57.33489  ? 138 PHE A CA  1 
ATOM   937  C C   . PHE A 1 131 ? 5.56703   30.98318 30.70722 1.000 52.28662  ? 138 PHE A C   1 
ATOM   938  O O   . PHE A 1 131 ? 5.17672   29.83884 30.96539 1.000 51.08410  ? 138 PHE A O   1 
ATOM   939  C CB  . PHE A 1 131 ? 4.69660   31.98086 28.58092 1.000 60.81406  ? 138 PHE A CB  1 
ATOM   940  C CG  . PHE A 1 131 ? 4.93021   30.61018 28.00982 1.000 58.97637  ? 138 PHE A CG  1 
ATOM   941  C CD1 . PHE A 1 131 ? 3.91334   29.66962 27.99594 1.000 62.98055  ? 138 PHE A CD1 1 
ATOM   942  C CD2 . PHE A 1 131 ? 6.16632   30.26067 27.49029 1.000 61.02367  ? 138 PHE A CD2 1 
ATOM   943  C CE1 . PHE A 1 131 ? 4.12314   28.40701 27.47311 1.000 55.90104  ? 138 PHE A CE1 1 
ATOM   944  C CE2 . PHE A 1 131 ? 6.38271   28.99892 26.96638 1.000 60.55941  ? 138 PHE A CE2 1 
ATOM   945  C CZ  . PHE A 1 131 ? 5.35933   28.07140 26.95784 1.000 58.05635  ? 138 PHE A CZ  1 
ATOM   946  N N   . TYR A 1 132 ? 6.82199   31.37440 30.93726 1.000 55.88077  ? 139 TYR A N   1 
ATOM   947  C CA  . TYR A 1 132 ? 7.80076   30.45389 31.50288 1.000 48.58874  ? 139 TYR A CA  1 
ATOM   948  C C   . TYR A 1 132 ? 7.45792   30.03217 32.92457 1.000 53.46983  ? 139 TYR A C   1 
ATOM   949  O O   . TYR A 1 132 ? 8.03811   29.05965 33.41976 1.000 54.02460  ? 139 TYR A O   1 
ATOM   950  C CB  . TYR A 1 132 ? 9.19276   31.08423 31.45865 1.000 41.78549  ? 139 TYR A CB  1 
ATOM   951  C CG  . TYR A 1 132 ? 9.67000   31.37812 30.05477 1.000 54.08423  ? 139 TYR A CG  1 
ATOM   952  C CD1 . TYR A 1 132 ? 10.04313  30.35001 29.19850 1.000 50.01177  ? 139 TYR A CD1 1 
ATOM   953  C CD2 . TYR A 1 132 ? 9.73890   32.68173 29.58202 1.000 57.34218  ? 139 TYR A CD2 1 
ATOM   954  C CE1 . TYR A 1 132 ? 10.47677  30.61190 27.91334 1.000 44.22212  ? 139 TYR A CE1 1 
ATOM   955  C CE2 . TYR A 1 132 ? 10.17163  32.95364 28.29744 1.000 59.54780  ? 139 TYR A CE2 1 
ATOM   956  C CZ  . TYR A 1 132 ? 10.53914  31.91533 27.46792 1.000 56.30193  ? 139 TYR A CZ  1 
ATOM   957  O OH  . TYR A 1 132 ? 10.97061  32.18208 26.18857 1.000 68.09732  ? 139 TYR A OH  1 
ATOM   958  N N   . SER A 1 133 ? 6.53096   30.72772 33.58741 1.000 55.18355  ? 140 SER A N   1 
ATOM   959  C CA  . SER A 1 133 ? 6.03242   30.28150 34.88167 1.000 51.83860  ? 140 SER A CA  1 
ATOM   960  C C   . SER A 1 133 ? 5.23267   28.98994 34.78354 1.000 53.18135  ? 140 SER A C   1 
ATOM   961  O O   . SER A 1 133 ? 4.86588   28.42784 35.82105 1.000 58.43179  ? 140 SER A O   1 
ATOM   962  C CB  . SER A 1 133 ? 5.17142   31.37378 35.51889 1.000 55.63902  ? 140 SER A CB  1 
ATOM   963  O OG  . SER A 1 133 ? 4.00499   31.61590 34.75118 1.000 58.43385  ? 140 SER A OG  1 
ATOM   964  N N   . ALA A 1 134 ? 4.95161   28.51309 33.56823 1.000 54.83481  ? 141 ALA A N   1 
ATOM   965  C CA  . ALA A 1 134 ? 4.24683   27.24686 33.40890 1.000 53.85829  ? 141 ALA A CA  1 
ATOM   966  C C   . ALA A 1 134 ? 5.07415   26.07630 33.92241 1.000 54.88938  ? 141 ALA A C   1 
ATOM   967  O O   . ALA A 1 134 ? 4.51521   25.06561 34.36330 1.000 55.59414  ? 141 ALA A O   1 
ATOM   968  C CB  . ALA A 1 134 ? 3.88582   27.03483 31.94023 1.000 46.83350  ? 141 ALA A CB  1 
ATOM   969  N N   . TYR A 1 135 ? 6.39989   26.19362 33.88056 1.000 53.36124  ? 142 TYR A N   1 
ATOM   970  C CA  . TYR A 1 135 ? 7.28964   25.13335 34.33433 1.000 54.52962  ? 142 TYR A CA  1 
ATOM   971  C C   . TYR A 1 135 ? 7.38099   25.04503 35.85096 1.000 55.87664  ? 142 TYR A C   1 
ATOM   972  O O   . TYR A 1 135 ? 8.10442   24.18389 36.36270 1.000 55.87582  ? 142 TYR A O   1 
ATOM   973  C CB  . TYR A 1 135 ? 8.67554   25.33768 33.72170 1.000 47.41317  ? 142 TYR A CB  1 
ATOM   974  C CG  . TYR A 1 135 ? 8.69256   25.05325 32.23965 1.000 54.14734  ? 142 TYR A CG  1 
ATOM   975  C CD1 . TYR A 1 135 ? 8.92309   23.77070 31.76132 1.000 53.01701  ? 142 TYR A CD1 1 
ATOM   976  C CD2 . TYR A 1 135 ? 8.42143   26.05695 31.31988 1.000 53.52189  ? 142 TYR A CD2 1 
ATOM   977  C CE1 . TYR A 1 135 ? 8.92284   23.50424 30.40517 1.000 49.61988  ? 142 TYR A CE1 1 
ATOM   978  C CE2 . TYR A 1 135 ? 8.40989   25.79925 29.96360 1.000 52.06284  ? 142 TYR A CE2 1 
ATOM   979  C CZ  . TYR A 1 135 ? 8.66549   24.52189 29.51110 1.000 52.59572  ? 142 TYR A CZ  1 
ATOM   980  O OH  . TYR A 1 135 ? 8.65931   24.26119 28.15985 1.000 55.99126  ? 142 TYR A OH  1 
ATOM   981  N N   . LEU A 1 136 ? 6.67160   25.91316 36.57614 1.000 55.76959  ? 143 LEU A N   1 
ATOM   982  C CA  . LEU A 1 136 ? 6.54317   25.74148 38.01790 1.000 57.71497  ? 143 LEU A CA  1 
ATOM   983  C C   . LEU A 1 136 ? 5.80091   24.45627 38.35415 1.000 56.08864  ? 143 LEU A C   1 
ATOM   984  O O   . LEU A 1 136 ? 6.07472   23.82996 39.38430 1.000 54.41663  ? 143 LEU A O   1 
ATOM   985  C CB  . LEU A 1 136 ? 5.81698   26.94212 38.62752 1.000 56.81924  ? 143 LEU A CB  1 
ATOM   986  C CG  . LEU A 1 136 ? 6.57257   28.26943 38.71214 1.000 63.09687  ? 143 LEU A CG  1 
ATOM   987  C CD1 . LEU A 1 136 ? 5.61882   29.40186 39.06097 1.000 62.00421  ? 143 LEU A CD1 1 
ATOM   988  C CD2 . LEU A 1 136 ? 7.69564   28.18214 39.73216 1.000 59.53950  ? 143 LEU A CD2 1 
ATOM   989  N N   . VAL A 1 137 ? 4.86692   24.04731 37.49851 1.000 54.24399  ? 144 VAL A N   1 
ATOM   990  C CA  . VAL A 1 137 ? 4.03797   22.87409 37.75117 1.000 55.64367  ? 144 VAL A CA  1 
ATOM   991  C C   . VAL A 1 137 ? 4.10873   21.84261 36.63660 1.000 58.01635  ? 144 VAL A C   1 
ATOM   992  O O   . VAL A 1 137 ? 3.62306   20.71734 36.82846 1.000 64.01996  ? 144 VAL A O   1 
ATOM   993  C CB  . VAL A 1 137 ? 2.56644   23.27044 38.00109 1.000 52.55232  ? 144 VAL A CB  1 
ATOM   994  C CG1 . VAL A 1 137 ? 2.47143   24.27743 39.13543 1.000 55.52533  ? 144 VAL A CG1 1 
ATOM   995  C CG2 . VAL A 1 137 ? 1.94750   23.83348 36.73038 1.000 53.06574  ? 144 VAL A CG2 1 
ATOM   996  N N   . ALA A 1 138 ? 4.68744   22.17187 35.48588 1.000 53.29399  ? 145 ALA A N   1 
ATOM   997  C CA  . ALA A 1 138 ? 4.72647   21.27485 34.33949 1.000 53.05022  ? 145 ALA A CA  1 
ATOM   998  C C   . ALA A 1 138 ? 6.15880   20.83737 34.07003 1.000 60.07402  ? 145 ALA A C   1 
ATOM   999  O O   . ALA A 1 138 ? 7.06982   21.67106 34.02643 1.000 58.75361  ? 145 ALA A O   1 
ATOM   1000 C CB  . ALA A 1 138 ? 4.13997   21.94876 33.09697 1.000 50.83395  ? 145 ALA A CB  1 
ATOM   1001 N N   . GLU A 1 139 ? 6.35320   19.52879 33.89350 1.000 56.80559  ? 146 GLU A N   1 
ATOM   1002 C CA  . GLU A 1 139 ? 7.64968   19.01136 33.47670 1.000 52.91997  ? 146 GLU A CA  1 
ATOM   1003 C C   . GLU A 1 139 ? 7.85174   19.10802 31.97139 1.000 55.62433  ? 146 GLU A C   1 
ATOM   1004 O O   . GLU A 1 139 ? 8.99697   19.07708 31.50825 1.000 57.67936  ? 146 GLU A O   1 
ATOM   1005 C CB  . GLU A 1 139 ? 7.81087   17.55618 33.92346 1.000 59.26991  ? 146 GLU A CB  1 
ATOM   1006 C CG  . GLU A 1 139 ? 6.58782   16.68854 33.67462 1.000 65.95398  ? 146 GLU A CG  1 
ATOM   1007 C CD  . GLU A 1 139 ? 6.66389   15.35334 34.39014 1.000 93.03633  ? 146 GLU A CD  1 
ATOM   1008 O OE1 . GLU A 1 139 ? 6.79480   14.31701 33.70512 1.000 99.87446  ? 146 GLU A OE1 1 
ATOM   1009 O OE2 . GLU A 1 139 ? 6.59400   15.33963 35.63732 1.000 95.54989  ? 146 GLU A OE2 1 
ATOM   1010 N N   . LYS A 1 140 ? 6.76935   19.22507 31.20526 1.000 57.46309  ? 147 LYS A N   1 
ATOM   1011 C CA  . LYS A 1 140 ? 6.83960   19.35337 29.75785 1.000 51.49799  ? 147 LYS A CA  1 
ATOM   1012 C C   . LYS A 1 140 ? 5.64694   20.17269 29.28909 1.000 50.33721  ? 147 LYS A C   1 
ATOM   1013 O O   . LYS A 1 140 ? 4.51976   19.95007 29.73829 1.000 50.35793  ? 147 LYS A O   1 
ATOM   1014 C CB  . LYS A 1 140 ? 6.85404   17.98071 29.07507 1.000 52.93434  ? 147 LYS A CB  1 
ATOM   1015 C CG  . LYS A 1 140 ? 6.80239   18.03396 27.55861 1.000 52.81494  ? 147 LYS A CG  1 
ATOM   1016 C CD  . LYS A 1 140 ? 7.15860   16.68706 26.95176 1.000 56.40284  ? 147 LYS A CD  1 
ATOM   1017 C CE  . LYS A 1 140 ? 5.97679   16.08002 26.21565 1.000 57.23952  ? 147 LYS A CE  1 
ATOM   1018 N NZ  . LYS A 1 140 ? 6.05288   14.59338 26.18062 1.000 64.36992  ? 147 LYS A NZ  1 
ATOM   1019 N N   . VAL A 1 141 ? 5.90190   21.12310 28.39369 1.000 46.93874  ? 148 VAL A N   1 
ATOM   1020 C CA  . VAL A 1 141 ? 4.87872   22.03079 27.88984 1.000 43.51904  ? 148 VAL A CA  1 
ATOM   1021 C C   . VAL A 1 141 ? 4.81145   21.89320 26.37623 1.000 47.38748  ? 148 VAL A C   1 
ATOM   1022 O O   . VAL A 1 141 ? 5.82901   22.03728 25.68860 1.000 54.47609  ? 148 VAL A O   1 
ATOM   1023 C CB  . VAL A 1 141 ? 5.16395   23.48923 28.29286 1.000 44.43037  ? 148 VAL A CB  1 
ATOM   1024 C CG1 . VAL A 1 141 ? 4.16644   24.42719 27.63082 1.000 50.48619  ? 148 VAL A CG1 1 
ATOM   1025 C CG2 . VAL A 1 141 ? 5.12354   23.63974 29.80553 1.000 46.73242  ? 148 VAL A CG2 1 
ATOM   1026 N N   . THR A 1 142 ? 3.61705   21.61407 25.86281 1.000 43.65173  ? 149 THR A N   1 
ATOM   1027 C CA  . THR A 1 142 ? 3.36775   21.52802 24.43058 1.000 45.41247  ? 149 THR A CA  1 
ATOM   1028 C C   . THR A 1 142 ? 2.43657   22.65958 24.01947 1.000 49.53777  ? 149 THR A C   1 
ATOM   1029 O O   . THR A 1 142 ? 1.41362   22.89401 24.67198 1.000 52.77164  ? 149 THR A O   1 
ATOM   1030 C CB  . THR A 1 142 ? 2.75522   20.17720 24.05279 1.000 46.50405  ? 149 THR A CB  1 
ATOM   1031 O OG1 . THR A 1 142 ? 3.39067   19.13449 24.80269 1.000 48.76791  ? 149 THR A OG1 1 
ATOM   1032 C CG2 . THR A 1 142 ? 2.93727   19.90887 22.56558 1.000 47.93399  ? 149 THR A CG2 1 
ATOM   1033 N N   . VAL A 1 143 ? 2.79117   23.35695 22.94301 1.000 45.37723  ? 150 VAL A N   1 
ATOM   1034 C CA  . VAL A 1 143 ? 2.03090   24.50226 22.45438 1.000 50.09901  ? 150 VAL A CA  1 
ATOM   1035 C C   . VAL A 1 143 ? 1.63428   24.23714 21.00884 1.000 51.81364  ? 150 VAL A C   1 
ATOM   1036 O O   . VAL A 1 143 ? 2.49982   24.03555 20.14756 1.000 55.45357  ? 150 VAL A O   1 
ATOM   1037 C CB  . VAL A 1 143 ? 2.82814   25.81125 22.56961 1.000 46.02762  ? 150 VAL A CB  1 
ATOM   1038 C CG1 . VAL A 1 143 ? 1.99236   26.98317 22.08211 1.000 50.43079  ? 150 VAL A CG1 1 
ATOM   1039 C CG2 . VAL A 1 143 ? 3.27186   26.03728 24.00468 1.000 49.66377  ? 150 VAL A CG2 1 
ATOM   1040 N N   . ILE A 1 144 ? 0.33053   24.23810 20.74586 1.000 48.40843  ? 151 ILE A N   1 
ATOM   1041 C CA  . ILE A 1 144 ? -0.21494  24.13135 19.39740 1.000 54.16085  ? 151 ILE A CA  1 
ATOM   1042 C C   . ILE A 1 144 ? -0.89265  25.45546 19.07617 1.000 51.83547  ? 151 ILE A C   1 
ATOM   1043 O O   . ILE A 1 144 ? -1.79313  25.89177 19.80420 1.000 55.74668  ? 151 ILE A O   1 
ATOM   1044 C CB  . ILE A 1 144 ? -1.19898  22.95826 19.27022 1.000 53.12318  ? 151 ILE A CB  1 
ATOM   1045 C CG1 . ILE A 1 144 ? -0.71049  21.75976 20.08775 1.000 45.73383  ? 151 ILE A CG1 1 
ATOM   1046 C CG2 . ILE A 1 144 ? -1.38853  22.57485 17.80855 1.000 52.43701  ? 151 ILE A CG2 1 
ATOM   1047 C CD1 . ILE A 1 144 ? 0.36338   20.94369 19.40050 1.000 51.99608  ? 151 ILE A CD1 1 
ATOM   1048 N N   . THR A 1 145 ? -0.45861  26.09959 17.99538 1.000 46.18714  ? 152 THR A N   1 
ATOM   1049 C CA  . THR A 1 145 ? -0.95693  27.41990 17.64238 1.000 50.28394  ? 152 THR A CA  1 
ATOM   1050 C C   . THR A 1 145 ? -1.27286  27.46904 16.15518 1.000 51.07080  ? 152 THR A C   1 
ATOM   1051 O O   . THR A 1 145 ? -0.80631  26.64033 15.36982 1.000 50.60802  ? 152 THR A O   1 
ATOM   1052 C CB  . THR A 1 145 ? 0.05091   28.52082 18.00066 1.000 49.61746  ? 152 THR A CB  1 
ATOM   1053 O OG1 . THR A 1 145 ? -0.52261  29.80471 17.72521 1.000 56.36444  ? 152 THR A OG1 1 
ATOM   1054 C CG2 . THR A 1 145 ? 1.32930   28.35640 17.19274 1.000 47.72320  ? 152 THR A CG2 1 
ATOM   1055 N N   . LYS A 1 146 ? -2.07710  28.46147 15.77797 1.000 50.46417  ? 153 LYS A N   1 
ATOM   1056 C CA  . LYS A 1 146 ? -2.46720  28.65051 14.38318 1.000 51.66317  ? 153 LYS A CA  1 
ATOM   1057 C C   . LYS A 1 146 ? -2.67301  30.14001 14.14876 1.000 52.39292  ? 153 LYS A C   1 
ATOM   1058 O O   . LYS A 1 146 ? -3.59590  30.73470 14.71327 1.000 54.88288  ? 153 LYS A O   1 
ATOM   1059 C CB  . LYS A 1 146 ? -3.73277  27.86290 14.05196 1.000 49.63787  ? 153 LYS A CB  1 
ATOM   1060 C CG  . LYS A 1 146 ? -4.22367  28.05199 12.62562 1.000 45.20320  ? 153 LYS A CG  1 
ATOM   1061 C CD  . LYS A 1 146 ? -3.15495  27.66407 11.61702 1.000 52.15399  ? 153 LYS A CD  1 
ATOM   1062 C CE  . LYS A 1 146 ? -3.63191  27.89766 10.19368 1.000 55.32542  ? 153 LYS A CE  1 
ATOM   1063 N NZ  . LYS A 1 146 ? -3.71398  29.34998 9.87510  1.000 50.19605  ? 153 LYS A NZ  1 
ATOM   1064 N N   . HIS A 1 147 ? -1.81804  30.73640 13.32418 1.000 53.91991  ? 154 HIS A N   1 
ATOM   1065 C CA  . HIS A 1 147 ? -1.93059  32.13799 12.95178 1.000 47.11647  ? 154 HIS A CA  1 
ATOM   1066 C C   . HIS A 1 147 ? -2.53858  32.25545 11.55890 1.000 53.09963  ? 154 HIS A C   1 
ATOM   1067 O O   . HIS A 1 147 ? -2.44363  31.33677 10.74077 1.000 60.98008  ? 154 HIS A O   1 
ATOM   1068 C CB  . HIS A 1 147 ? -0.56226  32.82510 12.99448 1.000 47.34701  ? 154 HIS A CB  1 
ATOM   1069 C CG  . HIS A 1 147 ? -0.62374  34.31368 12.83895 1.000 47.61906  ? 154 HIS A CG  1 
ATOM   1070 N ND1 . HIS A 1 147 ? -0.57838  34.93686 11.61056 1.000 47.20285  ? 154 HIS A ND1 1 
ATOM   1071 C CD2 . HIS A 1 147 ? -0.72653  35.30279 13.75806 1.000 49.44654  ? 154 HIS A CD2 1 
ATOM   1072 C CE1 . HIS A 1 147 ? -0.65060  36.24506 11.77909 1.000 47.54688  ? 154 HIS A CE1 1 
ATOM   1073 N NE2 . HIS A 1 147 ? -0.74155  36.49353 13.07301 1.000 55.34563  ? 154 HIS A NE2 1 
ATOM   1074 N N   . ASN A 1 148 ? -3.17203  33.40194 11.29829 1.000 51.79196  ? 155 ASN A N   1 
ATOM   1075 C CA  . ASN A 1 148 ? -3.85738  33.60738 10.02673 1.000 47.06501  ? 155 ASN A CA  1 
ATOM   1076 C C   . ASN A 1 148 ? -2.90146  33.62372 8.84113  1.000 54.60781  ? 155 ASN A C   1 
ATOM   1077 O O   . ASN A 1 148 ? -3.33621  33.39411 7.70711  1.000 59.02944  ? 155 ASN A O   1 
ATOM   1078 C CB  . ASN A 1 148 ? -4.65108  34.91496 10.06330 1.000 53.03819  ? 155 ASN A CB  1 
ATOM   1079 C CG  . ASN A 1 148 ? -6.05604  34.73096 10.60145 1.000 59.22584  ? 155 ASN A CG  1 
ATOM   1080 O OD1 . ASN A 1 148 ? -6.51132  33.60667 10.81158 1.000 61.98721  ? 155 ASN A OD1 1 
ATOM   1081 N ND2 . ASN A 1 148 ? -6.75283  35.83931 10.82585 1.000 51.67119  ? 155 ASN A ND2 1 
ATOM   1082 N N   . ASP A 1 149 ? -1.61415  33.88338 9.07262  1.000 53.22938  ? 156 ASP A N   1 
ATOM   1083 C CA  . ASP A 1 149 ? -0.63593  34.02049 8.00126  1.000 57.73045  ? 156 ASP A CA  1 
ATOM   1084 C C   . ASP A 1 149 ? 0.39568   32.89651 8.00189  1.000 55.85076  ? 156 ASP A C   1 
ATOM   1085 O O   . ASP A 1 149 ? 1.47434   33.05176 7.42080  1.000 58.02856  ? 156 ASP A O   1 
ATOM   1086 C CB  . ASP A 1 149 ? 0.06262   35.37723 8.10015  1.000 53.21065  ? 156 ASP A CB  1 
ATOM   1087 C CG  . ASP A 1 149 ? -0.87588  36.53732 7.83189  1.000 67.18290  ? 156 ASP A CG  1 
ATOM   1088 O OD1 . ASP A 1 149 ? -1.68006  36.44787 6.88018  1.000 75.12884  ? 156 ASP A OD1 1 
ATOM   1089 O OD2 . ASP A 1 149 ? -0.81125  37.53851 8.57575  1.000 67.29937  ? 156 ASP A OD2 1 
ATOM   1090 N N   . ASP A 1 150 ? 0.08981   31.76796 8.63794  1.000 51.05311  ? 157 ASP A N   1 
ATOM   1091 C CA  . ASP A 1 150 ? 1.02748   30.65683 8.70452  1.000 51.31182  ? 157 ASP A CA  1 
ATOM   1092 C C   . ASP A 1 150 ? 0.25349   29.35999 8.89130  1.000 54.53585  ? 157 ASP A C   1 
ATOM   1093 O O   . ASP A 1 150 ? -0.96854  29.35756 9.05877  1.000 52.22293  ? 157 ASP A O   1 
ATOM   1094 C CB  . ASP A 1 150 ? 2.04467   30.85060 9.83482  1.000 54.07973  ? 157 ASP A CB  1 
ATOM   1095 C CG  . ASP A 1 150 ? 3.40302   30.26657 9.50216  1.000 58.52117  ? 157 ASP A CG  1 
ATOM   1096 O OD1 . ASP A 1 150 ? 3.48058   29.42942 8.57853  1.000 58.59152  ? 157 ASP A OD1 1 
ATOM   1097 O OD2 . ASP A 1 150 ? 4.39292   30.64439 10.16433 1.000 57.59992  ? 157 ASP A OD2 1 
ATOM   1098 N N   . GLU A 1 151 ? 0.98617   28.24940 8.85796  1.000 52.31370  ? 158 GLU A N   1 
ATOM   1099 C CA  . GLU A 1 151 ? 0.40214   26.93510 9.06868  1.000 49.03567  ? 158 GLU A CA  1 
ATOM   1100 C C   . GLU A 1 151 ? 0.28887   26.64346 10.56387 1.000 52.57840  ? 158 GLU A C   1 
ATOM   1101 O O   . GLU A 1 151 ? 0.71071   27.43122 11.41536 1.000 60.70063  ? 158 GLU A O   1 
ATOM   1102 C CB  . GLU A 1 151 ? 1.23719   25.86408 8.37051  1.000 52.74659  ? 158 GLU A CB  1 
ATOM   1103 C CG  . GLU A 1 151 ? 1.14570   25.87837 6.85534  1.000 61.08972  ? 158 GLU A CG  1 
ATOM   1104 C CD  . GLU A 1 151 ? 1.79627   24.66141 6.22614  1.000 79.27030  ? 158 GLU A CD  1 
ATOM   1105 O OE1 . GLU A 1 151 ? 3.03282   24.52473 6.33767  1.000 81.90759  ? 158 GLU A OE1 1 
ATOM   1106 O OE2 . GLU A 1 151 ? 1.07351   23.84232 5.62024  1.000 87.98728  ? 158 GLU A OE2 1 
ATOM   1107 N N   . GLN A 1 152 ? -0.29051  25.49113 10.88960 1.000 50.80886  ? 159 GLN A N   1 
ATOM   1108 C CA  . GLN A 1 152 ? -0.35995  25.04292 12.27295 1.000 52.75927  ? 159 GLN A CA  1 
ATOM   1109 C C   . GLN A 1 152 ? 0.97063   24.42004 12.67515 1.000 56.78793  ? 159 GLN A C   1 
ATOM   1110 O O   . GLN A 1 152 ? 1.53185   23.60428 11.93694 1.000 61.46789  ? 159 GLN A O   1 
ATOM   1111 C CB  . GLN A 1 152 ? -1.49555  24.03729 12.45528 1.000 54.87268  ? 159 GLN A CB  1 
ATOM   1112 C CG  . GLN A 1 152 ? -2.33835  24.27680 13.69570 1.000 49.64540  ? 159 GLN A CG  1 
ATOM   1113 C CD  . GLN A 1 152 ? -3.66302  23.54434 13.64986 1.000 57.99252  ? 159 GLN A CD  1 
ATOM   1114 O OE1 . GLN A 1 152 ? -4.72147  24.16063 13.53162 1.000 72.42976  ? 159 GLN A OE1 1 
ATOM   1115 N NE2 . GLN A 1 152 ? -3.61170  22.22114 13.74642 1.000 64.09299  ? 159 GLN A NE2 1 
ATOM   1116 N N   . TYR A 1 153 ? 1.47539   24.80497 13.84449 1.000 51.76168  ? 160 TYR A N   1 
ATOM   1117 C CA  . TYR A 1 153 ? 2.77323   24.34803 14.31453 1.000 52.07884  ? 160 TYR A CA  1 
ATOM   1118 C C   . TYR A 1 153 ? 2.65579   23.82033 15.73706 1.000 56.69814  ? 160 TYR A C   1 
ATOM   1119 O O   . TYR A 1 153 ? 1.68285   24.08924 16.44636 1.000 55.46167  ? 160 TYR A O   1 
ATOM   1120 C CB  . TYR A 1 153 ? 3.81807   25.46990 14.25028 1.000 57.20309  ? 160 TYR A CB  1 
ATOM   1121 C CG  . TYR A 1 153 ? 4.32000   25.73938 12.85110 1.000 59.23865  ? 160 TYR A CG  1 
ATOM   1122 C CD1 . TYR A 1 153 ? 5.17240   24.84632 12.21639 1.000 55.24363  ? 160 TYR A CD1 1 
ATOM   1123 C CD2 . TYR A 1 153 ? 3.93534   26.88190 12.16149 1.000 59.29526  ? 160 TYR A CD2 1 
ATOM   1124 C CE1 . TYR A 1 153 ? 5.63107   25.08421 10.93618 1.000 62.72641  ? 160 TYR A CE1 1 
ATOM   1125 C CE2 . TYR A 1 153 ? 4.38951   27.12923 10.88006 1.000 59.16488  ? 160 TYR A CE2 1 
ATOM   1126 C CZ  . TYR A 1 153 ? 5.23653   26.22676 10.27229 1.000 67.04295  ? 160 TYR A CZ  1 
ATOM   1127 O OH  . TYR A 1 153 ? 5.69236   26.46828 8.99635  1.000 81.31058  ? 160 TYR A OH  1 
ATOM   1128 N N   . ALA A 1 154 ? 3.66939   23.05911 16.14616 1.000 60.18278  ? 161 ALA A N   1 
ATOM   1129 C CA  . ALA A 1 154 ? 3.71050   22.44330 17.46659 1.000 51.73503  ? 161 ALA A CA  1 
ATOM   1130 C C   . ALA A 1 154 ? 5.01055   22.82900 18.15381 1.000 48.93370  ? 161 ALA A C   1 
ATOM   1131 O O   . ALA A 1 154 ? 6.09633   22.52474 17.64941 1.000 51.79054  ? 161 ALA A O   1 
ATOM   1132 C CB  . ALA A 1 154 ? 3.58420   20.92043 17.37142 1.000 48.86043  ? 161 ALA A CB  1 
ATOM   1133 N N   . TRP A 1 155 ? 4.89628   23.49545 19.29833 1.000 45.45002  ? 162 TRP A N   1 
ATOM   1134 C CA  . TRP A 1 155 ? 6.03192   23.87381 20.12566 1.000 43.42369  ? 162 TRP A CA  1 
ATOM   1135 C C   . TRP A 1 155 ? 6.07778   22.96521 21.34601 1.000 47.49611  ? 162 TRP A C   1 
ATOM   1136 O O   . TRP A 1 155 ? 5.04330   22.68995 21.96092 1.000 56.05998  ? 162 TRP A O   1 
ATOM   1137 C CB  . TRP A 1 155 ? 5.92325   25.34078 20.55469 1.000 49.47430  ? 162 TRP A CB  1 
ATOM   1138 C CG  . TRP A 1 155 ? 7.10977   25.86775 21.30418 1.000 51.89933  ? 162 TRP A CG  1 
ATOM   1139 C CD1 . TRP A 1 155 ? 8.15282   26.57952 20.78769 1.000 50.18319  ? 162 TRP A CD1 1 
ATOM   1140 C CD2 . TRP A 1 155 ? 7.36444   25.74668 22.70990 1.000 51.00793  ? 162 TRP A CD2 1 
ATOM   1141 N NE1 . TRP A 1 155 ? 9.04523   26.90060 21.78096 1.000 43.71143  ? 162 TRP A NE1 1 
ATOM   1142 C CE2 . TRP A 1 155 ? 8.58473   26.40050 22.97035 1.000 48.45071  ? 162 TRP A CE2 1 
ATOM   1143 C CE3 . TRP A 1 155 ? 6.68238   25.14443 23.77186 1.000 50.01955  ? 162 TRP A CE3 1 
ATOM   1144 C CZ2 . TRP A 1 155 ? 9.13666   26.46926 24.24752 1.000 48.87788  ? 162 TRP A CZ2 1 
ATOM   1145 C CZ3 . TRP A 1 155 ? 7.23257   25.21385 25.03917 1.000 50.60740  ? 162 TRP A CZ3 1 
ATOM   1146 C CH2 . TRP A 1 155 ? 8.44718   25.87155 25.26592 1.000 50.50106  ? 162 TRP A CH2 1 
ATOM   1147 N N   . GLU A 1 156 ? 7.27389   22.49471 21.69336 1.000 45.88968  ? 163 GLU A N   1 
ATOM   1148 C CA  . GLU A 1 156 ? 7.41808   21.55120 22.79274 1.000 45.44496  ? 163 GLU A CA  1 
ATOM   1149 C C   . GLU A 1 156 ? 8.80111   21.69146 23.40960 1.000 50.39071  ? 163 GLU A C   1 
ATOM   1150 O O   . GLU A 1 156 ? 9.79101   21.87033 22.69472 1.000 50.17630  ? 163 GLU A O   1 
ATOM   1151 C CB  . GLU A 1 156 ? 7.19802   20.11020 22.31831 1.000 45.81360  ? 163 GLU A CB  1 
ATOM   1152 C CG  . GLU A 1 156 ? 7.23796   19.07418 23.42845 1.000 51.62424  ? 163 GLU A CG  1 
ATOM   1153 C CD  . GLU A 1 156 ? 6.46779   17.81808 23.07663 1.000 56.87637  ? 163 GLU A CD  1 
ATOM   1154 O OE1 . GLU A 1 156 ? 7.02873   16.95206 22.37222 1.000 61.97936  ? 163 GLU A OE1 1 
ATOM   1155 O OE2 . GLU A 1 156 ? 5.29828   17.70020 23.49788 1.000 58.88236  ? 163 GLU A OE2 1 
ATOM   1156 N N   . SER A 1 157 ? 8.86058   21.60102 24.73829 1.000 48.05972  ? 164 SER A N   1 
ATOM   1157 C CA  . SER A 1 157 ? 10.12887  21.67100 25.45300 1.000 52.61449  ? 164 SER A CA  1 
ATOM   1158 C C   . SER A 1 157 ? 9.95039   21.10212 26.85123 1.000 51.03203  ? 164 SER A C   1 
ATOM   1159 O O   . SER A 1 157 ? 9.01169   21.47813 27.55949 1.000 48.88627  ? 164 SER A O   1 
ATOM   1160 C CB  . SER A 1 157 ? 10.64162  23.11252 25.53567 1.000 56.08681  ? 164 SER A CB  1 
ATOM   1161 O OG  . SER A 1 157 ? 11.82631  23.18859 26.31102 1.000 62.86602  ? 164 SER A OG  1 
ATOM   1162 N N   . SER A 1 158 ? 10.84787  20.19847 27.23954 1.000 59.58317  ? 165 SER A N   1 
ATOM   1163 C CA  . SER A 1 158 ? 10.96193  19.72906 28.61886 1.000 56.81233  ? 165 SER A CA  1 
ATOM   1164 C C   . SER A 1 158 ? 12.06778  20.46981 29.35642 1.000 65.36363  ? 165 SER A C   1 
ATOM   1165 O O   . SER A 1 158 ? 12.78183  19.88740 30.17913 1.000 63.25861  ? 165 SER A O   1 
ATOM   1166 C CB  . SER A 1 158 ? 11.20570  18.22333 28.65413 1.000 47.68375  ? 165 SER A CB  1 
ATOM   1167 O OG  . SER A 1 158 ? 10.18290  17.52292 27.96892 1.000 62.94240  ? 165 SER A OG  1 
ATOM   1168 N N   . ALA A 1 159 ? 12.21876  21.75691 29.06365 1.000 59.76289  ? 166 ALA A N   1 
ATOM   1169 C CA  . ALA A 1 159 ? 13.31138  22.60516 29.56859 1.000 58.33633  ? 166 ALA A CA  1 
ATOM   1170 C C   . ALA A 1 159 ? 14.62734  21.96821 29.11137 1.000 57.48036  ? 166 ALA A C   1 
ATOM   1171 O O   . ALA A 1 159 ? 14.73755  21.54539 27.95023 1.000 63.87225  ? 166 ALA A O   1 
ATOM   1172 C CB  . ALA A 1 159 ? 13.17849  22.80710 31.06142 1.000 51.53439  ? 166 ALA A CB  1 
ATOM   1173 N N   . GLY A 1 160 ? 15.63393  21.88243 29.97925 1.000 50.26253  ? 167 GLY A N   1 
ATOM   1174 C CA  . GLY A 1 160 ? 16.91926  21.33446 29.60733 1.000 54.16105  ? 167 GLY A CA  1 
ATOM   1175 C C   . GLY A 1 160 ? 17.75145  22.19760 28.68764 1.000 62.38610  ? 167 GLY A C   1 
ATOM   1176 O O   . GLY A 1 160 ? 18.89805  21.83313 28.39917 1.000 73.61429  ? 167 GLY A O   1 
ATOM   1177 N N   . GLY A 1 161 ? 17.22278  23.32444 28.21266 1.000 60.11517  ? 168 GLY A N   1 
ATOM   1178 C CA  . GLY A 1 161 ? 17.96074  24.22601 27.35486 1.000 60.80671  ? 168 GLY A CA  1 
ATOM   1179 C C   . GLY A 1 161 ? 17.62717  24.14583 25.88108 1.000 54.46514  ? 168 GLY A C   1 
ATOM   1180 O O   . GLY A 1 161 ? 18.24700  24.86429 25.08761 1.000 62.23117  ? 168 GLY A O   1 
ATOM   1181 N N   . SER A 1 162 ? 16.67198  23.30604 25.48653 1.000 50.55162  ? 169 SER A N   1 
ATOM   1182 C CA  . SER A 1 162 ? 16.33086  23.13992 24.08161 1.000 52.78918  ? 169 SER A CA  1 
ATOM   1183 C C   . SER A 1 162 ? 14.82242  23.00476 23.92898 1.000 54.61339  ? 169 SER A C   1 
ATOM   1184 O O   . SER A 1 162 ? 14.11037  22.64069 24.86827 1.000 53.51177  ? 169 SER A O   1 
ATOM   1185 C CB  . SER A 1 162 ? 17.03090  21.91718 23.47123 1.000 52.85656  ? 169 SER A CB  1 
ATOM   1186 O OG  . SER A 1 162 ? 16.49282  20.71173 23.98691 1.000 49.11795  ? 169 SER A OG  1 
ATOM   1187 N N   . PHE A 1 163 ? 14.34292  23.30381 22.72231 1.000 47.38390  ? 170 PHE A N   1 
ATOM   1188 C CA  . PHE A 1 163 ? 12.93730  23.14390 22.38141 1.000 52.50896  ? 170 PHE A CA  1 
ATOM   1189 C C   . PHE A 1 163 ? 12.82305  22.70411 20.92912 1.000 51.60317  ? 170 PHE A C   1 
ATOM   1190 O O   . PHE A 1 163 ? 13.74298  22.88650 20.12794 1.000 47.55988  ? 170 PHE A O   1 
ATOM   1191 C CB  . PHE A 1 163 ? 12.13855  24.43512 22.62036 1.000 53.28964  ? 170 PHE A CB  1 
ATOM   1192 C CG  . PHE A 1 163 ? 12.52255  25.57420 21.71684 1.000 54.14036  ? 170 PHE A CG  1 
ATOM   1193 C CD1 . PHE A 1 163 ? 13.58894  26.39758 22.03572 1.000 54.01043  ? 170 PHE A CD1 1 
ATOM   1194 C CD2 . PHE A 1 163 ? 11.79566  25.84385 20.56764 1.000 52.44919  ? 170 PHE A CD2 1 
ATOM   1195 C CE1 . PHE A 1 163 ? 13.93826  27.45423 21.21624 1.000 55.05047  ? 170 PHE A CE1 1 
ATOM   1196 C CE2 . PHE A 1 163 ? 12.14040  26.90055 19.74346 1.000 55.51508  ? 170 PHE A CE2 1 
ATOM   1197 C CZ  . PHE A 1 163 ? 13.21114  27.70789 20.07072 1.000 56.92045  ? 170 PHE A CZ  1 
ATOM   1198 N N   . THR A 1 164 ? 11.67658  22.11524 20.59959 1.000 50.75955  ? 171 THR A N   1 
ATOM   1199 C CA  . THR A 1 164 ? 11.41492  21.59235 19.26842 1.000 47.50902  ? 171 THR A CA  1 
ATOM   1200 C C   . THR A 1 164 ? 10.23331  22.31922 18.64000 1.000 50.55891  ? 171 THR A C   1 
ATOM   1201 O O   . THR A 1 164 ? 9.31800   22.77193 19.33445 1.000 49.71437  ? 171 THR A O   1 
ATOM   1202 C CB  . THR A 1 164 ? 11.13356  20.08366 19.30684 1.000 44.94305  ? 171 THR A CB  1 
ATOM   1203 O OG1 . THR A 1 164 ? 9.94914   19.83450 20.07437 1.000 51.38631  ? 171 THR A OG1 1 
ATOM   1204 C CG2 . THR A 1 164 ? 12.30426  19.34033 19.93160 1.000 52.14049  ? 171 THR A CG2 1 
ATOM   1205 N N   . VAL A 1 165 ? 10.26770  22.43034 17.31380 1.000 52.66167  ? 172 VAL A N   1 
ATOM   1206 C CA  . VAL A 1 165 ? 9.19751   23.04775 16.53792 1.000 52.46075  ? 172 VAL A CA  1 
ATOM   1207 C C   . VAL A 1 165 ? 8.93871   22.17785 15.31634 1.000 53.07882  ? 172 VAL A C   1 
ATOM   1208 O O   . VAL A 1 165 ? 9.87602   21.81295 14.59921 1.000 51.02559  ? 172 VAL A O   1 
ATOM   1209 C CB  . VAL A 1 165 ? 9.54614   24.48859 16.11282 1.000 48.33171  ? 172 VAL A CB  1 
ATOM   1210 C CG1 . VAL A 1 165 ? 8.56064   24.99061 15.06750 1.000 51.70919  ? 172 VAL A CG1 1 
ATOM   1211 C CG2 . VAL A 1 165 ? 9.55938   25.41243 17.31908 1.000 50.93287  ? 172 VAL A CG2 1 
ATOM   1212 N N   . ARG A 1 166 ? 7.67199   21.84228 15.08135 1.000 55.61366  ? 173 ARG A N   1 
ATOM   1213 C CA  . ARG A 1 166 ? 7.30129   21.00266 13.95247 1.000 55.62941  ? 173 ARG A CA  1 
ATOM   1214 C C   . ARG A 1 166 ? 5.92865   21.42041 13.44880 1.000 57.39195  ? 173 ARG A C   1 
ATOM   1215 O O   . ARG A 1 166 ? 5.16886   22.09777 14.14553 1.000 57.99429  ? 173 ARG A O   1 
ATOM   1216 C CB  . ARG A 1 166 ? 7.29600   19.51776 14.33331 1.000 59.46646  ? 173 ARG A CB  1 
ATOM   1217 C CG  . ARG A 1 166 ? 6.65291   19.23258 15.68157 1.000 64.09809  ? 173 ARG A CG  1 
ATOM   1218 C CD  . ARG A 1 166 ? 6.05896   17.83385 15.73283 1.000 66.33159  ? 173 ARG A CD  1 
ATOM   1219 N NE  . ARG A 1 166 ? 4.93167   17.75593 16.65464 1.000 80.21890  ? 173 ARG A NE  1 
ATOM   1220 C CZ  . ARG A 1 166 ? 3.67045   17.57968 16.28477 1.000 75.73339  ? 173 ARG A CZ  1 
ATOM   1221 N NH1 . ARG A 1 166 ? 3.33512   17.44876 15.01175 1.000 73.45166  ? 173 ARG A NH1 1 
ATOM   1222 N NH2 . ARG A 1 166 ? 2.72164   17.53424 17.21578 1.000 70.64972  ? 173 ARG A NH2 1 
ATOM   1223 N N   . THR A 1 167 ? 5.61878   21.00632 12.22309 1.000 60.93020  ? 174 THR A N   1 
ATOM   1224 C CA  . THR A 1 167 ? 4.30012   21.24713 11.65490 1.000 60.18119  ? 174 THR A CA  1 
ATOM   1225 C C   . THR A 1 167 ? 3.30070   20.26576 12.25283 1.000 62.06285  ? 174 THR A C   1 
ATOM   1226 O O   . THR A 1 167 ? 3.50676   19.04920 12.20336 1.000 73.36995  ? 174 THR A O   1 
ATOM   1227 C CB  . THR A 1 167 ? 4.33262   21.10938 10.13288 1.000 56.61956  ? 174 THR A CB  1 
ATOM   1228 O OG1 . THR A 1 167 ? 5.56791   21.63271 9.62964  1.000 63.02690  ? 174 THR A OG1 1 
ATOM   1229 C CG2 . THR A 1 167 ? 3.17429   21.87066 9.50551  1.000 63.62675  ? 174 THR A CG2 1 
ATOM   1230 N N   . ASP A 1 168 ? 2.22154   20.79506 12.82155 1.000 63.41545  ? 175 ASP A N   1 
ATOM   1231 C CA  . ASP A 1 168 ? 1.23060   19.95888 13.48228 1.000 69.24894  ? 175 ASP A CA  1 
ATOM   1232 C C   . ASP A 1 168 ? 0.38385   19.21329 12.45959 1.000 76.72135  ? 175 ASP A C   1 
ATOM   1233 O O   . ASP A 1 168 ? -0.04356  19.78063 11.45010 1.000 80.08414  ? 175 ASP A O   1 
ATOM   1234 C CB  . ASP A 1 168 ? 0.33321   20.80318 14.38664 1.000 64.32776  ? 175 ASP A CB  1 
ATOM   1235 C CG  . ASP A 1 168 ? -0.61648  19.95887 15.21414 1.000 74.50187  ? 175 ASP A CG  1 
ATOM   1236 O OD1 . ASP A 1 168 ? -0.15098  18.98903 15.84882 1.000 78.09646  ? 175 ASP A OD1 1 
ATOM   1237 O OD2 . ASP A 1 168 ? -1.82779  20.26318 15.22970 1.000 83.15206  ? 175 ASP A OD2 1 
ATOM   1238 N N   . THR A 1 169 ? 0.14333   17.93136 12.73108 1.000 85.70667  ? 176 THR A N   1 
ATOM   1239 C CA  . THR A 1 169 ? -0.67224  17.08403 11.87328 1.000 96.52780  ? 176 THR A CA  1 
ATOM   1240 C C   . THR A 1 169 ? -1.99269  16.68574 12.51711 1.000 99.68741  ? 176 THR A C   1 
ATOM   1241 O O   . THR A 1 169 ? -2.79944  16.00607 11.87336 1.000 96.35013  ? 176 THR A O   1 
ATOM   1242 C CB  . THR A 1 169 ? 0.10462   15.82063 11.48011 1.000 100.94815 ? 176 THR A CB  1 
ATOM   1243 O OG1 . THR A 1 169 ? 0.44344   15.07863 12.65879 1.000 93.97374  ? 176 THR A OG1 1 
ATOM   1244 C CG2 . THR A 1 169 ? 1.37914   16.18706 10.73455 1.000 97.85158  ? 176 THR A CG2 1 
ATOM   1245 N N   . GLY A 1 170 ? -2.23782  17.09065 13.76205 1.000 96.56352  ? 177 GLY A N   1 
ATOM   1246 C CA  . GLY A 1 170 ? -3.43939  16.70752 14.47926 1.000 96.48389  ? 177 GLY A CA  1 
ATOM   1247 C C   . GLY A 1 170 ? -4.67547  17.45314 14.02492 1.000 96.76988  ? 177 GLY A C   1 
ATOM   1248 O O   . GLY A 1 170 ? -4.78857  17.88069 12.87036 1.000 94.04226  ? 177 GLY A O   1 
ATOM   1249 N N   . GLU A 1 171 ? -5.61903  17.61013 14.94598 1.000 106.19220 ? 178 GLU A N   1 
ATOM   1250 C CA  . GLU A 1 171 ? -6.87457  18.27950 14.62471 1.000 99.14217  ? 178 GLU A CA  1 
ATOM   1251 C C   . GLU A 1 171 ? -6.62430  19.75975 14.35760 1.000 82.14784  ? 178 GLU A C   1 
ATOM   1252 O O   . GLU A 1 171 ? -5.99380  20.43439 15.18079 1.000 78.95494  ? 178 GLU A O   1 
ATOM   1253 C CB  . GLU A 1 171 ? -7.87597  18.11084 15.76587 1.000 106.97170 ? 178 GLU A CB  1 
ATOM   1254 C CG  . GLU A 1 171 ? -9.31537  18.41644 15.38444 1.000 110.57465 ? 178 GLU A CG  1 
ATOM   1255 C CD  . GLU A 1 171 ? -9.92106  17.34845 14.49550 1.000 121.55626 ? 178 GLU A CD  1 
ATOM   1256 O OE1 . GLU A 1 171 ? -9.71707  16.14969 14.78004 1.000 126.60444 ? 178 GLU A OE1 1 
ATOM   1257 O OE2 . GLU A 1 171 ? -10.60388 17.70693 13.51347 1.000 120.99199 ? 178 GLU A OE2 1 
ATOM   1258 N N   . PRO A 1 172 ? -7.08432  20.29614 13.22711 1.000 79.92533  ? 179 PRO A N   1 
ATOM   1259 C CA  . PRO A 1 172 ? -6.89875  21.72719 12.96389 1.000 73.89624  ? 179 PRO A CA  1 
ATOM   1260 C C   . PRO A 1 172 ? -7.61071  22.58082 14.00216 1.000 74.40433  ? 179 PRO A C   1 
ATOM   1261 O O   . PRO A 1 172 ? -8.64915  22.20185 14.54862 1.000 87.81730  ? 179 PRO A O   1 
ATOM   1262 C CB  . PRO A 1 172 ? -7.50963  21.91532 11.57026 1.000 65.50716  ? 179 PRO A CB  1 
ATOM   1263 C CG  . PRO A 1 172 ? -7.46486  20.55710 10.95083 1.000 64.05037  ? 179 PRO A CG  1 
ATOM   1264 C CD  . PRO A 1 172 ? -7.68558  19.59605 12.08002 1.000 81.59017  ? 179 PRO A CD  1 
ATOM   1265 N N   . MET A 1 173 ? -7.03223  23.74980 14.27077 1.000 64.93454  ? 180 MET A N   1 
ATOM   1266 C CA  . MET A 1 173 ? -7.55356  24.66448 15.27763 1.000 62.17295  ? 180 MET A CA  1 
ATOM   1267 C C   . MET A 1 173 ? -8.28300  25.85954 14.68501 1.000 59.46821  ? 180 MET A C   1 
ATOM   1268 O O   . MET A 1 173 ? -9.15324  26.43080 15.34998 1.000 61.55931  ? 180 MET A O   1 
ATOM   1269 C CB  . MET A 1 173 ? -6.41400  25.17148 16.16835 1.000 69.66699  ? 180 MET A CB  1 
ATOM   1270 C CG  . MET A 1 173 ? -6.86036  25.71939 17.51516 1.000 82.85162  ? 180 MET A CG  1 
ATOM   1271 S SD  . MET A 1 173 ? -5.53227  25.76438 18.73738 1.000 90.58398  ? 180 MET A SD  1 
ATOM   1272 C CE  . MET A 1 173 ? -4.21742  24.91585 17.86537 1.000 57.53993  ? 180 MET A CE  1 
ATOM   1273 N N   . GLY A 1 174 ? -7.95335  26.24991 13.45670 1.000 57.49441  ? 181 GLY A N   1 
ATOM   1274 C CA  . GLY A 1 174 ? -8.54293  27.43036 12.85783 1.000 59.01225  ? 181 GLY A CA  1 
ATOM   1275 C C   . GLY A 1 174 ? -7.75422  28.68332 13.17482 1.000 59.91336  ? 181 GLY A C   1 
ATOM   1276 O O   . GLY A 1 174 ? -7.20485  29.32467 12.27369 1.000 57.30498  ? 181 GLY A O   1 
ATOM   1277 N N   . ARG A 1 175 ? -7.68908  29.03500 14.45816 1.000 58.08724  ? 182 ARG A N   1 
ATOM   1278 C CA  . ARG A 1 175 ? -6.92972  30.18635 14.92608 1.000 52.38315  ? 182 ARG A CA  1 
ATOM   1279 C C   . ARG A 1 175 ? -6.87882  30.15009 16.44528 1.000 57.10005  ? 182 ARG A C   1 
ATOM   1280 O O   . ARG A 1 175 ? -7.87183  29.80780 17.09176 1.000 67.39079  ? 182 ARG A O   1 
ATOM   1281 C CB  . ARG A 1 175 ? -7.55614  31.50483 14.44970 1.000 55.16683  ? 182 ARG A CB  1 
ATOM   1282 C CG  . ARG A 1 175 ? -6.58756  32.67577 14.41274 1.000 52.68811  ? 182 ARG A CG  1 
ATOM   1283 C CD  . ARG A 1 175 ? -7.29876  34.01684 14.56505 1.000 55.33069  ? 182 ARG A CD  1 
ATOM   1284 N NE  . ARG A 1 175 ? -8.34883  33.99305 15.57736 1.000 54.50564  ? 182 ARG A NE  1 
ATOM   1285 C CZ  . ARG A 1 175 ? -9.64774  34.03439 15.31283 1.000 55.02715  ? 182 ARG A CZ  1 
ATOM   1286 N NH1 . ARG A 1 175 ? -10.09824 34.09843 14.07080 1.000 56.23836  ? 182 ARG A NH1 1 
ATOM   1287 N NH2 . ARG A 1 175 ? -10.51606 34.01189 16.31998 1.000 53.76771  ? 182 ARG A NH2 1 
ATOM   1288 N N   . GLY A 1 176 ? -5.72002  30.49960 17.00713 1.000 51.45197  ? 183 GLY A N   1 
ATOM   1289 C CA  . GLY A 1 176 ? -5.56278  30.59573 18.43969 1.000 52.88580  ? 183 GLY A CA  1 
ATOM   1290 C C   . GLY A 1 176 ? -4.31535  29.87794 18.90279 1.000 52.05687  ? 183 GLY A C   1 
ATOM   1291 O O   . GLY A 1 176 ? -3.37184  29.66549 18.13296 1.000 46.57408  ? 183 GLY A O   1 
ATOM   1292 N N   . THR A 1 177 ? -4.31660  29.50122 20.18001 1.000 54.77550  ? 184 THR A N   1 
ATOM   1293 C CA  . THR A 1 177 ? -3.17583  28.83944 20.79512 1.000 47.74030  ? 184 THR A CA  1 
ATOM   1294 C C   . THR A 1 177 ? -3.67329  27.84417 21.83349 1.000 50.51138  ? 184 THR A C   1 
ATOM   1295 O O   . THR A 1 177 ? -4.56577  28.15755 22.62611 1.000 42.77798  ? 184 THR A O   1 
ATOM   1296 C CB  . THR A 1 177 ? -2.22735  29.85650 21.44406 1.000 44.54327  ? 184 THR A CB  1 
ATOM   1297 O OG1 . THR A 1 177 ? -1.61148  30.65526 20.42543 1.000 52.42767  ? 184 THR A OG1 1 
ATOM   1298 C CG2 . THR A 1 177 ? -1.14796  29.15241 22.25492 1.000 43.14893  ? 184 THR A CG2 1 
ATOM   1299 N N   . LYS A 1 178 ? -3.09273  26.64578 21.81824 1.000 47.44488  ? 185 LYS A N   1 
ATOM   1300 C CA  . LYS A 1 178 ? -3.41102  25.59227 22.77380 1.000 43.81033  ? 185 LYS A CA  1 
ATOM   1301 C C   . LYS A 1 178 ? -2.15270  25.25034 23.55857 1.000 50.74449  ? 185 LYS A C   1 
ATOM   1302 O O   . LYS A 1 178 ? -1.17311  24.76364 22.98389 1.000 56.30537  ? 185 LYS A O   1 
ATOM   1303 C CB  . LYS A 1 178 ? -3.95654  24.35363 22.06123 1.000 48.92126  ? 185 LYS A CB  1 
ATOM   1304 C CG  . LYS A 1 178 ? -4.29102  23.20002 22.98845 1.000 52.24814  ? 185 LYS A CG  1 
ATOM   1305 C CD  . LYS A 1 178 ? -4.57898  21.93099 22.20392 1.000 54.38631  ? 185 LYS A CD  1 
ATOM   1306 C CE  . LYS A 1 178 ? -5.81156  22.08979 21.32787 1.000 63.23853  ? 185 LYS A CE  1 
ATOM   1307 N NZ  . LYS A 1 178 ? -6.80124  20.99494 21.53678 1.000 83.89579  ? 185 LYS A NZ  1 
ATOM   1308 N N   . VAL A 1 179 ? -2.18165  25.50124 24.86480 1.000 44.74853  ? 186 VAL A N   1 
ATOM   1309 C CA  . VAL A 1 179 ? -1.04791  25.25758 25.75138 1.000 51.57024  ? 186 VAL A CA  1 
ATOM   1310 C C   . VAL A 1 179 ? -1.36640  24.03767 26.60469 1.000 49.43410  ? 186 VAL A C   1 
ATOM   1311 O O   . VAL A 1 179 ? -2.28890  24.07077 27.42863 1.000 49.81285  ? 186 VAL A O   1 
ATOM   1312 C CB  . VAL A 1 179 ? -0.74338  26.47931 26.63136 1.000 41.71311  ? 186 VAL A CB  1 
ATOM   1313 C CG1 . VAL A 1 179 ? 0.40567   26.17695 27.58073 1.000 46.88936  ? 186 VAL A CG1 1 
ATOM   1314 C CG2 . VAL A 1 179 ? -0.42590  27.68844 25.76708 1.000 41.44237  ? 186 VAL A CG2 1 
ATOM   1315 N N   . ILE A 1 180 ? -0.60172  22.96609 26.41405 1.000 42.41218  ? 187 ILE A N   1 
ATOM   1316 C CA  . ILE A 1 180 ? -0.80471  21.70504 27.11977 1.000 49.90237  ? 187 ILE A CA  1 
ATOM   1317 C C   . ILE A 1 180 ? 0.29526   21.56090 28.16202 1.000 47.74879  ? 187 ILE A C   1 
ATOM   1318 O O   . ILE A 1 180 ? 1.48108   21.48025 27.81736 1.000 47.13330  ? 187 ILE A O   1 
ATOM   1319 C CB  . ILE A 1 180 ? -0.80847  20.51029 26.15455 1.000 47.38586  ? 187 ILE A CB  1 
ATOM   1320 C CG1 . ILE A 1 180 ? -1.93253  20.65949 25.12739 1.000 53.93252  ? 187 ILE A CG1 1 
ATOM   1321 C CG2 . ILE A 1 180 ? -0.95046  19.20563 26.92219 1.000 43.36565  ? 187 ILE A CG2 1 
ATOM   1322 C CD1 . ILE A 1 180 ? -1.46048  20.58287 23.69302 1.000 53.28582  ? 187 ILE A CD1 1 
ATOM   1323 N N   . LEU A 1 181 ? -0.09561  21.52252 29.43432 1.000 52.71631  ? 188 LEU A N   1 
ATOM   1324 C CA  . LEU A 1 181 ? 0.84376   21.41479 30.54529 1.000 46.31913  ? 188 LEU A CA  1 
ATOM   1325 C C   . LEU A 1 181 ? 0.86996   19.97143 31.02985 1.000 51.48606  ? 188 LEU A C   1 
ATOM   1326 O O   . LEU A 1 181 ? -0.09188  19.49955 31.64395 1.000 53.48459  ? 188 LEU A O   1 
ATOM   1327 C CB  . LEU A 1 181 ? 0.45501   22.35314 31.68453 1.000 45.06404  ? 188 LEU A CB  1 
ATOM   1328 C CG  . LEU A 1 181 ? 0.14602   23.80002 31.31150 1.000 56.66657  ? 188 LEU A CG  1 
ATOM   1329 C CD1 . LEU A 1 181 ? -0.90502  24.37592 32.24651 1.000 51.93133  ? 188 LEU A CD1 1 
ATOM   1330 C CD2 . LEU A 1 181 ? 1.41229   24.62521 31.34362 1.000 54.08929  ? 188 LEU A CD2 1 
ATOM   1331 N N   . HIS A 1 182 ? 1.96813   19.27355 30.75786 1.000 53.07009  ? 189 HIS A N   1 
ATOM   1332 C CA  . HIS A 1 182 ? 2.18518   17.94416 31.32111 1.000 49.90057  ? 189 HIS A CA  1 
ATOM   1333 C C   . HIS A 1 182 ? 2.66231   18.13528 32.75432 1.000 57.21299  ? 189 HIS A C   1 
ATOM   1334 O O   . HIS A 1 182 ? 3.85259   18.33539 33.00709 1.000 55.44602  ? 189 HIS A O   1 
ATOM   1335 C CB  . HIS A 1 182 ? 3.18482   17.15799 30.48221 1.000 54.03410  ? 189 HIS A CB  1 
ATOM   1336 C CG  . HIS A 1 182 ? 2.70315   16.86220 29.09569 1.000 54.78328  ? 189 HIS A CG  1 
ATOM   1337 N ND1 . HIS A 1 182 ? 1.87588   15.79851 28.80596 1.000 57.40401  ? 189 HIS A ND1 1 
ATOM   1338 C CD2 . HIS A 1 182 ? 2.92337   17.49808 27.92062 1.000 47.44040  ? 189 HIS A CD2 1 
ATOM   1339 C CE1 . HIS A 1 182 ? 1.61262   15.78797 27.51143 1.000 56.37519  ? 189 HIS A CE1 1 
ATOM   1340 N NE2 . HIS A 1 182 ? 2.23575   16.80904 26.95136 1.000 49.24543  ? 189 HIS A NE2 1 
ATOM   1341 N N   . LEU A 1 183 ? 1.72270   18.08508 33.69513 1.000 58.15916  ? 190 LEU A N   1 
ATOM   1342 C CA  . LEU A 1 183 ? 1.99531   18.45748 35.07373 1.000 52.51225  ? 190 LEU A CA  1 
ATOM   1343 C C   . LEU A 1 183 ? 2.96148   17.47820 35.73337 1.000 62.11385  ? 190 LEU A C   1 
ATOM   1344 O O   . LEU A 1 183 ? 3.09425   16.31843 35.33200 1.000 59.14962  ? 190 LEU A O   1 
ATOM   1345 C CB  . LEU A 1 183 ? 0.69668   18.51690 35.87825 1.000 51.06643  ? 190 LEU A CB  1 
ATOM   1346 C CG  . LEU A 1 183 ? -0.34857  19.53894 35.42958 1.000 50.55204  ? 190 LEU A CG  1 
ATOM   1347 C CD1 . LEU A 1 183 ? -1.49343  19.60512 36.42687 1.000 53.05568  ? 190 LEU A CD1 1 
ATOM   1348 C CD2 . LEU A 1 183 ? 0.28399   20.90720 35.24467 1.000 56.03850  ? 190 LEU A CD2 1 
ATOM   1349 N N   . LYS A 1 184 ? 3.64126   17.96858 36.76598 1.000 68.83326  ? 191 LYS A N   1 
ATOM   1350 C CA  . LYS A 1 184 ? 4.50041   17.11938 37.57158 1.000 60.55280  ? 191 LYS A CA  1 
ATOM   1351 C C   . LYS A 1 184 ? 3.65581   16.17958 38.42802 1.000 61.91142  ? 191 LYS A C   1 
ATOM   1352 O O   . LYS A 1 184 ? 2.44605   16.36133 38.59269 1.000 68.83946  ? 191 LYS A O   1 
ATOM   1353 C CB  . LYS A 1 184 ? 5.41579   17.96763 38.45502 1.000 61.11728  ? 191 LYS A CB  1 
ATOM   1354 C CG  . LYS A 1 184 ? 6.43477   18.78907 37.67980 1.000 60.07265  ? 191 LYS A CG  1 
ATOM   1355 C CD  . LYS A 1 184 ? 7.10562   19.82614 38.56672 1.000 62.10840  ? 191 LYS A CD  1 
ATOM   1356 C CE  . LYS A 1 184 ? 7.80563   20.89428 37.73975 1.000 64.81520  ? 191 LYS A CE  1 
ATOM   1357 N NZ  . LYS A 1 184 ? 8.42392   21.94674 38.59420 1.000 64.33598  ? 191 LYS A NZ  1 
ATOM   1358 N N   . GLU A 1 185 ? 4.31480   15.15772 38.97808 1.000 64.85997  ? 192 GLU A N   1 
ATOM   1359 C CA  . GLU A 1 185 ? 3.59862   14.15657 39.76151 1.000 71.59020  ? 192 GLU A CA  1 
ATOM   1360 C C   . GLU A 1 185 ? 2.99213   14.75563 41.02488 1.000 76.65523  ? 192 GLU A C   1 
ATOM   1361 O O   . GLU A 1 185 ? 1.91113   14.33521 41.45379 1.000 80.09226  ? 192 GLU A O   1 
ATOM   1362 C CB  . GLU A 1 185 ? 4.53766   13.00039 40.11168 1.000 74.57720  ? 192 GLU A CB  1 
ATOM   1363 C CG  . GLU A 1 185 ? 3.94074   11.96444 41.05117 1.000 83.48155  ? 192 GLU A CG  1 
ATOM   1364 C CD  . GLU A 1 185 ? 4.71017   11.84386 42.35264 1.000 100.22000 ? 192 GLU A CD  1 
ATOM   1365 O OE1 . GLU A 1 185 ? 5.95592   11.76044 42.30540 1.000 100.31458 ? 192 GLU A OE1 1 
ATOM   1366 O OE2 . GLU A 1 185 ? 4.06881   11.83357 43.42421 1.000 105.23429 ? 192 GLU A OE2 1 
ATOM   1367 N N   . ASP A 1 186 ? 3.65639   15.74303 41.62272 1.000 74.20800  ? 193 ASP A N   1 
ATOM   1368 C CA  . ASP A 1 186 ? 3.21063   16.34479 42.87160 1.000 70.49653  ? 193 ASP A CA  1 
ATOM   1369 C C   . ASP A 1 186 ? 2.39890   17.61789 42.66309 1.000 68.62066  ? 193 ASP A C   1 
ATOM   1370 O O   . ASP A 1 186 ? 2.12242   18.32861 43.63469 1.000 72.49195  ? 193 ASP A O   1 
ATOM   1371 C CB  . ASP A 1 186 ? 4.41344   16.63717 43.77065 1.000 85.84279  ? 193 ASP A CB  1 
ATOM   1372 C CG  . ASP A 1 186 ? 5.49386   17.42720 43.05848 1.000 92.03256  ? 193 ASP A CG  1 
ATOM   1373 O OD1 . ASP A 1 186 ? 6.28030   16.81651 42.30391 1.000 91.90870  ? 193 ASP A OD1 1 
ATOM   1374 O OD2 . ASP A 1 186 ? 5.55485   18.65979 43.25036 1.000 87.18835  ? 193 ASP A OD2 1 
ATOM   1375 N N   . GLN A 1 187 ? 2.00975   17.92274 41.42547 1.000 68.59851  ? 194 GLN A N   1 
ATOM   1376 C CA  . GLN A 1 187 ? 1.23647   19.12078 41.12038 1.000 63.97633  ? 194 GLN A CA  1 
ATOM   1377 C C   . GLN A 1 187 ? -0.12097  18.77217 40.51759 1.000 64.22604  ? 194 GLN A C   1 
ATOM   1378 O O   . GLN A 1 187 ? -0.67631  19.54262 39.73187 1.000 62.26241  ? 194 GLN A O   1 
ATOM   1379 C CB  . GLN A 1 187 ? 2.01610   20.04436 40.18497 1.000 58.56341  ? 194 GLN A CB  1 
ATOM   1380 C CG  . GLN A 1 187 ? 3.39361   20.43428 40.69827 1.000 65.13643  ? 194 GLN A CG  1 
ATOM   1381 C CD  . GLN A 1 187 ? 3.33549   21.21384 41.99816 1.000 59.10584  ? 194 GLN A CD  1 
ATOM   1382 O OE1 . GLN A 1 187 ? 2.44202   22.03522 42.20451 1.000 62.68513  ? 194 GLN A OE1 1 
ATOM   1383 N NE2 . GLN A 1 187 ? 4.29339   20.96129 42.88212 1.000 63.07843  ? 194 GLN A NE2 1 
ATOM   1384 N N   . THR A 1 188 ? -0.66875  17.61424 40.88272 1.000 63.33587  ? 195 THR A N   1 
ATOM   1385 C CA  . THR A 1 188 ? -1.94547  17.16169 40.34481 1.000 55.49888  ? 195 THR A CA  1 
ATOM   1386 C C   . THR A 1 188 ? -3.14080  17.88566 40.95027 1.000 57.65954  ? 195 THR A C   1 
ATOM   1387 O O   . THR A 1 188 ? -4.27230  17.64441 40.51528 1.000 59.79909  ? 195 THR A O   1 
ATOM   1388 C CB  . THR A 1 188 ? -2.10412  15.65338 40.55750 1.000 61.67599  ? 195 THR A CB  1 
ATOM   1389 O OG1 . THR A 1 188 ? -2.02346  15.35375 41.95664 1.000 69.33509  ? 195 THR A OG1 1 
ATOM   1390 C CG2 . THR A 1 188 ? -1.01396  14.89336 39.81725 1.000 61.21011  ? 195 THR A CG2 1 
ATOM   1391 N N   . GLU A 1 189 ? -2.92480  18.75948 41.93656 1.000 58.44036  ? 196 GLU A N   1 
ATOM   1392 C CA  . GLU A 1 189 ? -4.03284  19.49603 42.53236 1.000 59.68182  ? 196 GLU A CA  1 
ATOM   1393 C C   . GLU A 1 189 ? -4.65964  20.48381 41.55815 1.000 56.58352  ? 196 GLU A C   1 
ATOM   1394 O O   . GLU A 1 189 ? -5.82407  20.85570 41.73633 1.000 65.58043  ? 196 GLU A O   1 
ATOM   1395 C CB  . GLU A 1 189 ? -3.56367  20.23087 43.79025 1.000 67.31554  ? 196 GLU A CB  1 
ATOM   1396 C CG  . GLU A 1 189 ? -2.81017  21.52489 43.51574 1.000 57.68542  ? 196 GLU A CG  1 
ATOM   1397 C CD  . GLU A 1 189 ? -2.03093  22.01822 44.72022 1.000 75.18487  ? 196 GLU A CD  1 
ATOM   1398 O OE1 . GLU A 1 189 ? -1.17095  21.26571 45.22447 1.000 85.34755  ? 196 GLU A OE1 1 
ATOM   1399 O OE2 . GLU A 1 189 ? -2.27684  23.16071 45.16162 1.000 80.43836  ? 196 GLU A OE2 1 
ATOM   1400 N N   . TYR A 1 190 ? -3.92309  20.90740 40.53287 1.000 57.98055  ? 197 TYR A N   1 
ATOM   1401 C CA  . TYR A 1 190 ? -4.42865  21.85127 39.54552 1.000 52.21102  ? 197 TYR A CA  1 
ATOM   1402 C C   . TYR A 1 190 ? -5.29499  21.18672 38.48364 1.000 52.74031  ? 197 TYR A C   1 
ATOM   1403 O O   . TYR A 1 190 ? -5.63410  21.83106 37.48525 1.000 52.09763  ? 197 TYR A O   1 
ATOM   1404 C CB  . TYR A 1 190 ? -3.25970  22.59612 38.89694 1.000 54.22545  ? 197 TYR A CB  1 
ATOM   1405 C CG  . TYR A 1 190 ? -2.39480  23.31399 39.90755 1.000 62.15485  ? 197 TYR A CG  1 
ATOM   1406 C CD1 . TYR A 1 190 ? -2.87168  24.42502 40.59058 1.000 59.82657  ? 197 TYR A CD1 1 
ATOM   1407 C CD2 . TYR A 1 190 ? -1.11261  22.86757 40.19776 1.000 65.51354  ? 197 TYR A CD2 1 
ATOM   1408 C CE1 . TYR A 1 190 ? -2.09111  25.08132 41.52335 1.000 64.49341  ? 197 TYR A CE1 1 
ATOM   1409 C CE2 . TYR A 1 190 ? -0.32457  23.51671 41.13077 1.000 72.72725  ? 197 TYR A CE2 1 
ATOM   1410 C CZ  . TYR A 1 190 ? -0.81883  24.62345 41.78983 1.000 70.24461  ? 197 TYR A CZ  1 
ATOM   1411 O OH  . TYR A 1 190 ? -0.03962  25.27416 42.71898 1.000 67.87976  ? 197 TYR A OH  1 
ATOM   1412 N N   . LEU A 1 191 ? -5.65227  19.91895 38.67684 1.000 56.51995  ? 198 LEU A N   1 
ATOM   1413 C CA  . LEU A 1 191 ? -6.62681  19.23325 37.84194 1.000 53.98774  ? 198 LEU A CA  1 
ATOM   1414 C C   . LEU A 1 191 ? -7.97631  19.08560 38.53050 1.000 56.45610  ? 198 LEU A C   1 
ATOM   1415 O O   . LEU A 1 191 ? -8.91952  18.57811 37.91642 1.000 62.59987  ? 198 LEU A O   1 
ATOM   1416 C CB  . LEU A 1 191 ? -6.09921  17.85302 37.43533 1.000 55.44600  ? 198 LEU A CB  1 
ATOM   1417 C CG  . LEU A 1 191 ? -4.76843  17.82659 36.68117 1.000 54.85306  ? 198 LEU A CG  1 
ATOM   1418 C CD1 . LEU A 1 191 ? -4.28780  16.39724 36.48163 1.000 53.92487  ? 198 LEU A CD1 1 
ATOM   1419 C CD2 . LEU A 1 191 ? -4.89491  18.54352 35.34654 1.000 56.00531  ? 198 LEU A CD2 1 
ATOM   1420 N N   . GLU A 1 192 ? -8.08711  19.51595 39.78552 1.000 56.56402  ? 199 GLU A N   1 
ATOM   1421 C CA  . GLU A 1 192 ? -9.33605  19.41997 40.52670 1.000 65.16130  ? 199 GLU A CA  1 
ATOM   1422 C C   . GLU A 1 192 ? -10.23969 20.60092 40.19863 1.000 63.89342  ? 199 GLU A C   1 
ATOM   1423 O O   . GLU A 1 192 ? -9.77711  21.73736 40.07226 1.000 59.56435  ? 199 GLU A O   1 
ATOM   1424 C CB  . GLU A 1 192 ? -9.05922  19.37349 42.02908 1.000 71.63062  ? 199 GLU A CB  1 
ATOM   1425 C CG  . GLU A 1 192 ? -8.59238  18.01857 42.52921 1.000 72.38002  ? 199 GLU A CG  1 
ATOM   1426 C CD  . GLU A 1 192 ? -9.70466  17.23147 43.19062 1.000 87.95843  ? 199 GLU A CD  1 
ATOM   1427 O OE1 . GLU A 1 192 ? -10.08655 17.58002 44.32762 1.000 98.64666  ? 199 GLU A OE1 1 
ATOM   1428 O OE2 . GLU A 1 192 ? -10.19947 16.26604 42.57168 1.000 87.32771  ? 199 GLU A OE2 1 
ATOM   1429 N N   . GLU A 1 193 ? -11.54209 20.32670 40.08084 1.000 66.83998  ? 200 GLU A N   1 
ATOM   1430 C CA  . GLU A 1 193 ? -12.47343 21.34675 39.60741 1.000 63.26249  ? 200 GLU A CA  1 
ATOM   1431 C C   . GLU A 1 193 ? -12.58339 22.52076 40.57484 1.000 64.99509  ? 200 GLU A C   1 
ATOM   1432 O O   . GLU A 1 193 ? -12.76945 23.66231 40.13874 1.000 66.12221  ? 200 GLU A O   1 
ATOM   1433 C CB  . GLU A 1 193 ? -13.84905 20.72312 39.35074 1.000 63.74493  ? 200 GLU A CB  1 
ATOM   1434 C CG  . GLU A 1 193 ? -14.75839 20.63704 40.56824 1.000 69.90063  ? 200 GLU A CG  1 
ATOM   1435 C CD  . GLU A 1 193 ? -15.98185 19.77800 40.32345 1.000 76.78827  ? 200 GLU A CD  1 
ATOM   1436 O OE1 . GLU A 1 193 ? -16.14575 19.28726 39.18708 1.000 66.73709  ? 200 GLU A OE1 1 
ATOM   1437 O OE2 . GLU A 1 193 ? -16.77863 19.59186 41.26765 1.000 87.05774  ? 200 GLU A OE2 1 
ATOM   1438 N N   . ARG A 1 194 ? -12.45930 22.27464 41.88123 1.000 67.11877  ? 201 ARG A N   1 
ATOM   1439 C CA  . ARG A 1 194 ? -12.58248 23.35931 42.84670 1.000 66.74434  ? 201 ARG A CA  1 
ATOM   1440 C C   . ARG A 1 194 ? -11.28592 24.13714 43.01977 1.000 64.67854  ? 201 ARG A C   1 
ATOM   1441 O O   . ARG A 1 194 ? -11.32699 25.29307 43.45472 1.000 70.81303  ? 201 ARG A O   1 
ATOM   1442 C CB  . ARG A 1 194 ? -13.05213 22.81887 44.20068 1.000 67.17591  ? 201 ARG A CB  1 
ATOM   1443 C CG  . ARG A 1 194 ? -12.01592 22.00507 44.95544 1.000 83.30080  ? 201 ARG A CG  1 
ATOM   1444 C CD  . ARG A 1 194 ? -12.67197 21.15720 46.03345 1.000 91.06906  ? 201 ARG A CD  1 
ATOM   1445 N NE  . ARG A 1 194 ? -11.70321 20.35070 46.76601 1.000 107.01853 ? 201 ARG A NE  1 
ATOM   1446 C CZ  . ARG A 1 194 ? -12.02224 19.45202 47.68739 1.000 110.90633 ? 201 ARG A CZ  1 
ATOM   1447 N NH1 . ARG A 1 194 ? -13.28188 19.21690 48.01662 1.000 110.63273 ? 201 ARG A NH1 1 
ATOM   1448 N NH2 . ARG A 1 194 ? -11.05320 18.77290 48.29456 1.000 118.22667 ? 201 ARG A NH2 1 
ATOM   1449 N N   . ARG A 1 195 ? -10.14240 23.53619 42.68546 1.000 66.90357  ? 202 ARG A N   1 
ATOM   1450 C CA  . ARG A 1 195 ? -8.87677  24.25665 42.76990 1.000 66.48384  ? 202 ARG A CA  1 
ATOM   1451 C C   . ARG A 1 195 ? -8.74102  25.25412 41.62717 1.000 65.64323  ? 202 ARG A C   1 
ATOM   1452 O O   . ARG A 1 195 ? -8.34546  26.40618 41.83939 1.000 65.77699  ? 202 ARG A O   1 
ATOM   1453 C CB  . ARG A 1 195 ? -7.70867  23.27122 42.76822 1.000 61.63294  ? 202 ARG A CB  1 
ATOM   1454 C CG  . ARG A 1 195 ? -6.34695  23.92603 42.93718 1.000 60.15927  ? 202 ARG A CG  1 
ATOM   1455 C CD  . ARG A 1 195 ? -6.21663  24.59510 44.29640 1.000 69.90756  ? 202 ARG A CD  1 
ATOM   1456 N NE  . ARG A 1 195 ? -4.82942  24.90750 44.61952 1.000 73.67041  ? 202 ARG A NE  1 
ATOM   1457 C CZ  . ARG A 1 195 ? -4.34296  26.13686 44.72281 1.000 71.95572  ? 202 ARG A CZ  1 
ATOM   1458 N NH1 . ARG A 1 195 ? -5.10844  27.20058 44.54183 1.000 75.44130  ? 202 ARG A NH1 1 
ATOM   1459 N NH2 . ARG A 1 195 ? -3.05661  26.30330 45.01685 1.000 65.90800  ? 202 ARG A NH2 1 
ATOM   1460 N N   . ILE A 1 196 ? -9.06420  24.82741 40.40312 1.000 66.37687  ? 203 ILE A N   1 
ATOM   1461 C CA  . ILE A 1 196 ? -9.02882  25.74531 39.26846 1.000 58.34253  ? 203 ILE A CA  1 
ATOM   1462 C C   . ILE A 1 196 ? -10.03173 26.87401 39.45470 1.000 61.78454  ? 203 ILE A C   1 
ATOM   1463 O O   . ILE A 1 196 ? -9.78292  28.00958 39.03223 1.000 60.03526  ? 203 ILE A O   1 
ATOM   1464 C CB  . ILE A 1 196 ? -9.27447  24.98770 37.94827 1.000 56.16914  ? 203 ILE A CB  1 
ATOM   1465 C CG1 . ILE A 1 196 ? -8.57978  23.62501 37.96752 1.000 56.22237  ? 203 ILE A CG1 1 
ATOM   1466 C CG2 . ILE A 1 196 ? -8.81190  25.81833 36.76047 1.000 59.33816  ? 203 ILE A CG2 1 
ATOM   1467 C CD1 . ILE A 1 196 ? -8.73276  22.84498 36.67934 1.000 53.79310  ? 203 ILE A CD1 1 
ATOM   1468 N N   . LYS A 1 197 ? -11.17356 26.59075 40.08700 1.000 64.82870  ? 204 LYS A N   1 
ATOM   1469 C CA  . LYS A 1 197 ? -12.14954 27.64301 40.35354 1.000 57.56290  ? 204 LYS A CA  1 
ATOM   1470 C C   . LYS A 1 197 ? -11.56064 28.71562 41.26149 1.000 63.39034  ? 204 LYS A C   1 
ATOM   1471 O O   . LYS A 1 197 ? -11.60823 29.90788 40.94168 1.000 69.38012  ? 204 LYS A O   1 
ATOM   1472 C CB  . LYS A 1 197 ? -13.41481 27.04645 40.97142 1.000 58.24191  ? 204 LYS A CB  1 
ATOM   1473 C CG  . LYS A 1 197 ? -14.37553 26.44097 39.95967 1.000 59.26127  ? 204 LYS A CG  1 
ATOM   1474 C CD  . LYS A 1 197 ? -15.81390 26.52355 40.44316 1.000 64.07037  ? 204 LYS A CD  1 
ATOM   1475 C CE  . LYS A 1 197 ? -16.55157 25.21932 40.19421 1.000 61.29077  ? 204 LYS A CE  1 
ATOM   1476 N NZ  . LYS A 1 197 ? -16.16900 24.17588 41.18467 1.000 68.79837  ? 204 LYS A NZ  1 
ATOM   1477 N N   . GLU A 1 198 ? -10.98262 28.30489 42.39428 1.000 58.18821  ? 205 GLU A N   1 
ATOM   1478 C CA  . GLU A 1 198 ? -10.40837 29.26761 43.33103 1.000 66.55562  ? 205 GLU A CA  1 
ATOM   1479 C C   . GLU A 1 198 ? -9.35693  30.14339 42.65887 1.000 70.66072  ? 205 GLU A C   1 
ATOM   1480 O O   . GLU A 1 198 ? -9.29906  31.35409 42.90351 1.000 79.90023  ? 205 GLU A O   1 
ATOM   1481 C CB  . GLU A 1 198 ? -9.80783  28.53558 44.53332 1.000 73.88509  ? 205 GLU A CB  1 
ATOM   1482 C CG  . GLU A 1 198 ? -8.50781  29.14195 45.04792 1.000 85.82770  ? 205 GLU A CG  1 
ATOM   1483 C CD  . GLU A 1 198 ? -8.19771  28.74360 46.47633 1.000 98.60625  ? 205 GLU A CD  1 
ATOM   1484 O OE1 . GLU A 1 198 ? -8.80087  27.76721 46.96684 1.000 99.09986  ? 205 GLU A OE1 1 
ATOM   1485 O OE2 . GLU A 1 198 ? -7.35096  29.40824 47.11001 1.000 99.53684  ? 205 GLU A OE2 1 
ATOM   1486 N N   . ILE A 1 199 ? -8.52739  29.55285 41.79647 1.000 67.55248  ? 206 ILE A N   1 
ATOM   1487 C CA  . ILE A 1 199 ? -7.45849  30.31229 41.15572 1.000 67.07019  ? 206 ILE A CA  1 
ATOM   1488 C C   . ILE A 1 199 ? -8.03071  31.32060 40.16628 1.000 75.09975  ? 206 ILE A C   1 
ATOM   1489 O O   . ILE A 1 199 ? -7.53912  32.45064 40.05839 1.000 85.52343  ? 206 ILE A O   1 
ATOM   1490 C CB  . ILE A 1 199 ? -6.45916  29.35563 40.47966 1.000 66.78739  ? 206 ILE A CB  1 
ATOM   1491 C CG1 . ILE A 1 199 ? -5.85344  28.40134 41.51011 1.000 68.03028  ? 206 ILE A CG1 1 
ATOM   1492 C CG2 . ILE A 1 199 ? -5.36249  30.13522 39.77061 1.000 70.58302  ? 206 ILE A CG2 1 
ATOM   1493 C CD1 . ILE A 1 199 ? -5.12385  27.22849 40.89694 1.000 62.95620  ? 206 ILE A CD1 1 
ATOM   1494 N N   . VAL A 1 200 ? -9.08103  30.93844 39.43721 1.000 74.66052  ? 207 VAL A N   1 
ATOM   1495 C CA  . VAL A 1 200 ? -9.63569  31.82373 38.41634 1.000 75.33859  ? 207 VAL A CA  1 
ATOM   1496 C C   . VAL A 1 200 ? -10.34891 33.00994 39.05778 1.000 85.54363  ? 207 VAL A C   1 
ATOM   1497 O O   . VAL A 1 200 ? -10.15630 34.16087 38.64955 1.000 89.43597  ? 207 VAL A O   1 
ATOM   1498 C CB  . VAL A 1 200 ? -10.56790 31.04315 37.47315 1.000 63.16541  ? 207 VAL A CB  1 
ATOM   1499 C CG1 . VAL A 1 200 ? -11.33156 32.00092 36.57673 1.000 73.82025  ? 207 VAL A CG1 1 
ATOM   1500 C CG2 . VAL A 1 200 ? -9.76356  30.07328 36.62790 1.000 57.05598  ? 207 VAL A CG2 1 
ATOM   1501 N N   . LYS A 1 201 ? -11.18067 32.75420 40.07213 1.000 84.24530  ? 208 LYS A N   1 
ATOM   1502 C CA  . LYS A 1 201 ? -11.92608 33.84506 40.69555 1.000 83.32250  ? 208 LYS A CA  1 
ATOM   1503 C C   . LYS A 1 201 ? -11.03208 34.75016 41.53516 1.000 86.99042  ? 208 LYS A C   1 
ATOM   1504 O O   . LYS A 1 201 ? -11.42894 35.87914 41.84328 1.000 95.80951  ? 208 LYS A O   1 
ATOM   1505 C CB  . LYS A 1 201 ? -13.06704 33.30921 41.57112 1.000 77.56709  ? 208 LYS A CB  1 
ATOM   1506 C CG  . LYS A 1 201 ? -13.75267 32.02908 41.09135 1.000 89.37665  ? 208 LYS A CG  1 
ATOM   1507 C CD  . LYS A 1 201 ? -14.13872 32.04962 39.61680 1.000 87.36466  ? 208 LYS A CD  1 
ATOM   1508 C CE  . LYS A 1 201 ? -15.10763 30.92343 39.29682 1.000 82.22481  ? 208 LYS A CE  1 
ATOM   1509 N NZ  . LYS A 1 201 ? -14.99297 30.48829 37.87886 1.000 79.47123  ? 208 LYS A NZ  1 
ATOM   1510 N N   . LYS A 1 202 ? -9.84123  34.28427 41.91152 1.000 90.55289  ? 209 LYS A N   1 
ATOM   1511 C CA  . LYS A 1 202 ? -8.92204  35.08144 42.71475 1.000 91.58737  ? 209 LYS A CA  1 
ATOM   1512 C C   . LYS A 1 202 ? -7.90513  35.83734 41.87037 1.000 93.93973  ? 209 LYS A C   1 
ATOM   1513 O O   . LYS A 1 202 ? -7.53318  36.96339 42.22271 1.000 99.04730  ? 209 LYS A O   1 
ATOM   1514 C CB  . LYS A 1 202 ? -8.19520  34.18160 43.72241 1.000 88.72780  ? 209 LYS A CB  1 
ATOM   1515 C CG  . LYS A 1 202 ? -6.76373  34.59124 44.04702 1.000 97.93279  ? 209 LYS A CG  1 
ATOM   1516 C CD  . LYS A 1 202 ? -6.22950  33.82519 45.24791 1.000 95.51049  ? 209 LYS A CD  1 
ATOM   1517 C CE  . LYS A 1 202 ? -4.98593  34.48315 45.82425 1.000 94.34073  ? 209 LYS A CE  1 
ATOM   1518 N NZ  . LYS A 1 202 ? -4.53072  33.79849 47.06615 1.000 98.27721  ? 209 LYS A NZ  1 
ATOM   1519 N N   . HIS A 1 203 ? -7.46314  35.25741 40.75473 1.000 98.81580  ? 210 HIS A N   1 
ATOM   1520 C CA  . HIS A 1 203 ? -6.39815  35.83695 39.94687 1.000 102.71498 ? 210 HIS A CA  1 
ATOM   1521 C C   . HIS A 1 203 ? -6.85912  36.39236 38.60802 1.000 100.48967 ? 210 HIS A C   1 
ATOM   1522 O O   . HIS A 1 203 ? -6.28907  37.37967 38.13987 1.000 99.80578  ? 210 HIS A O   1 
ATOM   1523 C CB  . HIS A 1 203 ? -5.30166  34.79512 39.69213 1.000 95.60545  ? 210 HIS A CB  1 
ATOM   1524 C CG  . HIS A 1 203 ? -4.38740  34.58020 40.85797 1.000 94.62722  ? 210 HIS A CG  1 
ATOM   1525 N ND1 . HIS A 1 203 ? -3.64079  35.59586 41.41527 1.000 95.01487  ? 210 HIS A ND1 1 
ATOM   1526 C CD2 . HIS A 1 203 ? -4.09360  33.46474 41.56738 1.000 85.19930  ? 210 HIS A CD2 1 
ATOM   1527 C CE1 . HIS A 1 203 ? -2.92988  35.11657 42.42033 1.000 92.40819  ? 210 HIS A CE1 1 
ATOM   1528 N NE2 . HIS A 1 203 ? -3.18610  33.82574 42.53348 1.000 89.91846  ? 210 HIS A NE2 1 
ATOM   1529 N N   . SER A 1 204 ? -7.86597  35.79181 37.97881 1.000 113.06390 ? 211 SER A N   1 
ATOM   1530 C CA  . SER A 1 204 ? -8.31185  36.18614 36.64425 1.000 110.37061 ? 211 SER A CA  1 
ATOM   1531 C C   . SER A 1 204 ? -9.81307  36.44014 36.63376 1.000 111.09256 ? 211 SER A C   1 
ATOM   1532 O O   . SER A 1 204 ? -10.54674 35.97698 35.75755 1.000 111.06324 ? 211 SER A O   1 
ATOM   1533 C CB  . SER A 1 204 ? -7.93137  35.12608 35.61484 1.000 114.04458 ? 211 SER A CB  1 
ATOM   1534 O OG  . SER A 1 204 ? -6.52667  35.06647 35.44381 1.000 106.37262 ? 211 SER A OG  1 
ATOM   1535 N N   . GLN A 1 205 ? -10.28616 37.19820 37.62206 1.000 101.90748 ? 212 GLN A N   1 
ATOM   1536 C CA  . GLN A 1 205 ? -11.70092 37.52448 37.73544 1.000 104.35487 ? 212 GLN A CA  1 
ATOM   1537 C C   . GLN A 1 205 ? -12.09602 38.74095 36.90891 1.000 102.97208 ? 212 GLN A C   1 
ATOM   1538 O O   . GLN A 1 205 ? -13.29341 39.01654 36.77344 1.000 105.15316 ? 212 GLN A O   1 
ATOM   1539 C CB  . GLN A 1 205 ? -12.07735 37.77432 39.20210 1.000 98.89336  ? 212 GLN A CB  1 
ATOM   1540 C CG  . GLN A 1 205 ? -11.41607 38.99613 39.88384 1.000 109.39178 ? 212 GLN A CG  1 
ATOM   1541 C CD  . GLN A 1 205 ? -9.89504  38.92495 40.02874 1.000 108.03868 ? 212 GLN A CD  1 
ATOM   1542 O OE1 . GLN A 1 205 ? -9.22078  38.13231 39.37307 1.000 105.66645 ? 212 GLN A OE1 1 
ATOM   1543 N NE2 . GLN A 1 205 ? -9.35318  39.76869 40.90207 1.000 101.35127 ? 212 GLN A NE2 1 
ATOM   1544 N N   . PHE A 1 206 ? -11.13000 39.47402 36.36316 1.000 100.07099 ? 213 PHE A N   1 
ATOM   1545 C CA  . PHE A 1 206 ? -11.38275 40.69263 35.60613 1.000 93.73798  ? 213 PHE A CA  1 
ATOM   1546 C C   . PHE A 1 206 ? -10.83143 40.58067 34.19025 1.000 89.06994  ? 213 PHE A C   1 
ATOM   1547 O O   . PHE A 1 206 ? -10.25395 41.52656 33.65112 1.000 75.35269  ? 213 PHE A O   1 
ATOM   1548 C CB  . PHE A 1 206 ? -10.79296 41.90546 36.32197 1.000 94.43713  ? 213 PHE A CB  1 
ATOM   1549 C CG  . PHE A 1 206 ? -11.32128 42.10289 37.71437 1.000 107.56114 ? 213 PHE A CG  1 
ATOM   1550 C CD1 . PHE A 1 206 ? -12.66841 41.93583 37.98614 1.000 110.61257 ? 213 PHE A CD1 1 
ATOM   1551 C CD2 . PHE A 1 206 ? -10.47136 42.45366 38.75146 1.000 111.13383 ? 213 PHE A CD2 1 
ATOM   1552 C CE1 . PHE A 1 206 ? -13.16057 42.11469 39.26482 1.000 119.64864 ? 213 PHE A CE1 1 
ATOM   1553 C CE2 . PHE A 1 206 ? -10.95788 42.63420 40.03353 1.000 110.31404 ? 213 PHE A CE2 1 
ATOM   1554 C CZ  . PHE A 1 206 ? -12.30422 42.46433 40.28981 1.000 121.47717 ? 213 PHE A CZ  1 
ATOM   1555 N N   . ILE A 1 207 ? -10.99968 39.41623 33.57323 1.000 84.20159  ? 214 ILE A N   1 
ATOM   1556 C CA  . ILE A 1 207 ? -10.59265 39.20467 32.18978 1.000 69.57642  ? 214 ILE A CA  1 
ATOM   1557 C C   . ILE A 1 207 ? -11.78292 39.49341 31.28682 1.000 62.48309  ? 214 ILE A C   1 
ATOM   1558 O O   . ILE A 1 207 ? -12.90031 39.03179 31.54809 1.000 68.45247  ? 214 ILE A O   1 
ATOM   1559 C CB  . ILE A 1 207 ? -10.06703 37.77493 31.98089 1.000 73.76853  ? 214 ILE A CB  1 
ATOM   1560 C CG1 . ILE A 1 207 ? -8.90211  37.50050 32.93657 1.000 75.25935  ? 214 ILE A CG1 1 
ATOM   1561 C CG2 . ILE A 1 207 ? -9.66375  37.55378 30.52414 1.000 63.29752  ? 214 ILE A CG2 1 
ATOM   1562 C CD1 . ILE A 1 207 ? -7.53439  37.72265 32.32663 1.000 68.17047  ? 214 ILE A CD1 1 
ATOM   1563 N N   . GLY A 1 208 ? -11.54626 40.25887 30.22431 1.000 59.47702  ? 215 GLY A N   1 
ATOM   1564 C CA  . GLY A 1 208 ? -12.61569 40.68533 29.34317 1.000 57.80694  ? 215 GLY A CA  1 
ATOM   1565 C C   . GLY A 1 208 ? -13.03637 39.65368 28.31703 1.000 54.06086  ? 215 GLY A C   1 
ATOM   1566 O O   . GLY A 1 208 ? -13.49394 40.00844 27.22643 1.000 60.62116  ? 215 GLY A O   1 
ATOM   1567 N N   . TYR A 1 209 ? -12.88971 38.37424 28.65152 1.000 53.82170  ? 216 TYR A N   1 
ATOM   1568 C CA  . TYR A 1 209 ? -13.27118 37.28427 27.76609 1.000 49.08610  ? 216 TYR A CA  1 
ATOM   1569 C C   . TYR A 1 209 ? -13.76637 36.12652 28.61603 1.000 50.26832  ? 216 TYR A C   1 
ATOM   1570 O O   . TYR A 1 209 ? -13.29383 35.94454 29.74471 1.000 48.62646  ? 216 TYR A O   1 
ATOM   1571 C CB  . TYR A 1 209 ? -12.09783 36.83817 26.88020 1.000 51.27379  ? 216 TYR A CB  1 
ATOM   1572 C CG  . TYR A 1 209 ? -11.58080 37.93161 25.97257 1.000 49.46817  ? 216 TYR A CG  1 
ATOM   1573 C CD1 . TYR A 1 209 ? -12.22721 38.23556 24.78164 1.000 46.11472  ? 216 TYR A CD1 1 
ATOM   1574 C CD2 . TYR A 1 209 ? -10.45156 38.66568 26.31108 1.000 54.09150  ? 216 TYR A CD2 1 
ATOM   1575 C CE1 . TYR A 1 209 ? -11.76167 39.23712 23.95131 1.000 48.85628  ? 216 TYR A CE1 1 
ATOM   1576 C CE2 . TYR A 1 209 ? -9.97838  39.66950 25.48735 1.000 53.77299  ? 216 TYR A CE2 1 
ATOM   1577 C CZ  . TYR A 1 209 ? -10.63712 39.95081 24.30886 1.000 52.61602  ? 216 TYR A CZ  1 
ATOM   1578 O OH  . TYR A 1 209 ? -10.16949 40.94877 23.48463 1.000 58.99965  ? 216 TYR A OH  1 
ATOM   1579 N N   . PRO A 1 210 ? -14.71641 35.33622 28.11482 1.000 53.59950  ? 217 PRO A N   1 
ATOM   1580 C CA  . PRO A 1 210 ? -15.26889 34.24233 28.92688 1.000 44.85241  ? 217 PRO A CA  1 
ATOM   1581 C C   . PRO A 1 210 ? -14.23165 33.15622 29.17481 1.000 48.15492  ? 217 PRO A C   1 
ATOM   1582 O O   . PRO A 1 210 ? -13.59832 32.65516 28.24308 1.000 54.44210  ? 217 PRO A O   1 
ATOM   1583 C CB  . PRO A 1 210 ? -16.43906 33.72336 28.08234 1.000 42.05054  ? 217 PRO A CB  1 
ATOM   1584 C CG  . PRO A 1 210 ? -16.13720 34.15988 26.69050 1.000 50.67034  ? 217 PRO A CG  1 
ATOM   1585 C CD  . PRO A 1 210 ? -15.36928 35.44170 26.79828 1.000 53.92508  ? 217 PRO A CD  1 
ATOM   1586 N N   . ILE A 1 211 ? -14.06295 32.79916 30.44408 1.000 44.21985  ? 218 ILE A N   1 
ATOM   1587 C CA  . ILE A 1 211 ? -13.16951 31.72542 30.86163 1.000 45.21874  ? 218 ILE A CA  1 
ATOM   1588 C C   . ILE A 1 211 ? -14.04202 30.54382 31.26122 1.000 52.19744  ? 218 ILE A C   1 
ATOM   1589 O O   . ILE A 1 211 ? -14.69001 30.56690 32.31492 1.000 56.56705  ? 218 ILE A O   1 
ATOM   1590 C CB  . ILE A 1 211 ? -12.25396 32.15775 32.01454 1.000 52.15410  ? 218 ILE A CB  1 
ATOM   1591 C CG1 . ILE A 1 211 ? -11.46203 33.40802 31.62689 1.000 50.30511  ? 218 ILE A CG1 1 
ATOM   1592 C CG2 . ILE A 1 211 ? -11.31459 31.02662 32.40244 1.000 51.96283  ? 218 ILE A CG2 1 
ATOM   1593 C CD1 . ILE A 1 211 ? -10.81877 34.11078 32.80102 1.000 51.27657  ? 218 ILE A CD1 1 
ATOM   1594 N N   . THR A 1 212 ? -14.06346 29.51063 30.42503 1.000 53.98633  ? 219 THR A N   1 
ATOM   1595 C CA  . THR A 1 212 ? -14.91581 28.34849 30.63599 1.000 50.02116  ? 219 THR A CA  1 
ATOM   1596 C C   . THR A 1 212 ? -14.08513 27.18637 31.16419 1.000 50.83631  ? 219 THR A C   1 
ATOM   1597 O O   . THR A 1 212 ? -13.07790 26.80941 30.55629 1.000 56.03786  ? 219 THR A O   1 
ATOM   1598 C CB  . THR A 1 212 ? -15.61867 27.94744 29.33806 1.000 53.15182  ? 219 THR A CB  1 
ATOM   1599 O OG1 . THR A 1 212 ? -16.40838 29.04417 28.86151 1.000 60.05937  ? 219 THR A OG1 1 
ATOM   1600 C CG2 . THR A 1 212 ? -16.51858 26.75066 29.57246 1.000 49.23657  ? 219 THR A CG2 1 
ATOM   1601 N N   . LEU A 1 213 ? -14.50668 26.62592 32.29441 1.000 53.15707  ? 220 LEU A N   1 
ATOM   1602 C CA  . LEU A 1 213 ? -13.83085 25.48168 32.89215 1.000 48.13999  ? 220 LEU A CA  1 
ATOM   1603 C C   . LEU A 1 213 ? -14.53589 24.21148 32.43332 1.000 50.57097  ? 220 LEU A C   1 
ATOM   1604 O O   . LEU A 1 213 ? -15.72222 24.01546 32.71942 1.000 57.47847  ? 220 LEU A O   1 
ATOM   1605 C CB  . LEU A 1 213 ? -13.82175 25.59856 34.41886 1.000 43.52662  ? 220 LEU A CB  1 
ATOM   1606 C CG  . LEU A 1 213 ? -13.12352 24.57069 35.32559 1.000 52.51926  ? 220 LEU A CG  1 
ATOM   1607 C CD1 . LEU A 1 213 ? -13.89525 23.26743 35.50599 1.000 51.79570  ? 220 LEU A CD1 1 
ATOM   1608 C CD2 . LEU A 1 213 ? -11.72966 24.28494 34.79311 1.000 55.42166  ? 220 LEU A CD2 1 
ATOM   1609 N N   . PHE A 1 214 ? -13.81052 23.36216 31.71075 1.000 48.91435  ? 221 PHE A N   1 
ATOM   1610 C CA  . PHE A 1 214 ? -14.35298 22.09945 31.22130 1.000 49.68503  ? 221 PHE A CA  1 
ATOM   1611 C C   . PHE A 1 214 ? -14.22553 21.05672 32.32488 1.000 57.23320  ? 221 PHE A C   1 
ATOM   1612 O O   . PHE A 1 214 ? -13.11323 20.66251 32.68862 1.000 60.88939  ? 221 PHE A O   1 
ATOM   1613 C CB  . PHE A 1 214 ? -13.61742 21.65294 29.96003 1.000 57.87756  ? 221 PHE A CB  1 
ATOM   1614 C CG  . PHE A 1 214 ? -14.10187 22.31523 28.69664 1.000 56.04142  ? 221 PHE A CG  1 
ATOM   1615 C CD1 . PHE A 1 214 ? -13.98137 21.66971 27.47666 1.000 59.88814  ? 221 PHE A CD1 1 
ATOM   1616 C CD2 . PHE A 1 214 ? -14.66824 23.57880 28.72422 1.000 54.68351  ? 221 PHE A CD2 1 
ATOM   1617 C CE1 . PHE A 1 214 ? -14.42038 22.26805 26.31048 1.000 56.05709  ? 221 PHE A CE1 1 
ATOM   1618 C CE2 . PHE A 1 214 ? -15.10847 24.18231 27.56017 1.000 49.48367  ? 221 PHE A CE2 1 
ATOM   1619 C CZ  . PHE A 1 214 ? -14.98433 23.52581 26.35293 1.000 48.35020  ? 221 PHE A CZ  1 
ATOM   1620 N N   . VAL A 1 215 ? -15.35282 20.61092 32.86237 1.000 54.46499  ? 222 VAL A N   1 
ATOM   1621 C CA  . VAL A 1 215 ? -15.34777 19.60756 33.91988 1.000 58.98031  ? 222 VAL A CA  1 
ATOM   1622 C C   . VAL A 1 215 ? -15.30584 18.22288 33.28819 1.000 58.98070  ? 222 VAL A C   1 
ATOM   1623 O O   . VAL A 1 215 ? -15.76561 18.01029 32.16052 1.000 61.51240  ? 222 VAL A O   1 
ATOM   1624 C CB  . VAL A 1 215 ? -16.56469 19.77198 34.85637 1.000 57.19578  ? 222 VAL A CB  1 
ATOM   1625 C CG1 . VAL A 1 215 ? -16.80133 21.23796 35.17325 1.000 61.29229  ? 222 VAL A CG1 1 
ATOM   1626 C CG2 . VAL A 1 215 ? -17.79986 19.16610 34.23868 1.000 57.51614  ? 222 VAL A CG2 1 
ATOM   1627 N N   . GLU A 1 216 ? -14.73437 17.27175 34.01717 1.000 58.14478  ? 223 GLU A N   1 
ATOM   1628 C CA  . GLU A 1 216 ? -14.60649 15.89939 33.55373 1.000 69.46440  ? 223 GLU A CA  1 
ATOM   1629 C C   . GLU A 1 216 ? -15.72726 15.03633 34.12238 1.000 65.77004  ? 223 GLU A C   1 
ATOM   1630 O O   . GLU A 1 216 ? -16.34237 15.36163 35.14079 1.000 66.48662  ? 223 GLU A O   1 
ATOM   1631 C CB  . GLU A 1 216 ? -13.24421 15.32003 33.94562 1.000 75.54318  ? 223 GLU A CB  1 
ATOM   1632 C CG  . GLU A 1 216 ? -12.10246 16.32155 33.87925 1.000 65.31880  ? 223 GLU A CG  1 
ATOM   1633 C CD  . GLU A 1 216 ? -10.80046 15.75878 34.41537 1.000 72.65722  ? 223 GLU A CD  1 
ATOM   1634 O OE1 . GLU A 1 216 ? -10.32657 14.73578 33.87714 1.000 71.88066  ? 223 GLU A OE1 1 
ATOM   1635 O OE2 . GLU A 1 216 ? -10.25037 16.34022 35.37441 1.000 76.86303  ? 223 GLU A OE2 1 
ATOM   1636 N N   . LYS A 1 217 ? -15.98587 13.92298 33.44470 1.000 57.51233  ? 224 LYS A N   1 
ATOM   1637 C CA  . LYS A 1 217 ? -17.04037 13.00438 33.85698 1.000 65.44936  ? 224 LYS A CA  1 
ATOM   1638 C C   . LYS A 1 217 ? -16.46966 11.63992 34.22913 1.000 80.31974  ? 224 LYS A C   1 
ATOM   1639 O O   . LYS A 1 217 ? -16.40792 11.28186 35.40527 1.000 80.84917  ? 224 LYS A O   1 
ATOM   1640 C CB  . LYS A 1 217 ? -18.08147 12.85366 32.74682 1.000 67.08040  ? 224 LYS A CB  1 
ATOM   1641 C CG  . LYS A 1 217 ? -17.98668 13.91176 31.66031 1.000 67.94851  ? 224 LYS A CG  1 
ATOM   1642 C CD  . LYS A 1 217 ? -17.37095 13.34361 30.39292 1.000 70.24453  ? 224 LYS A CD  1 
ATOM   1643 C CE  . LYS A 1 217 ? -18.33334 13.44194 29.22257 1.000 69.65622  ? 224 LYS A CE  1 
ATOM   1644 N NZ  . LYS A 1 217 ? -17.97506 14.55824 28.30879 1.000 68.00702  ? 224 LYS A NZ  1 
HETATM 1645 C CAG . WP1 B 2 .   ? 7.22674   34.43343 24.69782 1.000 74.45949  ? 301 WP1 A CAG 1 
HETATM 1646 C CAH . WP1 B 2 .   ? 5.96971   34.62591 25.56486 1.000 84.24135  ? 301 WP1 A CAH 1 
HETATM 1647 C CAJ . WP1 B 2 .   ? 6.29876   34.73686 27.03236 1.000 70.34541  ? 301 WP1 A CAJ 1 
HETATM 1648 C CAK . WP1 B 2 .   ? 5.09800   35.75866 25.08411 1.000 81.71793  ? 301 WP1 A CAK 1 
HETATM 1649 O OAI . WP1 B 2 .   ? 5.17361   33.38335 25.40133 1.000 80.38195  ? 301 WP1 A OAI 1 
HETATM 1650 C CAC . WP1 B 2 .   ? 5.85036   32.54160 24.55753 1.000 76.95816  ? 301 WP1 A CAC 1 
HETATM 1651 C CAB . WP1 B 2 .   ? 7.05062   33.06231 24.10333 1.000 73.20445  ? 301 WP1 A CAB 1 
HETATM 1652 C CAA . WP1 B 2 .   ? 7.85057   32.32670 23.23915 1.000 71.38638  ? 301 WP1 A CAA 1 
HETATM 1653 C CAF . WP1 B 2 .   ? 7.42228   31.06508 22.84867 1.000 62.97149  ? 301 WP1 A CAF 1 
HETATM 1654 C CAE . WP1 B 2 .   ? 6.22133   30.56312 23.31670 1.000 59.85792  ? 301 WP1 A CAE 1 
HETATM 1655 C CAD . WP1 B 2 .   ? 5.40195   31.28252 24.18036 1.000 72.78970  ? 301 WP1 A CAD 1 
HETATM 1656 C CAL . WP1 B 2 .   ? 4.11851   30.65204 24.63176 1.000 80.23160  ? 301 WP1 A CAL 1 
HETATM 1657 O OAN . WP1 B 2 .   ? 3.29887   31.30790 25.29190 1.000 82.18937  ? 301 WP1 A OAN 1 
HETATM 1658 N NAM . WP1 B 2 .   ? 3.90275   29.38800 24.29380 1.000 81.91566  ? 301 WP1 A NAM 1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLU A 9   ? 0.99468 1.21825 1.07952 -0.13365 0.10711  -0.41678 16  GLU A N   
2    C CA  . GLU A 9   ? 1.09881 1.29604 1.17620 -0.10015 0.10185  -0.37261 16  GLU A CA  
3    C C   . GLU A 9   ? 0.98586 1.19500 1.08701 -0.07356 0.07386  -0.33219 16  GLU A C   
4    O O   . GLU A 9   ? 0.89389 1.15402 0.98636 -0.06679 0.03909  -0.32824 16  GLU A O   
5    C CB  . GLU A 9   ? 1.21259 1.43777 1.24114 -0.09330 0.08488  -0.37528 16  GLU A CB  
6    C CG  . GLU A 9   ? 1.25781 1.44130 1.27734 -0.06975 0.09806  -0.34279 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.41218 1.61352 1.43041 -0.03919 0.06704  -0.30134 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.39456 1.63860 1.41362 -0.03368 0.03551  -0.29660 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.43545 1.60742 1.45325 -0.02165 0.07707  -0.27458 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.86528 1.02854 0.99497 -0.05746 0.09010  -0.30223 17  VAL A N   
11   C CA  . VAL A 10  ? 0.74852 0.91633 0.89985 -0.03533 0.06799  -0.26650 17  VAL A CA  
12   C C   . VAL A 10  ? 0.79702 0.94478 0.94894 -0.01085 0.06651  -0.23090 17  VAL A C   
13   O O   . VAL A 10  ? 0.77862 0.89022 0.94020 -0.00763 0.09496  -0.22591 17  VAL A O   
14   C CB  . VAL A 10  ? 0.73637 0.87508 0.92232 -0.03893 0.08666  -0.26408 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.69161 0.83288 0.89373 -0.01567 0.06413  -0.22713 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.79982 0.95994 0.99013 -0.06717 0.09130  -0.30228 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.74214 0.91358 0.88565 0.00573  0.03631  -0.20716 18  GLU A N   
18   C CA  . GLU A 11  ? 0.67712 0.83487 0.82503 0.02487  0.03369  -0.17583 18  GLU A CA  
19   C C   . GLU A 11  ? 0.64179 0.79294 0.81950 0.03704  0.02368  -0.14999 18  GLU A C   
20   O O   . GLU A 11  ? 0.62335 0.79053 0.80175 0.03708  0.00489  -0.14860 18  GLU A O   
21   C CB  . GLU A 11  ? 0.67802 0.85851 0.79110 0.03381  0.01314  -0.16774 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.71928 0.90504 0.79497 0.02674  0.02279  -0.18814 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.87839 1.08675 0.91308 0.04011  0.00282  -0.17773 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.94680 1.18413 0.97418 0.04691  -0.02164 -0.17276 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.87326 1.06764 0.88201 0.04587  0.01475  -0.17291 18  GLU A OE2 
26   N N   . THR A 12  ? 0.63559 0.76680 0.83747 0.04800  0.03619  -0.12993 19  THR A N   
27   C CA  . THR A 12  ? 0.60836 0.73785 0.83551 0.06054  0.02578  -0.10531 19  THR A CA  
28   C C   . THR A 12  ? 0.59012 0.73241 0.81655 0.06959  0.00938  -0.08463 19  THR A C   
29   O O   . THR A 12  ? 0.60146 0.74146 0.82982 0.07149  0.02068  -0.08126 19  THR A O   
30   C CB  . THR A 12  ? 0.61951 0.72532 0.87713 0.06887  0.05105  -0.09653 19  THR A CB  
31   O OG1 . THR A 12  ? 0.64537 0.72985 0.90147 0.05773  0.07361  -0.11793 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.59677 0.70752 0.87476 0.08390  0.03682  -0.07085 19  THR A CG2 
33   N N   . PHE A 13  ? 0.56792 0.72065 0.79146 0.07334  -0.01357 -0.07251 20  PHE A N   
34   C CA  . PHE A 13  ? 0.55633 0.71723 0.77690 0.07735  -0.02676 -0.05661 20  PHE A CA  
35   C C   . PHE A 13  ? 0.54773 0.71328 0.79430 0.08360  -0.03608 -0.03929 20  PHE A C   
36   O O   . PHE A 13  ? 0.60943 0.77036 0.86533 0.08766  -0.03773 -0.03697 20  PHE A O   
37   C CB  . PHE A 13  ? 0.57261 0.73938 0.75940 0.07634  -0.04352 -0.05794 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.59551 0.76746 0.75133 0.07402  -0.03926 -0.07308 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.58547 0.76613 0.73664 0.06742  -0.03696 -0.09322 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.61471 0.78404 0.74389 0.07792  -0.03655 -0.06813 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.61716 0.81199 0.73786 0.06446  -0.03651 -0.10946 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.72682 0.90429 0.82114 0.07927  -0.03429 -0.08028 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.72359 0.91798 0.81364 0.07240  -0.03660 -0.10163 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.65256 0.82831 0.90920 0.08353  -0.04103 -0.02821 21  ALA A N   
45   C CA  . ALA A 14  ? 0.56984 0.76013 0.84850 0.08701  -0.05380 -0.01434 21  ALA A CA  
46   C C   . ALA A 14  ? 0.61894 0.80691 0.87374 0.08021  -0.07156 -0.01234 21  ALA A C   
47   O O   . ALA A 14  ? 0.66601 0.84829 0.90341 0.07327  -0.06939 -0.01460 21  ALA A O   
48   C CB  . ALA A 14  ? 0.61443 0.82579 0.92691 0.08802  -0.04657 -0.00697 21  ALA A CB  
49   N N   . PHE A 15  ? 0.69325 0.87997 0.94395 0.08332  -0.08496 -0.00742 22  PHE A N   
50   C CA  . PHE A 15  ? 0.60245 0.78231 0.82966 0.07707  -0.09858 -0.00552 22  PHE A CA  
51   C C   . PHE A 15  ? 0.66950 0.86212 0.90646 0.06654  -0.10191 -0.00288 22  PHE A C   
52   O O   . PHE A 15  ? 0.69040 0.90881 0.96010 0.06657  -0.10175 0.00064  22  PHE A O   
53   C CB  . PHE A 15  ? 0.53180 0.70755 0.75434 0.08254  -0.10981 -0.00021 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.70363 0.86205 0.90573 0.08567  -0.10814 -0.00589 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.86855 1.01827 1.04488 0.08278  -0.10900 -0.01056 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.65884 0.81122 0.86903 0.09266  -0.10327 -0.00598 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.84009 0.98561 1.00426 0.08646  -0.10899 -0.01620 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.65860 0.80097 0.85659 0.09216  -0.10020 -0.01425 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.76687 0.91097 0.94443 0.08885  -0.10503 -0.01989 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.57633 0.75170 0.78619 0.05742  -0.10237 -0.00515 23  GLN A N   
61   C CA  . GLN A 16  ? 0.53859 0.72117 0.75528 0.04172  -0.10258 -0.00695 23  GLN A CA  
62   C C   . GLN A 16  ? 0.62290 0.83094 0.85642 0.03828  -0.12052 -0.00477 23  GLN A C   
63   O O   . GLN A 16  ? 0.70272 0.90528 0.92418 0.04744  -0.13141 -0.00025 23  GLN A O   
64   C CB  . GLN A 16  ? 0.56124 0.70934 0.73925 0.03397  -0.09473 -0.00907 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.59253 0.72101 0.75496 0.03525  -0.07404 -0.00945 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.75627 0.84537 0.87380 0.03748  -0.06336 -0.00607 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.79625 0.87126 0.89611 0.03649  -0.07032 -0.00472 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.91761 0.98620 1.01364 0.04312  -0.04376 -0.00295 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.65781 0.89742 0.91972 0.02515  -0.12304 -0.00844 24  ALA A N   
70   C CA  . ALA A 17  ? 0.53846 0.81595 0.81820 0.02349  -0.14318 -0.00659 24  ALA A CA  
71   C C   . ALA A 17  ? 0.56455 0.81998 0.80613 0.01683  -0.15472 -0.00932 24  ALA A C   
72   O O   . ALA A 17  ? 0.59865 0.86524 0.83521 0.02812  -0.17010 -0.00228 24  ALA A O   
73   C CB  . ALA A 17  ? 0.56699 0.88913 0.88401 0.00516  -0.14437 -0.01481 24  ALA A CB  
74   N N   . GLU A 18  ? 0.62289 0.84186 0.83390 0.00063  -0.14381 -0.01808 25  GLU A N   
75   C CA  . GLU A 18  ? 0.70494 0.89633 0.87729 -0.00622 -0.14962 -0.02131 25  GLU A CA  
76   C C   . GLU A 18  ? 0.68481 0.85235 0.83529 0.01590  -0.15316 -0.01048 25  GLU A C   
77   O O   . GLU A 18  ? 0.63780 0.80216 0.77067 0.01861  -0.16493 -0.00829 25  GLU A O   
78   C CB  . GLU A 18  ? 0.73836 0.88639 0.88122 -0.02374 -0.12914 -0.03021 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.86042 1.02554 1.02217 -0.05250 -0.12091 -0.04537 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.87107 1.04664 1.06204 -0.05137 -0.10485 -0.04418 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.76260 0.93799 0.95983 -0.02817 -0.10375 -0.03233 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.93777 1.12068 1.14485 -0.07565 -0.09113 -0.05697 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.68758 0.83996 0.83845 0.03048  -0.14214 -0.00528 26  ILE A N   
84   C CA  . ILE A 19  ? 0.67384 0.80978 0.81104 0.04774  -0.14338 0.00115  26  ILE A CA  
85   C C   . ILE A 19  ? 0.69551 0.85438 0.85360 0.06017  -0.15333 0.00807  26  ILE A C   
86   O O   . ILE A 19  ? 0.70940 0.85538 0.85227 0.06872  -0.15741 0.01287  26  ILE A O   
87   C CB  . ILE A 19  ? 0.57737 0.70172 0.71181 0.05718  -0.13063 0.00100  26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.64867 0.74397 0.75204 0.05327  -0.11925 -0.00006 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.61741 0.73792 0.75084 0.07120  -0.13158 0.00321  26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.70160 0.79586 0.80366 0.05850  -0.10655 -0.00031 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.67608 0.86630 0.86824 0.06342  -0.15391 0.01038  27  ALA A N   
92   C CA  . ALA A 20  ? 0.57410 0.78276 0.78512 0.08051  -0.15837 0.02085  27  ALA A CA  
93   C C   . ALA A 20  ? 0.66183 0.88416 0.86032 0.08200  -0.17576 0.02657  27  ALA A C   
94   O O   . ALA A 20  ? 0.71770 0.93287 0.90809 0.09909  -0.17697 0.03728  27  ALA A O   
95   C CB  . ALA A 20  ? 0.54264 0.78364 0.79369 0.08565  -0.15313 0.02391  27  ALA A CB  
96   N N   . GLN A 21  ? 0.63919 0.87987 0.83319 0.06327  -0.18732 0.01835  28  GLN A N   
97   C CA  . GLN A 21  ? 0.60368 0.85987 0.77885 0.06128  -0.20568 0.01985  28  GLN A CA  
98   C C   . GLN A 21  ? 0.68519 0.89410 0.81461 0.06098  -0.20292 0.01919  28  GLN A C   
99   O O   . GLN A 21  ? 0.71282 0.92264 0.82038 0.06963  -0.21343 0.02590  28  GLN A O   
100  C CB  . GLN A 21  ? 0.67661 0.96666 0.85979 0.03496  -0.21667 0.00511  28  GLN A CB  
101  C CG  . GLN A 21  ? 0.66495 1.00486 0.89853 0.03182  -0.21670 0.00352  28  GLN A CG  
102  C CD  . GLN A 21  ? 0.75126 1.13162 0.99751 0.00203  -0.22711 -0.01447 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.76378 1.12945 0.97678 -0.01863 -0.23281 -0.02774 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.80555 1.23667 1.10114 -0.00234 -0.22693 -0.01702 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.68922 0.85818 0.80265 0.05357  -0.18794 0.01266  29  LEU A N   
106  C CA  . LEU A 22  ? 0.67986 0.80613 0.75497 0.05538  -0.18232 0.01304  29  LEU A CA  
107  C C   . LEU A 22  ? 0.64792 0.76212 0.72289 0.07747  -0.17775 0.02475  29  LEU A C   
108  O O   . LEU A 22  ? 0.69864 0.79479 0.74642 0.08341  -0.17989 0.02967  29  LEU A O   
109  C CB  . LEU A 22  ? 0.81830 0.91240 0.88128 0.04822  -0.16629 0.00675  29  LEU A CB  
110  C CG  . LEU A 22  ? 0.73159 0.78432 0.75947 0.05201  -0.15749 0.00811  29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.69237 0.72958 0.68651 0.03725  -0.16231 0.00210  29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.83349 0.86401 0.85487 0.05368  -0.14153 0.00683  29  LEU A CD2 
113  N N   . MET A 23  ? 0.63873 0.75907 0.74190 0.08820  -0.16806 0.02779  30  MET A N   
114  C CA  . MET A 23  ? 0.67589 0.78050 0.78185 0.10510  -0.15726 0.03527  30  MET A CA  
115  C C   . MET A 23  ? 0.70105 0.81625 0.80468 0.12085  -0.16339 0.04928  30  MET A C   
116  O O   . MET A 23  ? 0.76667 0.85710 0.84724 0.13105  -0.15819 0.05658  30  MET A O   
117  C CB  . MET A 23  ? 0.60785 0.71789 0.74359 0.10859  -0.14373 0.03116  30  MET A CB  
118  C CG  . MET A 23  ? 0.67888 0.78935 0.81581 0.09663  -0.14089 0.01981  30  MET A CG  
119  S SD  . MET A 23  ? 0.64927 0.77124 0.81547 0.09902  -0.12715 0.01255  30  MET A SD  
120  C CE  . MET A 23  ? 0.57775 0.68045 0.74357 0.10472  -0.11266 0.00765  30  MET A CE  
121  N N   . SER A 24  ? 0.73062 0.88405 0.85769 0.12546  -0.17306 0.05476  31  SER A N   
122  C CA  . SER A 24  ? 0.68136 0.85352 0.80640 0.14639  -0.18031 0.07188  31  SER A CA  
123  C C   . SER A 24  ? 0.73393 0.90058 0.81713 0.14478  -0.19523 0.07424  31  SER A C   
124  O O   . SER A 24  ? 0.75926 0.91693 0.82207 0.16606  -0.19386 0.09002  31  SER A O   
125  C CB  . SER A 24  ? 0.64955 0.87607 0.80968 0.14989  -0.19211 0.07603  31  SER A CB  
126  O OG  . SER A 24  ? 0.72736 0.98534 0.88092 0.17015  -0.20651 0.09277  31  SER A OG  
127  N N   . LEU A 25  ? 0.77149 0.93844 0.83721 0.12004  -0.20623 0.05868  32  LEU A N   
128  C CA  . LEU A 25  ? 0.76598 0.91821 0.78573 0.11445  -0.21613 0.05675  32  LEU A CA  
129  C C   . LEU A 25  ? 0.83329 0.92949 0.82416 0.12316  -0.19730 0.06131  32  LEU A C   
130  O O   . LEU A 25  ? 0.90544 0.98480 0.85942 0.13323  -0.19913 0.06952  32  LEU A O   
131  C CB  . LEU A 25  ? 0.76638 0.92214 0.77398 0.08316  -0.22439 0.03640  32  LEU A CB  
132  C CG  . LEU A 25  ? 0.81470 0.97368 0.77873 0.07119  -0.23987 0.02929  32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.83429 1.05937 0.80953 0.07771  -0.26565 0.03408  32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.79802 0.93768 0.74549 0.03805  -0.23545 0.00691  32  LEU A CD2 
135  N N   . ILE A 26  ? 0.79996 0.87047 0.80738 0.11980  -0.17882 0.05571  33  ILE A N   
136  C CA  . ILE A 26  ? 0.75489 0.78059 0.74338 0.12519  -0.16016 0.05706  33  ILE A CA  
137  C C   . ILE A 26  ? 0.81380 0.82551 0.80351 0.14824  -0.14650 0.07220  33  ILE A C   
138  O O   . ILE A 26  ? 0.97925 0.95739 0.93860 0.15640  -0.13596 0.07857  33  ILE A O   
139  C CB  . ILE A 26  ? 0.71885 0.73490 0.72883 0.11602  -0.14708 0.04595  33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.65144 0.65577 0.64021 0.09924  -0.15028 0.03584  33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.79845 0.78726 0.81247 0.12511  -0.12584 0.04736  33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.62514 0.63161 0.63379 0.09415  -0.14177 0.02816  33  ILE A CD1 
143  N N   . ILE A 27  ? 0.80248 0.83420 0.82498 0.15977  -0.14212 0.07880  34  ILE A N   
144  C CA  . ILE A 27  ? 0.86629 0.87563 0.88973 0.18240  -0.12116 0.09360  34  ILE A CA  
145  C C   . ILE A 27  ? 1.02871 1.04385 1.02052 0.20418  -0.13133 0.11394  34  ILE A C   
146  O O   . ILE A 27  ? 1.10287 1.08225 1.07033 0.22276  -0.11284 0.12781  34  ILE A O   
147  C CB  . ILE A 27  ? 0.80875 0.83064 0.87462 0.18806  -0.10758 0.09358  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.67926 0.71793 0.77237 0.16563  -0.11138 0.07342  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.93073 0.91129 1.00026 0.20053  -0.07315 0.09856  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.62667 0.67507 0.75630 0.16844  -0.09696 0.07037  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.97968 1.04224 0.97079 0.20260  -0.15985 0.11578  35  ASN A N   
152  C CA  . ASN A 28  ? 1.02851 1.11410 0.99499 0.22693  -0.17384 0.13605  35  ASN A CA  
153  C C   . ASN A 28  ? 1.15425 1.23228 1.06641 0.22068  -0.19004 0.13370  35  ASN A C   
154  O O   . ASN A 28  ? 1.36154 1.44284 1.23911 0.24541  -0.19518 0.15276  35  ASN A O   
155  C CB  . ASN A 28  ? 0.97431 1.12834 0.97432 0.23002  -0.19711 0.13886  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.93787 1.09699 0.98680 0.24123  -0.17811 0.14455  35  ASN A CG  
157  O OD1 . ASN A 28  ? 1.11698 1.31458 1.20400 0.22815  -0.18759 0.13456  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.94904 1.06460 0.99538 0.26411  -0.14721 0.15938  35  ASN A ND2 
159  N N   . THR A 29  ? 1.15377 1.21933 1.05353 0.19038  -0.19596 0.11196  36  THR A N   
160  C CA  . THR A 29  ? 1.24233 1.29484 1.08713 0.18155  -0.20758 0.10682  36  THR A CA  
161  C C   . THR A 29  ? 1.22447 1.21517 1.03070 0.19728  -0.18244 0.11818  36  THR A C   
162  O O   . THR A 29  ? 1.17827 1.12799 0.99966 0.19299  -0.15658 0.11367  36  THR A O   
163  C CB  . THR A 29  ? 1.26046 1.30743 1.10207 0.14574  -0.21326 0.08106  36  THR A CB  
164  O OG1 . THR A 29  ? 1.14389 1.24664 1.01769 0.12923  -0.23418 0.06961  36  THR A OG1 
165  C CG2 . THR A 29  ? 1.20349 1.22578 0.98396 0.13486  -0.21870 0.07358  36  THR A CG2 
166  N N   . PHE A 30  ? 1.21006 1.19766 0.96637 0.21568  -0.18975 0.13251  37  PHE A N   
167  C CA  . PHE A 30  ? 1.23245 1.15798 0.94483 0.23122  -0.16383 0.14429  37  PHE A CA  
168  C C   . PHE A 30  ? 1.29620 1.18178 0.98277 0.20450  -0.15583 0.12447  37  PHE A C   
169  O O   . PHE A 30  ? 1.41893 1.31089 1.06326 0.18973  -0.17389 0.11371  37  PHE A O   
170  C CB  . PHE A 30  ? 1.34302 1.27838 1.00099 0.25954  -0.17574 0.16573  37  PHE A CB  
171  C CG  . PHE A 30  ? 1.43509 1.30258 1.04633 0.28133  -0.14391 0.18269  37  PHE A CG  
172  C CD1 . PHE A 30  ? 1.47063 1.29685 1.10602 0.30095  -0.10654 0.19758  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 1.39209 1.23407 0.93372 0.28029  -0.14798 0.18194  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 1.44559 1.20608 1.03982 0.31917  -0.07226 0.21218  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 1.33501 1.11078 0.83207 0.30085  -0.11511 0.19824  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 1.27497 1.00990 0.79999 0.32040  -0.07646 0.21380  37  PHE A CZ  
177  N N   . TYR A 31  ? 1.20903 1.05568 0.92153 0.19812  -0.12757 0.11867  38  TYR A N   
178  C CA  . TYR A 31  ? 1.23998 1.05150 0.93766 0.17717  -0.11604 0.10255  38  TYR A CA  
179  C C   . TYR A 31  ? 1.21270 0.97404 0.91555 0.18720  -0.07928 0.10846  38  TYR A C   
180  O O   . TYR A 31  ? 1.13353 0.89851 0.88406 0.19207  -0.06348 0.10985  38  TYR A O   
181  C CB  . TYR A 31  ? 1.13024 0.96725 0.86989 0.15315  -0.12497 0.08384  38  TYR A CB  
182  C CG  . TYR A 31  ? 1.11464 0.91720 0.83936 0.13591  -0.11158 0.07031  38  TYR A CG  
183  C CD1 . TYR A 31  ? 1.17608 0.96678 0.85483 0.11917  -0.12082 0.05935  38  TYR A CD1 
184  C CD2 . TYR A 31  ? 1.15936 0.94411 0.91687 0.13642  -0.08851 0.06768  38  TYR A CD2 
185  C CE1 . TYR A 31  ? 1.20001 0.95278 0.86340 0.10641  -0.10317 0.04913  38  TYR A CE1 
186  C CE2 . TYR A 31  ? 1.19058 0.94764 0.93648 0.12623  -0.07491 0.05903  38  TYR A CE2 
187  C CZ  . TYR A 31  ? 1.19765 0.93442 0.89550 0.11269  -0.08026 0.05123  38  TYR A CZ  
188  O OH  . TYR A 31  ? 1.12997 0.83254 0.81446 0.10548  -0.06133 0.04473  38  TYR A OH  
189  N N   . SER A 32  ? 1.35140 1.06668 1.00586 0.18808  -0.06389 0.10966  39  SER A N   
190  C CA  . SER A 32  ? 1.39157 1.05851 1.04636 0.19918  -0.02626 0.11680  39  SER A CA  
191  C C   . SER A 32  ? 1.36612 1.01917 1.05287 0.18358  -0.00704 0.10204  39  SER A C   
192  O O   . SER A 32  ? 1.48986 1.12166 1.20293 0.18852  0.02320  0.10326  39  SER A O   
193  C CB  . SER A 32  ? 1.58749 1.20881 1.16974 0.21316  -0.01519 0.12934  39  SER A CB  
194  O OG  . SER A 32  ? 1.70258 1.32970 1.26080 0.23866  -0.02036 0.15018  39  SER A OG  
195  N N   . ASN A 33  ? 1.20695 0.87250 0.89297 0.16578  -0.02139 0.08839  40  ASN A N   
196  C CA  . ASN A 33  ? 1.14104 0.79773 0.85566 0.15701  -0.00337 0.07837  40  ASN A CA  
197  C C   . ASN A 33  ? 1.09650 0.79818 0.87857 0.15217  -0.00912 0.07086  40  ASN A C   
198  O O   . ASN A 33  ? 1.16356 0.88387 0.96297 0.14238  -0.01713 0.06195  40  ASN A O   
199  C CB  . ASN A 33  ? 1.07757 0.71811 0.75588 0.14359  -0.00915 0.06950  40  ASN A CB  
200  C CG  . ASN A 33  ? 1.18753 0.79759 0.87112 0.14433  0.01980  0.06695  40  ASN A CG  
201  O OD1 . ASN A 33  ? 1.26807 0.86971 0.97843 0.15373  0.04352  0.07103  40  ASN A OD1 
202  N ND2 . ASN A 33  ? 1.29199 0.88561 0.95206 0.13436  0.02092  0.05982  40  ASN A ND2 
203  N N   . LYS A 34  ? 1.06793 0.87513 0.75500 -0.07201 -0.04025 -0.15476 41  LYS A N   
204  C CA  . LYS A 34  ? 0.95136 0.84576 0.75049 -0.09484 -0.03043 -0.14566 41  LYS A CA  
205  C C   . LYS A 34  ? 0.93656 0.83593 0.75838 -0.06529 0.00453  -0.14753 41  LYS A C   
206  O O   . LYS A 34  ? 0.91883 0.87255 0.81454 -0.08282 0.00740  -0.14309 41  LYS A O   
207  C CB  . LYS A 34  ? 0.82200 0.81572 0.71407 -0.10081 -0.01592 -0.13172 41  LYS A CB  
208  C CG  . LYS A 34  ? 0.87519 0.89269 0.77792 -0.13613 -0.05158 -0.12333 41  LYS A CG  
209  C CD  . LYS A 34  ? 0.81695 0.92163 0.80286 -0.13125 -0.03458 -0.11116 41  LYS A CD  
210  C CE  . LYS A 34  ? 0.79046 0.91556 0.77880 -0.15665 -0.06681 -0.09929 41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.70717 0.87189 0.73636 -0.19576 -0.09631 -0.08773 41  LYS A NZ  
212  N N   . GLU A 35  ? 1.00301 0.85048 0.76197 -0.01789 0.03138  -0.15108 42  GLU A N   
213  C CA  . GLU A 35  ? 0.94864 0.81298 0.74044 0.01305  0.06596  -0.14512 42  GLU A CA  
214  C C   . GLU A 35  ? 1.00891 0.82680 0.78158 -0.00144 0.04632  -0.15546 42  GLU A C   
215  O O   . GLU A 35  ? 1.00530 0.84930 0.82197 0.01532  0.06897  -0.14834 42  GLU A O   
216  C CB  . GLU A 35  ? 0.98316 0.81050 0.71033 0.07436  0.10318  -0.13918 42  GLU A CB  
217  C CG  . GLU A 35  ? 1.10736 0.80726 0.69213 0.10161  0.08752  -0.16075 42  GLU A CG  
218  C CD  . GLU A 35  ? 1.31053 0.98183 0.82877 0.17638  0.13411  -0.15215 42  GLU A CD  
219  O OE1 . GLU A 35  ? 1.28229 1.00441 0.81582 0.19994  0.16386  -0.13245 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 1.39927 1.00335 0.85496 0.21293  0.14123  -0.16009 42  GLU A OE2 
221  N N   . ILE A 36  ? 1.03139 0.78256 0.74438 -0.03505 0.00089  -0.16726 43  ILE A N   
222  C CA  . ILE A 36  ? 1.05221 0.75240 0.74461 -0.05241 -0.02285 -0.17206 43  ILE A CA  
223  C C   . ILE A 36  ? 0.89722 0.68746 0.69497 -0.08745 -0.02301 -0.15870 43  ILE A C   
224  O O   . ILE A 36  ? 0.98182 0.74563 0.77635 -0.09965 -0.03620 -0.15710 43  ILE A O   
225  C CB  . ILE A 36  ? 1.17969 0.77994 0.78278 -0.08595 -0.08095 -0.18125 43  ILE A CB  
226  C CG1 . ILE A 36  ? 1.13893 0.80460 0.79848 -0.14066 -0.11169 -0.16701 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 1.27909 0.76508 0.75005 -0.04338 -0.08562 -0.20050 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 1.04041 0.73013 0.74786 -0.19333 -0.14811 -0.14779 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.87136 0.76124 0.75456 -0.10029 -0.00977 -0.14915 44  PHE A N   
230  C CA  . PHE A 37  ? 0.80094 0.77001 0.76799 -0.12420 -0.00880 -0.13933 44  PHE A CA  
231  C C   . PHE A 37  ? 0.75953 0.74109 0.75696 -0.09880 0.01659  -0.13825 44  PHE A C   
232  O O   . PHE A 37  ? 0.74224 0.74385 0.76744 -0.11568 0.00886  -0.13310 44  PHE A O   
233  C CB  . PHE A 37  ? 0.73630 0.79325 0.77255 -0.13198 -0.00063 -0.13346 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.61092 0.70790 0.69412 -0.10016 0.03146  -0.13305 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.64547 0.72152 0.70421 -0.07224 0.04905  -0.13165 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.64499 0.79834 0.79435 -0.09891 0.04031  -0.13036 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.67662 0.79566 0.79001 -0.04891 0.07434  -0.12103 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.66153 0.84445 0.85766 -0.07677 0.05886  -0.12533 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.56183 0.73186 0.74707 -0.05439 0.07560  -0.11736 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.80145 0.77737 0.79725 -0.05817 0.04647  -0.13757 45  LEU A N   
241  C CA  . LEU A 38  ? 0.71829 0.71420 0.75355 -0.03493 0.06772  -0.12918 45  LEU A CA  
242  C C   . LEU A 38  ? 0.76334 0.68760 0.74319 -0.02575 0.06006  -0.13268 45  LEU A C   
243  O O   . LEU A 38  ? 0.72467 0.66851 0.74132 -0.02512 0.06281  -0.12534 45  LEU A O   
244  C CB  . LEU A 38  ? 0.66744 0.68683 0.72506 0.00527  0.10138  -0.11591 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.64597 0.72594 0.78781 0.01632  0.11684  -0.09687 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.55657 0.69075 0.76175 -0.01842 0.09617  -0.10111 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.61872 0.73617 0.79716 0.04808  0.14624  -0.07223 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.88422 0.71713 0.77004 -0.01778 0.04593  -0.14421 46  ARG A N   
249  C CA  . ARG A 39  ? 0.86818 0.61407 0.69010 -0.00827 0.03147  -0.14953 46  ARG A CA  
250  C C   . ARG A 39  ? 0.86677 0.62098 0.71370 -0.05867 -0.00233 -0.14417 46  ARG A C   
251  O O   . ARG A 39  ? 0.94997 0.68084 0.79648 -0.05467 -0.00578 -0.13886 46  ARG A O   
252  C CB  . ARG A 39  ? 1.08115 0.70989 0.78189 0.01091  0.01412  -0.16666 46  ARG A CB  
253  C CG  . ARG A 39  ? 1.16608 0.68585 0.79091 -0.00852 -0.03008 -0.17532 46  ARG A CG  
254  C CD  . ARG A 39  ? 1.24666 0.64207 0.74505 0.00009  -0.06226 -0.19530 46  ARG A CD  
255  N NE  . ARG A 39  ? 1.33624 0.73623 0.84478 -0.06508 -0.11306 -0.18829 46  ARG A NE  
256  C CZ  . ARG A 39  ? 1.37082 0.73524 0.82946 -0.07017 -0.13853 -0.18896 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 1.43368 0.73854 0.80938 -0.01683 -0.12198 -0.20257 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 1.30782 0.70435 0.80431 -0.12675 -0.17918 -0.17022 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.78490 0.57972 0.65763 -0.10411 -0.02559 -0.14021 47  GLU A N   
260  C CA  . GLU A 40  ? 0.79128 0.60902 0.69209 -0.15033 -0.05378 -0.12559 47  GLU A CA  
261  C C   . GLU A 40  ? 0.77117 0.67916 0.75178 -0.14934 -0.03236 -0.11547 47  GLU A C   
262  O O   . GLU A 40  ? 0.76793 0.67304 0.75586 -0.16347 -0.04321 -0.10392 47  GLU A O   
263  C CB  . GLU A 40  ? 0.76876 0.61794 0.68134 -0.19386 -0.08120 -0.11603 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.89426 0.64619 0.72228 -0.20274 -0.11518 -0.12465 47  GLU A CG  
265  C CD  . GLU A 40  ? 1.12287 0.74579 0.86271 -0.19620 -0.14273 -0.13235 47  GLU A CD  
266  O OE1 . GLU A 40  ? 1.10427 0.73039 0.86671 -0.21665 -0.15813 -0.11349 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 1.21128 0.74057 0.86399 -0.15968 -0.14350 -0.15274 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.71408 0.69541 0.74948 -0.13323 -0.00657 -0.11894 48  LEU A N   
269  C CA  . LEU A 41  ? 0.57201 0.62391 0.67006 -0.13056 0.00569  -0.11314 48  LEU A CA  
270  C C   . LEU A 41  ? 0.63896 0.66490 0.73831 -0.10495 0.01636  -0.11007 48  LEU A C   
271  O O   . LEU A 41  ? 0.69524 0.74684 0.81914 -0.11266 0.01141  -0.10188 48  LEU A O   
272  C CB  . LEU A 41  ? 0.48083 0.59583 0.62831 -0.11854 0.02185  -0.11863 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.44360 0.60195 0.60358 -0.13929 0.01351  -0.11877 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.45043 0.65416 0.64986 -0.11863 0.02542  -0.12095 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.54881 0.73333 0.70859 -0.16155 -0.00195 -0.10095 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.65824 0.63727 0.73013 -0.07060 0.03232  -0.11334 49  ILE A N   
277  C CA  . ILE A 42  ? 0.66518 0.62339 0.74110 -0.04084 0.04439  -0.10460 49  ILE A CA  
278  C C   . ILE A 42  ? 0.71635 0.60539 0.74065 -0.05186 0.02260  -0.10306 49  ILE A C   
279  O O   . ILE A 42  ? 0.69175 0.58616 0.73651 -0.04736 0.02106  -0.09201 49  ILE A O   
280  C CB  . ILE A 42  ? 0.74165 0.67734 0.80093 0.00700  0.07326  -0.10197 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.62478 0.64103 0.75809 0.01464  0.09227  -0.09144 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.78505 0.68759 0.83410 0.04454  0.08614  -0.08984 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.60449 0.61904 0.73296 0.06109  0.12503  -0.07783 49  ILE A CD1 
284  N N   . SER A 43  ? 0.71032 0.52964 0.66749 -0.06951 -0.00030 -0.11147 50  SER A N   
285  C CA  . SER A 43  ? 0.74376 0.49037 0.65376 -0.08921 -0.03119 -0.10597 50  SER A CA  
286  C C   . SER A 43  ? 0.77411 0.58552 0.73506 -0.13251 -0.04704 -0.08748 50  SER A C   
287  O O   . SER A 43  ? 0.77613 0.56109 0.73024 -0.14006 -0.06082 -0.07434 50  SER A O   
288  C CB  . SER A 43  ? 0.79232 0.44604 0.62103 -0.10629 -0.06338 -0.11597 50  SER A CB  
289  O OG  . SER A 43  ? 1.08130 0.68343 0.85436 -0.06243 -0.04564 -0.13458 50  SER A OG  
290  N N   . ASN A 44  ? 0.70997 0.60629 0.71797 -0.15666 -0.04384 -0.08428 51  ASN A N   
291  C CA  . ASN A 44  ? 0.56763 0.53656 0.61903 -0.18523 -0.05020 -0.06545 51  ASN A CA  
292  C C   . ASN A 44  ? 0.59331 0.59820 0.67950 -0.16236 -0.03400 -0.06373 51  ASN A C   
293  O O   . ASN A 44  ? 0.62027 0.64182 0.71370 -0.17676 -0.04384 -0.04657 51  ASN A O   
294  C CB  . ASN A 44  ? 0.53154 0.58271 0.61969 -0.20132 -0.04454 -0.06434 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.63423 0.67239 0.70380 -0.23875 -0.07041 -0.05052 51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.80004 0.77422 0.83403 -0.26369 -0.10004 -0.03615 51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.68754 0.78138 0.78257 -0.23881 -0.06309 -0.05101 51  ASN A ND2 
298  N N   . SER A 45  ? 0.60136 0.62062 0.71156 -0.12876 -0.01230 -0.07660 52  SER A N   
299  C CA  . SER A 45  ? 0.54509 0.59389 0.69253 -0.10994 -0.00499 -0.07095 52  SER A CA  
300  C C   . SER A 45  ? 0.59784 0.58793 0.72204 -0.09587 -0.00997 -0.05980 52  SER A C   
301  O O   . SER A 45  ? 0.60625 0.61531 0.75014 -0.09664 -0.01677 -0.04718 52  SER A O   
302  C CB  . SER A 45  ? 0.51439 0.59372 0.70275 -0.08294 0.01351  -0.07784 52  SER A CB  
303  O OG  . SER A 45  ? 0.57603 0.70917 0.78998 -0.09432 0.01316  -0.08737 52  SER A OG  
304  N N   . SER A 46  ? 0.61071 0.52301 0.68560 -0.07904 -0.00844 -0.06497 53  SER A N   
305  C CA  . SER A 46  ? 0.66785 0.51070 0.70992 -0.05887 -0.01428 -0.05609 53  SER A CA  
306  C C   . SER A 46  ? 0.73854 0.55483 0.75836 -0.09627 -0.04481 -0.04194 53  SER A C   
307  O O   . SER A 46  ? 0.70583 0.49888 0.72485 -0.08737 -0.05188 -0.02771 53  SER A O   
308  C CB  . SER A 46  ? 0.80465 0.55571 0.77904 -0.02523 -0.00770 -0.06916 53  SER A CB  
309  O OG  . SER A 46  ? 1.00194 0.66146 0.92250 -0.01066 -0.02335 -0.06425 53  SER A OG  
310  N N   . ASP A 47  ? 0.76840 0.59379 0.77599 -0.13859 -0.06361 -0.03943 54  ASP A N   
311  C CA  . ASP A 47  ? 0.71628 0.53519 0.71598 -0.17886 -0.09195 -0.01458 54  ASP A CA  
312  C C   . ASP A 47  ? 0.65377 0.56228 0.70241 -0.18593 -0.08393 0.00167  54  ASP A C   
313  O O   . ASP A 47  ? 0.66655 0.56394 0.71078 -0.19799 -0.09885 0.02440  54  ASP A O   
314  C CB  . ASP A 47  ? 0.84291 0.66558 0.83063 -0.22293 -0.11376 -0.00610 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.95599 0.66286 0.87566 -0.22452 -0.13911 -0.01806 54  ASP A CG  
316  O OD1 . ASP A 47  ? 1.09837 0.71175 0.96913 -0.19029 -0.14108 -0.03044 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.94527 0.65175 0.85604 -0.25696 -0.15885 -0.01443 54  ASP A OD2 
318  N N   . ALA A 48  ? 0.62632 0.61624 0.71423 -0.17694 -0.06372 -0.00993 55  ALA A N   
319  C CA  . ALA A 48  ? 0.55997 0.62100 0.67688 -0.17682 -0.06005 -0.00050 55  ALA A CA  
320  C C   . ALA A 48  ? 0.59690 0.63940 0.72517 -0.15131 -0.06056 0.00281  55  ALA A C   
321  O O   . ALA A 48  ? 0.64678 0.71475 0.77830 -0.15733 -0.06989 0.01940  55  ALA A O   
322  C CB  . ALA A 48  ? 0.54155 0.67168 0.68566 -0.16771 -0.04477 -0.01855 55  ALA A CB  
323  N N   . LEU A 49  ? 0.55849 0.56271 0.69385 -0.12053 -0.04989 -0.00824 56  LEU A N   
324  C CA  . LEU A 49  ? 0.50792 0.50282 0.66467 -0.09421 -0.05000 0.00285  56  LEU A CA  
325  C C   . LEU A 49  ? 0.58025 0.50690 0.70184 -0.09507 -0.06473 0.02055  56  LEU A C   
326  O O   . LEU A 49  ? 0.56774 0.50029 0.70475 -0.08719 -0.07338 0.03822  56  LEU A O   
327  C CB  . LEU A 49  ? 0.58485 0.57565 0.76879 -0.05662 -0.02908 -0.00458 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.52227 0.57819 0.75270 -0.05499 -0.02001 -0.01518 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.48543 0.53196 0.73056 -0.02390 0.00425  -0.01808 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.48679 0.59218 0.76482 -0.05456 -0.03469 -0.00329 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.69227 0.54691 0.76404 -0.10546 -0.07326 0.01706  57  ASP A N   
332  C CA  . ASP A 50  ? 0.72886 0.50352 0.76019 -0.11081 -0.09596 0.03430  57  ASP A CA  
333  C C   . ASP A 50  ? 0.71771 0.53047 0.75752 -0.15054 -0.11638 0.06205  57  ASP A C   
334  O O   . ASP A 50  ? 0.79546 0.57245 0.82550 -0.14933 -0.13222 0.08344  57  ASP A O   
335  C CB  . ASP A 50  ? 0.75241 0.42993 0.72043 -0.11936 -0.11189 0.02366  57  ASP A CB  
336  C CG  . ASP A 50  ? 0.87027 0.47884 0.80355 -0.06565 -0.09360 0.00140  57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.94596 0.57618 0.90910 -0.02127 -0.07020 0.00466  57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.88608 0.42134 0.76119 -0.06613 -0.10331 -0.01592 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.68037 0.56848 0.73691 -0.18146 -0.11413 0.06525  58  LYS A N   
340  C CA  . LYS A 51  ? 0.72982 0.66583 0.79043 -0.21379 -0.12726 0.09721  58  LYS A CA  
341  C C   . LYS A 51  ? 0.71035 0.69378 0.79142 -0.19501 -0.12293 0.10396  58  LYS A C   
342  O O   . LYS A 51  ? 0.85017 0.82138 0.92213 -0.20391 -0.13882 0.13217  58  LYS A O   
343  C CB  . LYS A 51  ? 0.72197 0.73439 0.79396 -0.24065 -0.11965 0.10146  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.78043 0.75620 0.83617 -0.27848 -0.13921 0.11764  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.91313 0.98348 0.99073 -0.31188 -0.13696 0.15039  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.87841 0.99175 0.95924 -0.32448 -0.14204 0.19205  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.69047 0.91758 0.79264 -0.34158 -0.12753 0.22573  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.62752 0.66009 0.73490 -0.17106 -0.10697 0.08041  59  ILE A N   
349  C CA  . ILE A 52  ? 0.70746 0.78029 0.82950 -0.15725 -0.11248 0.08600  59  ILE A CA  
350  C C   . ILE A 52  ? 0.66658 0.69178 0.80023 -0.13670 -0.12280 0.09900  59  ILE A C   
351  O O   . ILE A 52  ? 0.65450 0.69375 0.78812 -0.13661 -0.13797 0.11889  59  ILE A O   
352  C CB  . ILE A 52  ? 0.63005 0.75201 0.77619 -0.14040 -0.10327 0.05866  59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.53501 0.69078 0.68192 -0.13193 -0.12003 0.06375  59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.51913 0.61532 0.69897 -0.11694 -0.09225 0.04197  59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.50183 0.68683 0.60698 -0.14717 -0.12683 0.08461  59  ILE A CD1 
356  N N   . ARG A 53  ? 0.64606 0.61533 0.78573 -0.11445 -0.11395 0.09008  60  ARG A N   
357  C CA  . ARG A 53  ? 0.63665 0.56083 0.78565 -0.08670 -0.11965 0.10626  60  ARG A CA  
358  C C   . ARG A 53  ? 0.75033 0.61451 0.86011 -0.10367 -0.14046 0.13095  60  ARG A C   
359  O O   . ARG A 53  ? 0.80456 0.65204 0.92201 -0.09001 -0.15283 0.15304  60  ARG A O   
360  C CB  . ARG A 53  ? 0.63591 0.51683 0.79100 -0.04829 -0.09891 0.09204  60  ARG A CB  
361  C CG  . ARG A 53  ? 0.67156 0.51884 0.84334 -0.00640 -0.09713 0.11132  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.78149 0.62618 0.97606 0.04118  -0.06719 0.10321  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.93730 0.68372 1.06538 0.06658  -0.05773 0.08946  60  ARG A NE  
364  C CZ  . ARG A 53  ? 1.00996 0.68156 1.10752 0.10828  -0.05687 0.10061  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.84331 0.53609 0.98101 0.12806  -0.06246 0.12992  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 1.05153 0.61842 1.07084 0.13339  -0.05328 0.08154  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.77273 0.60507 0.84512 -0.13600 -0.14865 0.13232  61  TYR A N   
368  C CA  . TYR A 54  ? 0.81374 0.58575 0.85284 -0.16019 -0.17558 0.16217  61  TYR A CA  
369  C C   . TYR A 54  ? 0.78250 0.62052 0.83101 -0.18624 -0.18688 0.19448  61  TYR A C   
370  O O   . TYR A 54  ? 0.83814 0.64088 0.87593 -0.19081 -0.20725 0.22456  61  TYR A O   
371  C CB  . TYR A 54  ? 0.83466 0.55606 0.83872 -0.19350 -0.18874 0.16089  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.91670 0.58202 0.89363 -0.23136 -0.22451 0.19954  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.90649 0.63039 0.89266 -0.28265 -0.23565 0.23176  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 1.01104 0.56657 0.95543 -0.21419 -0.24764 0.20876  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.98353 0.66346 0.95483 -0.32295 -0.27133 0.27691  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 1.09501 0.59105 1.01572 -0.25310 -0.28698 0.24771  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 1.07852 0.63982 1.01663 -0.31105 -0.29991 0.28405  61  TYR A CZ  
378  O OH  . TYR A 54  ? 1.16288 0.67389 1.08770 -0.35564 -0.34159 0.33263  61  TYR A OH  
379  N N   . GLU A 55  ? 0.78616 0.71647 0.84784 -0.19889 -0.17371 0.18925  62  GLU A N   
380  C CA  . GLU A 55  ? 0.77556 0.77007 0.83174 -0.21410 -0.18041 0.21812  62  GLU A CA  
381  C C   . GLU A 55  ? 0.80323 0.80774 0.87169 -0.18671 -0.18830 0.21995  62  GLU A C   
382  O O   . GLU A 55  ? 0.80615 0.82591 0.86011 -0.19554 -0.20332 0.25152  62  GLU A O   
383  C CB  . GLU A 55  ? 0.78568 0.86847 0.83993 -0.22264 -0.16206 0.20826  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.85061 0.93953 0.90450 -0.24976 -0.15458 0.21043  62  GLU A CG  
385  C CD  . GLU A 55  ? 1.12944 1.29864 1.17548 -0.27588 -0.14905 0.24817  62  GLU A CD  
386  O OE1 . GLU A 55  ? 1.08093 1.32604 1.12397 -0.26156 -0.12763 0.23450  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 1.46112 1.61777 1.50379 -0.30836 -0.16625 0.29485  62  GLU A OE2 
388  N N   . SER A 56  ? 0.76579 0.76616 0.86441 -0.15518 -0.18065 0.19221  63  SER A N   
389  C CA  . SER A 56  ? 0.71396 0.72897 0.83648 -0.13268 -0.19411 0.19973  63  SER A CA  
390  C C   . SER A 56  ? 0.78508 0.74034 0.91157 -0.12083 -0.20893 0.22808  63  SER A C   
391  O O   . SER A 56  ? 0.86845 0.83908 1.01264 -0.10835 -0.22594 0.24618  63  SER A O   
392  C CB  . SER A 56  ? 0.66181 0.69717 0.82942 -0.10652 -0.18422 0.17297  63  SER A CB  
393  O OG  . SER A 56  ? 0.64040 0.62650 0.82704 -0.08414 -0.16794 0.16610  63  SER A OG  
394  N N   . LEU A 57  ? 0.80522 0.68594 0.91155 -0.12321 -0.20727 0.23238  64  LEU A N   
395  C CA  . LEU A 57  ? 0.86253 0.67092 0.96243 -0.10691 -0.22340 0.25753  64  LEU A CA  
396  C C   . LEU A 57  ? 0.90558 0.72100 0.98550 -0.13402 -0.24881 0.29757  64  LEU A C   
397  O O   . LEU A 57  ? 0.95521 0.73340 1.04032 -0.11712 -0.26555 0.32246  64  LEU A O   
398  C CB  . LEU A 57  ? 0.92851 0.63616 0.99337 -0.10222 -0.22271 0.24775  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.90599 0.59074 0.98069 -0.06170 -0.19629 0.21329  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.98317 0.57157 1.00221 -0.06784 -0.20029 0.19642  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.97868 0.64765 1.08431 -0.00584 -0.18795 0.22212  64  LEU A CD2 
402  N N   . THR A 58  ? 0.84795 0.86535 0.79558 0.01011  -0.11289 0.38026  65  THR A N   
403  C CA  . THR A 58  ? 0.91081 0.88524 0.73691 0.00617  -0.11679 0.40891  65  THR A CA  
404  C C   . THR A 58  ? 0.94277 0.93786 0.70744 0.00257  -0.10150 0.37804  65  THR A C   
405  O O   . THR A 58  ? 1.05636 1.01647 0.70547 0.00183  -0.09849 0.39903  65  THR A O   
406  C CB  . THR A 58  ? 0.93118 0.86553 0.73718 -0.01758 -0.07149 0.43240  65  THR A CB  
407  O OG1 . THR A 58  ? 1.10227 1.08029 0.95527 -0.03939 -0.01534 0.42843  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.95316 0.85400 0.81228 -0.01122 -0.08433 0.41824  65  THR A CG2 
409  N N   . ASP A 59  ? 1.00211 1.04363 0.83137 0.00098  -0.09256 0.32939  66  ASP A N   
410  C CA  . ASP A 59  ? 0.98946 1.03926 0.75968 0.00028  -0.08517 0.29174  66  ASP A CA  
411  C C   . ASP A 59  ? 0.96217 1.05172 0.81855 -0.00093 -0.10509 0.23943  66  ASP A C   
412  O O   . ASP A 59  ? 0.95627 1.06175 0.87171 -0.01265 -0.06668 0.21823  66  ASP A O   
413  C CB  . ASP A 59  ? 1.05562 1.10406 0.79270 -0.01267 -0.01651 0.29820  66  ASP A CB  
414  C CG  . ASP A 59  ? 1.16240 1.19787 0.78944 -0.00392 -0.00913 0.26912  66  ASP A CG  
415  O OD1 . ASP A 59  ? 1.18310 1.21728 0.79404 0.00521  -0.05504 0.22653  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 1.19161 1.21998 0.74832 -0.00593 0.04253  0.28820  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.94692 1.05392 0.81576 0.00979  -0.16569 0.21917  67  PRO A N   
418  C CA  . PRO A 60  ? 0.86316 1.01374 0.82403 -0.00057 -0.18385 0.17335  67  PRO A CA  
419  C C   . PRO A 60  ? 0.83836 0.97411 0.75912 -0.01410 -0.16985 0.13007  67  PRO A C   
420  O O   . PRO A 60  ? 0.78797 0.94525 0.78569 -0.03108 -0.17318 0.09563  67  PRO A O   
421  C CB  . PRO A 60  ? 0.80373 0.98377 0.77663 0.01503  -0.25590 0.16490  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.84919 0.99784 0.76457 0.03934  -0.27069 0.21221  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.90542 0.99675 0.71705 0.03175  -0.22211 0.24020  67  PRO A CD  
424  N N   . SER A 61  ? 0.91979 1.01394 0.71655 -0.00613 -0.15333 0.13119  68  SER A N   
425  C CA  . SER A 61  ? 0.98197 1.05153 0.72560 -0.01018 -0.13956 0.08620  68  SER A CA  
426  C C   . SER A 61  ? 0.90890 0.97903 0.71230 -0.01930 -0.07830 0.07823  68  SER A C   
427  O O   . SER A 61  ? 1.04069 1.08694 0.82462 -0.02185 -0.07129 0.03499  68  SER A O   
428  C CB  . SER A 61  ? 1.12287 1.14911 0.70691 0.00861  -0.13083 0.09155  68  SER A CB  
429  O OG  . SER A 61  ? 1.12393 1.14584 0.67992 0.01208  -0.06230 0.13126  68  SER A OG  
430  N N   . LYS A 62  ? 0.84742 0.93688 0.71783 -0.02167 -0.03934 0.11712  69  LYS A N   
431  C CA  . LYS A 62  ? 0.74746 0.83961 0.68053 -0.02632 0.01127  0.11004  69  LYS A CA  
432  C C   . LYS A 62  ? 0.76027 0.85854 0.78729 -0.04158 -0.00585 0.07902  69  LYS A C   
433  O O   . LYS A 62  ? 0.82504 0.90764 0.88235 -0.04321 0.02669  0.06126  69  LYS A O   
434  C CB  . LYS A 62  ? 0.67358 0.78349 0.65569 -0.02645 0.04641  0.15878  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.78504 0.88884 0.68455 -0.02127 0.06781  0.19852  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.68120 0.80252 0.63446 -0.02768 0.11492  0.23519  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.76310 0.88440 0.63655 -0.03023 0.14896  0.27341  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.87298 1.02743 0.77296 -0.02929 0.21220  0.27470  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.69135 0.81369 0.76574 -0.05202 -0.05503 0.07399  70  LEU A N   
440  C CA  . LEU A 63  ? 0.61549 0.75206 0.78264 -0.07325 -0.06931 0.04959  70  LEU A CA  
441  C C   . LEU A 63  ? 0.69982 0.81415 0.83599 -0.08987 -0.10636 0.00049  70  LEU A C   
442  O O   . LEU A 63  ? 0.73158 0.86046 0.94623 -0.11633 -0.12613 -0.01866 70  LEU A O   
443  C CB  . LEU A 63  ? 0.54753 0.73822 0.80078 -0.07531 -0.09710 0.07195  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.49225 0.69426 0.79641 -0.06256 -0.06465 0.11212  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.46197 0.71616 0.85511 -0.06057 -0.08863 0.12284  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.53055 0.70411 0.86066 -0.06782 -0.01510 0.10929  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.80784 0.88449 0.82820 -0.07638 -0.11658 -0.01974 71  ASP A N   
448  C CA  . ASP A 64  ? 0.90713 0.94662 0.88343 -0.08997 -0.15722 -0.07196 71  ASP A CA  
449  C C   . ASP A 64  ? 0.90875 0.90002 0.91045 -0.10433 -0.13097 -0.10219 71  ASP A C   
450  O O   . ASP A 64  ? 0.96664 0.92785 0.97816 -0.13034 -0.16934 -0.14238 71  ASP A O   
451  C CB  . ASP A 64  ? 1.03821 1.03674 0.86382 -0.06376 -0.16832 -0.08723 71  ASP A CB  
452  C CG  . ASP A 64  ? 1.06892 1.09775 0.85306 -0.05110 -0.20921 -0.06192 71  ASP A CG  
453  O OD1 . ASP A 64  ? 1.00705 1.08894 0.88269 -0.06383 -0.24770 -0.04921 71  ASP A OD1 
454  O OD2 . ASP A 64  ? 1.16405 1.16273 0.82034 -0.02548 -0.20169 -0.05383 71  ASP A OD2 
455  N N   . SER A 65  ? 0.85533 0.83443 0.86813 -0.08844 -0.07062 -0.08349 72  SER A N   
456  C CA  . SER A 65  ? 0.85748 0.78508 0.89361 -0.09482 -0.04515 -0.10703 72  SER A CA  
457  C C   . SER A 65  ? 0.76419 0.71293 0.92271 -0.12523 -0.04344 -0.09079 72  SER A C   
458  O O   . SER A 65  ? 0.78234 0.68640 0.96356 -0.12777 -0.01611 -0.09794 72  SER A O   
459  C CB  . SER A 65  ? 0.84841 0.76113 0.84615 -0.05880 0.01576  -0.09526 72  SER A CB  
460  O OG  . SER A 65  ? 0.79883 0.77076 0.83072 -0.04811 0.04279  -0.04497 72  SER A OG  
461  N N   . GLY A 66  ? 0.70476 0.71901 0.93668 -0.14385 -0.07059 -0.06874 73  GLY A N   
462  C CA  . GLY A 66  ? 0.62458 0.66902 0.96855 -0.16934 -0.06283 -0.05058 73  GLY A CA  
463  C C   . GLY A 66  ? 0.54400 0.66649 0.95037 -0.15875 -0.06230 -0.00939 73  GLY A C   
464  O O   . GLY A 66  ? 0.58947 0.71904 0.97163 -0.12909 -0.03643 0.01973  73  GLY A O   
465  N N   . LYS A 67  ? 0.64357 0.82575 1.13299 -0.18242 -0.09194 -0.00729 74  LYS A N   
466  C CA  . LYS A 67  ? 0.55133 0.80694 1.10044 -0.16526 -0.09421 0.02715  74  LYS A CA  
467  C C   . LYS A 67  ? 0.55512 0.82660 1.18313 -0.16820 -0.05395 0.05215  74  LYS A C   
468  O O   . LYS A 67  ? 0.50384 0.80519 1.15118 -0.13993 -0.04084 0.08279  74  LYS A O   
469  C CB  . LYS A 67  ? 0.59837 0.92706 1.19746 -0.17850 -0.14988 0.01549  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.55847 0.89867 1.08588 -0.14821 -0.18927 0.01855  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.76902 1.12364 1.28092 -0.16755 -0.25238 -0.01859 74  LYS A CD  
472  C CE  . LYS A 67  ? 0.85167 1.16623 1.23388 -0.13786 -0.28011 -0.02260 74  LYS A CE  
473  N NZ  . LYS A 67  ? 1.03032 1.32625 1.36476 -0.15590 -0.33825 -0.06754 74  LYS A NZ  
474  N N   . GLU A 68  ? 0.45650 0.69714 1.11586 -0.19938 -0.03564 0.03985  75  GLU A N   
475  C CA  . GLU A 68  ? 0.40551 0.62853 1.04526 -0.18174 0.00399  0.05721  75  GLU A CA  
476  C C   . GLU A 68  ? 0.44001 0.60720 1.02611 -0.14587 0.03684  0.07338  75  GLU A C   
477  O O   . GLU A 68  ? 0.38858 0.50732 0.95250 -0.14834 0.04749  0.06467  75  GLU A O   
478  C CB  . GLU A 68  ? 0.43114 0.62067 1.07548 -0.21829 0.01133  0.04258  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.55032 0.75283 1.22922 -0.26617 -0.02953 0.01266  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.76896 0.92891 1.44519 -0.30646 -0.02181 0.00370  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.75544 0.96563 1.46407 -0.31927 -0.01065 0.01748  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.80079 0.87259 1.43998 -0.32542 -0.02684 -0.01781 75  GLU A OE2 
483  N N   . LEU A 69  ? 0.39404 0.56565 0.96141 -0.11228 0.04991  0.09302  76  LEU A N   
484  C CA  . LEU A 69  ? 0.38884 0.51045 0.90803 -0.07734 0.06918  0.10506  76  LEU A CA  
485  C C   . LEU A 69  ? 0.42403 0.52086 0.93269 -0.06676 0.08523  0.10870  76  LEU A C   
486  O O   . LEU A 69  ? 0.39384 0.51237 0.91258 -0.05389 0.08501  0.12049  76  LEU A O   
487  C CB  . LEU A 69  ? 0.30648 0.44265 0.81300 -0.04947 0.05915  0.12468  76  LEU A CB  
488  C CG  . LEU A 69  ? 0.23282 0.41072 0.75912 -0.06030 0.03947  0.12943  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.25825 0.44175 0.76869 -0.03372 0.02910  0.15601  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.30003 0.45731 0.81700 -0.07570 0.05146  0.12092  76  LEU A CD2 
491  N N   . HIS A 70  ? 0.63757 0.63619 0.55160 0.17749  -0.02676 -0.06299 77  HIS A N   
492  C CA  . HIS A 70  ? 0.63564 0.64861 0.55265 0.16053  -0.03329 -0.05777 77  HIS A CA  
493  C C   . HIS A 70  ? 0.63030 0.61212 0.55750 0.13387  -0.04812 -0.06497 77  HIS A C   
494  O O   . HIS A 70  ? 0.62707 0.58288 0.56367 0.12768  -0.05384 -0.07227 77  HIS A O   
495  C CB  . HIS A 70  ? 0.57449 0.65204 0.52019 0.15249  -0.04213 -0.04394 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.48783 0.58087 0.46515 0.13519  -0.06081 -0.04725 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.57017 0.62387 0.55463 0.11829  -0.07332 -0.05686 77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.52778 0.67077 0.52793 0.13332  -0.06982 -0.04330 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.57320 0.64276 0.57727 0.10877  -0.08797 -0.05986 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.46981 0.59355 0.48454 0.11501  -0.08805 -0.05356 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.64873 0.63799 0.57273 0.12214  -0.05268 -0.06012 78  ILE A N   
502  C CA  . ILE A 71  ? 0.62911 0.60120 0.56195 0.10055  -0.06679 -0.06271 78  ILE A CA  
503  C C   . ILE A 71  ? 0.65356 0.66001 0.60559 0.08709  -0.07436 -0.04748 78  ILE A C   
504  O O   . ILE A 71  ? 0.65387 0.68947 0.59898 0.09445  -0.06599 -0.03608 78  ILE A O   
505  C CB  . ILE A 71  ? 0.61927 0.56007 0.52171 0.10129  -0.06437 -0.07285 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.64115 0.54081 0.52706 0.10956  -0.05474 -0.08715 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.63068 0.56766 0.54427 0.08204  -0.08044 -0.07296 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.61188 0.47564 0.46101 0.10953  -0.05125 -0.10096 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.59047 0.59114 0.56504 0.06931  -0.08747 -0.04505 79  ASN A N   
510  C CA  . ASN A 72  ? 0.61229 0.63382 0.60573 0.05360  -0.09280 -0.02957 79  ASN A CA  
511  C C   . ASN A 72  ? 0.61514 0.61592 0.60396 0.04543  -0.09940 -0.02589 79  ASN A C   
512  O O   . ASN A 72  ? 0.64730 0.62182 0.63566 0.04437  -0.10632 -0.03452 79  ASN A O   
513  C CB  . ASN A 72  ? 0.56139 0.58959 0.58119 0.04063  -0.10161 -0.02917 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.60451 0.67344 0.63440 0.04698  -0.09747 -0.02769 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.62532 0.72304 0.64594 0.06094  -0.08510 -0.02015 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.49109 0.56476 0.53688 0.03962  -0.10804 -0.03471 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.58014 0.59789 0.56580 0.04286  -0.09569 -0.01019 80  LEU A N   
518  C CA  . LEU A 73  ? 0.58515 0.59116 0.56434 0.03960  -0.10034 -0.00199 80  LEU A CA  
519  C C   . LEU A 73  ? 0.64386 0.65202 0.64449 0.02488  -0.09926 0.01764  80  LEU A C   
520  O O   . LEU A 73  ? 0.68746 0.72242 0.69770 0.02058  -0.09031 0.03397  80  LEU A O   
521  C CB  . LEU A 73  ? 0.61492 0.63372 0.56463 0.05302  -0.09535 0.00096  80  LEU A CB  
522  C CG  . LEU A 73  ? 0.61260 0.62386 0.53466 0.06612  -0.09287 -0.01870 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.71251 0.73087 0.59718 0.08023  -0.08972 -0.01762 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.60214 0.58550 0.52583 0.06107  -0.10280 -0.03828 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.71088 0.68912 0.71822 0.01777  -0.10645 0.01762  81  ILE A N   
526  C CA  . ILE A 74  ? 0.65850 0.62063 0.68170 0.00170  -0.10524 0.03251  81  ILE A CA  
527  C C   . ILE A 74  ? 0.67300 0.61413 0.68266 0.00868  -0.10312 0.04724  81  ILE A C   
528  O O   . ILE A 74  ? 0.70269 0.61616 0.70544 0.01511  -0.10909 0.04181  81  ILE A O   
529  C CB  . ILE A 74  ? 0.53314 0.46851 0.56800 -0.00906 -0.11431 0.01840  81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.56527 0.52841 0.60943 -0.00877 -0.11682 0.00374  81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.61303 0.52380 0.66080 -0.03063 -0.11388 0.03034  81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.64836 0.58800 0.69296 -0.00814 -0.12675 -0.01472 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.68143 0.63850 0.68558 0.01185  -0.09283 0.06886  82  PRO A N   
534  C CA  . PRO A 75  ? 0.63469 0.57301 0.62457 0.02183  -0.08830 0.08741  82  PRO A CA  
535  C C   . PRO A 75  ? 0.72922 0.62621 0.73037 0.00599  -0.08124 0.10297  82  PRO A C   
536  O O   . PRO A 75  ? 0.72405 0.62010 0.74736 -0.01695 -0.07735 0.10703  82  PRO A O   
537  C CB  . PRO A 75  ? 0.69909 0.67264 0.67452 0.03498  -0.07809 0.10490  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.76307 0.76360 0.75618 0.02307  -0.07104 0.10667  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.71610 0.71311 0.72243 0.01316  -0.08263 0.07960  82  PRO A CD  
540  N N   . ASN A 76  ? 0.79342 0.65574 0.77824 0.01841  -0.07955 0.11198  83  ASN A N   
541  C CA  . ASN A 76  ? 0.76888 0.57511 0.75331 0.00744  -0.07064 0.12646  83  ASN A CA  
542  C C   . ASN A 76  ? 0.85016 0.64412 0.81104 0.03112  -0.05702 0.15458  83  ASN A C   
543  O O   . ASN A 76  ? 0.93839 0.73312 0.88046 0.05625  -0.06172 0.15348  83  ASN A O   
544  C CB  . ASN A 76  ? 0.77386 0.53422 0.75373 0.00461  -0.08120 0.10604  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.85187 0.54518 0.82933 -0.01486 -0.07476 0.11246  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.94753 0.60762 0.91328 -0.01200 -0.05876 0.13794  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.94120 0.61090 0.92642 -0.03425 -0.08704 0.08880  83  ASN A ND2 
548  N N   . LYS A 77  ? 0.86697 0.65451 0.83053 0.02466  -0.03893 0.18243  84  LYS A N   
549  C CA  . LYS A 77  ? 0.87722 0.65514 0.81522 0.05179  -0.02250 0.21342  84  LYS A CA  
550  C C   . LYS A 77  ? 0.97368 0.67681 0.89311 0.05782  -0.01296 0.22449  84  LYS A C   
551  O O   . LYS A 77  ? 1.05804 0.75520 0.94960 0.09133  -0.00444 0.24358  84  LYS A O   
552  C CB  . LYS A 77  ? 0.82595 0.62244 0.77166 0.04663  -0.00203 0.24371  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.77966 0.64925 0.72273 0.06096  -0.00595 0.24155  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.91357 0.80198 0.83534 0.08741  0.01531  0.27840  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.86956 0.81802 0.79339 0.09253  0.01885  0.28181  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.89657 0.84990 0.86086 0.05788  0.02711  0.28598  84  LYS A NZ  
557  N N   . GLN A 78  ? 1.03638 0.68197 0.96672 0.02831  -0.01448 0.21252  85  GLN A N   
558  C CA  . GLN A 78  ? 1.06037 0.62108 0.96395 0.03532  -0.00468 0.21989  85  GLN A CA  
559  C C   . GLN A 78  ? 1.06544 0.62442 0.94579 0.06763  -0.01596 0.20588  85  GLN A C   
560  O O   . GLN A 78  ? 1.20042 0.73293 1.04980 0.10149  -0.00334 0.22650  85  GLN A O   
561  C CB  . GLN A 78  ? 1.16619 0.66527 1.08352 -0.00709 -0.00822 0.20402  85  GLN A CB  
562  C CG  . GLN A 78  ? 1.30437 0.75624 1.22912 -0.03294 0.01409  0.23153  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.54907 0.92785 1.43194 -0.00437 0.03960  0.26188  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.57665 0.98207 1.44901 0.02374  0.05865  0.29491  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 1.62188 0.90594 1.47515 -0.00743 0.04102  0.25120  85  GLN A NE2 
566  N N   . ASP A 79  ? 1.05368 0.64409 0.94946 0.06004  -0.03754 0.17411  86  ASP A N   
567  C CA  . ASP A 79  ? 1.05676 0.65560 0.93849 0.08855  -0.04718 0.16293  86  ASP A CA  
568  C C   . ASP A 79  ? 0.94708 0.62489 0.83272 0.11343  -0.05318 0.16928  86  ASP A C   
569  O O   . ASP A 79  ? 0.94284 0.63887 0.82241 0.13719  -0.05988 0.16577  86  ASP A O   
570  C CB  . ASP A 79  ? 1.10080 0.69820 0.99666 0.07155  -0.06516 0.12874  86  ASP A CB  
571  C CG  . ASP A 79  ? 1.19379 0.72112 1.08586 0.04301  -0.06542 0.11635  86  ASP A CG  
572  O OD1 . ASP A 79  ? 1.22728 0.70788 1.11242 0.02882  -0.05155 0.13366  86  ASP A OD1 
573  O OD2 . ASP A 79  ? 1.38462 0.90354 1.28008 0.03415  -0.07967 0.08926  86  ASP A OD2 
574  N N   . ARG A 80  ? 0.90448 0.63032 0.79936 0.10848  -0.05125 0.17860  87  ARG A N   
575  C CA  . ARG A 80  ? 0.81266 0.61209 0.70699 0.12783  -0.06075 0.17918  87  ARG A CA  
576  C C   . ARG A 80  ? 0.83908 0.67474 0.75103 0.12119  -0.08144 0.14845  87  ARG A C   
577  O O   . ARG A 80  ? 0.83090 0.70214 0.74169 0.13972  -0.09083 0.14651  87  ARG A O   
578  C CB  . ARG A 80  ? 0.81733 0.62530 0.68667 0.16591  -0.05266 0.20583  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.82149 0.70547 0.68496 0.18406  -0.06112 0.21164  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.86635 0.75716 0.70167 0.22306  -0.04768 0.24621  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.92613 0.83493 0.75870 0.24800  -0.05488 0.24870  87  ARG A NE  
582  C CZ  . ARG A 80  ? 1.02999 0.94317 0.83821 0.28752  -0.04258 0.27963  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.98441 0.87963 0.76572 0.30776  -0.02145 0.31092  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 1.04725 0.98627 0.85836 0.31010  -0.04940 0.28240  87  ARG A NH2 
585  N N   . THR A 81  ? 0.82468 0.65350 0.75500 0.09437  -0.08750 0.12624  88  THR A N   
586  C CA  . THR A 81  ? 0.74610 0.60011 0.69171 0.08768  -0.10261 0.09891  88  THR A CA  
587  C C   . THR A 81  ? 0.74061 0.62554 0.69747 0.06985  -0.10685 0.08439  88  THR A C   
588  O O   . THR A 81  ? 0.77211 0.64761 0.73407 0.05502  -0.09894 0.09038  88  THR A O   
589  C CB  . THR A 81  ? 0.76512 0.57418 0.71525 0.08142  -0.10436 0.08515  88  THR A CB  
590  O OG1 . THR A 81  ? 0.87791 0.65670 0.83455 0.05719  -0.10126 0.07948  88  THR A OG1 
591  C CG2 . THR A 81  ? 0.84365 0.61233 0.77454 0.10395  -0.09677 0.10082  88  THR A CG2 
592  N N   . LEU A 82  ? 0.68356 0.60486 0.64418 0.07161  -0.11806 0.06671  89  LEU A N   
593  C CA  . LEU A 82  ? 0.62922 0.57092 0.59430 0.05960  -0.12081 0.04971  89  LEU A CA  
594  C C   . LEU A 82  ? 0.61805 0.55146 0.59637 0.05331  -0.12716 0.02748  89  LEU A C   
595  O O   . LEU A 82  ? 0.62350 0.56494 0.60558 0.05978  -0.13416 0.02059  89  LEU A O   
596  C CB  . LEU A 82  ? 0.67366 0.65409 0.62234 0.06810  -0.12648 0.04649  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.56678 0.56013 0.50986 0.06142  -0.12700 0.02852  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.59383 0.58315 0.54256 0.05451  -0.11388 0.03904  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.68027 0.70175 0.59693 0.07139  -0.13416 0.02238  89  LEU A CD2 
600  N N   . THR A 83  ? 0.61924 0.54170 0.60638 0.04178  -0.12391 0.01870  90  THR A N   
601  C CA  . THR A 83  ? 0.66572 0.57744 0.66220 0.04002  -0.12710 0.00082  90  THR A CA  
602  C C   . THR A 83  ? 0.63506 0.56691 0.63004 0.03791  -0.12555 -0.01336 90  THR A C   
603  O O   . THR A 83  ? 0.57170 0.51875 0.56416 0.03384  -0.12025 -0.00918 90  THR A O   
604  C CB  . THR A 83  ? 0.64017 0.52245 0.64321 0.03233  -0.12615 0.00039  90  THR A CB  
605  O OG1 . THR A 83  ? 0.66010 0.51118 0.65597 0.03622  -0.12471 0.01403  90  THR A OG1 
606  C CG2 . THR A 83  ? 0.64777 0.52005 0.65467 0.03754  -0.12923 -0.01651 90  THR A CG2 
607  N N   . ILE A 84  ? 0.68261 0.61325 0.67854 0.04234  -0.12763 -0.02757 91  ILE A N   
608  C CA  . ILE A 84  ? 0.66909 0.60543 0.65832 0.04377  -0.12288 -0.04149 91  ILE A CA  
609  C C   . ILE A 84  ? 0.67000 0.59173 0.66858 0.04819  -0.11946 -0.04973 91  ILE A C   
610  O O   . ILE A 84  ? 0.76139 0.67092 0.76751 0.05245  -0.12074 -0.05221 91  ILE A O   
611  C CB  . ILE A 84  ? 0.62227 0.56280 0.60047 0.04384  -0.12630 -0.05171 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.70170 0.65986 0.66072 0.04418  -0.12988 -0.04673 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.66070 0.58893 0.62931 0.04697  -0.11811 -0.06698 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.78380 0.75545 0.74604 0.04409  -0.14032 -0.03763 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.55330 0.48211 0.55174 0.04968  -0.11457 -0.05185 92  VAL A N   
616  C CA  . VAL A 85  ? 0.59873 0.51999 0.60179 0.05771  -0.11216 -0.05920 92  VAL A CA  
617  C C   . VAL A 85  ? 0.69789 0.62627 0.68962 0.06933  -0.10092 -0.06661 92  VAL A C   
618  O O   . VAL A 85  ? 0.76096 0.70922 0.74471 0.07067  -0.09580 -0.06366 92  VAL A O   
619  C CB  . VAL A 85  ? 0.57648 0.50418 0.58873 0.05042  -0.11824 -0.05607 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.46048 0.38661 0.47203 0.06220  -0.11816 -0.06595 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.66505 0.57025 0.68077 0.04104  -0.12609 -0.04891 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.64629 0.55684 0.63539 0.08071  -0.09418 -0.07349 93  ASP A N   
623  C CA  . ASP A 86  ? 0.62620 0.53327 0.60056 0.09622  -0.07954 -0.07885 93  ASP A CA  
624  C C   . ASP A 86  ? 0.70553 0.60779 0.68258 0.11319  -0.07433 -0.08024 93  ASP A C   
625  O O   . ASP A 86  ? 0.61221 0.50378 0.59936 0.11336  -0.08031 -0.07937 93  ASP A O   
626  C CB  . ASP A 86  ? 0.63310 0.51447 0.59528 0.09389  -0.07184 -0.08544 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.71444 0.57517 0.69080 0.09245  -0.07001 -0.08618 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.67780 0.52411 0.65184 0.10814  -0.05632 -0.08607 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.83283 0.69612 0.82332 0.07805  -0.08074 -0.08410 93  ASP A OD2 
630  N N   . THR A 87  ? 0.69105 0.60242 0.65478 0.13223  -0.06183 -0.08097 94  THR A N   
631  C CA  . THR A 87  ? 0.68570 0.59750 0.64584 0.15500  -0.05495 -0.08132 94  THR A CA  
632  C C   . THR A 87  ? 0.71608 0.59475 0.66239 0.17253  -0.03301 -0.08085 94  THR A C   
633  O O   . THR A 87  ? 0.70560 0.58663 0.63660 0.19934  -0.01769 -0.07818 94  THR A O   
634  C CB  . THR A 87  ? 0.67277 0.62647 0.62917 0.16774  -0.05613 -0.07951 94  THR A CB  
635  O OG1 . THR A 87  ? 0.62437 0.59164 0.56949 0.17043  -0.04595 -0.07529 94  THR A OG1 
636  C CG2 . THR A 87  ? 0.48567 0.46642 0.46099 0.14812  -0.07888 -0.08095 94  THR A CG2 
637  N N   . GLY A 88  ? 0.72030 0.56927 0.67268 0.15741  -0.03064 -0.08219 95  GLY A N   
638  C CA  . GLY A 88  ? 0.74305 0.55522 0.68702 0.16551  -0.00970 -0.08156 95  GLY A CA  
639  C C   . GLY A 88  ? 0.78156 0.58442 0.73422 0.18386  0.00081  -0.07360 95  GLY A C   
640  O O   . GLY A 88  ? 0.79524 0.61919 0.74889 0.19973  -0.00597 -0.07108 95  GLY A O   
641  N N   . ILE A 89  ? 0.79246 0.56201 0.75052 0.18095  0.01775  -0.06963 96  ILE A N   
642  C CA  . ILE A 89  ? 0.77548 0.54309 0.74595 0.19487  0.03363  -0.05590 96  ILE A CA  
643  C C   . ILE A 89  ? 0.68957 0.47478 0.68152 0.19366  0.01956  -0.05028 96  ILE A C   
644  O O   . ILE A 89  ? 0.76289 0.56571 0.76158 0.20282  0.02676  -0.03889 96  ILE A O   
645  C CB  . ILE A 89  ? 0.78014 0.50528 0.75527 0.18869  0.05626  -0.05149 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.74751 0.48383 0.73340 0.20074  0.07266  -0.03410 96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.77968 0.49800 0.78224 0.15512  0.04420  -0.05486 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.81930 0.51570 0.79596 0.19994  0.09891  -0.02773 96  ILE A CD1 
649  N N   . GLY A 90  ? 0.65583 0.44945 0.66106 0.17237  -0.00189 -0.05586 97  GLY A N   
650  C CA  . GLY A 90  ? 0.64779 0.45510 0.67013 0.17300  -0.01301 -0.04821 97  GLY A CA  
651  C C   . GLY A 90  ? 0.60669 0.41143 0.65863 0.16403  -0.00303 -0.03501 97  GLY A C   
652  O O   . GLY A 90  ? 0.68969 0.47936 0.75227 0.15017  0.01020  -0.03401 97  GLY A O   
653  N N   . MET A 91  ? 0.58234 0.40167 0.64771 0.17194  -0.00893 -0.02389 98  MET A N   
654  C CA  . MET A 91  ? 0.59960 0.43164 0.69992 0.16465  -0.00089 -0.00674 98  MET A CA  
655  C C   . MET A 91  ? 0.60890 0.44451 0.70832 0.19940  0.01006  0.01102  98  MET A C   
656  O O   . MET A 91  ? 0.66103 0.49908 0.73773 0.21057  -0.00060 0.00620  98  MET A O   
657  C CB  . MET A 91  ? 0.66586 0.52439 0.78698 0.13651  -0.02170 -0.00773 98  MET A CB  
658  C CG  . MET A 91  ? 0.65586 0.51323 0.78298 0.10165  -0.02952 -0.02204 98  MET A CG  
659  S SD  . MET A 91  ? 0.60922 0.50500 0.75397 0.07513  -0.05608 -0.02330 98  MET A SD  
660  C CE  . MET A 91  ? 0.74352 0.62459 0.84959 0.06783  -0.07051 -0.04459 98  MET A CE  
661  N N   . THR A 92  ? 0.63001 0.47107 0.75644 0.20618  0.03177  0.03134  99  THR A N   
662  C CA  . THR A 92  ? 0.62669 0.48418 0.74797 0.22644  0.03954  0.04647  99  THR A CA  
663  C C   . THR A 92  ? 0.72752 0.61324 0.88136 0.23014  0.03738  0.06731  99  THR A C   
664  O O   . THR A 92  ? 0.79208 0.69819 0.97709 0.20319  0.02521  0.06753  99  THR A O   
665  C CB  . THR A 92  ? 0.63241 0.48582 0.75953 0.23228  0.06656  0.06035  99  THR A CB  
666  O OG1 . THR A 92  ? 0.67757 0.53436 0.86540 0.22288  0.08684  0.08364  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.55546 0.38606 0.65450 0.22918  0.07024  0.04389  99  THR A CG2 
668  N N   . LYS A 93  ? 0.64294 0.54265 0.78125 0.24461  0.04143  0.07684  100 LYS A N   
669  C CA  . LYS A 93  ? 0.67327 0.60501 0.83597 0.25181  0.04173  0.09869  100 LYS A CA  
670  C C   . LYS A 93  ? 0.70031 0.66957 0.93779 0.24562  0.06034  0.13083  100 LYS A C   
671  O O   . LYS A 93  ? 0.70444 0.71704 0.98105 0.23187  0.04979  0.14368  100 LYS A O   
672  C CB  . LYS A 93  ? 0.70858 0.64066 0.83703 0.26932  0.04805  0.10292  100 LYS A CB  
673  C CG  . LYS A 93  ? 0.69686 0.64366 0.82041 0.27787  0.03999  0.11169  100 LYS A CG  
674  C CD  . LYS A 93  ? 0.79862 0.73733 0.88409 0.29687  0.05036  0.11573  100 LYS A CD  
675  C CE  . LYS A 93  ? 0.79178 0.76986 0.90206 0.31238  0.07049  0.14903  100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.78020 0.74754 0.84703 0.33481  0.08370  0.15417  100 LYS A NZ  
677  N N   . ALA A 94  ? 0.61924 0.57809 0.87665 0.24310  0.08411  0.14000  101 ALA A N   
678  C CA  . ALA A 94  ? 0.62191 0.61492 0.94745 0.21052  0.09526  0.15925  101 ALA A CA  
679  C C   . ALA A 94  ? 0.69200 0.68810 1.03125 0.15610  0.06923  0.13263  101 ALA A C   
680  O O   . ALA A 94  ? 0.77113 0.81357 1.16068 0.12120  0.05992  0.14068  101 ALA A O   
681  C CB  . ALA A 94  ? 0.58223 0.54950 0.91823 0.21877  0.12951  0.17378  101 ALA A CB  
682  N N   . ASP A 95  ? 0.60103 0.55265 0.89515 0.14983  0.05667  0.10129  102 ASP A N   
683  C CA  . ASP A 95  ? 0.64674 0.59708 0.94283 0.10536  0.03264  0.07533  102 ASP A CA  
684  C C   . ASP A 95  ? 0.68626 0.68000 0.98920 0.09663  0.00469  0.07357  102 ASP A C   
685  O O   . ASP A 95  ? 0.72315 0.74865 1.05475 0.05945  -0.01267 0.06752  102 ASP A O   
686  C CB  . ASP A 95  ? 0.65165 0.55006 0.89562 0.10941  0.02917  0.04757  102 ASP A CB  
687  C CG  . ASP A 95  ? 0.77968 0.63489 1.01218 0.12102  0.05810  0.05006  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.82899 0.68564 1.09836 0.10855  0.07844  0.06727  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.79533 0.61750 0.98335 0.14289  0.06161  0.03672  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.68226 0.67515 0.95555 0.13153  0.00010  0.07832  103 LEU A N   
691  C CA  . LEU A 96  ? 0.68788 0.71295 0.96008 0.12925  -0.02228 0.07919  103 LEU A CA  
692  C C   . LEU A 96  ? 0.67593 0.76638 0.99939 0.12679  -0.02083 0.10780  103 LEU A C   
693  O O   . LEU A 96  ? 0.80022 0.93417 1.14327 0.10488  -0.04112 0.10687  103 LEU A O   
694  C CB  . LEU A 96  ? 0.64664 0.64192 0.87082 0.16679  -0.02422 0.07743  103 LEU A CB  
695  C CG  . LEU A 96  ? 0.60042 0.54879 0.77930 0.16322  -0.03406 0.04915  103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.73963 0.65746 0.87598 0.19664  -0.03556 0.04790  103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.59002 0.54922 0.76861 0.12996  -0.05580 0.03232  103 LEU A CD2 
698  N N   . ILE A 97  ? 0.63651 0.74086 0.98262 0.15143  0.00353  0.13546  104 ILE A N   
699  C CA  . ILE A 97  ? 0.70560 0.88142 1.10447 0.15473  0.00863  0.16889  104 ILE A CA  
700  C C   . ILE A 97  ? 0.71232 0.92843 1.17346 0.10397  0.00601  0.17043  104 ILE A C   
701  O O   . ILE A 97  ? 0.73831 1.00619 1.22931 0.07180  -0.01738 0.16642  104 ILE A O   
702  C CB  . ILE A 97  ? 0.71672 0.89319 1.11400 0.20478  0.03858  0.20105  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.66947 0.80691 1.00248 0.25296  0.03665  0.19784  104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.50753 0.76754 0.97053 0.20553  0.04867  0.24068  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.64366 0.73977 0.92055 0.27759  0.05831  0.19502  104 ILE A CD1 
706  N N   . ASN A 98  ? 0.74854 0.93931 1.22751 0.09643  0.02993  0.17593  105 ASN A N   
707  C CA  . ASN A 98  ? 0.58715 0.80328 1.12473 0.04500  0.03098  0.17738  105 ASN A CA  
708  C C   . ASN A 98  ? 0.62211 0.76760 1.12858 0.01328  0.02636  0.14042  105 ASN A C   
709  O O   . ASN A 98  ? 0.77976 0.89144 1.23595 0.01368  0.00660  0.11070  105 ASN A O   
710  C CB  . ASN A 98  ? 0.61002 0.84766 1.19532 0.05762  0.06636  0.21601  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.78816 1.12090 1.45570 0.02887  0.06205  0.24488  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.89298 1.26951 1.58618 -0.01358 0.03089  0.22947  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.78113 1.15224 1.49091 0.05362  0.09329  0.28841  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.73384 0.85506 1.26871 -0.01216 0.04718  0.14456  106 ASN A N   
715  C CA  . ASN A 99  ? 0.89908 0.94235 1.39845 -0.03364 0.05150  0.11429  106 ASN A CA  
716  C C   . ASN A 99  ? 0.84918 0.88431 1.32669 -0.07198 0.01600  0.07598  106 ASN A C   
717  O O   . ASN A 99  ? 0.93973 0.97451 1.44427 -0.12257 0.00573  0.06199  106 ASN A O   
718  C CB  . ASN A 99  ? 0.81268 0.79414 1.24812 0.01622  0.07007  0.10929  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.82329 0.79784 1.27025 0.05446  0.10883  0.14328  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.79002 0.81073 1.29448 0.04859  0.12368  0.17522  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.78725 0.70971 1.18004 0.09565  0.12566  0.13826  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.75850 0.80156 0.73896 0.02423  0.13523  0.11243  107 LEU A N   
723  C CA  . LEU A 100 ? 0.79256 0.75425 0.81334 0.02423  0.10748  0.10548  107 LEU A CA  
724  C C   . LEU A 100 ? 0.81912 0.81289 0.89637 0.05348  0.11158  0.08325  107 LEU A C   
725  O O   . LEU A 100 ? 0.76602 0.73673 0.89963 0.03928  0.09432  0.09308  107 LEU A O   
726  C CB  . LEU A 100 ? 0.85937 0.71496 0.81131 0.04027  0.08451  0.07658  107 LEU A CB  
727  C CG  . LEU A 100 ? 0.82363 0.63145 0.74917 0.00186  0.06348  0.10919  107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.91426 0.61970 0.81837 0.01032  0.03586  0.09409  107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.82784 0.66331 0.82531 -0.03782 0.06359  0.16500  107 LEU A CD2 
730  N N   . GLY A 101 ? 0.80066 0.84844 0.86115 0.09678  0.13360  0.05318  108 GLY A N   
731  C CA  . GLY A 101 ? 0.63396 0.73428 0.75992 0.12463  0.13570  0.04109  108 GLY A CA  
732  C C   . GLY A 101 ? 0.75081 0.95504 0.97134 0.08671  0.14201  0.08189  108 GLY A C   
733  O O   . GLY A 101 ? 0.71777 0.93803 1.00486 0.08155  0.12260  0.08344  108 GLY A O   
734  N N   . THR A 102 ? 0.72891 1.00396 0.95475 0.05617  0.16583  0.11791  109 THR A N   
735  C CA  . THR A 102 ? 0.61886 0.98612 0.94100 0.01026  0.16963  0.16592  109 THR A CA  
736  C C   . THR A 102 ? 0.65253 0.93872 1.01369 -0.03751 0.13336  0.18451  109 THR A C   
737  O O   . THR A 102 ? 0.76875 1.08935 1.21245 -0.06738 0.11771  0.20145  109 THR A O   
738  C CB  . THR A 102 ? 0.56229 1.01504 0.87298 -0.01272 0.20423  0.20834  109 THR A CB  
739  O OG1 . THR A 102 ? 0.61585 1.11936 0.85907 0.04044  0.24099  0.17996  109 THR A OG1 
740  C CG2 . THR A 102 ? 0.65088 1.22009 1.07369 -0.05610 0.21362  0.26253  109 THR A CG2 
741  N N   . ILE A 103 ? 0.63129 0.80847 0.93436 -0.04448 0.11893  0.18113  110 ILE A N   
742  C CA  . ILE A 103 ? 0.67317 0.76474 1.00521 -0.07736 0.09156  0.19496  110 ILE A CA  
743  C C   . ILE A 103 ? 0.70602 0.74415 1.04630 -0.05448 0.06643  0.15577  110 ILE A C   
744  O O   . ILE A 103 ? 0.76512 0.77187 1.14907 -0.08082 0.04519  0.16019  110 ILE A O   
745  C CB  . ILE A 103 ? 0.76666 0.77346 1.04310 -0.08444 0.08717  0.20871  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.75981 0.81914 1.02522 -0.11257 0.09927  0.24809  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.75425 0.67399 1.01415 -0.08378 0.05644  0.18511  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.72843 0.76799 1.00727 -0.13325 0.07792  0.24926  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.75071 0.77355 1.04411 -0.00511 0.06694  0.11689  111 ALA A N   
750  C CA  . ALA A 104 ? 0.67497 0.64516 0.96377 0.02080  0.04279  0.08514  111 ALA A CA  
751  C C   . ALA A 104 ? 0.76648 0.82239 1.11715 0.02737  0.03273  0.07711  111 ALA A C   
752  O O   . ALA A 104 ? 0.85085 0.87161 1.20205 0.04022  0.00594  0.05659  111 ALA A O   
753  C CB  . ALA A 104 ? 0.59543 0.50627 0.81356 0.06911  0.04455  0.05502  111 ALA A CB  
754  N N   . LYS A 105 ? 0.76463 0.93983 1.16859 0.01882  0.05291  0.09707  112 LYS A N   
755  C CA  . LYS A 105 ? 0.64532 0.92121 1.12336 0.02556  0.04229  0.09682  112 LYS A CA  
756  C C   . LYS A 105 ? 0.66695 0.93034 1.20226 -0.02628 0.00316  0.10713  112 LYS A C   
757  O O   . LYS A 105 ? 0.74388 1.04819 1.31980 -0.02049 -0.02553 0.09598  112 LYS A O   
758  C CB  . LYS A 105 ? 0.59427 1.01342 1.12451 0.02792  0.07940  0.12422  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.74105 1.22029 1.33804 -0.03862 0.08467  0.17402  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.68993 1.30431 1.31334 -0.02989 0.13320  0.20568  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.62364 1.28331 1.30169 -0.09826 0.14089  0.26432  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.64505 1.41564 1.31730 -0.08609 0.18434  0.28817  112 LYS A NZ  
763  N N   . SER A 106 ? 0.67637 0.87879 1.21322 -0.07634 -0.00161 0.12772  113 SER A N   
764  C CA  . SER A 106 ? 0.59031 0.75160 1.16688 -0.12496 -0.04044 0.12904  113 SER A CA  
765  C C   . SER A 106 ? 0.69425 0.72339 1.19801 -0.10500 -0.06594 0.09007  113 SER A C   
766  O O   . SER A 106 ? 0.69453 0.70225 1.20709 -0.11848 -0.10453 0.06945  113 SER A O   
767  C CB  . SER A 106 ? 0.62159 0.76469 1.23450 -0.18299 -0.03297 0.16976  113 SER A CB  
768  O OG  . SER A 106 ? 0.75854 0.85364 1.31615 -0.16907 -0.00188 0.18375  113 SER A OG  
769  N N   . GLY A 107 ? 0.80193 0.74668 1.23214 -0.07441 -0.04582 0.08196  114 GLY A N   
770  C CA  . GLY A 107 ? 0.83281 0.66682 1.19506 -0.04891 -0.06136 0.05201  114 GLY A CA  
771  C C   . GLY A 107 ? 0.79853 0.65480 1.13851 -0.00681 -0.07991 0.02339  114 GLY A C   
772  O O   . GLY A 107 ? 0.84056 0.63127 1.13889 0.00298  -0.10445 0.00022  114 GLY A O   
773  N N   . THR A 108 ? 0.76791 0.71572 1.13131 0.02258  -0.06687 0.02604  115 THR A N   
774  C CA  . THR A 108 ? 0.67421 0.65277 1.03052 0.06587  -0.08538 0.00643  115 THR A CA  
775  C C   . THR A 108 ? 0.75432 0.79535 1.16726 0.03815  -0.12641 0.00453  115 THR A C   
776  O O   . THR A 108 ? 0.81965 0.82828 1.20011 0.05286  -0.16005 -0.01485 115 THR A O   
777  C CB  . THR A 108 ? 0.72971 0.78589 1.10110 0.10986  -0.05703 0.00944  115 THR A CB  
778  O OG1 . THR A 108 ? 0.69977 0.68289 1.00635 0.13129  -0.02912 0.00510  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.78820 0.87840 1.16421 0.15930  -0.07638 -0.00424 115 THR A CG2 
780  N N   . LYS A 109 ? 0.71527 0.84986 1.21304 -0.00563 -0.12690 0.02823  116 LYS A N   
781  C CA  . LYS A 109 ? 0.62094 0.82209 1.18561 -0.04395 -0.17282 0.03118  116 LYS A CA  
782  C C   . LYS A 109 ? 0.77305 0.85640 1.28520 -0.07804 -0.21383 0.00527  116 LYS A C   
783  O O   . LYS A 109 ? 0.80373 0.89262 1.30797 -0.08120 -0.26114 -0.01360 116 LYS A O   
784  C CB  . LYS A 109 ? 0.62017 0.93293 1.28980 -0.09497 -0.16278 0.07005  116 LYS A CB  
785  C CG  . LYS A 109 ? 0.56983 1.04603 1.31780 -0.06359 -0.13947 0.09476  116 LYS A CG  
786  C CD  . LYS A 109 ? 0.57116 1.17561 1.44002 -0.12400 -0.14289 0.13948  116 LYS A CD  
787  C CE  . LYS A 109 ? 0.46967 1.08908 1.39504 -0.18082 -0.21147 0.13793  116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.51319 1.18696 1.49830 -0.24544 -0.20837 0.17238  116 LYS A NZ  
789  N N   . ALA A 110 ? 0.79398 0.76955 1.26558 -0.10057 -0.19639 0.00394  117 ALA A N   
790  C CA  . ALA A 110 ? 0.89989 0.75039 1.31177 -0.12358 -0.22639 -0.02512 117 ALA A CA  
791  C C   . ALA A 110 ? 0.99108 0.76396 1.30098 -0.06998 -0.23126 -0.05656 117 ALA A C   
792  O O   . ALA A 110 ? 1.20911 0.91852 1.46550 -0.07831 -0.26860 -0.08726 117 ALA A O   
793  C CB  . ALA A 110 ? 0.94963 0.70836 1.35224 -0.15057 -0.19949 -0.01241 117 ALA A CB  
794  N N   . PHE A 111 ? 0.97107 0.74490 1.24859 -0.01695 -0.19538 -0.04862 118 PHE A N   
795  C CA  . PHE A 111 ? 1.04086 0.74782 1.23007 0.03244  -0.19721 -0.06752 118 PHE A CA  
796  C C   . PHE A 111 ? 1.05479 0.82103 1.24206 0.04921  -0.24042 -0.07990 118 PHE A C   
797  O O   . PHE A 111 ? 1.18458 0.89068 1.29811 0.05920  -0.26742 -0.10240 118 PHE A O   
798  C CB  . PHE A 111 ? 0.96930 0.66736 1.13824 0.07704  -0.15527 -0.05154 118 PHE A CB  
799  C CG  . PHE A 111 ? 1.02056 0.68120 1.09711 0.10883  -0.13609 -0.05361 118 PHE A CG  
800  C CD1 . PHE A 111 ? 1.05517 0.66670 1.06982 0.09830  -0.12936 -0.06185 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.87714 0.57496 0.93752 0.13901  -0.11277 -0.04066 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 1.02760 0.63539 0.98776 0.11872  -0.10564 -0.05425 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.83435 0.52229 0.84176 0.14748  -0.08992 -0.03169 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.99748 0.64563 0.96241 0.13873  -0.08905 -0.03741 118 PHE A CZ  
805  N N   . MET A 112 ? 0.94656 0.83654 1.21335 0.05548  -0.24648 -0.06272 119 MET A N   
806  C CA  . MET A 112 ? 0.97728 0.94040 1.25815 0.07451  -0.28951 -0.06546 119 MET A CA  
807  C C   . MET A 112 ? 1.04569 1.01310 1.33226 0.02083  -0.34861 -0.08258 119 MET A C   
808  O O   . MET A 112 ? 1.08111 1.06213 1.33324 0.03305  -0.39425 -0.09382 119 MET A O   
809  C CB  . MET A 112 ? 0.80716 0.91043 1.18567 0.09678  -0.27696 -0.03928 119 MET A CB  
810  C CG  . MET A 112 ? 0.76010 0.84987 1.12777 0.14338  -0.21999 -0.02997 119 MET A CG  
811  S SD  . MET A 112 ? 1.00538 1.22433 1.44397 0.20521  -0.20581 -0.01202 119 MET A SD  
812  C CE  . MET A 112 ? 0.77657 0.89857 1.12347 0.27394  -0.20801 -0.02166 119 MET A CE  
813  N N   . GLU A 113 ? 1.13830 1.08964 1.46487 -0.04091 -0.35267 -0.08368 120 GLU A N   
814  C CA  . GLU A 113 ? 1.20053 1.12526 1.52010 -0.09838 -0.41303 -0.10705 120 GLU A CA  
815  C C   . GLU A 113 ? 1.42711 1.19764 1.60986 -0.08716 -0.42323 -0.14920 120 GLU A C   
816  O O   . GLU A 113 ? 1.56005 1.30417 1.69226 -0.10837 -0.48049 -0.17895 120 GLU A O   
817  C CB  . GLU A 113 ? 1.29598 1.23282 1.69959 -0.16887 -0.41344 -0.09255 120 GLU A CB  
818  C CG  . GLU A 113 ? 1.11900 1.22777 1.66418 -0.19123 -0.41339 -0.04838 120 GLU A CG  
819  C CD  . GLU A 113 ? 1.35351 1.47171 1.97704 -0.25068 -0.39327 -0.02043 120 GLU A CD  
820  O OE1 . GLU A 113 ? 1.53337 1.51864 2.10219 -0.26903 -0.37770 -0.03484 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 1.32030 1.58276 2.06232 -0.27597 -0.39007 0.02099  120 GLU A OE2 
822  N N   . ALA A 114 ? 1.73301 1.40604 1.85291 -0.05313 -0.36872 -0.15107 121 ALA A N   
823  C CA  . ALA A 114 ? 1.85951 1.39331 1.85414 -0.03529 -0.36592 -0.18579 121 ALA A CA  
824  C C   . ALA A 114 ? 1.83665 1.36863 1.74384 0.01977  -0.37648 -0.19310 121 ALA A C   
825  O O   . ALA A 114 ? 1.93788 1.38804 1.73792 0.02581  -0.39889 -0.22688 121 ALA A O   
826  C CB  . ALA A 114 ? 1.88095 1.34695 1.85722 -0.01645 -0.29460 -0.16851 121 ALA A CB  
827  N N   . LEU A 115 ? 1.46548 1.07999 1.41020 0.06217  -0.35951 -0.16165 122 LEU A N   
828  C CA  . LEU A 115 ? 1.47598 1.09098 1.34688 0.11415  -0.37110 -0.15883 122 LEU A CA  
829  C C   . LEU A 115 ? 1.52840 1.18684 1.37392 0.09571  -0.44302 -0.17735 122 LEU A C   
830  O O   . LEU A 115 ? 1.64481 1.25645 1.38206 0.12173  -0.46275 -0.19129 122 LEU A O   
831  C CB  . LEU A 115 ? 1.27185 0.96181 1.20067 0.16005  -0.34432 -0.12173 122 LEU A CB  
832  C CG  . LEU A 115 ? 1.20857 0.87077 1.16847 0.17331  -0.28282 -0.10299 122 LEU A CG  
833  C CD1 . LEU A 115 ? 1.04117 0.80091 1.08757 0.19644  -0.27000 -0.07851 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 1.26941 0.83903 1.14253 0.21097  -0.24730 -0.09567 122 LEU A CD2 
835  N N   . GLN A 116 ? 1.43708 1.19166 1.38152 0.04888  -0.48454 -0.17371 123 GLN A N   
836  C CA  . GLN A 116 ? 1.43536 1.24050 1.36744 0.02028  -0.56299 -0.18878 123 GLN A CA  
837  C C   . GLN A 116 ? 1.50086 1.19407 1.34386 -0.03064 -0.60023 -0.24016 123 GLN A C   
838  O O   . GLN A 116 ? 1.38468 1.09190 1.17802 -0.05010 -0.65373 -0.25697 123 GLN A O   
839  C CB  . GLN A 116 ? 1.25801 1.22051 1.34363 -0.01418 -0.59519 -0.15906 123 GLN A CB  
840  C CG  . GLN A 116 ? 1.12526 1.21616 1.28331 0.04355  -0.58624 -0.11519 123 GLN A CG  
841  C CD  . GLN A 116 ? 1.16557 1.20616 1.29121 0.11192  -0.51387 -0.09961 123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.15203 1.11957 1.26820 0.10771  -0.45969 -0.10544 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 1.14072 1.21969 1.25276 0.17297  -0.51704 -0.07641 123 GLN A NE2 
844  N N   . ALA A 117 ? 1.43935 2.02604 0.96260 -0.28807 -0.07548 -0.42125 124 ALA A N   
845  C CA  . ALA A 117 ? 1.42082 1.95704 0.95134 -0.33652 -0.05486 -0.51326 124 ALA A CA  
846  C C   . ALA A 117 ? 1.59494 2.07746 1.06881 -0.31724 -0.01450 -0.54072 124 ALA A C   
847  O O   . ALA A 117 ? 1.63156 2.05306 1.10993 -0.34635 0.01466  -0.61228 124 ALA A O   
848  C CB  . ALA A 117 ? 1.41485 1.84693 1.04907 -0.34972 -0.03087 -0.53404 124 ALA A CB  
849  N N   . GLY A 118 ? 1.75292 2.25191 1.17919 -0.26822 -0.00814 -0.48246 125 GLY A N   
850  C CA  . GLY A 118 ? 1.80674 2.27057 1.17947 -0.24946 0.02958  -0.49799 125 GLY A CA  
851  C C   . GLY A 118 ? 1.75031 2.16036 1.13782 -0.20569 0.06481  -0.46519 125 GLY A C   
852  O O   . GLY A 118 ? 1.78176 2.18803 1.12456 -0.17972 0.08925  -0.44659 125 GLY A O   
853  N N   . ALA A 119 ? 1.71387 2.07515 1.17487 -0.19528 0.06634  -0.44833 126 ALA A N   
854  C CA  . ALA A 119 ? 1.68918 1.98579 1.19643 -0.15103 0.09085  -0.40034 126 ALA A CA  
855  C C   . ALA A 119 ? 1.44968 1.79467 0.90458 -0.11523 0.07336  -0.32435 126 ALA A C   
856  O O   . ALA A 119 ? 1.44433 1.86212 0.85356 -0.11493 0.03819  -0.29107 126 ALA A O   
857  C CB  . ALA A 119 ? 1.51807 1.73859 1.12998 -0.14205 0.08415  -0.37584 126 ALA A CB  
858  N N   . ASP A 120 ? 1.34202 1.64550 0.81294 -0.08476 0.10064  -0.29477 127 ASP A N   
859  C CA  . ASP A 120 ? 1.19789 1.52532 0.62820 -0.05213 0.09271  -0.22460 127 ASP A CA  
860  C C   . ASP A 120 ? 1.15423 1.41318 0.65347 -0.02745 0.07993  -0.17102 127 ASP A C   
861  O O   . ASP A 120 ? 1.16580 1.37072 0.73627 -0.03371 0.07147  -0.18135 127 ASP A O   
862  C CB  . ASP A 120 ? 1.11427 1.45592 0.49736 -0.04264 0.13448  -0.23092 127 ASP A CB  
863  C CG  . ASP A 120 ? 1.15420 1.42807 0.61617 -0.03921 0.17878  -0.25879 127 ASP A CG  
864  O OD1 . ASP A 120 ? 1.20608 1.41956 0.76182 -0.03872 0.17156  -0.26124 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 1.14292 1.42737 0.57525 -0.03451 0.22352  -0.27360 127 ASP A OD2 
866  N N   . ILE A 121 ? 1.12622 1.38351 0.59817 -0.00072 0.07859  -0.11290 128 ILE A N   
867  C CA  . ILE A 121 ? 1.01682 1.20765 0.53270 0.01817  0.06138  -0.06446 128 ILE A CA  
868  C C   . ILE A 121 ? 1.01023 1.14000 0.61226 0.01744  0.07805  -0.07636 128 ILE A C   
869  O O   . ILE A 121 ? 0.99248 1.06405 0.64684 0.02260  0.05617  -0.05463 128 ILE A O   
870  C CB  . ILE A 121 ? 1.06144 1.26085 0.51939 0.04281  0.05817  -0.00398 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.96316 1.20449 0.37316 0.04957  0.03514  0.02121  128 ILE A CG1 
872  C CG2 . ILE A 121 ? 1.08656 1.20566 0.58110 0.05587  0.04646  0.03581  128 ILE A CG2 
873  C CD1 . ILE A 121 ? 1.14629 1.43070 0.53168 0.04492  0.04104  0.02211  128 ILE A CD1 
874  N N   . SER A 122 ? 0.97112 1.11627 0.59026 0.01203  0.11762  -0.10942 129 SER A N   
875  C CA  . SER A 122 ? 1.01772 1.11850 0.73542 0.01588  0.13857  -0.11373 129 SER A CA  
876  C C   . SER A 122 ? 0.96949 1.02268 0.76981 0.00948  0.12628  -0.13572 129 SER A C   
877  O O   . SER A 122 ? 0.99411 1.00880 0.88756 0.01785  0.12720  -0.12017 129 SER A O   
878  C CB  . SER A 122 ? 1.05130 1.18038 0.76998 0.01353  0.19515  -0.15004 129 SER A CB  
879  O OG  . SER A 122 ? 1.12759 1.26088 0.84094 -0.00344 0.21737  -0.21715 129 SER A OG  
880  N N   . MET A 123 ? 0.98763 1.04585 0.76306 -0.00576 0.11427  -0.16708 130 MET A N   
881  C CA  . MET A 123 ? 0.97255 0.98020 0.82332 -0.01218 0.10645  -0.18330 130 MET A CA  
882  C C   . MET A 123 ? 0.90267 0.87749 0.75218 -0.00475 0.06049  -0.13447 130 MET A C   
883  O O   . MET A 123 ? 0.90151 0.84735 0.78105 -0.01368 0.05092  -0.14416 130 MET A O   
884  C CB  . MET A 123 ? 1.02604 1.04862 0.85910 -0.03904 0.12464  -0.24871 130 MET A CB  
885  C CG  . MET A 123 ? 1.00669 1.00360 0.89439 -0.04493 0.17671  -0.30619 130 MET A CG  
886  S SD  . MET A 123 ? 1.20075 1.21360 1.03498 -0.08606 0.19877  -0.39572 130 MET A SD  
887  C CE  . MET A 123 ? 1.23605 1.30926 0.96925 -0.08769 0.23550  -0.42693 130 MET A CE  
888  N N   . ILE A 124 ? 0.92376 0.89533 0.73484 0.01064  0.03644  -0.08289 131 ILE A N   
889  C CA  . ILE A 124 ? 0.85592 0.78812 0.64510 0.01884  -0.00134 -0.03988 131 ILE A CA  
890  C C   . ILE A 124 ? 0.91381 0.78312 0.78067 0.02405  -0.01870 -0.02164 131 ILE A C   
891  O O   . ILE A 124 ? 0.97554 0.80523 0.83220 0.02690  -0.04296 0.00169  131 ILE A O   
892  C CB  . ILE A 124 ? 0.85812 0.79202 0.57539 0.03285  -0.01618 0.00389  131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.96977 0.86321 0.63857 0.04236  -0.04493 0.04037  131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.91744 0.82665 0.67481 0.03772  -0.01748 0.02430  131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.81668 0.70014 0.40783 0.05787  -0.05135 0.07872  131 ILE A CD1 
896  N N   . GLY A 125 ? 0.91362 0.77688 0.86142 0.02728  -0.00512 -0.02738 132 GLY A N   
897  C CA  . GLY A 125 ? 0.87524 0.69092 0.90617 0.03518  -0.02713 -0.00114 132 GLY A CA  
898  C C   . GLY A 125 ? 0.90159 0.68792 0.98637 0.03287  -0.01666 -0.02018 132 GLY A C   
899  O O   . GLY A 125 ? 0.86181 0.60290 0.98551 0.04137  -0.04363 0.01380  132 GLY A O   
900  N N   . GLN A 126 ? 0.88953 0.69751 0.97341 0.01939  0.02179  -0.07380 133 GLN A N   
901  C CA  . GLN A 126 ? 0.88937 0.66138 1.02808 0.01167  0.03879  -0.09864 133 GLN A CA  
902  C C   . GLN A 126 ? 0.96317 0.71237 1.05621 0.00479  0.01281  -0.07585 133 GLN A C   
903  O O   . GLN A 126 ? 1.01193 0.72460 1.15314 -0.00336 0.02607  -0.08823 133 GLN A O   
904  C CB  . GLN A 126 ? 0.89277 0.68976 1.03061 -0.00863 0.08636  -0.17113 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.96974 0.81168 1.08984 -0.00539 0.11500  -0.19514 133 GLN A CG  
906  C CD  . GLN A 126 ? 1.11281 0.93028 1.34156 0.01121  0.15370  -0.20538 133 GLN A CD  
907  O OE1 . GLN A 126 ? 1.33169 1.09915 1.65385 0.02249  0.15638  -0.19243 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 1.05448 0.90875 1.27616 0.01590  0.18779  -0.22323 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.97990 0.74460 0.98574 0.00904  -0.01720 -0.04164 134 PHE A N   
910  C CA  . PHE A 127 ? 0.98343 0.72979 0.94303 0.00659  -0.03385 -0.01592 134 PHE A CA  
911  C C   . PHE A 127 ? 1.02939 0.72485 0.95494 0.02663  -0.07012 0.04494  134 PHE A C   
912  O O   . PHE A 127 ? 1.09692 0.77071 0.96998 0.02955  -0.07963 0.07229  134 PHE A O   
913  C CB  . PHE A 127 ? 1.01462 0.82270 0.89539 -0.00371 -0.03085 -0.02893 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.99676 0.85835 0.89376 -0.03037 -0.00433 -0.09008 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.99094 0.89215 0.87845 -0.03399 0.01301  -0.12524 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 1.01594 0.88671 0.93371 -0.05511 0.00377  -0.11322 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 1.02302 0.96859 0.90553 -0.06136 0.03539  -0.18600 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 1.01809 0.93578 0.94258 -0.08719 0.02197  -0.17572 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 1.04561 0.99899 0.94446 -0.09012 0.03650  -0.21402 134 PHE A CZ  
920  N N   . GLY A 128 ? 1.00213 0.67939 0.95536 0.03854  -0.09004 0.06620  135 GLY A N   
921  C CA  . GLY A 128 ? 0.84788 0.47565 0.75999 0.05111  -0.13183 0.11847  135 GLY A CA  
922  C C   . GLY A 128 ? 0.92627 0.55026 0.72440 0.05445  -0.14769 0.13634  135 GLY A C   
923  O O   . GLY A 128 ? 1.12488 0.69553 0.85860 0.06201  -0.17674 0.17318  135 GLY A O   
924  N N   . VAL A 129 ? 0.97410 0.64838 0.73980 0.05047  -0.12696 0.11229  136 VAL A N   
925  C CA  . VAL A 129 ? 0.95804 0.62557 0.62303 0.05815  -0.13365 0.13128  136 VAL A CA  
926  C C   . VAL A 129 ? 0.96028 0.65501 0.62985 0.05568  -0.13096 0.12418  136 VAL A C   
927  O O   . VAL A 129 ? 0.97931 0.69561 0.58687 0.06109  -0.11767 0.12679  136 VAL A O   
928  C CB  . VAL A 129 ? 0.95698 0.66348 0.57440 0.06079  -0.10871 0.12358  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.96357 0.63576 0.57235 0.06332  -0.10866 0.14074  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.85267 0.63648 0.52013 0.04656  -0.08243 0.08005  136 VAL A CG2 
931  N N   . GLY A 130 ? 0.67677 0.79782 0.72571 -0.27284 0.03804  -0.05087 137 GLY A N   
932  C CA  . GLY A 130 ? 0.73371 0.83191 0.76450 -0.25709 0.03956  -0.04822 137 GLY A CA  
933  C C   . GLY A 130 ? 0.65133 0.75561 0.69501 -0.23098 0.03450  -0.03512 137 GLY A C   
934  O O   . GLY A 130 ? 0.61221 0.70845 0.64547 -0.21915 0.03184  -0.02792 137 GLY A O   
935  N N   . PHE A 131 ? 0.64158 0.75846 0.70649 -0.22111 0.03254  -0.03155 138 PHE A N   
936  C CA  . PHE A 131 ? 0.66354 0.77716 0.73776 -0.19548 0.02475  -0.02391 138 PHE A CA  
937  C C   . PHE A 131 ? 0.59045 0.73544 0.66076 -0.18136 0.01053  -0.01976 138 PHE A C   
938  O O   . PHE A 131 ? 0.58123 0.70888 0.65086 -0.16348 0.00356  -0.01171 138 PHE A O   
939  C CB  . PHE A 131 ? 0.69898 0.82139 0.79029 -0.18491 0.02495  -0.02496 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.67155 0.80077 0.76852 -0.15641 0.01161  -0.02346 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.73520 0.82412 0.83365 -0.14403 0.00596  -0.02026 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.68051 0.85604 0.78207 -0.14149 0.00405  -0.02496 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.64600 0.73032 0.74767 -0.11805 -0.00899 -0.02194 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.67444 0.85001 0.77654 -0.11039 -0.00847 -0.02667 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.66015 0.78483 0.76090 -0.09902 -0.01601 -0.02686 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.62035 0.81241 0.69045 -0.18959 0.00527  -0.02301 139 TYR A N   
947  C CA  . TYR A 132 ? 0.51619 0.74636 0.58360 -0.17385 -0.00817 -0.01729 139 TYR A CA  
948  C C   . TYR A 132 ? 0.58914 0.80577 0.63669 -0.17372 -0.01115 -0.01136 139 TYR A C   
949  O O   . TYR A 132 ? 0.58978 0.82853 0.63438 -0.15519 -0.02199 -0.00206 139 TYR A O   
950  C CB  . TYR A 132 ? 0.40645 0.69908 0.48213 -0.18648 -0.01331 -0.02002 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.54605 0.86579 0.64311 -0.18228 -0.00950 -0.01965 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.48527 0.82430 0.59065 -0.14857 -0.01458 -0.01545 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.58231 0.90701 0.68942 -0.20989 -0.00058 -0.02270 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.39630 0.76676 0.51718 -0.14056 -0.00971 -0.01436 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.59334 0.94894 0.72026 -0.20496 0.00461  -0.01741 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.54143 0.92373 0.67406 -0.16930 0.00062  -0.01326 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.67311 1.09272 0.82155 -0.16044 0.00710  -0.00737 139 TYR A OH  
958  N N   . SER A 133 ? 0.62696 0.81015 0.65962 -0.19052 -0.00091 -0.01479 140 SER A N   
959  C CA  . SER A 133 ? 0.59533 0.76677 0.60753 -0.18627 -0.00069 -0.00587 140 SER A CA  
960  C C   . SER A 133 ? 0.61924 0.76083 0.64058 -0.16473 -0.00214 0.01208  140 SER A C   
961  O O   . SER A 133 ? 0.69153 0.82828 0.70032 -0.15834 -0.00216 0.02665  140 SER A O   
962  C CB  . SER A 133 ? 0.65929 0.80307 0.65168 -0.20472 0.01287  -0.01472 140 SER A CB  
963  O OG  . SER A 133 ? 0.70445 0.80683 0.70895 -0.20503 0.02553  -0.01336 140 SER A OG  
964  N N   . ALA A 134 ? 0.63973 0.76145 0.68229 -0.15409 -0.00436 0.01196  141 ALA A N   
965  C CA  . ALA A 134 ? 0.63482 0.72286 0.68869 -0.13651 -0.01046 0.02675  141 ALA A CA  
966  C C   . ALA A 134 ? 0.64324 0.74793 0.69438 -0.11507 -0.02459 0.03903  141 ALA A C   
967  O O   . ALA A 134 ? 0.66023 0.73690 0.71519 -0.10466 -0.02924 0.05759  141 ALA A O   
968  C CB  . ALA A 134 ? 0.54712 0.61230 0.62004 -0.12911 -0.01366 0.01819  141 ALA A CB  
969  N N   . TYR A 135 ? 0.60951 0.76139 0.65658 -0.10825 -0.03155 0.03189  142 TYR A N   
970  C CA  . TYR A 135 ? 0.61761 0.79218 0.66208 -0.08381 -0.04466 0.04412  142 TYR A CA  
971  C C   . TYR A 135 ? 0.63465 0.82806 0.66035 -0.08742 -0.04458 0.05980  142 TYR A C   
972  O O   . TYR A 135 ? 0.62850 0.84390 0.65062 -0.06635 -0.05502 0.07386  142 TYR A O   
973  C CB  . TYR A 135 ? 0.50728 0.73713 0.55708 -0.07393 -0.05105 0.03327  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.59242 0.80810 0.65684 -0.05764 -0.05310 0.02219  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.58301 0.78028 0.65112 -0.02276 -0.06490 0.02578  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.58180 0.79828 0.65352 -0.07506 -0.04353 0.00800  142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.54207 0.72603 0.61723 -0.00450 -0.06794 0.01186  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.56297 0.77123 0.64395 -0.05773 -0.04529 -0.00171 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.57474 0.76801 0.65564 -0.02193 -0.05788 -0.00152 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.61925 0.80485 0.70331 -0.00133 -0.06084 -0.01491 142 TYR A OH  
981  N N   . LEU A 136 ? 0.64028 0.82724 0.65147 -0.11018 -0.03285 0.05786  143 LEU A N   
982  C CA  . LEU A 136 ? 0.66766 0.86854 0.65671 -0.10967 -0.03140 0.07424  143 LEU A CA  
983  C C   . LEU A 136 ? 0.65609 0.82176 0.65326 -0.09236 -0.03283 0.10375  143 LEU A C   
984  O O   . LEU A 136 ? 0.63272 0.81770 0.61716 -0.07988 -0.03696 0.12537  143 LEU A O   
985  C CB  . LEU A 136 ? 0.66496 0.86027 0.63364 -0.13303 -0.01707 0.06335  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.73864 0.96607 0.69268 -0.15400 -0.01791 0.03642  143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.74000 0.94031 0.67556 -0.17257 -0.00255 0.02329  143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.68168 0.96489 0.61567 -0.15068 -0.03090 0.03776  143 LEU A CD2 
989  N N   . VAL A 137 ? 0.64207 0.75734 0.66162 -0.09246 -0.03080 0.10665  144 VAL A N   
990  C CA  . VAL A 137 ? 0.66847 0.74356 0.70218 -0.08277 -0.03359 0.13573  144 VAL A CA  
991  C C   . VAL A 137 ? 0.70409 0.73855 0.76171 -0.06644 -0.04862 0.13394  144 VAL A C   
992  O O   . VAL A 137 ? 0.78820 0.78465 0.85961 -0.05721 -0.05622 0.15833  144 VAL A O   
993  C CB  . VAL A 137 ? 0.63585 0.68553 0.67537 -0.10135 -0.01816 0.14632  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.67149 0.75752 0.68070 -0.11190 -0.00302 0.14513  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.64554 0.66767 0.70305 -0.11363 -0.01506 0.12458  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.64094 0.68086 0.70313 -0.06190 -0.05369 0.10663  145 ALA A N   
997  C CA  . ALA A 138 ? 0.64545 0.64632 0.72390 -0.04330 -0.06814 0.09856  145 ALA A CA  
998  C C   . ALA A 138 ? 0.72624 0.75914 0.79716 -0.01443 -0.07913 0.09045  145 ALA A C   
999  O O   . ALA A 138 ? 0.69374 0.78319 0.75544 -0.01710 -0.07424 0.07704  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.61954 0.60375 0.70817 -0.05581 -0.06433 0.07478  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.69504 0.69177 0.77154 0.01330  -0.09445 0.09980  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.63915 0.66224 0.70933 0.04813  -0.10483 0.09123  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.67486 0.69035 0.74826 0.06157  -0.10934 0.06144  146 GLU A C   
1004 O O   . GLU A 139 ? 0.68822 0.74771 0.75562 0.08743  -0.11212 0.05069  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.73266 0.71514 0.80418 0.07769  -0.11939 0.11343  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.84120 0.73640 0.92835 0.07164  -0.12904 0.12227  146 GLU A CG  
1007 C CD  . GLU A 139 ? 1.19711 1.05011 1.28774 0.09342  -0.14154 0.15277  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 1.30172 1.09724 1.39581 0.12084  -0.15926 0.14502  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 1.22224 1.09794 1.31028 0.08473  -0.13399 0.18460  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.71111 0.67844 0.79379 0.04611  -0.10993 0.04957  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.63773 0.59889 0.72007 0.05866  -0.11421 0.02131  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.62622 0.56825 0.71812 0.02580  -0.10590 0.01334  147 LYS A C   
1013 O O   . LYS A 140 ? 0.63714 0.53561 0.74062 0.00522  -0.10693 0.02714  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.67669 0.57757 0.75701 0.09380  -0.13545 0.01211  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.68069 0.57078 0.75526 0.10969  -0.14189 -0.01953 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.74684 0.58569 0.81052 0.15389  -0.16380 -0.03352 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.78319 0.53926 0.85239 0.14692  -0.18247 -0.04903 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.90088 0.58022 0.96466 0.17849  -0.20734 -0.05234 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.57175 0.55091 0.66079 0.02179  -0.09693 -0.00543 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.52900 0.49855 0.62597 -0.00603 -0.08727 -0.01220 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.58228 0.54146 0.67676 0.01224  -0.09556 -0.03596 148 VAL A C   
1022 O O   . VAL A 141 ? 0.66126 0.66272 0.74586 0.03522  -0.09434 -0.04821 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.52338 0.54659 0.61819 -0.03165 -0.06686 -0.00951 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.60143 0.61334 0.70348 -0.05390 -0.05655 -0.01660 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.55100 0.58228 0.64235 -0.04860 -0.06018 0.01019  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.54871 0.45757 0.65229 0.00271  -0.10427 -0.04127 149 THR A N   
1027 C CA  . THR A 142 ? 0.57638 0.47402 0.67507 0.01762  -0.11391 -0.06517 149 THR A CA  
1028 C C   . THR A 142 ? 0.62147 0.53082 0.72991 -0.01054 -0.10058 -0.06472 149 THR A C   
1029 O O   . THR A 142 ? 0.66443 0.55226 0.78839 -0.03851 -0.09555 -0.04932 149 THR A O   
1030 C CB  . THR A 142 ? 0.61319 0.43978 0.71397 0.03178  -0.14095 -0.07521 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.65101 0.45417 0.74778 0.05119  -0.15135 -0.06606 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.63834 0.46075 0.72218 0.06111  -0.15455 -0.10653 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.55926 0.50599 0.65888 -0.00074 -0.09377 -0.07887 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.61136 0.57355 0.71862 -0.02272 -0.07985 -0.07693 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.63843 0.59191 0.73834 -0.00415 -0.09325 -0.09759 150 VAL A C   
1036 O O   . VAL A 143 ? 0.68143 0.66190 0.76366 0.02634  -0.09718 -0.11292 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.54101 0.56193 0.64590 -0.03298 -0.05637 -0.06900 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.59181 0.61977 0.70455 -0.05376 -0.04197 -0.06483 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.58303 0.61341 0.69055 -0.05002 -0.04715 -0.05327 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.60167 0.52313 0.71450 -0.02093 -0.10042 -0.09744 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.67813 0.59531 0.78442 -0.00807 -0.11390 -0.11647 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.63525 0.58263 0.75163 -0.02857 -0.09426 -0.10457 151 ILE A C   
1043 O O   . ILE A 144 ? 0.68251 0.61665 0.81896 -0.05661 -0.08520 -0.08674 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.68242 0.53787 0.79815 -0.01066 -0.14368 -0.12675 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.60316 0.41653 0.71798 -0.00138 -0.15828 -0.12608 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.68126 0.53197 0.77913 0.01349  -0.16487 -0.15603 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.69358 0.50257 0.77947 0.04146  -0.17331 -0.15190 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.55436 0.54409 0.65645 -0.01212 -0.08646 -0.11217 152 THR A N   
1049 C CA  . THR A 145 ? 0.59360 0.61311 0.70385 -0.02793 -0.06606 -0.09806 152 THR A CA  
1050 C C   . THR A 145 ? 0.60134 0.64030 0.69881 -0.00733 -0.07547 -0.11206 152 THR A C   
1051 O O   . THR A 145 ? 0.60204 0.64248 0.67836 0.02283  -0.09362 -0.13458 152 THR A O   
1052 C CB  . THR A 145 ? 0.57117 0.63410 0.67997 -0.03478 -0.03935 -0.08275 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.64808 0.72743 0.76608 -0.05137 -0.02021 -0.06748 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.53847 0.64622 0.62857 -0.00469 -0.03958 -0.09231 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.58496 0.63956 0.69288 -0.02102 -0.06286 -0.09868 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.59561 0.67575 0.69161 -0.00259 -0.06997 -0.10754 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.59023 0.70544 0.69502 -0.01437 -0.04223 -0.08264 153 LYS A C   
1058 O O   . LYS A 146 ? 0.62049 0.71886 0.74595 -0.03821 -0.03243 -0.06620 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.57898 0.62417 0.68286 -0.00635 -0.09798 -0.12119 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.51777 0.59210 0.60764 0.01238  -0.10846 -0.13167 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.60806 0.71213 0.66142 0.05160  -0.11533 -0.15348 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.64264 0.78224 0.67723 0.07294  -0.12486 -0.16304 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.55825 0.74760 0.60137 0.06640  -0.09394 -0.13137 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.72930 0.63455 0.68486 -0.00752 -0.02954 -0.03708 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.63764 0.54987 0.60270 -0.00254 -0.02462 -0.01912 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.70382 0.64912 0.66460 -0.00448 -0.02703 -0.00683 154 HIS A C   
1067 O O   . HIS A 147 ? 0.80521 0.76319 0.74856 -0.00894 -0.03310 -0.01672 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.64215 0.54253 0.61429 -0.00176 -0.02074 -0.01772 154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.64114 0.53851 0.62965 0.00219  -0.01785 0.00129  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.62357 0.54905 0.62087 0.00290  -0.01425 0.02074  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.67195 0.53845 0.66834 0.00723  -0.01852 0.00388  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.62588 0.53838 0.64230 0.00634  -0.01254 0.03681  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.73887 0.61144 0.75258 0.00917  -0.01594 0.02476  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.67889 0.63609 0.65288 0.00059  -0.02286 0.01449  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.60732 0.60167 0.57927 -0.00045 -0.02553 0.03062  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.70016 0.71426 0.66042 0.00076  -0.02343 0.03192  155 ASN A C   
1077 O O   . ASN A 148 ? 0.75065 0.79616 0.69604 0.00037  -0.02873 0.03748  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.67314 0.67603 0.66604 0.00758  -0.01831 0.05717  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.74661 0.75671 0.74700 0.00949  -0.02054 0.06655  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.78225 0.79658 0.77640 0.00129  -0.03047 0.05617  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.64467 0.65674 0.66186 0.02147  -0.01091 0.08957  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.68548 0.68517 0.65182 0.00345  -0.01645 0.02936  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.73568 0.76040 0.69741 0.00908  -0.01024 0.03913  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.72179 0.73763 0.66266 0.01099  -0.00924 0.01869  156 ASP A C   
1085 O O   . ASP A 149 ? 0.74300 0.77584 0.68598 0.01892  -0.00026 0.02974  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.66697 0.69129 0.66350 0.01141  -0.00244 0.06428  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.83337 0.86945 0.84982 0.01385  -0.00046 0.08856  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.92625 0.99739 0.93091 0.01709  -0.00097 0.09837  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.83550 0.84375 0.87782 0.01325  0.00048  0.09762  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.67450 0.66649 0.59879 0.00561  -0.01688 -0.00688 157 ASP A N   
1091 C CA  . ASP A 150 ? 0.68831 0.66744 0.59387 0.00920  -0.01477 -0.02609 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.74278 0.70350 0.62583 0.00303  -0.02718 -0.05104 157 ASP A C   
1093 O O   . ASP A 150 ? 0.71166 0.67316 0.59941 -0.00565 -0.03789 -0.05004 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.72233 0.68062 0.65184 0.00709  -0.00934 -0.02541 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.77894 0.74363 0.70097 0.01634  0.00014  -0.02651 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.78772 0.76151 0.67698 0.02680  0.00282  -0.03674 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.76033 0.72033 0.70787 0.01433  0.00406  -0.01647 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.72686 0.67154 0.58928 0.00802  -0.02576 -0.07022 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.69929 0.61927 0.54457 0.00133  -0.03903 -0.09400 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.74213 0.64010 0.61551 -0.00730 -0.03968 -0.09686 158 GLU A C   
1101 O O   . GLU A 151 ? 0.83678 0.73514 0.73443 -0.00673 -0.03109 -0.08491 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.76319 0.66971 0.57123 0.01426  -0.03604 -0.11382 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.87680 0.80132 0.64301 0.02620  -0.03892 -0.11688 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.13105 1.03113 0.84974 0.04274  -0.03802 -0.14261 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.16467 1.06488 0.88257 0.05974  -0.01819 -0.13884 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.26063 1.13984 0.94265 0.03938  -0.05821 -0.16581 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.72774 0.60547 0.59729 -0.01504 -0.05175 -0.11220 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.74945 0.61081 0.64435 -0.02008 -0.05096 -0.11286 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.80706 0.65231 0.69832 -0.01152 -0.03966 -0.12278 159 GLN A C   
1110 O O   . GLN A 152 ? 0.87875 0.71212 0.74462 -0.00426 -0.03875 -0.13744 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.77740 0.62811 0.67940 -0.03254 -0.06860 -0.11840 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.69706 0.55547 0.63377 -0.03742 -0.06864 -0.10113 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.79610 0.65812 0.74923 -0.05151 -0.08783 -0.09480 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.96634 0.85224 0.93343 -0.05584 -0.09324 -0.07565 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.88024 0.71897 0.83604 -0.05900 -0.09896 -0.10780 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.73612 0.58058 0.65001 -0.01041 -0.03137 -0.11442 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.74171 0.57841 0.65863 -0.00328 -0.02093 -0.11765 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.79678 0.62294 0.73455 -0.00664 -0.02183 -0.11742 160 TYR A C   
1119 O O   . TYR A 153 ? 0.77615 0.60448 0.72666 -0.01151 -0.02750 -0.11118 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.79861 0.65131 0.72353 0.00150  -0.01163 -0.10311 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.82489 0.69410 0.73182 0.01055  -0.00513 -0.09863 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.78140 0.64867 0.66894 0.02394  0.00422  -0.10561 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.81886 0.70704 0.72705 0.00932  -0.00643 -0.08521 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.87694 0.76327 0.74311 0.03796  0.01275  -0.09931 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.81530 0.72523 0.70747 0.02043  0.00105  -0.07700 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.92262 0.83282 0.79189 0.03578  0.01092  -0.08409 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 1.10174 1.03738 0.95031 0.05239  0.02087  -0.07380 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.84219 0.66090 0.78357 -0.00100 -0.01426 -0.12101 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.73053 0.54362 0.69154 -0.00181 -0.01351 -0.11866 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.68883 0.51079 0.65964 0.00283  -0.00556 -0.11015 161 ALA A C   
1131 O O   . ALA A 154 ? 0.72500 0.55025 0.69255 0.00954  0.00316  -0.10899 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.70019 0.49440 0.66188 -0.00101 -0.01478 -0.12904 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.63973 0.46613 0.62103 0.00067  -0.00940 -0.10299 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.60858 0.44179 0.59954 0.00160  -0.00860 -0.09523 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.65622 0.49022 0.65819 0.00529  -0.00694 -0.09358 162 TRP A C   
1136 O O   . TRP A 155 ? 0.76500 0.59659 0.76844 0.00702  -0.00918 -0.09403 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.68699 0.51806 0.67475 -0.00227 -0.01805 -0.09132 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.71356 0.54790 0.71048 -0.00561 -0.02451 -0.08406 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.68522 0.52764 0.69388 -0.01189 -0.02789 -0.07308 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.70284 0.53534 0.69989 -0.00372 -0.03108 -0.08431 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.59951 0.44310 0.61823 -0.01737 -0.03925 -0.06688 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.66554 0.50217 0.67319 -0.01175 -0.04166 -0.07573 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.69278 0.52425 0.68348 0.00462  -0.02964 -0.08793 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.67138 0.50780 0.67795 -0.01288 -0.05357 -0.07476 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.70040 0.53447 0.68798 0.00729  -0.03762 -0.08600 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.69708 0.53190 0.68983 -0.00199 -0.05081 -0.08152 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.62921 0.47187 0.64252 0.00784  -0.00191 -0.08698 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.61730 0.46540 0.64400 0.01266  0.00140  -0.08195 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.67053 0.53508 0.70900 0.01274  0.00107  -0.07003 163 GLU A C   
1150 O O   . GLU A 156 ? 0.66320 0.53582 0.70745 0.01181  0.00509  -0.06311 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.62261 0.46103 0.65706 0.01737  0.01088  -0.08558 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.68706 0.53216 0.74227 0.02265  0.01539  -0.07628 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.75613 0.58305 0.82186 0.02339  0.01793  -0.08059 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.82611 0.63696 0.89186 0.02829  0.02548  -0.08606 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.77843 0.60588 0.85296 0.01995  0.01164  -0.07713 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.63645 0.51023 0.67937 0.01498  -0.00395 -0.06444 164 SER A N   
1157 C CA  . SER A 157 ? 0.68366 0.57644 0.73901 0.01331  -0.00825 -0.05134 164 SER A CA  
1158 C C   . SER A 157 ? 0.65852 0.56354 0.71693 0.02068  -0.00934 -0.04554 164 SER A C   
1159 O O   . SER A 157 ? 0.63925 0.53812 0.68008 0.02539  -0.01553 -0.05205 164 SER A O   
1160 C CB  . SER A 157 ? 0.73111 0.62153 0.77840 0.00228  -0.02666 -0.05117 164 SER A CB  
1161 O OG  . SER A 157 ? 0.80572 0.71570 0.86719 -0.00271 -0.03658 -0.03694 164 SER A OG  
1162 N N   . SER A 158 ? 0.75252 0.67809 0.83328 0.02474  -0.00136 -0.03030 165 SER A N   
1163 C CA  . SER A 158 ? 0.70850 0.65500 0.79511 0.03196  -0.00327 -0.01909 165 SER A CA  
1164 C C   . SER A 158 ? 0.81167 0.77606 0.89579 0.02467  -0.02109 -0.01073 165 SER A C   
1165 O O   . SER A 158 ? 0.77058 0.76246 0.87050 0.02855  -0.02040 0.00622  165 SER A O   
1166 C CB  . SER A 158 ? 0.57879 0.53765 0.69533 0.04137  0.01592  -0.00449 165 SER A CB  
1167 O OG  . SER A 158 ? 0.77837 0.71478 0.89838 0.04473  0.02645  -0.01327 165 SER A OG  
1168 N N   . ALA A 159 ? 0.75164 0.70045 0.81862 0.01285  -0.03925 -0.02081 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.72986 0.68856 0.79810 -0.00027 -0.06321 -0.01334 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.69498 0.68525 0.80377 -0.00466 -0.05374 0.01284  166 ALA A C   
1171 O O   . ALA A 159 ? 0.77089 0.76043 0.89554 -0.00125 -0.03415 0.01757  166 ALA A O   
1172 C CB  . ALA A 159 ? 0.65070 0.61385 0.69352 0.00537  -0.08045 -0.01771 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.58871 0.60824 0.71279 -0.00989 -0.06676 0.03143  167 GLY A N   
1174 C CA  . GLY A 160 ? 0.61205 0.66754 0.77828 -0.01228 -0.05723 0.06231  167 GLY A CA  
1175 C C   . GLY A 160 ? 0.70724 0.76822 0.89493 -0.02766 -0.06670 0.07625  167 GLY A C   
1176 O O   . GLY A 160 ? 0.82436 0.92198 1.05066 -0.02835 -0.05897 0.10830  167 GLY A O   
1177 N N   . GLY A 161 ? 0.69550 0.72494 0.86366 -0.03834 -0.08161 0.05790  168 GLY A N   
1178 C CA  . GLY A 161 ? 0.69348 0.72989 0.88701 -0.05363 -0.09196 0.07504  168 GLY A CA  
1179 C C   . GLY A 161 ? 0.61470 0.64414 0.81059 -0.04357 -0.06626 0.07422  168 GLY A C   
1180 O O   . GLY A 161 ? 0.70062 0.74262 0.92126 -0.05302 -0.07093 0.09393  168 GLY A O   
1181 N N   . SER A 162 ? 0.57910 0.59044 0.75119 -0.02508 -0.04130 0.05405  169 SER A N   
1182 C CA  . SER A 162 ? 0.61198 0.61516 0.77861 -0.01387 -0.01896 0.05027  169 SER A CA  
1183 C C   . SER A 162 ? 0.65995 0.62567 0.78944 -0.00758 -0.01436 0.01682  169 SER A C   
1184 O O   . SER A 162 ? 0.65542 0.60840 0.76938 -0.00528 -0.01866 0.00202  169 SER A O   
1185 C CB  . SER A 162 ? 0.59957 0.62578 0.78296 0.00628  0.01114  0.06865  169 SER A CB  
1186 O OG  . SER A 162 ? 0.56046 0.57388 0.73192 0.01943  0.02441  0.05484  169 SER A OG  
1187 N N   . PHE A 163 ? 0.57641 0.52984 0.69412 -0.00388 -0.00545 0.00911  170 PHE A N   
1188 C CA  . PHE A 163 ? 0.66134 0.58482 0.74895 0.00115  -0.00117 -0.01764 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.65384 0.57490 0.73195 0.01345  0.01785  -0.02009 170 PHE A C   
1190 O O   . PHE A 163 ? 0.59126 0.53354 0.68225 0.01858  0.02680  -0.00098 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.68306 0.58658 0.75513 -0.01085 -0.02090 -0.03022 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.68915 0.59727 0.77067 -0.01926 -0.02712 -0.01915 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.67404 0.59649 0.78162 -0.03292 -0.04377 0.00125  170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.67511 0.57502 0.74270 -0.01482 -0.01871 -0.02642 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.67944 0.60808 0.80415 -0.04171 -0.05028 0.01677  170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.70674 0.61553 0.78705 -0.02115 -0.02307 -0.01174 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.70948 0.63245 0.82079 -0.03456 -0.03823 0.01100  170 PHE A CZ  
1198 N N   . THR A 164 ? 0.65902 0.55567 0.71395 0.01918  0.02288  -0.04199 171 THR A N   
1199 C CA  . THR A 164 ? 0.62765 0.51421 0.66326 0.03140  0.03650  -0.05100 171 THR A CA  
1200 C C   . THR A 164 ? 0.67815 0.54994 0.69292 0.02450  0.02723  -0.06593 171 THR A C   
1201 O O   . THR A 164 ? 0.67151 0.53298 0.68443 0.01438  0.01454  -0.07400 171 THR A O   
1202 C CB  . THR A 164 ? 0.60434 0.47102 0.63228 0.04324  0.04731  -0.06337 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.69211 0.54140 0.71893 0.03423  0.03625  -0.07666 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.68215 0.56564 0.73331 0.05253  0.05909  -0.04530 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.70967 0.58372 0.70751 0.03303  0.03508  -0.06711 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.71665 0.58207 0.69454 0.02836  0.02771  -0.07826 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.73922 0.59195 0.68559 0.04284  0.03640  -0.09281 172 VAL A C   
1208 O O   . VAL A 165 ? 0.71288 0.57551 0.65035 0.06040  0.05160  -0.08548 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.65354 0.54007 0.64277 0.02246  0.02381  -0.06031 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.70443 0.58815 0.67213 0.02258  0.02092  -0.06800 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.67992 0.56451 0.69079 0.00685  0.00863  -0.05383 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.78468 0.61553 0.71286 0.03687  0.02584  -0.11226 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.80347 0.61413 0.69607 0.04767  0.02671  -0.13111 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.83216 0.63743 0.71104 0.03541  0.01022  -0.14117 173 ARG A C   
1215 O O   . ARG A 166 ? 0.83054 0.64291 0.73007 0.02049  0.00059  -0.13447 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.86381 0.64254 0.75311 0.05279  0.02766  -0.14625 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.91388 0.68642 0.83513 0.03684  0.01792  -0.14396 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.95542 0.69163 0.87325 0.03589  0.01054  -0.16060 173 ARG A CD  
1219 N NE  . ARG A 166 ? 1.12210 0.85827 1.06758 0.01841  -0.00355 -0.15599 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 1.07064 0.79389 1.01300 0.00563  -0.02165 -0.16401 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 1.05916 0.76428 0.96738 0.00626  -0.03135 -0.18151 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.99266 0.72481 0.96690 -0.00693 -0.03071 -0.15165 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.89364 0.68674 0.73469 0.04406  0.00700  -0.15659 174 THR A N   
1224 C CA  . THR A 167 ? 0.89001 0.67947 0.71714 0.03174  -0.01147 -0.16551 174 THR A CA  
1225 C C   . THR A 167 ? 0.91997 0.68029 0.75785 0.01680  -0.02893 -0.17870 174 THR A C   
1226 O O   . THR A 167 ? 1.07822 0.80573 0.90378 0.02226  -0.03102 -0.19530 174 THR A O   
1227 C CB  . THR A 167 ? 0.86202 0.64905 0.64021 0.04658  -0.01227 -0.17814 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.93693 0.75022 0.70759 0.06763  0.00972  -0.16265 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.94763 0.75105 0.71885 0.03405  -0.02832 -0.17545 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.92442 0.69701 0.78806 -0.00049 -0.04074 -0.16824 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.99668 0.75219 0.88228 -0.01513 -0.05644 -0.17075 175 ASP A CA  
1232 C C   . ASP A 168 ? 1.10729 0.83937 0.96841 -0.02350 -0.07933 -0.18860 175 ASP A C   
1233 O O   . ASP A 168 ? 1.15420 0.89817 0.99046 -0.02466 -0.08766 -0.19122 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.91451 0.69574 0.83392 -0.02584 -0.05912 -0.14929 175 ASP A CB  
1235 C CG  . ASP A 168 ? 1.03518 0.80908 0.98647 -0.03785 -0.07126 -0.14245 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 1.08223 0.83850 1.04658 -0.03546 -0.06764 -0.14598 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 1.13410 0.92366 1.10164 -0.04883 -0.08357 -0.12922 175 ASP A OD2 
1238 N N   . THR A 169 ? 1.22978 0.92757 1.09911 -0.03008 -0.09167 -0.20000 176 THR A N   
1239 C CA  . THR A 169 ? 1.38441 1.04985 1.23336 -0.04194 -0.12036 -0.21908 176 THR A CA  
1240 C C   . THR A 169 ? 1.40762 1.07614 1.30391 -0.06719 -0.14342 -0.20317 176 THR A C   
1241 O O   . THR A 169 ? 1.37622 1.01962 1.26503 -0.08321 -0.17371 -0.21481 176 THR A O   
1242 C CB  . THR A 169 ? 1.46859 1.08107 1.28591 -0.02892 -0.12084 -0.24705 176 THR A CB  
1243 O OG1 . THR A 169 ? 1.37058 0.97120 1.22879 -0.02949 -0.11153 -0.23781 176 THR A OG1 
1244 C CG2 . THR A 169 ? 1.44429 1.05967 1.21395 0.00021  -0.09642 -0.25784 176 THR A CG2 
1245 N N   . GLY A 170 ? 1.34171 1.04136 1.28590 -0.07022 -0.13120 -0.17521 177 GLY A N   
1246 C CA  . GLY A 170 ? 1.31976 1.03121 1.31498 -0.08922 -0.14783 -0.15189 177 GLY A CA  
1247 C C   . GLY A 170 ? 1.30970 1.05295 1.31417 -0.10317 -0.16421 -0.13485 177 GLY A C   
1248 O O   . GLY A 170 ? 1.28789 1.03056 1.25473 -0.10461 -0.17443 -0.14867 177 GLY A O   
1249 N N   . GLU A 171 ? 1.40118 1.17683 1.45681 -0.11099 -0.16527 -0.10108 178 GLU A N   
1250 C CA  . GLU A 171 ? 1.29383 1.10573 1.36739 -0.12280 -0.17899 -0.07700 178 GLU A CA  
1251 C C   . GLU A 171 ? 1.07850 0.91800 1.12474 -0.10691 -0.15837 -0.07435 178 GLU A C   
1252 O O   . GLU A 171 ? 1.03484 0.88444 1.08065 -0.08875 -0.13162 -0.06903 178 GLU A O   
1253 C CB  . GLU A 171 ? 1.36075 1.20607 1.49761 -0.12829 -0.17900 -0.03552 178 GLU A CB  
1254 C CG  . GLU A 171 ? 1.38402 1.26564 1.55167 -0.14498 -0.19987 -0.00494 178 GLU A CG  
1255 C CD  . GLU A 171 ? 1.52847 1.38464 1.70548 -0.17512 -0.24241 -0.01365 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 1.59767 1.41907 1.79366 -0.18547 -0.25578 -0.02181 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 1.52087 1.39006 1.68621 -0.18878 -0.26432 -0.01215 178 GLU A OE2 
1258 N N   . PRO A 172 ? 1.05413 0.90495 1.07772 -0.11349 -0.17173 -0.07741 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.97497 0.85285 0.97989 -0.09881 -0.15231 -0.07016 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.95719 0.87060 0.99924 -0.09052 -0.13639 -0.03510 179 PRO A C   
1261 O O   . PRO A 172 ? 1.10671 1.03979 1.19016 -0.09921 -0.14572 -0.00835 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.87286 0.76112 0.85499 -0.11045 -0.17484 -0.07404 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.87341 0.72249 0.83772 -0.12562 -0.20338 -0.10057 179 PRO A CG  
1264 C CD  . PRO A 172 ? 1.08528 0.92031 1.09447 -0.13402 -0.20695 -0.09050 179 PRO A CD  
1265 N N   . MET A 173 ? 0.83993 0.76045 0.86684 -0.07190 -0.11240 -0.03389 180 MET A N   
1266 C CA  . MET A 173 ? 0.78998 0.73356 0.83875 -0.05714 -0.09461 -0.00689 180 MET A CA  
1267 C C   . MET A 173 ? 0.74664 0.71806 0.79482 -0.05269 -0.09168 0.01255  180 MET A C   
1268 O O   . MET A 173 ? 0.75743 0.75264 0.82891 -0.04197 -0.08211 0.04148  180 MET A O   
1269 C CB  . MET A 173 ? 0.89654 0.82101 0.92949 -0.03889 -0.07262 -0.01923 180 MET A CB  
1270 C CG  . MET A 173 ? 1.05430 0.99033 1.10335 -0.02061 -0.05657 0.00198  180 MET A CG  
1271 S SD  . MET A 173 ? 1.16670 1.07610 1.19898 -0.00528 -0.04119 -0.01590 180 MET A SD  
1272 C CE  . MET A 173 ? 0.76219 0.64687 0.77720 -0.01996 -0.04952 -0.04641 180 MET A CE  
1273 N N   . GLY A 174 ? 0.73041 0.70174 0.75238 -0.05748 -0.09775 0.00003  181 GLY A N   
1274 C CA  . GLY A 174 ? 0.74016 0.73919 0.76284 -0.05194 -0.09310 0.02011  181 GLY A CA  
1275 C C   . GLY A 174 ? 0.75957 0.74781 0.76905 -0.03272 -0.07001 0.01803  181 GLY A C   
1276 O O   . GLY A 174 ? 0.73202 0.72220 0.72311 -0.03104 -0.06746 0.01232  181 GLY A O   
1277 N N   . ARG A 175 ? 0.73737 0.71368 0.75601 -0.01771 -0.05466 0.02367  182 ARG A N   
1278 C CA  . ARG A 175 ? 0.67624 0.63215 0.68193 -0.00113 -0.03788 0.01888  182 ARG A CA  
1279 C C   . ARG A 175 ? 0.74106 0.67940 0.74908 0.01398  -0.02730 0.01861  182 ARG A C   
1280 O O   . ARG A 175 ? 0.85964 0.81540 0.88550 0.02037  -0.02518 0.03789  182 ARG A O   
1281 C CB  . ARG A 175 ? 0.70449 0.67645 0.71515 0.00876  -0.03015 0.04091  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.68545 0.63294 0.68351 0.01807  -0.02026 0.03328  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.71588 0.66476 0.72168 0.03565  -0.00831 0.05591  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.70154 0.65468 0.71475 0.05225  0.00004  0.07167  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.68924 0.67926 0.72228 0.05644  0.00224  0.10158  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.68899 0.71350 0.73432 0.04314  -0.00607 0.11668  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.66849 0.66504 0.70941 0.07598  0.01314  0.11968  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.68550 0.59308 0.67637 0.02029  -0.02157 -0.00040 183 GLY A N   
1289 C CA  . GLY A 176 ? 0.71235 0.60080 0.69627 0.03681  -0.01327 -0.00368 183 GLY A CA  
1290 C C   . GLY A 176 ? 0.71129 0.58017 0.68646 0.02999  -0.01703 -0.02607 183 GLY A C   
1291 O O   . GLY A 176 ? 0.64491 0.50850 0.61619 0.01671  -0.02253 -0.03939 183 GLY A O   
1292 N N   . THR A 177 ? 0.74890 0.61119 0.72113 0.04202  -0.01242 -0.02688 184 THR A N   
1293 C CA  . THR A 177 ? 0.66679 0.51433 0.63279 0.03808  -0.01500 -0.04403 184 THR A CA  
1294 C C   . THR A 177 ? 0.69340 0.55492 0.67088 0.04627  -0.01109 -0.03449 184 THR A C   
1295 O O   . THR A 177 ? 0.59262 0.46375 0.56900 0.06577  -0.00269 -0.01834 184 THR A O   
1296 C CB  . THR A 177 ? 0.64400 0.46111 0.58733 0.04676  -0.01538 -0.05728 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.74706 0.55496 0.68999 0.03584  -0.02007 -0.06166 184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.63045 0.43925 0.56977 0.04422  -0.01867 -0.06986 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.64969 0.51366 0.63933 0.03400  -0.01552 -0.04161 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.59292 0.47127 0.60041 0.03966  -0.01230 -0.03020 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.68877 0.55364 0.68565 0.04242  -0.01095 -0.04442 185 LYS A C   
1302 O O   . LYS A 178 ? 0.76221 0.61673 0.76041 0.02858  -0.01553 -0.05856 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.64290 0.53476 0.68113 0.02147  -0.02107 -0.02230 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.67011 0.57778 0.73731 0.02471  -0.01902 -0.00551 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.68781 0.59455 0.78407 0.00238  -0.03319 -0.00420 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.78946 0.71166 0.90165 -0.00930 -0.04485 0.01076  185 LYS A CE  
1307 N NZ  . LYS A 178 ? 1.02857 0.97052 1.18857 -0.02014 -0.05561 0.03765  185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.61615 0.48344 0.60066 0.06261  -0.00427 -0.03900 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.70922 0.56831 0.68190 0.06677  -0.00491 -0.04961 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.66571 0.55000 0.66256 0.07397  0.00156  -0.03182 186 VAL A C   
1311 O O   . VAL A 179 ? 0.66339 0.56744 0.66183 0.09409  0.01006  -0.01218 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.60400 0.44323 0.53767 0.08497  -0.00619 -0.05954 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.67476 0.50989 0.59694 0.08726  -0.01096 -0.06857 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.61451 0.42719 0.53292 0.07593  -0.01388 -0.07326 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.56968 0.45485 0.58694 0.06020  -0.00077 -0.03545 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.64689 0.55399 0.69518 0.06404  0.00460  -0.01672 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.62290 0.53274 0.65860 0.07374  0.00730  -0.02083 187 ILE A C   
1318 O O   . ILE A 180 ? 0.62163 0.51714 0.65208 0.06256  0.00284  -0.03634 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.60587 0.50708 0.68749 0.04296  -0.00085 -0.01697 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.68560 0.58600 0.77759 0.03147  -0.00843 -0.01265 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.53616 0.45591 0.65563 0.04607  0.00369  0.00432  187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.68940 0.56427 0.77095 0.01272  -0.01801 -0.03544 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.67975 0.61233 0.71091 0.09622  0.01491  -0.00385 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.60135 0.54192 0.61664 0.10803  0.01574  -0.00537 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.64294 0.61180 0.70150 0.10885  0.02386  0.01838  188 LEU A C   
1326 O O   . LEU A 181 ? 0.65111 0.64939 0.73167 0.12363  0.03322  0.04618  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.59820 0.54371 0.57032 0.13724  0.01837  -0.00399 188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.76918 0.68343 0.70046 0.14179  0.01212  -0.02317 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.71546 0.64074 0.61695 0.17730  0.02277  -0.01038 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.75845 0.64058 0.65612 0.13227  -0.00439 -0.05097 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.66003 0.62204 0.73436 0.09462  0.02146  0.01137  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.59875 0.58429 0.71296 0.09737  0.02954  0.03366  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.68917 0.70203 0.78263 0.11917  0.03312  0.04353  189 HIS A C   
1334 O O   . HIS A 182 ? 0.67395 0.68294 0.74981 0.11620  0.02727  0.03166  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.65084 0.61660 0.78561 0.07878  0.02797  0.02298  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.66538 0.60264 0.81350 0.06070  0.02309  0.01164  189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.68538 0.62138 0.87432 0.05391  0.02300  0.02671  189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.58932 0.49881 0.71439 0.04818  0.01600  -0.01237 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.68396 0.58938 0.86866 0.03771  0.01398  0.00871  189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.61136 0.50308 0.75667 0.03567  0.01154  -0.01428 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.69028 0.73414 0.78536 0.14239  0.04212  0.06779  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.62202 0.69098 0.68223 0.16938  0.04475  0.07457  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.72673 0.82158 0.81174 0.16991  0.04820  0.08964  190 LEU A C   
1344 O O   . LEU A 183 ? 0.66919 0.77010 0.80813 0.15655  0.05440  0.10536  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.59282 0.69554 0.65193 0.19961  0.05827  0.10335  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.60096 0.68609 0.63369 0.20709  0.05845  0.09530  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.62059 0.74727 0.64802 0.24531  0.07550  0.12919  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.70663 0.74771 0.67487 0.20536  0.04382  0.05449  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.75697 0.85390 1.00448 0.17906  -0.07124 0.25640  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.63779 0.75784 0.90510 0.20988  -0.09745 0.29331  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.69415 0.74838 0.90982 0.20899  -0.10481 0.32833  191 LYS A C   
1352 O O   . LYS A 184 ? 0.81035 0.82453 0.98071 0.17684  -0.09101 0.32229  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.60718 0.82352 0.89148 0.19978  -0.12638 0.29689  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.54729 0.83600 0.89920 0.19750  -0.11831 0.26998  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.53896 0.91585 0.90502 0.16986  -0.14801 0.26296  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.53506 0.96675 0.96087 0.14686  -0.13003 0.23261  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.49688 1.00661 0.94098 0.11103  -0.16118 0.21901  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.73152 0.77644 0.95642 0.24560  -0.12497 0.36698  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.86125 0.82963 1.02922 0.24053  -0.12599 0.39830  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.93578 0.93380 1.04297 0.20989  -0.13674 0.42286  192 GLU A C   
1361 O O   . GLU A 185 ? 1.01450 0.95475 1.07389 0.18658  -0.12076 0.44195  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.90530 0.85055 1.07775 0.28212  -0.14480 0.41797  192 GLU A CB  
1363 C CG  . GLU A 185 ? 1.06591 0.93091 1.17509 0.27858  -0.14794 0.45815  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.27514 1.18212 1.35064 0.29887  -0.18265 0.49190  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.24518 1.20416 1.36216 0.33705  -0.20779 0.48621  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.36646 1.25852 1.37344 0.27734  -0.18460 0.52265  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.87398 0.96442 0.98116 0.20622  -0.16203 0.41762  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.83986 0.96269 0.87600 0.18005  -0.17460 0.42787  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.81656 0.95706 0.83366 0.13657  -0.15430 0.37940  193 ASP A C   
1370 O O   . ASP A 186 ? 0.87256 1.04872 0.83309 0.11681  -0.16433 0.37442  193 ASP A O   
1371 C CB  . ASP A 186 ? 1.00649 1.21307 1.04207 0.19893  -0.21936 0.43624  193 ASP A CB  
1372 C CG  . ASP A 186 ? 1.03029 1.31734 1.14919 0.20317  -0.23345 0.40038  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 1.00626 1.29344 1.19242 0.23542  -0.23081 0.40021  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.95271 1.29339 1.06666 0.16980  -0.24063 0.36244  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.81199 0.92571 0.86873 0.12597  -0.12712 0.34300  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.75598 0.87802 0.79681 0.09296  -0.10872 0.29931  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.78302 0.84325 0.81403 0.07880  -0.07621 0.29132  194 GLN A C   
1378 O O   . GLN A 187 ? 0.75677 0.81221 0.79671 0.06513  -0.05934 0.25340  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.65847 0.81522 0.75145 0.09155  -0.10871 0.26175  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.70639 0.93865 0.82985 0.09856  -0.14151 0.26406  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.63453 0.90771 0.70351 0.07718  -0.16652 0.25753  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.70134 0.95628 0.72412 0.05178  -0.15286 0.23167  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.66452 0.99561 0.73657 0.09173  -0.20541 0.27822  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.79307 0.80585 0.80756 0.08116  -0.06873 0.32807  195 THR A N   
1385 C CA  . THR A 188 ? 0.70983 0.67070 0.72818 0.06220  -0.04114 0.32050  195 THR A CA  
1386 C C   . THR A 188 ? 0.74178 0.72804 0.72098 0.03149  -0.02333 0.30776  195 THR A C   
1387 O O   . THR A 188 ? 0.77225 0.73488 0.76496 0.01275  -0.00131 0.29644  195 THR A O   
1388 C CB  . THR A 188 ? 0.80974 0.70368 0.82998 0.06872  -0.03742 0.36570  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.92083 0.82568 0.88791 0.06748  -0.04496 0.41485  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.80046 0.66134 0.86391 0.10697  -0.05157 0.37088  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.74950 0.78749 0.68347 0.02730  -0.03322 0.30536  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.76953 0.83464 0.66346 0.00544  -0.01333 0.28823  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.71943 0.78997 0.64052 -0.00041 -0.00100 0.23562  196 GLU A C   
1394 O O   . GLU A 189 ? 0.83238 0.91805 0.74133 -0.01390 0.02101  0.21981  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.87115 0.98466 0.70187 0.00709  -0.03031 0.28986  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.73648 0.87977 0.57553 0.01046  -0.05120 0.24413  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.96112 1.14911 0.74645 0.01299  -0.08098 0.24588  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 1.08795 1.28759 0.86727 0.02764  -0.10622 0.28407  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 1.03295 1.24291 0.78043 0.00310  -0.08201 0.20669  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.72816 0.78954 0.68530 0.01215  -0.01291 0.21103  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.65093 0.70827 0.62458 0.01188  -0.00318 0.16787  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.65631 0.68228 0.66530 0.01184  0.01076  0.16008  197 TYR A C   
1403 O O   . TYR A 190 ? 0.64632 0.66519 0.66796 0.01866  0.01436  0.12799  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.66958 0.72941 0.66132 0.02211  -0.01723 0.15031  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.76638 0.86245 0.73278 0.01609  -0.03686 0.14968  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.74636 0.85661 0.67016 0.00498  -0.03577 0.12311  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.79462 0.91357 0.78102 0.02383  -0.05921 0.17187  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.80444 0.94478 0.70124 -0.00310 -0.05839 0.11476  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.87821 1.03959 0.84550 0.01597  -0.08413 0.16663  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.86003 1.02907 0.77988 0.00004  -0.08461 0.13624  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.82465 1.03263 0.72184 -0.01023 -0.11381 0.12339  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.70732 0.71053 0.72965 0.00384  0.01651  0.18870  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.67234 0.64911 0.72985 -0.00523 0.02700  0.17720  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.69461 0.69844 0.75202 -0.03193 0.04726  0.18287  198 LEU A C   
1415 O O   . LEU A 191 ? 0.76204 0.75815 0.85833 -0.04645 0.05463  0.16948  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.70131 0.62131 0.78408 0.00076  0.02063  0.20013  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.69667 0.59752 0.78997 0.03168  0.00612  0.19451  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.69788 0.53895 0.81208 0.04384  0.00141  0.21858  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.70729 0.60969 0.81096 0.04347  0.00715  0.15043  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.69722 0.73872 0.71324 -0.03919 0.05675  0.19996  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.79407 0.87379 0.80797 -0.06301 0.08390  0.20770  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.75866 0.88728 0.78172 -0.05623 0.09244  0.16069  199 GLU A C   
1423 O O   . GLU A 192 ? 0.71069 0.84555 0.70694 -0.03459 0.08060  0.13329  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.88977 0.99026 0.84160 -0.06783 0.09304  0.24591  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.91788 0.97200 0.86023 -0.07714 0.09248  0.30419  199 GLU A CG  
1426 C CD  . GLU A 192 ? 1.11127 1.17315 1.05760 -0.11117 0.12833  0.33909  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 1.24880 1.35753 1.14180 -0.11760 0.15014  0.35603  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 1.09812 1.11945 1.10048 -0.13339 0.13627  0.34808  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.77017 0.93376 0.83568 -0.07505 0.11300  0.15216  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.70125 0.91400 0.78843 -0.06099 0.11731  0.10658  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.72701 0.98130 0.76121 -0.04433 0.13053  0.09304  200 GLU A C   
1432 O O   . GLU A 193 ? 0.74009 1.00377 0.76848 -0.01731 0.12305  0.05402  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.66875 0.92731 0.82596 -0.08672 0.13489  0.10057  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.72366 1.05086 0.88138 -0.10881 0.17451  0.11957  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.76746 1.13953 1.01062 -0.14682 0.19326  0.12189  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.62974 0.97721 0.92876 -0.15433 0.16926  0.10213  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.87267 1.30777 1.12736 -0.17098 0.23271  0.14193  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.76338 1.03579 0.75104 -0.05709 0.14936  0.12402  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.76597 1.07609 0.69392 -0.03990 0.16190  0.10462  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.77326 1.04163 0.64260 -0.02127 0.13223  0.09315  201 ARG A C   
1441 O O   . ARG A 194 ? 0.86086 1.14195 0.68775 -0.00249 0.13295  0.05886  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.76917 1.12329 0.65992 -0.05960 0.19697  0.14028  201 ARG A CB  
1443 C CG  . ARG A 194 ? 1.00479 1.31963 0.84063 -0.07134 0.18625  0.19196  201 ARG A CG  
1444 C CD  . ARG A 194 ? 1.10011 1.44860 0.91150 -0.09702 0.22664  0.24070  201 ARG A CD  
1445 N NE  . ARG A 194 ? 1.33651 1.64212 1.08759 -0.10197 0.21379  0.29654  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 1.39558 1.70677 1.11159 -0.12366 0.24456  0.35461  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 1.36594 1.73023 1.10737 -0.14901 0.29506  0.36488  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 1.52356 1.78915 1.17936 -0.11891 0.22523  0.40636  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.81665 1.03715 0.68824 -0.02613 0.10633  0.11811  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.83249 1.02619 0.66741 -0.01361 0.07705  0.10599  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.82229 0.98871 0.68314 0.00268  0.06442  0.06518  202 ARG A C   
1452 O O   . ARG A 195 ? 0.83830 0.99515 0.66578 0.01243  0.05449  0.03538  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.77896 0.94391 0.61891 -0.01934 0.05538  0.14663  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.77102 0.92764 0.58712 -0.01092 0.02385  0.13651  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.90838 1.09693 0.65086 -0.01128 0.01873  0.12700  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.96054 1.15137 0.68724 -0.00989 -0.01802 0.12542  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.94458 1.13543 0.65397 -0.01120 -0.03548 0.08258  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.99754 1.17474 0.69415 -0.00785 -0.01930 0.03898  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.86351 1.06786 0.57283 -0.01576 -0.07127 0.08271  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.81967 0.96751 0.73484 0.00530  0.06410  0.06345  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.72246 0.84237 0.65192 0.02418  0.05484  0.03108  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.76467 0.90463 0.67823 0.04194  0.06720  -0.00473 203 ILE A C   
1463 O O   . ILE A 196 ? 0.75969 0.86612 0.65526 0.05946  0.05901  -0.03074 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.68451 0.78590 0.66376 0.02688  0.05070  0.03453  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.68480 0.76891 0.68249 0.01157  0.04504  0.07001  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.73839 0.80046 0.71573 0.04727  0.03891  0.01391  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.64938 0.70626 0.68825 0.01530  0.03908  0.06623  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.78259 0.97594 0.70466 0.03891  0.08951  -0.00547 204 LYS A N   
1469 C CA  . LYS A 197 ? 0.68476 0.90709 0.59528 0.06308  0.10414  -0.04151 204 LYS A CA  
1470 C C   . LYS A 197 ? 0.78854 0.98894 0.63107 0.07215  0.10108  -0.06260 204 LYS A C   
1471 O O   . LYS A 197 ? 0.88189 1.04734 0.70689 0.09698  0.09501  -0.09674 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.65792 0.95772 0.59729 0.05447  0.13462  -0.03524 204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.63392 0.96591 0.65183 0.05233  0.13537  -0.03731 204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.65191 1.07459 0.70789 0.05756  0.16609  -0.05217 204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.57504 1.04634 0.70739 0.02132  0.17723  -0.02964 204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.67876 1.14629 0.78898 -0.01938 0.19799  0.01700  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.73225 0.94673 0.53190 0.05277  0.10244  -0.04302 205 GLU A N   
1478 C CA  . GLU A 198 ? 0.86676 1.06492 0.59713 0.05820  0.09410  -0.06894 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.94243 1.07235 0.67001 0.05955  0.06520  -0.08817 205 GLU A C   
1480 O O   . GLU A 198 ? 1.08294 1.17921 0.77369 0.07264  0.06067  -0.12818 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.96644 1.19176 0.64910 0.03753  0.09120  -0.03848 205 GLU A CB  
1482 C CG  . GLU A 198 ? 1.14426 1.33895 0.77786 0.03053  0.05800  -0.05265 205 GLU A CG  
1483 C CD  . GLU A 198 ? 1.31746 1.55002 0.87910 0.02244  0.05501  -0.03635 205 GLU A CD  
1484 O OE1 . GLU A 198 ? 1.31283 1.58574 0.86677 0.01765  0.07985  0.00198  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 1.35002 1.57121 0.86071 0.01936  0.02702  -0.06129 205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.89769 1.00380 0.66519 0.04571  0.04848  -0.06083 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.90862 0.95945 0.68029 0.04099  0.02737  -0.07237 206 ILE A CA  
1488 C C   . ILE A 199 ? 1.02327 1.02644 0.80374 0.06473  0.03401  -0.09878 206 ILE A C   
1489 O O   . ILE A 199 ? 1.18073 1.12910 0.93967 0.06525  0.02539  -0.12300 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.89139 0.94043 0.70579 0.02541  0.01430  -0.03551 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.89800 0.98773 0.69911 0.00945  0.00360  -0.00622 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.95002 0.95409 0.77772 0.01739  0.00012  -0.04436 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.81773 0.90954 0.66477 0.00419  -0.00447 0.03229  206 ILE A CD1 
1494 N N   . VAL A 200 ? 1.00129 1.02222 0.81325 0.08443  0.04730  -0.09412 207 VAL A N   
1495 C CA  . VAL A 200 ? 1.02234 1.00057 0.83961 0.11434  0.04876  -0.11343 207 VAL A CA  
1496 C C   . VAL A 200 ? 1.16891 1.13261 0.94874 0.14084  0.05733  -0.15288 207 VAL A C   
1497 O O   . VAL A 200 ? 1.24992 1.14169 1.00654 0.15700  0.05187  -0.17254 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.84132 0.85409 0.70458 0.12946  0.05312  -0.10159 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.98765 0.96900 0.84819 0.17003  0.05138  -0.12269 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.75845 0.76036 0.64905 0.11072  0.04323  -0.07145 207 VAL A CG2 
1501 N N   . LYS A 201 ? 1.13417 1.16139 0.90538 0.14703  0.07393  -0.16439 208 LYS A N   
1502 C CA  . LYS A 201 ? 1.13694 1.15656 0.87238 0.17999  0.08615  -0.20689 208 LYS A CA  
1503 C C   . LYS A 201 ? 1.22347 1.18513 0.89664 0.16797  0.07522  -0.23438 208 LYS A C   
1504 O O   . LYS A 201 ? 1.36130 1.28079 0.99823 0.19732  0.07995  -0.27615 208 LYS A O   
1505 C CB  . LYS A 201 ? 1.02924 1.14462 0.77334 0.19000  0.11397  -0.21187 208 LYS A CB  
1506 C CG  . LYS A 201 ? 1.13117 1.32154 0.94319 0.17771  0.12401  -0.17855 208 LYS A CG  
1507 C CD  . LYS A 201 ? 1.09414 1.26727 0.95805 0.19751  0.10957  -0.17526 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.97666 1.23608 0.91143 0.18807  0.11986  -0.15832 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.93694 1.17180 0.91081 0.18814  0.09604  -0.14499 208 LYS A NZ  
1510 N N   . LYS A 202 ? 1.27299 1.23209 0.93552 0.12733  0.05815  -0.21518 209 LYS A N   
1511 C CA  . LYS A 202 ? 1.31809 1.23279 0.92902 0.10904  0.04034  -0.24443 209 LYS A CA  
1512 C C   . LYS A 202 ? 1.37184 1.20038 0.99706 0.09128  0.02076  -0.24620 209 LYS A C   
1513 O O   . LYS A 202 ? 1.47099 1.23251 1.05985 0.08702  0.01048  -0.28491 209 LYS A O   
1514 C CB  . LYS A 202 ? 1.26877 1.24256 0.85992 0.07698  0.02854  -0.22398 209 LYS A CB  
1515 C CG  . LYS A 202 ? 1.40168 1.34224 0.97708 0.04270  -0.00491 -0.23424 209 LYS A CG  
1516 C CD  . LYS A 202 ? 1.36131 1.36731 0.90034 0.02389  -0.02019 -0.22076 209 LYS A CD  
1517 C CE  . LYS A 202 ? 1.36222 1.34624 0.87606 -0.00533 -0.05850 -0.24972 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 1.40590 1.45758 0.87061 -0.01545 -0.07875 -0.23900 209 LYS A NZ  
1519 N N   . HIS A 203 ? 1.41753 1.24338 1.09364 0.07995  0.01805  -0.20656 210 HIS A N   
1520 C CA  . HIS A 203 ? 1.48360 1.24162 1.17749 0.05730  0.00638  -0.19910 210 HIS A CA  
1521 C C   . HIS A 203 ? 1.47321 1.16658 1.17835 0.08460  0.01816  -0.19020 210 HIS A C   
1522 O O   . HIS A 203 ? 1.49555 1.10494 1.19167 0.07449  0.01572  -0.19663 210 HIS A O   
1523 C CB  . HIS A 203 ? 1.36329 1.16823 1.10104 0.02420  -0.00444 -0.15978 210 HIS A CB  
1524 C CG  . HIS A 203 ? 1.34094 1.18706 1.06741 -0.00762 -0.02666 -0.16738 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 1.36577 1.17273 1.07163 -0.03326 -0.04542 -0.20195 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 1.19507 1.11621 0.92591 -0.01689 -0.03659 -0.14458 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 1.31538 1.18221 1.01350 -0.05555 -0.06948 -0.20297 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 1.25738 1.19194 0.96718 -0.04330 -0.06382 -0.16513 210 HIS A NE2 
1529 N N   . SER A 204 ? 1.84980 1.00890 1.43721 -0.17986 -0.55000 0.04201  211 SER A N   
1530 C CA  . SER A 204 ? 1.77706 0.98919 1.42733 -0.15001 -0.47552 0.04080  211 SER A CA  
1531 C C   . SER A 204 ? 1.84113 1.02952 1.35037 -0.08321 -0.40706 0.00935  211 SER A C   
1532 O O   . SER A 204 ? 1.78801 1.08182 1.35007 -0.04861 -0.33360 0.01376  211 SER A O   
1533 C CB  . SER A 204 ? 1.70511 1.07829 1.54978 -0.15527 -0.43194 0.07163  211 SER A CB  
1534 O OG  . SER A 204 ? 1.54679 0.95659 1.53829 -0.20612 -0.47998 0.10943  211 SER A OG  
1535 N N   . GLN A 205 ? 1.83363 0.88131 1.15708 -0.06477 -0.43074 -0.02096 212 GLN A N   
1536 C CA  . GLN A 205 ? 1.92120 0.93905 1.10476 0.00521  -0.36483 -0.04432 212 GLN A CA  
1537 C C   . GLN A 205 ? 1.92901 0.89404 1.08942 0.03393  -0.32301 -0.05003 212 GLN A C   
1538 O O   . GLN A 205 ? 1.98393 0.95091 1.06050 0.09730  -0.25704 -0.05735 212 GLN A O   
1539 C CB  . GLN A 205 ? 1.96343 0.84913 0.94494 0.02233  -0.39822 -0.07437 212 GLN A CB  
1540 C CG  . GLN A 205 ? 2.17801 0.90831 1.07007 -0.00572 -0.45472 -0.08884 212 GLN A CG  
1541 C CD  . GLN A 205 ? 2.11722 0.86307 1.12469 -0.08518 -0.53762 -0.06285 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 1.99428 0.85168 1.16889 -0.12084 -0.55217 -0.03452 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 2.09546 0.73650 1.01893 -0.11012 -0.58673 -0.06765 212 GLN A NE2 
1544 N N   . PHE A 206 ? 1.87969 0.80360 1.11895 -0.01016 -0.35902 -0.03936 213 PHE A N   
1545 C CA  . PHE A 206 ? 1.82465 0.68773 1.04924 0.01126  -0.32670 -0.03835 213 PHE A CA  
1546 C C   . PHE A 206 ? 1.65802 0.65130 1.07493 -0.01337 -0.30249 -0.00009 213 PHE A C   
1547 O O   . PHE A 206 ? 1.48684 0.42750 0.94872 -0.03736 -0.31877 0.01421  213 PHE A O   
1548 C CB  . PHE A 206 ? 1.91282 0.62646 1.04890 -0.01682 -0.38314 -0.05633 213 PHE A CB  
1549 C CG  . PHE A 206 ? 2.17973 0.78331 1.12379 0.00980  -0.39779 -0.08999 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 2.26378 0.85294 1.08605 0.08514  -0.33237 -0.10621 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 2.26766 0.79564 1.15928 -0.03746 -0.47166 -0.09655 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 2.45853 0.96555 1.12202 0.11334  -0.33556 -0.12561 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 2.34872 0.77639 1.06632 -0.01181 -0.47885 -0.12094 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 2.52948 0.94809 1.13801 0.06442  -0.40820 -0.13495 213 PHE A CZ  
1555 N N   . ILE A 207 ? 1.50365 0.66401 1.03162 -0.00863 -0.26218 0.01711  214 ILE A N   
1556 C CA  . ILE A 207 ? 1.21977 0.51101 0.91281 -0.02434 -0.22670 0.04892  214 ILE A CA  
1557 C C   . ILE A 207 ? 1.11652 0.47245 0.78510 0.02990  -0.14568 0.05479  214 ILE A C   
1558 O O   . ILE A 207 ? 1.20576 0.59758 0.79754 0.07347  -0.10534 0.04306  214 ILE A O   
1559 C CB  . ILE A 207 ? 1.18610 0.60964 1.00713 -0.05068 -0.22594 0.06107  214 ILE A CB  
1560 C CG1 . ILE A 207 ? 1.21312 0.58180 1.06460 -0.10215 -0.30899 0.06639  214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.95946 0.51124 0.93431 -0.06204 -0.18089 0.08890  214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 1.05996 0.46158 1.06863 -0.15393 -0.34201 0.10319  214 ILE A CD1 
1563 N N   . GLY A 208 ? 1.04698 0.42663 0.78625 0.02558  -0.12334 0.08037  215 GLY A N   
1564 C CA  . GLY A 208 ? 1.01239 0.45257 0.73144 0.07381  -0.05285 0.09562  215 GLY A CA  
1565 C C   . GLY A 208 ? 0.87510 0.49786 0.68111 0.07757  0.00243  0.10912  215 GLY A C   
1566 O O   . GLY A 208 ? 0.91962 0.62341 0.76030 0.09474  0.05143  0.13471  215 GLY A O   
1567 N N   . TYR A 209 ? 0.84098 0.52552 0.67848 0.05956  -0.00608 0.09300  216 TYR A N   
1568 C CA  . TYR A 209 ? 0.70704 0.54452 0.61349 0.05700  0.04214  0.09680  216 TYR A CA  
1569 C C   . TYR A 209 ? 0.73098 0.58509 0.59390 0.06213  0.03681  0.07435  216 TYR A C   
1570 O O   . TYR A 209 ? 0.74922 0.51882 0.57954 0.05055  -0.01304 0.06049  216 TYR A O   
1571 C CB  . TYR A 209 ? 0.66254 0.57234 0.71329 0.01432  0.04175  0.10952  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.62103 0.53118 0.72736 0.00661  0.04990  0.14031  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.54434 0.54736 0.66045 0.02489  0.10634  0.16050  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.69415 0.51618 0.84490 -0.02295 -0.00226 0.15494  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.55941 0.56766 0.72924 0.01854  0.11500  0.19564  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.67039 0.49365 0.87909 -0.03270 0.00446  0.18959  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.62140 0.53787 0.83990 -0.00951 0.06539  0.21043  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.67983 0.60267 0.95922 -0.01858 0.07335  0.25162  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.73786 0.70052 0.59816 0.07528  0.08365  0.07408  217 PRO A N   
1580 C CA  . PRO A 210 ? 0.63436 0.61421 0.45562 0.07922  0.07976  0.05912  217 PRO A CA  
1581 C C   . PRO A 210 ? 0.64433 0.63095 0.55439 0.03914  0.05053  0.04768  217 PRO A C   
1582 O O   . PRO A 210 ? 0.66739 0.71993 0.68123 0.01276  0.06852  0.04883  217 PRO A O   
1583 C CB  . PRO A 210 ? 0.55833 0.66308 0.37632 0.09099  0.13506  0.06815  217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.62285 0.79342 0.50897 0.07767  0.16396  0.08126  217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.69524 0.77064 0.58302 0.08345  0.13855  0.09183  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.63175 0.55015 0.49825 0.03806  0.00838  0.03976  218 ILE A N   
1587 C CA  . ILE A 211 ? 0.61531 0.53966 0.56314 0.00586  -0.02153 0.03763  218 ILE A CA  
1588 C C   . ILE A 211 ? 0.69577 0.67053 0.61697 0.01376  -0.00208 0.03238  218 ILE A C   
1589 O O   . ILE A 211 ? 0.79777 0.73097 0.62055 0.03519  -0.01802 0.03286  218 ILE A O   
1590 C CB  . ILE A 211 ? 0.74600 0.56369 0.67193 -0.00926 -0.09176 0.04118  218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.73404 0.49495 0.68237 -0.02263 -0.11498 0.04960  218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.70227 0.54250 0.72958 -0.04055 -0.12140 0.05106  218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.80963 0.44504 0.69361 -0.03892 -0.18861 0.04881  218 ILE A CD1 
1594 N N   . THR A 212 ? 0.66246 0.72214 0.66663 -0.00418 0.03366  0.02779  219 THR A N   
1595 C CA  . THR A 212 ? 0.60008 0.71047 0.59003 -0.00484 0.05422  0.02436  219 THR A CA  
1596 C C   . THR A 212 ? 0.58787 0.68428 0.65940 -0.02848 0.03052  0.02578  219 THR A C   
1597 O O   . THR A 212 ? 0.61425 0.72216 0.79278 -0.04888 0.03632  0.02328  219 THR A O   
1598 C CB  . THR A 212 ? 0.60084 0.80568 0.61300 -0.01375 0.10910  0.01569  219 THR A CB  
1599 O OG1 . THR A 212 ? 0.70292 0.93168 0.64738 0.01057  0.13019  0.02520  219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.54040 0.79193 0.53843 -0.02300 0.12417  0.01439  219 THR A CG2 
1601 N N   . LEU A 213 ? 0.64002 0.71538 0.66432 -0.02202 0.00753  0.03540  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.55454 0.61986 0.65470 -0.04108 -0.01518 0.04572  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.55446 0.67915 0.68786 -0.05303 0.02574  0.03911  220 LEU A C   
1604 O O   . LEU A 213 ? 0.65684 0.81083 0.71625 -0.04343 0.03886  0.04426  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.53968 0.54690 0.56722 -0.03084 -0.06785 0.06486  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.63704 0.62982 0.72863 -0.04726 -0.10468 0.08876  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.60788 0.64497 0.71515 -0.04973 -0.07879 0.09792  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.62508 0.62019 0.86050 -0.07002 -0.11346 0.09608  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.49160 0.63134 0.73559 -0.07412 0.04756  0.02930  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.47894 0.65343 0.75544 -0.09221 0.08511  0.01635  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.57257 0.72046 0.88157 -0.09658 0.05899  0.04061  221 PHE A C   
1612 O O   . PHE A 214 ? 0.60001 0.71587 0.99764 -0.09900 0.03895  0.05615  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.54842 0.73461 0.91606 -0.10793 0.12686  -0.00928 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.52557 0.75657 0.84719 -0.11014 0.16263  -0.03321 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.57991 0.80237 0.89320 -0.11243 0.18311  -0.05426 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.52751 0.77914 0.77107 -0.09428 0.15341  -0.02467 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.54530 0.78887 0.79574 -0.10551 0.19061  -0.06083 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.47131 0.74510 0.66374 -0.08410 0.16755  -0.02860 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.45767 0.72450 0.65491 -0.08900 0.17872  -0.04177 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.55160 0.72079 0.79703 -0.09719 0.05920  0.05202  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.60580 0.75698 0.87821 -0.10174 0.03613  0.08192  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.57625 0.72849 0.93626 -0.12892 0.07055  0.06903  222 VAL A C   
1623 O O   . VAL A 215 ? 0.60126 0.77775 0.95819 -0.14741 0.11136  0.03552  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.61069 0.78643 0.77606 -0.08758 0.02243  0.10782  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.70128 0.86746 0.76008 -0.05666 0.00655  0.10693  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.60162 0.83543 0.74829 -0.10624 0.05988  0.10211  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.55127 0.67154 0.98642 -0.13248 0.05344  0.09628  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.67278 0.77144 1.19511 -0.15439 0.08600  0.08671  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.63182 0.74562 1.12153 -0.17202 0.08342  0.10880  223 GLU A C   
1630 O O   . GLU A 216 ? 0.65466 0.79482 1.07671 -0.16007 0.05191  0.14503  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.72504 0.77979 1.36547 -0.14287 0.07385  0.11106  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.58523 0.63819 1.25840 -0.12428 0.05352  0.11592  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.65303 0.68114 1.42647 -0.10473 0.03209  0.15182  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.62811 0.63382 1.46920 -0.09314 0.06869  0.14032  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.69983 0.73315 1.48746 -0.10233 -0.02253 0.19440  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.52080 0.61312 1.05129 -0.20006 0.11760  0.08620  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.62375 0.72796 1.13507 -0.22586 0.11567  0.10787  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.80957 0.84865 1.39356 -0.22461 0.11422  0.12135  224 LYS A C   
1639 O O   . LYS A 217 ? 0.80583 0.84577 1.42030 -0.21495 0.08534  0.17524  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.65624 0.78905 1.10346 -0.26015 0.14251  0.06811  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.67454 0.83458 1.07262 -0.25097 0.15960  0.02659  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.71629 0.81974 1.13294 -0.25585 0.18921  -0.02605 224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.72314 0.86000 1.06348 -0.28118 0.20410  -0.05971 224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.70724 0.86733 1.00939 -0.26103 0.21730  -0.08775 224 LYS A NZ  
# 
