data_7HBJ
# 
_entry.id   7HBJ 
# 
_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   7HBJ         pdb_00007hbj 10.2210/pdb7hbj/pdb 
WWPDB D_1001407265 ?            ?                   
# 
_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                        7HBJ 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, L.' 1  ? 
'Wang, W.'  2  ? 
'Zhu, Z.'   3  ? 
'Li, Q.'    4  ? 
'Li, M.'    5  ? 
'Zhou, H.'  6  ? 
'Xu, Q.'    7  ? 
'Wen, W.'   8  ? 
'Wang, Q.'  9  ? 
'Yu, F.'    10 ? 
# 
_citation.id                        primary 
_citation.title                     
;Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.
;
_citation.journal_abbrev            Iucrj 
_citation.journal_volume            12 
_citation.page_first                177 
_citation.page_last                 187 
_citation.year                      2025 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   39819741 
_citation.pdbx_database_id_DOI      10.1107/S2052252524012247 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Huang, L.' 0009-0001-8431-0182 1  
primary 'Wang, W.'  ?                   2  
primary 'Zhu, Z.'   ?                   3  
primary 'Li, Q.'    ?                   4  
primary 'Li, M.'    ?                   5  
primary 'Zhou, H.'  ?                   6  
primary 'Xu, Q.'    0000-0002-7137-0768 7  
primary 'Wen, W.'   ?                   8  
primary 'Wang, Q.'  ?                   9  
primary 'Yu, F.'    0000-0002-9502-3277 10 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Heat shock protein HSP 90-alpha'             26859.117 1  3.6.4.10 ? ? ? 
2 non-polymer syn '6-(4-chloro-3-methylphenoxy)pyridin-3-amine' 234.682   1  ?        ? ? ? 
3 water       nat water                                         18.015    55 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Heat shock 86 kDa,HSP 86,HSP86,Heat shock protein family C member 1,Lipopolysaccharide-associated protein 2,LAP-2,LPS-associated protein 2,Renal carcinoma antigen NY-REN-38
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '6-(4-chloro-3-methylphenoxy)pyridin-3-amine' A1AYE 
3 water                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   GLN n 
1 4   PRO n 
1 5   MET n 
1 6   GLU n 
1 7   GLU n 
1 8   GLU n 
1 9   GLU n 
1 10  VAL n 
1 11  GLU n 
1 12  THR n 
1 13  PHE n 
1 14  ALA n 
1 15  PHE n 
1 16  GLN n 
1 17  ALA n 
1 18  GLU n 
1 19  ILE n 
1 20  ALA n 
1 21  GLN n 
1 22  LEU n 
1 23  MET n 
1 24  SER n 
1 25  LEU n 
1 26  ILE n 
1 27  ILE n 
1 28  ASN n 
1 29  THR n 
1 30  PHE n 
1 31  TYR n 
1 32  SER n 
1 33  ASN n 
1 34  LYS n 
1 35  GLU n 
1 36  ILE n 
1 37  PHE n 
1 38  LEU n 
1 39  ARG n 
1 40  GLU n 
1 41  LEU n 
1 42  ILE n 
1 43  SER n 
1 44  ASN n 
1 45  SER n 
1 46  SER n 
1 47  ASP n 
1 48  ALA n 
1 49  LEU n 
1 50  ASP n 
1 51  LYS n 
1 52  ILE n 
1 53  ARG n 
1 54  TYR n 
1 55  GLU n 
1 56  SER n 
1 57  LEU n 
1 58  THR n 
1 59  ASP n 
1 60  PRO n 
1 61  SER n 
1 62  LYS n 
1 63  LEU n 
1 64  ASP n 
1 65  SER n 
1 66  GLY n 
1 67  LYS n 
1 68  GLU n 
1 69  LEU n 
1 70  HIS n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ILE n 
1 75  PRO n 
1 76  ASN n 
1 77  LYS n 
1 78  GLN n 
1 79  ASP n 
1 80  ARG n 
1 81  THR n 
1 82  LEU n 
1 83  THR n 
1 84  ILE n 
1 85  VAL n 
1 86  ASP n 
1 87  THR n 
1 88  GLY n 
1 89  ILE n 
1 90  GLY n 
1 91  MET n 
1 92  THR n 
1 93  LYS n 
1 94  ALA n 
1 95  ASP n 
1 96  LEU n 
1 97  ILE n 
1 98  ASN n 
1 99  ASN n 
1 100 LEU n 
1 101 GLY n 
1 102 THR n 
1 103 ILE n 
1 104 ALA n 
1 105 LYS n 
1 106 SER n 
1 107 GLY n 
1 108 THR n 
1 109 LYS n 
1 110 ALA n 
1 111 PHE n 
1 112 MET n 
1 113 GLU n 
1 114 ALA n 
1 115 LEU n 
1 116 GLN n 
1 117 ALA n 
1 118 GLY n 
1 119 ALA n 
1 120 ASP n 
1 121 ILE n 
1 122 SER n 
1 123 MET n 
1 124 ILE n 
1 125 GLY n 
1 126 GLN n 
1 127 PHE n 
1 128 GLY n 
1 129 VAL n 
1 130 GLY n 
1 131 PHE n 
1 132 TYR n 
1 133 SER n 
1 134 ALA n 
1 135 TYR n 
1 136 LEU n 
1 137 VAL n 
1 138 ALA n 
1 139 GLU n 
1 140 LYS n 
1 141 VAL n 
1 142 THR n 
1 143 VAL n 
1 144 ILE n 
1 145 THR n 
1 146 LYS n 
1 147 HIS n 
1 148 ASN n 
1 149 ASP n 
1 150 ASP n 
1 151 GLU n 
1 152 GLN n 
1 153 TYR n 
1 154 ALA n 
1 155 TRP n 
1 156 GLU n 
1 157 SER n 
1 158 SER n 
1 159 ALA n 
1 160 GLY n 
1 161 GLY n 
1 162 SER n 
1 163 PHE n 
1 164 THR n 
1 165 VAL n 
1 166 ARG n 
1 167 THR n 
1 168 ASP n 
1 169 THR n 
1 170 GLY n 
1 171 GLU n 
1 172 PRO n 
1 173 MET n 
1 174 GLY n 
1 175 ARG n 
1 176 GLY n 
1 177 THR n 
1 178 LYS n 
1 179 VAL n 
1 180 ILE n 
1 181 LEU n 
1 182 HIS n 
1 183 LEU n 
1 184 LYS n 
1 185 GLU n 
1 186 ASP n 
1 187 GLN n 
1 188 THR n 
1 189 GLU n 
1 190 TYR n 
1 191 LEU n 
1 192 GLU n 
1 193 GLU n 
1 194 ARG n 
1 195 ARG n 
1 196 ILE n 
1 197 LYS n 
1 198 GLU n 
1 199 ILE n 
1 200 VAL n 
1 201 LYS n 
1 202 LYS n 
1 203 HIS n 
1 204 SER n 
1 205 GLN n 
1 206 PHE n 
1 207 ILE n 
1 208 GLY n 
1 209 TYR n 
1 210 PRO n 
1 211 ILE n 
1 212 THR n 
1 213 LEU n 
1 214 PHE n 
1 215 VAL n 
1 216 GLU n 
1 217 LYS n 
1 218 GLU n 
1 219 ARG n 
1 220 ASP n 
1 221 LYS n 
1 222 GLU n 
1 223 VAL n 
1 224 SER n 
1 225 ASP n 
1 226 ASP n 
1 227 GLU n 
1 228 ALA n 
1 229 GLU n 
1 230 LEU n 
1 231 GLU n 
1 232 HIS n 
1 233 HIS n 
1 234 HIS n 
1 235 HIS n 
1 236 HIS n 
1 237 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   237 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HSP90AA1, HSP90A, HSPC1, HSPCA' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET28 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1AYE non-polymer         . '6-(4-chloro-3-methylphenoxy)pyridin-3-amine' ? 'C12 H11 Cl N2 O' 234.682 
ALA   'L-peptide linking' y ALANINE                                       ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                      ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                    ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                               ? 'C4 H7 N O4'      133.103 
GLN   'L-peptide linking' y GLUTAMINE                                     ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                               ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                       ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                     ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                         ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                    ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                       ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                        ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                    ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                 ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                       ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                        ? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                     ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                    ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                      ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                        ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   8   ?   ?   ?   A . n 
A 1 2   ASP 2   9   ?   ?   ?   A . n 
A 1 3   GLN 3   10  ?   ?   ?   A . n 
A 1 4   PRO 4   11  ?   ?   ?   A . n 
A 1 5   MET 5   12  ?   ?   ?   A . n 
A 1 6   GLU 6   13  ?   ?   ?   A . n 
A 1 7   GLU 7   14  ?   ?   ?   A . n 
A 1 8   GLU 8   15  ?   ?   ?   A . n 
A 1 9   GLU 9   16  16  GLU GLU A . n 
A 1 10  VAL 10  17  17  VAL VAL A . n 
A 1 11  GLU 11  18  18  GLU GLU A . n 
A 1 12  THR 12  19  19  THR THR A . n 
A 1 13  PHE 13  20  20  PHE PHE A . n 
A 1 14  ALA 14  21  21  ALA ALA A . n 
A 1 15  PHE 15  22  22  PHE PHE A . n 
A 1 16  GLN 16  23  23  GLN GLN A . n 
A 1 17  ALA 17  24  24  ALA ALA A . n 
A 1 18  GLU 18  25  25  GLU GLU A . n 
A 1 19  ILE 19  26  26  ILE ILE A . n 
A 1 20  ALA 20  27  27  ALA ALA A . n 
A 1 21  GLN 21  28  28  GLN GLN A . n 
A 1 22  LEU 22  29  29  LEU LEU A . n 
A 1 23  MET 23  30  30  MET MET A . n 
A 1 24  SER 24  31  31  SER SER A . n 
A 1 25  LEU 25  32  32  LEU LEU A . n 
A 1 26  ILE 26  33  33  ILE ILE A . n 
A 1 27  ILE 27  34  34  ILE ILE A . n 
A 1 28  ASN 28  35  35  ASN ASN A . n 
A 1 29  THR 29  36  36  THR THR A . n 
A 1 30  PHE 30  37  37  PHE PHE A . n 
A 1 31  TYR 31  38  38  TYR TYR A . n 
A 1 32  SER 32  39  39  SER SER A . n 
A 1 33  ASN 33  40  40  ASN ASN A . n 
A 1 34  LYS 34  41  41  LYS LYS A . n 
A 1 35  GLU 35  42  42  GLU GLU A . n 
A 1 36  ILE 36  43  43  ILE ILE A . n 
A 1 37  PHE 37  44  44  PHE PHE A . n 
A 1 38  LEU 38  45  45  LEU LEU A . n 
A 1 39  ARG 39  46  46  ARG ARG A . n 
A 1 40  GLU 40  47  47  GLU GLU A . n 
A 1 41  LEU 41  48  48  LEU LEU A . n 
A 1 42  ILE 42  49  49  ILE ILE A . n 
A 1 43  SER 43  50  50  SER SER A . n 
A 1 44  ASN 44  51  51  ASN ASN A . n 
A 1 45  SER 45  52  52  SER SER A . n 
A 1 46  SER 46  53  53  SER SER A . n 
A 1 47  ASP 47  54  54  ASP ASP A . n 
A 1 48  ALA 48  55  55  ALA ALA A . n 
A 1 49  LEU 49  56  56  LEU LEU A . n 
A 1 50  ASP 50  57  57  ASP ASP A . n 
A 1 51  LYS 51  58  58  LYS LYS A . n 
A 1 52  ILE 52  59  59  ILE ILE A . n 
A 1 53  ARG 53  60  60  ARG ARG A . n 
A 1 54  TYR 54  61  61  TYR TYR A . n 
A 1 55  GLU 55  62  62  GLU GLU A . n 
A 1 56  SER 56  63  63  SER SER A . n 
A 1 57  LEU 57  64  64  LEU LEU A . n 
A 1 58  THR 58  65  65  THR THR A . n 
A 1 59  ASP 59  66  66  ASP ASP A . n 
A 1 60  PRO 60  67  67  PRO PRO A . n 
A 1 61  SER 61  68  68  SER SER A . n 
A 1 62  LYS 62  69  69  LYS LYS A . n 
A 1 63  LEU 63  70  70  LEU LEU A . n 
A 1 64  ASP 64  71  71  ASP ASP A . n 
A 1 65  SER 65  72  72  SER SER A . n 
A 1 66  GLY 66  73  73  GLY GLY A . n 
A 1 67  LYS 67  74  74  LYS LYS A . n 
A 1 68  GLU 68  75  75  GLU GLU A . n 
A 1 69  LEU 69  76  76  LEU LEU A . n 
A 1 70  HIS 70  77  77  HIS HIS A . n 
A 1 71  ILE 71  78  78  ILE ILE A . n 
A 1 72  ASN 72  79  79  ASN ASN A . n 
A 1 73  LEU 73  80  80  LEU LEU A . n 
A 1 74  ILE 74  81  81  ILE ILE A . n 
A 1 75  PRO 75  82  82  PRO PRO A . n 
A 1 76  ASN 76  83  83  ASN ASN A . n 
A 1 77  LYS 77  84  84  LYS LYS A . n 
A 1 78  GLN 78  85  85  GLN GLN A . n 
A 1 79  ASP 79  86  86  ASP ASP A . n 
A 1 80  ARG 80  87  87  ARG ARG A . n 
A 1 81  THR 81  88  88  THR THR A . n 
A 1 82  LEU 82  89  89  LEU LEU A . n 
A 1 83  THR 83  90  90  THR THR A . n 
A 1 84  ILE 84  91  91  ILE ILE A . n 
A 1 85  VAL 85  92  92  VAL VAL A . n 
A 1 86  ASP 86  93  93  ASP ASP A . n 
A 1 87  THR 87  94  94  THR THR A . n 
A 1 88  GLY 88  95  95  GLY GLY A . n 
A 1 89  ILE 89  96  96  ILE ILE A . n 
A 1 90  GLY 90  97  97  GLY GLY A . n 
A 1 91  MET 91  98  98  MET MET A . n 
A 1 92  THR 92  99  99  THR THR A . n 
A 1 93  LYS 93  100 100 LYS LYS A . n 
A 1 94  ALA 94  101 101 ALA ALA A . n 
A 1 95  ASP 95  102 102 ASP ASP A . n 
A 1 96  LEU 96  103 103 LEU LEU A . n 
A 1 97  ILE 97  104 104 ILE ILE A . n 
A 1 98  ASN 98  105 105 ASN ASN A . n 
A 1 99  ASN 99  106 106 ASN ASN A . n 
A 1 100 LEU 100 107 107 LEU LEU A . n 
A 1 101 GLY 101 108 108 GLY GLY A . n 
A 1 102 THR 102 109 109 THR THR A . n 
A 1 103 ILE 103 110 110 ILE ILE A . n 
A 1 104 ALA 104 111 111 ALA ALA A . n 
A 1 105 LYS 105 112 112 LYS LYS A . n 
A 1 106 SER 106 113 113 SER SER A . n 
A 1 107 GLY 107 114 114 GLY GLY A . n 
A 1 108 THR 108 115 115 THR THR A . n 
A 1 109 LYS 109 116 116 LYS LYS A . n 
A 1 110 ALA 110 117 117 ALA ALA A . n 
A 1 111 PHE 111 118 118 PHE PHE A . n 
A 1 112 MET 112 119 119 MET MET A . n 
A 1 113 GLU 113 120 120 GLU GLU A . n 
A 1 114 ALA 114 121 121 ALA ALA A . n 
A 1 115 LEU 115 122 122 LEU LEU A . n 
A 1 116 GLN 116 123 123 GLN GLN A . n 
A 1 117 ALA 117 124 124 ALA ALA A . n 
A 1 118 GLY 118 125 125 GLY GLY A . n 
A 1 119 ALA 119 126 126 ALA ALA A . n 
A 1 120 ASP 120 127 127 ASP ASP A . n 
A 1 121 ILE 121 128 128 ILE ILE A . n 
A 1 122 SER 122 129 129 SER SER A . n 
A 1 123 MET 123 130 130 MET MET A . n 
A 1 124 ILE 124 131 131 ILE ILE A . n 
A 1 125 GLY 125 132 132 GLY GLY A . n 
A 1 126 GLN 126 133 133 GLN GLN A . n 
A 1 127 PHE 127 134 134 PHE PHE A . n 
A 1 128 GLY 128 135 135 GLY GLY A . n 
A 1 129 VAL 129 136 136 VAL VAL A . n 
A 1 130 GLY 130 137 137 GLY GLY A . n 
A 1 131 PHE 131 138 138 PHE PHE A . n 
A 1 132 TYR 132 139 139 TYR TYR A . n 
A 1 133 SER 133 140 140 SER SER A . n 
A 1 134 ALA 134 141 141 ALA ALA A . n 
A 1 135 TYR 135 142 142 TYR TYR A . n 
A 1 136 LEU 136 143 143 LEU LEU A . n 
A 1 137 VAL 137 144 144 VAL VAL A . n 
A 1 138 ALA 138 145 145 ALA ALA A . n 
A 1 139 GLU 139 146 146 GLU GLU A . n 
A 1 140 LYS 140 147 147 LYS LYS A . n 
A 1 141 VAL 141 148 148 VAL VAL A . n 
A 1 142 THR 142 149 149 THR THR A . n 
A 1 143 VAL 143 150 150 VAL VAL A . n 
A 1 144 ILE 144 151 151 ILE ILE A . n 
A 1 145 THR 145 152 152 THR THR A . n 
A 1 146 LYS 146 153 153 LYS LYS A . n 
A 1 147 HIS 147 154 154 HIS HIS A . n 
A 1 148 ASN 148 155 155 ASN ASN A . n 
A 1 149 ASP 149 156 156 ASP ASP A . n 
A 1 150 ASP 150 157 157 ASP ASP A . n 
A 1 151 GLU 151 158 158 GLU GLU A . n 
A 1 152 GLN 152 159 159 GLN GLN A . n 
A 1 153 TYR 153 160 160 TYR TYR A . n 
A 1 154 ALA 154 161 161 ALA ALA A . n 
A 1 155 TRP 155 162 162 TRP TRP A . n 
A 1 156 GLU 156 163 163 GLU GLU A . n 
A 1 157 SER 157 164 164 SER SER A . n 
A 1 158 SER 158 165 165 SER SER A . n 
A 1 159 ALA 159 166 166 ALA ALA A . n 
A 1 160 GLY 160 167 167 GLY GLY A . n 
A 1 161 GLY 161 168 168 GLY GLY A . n 
A 1 162 SER 162 169 169 SER SER A . n 
A 1 163 PHE 163 170 170 PHE PHE A . n 
A 1 164 THR 164 171 171 THR THR A . n 
A 1 165 VAL 165 172 172 VAL VAL A . n 
A 1 166 ARG 166 173 173 ARG ARG A . n 
A 1 167 THR 167 174 174 THR THR A . n 
A 1 168 ASP 168 175 175 ASP ASP A . n 
A 1 169 THR 169 176 176 THR THR A . n 
A 1 170 GLY 170 177 177 GLY GLY A . n 
A 1 171 GLU 171 178 178 GLU GLU A . n 
A 1 172 PRO 172 179 179 PRO PRO A . n 
A 1 173 MET 173 180 180 MET MET A . n 
A 1 174 GLY 174 181 181 GLY GLY A . n 
A 1 175 ARG 175 182 182 ARG ARG A . n 
A 1 176 GLY 176 183 183 GLY GLY A . n 
A 1 177 THR 177 184 184 THR THR A . n 
A 1 178 LYS 178 185 185 LYS LYS A . n 
A 1 179 VAL 179 186 186 VAL VAL A . n 
A 1 180 ILE 180 187 187 ILE ILE A . n 
A 1 181 LEU 181 188 188 LEU LEU A . n 
A 1 182 HIS 182 189 189 HIS HIS A . n 
A 1 183 LEU 183 190 190 LEU LEU A . n 
A 1 184 LYS 184 191 191 LYS LYS A . n 
A 1 185 GLU 185 192 192 GLU GLU A . n 
A 1 186 ASP 186 193 193 ASP ASP A . n 
A 1 187 GLN 187 194 194 GLN GLN A . n 
A 1 188 THR 188 195 195 THR THR A . n 
A 1 189 GLU 189 196 196 GLU GLU A . n 
A 1 190 TYR 190 197 197 TYR TYR A . n 
A 1 191 LEU 191 198 198 LEU LEU A . n 
A 1 192 GLU 192 199 199 GLU GLU A . n 
A 1 193 GLU 193 200 200 GLU GLU A . n 
A 1 194 ARG 194 201 201 ARG ARG A . n 
A 1 195 ARG 195 202 202 ARG ARG A . n 
A 1 196 ILE 196 203 203 ILE ILE A . n 
A 1 197 LYS 197 204 204 LYS LYS A . n 
A 1 198 GLU 198 205 205 GLU GLU A . n 
A 1 199 ILE 199 206 206 ILE ILE A . n 
A 1 200 VAL 200 207 207 VAL VAL A . n 
A 1 201 LYS 201 208 208 LYS LYS A . n 
A 1 202 LYS 202 209 209 LYS LYS A . n 
A 1 203 HIS 203 210 210 HIS HIS A . n 
A 1 204 SER 204 211 211 SER SER A . n 
A 1 205 GLN 205 212 212 GLN GLN A . n 
A 1 206 PHE 206 213 213 PHE PHE A . n 
A 1 207 ILE 207 214 214 ILE ILE A . n 
A 1 208 GLY 208 215 215 GLY GLY A . n 
A 1 209 TYR 209 216 216 TYR TYR A . n 
A 1 210 PRO 210 217 217 PRO PRO A . n 
A 1 211 ILE 211 218 218 ILE ILE A . n 
A 1 212 THR 212 219 219 THR THR A . n 
A 1 213 LEU 213 220 220 LEU LEU A . n 
A 1 214 PHE 214 221 221 PHE PHE A . n 
A 1 215 VAL 215 222 222 VAL VAL A . n 
A 1 216 GLU 216 223 223 GLU GLU A . n 
A 1 217 LYS 217 224 224 LYS LYS A . n 
A 1 218 GLU 218 225 ?   ?   ?   A . n 
A 1 219 ARG 219 226 ?   ?   ?   A . n 
A 1 220 ASP 220 227 ?   ?   ?   A . n 
A 1 221 LYS 221 228 ?   ?   ?   A . n 
A 1 222 GLU 222 229 ?   ?   ?   A . n 
A 1 223 VAL 223 230 ?   ?   ?   A . n 
A 1 224 SER 224 231 ?   ?   ?   A . n 
A 1 225 ASP 225 232 ?   ?   ?   A . n 
A 1 226 ASP 226 233 ?   ?   ?   A . n 
A 1 227 GLU 227 234 ?   ?   ?   A . n 
A 1 228 ALA 228 235 ?   ?   ?   A . n 
A 1 229 GLU 229 236 ?   ?   ?   A . n 
A 1 230 LEU 230 237 ?   ?   ?   A . n 
A 1 231 GLU 231 238 ?   ?   ?   A . n 
A 1 232 HIS 232 239 ?   ?   ?   A . n 
A 1 233 HIS 233 240 ?   ?   ?   A . n 
A 1 234 HIS 234 241 ?   ?   ?   A . n 
A 1 235 HIS 235 242 ?   ?   ?   A . n 
A 1 236 HIS 236 243 ?   ?   ?   A . n 
A 1 237 HIS 237 244 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AYE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AYE 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1AYE 1  301 301 A1AYE GE5 A . 
C 3 HOH   1  401 13  HOH   HOH A . 
C 3 HOH   2  402 7   HOH   HOH A . 
C 3 HOH   3  403 5   HOH   HOH A . 
C 3 HOH   4  404 38  HOH   HOH A . 
C 3 HOH   5  405 21  HOH   HOH A . 
C 3 HOH   6  406 34  HOH   HOH A . 
C 3 HOH   7  407 39  HOH   HOH A . 
C 3 HOH   8  408 28  HOH   HOH A . 
C 3 HOH   9  409 24  HOH   HOH A . 
C 3 HOH   10 410 40  HOH   HOH A . 
C 3 HOH   11 411 20  HOH   HOH A . 
C 3 HOH   12 412 14  HOH   HOH A . 
C 3 HOH   13 413 15  HOH   HOH A . 
C 3 HOH   14 414 31  HOH   HOH A . 
C 3 HOH   15 415 3   HOH   HOH A . 
C 3 HOH   16 416 1   HOH   HOH A . 
C 3 HOH   17 417 8   HOH   HOH A . 
C 3 HOH   18 418 27  HOH   HOH A . 
C 3 HOH   19 419 32  HOH   HOH A . 
C 3 HOH   20 420 16  HOH   HOH A . 
C 3 HOH   21 421 36  HOH   HOH A . 
C 3 HOH   22 422 30  HOH   HOH A . 
C 3 HOH   23 423 11  HOH   HOH A . 
C 3 HOH   24 424 17  HOH   HOH A . 
C 3 HOH   25 425 48  HOH   HOH A . 
C 3 HOH   26 426 50  HOH   HOH A . 
C 3 HOH   27 427 22  HOH   HOH A . 
C 3 HOH   28 428 54  HOH   HOH A . 
C 3 HOH   29 429 2   HOH   HOH A . 
C 3 HOH   30 430 4   HOH   HOH A . 
C 3 HOH   31 431 10  HOH   HOH A . 
C 3 HOH   32 432 12  HOH   HOH A . 
C 3 HOH   33 433 6   HOH   HOH A . 
C 3 HOH   34 434 19  HOH   HOH A . 
C 3 HOH   35 435 41  HOH   HOH A . 
C 3 HOH   36 436 25  HOH   HOH A . 
C 3 HOH   37 437 33  HOH   HOH A . 
C 3 HOH   38 438 43  HOH   HOH A . 
C 3 HOH   39 439 51  HOH   HOH A . 
C 3 HOH   40 440 46  HOH   HOH A . 
C 3 HOH   41 441 9   HOH   HOH A . 
C 3 HOH   42 442 26  HOH   HOH A . 
C 3 HOH   43 443 18  HOH   HOH A . 
C 3 HOH   44 444 44  HOH   HOH A . 
C 3 HOH   45 445 55  HOH   HOH A . 
C 3 HOH   46 446 47  HOH   HOH A . 
C 3 HOH   47 447 23  HOH   HOH A . 
C 3 HOH   48 448 37  HOH   HOH A . 
C 3 HOH   49 449 29  HOH   HOH A . 
C 3 HOH   50 450 35  HOH   HOH A . 
C 3 HOH   51 451 49  HOH   HOH A . 
C 3 HOH   52 452 42  HOH   HOH A . 
C 3 HOH   53 453 45  HOH   HOH A . 
C 3 HOH   54 454 53  HOH   HOH A . 
C 3 HOH   55 455 52  HOH   HOH A . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 XDS         .           ?               package 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://www.mpimf-heidelberg.mpg.de/~kabsch/xds/     ?   ? 
2 Aimless     0.7.7       23/04/21        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 DIMPLE      .           ?               program 'Marcin Wojdyr'   wojdyr@gmail.com                        phasing           
http://ccp4.github.io/dimple/                       ?   ? 
4 PHENIX      1.20.1_4487 ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                       C++ ? 
5 PDB_EXTRACT 3.28        'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.volume             599161.590 
_cell.length_a           69.838 
_cell.length_b           88.675 
_cell.length_c           96.750 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HBJ 
_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                         7HBJ 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HBJ 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 S 9M' 
_diffrn_detector.pdbx_collection_date   2023-07-23 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HBJ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             54.870 
_reflns.d_resolution_high            2.650 
_reflns.number_obs                   7081 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         79.200 
_reflns.pdbx_Rmerge_I_obs            0.197 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        4.900 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              2.800 
_reflns.pdbx_Rrim_I_all              0.244 
_reflns.pdbx_Rpim_I_all              0.140 
_reflns.pdbx_CC_half                 0.922 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     19856 
_reflns.pdbx_scaling_rejects         74 
_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 2.650 2.790  ? 2804 1018 ? 0.575 ? ? ? 2.800 ? 2.400 ? ? ? ? ? ? 79.500 0.704 0.398 0.545 
1 2 8.360 54.870 ? 634  228  ? 0.056 ? ? ? 2.800 ? 9.600 ? ? ? ? ? ? 72.400 0.069 0.038 0.992 
# 
_refine.entry_id                                 7HBJ 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.ls_percent_reflns_R_free                 5.35 
_refine.pdbx_overall_phase_error                 25.8245 
_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                          0.2199 
_refine.B_iso_mean                               42.11 
_refine.ls_number_reflns_R_free                  368 
_refine.ls_percent_reflns_obs                    75.67 
_refine.ls_R_factor_R_work                       0.2172 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            2.65 
_refine.ls_number_reflns_obs                     6873 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  6505 
_refine.ls_d_res_low                             54.87 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2652 
_refine.overall_SU_ML                            0.4261 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         16 
_refine_hist.number_atoms_solvent             55 
_refine_hist.number_atoms_total               1715 
_refine_hist.d_res_high                       2.65 
_refine_hist.d_res_low                        54.87 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           1687 0.0028 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2274 0.5937 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     259  0.0425 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0029 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 224  6.7252 ? ? ? 
# 
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' 2.65 3.03  2128 0.2886 75.82 0.3489 124 . . . . . 
'X-RAY DIFFRACTION' 3.03 3.82  2181 0.2274 77.04 0.2757 118 . . . . . 
'X-RAY DIFFRACTION' 3.82 54.87 2196 0.1824 74.21 0.2254 126 . . . . . 
# 
_struct.entry_id                  7HBJ 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13498' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HBJ 
_struct_keywords.pdbx_keywords   CHAPERONE 
_struct_keywords.text            
'Crystallographic Fragment Screening; Fragment-Based Drug Discovery (FBDD); Heat shock protein 90 (HSP90), CHAPERONE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HS90A_HUMAN 
_struct_ref.pdbx_db_accession          P07900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRT
LTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGG
SFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAE
;
_struct_ref.pdbx_align_begin           9 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HBJ 
_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 7HBJ MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HBJ LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HBJ GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HBJ HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HBJ HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HBJ HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HBJ HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HBJ HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HBJ HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2  AA2 GLU A 35  ? 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  ? ILE A 97  ? THR A 99  ILE A 104 1 ? 6  
HELX_P HELX_P5  AA5 ASN A 98  ? ILE A 103 ? ASN A 105 ILE A 110 1 ? 6  
HELX_P HELX_P6  AA6 ALA A 104 ? ALA A 117 ? ALA A 111 ALA A 124 1 ? 14 
HELX_P HELX_P7  AA7 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P8  AA8 VAL A 129 ? TYR A 132 ? VAL A 136 TYR A 139 5 ? 4  
HELX_P HELX_P9  AA9 SER A 133 ? VAL A 137 ? SER A 140 VAL A 144 1 ? 5  
HELX_P HELX_P10 AB1 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P11 AB2 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N ILE A 144 ? N ILE A 151 O LYS A 178 ? O LYS A 185 
AA1 5 6 O VAL A 179 ? O VAL A 186 N ILE A 84  ? N ILE A 91  
AA1 6 7 O THR A 83  ? O THR A 90  N ILE A 74  ? N ILE A 81  
AA1 7 8 N ILE A 71  ? N ILE A 78  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HBJ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG1 A THR 65  ? ? O A HOH 401 ? ? 2.03 
2 1 OD1 A ASN 155 ? ? O A HOH 402 ? ? 2.04 
3 1 O   A LEU 48  ? ? O A HOH 403 ? ? 2.09 
4 1 O   A ILE 96  ? ? O A HOH 402 ? ? 2.14 
5 1 O   A LEU 107 ? ? O A HOH 404 ? ? 2.15 
6 1 NH1 A ARG 173 ? ? O A HOH 405 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 38  ? ? -161.00 104.30  
2 1 LEU A 103 ? ? -67.79  -71.85  
3 1 ASN A 105 ? ? 103.67  -98.74  
4 1 ASN A 106 ? ? -39.49  -79.57  
5 1 ALA A 111 ? ? -170.04 -30.42  
6 1 ALA A 166 ? ? 57.12   -137.52 
7 1 ARG A 182 ? ? -170.51 148.16  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1  ? 'X-RAY DIFFRACTION' refined 14.0991708285   27.4834965715 30.9805403497 0.307571947817 0.373745227433 0.733278037641 
0.0397776532246  -0.0587654022772 0.0602528241515  4.31693772692 4.09847424099 5.18259566671 -1.48235716196   -2.28173508221  
1.69186112858    -0.124809796375  -0.557776705593  -0.373412416953 0.318205346746   0.222674000555   -0.722782467759 
-0.191562800605 0.379967590198    -0.038844942365  
2  ? 'X-RAY DIFFRACTION' refined -3.98057319524  37.6010627998 26.8285204404 0.250565355917 0.304364300521 0.560536001211 
-0.015540130188  -0.0757339885257 -0.0472639121389 1.13949935833 4.95019171279 6.09674594612 -0.360160053615  0.327358440051  
-3.55248752833   0.0144496891402  0.115082587767   -0.276347061048 0.140700348043   -0.0301078550918 -0.512201484164 
-0.242353771135 0.501492703609    0.0248904374102  
3  ? 'X-RAY DIFFRACTION' refined -8.6795813407   27.2807416543 23.4400449247 0.253619650251 0.304445190077 0.445394659304 
-0.0611812555162 -0.100473652717  0.0028137406553  2.30550078501 5.0708737712  4.60251226939 -0.0574704491286 -0.978360631313 
-2.73377585046   0.152722801149   -0.0024281899283 -0.361925634201 -0.450868209582  -0.0373740029456 0.293220112088  
0.565529645128  -0.22391086441    -0.433509320024  
4  ? 'X-RAY DIFFRACTION' refined 6.66517444094   34.114925098  17.7543353136 0.359598973748 0.351390306428 0.793426672014 
0.0350010328603  0.0841864023732  -0.0895387214312 3.44741694953 4.20370150891 4.13758520318 -2.35970702607   -1.79862274103  
-0.0233086160972 -0.0225987269113 -0.573287033538  0.943911662112  0.366360277134   0.400780483619   -1.77571673726  
0.0685656508732 0.623617939481    -0.177905007381  
5  ? 'X-RAY DIFFRACTION' refined 12.8699815367   39.4028487576 36.7415135619 0.418931194314 0.53781779528  0.430854764435 
-0.0168984328012 -0.104712879692  -0.106505713188  5.8136447826  8.22680457806 8.65161511464 0.193622458311   1.5366646032    
-2.57890118099   -0.0630007433039 -1.00882664736   1.14183006795   0.598197303729   -0.395844138349  -0.240974866236 
-1.06691033974  0.439738498863    0.50225640486    
6  ? 'X-RAY DIFFRACTION' refined 4.79036497217   26.0328580111 23.1568315401 0.228322360724 0.212782994947 0.322283425691 
0.0106661778415  0.0515770331588  -0.0640706965384 4.64410728399 2.75573034628 5.49652983657 -0.627102407074  -0.871677204683 
-2.60434469566   0.246842596419   0.115732761068   -0.5248819643   -0.337619235512  -0.11191465299   0.235725693841  
0.750231700705  0.269286219111    -0.0714865638306 
7  ? 'X-RAY DIFFRACTION' refined 1.75508516615   22.6513210858 16.122827586  0.368908774649 0.354434690786 0.465165095009 
-0.0385748390861 -0.0352469408858 -0.130099213803  6.11507038909 2.9854599062  3.50581867535 -2.16557594547   0.463112097105  
-1.78125566012   -0.458108222139  1.04035680378    -0.674952339299 -0.0732265678708 -0.028364016005  1.0831304684    
0.404447096813  -0.00567113710842 -0.391782579336  
8  ? 'X-RAY DIFFRACTION' refined -0.534269806762 20.7743720027 34.9975496311 0.266903304747 0.40367731455  0.425552848665 
0.065313162594   0.0468602985045  0.116485901536   2.64000967054 4.30591625914 4.92967555589 1.84764939344    -2.73608402423  
-1.25373911266   -0.0482137708851 -0.712033956348  -0.931285499154 0.172896595903   0.217679736046   -0.257711142898 
0.904426848335  -0.0131848995937  0.147650506547   
9  ? 'X-RAY DIFFRACTION' refined -9.29103065213  28.9885782866 41.7471578555 0.377018595071 0.736712144793 0.318042056589 
0.10060660501    -0.0301044056174 0.0537882055645  8.81882622042 1.99821734941 8.05777448281 -1.18441834305   3.54532933174   
0.381042972164   -0.147462029069  -0.981425992003  0.232997387245  1.15645885407    -0.751304658193  -0.495344437583 
-0.972076153816 0.0930254303403   0.8955127488     
10 ? 'X-RAY DIFFRACTION' refined -12.7151278694  30.2479746096 32.4349940504 0.295146564801 0.380662828011 0.617154791882 
0.0234394454479  -0.0190486594676 0.0945655405028  1.95154661743 5.78576986358 4.70527481924 0.598617485339   -0.30113670363  
-0.28456647875   0.0253208827543  -0.620934698718  -0.22976304983  0.0347617976388  -0.291426149357  -0.30946262544  
-0.642183419014 -0.460372053656   0.33088541252    
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  1  'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2  2  'X-RAY DIFFRACTION' A 41  A 26  A 65  A 50  . 
;chain 'A' and (resid 41 through 65 )
;
3  3  'X-RAY DIFFRACTION' A 66  A 51  A 93  A 78  . 
;chain 'A' and (resid 66 through 93 )
;
4  4  'X-RAY DIFFRACTION' A 94  A 79  A 111 A 96  . 
;chain 'A' and (resid 94 through 111 )
;
5  5  'X-RAY DIFFRACTION' A 112 A 97  A 136 A 121 . 
;chain 'A' and (resid 112 through 136 )
;
6  6  'X-RAY DIFFRACTION' A 137 A 122 A 168 A 153 . 
;chain 'A' and (resid 137 through 168 )
;
7  7  'X-RAY DIFFRACTION' A 169 A 154 A 182 A 167 . 
;chain 'A' and (resid 169 through 182 )
;
8  8  'X-RAY DIFFRACTION' A 183 A 168 A 199 A 184 . 
;chain 'A' and (resid 183 through 199 )
;
9  9  'X-RAY DIFFRACTION' A 200 A 185 A 210 A 195 . 
;chain 'A' and (resid 200 through 210 )
;
10 10 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AYE C10  C  Y N 1   
A1AYE C11  C  Y N 2   
A1AYE C12  C  Y N 3   
A1AYE C1   C  N N 4   
A1AYE C2   C  Y N 5   
A1AYE C3   C  Y N 6   
A1AYE C4   C  Y N 7   
A1AYE C5   C  Y N 8   
A1AYE C6   C  Y N 9   
A1AYE C7   C  Y N 10  
A1AYE C8   C  Y N 11  
A1AYE C9   C  Y N 12  
A1AYE N1   N  N N 13  
A1AYE N2   N  Y N 14  
A1AYE O1   O  N N 15  
A1AYE CL1  CL N N 16  
A1AYE H10  H  N N 17  
A1AYE H11  H  N N 18  
A1AYE H12  H  N N 19  
A1AYE H13  H  N N 20  
A1AYE H14  H  N N 21  
A1AYE H3   H  N N 22  
A1AYE H6   H  N N 23  
A1AYE H7   H  N N 24  
A1AYE H9   H  N N 25  
A1AYE HN12 H  N N 26  
A1AYE HN11 H  N N 27  
ALA   N    N  N N 28  
ALA   CA   C  N S 29  
ALA   C    C  N N 30  
ALA   O    O  N N 31  
ALA   CB   C  N N 32  
ALA   OXT  O  N N 33  
ALA   H    H  N N 34  
ALA   H2   H  N N 35  
ALA   HA   H  N N 36  
ALA   HB1  H  N N 37  
ALA   HB2  H  N N 38  
ALA   HB3  H  N N 39  
ALA   HXT  H  N N 40  
ARG   N    N  N N 41  
ARG   CA   C  N S 42  
ARG   C    C  N N 43  
ARG   O    O  N N 44  
ARG   CB   C  N N 45  
ARG   CG   C  N N 46  
ARG   CD   C  N N 47  
ARG   NE   N  N N 48  
ARG   CZ   C  N N 49  
ARG   NH1  N  N N 50  
ARG   NH2  N  N N 51  
ARG   OXT  O  N N 52  
ARG   H    H  N N 53  
ARG   H2   H  N N 54  
ARG   HA   H  N N 55  
ARG   HB2  H  N N 56  
ARG   HB3  H  N N 57  
ARG   HG2  H  N N 58  
ARG   HG3  H  N N 59  
ARG   HD2  H  N N 60  
ARG   HD3  H  N N 61  
ARG   HE   H  N N 62  
ARG   HH11 H  N N 63  
ARG   HH12 H  N N 64  
ARG   HH21 H  N N 65  
ARG   HH22 H  N N 66  
ARG   HXT  H  N N 67  
ASN   N    N  N N 68  
ASN   CA   C  N S 69  
ASN   C    C  N N 70  
ASN   O    O  N N 71  
ASN   CB   C  N N 72  
ASN   CG   C  N N 73  
ASN   OD1  O  N N 74  
ASN   ND2  N  N N 75  
ASN   OXT  O  N N 76  
ASN   H    H  N N 77  
ASN   H2   H  N N 78  
ASN   HA   H  N N 79  
ASN   HB2  H  N N 80  
ASN   HB3  H  N N 81  
ASN   HD21 H  N N 82  
ASN   HD22 H  N N 83  
ASN   HXT  H  N N 84  
ASP   N    N  N N 85  
ASP   CA   C  N S 86  
ASP   C    C  N N 87  
ASP   O    O  N N 88  
ASP   CB   C  N N 89  
ASP   CG   C  N N 90  
ASP   OD1  O  N N 91  
ASP   OD2  O  N N 92  
ASP   OXT  O  N N 93  
ASP   H    H  N N 94  
ASP   H2   H  N N 95  
ASP   HA   H  N N 96  
ASP   HB2  H  N N 97  
ASP   HB3  H  N N 98  
ASP   HD2  H  N N 99  
ASP   HXT  H  N N 100 
GLN   N    N  N N 101 
GLN   CA   C  N S 102 
GLN   C    C  N N 103 
GLN   O    O  N N 104 
GLN   CB   C  N N 105 
GLN   CG   C  N N 106 
GLN   CD   C  N N 107 
GLN   OE1  O  N N 108 
GLN   NE2  N  N N 109 
GLN   OXT  O  N N 110 
GLN   H    H  N N 111 
GLN   H2   H  N N 112 
GLN   HA   H  N N 113 
GLN   HB2  H  N N 114 
GLN   HB3  H  N N 115 
GLN   HG2  H  N N 116 
GLN   HG3  H  N N 117 
GLN   HE21 H  N N 118 
GLN   HE22 H  N N 119 
GLN   HXT  H  N N 120 
GLU   N    N  N N 121 
GLU   CA   C  N S 122 
GLU   C    C  N N 123 
GLU   O    O  N N 124 
GLU   CB   C  N N 125 
GLU   CG   C  N N 126 
GLU   CD   C  N N 127 
GLU   OE1  O  N N 128 
GLU   OE2  O  N N 129 
GLU   OXT  O  N N 130 
GLU   H    H  N N 131 
GLU   H2   H  N N 132 
GLU   HA   H  N N 133 
GLU   HB2  H  N N 134 
GLU   HB3  H  N N 135 
GLU   HG2  H  N N 136 
GLU   HG3  H  N N 137 
GLU   HE2  H  N N 138 
GLU   HXT  H  N N 139 
GLY   N    N  N N 140 
GLY   CA   C  N N 141 
GLY   C    C  N N 142 
GLY   O    O  N N 143 
GLY   OXT  O  N N 144 
GLY   H    H  N N 145 
GLY   H2   H  N N 146 
GLY   HA2  H  N N 147 
GLY   HA3  H  N N 148 
GLY   HXT  H  N N 149 
HIS   N    N  N N 150 
HIS   CA   C  N S 151 
HIS   C    C  N N 152 
HIS   O    O  N N 153 
HIS   CB   C  N N 154 
HIS   CG   C  Y N 155 
HIS   ND1  N  Y N 156 
HIS   CD2  C  Y N 157 
HIS   CE1  C  Y N 158 
HIS   NE2  N  Y N 159 
HIS   OXT  O  N N 160 
HIS   H    H  N N 161 
HIS   H2   H  N N 162 
HIS   HA   H  N N 163 
HIS   HB2  H  N N 164 
HIS   HB3  H  N N 165 
HIS   HD1  H  N N 166 
HIS   HD2  H  N N 167 
HIS   HE1  H  N N 168 
HIS   HE2  H  N N 169 
HIS   HXT  H  N N 170 
HOH   O    O  N N 171 
HOH   H1   H  N N 172 
HOH   H2   H  N N 173 
ILE   N    N  N N 174 
ILE   CA   C  N S 175 
ILE   C    C  N N 176 
ILE   O    O  N N 177 
ILE   CB   C  N S 178 
ILE   CG1  C  N N 179 
ILE   CG2  C  N N 180 
ILE   CD1  C  N N 181 
ILE   OXT  O  N N 182 
ILE   H    H  N N 183 
ILE   H2   H  N N 184 
ILE   HA   H  N N 185 
ILE   HB   H  N N 186 
ILE   HG12 H  N N 187 
ILE   HG13 H  N N 188 
ILE   HG21 H  N N 189 
ILE   HG22 H  N N 190 
ILE   HG23 H  N N 191 
ILE   HD11 H  N N 192 
ILE   HD12 H  N N 193 
ILE   HD13 H  N N 194 
ILE   HXT  H  N N 195 
LEU   N    N  N N 196 
LEU   CA   C  N S 197 
LEU   C    C  N N 198 
LEU   O    O  N N 199 
LEU   CB   C  N N 200 
LEU   CG   C  N N 201 
LEU   CD1  C  N N 202 
LEU   CD2  C  N N 203 
LEU   OXT  O  N N 204 
LEU   H    H  N N 205 
LEU   H2   H  N N 206 
LEU   HA   H  N N 207 
LEU   HB2  H  N N 208 
LEU   HB3  H  N N 209 
LEU   HG   H  N N 210 
LEU   HD11 H  N N 211 
LEU   HD12 H  N N 212 
LEU   HD13 H  N N 213 
LEU   HD21 H  N N 214 
LEU   HD22 H  N N 215 
LEU   HD23 H  N N 216 
LEU   HXT  H  N N 217 
LYS   N    N  N N 218 
LYS   CA   C  N S 219 
LYS   C    C  N N 220 
LYS   O    O  N N 221 
LYS   CB   C  N N 222 
LYS   CG   C  N N 223 
LYS   CD   C  N N 224 
LYS   CE   C  N N 225 
LYS   NZ   N  N N 226 
LYS   OXT  O  N N 227 
LYS   H    H  N N 228 
LYS   H2   H  N N 229 
LYS   HA   H  N N 230 
LYS   HB2  H  N N 231 
LYS   HB3  H  N N 232 
LYS   HG2  H  N N 233 
LYS   HG3  H  N N 234 
LYS   HD2  H  N N 235 
LYS   HD3  H  N N 236 
LYS   HE2  H  N N 237 
LYS   HE3  H  N N 238 
LYS   HZ1  H  N N 239 
LYS   HZ2  H  N N 240 
LYS   HZ3  H  N N 241 
LYS   HXT  H  N N 242 
MET   N    N  N N 243 
MET   CA   C  N S 244 
MET   C    C  N N 245 
MET   O    O  N N 246 
MET   CB   C  N N 247 
MET   CG   C  N N 248 
MET   SD   S  N N 249 
MET   CE   C  N N 250 
MET   OXT  O  N N 251 
MET   H    H  N N 252 
MET   H2   H  N N 253 
MET   HA   H  N N 254 
MET   HB2  H  N N 255 
MET   HB3  H  N N 256 
MET   HG2  H  N N 257 
MET   HG3  H  N N 258 
MET   HE1  H  N N 259 
MET   HE2  H  N N 260 
MET   HE3  H  N N 261 
MET   HXT  H  N N 262 
PHE   N    N  N N 263 
PHE   CA   C  N S 264 
PHE   C    C  N N 265 
PHE   O    O  N N 266 
PHE   CB   C  N N 267 
PHE   CG   C  Y N 268 
PHE   CD1  C  Y N 269 
PHE   CD2  C  Y N 270 
PHE   CE1  C  Y N 271 
PHE   CE2  C  Y N 272 
PHE   CZ   C  Y N 273 
PHE   OXT  O  N N 274 
PHE   H    H  N N 275 
PHE   H2   H  N N 276 
PHE   HA   H  N N 277 
PHE   HB2  H  N N 278 
PHE   HB3  H  N N 279 
PHE   HD1  H  N N 280 
PHE   HD2  H  N N 281 
PHE   HE1  H  N N 282 
PHE   HE2  H  N N 283 
PHE   HZ   H  N N 284 
PHE   HXT  H  N N 285 
PRO   N    N  N N 286 
PRO   CA   C  N S 287 
PRO   C    C  N N 288 
PRO   O    O  N N 289 
PRO   CB   C  N N 290 
PRO   CG   C  N N 291 
PRO   CD   C  N N 292 
PRO   OXT  O  N N 293 
PRO   H    H  N N 294 
PRO   HA   H  N N 295 
PRO   HB2  H  N N 296 
PRO   HB3  H  N N 297 
PRO   HG2  H  N N 298 
PRO   HG3  H  N N 299 
PRO   HD2  H  N N 300 
PRO   HD3  H  N N 301 
PRO   HXT  H  N N 302 
SER   N    N  N N 303 
SER   CA   C  N S 304 
SER   C    C  N N 305 
SER   O    O  N N 306 
SER   CB   C  N N 307 
SER   OG   O  N N 308 
SER   OXT  O  N N 309 
SER   H    H  N N 310 
SER   H2   H  N N 311 
SER   HA   H  N N 312 
SER   HB2  H  N N 313 
SER   HB3  H  N N 314 
SER   HG   H  N N 315 
SER   HXT  H  N N 316 
THR   N    N  N N 317 
THR   CA   C  N S 318 
THR   C    C  N N 319 
THR   O    O  N N 320 
THR   CB   C  N R 321 
THR   OG1  O  N N 322 
THR   CG2  C  N N 323 
THR   OXT  O  N N 324 
THR   H    H  N N 325 
THR   H2   H  N N 326 
THR   HA   H  N N 327 
THR   HB   H  N N 328 
THR   HG1  H  N N 329 
THR   HG21 H  N N 330 
THR   HG22 H  N N 331 
THR   HG23 H  N N 332 
THR   HXT  H  N N 333 
TRP   N    N  N N 334 
TRP   CA   C  N S 335 
TRP   C    C  N N 336 
TRP   O    O  N N 337 
TRP   CB   C  N N 338 
TRP   CG   C  Y N 339 
TRP   CD1  C  Y N 340 
TRP   CD2  C  Y N 341 
TRP   NE1  N  Y N 342 
TRP   CE2  C  Y N 343 
TRP   CE3  C  Y N 344 
TRP   CZ2  C  Y N 345 
TRP   CZ3  C  Y N 346 
TRP   CH2  C  Y N 347 
TRP   OXT  O  N N 348 
TRP   H    H  N N 349 
TRP   H2   H  N N 350 
TRP   HA   H  N N 351 
TRP   HB2  H  N N 352 
TRP   HB3  H  N N 353 
TRP   HD1  H  N N 354 
TRP   HE1  H  N N 355 
TRP   HE3  H  N N 356 
TRP   HZ2  H  N N 357 
TRP   HZ3  H  N N 358 
TRP   HH2  H  N N 359 
TRP   HXT  H  N N 360 
TYR   N    N  N N 361 
TYR   CA   C  N S 362 
TYR   C    C  N N 363 
TYR   O    O  N N 364 
TYR   CB   C  N N 365 
TYR   CG   C  Y N 366 
TYR   CD1  C  Y N 367 
TYR   CD2  C  Y N 368 
TYR   CE1  C  Y N 369 
TYR   CE2  C  Y N 370 
TYR   CZ   C  Y N 371 
TYR   OH   O  N N 372 
TYR   OXT  O  N N 373 
TYR   H    H  N N 374 
TYR   H2   H  N N 375 
TYR   HA   H  N N 376 
TYR   HB2  H  N N 377 
TYR   HB3  H  N N 378 
TYR   HD1  H  N N 379 
TYR   HD2  H  N N 380 
TYR   HE1  H  N N 381 
TYR   HE2  H  N N 382 
TYR   HH   H  N N 383 
TYR   HXT  H  N N 384 
VAL   N    N  N N 385 
VAL   CA   C  N S 386 
VAL   C    C  N N 387 
VAL   O    O  N N 388 
VAL   CB   C  N N 389 
VAL   CG1  C  N N 390 
VAL   CG2  C  N N 391 
VAL   OXT  O  N N 392 
VAL   H    H  N N 393 
VAL   H2   H  N N 394 
VAL   HA   H  N N 395 
VAL   HB   H  N N 396 
VAL   HG11 H  N N 397 
VAL   HG12 H  N N 398 
VAL   HG13 H  N N 399 
VAL   HG21 H  N N 400 
VAL   HG22 H  N N 401 
VAL   HG23 H  N N 402 
VAL   HXT  H  N N 403 
# 
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 
A1AYE C1  C2   sing N N 1   
A1AYE C2  C3   doub Y N 2   
A1AYE C2  C12  sing Y N 3   
A1AYE C3  C4   sing Y N 4   
A1AYE C4  O1   sing N N 5   
A1AYE C4  C10  doub Y N 6   
A1AYE O1  C5   sing N N 7   
A1AYE C5  C6   doub Y N 8   
A1AYE C5  N2   sing Y N 9   
A1AYE C6  C7   sing Y N 10  
A1AYE C7  C8   doub Y N 11  
A1AYE C8  N1   sing N N 12  
A1AYE C8  C9   sing Y N 13  
A1AYE C9  N2   doub Y N 14  
A1AYE C10 C11  sing Y N 15  
A1AYE C11 C12  doub Y N 16  
A1AYE C12 CL1  sing N N 17  
A1AYE C10 H10  sing N N 18  
A1AYE C11 H11  sing N N 19  
A1AYE C1  H12  sing N N 20  
A1AYE C1  H13  sing N N 21  
A1AYE C1  H14  sing N N 22  
A1AYE C3  H3   sing N N 23  
A1AYE C6  H6   sing N N 24  
A1AYE C7  H7   sing N N 25  
A1AYE C9  H9   sing N N 26  
A1AYE N1  HN12 sing N N 27  
A1AYE N1  HN11 sing N N 28  
ALA   N   CA   sing N N 29  
ALA   N   H    sing N N 30  
ALA   N   H2   sing N N 31  
ALA   CA  C    sing N N 32  
ALA   CA  CB   sing N N 33  
ALA   CA  HA   sing N N 34  
ALA   C   O    doub N N 35  
ALA   C   OXT  sing N N 36  
ALA   CB  HB1  sing N N 37  
ALA   CB  HB2  sing N N 38  
ALA   CB  HB3  sing N N 39  
ALA   OXT HXT  sing N N 40  
ARG   N   CA   sing N N 41  
ARG   N   H    sing N N 42  
ARG   N   H2   sing N N 43  
ARG   CA  C    sing N N 44  
ARG   CA  CB   sing N N 45  
ARG   CA  HA   sing N N 46  
ARG   C   O    doub N N 47  
ARG   C   OXT  sing N N 48  
ARG   CB  CG   sing N N 49  
ARG   CB  HB2  sing N N 50  
ARG   CB  HB3  sing N N 51  
ARG   CG  CD   sing N N 52  
ARG   CG  HG2  sing N N 53  
ARG   CG  HG3  sing N N 54  
ARG   CD  NE   sing N N 55  
ARG   CD  HD2  sing N N 56  
ARG   CD  HD3  sing N N 57  
ARG   NE  CZ   sing N N 58  
ARG   NE  HE   sing N N 59  
ARG   CZ  NH1  sing N N 60  
ARG   CZ  NH2  doub N N 61  
ARG   NH1 HH11 sing N N 62  
ARG   NH1 HH12 sing N N 63  
ARG   NH2 HH21 sing N N 64  
ARG   NH2 HH22 sing N N 65  
ARG   OXT HXT  sing N N 66  
ASN   N   CA   sing N N 67  
ASN   N   H    sing N N 68  
ASN   N   H2   sing N N 69  
ASN   CA  C    sing N N 70  
ASN   CA  CB   sing N N 71  
ASN   CA  HA   sing N N 72  
ASN   C   O    doub N N 73  
ASN   C   OXT  sing N N 74  
ASN   CB  CG   sing N N 75  
ASN   CB  HB2  sing N N 76  
ASN   CB  HB3  sing N N 77  
ASN   CG  OD1  doub N N 78  
ASN   CG  ND2  sing N N 79  
ASN   ND2 HD21 sing N N 80  
ASN   ND2 HD22 sing N N 81  
ASN   OXT HXT  sing N N 82  
ASP   N   CA   sing N N 83  
ASP   N   H    sing N N 84  
ASP   N   H2   sing N N 85  
ASP   CA  C    sing N N 86  
ASP   CA  CB   sing N N 87  
ASP   CA  HA   sing N N 88  
ASP   C   O    doub N N 89  
ASP   C   OXT  sing N N 90  
ASP   CB  CG   sing N N 91  
ASP   CB  HB2  sing N N 92  
ASP   CB  HB3  sing N N 93  
ASP   CG  OD1  doub N N 94  
ASP   CG  OD2  sing N N 95  
ASP   OD2 HD2  sing N N 96  
ASP   OXT HXT  sing N N 97  
GLN   N   CA   sing N N 98  
GLN   N   H    sing N N 99  
GLN   N   H2   sing N N 100 
GLN   CA  C    sing N N 101 
GLN   CA  CB   sing N N 102 
GLN   CA  HA   sing N N 103 
GLN   C   O    doub N N 104 
GLN   C   OXT  sing N N 105 
GLN   CB  CG   sing N N 106 
GLN   CB  HB2  sing N N 107 
GLN   CB  HB3  sing N N 108 
GLN   CG  CD   sing N N 109 
GLN   CG  HG2  sing N N 110 
GLN   CG  HG3  sing N N 111 
GLN   CD  OE1  doub N N 112 
GLN   CD  NE2  sing N N 113 
GLN   NE2 HE21 sing N N 114 
GLN   NE2 HE22 sing N N 115 
GLN   OXT HXT  sing N N 116 
GLU   N   CA   sing N N 117 
GLU   N   H    sing N N 118 
GLU   N   H2   sing N N 119 
GLU   CA  C    sing N N 120 
GLU   CA  CB   sing N N 121 
GLU   CA  HA   sing N N 122 
GLU   C   O    doub N N 123 
GLU   C   OXT  sing N N 124 
GLU   CB  CG   sing N N 125 
GLU   CB  HB2  sing N N 126 
GLU   CB  HB3  sing N N 127 
GLU   CG  CD   sing N N 128 
GLU   CG  HG2  sing N N 129 
GLU   CG  HG3  sing N N 130 
GLU   CD  OE1  doub N N 131 
GLU   CD  OE2  sing N N 132 
GLU   OE2 HE2  sing N N 133 
GLU   OXT HXT  sing N N 134 
GLY   N   CA   sing N N 135 
GLY   N   H    sing N N 136 
GLY   N   H2   sing N N 137 
GLY   CA  C    sing N N 138 
GLY   CA  HA2  sing N N 139 
GLY   CA  HA3  sing N N 140 
GLY   C   O    doub N N 141 
GLY   C   OXT  sing N N 142 
GLY   OXT HXT  sing N N 143 
HIS   N   CA   sing N N 144 
HIS   N   H    sing N N 145 
HIS   N   H2   sing N N 146 
HIS   CA  C    sing N N 147 
HIS   CA  CB   sing N N 148 
HIS   CA  HA   sing N N 149 
HIS   C   O    doub N N 150 
HIS   C   OXT  sing N N 151 
HIS   CB  CG   sing N N 152 
HIS   CB  HB2  sing N N 153 
HIS   CB  HB3  sing N N 154 
HIS   CG  ND1  sing Y N 155 
HIS   CG  CD2  doub Y N 156 
HIS   ND1 CE1  doub Y N 157 
HIS   ND1 HD1  sing N N 158 
HIS   CD2 NE2  sing Y N 159 
HIS   CD2 HD2  sing N N 160 
HIS   CE1 NE2  sing Y N 161 
HIS   CE1 HE1  sing N N 162 
HIS   NE2 HE2  sing N N 163 
HIS   OXT HXT  sing N N 164 
HOH   O   H1   sing N N 165 
HOH   O   H2   sing N N 166 
ILE   N   CA   sing N N 167 
ILE   N   H    sing N N 168 
ILE   N   H2   sing N N 169 
ILE   CA  C    sing N N 170 
ILE   CA  CB   sing N N 171 
ILE   CA  HA   sing N N 172 
ILE   C   O    doub N N 173 
ILE   C   OXT  sing N N 174 
ILE   CB  CG1  sing N N 175 
ILE   CB  CG2  sing N N 176 
ILE   CB  HB   sing N N 177 
ILE   CG1 CD1  sing N N 178 
ILE   CG1 HG12 sing N N 179 
ILE   CG1 HG13 sing N N 180 
ILE   CG2 HG21 sing N N 181 
ILE   CG2 HG22 sing N N 182 
ILE   CG2 HG23 sing N N 183 
ILE   CD1 HD11 sing N N 184 
ILE   CD1 HD12 sing N N 185 
ILE   CD1 HD13 sing N N 186 
ILE   OXT HXT  sing N N 187 
LEU   N   CA   sing N N 188 
LEU   N   H    sing N N 189 
LEU   N   H2   sing N N 190 
LEU   CA  C    sing N N 191 
LEU   CA  CB   sing N N 192 
LEU   CA  HA   sing N N 193 
LEU   C   O    doub N N 194 
LEU   C   OXT  sing N N 195 
LEU   CB  CG   sing N N 196 
LEU   CB  HB2  sing N N 197 
LEU   CB  HB3  sing N N 198 
LEU   CG  CD1  sing N N 199 
LEU   CG  CD2  sing N N 200 
LEU   CG  HG   sing N N 201 
LEU   CD1 HD11 sing N N 202 
LEU   CD1 HD12 sing N N 203 
LEU   CD1 HD13 sing N N 204 
LEU   CD2 HD21 sing N N 205 
LEU   CD2 HD22 sing N N 206 
LEU   CD2 HD23 sing N N 207 
LEU   OXT HXT  sing N N 208 
LYS   N   CA   sing N N 209 
LYS   N   H    sing N N 210 
LYS   N   H2   sing N N 211 
LYS   CA  C    sing N N 212 
LYS   CA  CB   sing N N 213 
LYS   CA  HA   sing N N 214 
LYS   C   O    doub N N 215 
LYS   C   OXT  sing N N 216 
LYS   CB  CG   sing N N 217 
LYS   CB  HB2  sing N N 218 
LYS   CB  HB3  sing N N 219 
LYS   CG  CD   sing N N 220 
LYS   CG  HG2  sing N N 221 
LYS   CG  HG3  sing N N 222 
LYS   CD  CE   sing N N 223 
LYS   CD  HD2  sing N N 224 
LYS   CD  HD3  sing N N 225 
LYS   CE  NZ   sing N N 226 
LYS   CE  HE2  sing N N 227 
LYS   CE  HE3  sing N N 228 
LYS   NZ  HZ1  sing N N 229 
LYS   NZ  HZ2  sing N N 230 
LYS   NZ  HZ3  sing N N 231 
LYS   OXT HXT  sing N N 232 
MET   N   CA   sing N N 233 
MET   N   H    sing N N 234 
MET   N   H2   sing N N 235 
MET   CA  C    sing N N 236 
MET   CA  CB   sing N N 237 
MET   CA  HA   sing N N 238 
MET   C   O    doub N N 239 
MET   C   OXT  sing N N 240 
MET   CB  CG   sing N N 241 
MET   CB  HB2  sing N N 242 
MET   CB  HB3  sing N N 243 
MET   CG  SD   sing N N 244 
MET   CG  HG2  sing N N 245 
MET   CG  HG3  sing N N 246 
MET   SD  CE   sing N N 247 
MET   CE  HE1  sing N N 248 
MET   CE  HE2  sing N N 249 
MET   CE  HE3  sing N N 250 
MET   OXT HXT  sing N N 251 
PHE   N   CA   sing N N 252 
PHE   N   H    sing N N 253 
PHE   N   H2   sing N N 254 
PHE   CA  C    sing N N 255 
PHE   CA  CB   sing N N 256 
PHE   CA  HA   sing N N 257 
PHE   C   O    doub N N 258 
PHE   C   OXT  sing N N 259 
PHE   CB  CG   sing N N 260 
PHE   CB  HB2  sing N N 261 
PHE   CB  HB3  sing N N 262 
PHE   CG  CD1  doub Y N 263 
PHE   CG  CD2  sing Y N 264 
PHE   CD1 CE1  sing Y N 265 
PHE   CD1 HD1  sing N N 266 
PHE   CD2 CE2  doub Y N 267 
PHE   CD2 HD2  sing N N 268 
PHE   CE1 CZ   doub Y N 269 
PHE   CE1 HE1  sing N N 270 
PHE   CE2 CZ   sing Y N 271 
PHE   CE2 HE2  sing N N 272 
PHE   CZ  HZ   sing N N 273 
PHE   OXT HXT  sing N N 274 
PRO   N   CA   sing N N 275 
PRO   N   CD   sing N N 276 
PRO   N   H    sing N N 277 
PRO   CA  C    sing N N 278 
PRO   CA  CB   sing N N 279 
PRO   CA  HA   sing N N 280 
PRO   C   O    doub N N 281 
PRO   C   OXT  sing N N 282 
PRO   CB  CG   sing N N 283 
PRO   CB  HB2  sing N N 284 
PRO   CB  HB3  sing N N 285 
PRO   CG  CD   sing N N 286 
PRO   CG  HG2  sing N N 287 
PRO   CG  HG3  sing N N 288 
PRO   CD  HD2  sing N N 289 
PRO   CD  HD3  sing N N 290 
PRO   OXT HXT  sing N N 291 
SER   N   CA   sing N N 292 
SER   N   H    sing N N 293 
SER   N   H2   sing N N 294 
SER   CA  C    sing N N 295 
SER   CA  CB   sing N N 296 
SER   CA  HA   sing N N 297 
SER   C   O    doub N N 298 
SER   C   OXT  sing N N 299 
SER   CB  OG   sing N N 300 
SER   CB  HB2  sing N N 301 
SER   CB  HB3  sing N N 302 
SER   OG  HG   sing N N 303 
SER   OXT HXT  sing N N 304 
THR   N   CA   sing N N 305 
THR   N   H    sing N N 306 
THR   N   H2   sing N N 307 
THR   CA  C    sing N N 308 
THR   CA  CB   sing N N 309 
THR   CA  HA   sing N N 310 
THR   C   O    doub N N 311 
THR   C   OXT  sing N N 312 
THR   CB  OG1  sing N N 313 
THR   CB  CG2  sing N N 314 
THR   CB  HB   sing N N 315 
THR   OG1 HG1  sing N N 316 
THR   CG2 HG21 sing N N 317 
THR   CG2 HG22 sing N N 318 
THR   CG2 HG23 sing N N 319 
THR   OXT HXT  sing N N 320 
TRP   N   CA   sing N N 321 
TRP   N   H    sing N N 322 
TRP   N   H2   sing N N 323 
TRP   CA  C    sing N N 324 
TRP   CA  CB   sing N N 325 
TRP   CA  HA   sing N N 326 
TRP   C   O    doub N N 327 
TRP   C   OXT  sing N N 328 
TRP   CB  CG   sing N N 329 
TRP   CB  HB2  sing N N 330 
TRP   CB  HB3  sing N N 331 
TRP   CG  CD1  doub Y N 332 
TRP   CG  CD2  sing Y N 333 
TRP   CD1 NE1  sing Y N 334 
TRP   CD1 HD1  sing N N 335 
TRP   CD2 CE2  doub Y N 336 
TRP   CD2 CE3  sing Y N 337 
TRP   NE1 CE2  sing Y N 338 
TRP   NE1 HE1  sing N N 339 
TRP   CE2 CZ2  sing Y N 340 
TRP   CE3 CZ3  doub Y N 341 
TRP   CE3 HE3  sing N N 342 
TRP   CZ2 CH2  doub Y N 343 
TRP   CZ2 HZ2  sing N N 344 
TRP   CZ3 CH2  sing Y N 345 
TRP   CZ3 HZ3  sing N N 346 
TRP   CH2 HH2  sing N N 347 
TRP   OXT HXT  sing N N 348 
TYR   N   CA   sing N N 349 
TYR   N   H    sing N N 350 
TYR   N   H2   sing N N 351 
TYR   CA  C    sing N N 352 
TYR   CA  CB   sing N N 353 
TYR   CA  HA   sing N N 354 
TYR   C   O    doub N N 355 
TYR   C   OXT  sing N N 356 
TYR   CB  CG   sing N N 357 
TYR   CB  HB2  sing N N 358 
TYR   CB  HB3  sing N N 359 
TYR   CG  CD1  doub Y N 360 
TYR   CG  CD2  sing Y N 361 
TYR   CD1 CE1  sing Y N 362 
TYR   CD1 HD1  sing N N 363 
TYR   CD2 CE2  doub Y N 364 
TYR   CD2 HD2  sing N N 365 
TYR   CE1 CZ   doub Y N 366 
TYR   CE1 HE1  sing N N 367 
TYR   CE2 CZ   sing Y N 368 
TYR   CE2 HE2  sing N N 369 
TYR   CZ  OH   sing N N 370 
TYR   OH  HH   sing N N 371 
TYR   OXT HXT  sing N N 372 
VAL   N   CA   sing N N 373 
VAL   N   H    sing N N 374 
VAL   N   H2   sing N N 375 
VAL   CA  C    sing N N 376 
VAL   CA  CB   sing N N 377 
VAL   CA  HA   sing N N 378 
VAL   C   O    doub N N 379 
VAL   C   OXT  sing N N 380 
VAL   CB  CG1  sing N N 381 
VAL   CB  CG2  sing N N 382 
VAL   CB  HB   sing N N 383 
VAL   CG1 HG11 sing N N 384 
VAL   CG1 HG12 sing N N 385 
VAL   CG1 HG13 sing N N 386 
VAL   CG2 HG21 sing N N 387 
VAL   CG2 HG22 sing N N 388 
VAL   CG2 HG23 sing N N 389 
VAL   OXT HXT  sing N N 390 
# 
_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                    7HBJ 
_atom_sites.fract_transf_matrix[1][1]   0.014319 
_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]   0.011277 
_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.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 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   ? 9.06218   15.68039 10.59391 1.000 64.20318  ? 16  GLU   A N   1 
ATOM   2    C  CA  . GLU   A 1 9   ? 10.28811  16.46831 10.54480 1.000 68.59956  ? 16  GLU   A CA  1 
ATOM   3    C  C   . GLU   A 1 9   ? 10.31125  17.48176 11.68572 1.000 65.88909  ? 16  GLU   A C   1 
ATOM   4    O  O   . GLU   A 1 9   ? 9.53654   18.43924 11.69353 1.000 83.33236  ? 16  GLU   A O   1 
ATOM   5    C  CB  . GLU   A 1 9   ? 10.41642  17.17402 9.19282  1.000 68.69746  ? 16  GLU   A CB  1 
ATOM   6    C  CG  . GLU   A 1 9   ? 11.84830  17.46028 8.76610  1.000 78.95480  ? 16  GLU   A CG  1 
ATOM   7    C  CD  . GLU   A 1 9   ? 12.19885  18.93480 8.85000  1.000 95.61852  ? 16  GLU   A CD  1 
ATOM   8    O  OE1 . GLU   A 1 9   ? 11.37102  19.71662 9.36526  1.000 80.67693  ? 16  GLU   A OE1 1 
ATOM   9    O  OE2 . GLU   A 1 9   ? 13.30024  19.31350 8.39577  1.000 83.12491  ? 16  GLU   A OE2 1 
ATOM   10   N  N   . VAL   A 1 10  ? 11.20258  17.26234 12.65004 1.000 56.12552  ? 17  VAL   A N   1 
ATOM   11   C  CA  . VAL   A 1 10  ? 11.29102  18.07712 13.85627 1.000 47.30344  ? 17  VAL   A CA  1 
ATOM   12   C  C   . VAL   A 1 10  ? 12.62895  18.80138 13.85967 1.000 46.28351  ? 17  VAL   A C   1 
ATOM   13   O  O   . VAL   A 1 10  ? 13.67824  18.17877 13.66043 1.000 47.25447  ? 17  VAL   A O   1 
ATOM   14   C  CB  . VAL   A 1 10  ? 11.13472  17.22514 15.12951 1.000 46.83588  ? 17  VAL   A CB  1 
ATOM   15   C  CG1 . VAL   A 1 10  ? 10.69421  18.09315 16.29984 1.000 44.50370  ? 17  VAL   A CG1 1 
ATOM   16   C  CG2 . VAL   A 1 10  ? 10.15420  16.08014 14.89256 1.000 49.13039  ? 17  VAL   A CG2 1 
ATOM   17   N  N   . GLU   A 1 11  ? 12.58887  20.10978 14.09231 1.000 44.71448  ? 18  GLU   A N   1 
ATOM   18   C  CA  . GLU   A 1 11  ? 13.78600  20.93151 14.21388 1.000 44.01895  ? 18  GLU   A CA  1 
ATOM   19   C  C   . GLU   A 1 11  ? 14.02261  21.26272 15.68154 1.000 42.09187  ? 18  GLU   A C   1 
ATOM   20   O  O   . GLU   A 1 11  ? 13.11297  21.73928 16.36881 1.000 40.80710  ? 18  GLU   A O   1 
ATOM   21   C  CB  . GLU   A 1 11  ? 13.65219  22.22123 13.40105 1.000 44.31754  ? 18  GLU   A CB  1 
ATOM   22   C  CG  . GLU   A 1 11  ? 13.78235  22.05188 11.89359 1.000 52.74312  ? 18  GLU   A CG  1 
ATOM   23   C  CD  . GLU   A 1 11  ? 13.59730  23.36127 11.13988 1.000 61.28054  ? 18  GLU   A CD  1 
ATOM   24   O  OE1 . GLU   A 1 11  ? 12.52021  23.98412 11.27400 1.000 47.07471  ? 18  GLU   A OE1 1 
ATOM   25   O  OE2 . GLU   A 1 11  ? 14.53147  23.76868 10.41532 1.000 55.68149  ? 18  GLU   A OE2 1 
ATOM   26   N  N   . THR   A 1 12  ? 15.23950  21.01407 16.15652 1.000 42.25198  ? 19  THR   A N   1 
ATOM   27   C  CA  . THR   A 1 12  ? 15.62084  21.29852 17.53409 1.000 41.04034  ? 19  THR   A CA  1 
ATOM   28   C  C   . THR   A 1 12  ? 16.51950  22.52889 17.56736 1.000 40.88427  ? 19  THR   A C   1 
ATOM   29   O  O   . THR   A 1 12  ? 17.48494  22.61790 16.80221 1.000 42.26290  ? 19  THR   A O   1 
ATOM   30   C  CB  . THR   A 1 12  ? 16.33398  20.10095 18.16849 1.000 42.00911  ? 19  THR   A CB  1 
ATOM   31   O  OG1 . THR   A 1 12  ? 15.76200  18.88220 17.67575 1.000 43.17444  ? 19  THR   A OG1 1 
ATOM   32   C  CG2 . THR   A 1 12  ? 16.19361  20.13891 19.68326 1.000 41.05126  ? 19  THR   A CG2 1 
ATOM   33   N  N   . PHE   A 1 13  ? 16.19482  23.47543 18.44601 1.000 39.56295  ? 20  PHE   A N   1 
ATOM   34   C  CA  . PHE   A 1 13  ? 16.94694  24.71200 18.59501 1.000 39.74024  ? 20  PHE   A CA  1 
ATOM   35   C  C   . PHE   A 1 13  ? 17.38290  24.88119 20.04375 1.000 39.28969  ? 20  PHE   A C   1 
ATOM   36   O  O   . PHE   A 1 13  ? 16.75763  24.35880 20.97031 1.000 38.40063  ? 20  PHE   A O   1 
ATOM   37   C  CB  . PHE   A 1 13  ? 16.12879  25.94483 18.16944 1.000 39.23373  ? 20  PHE   A CB  1 
ATOM   38   C  CG  . PHE   A 1 13  ? 15.35891  25.76595 16.89068 1.000 39.83433  ? 20  PHE   A CG  1 
ATOM   39   C  CD1 . PHE   A 1 13  ? 14.12847  25.12144 16.88216 1.000 39.22419  ? 20  PHE   A CD1 1 
ATOM   40   C  CD2 . PHE   A 1 13  ? 15.85734  26.26076 15.69851 1.000 41.47710  ? 20  PHE   A CD2 1 
ATOM   41   C  CE1 . PHE   A 1 13  ? 13.42123  24.96127 15.70590 1.000 40.30711  ? 20  PHE   A CE1 1 
ATOM   42   C  CE2 . PHE   A 1 13  ? 15.15418  26.10480 14.51933 1.000 43.41066  ? 20  PHE   A CE2 1 
ATOM   43   C  CZ  . PHE   A 1 13  ? 13.93598  25.45434 14.52281 1.000 41.94970  ? 20  PHE   A CZ  1 
ATOM   44   N  N   . ALA   A 1 14  ? 18.46225  25.63456 20.22877 1.000 43.78471  ? 21  ALA   A N   1 
ATOM   45   C  CA  . ALA   A 1 14  ? 18.98188  25.92419 21.55479 1.000 40.54220  ? 21  ALA   A CA  1 
ATOM   46   C  C   . ALA   A 1 14  ? 18.38702  27.21987 22.09644 1.000 45.08043  ? 21  ALA   A C   1 
ATOM   47   O  O   . ALA   A 1 14  ? 18.24565  28.21226 21.37394 1.000 39.92926  ? 21  ALA   A O   1 
ATOM   48   C  CB  . ALA   A 1 14  ? 20.50736  26.01579 21.52353 1.000 42.79370  ? 21  ALA   A CB  1 
ATOM   49   N  N   . PHE   A 1 15  ? 18.02083  27.18856 23.37252 1.000 39.00656  ? 22  PHE   A N   1 
ATOM   50   C  CA  . PHE   A 1 15  ? 17.57317  28.37926 24.07870 1.000 40.45966  ? 22  PHE   A CA  1 
ATOM   51   C  C   . PHE   A 1 15  ? 18.68217  29.42571 24.10493 1.000 46.99180  ? 22  PHE   A C   1 
ATOM   52   O  O   . PHE   A 1 15  ? 19.87214  29.09866 24.09161 1.000 45.24090  ? 22  PHE   A O   1 
ATOM   53   C  CB  . PHE   A 1 15  ? 17.19090  27.98493 25.50036 1.000 38.11705  ? 22  PHE   A CB  1 
ATOM   54   C  CG  . PHE   A 1 15  ? 15.81020  27.42430 25.62704 1.000 36.47134  ? 22  PHE   A CG  1 
ATOM   55   C  CD1 . PHE   A 1 15  ? 14.87134  27.59791 24.63059 1.000 40.04016  ? 22  PHE   A CD1 1 
ATOM   56   C  CD2 . PHE   A 1 15  ? 15.50183  26.58625 26.67874 1.000 38.47060  ? 22  PHE   A CD2 1 
ATOM   57   C  CE1 . PHE   A 1 15  ? 13.60490  27.05065 24.75152 1.000 40.98620  ? 22  PHE   A CE1 1 
ATOM   58   C  CE2 . PHE   A 1 15  ? 14.25144  26.01372 26.78549 1.000 45.22146  ? 22  PHE   A CE2 1 
ATOM   59   C  CZ  . PHE   A 1 15  ? 13.30042  26.25196 25.82548 1.000 40.93870  ? 22  PHE   A CZ  1 
ATOM   60   N  N   . GLN   A 1 16  ? 18.29107  30.69730 24.13871 1.000 40.55430  ? 23  GLN   A N   1 
ATOM   61   C  CA  . GLN   A 1 16  ? 19.26266  31.73797 24.43840 1.000 42.77749  ? 23  GLN   A CA  1 
ATOM   62   C  C   . GLN   A 1 16  ? 19.68965  31.60924 25.89269 1.000 43.55605  ? 23  GLN   A C   1 
ATOM   63   O  O   . GLN   A 1 16  ? 18.87043  31.31697 26.76846 1.000 45.82226  ? 23  GLN   A O   1 
ATOM   64   C  CB  . GLN   A 1 16  ? 18.68918  33.12622 24.15794 1.000 43.09491  ? 23  GLN   A CB  1 
ATOM   65   C  CG  . GLN   A 1 16  ? 18.81816  33.54481 22.70080 1.000 44.03653  ? 23  GLN   A CG  1 
ATOM   66   C  CD  . GLN   A 1 16  ? 17.73278  34.50735 22.26141 1.000 64.20020  ? 23  GLN   A CD  1 
ATOM   67   O  OE1 . GLN   A 1 16  ? 16.93413  34.97205 23.07216 1.000 69.45736  ? 23  GLN   A OE1 1 
ATOM   68   N  NE2 . GLN   A 1 16  ? 17.70430  34.81842 20.97061 1.000 63.59389  ? 23  GLN   A NE2 1 
ATOM   69   N  N   . ALA   A 1 17  ? 20.98909  31.80812 26.13705 1.000 46.18541  ? 24  ALA   A N   1 
ATOM   70   C  CA  . ALA   A 1 17  ? 21.58140  31.46374 27.42699 1.000 47.62919  ? 24  ALA   A CA  1 
ATOM   71   C  C   . ALA   A 1 17  ? 20.83962  32.11501 28.58553 1.000 47.21195  ? 24  ALA   A C   1 
ATOM   72   O  O   . ALA   A 1 17  ? 20.60543  31.47896 29.61952 1.000 46.99142  ? 24  ALA   A O   1 
ATOM   73   C  CB  . ALA   A 1 17  ? 23.05778  31.86297 27.44368 1.000 52.85412  ? 24  ALA   A CB  1 
ATOM   74   N  N   . GLU   A 1 18  ? 20.46057  33.38288 28.42982 1.000 47.44435  ? 25  GLU   A N   1 
ATOM   75   C  CA  . GLU   A 1 18  ? 19.70087  34.06396 29.47188 1.000 47.21493  ? 25  GLU   A CA  1 
ATOM   76   C  C   . GLU   A 1 18  ? 18.36420  33.37280 29.70813 1.000 44.24978  ? 25  GLU   A C   1 
ATOM   77   O  O   . GLU   A 1 18  ? 17.97915  33.10905 30.85346 1.000 44.17106  ? 25  GLU   A O   1 
ATOM   78   C  CB  . GLU   A 1 18  ? 19.49076  35.53270 29.09232 1.000 48.23788  ? 25  GLU   A CB  1 
ATOM   79   C  CG  . GLU   A 1 18  ? 20.73856  36.25718 28.57726 1.000 60.56055  ? 25  GLU   A CG  1 
ATOM   80   C  CD  . GLU   A 1 18  ? 21.06589  35.94607 27.12099 1.000 61.54927  ? 25  GLU   A CD  1 
ATOM   81   O  OE1 . GLU   A 1 18  ? 20.47412  35.00042 26.55892 1.000 72.70530  ? 25  GLU   A OE1 1 
ATOM   82   O  OE2 . GLU   A 1 18  ? 21.91871  36.64758 26.53797 1.000 70.12572  ? 25  GLU   A OE2 1 
ATOM   83   N  N   . ILE   A 1 19  ? 17.64888  33.05503 28.62784 1.000 42.19807  ? 26  ILE   A N   1 
ATOM   84   C  CA  . ILE   A 1 19  ? 16.32715  32.45649 28.76634 1.000 39.84035  ? 26  ILE   A CA  1 
ATOM   85   C  C   . ILE   A 1 19  ? 16.43890  31.02895 29.28860 1.000 40.78472  ? 26  ILE   A C   1 
ATOM   86   O  O   . ILE   A 1 19  ? 15.61081  30.58037 30.09058 1.000 38.61928  ? 26  ILE   A O   1 
ATOM   87   C  CB  . ILE   A 1 19  ? 15.57260  32.52088 27.42801 1.000 38.43889  ? 26  ILE   A CB  1 
ATOM   88   C  CG1 . ILE   A 1 19  ? 15.71804  33.89741 26.79248 1.000 47.55328  ? 26  ILE   A CG1 1 
ATOM   89   C  CG2 . ILE   A 1 19  ? 14.11310  32.32315 27.65052 1.000 36.72551  ? 26  ILE   A CG2 1 
ATOM   90   C  CD1 . ILE   A 1 19  ? 15.04338  33.99078 25.44568 1.000 39.47219  ? 26  ILE   A CD1 1 
ATOM   91   N  N   . ALA   A 1 20  ? 17.46274  30.29406 28.84628 1.000 40.32676  ? 27  ALA   A N   1 
ATOM   92   C  CA  . ALA   A 1 20  ? 17.73024  28.97725 29.41584 1.000 46.95992  ? 27  ALA   A CA  1 
ATOM   93   C  C   . ALA   A 1 20  ? 18.05846  29.07989 30.89973 1.000 42.41315  ? 27  ALA   A C   1 
ATOM   94   O  O   . ALA   A 1 20  ? 17.65029  28.22716 31.69701 1.000 42.43721  ? 27  ALA   A O   1 
ATOM   95   C  CB  . ALA   A 1 20  ? 18.87424  28.30192 28.65880 1.000 41.91329  ? 27  ALA   A CB  1 
ATOM   96   N  N   . GLN   A 1 21  ? 18.79027  30.12656 31.28766 1.000 44.29014  ? 28  GLN   A N   1 
ATOM   97   C  CA  . GLN   A 1 21  ? 19.13329  30.32535 32.69070 1.000 46.45357  ? 28  GLN   A CA  1 
ATOM   98   C  C   . GLN   A 1 21  ? 17.90093  30.59003 33.54791 1.000 45.30604  ? 28  GLN   A C   1 
ATOM   99   O  O   . GLN   A 1 21  ? 17.87695  30.21874 34.72708 1.000 46.68031  ? 28  GLN   A O   1 
ATOM   100  C  CB  . GLN   A 1 21  ? 20.12307  31.48072 32.81576 1.000 49.06465  ? 28  GLN   A CB  1 
ATOM   101  C  CG  . GLN   A 1 21  ? 21.24705  31.24641 33.79729 1.000 52.61418  ? 28  GLN   A CG  1 
ATOM   102  C  CD  . GLN   A 1 21  ? 21.97265  32.52902 34.13835 1.000 63.25606  ? 28  GLN   A CD  1 
ATOM   103  O  OE1 . GLN   A 1 21  ? 22.53185  33.18782 33.26193 1.000 64.27026  ? 28  GLN   A OE1 1 
ATOM   104  N  NE2 . GLN   A 1 21  ? 21.96000  32.89744 35.41458 1.000 62.81149  ? 28  GLN   A NE2 1 
ATOM   105  N  N   . LEU   A 1 22  ? 16.87145  31.22757 32.98133 1.000 50.11692  ? 29  LEU   A N   1 
ATOM   106  C  CA  . LEU   A 1 22  ? 15.67820  31.53971 33.76417 1.000 42.36107  ? 29  LEU   A CA  1 
ATOM   107  C  C   . LEU   A 1 22  ? 14.87275  30.28761 34.08777 1.000 41.24449  ? 29  LEU   A C   1 
ATOM   108  O  O   . LEU   A 1 22  ? 14.40368  30.12481 35.21904 1.000 42.02188  ? 29  LEU   A O   1 
ATOM   109  C  CB  . LEU   A 1 22  ? 14.80124  32.54681 33.02510 1.000 40.86889  ? 29  LEU   A CB  1 
ATOM   110  C  CG  . LEU   A 1 22  ? 13.60347  33.07400 33.82261 1.000 40.47685  ? 29  LEU   A CG  1 
ATOM   111  C  CD1 . LEU   A 1 22  ? 14.04073  33.59838 35.18442 1.000 42.85859  ? 29  LEU   A CD1 1 
ATOM   112  C  CD2 . LEU   A 1 22  ? 12.83384  34.13338 33.04614 1.000 39.60678  ? 29  LEU   A CD2 1 
ATOM   113  N  N   . MET   A 1 23  ? 14.68659  29.39726 33.11073 1.000 39.79310  ? 30  MET   A N   1 
ATOM   114  C  CA  . MET   A 1 23  ? 13.87510  28.21080 33.36312 1.000 44.75115  ? 30  MET   A CA  1 
ATOM   115  C  C   . MET   A 1 23  ? 14.57440  27.22023 34.28561 1.000 41.25316  ? 30  MET   A C   1 
ATOM   116  O  O   . MET   A 1 23  ? 13.90301  26.50423 35.03693 1.000 44.63974  ? 30  MET   A O   1 
ATOM   117  C  CB  . MET   A 1 23  ? 13.47901  27.54967 32.04465 1.000 46.65857  ? 30  MET   A CB  1 
ATOM   118  C  CG  . MET   A 1 23  ? 13.10239  28.54067 30.95744 1.000 49.32554  ? 30  MET   A CG  1 
ATOM   119  S  SD  . MET   A 1 23  ? 12.78762  27.75118 29.36653 1.000 38.12167  ? 30  MET   A SD  1 
ATOM   120  C  CE  . MET   A 1 23  ? 13.30410  29.04346 28.24957 1.000 41.49858  ? 30  MET   A CE  1 
ATOM   121  N  N   . SER   A 1 24  ? 15.90702  27.16252 34.25883 1.000 42.96186  ? 31  SER   A N   1 
ATOM   122  C  CA  . SER   A 1 24  ? 16.60403  26.38560 35.27790 1.000 45.67128  ? 31  SER   A CA  1 
ATOM   123  C  C   . SER   A 1 24  ? 16.42136  27.00570 36.65556 1.000 47.35109  ? 31  SER   A C   1 
ATOM   124  O  O   . SER   A 1 24  ? 16.31909  26.28374 37.65347 1.000 49.22671  ? 31  SER   A O   1 
ATOM   125  C  CB  . SER   A 1 24  ? 18.08822  26.26581 34.93566 1.000 49.00346  ? 31  SER   A CB  1 
ATOM   126  O  OG  . SER   A 1 24  ? 18.26592  26.04903 33.54787 1.000 49.94110  ? 31  SER   A OG  1 
ATOM   127  N  N   . LEU   A 1 25  ? 16.36153  28.33645 36.72530 1.000 47.05473  ? 32  LEU   A N   1 
ATOM   128  C  CA  . LEU   A 1 25  ? 16.08774  29.00335 37.99295 1.000 51.64432  ? 32  LEU   A CA  1 
ATOM   129  C  C   . LEU   A 1 25  ? 14.66587  28.72578 38.46816 1.000 47.76167  ? 32  LEU   A C   1 
ATOM   130  O  O   . LEU   A 1 25  ? 14.43570  28.51575 39.66430 1.000 49.43682  ? 32  LEU   A O   1 
ATOM   131  C  CB  . LEU   A 1 25  ? 16.32370  30.50719 37.84767 1.000 48.90733  ? 32  LEU   A CB  1 
ATOM   132  C  CG  . LEU   A 1 25  ? 16.20412  31.37576 39.10064 1.000 52.09438  ? 32  LEU   A CG  1 
ATOM   133  C  CD1 . LEU   A 1 25  ? 17.18942  30.92824 40.17031 1.000 54.92697  ? 32  LEU   A CD1 1 
ATOM   134  C  CD2 . LEU   A 1 25  ? 16.41291  32.84056 38.74560 1.000 54.44036  ? 32  LEU   A CD2 1 
ATOM   135  N  N   . ILE   A 1 26  ? 13.70261  28.70649 37.54424 1.000 44.61467  ? 33  ILE   A N   1 
ATOM   136  C  CA  . ILE   A 1 26  ? 12.29920  28.57579 37.92765 1.000 56.13090  ? 33  ILE   A CA  1 
ATOM   137  C  C   . ILE   A 1 26  ? 11.99564  27.15212 38.37957 1.000 55.72908  ? 33  ILE   A C   1 
ATOM   138  O  O   . ILE   A 1 26  ? 11.33660  26.93566 39.40405 1.000 50.25428  ? 33  ILE   A O   1 
ATOM   139  C  CB  . ILE   A 1 26  ? 11.38530  29.00837 36.76597 1.000 44.91950  ? 33  ILE   A CB  1 
ATOM   140  C  CG1 . ILE   A 1 26  ? 11.18366  30.52449 36.77712 1.000 40.73039  ? 33  ILE   A CG1 1 
ATOM   141  C  CG2 . ILE   A 1 26  ? 10.04321  28.29365 36.83377 1.000 40.20701  ? 33  ILE   A CG2 1 
ATOM   142  C  CD1 . ILE   A 1 26  ? 10.97766  31.11571 35.40037 1.000 38.85647  ? 33  ILE   A CD1 1 
ATOM   143  N  N   . ILE   A 1 27  ? 12.47220  26.16094 37.62396 1.000 44.35176  ? 34  ILE   A N   1 
ATOM   144  C  CA  . ILE   A 1 27  ? 12.17025  24.77012 37.94662 1.000 45.59304  ? 34  ILE   A CA  1 
ATOM   145  C  C   . ILE   A 1 27  ? 12.80368  24.37040 39.27420 1.000 53.13893  ? 34  ILE   A C   1 
ATOM   146  O  O   . ILE   A 1 27  ? 12.16710  23.71730 40.10952 1.000 70.67795  ? 34  ILE   A O   1 
ATOM   147  C  CB  . ILE   A 1 27  ? 12.63230  23.84548 36.80541 1.000 48.19160  ? 34  ILE   A CB  1 
ATOM   148  C  CG1 . ILE   A 1 27  ? 11.79517  24.07369 35.54873 1.000 44.87454  ? 34  ILE   A CG1 1 
ATOM   149  C  CG2 . ILE   A 1 27  ? 12.54148  22.38945 37.22609 1.000 60.09328  ? 34  ILE   A CG2 1 
ATOM   150  C  CD1 . ILE   A 1 27  ? 12.30327  23.31377 34.34422 1.000 41.47987  ? 34  ILE   A CD1 1 
ATOM   151  N  N   . ASN   A 1 28  ? 14.05349  24.76806 39.50023 1.000 50.56972  ? 35  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 28  ? 14.84541  24.19953 40.58193 1.000 61.31192  ? 35  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 28  ? 14.69189  24.92611 41.91287 1.000 74.75496  ? 35  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 28  ? 14.94098  24.31765 42.96054 1.000 85.73539  ? 35  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 28  ? 16.32353  24.17501 40.17814 1.000 69.75662  ? 35  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 28  ? 16.57823  23.30416 38.95821 1.000 60.86747  ? 35  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 28  ? 17.35052  23.66606 38.06967 1.000 66.16813  ? 35  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 28  ? 15.92816  22.14722 38.91286 1.000 54.46883  ? 35  ASN   A ND2 1 
ATOM   159  N  N   . THR   A 1 29  ? 14.29764  26.19755 41.90747 1.000 77.62123  ? 36  THR   A N   1 
ATOM   160  C  CA  . THR   A 1 29  ? 14.19830  26.95735 43.14667 1.000 84.75526  ? 36  THR   A CA  1 
ATOM   161  C  C   . THR   A 1 29  ? 12.89057  26.64309 43.86208 1.000 60.16193  ? 36  THR   A C   1 
ATOM   162  O  O   . THR   A 1 29  ? 11.82272  26.60151 43.24535 1.000 54.85559  ? 36  THR   A O   1 
ATOM   163  C  CB  . THR   A 1 29  ? 14.29611  28.46040 42.87203 1.000 81.42480  ? 36  THR   A CB  1 
ATOM   164  O  OG1 . THR   A 1 29  ? 15.58720  28.76847 42.32810 1.000 83.81433  ? 36  THR   A OG1 1 
ATOM   165  C  CG2 . THR   A 1 29  ? 14.08963  29.25495 44.15857 1.000 58.84765  ? 36  THR   A CG2 1 
ATOM   166  N  N   . PHE   A 1 30  ? 12.98545  26.40374 45.16922 1.000 73.81938  ? 37  PHE   A N   1 
ATOM   167  C  CA  . PHE   A 1 30  ? 11.80092  26.20513 45.99461 1.000 62.25315  ? 37  PHE   A CA  1 
ATOM   168  C  C   . PHE   A 1 30  ? 11.02547  27.51300 46.05864 1.000 71.79385  ? 37  PHE   A C   1 
ATOM   169  O  O   . PHE   A 1 30  ? 11.57858  28.55601 46.42260 1.000 79.37631  ? 37  PHE   A O   1 
ATOM   170  C  CB  . PHE   A 1 30  ? 12.21105  25.72229 47.39182 1.000 70.12824  ? 37  PHE   A CB  1 
ATOM   171  C  CG  . PHE   A 1 30  ? 11.05090  25.44862 48.34388 1.000 81.35965  ? 37  PHE   A CG  1 
ATOM   172  C  CD1 . PHE   A 1 30  ? 10.15258  26.44131 48.71546 1.000 68.17971  ? 37  PHE   A CD1 1 
ATOM   173  C  CD2 . PHE   A 1 30  ? 10.85346  24.17026 48.84428 1.000 71.76203  ? 37  PHE   A CD2 1 
ATOM   174  C  CE1 . PHE   A 1 30  ? 9.10756   26.16911 49.56968 1.000 70.07678  ? 37  PHE   A CE1 1 
ATOM   175  C  CE2 . PHE   A 1 30  ? 9.80281   23.89997 49.68988 1.000 73.74533  ? 37  PHE   A CE2 1 
ATOM   176  C  CZ  . PHE   A 1 30  ? 8.93500   24.90205 50.05747 1.000 78.85342  ? 37  PHE   A CZ  1 
ATOM   177  N  N   . TYR   A 1 31  ? 9.73778   27.45187 45.72527 1.000 68.38620  ? 38  TYR   A N   1 
ATOM   178  C  CA  . TYR   A 1 31  ? 8.89217   28.64088 45.74414 1.000 71.21459  ? 38  TYR   A CA  1 
ATOM   179  C  C   . TYR   A 1 31  ? 7.45150   28.13877 45.78756 1.000 63.71410  ? 38  TYR   A C   1 
ATOM   180  O  O   . TYR   A 1 31  ? 6.92817   27.67988 44.77144 1.000 53.96726  ? 38  TYR   A O   1 
ATOM   181  C  CB  . TYR   A 1 31  ? 9.15071   29.51877 44.53234 1.000 53.87050  ? 38  TYR   A CB  1 
ATOM   182  C  CG  . TYR   A 1 31  ? 8.24489   30.71982 44.44487 1.000 52.65745  ? 38  TYR   A CG  1 
ATOM   183  C  CD1 . TYR   A 1 31  ? 8.42209   31.80781 45.28894 1.000 54.67290  ? 38  TYR   A CD1 1 
ATOM   184  C  CD2 . TYR   A 1 31  ? 7.22207   30.77499 43.50889 1.000 58.26757  ? 38  TYR   A CD2 1 
ATOM   185  C  CE1 . TYR   A 1 31  ? 7.59835   32.91163 45.21153 1.000 56.14989  ? 38  TYR   A CE1 1 
ATOM   186  C  CE2 . TYR   A 1 31  ? 6.39642   31.87642 43.42137 1.000 54.48587  ? 38  TYR   A CE2 1 
ATOM   187  C  CZ  . TYR   A 1 31  ? 6.58856   32.93960 44.27572 1.000 59.52939  ? 38  TYR   A CZ  1 
ATOM   188  O  OH  . TYR   A 1 31  ? 5.76674   34.03530 44.19405 1.000 60.11001  ? 38  TYR   A OH  1 
ATOM   189  N  N   . SER   A 1 32  ? 6.83014   28.22839 46.96318 1.000 68.70904  ? 39  SER   A N   1 
ATOM   190  C  CA  . SER   A 1 32  ? 5.55848   27.54707 47.17438 1.000 59.61963  ? 39  SER   A CA  1 
ATOM   191  C  C   . SER   A 1 32  ? 4.41747   28.19078 46.39807 1.000 57.45551  ? 39  SER   A C   1 
ATOM   192  O  O   . SER   A 1 32  ? 3.43334   27.51331 46.08038 1.000 56.50781  ? 39  SER   A O   1 
ATOM   193  C  CB  . SER   A 1 32  ? 5.22889   27.50961 48.66396 1.000 63.66623  ? 39  SER   A CB  1 
ATOM   194  O  OG  . SER   A 1 32  ? 5.92816   26.45959 49.30918 1.000 66.81563  ? 39  SER   A OG  1 
ATOM   195  N  N   . ASN   A 1 33  ? 4.52111   29.48171 46.08069 1.000 58.45094  ? 40  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 33  ? 3.44484   30.19306 45.38899 1.000 58.67769  ? 40  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 33  ? 3.42745   29.83850 43.89882 1.000 50.11116  ? 40  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 33  ? 3.60698   30.67704 43.01689 1.000 48.03683  ? 40  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 33  ? 3.58519   31.69326 45.60326 1.000 53.29811  ? 40  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 33  ? 2.29108   32.43530 45.36107 1.000 55.91391  ? 40  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 33  ? 1.20836   31.93874 45.67551 1.000 53.62664  ? 40  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 33  ? 2.39478   33.63770 44.81053 1.000 65.81312  ? 40  ASN   A ND2 1 
ATOM   203  N  N   . LYS   A 1 34  ? 3.17671   28.55546 43.63235 1.000 50.10768  ? 41  LYS   A N   1 
ATOM   204  C  CA  . LYS   A 1 34  ? 3.21358   28.04255 42.26881 1.000 51.67989  ? 41  LYS   A CA  1 
ATOM   205  C  C   . LYS   A 1 34  ? 2.00001   28.45597 41.45001 1.000 45.62307  ? 41  LYS   A C   1 
ATOM   206  O  O   . LYS   A 1 34  ? 2.07012   28.43882 40.21735 1.000 44.72562  ? 41  LYS   A O   1 
ATOM   207  C  CB  . LYS   A 1 34  ? 3.31584   26.51739 42.29108 1.000 49.55649  ? 41  LYS   A CB  1 
ATOM   208  C  CG  . LYS   A 1 34  ? 4.29991   25.98408 43.30757 1.000 52.80376  ? 41  LYS   A CG  1 
ATOM   209  C  CD  . LYS   A 1 34  ? 5.68711   25.89863 42.70937 1.000 58.76615  ? 41  LYS   A CD  1 
ATOM   210  C  CE  . LYS   A 1 34  ? 5.78814   24.76483 41.72039 1.000 55.66825  ? 41  LYS   A CE  1 
ATOM   211  N  NZ  . LYS   A 1 34  ? 6.31926   23.52745 42.35104 1.000 58.28477  ? 41  LYS   A NZ  1 
ATOM   212  N  N   . GLU   A 1 35  ? 0.89955   28.83611 42.10355 1.000 45.23747  ? 42  GLU   A N   1 
ATOM   213  C  CA  . GLU   A 1 35  ? -0.36375  29.05245 41.40555 1.000 41.55521  ? 42  GLU   A CA  1 
ATOM   214  C  C   . GLU   A 1 35  ? -0.33172  30.24881 40.46089 1.000 45.92476  ? 42  GLU   A C   1 
ATOM   215  O  O   . GLU   A 1 35  ? -1.20053  30.34883 39.58645 1.000 44.57608  ? 42  GLU   A O   1 
ATOM   216  C  CB  . GLU   A 1 35  ? -1.49322  29.22255 42.42170 1.000 41.02869  ? 42  GLU   A CB  1 
ATOM   217  C  CG  . GLU   A 1 35  ? -1.40965  30.49848 43.23845 1.000 42.05343  ? 42  GLU   A CG  1 
ATOM   218  C  CD  . GLU   A 1 35  ? -2.57936  30.65176 44.18541 1.000 43.21497  ? 42  GLU   A CD  1 
ATOM   219  O  OE1 . GLU   A 1 35  ? -2.78314  29.74523 45.02053 1.000 43.05715  ? 42  GLU   A OE1 1 
ATOM   220  O  OE2 . GLU   A 1 35  ? -3.29329  31.67353 44.09596 1.000 43.81777  ? 42  GLU   A OE2 1 
ATOM   221  N  N   . ILE   A 1 36  ? 0.64389   31.14939 40.60574 1.000 42.19641  ? 43  ILE   A N   1 
ATOM   222  C  CA  . ILE   A 1 36  ? 0.74071   32.31598 39.73862 1.000 41.60499  ? 43  ILE   A CA  1 
ATOM   223  C  C   . ILE   A 1 36  ? 0.99253   31.94678 38.28274 1.000 45.68357  ? 43  ILE   A C   1 
ATOM   224  O  O   . ILE   A 1 36  ? 0.87779   32.81091 37.40610 1.000 39.87486  ? 43  ILE   A O   1 
ATOM   225  C  CB  . ILE   A 1 36  ? 1.83960   33.27488 40.25259 1.000 45.35258  ? 43  ILE   A CB  1 
ATOM   226  C  CG1 . ILE   A 1 36  ? 3.22753   32.63842 40.13119 1.000 46.73850  ? 43  ILE   A CG1 1 
ATOM   227  C  CG2 . ILE   A 1 36  ? 1.57049   33.66421 41.68949 1.000 51.80563  ? 43  ILE   A CG2 1 
ATOM   228  C  CD1 . ILE   A 1 36  ? 4.08383   33.22408 39.02366 1.000 47.66356  ? 43  ILE   A CD1 1 
ATOM   229  N  N   . PHE   A 1 37  ? 1.33346   30.68280 38.00476 1.000 41.23359  ? 44  PHE   A N   1 
ATOM   230  C  CA  . PHE   A 1 37  ? 1.52840   30.24546 36.62554 1.000 40.83928  ? 44  PHE   A CA  1 
ATOM   231  C  C   . PHE   A 1 37  ? 0.24834   30.39639 35.81379 1.000 38.20680  ? 44  PHE   A C   1 
ATOM   232  O  O   . PHE   A 1 37  ? 0.29496   30.72263 34.62221 1.000 37.66893  ? 44  PHE   A O   1 
ATOM   233  C  CB  . PHE   A 1 37  ? 2.01719   28.79352 36.59745 1.000 42.28045  ? 44  PHE   A CB  1 
ATOM   234  C  CG  . PHE   A 1 37  ? 0.90954   27.77120 36.68467 1.000 40.86806  ? 44  PHE   A CG  1 
ATOM   235  C  CD1 . PHE   A 1 37  ? 0.37780   27.40925 37.91062 1.000 40.75672  ? 44  PHE   A CD1 1 
ATOM   236  C  CD2 . PHE   A 1 37  ? 0.40096   27.17396 35.54183 1.000 40.04416  ? 44  PHE   A CD2 1 
ATOM   237  C  CE1 . PHE   A 1 37  ? -0.63790  26.47499 37.99725 1.000 39.85348  ? 44  PHE   A CE1 1 
ATOM   238  C  CE2 . PHE   A 1 37  ? -0.61818  26.24021 35.62419 1.000 40.02821  ? 44  PHE   A CE2 1 
ATOM   239  C  CZ  . PHE   A 1 37  ? -1.13598  25.89017 36.85271 1.000 39.15871  ? 44  PHE   A CZ  1 
ATOM   240  N  N   . LEU   A 1 38  ? -0.90647  30.16300 36.44287 1.000 36.87824  ? 45  LEU   A N   1 
ATOM   241  C  CA  . LEU   A 1 38  ? -2.17404  30.28962 35.73289 1.000 34.87044  ? 45  LEU   A CA  1 
ATOM   242  C  C   . LEU   A 1 38  ? -2.49740  31.74932 35.43622 1.000 33.98499  ? 45  LEU   A C   1 
ATOM   243  O  O   . LEU   A 1 38  ? -2.95152  32.07798 34.33358 1.000 33.40586  ? 45  LEU   A O   1 
ATOM   244  C  CB  . LEU   A 1 38  ? -3.29360  29.64225 36.54636 1.000 39.10050  ? 45  LEU   A CB  1 
ATOM   245  C  CG  . LEU   A 1 38  ? -4.60374  29.37187 35.80622 1.000 35.89051  ? 45  LEU   A CG  1 
ATOM   246  C  CD1 . LEU   A 1 38  ? -4.33151  28.67547 34.47940 1.000 33.12283  ? 45  LEU   A CD1 1 
ATOM   247  C  CD2 . LEU   A 1 38  ? -5.55126  28.55536 36.67516 1.000 34.80724  ? 45  LEU   A CD2 1 
ATOM   248  N  N   . ARG   A 1 39  ? -2.27075  32.63809 36.40829 1.000 34.65596  ? 46  ARG   A N   1 
ATOM   249  C  CA  . ARG   A 1 39  ? -2.49766  34.06223 36.18102 1.000 34.27297  ? 46  ARG   A CA  1 
ATOM   250  C  C   . ARG   A 1 39  ? -1.65359  34.58049 35.02432 1.000 42.06767  ? 46  ARG   A C   1 
ATOM   251  O  O   . ARG   A 1 39  ? -2.10663  35.42781 34.24597 1.000 38.95103  ? 46  ARG   A O   1 
ATOM   252  C  CB  . ARG   A 1 39  ? -2.19326  34.85479 37.45093 1.000 37.05697  ? 46  ARG   A CB  1 
ATOM   253  C  CG  . ARG   A 1 39  ? -2.51992  36.33589 37.33661 1.000 42.67547  ? 46  ARG   A CG  1 
ATOM   254  C  CD  . ARG   A 1 39  ? -1.33297  37.21019 37.70144 1.000 42.50914  ? 46  ARG   A CD  1 
ATOM   255  N  NE  . ARG   A 1 39  ? -0.91246  37.01861 39.08397 1.000 64.86396  ? 46  ARG   A NE  1 
ATOM   256  C  CZ  . ARG   A 1 39  ? 0.34163   36.81890 39.46634 1.000 65.84429  ? 46  ARG   A CZ  1 
ATOM   257  N  NH1 . ARG   A 1 39  ? 1.33385   36.77535 38.59111 1.000 42.99903  ? 46  ARG   A NH1 1 
ATOM   258  N  NH2 . ARG   A 1 39  ? 0.60810   36.66718 40.76032 1.000 69.19633  ? 46  ARG   A NH2 1 
ATOM   259  N  N   . GLU   A 1 40  ? -0.42373  34.08124 34.89234 1.000 36.14436  ? 47  GLU   A N   1 
ATOM   260  C  CA  . GLU   A 1 40  ? 0.43813   34.52580 33.80399 1.000 37.41088  ? 47  GLU   A CA  1 
ATOM   261  C  C   . GLU   A 1 40  ? 0.02262   33.92267 32.46766 1.000 35.70540  ? 47  GLU   A C   1 
ATOM   262  O  O   . GLU   A 1 40  ? 0.10038   34.59315 31.43268 1.000 38.44883  ? 47  GLU   A O   1 
ATOM   263  C  CB  . GLU   A 1 40  ? 1.89580   34.18794 34.11642 1.000 39.67842  ? 47  GLU   A CB  1 
ATOM   264  C  CG  . GLU   A 1 40  ? 2.49534   35.06830 35.19374 1.000 41.58172  ? 47  GLU   A CG  1 
ATOM   265  C  CD  . GLU   A 1 40  ? 2.23743   36.54062 34.93659 1.000 51.97203  ? 47  GLU   A CD  1 
ATOM   266  O  OE1 . GLU   A 1 40  ? 2.40804   36.98195 33.77814 1.000 40.98446  ? 47  GLU   A OE1 1 
ATOM   267  O  OE2 . GLU   A 1 40  ? 1.85733   37.25363 35.89049 1.000 59.83491  ? 47  GLU   A OE2 1 
ATOM   268  N  N   . LEU   A 1 41  ? -0.42399  32.66718 32.46160 1.000 35.24892  ? 48  LEU   A N   1 
ATOM   269  C  CA  . LEU   A 1 41  ? -0.83427  32.05823 31.20067 1.000 35.16736  ? 48  LEU   A CA  1 
ATOM   270  C  C   . LEU   A 1 41  ? -2.13242  32.66669 30.67874 1.000 32.59043  ? 48  LEU   A C   1 
ATOM   271  O  O   . LEU   A 1 41  ? -2.26763  32.89714 29.47152 1.000 33.88754  ? 48  LEU   A O   1 
ATOM   272  C  CB  . LEU   A 1 41  ? -0.96954  30.54514 31.36167 1.000 46.77701  ? 48  LEU   A CB  1 
ATOM   273  C  CG  . LEU   A 1 41  ? 0.34731   29.78608 31.53348 1.000 40.77468  ? 48  LEU   A CG  1 
ATOM   274  C  CD1 . LEU   A 1 41  ? 0.11775   28.28831 31.43767 1.000 38.36560  ? 48  LEU   A CD1 1 
ATOM   275  C  CD2 . LEU   A 1 41  ? 1.36780   30.24598 30.50254 1.000 39.11627  ? 48  LEU   A CD2 1 
ATOM   276  N  N   . ILE   A 1 42  ? -3.09970  32.93140 31.56424 1.000 31.55898  ? 49  ILE   A N   1 
ATOM   277  C  CA  . ILE   A 1 42  ? -4.34920  33.55038 31.12315 1.000 30.61847  ? 49  ILE   A CA  1 
ATOM   278  C  C   . ILE   A 1 42  ? -4.10033  34.98347 30.67166 1.000 29.96969  ? 49  ILE   A C   1 
ATOM   279  O  O   . ILE   A 1 42  ? -4.71069  35.46031 29.70684 1.000 29.19924  ? 49  ILE   A O   1 
ATOM   280  C  CB  . ILE   A 1 42  ? -5.41866  33.48308 32.23301 1.000 38.83802  ? 49  ILE   A CB  1 
ATOM   281  C  CG1 . ILE   A 1 42  ? -5.81439  32.03441 32.51684 1.000 29.94319  ? 49  ILE   A CG1 1 
ATOM   282  C  CG2 . ILE   A 1 42  ? -6.66414  34.28109 31.84638 1.000 28.76031  ? 49  ILE   A CG2 1 
ATOM   283  C  CD1 . ILE   A 1 42  ? -6.49294  31.84002 33.85326 1.000 30.12819  ? 49  ILE   A CD1 1 
ATOM   284  N  N   . SER   A 1 43  ? -3.19420  35.68888 31.35357 1.000 33.15077  ? 50  SER   A N   1 
ATOM   285  C  CA  . SER   A 1 43  ? -2.88047  37.06247 30.97154 1.000 36.43802  ? 50  SER   A CA  1 
ATOM   286  C  C   . SER   A 1 43  ? -2.27712  37.12409 29.57240 1.000 31.55783  ? 50  SER   A C   1 
ATOM   287  O  O   . SER   A 1 43  ? -2.61913  38.01023 28.78032 1.000 31.05363  ? 50  SER   A O   1 
ATOM   288  C  CB  . SER   A 1 43  ? -1.93699  37.68591 31.99926 1.000 33.02631  ? 50  SER   A CB  1 
ATOM   289  O  OG  . SER   A 1 43  ? -1.34546  38.87110 31.50273 1.000 39.59347  ? 50  SER   A OG  1 
ATOM   290  N  N   . ASN   A 1 44  ? -1.38154  36.18751 29.24638 1.000 32.63016  ? 51  ASN   A N   1 
ATOM   291  C  CA  . ASN   A 1 44  ? -0.85868  36.11315 27.88589 1.000 33.24911  ? 51  ASN   A CA  1 
ATOM   292  C  C   . ASN   A 1 44  ? -1.94171  35.71653 26.89121 1.000 31.86185  ? 51  ASN   A C   1 
ATOM   293  O  O   . ASN   A 1 44  ? -1.88805  36.11798 25.72372 1.000 31.98954  ? 51  ASN   A O   1 
ATOM   294  C  CB  . ASN   A 1 44  ? 0.30659   35.12689 27.82135 1.000 35.25872  ? 51  ASN   A CB  1 
ATOM   295  C  CG  . ASN   A 1 44  ? 1.47388   35.54863 28.68735 1.000 37.25828  ? 51  ASN   A CG  1 
ATOM   296  O  OD1 . ASN   A 1 44  ? 1.58814   36.71249 29.07291 1.000 37.45503  ? 51  ASN   A OD1 1 
ATOM   297  N  ND2 . ASN   A 1 44  ? 2.34867   34.60100 29.00160 1.000 39.14449  ? 51  ASN   A ND2 1 
ATOM   298  N  N   . SER   A 1 45  ? -2.92220  34.92516 27.32927 1.000 30.87036  ? 52  SER   A N   1 
ATOM   299  C  CA  . SER   A 1 45  ? -4.06552  34.62099 26.47714 1.000 29.94649  ? 52  SER   A CA  1 
ATOM   300  C  C   . SER   A 1 45  ? -4.94552  35.85005 26.28326 1.000 28.83740  ? 52  SER   A C   1 
ATOM   301  O  O   . SER   A 1 45  ? -5.43808  36.09949 25.17649 1.000 28.60211  ? 52  SER   A O   1 
ATOM   302  C  CB  . SER   A 1 45  ? -4.86727  33.46910 27.07757 1.000 29.69394  ? 52  SER   A CB  1 
ATOM   303  O  OG  . SER   A 1 45  ? -4.09658  32.28370 27.10214 1.000 30.98845  ? 52  SER   A OG  1 
ATOM   304  N  N   . SER   A 1 46  ? -5.15131  36.62989 27.34983 1.000 28.48058  ? 53  SER   A N   1 
ATOM   305  C  CA  . SER   A 1 46  ? -5.86654  37.89549 27.22137 1.000 27.93649  ? 53  SER   A CA  1 
ATOM   306  C  C   . SER   A 1 46  ? -5.12488  38.87308 26.32005 1.000 28.41475  ? 53  SER   A C   1 
ATOM   307  O  O   . SER   A 1 46  ? -5.75609  39.69381 25.64462 1.000 28.14514  ? 53  SER   A O   1 
ATOM   308  C  CB  . SER   A 1 46  ? -6.08880  38.52069 28.59864 1.000 29.46456  ? 53  SER   A CB  1 
ATOM   309  O  OG  . SER   A 1 46  ? -7.07960  39.53327 28.54103 1.000 32.14273  ? 53  SER   A OG  1 
ATOM   310  N  N   . ASP   A 1 47  ? -3.79117  38.81309 26.30292 1.000 29.55158  ? 54  ASP   A N   1 
ATOM   311  C  CA  . ASP   A 1 47  ? -3.03175  39.68082 25.41009 1.000 30.42257  ? 54  ASP   A CA  1 
ATOM   312  C  C   . ASP   A 1 47  ? -3.13641  39.22306 23.96105 1.000 30.39884  ? 54  ASP   A C   1 
ATOM   313  O  O   . ASP   A 1 47  ? -3.13599  40.05595 23.04803 1.000 30.58952  ? 54  ASP   A O   1 
ATOM   314  C  CB  . ASP   A 1 47  ? -1.56711  39.73651 25.84541 1.000 36.52529  ? 54  ASP   A CB  1 
ATOM   315  C  CG  . ASP   A 1 47  ? -1.37828  40.43020 27.18402 1.000 38.14245  ? 54  ASP   A CG  1 
ATOM   316  O  OD1 . ASP   A 1 47  ? -2.35337  41.02205 27.69446 1.000 33.46467  ? 54  ASP   A OD1 1 
ATOM   317  O  OD2 . ASP   A 1 47  ? -0.25237  40.38059 27.72631 1.000 34.66730  ? 54  ASP   A OD2 1 
ATOM   318  N  N   . ALA   A 1 48  ? -3.23018  37.91193 23.72968 1.000 30.45714  ? 55  ALA   A N   1 
ATOM   319  C  CA  . ALA   A 1 48  ? -3.36333  37.41038 22.36542 1.000 30.90432  ? 55  ALA   A CA  1 
ATOM   320  C  C   . ALA   A 1 48  ? -4.72793  37.75544 21.77986 1.000 29.76873  ? 55  ALA   A C   1 
ATOM   321  O  O   . ALA   A 1 48  ? -4.83302  38.10461 20.59774 1.000 30.16712  ? 55  ALA   A O   1 
ATOM   322  C  CB  . ALA   A 1 48  ? -3.12862  35.90034 22.33663 1.000 31.76282  ? 55  ALA   A CB  1 
ATOM   323  N  N   . LEU   A 1 49  ? -5.78269  37.66781 22.59368 1.000 28.68453  ? 56  LEU   A N   1 
ATOM   324  C  CA  . LEU   A 1 49  ? -7.11794  38.01945 22.12134 1.000 28.07874  ? 56  LEU   A CA  1 
ATOM   325  C  C   . LEU   A 1 49  ? -7.22375  39.50822 21.81258 1.000 27.86492  ? 56  LEU   A C   1 
ATOM   326  O  O   . LEU   A 1 49  ? -7.90116  39.90249 20.85643 1.000 27.94634  ? 56  LEU   A O   1 
ATOM   327  C  CB  . LEU   A 1 49  ? -8.16077  37.60728 23.15844 1.000 27.50167  ? 56  LEU   A CB  1 
ATOM   328  C  CG  . LEU   A 1 49  ? -8.27106  36.10208 23.40527 1.000 27.91371  ? 56  LEU   A CG  1 
ATOM   329  C  CD1 . LEU   A 1 49  ? -8.71963  35.82006 24.83025 1.000 27.52293  ? 56  LEU   A CD1 1 
ATOM   330  C  CD2 . LEU   A 1 49  ? -9.21263  35.46620 22.39936 1.000 28.57594  ? 56  LEU   A CD2 1 
ATOM   331  N  N   . ASP   A 1 50  ? -6.55718  40.34848 22.60808 1.000 34.37749  ? 57  ASP   A N   1 
ATOM   332  C  CA  . ASP   A 1 50  ? -6.58515  41.78698 22.36125 1.000 28.64796  ? 57  ASP   A CA  1 
ATOM   333  C  C   . ASP   A 1 50  ? -6.01786  42.12407 20.98862 1.000 34.31694  ? 57  ASP   A C   1 
ATOM   334  O  O   . ASP   A 1 50  ? -6.50663  43.03738 20.31293 1.000 31.48758  ? 57  ASP   A O   1 
ATOM   335  C  CB  . ASP   A 1 50  ? -5.80515  42.52201 23.45176 1.000 28.65128  ? 57  ASP   A CB  1 
ATOM   336  C  CG  . ASP   A 1 50  ? -6.57447  42.62709 24.75411 1.000 38.18397  ? 57  ASP   A CG  1 
ATOM   337  O  OD1 . ASP   A 1 50  ? -7.81624  42.47540 24.73549 1.000 38.26350  ? 57  ASP   A OD1 1 
ATOM   338  O  OD2 . ASP   A 1 50  ? -5.93205  42.86145 25.79983 1.000 34.87311  ? 57  ASP   A OD2 1 
ATOM   339  N  N   . LYS   A 1 51  ? -4.99155  41.39052 20.55393 1.000 42.85271  ? 58  LYS   A N   1 
ATOM   340  C  CA  . LYS   A 1 51  ? -4.32877  41.72314 19.29662 1.000 50.11350  ? 58  LYS   A CA  1 
ATOM   341  C  C   . LYS   A 1 51  ? -5.19647  41.34700 18.10095 1.000 40.88231  ? 58  LYS   A C   1 
ATOM   342  O  O   . LYS   A 1 51  ? -5.33771  42.12999 17.15422 1.000 36.21878  ? 58  LYS   A O   1 
ATOM   343  C  CB  . LYS   A 1 51  ? -2.96288  41.03443 19.21916 1.000 44.84661  ? 58  LYS   A CB  1 
ATOM   344  C  CG  . LYS   A 1 51  ? -1.97421  41.43963 20.31577 1.000 42.03833  ? 58  LYS   A CG  1 
ATOM   345  C  CD  . LYS   A 1 51  ? -2.20981  42.86356 20.81885 1.000 63.19822  ? 58  LYS   A CD  1 
ATOM   346  C  CE  . LYS   A 1 51  ? -1.39726  43.15389 22.07256 1.000 69.67642  ? 58  LYS   A CE  1 
ATOM   347  N  NZ  . LYS   A 1 51  ? -2.26290  43.58408 23.20630 1.000 53.71182  ? 58  LYS   A NZ  1 
ATOM   348  N  N   . ILE   A 1 52  ? -5.78992  40.15068 18.12457 1.000 37.79353  ? 59  ILE   A N   1 
ATOM   349  C  CA  . ILE   A 1 52  ? -6.66029  39.75598 17.02165 1.000 30.79005  ? 59  ILE   A CA  1 
ATOM   350  C  C   . ILE   A 1 52  ? -7.94042  40.58407 17.02750 1.000 30.00393  ? 59  ILE   A C   1 
ATOM   351  O  O   . ILE   A 1 52  ? -8.50818  40.86501 15.96529 1.000 30.61574  ? 59  ILE   A O   1 
ATOM   352  C  CB  . ILE   A 1 52  ? -6.95002  38.24030 17.07024 1.000 31.27825  ? 59  ILE   A CB  1 
ATOM   353  C  CG1 . ILE   A 1 52  ? -7.56109  37.76151 15.74969 1.000 32.57433  ? 59  ILE   A CG1 1 
ATOM   354  C  CG2 . ILE   A 1 52  ? -7.86430  37.88720 18.23605 1.000 30.15350  ? 59  ILE   A CG2 1 
ATOM   355  C  CD1 . ILE   A 1 52  ? -6.73327  38.09660 14.52957 1.000 34.02715  ? 59  ILE   A CD1 1 
ATOM   356  N  N   . ARG   A 1 53  ? -8.40308  41.01276 18.20501 1.000 29.00480  ? 60  ARG   A N   1 
ATOM   357  C  CA  . ARG   A 1 53  ? -9.60705  41.83516 18.26325 1.000 28.75355  ? 60  ARG   A CA  1 
ATOM   358  C  C   . ARG   A 1 53  ? -9.35598  43.21362 17.66784 1.000 33.60682  ? 60  ARG   A C   1 
ATOM   359  O  O   . ARG   A 1 53  ? -10.13853 43.69353 16.83894 1.000 34.96929  ? 60  ARG   A O   1 
ATOM   360  C  CB  . ARG   A 1 53  ? -10.10153 41.96033 19.70402 1.000 30.07065  ? 60  ARG   A CB  1 
ATOM   361  C  CG  . ARG   A 1 53  ? -11.12508 43.06843 19.89335 1.000 28.32802  ? 60  ARG   A CG  1 
ATOM   362  C  CD  . ARG   A 1 53  ? -11.93089 42.88508 21.16445 1.000 30.58833  ? 60  ARG   A CD  1 
ATOM   363  N  NE  . ARG   A 1 53  ? -11.25455 43.45889 22.32180 1.000 64.90869  ? 60  ARG   A NE  1 
ATOM   364  C  CZ  . ARG   A 1 53  ? -11.75996 44.41290 23.09238 1.000 63.15724  ? 60  ARG   A CZ  1 
ATOM   365  N  NH1 . ARG   A 1 53  ? -12.94549 44.94916 22.84463 1.000 39.15555  ? 60  ARG   A NH1 1 
ATOM   366  N  NH2 . ARG   A 1 53  ? -11.05759 44.84068 24.13745 1.000 64.15106  ? 60  ARG   A NH2 1 
ATOM   367  N  N   . TYR   A 1 54  ? -8.26610  43.86770 18.08306 1.000 39.30899  ? 61  TYR   A N   1 
ATOM   368  C  CA  . TYR   A 1 54  ? -7.94983  45.18876 17.55002 1.000 33.43525  ? 61  TYR   A CA  1 
ATOM   369  C  C   . TYR   A 1 54  ? -7.70886  45.12820 16.04742 1.000 33.76693  ? 61  TYR   A C   1 
ATOM   370  O  O   . TYR   A 1 54  ? -8.05387  46.06421 15.31639 1.000 31.12947  ? 61  TYR   A O   1 
ATOM   371  C  CB  . TYR   A 1 54  ? -6.73437  45.77440 18.27749 1.000 30.21929  ? 61  TYR   A CB  1 
ATOM   372  C  CG  . TYR   A 1 54  ? -6.14149  47.00107 17.61169 1.000 31.36530  ? 61  TYR   A CG  1 
ATOM   373  C  CD1 . TYR   A 1 54  ? -5.22910  46.88488 16.56607 1.000 38.53568  ? 61  TYR   A CD1 1 
ATOM   374  C  CD2 . TYR   A 1 54  ? -6.51211  48.27636 18.01415 1.000 31.79864  ? 61  TYR   A CD2 1 
ATOM   375  C  CE1 . TYR   A 1 54  ? -4.69931  48.00125 15.95066 1.000 43.55456  ? 61  TYR   A CE1 1 
ATOM   376  C  CE2 . TYR   A 1 54  ? -5.98408  49.40074 17.40461 1.000 36.23056  ? 61  TYR   A CE2 1 
ATOM   377  C  CZ  . TYR   A 1 54  ? -5.07913  49.25768 16.37394 1.000 33.97478  ? 61  TYR   A CZ  1 
ATOM   378  O  OH  . TYR   A 1 54  ? -4.55435  50.37342 15.76372 1.000 35.50913  ? 61  TYR   A OH  1 
ATOM   379  N  N   . GLU   A 1 55  ? -7.11059  44.03513 15.56949 1.000 38.27205  ? 62  GLU   A N   1 
ATOM   380  C  CA  . GLU   A 1 55  ? -6.83019  43.90585 14.14423 1.000 40.76626  ? 62  GLU   A CA  1 
ATOM   381  C  C   . GLU   A 1 55  ? -8.10545  43.73995 13.32686 1.000 41.70882  ? 62  GLU   A C   1 
ATOM   382  O  O   . GLU   A 1 55  ? -8.17421  44.21277 12.18599 1.000 38.64062  ? 62  GLU   A O   1 
ATOM   383  C  CB  . GLU   A 1 55  ? -5.88861  42.72850 13.90668 1.000 33.15652  ? 62  GLU   A CB  1 
ATOM   384  C  CG  . GLU   A 1 55  ? -4.43889  43.02676 14.22361 1.000 34.82261  ? 62  GLU   A CG  1 
ATOM   385  C  CD  . GLU   A 1 55  ? -3.49889  41.98045 13.66492 1.000 43.25786  ? 62  GLU   A CD  1 
ATOM   386  O  OE1 . GLU   A 1 55  ? -3.96494  41.11447 12.89559 1.000 46.32245  ? 62  GLU   A OE1 1 
ATOM   387  O  OE2 . GLU   A 1 55  ? -2.29532  42.02235 13.99495 1.000 49.12175  ? 62  GLU   A OE2 1 
ATOM   388  N  N   . SER   A 1 56  ? -9.12075  43.07871 13.88559 1.000 31.80449  ? 63  SER   A N   1 
ATOM   389  C  CA  . SER   A 1 56  ? -10.37440 42.88867 13.16779 1.000 37.08594  ? 63  SER   A CA  1 
ATOM   390  C  C   . SER   A 1 56  ? -11.20596 44.16188 13.08463 1.000 37.97668  ? 63  SER   A C   1 
ATOM   391  O  O   . SER   A 1 56  ? -12.18036 44.19518 12.32527 1.000 42.29808  ? 63  SER   A O   1 
ATOM   392  C  CB  . SER   A 1 56  ? -11.18904 41.77362 13.82585 1.000 32.31882  ? 63  SER   A CB  1 
ATOM   393  O  OG  . SER   A 1 56  ? -11.57026 42.12812 15.14292 1.000 31.15355  ? 63  SER   A OG  1 
ATOM   394  N  N   . LEU   A 1 57  ? -10.84857 45.20412 13.83794 1.000 34.94544  ? 64  LEU   A N   1 
ATOM   395  C  CA  . LEU   A 1 57  ? -11.59477 46.45529 13.76609 1.000 35.07624  ? 64  LEU   A CA  1 
ATOM   396  C  C   . LEU   A 1 57  ? -11.36834 47.16666 12.43789 1.000 38.28436  ? 64  LEU   A C   1 
ATOM   397  O  O   . LEU   A 1 57  ? -12.24121 47.91336 11.98065 1.000 47.62856  ? 64  LEU   A O   1 
ATOM   398  C  CB  . LEU   A 1 57  ? -11.20947 47.36362 14.93417 1.000 36.74545  ? 64  LEU   A CB  1 
ATOM   399  C  CG  . LEU   A 1 57  ? -11.31738 46.73607 16.32702 1.000 37.33641  ? 64  LEU   A CG  1 
ATOM   400  C  CD1 . LEU   A 1 57  ? -11.07485 47.77372 17.41425 1.000 30.77738  ? 64  LEU   A CD1 1 
ATOM   401  C  CD2 . LEU   A 1 57  ? -12.66693 46.05532 16.51276 1.000 30.92396  ? 64  LEU   A CD2 1 
ATOM   402  N  N   . THR   A 1 58  ? -10.21098 46.95206 11.80826 1.000 39.91864  ? 65  THR   A N   1 
ATOM   403  C  CA  . THR   A 1 58  ? -9.93295  47.49570 10.48481 1.000 36.42513  ? 65  THR   A CA  1 
ATOM   404  C  C   . THR   A 1 58  ? -10.02076 46.45228 9.38161  1.000 41.69479  ? 65  THR   A C   1 
ATOM   405  O  O   . THR   A 1 58  ? -10.21540 46.81818 8.21760  1.000 44.46343  ? 65  THR   A O   1 
ATOM   406  C  CB  . THR   A 1 58  ? -8.53788  48.13642 10.44102 1.000 42.35017  ? 65  THR   A CB  1 
ATOM   407  O  OG1 . THR   A 1 58  ? -7.63215  47.38692 11.26089 1.000 48.06858  ? 65  THR   A OG1 1 
ATOM   408  C  CG2 . THR   A 1 58  ? -8.59089  49.57122 10.92836 1.000 35.30955  ? 65  THR   A CG2 1 
ATOM   409  N  N   . ASP   A 1 59  ? -9.87527  45.17177 9.71553  1.000 52.02288  ? 66  ASP   A N   1 
ATOM   410  C  CA  . ASP   A 1 59  ? -9.96520  44.09142 8.73642  1.000 50.09687  ? 66  ASP   A CA  1 
ATOM   411  C  C   . ASP   A 1 59  ? -10.80603 42.97874 9.34128  1.000 42.92143  ? 66  ASP   A C   1 
ATOM   412  O  O   . ASP   A 1 59  ? -10.28559 42.08414 10.01964 1.000 46.68671  ? 66  ASP   A O   1 
ATOM   413  C  CB  . ASP   A 1 59  ? -8.58064  43.58191 8.33522  1.000 43.31414  ? 66  ASP   A CB  1 
ATOM   414  C  CG  . ASP   A 1 59  ? -8.61716  42.69906 7.10217  1.000 49.75364  ? 66  ASP   A CG  1 
ATOM   415  O  OD1 . ASP   A 1 59  ? -9.72489  42.28865 6.69441  1.000 43.42327  ? 66  ASP   A OD1 1 
ATOM   416  O  OD2 . ASP   A 1 59  ? -7.53607  42.41330 6.54133  1.000 47.87980  ? 66  ASP   A OD2 1 
ATOM   417  N  N   . PRO   A 1 60  ? -12.12121 43.00479 9.11818  1.000 48.03546  ? 67  PRO   A N   1 
ATOM   418  C  CA  . PRO   A 1 60  ? -12.98104 41.95027 9.67896  1.000 40.17809  ? 67  PRO   A CA  1 
ATOM   419  C  C   . PRO   A 1 60  ? -12.68285 40.56330 9.13526  1.000 38.52357  ? 67  PRO   A C   1 
ATOM   420  O  O   . PRO   A 1 60  ? -13.07887 39.57355 9.76277  1.000 39.77975  ? 67  PRO   A O   1 
ATOM   421  C  CB  . PRO   A 1 60  ? -14.39435 42.41173 9.29570  1.000 40.91070  ? 67  PRO   A CB  1 
ATOM   422  C  CG  . PRO   A 1 60  ? -14.26080 43.88554 9.05563  1.000 41.46597  ? 67  PRO   A CG  1 
ATOM   423  C  CD  . PRO   A 1 60  ? -12.90292 44.06030 8.45504  1.000 40.45467  ? 67  PRO   A CD  1 
ATOM   424  N  N   . SER   A 1 61  ? -11.99493 40.45424 7.99559  1.000 53.07386  ? 68  SER   A N   1 
ATOM   425  C  CA  . SER   A 1 61  ? -11.65620 39.14798 7.44218  1.000 47.32846  ? 68  SER   A CA  1 
ATOM   426  C  C   . SER   A 1 61  ? -10.61451 38.40952 8.26892  1.000 44.89787  ? 68  SER   A C   1 
ATOM   427  O  O   . SER   A 1 61  ? -10.35203 37.23392 7.99417  1.000 51.61968  ? 68  SER   A O   1 
ATOM   428  C  CB  . SER   A 1 61  ? -11.15122 39.29200 6.00629  1.000 50.02191  ? 68  SER   A CB  1 
ATOM   429  O  OG  . SER   A 1 61  ? -10.08338 40.21855 5.93481  1.000 56.83027  ? 68  SER   A OG  1 
ATOM   430  N  N   . LYS   A 1 62  ? -10.00821 39.06497 9.25936  1.000 35.51867  ? 69  LYS   A N   1 
ATOM   431  C  CA  . LYS   A 1 62  ? -9.06865  38.36492 10.12405 1.000 41.86462  ? 69  LYS   A CA  1 
ATOM   432  C  C   . LYS   A 1 62  ? -9.78634  37.40535 11.06214 1.000 46.15424  ? 69  LYS   A C   1 
ATOM   433  O  O   . LYS   A 1 62  ? -9.21036  36.38863 11.46727 1.000 43.87006  ? 69  LYS   A O   1 
ATOM   434  C  CB  . LYS   A 1 62  ? -8.23273  39.37256 10.91025 1.000 31.73035  ? 69  LYS   A CB  1 
ATOM   435  C  CG  . LYS   A 1 62  ? -7.30080  40.18290 10.02978 1.000 32.43037  ? 69  LYS   A CG  1 
ATOM   436  C  CD  . LYS   A 1 62  ? -6.52229  41.19842 10.82958 1.000 31.12244  ? 69  LYS   A CD  1 
ATOM   437  C  CE  . LYS   A 1 62  ? -5.47972  41.88478 9.96898  1.000 33.74671  ? 69  LYS   A CE  1 
ATOM   438  N  NZ  . LYS   A 1 62  ? -4.11307  41.75204 10.53591 1.000 45.03371  ? 69  LYS   A NZ  1 
ATOM   439  N  N   . LEU   A 1 63  ? -11.03940 37.69882 11.40489 1.000 42.16927  ? 70  LEU   A N   1 
ATOM   440  C  CA  . LEU   A 1 63  ? -11.82278 36.82125 12.26306 1.000 36.37166  ? 70  LEU   A CA  1 
ATOM   441  C  C   . LEU   A 1 63  ? -12.48356 35.68234 11.49957 1.000 35.72671  ? 70  LEU   A C   1 
ATOM   442  O  O   . LEU   A 1 63  ? -13.24437 34.91694 12.10168 1.000 36.17619  ? 70  LEU   A O   1 
ATOM   443  C  CB  . LEU   A 1 63  ? -12.88238 37.63032 13.01328 1.000 34.12697  ? 70  LEU   A CB  1 
ATOM   444  C  CG  . LEU   A 1 63  ? -12.37188 38.35802 14.25860 1.000 39.76173  ? 70  LEU   A CG  1 
ATOM   445  C  CD1 . LEU   A 1 63  ? -13.52338 39.00119 15.01544 1.000 32.07998  ? 70  LEU   A CD1 1 
ATOM   446  C  CD2 . LEU   A 1 63  ? -11.58332 37.41359 15.16202 1.000 29.63219  ? 70  LEU   A CD2 1 
ATOM   447  N  N   . ASP   A 1 64  ? -12.20720 35.55027 10.19894 1.000 37.52204  ? 71  ASP   A N   1 
ATOM   448  C  CA  . ASP   A 1 64  ? -12.74553 34.44234 9.41841  1.000 40.23165  ? 71  ASP   A CA  1 
ATOM   449  C  C   . ASP   A 1 64  ? -12.28669 33.08901 9.94577  1.000 44.63188  ? 71  ASP   A C   1 
ATOM   450  O  O   . ASP   A 1 64  ? -12.95812 32.07929 9.70364  1.000 41.88063  ? 71  ASP   A O   1 
ATOM   451  C  CB  . ASP   A 1 64  ? -12.33632 34.58927 7.95238  1.000 42.38342  ? 71  ASP   A CB  1 
ATOM   452  C  CG  . ASP   A 1 64  ? -12.97466 35.78883 7.28644  1.000 43.75767  ? 71  ASP   A CG  1 
ATOM   453  O  OD1 . ASP   A 1 64  ? -13.85229 36.42281 7.91000  1.000 43.43617  ? 71  ASP   A OD1 1 
ATOM   454  O  OD2 . ASP   A 1 64  ? -12.59266 36.10166 6.13943  1.000 49.41524  ? 71  ASP   A OD2 1 
ATOM   455  N  N   . SER   A 1 65  ? -11.16013 33.04601 10.65645 1.000 38.69963  ? 72  SER   A N   1 
ATOM   456  C  CA  . SER   A 1 65  ? -10.62667 31.81825 11.22612 1.000 36.75986  ? 72  SER   A CA  1 
ATOM   457  C  C   . SER   A 1 65  ? -11.14570 31.55018 12.63437 1.000 37.42206  ? 72  SER   A C   1 
ATOM   458  O  O   . SER   A 1 65  ? -10.51363 30.79996 13.38654 1.000 35.37094  ? 72  SER   A O   1 
ATOM   459  C  CB  . SER   A 1 65  ? -9.09785  31.86850 11.23395 1.000 37.52065  ? 72  SER   A CB  1 
ATOM   460  O  OG  . SER   A 1 65  ? -8.63511  33.13716 11.66714 1.000 36.72208  ? 72  SER   A OG  1 
ATOM   461  N  N   . GLY   A 1 66  ? -12.27392 32.14549 13.00785 1.000 35.36671  ? 73  GLY   A N   1 
ATOM   462  C  CA  . GLY   A 1 66  ? -12.80062 31.97651 14.34596 1.000 34.24083  ? 73  GLY   A CA  1 
ATOM   463  C  C   . GLY   A 1 66  ? -13.25814 33.28424 14.95362 1.000 33.19813  ? 73  GLY   A C   1 
ATOM   464  O  O   . GLY   A 1 66  ? -12.43889 34.10145 15.38305 1.000 42.08545  ? 73  GLY   A O   1 
ATOM   465  N  N   . LYS   A 1 67  ? -14.57359 33.49114 14.99407 1.000 38.36631  ? 74  LYS   A N   1 
ATOM   466  C  CA  . LYS   A 1 67  ? -15.12271 34.74496 15.49423 1.000 42.02873  ? 74  LYS   A CA  1 
ATOM   467  C  C   . LYS   A 1 67  ? -15.12394 34.80099 17.01587 1.000 35.12746  ? 74  LYS   A C   1 
ATOM   468  O  O   . LYS   A 1 67  ? -15.00278 35.88698 17.59176 1.000 32.03981  ? 74  LYS   A O   1 
ATOM   469  C  CB  . LYS   A 1 67  ? -16.54454 34.95184 14.95723 1.000 38.29744  ? 74  LYS   A CB  1 
ATOM   470  C  CG  . LYS   A 1 67  ? -16.66353 34.92896 13.43116 1.000 44.86062  ? 74  LYS   A CG  1 
ATOM   471  C  CD  . LYS   A 1 67  ? -16.81818 33.51121 12.88543 1.000 57.10533  ? 74  LYS   A CD  1 
ATOM   472  C  CE  . LYS   A 1 67  ? -16.14099 33.35893 11.52937 1.000 59.58654  ? 74  LYS   A CE  1 
ATOM   473  N  NZ  . LYS   A 1 67  ? -15.80830 31.93678 11.22403 1.000 43.67179  ? 74  LYS   A NZ  1 
ATOM   474  N  N   . GLU   A 1 68  ? -15.24333 33.65459 17.67691 1.000 32.97993  ? 75  GLU   A N   1 
ATOM   475  C  CA  . GLU   A 1 68  ? -15.34908 33.61613 19.12825 1.000 35.53940  ? 75  GLU   A CA  1 
ATOM   476  C  C   . GLU   A 1 68  ? -13.99449 33.89390 19.77178 1.000 35.54665  ? 75  GLU   A C   1 
ATOM   477  O  O   . GLU   A 1 68  ? -12.98053 33.29849 19.39380 1.000 29.27034  ? 75  GLU   A O   1 
ATOM   478  C  CB  . GLU   A 1 68  ? -15.88624 32.25816 19.58228 1.000 51.61841  ? 75  GLU   A CB  1 
ATOM   479  C  CG  . GLU   A 1 68  ? -17.32000 31.96629 19.14738 1.000 54.99210  ? 75  GLU   A CG  1 
ATOM   480  C  CD  . GLU   A 1 68  ? -17.43637 31.59566 17.67596 1.000 71.68302  ? 75  GLU   A CD  1 
ATOM   481  O  OE1 . GLU   A 1 68  ? -16.39519 31.31795 17.04136 1.000 50.72789  ? 75  GLU   A OE1 1 
ATOM   482  O  OE2 . GLU   A 1 68  ? -18.57206 31.58472 17.15342 1.000 74.93753  ? 75  GLU   A OE2 1 
ATOM   483  N  N   . LEU   A 1 69  ? -13.98356 34.79949 20.74788 1.000 32.93881  ? 76  LEU   A N   1 
ATOM   484  C  CA  . LEU   A 1 69  ? -12.78248 35.16500 21.49248 1.000 26.83883  ? 76  LEU   A CA  1 
ATOM   485  C  C   . LEU   A 1 69  ? -12.99181 34.76159 22.94633 1.000 28.43258  ? 76  LEU   A C   1 
ATOM   486  O  O   . LEU   A 1 69  ? -13.76585 35.40012 23.66778 1.000 27.49981  ? 76  LEU   A O   1 
ATOM   487  C  CB  . LEU   A 1 69  ? -12.49624 36.66093 21.36874 1.000 26.58004  ? 76  LEU   A CB  1 
ATOM   488  C  CG  . LEU   A 1 69  ? -12.57596 37.25002 19.95989 1.000 27.25465  ? 76  LEU   A CG  1 
ATOM   489  C  CD1 . LEU   A 1 69  ? -12.31626 38.74063 19.99776 1.000 27.22012  ? 76  LEU   A CD1 1 
ATOM   490  C  CD2 . LEU   A 1 69  ? -11.59021 36.56073 19.03308 1.000 32.26077  ? 76  LEU   A CD2 1 
ATOM   491  N  N   . HIS   A 1 70  ? -12.30481 33.70682 23.37687 1.000 27.60444  ? 77  HIS   A N   1 
ATOM   492  C  CA  . HIS   A 1 70  ? -12.51812 33.15788 24.70689 1.000 26.84918  ? 77  HIS   A CA  1 
ATOM   493  C  C   . HIS   A 1 70  ? -11.25520 32.44771 25.16866 1.000 25.19662  ? 77  HIS   A C   1 
ATOM   494  O  O   . HIS   A 1 70  ? -10.28563 32.30250 24.42051 1.000 24.32756  ? 77  HIS   A O   1 
ATOM   495  C  CB  . HIS   A 1 70  ? -13.70687 32.19278 24.72242 1.000 27.63066  ? 77  HIS   A CB  1 
ATOM   496  C  CG  . HIS   A 1 70  ? -13.62703 31.13103 23.67147 1.000 28.11060  ? 77  HIS   A CG  1 
ATOM   497  N  ND1 . HIS   A 1 70  ? -12.71507 30.09957 23.72458 1.000 27.52276  ? 77  HIS   A ND1 1 
ATOM   498  C  CD2 . HIS   A 1 70  ? -14.32739 30.95550 22.52630 1.000 29.52434  ? 77  HIS   A CD2 1 
ATOM   499  C  CE1 . HIS   A 1 70  ? -12.86521 29.32676 22.66402 1.000 28.57464  ? 77  HIS   A CE1 1 
ATOM   500  N  NE2 . HIS   A 1 70  ? -13.83744 29.82411 21.92095 1.000 29.81865  ? 77  HIS   A NE2 1 
ATOM   501  N  N   . ILE   A 1 71  ? -11.28785 31.99766 26.42100 1.000 27.11272  ? 78  ILE   A N   1 
ATOM   502  C  CA  . ILE   A 1 71  ? -10.22087 31.20854 27.02368 1.000 30.75964  ? 78  ILE   A CA  1 
ATOM   503  C  C   . ILE   A 1 71  ? -10.85092 29.98028 27.66368 1.000 25.57616  ? 78  ILE   A C   1 
ATOM   504  O  O   . ILE   A 1 71  ? -11.82315 30.10009 28.41648 1.000 26.48368  ? 78  ILE   A O   1 
ATOM   505  C  CB  . ILE   A 1 71  ? -9.42912  32.01782 28.07080 1.000 27.94872  ? 78  ILE   A CB  1 
ATOM   506  C  CG1 . ILE   A 1 71  ? -8.68803  33.18028 27.40727 1.000 23.63663  ? 78  ILE   A CG1 1 
ATOM   507  C  CG2 . ILE   A 1 71  ? -8.46705  31.11936 28.83732 1.000 24.28400  ? 78  ILE   A CG2 1 
ATOM   508  C  CD1 . ILE   A 1 71  ? -8.28904  34.27433 28.37273 1.000 23.93785  ? 78  ILE   A CD1 1 
ATOM   509  N  N   . ASN   A 1 72  ? -10.30863 28.80493 27.36046 1.000 25.67303  ? 79  ASN   A N   1 
ATOM   510  C  CA  . ASN   A 1 72  ? -10.76009 27.55969 27.96347 1.000 34.07906  ? 79  ASN   A CA  1 
ATOM   511  C  C   . ASN   A 1 72  ? -9.64911  26.95413 28.81139 1.000 33.91699  ? 79  ASN   A C   1 
ATOM   512  O  O   . ASN   A 1 72  ? -8.46314  27.06528 28.48580 1.000 35.62714  ? 79  ASN   A O   1 
ATOM   513  C  CB  . ASN   A 1 72  ? -11.21057 26.54658 26.90176 1.000 27.80009  ? 79  ASN   A CB  1 
ATOM   514  C  CG  . ASN   A 1 72  ? -12.42406 27.01493 26.12753 1.000 31.61973  ? 79  ASN   A CG  1 
ATOM   515  O  OD1 . ASN   A 1 72  ? -13.19069 27.85374 26.60279 1.000 32.25205  ? 79  ASN   A OD1 1 
ATOM   516  N  ND2 . ASN   A 1 72  ? -12.60849 26.47119 24.92787 1.000 29.57627  ? 79  ASN   A ND2 1 
ATOM   517  N  N   . LEU   A 1 73  ? -10.04630 26.31494 29.90893 1.000 27.47713  ? 80  LEU   A N   1 
ATOM   518  C  CA  . LEU   A 1 73  ? -9.12624  25.61931 30.79985 1.000 30.31832  ? 80  LEU   A CA  1 
ATOM   519  C  C   . LEU   A 1 73  ? -9.54567  24.15876 30.87026 1.000 36.48837  ? 80  LEU   A C   1 
ATOM   520  O  O   . LEU   A 1 73  ? -10.63011 23.84529 31.37328 1.000 37.81101  ? 80  LEU   A O   1 
ATOM   521  C  CB  . LEU   A 1 73  ? -9.11589  26.25377 32.19278 1.000 40.26075  ? 80  LEU   A CB  1 
ATOM   522  C  CG  . LEU   A 1 73  ? -8.96292  27.77611 32.25354 1.000 32.68308  ? 80  LEU   A CG  1 
ATOM   523  C  CD1 . LEU   A 1 73  ? -8.94633  28.25633 33.69741 1.000 28.15551  ? 80  LEU   A CD1 1 
ATOM   524  C  CD2 . LEU   A 1 73  ? -7.70977  28.22615 31.51444 1.000 26.25355  ? 80  LEU   A CD2 1 
ATOM   525  N  N   . ILE   A 1 74  ? -8.69203  23.27287 30.36570 1.000 36.18427  ? 81  ILE   A N   1 
ATOM   526  C  CA  . ILE   A 1 74  ? -9.02765  21.85716 30.23814 1.000 31.11589  ? 81  ILE   A CA  1 
ATOM   527  C  C   . ILE   A 1 74  ? -8.08458  21.01657 31.09052 1.000 31.94221  ? 81  ILE   A C   1 
ATOM   528  O  O   . ILE   A 1 74  ? -6.99562  20.64810 30.62729 1.000 32.10155  ? 81  ILE   A O   1 
ATOM   529  C  CB  . ILE   A 1 74  ? -8.97651  21.40884 28.76924 1.000 31.55983  ? 81  ILE   A CB  1 
ATOM   530  C  CG1 . ILE   A 1 74  ? -9.73481  22.39687 27.88107 1.000 30.79732  ? 81  ILE   A CG1 1 
ATOM   531  C  CG2 . ILE   A 1 74  ? -9.54137  20.00852 28.62175 1.000 33.73939  ? 81  ILE   A CG2 1 
ATOM   532  C  CD1 . ILE   A 1 74  ? -9.34340  22.33116 26.42608 1.000 30.95492  ? 81  ILE   A CD1 1 
ATOM   533  N  N   . PRO   A 1 75  ? -8.44792  20.68995 32.32613 1.000 32.79808  ? 82  PRO   A N   1 
ATOM   534  C  CA  . PRO   A 1 75  ? -7.63806  19.75369 33.10584 1.000 34.05517  ? 82  PRO   A CA  1 
ATOM   535  C  C   . PRO   A 1 75  ? -7.91200  18.31611 32.69637 1.000 35.90151  ? 82  PRO   A C   1 
ATOM   536  O  O   . PRO   A 1 75  ? -9.02146  17.95190 32.30018 1.000 36.67460  ? 82  PRO   A O   1 
ATOM   537  C  CB  . PRO   A 1 75  ? -8.08791  20.01699 34.54671 1.000 34.54949  ? 82  PRO   A CB  1 
ATOM   538  C  CG  . PRO   A 1 75  ? -9.49897  20.46126 34.40748 1.000 34.41829  ? 82  PRO   A CG  1 
ATOM   539  C  CD  . PRO   A 1 75  ? -9.59719  21.19996 33.09364 1.000 43.60037  ? 82  PRO   A CD  1 
ATOM   540  N  N   . ASN   A 1 76  ? -6.86831  17.49628 32.79129 1.000 42.08256  ? 83  ASN   A N   1 
ATOM   541  C  CA  . ASN   A 1 76  ? -6.93847  16.09075 32.40191 1.000 39.17582  ? 83  ASN   A CA  1 
ATOM   542  C  C   . ASN   A 1 76  ? -6.13971  15.28732 33.41612 1.000 40.78948  ? 83  ASN   A C   1 
ATOM   543  O  O   . ASN   A 1 76  ? -4.90624  15.32745 33.40765 1.000 50.00743  ? 83  ASN   A O   1 
ATOM   544  C  CB  . ASN   A 1 76  ? -6.39860  15.88001 30.98678 1.000 39.37608  ? 83  ASN   A CB  1 
ATOM   545  C  CG  . ASN   A 1 76  ? -6.81965  14.55077 30.39143 1.000 41.91217  ? 83  ASN   A CG  1 
ATOM   546  O  OD1 . ASN   A 1 76  ? -6.70584  13.50463 31.02920 1.000 48.68301  ? 83  ASN   A OD1 1 
ATOM   547  N  ND2 . ASN   A 1 76  ? -7.30945  14.58656 29.15825 1.000 42.14833  ? 83  ASN   A ND2 1 
ATOM   548  N  N   . LYS   A 1 77  ? -6.83957  14.55931 34.28733 1.000 42.33292  ? 84  LYS   A N   1 
ATOM   549  C  CA  . LYS   A 1 77  ? -6.15094  13.77421 35.30516 1.000 49.33611  ? 84  LYS   A CA  1 
ATOM   550  C  C   . LYS   A 1 77  ? -5.47554  12.54258 34.71337 1.000 46.38310  ? 84  LYS   A C   1 
ATOM   551  O  O   . LYS   A 1 77  ? -4.42842  12.11698 35.21265 1.000 47.86665  ? 84  LYS   A O   1 
ATOM   552  C  CB  . LYS   A 1 77  ? -7.13079  13.37615 36.40903 1.000 45.40974  ? 84  LYS   A CB  1 
ATOM   553  C  CG  . LYS   A 1 77  ? -7.56380  14.54600 37.27948 1.000 43.93767  ? 84  LYS   A CG  1 
ATOM   554  C  CD  . LYS   A 1 77  ? -8.53633  14.11845 38.36405 1.000 45.59783  ? 84  LYS   A CD  1 
ATOM   555  C  CE  . LYS   A 1 77  ? -9.55438  15.21450 38.64648 1.000 49.19858  ? 84  LYS   A CE  1 
ATOM   556  N  NZ  . LYS   A 1 77  ? -10.45060 14.86742 39.78411 1.000 54.38466  ? 84  LYS   A NZ  1 
ATOM   557  N  N   . GLN   A 1 78  ? -6.04364  11.96494 33.65173 1.000 49.03067  ? 85  GLN   A N   1 
ATOM   558  C  CA  . GLN   A 1 78  ? -5.45595  10.76523 33.06124 1.000 54.07838  ? 85  GLN   A CA  1 
ATOM   559  C  C   . GLN   A 1 78  ? -4.13098  11.08380 32.37604 1.000 49.44970  ? 85  GLN   A C   1 
ATOM   560  O  O   . GLN   A 1 78  ? -3.12245  10.40594 32.60545 1.000 55.03686  ? 85  GLN   A O   1 
ATOM   561  C  CB  . GLN   A 1 78  ? -6.44170  10.12724 32.07932 1.000 61.43548  ? 85  GLN   A CB  1 
ATOM   562  C  CG  . GLN   A 1 78  ? -5.79915  9.47650  30.86103 1.000 67.09895  ? 85  GLN   A CG  1 
ATOM   563  C  CD  . GLN   A 1 78  ? -6.80823  9.12993  29.78133 1.000 79.87058  ? 85  GLN   A CD  1 
ATOM   564  O  OE1 . GLN   A 1 78  ? -7.25507  10.00001 29.03056 1.000 68.45424  ? 85  GLN   A OE1 1 
ATOM   565  N  NE2 . GLN   A 1 78  ? -7.17288  7.85372  29.69786 1.000 57.85499  ? 85  GLN   A NE2 1 
ATOM   566  N  N   . ASP   A 1 79  ? -4.11108  12.11529 31.53242 1.000 47.19303  ? 86  ASP   A N   1 
ATOM   567  C  CA  . ASP   A 1 79  ? -2.87143  12.53847 30.89652 1.000 52.28403  ? 86  ASP   A CA  1 
ATOM   568  C  C   . ASP   A 1 79  ? -2.01489  13.41233 31.80062 1.000 45.55286  ? 86  ASP   A C   1 
ATOM   569  O  O   . ASP   A 1 79  ? -0.87679  13.72141 31.43096 1.000 47.94897  ? 86  ASP   A O   1 
ATOM   570  C  CB  . ASP   A 1 79  ? -3.16804  13.28957 29.59536 1.000 50.34977  ? 86  ASP   A CB  1 
ATOM   571  C  CG  . ASP   A 1 79  ? -4.06403  12.50424 28.65899 1.000 57.33593  ? 86  ASP   A CG  1 
ATOM   572  O  OD1 . ASP   A 1 79  ? -4.12166  11.26201 28.78706 1.000 55.43089  ? 86  ASP   A OD1 1 
ATOM   573  O  OD2 . ASP   A 1 79  ? -4.70777  13.13105 27.79130 1.000 61.04749  ? 86  ASP   A OD2 1 
ATOM   574  N  N   . ARG   A 1 80  ? -2.53081  13.80738 32.96713 1.000 44.61340  ? 87  ARG   A N   1 
ATOM   575  C  CA  . ARG   A 1 80  ? -1.81173  14.67515 33.90094 1.000 50.08569  ? 87  ARG   A CA  1 
ATOM   576  C  C   . ARG   A 1 80  ? -1.42437  15.99486 33.23566 1.000 48.33013  ? 87  ARG   A C   1 
ATOM   577  O  O   . ARG   A 1 80  ? -0.34369  16.53968 33.47253 1.000 41.70521  ? 87  ARG   A O   1 
ATOM   578  C  CB  . ARG   A 1 80  ? -0.58196  13.96812 34.47711 1.000 46.32560  ? 87  ARG   A CB  1 
ATOM   579  C  CG  . ARG   A 1 80  ? -0.16615  14.44491 35.85897 1.000 46.62287  ? 87  ARG   A CG  1 
ATOM   580  C  CD  . ARG   A 1 80  ? 0.88555   13.52165 36.45399 1.000 72.15493  ? 87  ARG   A CD  1 
ATOM   581  N  NE  . ARG   A 1 80  ? 0.60592   13.19399 37.84681 1.000 83.40553  ? 87  ARG   A NE  1 
ATOM   582  C  CZ  . ARG   A 1 80  ? 0.22153   11.99948 38.27572 1.000 71.97458  ? 87  ARG   A CZ  1 
ATOM   583  N  NH1 . ARG   A 1 80  ? 0.05816   10.98514 37.44221 1.000 72.81106  ? 87  ARG   A NH1 1 
ATOM   584  N  NH2 . ARG   A 1 80  ? -0.00499  11.81831 39.57391 1.000 71.51716  ? 87  ARG   A NH2 1 
ATOM   585  N  N   . THR   A 1 81  ? -2.31494  16.51526 32.39296 1.000 39.77695  ? 88  THR   A N   1 
ATOM   586  C  CA  . THR   A 1 81  ? -2.05525  17.72756 31.62792 1.000 43.52290  ? 88  THR   A CA  1 
ATOM   587  C  C   . THR   A 1 81  ? -3.13257  18.76639 31.89632 1.000 35.71195  ? 88  THR   A C   1 
ATOM   588  O  O   . THR   A 1 81  ? -4.32791  18.46787 31.81414 1.000 35.62019  ? 88  THR   A O   1 
ATOM   589  C  CB  . THR   A 1 81  ? -1.98620  17.44358 30.12284 1.000 38.49285  ? 88  THR   A CB  1 
ATOM   590  O  OG1 . THR   A 1 81  ? -3.22683  16.87921 29.67960 1.000 42.05672  ? 88  THR   A OG1 1 
ATOM   591  C  CG2 . THR   A 1 81  ? -0.84077  16.49400 29.80151 1.000 40.55515  ? 88  THR   A CG2 1 
ATOM   592  N  N   . LEU   A 1 82  ? -2.70041  19.98213 32.21109 1.000 35.90508  ? 89  LEU   A N   1 
ATOM   593  C  CA  . LEU   A 1 82  ? -3.56758  21.15100 32.24304 1.000 36.51769  ? 89  LEU   A CA  1 
ATOM   594  C  C   . LEU   A 1 82  ? -3.39166  21.89780 30.92658 1.000 31.31628  ? 89  LEU   A C   1 
ATOM   595  O  O   . LEU   A 1 82  ? -2.26902  22.25993 30.56216 1.000 32.53988  ? 89  LEU   A O   1 
ATOM   596  C  CB  . LEU   A 1 82  ? -3.22728  22.04955 33.43102 1.000 32.42235  ? 89  LEU   A CB  1 
ATOM   597  C  CG  . LEU   A 1 82  ? -4.10346  23.28213 33.64784 1.000 31.03602  ? 89  LEU   A CG  1 
ATOM   598  C  CD1 . LEU   A 1 82  ? -5.58328  22.92198 33.58242 1.000 30.89594  ? 89  LEU   A CD1 1 
ATOM   599  C  CD2 . LEU   A 1 82  ? -3.75651  23.93818 34.97383 1.000 31.71858  ? 89  LEU   A CD2 1 
ATOM   600  N  N   . THR   A 1 83  ? -4.49064  22.11794 30.21241 1.000 30.47072  ? 90  THR   A N   1 
ATOM   601  C  CA  . THR   A 1 83  ? -4.45294  22.69682 28.87481 1.000 29.61515  ? 90  THR   A CA  1 
ATOM   602  C  C   . THR   A 1 83  ? -5.15970  24.04514 28.88417 1.000 28.06323  ? 90  THR   A C   1 
ATOM   603  O  O   . THR   A 1 83  ? -6.33440  24.13137 29.25844 1.000 27.96417  ? 90  THR   A O   1 
ATOM   604  C  CB  . THR   A 1 83  ? -5.10039  21.75409 27.85833 1.000 30.59744  ? 90  THR   A CB  1 
ATOM   605  O  OG1 . THR   A 1 83  ? -4.21547  20.66149 27.58626 1.000 32.26985  ? 90  THR   A OG1 1 
ATOM   606  C  CG2 . THR   A 1 83  ? -5.40132  22.48288 26.56843 1.000 29.82739  ? 90  THR   A CG2 1 
ATOM   607  N  N   . ILE   A 1 84  ? -4.44703  25.09021 28.46740 1.000 29.24953  ? 91  ILE   A N   1 
ATOM   608  C  CA  . ILE   A 1 84  ? -4.98787  26.44369 28.37245 1.000 30.88472  ? 91  ILE   A CA  1 
ATOM   609  C  C   . ILE   A 1 84  ? -5.07764  26.80908 26.89726 1.000 28.87311  ? 91  ILE   A C   1 
ATOM   610  O  O   . ILE   A 1 84  ? -4.06662  26.78724 26.18365 1.000 31.69732  ? 91  ILE   A O   1 
ATOM   611  C  CB  . ILE   A 1 84  ? -4.12820  27.45919 29.14235 1.000 30.14668  ? 91  ILE   A CB  1 
ATOM   612  C  CG1 . ILE   A 1 84  ? -4.22334  27.21126 30.65141 1.000 42.58230  ? 91  ILE   A CG1 1 
ATOM   613  C  CG2 . ILE   A 1 84  ? -4.55233  28.88482 28.80727 1.000 24.76944  ? 91  ILE   A CG2 1 
ATOM   614  C  CD1 . ILE   A 1 84  ? -3.18624  26.23933 31.19307 1.000 30.76740  ? 91  ILE   A CD1 1 
ATOM   615  N  N   . VAL   A 1 85  ? -6.28537  27.14407 26.44171 1.000 28.63557  ? 92  VAL   A N   1 
ATOM   616  C  CA  . VAL   A 1 85  ? -6.55776  27.45586 25.04288 1.000 34.00718  ? 92  VAL   A CA  1 
ATOM   617  C  C   . VAL   A 1 85  ? -7.08363  28.88077 24.94373 1.000 34.88569  ? 92  VAL   A C   1 
ATOM   618  O  O   . VAL   A 1 85  ? -7.83361  29.33705 25.81355 1.000 42.29846  ? 92  VAL   A O   1 
ATOM   619  C  CB  . VAL   A 1 85  ? -7.57620  26.47204 24.42492 1.000 30.18382  ? 92  VAL   A CB  1 
ATOM   620  C  CG1 . VAL   A 1 85  ? -7.45013  26.45114 22.90608 1.000 26.93321  ? 92  VAL   A CG1 1 
ATOM   621  C  CG2 . VAL   A 1 85  ? -7.40377  25.08119 25.00632 1.000 27.68185  ? 92  VAL   A CG2 1 
ATOM   622  N  N   . ASP   A 1 86  ? -6.69424  29.57952 23.87853 1.000 31.08789  ? 93  ASP   A N   1 
ATOM   623  C  CA  . ASP   A 1 86  ? -7.31293  30.84715 23.51570 1.000 28.17652  ? 93  ASP   A CA  1 
ATOM   624  C  C   . ASP   A 1 86  ? -7.48386  30.89178 22.00476 1.000 24.06125  ? 93  ASP   A C   1 
ATOM   625  O  O   . ASP   A 1 86  ? -6.83765  30.14825 21.26286 1.000 24.65580  ? 93  ASP   A O   1 
ATOM   626  C  CB  . ASP   A 1 86  ? -6.50049  32.06067 24.00685 1.000 27.61380  ? 93  ASP   A CB  1 
ATOM   627  C  CG  . ASP   A 1 86  ? -5.12800  32.16454 23.35270 1.000 24.54152  ? 93  ASP   A CG  1 
ATOM   628  O  OD1 . ASP   A 1 86  ? -5.05211  32.52422 22.15743 1.000 23.76281  ? 93  ASP   A OD1 1 
ATOM   629  O  OD2 . ASP   A 1 86  ? -4.12047  31.90079 24.04369 1.000 23.05936  ? 93  ASP   A OD2 1 
ATOM   630  N  N   . THR   A 1 87  ? -8.37630  31.77064 21.55584 1.000 23.86791  ? 94  THR   A N   1 
ATOM   631  C  CA  . THR   A 1 87  ? -8.63398  31.97849 20.13679 1.000 22.67180  ? 94  THR   A CA  1 
ATOM   632  C  C   . THR   A 1 87  ? -8.03110  33.29134 19.64411 1.000 22.52924  ? 94  THR   A C   1 
ATOM   633  O  O   . THR   A 1 87  ? -8.57132  33.93259 18.73917 1.000 21.97138  ? 94  THR   A O   1 
ATOM   634  C  CB  . THR   A 1 87  ? -10.13557 31.93548 19.85558 1.000 37.34770  ? 94  THR   A CB  1 
ATOM   635  O  OG1 . THR   A 1 87  ? -10.84629 32.56780 20.92906 1.000 23.61226  ? 94  THR   A OG1 1 
ATOM   636  C  CG2 . THR   A 1 87  ? -10.61099 30.49587 19.71671 1.000 23.49536  ? 94  THR   A CG2 1 
ATOM   637  N  N   . GLY   A 1 88  ? -6.90478  33.69214 20.23192 1.000 26.00727  ? 95  GLY   A N   1 
ATOM   638  C  CA  . GLY   A 1 88  ? -6.27005  34.95530 19.92374 1.000 23.93150  ? 95  GLY   A CA  1 
ATOM   639  C  C   . GLY   A 1 88  ? -5.51475  34.92933 18.61115 1.000 23.47146  ? 95  GLY   A C   1 
ATOM   640  O  O   . GLY   A 1 88  ? -5.75763  34.10010 17.73104 1.000 26.24214  ? 95  GLY   A O   1 
ATOM   641  N  N   . ILE   A 1 89  ? -4.56492  35.86028 18.49141 1.000 24.55283  ? 96  ILE   A N   1 
ATOM   642  C  CA  . ILE   A 1 89  ? -3.83648  36.03263 17.24099 1.000 30.94759  ? 96  ILE   A CA  1 
ATOM   643  C  C   . ILE   A 1 89  ? -2.93596  34.84233 16.91573 1.000 26.53346  ? 96  ILE   A C   1 
ATOM   644  O  O   . ILE   A 1 89  ? -2.59055  34.64020 15.74684 1.000 31.59691  ? 96  ILE   A O   1 
ATOM   645  C  CB  . ILE   A 1 89  ? -3.02414  37.34335 17.28334 1.000 30.44500  ? 96  ILE   A CB  1 
ATOM   646  C  CG1 . ILE   A 1 89  ? -2.72137  37.83738 15.86768 1.000 26.40812  ? 96  ILE   A CG1 1 
ATOM   647  C  CG2 . ILE   A 1 89  ? -1.74082  37.16125 18.07526 1.000 28.04207  ? 96  ILE   A CG2 1 
ATOM   648  C  CD1 . ILE   A 1 89  ? -2.25929  39.27322 15.81183 1.000 28.32420  ? 96  ILE   A CD1 1 
ATOM   649  N  N   . GLY   A 1 90  ? -2.55138  34.03796 17.90434 1.000 25.01575  ? 97  GLY   A N   1 
ATOM   650  C  CA  . GLY   A 1 90  ? -1.64251  32.94008 17.62550 1.000 25.32689  ? 97  GLY   A CA  1 
ATOM   651  C  C   . GLY   A 1 90  ? -0.22035  33.42795 17.37445 1.000 31.42663  ? 97  GLY   A C   1 
ATOM   652  O  O   . GLY   A 1 90  ? 0.12037   34.59392 17.57701 1.000 37.63026  ? 97  GLY   A O   1 
ATOM   653  N  N   . MET   A 1 91  ? 0.62700   32.49414 16.93782 1.000 27.42842  ? 98  MET   A N   1 
ATOM   654  C  CA  . MET   A 1 91  ? 2.02704   32.80415 16.67511 1.000 29.37467  ? 98  MET   A CA  1 
ATOM   655  C  C   . MET   A 1 91  ? 2.49791   32.10175 15.41318 1.000 29.11347  ? 98  MET   A C   1 
ATOM   656  O  O   . MET   A 1 91  ? 2.17968   30.93156 15.18238 1.000 28.17069  ? 98  MET   A O   1 
ATOM   657  C  CB  . MET   A 1 91  ? 2.93219   32.38755 17.83540 1.000 31.39597  ? 98  MET   A CB  1 
ATOM   658  C  CG  . MET   A 1 91  ? 2.21955   32.32001 19.14792 1.000 31.31393  ? 98  MET   A CG  1 
ATOM   659  S  SD  . MET   A 1 91  ? 3.27511   32.17838 20.58085 1.000 34.46140  ? 98  MET   A SD  1 
ATOM   660  C  CE  . MET   A 1 91  ? 2.14341   31.26613 21.61877 1.000 33.42877  ? 98  MET   A CE  1 
ATOM   661  N  N   . THR   A 1 92  ? 3.27402   32.82537 14.61342 1.000 30.32068  ? 99  THR   A N   1 
ATOM   662  C  CA  . THR   A 1 92  ? 3.87879   32.28262 13.41142 1.000 30.65564  ? 99  THR   A CA  1 
ATOM   663  C  C   . THR   A 1 92  ? 5.10630   31.45165 13.77596 1.000 32.48702  ? 99  THR   A C   1 
ATOM   664  O  O   . THR   A 1 92  ? 5.51736   31.37466 14.93743 1.000 34.41532  ? 99  THR   A O   1 
ATOM   665  C  CB  . THR   A 1 92  ? 4.25249   33.41076 12.45400 1.000 40.18690  ? 99  THR   A CB  1 
ATOM   666  O  OG1 . THR   A 1 92  ? 5.42869   34.07768 12.93248 1.000 36.24216  ? 99  THR   A OG1 1 
ATOM   667  C  CG2 . THR   A 1 92  ? 3.12013   34.41572 12.36082 1.000 30.50716  ? 99  THR   A CG2 1 
ATOM   668  N  N   . LYS   A 1 93  ? 5.70148   30.81288 12.76508 1.000 37.28803  ? 100 LYS   A N   1 
ATOM   669  C  CA  . LYS   A 1 93  ? 6.93815   30.07443 12.99523 1.000 40.14049  ? 100 LYS   A CA  1 
ATOM   670  C  C   . LYS   A 1 93  ? 8.08346   31.00983 13.35420 1.000 37.99246  ? 100 LYS   A C   1 
ATOM   671  O  O   . LYS   A 1 93  ? 8.96580   30.63520 14.13456 1.000 40.09844  ? 100 LYS   A O   1 
ATOM   672  C  CB  . LYS   A 1 93  ? 7.29529   29.24147 11.76527 1.000 35.35134  ? 100 LYS   A CB  1 
ATOM   673  C  CG  . LYS   A 1 93  ? 8.09190   27.99037 12.08391 1.000 36.75783  ? 100 LYS   A CG  1 
ATOM   674  C  CD  . LYS   A 1 93  ? 9.26214   27.82307 11.13172 1.000 38.99233  ? 100 LYS   A CD  1 
ATOM   675  C  CE  . LYS   A 1 93  ? 9.60491   26.35475 10.94185 1.000 39.61897  ? 100 LYS   A CE  1 
ATOM   676  N  NZ  . LYS   A 1 93  ? 10.50866  26.13143 9.77889  1.000 42.58547  ? 100 LYS   A NZ  1 
ATOM   677  N  N   . ALA   A 1 94  ? 8.08027   32.22874 12.80615 1.000 40.37424  ? 101 ALA   A N   1 
ATOM   678  C  CA  . ALA   A 1 94  ? 9.10107   33.20604 13.16646 1.000 41.60633  ? 101 ALA   A CA  1 
ATOM   679  C  C   . ALA   A 1 94  ? 8.95952   33.65994 14.61234 1.000 42.29718  ? 101 ALA   A C   1 
ATOM   680  O  O   . ALA   A 1 94  ? 9.93966   34.10361 15.21823 1.000 45.48489  ? 101 ALA   A O   1 
ATOM   681  C  CB  . ALA   A 1 94  ? 9.03959   34.40614 12.22602 1.000 42.19431  ? 101 ALA   A CB  1 
ATOM   682  N  N   . ASP   A 1 95  ? 7.75476   33.56399 15.17773 1.000 41.90685  ? 102 ASP   A N   1 
ATOM   683  C  CA  . ASP   A 1 95  ? 7.57772   33.86769 16.59338 1.000 40.50830  ? 102 ASP   A CA  1 
ATOM   684  C  C   . ASP   A 1 95  ? 8.31577   32.86406 17.46336 1.000 42.16667  ? 102 ASP   A C   1 
ATOM   685  O  O   . ASP   A 1 95  ? 9.00488   33.24327 18.41626 1.000 45.02899  ? 102 ASP   A O   1 
ATOM   686  C  CB  . ASP   A 1 95  ? 6.09358   33.87841 16.94694 1.000 37.53131  ? 102 ASP   A CB  1 
ATOM   687  C  CG  . ASP   A 1 95  ? 5.46515   35.22641 16.74065 1.000 37.18696  ? 102 ASP   A CG  1 
ATOM   688  O  OD1 . ASP   A 1 95  ? 5.99075   36.20545 17.30851 1.000 52.41699  ? 102 ASP   A OD1 1 
ATOM   689  O  OD2 . ASP   A 1 95  ? 4.45485   35.30682 16.00992 1.000 34.78568  ? 102 ASP   A OD2 1 
ATOM   690  N  N   . LEU   A 1 96  ? 8.17819   31.57962 17.15438 1.000 40.76836  ? 103 LEU   A N   1 
ATOM   691  C  CA  . LEU   A 1 96  ? 8.88545   30.55105 17.89833 1.000 42.56004  ? 103 LEU   A CA  1 
ATOM   692  C  C   . LEU   A 1 96  ? 10.38184  30.67113 17.62483 1.000 47.55033  ? 103 LEU   A C   1 
ATOM   693  O  O   . LEU   A 1 96  ? 11.13796  31.13505 18.48404 1.000 69.93146  ? 103 LEU   A O   1 
ATOM   694  C  CB  . LEU   A 1 96  ? 8.32770   29.17240 17.53777 1.000 48.48935  ? 103 LEU   A CB  1 
ATOM   695  C  CG  . LEU   A 1 96  ? 6.78860   29.15883 17.58106 1.000 40.34173  ? 103 LEU   A CG  1 
ATOM   696  C  CD1 . LEU   A 1 96  ? 6.18530   28.24296 16.52265 1.000 35.08311  ? 103 LEU   A CD1 1 
ATOM   697  C  CD2 . LEU   A 1 96  ? 6.25962   28.80894 18.97161 1.000 37.36329  ? 103 LEU   A CD2 1 
ATOM   698  N  N   . ILE   A 1 97  ? 10.82129  30.30677 16.42550 1.000 45.93547  ? 104 ILE   A N   1 
ATOM   699  C  CA  . ILE   A 1 97  ? 12.20839  30.53237 16.02958 1.000 54.95009  ? 104 ILE   A CA  1 
ATOM   700  C  C   . ILE   A 1 97  ? 12.33579  31.97058 15.53620 1.000 72.07278  ? 104 ILE   A C   1 
ATOM   701  O  O   . ILE   A 1 97  ? 11.80447  32.30669 14.47595 1.000 92.19519  ? 104 ILE   A O   1 
ATOM   702  C  CB  . ILE   A 1 97  ? 12.65346  29.53933 14.95346 1.000 49.33385  ? 104 ILE   A CB  1 
ATOM   703  C  CG1 . ILE   A 1 97  ? 12.07746  28.15889 15.25069 1.000 47.46960  ? 104 ILE   A CG1 1 
ATOM   704  C  CG2 . ILE   A 1 97  ? 14.16972  29.49793 14.86703 1.000 55.86605  ? 104 ILE   A CG2 1 
ATOM   705  C  CD1 . ILE   A 1 97  ? 11.02678  27.72119 14.27464 1.000 45.06755  ? 104 ILE   A CD1 1 
ATOM   706  N  N   . ASN   A 1 98  ? 13.03039  32.81277 16.32117 1.000 60.21580  ? 105 ASN   A N   1 
ATOM   707  C  CA  . ASN   A 1 98  ? 13.41096  34.20910 16.06420 1.000 55.99509  ? 105 ASN   A CA  1 
ATOM   708  C  C   . ASN   A 1 98  ? 12.54464  35.20014 16.83730 1.000 55.15622  ? 105 ASN   A C   1 
ATOM   709  O  O   . ASN   A 1 98  ? 12.79780  35.43373 18.02105 1.000 61.53830  ? 105 ASN   A O   1 
ATOM   710  C  CB  . ASN   A 1 98  ? 13.39050  34.57341 14.57540 1.000 55.20060  ? 105 ASN   A CB  1 
ATOM   711  C  CG  . ASN   A 1 98  ? 14.34315  33.72908 13.75659 1.000 58.83196  ? 105 ASN   A CG  1 
ATOM   712  O  OD1 . ASN   A 1 98  ? 15.51188  33.56713 14.11028 1.000 77.27144  ? 105 ASN   A OD1 1 
ATOM   713  N  ND2 . ASN   A 1 98  ? 13.84206  33.17160 12.66034 1.000 54.21289  ? 105 ASN   A ND2 1 
ATOM   714  N  N   . ASN   A 1 99  ? 11.53025  35.78023 16.18087 1.000 61.95611  ? 106 ASN   A N   1 
ATOM   715  C  CA  . ASN   A 1 99  ? 10.80965  36.97276 16.64410 1.000 65.29140  ? 106 ASN   A CA  1 
ATOM   716  C  C   . ASN   A 1 99  ? 10.54111  37.02364 18.14458 1.000 52.81348  ? 106 ASN   A C   1 
ATOM   717  O  O   . ASN   A 1 99  ? 11.23719  37.73162 18.87949 1.000 65.21615  ? 106 ASN   A O   1 
ATOM   718  C  CB  . ASN   A 1 99  ? 9.47083   37.10842 15.91297 1.000 48.04296  ? 106 ASN   A CB  1 
ATOM   719  C  CG  . ASN   A 1 99  ? 9.63443   37.48212 14.45675 1.000 62.73270  ? 106 ASN   A CG  1 
ATOM   720  O  OD1 . ASN   A 1 99  ? 10.73644  37.79383 13.99720 1.000 51.20184  ? 106 ASN   A OD1 1 
ATOM   721  N  ND2 . ASN   A 1 99  ? 8.53097   37.45498 13.71867 1.000 54.66639  ? 106 ASN   A ND2 1 
ATOM   722  N  N   . LEU   A 1 100 ? 9.51521   36.30293 18.60395 1.000 61.98928  ? 107 LEU   A N   1 
ATOM   723  C  CA  . LEU   A 1 100 ? 9.20688   36.28776 20.03041 1.000 64.50865  ? 107 LEU   A CA  1 
ATOM   724  C  C   . LEU   A 1 100 ? 10.38019  35.76264 20.84751 1.000 60.09662  ? 107 LEU   A C   1 
ATOM   725  O  O   . LEU   A 1 100 ? 10.51615  36.10555 22.02746 1.000 59.49800  ? 107 LEU   A O   1 
ATOM   726  C  CB  . LEU   A 1 100 ? 7.94639   35.45524 20.28404 1.000 75.46626  ? 107 LEU   A CB  1 
ATOM   727  C  CG  . LEU   A 1 100 ? 7.57148   35.06737 21.71641 1.000 67.54592  ? 107 LEU   A CG  1 
ATOM   728  C  CD1 . LEU   A 1 100 ? 6.09326   35.31231 21.95290 1.000 46.71061  ? 107 LEU   A CD1 1 
ATOM   729  C  CD2 . LEU   A 1 100 ? 7.92563   33.61173 21.99665 1.000 57.06732  ? 107 LEU   A CD2 1 
ATOM   730  N  N   . GLY   A 1 101 ? 11.24329  34.94696 20.23650 1.000 63.25386  ? 108 GLY   A N   1 
ATOM   731  C  CA  . GLY   A 1 101 ? 12.43679  34.49192 20.93179 1.000 62.80135  ? 108 GLY   A CA  1 
ATOM   732  C  C   . GLY   A 1 101 ? 13.31573  35.63470 21.40749 1.000 63.63229  ? 108 GLY   A C   1 
ATOM   733  O  O   . GLY   A 1 101 ? 13.81860  35.61421 22.53355 1.000 75.70021  ? 108 GLY   A O   1 
ATOM   734  N  N   . THR   A 1 102 ? 13.50769  36.65199 20.56265 1.000 65.53988  ? 109 THR   A N   1 
ATOM   735  C  CA  . THR   A 1 102 ? 14.34356  37.78881 20.93360 1.000 69.37828  ? 109 THR   A CA  1 
ATOM   736  C  C   . THR   A 1 102 ? 13.64918  38.76367 21.87892 1.000 69.97439  ? 109 THR   A C   1 
ATOM   737  O  O   . THR   A 1 102 ? 14.32366  39.62459 22.45157 1.000 74.72728  ? 109 THR   A O   1 
ATOM   738  C  CB  . THR   A 1 102 ? 14.81585  38.54491 19.68685 1.000 70.48066  ? 109 THR   A CB  1 
ATOM   739  O  OG1 . THR   A 1 102 ? 13.83241  39.52014 19.32042 1.000 68.24779  ? 109 THR   A OG1 1 
ATOM   740  C  CG2 . THR   A 1 102 ? 15.05796  37.58761 18.52368 1.000 68.32175  ? 109 THR   A CG2 1 
ATOM   741  N  N   . ILE   A 1 103 ? 12.33515  38.65079 22.06831 1.000 65.69310  ? 110 ILE   A N   1 
ATOM   742  C  CA  . ILE   A 1 103 ? 11.62634  39.50400 23.01687 1.000 68.76258  ? 110 ILE   A CA  1 
ATOM   743  C  C   . ILE   A 1 103 ? 11.47655  38.73251 24.32087 1.000 74.59942  ? 110 ILE   A C   1 
ATOM   744  O  O   . ILE   A 1 103 ? 10.37071  38.32781 24.70014 1.000 96.16741  ? 110 ILE   A O   1 
ATOM   745  C  CB  . ILE   A 1 103 ? 10.25806  39.96145 22.47247 1.000 73.50238  ? 110 ILE   A CB  1 
ATOM   746  C  CG1 . ILE   A 1 103 ? 10.40861  40.61091 21.09711 1.000 65.89016  ? 110 ILE   A CG1 1 
ATOM   747  C  CG2 . ILE   A 1 103 ? 9.60637   40.96446 23.41486 1.000 73.25154  ? 110 ILE   A CG2 1 
ATOM   748  C  CD1 . ILE   A 1 103 ? 9.08675   40.98561 20.46175 1.000 57.33304  ? 110 ILE   A CD1 1 
ATOM   749  N  N   . ALA   A 1 104 ? 12.59975  38.49751 24.99481 1.000 71.42513  ? 111 ALA   A N   1 
ATOM   750  C  CA  . ALA   A 1 104 ? 12.61050  37.84644 26.29735 1.000 73.07903  ? 111 ALA   A CA  1 
ATOM   751  C  C   . ALA   A 1 104 ? 13.99755  37.94358 26.91014 1.000 79.38042  ? 111 ALA   A C   1 
ATOM   752  O  O   . ALA   A 1 104 ? 14.13336  37.97633 28.13647 1.000 82.71499  ? 111 ALA   A O   1 
ATOM   753  C  CB  . ALA   A 1 104 ? 12.18679  36.38165 26.19397 1.000 69.41946  ? 111 ALA   A CB  1 
ATOM   754  N  N   . LYS   A 1 105 ? 15.02889  37.97220 26.05901 1.000 68.50596  ? 112 LYS   A N   1 
ATOM   755  C  CA  . LYS   A 1 105 ? 16.39793  38.14586 26.53639 1.000 51.77290  ? 112 LYS   A CA  1 
ATOM   756  C  C   . LYS   A 1 105 ? 16.49865  39.35784 27.44749 1.000 43.78522  ? 112 LYS   A C   1 
ATOM   757  O  O   . LYS   A 1 105 ? 17.02658  39.27384 28.56098 1.000 45.83088  ? 112 LYS   A O   1 
ATOM   758  C  CB  . LYS   A 1 105 ? 17.35266  38.29018 25.34918 1.000 58.08819  ? 112 LYS   A CB  1 
ATOM   759  C  CG  . LYS   A 1 105 ? 18.81558  38.05194 25.67866 1.000 62.64896  ? 112 LYS   A CG  1 
ATOM   760  C  CD  . LYS   A 1 105 ? 19.68910  38.08150 24.42474 1.000 69.35725  ? 112 LYS   A CD  1 
ATOM   761  C  CE  . LYS   A 1 105 ? 18.96534  37.50607 23.21274 1.000 70.42195  ? 112 LYS   A CE  1 
ATOM   762  N  NZ  . LYS   A 1 105 ? 19.82951  37.46203 21.99916 1.000 78.31599  ? 112 LYS   A NZ  1 
ATOM   763  N  N   . SER   A 1 106 ? 15.97336  40.49569 26.99045 1.000 44.18908  ? 113 SER   A N   1 
ATOM   764  C  CA  . SER   A 1 106 ? 15.97323  41.69477 27.81836 1.000 40.62738  ? 113 SER   A CA  1 
ATOM   765  C  C   . SER   A 1 106 ? 15.11023  41.50540 29.05829 1.000 38.42265  ? 113 SER   A C   1 
ATOM   766  O  O   . SER   A 1 106 ? 15.51311  41.87762 30.16647 1.000 39.74476  ? 113 SER   A O   1 
ATOM   767  C  CB  . SER   A 1 106 ? 15.49118  42.89338 27.00064 1.000 46.40156  ? 113 SER   A CB  1 
ATOM   768  O  OG  . SER   A 1 106 ? 14.47591  42.51579 26.08573 1.000 41.39796  ? 113 SER   A OG  1 
ATOM   769  N  N   . GLY   A 1 107 ? 13.92139  40.92272 28.89367 1.000 40.58521  ? 114 GLY   A N   1 
ATOM   770  C  CA  . GLY   A 1 107 ? 13.05183  40.71150 30.03872 1.000 38.07673  ? 114 GLY   A CA  1 
ATOM   771  C  C   . GLY   A 1 107 ? 13.61758  39.70532 31.02107 1.000 32.95899  ? 114 GLY   A C   1 
ATOM   772  O  O   . GLY   A 1 107 ? 13.44621  39.84397 32.23494 1.000 33.45702  ? 114 GLY   A O   1 
ATOM   773  N  N   . THR   A 1 108 ? 14.30458  38.68294 30.51292 1.000 31.87532  ? 115 THR   A N   1 
ATOM   774  C  CA  . THR   A 1 108 ? 14.89576  37.68100 31.39229 1.000 41.69173  ? 115 THR   A CA  1 
ATOM   775  C  C   . THR   A 1 108 ? 16.02750  38.27819 32.22071 1.000 39.69624  ? 115 THR   A C   1 
ATOM   776  O  O   . THR   A 1 108 ? 16.09197  38.07296 33.43809 1.000 34.25507  ? 115 THR   A O   1 
ATOM   777  C  CB  . THR   A 1 108 ? 15.39926  36.49458 30.57141 1.000 38.76594  ? 115 THR   A CB  1 
ATOM   778  O  OG1 . THR   A 1 108 ? 14.32700  35.97447 29.77637 1.000 31.74454  ? 115 THR   A OG1 1 
ATOM   779  C  CG2 . THR   A 1 108 ? 15.90911  35.40869 31.48372 1.000 32.54849  ? 115 THR   A CG2 1 
ATOM   780  N  N   . LYS   A 1 109 ? 16.92903  39.02485 31.57592 1.000 36.51717  ? 116 LYS   A N   1 
ATOM   781  C  CA  . LYS   A 1 109 ? 18.03953  39.64066 32.29818 1.000 42.41269  ? 116 LYS   A CA  1 
ATOM   782  C  C   . LYS   A 1 109 ? 17.53784  40.55177 33.41196 1.000 42.27028  ? 116 LYS   A C   1 
ATOM   783  O  O   . LYS   A 1 109 ? 17.99695  40.46273 34.55686 1.000 43.03974  ? 116 LYS   A O   1 
ATOM   784  C  CB  . LYS   A 1 109 ? 18.93339  40.42245 31.33285 1.000 45.20300  ? 116 LYS   A CB  1 
ATOM   785  C  CG  . LYS   A 1 109 ? 19.56593  39.58918 30.23029 1.000 51.69287  ? 116 LYS   A CG  1 
ATOM   786  C  CD  . LYS   A 1 109 ? 20.51905  40.41574 29.37280 1.000 60.46330  ? 116 LYS   A CD  1 
ATOM   787  C  CE  . LYS   A 1 109 ? 21.31276  41.41005 30.20901 1.000 54.71283  ? 116 LYS   A CE  1 
ATOM   788  N  NZ  . LYS   A 1 109 ? 22.30154  40.72395 31.08857 1.000 53.55626  ? 116 LYS   A NZ  1 
ATOM   789  N  N   . ALA   A 1 110 ? 16.59106  41.43808 33.09307 1.000 41.44712  ? 117 ALA   A N   1 
ATOM   790  C  CA  . ALA   A 1 110 ? 16.08868  42.37184 34.09423 1.000 43.71777  ? 117 ALA   A CA  1 
ATOM   791  C  C   . ALA   A 1 110 ? 15.39594  41.64924 35.23995 1.000 42.08023  ? 117 ALA   A C   1 
ATOM   792  O  O   . ALA   A 1 110 ? 15.40979  42.13543 36.37702 1.000 44.82931  ? 117 ALA   A O   1 
ATOM   793  C  CB  . ALA   A 1 110 ? 15.13461  43.37365 33.44555 1.000 48.36104  ? 117 ALA   A CB  1 
ATOM   794  N  N   . PHE   A 1 111 ? 14.79620  40.48772 34.96458 1.000 38.29504  ? 118 PHE   A N   1 
ATOM   795  C  CA  . PHE   A 1 111 ? 14.07288  39.75618 36.00005 1.000 37.17689  ? 118 PHE   A CA  1 
ATOM   796  C  C   . PHE   A 1 111 ? 15.03258  39.13158 37.00682 1.000 41.63388  ? 118 PHE   A C   1 
ATOM   797  O  O   . PHE   A 1 111 ? 14.82412  39.23251 38.22136 1.000 40.26754  ? 118 PHE   A O   1 
ATOM   798  C  CB  . PHE   A 1 111 ? 13.18351  38.68856 35.35970 1.000 33.56650  ? 118 PHE   A CB  1 
ATOM   799  C  CG  . PHE   A 1 111 ? 12.36130  37.90468 36.34688 1.000 34.39780  ? 118 PHE   A CG  1 
ATOM   800  C  CD1 . PHE   A 1 111 ? 11.65544  38.54766 37.35107 1.000 35.24511  ? 118 PHE   A CD1 1 
ATOM   801  C  CD2 . PHE   A 1 111 ? 12.29179  36.52189 36.26656 1.000 37.35982  ? 118 PHE   A CD2 1 
ATOM   802  C  CE1 . PHE   A 1 111 ? 10.89793  37.82555 38.25817 1.000 35.36442  ? 118 PHE   A CE1 1 
ATOM   803  C  CE2 . PHE   A 1 111 ? 11.53787  35.79468 37.17180 1.000 30.70669  ? 118 PHE   A CE2 1 
ATOM   804  C  CZ  . PHE   A 1 111 ? 10.84152  36.44726 38.16830 1.000 33.03819  ? 118 PHE   A CZ  1 
ATOM   805  N  N   . MET   A 1 112 ? 16.09567  38.48191 36.52458 1.000 41.54665  ? 119 MET   A N   1 
ATOM   806  C  CA  . MET   A 1 112 ? 17.03421  37.85941 37.45209 1.000 45.21795  ? 119 MET   A CA  1 
ATOM   807  C  C   . MET   A 1 112 ? 17.80508  38.90020 38.25194 1.000 44.19106  ? 119 MET   A C   1 
ATOM   808  O  O   . MET   A 1 112 ? 18.16515  38.64662 39.40703 1.000 52.96530  ? 119 MET   A O   1 
ATOM   809  C  CB  . MET   A 1 112 ? 18.00684  36.94592 36.70931 1.000 43.66231  ? 119 MET   A CB  1 
ATOM   810  C  CG  . MET   A 1 112 ? 17.40901  36.18564 35.54623 1.000 36.84132  ? 119 MET   A CG  1 
ATOM   811  S  SD  . MET   A 1 112 ? 18.44185  34.78398 35.08705 1.000 51.18233  ? 119 MET   A SD  1 
ATOM   812  C  CE  . MET   A 1 112 ? 18.90745  35.23040 33.41580 1.000 45.36899  ? 119 MET   A CE  1 
ATOM   813  N  N   . GLU   A 1 113 ? 18.07471  40.06596 37.66021 1.000 46.18547  ? 120 GLU   A N   1 
ATOM   814  C  CA  . GLU   A 1 113 ? 18.70359  41.14531 38.41487 1.000 51.29559  ? 120 GLU   A CA  1 
ATOM   815  C  C   . GLU   A 1 113 ? 17.81586  41.58356 39.57135 1.000 52.85622  ? 120 GLU   A C   1 
ATOM   816  O  O   . GLU   A 1 113 ? 18.27979  41.72622 40.70879 1.000 56.64648  ? 120 GLU   A O   1 
ATOM   817  C  CB  . GLU   A 1 113 ? 19.00710  42.32789 37.49508 1.000 53.48058  ? 120 GLU   A CB  1 
ATOM   818  C  CG  . GLU   A 1 113 ? 20.24308  42.15595 36.63218 1.000 54.73742  ? 120 GLU   A CG  1 
ATOM   819  C  CD  . GLU   A 1 113 ? 20.21994  43.05059 35.40844 1.000 74.21256  ? 120 GLU   A CD  1 
ATOM   820  O  OE1 . GLU   A 1 113 ? 19.22841  43.79047 35.23055 1.000 75.85802  ? 120 GLU   A OE1 1 
ATOM   821  O  OE2 . GLU   A 1 113 ? 21.19306  43.01652 34.62627 1.000 75.54993  ? 120 GLU   A OE2 1 
ATOM   822  N  N   . ALA   A 1 114 ? 16.52608  41.79676 39.29586 1.000 50.63908  ? 121 ALA   A N   1 
ATOM   823  C  CA  . ALA   A 1 114 ? 15.59502  42.17570 40.35153 1.000 52.69246  ? 121 ALA   A CA  1 
ATOM   824  C  C   . ALA   A 1 114 ? 15.41102  41.05666 41.36699 1.000 55.55411  ? 121 ALA   A C   1 
ATOM   825  O  O   . ALA   A 1 114 ? 15.12963  41.32788 42.53981 1.000 71.12637  ? 121 ALA   A O   1 
ATOM   826  C  CB  . ALA   A 1 114 ? 14.24837  42.56990 39.74811 1.000 50.96370  ? 121 ALA   A CB  1 
ATOM   827  N  N   . LEU   A 1 115 ? 15.57232  39.80055 40.94177 1.000 47.99697  ? 122 LEU   A N   1 
ATOM   828  C  CA  . LEU   A 1 115 ? 15.40275  38.68018 41.86093 1.000 51.99699  ? 122 LEU   A CA  1 
ATOM   829  C  C   . LEU   A 1 115 ? 16.44548  38.69727 42.97115 1.000 61.81171  ? 122 LEU   A C   1 
ATOM   830  O  O   . LEU   A 1 115 ? 16.17353  38.23201 44.08406 1.000 62.73128  ? 122 LEU   A O   1 
ATOM   831  C  CB  . LEU   A 1 115 ? 15.45944  37.36133 41.09212 1.000 44.74081  ? 122 LEU   A CB  1 
ATOM   832  C  CG  . LEU   A 1 115 ? 14.15472  36.97634 40.39156 1.000 45.79986  ? 122 LEU   A CG  1 
ATOM   833  C  CD1 . LEU   A 1 115 ? 14.38141  35.85249 39.39031 1.000 42.27893  ? 122 LEU   A CD1 1 
ATOM   834  C  CD2 . LEU   A 1 115 ? 13.09353  36.59071 41.41057 1.000 46.90140  ? 122 LEU   A CD2 1 
ATOM   835  N  N   . GLN   A 1 116 ? 17.63641  39.22538 42.69433 1.000 63.78198  ? 123 GLN   A N   1 
ATOM   836  C  CA  . GLN   A 1 116 ? 18.66277  39.38095 43.71455 1.000 59.40636  ? 123 GLN   A CA  1 
ATOM   837  C  C   . GLN   A 1 116 ? 18.58885  40.72429 44.42474 1.000 72.57378  ? 123 GLN   A C   1 
ATOM   838  O  O   . GLN   A 1 116 ? 19.29167  40.92029 45.42227 1.000 90.37587  ? 123 GLN   A O   1 
ATOM   839  C  CB  . GLN   A 1 116 ? 20.05347  39.20802 43.09854 1.000 60.36682  ? 123 GLN   A CB  1 
ATOM   840  C  CG  . GLN   A 1 116 ? 20.25420  37.87960 42.39556 1.000 65.53549  ? 123 GLN   A CG  1 
ATOM   841  C  CD  . GLN   A 1 116 ? 21.33329  37.94213 41.33423 1.000 76.06551  ? 123 GLN   A CD  1 
ATOM   842  O  OE1 . GLN   A 1 116 ? 21.92272  38.99580 41.09222 1.000 96.61041  ? 123 GLN   A OE1 1 
ATOM   843  N  NE2 . GLN   A 1 116 ? 21.59522  36.81115 40.69063 1.000 63.06657  ? 123 GLN   A NE2 1 
ATOM   844  N  N   . ALA   A 1 117 ? 17.76443  41.65003 43.93585 1.000 64.18293  ? 124 ALA   A N   1 
ATOM   845  C  CA  . ALA   A 1 117 ? 17.57545  42.95062 44.56335 1.000 69.85366  ? 124 ALA   A CA  1 
ATOM   846  C  C   . ALA   A 1 117 ? 16.21208  43.05699 45.24004 1.000 84.01579  ? 124 ALA   A C   1 
ATOM   847  O  O   . ALA   A 1 117 ? 15.61906  44.13734 45.29085 1.000 96.14870  ? 124 ALA   A O   1 
ATOM   848  C  CB  . ALA   A 1 117 ? 17.75629  44.07149 43.54138 1.000 70.47547  ? 124 ALA   A CB  1 
ATOM   849  N  N   . GLY   A 1 118 ? 15.69896  41.93864 45.74979 1.000 80.49922  ? 125 GLY   A N   1 
ATOM   850  C  CA  . GLY   A 1 118 ? 14.46816  41.95163 46.51559 1.000 85.38454  ? 125 GLY   A CA  1 
ATOM   851  C  C   . GLY   A 1 118 ? 13.29879  41.23147 45.87526 1.000 68.40317  ? 125 GLY   A C   1 
ATOM   852  O  O   . GLY   A 1 118 ? 12.55021  40.52944 46.56210 1.000 82.67001  ? 125 GLY   A O   1 
ATOM   853  N  N   . ALA   A 1 119 ? 13.13341  41.39302 44.56379 1.000 65.32852  ? 126 ALA   A N   1 
ATOM   854  C  CA  . ALA   A 1 119 ? 11.94779  40.88527 43.88582 1.000 56.21935  ? 126 ALA   A CA  1 
ATOM   855  C  C   . ALA   A 1 119 ? 11.87664  39.36392 43.95921 1.000 52.63892  ? 126 ALA   A C   1 
ATOM   856  O  O   . ALA   A 1 119 ? 12.89036  38.67331 44.09285 1.000 51.82574  ? 126 ALA   A O   1 
ATOM   857  C  CB  . ALA   A 1 119 ? 11.93501  41.33845 42.42593 1.000 53.03729  ? 126 ALA   A CB  1 
ATOM   858  N  N   . ASP   A 1 120 ? 10.65715  38.84586 43.87285 1.000 51.17876  ? 127 ASP   A N   1 
ATOM   859  C  CA  . ASP   A 1 120 ? 10.39018  37.41500 43.89215 1.000 53.06233  ? 127 ASP   A CA  1 
ATOM   860  C  C   . ASP   A 1 120 ? 9.71861   36.99962 42.58365 1.000 46.26454  ? 127 ASP   A C   1 
ATOM   861  O  O   . ASP   A 1 120 ? 9.40754   37.82897 41.72505 1.000 43.53340  ? 127 ASP   A O   1 
ATOM   862  C  CB  . ASP   A 1 120 ? 9.53588   37.03849 45.10627 1.000 55.29756  ? 127 ASP   A CB  1 
ATOM   863  C  CG  . ASP   A 1 120 ? 8.11052   37.53378 44.99093 1.000 59.62096  ? 127 ASP   A CG  1 
ATOM   864  O  OD1 . ASP   A 1 120 ? 7.92091   38.71538 44.63309 1.000 57.54423  ? 127 ASP   A OD1 1 
ATOM   865  O  OD2 . ASP   A 1 120 ? 7.17985   36.74287 45.25843 1.000 53.71587  ? 127 ASP   A OD2 1 
ATOM   866  N  N   . ILE   A 1 121 ? 9.48703   35.69069 42.44861 1.000 49.55586  ? 128 ILE   A N   1 
ATOM   867  C  CA  . ILE   A 1 121 ? 9.06414   35.11928 41.17161 1.000 45.99756  ? 128 ILE   A CA  1 
ATOM   868  C  C   . ILE   A 1 121 ? 7.68954   35.63121 40.75621 1.000 47.21011  ? 128 ILE   A C   1 
ATOM   869  O  O   . ILE   A 1 121 ? 7.40858   35.76929 39.55863 1.000 48.87533  ? 128 ILE   A O   1 
ATOM   870  C  CB  . ILE   A 1 121 ? 9.10052   33.57780 41.25182 1.000 39.17932  ? 128 ILE   A CB  1 
ATOM   871  C  CG1 . ILE   A 1 121 ? 10.52509  33.09430 41.52348 1.000 45.04982  ? 128 ILE   A CG1 1 
ATOM   872  C  CG2 . ILE   A 1 121 ? 8.58497   32.94590 39.96649 1.000 36.12279  ? 128 ILE   A CG2 1 
ATOM   873  C  CD1 . ILE   A 1 121 ? 10.60293  31.65247 41.96949 1.000 39.66699  ? 128 ILE   A CD1 1 
ATOM   874  N  N   . SER   A 1 122 ? 6.82180   35.94689 41.72214 1.000 42.17155  ? 129 SER   A N   1 
ATOM   875  C  CA  . SER   A 1 122 ? 5.45692   36.35533 41.39763 1.000 51.25257  ? 129 SER   A CA  1 
ATOM   876  C  C   . SER   A 1 122 ? 5.39004   37.64873 40.59526 1.000 43.96228  ? 129 SER   A C   1 
ATOM   877  O  O   . SER   A 1 122 ? 4.30349   38.00919 40.12858 1.000 45.26525  ? 129 SER   A O   1 
ATOM   878  C  CB  . SER   A 1 122 ? 4.62896   36.51094 42.67512 1.000 62.01460  ? 129 SER   A CB  1 
ATOM   879  O  OG  . SER   A 1 122 ? 5.42479   36.97438 43.75049 1.000 62.55763  ? 129 SER   A OG  1 
ATOM   880  N  N   . MET   A 1 123 ? 6.50979   38.35065 40.42298 1.000 43.36687  ? 130 MET   A N   1 
ATOM   881  C  CA  . MET   A 1 123 ? 6.55888   39.57965 39.64520 1.000 44.03788  ? 130 MET   A CA  1 
ATOM   882  C  C   . MET   A 1 123 ? 7.06669   39.34846 38.22716 1.000 39.98829  ? 130 MET   A C   1 
ATOM   883  O  O   . MET   A 1 123 ? 7.44078   40.30907 37.54567 1.000 44.34337  ? 130 MET   A O   1 
ATOM   884  C  CB  . MET   A 1 123 ? 7.43435   40.61482 40.35088 1.000 47.22879  ? 130 MET   A CB  1 
ATOM   885  C  CG  . MET   A 1 123 ? 7.17161   40.75254 41.84072 1.000 53.64712  ? 130 MET   A CG  1 
ATOM   886  S  SD  . MET   A 1 123 ? 8.22962   41.99397 42.61091 1.000 57.99465  ? 130 MET   A SD  1 
ATOM   887  C  CE  . MET   A 1 123 ? 8.91861   42.79367 41.16587 1.000 62.48598  ? 130 MET   A CE  1 
ATOM   888  N  N   . ILE   A 1 124 ? 7.08657   38.09282 37.77123 1.000 39.77479  ? 131 ILE   A N   1 
ATOM   889  C  CA  . ILE   A 1 124 ? 7.62827   37.76827 36.45672 1.000 33.49777  ? 131 ILE   A CA  1 
ATOM   890  C  C   . ILE   A 1 124 ? 6.81931   38.40763 35.33435 1.000 44.77591  ? 131 ILE   A C   1 
ATOM   891  O  O   . ILE   A 1 124 ? 7.35085   38.63457 34.24162 1.000 32.43916  ? 131 ILE   A O   1 
ATOM   892  C  CB  . ILE   A 1 124 ? 7.71003   36.23364 36.28933 1.000 32.59384  ? 131 ILE   A CB  1 
ATOM   893  C  CG1 . ILE   A 1 124 ? 8.62549   35.86472 35.12025 1.000 28.49935  ? 131 ILE   A CG1 1 
ATOM   894  C  CG2 . ILE   A 1 124 ? 6.32056   35.63037 36.11170 1.000 31.25908  ? 131 ILE   A CG2 1 
ATOM   895  C  CD1 . ILE   A 1 124 ? 8.99105   34.39885 35.07509 1.000 26.85807  ? 131 ILE   A CD1 1 
ATOM   896  N  N   . GLY   A 1 125 ? 5.54263   38.71742 35.57888 1.000 49.48147  ? 132 GLY   A N   1 
ATOM   897  C  CA  . GLY   A 1 125 ? 4.73590   39.35858 34.55559 1.000 37.17237  ? 132 GLY   A CA  1 
ATOM   898  C  C   . GLY   A 1 125 ? 5.19884   40.76198 34.22201 1.000 41.99773  ? 132 GLY   A C   1 
ATOM   899  O  O   . GLY   A 1 125 ? 5.11595   41.18738 33.06583 1.000 38.96120  ? 132 GLY   A O   1 
ATOM   900  N  N   . GLN   A 1 126 ? 5.70949   41.49270 35.21689 1.000 42.00091  ? 133 GLN   A N   1 
ATOM   901  C  CA  . GLN   A 1 126 ? 6.17671   42.85714 34.99938 1.000 44.09515  ? 133 GLN   A CA  1 
ATOM   902  C  C   . GLN   A 1 126 ? 7.37314   42.93194 34.06172 1.000 41.93511  ? 133 GLN   A C   1 
ATOM   903  O  O   . GLN   A 1 126 ? 7.78214   44.03882 33.69552 1.000 52.60625  ? 133 GLN   A O   1 
ATOM   904  C  CB  . GLN   A 1 126 ? 6.53368   43.50562 36.33748 1.000 47.63895  ? 133 GLN   A CB  1 
ATOM   905  C  CG  . GLN   A 1 126 ? 5.36525   44.18085 37.03366 1.000 63.44615  ? 133 GLN   A CG  1 
ATOM   906  C  CD  . GLN   A 1 126 ? 5.28694   43.83128 38.50697 1.000 78.77486  ? 133 GLN   A CD  1 
ATOM   907  O  OE1 . GLN   A 1 126 ? 6.25959   43.98768 39.24895 1.000 69.22600  ? 133 GLN   A OE1 1 
ATOM   908  N  NE2 . GLN   A 1 126 ? 4.12514   43.34865 38.93840 1.000 55.93758  ? 133 GLN   A NE2 1 
ATOM   909  N  N   . PHE   A 1 127 ? 7.94458   41.79552 33.67180 1.000 41.64594  ? 134 PHE   A N   1 
ATOM   910  C  CA  . PHE   A 1 127 ? 9.07025   41.75867 32.75150 1.000 46.22707  ? 134 PHE   A CA  1 
ATOM   911  C  C   . PHE   A 1 127 ? 8.71468   41.11447 31.41875 1.000 34.50227  ? 134 PHE   A C   1 
ATOM   912  O  O   . PHE   A 1 127 ? 9.59758   40.94346 30.57049 1.000 33.62518  ? 134 PHE   A O   1 
ATOM   913  C  CB  . PHE   A 1 127 ? 10.25336  41.02510 33.39782 1.000 35.30274  ? 134 PHE   A CB  1 
ATOM   914  C  CG  . PHE   A 1 127 ? 10.71242  41.64098 34.69320 1.000 38.08819  ? 134 PHE   A CG  1 
ATOM   915  C  CD1 . PHE   A 1 127 ? 10.08676  41.32390 35.88908 1.000 38.86786  ? 134 PHE   A CD1 1 
ATOM   916  C  CD2 . PHE   A 1 127 ? 11.76303  42.54580 34.71291 1.000 40.67715  ? 134 PHE   A CD2 1 
ATOM   917  C  CE1 . PHE   A 1 127 ? 10.50245  41.89291 37.07954 1.000 42.15482  ? 134 PHE   A CE1 1 
ATOM   918  C  CE2 . PHE   A 1 127 ? 12.18286  43.11589 35.90012 1.000 43.98976  ? 134 PHE   A CE2 1 
ATOM   919  C  CZ  . PHE   A 1 127 ? 11.55262  42.78741 37.08430 1.000 44.71994  ? 134 PHE   A CZ  1 
ATOM   920  N  N   . GLY   A 1 128 ? 7.44881   40.75447 31.21377 1.000 34.31542  ? 135 GLY   A N   1 
ATOM   921  C  CA  . GLY   A 1 128 ? 7.00688   40.23224 29.93730 1.000 33.23279  ? 135 GLY   A CA  1 
ATOM   922  C  C   . GLY   A 1 128 ? 7.45552   38.82571 29.62499 1.000 30.37370  ? 135 GLY   A C   1 
ATOM   923  O  O   . GLY   A 1 128 ? 7.45382   38.43572 28.45529 1.000 29.95333  ? 135 GLY   A O   1 
ATOM   924  N  N   . VAL   A 1 129 ? 7.83977   38.04643 30.63544 1.000 29.00600  ? 136 VAL   A N   1 
ATOM   925  C  CA  . VAL   A 1 129 ? 8.31788   36.68444 30.41574 1.000 28.38674  ? 136 VAL   A CA  1 
ATOM   926  C  C   . VAL   A 1 129 ? 7.59556   35.73537 31.36347 1.000 26.82894  ? 136 VAL   A C   1 
ATOM   927  O  O   . VAL   A 1 129 ? 8.19056   34.78273 31.88173 1.000 31.65538  ? 136 VAL   A O   1 
ATOM   928  C  CB  . VAL   A 1 129 ? 9.84787   36.58886 30.59044 1.000 34.98865  ? 136 VAL   A CB  1 
ATOM   929  C  CG1 . VAL   A 1 129 ? 10.56417  37.26847 29.42829 1.000 27.43302  ? 136 VAL   A CG1 1 
ATOM   930  C  CG2 . VAL   A 1 129 ? 10.28288  37.19552 31.91990 1.000 27.50751  ? 136 VAL   A CG2 1 
ATOM   931  N  N   . GLY   A 1 130 ? 6.30154   35.98170 31.58373 1.000 21.21503  ? 137 GLY   A N   1 
ATOM   932  C  CA  . GLY   A 1 130 ? 5.53516   35.18007 32.52127 1.000 25.60895  ? 137 GLY   A CA  1 
ATOM   933  C  C   . GLY   A 1 130 ? 5.25832   33.76222 32.06212 1.000 28.78035  ? 137 GLY   A C   1 
ATOM   934  O  O   . GLY   A 1 130 ? 4.84096   32.93284 32.87717 1.000 25.94023  ? 137 GLY   A O   1 
ATOM   935  N  N   . PHE   A 1 131 ? 5.48014   33.46261 30.77915 1.000 28.39738  ? 138 PHE   A N   1 
ATOM   936  C  CA  . PHE   A 1 131 ? 5.19755   32.11988 30.27981 1.000 30.23093  ? 138 PHE   A CA  1 
ATOM   937  C  C   . PHE   A 1 131 ? 6.04783   31.07065 30.98635 1.000 32.14386  ? 138 PHE   A C   1 
ATOM   938  O  O   . PHE   A 1 131 ? 5.55709   29.98413 31.31702 1.000 22.61386  ? 138 PHE   A O   1 
ATOM   939  C  CB  . PHE   A 1 131 ? 5.42354   32.05287 28.76864 1.000 29.34999  ? 138 PHE   A CB  1 
ATOM   940  C  CG  . PHE   A 1 131 ? 5.52429   30.64826 28.23787 1.000 34.64770  ? 138 PHE   A CG  1 
ATOM   941  C  CD1 . PHE   A 1 131 ? 4.38231   29.89700 28.01037 1.000 17.17487  ? 138 PHE   A CD1 1 
ATOM   942  C  CD2 . PHE   A 1 131 ? 6.76239   30.07458 27.97938 1.000 36.32345  ? 138 PHE   A CD2 1 
ATOM   943  C  CE1 . PHE   A 1 131 ? 4.46931   28.60480 27.52971 1.000 29.39501  ? 138 PHE   A CE1 1 
ATOM   944  C  CE2 . PHE   A 1 131 ? 6.85679   28.78121 27.50175 1.000 24.39325  ? 138 PHE   A CE2 1 
ATOM   945  C  CZ  . PHE   A 1 131 ? 5.70802   28.04456 27.27618 1.000 27.55324  ? 138 PHE   A CZ  1 
ATOM   946  N  N   . TYR   A 1 132 ? 7.32644   31.37519 31.22513 1.000 33.23166  ? 139 TYR   A N   1 
ATOM   947  C  CA  . TYR   A 1 132 ? 8.24027   30.40741 31.82358 1.000 30.04633  ? 139 TYR   A CA  1 
ATOM   948  C  C   . TYR   A 1 132 ? 7.86100   30.03345 33.24945 1.000 32.85474  ? 139 TYR   A C   1 
ATOM   949  O  O   . TYR   A 1 132 ? 8.43004   29.07892 33.79109 1.000 30.39073  ? 139 TYR   A O   1 
ATOM   950  C  CB  . TYR   A 1 132 ? 9.66892   30.94726 31.79202 1.000 38.40979  ? 139 TYR   A CB  1 
ATOM   951  C  CG  . TYR   A 1 132 ? 10.06154  31.51243 30.45127 1.000 30.81461  ? 139 TYR   A CG  1 
ATOM   952  C  CD1 . TYR   A 1 132 ? 10.21092  30.68686 29.34481 1.000 20.80701  ? 139 TYR   A CD1 1 
ATOM   953  C  CD2 . TYR   A 1 132 ? 10.27229  32.87321 30.28939 1.000 25.34775  ? 139 TYR   A CD2 1 
ATOM   954  C  CE1 . TYR   A 1 132 ? 10.56586  31.20125 28.11656 1.000 19.75837  ? 139 TYR   A CE1 1 
ATOM   955  C  CE2 . TYR   A 1 132 ? 10.62653  33.39602 29.06767 1.000 34.72638  ? 139 TYR   A CE2 1 
ATOM   956  C  CZ  . TYR   A 1 132 ? 10.77118  32.55682 27.98545 1.000 31.64353  ? 139 TYR   A CZ  1 
ATOM   957  O  OH  . TYR   A 1 132 ? 11.12944  33.08428 26.77121 1.000 30.51714  ? 139 TYR   A OH  1 
ATOM   958  N  N   . SER   A 1 133 ? 6.92757   30.75837 33.87018 1.000 34.08193  ? 140 SER   A N   1 
ATOM   959  C  CA  . SER   A 1 133 ? 6.35376   30.30810 35.13030 1.000 32.54117  ? 140 SER   A CA  1 
ATOM   960  C  C   . SER   A 1 133 ? 5.55056   29.02660 34.96723 1.000 28.11890  ? 140 SER   A C   1 
ATOM   961  O  O   . SER   A 1 133 ? 5.23309   28.38155 35.97169 1.000 29.19904  ? 140 SER   A O   1 
ATOM   962  C  CB  . SER   A 1 133 ? 5.46706   31.40033 35.73044 1.000 28.15433  ? 140 SER   A CB  1 
ATOM   963  O  OG  . SER   A 1 133 ? 4.38995   31.71489 34.86426 1.000 32.91269  ? 140 SER   A OG  1 
ATOM   964  N  N   . ALA   A 1 134 ? 5.21166   28.65016 33.73085 1.000 26.27793  ? 141 ALA   A N   1 
ATOM   965  C  CA  . ALA   A 1 134 ? 4.55321   27.37050 33.49970 1.000 38.93405  ? 141 ALA   A CA  1 
ATOM   966  C  C   . ALA   A 1 134 ? 5.42964   26.20976 33.94187 1.000 31.41595  ? 141 ALA   A C   1 
ATOM   967  O  O   . ALA   A 1 134 ? 4.91552   25.14751 34.30833 1.000 32.91883  ? 141 ALA   A O   1 
ATOM   968  C  CB  . ALA   A 1 134 ? 4.18808   27.22462 32.02306 1.000 35.04601  ? 141 ALA   A CB  1 
ATOM   969  N  N   . TYR   A 1 135 ? 6.74895   26.39485 33.92445 1.000 29.10034  ? 142 TYR   A N   1 
ATOM   970  C  CA  . TYR   A 1 135 ? 7.66868   25.35058 34.34757 1.000 31.00950  ? 142 TYR   A CA  1 
ATOM   971  C  C   . TYR   A 1 135 ? 7.79162   25.24384 35.85988 1.000 30.44758  ? 142 TYR   A C   1 
ATOM   972  O  O   . TYR   A 1 135 ? 8.46879   24.33018 36.34369 1.000 33.44106  ? 142 TYR   A O   1 
ATOM   973  C  CB  . TYR   A 1 135 ? 9.03749   25.58264 33.71119 1.000 29.68156  ? 142 TYR   A CB  1 
ATOM   974  C  CG  . TYR   A 1 135 ? 9.02436   25.28159 32.23327 1.000 34.67525  ? 142 TYR   A CG  1 
ATOM   975  C  CD1 . TYR   A 1 135 ? 8.73164   26.27487 31.30447 1.000 23.97561  ? 142 TYR   A CD1 1 
ATOM   976  C  CD2 . TYR   A 1 135 ? 9.26847   23.99486 31.76738 1.000 26.01936  ? 142 TYR   A CD2 1 
ATOM   977  C  CE1 . TYR   A 1 135 ? 8.70330   25.99972 29.95004 1.000 22.90257  ? 142 TYR   A CE1 1 
ATOM   978  C  CE2 . TYR   A 1 135 ? 9.24230   23.70871 30.41638 1.000 27.55849  ? 142 TYR   A CE2 1 
ATOM   979  C  CZ  . TYR   A 1 135 ? 8.95915   24.71475 29.51132 1.000 31.69668  ? 142 TYR   A CZ  1 
ATOM   980  O  OH  . TYR   A 1 135 ? 8.93339   24.43372 28.16361 1.000 31.98547  ? 142 TYR   A OH  1 
ATOM   981  N  N   . LEU   A 1 136 ? 7.16210   26.14827 36.61383 1.000 27.49093  ? 143 LEU   A N   1 
ATOM   982  C  CA  . LEU   A 1 136 ? 6.97363   25.90553 38.03877 1.000 27.93781  ? 143 LEU   A CA  1 
ATOM   983  C  C   . LEU   A 1 136 ? 6.20835   24.60754 38.25491 1.000 37.36766  ? 143 LEU   A C   1 
ATOM   984  O  O   . LEU   A 1 136 ? 6.64433   23.72834 39.00641 1.000 46.65138  ? 143 LEU   A O   1 
ATOM   985  C  CB  . LEU   A 1 136 ? 6.22735   27.07371 38.68558 1.000 29.04514  ? 143 LEU   A CB  1 
ATOM   986  C  CG  . LEU   A 1 136 ? 6.90141   28.43517 38.85754 1.000 34.92976  ? 143 LEU   A CG  1 
ATOM   987  C  CD1 . LEU   A 1 136 ? 5.85386   29.48039 39.21737 1.000 28.32817  ? 143 LEU   A CD1 1 
ATOM   988  C  CD2 . LEU   A 1 136 ? 7.98740   28.38018 39.91891 1.000 31.57106  ? 143 LEU   A CD2 1 
ATOM   989  N  N   . VAL   A 1 137 ? 5.07472   24.45868 37.57148 1.000 28.60629  ? 144 VAL   A N   1 
ATOM   990  C  CA  . VAL   A 1 137 ? 4.21500   23.29839 37.75757 1.000 28.70426  ? 144 VAL   A CA  1 
ATOM   991  C  C   . VAL   A 1 137 ? 4.43134   22.21321 36.70672 1.000 28.78306  ? 144 VAL   A C   1 
ATOM   992  O  O   . VAL   A 1 137 ? 4.11725   21.04360 36.97380 1.000 34.10860  ? 144 VAL   A O   1 
ATOM   993  C  CB  . VAL   A 1 137 ? 2.73058   23.72238 37.77841 1.000 33.56708  ? 144 VAL   A CB  1 
ATOM   994  C  CG1 . VAL   A 1 137 ? 2.47850   24.72994 38.89076 1.000 28.83756  ? 144 VAL   A CG1 1 
ATOM   995  C  CG2 . VAL   A 1 137 ? 2.32637   24.29892 36.43144 1.000 38.98818  ? 144 VAL   A CG2 1 
ATOM   996  N  N   . ALA   A 1 138 ? 4.95575   22.55467 35.53340 1.000 30.65717  ? 145 ALA   A N   1 
ATOM   997  C  CA  . ALA   A 1 138 ? 5.06803   21.60937 34.43144 1.000 27.67229  ? 145 ALA   A CA  1 
ATOM   998  C  C   . ALA   A 1 138 ? 6.50664   21.14934 34.25731 1.000 28.60431  ? 145 ALA   A C   1 
ATOM   999  O  O   . ALA   A 1 138 ? 7.44229   21.95004 34.34426 1.000 27.94079  ? 145 ALA   A O   1 
ATOM   1000 C  CB  . ALA   A 1 138 ? 4.56642   22.22199 33.12193 1.000 27.59078  ? 145 ALA   A CB  1 
ATOM   1001 N  N   . GLU   A 1 139 ? 6.67133   19.84669 34.02152 1.000 33.64438  ? 146 GLU   A N   1 
ATOM   1002 C  CA  . GLU   A 1 139 ? 7.94925   19.27350 33.62089 1.000 31.91342  ? 146 GLU   A CA  1 
ATOM   1003 C  C   . GLU   A 1 139 ? 8.17425   19.35661 32.11887 1.000 31.19341  ? 146 GLU   A C   1 
ATOM   1004 O  O   . GLU   A 1 139 ? 9.30245   19.14460 31.66121 1.000 36.88154  ? 146 GLU   A O   1 
ATOM   1005 C  CB  . GLU   A 1 139 ? 8.02863   17.81141 34.05918 1.000 35.00507  ? 146 GLU   A CB  1 
ATOM   1006 C  CG  . GLU   A 1 139 ? 7.23669   16.88149 33.15881 1.000 36.15582  ? 146 GLU   A CG  1 
ATOM   1007 C  CD  . GLU   A 1 139 ? 7.05546   15.50605 33.75304 1.000 47.57309  ? 146 GLU   A CD  1 
ATOM   1008 O  OE1 . GLU   A 1 139 ? 7.03590   15.39845 34.99691 1.000 58.78512  ? 146 GLU   A OE1 1 
ATOM   1009 O  OE2 . GLU   A 1 139 ? 6.91951   14.53521 32.97760 1.000 54.14940  ? 146 GLU   A OE2 1 
ATOM   1010 N  N   . LYS   A 1 140 ? 7.12630   19.64665 31.35223 1.000 32.73085  ? 147 LYS   A N   1 
ATOM   1011 C  CA  . LYS   A 1 140 ? 7.20224   19.75422 29.90459 1.000 29.30779  ? 147 LYS   A CA  1 
ATOM   1012 C  C   . LYS   A 1 140 ? 5.97472   20.51423 29.43309 1.000 27.47649  ? 147 LYS   A C   1 
ATOM   1013 O  O   . LYS   A 1 140 ? 4.86855   20.28199 29.92577 1.000 32.46414  ? 147 LYS   A O   1 
ATOM   1014 C  CB  . LYS   A 1 140 ? 7.27166   18.37702 29.23277 1.000 32.04583  ? 147 LYS   A CB  1 
ATOM   1015 C  CG  . LYS   A 1 140 ? 7.05801   18.40905 27.72779 1.000 32.00962  ? 147 LYS   A CG  1 
ATOM   1016 C  CD  . LYS   A 1 140 ? 7.25903   17.03864 27.11146 1.000 35.39267  ? 147 LYS   A CD  1 
ATOM   1017 C  CE  . LYS   A 1 140 ? 5.96676   16.48928 26.53300 1.000 36.67129  ? 147 LYS   A CE  1 
ATOM   1018 N  NZ  . LYS   A 1 140 ? 5.83868   15.02509 26.77177 1.000 40.48781  ? 147 LYS   A NZ  1 
ATOM   1019 N  N   . VAL   A 1 141 ? 6.17939   21.43166 28.49613 1.000 25.85438  ? 148 VAL   A N   1 
ATOM   1020 C  CA  . VAL   A 1 141 ? 5.10839   22.25230 27.95103 1.000 24.31804  ? 148 VAL   A CA  1 
ATOM   1021 C  C   . VAL   A 1 141 ? 5.10365   22.06730 26.44237 1.000 24.76157  ? 148 VAL   A C   1 
ATOM   1022 O  O   . VAL   A 1 141 ? 6.09102   22.38861 25.76928 1.000 26.50908  ? 148 VAL   A O   1 
ATOM   1023 C  CB  . VAL   A 1 141 ? 5.27459   23.73469 28.32429 1.000 22.20349  ? 148 VAL   A CB  1 
ATOM   1024 C  CG1 . VAL   A 1 141 ? 4.05769   24.53437 27.88922 1.000 21.06661  ? 148 VAL   A CG1 1 
ATOM   1025 C  CG2 . VAL   A 1 141 ? 5.50970   23.88402 29.81950 1.000 22.35290  ? 148 VAL   A CG2 1 
ATOM   1026 N  N   . THR   A 1 142 ? 4.00734   21.53156 25.91707 1.000 25.81718  ? 149 THR   A N   1 
ATOM   1027 C  CA  . THR   A 1 142 ? 3.75569   21.51391 24.48401 1.000 26.41364  ? 149 THR   A CA  1 
ATOM   1028 C  C   . THR   A 1 142 ? 2.79682   22.64922 24.15041 1.000 24.73221  ? 149 THR   A C   1 
ATOM   1029 O  O   . THR   A 1 142 ? 1.77727   22.82657 24.82646 1.000 24.46448  ? 149 THR   A O   1 
ATOM   1030 C  CB  . THR   A 1 142 ? 3.17694   20.17050 24.03328 1.000 29.41699  ? 149 THR   A CB  1 
ATOM   1031 O  OG1 . THR   A 1 142 ? 4.01885   19.10487 24.49314 1.000 31.80234  ? 149 THR   A OG1 1 
ATOM   1032 C  CG2 . THR   A 1 142 ? 3.08765   20.11100 22.51421 1.000 30.58695  ? 149 THR   A CG2 1 
ATOM   1033 N  N   . VAL   A 1 143 ? 3.13461   23.42824 23.12784 1.000 23.88404  ? 150 VAL   A N   1 
ATOM   1034 C  CA  . VAL   A 1 143 ? 2.32918   24.56889 22.71082 1.000 22.58215  ? 150 VAL   A CA  1 
ATOM   1035 C  C   . VAL   A 1 143 ? 1.92521   24.36297 21.25914 1.000 28.60758  ? 150 VAL   A C   1 
ATOM   1036 O  O   . VAL   A 1 143 ? 2.78331   24.15991 20.39117 1.000 24.71291  ? 150 VAL   A O   1 
ATOM   1037 C  CB  . VAL   A 1 143 ? 3.07786   25.89840 22.88957 1.000 20.51764  ? 150 VAL   A CB  1 
ATOM   1038 C  CG1 . VAL   A 1 143 ? 2.30719   27.03027 22.22757 1.000 19.74242  ? 150 VAL   A CG1 1 
ATOM   1039 C  CG2 . VAL   A 1 143 ? 3.28293   26.18944 24.36717 1.000 26.84905  ? 150 VAL   A CG2 1 
ATOM   1040 N  N   . ILE   A 1 144 ? 0.62217   24.40707 20.99981 1.000 29.88850  ? 151 ILE   A N   1 
ATOM   1041 C  CA  . ILE   A 1 144 ? 0.07457   24.35132 19.65013 1.000 33.69512  ? 151 ILE   A CA  1 
ATOM   1042 C  C   . ILE   A 1 144 ? -0.48656  25.73083 19.33297 1.000 24.93885  ? 151 ILE   A C   1 
ATOM   1043 O  O   . ILE   A 1 144 ? -1.35051  26.23829 20.05869 1.000 24.24648  ? 151 ILE   A O   1 
ATOM   1044 C  CB  . ILE   A 1 144 ? -1.00449  23.26463 19.51654 1.000 39.12530  ? 151 ILE   A CB  1 
ATOM   1045 C  CG1 . ILE   A 1 144 ? -0.63312  22.02736 20.34090 1.000 30.41328  ? 151 ILE   A CG1 1 
ATOM   1046 C  CG2 . ILE   A 1 144 ? -1.20877  22.89323 18.05495 1.000 31.72229  ? 151 ILE   A CG2 1 
ATOM   1047 C  CD1 . ILE   A 1 144 ? 0.64219   21.34292 19.89297 1.000 31.39992  ? 151 ILE   A CD1 1 
ATOM   1048 N  N   . THR   A 1 145 ? 0.00608   26.34218 18.25878 1.000 30.49468  ? 152 THR   A N   1 
ATOM   1049 C  CA  . THR   A 1 145 ? -0.38090  27.69760 17.89790 1.000 32.81733  ? 152 THR   A CA  1 
ATOM   1050 C  C   . THR   A 1 145 ? -0.76662  27.76409 16.42671 1.000 28.54901  ? 152 THR   A C   1 
ATOM   1051 O  O   . THR   A 1 145 ? -0.40482  26.89933 15.62373 1.000 28.56042  ? 152 THR   A O   1 
ATOM   1052 C  CB  . THR   A 1 145 ? 0.74152   28.70336 18.18768 1.000 21.88989  ? 152 THR   A CB  1 
ATOM   1053 O  OG1 . THR   A 1 145 ? 0.24180   30.03691 18.02686 1.000 25.72274  ? 152 THR   A OG1 1 
ATOM   1054 C  CG2 . THR   A 1 145 ? 1.91161   28.48190 17.24750 1.000 22.26530  ? 152 THR   A CG2 1 
ATOM   1055 N  N   . LYS   A 1 146 ? -1.50508  28.81905 16.08603 1.000 25.42103  ? 153 LYS   A N   1 
ATOM   1056 C  CA  . LYS   A 1 146 ? -2.03733  28.99689 14.73957 1.000 27.47434  ? 153 LYS   A CA  1 
ATOM   1057 C  C   . LYS   A 1 146 ? -2.25534  30.48106 14.49075 1.000 30.47136  ? 153 LYS   A C   1 
ATOM   1058 O  O   . LYS   A 1 146 ? -3.06662  31.11471 15.17312 1.000 25.96766  ? 153 LYS   A O   1 
ATOM   1059 C  CB  . LYS   A 1 146 ? -3.34605  28.22255 14.56338 1.000 43.97721  ? 153 LYS   A CB  1 
ATOM   1060 C  CG  . LYS   A 1 146 ? -3.89574  28.22050 13.14566 1.000 34.03334  ? 153 LYS   A CG  1 
ATOM   1061 C  CD  . LYS   A 1 146 ? -2.78968  28.07685 12.11793 1.000 33.50301  ? 153 LYS   A CD  1 
ATOM   1062 C  CE  . LYS   A 1 146 ? -3.35140  28.08057 10.71258 1.000 36.72291  ? 153 LYS   A CE  1 
ATOM   1063 N  NZ  . LYS   A 1 146 ? -3.11725  29.38213 10.03884 1.000 39.04725  ? 153 LYS   A NZ  1 
ATOM   1064 N  N   . HIS   A 1 147 ? -1.53611  31.02338 13.51494 1.000 26.78012  ? 154 HIS   A N   1 
ATOM   1065 C  CA  . HIS   A 1 147 ? -1.63828  32.41501 13.10574 1.000 26.45422  ? 154 HIS   A CA  1 
ATOM   1066 C  C   . HIS   A 1 147 ? -2.24084  32.47348 11.70523 1.000 29.11284  ? 154 HIS   A C   1 
ATOM   1067 O  O   . HIS   A 1 147 ? -2.05771  31.55247 10.90449 1.000 33.28148  ? 154 HIS   A O   1 
ATOM   1068 C  CB  . HIS   A 1 147 ? -0.25262  33.07652 13.13754 1.000 24.93146  ? 154 HIS   A CB  1 
ATOM   1069 C  CG  . HIS   A 1 147 ? -0.27343  34.56231 12.95874 1.000 24.62737  ? 154 HIS   A CG  1 
ATOM   1070 N  ND1 . HIS   A 1 147 ? -0.32402  35.16277 11.71950 1.000 26.25770  ? 154 HIS   A ND1 1 
ATOM   1071 C  CD2 . HIS   A 1 147 ? -0.22394  35.56912 13.86253 1.000 23.28787  ? 154 HIS   A CD2 1 
ATOM   1072 C  CE1 . HIS   A 1 147 ? -0.32015  36.47500 11.86803 1.000 25.90362  ? 154 HIS   A CE1 1 
ATOM   1073 N  NE2 . HIS   A 1 147 ? -0.26064  36.74770 13.15868 1.000 24.18841  ? 154 HIS   A NE2 1 
ATOM   1074 N  N   . ASN   A 1 148 ? -2.97487  33.55496 11.40899 1.000 29.70808  ? 155 ASN   A N   1 
ATOM   1075 C  CA  . ASN   A 1 148 ? -3.63313  33.65043 10.10597 1.000 33.37219  ? 155 ASN   A CA  1 
ATOM   1076 C  C   . ASN   A 1 148 ? -2.64585  33.62802 8.94783  1.000 33.61131  ? 155 ASN   A C   1 
ATOM   1077 O  O   . ASN   A 1 148 ? -3.03268  33.28313 7.82608  1.000 37.31688  ? 155 ASN   A O   1 
ATOM   1078 C  CB  . ASN   A 1 148 ? -4.48246  34.92224 9.98641  1.000 39.79433  ? 155 ASN   A CB  1 
ATOM   1079 C  CG  . ASN   A 1 148 ? -5.17555  35.29885 11.27466 1.000 42.72020  ? 155 ASN   A CG  1 
ATOM   1080 O  OD1 . ASN   A 1 148 ? -4.53343  35.54059 12.29245 1.000 39.87032  ? 155 ASN   A OD1 1 
ATOM   1081 N  ND2 . ASN   A 1 148 ? -6.49994  35.36061 11.23274 1.000 33.90327  ? 155 ASN   A ND2 1 
ATOM   1082 N  N   . ASP   A 1 149 ? -1.38662  33.98455 9.18797  1.000 31.71895  ? 156 ASP   A N   1 
ATOM   1083 C  CA  . ASP   A 1 149 ? -0.40716  34.14042 8.12273  1.000 35.94051  ? 156 ASP   A CA  1 
ATOM   1084 C  C   . ASP   A 1 149 ? 0.60720   33.00538 8.07868  1.000 32.87075  ? 156 ASP   A C   1 
ATOM   1085 O  O   . ASP   A 1 149 ? 1.60080   33.10612 7.35303  1.000 33.65706  ? 156 ASP   A O   1 
ATOM   1086 C  CB  . ASP   A 1 149 ? 0.30838   35.48595 8.26848  1.000 31.45443  ? 156 ASP   A CB  1 
ATOM   1087 C  CG  . ASP   A 1 149 ? -0.65756  36.66169 8.26912  1.000 37.72473  ? 156 ASP   A CG  1 
ATOM   1088 O  OD1 . ASP   A 1 149 ? -1.79621  36.49808 7.77951  1.000 34.85145  ? 156 ASP   A OD1 1 
ATOM   1089 O  OD2 . ASP   A 1 149 ? -0.28059  37.74900 8.75519  1.000 33.30570  ? 156 ASP   A OD2 1 
ATOM   1090 N  N   . ASP   A 1 150 ? 0.38093   31.92687 8.82400  1.000 32.41303  ? 157 ASP   A N   1 
ATOM   1091 C  CA  . ASP   A 1 150 ? 1.32288   30.81894 8.85734  1.000 38.29710  ? 157 ASP   A CA  1 
ATOM   1092 C  C   . ASP   A 1 150 ? 0.55456   29.51983 9.05756  1.000 35.86452  ? 157 ASP   A C   1 
ATOM   1093 O  O   . ASP   A 1 150 ? -0.65277  29.51795 9.30952  1.000 34.77932  ? 157 ASP   A O   1 
ATOM   1094 C  CB  . ASP   A 1 150 ? 2.37278   31.01582 9.95795  1.000 29.99607  ? 157 ASP   A CB  1 
ATOM   1095 C  CG  . ASP   A 1 150 ? 3.68067   30.31345 9.64856  1.000 30.81277  ? 157 ASP   A CG  1 
ATOM   1096 O  OD1 . ASP   A 1 150 ? 3.73370   29.57125 8.64545  1.000 33.57513  ? 157 ASP   A OD1 1 
ATOM   1097 O  OD2 . ASP   A 1 150 ? 4.65324   30.49922 10.41043 1.000 29.06684  ? 157 ASP   A OD2 1 
ATOM   1098 N  N   . GLU   A 1 151 ? 1.27144   28.40576 8.93212  1.000 35.61529  ? 158 GLU   A N   1 
ATOM   1099 C  CA  . GLU   A 1 151 ? 0.68043   27.09911 9.16380  1.000 37.50693  ? 158 GLU   A CA  1 
ATOM   1100 C  C   . GLU   A 1 151 ? 0.60790   26.81686 10.66279 1.000 35.00455  ? 158 GLU   A C   1 
ATOM   1101 O  O   . GLU   A 1 151 ? 1.03071   27.61952 11.49890 1.000 31.95542  ? 158 GLU   A O   1 
ATOM   1102 C  CB  . GLU   A 1 151 ? 1.47394   26.01611 8.43457  1.000 40.42039  ? 158 GLU   A CB  1 
ATOM   1103 C  CG  . GLU   A 1 151 ? 1.17419   25.91297 6.94458  1.000 44.23730  ? 158 GLU   A CG  1 
ATOM   1104 C  CD  . GLU   A 1 151 ? -0.25576  26.29901 6.60144  1.000 65.33292  ? 158 GLU   A CD  1 
ATOM   1105 O  OE1 . GLU   A 1 151 ? -1.19075  25.57953 7.01555  1.000 53.60852  ? 158 GLU   A OE1 1 
ATOM   1106 O  OE2 . GLU   A 1 151 ? -0.44561  27.32577 5.91579  1.000 76.80055  ? 158 GLU   A OE2 1 
ATOM   1107 N  N   . GLN   A 1 152 ? 0.05184   25.66092 11.00811 1.000 36.70500  ? 159 GLN   A N   1 
ATOM   1108 C  CA  . GLN   A 1 152 ? -0.01308  25.23754 12.39785 1.000 38.00711  ? 159 GLN   A CA  1 
ATOM   1109 C  C   . GLN   A 1 152 ? 1.31133   24.61158 12.81721 1.000 34.49621  ? 159 GLN   A C   1 
ATOM   1110 O  O   . GLN   A 1 152 ? 1.90597   23.82469 12.07521 1.000 36.96983  ? 159 GLN   A O   1 
ATOM   1111 C  CB  . GLN   A 1 152 ? -1.15501  24.24248 12.59534 1.000 42.46667  ? 159 GLN   A CB  1 
ATOM   1112 C  CG  . GLN   A 1 152 ? -1.43735  23.89484 14.04291 1.000 46.07401  ? 159 GLN   A CG  1 
ATOM   1113 C  CD  . GLN   A 1 152 ? -2.90181  23.61007 14.29371 1.000 57.35848  ? 159 GLN   A CD  1 
ATOM   1114 O  OE1 . GLN   A 1 152 ? -3.25634  22.93641 15.26063 1.000 52.86615  ? 159 GLN   A OE1 1 
ATOM   1115 N  NE2 . GLN   A 1 152 ? -3.76409  24.12850 13.42551 1.000 55.32433  ? 159 GLN   A NE2 1 
ATOM   1116 N  N   . TYR   A 1 153 ? 1.77724   24.97115 14.01123 1.000 39.10163  ? 160 TYR   A N   1 
ATOM   1117 C  CA  . TYR   A 1 153 ? 3.05862   24.49975 14.51249 1.000 34.82286  ? 160 TYR   A CA  1 
ATOM   1118 C  C   . TYR   A 1 153 ? 2.92358   24.04391 15.95577 1.000 29.81514  ? 160 TYR   A C   1 
ATOM   1119 O  O   . TYR   A 1 153 ? 2.07836   24.53580 16.70828 1.000 29.89898  ? 160 TYR   A O   1 
ATOM   1120 C  CB  . TYR   A 1 153 ? 4.14411   25.58335 14.41966 1.000 39.10705  ? 160 TYR   A CB  1 
ATOM   1121 C  CG  . TYR   A 1 153 ? 4.52950   25.93881 13.00467 1.000 34.22529  ? 160 TYR   A CG  1 
ATOM   1122 C  CD1 . TYR   A 1 153 ? 5.45152   25.17550 12.30384 1.000 32.99575  ? 160 TYR   A CD1 1 
ATOM   1123 C  CD2 . TYR   A 1 153 ? 3.97320   27.04166 12.37130 1.000 39.34477  ? 160 TYR   A CD2 1 
ATOM   1124 C  CE1 . TYR   A 1 153 ? 5.80410   25.49664 11.00963 1.000 34.74995  ? 160 TYR   A CE1 1 
ATOM   1125 C  CE2 . TYR   A 1 153 ? 4.31878   27.37069 11.07726 1.000 37.83508  ? 160 TYR   A CE2 1 
ATOM   1126 C  CZ  . TYR   A 1 153 ? 5.23471   26.59591 10.40091 1.000 38.93534  ? 160 TYR   A CZ  1 
ATOM   1127 O  OH  . TYR   A 1 153 ? 5.58242   26.92358 9.11092  1.000 37.84876  ? 160 TYR   A OH  1 
ATOM   1128 N  N   . ALA   A 1 154 ? 3.77347   23.09404 16.32994 1.000 44.72577  ? 161 ALA   A N   1 
ATOM   1129 C  CA  . ALA   A 1 154 ? 3.83999   22.57599 17.68795 1.000 38.25904  ? 161 ALA   A CA  1 
ATOM   1130 C  C   . ALA   A 1 154 ? 5.17906   22.97173 18.29314 1.000 28.47387  ? 161 ALA   A C   1 
ATOM   1131 O  O   . ALA   A 1 154 ? 6.23561   22.68039 17.72177 1.000 30.32328  ? 161 ALA   A O   1 
ATOM   1132 C  CB  . ALA   A 1 154 ? 3.66075   21.05815 17.70827 1.000 33.28579  ? 161 ALA   A CB  1 
ATOM   1133 N  N   . TRP   A 1 155 ? 5.12781   23.64734 19.43353 1.000 26.08520  ? 162 TRP   A N   1 
ATOM   1134 C  CA  . TRP   A 1 155 ? 6.30603   24.00534 20.20428 1.000 24.90318  ? 162 TRP   A CA  1 
ATOM   1135 C  C   . TRP   A 1 155 ? 6.33085   23.16212 21.46812 1.000 25.32325  ? 162 TRP   A C   1 
ATOM   1136 O  O   . TRP   A 1 155 ? 5.28068   22.86024 22.04251 1.000 31.10543  ? 162 TRP   A O   1 
ATOM   1137 C  CB  . TRP   A 1 155 ? 6.29766   25.49282 20.55588 1.000 22.42509  ? 162 TRP   A CB  1 
ATOM   1138 C  CG  . TRP   A 1 155 ? 7.45268   25.93447 21.39640 1.000 31.93575  ? 162 TRP   A CG  1 
ATOM   1139 C  CD1 . TRP   A 1 155 ? 8.61905   26.48000 20.95625 1.000 21.73418  ? 162 TRP   A CD1 1 
ATOM   1140 C  CD2 . TRP   A 1 155 ? 7.54318   25.89348 22.82795 1.000 32.12529  ? 162 TRP   A CD2 1 
ATOM   1141 N  NE1 . TRP   A 1 155 ? 9.43597   26.76732 22.02015 1.000 21.32193  ? 162 TRP   A NE1 1 
ATOM   1142 C  CE2 . TRP   A 1 155 ? 8.79874   26.42163 23.18030 1.000 21.27971  ? 162 TRP   A CE2 1 
ATOM   1143 C  CE3 . TRP   A 1 155 ? 6.68582   25.45703 23.84356 1.000 31.11089  ? 162 TRP   A CE3 1 
ATOM   1144 C  CZ2 . TRP   A 1 155 ? 9.22187   26.52536 24.50255 1.000 29.04178  ? 162 TRP   A CZ2 1 
ATOM   1145 C  CZ3 . TRP   A 1 155 ? 7.10672   25.55959 25.15686 1.000 21.69342  ? 162 TRP   A CZ3 1 
ATOM   1146 C  CH2 . TRP   A 1 155 ? 8.36431   26.08969 25.47424 1.000 33.44563  ? 162 TRP   A CH2 1 
ATOM   1147 N  N   . GLU   A 1 156 ? 7.52738   22.78173 21.89950 1.000 25.99013  ? 163 GLU   A N   1 
ATOM   1148 C  CA  . GLU   A 1 156 ? 7.64300   21.85200 23.01005 1.000 26.99903  ? 163 GLU   A CA  1 
ATOM   1149 C  C   . GLU   A 1 156 ? 9.02011   22.00142 23.63219 1.000 32.49951  ? 163 GLU   A C   1 
ATOM   1150 O  O   . GLU   A 1 156 ? 10.00949  22.19532 22.92022 1.000 27.66864  ? 163 GLU   A O   1 
ATOM   1151 C  CB  . GLU   A 1 156 ? 7.40935   20.41154 22.53803 1.000 30.03534  ? 163 GLU   A CB  1 
ATOM   1152 C  CG  . GLU   A 1 156 ? 7.57499   19.34461 23.60099 1.000 31.69492  ? 163 GLU   A CG  1 
ATOM   1153 C  CD  . GLU   A 1 156 ? 7.21616   17.96675 23.07804 1.000 54.09329  ? 163 GLU   A CD  1 
ATOM   1154 O  OE1 . GLU   A 1 156 ? 6.35007   17.88485 22.18089 1.000 55.45023  ? 163 GLU   A OE1 1 
ATOM   1155 O  OE2 . GLU   A 1 156 ? 7.80727   16.96943 23.54734 1.000 41.39555  ? 163 GLU   A OE2 1 
ATOM   1156 N  N   . SER   A 1 157 ? 9.07183   21.91653 24.96061 1.000 33.84836  ? 164 SER   A N   1 
ATOM   1157 C  CA  . SER   A 1 157 ? 10.34023  21.98913 25.67167 1.000 41.41052  ? 164 SER   A CA  1 
ATOM   1158 C  C   . SER   A 1 157 ? 10.16766  21.45420 27.08426 1.000 40.59244  ? 164 SER   A C   1 
ATOM   1159 O  O   . SER   A 1 157 ? 9.26494   21.88435 27.80849 1.000 29.26333  ? 164 SER   A O   1 
ATOM   1160 C  CB  . SER   A 1 157 ? 10.86769  23.42579 25.71411 1.000 36.68430  ? 164 SER   A CB  1 
ATOM   1161 O  OG  . SER   A 1 157 ? 11.90984  23.54795 26.66570 1.000 41.86304  ? 164 SER   A OG  1 
ATOM   1162 N  N   . SER   A 1 158 ? 11.03041  20.50967 27.46378 1.000 43.44367  ? 165 SER   A N   1 
ATOM   1163 C  CA  . SER   A 1 158 ? 11.20356  20.10961 28.85371 1.000 32.16021  ? 165 SER   A CA  1 
ATOM   1164 C  C   . SER   A 1 158 ? 12.25999  20.94879 29.55708 1.000 36.04002  ? 165 SER   A C   1 
ATOM   1165 O  O   . SER   A 1 158 ? 12.90356  20.46668 30.50039 1.000 32.54857  ? 165 SER   A O   1 
ATOM   1166 C  CB  . SER   A 1 158 ? 11.57008  18.62638 28.93619 1.000 37.76696  ? 165 SER   A CB  1 
ATOM   1167 O  OG  . SER   A 1 158 ? 10.63813  17.81405 28.24471 1.000 40.53186  ? 165 SER   A OG  1 
ATOM   1168 N  N   . ALA   A 1 159 ? 12.45125  22.18780 29.11635 1.000 34.07435  ? 166 ALA   A N   1 
ATOM   1169 C  CA  . ALA   A 1 159 ? 13.59226  23.03359 29.50616 1.000 39.11420  ? 166 ALA   A CA  1 
ATOM   1170 C  C   . ALA   A 1 159 ? 14.86217  22.26058 29.13277 1.000 44.09877  ? 166 ALA   A C   1 
ATOM   1171 O  O   . ALA   A 1 159 ? 14.92459  21.65677 28.05039 1.000 46.54722  ? 166 ALA   A O   1 
ATOM   1172 C  CB  . ALA   A 1 159 ? 13.48701  23.44392 30.96003 1.000 29.18217  ? 166 ALA   A CB  1 
ATOM   1173 N  N   . GLY   A 1 160 ? 15.88193  22.24384 29.98382 1.000 33.65589  ? 167 GLY   A N   1 
ATOM   1174 C  CA  . GLY   A 1 160 ? 17.10860  21.58384 29.59576 1.000 36.47067  ? 167 GLY   A CA  1 
ATOM   1175 C  C   . GLY   A 1 160 ? 17.87561  22.28878 28.50429 1.000 36.46751  ? 167 GLY   A C   1 
ATOM   1176 O  O   . GLY   A 1 160 ? 18.75223  21.68177 27.88517 1.000 65.26553  ? 167 GLY   A O   1 
ATOM   1177 N  N   . GLY   A 1 161 ? 17.55575  23.55267 28.23512 1.000 34.14851  ? 168 GLY   A N   1 
ATOM   1178 C  CA  . GLY   A 1 161 ? 18.33428  24.37653 27.33838 1.000 34.38135  ? 168 GLY   A CA  1 
ATOM   1179 C  C   . GLY   A 1 161 ? 17.96071  24.31074 25.87404 1.000 33.61525  ? 168 GLY   A C   1 
ATOM   1180 O  O   . GLY   A 1 161 ? 18.58956  25.00528 25.06592 1.000 39.76963  ? 168 GLY   A O   1 
ATOM   1181 N  N   . SER   A 1 162 ? 16.96461  23.51211 25.49691 1.000 30.20655  ? 169 SER   A N   1 
ATOM   1182 C  CA  . SER   A 1 162 ? 16.58972  23.38259 24.09566 1.000 30.36076  ? 169 SER   A CA  1 
ATOM   1183 C  C   . SER   A 1 162 ? 15.07579  23.25741 23.96820 1.000 28.58875  ? 169 SER   A C   1 
ATOM   1184 O  O   . SER   A 1 162 ? 14.35733  23.02250 24.94401 1.000 22.66540  ? 169 SER   A O   1 
ATOM   1185 C  CB  . SER   A 1 162 ? 17.29141  22.18397 23.43647 1.000 27.91266  ? 169 SER   A CB  1 
ATOM   1186 O  OG  . SER   A 1 162 ? 16.65507  20.96017 23.76358 1.000 27.45007  ? 169 SER   A OG  1 
ATOM   1187 N  N   . PHE   A 1 163 ? 14.59676  23.42871 22.73861 1.000 22.58065  ? 170 PHE   A N   1 
ATOM   1188 C  CA  . PHE   A 1 163 ? 13.18751  23.26563 22.42156 1.000 22.33686  ? 170 PHE   A CA  1 
ATOM   1189 C  C   . PHE   A 1 163 ? 13.07601  22.70192 21.01495 1.000 25.28137  ? 170 PHE   A C   1 
ATOM   1190 O  O   . PHE   A 1 163 ? 14.04363  22.69015 20.24895 1.000 23.47421  ? 170 PHE   A O   1 
ATOM   1191 C  CB  . PHE   A 1 163 ? 12.41728  24.58823 22.53918 1.000 24.25176  ? 170 PHE   A CB  1 
ATOM   1192 C  CG  . PHE   A 1 163 ? 12.75214  25.59442 21.46384 1.000 27.27492  ? 170 PHE   A CG  1 
ATOM   1193 C  CD1 . PHE   A 1 163 ? 13.86307  26.41704 21.58260 1.000 34.43776  ? 170 PHE   A CD1 1 
ATOM   1194 C  CD2 . PHE   A 1 163 ? 11.95104  25.72455 20.34116 1.000 22.29422  ? 170 PHE   A CD2 1 
ATOM   1195 C  CE1 . PHE   A 1 163 ? 14.16867  27.34857 20.60862 1.000 24.70222  ? 170 PHE   A CE1 1 
ATOM   1196 C  CE2 . PHE   A 1 163 ? 12.25536  26.64832 19.35915 1.000 22.81136  ? 170 PHE   A CE2 1 
ATOM   1197 C  CZ  . PHE   A 1 163 ? 13.36416  27.46372 19.49497 1.000 31.93495  ? 170 PHE   A CZ  1 
ATOM   1198 N  N   . THR   A 1 164 ? 11.87670  22.23227 20.68148 1.000 27.97545  ? 171 THR   A N   1 
ATOM   1199 C  CA  . THR   A 1 164 ? 11.57874  21.71996 19.35452 1.000 24.96503  ? 171 THR   A CA  1 
ATOM   1200 C  C   . THR   A 1 164 ? 10.45471  22.53201 18.73022 1.000 25.31110  ? 171 THR   A C   1 
ATOM   1201 O  O   . THR   A 1 164 ? 9.63274   23.13144 19.42942 1.000 23.56987  ? 171 THR   A O   1 
ATOM   1202 C  CB  . THR   A 1 164 ? 11.18154  20.23435 19.38693 1.000 25.51599  ? 171 THR   A CB  1 
ATOM   1203 O  OG1 . THR   A 1 164 ? 10.42045  19.96087 20.56956 1.000 27.01211  ? 171 THR   A OG1 1 
ATOM   1204 C  CG2 . THR   A 1 164 ? 12.41712  19.35062 19.36411 1.000 26.31114  ? 171 THR   A CG2 1 
ATOM   1205 N  N   . VAL   A 1 165 ? 10.44455  22.55988 17.40173 1.000 28.20165  ? 172 VAL   A N   1 
ATOM   1206 C  CA  . VAL   A 1 165 ? 9.34781   23.12367 16.62520 1.000 32.34768  ? 172 VAL   A CA  1 
ATOM   1207 C  C   . VAL   A 1 165 ? 9.10891   22.20069 15.44120 1.000 34.70391  ? 172 VAL   A C   1 
ATOM   1208 O  O   . VAL   A 1 165 ? 10.04760  21.86266 14.71253 1.000 28.87367  ? 172 VAL   A O   1 
ATOM   1209 C  CB  . VAL   A 1 165 ? 9.63786   24.56203 16.14637 1.000 32.88179  ? 172 VAL   A CB  1 
ATOM   1210 C  CG1 . VAL   A 1 165 ? 8.65427   24.97129 15.06110 1.000 26.67917  ? 172 VAL   A CG1 1 
ATOM   1211 C  CG2 . VAL   A 1 165 ? 9.56356   25.53844 17.30768 1.000 24.12477  ? 172 VAL   A CG2 1 
ATOM   1212 N  N   . ARG   A 1 166 ? 7.86204   21.77376 15.26365 1.000 35.75489  ? 173 ARG   A N   1 
ATOM   1213 C  CA  . ARG   A 1 166 ? 7.48741   20.93867 14.13553 1.000 31.34322  ? 173 ARG   A CA  1 
ATOM   1214 C  C   . ARG   A 1 166 ? 6.17764   21.45210 13.56277 1.000 33.46722  ? 173 ARG   A C   1 
ATOM   1215 O  O   . ARG   A 1 166 ? 5.37767   22.07160 14.26851 1.000 31.09611  ? 173 ARG   A O   1 
ATOM   1216 C  CB  . ARG   A 1 166 ? 7.34304   19.46368 14.53911 1.000 32.65522  ? 173 ARG   A CB  1 
ATOM   1217 C  CG  . ARG   A 1 166 ? 6.36759   19.22060 15.68628 1.000 46.64799  ? 173 ARG   A CG  1 
ATOM   1218 C  CD  . ARG   A 1 166 ? 6.16132   17.72963 15.93249 1.000 34.84690  ? 173 ARG   A CD  1 
ATOM   1219 N  NE  . ARG   A 1 166 ? 7.24720   17.13238 16.70284 1.000 57.70587  ? 173 ARG   A NE  1 
ATOM   1220 C  CZ  . ARG   A 1 166 ? 7.45094   17.32993 17.99902 1.000 57.07657  ? 173 ARG   A CZ  1 
ATOM   1221 N  NH1 . ARG   A 1 166 ? 6.63134   18.07634 18.72271 1.000 44.55236  ? 173 ARG   A NH1 1 
ATOM   1222 N  NH2 . ARG   A 1 166 ? 8.49760   16.75484 18.58680 1.000 31.43418  ? 173 ARG   A NH2 1 
ATOM   1223 N  N   . THR   A 1 167 ? 5.97225   21.20642 12.27137 1.000 44.78077  ? 174 THR   A N   1 
ATOM   1224 C  CA  . THR   A 1 167 ? 4.67301   21.46722 11.66642 1.000 36.94051  ? 174 THR   A CA  1 
ATOM   1225 C  C   . THR   A 1 167 ? 3.66217   20.49266 12.25334 1.000 39.60740  ? 174 THR   A C   1 
ATOM   1226 O  O   . THR   A 1 167 ? 3.86547   19.27421 12.20447 1.000 38.95053  ? 174 THR   A O   1 
ATOM   1227 C  CB  . THR   A 1 167 ? 4.74296   21.32955 10.14651 1.000 39.14280  ? 174 THR   A CB  1 
ATOM   1228 O  OG1 . THR   A 1 167 ? 5.26458   22.53711 9.57783  1.000 38.52441  ? 174 THR   A OG1 1 
ATOM   1229 C  CG2 . THR   A 1 167 ? 3.35892   21.06856 9.56638  1.000 42.91565  ? 174 THR   A CG2 1 
ATOM   1230 N  N   . ASP   A 1 168 ? 2.58759   21.02445 12.82786 1.000 40.49627  ? 175 ASP   A N   1 
ATOM   1231 C  CA  . ASP   A 1 168 ? 1.63243   20.17494 13.51907 1.000 37.68331  ? 175 ASP   A CA  1 
ATOM   1232 C  C   . ASP   A 1 168 ? 0.82531   19.34160 12.53208 1.000 45.62303  ? 175 ASP   A C   1 
ATOM   1233 O  O   . ASP   A 1 168 ? 0.51940   19.77224 11.41581 1.000 42.98974  ? 175 ASP   A O   1 
ATOM   1234 C  CB  . ASP   A 1 168 ? 0.69304   21.00856 14.38516 1.000 36.36506  ? 175 ASP   A CB  1 
ATOM   1235 C  CG  . ASP   A 1 168 ? -0.03849  20.17040 15.41000 1.000 45.17850  ? 175 ASP   A CG  1 
ATOM   1236 O  OD1 . ASP   A 1 168 ? 0.53579   19.15500 15.85838 1.000 44.24216  ? 175 ASP   A OD1 1 
ATOM   1237 O  OD2 . ASP   A 1 168 ? -1.18751  20.51691 15.75780 1.000 54.55287  ? 175 ASP   A OD2 1 
ATOM   1238 N  N   . THR   A 1 169 ? 0.48774   18.12574 12.96167 1.000 43.24035  ? 176 THR   A N   1 
ATOM   1239 C  CA  . THR   A 1 169 ? -0.35079  17.22621 12.18716 1.000 47.36912  ? 176 THR   A CA  1 
ATOM   1240 C  C   . THR   A 1 169 ? -1.69113  16.93087 12.84696 1.000 48.81267  ? 176 THR   A C   1 
ATOM   1241 O  O   . THR   A 1 169 ? -2.52554  16.25426 12.23432 1.000 58.16614  ? 176 THR   A O   1 
ATOM   1242 C  CB  . THR   A 1 169 ? 0.38210   15.89912 11.93659 1.000 69.93917  ? 176 THR   A CB  1 
ATOM   1243 O  OG1 . THR   A 1 169 ? 0.49530   15.17241 13.16633 1.000 73.63098  ? 176 THR   A OG1 1 
ATOM   1244 C  CG2 . THR   A 1 169 ? 1.78116   16.15038 11.38091 1.000 50.77398  ? 176 THR   A CG2 1 
ATOM   1245 N  N   . GLY   A 1 170 ? -1.92253  17.42205 14.06491 1.000 58.39609  ? 177 GLY   A N   1 
ATOM   1246 C  CA  . GLY   A 1 170 ? -3.12323  17.10631 14.81976 1.000 63.43660  ? 177 GLY   A CA  1 
ATOM   1247 C  C   . GLY   A 1 170 ? -4.37411  17.79729 14.30424 1.000 56.86527  ? 177 GLY   A C   1 
ATOM   1248 O  O   . GLY   A 1 170 ? -4.44879  18.17438 13.13368 1.000 68.18413  ? 177 GLY   A O   1 
ATOM   1249 N  N   . GLU   A 1 171 ? -5.35649  17.97602 15.17519 1.000 63.79470  ? 178 GLU   A N   1 
ATOM   1250 C  CA  . GLU   A 1 171 ? -6.63212  18.56144 14.78359 1.000 68.91164  ? 178 GLU   A CA  1 
ATOM   1251 C  C   . GLU   A 1 171 ? -6.43485  20.02988 14.41999 1.000 52.10315  ? 178 GLU   A C   1 
ATOM   1252 O  O   . GLU   A 1 171 ? -5.84958  20.78932 15.20750 1.000 45.49696  ? 178 GLU   A O   1 
ATOM   1253 C  CB  . GLU   A 1 171 ? -7.64625  18.42626 15.92163 1.000 76.32979  ? 178 GLU   A CB  1 
ATOM   1254 C  CG  . GLU   A 1 171 ? -7.03991  18.55183 17.31173 1.000 92.34375  ? 178 GLU   A CG  1 
ATOM   1255 C  CD  . GLU   A 1 171 ? -8.06313  18.95288 18.36776 1.000 105.39854 ? 178 GLU   A CD  1 
ATOM   1256 O  OE1 . GLU   A 1 171 ? -9.03120  19.64775 18.00550 1.000 98.41996  ? 178 GLU   A OE1 1 
ATOM   1257 O  OE2 . GLU   A 1 171 ? -7.91254  18.57682 19.55411 1.000 118.38902 ? 178 GLU   A OE2 1 
ATOM   1258 N  N   . PRO   A 1 172 ? -6.90451  20.46504 13.24950 1.000 63.95216  ? 179 PRO   A N   1 
ATOM   1259 C  CA  . PRO   A 1 172 ? -6.71734  21.87140 12.86416 1.000 52.26255  ? 179 PRO   A CA  1 
ATOM   1260 C  C   . PRO   A 1 172 ? -7.36461  22.81829 13.86244 1.000 53.03838  ? 179 PRO   A C   1 
ATOM   1261 O  O   . PRO   A 1 172 ? -8.34121  22.48167 14.53228 1.000 55.28163  ? 179 PRO   A O   1 
ATOM   1262 C  CB  . PRO   A 1 172 ? -7.38781  21.97237 11.48373 1.000 51.79185  ? 179 PRO   A CB  1 
ATOM   1263 C  CG  . PRO   A 1 172 ? -7.78321  20.62113 11.08217 1.000 60.92741  ? 179 PRO   A CG  1 
ATOM   1264 C  CD  . PRO   A 1 172 ? -7.48014  19.64256 12.17638 1.000 65.31442  ? 179 PRO   A CD  1 
ATOM   1265 N  N   . MET   A 1 173 ? -6.80602  24.02480 13.94649 1.000 56.13977  ? 180 MET   A N   1 
ATOM   1266 C  CA  . MET   A 1 173 ? -7.13997  24.97961 14.99235 1.000 42.78572  ? 180 MET   A CA  1 
ATOM   1267 C  C   . MET   A 1 173 ? -7.93156  26.17895 14.51182 1.000 43.68739  ? 180 MET   A C   1 
ATOM   1268 O  O   . MET   A 1 173 ? -8.66040  26.76952 15.30758 1.000 43.80299  ? 180 MET   A O   1 
ATOM   1269 C  CB  . MET   A 1 173 ? -5.86008  25.48952 15.66201 1.000 56.75069  ? 180 MET   A CB  1 
ATOM   1270 C  CG  . MET   A 1 173 ? -5.43249  24.67277 16.85383 1.000 68.11070  ? 180 MET   A CG  1 
ATOM   1271 S  SD  . MET   A 1 173 ? -4.48795  25.60229 18.06653 1.000 48.80633  ? 180 MET   A SD  1 
ATOM   1272 C  CE  . MET   A 1 173 ? -5.13179  24.81929 19.53239 1.000 45.62432  ? 180 MET   A CE  1 
ATOM   1273 N  N   . GLY   A 1 174 ? -7.80328  26.55708 13.24372 1.000 55.34295  ? 181 GLY   A N   1 
ATOM   1274 C  CA  . GLY   A 1 174 ? -8.35019  27.81662 12.78499 1.000 45.31094  ? 181 GLY   A CA  1 
ATOM   1275 C  C   . GLY   A 1 174 ? -7.45873  28.97786 13.17225 1.000 42.62309  ? 181 GLY   A C   1 
ATOM   1276 O  O   . GLY   A 1 174 ? -6.81716  29.59272 12.31431 1.000 42.40328  ? 181 GLY   A O   1 
ATOM   1277 N  N   . ARG   A 1 175 ? -7.39588  29.26737 14.47000 1.000 40.97075  ? 182 ARG   A N   1 
ATOM   1278 C  CA  . ARG   A 1 175 ? -6.62896  30.38734 14.99646 1.000 38.94338  ? 182 ARG   A CA  1 
ATOM   1279 C  C   . ARG   A 1 175 ? -6.58895  30.27905 16.51421 1.000 37.68409  ? 182 ARG   A C   1 
ATOM   1280 O  O   . ARG   A 1 175 ? -7.53571  29.78627 17.13509 1.000 38.93077  ? 182 ARG   A O   1 
ATOM   1281 C  CB  . ARG   A 1 175 ? -7.24639  31.72526 14.57389 1.000 45.59712  ? 182 ARG   A CB  1 
ATOM   1282 C  CG  . ARG   A 1 175 ? -6.25148  32.83068 14.28982 1.000 39.17193  ? 182 ARG   A CG  1 
ATOM   1283 C  CD  . ARG   A 1 175 ? -6.91386  34.19515 14.40649 1.000 40.51362  ? 182 ARG   A CD  1 
ATOM   1284 N  NE  . ARG   A 1 175 ? -7.83484  34.27068 15.53562 1.000 41.07047  ? 182 ARG   A NE  1 
ATOM   1285 C  CZ  . ARG   A 1 175 ? -9.15567  34.32066 15.42743 1.000 43.35863  ? 182 ARG   A CZ  1 
ATOM   1286 N  NH1 . ARG   A 1 175 ? -9.75403  34.29196 14.24786 1.000 45.33365  ? 182 ARG   A NH1 1 
ATOM   1287 N  NH2 . ARG   A 1 175 ? -9.89419  34.39999 16.53053 1.000 44.00621  ? 182 ARG   A NH2 1 
ATOM   1288 N  N   . GLY   A 1 176 ? -5.49152  30.74275 17.10068 1.000 23.83036  ? 183 GLY   A N   1 
ATOM   1289 C  CA  . GLY   A 1 176 ? -5.31935  30.74810 18.53974 1.000 21.95839  ? 183 GLY   A CA  1 
ATOM   1290 C  C   . GLY   A 1 176 ? -4.11514  29.93430 18.96927 1.000 20.45187  ? 183 GLY   A C   1 
ATOM   1291 O  O   . GLY   A 1 176 ? -3.28640  29.51341 18.15706 1.000 20.57740  ? 183 GLY   A O   1 
ATOM   1292 N  N   . THR   A 1 177 ? -4.02934  29.70288 20.27952 1.000 20.66533  ? 184 THR   A N   1 
ATOM   1293 C  CA  . THR   A 1 177 ? -2.88159  29.03521 20.88104 1.000 19.84057  ? 184 THR   A CA  1 
ATOM   1294 C  C   . THR   A 1 177 ? -3.33851  28.13069 22.01548 1.000 18.79863  ? 184 THR   A C   1 
ATOM   1295 O  O   . THR   A 1 177 ? -4.10426  28.55770 22.88406 1.000 25.43255  ? 184 THR   A O   1 
ATOM   1296 C  CB  . THR   A 1 177 ? -1.86516  30.05470 21.41018 1.000 16.11568  ? 184 THR   A CB  1 
ATOM   1297 O  OG1 . THR   A 1 177 ? -1.15153  30.63560 20.31193 1.000 16.08201  ? 184 THR   A OG1 1 
ATOM   1298 C  CG2 . THR   A 1 177 ? -0.87988  29.38406 22.35674 1.000 15.47221  ? 184 THR   A CG2 1 
ATOM   1299 N  N   . LYS   A 1 178 ? -2.86072  26.88967 22.00794 1.000 19.66952  ? 185 LYS   A N   1 
ATOM   1300 C  CA  . LYS   A 1 178 ? -3.11236  25.93067 23.07488 1.000 24.91743  ? 185 LYS   A CA  1 
ATOM   1301 C  C   . LYS   A 1 178 ? -1.80577  25.64039 23.79892 1.000 27.87623  ? 185 LYS   A C   1 
ATOM   1302 O  O   . LYS   A 1 178 ? -0.80302  25.29647 23.16351 1.000 26.77301  ? 185 LYS   A O   1 
ATOM   1303 C  CB  . LYS   A 1 178 ? -3.70654  24.63527 22.51811 1.000 31.53661  ? 185 LYS   A CB  1 
ATOM   1304 C  CG  . LYS   A 1 178 ? -4.09528  23.61164 23.55814 1.000 27.38628  ? 185 LYS   A CG  1 
ATOM   1305 C  CD  . LYS   A 1 178 ? -3.87588  22.19583 23.05579 1.000 47.32378  ? 185 LYS   A CD  1 
ATOM   1306 C  CE  . LYS   A 1 178 ? -5.16232  21.56441 22.54383 1.000 55.64032  ? 185 LYS   A CE  1 
ATOM   1307 N  NZ  . LYS   A 1 178 ? -4.91118  20.23286 21.91410 1.000 49.29386  ? 185 LYS   A NZ  1 
ATOM   1308 N  N   . VAL   A 1 179 ? -1.81707  25.77868 25.12001 1.000 22.45187  ? 186 VAL   A N   1 
ATOM   1309 C  CA  . VAL   A 1 179 ? -0.63960  25.53963 25.94655 1.000 30.64920  ? 186 VAL   A CA  1 
ATOM   1310 C  C   . VAL   A 1 179 ? -0.92417  24.30669 26.79639 1.000 25.40136  ? 186 VAL   A C   1 
ATOM   1311 O  O   . VAL   A 1 179 ? -1.75062  24.35046 27.71677 1.000 23.81354  ? 186 VAL   A O   1 
ATOM   1312 C  CB  . VAL   A 1 179 ? -0.29426  26.75941 26.81459 1.000 26.68738  ? 186 VAL   A CB  1 
ATOM   1313 C  CG1 . VAL   A 1 179 ? 0.65207   26.36968 27.94768 1.000 20.88442  ? 186 VAL   A CG1 1 
ATOM   1314 C  CG2 . VAL   A 1 179 ? 0.29952   27.87987 25.95738 1.000 20.82479  ? 186 VAL   A CG2 1 
ATOM   1315 N  N   . ILE   A 1 180 ? -0.25507  23.20053 26.48227 1.000 21.75855  ? 187 ILE   A N   1 
ATOM   1316 C  CA  . ILE   A 1 180 ? -0.41730  21.94784 27.21171 1.000 26.37440  ? 187 ILE   A CA  1 
ATOM   1317 C  C   . ILE   A 1 180 ? 0.67929   21.86781 28.26259 1.000 26.94477  ? 187 ILE   A C   1 
ATOM   1318 O  O   . ILE   A 1 180 ? 1.87073   21.92223 27.93640 1.000 24.00798  ? 187 ILE   A O   1 
ATOM   1319 C  CB  . ILE   A 1 180 ? -0.36439  20.73175 26.27490 1.000 27.95651  ? 187 ILE   A CB  1 
ATOM   1320 C  CG1 . ILE   A 1 180 ? -1.44847  20.82541 25.20606 1.000 26.38230  ? 187 ILE   A CG1 1 
ATOM   1321 C  CG2 . ILE   A 1 180 ? -0.52282  19.44724 27.06975 1.000 28.45948  ? 187 ILE   A CG2 1 
ATOM   1322 C  CD1 . ILE   A 1 180 ? -1.11096  20.05953 23.94873 1.000 28.22240  ? 187 ILE   A CD1 1 
ATOM   1323 N  N   . LEU   A 1 181 ? 0.27969   21.72587 29.51818 1.000 29.22734  ? 188 LEU   A N   1 
ATOM   1324 C  CA  . LEU   A 1 181 ? 1.20083   21.66063 30.64590 1.000 25.07721  ? 188 LEU   A CA  1 
ATOM   1325 C  C   . LEU   A 1 181 ? 1.24836   20.22249 31.14403 1.000 32.71644  ? 188 LEU   A C   1 
ATOM   1326 O  O   . LEU   A 1 181 ? 0.33862   19.77081 31.84469 1.000 29.17458  ? 188 LEU   A O   1 
ATOM   1327 C  CB  . LEU   A 1 181 ? 0.76075   22.60624 31.75461 1.000 23.95371  ? 188 LEU   A CB  1 
ATOM   1328 C  CG  . LEU   A 1 181 ? 0.60491   24.06615 31.35786 1.000 24.74161  ? 188 LEU   A CG  1 
ATOM   1329 C  CD1 . LEU   A 1 181 ? 0.03939   24.83712 32.52408 1.000 27.74784  ? 188 LEU   A CD1 1 
ATOM   1330 C  CD2 . LEU   A 1 181 ? 1.94885   24.62344 30.93744 1.000 20.84879  ? 188 LEU   A CD2 1 
ATOM   1331 N  N   . HIS   A 1 182 ? 2.30815   19.50651 30.78121 1.000 29.57228  ? 189 HIS   A N   1 
ATOM   1332 C  CA  . HIS   A 1 182 ? 2.56646   18.18692 31.34864 1.000 32.73363  ? 189 HIS   A CA  1 
ATOM   1333 C  C   . HIS   A 1 182 ? 3.06430   18.38292 32.77425 1.000 33.47521  ? 189 HIS   A C   1 
ATOM   1334 O  O   . HIS   A 1 182 ? 4.22963   18.71109 33.00628 1.000 33.89733  ? 189 HIS   A O   1 
ATOM   1335 C  CB  . HIS   A 1 182 ? 3.56609   17.42356 30.49018 1.000 34.71440  ? 189 HIS   A CB  1 
ATOM   1336 C  CG  . HIS   A 1 182 ? 3.19047   17.36923 29.04239 1.000 34.10320  ? 189 HIS   A CG  1 
ATOM   1337 N  ND1 . HIS   A 1 182 ? 2.59913   16.26505 28.46693 1.000 36.29746  ? 189 HIS   A ND1 1 
ATOM   1338 C  CD2 . HIS   A 1 182 ? 3.31219   18.28778 28.05523 1.000 31.87628  ? 189 HIS   A CD2 1 
ATOM   1339 C  CE1 . HIS   A 1 182 ? 2.37845   16.50366 27.18636 1.000 35.52930  ? 189 HIS   A CE1 1 
ATOM   1340 N  NE2 . HIS   A 1 182 ? 2.80306   17.72367 26.91091 1.000 32.81409  ? 189 HIS   A NE2 1 
ATOM   1341 N  N   . LEU   A 1 183 ? 2.16679   18.18634 33.73338 1.000 39.38985  ? 190 LEU   A N   1 
ATOM   1342 C  CA  . LEU   A 1 183 ? 2.39483   18.58640 35.11243 1.000 34.41664  ? 190 LEU   A CA  1 
ATOM   1343 C  C   . LEU   A 1 183 ? 3.36132   17.64599 35.82079 1.000 48.86759  ? 190 LEU   A C   1 
ATOM   1344 O  O   . LEU   A 1 183 ? 3.51233   16.47573 35.45502 1.000 54.13777  ? 190 LEU   A O   1 
ATOM   1345 C  CB  . LEU   A 1 183 ? 1.06486   18.62934 35.86649 1.000 34.16813  ? 190 LEU   A CB  1 
ATOM   1346 C  CG  . LEU   A 1 183 ? 0.07733   19.72852 35.46407 1.000 50.73438  ? 190 LEU   A CG  1 
ATOM   1347 C  CD1 . LEU   A 1 183 ? -0.75555  20.15837 36.65450 1.000 48.65614  ? 190 LEU   A CD1 1 
ATOM   1348 C  CD2 . LEU   A 1 183 ? 0.82041   20.93108 34.89647 1.000 34.33603  ? 190 LEU   A CD2 1 
ATOM   1349 N  N   . LYS   A 1 184 ? 4.02516   18.18033 36.84316 1.000 48.82281  ? 191 LYS   A N   1 
ATOM   1350 C  CA  . LYS   A 1 184 ? 4.83300   17.36170 37.73059 1.000 42.85299  ? 191 LYS   A CA  1 
ATOM   1351 C  C   . LYS   A 1 184 ? 3.93296   16.47603 38.58834 1.000 46.31949  ? 191 LYS   A C   1 
ATOM   1352 O  O   . LYS   A 1 184 ? 2.74521   16.75204 38.78151 1.000 53.15366  ? 191 LYS   A O   1 
ATOM   1353 C  CB  . LYS   A 1 184 ? 5.70885   18.24117 38.62345 1.000 42.75620  ? 191 LYS   A CB  1 
ATOM   1354 C  CG  . LYS   A 1 184 ? 6.65138   19.16726 37.86883 1.000 41.10157  ? 191 LYS   A CG  1 
ATOM   1355 C  CD  . LYS   A 1 184 ? 7.28858   20.16966 38.81754 1.000 41.50274  ? 191 LYS   A CD  1 
ATOM   1356 C  CE  . LYS   A 1 184 ? 8.26047   21.08979 38.10208 1.000 40.22208  ? 191 LYS   A CE  1 
ATOM   1357 N  NZ  . LYS   A 1 184 ? 8.81702   22.11938 39.02728 1.000 40.83621  ? 191 LYS   A NZ  1 
ATOM   1358 N  N   . GLU   A 1 185 ? 4.51455   15.39131 39.10494 1.000 48.25697  ? 192 GLU   A N   1 
ATOM   1359 C  CA  . GLU   A 1 185 ? 3.74620   14.48849 39.95543 1.000 50.66752  ? 192 GLU   A CA  1 
ATOM   1360 C  C   . GLU   A 1 185 ? 3.26791   15.18332 41.22482 1.000 52.02214  ? 192 GLU   A C   1 
ATOM   1361 O  O   . GLU   A 1 185 ? 2.20846   14.83717 41.76034 1.000 58.19101  ? 192 GLU   A O   1 
ATOM   1362 C  CB  . GLU   A 1 185 ? 4.57837   13.25155 40.30083 1.000 60.86297  ? 192 GLU   A CB  1 
ATOM   1363 C  CG  . GLU   A 1 185 ? 5.64889   13.48460 41.35569 1.000 58.13664  ? 192 GLU   A CG  1 
ATOM   1364 C  CD  . GLU   A 1 185 ? 5.82760   12.29525 42.27409 1.000 71.39775  ? 192 GLU   A CD  1 
ATOM   1365 O  OE1 . GLU   A 1 185 ? 5.95622   11.16293 41.76413 1.000 86.90362  ? 192 GLU   A OE1 1 
ATOM   1366 O  OE2 . GLU   A 1 185 ? 5.83591   12.49274 43.50737 1.000 86.45298  ? 192 GLU   A OE2 1 
ATOM   1367 N  N   . ASP   A 1 186 ? 4.02008   16.16824 41.71001 1.000 50.52884  ? 193 ASP   A N   1 
ATOM   1368 C  CA  . ASP   A 1 186 ? 3.67805   16.90372 42.91810 1.000 54.06884  ? 193 ASP   A CA  1 
ATOM   1369 C  C   . ASP   A 1 186 ? 2.79434   18.11249 42.63898 1.000 45.77004  ? 193 ASP   A C   1 
ATOM   1370 O  O   . ASP   A 1 186 ? 2.55072   18.90987 43.55045 1.000 52.81017  ? 193 ASP   A O   1 
ATOM   1371 C  CB  . ASP   A 1 186 ? 4.95649   17.34851 43.63832 1.000 52.03110  ? 193 ASP   A CB  1 
ATOM   1372 C  CG  . ASP   A 1 186 ? 4.86361   17.19586 45.14544 1.000 75.92213  ? 193 ASP   A CG  1 
ATOM   1373 O  OD1 . ASP   A 1 186 ? 5.23468   18.14765 45.86491 1.000 81.52776  ? 193 ASP   A OD1 1 
ATOM   1374 O  OD2 . ASP   A 1 186 ? 4.42128   16.12487 45.61164 1.000 84.77070  ? 193 ASP   A OD2 1 
ATOM   1375 N  N   . GLN   A 1 187 ? 2.30578   18.26401 41.40612 1.000 42.88396  ? 194 GLN   A N   1 
ATOM   1376 C  CA  . GLN   A 1 187 ? 1.54642   19.44411 41.00807 1.000 42.70312  ? 194 GLN   A CA  1 
ATOM   1377 C  C   . GLN   A 1 187 ? 0.15003   19.09555 40.50185 1.000 43.94868  ? 194 GLN   A C   1 
ATOM   1378 O  O   . GLN   A 1 187 ? -0.45527  19.88790 39.77367 1.000 47.34598  ? 194 GLN   A O   1 
ATOM   1379 C  CB  . GLN   A 1 187 ? 2.31370   20.23054 39.94266 1.000 42.25628  ? 194 GLN   A CB  1 
ATOM   1380 C  CG  . GLN   A 1 187 ? 3.67804   20.72457 40.39996 1.000 38.20995  ? 194 GLN   A CG  1 
ATOM   1381 C  CD  . GLN   A 1 187 ? 3.59776   21.62978 41.61447 1.000 38.66962  ? 194 GLN   A CD  1 
ATOM   1382 O  OE1 . GLN   A 1 187 ? 4.34408   21.46255 42.57896 1.000 41.56770  ? 194 GLN   A OE1 1 
ATOM   1383 N  NE2 . GLN   A 1 187 ? 2.69631   22.60296 41.56809 1.000 36.21038  ? 194 GLN   A NE2 1 
ATOM   1384 N  N   . THR   A 1 188 ? -0.38218  17.93303 40.88000 1.000 40.59221  ? 195 THR   A N   1 
ATOM   1385 C  CA  . THR   A 1 188 ? -1.68381  17.50320 40.37941 1.000 52.48429  ? 195 THR   A CA  1 
ATOM   1386 C  C   . THR   A 1 188 ? -2.85045  18.26779 40.99501 1.000 47.29968  ? 195 THR   A C   1 
ATOM   1387 O  O   . THR   A 1 188 ? -3.99609  18.02640 40.59835 1.000 38.90987  ? 195 THR   A O   1 
ATOM   1388 C  CB  . THR   A 1 188 ? -1.86932  16.00480 40.62236 1.000 47.41391  ? 195 THR   A CB  1 
ATOM   1389 O  OG1 . THR   A 1 188 ? -1.91850  15.74988 42.03171 1.000 53.61000  ? 195 THR   A OG1 1 
ATOM   1390 C  CG2 . THR   A 1 188 ? -0.71805  15.22803 40.01527 1.000 44.88230  ? 195 THR   A CG2 1 
ATOM   1391 N  N   . GLU   A 1 189 ? -2.60165  19.17178 41.94564 1.000 48.54575  ? 196 GLU   A N   1 
ATOM   1392 C  CA  . GLU   A 1 189 ? -3.68755  19.95855 42.51631 1.000 38.31436  ? 196 GLU   A CA  1 
ATOM   1393 C  C   . GLU   A 1 189 ? -4.29547  20.91776 41.50377 1.000 40.76706  ? 196 GLU   A C   1 
ATOM   1394 O  O   . GLU   A 1 189 ? -5.45337  21.31641 41.66409 1.000 45.65787  ? 196 GLU   A O   1 
ATOM   1395 C  CB  . GLU   A 1 189 ? -3.19558  20.73720 43.73777 1.000 47.44825  ? 196 GLU   A CB  1 
ATOM   1396 C  CG  . GLU   A 1 189 ? -2.48875  22.04262 43.40594 1.000 36.99157  ? 196 GLU   A CG  1 
ATOM   1397 C  CD  . GLU   A 1 189 ? -1.76607  22.63558 44.59900 1.000 41.61752  ? 196 GLU   A CD  1 
ATOM   1398 O  OE1 . GLU   A 1 189 ? -0.86614  21.96297 45.14751 1.000 41.06934  ? 196 GLU   A OE1 1 
ATOM   1399 O  OE2 . GLU   A 1 189 ? -2.09822  23.77507 44.98771 1.000 37.90061  ? 196 GLU   A OE2 1 
ATOM   1400 N  N   . TYR   A 1 190 ? -3.55163  21.28808 40.46541 1.000 33.48388  ? 197 TYR   A N   1 
ATOM   1401 C  CA  . TYR   A 1 190 ? -4.04919  22.21204 39.45712 1.000 32.42136  ? 197 TYR   A CA  1 
ATOM   1402 C  C   . TYR   A 1 190 ? -4.87513  21.51827 38.38242 1.000 30.93978  ? 197 TYR   A C   1 
ATOM   1403 O  O   . TYR   A 1 190 ? -5.26121  22.15907 37.40002 1.000 31.08553  ? 197 TYR   A O   1 
ATOM   1404 C  CB  . TYR   A 1 190 ? -2.87773  22.98250 38.84386 1.000 41.76460  ? 197 TYR   A CB  1 
ATOM   1405 C  CG  . TYR   A 1 190 ? -2.08561  23.72365 39.89635 1.000 38.55055  ? 197 TYR   A CG  1 
ATOM   1406 C  CD1 . TYR   A 1 190 ? -2.56333  24.90581 40.44333 1.000 29.06119  ? 197 TYR   A CD1 1 
ATOM   1407 C  CD2 . TYR   A 1 190 ? -0.87880  23.22198 40.36990 1.000 38.41222  ? 197 TYR   A CD2 1 
ATOM   1408 C  CE1 . TYR   A 1 190 ? -1.85550  25.57888 41.41666 1.000 29.92901  ? 197 TYR   A CE1 1 
ATOM   1409 C  CE2 . TYR   A 1 190 ? -0.16337  23.88912 41.34555 1.000 37.94984  ? 197 TYR   A CE2 1 
ATOM   1410 C  CZ  . TYR   A 1 190 ? -0.65747  25.06710 41.86518 1.000 39.43394  ? 197 TYR   A CZ  1 
ATOM   1411 O  OH  . TYR   A 1 190 ? 0.04853   25.73766 42.83609 1.000 46.57562  ? 197 TYR   A OH  1 
ATOM   1412 N  N   . LEU   A 1 191 ? -5.15397  20.22769 38.55000 1.000 33.08870  ? 198 LEU   A N   1 
ATOM   1413 C  CA  . LEU   A 1 191 ? -6.17008  19.54619 37.76524 1.000 33.81670  ? 198 LEU   A CA  1 
ATOM   1414 C  C   . LEU   A 1 191 ? -7.50140  19.45834 38.49725 1.000 35.29605  ? 198 LEU   A C   1 
ATOM   1415 O  O   . LEU   A 1 191 ? -8.49403  19.03344 37.89859 1.000 36.17429  ? 198 LEU   A O   1 
ATOM   1416 C  CB  . LEU   A 1 191 ? -5.69804  18.13789 37.38542 1.000 35.71967  ? 198 LEU   A CB  1 
ATOM   1417 C  CG  . LEU   A 1 191 ? -4.35806  18.03908 36.65181 1.000 40.02783  ? 198 LEU   A CG  1 
ATOM   1418 C  CD1 . LEU   A 1 191 ? -4.00301  16.58232 36.39070 1.000 42.89952  ? 198 LEU   A CD1 1 
ATOM   1419 C  CD2 . LEU   A 1 191 ? -4.36947  18.83746 35.35177 1.000 32.57242  ? 198 LEU   A CD2 1 
ATOM   1420 N  N   . GLU   A 1 192 ? -7.54236  19.85078 39.76764 1.000 35.91894  ? 199 GLU   A N   1 
ATOM   1421 C  CA  . GLU   A 1 192 ? -8.77762  19.85659 40.53336 1.000 37.50653  ? 199 GLU   A CA  1 
ATOM   1422 C  C   . GLU   A 1 192 ? -9.62090  21.07736 40.18100 1.000 42.71351  ? 199 GLU   A C   1 
ATOM   1423 O  O   . GLU   A 1 192 ? -9.10150  22.16331 39.90495 1.000 34.55397  ? 199 GLU   A O   1 
ATOM   1424 C  CB  . GLU   A 1 192 ? -8.47772  19.83808 42.03287 1.000 39.04035  ? 199 GLU   A CB  1 
ATOM   1425 C  CG  . GLU   A 1 192 ? -9.37688  18.91317 42.83869 1.000 49.34704  ? 199 GLU   A CG  1 
ATOM   1426 C  CD  . GLU   A 1 192 ? -9.67827  17.61130 42.11898 1.000 53.47094  ? 199 GLU   A CD  1 
ATOM   1427 O  OE1 . GLU   A 1 192 ? -8.76486  16.76672 42.00598 1.000 44.11011  ? 199 GLU   A OE1 1 
ATOM   1428 O  OE2 . GLU   A 1 192 ? -10.82964 17.43410 41.66425 1.000 55.96980  ? 199 GLU   A OE2 1 
ATOM   1429 N  N   . GLU   A 1 193 ? -10.94225 20.88578 40.20259 1.000 40.60660  ? 200 GLU   A N   1 
ATOM   1430 C  CA  . GLU   A 1 193 ? -11.86036 21.93004 39.75680 1.000 38.41660  ? 200 GLU   A CA  1 
ATOM   1431 C  C   . GLU   A 1 193 ? -11.90845 23.08816 40.74579 1.000 34.27642  ? 200 GLU   A C   1 
ATOM   1432 O  O   . GLU   A 1 193 ? -11.69947 24.24800 40.37016 1.000 32.08930  ? 200 GLU   A O   1 
ATOM   1433 C  CB  . GLU   A 1 193 ? -13.25460 21.33973 39.55176 1.000 34.74554  ? 200 GLU   A CB  1 
ATOM   1434 C  CG  . GLU   A 1 193 ? -14.27446 22.31539 38.99751 1.000 39.64104  ? 200 GLU   A CG  1 
ATOM   1435 C  CD  . GLU   A 1 193 ? -15.66388 21.71676 38.94478 1.000 47.39782  ? 200 GLU   A CD  1 
ATOM   1436 O  OE1 . GLU   A 1 193 ? -15.78145 20.48524 39.12265 1.000 36.63620  ? 200 GLU   A OE1 1 
ATOM   1437 O  OE2 . GLU   A 1 193 ? -16.63551 22.47479 38.73583 1.000 46.85103  ? 200 GLU   A OE2 1 
ATOM   1438 N  N   . ARG   A 1 194 ? -12.19015 22.79216 42.01695 1.000 36.67655  ? 201 ARG   A N   1 
ATOM   1439 C  CA  . ARG   A 1 194 ? -12.26782 23.83905 43.02865 1.000 40.05061  ? 201 ARG   A CA  1 
ATOM   1440 C  C   . ARG   A 1 194 ? -10.93965 24.55984 43.21360 1.000 41.68533  ? 201 ARG   A C   1 
ATOM   1441 O  O   . ARG   A 1 194 ? -10.92938 25.70890 43.66791 1.000 43.38880  ? 201 ARG   A O   1 
ATOM   1442 C  CB  . ARG   A 1 194 ? -12.74062 23.24944 44.36004 1.000 41.58429  ? 201 ARG   A CB  1 
ATOM   1443 C  CG  . ARG   A 1 194 ? -11.77525 22.24595 44.95983 1.000 71.23078  ? 201 ARG   A CG  1 
ATOM   1444 C  CD  . ARG   A 1 194 ? -12.43983 21.35015 45.99403 1.000 77.42325  ? 201 ARG   A CD  1 
ATOM   1445 N  NE  . ARG   A 1 194 ? -11.51203 20.34243 46.49689 1.000 88.12797  ? 201 ARG   A NE  1 
ATOM   1446 C  CZ  . ARG   A 1 194 ? -11.79680 19.46011 47.44562 1.000 83.21455  ? 201 ARG   A CZ  1 
ATOM   1447 N  NH1 . ARG   A 1 194 ? -12.98223 19.43339 48.03343 1.000 64.18871  ? 201 ARG   A NH1 1 
ATOM   1448 N  NH2 . ARG   A 1 194 ? -10.86589 18.58643 47.81891 1.000 77.08952  ? 201 ARG   A NH2 1 
ATOM   1449 N  N   . ARG   A 1 195 ? -9.82193  23.91696 42.86871 1.000 48.04908  ? 202 ARG   A N   1 
ATOM   1450 C  CA  . ARG   A 1 195 ? -8.53187  24.59484 42.92105 1.000 40.98837  ? 202 ARG   A CA  1 
ATOM   1451 C  C   . ARG   A 1 195 ? -8.35218  25.53937 41.73858 1.000 43.78378  ? 202 ARG   A C   1 
ATOM   1452 O  O   . ARG   A 1 195 ? -7.85855  26.65968 41.90660 1.000 40.57781  ? 202 ARG   A O   1 
ATOM   1453 C  CB  . ARG   A 1 195 ? -7.39984  23.56956 42.96251 1.000 41.01660  ? 202 ARG   A CB  1 
ATOM   1454 C  CG  . ARG   A 1 195 ? -6.01849  24.17637 43.15090 1.000 43.19663  ? 202 ARG   A CG  1 
ATOM   1455 C  CD  . ARG   A 1 195 ? -5.89115  24.84961 44.50657 1.000 49.65992  ? 202 ARG   A CD  1 
ATOM   1456 N  NE  . ARG   A 1 195 ? -4.51589  25.24152 44.79132 1.000 60.68448  ? 202 ARG   A NE  1 
ATOM   1457 C  CZ  . ARG   A 1 195 ? -4.10084  26.49687 44.89622 1.000 49.26856  ? 202 ARG   A CZ  1 
ATOM   1458 N  NH1 . ARG   A 1 195 ? -4.93100  27.51463 44.73811 1.000 46.49978  ? 202 ARG   A NH1 1 
ATOM   1459 N  NH2 . ARG   A 1 195 ? -2.82142  26.73694 45.16977 1.000 48.99738  ? 202 ARG   A NH2 1 
ATOM   1460 N  N   . ILE   A 1 196 ? -8.74969  25.10729 40.53974 1.000 36.61959  ? 203 ILE   A N   1 
ATOM   1461 C  CA  . ILE   A 1 196 ? -8.65903  25.97533 39.37024 1.000 31.77613  ? 203 ILE   A CA  1 
ATOM   1462 C  C   . ILE   A 1 196 ? -9.58370  27.17718 39.52022 1.000 42.29324  ? 203 ILE   A C   1 
ATOM   1463 O  O   . ILE   A 1 196 ? -9.20242  28.31217 39.20845 1.000 43.00323  ? 203 ILE   A O   1 
ATOM   1464 C  CB  . ILE   A 1 196 ? -8.96872  25.17972 38.08945 1.000 33.10334  ? 203 ILE   A CB  1 
ATOM   1465 C  CG1 . ILE   A 1 196 ? -7.84985  24.17606 37.79725 1.000 35.20216  ? 203 ILE   A CG1 1 
ATOM   1466 C  CG2 . ILE   A 1 196 ? -9.16568  26.11978 36.90916 1.000 28.15978  ? 203 ILE   A CG2 1 
ATOM   1467 C  CD1 . ILE   A 1 196 ? -8.22478  23.12816 36.76782 1.000 33.76970  ? 203 ILE   A CD1 1 
ATOM   1468 N  N   . LYS   A 1 197 ? -10.80854 26.95278 40.00716 1.000 39.54641  ? 204 LYS   A N   1 
ATOM   1469 C  CA  . LYS   A 1 197 ? -11.76203 28.05016 40.14028 1.000 37.15682  ? 204 LYS   A CA  1 
ATOM   1470 C  C   . LYS   A 1 197 ? -11.29920 29.08575 41.15468 1.000 35.82709  ? 204 LYS   A C   1 
ATOM   1471 O  O   . LYS   A 1 197 ? -11.60029 30.27583 41.00732 1.000 36.96044  ? 204 LYS   A O   1 
ATOM   1472 C  CB  . LYS   A 1 197 ? -13.14165 27.51548 40.53222 1.000 33.03216  ? 204 LYS   A CB  1 
ATOM   1473 C  CG  . LYS   A 1 197 ? -14.03668 27.15149 39.35459 1.000 30.64658  ? 204 LYS   A CG  1 
ATOM   1474 C  CD  . LYS   A 1 197 ? -13.86061 28.12034 38.18782 1.000 52.47643  ? 204 LYS   A CD  1 
ATOM   1475 C  CE  . LYS   A 1 197 ? -14.46301 29.48963 38.47641 1.000 53.89859  ? 204 LYS   A CE  1 
ATOM   1476 N  NZ  . LYS   A 1 197 ? -13.99556 30.49867 37.48844 1.000 39.28954  ? 204 LYS   A NZ  1 
ATOM   1477 N  N   . GLU   A 1 198 ? -10.57179 28.65993 42.18733 1.000 37.69580  ? 205 GLU   A N   1 
ATOM   1478 C  CA  . GLU   A 1 198 ? -10.13125 29.60684 43.20440 1.000 41.29180  ? 205 GLU   A CA  1 
ATOM   1479 C  C   . GLU   A 1 198 ? -9.01592  30.50416 42.68048 1.000 45.82053  ? 205 GLU   A C   1 
ATOM   1480 O  O   . GLU   A 1 198 ? -8.97342  31.69729 43.00096 1.000 46.87370  ? 205 GLU   A O   1 
ATOM   1481 C  CB  . GLU   A 1 198 ? -9.67641  28.86207 44.45634 1.000 43.36854  ? 205 GLU   A CB  1 
ATOM   1482 C  CG  . GLU   A 1 198 ? -9.19952  29.78010 45.56245 1.000 47.74640  ? 205 GLU   A CG  1 
ATOM   1483 C  CD  . GLU   A 1 198 ? -8.16288  29.12870 46.44277 1.000 61.22296  ? 205 GLU   A CD  1 
ATOM   1484 O  OE1 . GLU   A 1 198 ? -7.28694  28.42559 45.89758 1.000 65.89430  ? 205 GLU   A OE1 1 
ATOM   1485 O  OE2 . GLU   A 1 198 ? -8.22810  29.30993 47.67604 1.000 66.89398  ? 205 GLU   A OE2 1 
ATOM   1486 N  N   . ILE   A 1 199 ? -8.10483  29.95250 41.87364 1.000 41.62997  ? 206 ILE   A N   1 
ATOM   1487 C  CA  . ILE   A 1 199 ? -7.02242  30.76302 41.32223 1.000 46.58410  ? 206 ILE   A CA  1 
ATOM   1488 C  C   . ILE   A 1 199 ? -7.56433  31.74248 40.28599 1.000 46.43446  ? 206 ILE   A C   1 
ATOM   1489 O  O   . ILE   A 1 199 ? -7.13637  32.90217 40.22536 1.000 44.87193  ? 206 ILE   A O   1 
ATOM   1490 C  CB  . ILE   A 1 199 ? -5.91682  29.86430 40.73296 1.000 39.85121  ? 206 ILE   A CB  1 
ATOM   1491 C  CG1 . ILE   A 1 199 ? -5.19501  29.09037 41.83551 1.000 41.52508  ? 206 ILE   A CG1 1 
ATOM   1492 C  CG2 . ILE   A 1 199 ? -4.90052  30.69131 39.97109 1.000 41.27651  ? 206 ILE   A CG2 1 
ATOM   1493 C  CD1 . ILE   A 1 199 ? -4.88725  27.65532 41.46496 1.000 39.80068  ? 206 ILE   A CD1 1 
ATOM   1494 N  N   . VAL   A 1 200 ? -8.52037  31.29837 39.46379 1.000 37.55982  ? 207 VAL   A N   1 
ATOM   1495 C  CA  . VAL   A 1 200 ? -9.09372  32.16869 38.43806 1.000 40.27935  ? 207 VAL   A CA  1 
ATOM   1496 C  C   . VAL   A 1 200 ? -9.84948  33.32847 39.07750 1.000 49.80006  ? 207 VAL   A C   1 
ATOM   1497 O  O   . VAL   A 1 200 ? -9.74021  34.48008 38.63769 1.000 46.71754  ? 207 VAL   A O   1 
ATOM   1498 C  CB  . VAL   A 1 200 ? -9.99699  31.35415 37.49304 1.000 33.79057  ? 207 VAL   A CB  1 
ATOM   1499 C  CG1 . VAL   A 1 200 ? -10.79670 32.27704 36.59290 1.000 34.58929  ? 207 VAL   A CG1 1 
ATOM   1500 C  CG2 . VAL   A 1 200 ? -9.16282  30.40001 36.66328 1.000 31.92619  ? 207 VAL   A CG2 1 
ATOM   1501 N  N   . LYS   A 1 201 ? -10.62727 33.04549 40.12422 1.000 46.75057  ? 208 LYS   A N   1 
ATOM   1502 C  CA  . LYS   A 1 201 ? -11.33374 34.10836 40.83077 1.000 46.11872  ? 208 LYS   A CA  1 
ATOM   1503 C  C   . LYS   A 1 201 ? -10.37043 35.02046 41.58398 1.000 51.51944  ? 208 LYS   A C   1 
ATOM   1504 O  O   . LYS   A 1 201 ? -10.60665 36.23109 41.67604 1.000 52.33729  ? 208 LYS   A O   1 
ATOM   1505 C  CB  . LYS   A 1 201 ? -12.36143 33.49543 41.78495 1.000 47.21569  ? 208 LYS   A CB  1 
ATOM   1506 C  CG  . LYS   A 1 201 ? -12.85798 34.42631 42.87810 1.000 48.95699  ? 208 LYS   A CG  1 
ATOM   1507 C  CD  . LYS   A 1 201 ? -14.32368 34.18180 43.18598 1.000 49.27808  ? 208 LYS   A CD  1 
ATOM   1508 C  CE  . LYS   A 1 201 ? -15.17767 34.30185 41.93664 1.000 46.83521  ? 208 LYS   A CE  1 
ATOM   1509 N  NZ  . LYS   A 1 201 ? -15.03235 35.64020 41.29893 1.000 57.32181  ? 208 LYS   A NZ  1 
ATOM   1510 N  N   . LYS   A 1 202 ? -9.27659  34.46591 42.11213 1.000 59.29973  ? 209 LYS   A N   1 
ATOM   1511 C  CA  . LYS   A 1 202 ? -8.33531  35.26862 42.88807 1.000 52.92392  ? 209 LYS   A CA  1 
ATOM   1512 C  C   . LYS   A 1 202 ? -7.49016  36.16563 41.99341 1.000 54.53132  ? 209 LYS   A C   1 
ATOM   1513 O  O   . LYS   A 1 202 ? -7.29552  37.34840 42.29657 1.000 65.24409  ? 209 LYS   A O   1 
ATOM   1514 C  CB  . LYS   A 1 202 ? -7.43364  34.35754 43.72013 1.000 52.93819  ? 209 LYS   A CB  1 
ATOM   1515 C  CG  . LYS   A 1 202 ? -6.44157  35.09150 44.60518 1.000 57.75622  ? 209 LYS   A CG  1 
ATOM   1516 C  CD  . LYS   A 1 202 ? -5.66279  34.11491 45.47437 1.000 57.92947  ? 209 LYS   A CD  1 
ATOM   1517 C  CE  . LYS   A 1 202 ? -4.76830  34.83880 46.46878 1.000 63.21102  ? 209 LYS   A CE  1 
ATOM   1518 N  NZ  . LYS   A 1 202 ? -4.36631  33.95035 47.59445 1.000 64.22389  ? 209 LYS   A NZ  1 
ATOM   1519 N  N   . HIS   A 1 203 ? -6.98582  35.62551 40.88633 1.000 53.07650  ? 210 HIS   A N   1 
ATOM   1520 C  CA  . HIS   A 1 203 ? -5.97041  36.29730 40.08833 1.000 53.51447  ? 210 HIS   A CA  1 
ATOM   1521 C  C   . HIS   A 1 203 ? -6.48204  36.89134 38.78499 1.000 60.75070  ? 210 HIS   A C   1 
ATOM   1522 O  O   . HIS   A 1 203 ? -5.97421  37.93114 38.35950 1.000 68.70785  ? 210 HIS   A O   1 
ATOM   1523 C  CB  . HIS   A 1 203 ? -4.83085  35.32333 39.76774 1.000 52.59914  ? 210 HIS   A CB  1 
ATOM   1524 C  CG  . HIS   A 1 203 ? -3.97537  34.98176 40.94753 1.000 55.42554  ? 210 HIS   A CG  1 
ATOM   1525 N  ND1 . HIS   A 1 203 ? -3.38291  35.94074 41.74063 1.000 66.64321  ? 210 HIS   A ND1 1 
ATOM   1526 C  CD2 . HIS   A 1 203 ? -3.60876  33.78597 41.46636 1.000 57.10977  ? 210 HIS   A CD2 1 
ATOM   1527 C  CE1 . HIS   A 1 203 ? -2.69016  35.35062 42.69844 1.000 63.65529  ? 210 HIS   A CE1 1 
ATOM   1528 N  NE2 . HIS   A 1 203 ? -2.81002  34.04324 42.55421 1.000 57.87946  ? 210 HIS   A NE2 1 
ATOM   1529 N  N   . SER   A 1 204 ? -7.46264  36.26783 38.13836 1.000 49.34238  ? 211 SER   A N   1 
ATOM   1530 C  CA  . SER   A 1 204 ? -7.90266  36.68448 36.81169 1.000 57.14323  ? 211 SER   A CA  1 
ATOM   1531 C  C   . SER   A 1 204 ? -9.40349  36.93355 36.78427 1.000 54.60330  ? 211 SER   A C   1 
ATOM   1532 O  O   . SER   A 1 204 ? -10.10555 36.51044 35.86161 1.000 53.75575  ? 211 SER   A O   1 
ATOM   1533 C  CB  . SER   A 1 204 ? -7.50985  35.64852 35.76082 1.000 54.76158  ? 211 SER   A CB  1 
ATOM   1534 O  OG  . SER   A 1 204 ? -6.10259  35.59082 35.60155 1.000 46.43163  ? 211 SER   A OG  1 
ATOM   1535 N  N   . GLN   A 1 205 ? -9.92172  37.63366 37.79334 1.000 58.49644  ? 212 GLN   A N   1 
ATOM   1536 C  CA  . GLN   A 1 205 ? -11.34685 37.93443 37.83302 1.000 50.48441  ? 212 GLN   A CA  1 
ATOM   1537 C  C   . GLN   A 1 205 ? -11.72638 39.10884 36.93973 1.000 45.61422  ? 212 GLN   A C   1 
ATOM   1538 O  O   . GLN   A 1 205 ? -12.90638 39.26003 36.60739 1.000 52.61703  ? 212 GLN   A O   1 
ATOM   1539 C  CB  . GLN   A 1 205 ? -11.78462 38.21958 39.27144 1.000 49.37619  ? 212 GLN   A CB  1 
ATOM   1540 C  CG  . GLN   A 1 205 ? -11.68576 39.68018 39.66336 1.000 50.36245  ? 212 GLN   A CG  1 
ATOM   1541 C  CD  . GLN   A 1 205 ? -11.46433 39.87759 41.14813 1.000 77.87900  ? 212 GLN   A CD  1 
ATOM   1542 O  OE1 . GLN   A 1 205 ? -10.33089 40.04022 41.60217 1.000 79.44370  ? 212 GLN   A OE1 1 
ATOM   1543 N  NE2 . GLN   A 1 205 ? -12.54914 39.86800 41.91474 1.000 89.66490  ? 212 GLN   A NE2 1 
ATOM   1544 N  N   . PHE   A 1 206 ? -10.76082 39.93386 36.53585 1.000 57.42164  ? 213 PHE   A N   1 
ATOM   1545 C  CA  . PHE   A 1 206 ? -11.02556 41.13021 35.74583 1.000 54.20953  ? 213 PHE   A CA  1 
ATOM   1546 C  C   . PHE   A 1 206 ? -10.52947 40.99191 34.30908 1.000 45.59266  ? 213 PHE   A C   1 
ATOM   1547 O  O   . PHE   A 1 206 ? -10.10511 41.97255 33.69297 1.000 49.65680  ? 213 PHE   A O   1 
ATOM   1548 C  CB  . PHE   A 1 206 ? -10.40083 42.35162 36.41624 1.000 58.71038  ? 213 PHE   A CB  1 
ATOM   1549 C  CG  . PHE   A 1 206 ? -10.96393 42.64291 37.77652 1.000 63.48925  ? 213 PHE   A CG  1 
ATOM   1550 C  CD1 . PHE   A 1 206 ? -12.33503 42.68465 37.97770 1.000 52.47971  ? 213 PHE   A CD1 1 
ATOM   1551 C  CD2 . PHE   A 1 206 ? -10.12534 42.85748 38.85748 1.000 60.16934  ? 213 PHE   A CD2 1 
ATOM   1552 C  CE1 . PHE   A 1 206 ? -12.85881 42.94822 39.22892 1.000 54.83379  ? 213 PHE   A CE1 1 
ATOM   1553 C  CE2 . PHE   A 1 206 ? -10.64366 43.11712 40.11190 1.000 58.38523  ? 213 PHE   A CE2 1 
ATOM   1554 C  CZ  . PHE   A 1 206 ? -12.01147 43.16594 40.29771 1.000 66.20100  ? 213 PHE   A CZ  1 
ATOM   1555 N  N   . ILE   A 1 207 ? -10.58082 39.78095 33.76745 1.000 46.26504  ? 214 ILE   A N   1 
ATOM   1556 C  CA  . ILE   A 1 207 ? -10.19377 39.52128 32.38674 1.000 44.02127  ? 214 ILE   A CA  1 
ATOM   1557 C  C   . ILE   A 1 207 ? -11.40531 39.75719 31.49454 1.000 41.74316  ? 214 ILE   A C   1 
ATOM   1558 O  O   . ILE   A 1 207 ? -12.50036 39.25350 31.77191 1.000 60.07617  ? 214 ILE   A O   1 
ATOM   1559 C  CB  . ILE   A 1 207 ? -9.65489  38.08900 32.23181 1.000 40.28464  ? 214 ILE   A CB  1 
ATOM   1560 C  CG1 . ILE   A 1 207 ? -8.30498  37.95013 32.94603 1.000 41.16513  ? 214 ILE   A CG1 1 
ATOM   1561 C  CG2 . ILE   A 1 207 ? -9.55890  37.69813 30.76113 1.000 39.07224  ? 214 ILE   A CG2 1 
ATOM   1562 C  CD1 . ILE   A 1 207 ? -7.11590  38.43929 32.14403 1.000 41.94575  ? 214 ILE   A CD1 1 
ATOM   1563 N  N   . GLY   A 1 208 ? -11.21370 40.52328 30.42394 1.000 42.32152  ? 215 GLY   A N   1 
ATOM   1564 C  CA  . GLY   A 1 208 ? -12.31441 40.90169 29.55882 1.000 42.67579  ? 215 GLY   A CA  1 
ATOM   1565 C  C   . GLY   A 1 208 ? -12.72947 39.85267 28.54697 1.000 41.02080  ? 215 GLY   A C   1 
ATOM   1566 O  O   . GLY   A 1 208 ? -13.35797 40.17809 27.53563 1.000 41.57059  ? 215 GLY   A O   1 
ATOM   1567 N  N   . TYR   A 1 209 ? -12.38858 38.59454 28.80233 1.000 39.33371  ? 216 TYR   A N   1 
ATOM   1568 C  CA  . TYR   A 1 209 ? -12.78060 37.48697 27.94754 1.000 37.98217  ? 216 TYR   A CA  1 
ATOM   1569 C  C   . TYR   A 1 209 ? -13.29438 36.33704 28.79971 1.000 36.99684  ? 216 TYR   A C   1 
ATOM   1570 O  O   . TYR   A 1 209 ? -12.80775 36.11946 29.91417 1.000 36.92210  ? 216 TYR   A O   1 
ATOM   1571 C  CB  . TYR   A 1 209 ? -11.60610 37.00870 27.08165 1.000 39.56224  ? 216 TYR   A CB  1 
ATOM   1572 C  CG  . TYR   A 1 209 ? -11.08649 38.07364 26.14686 1.000 42.49529  ? 216 TYR   A CG  1 
ATOM   1573 C  CD1 . TYR   A 1 209 ? -11.66040 38.26860 24.89672 1.000 39.03761  ? 216 TYR   A CD1 1 
ATOM   1574 C  CD2 . TYR   A 1 209 ? -10.02994 38.89299 26.52039 1.000 39.60216  ? 216 TYR   A CD2 1 
ATOM   1575 C  CE1 . TYR   A 1 209 ? -11.19204 39.24552 24.04259 1.000 40.51886  ? 216 TYR   A CE1 1 
ATOM   1576 C  CE2 . TYR   A 1 209 ? -9.55444  39.87133 25.67507 1.000 41.09082  ? 216 TYR   A CE2 1 
ATOM   1577 C  CZ  . TYR   A 1 209 ? -10.13899 40.04622 24.43772 1.000 43.23814  ? 216 TYR   A CZ  1 
ATOM   1578 O  OH  . TYR   A 1 209 ? -9.66279  41.02368 23.59305 1.000 43.31238  ? 216 TYR   A OH  1 
ATOM   1579 N  N   . PRO   A 1 210 ? -14.27988 35.58772 28.30273 1.000 44.27209  ? 217 PRO   A N   1 
ATOM   1580 C  CA  . PRO   A 1 210 ? -14.86164 34.50516 29.11026 1.000 36.03541  ? 217 PRO   A CA  1 
ATOM   1581 C  C   . PRO   A 1 210 ? -13.87981 33.35400 29.28003 1.000 34.72150  ? 217 PRO   A C   1 
ATOM   1582 O  O   . PRO   A 1 210 ? -13.35593 32.81461 28.30312 1.000 34.02717  ? 217 PRO   A O   1 
ATOM   1583 C  CB  . PRO   A 1 210 ? -16.09594 34.08065 28.30559 1.000 36.38555  ? 217 PRO   A CB  1 
ATOM   1584 C  CG  . PRO   A 1 210 ? -15.82039 34.51165 26.90977 1.000 36.52455  ? 217 PRO   A CG  1 
ATOM   1585 C  CD  . PRO   A 1 210 ? -14.89799 35.69312 26.96877 1.000 36.97501  ? 217 PRO   A CD  1 
ATOM   1586 N  N   . ILE   A 1 211 ? -13.63236 32.98366 30.53184 1.000 34.75040  ? 218 ILE   A N   1 
ATOM   1587 C  CA  . ILE   A 1 211 ? -12.74409 31.87713 30.86578 1.000 33.98902  ? 218 ILE   A CA  1 
ATOM   1588 C  C   . ILE   A 1 211 ? -13.62755 30.69886 31.25878 1.000 34.24218  ? 218 ILE   A C   1 
ATOM   1589 O  O   . ILE   A 1 211 ? -14.12479 30.62450 32.38608 1.000 39.11707  ? 218 ILE   A O   1 
ATOM   1590 C  CB  . ILE   A 1 211 ? -11.75680 32.24683 31.97666 1.000 35.10012  ? 218 ILE   A CB  1 
ATOM   1591 C  CG1 . ILE   A 1 211 ? -10.99384 33.52397 31.61628 1.000 35.32933  ? 218 ILE   A CG1 1 
ATOM   1592 C  CG2 . ILE   A 1 211 ? -10.78393 31.09896 32.22823 1.000 34.29615  ? 218 ILE   A CG2 1 
ATOM   1593 C  CD1 . ILE   A 1 211 ? -10.32815 34.19378 32.80052 1.000 36.65265  ? 218 ILE   A CD1 1 
ATOM   1594 N  N   . THR   A 1 212 ? -13.82628 29.77323 30.32450 1.000 33.13537  ? 219 THR   A N   1 
ATOM   1595 C  CA  . THR   A 1 212 ? -14.63056 28.58516 30.56963 1.000 33.21421  ? 219 THR   A CA  1 
ATOM   1596 C  C   . THR   A 1 212 ? -13.75803 27.48540 31.15480 1.000 32.95161  ? 219 THR   A C   1 
ATOM   1597 O  O   . THR   A 1 212 ? -12.70791 27.15684 30.59541 1.000 32.49514  ? 219 THR   A O   1 
ATOM   1598 C  CB  . THR   A 1 212 ? -15.28479 28.09427 29.27870 1.000 33.10641  ? 219 THR   A CB  1 
ATOM   1599 O  OG1 . THR   A 1 212 ? -15.99201 29.17322 28.65704 1.000 41.61152  ? 219 THR   A OG1 1 
ATOM   1600 C  CG2 . THR   A 1 212 ? -16.24967 26.96361 29.57457 1.000 33.66632  ? 219 THR   A CG2 1 
ATOM   1601 N  N   . LEU   A 1 213 ? -14.19694 26.91455 32.27405 1.000 42.36495  ? 220 LEU   A N   1 
ATOM   1602 C  CA  . LEU   A 1 213 ? -13.50904 25.79195 32.90316 1.000 33.81431  ? 220 LEU   A CA  1 
ATOM   1603 C  C   . LEU   A 1 213 ? -14.21049 24.50218 32.49214 1.000 33.96007  ? 220 LEU   A C   1 
ATOM   1604 O  O   . LEU   A 1 213 ? -15.34462 24.24437 32.90724 1.000 41.11822  ? 220 LEU   A O   1 
ATOM   1605 C  CB  . LEU   A 1 213 ? -13.48236 25.93964 34.42250 1.000 34.90778  ? 220 LEU   A CB  1 
ATOM   1606 C  CG  . LEU   A 1 213 ? -12.97052 24.70269 35.16504 1.000 42.79853  ? 220 LEU   A CG  1 
ATOM   1607 C  CD1 . LEU   A 1 213 ? -11.54372 24.38456 34.74816 1.000 36.95366  ? 220 LEU   A CD1 1 
ATOM   1608 C  CD2 . LEU   A 1 213 ? -13.06139 24.88516 36.66998 1.000 40.17942  ? 220 LEU   A CD2 1 
ATOM   1609 N  N   . PHE   A 1 214 ? -13.53620 23.69622 31.67712 1.000 38.01855  ? 221 PHE   A N   1 
ATOM   1610 C  CA  . PHE   A 1 214 ? -14.09416 22.41743 31.26051 1.000 38.31575  ? 221 PHE   A CA  1 
ATOM   1611 C  C   . PHE   A 1 214 ? -14.02639 21.42626 32.41574 1.000 39.37152  ? 221 PHE   A C   1 
ATOM   1612 O  O   . PHE   A 1 214 ? -12.99680 21.31046 33.08745 1.000 42.83858  ? 221 PHE   A O   1 
ATOM   1613 C  CB  . PHE   A 1 214 ? -13.33844 21.86986 30.04869 1.000 38.74806  ? 221 PHE   A CB  1 
ATOM   1614 C  CG  . PHE   A 1 214 ? -13.73287 22.50279 28.73711 1.000 46.68855  ? 221 PHE   A CG  1 
ATOM   1615 C  CD1 . PHE   A 1 214 ? -14.18799 23.81084 28.68105 1.000 48.25442  ? 221 PHE   A CD1 1 
ATOM   1616 C  CD2 . PHE   A 1 214 ? -13.64337 21.78302 27.55634 1.000 49.84512  ? 221 PHE   A CD2 1 
ATOM   1617 C  CE1 . PHE   A 1 214 ? -14.54477 24.38799 27.47176 1.000 46.27913  ? 221 PHE   A CE1 1 
ATOM   1618 C  CE2 . PHE   A 1 214 ? -13.99961 22.35325 26.34542 1.000 45.03299  ? 221 PHE   A CE2 1 
ATOM   1619 C  CZ  . PHE   A 1 214 ? -14.45083 23.65720 26.30372 1.000 41.21535  ? 221 PHE   A CZ  1 
ATOM   1620 N  N   . VAL   A 1 215 ? -15.12643 20.71365 32.64782 1.000 35.99044  ? 222 VAL   A N   1 
ATOM   1621 C  CA  . VAL   A 1 215 ? -15.22937 19.73890 33.72827 1.000 40.60556  ? 222 VAL   A CA  1 
ATOM   1622 C  C   . VAL   A 1 215 ? -15.05724 18.34190 33.14902 1.000 38.01705  ? 222 VAL   A C   1 
ATOM   1623 O  O   . VAL   A 1 215 ? -15.53894 18.04618 32.04719 1.000 37.88622  ? 222 VAL   A O   1 
ATOM   1624 C  CB  . VAL   A 1 215 ? -16.57322 19.87883 34.47120 1.000 41.72049  ? 222 VAL   A CB  1 
ATOM   1625 C  CG1 . VAL   A 1 215 ? -16.65738 18.89916 35.63120 1.000 40.36027  ? 222 VAL   A CG1 1 
ATOM   1626 C  CG2 . VAL   A 1 215 ? -16.75480 21.30478 34.96547 1.000 38.26432  ? 222 VAL   A CG2 1 
ATOM   1627 N  N   . GLU   A 1 216 ? -14.35177 17.48619 33.88289 1.000 39.04426  ? 223 GLU   A N   1 
ATOM   1628 C  CA  . GLU   A 1 216 ? -14.12910 16.11567 33.45150 1.000 42.46542  ? 223 GLU   A CA  1 
ATOM   1629 C  C   . GLU   A 1 216 ? -15.33209 15.24352 33.79237 1.000 41.74347  ? 223 GLU   A C   1 
ATOM   1630 O  O   . GLU   A 1 216 ? -16.03032 15.46609 34.78556 1.000 42.56634  ? 223 GLU   A O   1 
ATOM   1631 C  CB  . GLU   A 1 216 ? -12.86645 15.54701 34.10205 1.000 41.05861  ? 223 GLU   A CB  1 
ATOM   1632 C  CG  . GLU   A 1 216 ? -11.61442 16.38724 33.87171 1.000 51.70434  ? 223 GLU   A CG  1 
ATOM   1633 C  CD  . GLU   A 1 216 ? -10.35727 15.73908 34.43017 1.000 49.44032  ? 223 GLU   A CD  1 
ATOM   1634 O  OE1 . GLU   A 1 216 ? -9.82581  14.81109 33.78423 1.000 42.47750  ? 223 GLU   A OE1 1 
ATOM   1635 O  OE2 . GLU   A 1 216 ? -9.89702  16.16236 35.51227 1.000 46.75634  ? 223 GLU   A OE2 1 
ATOM   1636 N  N   . LYS   A 1 217 ? -15.56882 14.24210 32.95285 1.000 44.44128  ? 224 LYS   A N   1 
ATOM   1637 C  CA  . LYS   A 1 217 ? -16.69615 13.33986 33.14008 1.000 44.50704  ? 224 LYS   A CA  1 
ATOM   1638 C  C   . LYS   A 1 217 ? -16.26518 12.06496 33.85735 1.000 46.72727  ? 224 LYS   A C   1 
ATOM   1639 O  O   . LYS   A 1 217 ? -16.30449 11.98842 35.08540 1.000 47.62274  ? 224 LYS   A O   1 
ATOM   1640 C  CB  . LYS   A 1 217 ? -17.33352 13.00061 31.79228 1.000 44.74355  ? 224 LYS   A CB  1 
ATOM   1641 C  CG  . LYS   A 1 217 ? -17.58547 14.20936 30.90754 1.000 42.97399  ? 224 LYS   A CG  1 
ATOM   1642 C  CD  . LYS   A 1 217 ? -17.04896 13.98140 29.50466 1.000 42.53799  ? 224 LYS   A CD  1 
ATOM   1643 C  CE  . LYS   A 1 217 ? -15.58578 14.40047 29.40907 1.000 52.83722  ? 224 LYS   A CE  1 
ATOM   1644 N  NZ  . LYS   A 1 217 ? -14.91153 13.82666 28.21193 1.000 52.40166  ? 224 LYS   A NZ  1 
HETATM 1645 C  C10 . A1AYE B 2 .   ? 10.75258  31.73578 24.23483 0.796 33.31787  ? 301 A1AYE A C10 1 
HETATM 1646 C  C11 . A1AYE B 2 .   ? 11.81631  31.68699 23.34887 0.796 35.44010  ? 301 A1AYE A C11 1 
HETATM 1647 C  C12 . A1AYE B 2 .   ? 11.71868  30.89268 22.22265 0.796 29.03310  ? 301 A1AYE A C12 1 
HETATM 1648 C  C1  . A1AYE B 2 .   ? 10.50183  29.27945 20.72189 0.796 41.42802  ? 301 A1AYE A C1  1 
HETATM 1649 C  C2  . A1AYE B 2 .   ? 10.58620  30.13737 21.94776 0.796 39.54404  ? 301 A1AYE A C2  1 
HETATM 1650 C  C3  . A1AYE B 2 .   ? 9.52800   30.20586 22.85731 0.796 39.88978  ? 301 A1AYE A C3  1 
HETATM 1651 C  C4  . A1AYE B 2 .   ? 9.61649   30.99672 23.98342 0.796 36.87955  ? 301 A1AYE A C4  1 
HETATM 1652 C  C5  . A1AYE B 2 .   ? 7.23905   30.90742 24.75774 0.796 36.04627  ? 301 A1AYE A C5  1 
HETATM 1653 C  C6  . A1AYE B 2 .   ? 6.43011   31.99925 25.01109 0.796 26.20165  ? 301 A1AYE A C6  1 
HETATM 1654 C  C7  . A1AYE B 2 .   ? 5.08290   31.84563 24.86674 0.796 28.14918  ? 301 A1AYE A C7  1 
HETATM 1655 C  C8  . A1AYE B 2 .   ? 4.55913   30.61077 24.49365 0.796 46.53381  ? 301 A1AYE A C8  1 
HETATM 1656 C  C9  . A1AYE B 2 .   ? 5.47211   29.56212 24.27598 0.796 32.95507  ? 301 A1AYE A C9  1 
HETATM 1657 N  N1  . A1AYE B 2 .   ? 3.21311   30.40020 24.34995 0.796 24.76114  ? 301 A1AYE A N1  1 
HETATM 1658 N  N2  . A1AYE B 2 .   ? 6.80198   29.71318 24.41786 0.796 36.70217  ? 301 A1AYE A N2  1 
HETATM 1659 O  O1  . A1AYE B 2 .   ? 8.58592   31.10479 24.93522 0.796 38.79356  ? 301 A1AYE A O1  1 
HETATM 1660 CL CL1 . A1AYE B 2 .   ? 13.07637  30.85294 21.12545 0.796 69.90552  ? 301 A1AYE A CL1 1 
HETATM 1661 O  O   . HOH   C 3 .   ? -7.03348  47.86458 13.13577 1.000 38.33472  ? 401 HOH   A O   1 
HETATM 1662 O  O   . HOH   C 3 .   ? -3.19884  35.37874 13.83047 1.000 21.04959  ? 402 HOH   A O   1 
HETATM 1663 O  O   . HOH   C 3 .   ? -1.29330  31.40573 28.38000 1.000 24.72829  ? 403 HOH   A O   1 
HETATM 1664 O  O   . HOH   C 3 .   ? 11.15878  34.91208 23.69759 1.000 62.53030  ? 404 HOH   A O   1 
HETATM 1665 O  O   . HOH   C 3 .   ? 7.35551   20.11444 19.06363 1.000 23.51231  ? 405 HOH   A O   1 
HETATM 1666 O  O   . HOH   C 3 .   ? 14.97077  37.05162 23.75986 1.000 52.55787  ? 406 HOH   A O   1 
HETATM 1667 O  O   . HOH   C 3 .   ? -4.10288  29.87881 8.11283  1.000 32.80541  ? 407 HOH   A O   1 
HETATM 1668 O  O   . HOH   C 3 .   ? 4.52654   16.62656 21.93000 1.000 29.81366  ? 408 HOH   A O   1 
HETATM 1669 O  O   . HOH   C 3 .   ? -14.44550 30.23621 34.60052 1.000 31.92929  ? 409 HOH   A O   1 
HETATM 1670 O  O   . HOH   C 3 .   ? -15.54884 36.57012 9.47449  1.000 29.53687  ? 410 HOH   A O   1 
HETATM 1671 O  O   . HOH   C 3 .   ? 7.90679   14.64337 24.05305 1.000 29.99882  ? 411 HOH   A O   1 
HETATM 1672 O  O   . HOH   C 3 .   ? -4.21573  36.55581 34.01976 1.000 32.74474  ? 412 HOH   A O   1 
HETATM 1673 O  O   . HOH   C 3 .   ? 17.11595  25.44909 31.46651 1.000 32.16357  ? 413 HOH   A O   1 
HETATM 1674 O  O   . HOH   C 3 .   ? 6.99403   14.88547 37.39560 1.000 30.08571  ? 414 HOH   A O   1 
HETATM 1675 O  O   . HOH   C 3 .   ? 0.61860   39.29501 29.85049 1.000 25.93559  ? 415 HOH   A O   1 
HETATM 1676 O  O   . HOH   C 3 .   ? -3.15089  33.02305 20.53407 1.000 11.07729  ? 416 HOH   A O   1 
HETATM 1677 O  O   . HOH   C 3 .   ? 10.99302  18.47396 22.57500 1.000 27.14445  ? 417 HOH   A O   1 
HETATM 1678 O  O   . HOH   C 3 .   ? -13.08522 14.39375 26.49801 1.000 28.82710  ? 418 HOH   A O   1 
HETATM 1679 O  O   . HOH   C 3 .   ? 14.79619  44.68665 42.90442 1.000 37.24877  ? 419 HOH   A O   1 
HETATM 1680 O  O   . HOH   C 3 .   ? -15.78981 37.04347 23.69952 1.000 21.49388  ? 420 HOH   A O   1 
HETATM 1681 O  O   . HOH   C 3 .   ? -1.13687  29.83635 5.55168  1.000 37.76096  ? 421 HOH   A O   1 
HETATM 1682 O  O   . HOH   C 3 .   ? -12.50952 19.99258 42.15272 1.000 32.93179  ? 422 HOH   A O   1 
HETATM 1683 O  O   . HOH   C 3 .   ? 9.71701   24.74146 40.28434 1.000 24.38110  ? 423 HOH   A O   1 
HETATM 1684 O  O   . HOH   C 3 .   ? 2.50828   14.17048 30.11392 1.000 37.62613  ? 424 HOH   A O   1 
HETATM 1685 O  O   . HOH   C 3 .   ? -0.52697  19.32648 44.71065 1.000 30.06977  ? 425 HOH   A O   1 
HETATM 1686 O  O   . HOH   C 3 .   ? -4.96189  42.08556 28.26146 1.000 22.46125  ? 426 HOH   A O   1 
HETATM 1687 O  O   . HOH   C 3 .   ? 10.95535  22.08908 41.98828 1.000 49.22583  ? 427 HOH   A O   1 
HETATM 1688 O  O   . HOH   C 3 .   ? -12.11395 42.75191 5.36706  1.000 40.98083  ? 428 HOH   A O   1 
HETATM 1689 O  O   . HOH   C 3 .   ? -17.27846 24.68766 34.85258 1.000 20.87883  ? 429 HOH   A O   1 
HETATM 1690 O  O   . HOH   C 3 .   ? -5.59423  18.61237 29.32370 1.000 20.91140  ? 430 HOH   A O   1 
HETATM 1691 O  O   . HOH   C 3 .   ? 3.06263   40.97974 37.74427 1.000 36.36791  ? 431 HOH   A O   1 
HETATM 1692 O  O   . HOH   C 3 .   ? -2.09650  31.81528 5.54444  1.000 32.92959  ? 432 HOH   A O   1 
HETATM 1693 O  O   . HOH   C 3 .   ? 16.03469  25.65327 29.47388 1.000 24.46382  ? 433 HOH   A O   1 
HETATM 1694 O  O   . HOH   C 3 .   ? 22.73552  32.50462 23.93524 1.000 23.53015  ? 434 HOH   A O   1 
HETATM 1695 O  O   . HOH   C 3 .   ? 15.77037  31.65493 22.94064 1.000 17.02704  ? 435 HOH   A O   1 
HETATM 1696 O  O   . HOH   C 3 .   ? 4.01322   37.80422 31.09312 1.000 19.15103  ? 436 HOH   A O   1 
HETATM 1697 O  O   . HOH   C 3 .   ? 3.58646   13.00592 26.47561 1.000 33.37151  ? 437 HOH   A O   1 
HETATM 1698 O  O   . HOH   C 3 .   ? 0.37932   15.69866 44.06929 1.000 29.87940  ? 438 HOH   A O   1 
HETATM 1699 O  O   . HOH   C 3 .   ? 6.57476   33.11507 10.25130 1.000 31.35311  ? 439 HOH   A O   1 
HETATM 1700 O  O   . HOH   C 3 .   ? -13.18014 18.64293 36.47705 1.000 30.50658  ? 440 HOH   A O   1 
HETATM 1701 O  O   . HOH   C 3 .   ? -16.88541 35.11086 21.76186 1.000 22.75853  ? 441 HOH   A O   1 
HETATM 1702 O  O   . HOH   C 3 .   ? 1.36008   39.89636 34.03344 1.000 14.76680  ? 442 HOH   A O   1 
HETATM 1703 O  O   . HOH   C 3 .   ? -4.93335  38.59878 35.48741 1.000 23.56278  ? 443 HOH   A O   1 
HETATM 1704 O  O   . HOH   C 3 .   ? 19.27348  27.97768 37.82997 1.000 30.15514  ? 444 HOH   A O   1 
HETATM 1705 O  O   . HOH   C 3 .   ? -11.20287 27.93513 16.72488 1.000 32.24965  ? 445 HOH   A O   1 
HETATM 1706 O  O   . HOH   C 3 .   ? -3.85291  40.72200 31.08565 1.000 25.14064  ? 446 HOH   A O   1 
HETATM 1707 O  O   . HOH   C 3 .   ? -6.06449  45.11564 9.69926  1.000 23.27809  ? 447 HOH   A O   1 
HETATM 1708 O  O   . HOH   C 3 .   ? 3.67574   17.90762 19.95464 1.000 28.84364  ? 448 HOH   A O   1 
HETATM 1709 O  O   . HOH   C 3 .   ? 3.08672   17.81854 17.35473 1.000 29.85893  ? 449 HOH   A O   1 
HETATM 1710 O  O   . HOH   C 3 .   ? 3.04140   17.10903 15.23023 1.000 34.62029  ? 450 HOH   A O   1 
HETATM 1711 O  O   . HOH   C 3 .   ? 0.73894   12.60553 28.68886 1.000 38.34618  ? 451 HOH   A O   1 
HETATM 1712 O  O   . HOH   C 3 .   ? -16.14737 28.00166 35.36049 1.000 14.25503  ? 452 HOH   A O   1 
HETATM 1713 O  O   . HOH   C 3 .   ? 14.78567  32.29764 20.19568 1.000 28.25009  ? 453 HOH   A O   1 
HETATM 1714 O  O   . HOH   C 3 .   ? 11.10047  12.99491 23.77961 1.000 23.53802  ? 454 HOH   A O   1 
HETATM 1715 O  O   . HOH   C 3 .   ? 9.51392   12.48168 21.43379 1.000 21.32489  ? 455 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLU A 9   ? 0.58582 0.73217 1.12143 -0.00926 0.12255  -0.34672 16  GLU A N   
2    C CA  . GLU A 9   ? 0.66005 0.77790 1.16852 0.00761  0.13247  -0.31222 16  GLU A CA  
3    C C   . GLU A 9   ? 0.63015 0.74162 1.13172 0.01358  0.12104  -0.26744 16  GLU A C   
4    O O   . GLU A 9   ? 0.85685 0.99230 1.31710 0.02498  0.10362  -0.26041 16  GLU A O   
5    C CB  . GLU A 9   ? 0.67922 0.81156 1.11940 0.02797  0.13323  -0.32577 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.82472 0.92354 1.25167 0.03727  0.15717  -0.30803 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.05600 1.14545 1.43163 0.05429  0.15622  -0.27105 16  GLU A CD  
8    O OE1 . GLU A 9   ? 0.86972 0.97351 1.22212 0.06054  0.13613  -0.25571 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 0.91073 0.97691 1.27073 0.06073  0.17833  -0.25859 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.50367 0.58408 1.04476 0.00820  0.13035  -0.23876 17  VAL A N   
11   C CA  . VAL A 10  ? 0.39422 0.46800 0.93509 0.01123  0.11962  -0.20003 17  VAL A CA  
12   C C   . VAL A 10  ? 0.39109 0.44477 0.92270 0.02030  0.12989  -0.17541 17  VAL A C   
13   O O   . VAL A 10  ? 0.39806 0.43584 0.96155 0.01887  0.14676  -0.17772 17  VAL A O   
14   C CB  . VAL A 10  ? 0.37513 0.43541 0.96902 -0.00177 0.11921  -0.18732 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.34790 0.41396 0.92908 0.00119  0.10287  -0.15702 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.39195 0.46134 1.01344 -0.01793 0.12295  -0.22071 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.38424 0.43902 0.87569 0.02910  0.12159  -0.15377 18  GLU A N   
18   C CA  . GLU A 11  ? 0.38304 0.42028 0.86921 0.03264  0.13230  -0.13179 18  GLU A CA  
19   C C   . GLU A 11  ? 0.35125 0.38429 0.86376 0.02790  0.12029  -0.10448 18  GLU A C   
20   O O   . GLU A 11  ? 0.33899 0.37850 0.83299 0.02911  0.10370  -0.09486 18  GLU A O   
21   C CB  . GLU A 11  ? 0.41131 0.44317 0.82938 0.04514  0.13683  -0.12752 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.52982 0.56159 0.91259 0.05395  0.15336  -0.14980 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.66802 0.68709 0.97328 0.07124  0.15976  -0.13973 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.49837 0.52699 0.76326 0.08349  0.14162  -0.13514 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.61122 0.60903 0.89540 0.07407  0.18538  -0.13546 18  GLU A OE2 
26   N N   . THR A 12  ? 0.34123 0.36778 0.89637 0.02447  0.12804  -0.09378 19  THR A N   
27   C CA  . THR A 12  ? 0.31726 0.34510 0.89698 0.02231  0.11505  -0.07046 19  THR A CA  
28   C C   . THR A 12  ? 0.32033 0.34540 0.88769 0.02044  0.12073  -0.05989 19  THR A C   
29   O O   . THR A 12  ? 0.33479 0.35832 0.91269 0.01883  0.14032  -0.06722 19  THR A O   
30   C CB  . THR A 12  ? 0.30938 0.33788 0.94890 0.02323  0.11633  -0.06644 19  THR A CB  
31   O OG1 . THR A 12  ? 0.32212 0.34315 0.97517 0.02214  0.12388  -0.08401 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.29195 0.32343 0.94437 0.02502  0.09721  -0.04359 19  THR A CG2 
33   N N   . PHE A 13  ? 0.31127 0.33452 0.85742 0.01908  0.10655  -0.04477 20  PHE A N   
34   C CA  . PHE A 13  ? 0.31973 0.33587 0.85435 0.01321  0.11277  -0.03732 20  PHE A CA  
35   C C   . PHE A 13  ? 0.29938 0.32875 0.86470 0.00894  0.09448  -0.02489 20  PHE A C   
36   O O   . PHE A 13  ? 0.28377 0.32004 0.85524 0.01381  0.07582  -0.01642 20  PHE A O   
37   C CB  . PHE A 13  ? 0.34331 0.33742 0.80998 0.01744  0.11589  -0.03375 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.36715 0.35502 0.79136 0.02860  0.12496  -0.04502 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.35782 0.36044 0.77208 0.03634  0.10935  -0.05236 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.40432 0.37416 0.79746 0.03134  0.14986  -0.04982 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.38266 0.38929 0.75953 0.04735  0.11385  -0.06771 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.44487 0.41264 0.79190 0.04549  0.15569  -0.06107 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.42144 0.41110 0.76136 0.05392  0.13531  -0.07171 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.34869 0.38281 0.93211 -0.00081 0.10131  -0.02539 21  ALA A N   
45   C CA  . ALA A 14  ? 0.29206 0.34548 0.90288 -0.00517 0.08234  -0.01885 21  ALA A CA  
46   C C   . ALA A 14  ? 0.37172 0.40586 0.93528 -0.01053 0.07558  -0.01364 21  ALA A C   
47   O O   . ALA A 14  ? 0.32901 0.33483 0.85329 -0.01594 0.09387  -0.01642 21  ALA A O   
48   C CB  . ALA A 14  ? 0.29347 0.37281 0.95969 -0.01492 0.09168  -0.02846 21  ALA A CB  
49   N N   . PHE A 15  ? 0.29118 0.33655 0.85434 -0.00649 0.05127  -0.00500 22  PHE A N   
50   C CA  . PHE A 15  ? 0.32777 0.35757 0.85194 -0.01110 0.04347  -0.00231 22  PHE A CA  
51   C C   . PHE A 15  ? 0.40544 0.43470 0.94533 -0.02979 0.05418  -0.01433 22  PHE A C   
52   O O   . PHE A 15  ? 0.35502 0.41426 0.94967 -0.03807 0.05661  -0.02373 22  PHE A O   
53   C CB  . PHE A 15  ? 0.29078 0.33908 0.81841 -0.00283 0.01633  0.00762  22  PHE A CB  
54   C CG  . PHE A 15  ? 0.28317 0.32178 0.78079 0.01014  0.01054  0.01865  22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.34652 0.36511 0.80972 0.01397  0.02350  0.01624  22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.29990 0.35336 0.80845 0.01950  -0.00617 0.03061  22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.36380 0.38395 0.80954 0.02342  0.01794  0.02143  22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.39441 0.44062 0.88318 0.02726  -0.00660 0.03869  22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.35346 0.38681 0.81521 0.02751  0.00483  0.03189  22  PHE A CZ  
60   N N   . GLN A 16  ? 0.35048 0.34556 0.84484 -0.03667 0.06261  -0.01563 23  GLN A N   
61   C CA  . GLN A 16  ? 0.37405 0.36627 0.88503 -0.05879 0.07173  -0.02984 23  GLN A CA  
62   C C   . GLN A 16  ? 0.35947 0.39268 0.90278 -0.06192 0.04114  -0.03604 23  GLN A C   
63   O O   . GLN A 16  ? 0.39452 0.43246 0.91406 -0.04714 0.01809  -0.02535 23  GLN A O   
64   C CB  . GLN A 16  ? 0.41758 0.35273 0.86710 -0.06362 0.09112  -0.02892 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.45157 0.34623 0.87539 -0.06587 0.12834  -0.02683 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.75326 0.58860 1.09746 -0.05155 0.14239  -0.01498 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.83424 0.65791 1.14692 -0.04299 0.12638  -0.01095 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.77010 0.56774 1.07844 -0.04569 0.17327  -0.00879 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.36310 0.43023 0.96151 -0.08040 0.04151  -0.05452 24  ALA A N   
70   C CA  . ALA A 17  ? 0.35007 0.47182 0.98780 -0.07837 0.00858  -0.06246 24  ALA A CA  
71   C C   . ALA A 17  ? 0.36440 0.47334 0.95609 -0.07530 -0.01200 -0.06139 24  ALA A C   
72   O O   . ALA A 17  ? 0.35229 0.49050 0.94267 -0.05771 -0.04161 -0.05265 24  ALA A O   
73   C CB  . ALA A 17  ? 0.38040 0.54378 1.08404 -0.10252 0.01414  -0.08951 24  ALA A CB  
74   N N   . GLU A 18  ? 0.39727 0.45834 0.94706 -0.09030 0.00589  -0.06922 25  GLU A N   
75   C CA  . GLU A 18  ? 0.41625 0.45945 0.91824 -0.08636 -0.00981 -0.06990 25  GLU A CA  
76   C C   . GLU A 18  ? 0.39732 0.42884 0.85513 -0.05777 -0.02196 -0.04376 25  GLU A C   
77   O O   . GLU A 18  ? 0.39450 0.44584 0.83797 -0.04548 -0.04717 -0.03881 25  GLU A O   
78   C CB  . GLU A 18  ? 0.46282 0.44492 0.92507 -0.10467 0.01830  -0.08114 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.60525 0.58525 1.11053 -0.13810 0.04352  -0.10624 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.61841 0.58163 1.13855 -0.14055 0.07573  -0.09716 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.76277 0.72907 1.27063 -0.11645 0.07224  -0.07522 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.72469 0.67116 1.26861 -0.16791 0.10660  -0.11376 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.38812 0.39058 0.82463 -0.04722 -0.00331 -0.02841 26  ILE A N   
84   C CA  . ILE A 19  ? 0.37275 0.36761 0.77339 -0.02425 -0.01152 -0.00861 26  ILE A CA  
85   C C   . ILE A 19  ? 0.35937 0.39602 0.79424 -0.01149 -0.03142 0.00271  26  ILE A C   
86   O O   . ILE A 19  ? 0.33737 0.37925 0.75074 0.00298  -0.04539 0.01565  26  ILE A O   
87   C CB  . ILE A 19  ? 0.37606 0.33687 0.74758 -0.01638 0.01158  -0.00056 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.51834 0.43132 0.85714 -0.02687 0.03660  -0.00872 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.37038 0.32361 0.70141 0.00352  0.00454  0.01252  26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.43862 0.31972 0.74142 -0.01363 0.05814  0.00054  26  ILE A CD1 
91   N N   . ALA A 20  ? 0.32700 0.39068 0.81456 -0.01545 -0.02981 -0.00111 27  ALA A N   
92   C CA  . ALA A 20  ? 0.38844 0.48685 0.90898 -0.00052 -0.04740 0.01027  27  ALA A CA  
93   C C   . ALA A 20  ? 0.32151 0.44900 0.84099 0.00541  -0.07500 0.00988  27  ALA A C   
94   O O   . ALA A 20  ? 0.32147 0.45892 0.83204 0.02432  -0.08955 0.02763  27  ALA A O   
95   C CB  . ALA A 20  ? 0.29700 0.41955 0.87596 -0.00382 -0.03920 0.00348  27  ALA A CB  
96   N N   . GLN A 21  ? 0.33897 0.47881 0.86504 -0.01093 -0.08086 -0.01140 28  GLN A N   
97   C CA  . GLN A 21  ? 0.35696 0.52963 0.87843 -0.00573 -0.10959 -0.01771 28  GLN A CA  
98   C C   . GLN A 21  ? 0.37211 0.51921 0.83011 0.00585  -0.11672 -0.00508 28  GLN A C   
99   O O   . GLN A 21  ? 0.38625 0.55746 0.82993 0.02193  -0.14007 0.00250  28  GLN A O   
100  C CB  . GLN A 21  ? 0.37655 0.56646 0.92122 -0.03163 -0.11085 -0.05048 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.38536 0.64247 0.97127 -0.02786 -0.14198 -0.06607 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.51018 0.78278 1.11048 -0.05733 -0.14477 -0.10407 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.51682 0.77717 1.14800 -0.08513 -0.11955 -0.12347 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.50446 0.80156 1.08053 -0.05255 -0.17295 -0.11626 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.46210 0.56244 0.87968 0.00089  -0.09638 -0.00220 29  LEU A N   
106  C CA  . LEU A 22  ? 0.38963 0.46912 0.75078 0.01229  -0.10041 0.00750  29  LEU A CA  
107  C C   . LEU A 22  ? 0.37632 0.46149 0.72929 0.03356  -0.10393 0.03452  29  LEU A C   
108  O O   . LEU A 22  ? 0.39422 0.48587 0.71655 0.04667  -0.11657 0.04455  29  LEU A O   
109  C CB  . LEU A 22  ? 0.39916 0.43114 0.72253 0.00607  -0.07765 0.00337  29  LEU A CB  
110  C CG  . LEU A 22  ? 0.41957 0.43156 0.68681 0.01785  -0.07961 0.00867  29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.44975 0.47772 0.70095 0.01547  -0.09984 -0.00500 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.43596 0.40169 0.66723 0.01675  -0.05746 0.00420  29  LEU A CD2 
113  N N   . MET A 23  ? 0.35128 0.43126 0.72942 0.03613  -0.09008 0.04533  30  MET A N   
114  C CA  . MET A 23  ? 0.41590 0.49483 0.78962 0.05149  -0.08775 0.06800  30  MET A CA  
115  C C   . MET A 23  ? 0.35717 0.46130 0.74896 0.06652  -0.10456 0.08210  30  MET A C   
116  O O   . MET A 23  ? 0.40909 0.50758 0.77944 0.08101  -0.10483 0.10275  30  MET A O   
117  C CB  . MET A 23  ? 0.43685 0.50308 0.83288 0.04805  -0.06800 0.07005  30  MET A CB  
118  C CG  . MET A 23  ? 0.48290 0.52841 0.86284 0.03765  -0.05322 0.05563  30  MET A CG  
119  S SD  . MET A 23  ? 0.33544 0.37420 0.73881 0.03572  -0.03383 0.05344  30  MET A SD  
120  C CE  . MET A 23  ? 0.38919 0.40783 0.77973 0.02493  -0.02037 0.03687  30  MET A CE  
121  N N   . SER A 24  ? 0.35650 0.48908 0.78677 0.06530  -0.11716 0.07206  31  SER A N   
122  C CA  . SER A 24  ? 0.37779 0.53979 0.81772 0.08625  -0.13826 0.08496  31  SER A CA  
123  C C   . SER A 24  ? 0.41078 0.58422 0.80413 0.09457  -0.15867 0.08451  31  SER A C   
124  O O   . SER A 24  ? 0.43979 0.62004 0.81057 0.11829  -0.16996 0.10615  31  SER A O   
125  C CB  . SER A 24  ? 0.38793 0.58902 0.88496 0.08471  -0.14924 0.06995  31  SER A CB  
126  O OG  . SER A 24  ? 0.39168 0.57986 0.92600 0.07141  -0.12696 0.06286  31  SER A OG  
127  N N   . LEU A 25  ? 0.41439 0.58515 0.78833 0.07655  -0.16114 0.06044  32  LEU A N   
128  C CA  . LEU A 25  ? 0.48677 0.66404 0.81144 0.08279  -0.17804 0.05558  32  LEU A CA  
129  C C   . LEU A 25  ? 0.46563 0.61091 0.73819 0.09498  -0.16501 0.07898  32  LEU A C   
130  O O   . LEU A 25  ? 0.49752 0.65069 0.73017 0.11325  -0.17744 0.09151  32  LEU A O   
131  C CB  . LEU A 25  ? 0.45597 0.62802 0.77427 0.05805  -0.17780 0.02170  32  LEU A CB  
132  C CG  . LEU A 25  ? 0.50951 0.68928 0.78056 0.05985  -0.19558 0.00625  32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.52422 0.75927 0.80349 0.07630  -0.22949 0.00255  32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.54580 0.70679 0.81589 0.03161  -0.18697 -0.02842 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.43653 0.54957 0.70906 0.08610  -0.13952 0.08422  33  ILE A N   
136  C CA  . ILE A 26  ? 0.60388 0.69385 0.83499 0.09386  -0.12492 0.10033  33  ILE A CA  
137  C C   . ILE A 26  ? 0.59885 0.68751 0.83109 0.11118  -0.11929 0.13096  33  ILE A C   
138  O O   . ILE A 26  ? 0.54529 0.62812 0.73602 0.12460  -0.11730 0.14753  33  ILE A O   
139  C CB  . ILE A 26  ? 0.46862 0.53444 0.70368 0.08125  -0.10229 0.09287  33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.43067 0.48205 0.63485 0.07272  -0.10213 0.07097  33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.41693 0.47194 0.63882 0.08859  -0.08420 0.11149  33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.40962 0.44029 0.62645 0.06138  -0.08559 0.05914  33  ILE A CD1 
143  N N   . ILE A 27  ? 0.43944 0.52871 0.71702 0.11135  -0.11313 0.13910  34  ILE A N   
144  C CA  . ILE A 27  ? 0.45849 0.53480 0.73903 0.12633  -0.10153 0.16823  34  ILE A CA  
145  C C   . ILE A 27  ? 0.55884 0.64838 0.81182 0.15215  -0.12084 0.18699  34  ILE A C   
146  O O   . ILE A 27  ? 0.79881 0.86997 1.01665 0.16753  -0.11027 0.21342  34  ILE A O   
147  C CB  . ILE A 27  ? 0.47490 0.54570 0.81046 0.12136  -0.09020 0.16874  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.43168 0.48903 0.78431 0.10022  -0.06969 0.15315  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.63099 0.68194 0.97034 0.13883  -0.07787 0.19873  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.37308 0.42699 0.77597 0.09376  -0.05944 0.14712  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.51015 0.63393 0.77733 0.15807  -0.14859 0.17298  35  ASN A N   
152  C CA  . ASN A 28  ? 0.64437 0.79014 0.89507 0.18839  -0.17096 0.19027  35  ASN A CA  
153  C C   . ASN A 28  ? 0.83015 0.99108 1.01913 0.20019  -0.19047 0.18779  35  ASN A C   
154  O O   . ASN A 28  ? 0.97840 1.14687 1.13228 0.23119  -0.20295 0.21125  35  ASN A O   
155  C CB  . ASN A 28  ? 0.71930 0.90725 1.02388 0.19157  -0.19358 0.17330  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.59251 0.76571 0.95446 0.18605  -0.17404 0.17801  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.63567 0.83095 1.04746 0.17019  -0.17728 0.15379  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.52714 0.66064 0.88179 0.19788  -0.15072 0.20784  35  ASN A ND2 
159  N N   . THR A 29  ? 0.87200 1.03471 1.04254 0.17911  -0.19245 0.16053  36  THR A N   
160  C CA  . THR A 29  ? 0.97704 1.15429 1.08899 0.18871  -0.21099 0.15201  36  THR A CA  
161  C C   . THR A 29  ? 0.69667 0.83959 0.74961 0.20034  -0.18882 0.17896  36  THR A C   
162  O O   . THR A 29  ? 0.63809 0.74953 0.69665 0.18551  -0.15911 0.18427  36  THR A O   
163  C CB  . THR A 29  ? 0.93138 1.11628 1.04611 0.16144  -0.21774 0.11065  36  THR A CB  
164  O OG1 . THR A 29  ? 0.93140 1.15157 1.10159 0.14879  -0.23631 0.08410  36  THR A OG1 
165  C CG2 . THR A 29  ? 0.66349 0.85839 0.71406 0.17014  -0.23400 0.09832  36  THR A CG2 
166  N N   . PHE A 30  ? 0.88509 1.03812 0.88159 0.22822  -0.20299 0.19527  37  PHE A N   
167  C CA  . PHE A 30  ? 0.76959 0.89239 0.70335 0.23970  -0.18041 0.21946  37  PHE A CA  
168  C C   . PHE A 30  ? 0.90068 1.01805 0.80911 0.21991  -0.17430 0.19097  37  PHE A C   
169  O O   . PHE A 30  ? 0.99340 1.13515 0.88739 0.21512  -0.19955 0.15895  37  PHE A O   
170  C CB  . PHE A 30  ? 0.88584 1.02177 0.75695 0.27779  -0.19887 0.24277  37  PHE A CB  
171  C CG  . PHE A 30  ? 1.06306 1.16581 0.86242 0.29239  -0.17181 0.27154  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.91104 1.00760 0.67188 0.27975  -0.16148 0.25309  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.96058 1.03418 0.73188 0.31932  -0.15225 0.31820  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.96459 1.03423 0.66378 0.29276  -0.13347 0.27875  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 1.01782 1.05874 0.72543 0.33030  -0.12175 0.34536  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 1.09354 1.13610 0.76643 0.31660  -0.11279 0.32484  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.86914 0.95560 0.77362 0.20913  -0.13996 0.20081  38  TYR A N   
178  C CA  . TYR A 31  ? 0.91533 0.99410 0.79640 0.19549  -0.13055 0.17679  38  TYR A CA  
179  C C   . TYR A 31  ? 0.83285 0.88715 0.70085 0.19586  -0.09238 0.19951  38  TYR A C   
180  O O   . TYR A 31  ? 0.69678 0.74095 0.61278 0.18134  -0.07146 0.20391  38  TYR A O   
181  C CB  . TYR A 31  ? 0.67910 0.75891 0.60882 0.17011  -0.13424 0.14484  38  TYR A CB  
182  C CG  . TYR A 31  ? 0.67672 0.74118 0.58284 0.16041  -0.12138 0.12305  38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.71676 0.78422 0.57634 0.16319  -0.13595 0.09894  38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.74501 0.79347 0.67543 0.15047  -0.09535 0.12437  38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.74987 0.79723 0.58634 0.15761  -0.12183 0.07946  38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.70895 0.74424 0.61702 0.14778  -0.08406 0.10601  38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.79007 0.82111 0.65066 0.15197  -0.09586 0.08491  38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.81170 0.82369 0.64852 0.15243  -0.08219 0.06724  38  TYR A OH  
189  N N   . SER A 32  ? 0.91917 0.96792 0.72355 0.21182  -0.08310 0.21117  39  SER A N   
190  C CA  . SER A 32  ? 0.81421 0.84351 0.60755 0.21340  -0.04372 0.23684  39  SER A CA  
191  C C   . SER A 32  ? 0.77764 0.80635 0.59906 0.19460  -0.02157 0.21753  39  SER A C   
192  O O   . SER A 32  ? 0.75969 0.78182 0.60553 0.18696  0.01067  0.23177  39  SER A O   
193  C CB  . SER A 32  ? 0.89409 0.91777 0.60717 0.23691  -0.03709 0.25470  39  SER A CB  
194  O OG  . SER A 32  ? 0.94472 0.96121 0.63276 0.25939  -0.04363 0.28747  39  SER A OG  
195  N N   . ASN A 33  ? 0.78851 0.82431 0.60806 0.18779  -0.03715 0.18445  40  ASN A N   
196  C CA  . ASN A 33  ? 0.78526 0.82077 0.62345 0.17788  -0.01838 0.16693  40  ASN A CA  
197  C C   . ASN A 33  ? 0.65255 0.69133 0.56012 0.16102  -0.01429 0.16224  40  ASN A C   
198  O O   . ASN A 33  ? 0.61997 0.65768 0.54753 0.15319  -0.02371 0.13934  40  ASN A O   
199  C CB  . ASN A 33  ? 0.72962 0.76098 0.53448 0.18010  -0.03316 0.13566  40  ASN A CB  
200  C CG  . ASN A 33  ? 0.76494 0.79417 0.56536 0.18231  -0.01017 0.12365  40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.73404 0.77186 0.53167 0.18750  0.01649  0.13849  40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.89430 0.91165 0.69465 0.17947  -0.01826 0.09659  40  ASN A ND2 
203  N N   . LYS A 34  ? 0.50577 0.53139 0.86670 0.02602  -0.34520 0.10957  41  LYS A N   
204  C CA  . LYS A 34  ? 0.49403 0.56128 0.90829 0.04336  -0.31220 0.10026  41  LYS A CA  
205  C C   . LYS A 34  ? 0.43331 0.47352 0.82664 0.04490  -0.28728 0.07974  41  LYS A C   
206  O O   . LYS A 34  ? 0.39953 0.47056 0.82928 0.05137  -0.26717 0.07153  41  LYS A O   
207  C CB  . LYS A 34  ? 0.45808 0.53151 0.89333 0.07161  -0.29567 0.10308  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.49188 0.58097 0.93346 0.07318  -0.31591 0.12301  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.52543 0.68441 1.02301 0.07723  -0.31156 0.13706  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.46960 0.64717 0.99837 0.11126  -0.27892 0.13220  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.49907 0.68048 1.03500 0.13525  -0.28042 0.14589  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.46896 0.45156 0.79830 0.03967  -0.28318 0.07250  42  GLU A N   
213  C CA  . GLU A 35  ? 0.43628 0.39666 0.74597 0.04390  -0.25441 0.05731  42  GLU A CA  
214  C C   . GLU A 35  ? 0.48684 0.46061 0.79747 0.02916  -0.24678 0.04770  42  GLU A C   
215  O O   . GLU A 35  ? 0.47064 0.44146 0.78159 0.03395  -0.22322 0.03650  42  GLU A O   
216  C CB  . GLU A 35  ? 0.47053 0.37342 0.71495 0.04553  -0.24966 0.05881  42  GLU A CB  
217  C CG  . GLU A 35  ? 0.51857 0.38078 0.69849 0.02917  -0.26470 0.06083  42  GLU A CG  
218  C CD  . GLU A 35  ? 0.57636 0.37897 0.68664 0.03865  -0.25191 0.06397  42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.58230 0.36994 0.68374 0.04996  -0.25428 0.07349  42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.61032 0.38079 0.67377 0.03723  -0.23742 0.05899  42  GLU A OE2 
221  N N   . ILE A 36  ? 0.43480 0.42287 0.74560 0.00908  -0.26830 0.05395  43  ILE A N   
222  C CA  . ILE A 36  ? 0.42479 0.42225 0.73376 -0.00743 -0.26284 0.04679  43  ILE A CA  
223  C C   . ILE A 36  ? 0.43870 0.48819 0.80888 0.00252  -0.24177 0.04079  43  ILE A C   
224  O O   . ILE A 36  ? 0.36366 0.41934 0.73206 -0.00756 -0.23116 0.03318  43  ILE A O   
225  C CB  . ILE A 36  ? 0.47467 0.47617 0.77235 -0.03654 -0.29600 0.05918  43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.44362 0.51590 0.81633 -0.03744 -0.31334 0.07774  43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.60505 0.53889 0.82443 -0.04641 -0.31801 0.06336  43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.41906 0.54925 0.84270 -0.05045 -0.30878 0.08343  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.35683 0.43645 0.77341 0.02384  -0.23461 0.04421  44  PHE A N   
230  C CA  . PHE A 37  ? 0.32571 0.44036 0.78564 0.03812  -0.21171 0.03751  44  PHE A CA  
231  C C   . PHE A 37  ? 0.31178 0.39596 0.74394 0.04051  -0.18869 0.01960  44  PHE A C   
232  O O   . PHE A 37  ? 0.29409 0.39629 0.74087 0.04040  -0.17302 0.01173  44  PHE A O   
233  C CB  . PHE A 37  ? 0.32579 0.45836 0.82231 0.06517  -0.20709 0.04405  44  PHE A CB  
234  C CG  . PHE A 37  ? 0.33206 0.41889 0.80184 0.08026  -0.19531 0.03386  44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.35243 0.40442 0.79173 0.07905  -0.20802 0.03923  44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.32492 0.40046 0.79612 0.09322  -0.17317 0.02089  44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.36035 0.37462 0.77928 0.08898  -0.19831 0.03435  44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.34761 0.37971 0.79357 0.10030  -0.16755 0.01489  44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.35288 0.35811 0.77686 0.09746  -0.17983 0.02289  44  PHE A CZ  
240  N N   . LEU A 38  ? 0.32222 0.36330 0.71569 0.04257  -0.18657 0.01615  45  LEU A N   
241  C CA  . LEU A 38  ? 0.31038 0.33059 0.68394 0.04322  -0.16777 0.00549  45  LEU A CA  
242  C C   . LEU A 38  ? 0.31025 0.32362 0.65741 0.02812  -0.16395 0.00128  45  LEU A C   
243  O O   . LEU A 38  ? 0.29969 0.31932 0.65026 0.02686  -0.14923 -0.00722 45  LEU A O   
244  C CB  . LEU A 38  ? 0.38403 0.37010 0.73151 0.04924  -0.16611 0.01025  45  LEU A CB  
245  C CG  . LEU A 38  ? 0.34912 0.32388 0.69067 0.05015  -0.15005 0.00620  45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.30106 0.28857 0.66889 0.05482  -0.14287 -0.00413 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.34817 0.29901 0.67533 0.05473  -0.15015 0.01750  45  LEU A CD2 
248  N N   . ARG A 39  ? 0.33686 0.32983 0.65008 0.01658  -0.17822 0.00736  46  ARG A N   
249  C CA  . ARG A 39  ? 0.35008 0.32443 0.62770 0.00292  -0.17576 0.00374  46  ARG A CA  
250  C C   . ARG A 39  ? 0.42513 0.43696 0.73628 -0.00800 -0.17400 -0.00028 46  ARG A C   
251  O O   . ARG A 39  ? 0.39320 0.39797 0.68879 -0.01326 -0.16185 -0.00689 46  ARG A O   
252  C CB  . ARG A 39  ? 0.41647 0.35024 0.64129 -0.00928 -0.19589 0.01089  46  ARG A CB  
253  C CG  . ARG A 39  ? 0.51888 0.41366 0.68893 -0.02121 -0.19308 0.00710  46  ARG A CG  
254  C CD  . ARG A 39  ? 0.52593 0.41127 0.67796 -0.04846 -0.22126 0.01231  46  ARG A CD  
255  N NE  . ARG A 39  ? 0.83121 0.68468 0.94865 -0.05456 -0.24683 0.02149  46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.82449 0.70639 0.97090 -0.07310 -0.27699 0.03289  46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.49023 0.43816 0.70538 -0.08523 -0.28244 0.03869  46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.89282 0.73804 0.99829 -0.07883 -0.30195 0.04158  46  ARG A NH2 
259  N N   . GLU A 40  ? 0.32003 0.37458 0.67871 -0.00953 -0.18430 0.00655  47  GLU A N   
260  C CA  . GLU A 40  ? 0.30948 0.40686 0.70511 -0.01766 -0.17924 0.00757  47  GLU A CA  
261  C C   . GLU A 40  ? 0.27533 0.38809 0.69322 -0.00032 -0.15308 -0.00366 47  GLU A C   
262  O O   . GLU A 40  ? 0.30467 0.42999 0.72622 -0.00665 -0.14128 -0.00830 47  GLU A O   
263  C CB  . GLU A 40  ? 0.30538 0.45198 0.75024 -0.02194 -0.19655 0.02503  47  GLU A CB  
264  C CG  . GLU A 40  ? 0.34180 0.47550 0.76262 -0.04987 -0.22862 0.03833  47  GLU A CG  
265  C CD  . GLU A 40  ? 0.49945 0.60064 0.87461 -0.07482 -0.23152 0.03331  47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.34369 0.47199 0.74154 -0.07838 -0.21577 0.03051  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.64051 0.68255 0.95039 -0.08903 -0.24832 0.03238  47  GLU A OE2 
268  N N   . LEU A 41  ? 0.26940 0.37451 0.69539 0.01984  -0.14532 -0.00778 48  LEU A N   
269  C CA  . LEU A 41  ? 0.26573 0.37130 0.69917 0.03345  -0.12470 -0.01892 48  LEU A CA  
270  C C   . LEU A 41  ? 0.25419 0.33132 0.65278 0.02581  -0.11579 -0.02853 48  LEU A C   
271  O O   . LEU A 41  ? 0.26898 0.35121 0.66738 0.02592  -0.10242 -0.03641 48  LEU A O   
272  C CB  . LEU A 41  ? 0.41440 0.50715 0.85576 0.05371  -0.12255 -0.01987 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.31462 0.43947 0.79516 0.07044  -0.12442 -0.00939 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.29462 0.39239 0.77070 0.09354  -0.11793 -0.01327 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.26873 0.43712 0.78039 0.07394  -0.11105 -0.00579 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.26077 0.30915 0.62917 0.02130  -0.12172 -0.02545 49  ILE A N   
277  C CA  . ILE A 42  ? 0.26418 0.29378 0.60540 0.01736  -0.11209 -0.02847 49  ILE A CA  
278  C C   . ILE A 42  ? 0.26052 0.29208 0.58611 0.00542  -0.10897 -0.03049 49  ILE A C   
279  O O   . ILE A 42  ? 0.25426 0.28431 0.57087 0.00371  -0.09793 -0.03516 49  ILE A O   
280  C CB  . ILE A 42  ? 0.38570 0.38906 0.70091 0.02078  -0.11437 -0.01921 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.26922 0.26897 0.59951 0.02924  -0.11690 -0.01568 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.26951 0.26203 0.56122 0.02009  -0.10254 -0.01593 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.28479 0.26454 0.59541 0.03364  -0.12016 -0.00270 49  ILE A CD1 
284  N N   . SER A 43  ? 0.30276 0.33470 0.62212 -0.00532 -0.12123 -0.02552 50  SER A N   
285  C CA  . SER A 43  ? 0.35297 0.37930 0.65222 -0.02087 -0.12148 -0.02596 50  SER A CA  
286  C C   . SER A 43  ? 0.26895 0.33023 0.59987 -0.02356 -0.11048 -0.03063 50  SER A C   
287  O O   . SER A 43  ? 0.27140 0.32459 0.58391 -0.02981 -0.10125 -0.03445 50  SER A O   
288  C CB  . SER A 43  ? 0.31796 0.33430 0.60259 -0.03773 -0.14315 -0.01730 50  SER A CB  
289  O OG  . SER A 43  ? 0.40453 0.42121 0.67863 -0.05799 -0.14702 -0.01563 50  SER A OG  
290  N N   . ASN A 44  ? 0.25561 0.35347 0.63071 -0.01572 -0.10903 -0.02892 51  ASN A N   
291  C CA  . ASN A 44  ? 0.24556 0.37260 0.64515 -0.01152 -0.09282 -0.03239 51  ASN A CA  
292  C C   . ASN A 44  ? 0.24128 0.34750 0.62183 -0.00073 -0.07764 -0.04498 51  ASN A C   
293  O O   . ASN A 44  ? 0.24207 0.35445 0.61894 -0.00199 -0.06452 -0.04979 51  ASN A O   
294  C CB  . ASN A 44  ? 0.24205 0.40905 0.68857 0.00217  -0.09037 -0.02480 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.24711 0.44681 0.72172 -0.01228 -0.10888 -0.00677 51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.25882 0.44968 0.71462 -0.03704 -0.12281 -0.00139 51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.24559 0.47972 0.76200 0.00251  -0.11101 0.00446  51  ASN A ND2 
298  N N   . SER A 45  ? 0.24116 0.32294 0.60883 0.00760  -0.08105 -0.04804 52  SER A N   
299  C CA  . SER A 45  ? 0.24258 0.30434 0.59091 0.01079  -0.07364 -0.05535 52  SER A CA  
300  C C   . SER A 45  ? 0.24128 0.29139 0.56301 0.00071  -0.07149 -0.05339 52  SER A C   
301  O O   . SER A 45  ? 0.24342 0.28990 0.55343 -0.00107 -0.06385 -0.05802 52  SER A O   
302  C CB  . SER A 45  ? 0.24641 0.28937 0.59246 0.01752  -0.08092 -0.05347 52  SER A CB  
303  O OG  . SER A 45  ? 0.25640 0.30129 0.61973 0.03003  -0.08106 -0.05613 52  SER A OG  
304  N N   . SER A 46  ? 0.24598 0.28454 0.55162 -0.00396 -0.07785 -0.04580 53  SER A N   
305  C CA  . SER A 46  ? 0.25563 0.27658 0.52925 -0.00858 -0.07292 -0.04245 53  SER A CA  
306  C C   . SER A 46  ? 0.26083 0.28878 0.53002 -0.01940 -0.06780 -0.04664 53  SER A C   
307  O O   . SER A 46  ? 0.26868 0.28530 0.51540 -0.02089 -0.06015 -0.04652 53  SER A O   
308  C CB  . SER A 46  ? 0.29409 0.28766 0.53777 -0.00790 -0.07894 -0.03410 53  SER A CB  
309  O OG  . SER A 46  ? 0.34829 0.31759 0.55540 -0.00316 -0.06973 -0.02837 53  SER A OG  
310  N N   . ASP A 47  ? 0.26000 0.30997 0.55285 -0.02689 -0.07170 -0.04692 54  ASP A N   
311  C CA  . ASP A 47  ? 0.26588 0.32931 0.56073 -0.03894 -0.06564 -0.04683 54  ASP A CA  
312  C C   . ASP A 47  ? 0.25742 0.33532 0.56227 -0.03056 -0.04979 -0.05437 54  ASP A C   
313  O O   . ASP A 47  ? 0.26542 0.34126 0.55558 -0.03741 -0.04108 -0.05534 54  ASP A O   
314  C CB  . ASP A 47  ? 0.32313 0.41613 0.64853 -0.05078 -0.07514 -0.03798 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.36030 0.42775 0.66120 -0.06615 -0.09563 -0.03018 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.33247 0.35370 0.58534 -0.06452 -0.09718 -0.03268 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.29945 0.39145 0.62630 -0.07887 -0.11028 -0.01953 54  ASP A OD2 
318  N N   . ALA A 48  ? 0.25055 0.33479 0.57189 -0.01598 -0.04653 -0.05976 55  ALA A N   
319  C CA  . ALA A 48  ? 0.25898 0.34127 0.57397 -0.00754 -0.03316 -0.06827 55  ALA A CA  
320  C C   . ALA A 48  ? 0.26387 0.32070 0.54651 -0.01095 -0.03425 -0.07145 55  ALA A C   
321  O O   . ALA A 48  ? 0.27645 0.32824 0.54153 -0.01250 -0.02518 -0.07574 55  ALA A O   
322  C CB  . ALA A 48  ? 0.26645 0.34644 0.59396 0.00904  -0.03142 -0.07326 55  ALA A CB  
323  N N   . LEU A 49  ? 0.25677 0.30056 0.53255 -0.01130 -0.04480 -0.06623 56  LEU A N   
324  C CA  . LEU A 49  ? 0.26046 0.29138 0.51502 -0.01358 -0.04661 -0.06205 56  LEU A CA  
325  C C   . LEU A 49  ? 0.26605 0.29276 0.49992 -0.01892 -0.04012 -0.05792 56  LEU A C   
326  O O   . LEU A 49  ? 0.27458 0.29598 0.49128 -0.02049 -0.03733 -0.05664 56  LEU A O   
327  C CB  . LEU A 49  ? 0.25286 0.28000 0.51208 -0.01014 -0.05576 -0.05106 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.25402 0.27834 0.52824 -0.00765 -0.06446 -0.05304 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.24530 0.27064 0.52981 -0.00348 -0.07032 -0.04139 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.26926 0.28360 0.53290 -0.01401 -0.07177 -0.05218 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.35077 0.37447 0.58095 -0.02323 -0.03995 -0.05485 57  ASP A N   
332  C CA  . ASP A 50  ? 0.29315 0.30088 0.49446 -0.02971 -0.03493 -0.05101 57  ASP A CA  
333  C C   . ASP A 50  ? 0.36251 0.37945 0.56193 -0.03662 -0.02573 -0.05654 57  ASP A C   
334  O O   . ASP A 50  ? 0.34018 0.34301 0.51319 -0.03855 -0.02042 -0.05376 57  ASP A O   
335  C CB  . ASP A 50  ? 0.30181 0.29490 0.49190 -0.03867 -0.04134 -0.04732 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.43878 0.40526 0.60678 -0.02912 -0.04631 -0.04024 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.44335 0.40605 0.60444 -0.01485 -0.04083 -0.03392 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.40608 0.35616 0.56278 -0.03606 -0.05594 -0.03846 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.45440 0.49419 0.67961 -0.03735 -0.02148 -0.06244 58  LYS A N   
340  C CA  . LYS A 51  ? 0.54418 0.59375 0.76615 -0.04133 -0.00832 -0.06511 58  LYS A CA  
341  C C   . LYS A 51  ? 0.43949 0.47515 0.63870 -0.03433 -0.00369 -0.07148 58  LYS A C   
342  O O   . LYS A 51  ? 0.39126 0.41826 0.56663 -0.03881 0.00360  -0.07076 58  LYS A O   
343  C CB  . LYS A 51  ? 0.45514 0.53655 0.71227 -0.03834 -0.00069 -0.06487 58  LYS A CB  
344  C CG  . LYS A 51  ? 0.40370 0.50588 0.68768 -0.05056 -0.00988 -0.05413 58  LYS A CG  
345  C CD  . LYS A 51  ? 0.68982 0.76679 0.94463 -0.06940 -0.01980 -0.04780 58  LYS A CD  
346  C CE  . LYS A 51  ? 0.76524 0.84823 1.03392 -0.08487 -0.03685 -0.03782 58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.59113 0.62864 0.82104 -0.08543 -0.05063 -0.03892 58  LYS A NZ  
348  N N   . ILE A 52  ? 0.40155 0.43078 0.60366 -0.02581 -0.01050 -0.07651 59  ILE A N   
349  C CA  . ILE A 52  ? 0.32854 0.33833 0.50301 -0.02471 -0.01305 -0.08073 59  ILE A CA  
350  C C   . ILE A 52  ? 0.32576 0.32914 0.48510 -0.02972 -0.02188 -0.07003 59  ILE A C   
351  O O   . ILE A 52  ? 0.34582 0.33797 0.47947 -0.03288 -0.02292 -0.06910 59  ILE A O   
352  C CB  . ILE A 52  ? 0.33890 0.33523 0.51430 -0.01899 -0.02222 -0.08708 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.37879 0.34469 0.51419 -0.02175 -0.02691 -0.09316 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.31695 0.31788 0.51087 -0.02113 -0.03825 -0.07783 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.40971 0.36541 0.51775 -0.01678 -0.00797 -0.10132 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.30715 0.31612 0.47878 -0.02801 -0.02697 -0.05985 60  ARG A N   
357  C CA  . ARG A 53  ? 0.30975 0.31493 0.46783 -0.02561 -0.03013 -0.04538 60  ARG A CA  
358  C C   . ARG A 53  ? 0.38411 0.37733 0.51546 -0.02798 -0.01986 -0.04376 60  ARG A C   
359  O O   . ARG A 53  ? 0.40905 0.39781 0.52182 -0.02706 -0.02062 -0.03646 60  ARG A O   
360  C CB  . ARG A 53  ? 0.32202 0.32929 0.49124 -0.01743 -0.03248 -0.03388 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.30873 0.30877 0.45883 -0.00736 -0.02757 -0.01637 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.33244 0.33703 0.49275 0.00607  -0.02763 -0.00066 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.78214 0.76084 0.92325 0.01072  -0.02155 -0.00447 60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.77918 0.73183 0.88867 0.02661  -0.01169 0.00804  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.47661 0.43368 0.57744 0.04368  -0.00300 0.02777  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.81239 0.73072 0.89434 0.02652  -0.01081 0.00241  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.45919 0.44657 0.58781 -0.03322 -0.01252 -0.04817 61  TYR A N   
368  C CA  . TYR A 54  ? 0.40001 0.37041 0.49997 -0.03944 -0.00416 -0.04550 61  TYR A CA  
369  C C   . TYR A 54  ? 0.40633 0.38074 0.49592 -0.04399 0.00265  -0.05112 61  TYR A C   
370  O O   . TYR A 54  ? 0.38762 0.34677 0.44839 -0.04533 0.00715  -0.04585 61  TYR A O   
371  C CB  . TYR A 54  ? 0.36077 0.32528 0.46214 -0.05141 -0.00285 -0.04665 61  TYR A CB  
372  C CG  . TYR A 54  ? 0.38951 0.33775 0.46448 -0.06466 0.00441  -0.04365 61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.46931 0.43856 0.55631 -0.07382 0.01396  -0.04692 61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.42274 0.32988 0.45559 -0.06623 0.00361  -0.03590 61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.54468 0.50105 0.60914 -0.08795 0.02098  -0.04119 61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.49557 0.38130 0.49972 -0.08089 0.00861  -0.03210 61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.45124 0.36502 0.47463 -0.09360 0.01654  -0.03408 61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.48599 0.38061 0.48259 -0.11022 0.02191  -0.02745 61  TYR A OH  
379  N N   . GLU A 55  ? 0.45295 0.44197 0.55924 -0.04391 0.00494  -0.06127 62  GLU A N   
380  C CA  . GLU A 55  ? 0.49294 0.47714 0.57885 -0.04488 0.01427  -0.06727 62  GLU A CA  
381  C C   . GLU A 55  ? 0.51906 0.48755 0.57814 -0.04283 0.00372  -0.06480 62  GLU A C   
382  O O   . GLU A 55  ? 0.49508 0.45015 0.52293 -0.04537 0.00900  -0.06482 62  GLU A O   
383  C CB  . GLU A 55  ? 0.38769 0.38268 0.48943 -0.03910 0.02242  -0.07756 62  GLU A CB  
384  C CG  . GLU A 55  ? 0.39111 0.41168 0.52031 -0.04231 0.03651  -0.07444 62  GLU A CG  
385  C CD  . GLU A 55  ? 0.49064 0.52305 0.62991 -0.02947 0.05236  -0.08041 62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.54797 0.55444 0.65763 -0.01897 0.05312  -0.09037 62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.54236 0.60775 0.71629 -0.02941 0.06359  -0.07305 62  GLU A OE2 
388  N N   . SER A 56  ? 0.38823 0.36033 0.45987 -0.04007 -0.01259 -0.05970 63  SER A N   
389  C CA  . SER A 56  ? 0.46325 0.42865 0.51720 -0.04261 -0.02801 -0.05128 63  SER A CA  
390  C C   . SER A 56  ? 0.47739 0.44502 0.52053 -0.03941 -0.02811 -0.03397 63  SER A C   
391  O O   . SER A 56  ? 0.53703 0.50421 0.56590 -0.04203 -0.04074 -0.02300 63  SER A O   
392  C CB  . SER A 56  ? 0.39186 0.36691 0.46920 -0.04389 -0.04645 -0.04557 63  SER A CB  
393  O OG  . SER A 56  ? 0.36095 0.35514 0.46761 -0.03643 -0.04552 -0.03305 63  SER A OG  
394  N N   . LEU A 57  ? 0.43907 0.40463 0.48406 -0.03384 -0.01585 -0.02980 64  LEU A N   
395  C CA  . LEU A 57  ? 0.45036 0.40708 0.47530 -0.02591 -0.01260 -0.01331 64  LEU A CA  
396  C C   . LEU A 57  ? 0.50840 0.44820 0.49804 -0.03164 -0.00701 -0.01523 64  LEU A C   
397  O O   . LEU A 57  ? 0.63461 0.56938 0.60567 -0.02492 -0.00950 0.00028  64  LEU A O   
398  C CB  . LEU A 57  ? 0.47852 0.41937 0.49827 -0.01920 -0.00191 -0.01041 64  LEU A CB  
399  C CG  . LEU A 57  ? 0.47359 0.42468 0.52034 -0.01267 -0.00548 -0.00901 64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.40895 0.32891 0.43154 -0.00532 0.00321  -0.00472 64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.37587 0.35294 0.44615 -0.00238 -0.01557 0.00779  64  LEU A CD2 
402  N N   . THR A 58  ? 0.53444 0.46731 0.51497 -0.04168 0.00227  -0.03122 65  THR A N   
403  C CA  . THR A 58  ? 0.50771 0.42403 0.45225 -0.04697 0.00980  -0.03304 65  THR A CA  
404  C C   . THR A 58  ? 0.58184 0.49292 0.50945 -0.05065 0.00296  -0.04227 65  THR A C   
405  O O   . THR A 58  ? 0.63546 0.52878 0.52517 -0.05332 0.00332  -0.04035 65  THR A O   
406  C CB  . THR A 58  ? 0.58611 0.49679 0.52622 -0.05514 0.02895  -0.03936 65  THR A CB  
407  O OG1 . THR A 58  ? 0.64015 0.57021 0.61603 -0.05740 0.03231  -0.04810 65  THR A OG1 
408  C CG2 . THR A 58  ? 0.50914 0.40014 0.43232 -0.05652 0.03325  -0.02807 65  THR A CG2 
409  N N   . ASP A 59  ? 0.65216 0.66166 0.66282 0.13527  -0.00425 0.09671  66  ASP A N   
410  C CA  . ASP A 59  ? 0.64055 0.64756 0.61534 0.13262  -0.02984 0.09205  66  ASP A CA  
411  C C   . ASP A 59  ? 0.53283 0.56697 0.53101 0.11723  -0.05711 0.08461  66  ASP A C   
412  O O   . ASP A 59  ? 0.57918 0.61083 0.58388 0.10309  -0.05724 0.06798  66  ASP A O   
413  C CB  . ASP A 59  ? 0.57591 0.55322 0.51661 0.12997  -0.01626 0.07905  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.68297 0.63996 0.56749 0.13314  -0.03542 0.07552  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.60217 0.57100 0.47672 0.12994  -0.06663 0.07960  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.68084 0.60868 0.52970 0.13835  -0.01899 0.06973  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.58233 0.64548 0.59732 0.11935  -0.08073 0.09965  67  PRO A N   
418  C CA  . PRO A 60  ? 0.46370 0.55620 0.50668 0.10200  -0.10733 0.09607  67  PRO A CA  
419  C C   . PRO A 60  ? 0.46353 0.53483 0.46536 0.08574  -0.13131 0.07897  67  PRO A C   
420  O O   . PRO A 60  ? 0.46805 0.55310 0.49030 0.06791  -0.14750 0.07114  67  PRO A O   
421  C CB  . PRO A 60  ? 0.45110 0.58238 0.52094 0.10968  -0.12791 0.12246  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.46058 0.58369 0.53125 0.13423  -0.10080 0.13874  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.48104 0.55662 0.49944 0.13794  -0.08232 0.12464  67  PRO A CD  
424  N N   . SER A 61  ? 0.68097 0.71393 0.62166 0.09222  -0.13141 0.07337  68  SER A N   
425  C CA  . SER A 61  ? 0.63650 0.63569 0.52608 0.07982  -0.14909 0.05571  68  SER A CA  
426  C C   . SER A 61  ? 0.60932 0.59133 0.50527 0.07364  -0.12882 0.03674  68  SER A C   
427  O O   . SER A 61  ? 0.71711 0.66860 0.57560 0.06427  -0.13994 0.02191  68  SER A O   
428  C CB  . SER A 61  ? 0.70990 0.66601 0.52469 0.09267  -0.14812 0.05579  68  SER A CB  
429  O OG  . SER A 61  ? 0.80184 0.74386 0.61359 0.11146  -0.10956 0.05928  68  SER A OG  
430  N N   . LYS A 62  ? 0.47117 0.46856 0.40982 0.07839  -0.10012 0.03771  69  LYS A N   
431  C CA  . LYS A 62  ? 0.55006 0.53954 0.50107 0.07130  -0.08503 0.02374  69  LYS A CA  
432  C C   . LYS A 62  ? 0.58742 0.59673 0.56950 0.05286  -0.10424 0.01783  69  LYS A C   
433  O O   . LYS A 62  ? 0.56562 0.55969 0.54155 0.04539  -0.10247 0.00567  69  LYS A O   
434  C CB  . LYS A 62  ? 0.40728 0.40709 0.39124 0.07704  -0.05413 0.02760  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.43298 0.41047 0.38875 0.09251  -0.03150 0.03380  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.40224 0.38851 0.39176 0.09199  -0.00510 0.03829  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.45015 0.41555 0.41652 0.10436  0.01877  0.04626  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.58554 0.55341 0.57213 0.09825  0.03880  0.04432  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.51364 0.55752 0.53108 0.04689  -0.12075 0.02908  70  LEU A N   
440  C CA  . LEU A 63  ? 0.42151 0.48793 0.47251 0.02892  -0.13807 0.02752  70  LEU A CA  
441  C C   . LEU A 63  ? 0.42780 0.48066 0.44899 0.01310  -0.17296 0.02344  70  LEU A C   
442  O O   . LEU A 63  ? 0.41745 0.48951 0.46756 -0.00495 -0.19072 0.02472  70  LEU A O   
443  C CB  . LEU A 63  ? 0.35932 0.47118 0.46618 0.03093  -0.13614 0.04492  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.41843 0.53717 0.55517 0.03703  -0.10464 0.04375  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.29261 0.44865 0.47763 0.04104  -0.09996 0.06078  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.29397 0.40071 0.43120 0.02465  -0.09884 0.02832  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.48310 0.49931 0.44326 0.01795  -0.18287 0.01876  71  ASP A N   
448  C CA  . ASP A 64  ? 0.54128 0.53027 0.45707 -0.00009 -0.21749 0.01144  71  ASP A CA  
449  C C   . ASP A 64  ? 0.61198 0.56924 0.51460 -0.01393 -0.21706 -0.00649 71  ASP A C   
450  O O   . ASP A 64  ? 0.58905 0.52993 0.47229 -0.03630 -0.24766 -0.01171 71  ASP A O   
451  C CB  . ASP A 64  ? 0.60998 0.55268 0.44772 0.01091  -0.22164 0.00725  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.61555 0.58712 0.45992 0.02225  -0.22989 0.02782  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.57083 0.59834 0.48121 0.02095  -0.23520 0.04604  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.71964 0.65620 0.50171 0.03480  -0.22850 0.02751  71  ASP A OD2 
455  N N   . SER A 65  ? 0.53654 0.48431 0.44956 -0.00225 -0.18432 -0.01422 72  SER A N   
456  C CA  . SER A 65  ? 0.52412 0.44374 0.42885 -0.01043 -0.17934 -0.02759 72  SER A CA  
457  C C   . SER A 65  ? 0.49703 0.45777 0.46707 -0.02462 -0.18136 -0.02213 72  SER A C   
458  O O   . SER A 65  ? 0.47327 0.42095 0.44971 -0.02617 -0.16869 -0.02910 72  SER A O   
459  C CB  . SER A 65  ? 0.54913 0.44219 0.43429 0.01085  -0.14380 -0.03396 72  SER A CB  
460  O OG  . SER A 65  ? 0.51379 0.44328 0.43820 0.02425  -0.12095 -0.02351 72  SER A OG  
461  N N   . GLY A 66  ? 0.43853 0.44855 0.45669 -0.03272 -0.19480 -0.00744 73  GLY A N   
462  C CA  . GLY A 66  ? 0.39159 0.44012 0.46929 -0.04324 -0.19193 0.00002  73  GLY A CA  
463  C C   . GLY A 66  ? 0.34559 0.44264 0.47314 -0.03213 -0.17734 0.01593  73  GLY A C   
464  O O   . GLY A 66  ? 0.45688 0.55374 0.58844 -0.01666 -0.14998 0.01422  73  GLY A O   
465  N N   . LYS A 67  ? 0.38481 0.52224 0.55069 -0.04032 -0.19502 0.03302  74  LYS A N   
466  C CA  . LYS A 67  ? 0.40249 0.58150 0.61292 -0.02567 -0.17831 0.05073  74  LYS A CA  
467  C C   . LYS A 67  ? 0.29590 0.49321 0.54557 -0.02550 -0.15477 0.05292  74  LYS A C   
468  O O   . LYS A 67  ? 0.24862 0.45549 0.51326 -0.00946 -0.12874 0.05833  74  LYS A O   
469  C CB  . LYS A 67  ? 0.33036 0.55162 0.57314 -0.03101 -0.20402 0.07363  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.43403 0.63796 0.63251 -0.03326 -0.23255 0.07377  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.60997 0.78572 0.77404 -0.06104 -0.26712 0.06190  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.68639 0.80735 0.77028 -0.05792 -0.27894 0.04664  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.52014 0.58709 0.55210 -0.07924 -0.29672 0.02578  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.26568 0.46164 0.52577 -0.04326 -0.16264 0.04855  75  GLU A N   
475  C CA  . GLU A 68  ? 0.28145 0.49431 0.57458 -0.04419 -0.14218 0.05270  75  GLU A CA  
476  C C   . GLU A 68  ? 0.29997 0.48382 0.56683 -0.03512 -0.11752 0.03729  75  GLU A C   
477  O O   . GLU A 68  ? 0.24272 0.39423 0.47519 -0.03735 -0.12098 0.02277  75  GLU A O   
478  C CB  . GLU A 68  ? 0.47733 0.69579 0.78815 -0.06694 -0.15899 0.05498  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.50245 0.74937 0.83763 -0.07830 -0.17752 0.07152  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.73153 0.95946 1.03264 -0.08834 -0.20907 0.06622  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.49434 0.68181 0.75128 -0.08899 -0.21916 0.04863  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.75983 1.01139 1.07607 -0.09546 -0.22413 0.08031  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.25832 0.45273 0.54047 -0.02504 -0.09246 0.04199  76  LEU A N   
484  C CA  . LEU A 69  ? 0.19607 0.36738 0.45631 -0.02106 -0.07245 0.03006  76  LEU A CA  
485  C C   . LEU A 69  ? 0.20852 0.38774 0.48404 -0.02831 -0.06161 0.03290  76  LEU A C   
486  O O   . LEU A 69  ? 0.18534 0.37984 0.47969 -0.02210 -0.04555 0.04340  76  LEU A O   
487  C CB  . LEU A 69  ? 0.19867 0.36225 0.44900 -0.00585 -0.05306 0.03083  76  LEU A CB  
488  C CG  . LEU A 69  ? 0.21186 0.37248 0.45122 0.00459  -0.06067 0.03406  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.21830 0.36690 0.44904 0.01910  -0.03789 0.03645  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.29334 0.43092 0.50150 0.00069  -0.07345 0.02215  76  LEU A CD2 
491  N N   . HIS A 70  ? 0.20589 0.37225 0.47071 -0.03905 -0.06790 0.02524  77  HIS A N   
492  C CA  . HIS A 70  ? 0.19066 0.36313 0.46635 -0.04682 -0.06024 0.02964  77  HIS A CA  
493  C C   . HIS A 70  ? 0.18385 0.33598 0.43752 -0.05239 -0.06196 0.02032  77  HIS A C   
494  O O   . HIS A 70  ? 0.18410 0.32043 0.41980 -0.04949 -0.06802 0.01210  77  HIS A O   
495  C CB  . HIS A 70  ? 0.18333 0.37659 0.48991 -0.05772 -0.07289 0.04164  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.19632 0.37681 0.49495 -0.06834 -0.09817 0.03630  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.20610 0.35822 0.48143 -0.07427 -0.10398 0.02639  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.21009 0.39690 0.51481 -0.07372 -0.11901 0.03959  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.22960 0.36402 0.49209 -0.08214 -0.12442 0.02172  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.23352 0.38822 0.51123 -0.08405 -0.13612 0.02877  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.20653 0.36083 0.46280 -0.05869 -0.05503 0.02459  78  ILE A N   
502  C CA  . ILE A 71  ? 0.26207 0.40333 0.50332 -0.06382 -0.05796 0.02138  78  ILE A CA  
503  C C   . ILE A 71  ? 0.19062 0.33545 0.44571 -0.07331 -0.06230 0.03016  78  ILE A C   
504  O O   . ILE A 71  ? 0.19241 0.35136 0.46249 -0.07600 -0.05288 0.03970  78  ILE A O   
505  C CB  . ILE A 71  ? 0.23481 0.37093 0.45618 -0.06372 -0.04589 0.01907  78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.18681 0.31588 0.39539 -0.05797 -0.04258 0.01121  78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.19306 0.32445 0.40517 -0.06975 -0.05164 0.02168  78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.20154 0.32026 0.38772 -0.06165 -0.03071 0.00820  78  ILE A CD1 
509  N N   . ASN A 72  ? 0.19878 0.32822 0.44846 -0.07702 -0.07358 0.02860  79  ASN A N   
510  C CA  . ASN A 72  ? 0.30351 0.42869 0.56265 -0.08700 -0.07737 0.03726  79  ASN A CA  
511  C C   . ASN A 72  ? 0.31047 0.42410 0.55413 -0.08493 -0.07430 0.04009  79  ASN A C   
512  O O   . ASN A 72  ? 0.33932 0.44506 0.56929 -0.07670 -0.07557 0.03520  79  ASN A O   
513  C CB  . ASN A 72  ? 0.22867 0.33670 0.49091 -0.09486 -0.09392 0.03488  79  ASN A CB  
514  C CG  . ASN A 72  ? 0.26440 0.39043 0.54658 -0.10077 -0.10268 0.03695  79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.25514 0.41070 0.55958 -0.09882 -0.09285 0.04560  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.24852 0.35499 0.52025 -0.10725 -0.12097 0.03045  79  ASN A ND2 
517  N N   . LEU A 73  ? 0.22642 0.34241 0.47517 -0.09180 -0.06970 0.05128  80  LEU A N   
518  C CA  . LEU A 73  ? 0.26978 0.37694 0.50524 -0.09021 -0.06860 0.05857  80  LEU A CA  
519  C C   . LEU A 73  ? 0.35133 0.44055 0.59451 -0.09713 -0.07287 0.06728  80  LEU A C   
520  O O   . LEU A 73  ? 0.36091 0.45663 0.61911 -0.10746 -0.06898 0.07631  80  LEU A O   
521  C CB  . LEU A 73  ? 0.39581 0.51521 0.61871 -0.09197 -0.05792 0.06514  80  LEU A CB  
522  C CG  . LEU A 73  ? 0.30145 0.42930 0.51105 -0.08895 -0.05131 0.05594  80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.25345 0.37976 0.43657 -0.09253 -0.04096 0.06109  80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.22255 0.34932 0.42564 -0.08364 -0.05982 0.04747  80  LEU A CD2 
525  N N   . ILE A 74  ? 0.35896 0.42360 0.59228 -0.09083 -0.07852 0.06623  81  ILE A N   
526  C CA  . ILE A 74  ? 0.30491 0.33896 0.53839 -0.09725 -0.08230 0.07193  81  ILE A CA  
527  C C   . ILE A 74  ? 0.32248 0.34476 0.54642 -0.08843 -0.07734 0.08558  81  ILE A C   
528  O O   . ILE A 74  ? 0.33351 0.33936 0.54684 -0.07363 -0.07692 0.08516  81  ILE A O   
529  C CB  . ILE A 74  ? 0.32576 0.32634 0.54703 -0.09604 -0.09119 0.05869  81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.30792 0.32569 0.53655 -0.10193 -0.09846 0.04722  81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.36849 0.32886 0.58460 -0.10867 -0.09666 0.06232  81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.32784 0.31559 0.53272 -0.09538 -0.10569 0.03259  81  ILE A CD1 
533  N N   . PRO A 75  ? 0.32921 0.36015 0.55683 -0.09487 -0.07195 0.10050  82  PRO A N   
534  C CA  . PRO A 75  ? 0.35266 0.37026 0.57102 -0.08646 -0.06889 0.11693  82  PRO A CA  
535  C C   . PRO A 75  ? 0.39173 0.36446 0.60790 -0.08939 -0.06885 0.12131  82  PRO A C   
536  O O   . PRO A 75  ? 0.40395 0.36136 0.62816 -0.10635 -0.07206 0.11689  82  PRO A O   
537  C CB  . PRO A 75  ? 0.35237 0.39180 0.56855 -0.09382 -0.06240 0.13059  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.34207 0.39184 0.57383 -0.10826 -0.05830 0.12507  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.45442 0.50845 0.69374 -0.10735 -0.06566 0.10572  82  PRO A CD  
540  N N   . ASN A 76  ? 0.48087 0.43156 0.68652 -0.07303 -0.06541 0.13181  83  ASN A N   
541  C CA  . ASN A 76  ? 0.46607 0.36155 0.66088 -0.07185 -0.06207 0.13601  83  ASN A CA  
542  C C   . ASN A 76  ? 0.48950 0.37948 0.68084 -0.05707 -0.05436 0.16092  83  ASN A C   
543  O O   . ASN A 76  ? 0.60323 0.50312 0.79371 -0.03456 -0.05156 0.16946  83  ASN A O   
544  C CB  . ASN A 76  ? 0.48681 0.34481 0.66449 -0.05950 -0.06194 0.12007  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.54997 0.33699 0.70551 -0.06599 -0.06023 0.11659  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.64724 0.40470 0.79778 -0.06290 -0.05266 0.13316  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.56975 0.32449 0.70721 -0.07617 -0.06814 0.09520  83  ASN A ND2 
548  N N   . LYS A 77  ? 0.51285 0.39026 0.70535 -0.06934 -0.05069 0.17573  84  LYS A N   
549  C CA  . LYS A 77  ? 0.60528 0.47686 0.79240 -0.05525 -0.04378 0.20242  84  LYS A CA  
550  C C   . LYS A 77  ? 0.59126 0.40553 0.76555 -0.03669 -0.03535 0.20896  84  LYS A C   
551  O O   . LYS A 77  ? 0.60901 0.42691 0.78279 -0.01321 -0.02969 0.23079  84  LYS A O   
552  C CB  . LYS A 77  ? 0.55453 0.42690 0.74394 -0.07311 -0.03929 0.21793  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.51689 0.44236 0.71018 -0.08291 -0.04105 0.21803  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.53834 0.46231 0.73185 -0.09742 -0.03121 0.23594  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.56901 0.52892 0.77140 -0.11241 -0.02763 0.22716  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.63406 0.59628 0.83604 -0.12298 -0.01297 0.24804  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.64756 0.40657 0.80881 -0.04628 -0.03444 0.19157  85  GLN A N   
558  C CA  . GLN A 78  ? 0.74259 0.43174 0.88041 -0.02804 -0.02264 0.19547  85  GLN A CA  
559  C C   . GLN A 78  ? 0.68281 0.37897 0.81709 0.00474  -0.01545 0.19388  85  GLN A C   
560  O O   . GLN A 78  ? 0.75946 0.44001 0.89168 0.03394  -0.00180 0.21525  85  GLN A O   
561  C CB  . GLN A 78  ? 0.86598 0.48735 0.98094 -0.05160 -0.02652 0.17442  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.97494 0.52282 1.05170 -0.03251 -0.01666 0.16113  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.16729 0.65343 1.21400 -0.06194 -0.02806 0.13476  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.01404 0.52455 1.06235 -0.07598 -0.04262 0.11366  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.92578 0.32951 0.94294 -0.07289 -0.02307 0.13694  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.64484 0.36671 0.78156 0.00187  -0.02278 0.17193  86  ASP A N   
567  C CA  . ASP A 79  ? 0.70346 0.44050 0.84260 0.03151  -0.01448 0.17269  86  ASP A CA  
568  C C   . ASP A 79  ? 0.58032 0.39764 0.75284 0.04163  -0.01988 0.19213  86  ASP A C   
569  O O   . ASP A 79  ? 0.59899 0.43903 0.78382 0.06615  -0.01313 0.20048  86  ASP A O   
570  C CB  . ASP A 79  ? 0.68642 0.41525 0.81139 0.02431  -0.01940 0.14295  86  ASP A CB  
571  C CG  . ASP A 79  ? 0.81450 0.46374 0.90026 0.00833  -0.02057 0.12193  86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.81872 0.40477 0.88263 0.01156  -0.01106 0.12985  86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.86575 0.51337 0.94040 -0.00863 -0.03230 0.09832  86  ASP A OD2 
574  N N   . ARG A 80  ? 0.55058 0.40886 0.73567 0.02246  -0.03152 0.20049  87  ARG A N   
575  C CA  . ARG A 80  ? 0.58994 0.51738 0.79570 0.02540  -0.04109 0.21651  87  ARG A CA  
576  C C   . ARG A 80  ? 0.55081 0.51801 0.76751 0.02407  -0.04775 0.19993  87  ARG A C   
577  O O   . ARG A 80  ? 0.44551 0.45810 0.68100 0.03560  -0.05214 0.21406  87  ARG A O   
578  C CB  . ARG A 80  ? 0.53464 0.47285 0.75268 0.05273  -0.03545 0.25043  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.51529 0.51191 0.74426 0.04685  -0.05040 0.27324  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.83227 0.83525 1.07404 0.07346  -0.04611 0.31157  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.97494 0.98864 1.20545 0.06372  -0.05460 0.33275  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.84947 0.81838 1.06685 0.06989  -0.04315 0.34848  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.88345 0.78838 1.09466 0.08410  -0.02358 0.34418  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.84321 0.82623 1.04789 0.06089  -0.05085 0.36897  87  ARG A NH2 
585  N N   . THR A 81  ? 0.45101 0.40251 0.65782 0.00860  -0.04967 0.17201  88  THR A N   
586  C CA  . THR A 81  ? 0.48686 0.46658 0.70023 0.00774  -0.05365 0.15531  88  THR A CA  
587  C C   . THR A 81  ? 0.38079 0.38313 0.59297 -0.01790 -0.06364 0.13848  88  THR A C   
588  O O   . THR A 81  ? 0.39010 0.36866 0.59465 -0.03381 -0.06452 0.12855  88  THR A O   
589  C CB  . THR A 81  ? 0.44287 0.37860 0.64109 0.01971  -0.04390 0.13865  88  THR A CB  
590  O OG1 . THR A 81  ? 0.51145 0.39863 0.68788 0.00250  -0.04624 0.12189  88  THR A OG1 
591  C CG2 . THR A 81  ? 0.47779 0.38801 0.67511 0.05111  -0.02744 0.15648  88  THR A CG2 
592  N N   . LEU A 82  ? 0.36532 0.41263 0.58628 -0.02185 -0.07035 0.13721  89  LEU A N   
593  C CA  . LEU A 82  ? 0.36847 0.43300 0.58605 -0.03999 -0.07515 0.11993  89  LEU A CA  
594  C C   . LEU A 82  ? 0.30214 0.36591 0.52182 -0.03493 -0.07384 0.10251  89  LEU A C   
595  O O   . LEU A 82  ? 0.30909 0.38970 0.53757 -0.02251 -0.07265 0.10742  89  LEU A O   
596  C CB  . LEU A 82  ? 0.30516 0.40693 0.51982 -0.04901 -0.08224 0.12773  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.28729 0.39993 0.49201 -0.06476 -0.08237 0.11198  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.29195 0.38551 0.49645 -0.07356 -0.07543 0.10536  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.29502 0.42819 0.48194 -0.07431 -0.08835 0.12028  89  LEU A CD2 
600  N N   . THR A 83  ? 0.29894 0.34600 0.51281 -0.04456 -0.07426 0.08523  90  THR A N   
601  C CA  . THR A 83  ? 0.29217 0.33135 0.50172 -0.03943 -0.07350 0.06933  90  THR A CA  
602  C C   . THR A 83  ? 0.26293 0.32700 0.47634 -0.05137 -0.07674 0.05830  90  THR A C   
603  O O   . THR A 83  ? 0.25990 0.32623 0.47638 -0.06460 -0.07863 0.05592  90  THR A O   
604  C CB  . THR A 83  ? 0.32549 0.31794 0.51913 -0.03993 -0.07398 0.05952  90  THR A CB  
605  O OG1 . THR A 83  ? 0.36131 0.32095 0.54385 -0.02225 -0.06554 0.06756  90  THR A OG1 
606  C CG2 . THR A 83  ? 0.32149 0.30714 0.50467 -0.03980 -0.07673 0.04232  90  THR A CG2 
607  N N   . ILE A 84  ? 0.27129 0.35347 0.48659 -0.04564 -0.07521 0.05395  91  ILE A N   
608  C CA  . ILE A 84  ? 0.28640 0.38526 0.50182 -0.05355 -0.07537 0.04383  91  ILE A CA  
609  C C   . ILE A 84  ? 0.26700 0.35301 0.47704 -0.04624 -0.07437 0.03201  91  ILE A C   
610  O O   . ILE A 84  ? 0.30516 0.38655 0.51264 -0.03349 -0.07000 0.03302  91  ILE A O   
611  C CB  . ILE A 84  ? 0.26826 0.39264 0.48454 -0.05696 -0.07542 0.04847  91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.42495 0.55770 0.63528 -0.06666 -0.07820 0.05872  91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.19993 0.32996 0.41124 -0.06177 -0.07214 0.03681  91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.27120 0.41020 0.48762 -0.06074 -0.08300 0.07612  91  ILE A CD1 
615  N N   . VAL A 85  ? 0.26553 0.34783 0.47466 -0.05329 -0.07773 0.02356  92  VAL A N   
616  C CA  . VAL A 85  ? 0.34145 0.41018 0.54049 -0.04826 -0.08031 0.01343  92  VAL A CA  
617  C C   . VAL A 85  ? 0.34369 0.43292 0.54890 -0.05042 -0.07785 0.00970  92  VAL A C   
618  O O   . VAL A 85  ? 0.42831 0.53407 0.64477 -0.05814 -0.07542 0.01318  92  VAL A O   
619  C CB  . VAL A 85  ? 0.30388 0.34764 0.49533 -0.05612 -0.09126 0.00939  92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.28054 0.29672 0.44608 -0.04867 -0.09535 -0.00093 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.28016 0.30274 0.46888 -0.05904 -0.09196 0.01564  92  VAL A CG2 
622  N N   . ASP A 86  ? 0.30050 0.38492 0.49577 -0.04148 -0.07544 0.00398  93  ASP A N   
623  C CA  . ASP A 86  ? 0.25881 0.35494 0.45683 -0.04101 -0.07308 0.00119  93  ASP A CA  
624  C C   . ASP A 86  ? 0.21776 0.29741 0.39905 -0.03355 -0.07848 -0.00446 93  ASP A C   
625  O O   . ASP A 86  ? 0.23973 0.29556 0.40152 -0.02669 -0.07935 -0.00786 93  ASP A O   
626  C CB  . ASP A 86  ? 0.24748 0.35518 0.44654 -0.03931 -0.06188 0.00215  93  ASP A CB  
627  C CG  . ASP A 86  ? 0.21225 0.31511 0.40511 -0.03068 -0.05697 0.00286  93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.20937 0.30200 0.39151 -0.02139 -0.05430 -0.00035 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.18805 0.29990 0.38820 -0.03278 -0.05537 0.00925  93  ASP A OD2 
630  N N   . THR A 87  ? 0.40239 0.33293 0.17155 0.02610  0.09551  0.08148  94  THR A N   
631  C CA  . THR A 87  ? 0.36725 0.32260 0.17158 0.00691  0.09852  0.08070  94  THR A CA  
632  C C   . THR A 87  ? 0.36247 0.31118 0.18236 0.01700  0.11123  0.07744  94  THR A C   
633  O O   . THR A 87  ? 0.34062 0.31051 0.18368 0.00819  0.11194  0.07698  94  THR A O   
634  C CB  . THR A 87  ? 0.54173 0.52448 0.35283 -0.00915 0.09381  0.08362  94  THR A CB  
635  O OG1 . THR A 87  ? 0.37313 0.35376 0.17027 0.00199  0.09415  0.08576  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.36737 0.35443 0.17092 -0.02265 0.09120  0.08897  94  THR A CG2 
637  N N   . GLY A 88  ? 0.42358 0.33887 0.22570 0.03612  0.12308  0.07433  95  GLY A N   
638  C CA  . GLY A 88  ? 0.39227 0.29831 0.21871 0.04269  0.13997  0.06757  95  GLY A CA  
639  C C   . GLY A 88  ? 0.37039 0.27971 0.24170 0.03061  0.15386  0.06705  95  GLY A C   
640  O O   . GLY A 88  ? 0.39839 0.32283 0.27586 0.01826  0.14533  0.07135  95  GLY A O   
641  N N   . ILE A 89  ? 0.36940 0.27213 0.29136 0.03246  0.15547  0.04977  96  ILE A N   
642  C CA  . ILE A 89  ? 0.43439 0.33868 0.40279 0.02384  0.17511  0.05148  96  ILE A CA  
643  C C   . ILE A 89  ? 0.37445 0.27711 0.35659 0.01898  0.16655  0.04686  96  ILE A C   
644  O O   . ILE A 89  ? 0.43151 0.33565 0.43337 0.01284  0.18600  0.05514  96  ILE A O   
645  C CB  . ILE A 89  ? 0.41175 0.30711 0.43791 0.02517  0.18196  0.03377  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.34849 0.24350 0.41140 0.01963  0.21599  0.04633  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.36826 0.26104 0.43618 0.02599  0.15491  0.00442  96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.36064 0.24159 0.47396 0.01992  0.23338  0.03603  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.36174 0.25934 0.32941 0.02506  0.13977  0.03528  97  GLY A N   
650  C CA  . GLY A 90  ? 0.36253 0.25615 0.34363 0.02451  0.13322  0.03150  97  GLY A CA  
651  C C   . GLY A 90  ? 0.41324 0.31275 0.46808 0.02541  0.13241  0.01280  97  GLY A C   
652  O O   . GLY A 90  ? 0.47601 0.38016 0.57361 0.02466  0.13323  -0.00115 97  GLY A O   
653  N N   . MET A 91  ? 0.35722 0.25567 0.42927 0.02677  0.13215  0.01219  98  MET A N   
654  C CA  . MET A 91  ? 0.35261 0.26265 0.50084 0.02811  0.13263  -0.00385 98  MET A CA  
655  C C   . MET A 91  ? 0.34667 0.25216 0.50735 0.02534  0.15718  0.00939  98  MET A C   
656  O O   . MET A 91  ? 0.35569 0.24723 0.46744 0.02747  0.15761  0.02110  98  MET A O   
657  C CB  . MET A 91  ? 0.36854 0.28899 0.53537 0.04189  0.09690  -0.02591 98  MET A CB  
658  C CG  . MET A 91  ? 0.38823 0.30267 0.49889 0.05227  0.06972  -0.03125 98  MET A CG  
659  S SD  . MET A 91  ? 0.41526 0.34653 0.54758 0.07344  0.02446  -0.06152 98  MET A SD  
660  C CE  . MET A 91  ? 0.44503 0.35260 0.47251 0.08981  0.01030  -0.04601 98  MET A CE  
661  N N   . THR A 92  ? 0.33731 0.25124 0.56350 0.02105  0.17954  0.00699  99  THR A N   
662  C CA  . THR A 92  ? 0.33694 0.24668 0.58115 0.02220  0.20582  0.01843  99  THR A CA  
663  C C   . THR A 92  ? 0.34445 0.26432 0.62558 0.03302  0.18922  0.00600  99  THR A C   
664  O O   . THR A 92  ? 0.35924 0.29294 0.65545 0.04013  0.15622  -0.01225 99  THR A O   
665  C CB  . THR A 92  ? 0.43749 0.35099 0.73843 0.01653  0.24071  0.02363  99  THR A CB  
666  O OG1 . THR A 92  ? 0.35140 0.28446 0.74118 0.01481  0.23354  0.00259  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.33193 0.23378 0.59342 0.01150  0.24358  0.03182  99  THR A CG2 
668  N N   . LYS A 93  ? 0.40354 0.31714 0.69610 0.03774  0.21244  0.01630  100 LYS A N   
669  C CA  . LYS A 93  ? 0.42142 0.34771 0.75603 0.05128  0.20165  0.00693  100 LYS A CA  
670  C C   . LYS A 93  ? 0.34790 0.31024 0.78540 0.05001  0.19570  -0.01270 100 LYS A C   
671  O O   . LYS A 93  ? 0.35386 0.34034 0.82936 0.06155  0.16837  -0.02918 100 LYS A O   
672  C CB  . LYS A 93  ? 0.37095 0.27929 0.69295 0.05823  0.23241  0.02307  100 LYS A CB  
673  C CG  . LYS A 93  ? 0.39069 0.29644 0.70950 0.07662  0.21880  0.01991  100 LYS A CG  
674  C CD  . LYS A 93  ? 0.39786 0.31254 0.77114 0.08516  0.24530  0.02517  100 LYS A CD  
675  C CE  . LYS A 93  ? 0.42790 0.31815 0.75930 0.10424  0.24721  0.03204  100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.45944 0.35000 0.80862 0.10498  0.27096  0.04313  100 LYS A NZ  
677  N N   . ALA A 94  ? 0.36082 0.32775 0.84547 0.03656  0.22101  -0.01168 101 ALA A N   
678  C CA  . ALA A 94  ? 0.33387 0.33063 0.91635 0.02820  0.21464  -0.03243 101 ALA A CA  
679  C C   . ALA A 94  ? 0.33343 0.34756 0.92611 0.02716  0.17239  -0.06013 101 ALA A C   
680  O O   . ALA A 94  ? 0.33543 0.38309 1.00970 0.02502  0.15239  -0.08613 101 ALA A O   
681  C CB  . ALA A 94  ? 0.34736 0.31896 0.93687 0.00981  0.24287  -0.02000 101 ALA A CB  
682  N N   . ASP A 95  ? 0.36443 0.35650 0.87134 0.02803  0.15640  -0.05553 102 ASP A N   
683  C CA  . ASP A 95  ? 0.34715 0.34933 0.84265 0.03131  0.11398  -0.07976 102 ASP A CA  
684  C C   . ASP A 95  ? 0.36096 0.38450 0.85669 0.05091  0.07611  -0.09356 102 ASP A C   
685  O O   . ASP A 95  ? 0.37166 0.42463 0.91461 0.05537  0.04216  -0.12288 102 ASP A O   
686  C CB  . ASP A 95  ? 0.35075 0.32439 0.75088 0.03112  0.11070  -0.06670 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.34683 0.30921 0.75689 0.01701  0.13011  -0.06660 102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.51612 0.49037 0.98512 0.01057  0.11798  -0.09240 102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.34010 0.28195 0.69965 0.01311  0.15713  -0.04179 102 ASP A OD2 
690  N N   . LEU A 96  ? 0.36658 0.37459 0.80784 0.06424  0.08099  -0.07368 103 LEU A N   
691  C CA  . LEU A 96  ? 0.38600 0.40919 0.82190 0.08778  0.05038  -0.08176 103 LEU A CA  
692  C C   . LEU A 96  ? 0.40011 0.46556 0.94103 0.09188  0.04995  -0.09649 103 LEU A C   
693  O O   . LEU A 96  ? 0.65064 0.75544 1.25100 0.09653  0.01682  -0.12517 103 LEU A O   
694  C CB  . LEU A 96  ? 0.50134 0.48820 0.85283 0.09899  0.06273  -0.05546 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.43999 0.39037 0.70245 0.08813  0.07088  -0.03932 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.40341 0.31883 0.61076 0.08281  0.10190  -0.01353 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.42516 0.36814 0.62633 0.10316  0.03681  -0.04503 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.37233 0.43284 0.94016 0.09009  0.08665  -0.07860 104 ILE A N   
699  C CA  . ILE A 97  ? 0.43602 0.53875 1.11308 0.09173  0.09494  -0.08916 104 ILE A CA  
700  C C   . ILE A 97  ? 0.62345 0.73728 1.37771 0.06508  0.11866  -0.09770 104 ILE A C   
701  O O   . ILE A 97  ? 0.89671 0.97865 1.62764 0.05175  0.15962  -0.07554 104 ILE A O   
702  C CB  . ILE A 97  ? 0.37135 0.46075 1.04236 0.10454  0.12824  -0.06516 104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.39479 0.44776 0.96108 0.12487  0.11651  -0.05033 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.40773 0.54428 1.17064 0.11134  0.12423  -0.07513 104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.41026 0.40928 0.89282 0.11587  0.15050  -0.02458 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.43166 0.58698 1.26929 0.05717  0.09115  -0.13001 105 ASN A N   
707  C CA  . ASN A 98  ? 0.34991 0.51263 1.26502 0.02880  0.10644  -0.14403 105 ASN A CA  
708  C C   . ASN A 98  ? 0.34782 0.49957 1.24829 0.01660  0.08997  -0.16355 105 ASN A C   
709  O O   . ASN A 98  ? 0.41478 0.59213 1.33126 0.01961  0.04344  -0.19621 105 ASN A O   
710  C CB  . ASN A 98  ? 0.35978 0.47935 1.25824 0.01285  0.15998  -0.11218 105 ASN A CB  
711  C CG  . ASN A 98  ? 0.40114 0.52546 1.30876 0.02280  0.17643  -0.09401 105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.59818 0.76338 1.57440 0.02747  0.15838  -0.11042 105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.37986 0.46402 1.21595 0.02730  0.20915  -0.06110 105 ASN A ND2 
714  N N   . ASN A 99  ? 0.46457 0.57230 1.31717 0.00413  0.12533  -0.14244 106 ASN A N   
715  C CA  . ASN A 99  ? 0.51739 0.60430 1.35909 -0.01162 0.12239  -0.15592 106 ASN A CA  
716  C C   . ASN A 99  ? 0.36850 0.46433 1.17384 -0.00387 0.06716  -0.18612 106 ASN A C   
717  O O   . ASN A 99  ? 0.49264 0.61588 1.36940 -0.01278 0.04006  -0.22330 106 ASN A O   
718  C CB  . ASN A 99  ? 0.34445 0.38344 1.09753 -0.01292 0.15732  -0.12234 106 ASN A CB  
719  C CG  . ASN A 99  ? 0.53445 0.54780 1.30131 -0.02131 0.20897  -0.09443 106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.36897 0.38336 1.19311 -0.02672 0.21798  -0.09874 106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.47390 0.44893 1.15425 -0.01794 0.23337  -0.06400 106 ASN A ND2 
722  N N   . LEU A 100 ? 0.52969 0.60156 1.22405 0.01250  0.05135  -0.17123 107 LEU A N   
723  C CA  . LEU A 100 ? 0.57581 0.65184 1.22338 0.02522  0.00246  -0.19566 107 LEU A CA  
724  C C   . LEU A 100 ? 0.48794 0.61117 1.18429 0.04066  -0.04214 -0.22436 107 LEU A C   
725  O O   . LEU A 100 ? 0.47603 0.61468 1.16994 0.04820  -0.08559 -0.25707 107 LEU A O   
726  C CB  . LEU A 100 ? 0.76672 0.80972 1.29093 0.04119  0.00030  -0.16886 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.68964 0.73221 1.14458 0.06310  -0.04531 -0.18367 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.46897 0.47335 0.83247 0.06311  -0.03460 -0.16609 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.56608 0.61817 0.98405 0.08820  -0.06364 -0.17277 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.50531 0.65323 1.24482 0.04818  -0.03253 -0.21327 108 GLY A N   
731  C CA  . GLY A 101 ? 0.46275 0.66359 1.25982 0.06501  -0.07314 -0.23952 108 GLY A CA  
732  C C   . GLY A 101 ? 0.42276 0.66565 1.32933 0.04705  -0.09603 -0.28386 108 GLY A C   
733  O O   . GLY A 101 ? 0.55889 0.83827 1.47911 0.06129  -0.14814 -0.31814 108 GLY A O   
734  N N   . THR A 102 ? 0.42267 0.65981 1.40774 0.01608  -0.05718 -0.28469 109 THR A N   
735  C CA  . THR A 102 ? 0.42159 0.69383 1.52064 -0.00717 -0.07310 -0.32792 109 THR A CA  
736  C C   . THR A 102 ? 0.45052 0.69687 1.51132 -0.01616 -0.09851 -0.35724 109 THR A C   
737  O O   . THR A 102 ? 0.48382 0.74872 1.60676 -0.02890 -0.12098 -0.39654 109 THR A O   
738  C CB  . THR A 102 ? 0.42652 0.67133 1.58010 -0.03196 -0.01449 -0.30897 109 THR A CB  
739  O OG1 . THR A 102 ? 0.42475 0.61882 1.54954 -0.04925 0.01941  -0.29880 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.40668 0.64413 1.54510 -0.02196 0.02378  -0.26638 109 THR A CG2 
741  N N   . ILE A 103 ? 0.45395 0.64801 1.39407 -0.00564 -0.09191 -0.33507 110 ILE A N   
742  C CA  . ILE A 103 ? 0.51775 0.68469 1.41023 -0.00835 -0.11528 -0.36063 110 ILE A CA  
743  C C   . ILE A 103 ? 0.61338 0.79495 1.42611 0.02518  -0.17216 -0.37589 110 ILE A C   
744  O O   . ILE A 103 ? 0.93731 1.08163 1.63499 0.04369  -0.17301 -0.35418 110 ILE A O   
745  C CB  . ILE A 103 ? 0.62499 0.72931 1.43846 -0.01518 -0.07168 -0.32718 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.51105 0.59932 1.39316 -0.04112 -0.01172 -0.30552 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.64454 0.71972 1.41896 -0.01792 -0.09117 -0.35497 110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.44693 0.48056 1.25091 -0.04282 0.03141  -0.26913 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.53349 0.77200 1.40834 0.03512  -0.21845 -0.41156 111 ALA A N   
750  C CA  . ALA A 104 ? 0.57138 0.82862 1.37667 0.07130  -0.27592 -0.43034 111 ALA A CA  
751  C C   . ALA A 104 ? 0.59384 0.92359 1.49867 0.07495  -0.32603 -0.47844 111 ALA A C   
752  O O   . ALA A 104 ? 0.64787 0.98847 1.50645 0.09850  -0.37439 -0.50786 111 ALA A O   
753  C CB  . ALA A 104 ? 0.56006 0.80477 1.27280 0.10391  -0.26931 -0.38655 111 ALA A CB  
754  N N   . LYS A 105 ? 0.89349 0.86625 0.84317 0.04262  -0.00913 0.13757  112 LYS A N   
755  C CA  . LYS A 105 ? 0.64244 0.68165 0.64305 0.02617  0.00655  0.15449  112 LYS A CA  
756  C C   . LYS A 105 ? 0.52206 0.56722 0.57435 -0.00811 -0.01843 0.14117  112 LYS A C   
757  O O   . LYS A 105 ? 0.51777 0.61448 0.60912 -0.02111 -0.02684 0.13024  112 LYS A O   
758  C CB  . LYS A 105 ? 0.72325 0.77127 0.71257 0.02589  0.03860  0.19498  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.73161 0.86998 0.77879 0.01964  0.06322  0.22010  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.81540 0.97111 0.84875 0.02621  0.10563  0.26248  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.88756 0.96750 0.82066 0.05922  0.12139  0.26089  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.99219 1.08793 0.89553 0.07082  0.16996  0.30028  112 LYS A NZ  
763  N N   . SER A 106 ? 0.54995 0.53342 0.59561 -0.02219 -0.03407 0.14111  113 SER A N   
764  C CA  . SER A 106 ? 0.49921 0.46354 0.58091 -0.05170 -0.06032 0.12274  113 SER A CA  
765  C C   . SER A 106 ? 0.47101 0.43553 0.55335 -0.04005 -0.07853 0.07675  113 SER A C   
766  O O   . SER A 106 ? 0.47272 0.45809 0.57931 -0.06067 -0.09261 0.05672  113 SER A O   
767  C CB  . SER A 106 ? 0.60408 0.48715 0.67182 -0.06148 -0.07381 0.13365  113 SER A CB  
768  O OG  . SER A 106 ? 0.57033 0.41113 0.59147 -0.03075 -0.07255 0.13710  113 SER A OG  
769  N N   . GLY A 107 ? 0.51484 0.45879 0.56843 -0.00950 -0.07889 0.06107  114 GLY A N   
770  C CA  . GLY A 107 ? 0.47860 0.43294 0.53520 0.00218  -0.08879 0.02234  114 GLY A CA  
771  C C   . GLY A 107 ? 0.39028 0.41128 0.45074 0.00011  -0.08082 0.01668  114 GLY A C   
772  O O   . GLY A 107 ? 0.38954 0.42724 0.45443 -0.00559 -0.08969 -0.01212 114 GLY A O   
773  N N   . THR A 108 ? 0.36770 0.42299 0.42043 0.00765  -0.06371 0.04436  115 THR A N   
774  C CA  . THR A 108 ? 0.47030 0.58538 0.52841 0.01000  -0.05863 0.04527  115 THR A CA  
775  C C   . THR A 108 ? 0.41850 0.57623 0.51355 -0.01905 -0.07015 0.04682  115 THR A C   
776  O O   . THR A 108 ? 0.33934 0.52760 0.43460 -0.02643 -0.08288 0.02855  115 THR A O   
777  C CB  . THR A 108 ? 0.43398 0.56456 0.47440 0.03197  -0.03669 0.07428  115 THR A CB  
778  O OG1 . THR A 108 ? 0.37627 0.45630 0.37358 0.05220  -0.03414 0.07084  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.33616 0.51903 0.38151 0.04045  -0.03460 0.07738  115 THR A CG2 
780  N N   . LYS A 109 ? 0.36731 0.52852 0.49166 -0.03972 -0.06812 0.07117  116 LYS A N   
781  C CA  . LYS A 109 ? 0.41303 0.61766 0.58080 -0.07603 -0.08565 0.07706  116 LYS A CA  
782  C C   . LYS A 109 ? 0.42831 0.59469 0.58308 -0.09766 -0.11602 0.03473  116 LYS A C   
783  O O   . LYS A 109 ? 0.42407 0.62780 0.58345 -0.11470 -0.13557 0.02148  116 LYS A O   
784  C CB  . LYS A 109 ? 0.43488 0.64336 0.63927 -0.10105 -0.07804 0.11339  116 LYS A CB  
785  C CG  . LYS A 109 ? 0.50018 0.75120 0.71271 -0.07730 -0.04074 0.15524  116 LYS A CG  
786  C CD  . LYS A 109 ? 0.59168 0.86071 0.84494 -0.10714 -0.02856 0.19609  116 LYS A CD  
787  C CE  . LYS A 109 ? 0.48975 0.78794 0.80115 -0.16156 -0.06143 0.19818  116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.42304 0.82446 0.78739 -0.16616 -0.06887 0.20937  116 LYS A NZ  
789  N N   . ALA A 110 ? 0.45115 0.53923 0.58442 -0.09417 -0.12106 0.01265  117 ALA A N   
790  C CA  . ALA A 110 ? 0.50267 0.54169 0.61671 -0.10683 -0.14497 -0.03198 117 ALA A CA  
791  C C   . ALA A 110 ? 0.48489 0.54807 0.56590 -0.08614 -0.14274 -0.06504 117 ALA A C   
792  O O   . ALA A 110 ? 0.53154 0.58207 0.58970 -0.10108 -0.16127 -0.09944 117 ALA A O   
793  C CB  . ALA A 110 ? 0.59526 0.54531 0.69694 -0.09500 -0.14717 -0.04598 117 ALA A CB  
794  N N   . PHE A 111 ? 0.43022 0.52339 0.50143 -0.05468 -0.12096 -0.05436 118 PHE A N   
795  C CA  . PHE A 111 ? 0.41790 0.53579 0.45885 -0.03828 -0.11554 -0.07826 118 PHE A CA  
796  C C   . PHE A 111 ? 0.45624 0.63389 0.49177 -0.05557 -0.12695 -0.07120 118 PHE A C   
797  O O   . PHE A 111 ? 0.44866 0.63116 0.45016 -0.06222 -0.13680 -0.10039 118 PHE A O   
798  C CB  . PHE A 111 ? 0.37116 0.49802 0.40620 -0.00795 -0.09459 -0.06352 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.38098 0.53573 0.39025 0.00447  -0.08621 -0.08033 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.40185 0.54588 0.39142 0.00632  -0.08614 -0.11919 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.41079 0.59772 0.41099 0.01476  -0.07624 -0.05630 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.40042 0.57808 0.36519 0.01601  -0.07239 -0.12980 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.32588 0.53806 0.30277 0.02015  -0.06828 -0.06506 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.36015 0.57408 0.32107 0.01965  -0.06441 -0.09982 118 PHE A CZ  
805  N N   . MET A 112 ? 0.42902 0.65410 0.49546 -0.06017 -0.12539 -0.03146 119 MET A N   
806  C CA  . MET A 112 ? 0.45297 0.74145 0.52366 -0.07265 -0.14067 -0.01864 119 MET A CA  
807  C C   . MET A 112 ? 0.43694 0.72801 0.51411 -0.11352 -0.17491 -0.03438 119 MET A C   
808  O O   . MET A 112 ? 0.54478 0.86844 0.59922 -0.12708 -0.19693 -0.04277 119 MET A O   
809  C CB  . MET A 112 ? 0.40163 0.74407 0.51328 -0.06008 -0.12832 0.02870  119 MET A CB  
810  C CG  . MET A 112 ? 0.32737 0.64362 0.42881 -0.02532 -0.09732 0.04389  119 MET A CG  
811  S SD  . MET A 112 ? 0.48233 0.85525 0.60712 0.00289  -0.08008 0.08917  119 MET A SD  
812  C CE  . MET A 112 ? 0.40483 0.76316 0.55582 0.01003  -0.05298 0.11438  119 MET A CE  
813  N N   . GLU A 113 ? 0.46704 0.71847 0.56932 -0.13686 -0.18382 -0.03675 120 GLU A N   
814  C CA  . GLU A 113 ? 0.53837 0.77180 0.63884 -0.18188 -0.22222 -0.05661 120 GLU A CA  
815  C C   . GLU A 113 ? 0.60153 0.77893 0.62783 -0.17918 -0.23352 -0.11336 120 GLU A C   
816  O O   . GLU A 113 ? 0.65645 0.84547 0.65038 -0.20511 -0.26468 -0.13196 120 GLU A O   
817  C CB  . GLU A 113 ? 0.57104 0.75450 0.70649 -0.20795 -0.22816 -0.04712 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.53871 0.79119 0.74987 -0.22769 -0.22380 0.00988  120 GLU A CG  
819  C CD  . GLU A 113 ? 0.79505 0.99461 1.03008 -0.23936 -0.21209 0.02850  120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.86093 0.96590 1.05544 -0.22941 -0.21195 -0.00281 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.77345 1.02854 1.06856 -0.25661 -0.20170 0.07717  120 GLU A OE2 
822  N N   . ALA A 114 ? 0.60249 0.72193 0.59964 -0.14612 -0.20803 -0.14070 121 ALA A N   
823  C CA  . ALA A 114 ? 0.66623 0.74021 0.59563 -0.13362 -0.20720 -0.19440 121 ALA A CA  
824  C C   . ALA A 114 ? 0.69614 0.82980 0.58486 -0.12177 -0.19934 -0.19571 121 ALA A C   
825  O O   . ALA A 114 ? 0.92204 1.03621 0.74422 -0.12595 -0.20755 -0.23519 121 ALA A O   
826  C CB  . ALA A 114 ? 0.66371 0.68199 0.59069 -0.09517 -0.17854 -0.21471 121 ALA A CB  
827  N N   . LEU A 115 ? 0.56870 0.76707 0.48789 -0.10668 -0.18348 -0.15295 122 LEU A N   
828  C CA  . LEU A 115 ? 0.61575 0.86374 0.49616 -0.09689 -0.17762 -0.14652 122 LEU A CA  
829  C C   . LEU A 115 ? 0.73923 1.01848 0.59086 -0.12945 -0.21615 -0.14693 122 LEU A C   
830  O O   . LEU A 115 ? 0.76782 1.05758 0.55810 -0.12639 -0.21652 -0.15764 122 LEU A O   
831  C CB  . LEU A 115 ? 0.49629 0.78950 0.41416 -0.07491 -0.15801 -0.09945 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.51674 0.78660 0.43685 -0.04380 -0.12396 -0.10156 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.45425 0.74520 0.40695 -0.02700 -0.11157 -0.05806 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.54561 0.82250 0.41393 -0.03320 -0.10767 -0.12365 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.74450 1.03732 0.64161 -0.16152 -0.24841 -0.12992 123 GLN A N   
836  C CA  . GLN A 116 ? 0.68883 0.99620 0.57214 -0.18903 -0.28710 -0.12644 123 GLN A CA  
837  C C   . GLN A 116 ? 0.89851 1.12974 0.72923 -0.21419 -0.31334 -0.17781 123 GLN A C   
838  O O   . GLN A 116 ? 1.13234 1.36369 0.93784 -0.23185 -0.34501 -0.18434 123 GLN A O   
839  C CB  . GLN A 116 ? 0.65052 1.01877 0.62437 -0.20527 -0.30358 -0.07686 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.67852 1.11101 0.70052 -0.17293 -0.27642 -0.02767 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.76401 1.24636 0.87977 -0.18030 -0.27431 0.01541  123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.01559 1.48870 1.16647 -0.21520 -0.29318 0.01308  123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.57120 1.10074 0.72431 -0.14608 -0.24783 0.05532  123 GLN A NE2 
844  N N   . ALA A 117 ? 0.82145 0.98330 0.63392 -0.21322 -0.30139 -0.21623 124 ALA A N   
845  C CA  . ALA A 117 ? 0.94256 1.01248 0.69909 -0.22688 -0.32108 -0.27069 124 ALA A CA  
846  C C   . ALA A 117 ? 1.17221 1.18317 0.83683 -0.19162 -0.28991 -0.31815 124 ALA A C   
847  O O   . ALA A 117 ? 1.37100 1.28949 0.99272 -0.18930 -0.28351 -0.36184 124 ALA A O   
848  C CB  . ALA A 117 ? 0.95376 0.96600 0.75799 -0.25005 -0.32965 -0.27406 124 ALA A CB  
849  N N   . GLY A 118 ? 1.11861 1.18392 0.75608 -0.16542 -0.26091 -0.30323 125 GLY A N   
850  C CA  . GLY A 118 ? 1.21662 1.24926 0.77834 -0.13249 -0.22247 -0.33895 125 GLY A CA  
851  C C   . GLY A 118 ? 0.97419 1.05214 0.57268 -0.09196 -0.17151 -0.33116 125 GLY A C   
852  O O   . GLY A 118 ? 1.15791 1.26473 0.71844 -0.07081 -0.13972 -0.32826 125 GLY A O   
853  N N   . ALA A 119 ? 0.90933 0.98864 0.58422 -0.08184 -0.16500 -0.32065 126 ALA A N   
854  C CA  . ALA A 119 ? 0.77366 0.87405 0.48837 -0.04188 -0.12145 -0.30786 126 ALA A CA  
855  C C   . ALA A 119 ? 0.69831 0.87831 0.42342 -0.03771 -0.10642 -0.26361 126 ALA A C   
856  O O   . ALA A 119 ? 0.67367 0.89257 0.40290 -0.06016 -0.13013 -0.23036 126 ALA A O   
857  C CB  . ALA A 119 ? 0.71785 0.78815 0.50918 -0.03518 -0.12285 -0.28778 126 ALA A CB  
858  N N   . ASP A 120 ? 0.66912 0.87272 0.40272 -0.00856 -0.06833 -0.26130 127 ASP A N   
859  C CA  . ASP A 120 ? 0.66983 0.93431 0.41199 -0.00574 -0.05291 -0.21973 127 ASP A CA  
860  C C   . ASP A 120 ? 0.55875 0.82767 0.37142 0.01221  -0.03784 -0.19250 127 ASP A C   
861  O O   . ASP A 120 ? 0.52368 0.75475 0.37564 0.02476  -0.03785 -0.20492 127 ASP A O   
862  C CB  . ASP A 120 ? 0.70808 1.00405 0.38893 0.00249  -0.02363 -0.23551 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.75636 1.05149 0.45748 0.03432  0.01617  -0.26204 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.74181 0.98606 0.45855 0.05019  0.01469  -0.29736 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.66255 1.00956 0.36886 0.04330  0.04801  -0.24450 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.58436 0.89264 0.40590 0.01167  -0.02877 -0.15410 128 ILE A N   
867  C CA  . ILE A 121 ? 0.52262 0.82711 0.39797 0.02135  -0.02486 -0.12452 128 ILE A CA  
868  C C   . ILE A 121 ? 0.52701 0.82904 0.43772 0.04200  -0.00394 -0.14156 128 ILE A C   
869  O O   . ILE A 121 ? 0.54099 0.82021 0.49584 0.05085  -0.01026 -0.13020 128 ILE A O   
870  C CB  . ILE A 121 ? 0.43032 0.76320 0.29511 0.01379  -0.02335 -0.08309 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.51035 0.84742 0.35392 0.00176  -0.04681 -0.06170 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.38372 0.70005 0.28873 0.02129  -0.02258 -0.05757 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.44404 0.80161 0.26151 -0.00314 -0.04705 -0.02473 128 ILE A CD1 
874  N N   . SER A 122 ? 0.46082 0.78891 0.35259 0.05237  0.02143  -0.16791 129 SER A N   
875  C CA  . SER A 122 ? 0.55455 0.89890 0.49391 0.07714  0.04442  -0.17938 129 SER A CA  
876  C C   . SER A 122 ? 0.46878 0.75945 0.44214 0.09749  0.03324  -0.20363 129 SER A C   
877  O O   . SER A 122 ? 0.46421 0.76648 0.48919 0.12208  0.04532  -0.20737 129 SER A O   
878  C CB  . SER A 122 ? 0.68577 1.07471 0.59579 0.08978  0.08160  -0.20476 129 SER A CB  
879  O OG  . SER A 122 ? 0.72649 1.09202 0.55839 0.08214  0.07846  -0.23541 129 SER A OG  
880  N N   . MET A 123 ? 0.48742 0.72236 0.43796 0.08637  0.00846  -0.21583 130 MET A N   
881  C CA  . MET A 123 ? 0.50817 0.68025 0.48482 0.09948  -0.00583 -0.23285 130 MET A CA  
882  C C   . MET A 123 ? 0.45334 0.60179 0.46424 0.08873  -0.02852 -0.19548 130 MET A C   
883  O O   . MET A 123 ? 0.52358 0.61489 0.54638 0.08927  -0.04520 -0.20017 130 MET A O   
884  C CB  . MET A 123 ? 0.58283 0.70079 0.51086 0.08810  -0.02027 -0.26964 130 MET A CB  
885  C CG  . MET A 123 ? 0.68009 0.81239 0.54587 0.09401  -0.00054 -0.30889 130 MET A CG  
886  S SD  . MET A 123 ? 0.78548 0.83611 0.58194 0.07370  -0.02910 -0.35557 130 MET A SD  
887  C CE  . MET A 123 ? 0.84542 0.83004 0.69873 0.05987  -0.06311 -0.33493 130 MET A CE  
888  N N   . ILE A 124 ? 0.43593 0.62014 0.45519 0.07888  -0.02864 -0.15837 131 ILE A N   
889  C CA  . ILE A 124 ? 0.36009 0.51849 0.39419 0.07137  -0.04560 -0.12538 131 ILE A CA  
890  C C   . ILE A 124 ? 0.50177 0.62692 0.57259 0.08956  -0.05301 -0.12160 131 ILE A C   
891  O O   . ILE A 124 ? 0.35835 0.44350 0.43069 0.08481  -0.06765 -0.10216 131 ILE A O   
892  C CB  . ILE A 124 ? 0.34168 0.53203 0.36471 0.06186  -0.04338 -0.09249 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.30190 0.46127 0.31968 0.05626  -0.05592 -0.06378 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.30752 0.52500 0.35519 0.07040  -0.03559 -0.08393 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.28383 0.45811 0.27854 0.05092  -0.05431 -0.03653 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.54436 0.68967 0.64604 0.11192  -0.04255 -0.13695 132 GLY A N   
897  C CA  . GLY A 125 ? 0.38377 0.50217 0.52644 0.13245  -0.05503 -0.13048 132 GLY A CA  
898  C C   . GLY A 125 ? 0.46945 0.51669 0.60958 0.14047  -0.06772 -0.14611 132 GLY A C   
899  O O   . GLY A 125 ? 0.44059 0.44506 0.59471 0.14536  -0.08698 -0.12629 132 GLY A O   
900  N N   . GLN A 126 ? 0.48507 0.51105 0.59972 0.13849  -0.06041 -0.18017 133 GLN A N   
901  C CA  . GLN A 126 ? 0.54080 0.48626 0.64836 0.14012  -0.07597 -0.19674 133 GLN A CA  
902  C C   . GLN A 126 ? 0.53037 0.43763 0.62534 0.10864  -0.09626 -0.16496 133 GLN A C   
903  O O   . GLN A 126 ? 0.68967 0.52659 0.78254 0.10279  -0.11221 -0.16811 133 GLN A O   
904  C CB  . GLN A 126 ? 0.60546 0.53003 0.67457 0.13766  -0.06820 -0.24275 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.80475 0.72275 0.88317 0.18135  -0.04805 -0.28355 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.99951 0.96020 1.03338 0.18256  -0.02209 -0.31796 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.90601 0.84121 0.88305 0.15434  -0.03182 -0.33701 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.67850 0.70902 0.73785 0.21270  0.00988  -0.32277 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.51562 0.46510 0.60163 0.08947  -0.09392 -0.13349 134 PHE A N   
910  C CA  . PHE A 127 ? 0.58391 0.51184 0.66066 0.06530  -0.10383 -0.10046 134 PHE A CA  
911  C C   . PHE A 127 ? 0.43594 0.36157 0.51342 0.07370  -0.10628 -0.06488 134 PHE A C   
912  O O   . PHE A 127 ? 0.43420 0.34703 0.49637 0.05879  -0.10694 -0.03539 134 PHE A O   
913  C CB  . PHE A 127 ? 0.43596 0.40956 0.49582 0.03991  -0.09825 -0.09395 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.47603 0.44813 0.52302 0.02486  -0.10385 -0.12750 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.48165 0.48456 0.51059 0.03655  -0.09314 -0.15824 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.51995 0.45781 0.56779 -0.00445 -0.12114 -0.12717 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.53668 0.52910 0.53591 0.02267  -0.10031 -0.19230 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.57284 0.49960 0.59897 -0.02295 -0.13390 -0.16062 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.58445 0.53487 0.57984 -0.00769 -0.12389 -0.19539 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.42349 0.36346 0.51688 0.09626  -0.10781 -0.06636 135 GLY A N   
921  C CA  . GLY A 128 ? 0.41671 0.34345 0.50253 0.10154  -0.11925 -0.03590 135 GLY A CA  
922  C C   . GLY A 128 ? 0.38309 0.33498 0.43600 0.09013  -0.11193 -0.01580 135 GLY A C   
923  O O   . GLY A 128 ? 0.39701 0.31977 0.42130 0.09016  -0.12106 0.00881  135 GLY A O   
924  N N   . VAL A 129 ? 0.35221 0.34954 0.40034 0.08222  -0.09686 -0.02576 136 VAL A N   
925  C CA  . VAL A 129 ? 0.35062 0.36194 0.36601 0.07593  -0.09015 -0.00717 136 VAL A CA  
926  C C   . VAL A 129 ? 0.31343 0.36992 0.33603 0.07497  -0.08504 -0.01578 136 VAL A C   
927  O O   . VAL A 129 ? 0.37480 0.45179 0.37617 0.06820  -0.07598 -0.00921 136 VAL A O   
928  C CB  . VAL A 129 ? 0.43629 0.45621 0.43690 0.06556  -0.07761 0.00214  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.35730 0.33783 0.34720 0.06284  -0.07778 0.02225  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.32387 0.37545 0.34584 0.05499  -0.07472 -0.02033 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.23516 0.29638 0.27454 -0.10119 0.12945  -0.08462 137 GLY A N   
932  C CA  . GLY A 130 ? 0.29009 0.35783 0.32511 -0.09369 0.13097  -0.07788 137 GLY A CA  
933  C C   . GLY A 130 ? 0.31792 0.40135 0.37425 -0.07746 0.12033  -0.05983 137 GLY A C   
934  O O   . GLY A 130 ? 0.27772 0.37355 0.33434 -0.07385 0.12129  -0.05087 137 GLY A O   
935  N N   . PHE A 131 ? 0.30811 0.39028 0.38058 -0.06903 0.11261  -0.05497 138 PHE A N   
936  C CA  . PHE A 131 ? 0.32301 0.41272 0.41291 -0.05787 0.10644  -0.04392 138 PHE A CA  
937  C C   . PHE A 131 ? 0.33651 0.45573 0.42908 -0.05871 0.10376  -0.03796 138 PHE A C   
938  O O   . PHE A 131 ? 0.21071 0.33332 0.31519 -0.05427 0.10530  -0.02839 138 PHE A O   
939  C CB  . PHE A 131 ? 0.31004 0.39476 0.41037 -0.05003 0.10159  -0.04472 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.36914 0.46157 0.48575 -0.04149 0.09885  -0.04128 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.14803 0.22546 0.27907 -0.03950 0.09818  -0.03724 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.38310 0.49595 0.50108 -0.03433 0.09628  -0.04094 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.30673 0.37090 0.43925 -0.02984 0.08625  -0.03403 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.23579 0.33648 0.35457 -0.01860 0.08762  -0.03627 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.28407 0.35500 0.40782 -0.01761 0.08219  -0.03491 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.34438 0.48887 0.42941 -0.06539 0.10035  -0.04092 139 TYR A N   
947  C CA  . TYR A 132 ? 0.28959 0.47342 0.37861 -0.06310 0.09668  -0.03077 139 TYR A CA  
948  C C   . TYR A 132 ? 0.32470 0.52094 0.40269 -0.06754 0.09863  -0.02359 139 TYR A C   
949  O O   . TYR A 132 ? 0.28438 0.50604 0.36429 -0.05885 0.09206  -0.00761 139 TYR A O   
950  C CB  . TYR A 132 ? 0.38613 0.60249 0.47078 -0.07089 0.08975  -0.03144 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.29111 0.49598 0.38372 -0.06666 0.08883  -0.03524 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.15921 0.36521 0.26615 -0.04649 0.08958  -0.02932 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.22836 0.42211 0.31263 -0.08265 0.08940  -0.04532 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.14664 0.34665 0.25744 -0.04077 0.08988  -0.03069 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.34647 0.53366 0.43931 -0.07787 0.08971  -0.04395 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.30149 0.49399 0.40683 -0.05635 0.08955  -0.03530 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.28581 0.47673 0.39698 -0.05036 0.09117  -0.03214 139 TYR A OH  
958  N N   . SER A 133 ? 0.35176 0.52759 0.41560 -0.07559 0.10664  -0.03149 140 SER A N   
959  C CA  . SER A 133 ? 0.33152 0.51939 0.38550 -0.07588 0.11222  -0.02208 140 SER A CA  
960  C C   . SER A 133 ? 0.27192 0.44827 0.34820 -0.06108 0.11088  -0.00201 140 SER A C   
961  O O   . SER A 133 ? 0.28196 0.47216 0.35530 -0.05768 0.11269  0.01411  140 SER A O   
962  C CB  . SER A 133 ? 0.29143 0.45471 0.32359 -0.08157 0.12303  -0.03440 140 SER A CB  
963  O OG  . SER A 133 ? 0.35851 0.48654 0.40548 -0.07267 0.12737  -0.03443 140 SER A OG  
964  N N   . ALA A 134 ? 0.25042 0.40088 0.34714 -0.05370 0.10692  -0.00224 141 ALA A N   
965  C CA  . ALA A 134 ? 0.41018 0.54293 0.52621 -0.04425 0.10179  0.01450  141 ALA A CA  
966  C C   . ALA A 134 ? 0.30998 0.45679 0.42689 -0.03327 0.09466  0.03111  141 ALA A C   
967  O O   . ALA A 134 ? 0.32895 0.46443 0.45738 -0.02790 0.09331  0.04999  141 ALA A O   
968  C CB  . ALA A 134 ? 0.36646 0.46899 0.49615 -0.04069 0.09586  0.00635  141 ALA A CB  
969  N N   . TYR A 135 ? 0.27483 0.44849 0.38236 -0.02962 0.09085  0.02783  142 TYR A N   
970  C CA  . TYR A 135 ? 0.29123 0.48590 0.40109 -0.01482 0.08613  0.04765  142 TYR A CA  
971  C C   . TYR A 135 ? 0.27458 0.50800 0.37429 -0.01866 0.08822  0.06417  142 TYR A C   
972  O O   . TYR A 135 ? 0.30375 0.55954 0.40732 -0.00455 0.08547  0.08671  142 TYR A O   
973  C CB  . TYR A 135 ? 0.26663 0.48626 0.37488 -0.00751 0.08188  0.04298  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.33980 0.52237 0.45533 0.00519  0.08058  0.03323  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.20933 0.37831 0.32332 -0.00480 0.08186  0.01262  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.23691 0.39437 0.35734 0.02848  0.07914  0.04469  142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.20486 0.34450 0.32084 0.00753  0.08019  0.00394  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.26954 0.38960 0.38795 0.04066  0.07793  0.03212  142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.32453 0.43965 0.44014 0.02978  0.07769  0.01184  142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.34108 0.42398 0.45025 0.04263  0.07599  -0.00036 142 TYR A OH  
981  N N   . LEU A 136 ? 0.23939 0.48145 0.32368 -0.03468 0.09438  0.05458  143 LEU A N   
982  C CA  . LEU A 136 ? 0.23921 0.51173 0.31057 -0.03583 0.09813  0.07146  143 LEU A CA  
983  C C   . LEU A 136 ? 0.35787 0.61187 0.45006 -0.02295 0.10083  0.09928  143 LEU A C   
984  O O   . LEU A 136 ? 0.46633 0.74555 0.56065 -0.01194 0.09946  0.12565  143 LEU A O   
985  C CB  . LEU A 136 ? 0.26141 0.53347 0.30870 -0.05108 0.10815  0.05383  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.34102 0.62720 0.35895 -0.06900 0.10710  0.02627  143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.27304 0.53377 0.26953 -0.07729 0.12222  0.00793  143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.28760 0.62895 0.28300 -0.07531 0.09803  0.03316  143 LEU A CD2 
989  N N   . VAL A 137 ? 0.25524 0.46648 0.36519 -0.02525 0.10398  0.09619  144 VAL A N   
990  C CA  . VAL A 137 ? 0.25599 0.44607 0.38858 -0.02008 0.10545  0.12232  144 VAL A CA  
991  C C   . VAL A 137 ? 0.26510 0.41204 0.41649 -0.01055 0.09651  0.12637  144 VAL A C   
992  O O   . VAL A 137 ? 0.33358 0.46141 0.50099 -0.00468 0.09613  0.15147  144 VAL A O   
993  C CB  . VAL A 137 ? 0.31854 0.49513 0.46172 -0.03126 0.11358  0.12168  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.25514 0.46733 0.37322 -0.03545 0.12652  0.11775  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.39514 0.53950 0.54673 -0.03800 0.10938  0.09752  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.29642 0.42451 0.44390 -0.00829 0.09047  0.10290  145 ALA A N   
997  C CA  . ALA A 138 ? 0.27163 0.35147 0.42832 0.00159  0.08319  0.10051  145 ALA A CA  
998  C C   . ALA A 138 ? 0.28275 0.37344 0.43065 0.02344  0.08216  0.10468  145 ALA A C   
999  O O   . ALA A 138 ? 0.26390 0.39711 0.40062 0.02516  0.08286  0.09651  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.27996 0.33165 0.43671 -0.00736 0.07817  0.07357  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.35760 0.40913 0.51160 0.04001  0.08122  0.11928  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.33821 0.38937 0.48499 0.06750  0.08304  0.12420  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.34548 0.35811 0.48162 0.07523  0.07963  0.09712  146 GLU A C   
1004 O O   . GLU A 139 ? 0.41713 0.43906 0.54514 0.09984  0.08349  0.09806  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.38587 0.40364 0.54052 0.08652  0.08729  0.15334  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.42907 0.35991 0.58477 0.08457  0.08311  0.14359  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.58383 0.47335 0.75038 0.09540  0.08788  0.17444  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.70732 0.63972 0.88653 0.09502  0.09337  0.20540  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.69531 0.50674 0.85537 0.10390  0.08646  0.16766  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.37741 0.35276 0.51345 0.05647  0.07310  0.07584  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.35023 0.29099 0.47234 0.06190  0.06863  0.04956  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.32798 0.26058 0.45542 0.03458  0.06125  0.03223  147 LYS A C   
1013 O O   . LYS A 140 ? 0.39034 0.31040 0.53275 0.01576  0.05770  0.04138  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.41253 0.28210 0.52296 0.08034  0.06705  0.04798  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.43367 0.25931 0.52324 0.08154  0.06005  0.01748  147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.50940 0.25753 0.57784 0.10236  0.06016  0.01218  147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.54941 0.23075 0.61318 0.07616  0.04472  -0.00399 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.62471 0.23037 0.68327 0.08287  0.04503  0.00589  147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.30629 0.25177 0.42429 0.03383  0.06023  0.01156  148 VAL A N   
1020 C CA  . VAL A 141 ? 0.28530 0.22990 0.40878 0.01259  0.05492  -0.00217 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.30817 0.21844 0.41422 0.01962  0.04730  -0.02347 148 VAL A C   
1022 O O   . VAL A 141 ? 0.33113 0.25405 0.42205 0.03754  0.05196  -0.03260 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.24002 0.23596 0.36765 0.00358  0.06283  -0.00476 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.22310 0.21752 0.35981 -0.01444 0.06074  -0.01262 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.22836 0.25884 0.36211 -0.00047 0.07007  0.01250  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.33428 0.20493 0.44172 0.00485  0.03510  -0.03002 149 THR A N   
1027 C CA  . THR A 142 ? 0.35718 0.20125 0.44517 0.00524  0.02484  -0.05227 149 THR A CA  
1028 C C   . THR A 142 ? 0.31989 0.19703 0.42279 -0.01440 0.02137  -0.05451 149 THR A C   
1029 O O   . THR A 142 ? 0.30367 0.19419 0.43168 -0.03440 0.01964  -0.04087 149 THR A O   
1030 C CB  . THR A 142 ? 0.42155 0.19877 0.49739 -0.00160 0.01040  -0.06014 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.46719 0.20913 0.53202 0.01943  0.01750  -0.05317 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.45608 0.20539 0.50069 0.00154  -0.00089 -0.08721 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.30835 0.20195 0.39718 -0.00587 0.02267  -0.06802 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.27671 0.20246 0.37885 -0.01893 0.02215  -0.06741 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.36562 0.27373 0.44760 -0.01960 0.00753  -0.08396 150 VAL A C   
1036 O O   . VAL A 143 ? 0.33048 0.22560 0.38290 -0.00011 0.00819  -0.09857 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.23514 0.20302 0.34141 -0.01020 0.03892  -0.06398 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.21407 0.20597 0.33008 -0.01799 0.04024  -0.06315 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.30363 0.29074 0.42577 -0.01531 0.05041  -0.05012 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.37534 0.28789 0.47240 -0.04129 -0.00558 -0.08014 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.43094 0.33888 0.51044 -0.04684 -0.02239 -0.09366 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.29556 0.25665 0.39535 -0.04926 -0.01566 -0.08141 151 ILE A C   
1043 O O   . ILE A 144 ? 0.26657 0.25440 0.40028 -0.06229 -0.01082 -0.06205 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.50962 0.38515 0.59180 -0.07315 -0.04632 -0.09659 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.41782 0.24176 0.49599 -0.07386 -0.04660 -0.09709 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.43444 0.29034 0.48052 -0.07628 -0.06676 -0.11970 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.45967 0.23805 0.49534 -0.04652 -0.04143 -0.11753 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.36776 0.34422 0.44668 -0.03389 -0.01289 -0.09018 152 THR A N   
1049 C CA  . THR A 145 ? 0.37569 0.39878 0.47244 -0.03149 -0.00303 -0.07612 152 THR A CA  
1050 C C   . THR A 145 ? 0.32410 0.36062 0.40002 -0.02991 -0.01806 -0.08360 152 THR A C   
1051 O O   . THR A 145 ? 0.34642 0.35411 0.38463 -0.02520 -0.03209 -0.10488 152 THR A O   
1052 C CB  . THR A 145 ? 0.23153 0.27083 0.32936 -0.01340 0.02119  -0.07177 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.26114 0.33589 0.38032 -0.01313 0.03339  -0.05530 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.25022 0.28191 0.31385 0.00728  0.02229  -0.08643 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.26240 0.34290 0.36059 -0.03175 -0.01367 -0.06522 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.28450 0.39141 0.36799 -0.03151 -0.02863 -0.06578 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.29864 0.45302 0.40612 -0.01962 -0.00973 -0.04107 153 LYS A C   
1058 O O   . LYS A 146 ? 0.22170 0.39803 0.36693 -0.02607 -0.00008 -0.01880 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.48921 0.60026 0.58146 -0.05889 -0.05682 -0.06459 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.36118 0.50064 0.43129 -0.06288 -0.07868 -0.06860 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.37838 0.49916 0.39543 -0.04025 -0.07742 -0.09239 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.41794 0.57040 0.40697 -0.04376 -0.09980 -0.09695 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.42739 0.63333 0.42289 -0.01989 -0.08137 -0.07532 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.25466 0.42319 0.33967 -0.00025 -0.00247 -0.04322 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.23086 0.43939 0.33489 0.01319  0.01625  -0.01859 154 HIS A CA  
1066 C C   . HIS A 147 ? 0.25713 0.50401 0.34502 0.01661  -0.00061 -0.01294 154 HIS A C   
1067 O O   . HIS A 147 ? 0.32715 0.56261 0.37478 0.01513  -0.02184 -0.03553 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.21731 0.41728 0.31269 0.03157  0.03999  -0.01981 154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.19624 0.42387 0.31562 0.04244  0.06346  0.00677  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.20771 0.47083 0.31913 0.05689  0.06524  0.02135  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.17227 0.39225 0.32031 0.04151  0.08722  0.02119  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.19041 0.46500 0.32881 0.06458  0.08997  0.04629  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.17172 0.41665 0.33069 0.05487  0.10357  0.04452  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.24016 0.53190 0.35671 0.02245  0.00927  0.01755  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.27481 0.61424 0.37894 0.02544  -0.00797 0.02811  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.29171 0.63460 0.35076 0.04453  -0.00805 0.01544  155 ASN A C   
1077 O O   . ASN A 148 ? 0.33877 0.71053 0.36858 0.04438  -0.02977 0.01122  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.32552 0.71566 0.47081 0.03529  0.00820  0.06935  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.34988 0.73262 0.54067 0.02790  0.02339  0.08625  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.32519 0.66663 0.52307 0.02996  0.04432  0.07864  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.21313 0.64090 0.43414 0.01987  0.01303  0.11079  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.27814 0.59690 0.33013 0.06043  0.01523  0.01047  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.33917 0.67074 0.35567 0.08275  0.02169  0.00680  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.32886 0.61880 0.30128 0.08768  0.01454  -0.02813 156 ASP A C   
1085 O O   . ASP A 149 ? 0.34540 0.64378 0.28963 0.10979  0.02512  -0.03071 156 ASP A O   
1086 C CB  . ASP A 149 ? 0.26861 0.61345 0.31306 0.09849  0.05511  0.03398  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.32316 0.70163 0.40858 0.09956  0.06712  0.07049  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.27485 0.68676 0.36259 0.09448  0.04872  0.07987  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.25979 0.63090 0.37477 0.10534  0.09502  0.09063  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.33946 0.58597 0.30611 0.07002  -0.00117 -0.05193 157 ASP A N   
1091 C CA  . ASP A 150 ? 0.44266 0.64343 0.36903 0.07799  -0.00510 -0.08272 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.43157 0.59208 0.33904 0.05548  -0.03395 -0.10819 157 ASP A C   
1093 O O   . ASP A 150 ? 0.40498 0.57846 0.33803 0.03113  -0.05002 -0.09928 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.33684 0.51656 0.28631 0.08383  0.01816  -0.07917 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.36753 0.52509 0.27813 0.10687  0.02508  -0.09755 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.42294 0.56939 0.28337 0.11902  0.01245  -0.11785 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.34103 0.49379 0.26958 0.11348  0.04328  -0.09138 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.45955 0.57074 0.32293 0.06439  -0.03932 -0.13795 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.50791 0.56650 0.35068 0.04253  -0.06475 -0.16377 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.47156 0.50182 0.35664 0.02690  -0.05848 -0.15664 158 GLU A C   
1101 O O   . GLU A 151 ? 0.41312 0.46375 0.33730 0.03307  -0.03583 -0.13556 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.58460 0.59205 0.35913 0.06201  -0.06972 -0.19861 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.64627 0.66915 0.36540 0.06785  -0.08716 -0.21507 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.89161 0.95891 0.63184 0.03650  -0.11270 -0.20234 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.74879 0.78922 0.49887 0.00225  -0.13763 -0.21159 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.01175 1.14472 0.76161 0.04640  -0.10730 -0.17946 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.51253 0.49428 0.38781 0.00481  -0.07935 -0.17426 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.52686 0.48003 0.43721 -0.00868 -0.07417 -0.16700 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.50469 0.41331 0.39271 0.01624  -0.05732 -0.17964 159 GLN A C   
1110 O O   . GLN A 152 ? 0.56682 0.43507 0.40279 0.03360  -0.06099 -0.20470 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.59291 0.51412 0.50651 -0.04399 -0.10275 -0.17558 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.63006 0.53369 0.58685 -0.06039 -0.09758 -0.16056 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.75791 0.67454 0.74691 -0.09916 -0.12092 -0.14848 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.70197 0.59172 0.71498 -0.11741 -0.12419 -0.14140 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.71501 0.67955 0.70751 -0.11161 -0.13694 -0.14202 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.54733 0.46548 0.47288 0.01965  -0.03810 -0.16143 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.50586 0.39794 0.41931 0.04376  -0.02099 -0.16560 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.43815 0.31066 0.38403 0.02988  -0.01822 -0.15436 160 TYR A C   
1119 O O   . TYR A 153 ? 0.41811 0.31438 0.40353 0.00728  -0.02006 -0.13732 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.54101 0.48099 0.46388 0.06760  0.00316  -0.15114 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.48415 0.44434 0.37191 0.08855  0.00522  -0.15897 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.49355 0.42640 0.33374 0.11798  0.01000  -0.17679 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.52863 0.53656 0.42973 0.08226  0.00471  -0.14605 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.52020 0.47531 0.32483 0.13966  0.01360  -0.18274 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.51248 0.54396 0.38112 0.10254  0.00730  -0.14972 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.55120 0.55757 0.37059 0.13078  0.01148  -0.16863 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.54025 0.57384 0.32399 0.15345  0.01577  -0.17113 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.64694 0.47794 0.57450 0.04697  -0.01182 -0.16182 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.56187 0.37598 0.51582 0.03978  -0.00696 -0.14866 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.42498 0.26880 0.38810 0.06465  0.01564  -0.13523 161 ALA A C   
1131 O O   . ALA A 154 ? 0.46016 0.29690 0.39508 0.09453  0.02534  -0.14255 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.53218 0.27158 0.46095 0.03755  -0.01887 -0.16358 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.36993 0.25013 0.37105 0.05224  0.02386  -0.11515 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.33992 0.25276 0.35353 0.06730  0.04099  -0.10080 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.34729 0.24071 0.37417 0.06363  0.04153  -0.08926 162 TRP A C   
1136 O O   . TRP A 155 ? 0.42132 0.29704 0.46350 0.04131  0.03243  -0.08518 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.28151 0.24875 0.32179 0.05462  0.04991  -0.08881 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.38525 0.38940 0.43876 0.06171  0.06348  -0.07512 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.24539 0.28458 0.29583 0.07748  0.07402  -0.07069 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.37731 0.39361 0.44969 0.05080  0.06658  -0.06225 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.22315 0.29620 0.29079 0.07411  0.08120  -0.05646 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.22367 0.28285 0.30201 0.05849  0.07661  -0.05238 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.36594 0.36551 0.45062 0.03488  0.06167  -0.05625 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.30882 0.39389 0.40074 0.04974  0.07971  -0.03960 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.23438 0.25858 0.33130 0.02987  0.06752  -0.04263 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.36875 0.43490 0.46714 0.03677  0.07541  -0.03585 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.35379 0.25654 0.37717 0.08650  0.05284  -0.08008 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.36980 0.25362 0.40242 0.08873  0.05426  -0.06617 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.42178 0.35109 0.46196 0.10953  0.06812  -0.04851 163 GLU A C   
1150 O O   . GLU A 156 ? 0.35775 0.30783 0.38570 0.13281  0.07645  -0.05021 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.44158 0.25107 0.44856 0.10034  0.04777  -0.07741 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.46859 0.25108 0.48459 0.10681  0.05143  -0.05957 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.79030 0.48552 0.77948 0.11358  0.04464  -0.07306 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.82552 0.48374 0.79759 0.09605  0.02993  -0.09575 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.64218 0.30469 0.62597 0.13614  0.05376  -0.06075 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.42474 0.37569 0.48565 0.10075  0.07022  -0.02933 164 SER A N   
1157 C CA  . SER A 157 ? 0.50061 0.50220 0.57060 0.11701  0.08005  -0.00932 164 SER A CA  
1158 C C   . SER A 157 ? 0.48330 0.49075 0.56828 0.11019  0.07972  0.01138  164 SER A C   
1159 O O   . SER A 157 ? 0.33404 0.34677 0.43107 0.08345  0.07495  0.01250  164 SER A O   
1160 C CB  . SER A 157 ? 0.41527 0.48144 0.49713 0.10370  0.08314  -0.00838 164 SER A CB  
1161 O OG  . SER A 157 ? 0.45785 0.58004 0.55272 0.10807  0.08778  0.01267  164 SER A OG  
1162 N N   . SER A 158 ? 0.51944 0.52808 0.60314 0.13761  0.08669  0.03028  165 SER A N   
1163 C CA  . SER A 158 ? 0.36251 0.39799 0.46144 0.13659  0.08857  0.05705  165 SER A CA  
1164 C C   . SER A 158 ? 0.37891 0.50074 0.48970 0.13442  0.09112  0.07254  165 SER A C   
1165 O O   . SER A 158 ? 0.31983 0.47752 0.43934 0.14658  0.09436  0.09936  165 SER A O   
1166 C CB  . SER A 158 ? 0.44996 0.44200 0.54302 0.16880  0.09564  0.07406  165 SER A CB  
1167 O OG  . SER A 158 ? 0.51888 0.42368 0.59746 0.16692  0.09128  0.05695  165 SER A OG  
1168 N N   . ALA A 159 ? 0.34219 0.49867 0.45382 0.11770  0.08896  0.05776  166 ALA A N   
1169 C CA  . ALA A 159 ? 0.37628 0.61185 0.49804 0.11288  0.08964  0.06924  166 ALA A CA  
1170 C C   . ALA A 159 ? 0.43002 0.69094 0.55459 0.15153  0.09808  0.08997  166 ALA A C   
1171 O O   . ALA A 159 ? 0.47986 0.69687 0.59185 0.17846  0.10500  0.08192  166 ALA A O   
1172 C CB  . ALA A 159 ? 0.23444 0.51182 0.36253 0.08871  0.08421  0.08029  166 ALA A CB  
1173 N N   . GLY A 160 ? 0.26921 0.60159 0.40797 0.15703  0.09831  0.11725  167 GLY A N   
1174 C CA  . GLY A 160 ? 0.29685 0.65293 0.43595 0.19209  0.10577  0.13920  167 GLY A CA  
1175 C C   . GLY A 160 ? 0.29495 0.66456 0.42608 0.18959  0.10469  0.13024  167 GLY A C   
1176 O O   . GLY A 160 ? 0.66387 1.03104 0.78488 0.21837  0.11213  0.14290  167 GLY A O   
1177 N N   . GLY A 161 ? 0.26094 0.64133 0.39521 0.15630  0.09726  0.11030  168 GLY A N   
1178 C CA  . GLY A 161 ? 0.25773 0.65872 0.38989 0.14947  0.09505  0.10747  168 GLY A CA  
1179 C C   . GLY A 161 ? 0.26999 0.62067 0.38657 0.16496  0.10243  0.08808  168 GLY A C   
1180 O O   . GLY A 161 ? 0.34219 0.71110 0.45778 0.16062  0.10180  0.08856  168 GLY A O   
1181 N N   . SER A 162 ? 0.46760 0.43656 0.24355 0.06417  -0.00119 0.10464  169 SER A N   
1182 C CA  . SER A 162 ? 0.46416 0.44441 0.24500 0.05783  -0.00079 0.10293  169 SER A CA  
1183 C C   . SER A 162 ? 0.45480 0.40599 0.22545 0.07060  0.01295  0.09207  169 SER A C   
1184 O O   . SER A 162 ? 0.39600 0.31013 0.15505 0.08859  0.03083  0.08521  169 SER A O   
1185 C CB  . SER A 162 ? 0.42355 0.42734 0.20966 0.07079  0.02171  0.10378  169 SER A CB  
1186 O OG  . SER A 162 ? 0.42749 0.40769 0.20780 0.09791  0.05670  0.09534  169 SER A OG  
1187 N N   . PHE A 163 ? 0.37455 0.33789 0.14552 0.06211  0.00500  0.09019  170 PHE A N   
1188 C CA  . PHE A 163 ? 0.38482 0.31660 0.14728 0.06957  0.01641  0.07518  170 PHE A CA  
1189 C C   . PHE A 163 ? 0.40747 0.37010 0.18301 0.06320  0.02003  0.06280  170 PHE A C   
1190 O O   . PHE A 163 ? 0.37347 0.38084 0.13760 0.06235  0.01134  0.07789  170 PHE A O   
1191 C CB  . PHE A 163 ? 0.40984 0.32785 0.18377 0.05474  -0.01441 0.07278  170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.43179 0.38984 0.21469 0.03401  -0.05131 0.08723  170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.51255 0.48726 0.30867 0.03235  -0.06528 0.09477  170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.35508 0.33126 0.16074 0.02211  -0.05914 0.07532  170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.37072 0.37386 0.19400 0.01963  -0.08324 0.09803  170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.34336 0.35840 0.16497 0.00825  -0.08607 0.08842  170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.45121 0.47365 0.28852 0.00897  -0.09096 0.09573  170 PHE A CZ  
1198 N N   . THR A 164 ? 0.44036 0.38215 0.24043 0.05996  0.03235  0.03505  171 THR A N   
1199 C CA  . THR A 164 ? 0.38959 0.35733 0.20164 0.05393  0.03171  0.01507  171 THR A CA  
1200 C C   . THR A 164 ? 0.38321 0.35853 0.21996 0.03562  0.00727  0.00316  171 THR A C   
1201 O O   . THR A 164 ? 0.36559 0.31209 0.21787 0.03114  0.00259  0.00242  171 THR A O   
1202 C CB  . THR A 164 ? 0.40206 0.34009 0.22734 0.06576  0.06711  -0.01143 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.43117 0.32030 0.27486 0.07103  0.08872  -0.01438 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.41680 0.36584 0.21706 0.08492  0.08726  -0.00220 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.40497 0.42348 0.24309 0.02823  -0.00806 -0.00487 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.44408 0.47805 0.30694 0.01314  -0.02944 -0.01855 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.46462 0.52440 0.32957 0.01479  -0.02518 -0.04862 172 VAL A C   
1208 O O   . VAL A 165 ? 0.38733 0.48445 0.22529 0.02410  -0.02494 -0.04449 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.43913 0.51163 0.29860 0.00126  -0.06511 0.01134  172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.34297 0.44663 0.22409 -0.01033 -0.08591 -0.00098 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.33901 0.37498 0.20264 -0.00197 -0.07454 0.03023  172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.47327 0.51457 0.37069 0.00717  -0.02214 -0.07974 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.40859 0.47113 0.31118 0.00657  -0.02423 -0.11548 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.41851 0.49812 0.35498 -0.01011 -0.04727 -0.13068 173 ARG A C   
1215 O O   . ARG A 166 ? 0.38649 0.44337 0.35165 -0.01866 -0.04962 -0.12067 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.43657 0.45136 0.35282 0.01487  0.00746  -0.14556 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.61768 0.57787 0.57685 0.00870  0.02672  -0.14824 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.47514 0.39085 0.45803 0.01438  0.05642  -0.17583 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.78201 0.67153 0.73903 0.03441  0.08509  -0.15818 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.78384 0.64536 0.73945 0.04266  0.10455  -0.12857 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.62148 0.47250 0.59881 0.03462  0.10103  -0.11518 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.47274 0.31879 0.40282 0.06232  0.12830  -0.11239 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.54894 0.67270 0.47982 -0.01195 -0.06473 -0.15467 174 THR A N   
1224 C CA  . THR A 167 ? 0.43140 0.57454 0.39763 -0.02693 -0.08622 -0.17500 174 THR A CA  
1225 C C   . THR A 167 ? 0.46662 0.55812 0.48016 -0.03489 -0.06759 -0.20704 174 THR A C   
1226 O O   . THR A 167 ? 0.46711 0.53200 0.48083 -0.02931 -0.04990 -0.23640 174 THR A O   
1227 C CB  . THR A 167 ? 0.44577 0.65198 0.38950 -0.02386 -0.10969 -0.19630 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.42703 0.69085 0.34587 -0.02165 -0.13199 -0.15735 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.47640 0.69336 0.46083 -0.03835 -0.12731 -0.23302 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.46828 0.54513 0.52526 -0.04672 -0.07033 -0.19896 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.43024 0.46157 0.53999 -0.05433 -0.04937 -0.21901 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.51439 0.56227 0.65680 -0.06731 -0.06384 -0.26429 175 ASP A C   
1233 O O   . ASP A 168 ? 0.46530 0.56688 0.60124 -0.07331 -0.09567 -0.27668 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.40527 0.42406 0.55238 -0.05974 -0.04726 -0.19562 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.51654 0.48652 0.71352 -0.06169 -0.01573 -0.20142 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.51928 0.45212 0.70960 -0.05406 0.01090  -0.20818 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.61852 0.59018 0.86407 -0.06939 -0.01626 -0.19617 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.48737 0.48868 0.66689 -0.07137 -0.04110 -0.28851 176 THR A N   
1239 C CA  . THR A 169 ? 0.52426 0.52905 0.74650 -0.08694 -0.05486 -0.33502 176 THR A CA  
1240 C C   . THR A 169 ? 0.52472 0.50740 0.82254 -0.10185 -0.04345 -0.32707 176 THR A C   
1241 O O   . THR A 169 ? 0.62886 0.61980 0.96139 -0.11298 -0.05545 -0.34806 176 THR A O   
1242 C CB  . THR A 169 ? 0.82841 0.80009 1.02887 -0.07539 -0.03880 -0.35836 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.88673 0.79719 1.11372 -0.07078 -0.00008 -0.34112 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.60282 0.59953 0.72682 -0.05517 -0.04377 -0.36113 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.64617 0.60382 0.96880 -0.10050 -0.02081 -0.29656 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.69215 0.63304 1.08511 -0.10935 -0.00344 -0.28275 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.57963 0.56767 1.01332 -0.12356 -0.03059 -0.28264 177 GLY A C   
1248 O O   . GLY A 170 ? 0.71552 0.74886 1.12630 -0.12833 -0.06487 -0.29891 177 GLY A O   
1249 N N   . GLU A 171 ? 0.65044 0.63177 1.14170 -0.12682 -0.01359 -0.26025 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.68545 0.71089 1.22199 -0.13796 -0.03516 -0.25630 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.47112 0.53585 0.97271 -0.13272 -0.06082 -0.24339 178 GLU A C   
1252 O O   . GLU A 171 ? 0.40385 0.45054 0.87429 -0.11741 -0.04720 -0.21741 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.76086 0.77141 1.36791 -0.13813 -0.00565 -0.23086 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.98230 0.94812 1.57822 -0.12066 0.03443  -0.20283 178 GLU A CG  
1255 C CD  . GLU A 171 ? 1.12675 1.09520 1.78271 -0.11485 0.05940  -0.17078 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 1.01172 1.02337 1.70442 -0.12174 0.03940  -0.16702 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 1.30089 1.23281 1.96454 -0.09976 0.10011  -0.14634 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.60701 0.72309 1.09979 -0.13921 -0.09606 -0.25232 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.45707 0.61243 0.91624 -0.13162 -0.12010 -0.23248 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.45390 0.60720 0.95412 -0.12527 -0.10937 -0.20247 179 PRO A C   
1261 O O   . PRO A 172 ? 0.46476 0.60844 1.02725 -0.12900 -0.09013 -0.19633 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.43544 0.64347 0.88895 -0.13975 -0.15279 -0.24292 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.54720 0.74269 1.02507 -0.15205 -0.15077 -0.27472 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.61344 0.75014 1.11807 -0.15183 -0.11544 -0.28016 179 PRO A CD  
1265 N N   . MET A 173 ? 0.50708 0.66592 0.96006 -0.11004 -0.11883 -0.17634 180 MET A N   
1266 C CA  . MET A 173 ? 0.34302 0.48129 0.80135 -0.09248 -0.10331 -0.14279 180 MET A CA  
1267 C C   . MET A 173 ? 0.33271 0.51549 0.81172 -0.08975 -0.12990 -0.12568 180 MET A C   
1268 O O   . MET A 173 ? 0.32793 0.50080 0.83559 -0.07664 -0.11649 -0.10505 180 MET A O   
1269 C CB  . MET A 173 ? 0.55720 0.65382 0.94525 -0.07437 -0.09222 -0.12388 180 MET A CB  
1270 C CG  . MET A 173 ? 0.72204 0.76405 1.10180 -0.06470 -0.05283 -0.12267 180 MET A CG  
1271 S SD  . MET A 173 ? 0.51356 0.50949 0.83136 -0.03821 -0.03911 -0.09385 180 MET A SD  
1272 C CE  . MET A 173 ? 0.47412 0.43183 0.82757 -0.02400 0.00858  -0.08710 180 MET A CE  
1273 N N   . GLY A 174 ? 0.46846 0.70183 0.93249 -0.09844 -0.16578 -0.13188 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.32723 0.59806 0.79632 -0.09126 -0.18894 -0.10713 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.31754 0.56262 0.73933 -0.07451 -0.19353 -0.07810 181 GLY A C   
1276 O O   . GLY A 174 ? 0.32042 0.59093 0.69979 -0.07437 -0.21508 -0.06536 181 GLY A O   
1277 N N   . ARG A 175 ? 0.31709 0.50652 0.73309 -0.05820 -0.16713 -0.06438 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.31818 0.47177 0.68972 -0.04169 -0.17088 -0.03924 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.32574 0.41743 0.68865 -0.02352 -0.13694 -0.03657 182 ARG A C   
1280 O O   . ARG A 175 ? 0.32873 0.41626 0.73421 -0.01827 -0.11304 -0.04187 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.38706 0.56697 0.77845 -0.03357 -0.19633 -0.01504 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.32335 0.49316 0.67184 -0.02917 -0.21938 0.00956  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.33381 0.50003 0.70549 -0.01355 -0.23404 0.03515  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.34346 0.47493 0.74210 0.00568  -0.20937 0.03097  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.34300 0.50774 0.79669 0.01137  -0.20639 0.03230  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.33358 0.56672 0.82217 -0.00212 -0.22896 0.03516  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.35476 0.48851 0.82877 0.03294  -0.18017 0.03189  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.27726 0.40351 0.22468 -0.08496 0.04833  -0.02082 183 GLY A N   
1289 C CA  . GLY A 176 ? 0.23198 0.38031 0.22203 -0.05835 0.06189  -0.01778 183 GLY A CA  
1290 C C   . GLY A 176 ? 0.23181 0.32848 0.21679 -0.05838 0.07369  -0.05107 183 GLY A C   
1291 O O   . GLY A 176 ? 0.26363 0.30308 0.21513 -0.07281 0.07862  -0.07987 183 GLY A O   
1292 N N   . THR A 177 ? 0.21588 0.33398 0.23533 -0.04128 0.07943  -0.04478 184 THR A N   
1293 C CA  . THR A 177 ? 0.21592 0.29788 0.24005 -0.03385 0.09011  -0.06907 184 THR A CA  
1294 C C   . THR A 177 ? 0.18569 0.29033 0.23824 -0.03569 0.08076  -0.04951 184 THR A C   
1295 O O   . THR A 177 ? 0.24490 0.39888 0.32254 -0.02426 0.07991  -0.02482 184 THR A O   
1296 C CB  . THR A 177 ? 0.17446 0.23981 0.19805 -0.00191 0.09159  -0.07034 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.19408 0.22383 0.19314 -0.00283 0.08704  -0.07857 184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.16779 0.21803 0.20205 0.00634  0.08607  -0.07237 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.21225 0.27609 0.25902 -0.04922 0.07750  -0.06011 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.26868 0.34116 0.33690 -0.05007 0.07150  -0.04361 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.31014 0.35896 0.39007 -0.02692 0.08412  -0.05981 185 LYS A C   
1302 O O   . LYS A 178 ? 0.31600 0.31746 0.38380 -0.02642 0.09369  -0.08438 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.36852 0.41028 0.41945 -0.08601 0.05879  -0.03782 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.30869 0.35464 0.37723 -0.09032 0.05393  -0.01836 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.59165 0.57095 0.63548 -0.11675 0.05527  -0.02837 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.70040 0.68599 0.72769 -0.16097 0.03929  -0.01290 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.65830 0.56528 0.64936 -0.19230 0.04598  -0.02799 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.22188 0.30557 0.32561 -0.00854 0.08463  -0.04472 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.32354 0.39935 0.44164 0.01297  0.09157  -0.05349 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.25597 0.32492 0.38425 0.00905  0.08283  -0.03178 186 VAL A C   
1311 O O   . VAL A 179 ? 0.22142 0.32540 0.35799 0.00816  0.07690  -0.00796 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.26578 0.37241 0.37581 0.03266  0.08782  -0.04664 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.18768 0.29981 0.30602 0.04731  0.08404  -0.04259 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.21154 0.29301 0.28670 0.03462  0.08069  -0.05267 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.22708 0.24637 0.35327 0.00706  0.08559  -0.03922 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.29008 0.28998 0.42205 0.00494  0.08116  -0.01871 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.28516 0.29854 0.44008 0.03520  0.08287  -0.01399 187 ILE A C   
1318 O O   . ILE A 180 ? 0.24924 0.24754 0.41541 0.05181  0.09155  -0.03193 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.33984 0.26971 0.45267 -0.01505 0.08765  -0.02703 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.33157 0.25401 0.41682 -0.05144 0.08177  -0.03132 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.35408 0.25702 0.47023 -0.01569 0.08719  -0.00446 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.38971 0.23862 0.44399 -0.07357 0.09314  -0.05330 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.30137 0.34564 0.46349 0.04094  0.07444  0.01139  188 LEU A N   
1324 C CA  . LEU A 181 ? 0.23573 0.30188 0.41520 0.06584  0.07087  0.02174  188 LEU A CA  
1325 C C   . LEU A 181 ? 0.34365 0.37336 0.52607 0.06941  0.06848  0.04512  188 LEU A C   
1326 O O   . LEU A 181 ? 0.30109 0.33403 0.47339 0.05836  0.06285  0.06874  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.20380 0.32646 0.37988 0.06820  0.06547  0.03334  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.20591 0.35878 0.37538 0.06564  0.07305  0.01339  188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.23243 0.42856 0.39330 0.06580  0.07392  0.02738  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.15282 0.30733 0.33201 0.07980  0.07890  -0.01284 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.31130 0.30403 0.50829 0.08585  0.07601  0.03955  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.36130 0.31784 0.56459 0.09774  0.07724  0.06478  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.34812 0.35685 0.56694 0.12001  0.06248  0.08909  189 HIS A C   
1334 O O   . HIS A 182 ? 0.33476 0.37345 0.57974 0.14352  0.05913  0.08579  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.40053 0.30054 0.61792 0.11202  0.09502  0.05248  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.41788 0.26633 0.61155 0.08635  0.11022  0.02392  189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.47882 0.25485 0.64547 0.06391  0.12299  0.02553  189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.38920 0.24582 0.57614 0.07629  0.11476  -0.00673 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.48749 0.23208 0.63039 0.03928  0.13274  -0.00311 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.43300 0.22548 0.58830 0.04799  0.12764  -0.02188 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.42451 0.44644 0.62568 0.10966  0.05349  0.11391  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.34369 0.41864 0.54535 0.12128  0.03873  0.13476  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.52348 0.59025 0.74301 0.14875  0.03194  0.16225  190 LEU A C   
1344 O O   . LEU A 183 ? 0.60738 0.61651 0.83310 0.15726  0.04200  0.17337  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.34634 0.43130 0.52059 0.09984  0.03586  0.15258  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.55097 0.66288 0.71382 0.07803  0.04121  0.13416  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.51925 0.66614 0.66331 0.06861  0.03894  0.15309  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.32982 0.47152 0.50327 0.08601  0.04367  0.10420  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.50148 0.62606 0.72751 0.16187  0.01570  0.17430  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.41847 0.55003 0.65972 0.18741  0.00336  0.20908  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.48272 0.58352 0.69369 0.17982  0.00114  0.24315  191 LYS A C   
1352 O O   . LYS A 184 ? 0.58120 0.67759 0.76080 0.15341  0.00511  0.24014  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.38863 0.59776 0.63815 0.19547  -0.01712 0.21291  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.34614 0.59029 0.62524 0.20036  -0.01424 0.17924  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.33073 0.64609 0.60010 0.19211  -0.03305 0.17574  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.29985 0.63895 0.58946 0.18824  -0.02850 0.13741  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.29041 0.69543 0.56575 0.17457  -0.04421 0.13323  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.51039 0.58986 0.73330 0.20466  -0.00336 0.27787  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.56305 0.60759 0.75450 0.19888  -0.00383 0.31269  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.57414 0.67100 0.73147 0.18302  -0.02093 0.32606  192 GLU A C   
1361 O O   . GLU A 185 ? 0.67218 0.74427 0.79455 0.16372  -0.01573 0.34083  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.69850 0.71075 0.90326 0.22614  -0.00419 0.33979  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.63999 0.71592 0.85303 0.24115  -0.02963 0.35371  192 GLU A CG  
1364 C CD  . GLU A 185 ? 0.82225 0.86959 1.02094 0.25443  -0.03458 0.38978  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.03690 1.01944 1.24560 0.26896  -0.01590 0.39711  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.00844 1.09447 1.18192 0.24904  -0.05540 0.40980  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.52977 0.69636 0.69374 0.18753  -0.03863 0.31953  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.57222 0.78526 0.69689 0.16966  -0.05197 0.32866  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.46875 0.69807 0.57223 0.14039  -0.03871 0.29357  193 ASP A C   
1370 O O   . ASP A 186 ? 0.55723 0.82279 0.62652 0.12395  -0.04335 0.29393  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.52390 0.79645 0.65659 0.17823  -0.07475 0.33000  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.83567 1.12431 0.92472 0.16704  -0.09050 0.35631  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.89592 1.23832 0.96344 0.15214  -0.10371 0.34871  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.96827 1.21194 1.04069 0.17087  -0.08810 0.38291  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.43588 0.63713 0.55638 0.13336  -0.02080 0.26486  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.43150 0.65090 0.54012 0.11146  -0.00764 0.23408  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.46265 0.64413 0.56307 0.09221  0.00913  0.23288  194 GLN A C   
1378 O O   . GLN A 187 ? 0.50165 0.69141 0.60587 0.07917  0.02107  0.20828  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.41075 0.64696 0.54784 0.11852  -0.00428 0.19886  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.33916 0.62406 0.48858 0.13229  -0.02017 0.19643  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.34268 0.67266 0.45392 0.11633  -0.02698 0.19990  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.37102 0.73348 0.47488 0.12180  -0.04697 0.22111  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.31965 0.65127 0.40490 0.09593  -0.00912 0.18008  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.43685 0.57917 0.52630 0.08912  0.01024  0.26070  195 THR A N   
1385 C CA  . THR A 188 ? 0.60004 0.70970 0.68442 0.06648  0.02489  0.26043  195 THR A CA  
1386 C C   . THR A 188 ? 0.53084 0.67111 0.59523 0.04488  0.03435  0.26225  195 THR A C   
1387 O O   . THR A 188 ? 0.42819 0.55538 0.49483 0.02432  0.04573  0.26318  195 THR A O   
1388 C CB  . THR A 188 ? 0.55765 0.61075 0.63311 0.06710  0.02677  0.28893  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.64251 0.70429 0.69013 0.06983  0.02003  0.32049  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.53025 0.54724 0.62784 0.09227  0.02390  0.28924  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.53970 0.72022 0.58459 0.04717  0.03190  0.26305  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.40850 0.61288 0.43439 0.02873  0.04805  0.26338  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.42564 0.64935 0.47397 0.02172  0.06210  0.23720  196 GLU A C   
1394 O O   . GLU A 189 ? 0.48337 0.72090 0.53051 0.00723  0.07918  0.24145  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.52565 0.76030 0.51687 0.02987  0.04579  0.26679  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.38091 0.64877 0.37584 0.03509  0.04747  0.23630  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.44403 0.73775 0.39949 0.03203  0.04066  0.23920  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.43850 0.73490 0.38705 0.04129  0.01726  0.25771  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.39979 0.71059 0.32967 0.01954  0.05966  0.22409  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.32544 0.55118 0.39561 0.03264  0.05649  0.21259  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.30053 0.54257 0.38877 0.02789  0.06827  0.18981  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.28163 0.50282 0.39112 0.01458  0.06869  0.19118  197 TYR A C   
1403 O O   . TYR A 190 ? 0.27380 0.50795 0.39936 0.01031  0.07411  0.17519  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.41300 0.66485 0.50902 0.04249  0.06395  0.16190  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.37173 0.64919 0.44382 0.04846  0.06285  0.15878  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.25106 0.55158 0.30156 0.04087  0.08182  0.15162  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.37031 0.64902 0.44016 0.06014  0.04406  0.16485  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.26623 0.58545 0.28548 0.03923  0.08229  0.14642  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.36287 0.67128 0.40777 0.05955  0.03946  0.16297  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.38559 0.71168 0.40104 0.04623  0.05869  0.15186  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.47903 0.82998 0.46066 0.03894  0.05568  0.14728  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.32112 0.50894 0.42716 0.00574  0.06338  0.21061  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.33210 0.50292 0.44986 -0.01700 0.06598  0.21513  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.34472 0.53597 0.46040 -0.03624 0.07669  0.23768  198 LEU A C   
1415 O O   . LEU A 191 ? 0.35111 0.54286 0.48049 -0.05979 0.07883  0.24277  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.37766 0.48948 0.49005 -0.01942 0.05935  0.21991  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.43881 0.52437 0.55770 0.00094  0.05316  0.20015  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.49953 0.51888 0.61157 -0.00016 0.05433  0.20912  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.33547 0.43417 0.46797 -0.00416 0.05443  0.17144  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.35261 0.56179 0.45035 -0.02947 0.08421  0.25094  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.37031 0.59111 0.46365 -0.04338 0.09450  0.26037  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.41959 0.67275 0.53058 -0.04102 0.10099  0.23834  199 GLU A C   
1423 O O   . GLU A 192 ? 0.31176 0.57796 0.42317 -0.02559 0.10203  0.21925  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.40387 0.61705 0.46244 -0.03652 0.09772  0.27188  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.54675 0.73752 0.59069 -0.05306 0.10305  0.28890  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.60624 0.76470 0.66071 -0.06965 0.09830  0.30127  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.50413 0.62493 0.54693 -0.06276 0.08957  0.31508  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.62864 0.79604 0.70191 -0.08942 0.10354  0.29655  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.31246 0.74037 0.49003 0.12423  0.07731  0.12021  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.30629 0.70569 0.44768 0.12140  0.08398  0.07538  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.25803 0.69354 0.35078 0.12154  0.08525  0.07744  200 GLU A C   
1432 O O   . GLU A 193 ? 0.24027 0.66444 0.31454 0.12872  0.07497  0.06045  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.26301 0.64427 0.41290 0.11259  0.10171  0.04794  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.34587 0.68923 0.47107 0.10831  0.10385  0.00813  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.44272 0.77801 0.58018 0.09706  0.12218  -0.01086 200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.28687 0.64570 0.45944 0.09185  0.13307  0.00065  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.44636 0.77635 0.55742 0.10074  0.12261  -0.03031 200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.28331 0.76250 0.34773 0.10964  0.09837  0.09757  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.34909 0.83281 0.33984 0.10136  0.09078  0.08568  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.38175 0.84412 0.35798 0.09587  0.05484  0.10209  201 ARG A C   
1441 O O   . ARG A 194 ? 0.42580 0.87291 0.34987 0.09446  0.03944  0.07852  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.37624 0.88204 0.32173 0.07754  0.09935  0.10566  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.75035 1.24835 0.70775 0.05813  0.08090  0.16312  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.82949 1.35215 0.76010 0.03256  0.09584  0.19347  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.96600 1.47159 0.91087 0.01770  0.07427  0.25290  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.90675 1.42507 0.82996 -0.00865 0.07820  0.29774  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.66446 1.22022 0.55420 -0.02677 0.10385  0.28828  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.83239 1.32592 0.77075 -0.01601 0.05279  0.35245  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.44630 0.90964 0.46970 0.09366  0.03847  0.13918  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.35968 0.81752 0.38017 0.08571  0.00474  0.15600  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.38774 0.84056 0.43529 0.09835  0.00077  0.13627  202 ARG A C   
1452 O O   . ARG A 195 ? 0.36291 0.79651 0.38235 0.08623  -0.02412 0.13136  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.33975 0.81531 0.40338 0.08335  -0.01176 0.20151  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.36378 0.85086 0.42663 0.07071  -0.04762 0.22299  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.47485 0.94839 0.46361 0.04660  -0.06873 0.22213  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.61024 1.08992 0.60558 0.02869  -0.10192 0.24025  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.47846 0.94446 0.44907 0.01129  -0.12757 0.22576  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.46527 0.90158 0.39993 0.01326  -0.12649 0.19043  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.46916 0.93886 0.45366 -0.00863 -0.15249 0.23977  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.27332 0.74312 0.37493 0.12112  0.02247  0.12611  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.21591 0.66471 0.32673 0.12685  0.02093  0.10851  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.36648 0.80228 0.43819 0.13690  0.02280  0.07493  203 ILE A C   
1463 O O   . ILE A 196 ? 0.38776 0.79938 0.44679 0.13126  0.00142  0.07365  203 ILE A O   
1464 C CB  . ILE A 196 ? 0.24696 0.64006 0.37075 0.12572  0.03479  0.08791  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.26457 0.65685 0.41610 0.11988  0.02712  0.10711  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.19510 0.56114 0.31370 0.12619  0.03382  0.06939  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.25321 0.60617 0.42371 0.12172  0.03364  0.08050  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.34337 0.77473 0.38448 0.14564  0.04574  0.04463  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.33892 0.74221 0.33066 0.15832  0.04716  0.00155  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.35665 0.71817 0.28645 0.14145  0.01304  -0.00425 204 LYS A C   
1471 O O   . LYS A 197 ? 0.39545 0.71474 0.29414 0.15216  -0.00343 -0.03364 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.29678 0.68757 0.27072 0.15502  0.06571  -0.02400 204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.27278 0.61236 0.27929 0.14547  0.06942  -0.03377 204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.55654 0.86768 0.56964 0.15376  0.05771  -0.03912 204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.59103 0.89096 0.56591 0.17353  0.04859  -0.06876 204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.40944 0.69517 0.38822 0.18950  0.03601  -0.06706 204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.38405 0.75340 0.29482 0.11705  -0.00173 0.02160  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.46099 0.79614 0.31177 0.10137  -0.03709 0.01045  205 GLU A CA  
1479 C C   . GLU A 198 ? 0.52390 0.82349 0.39358 0.08449  -0.07450 0.02850  205 GLU A C   
1480 O O   . GLU A 198 ? 0.56872 0.81531 0.39696 0.07978  -0.10611 0.00309  205 GLU A O   
1481 C CB  . GLU A 198 ? 0.48668 0.85061 0.31052 0.08084  -0.04269 0.03517  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.57181 0.91031 0.33203 0.06594  -0.08136 0.01919  205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.73457 1.10208 0.48955 0.04064  -0.09949 0.06113  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.76801 1.15432 0.58135 0.03120  -0.10085 0.10586  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.82383 1.20223 0.51561 0.03420  -0.11328 0.04763  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.43910 0.77007 0.37257 0.07493  -0.07375 0.07161  206 ILE A N   
1487 C CA  . ILE A 199 ? 0.49841 0.81505 0.45652 0.05297  -0.10670 0.09658  206 ILE A CA  
1488 C C   . ILE A 199 ? 0.50742 0.78586 0.47101 0.06670  -0.10726 0.07880  206 ILE A C   
1489 O O   . ILE A 199 ? 0.50967 0.73717 0.45808 0.04706  -0.14332 0.08074  206 ILE A O   
1490 C CB  . ILE A 199 ? 0.36851 0.75103 0.39463 0.04439  -0.10351 0.14558  206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.38407 0.79346 0.40024 0.02905  -0.11559 0.16800  206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.37284 0.76276 0.43272 0.02069  -0.13089 0.17506  206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.32569 0.79025 0.39630 0.04531  -0.09325 0.19435  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.38071 0.68026 0.36613 0.09946  -0.07068 0.06236  207 VAL A N   
1495 C CA  . VAL A 200 ? 0.42370 0.69334 0.41339 0.11794  -0.07020 0.04763  207 VAL A CA  
1496 C C   . VAL A 200 ? 0.59295 0.78332 0.51591 0.12735  -0.09235 0.00216  207 VAL A C   
1497 O O   . VAL A 200 ? 0.57733 0.70781 0.48992 0.12335  -0.12198 0.00211  207 VAL A O   
1498 C CB  . VAL A 200 ? 0.31265 0.63204 0.33921 0.15369  -0.02671 0.03433  207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.33586 0.62409 0.35429 0.17947  -0.02606 0.01218  207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.24197 0.63384 0.33723 0.15077  -0.01366 0.07368  207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.56961 0.76046 0.44624 0.14119  -0.08053 -0.03674 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.60492 0.73237 0.41500 0.15773  -0.10341 -0.08886 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.70482 0.77033 0.48235 0.12579  -0.15685 -0.08454 208 LYS A C   
1504 O O   . LYS A 201 ? 0.75426 0.73955 0.49477 0.13476  -0.19281 -0.11701 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.61773 0.78788 0.38837 0.17912  -0.07429 -0.12844 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.67911 0.80725 0.37377 0.19462  -0.10113 -0.18417 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.67242 0.84389 0.35603 0.22659  -0.06462 -0.22378 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.62435 0.79283 0.36234 0.24618  -0.04450 -0.22072 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.79320 0.87765 0.50712 0.26973  -0.08297 -0.24414 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.78725 0.88599 0.57988 0.08964  -0.16668 -0.04639 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.73210 0.78229 0.49648 0.05577  -0.21908 -0.04416 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.75655 0.75816 0.55723 0.02606  -0.25467 -0.00961 209 LYS A C   
1513 O O   . LYS A 202 ? 0.93101 0.84773 0.70024 0.01164  -0.30365 -0.02935 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.70951 0.82134 0.48056 0.02838  -0.21871 -0.01212 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.79182 0.86816 0.53449 -0.00772 -0.27322 -0.01227 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.76995 0.91660 0.51450 -0.02699 -0.27051 0.01766  209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.85730 0.97713 0.56731 -0.05998 -0.32589 0.00892  209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.85593 1.04220 0.54208 -0.06559 -0.32241 0.02209  209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.69763 0.75429 0.56475 0.01611  -0.23291 0.04196  210 HIS A N   
1520 C CA  . HIS A 203 ? 0.69366 0.73702 0.60263 -0.02243 -0.26339 0.09046  210 HIS A CA  
1521 C C   . HIS A 203 ? 0.78761 0.80321 0.71743 -0.00623 -0.25686 0.10031  210 HIS A C   
1522 O O   . HIS A 203 ? 0.90467 0.86419 0.84172 -0.03717 -0.29621 0.12610  210 HIS A O   
1523 C CB  . HIS A 203 ? 0.62715 0.77310 0.59828 -0.04699 -0.24885 0.14685  210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.65975 0.82882 0.61736 -0.07452 -0.27070 0.15300  210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.83195 0.94208 0.75811 -0.11172 -0.32364 0.14532  210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.65188 0.89501 0.62302 -0.06915 -0.25020 0.16629  210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.78072 0.93748 0.70041 -0.12723 -0.33258 0.15282  210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.67256 0.90825 0.61835 -0.10122 -0.28864 0.16823  210 HIS A NE2 
1529 N N   . SER A 204 ? 0.60359 0.53560 0.73560 -0.07559 -0.12429 0.08785  211 SER A N   
1530 C CA  . SER A 204 ? 0.71280 0.61667 0.84171 -0.05528 -0.10353 0.07545  211 SER A CA  
1531 C C   . SER A 204 ? 0.69723 0.59582 0.78163 -0.02310 -0.09055 0.05604  211 SER A C   
1532 O O   . SER A 204 ? 0.67575 0.58681 0.77991 -0.00274 -0.07512 0.05380  211 SER A O   
1533 C CB  . SER A 204 ? 0.64913 0.58217 0.84939 -0.05535 -0.08986 0.09228  211 SER A CB  
1534 O OG  . SER A 204 ? 0.52745 0.46268 0.77406 -0.08109 -0.09688 0.10802  211 SER A OG  
1535 N N   . GLN A 205 ? 0.77288 0.65294 0.79678 -0.01788 -0.09667 0.04118  212 GLN A N   
1536 C CA  . GLN A 205 ? 0.68358 0.56338 0.67122 0.01519  -0.08228 0.02210  212 GLN A CA  
1537 C C   . GLN A 205 ? 0.65446 0.47670 0.60197 0.03835  -0.07535 0.00259  212 GLN A C   
1538 O O   . GLN A 205 ? 0.74489 0.57348 0.68084 0.07084  -0.06348 -0.01057 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.68740 0.56644 0.62223 0.01456  -0.08613 0.01280  212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.74951 0.55747 0.60657 0.01739  -0.09172 -0.00862 212 GLN A CG  
1541 C CD  . GLN A 205 ? 1.11967 0.91562 0.92376 -0.00112 -0.10378 -0.01154 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 1.14874 0.92502 0.94474 -0.03420 -0.12654 -0.00262 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 1.27721 1.08529 1.04435 0.01929  -0.08857 -0.02413 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.82899 0.59584 0.75693 0.02215  -0.08301 0.00150  213 PHE A N   
1545 C CA  . PHE A 206 ? 0.82759 0.52609 0.70604 0.04150  -0.07771 -0.01549 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.71339 0.39585 0.62307 0.03841  -0.07064 -0.00605 213 PHE A C   
1547 O O   . PHE A 206 ? 0.79977 0.41519 0.67178 0.03565  -0.06984 -0.01244 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.92864 0.55963 0.74247 0.02449  -0.08926 -0.02719 213 PHE A CB  
1549 C CG  . PHE A 206 ? 1.00612 0.63604 0.77015 0.03068  -0.09325 -0.04068 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.86845 0.51355 0.61200 0.06958  -0.07885 -0.05531 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.97759 0.59279 0.71578 -0.00297 -0.11109 -0.03866 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.91558 0.55752 0.61033 0.07591  -0.07662 -0.06853 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.97684 0.58340 0.65814 0.00179  -0.11298 -0.05186 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 1.07973 0.69797 0.73763 0.04178  -0.09294 -0.06722 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.68274 0.42004 0.65508 0.03785  -0.06373 0.00886  214 ILE A N   
1556 C CA  . ILE A 207 ? 0.65096 0.37301 0.64863 0.03650  -0.05329 0.01706  214 ILE A CA  
1557 C C   . ILE A 207 ? 0.63678 0.34199 0.60728 0.07328  -0.04697 0.00458  214 ILE A C   
1558 O O   . ILE A 207 ? 0.84968 0.60062 0.83232 0.09477  -0.04701 -0.00025 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.55859 0.34042 0.63163 0.01907  -0.04839 0.03800  214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.55459 0.34932 0.66018 -0.01622 -0.05761 0.05270  214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.54245 0.30864 0.63348 0.02457  -0.03314 0.04298  214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.57432 0.32907 0.69036 -0.03729 -0.05068 0.05874  214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.67792 0.31803 0.61208 0.07960  -0.04238 0.00027  215 GLY A N   
1564 C CA  . GLY A 208 ? 0.70243 0.31682 0.60224 0.11573  -0.04204 -0.01090 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.65812 0.30562 0.59486 0.12313  -0.03684 -0.00303 215 GLY A C   
1566 O O   . GLY A 208 ? 0.68701 0.30024 0.59225 0.14648  -0.03875 -0.00884 215 GLY A O   
1567 N N   . TYR A 209 ? 0.59569 0.30446 0.59435 0.10350  -0.03199 0.01029  216 TYR A N   
1568 C CA  . TYR A 209 ? 0.55694 0.29648 0.58972 0.10711  -0.02679 0.01689  216 TYR A CA  
1569 C C   . TYR A 209 ? 0.49983 0.31990 0.58598 0.10345  -0.02869 0.02226  216 TYR A C   
1570 O O   . TYR A 209 ? 0.48175 0.33135 0.58977 0.08655  -0.02995 0.02882  216 TYR A O   
1571 C CB  . TYR A 209 ? 0.57902 0.29359 0.63058 0.08279  -0.01181 0.03047  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.66211 0.29386 0.65865 0.08275  -0.00537 0.02683  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.64767 0.23424 0.60134 0.10149  -0.00452 0.02149  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.64167 0.23753 0.62550 0.06192  -0.00155 0.02928  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.71373 0.21714 0.60866 0.10061  0.00254  0.01972  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.70466 0.22092 0.63568 0.05860  0.00676  0.02677  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.76362 0.23147 0.64776 0.07864  0.01005  0.02246  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.79754 0.21118 0.63696 0.07044  0.01771  0.02060  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.57442 0.42854 0.67919 0.11705  -0.03030 0.02017  217 PRO A N   
1580 C CA  . PRO A 210 ? 0.42955 0.35758 0.58205 0.11185  -0.03038 0.02516  217 PRO A CA  
1581 C C   . PRO A 210 ? 0.39062 0.33953 0.58911 0.08284  -0.02142 0.04386  217 PRO A C   
1582 O O   . PRO A 210 ? 0.38536 0.31263 0.59489 0.07407  -0.01298 0.05092  217 PRO A O   
1583 C CB  . PRO A 210 ? 0.42442 0.37457 0.58350 0.13066  -0.03582 0.01771  217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.45980 0.34592 0.58205 0.13713  -0.03696 0.01517  217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.50057 0.32404 0.58026 0.13516  -0.03379 0.01377  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.37037 0.35783 0.59215 0.06948  -0.02283 0.05208  218 ILE A N   
1587 C CA  . ILE A 211 ? 0.33746 0.34859 0.60537 0.04538  -0.01770 0.07187  218 ILE A CA  
1588 C C   . ILE A 211 ? 0.31217 0.37775 0.61113 0.04408  -0.01597 0.07670  218 ILE A C   
1589 O O   . ILE A 211 ? 0.36198 0.46336 0.66093 0.04329  -0.01958 0.07682  218 ILE A O   
1590 C CB  . ILE A 211 ? 0.35095 0.36231 0.62039 0.02863  -0.02475 0.08076  218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.38369 0.33964 0.61902 0.02716  -0.02695 0.07361  218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.31506 0.35045 0.63760 0.00746  -0.02208 0.10351  218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.40684 0.35863 0.62716 0.01264  -0.03972 0.07543  218 ILE A CD1 
1594 N N   . THR A 212 ? 0.29029 0.35762 0.61108 0.04188  -0.00896 0.08033  219 THR A N   
1595 C CA  . THR A 212 ? 0.26624 0.37900 0.61675 0.03607  -0.00658 0.08530  219 THR A CA  
1596 C C   . THR A 212 ? 0.24611 0.37245 0.63345 0.01514  -0.00115 0.10719  219 THR A C   
1597 O O   . THR A 212 ? 0.24427 0.34268 0.64771 0.00759  0.00581  0.11738  219 THR A O   
1598 C CB  . THR A 212 ? 0.26842 0.37042 0.61905 0.04131  -0.00450 0.07775  219 THR A CB  
1599 O OG1 . THR A 212 ? 0.39424 0.47784 0.70896 0.06332  -0.01342 0.05963  219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.24956 0.40009 0.62951 0.03261  -0.00377 0.08057  219 THR A CG2 
1601 N N   . LEU A 213 ? 0.34717 0.51507 0.74743 0.00700  -0.00300 0.11509  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.22431 0.40453 0.65594 -0.01094 -0.00058 0.13791  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.21369 0.40912 0.66752 -0.01856 0.00807  0.14210  220 LEU A C   
1604 O O   . LEU A 213 ? 0.29333 0.52360 0.74538 -0.02024 0.00884  0.13655  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.23306 0.43898 0.65429 -0.01811 -0.00867 0.14632  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.31951 0.53911 0.76752 -0.03529 -0.00917 0.17187  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.24333 0.43808 0.72266 -0.03971 -0.01111 0.18809  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.28764 0.52726 0.71173 -0.04290 -0.01825 0.17937  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.26721 0.43530 0.74202 -0.02414 0.01636  0.15127  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.26463 0.43574 0.75546 -0.03424 0.02455  0.15530  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.27241 0.45805 0.76548 -0.04611 0.02355  0.17205  221 PHE A C   
1612 O O   . PHE A 214 ? 0.31896 0.49428 0.81442 -0.04625 0.01902  0.18711  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.28269 0.40731 0.78226 -0.03419 0.03644  0.15767  221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.40269 0.49777 0.87349 -0.02369 0.03750  0.13680  221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.42984 0.53060 0.87300 -0.00988 0.02681  0.12090  221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.45805 0.51281 0.92303 -0.02699 0.04888  0.13334  221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.42630 0.49445 0.83765 0.00099  0.02501  0.10404  221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.42022 0.44157 0.84926 -0.01832 0.04762  0.11526  221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.37815 0.40695 0.78089 -0.00405 0.03442  0.10164  221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.22291 0.43143 0.71313 -0.05598 0.02630  0.16910  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.27964 0.49804 0.76515 -0.06869 0.02725  0.18402  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.25736 0.44228 0.74483 -0.07550 0.03422  0.18951  222 VAL A C   
1623 O O   . VAL A 215 ? 0.25948 0.43111 0.74891 -0.07782 0.03941  0.17735  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.27849 0.54635 0.76035 -0.07737 0.02969  0.17725  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.26142 0.53602 0.73607 -0.09359 0.03348  0.19526  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.22390 0.52485 0.70512 -0.06590 0.02490  0.16982  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.27468 0.44555 0.76327 -0.07867 0.03322  0.20876  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.32807 0.46649 0.81893 -0.08285 0.04047  0.21469  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.31809 0.46986 0.79811 -0.10367 0.04602  0.21318  223 GLU A C   
1630 O O   . GLU A 216 ? 0.31894 0.50578 0.79260 -0.11410 0.04491  0.21637  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.31127 0.43346 0.81532 -0.07517 0.03583  0.23716  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.44165 0.55844 0.96444 -0.05726 0.02993  0.23999  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.40603 0.51606 0.95642 -0.04912 0.02384  0.26324  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.32042 0.40657 0.88697 -0.04121 0.03428  0.26439  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.36249 0.49321 0.92083 -0.05140 0.00830  0.28098  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.36298 0.48557 0.84002 -0.11150 0.05390  0.20773  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.36421 0.49493 0.83192 -0.13543 0.05970  0.20500  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.40448 0.50732 0.86362 -0.14363 0.06394  0.22425  224 LYS A C   
1639 O O   . LYS A 217 ? 0.41157 0.53203 0.86584 -0.14969 0.06196  0.23944  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.37326 0.48693 0.83986 -0.14518 0.06367  0.18752  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.34162 0.47262 0.81858 -0.13461 0.05788  0.17133  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.35473 0.43482 0.82671 -0.12924 0.06243  0.16396  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.49411 0.54628 0.96719 -0.10414 0.06603  0.17108  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.51135 0.50729 0.97238 -0.09859 0.07763  0.16523  224 LYS A NZ  
# 
