data_7HAB
# 
_entry.id   7HAB 
# 
_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   7HAB         pdb_00007hab 10.2210/pdb7hab/pdb 
WWPDB D_1001407222 ?            ?                   
# 
_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                        7HAB 
_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 '(morpholin-4-yl)(phenyl)methanone' 191.226   1   ?        ? ? ? 
3 water       nat water                               18.015    329 ?        ? ? ? 
# 
_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 '(morpholin-4-yl)(phenyl)methanone' A1AXC 
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 
A1AXC non-polymer         . '(morpholin-4-yl)(phenyl)methanone' ? 'C11 H13 N O2'   191.226 
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        A1AXC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AXC 
_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 A1AXC 1   301 301 A1AXC DYQ A . 
C 3 HOH   1   401 144 HOH   HOH A . 
C 3 HOH   2   402 300 HOH   HOH A . 
C 3 HOH   3   403 223 HOH   HOH A . 
C 3 HOH   4   404 92  HOH   HOH A . 
C 3 HOH   5   405 192 HOH   HOH A . 
C 3 HOH   6   406 195 HOH   HOH A . 
C 3 HOH   7   407 207 HOH   HOH A . 
C 3 HOH   8   408 108 HOH   HOH A . 
C 3 HOH   9   409 188 HOH   HOH A . 
C 3 HOH   10  410 170 HOH   HOH A . 
C 3 HOH   11  411 199 HOH   HOH A . 
C 3 HOH   12  412 145 HOH   HOH A . 
C 3 HOH   13  413 51  HOH   HOH A . 
C 3 HOH   14  414 119 HOH   HOH A . 
C 3 HOH   15  415 128 HOH   HOH A . 
C 3 HOH   16  416 157 HOH   HOH A . 
C 3 HOH   17  417 113 HOH   HOH A . 
C 3 HOH   18  418 218 HOH   HOH A . 
C 3 HOH   19  419 253 HOH   HOH A . 
C 3 HOH   20  420 319 HOH   HOH A . 
C 3 HOH   21  421 180 HOH   HOH A . 
C 3 HOH   22  422 219 HOH   HOH A . 
C 3 HOH   23  423 285 HOH   HOH A . 
C 3 HOH   24  424 244 HOH   HOH A . 
C 3 HOH   25  425 68  HOH   HOH A . 
C 3 HOH   26  426 248 HOH   HOH A . 
C 3 HOH   27  427 240 HOH   HOH A . 
C 3 HOH   28  428 66  HOH   HOH A . 
C 3 HOH   29  429 93  HOH   HOH A . 
C 3 HOH   30  430 25  HOH   HOH A . 
C 3 HOH   31  431 85  HOH   HOH A . 
C 3 HOH   32  432 316 HOH   HOH A . 
C 3 HOH   33  433 169 HOH   HOH A . 
C 3 HOH   34  434 91  HOH   HOH A . 
C 3 HOH   35  435 53  HOH   HOH A . 
C 3 HOH   36  436 265 HOH   HOH A . 
C 3 HOH   37  437 12  HOH   HOH A . 
C 3 HOH   38  438 72  HOH   HOH A . 
C 3 HOH   39  439 194 HOH   HOH A . 
C 3 HOH   40  440 146 HOH   HOH A . 
C 3 HOH   41  441 158 HOH   HOH A . 
C 3 HOH   42  442 198 HOH   HOH A . 
C 3 HOH   43  443 196 HOH   HOH A . 
C 3 HOH   44  444 31  HOH   HOH A . 
C 3 HOH   45  445 137 HOH   HOH A . 
C 3 HOH   46  446 176 HOH   HOH A . 
C 3 HOH   47  447 312 HOH   HOH A . 
C 3 HOH   48  448 107 HOH   HOH A . 
C 3 HOH   49  449 97  HOH   HOH A . 
C 3 HOH   50  450 125 HOH   HOH A . 
C 3 HOH   51  451 15  HOH   HOH A . 
C 3 HOH   52  452 30  HOH   HOH A . 
C 3 HOH   53  453 8   HOH   HOH A . 
C 3 HOH   54  454 179 HOH   HOH A . 
C 3 HOH   55  455 16  HOH   HOH A . 
C 3 HOH   56  456 127 HOH   HOH A . 
C 3 HOH   57  457 314 HOH   HOH A . 
C 3 HOH   58  458 155 HOH   HOH A . 
C 3 HOH   59  459 103 HOH   HOH A . 
C 3 HOH   60  460 153 HOH   HOH A . 
C 3 HOH   61  461 235 HOH   HOH A . 
C 3 HOH   62  462 166 HOH   HOH A . 
C 3 HOH   63  463 70  HOH   HOH A . 
C 3 HOH   64  464 112 HOH   HOH A . 
C 3 HOH   65  465 1   HOH   HOH A . 
C 3 HOH   66  466 204 HOH   HOH A . 
C 3 HOH   67  467 49  HOH   HOH A . 
C 3 HOH   68  468 59  HOH   HOH A . 
C 3 HOH   69  469 47  HOH   HOH A . 
C 3 HOH   70  470 225 HOH   HOH A . 
C 3 HOH   71  471 21  HOH   HOH A . 
C 3 HOH   72  472 7   HOH   HOH A . 
C 3 HOH   73  473 78  HOH   HOH A . 
C 3 HOH   74  474 11  HOH   HOH A . 
C 3 HOH   75  475 232 HOH   HOH A . 
C 3 HOH   76  476 262 HOH   HOH A . 
C 3 HOH   77  477 99  HOH   HOH A . 
C 3 HOH   78  478 45  HOH   HOH A . 
C 3 HOH   79  479 172 HOH   HOH A . 
C 3 HOH   80  480 22  HOH   HOH A . 
C 3 HOH   81  481 64  HOH   HOH A . 
C 3 HOH   82  482 106 HOH   HOH A . 
C 3 HOH   83  483 268 HOH   HOH A . 
C 3 HOH   84  484 32  HOH   HOH A . 
C 3 HOH   85  485 309 HOH   HOH A . 
C 3 HOH   86  486 181 HOH   HOH A . 
C 3 HOH   87  487 27  HOH   HOH A . 
C 3 HOH   88  488 320 HOH   HOH A . 
C 3 HOH   89  489 46  HOH   HOH A . 
C 3 HOH   90  490 3   HOH   HOH A . 
C 3 HOH   91  491 9   HOH   HOH A . 
C 3 HOH   92  492 296 HOH   HOH A . 
C 3 HOH   93  493 34  HOH   HOH A . 
C 3 HOH   94  494 57  HOH   HOH A . 
C 3 HOH   95  495 124 HOH   HOH A . 
C 3 HOH   96  496 239 HOH   HOH A . 
C 3 HOH   97  497 229 HOH   HOH A . 
C 3 HOH   98  498 23  HOH   HOH A . 
C 3 HOH   99  499 161 HOH   HOH A . 
C 3 HOH   100 500 138 HOH   HOH A . 
C 3 HOH   101 501 38  HOH   HOH A . 
C 3 HOH   102 502 48  HOH   HOH A . 
C 3 HOH   103 503 134 HOH   HOH A . 
C 3 HOH   104 504 14  HOH   HOH A . 
C 3 HOH   105 505 327 HOH   HOH A . 
C 3 HOH   106 506 10  HOH   HOH A . 
C 3 HOH   107 507 67  HOH   HOH A . 
C 3 HOH   108 508 117 HOH   HOH A . 
C 3 HOH   109 509 69  HOH   HOH A . 
C 3 HOH   110 510 241 HOH   HOH A . 
C 3 HOH   111 511 79  HOH   HOH A . 
C 3 HOH   112 512 74  HOH   HOH A . 
C 3 HOH   113 513 215 HOH   HOH A . 
C 3 HOH   114 514 303 HOH   HOH A . 
C 3 HOH   115 515 62  HOH   HOH A . 
C 3 HOH   116 516 44  HOH   HOH A . 
C 3 HOH   117 517 96  HOH   HOH A . 
C 3 HOH   118 518 94  HOH   HOH A . 
C 3 HOH   119 519 24  HOH   HOH A . 
C 3 HOH   120 520 130 HOH   HOH A . 
C 3 HOH   121 521 98  HOH   HOH A . 
C 3 HOH   122 522 37  HOH   HOH A . 
C 3 HOH   123 523 100 HOH   HOH A . 
C 3 HOH   124 524 63  HOH   HOH A . 
C 3 HOH   125 525 77  HOH   HOH A . 
C 3 HOH   126 526 90  HOH   HOH A . 
C 3 HOH   127 527 234 HOH   HOH A . 
C 3 HOH   128 528 29  HOH   HOH A . 
C 3 HOH   129 529 39  HOH   HOH A . 
C 3 HOH   130 530 35  HOH   HOH A . 
C 3 HOH   131 531 210 HOH   HOH A . 
C 3 HOH   132 532 13  HOH   HOH A . 
C 3 HOH   133 533 178 HOH   HOH A . 
C 3 HOH   134 534 65  HOH   HOH A . 
C 3 HOH   135 535 120 HOH   HOH A . 
C 3 HOH   136 536 28  HOH   HOH A . 
C 3 HOH   137 537 81  HOH   HOH A . 
C 3 HOH   138 538 101 HOH   HOH A . 
C 3 HOH   139 539 5   HOH   HOH A . 
C 3 HOH   140 540 110 HOH   HOH A . 
C 3 HOH   141 541 256 HOH   HOH A . 
C 3 HOH   142 542 305 HOH   HOH A . 
C 3 HOH   143 543 118 HOH   HOH A . 
C 3 HOH   144 544 143 HOH   HOH A . 
C 3 HOH   145 545 87  HOH   HOH A . 
C 3 HOH   146 546 283 HOH   HOH A . 
C 3 HOH   147 547 222 HOH   HOH A . 
C 3 HOH   148 548 295 HOH   HOH A . 
C 3 HOH   149 549 173 HOH   HOH A . 
C 3 HOH   150 550 105 HOH   HOH A . 
C 3 HOH   151 551 280 HOH   HOH A . 
C 3 HOH   152 552 301 HOH   HOH A . 
C 3 HOH   153 553 42  HOH   HOH A . 
C 3 HOH   154 554 147 HOH   HOH A . 
C 3 HOH   155 555 297 HOH   HOH A . 
C 3 HOH   156 556 276 HOH   HOH A . 
C 3 HOH   157 557 116 HOH   HOH A . 
C 3 HOH   158 558 115 HOH   HOH A . 
C 3 HOH   159 559 109 HOH   HOH A . 
C 3 HOH   160 560 20  HOH   HOH A . 
C 3 HOH   161 561 184 HOH   HOH A . 
C 3 HOH   162 562 186 HOH   HOH A . 
C 3 HOH   163 563 19  HOH   HOH A . 
C 3 HOH   164 564 95  HOH   HOH A . 
C 3 HOH   165 565 246 HOH   HOH A . 
C 3 HOH   166 566 18  HOH   HOH A . 
C 3 HOH   167 567 126 HOH   HOH A . 
C 3 HOH   168 568 4   HOH   HOH A . 
C 3 HOH   169 569 156 HOH   HOH A . 
C 3 HOH   170 570 282 HOH   HOH A . 
C 3 HOH   171 571 40  HOH   HOH A . 
C 3 HOH   172 572 266 HOH   HOH A . 
C 3 HOH   173 573 73  HOH   HOH A . 
C 3 HOH   174 574 26  HOH   HOH A . 
C 3 HOH   175 575 114 HOH   HOH A . 
C 3 HOH   176 576 160 HOH   HOH A . 
C 3 HOH   177 577 60  HOH   HOH A . 
C 3 HOH   178 578 89  HOH   HOH A . 
C 3 HOH   179 579 177 HOH   HOH A . 
C 3 HOH   180 580 58  HOH   HOH A . 
C 3 HOH   181 581 2   HOH   HOH A . 
C 3 HOH   182 582 151 HOH   HOH A . 
C 3 HOH   183 583 187 HOH   HOH A . 
C 3 HOH   184 584 264 HOH   HOH A . 
C 3 HOH   185 585 208 HOH   HOH A . 
C 3 HOH   186 586 154 HOH   HOH A . 
C 3 HOH   187 587 121 HOH   HOH A . 
C 3 HOH   188 588 263 HOH   HOH A . 
C 3 HOH   189 589 6   HOH   HOH A . 
C 3 HOH   190 590 224 HOH   HOH A . 
C 3 HOH   191 591 17  HOH   HOH A . 
C 3 HOH   192 592 150 HOH   HOH A . 
C 3 HOH   193 593 190 HOH   HOH A . 
C 3 HOH   194 594 71  HOH   HOH A . 
C 3 HOH   195 595 50  HOH   HOH A . 
C 3 HOH   196 596 152 HOH   HOH A . 
C 3 HOH   197 597 86  HOH   HOH A . 
C 3 HOH   198 598 164 HOH   HOH A . 
C 3 HOH   199 599 141 HOH   HOH A . 
C 3 HOH   200 600 255 HOH   HOH A . 
C 3 HOH   201 601 310 HOH   HOH A . 
C 3 HOH   202 602 135 HOH   HOH A . 
C 3 HOH   203 603 293 HOH   HOH A . 
C 3 HOH   204 604 278 HOH   HOH A . 
C 3 HOH   205 605 245 HOH   HOH A . 
C 3 HOH   206 606 83  HOH   HOH A . 
C 3 HOH   207 607 162 HOH   HOH A . 
C 3 HOH   208 608 260 HOH   HOH A . 
C 3 HOH   209 609 56  HOH   HOH A . 
C 3 HOH   210 610 329 HOH   HOH A . 
C 3 HOH   211 611 307 HOH   HOH A . 
C 3 HOH   212 612 54  HOH   HOH A . 
C 3 HOH   213 613 288 HOH   HOH A . 
C 3 HOH   214 614 84  HOH   HOH A . 
C 3 HOH   215 615 311 HOH   HOH A . 
C 3 HOH   216 616 259 HOH   HOH A . 
C 3 HOH   217 617 55  HOH   HOH A . 
C 3 HOH   218 618 41  HOH   HOH A . 
C 3 HOH   219 619 163 HOH   HOH A . 
C 3 HOH   220 620 104 HOH   HOH A . 
C 3 HOH   221 621 272 HOH   HOH A . 
C 3 HOH   222 622 257 HOH   HOH A . 
C 3 HOH   223 623 52  HOH   HOH A . 
C 3 HOH   224 624 292 HOH   HOH A . 
C 3 HOH   225 625 174 HOH   HOH A . 
C 3 HOH   226 626 227 HOH   HOH A . 
C 3 HOH   227 627 321 HOH   HOH A . 
C 3 HOH   228 628 324 HOH   HOH A . 
C 3 HOH   229 629 82  HOH   HOH A . 
C 3 HOH   230 630 185 HOH   HOH A . 
C 3 HOH   231 631 267 HOH   HOH A . 
C 3 HOH   232 632 33  HOH   HOH A . 
C 3 HOH   233 633 299 HOH   HOH A . 
C 3 HOH   234 634 76  HOH   HOH A . 
C 3 HOH   235 635 191 HOH   HOH A . 
C 3 HOH   236 636 182 HOH   HOH A . 
C 3 HOH   237 637 88  HOH   HOH A . 
C 3 HOH   238 638 136 HOH   HOH A . 
C 3 HOH   239 639 140 HOH   HOH A . 
C 3 HOH   240 640 206 HOH   HOH A . 
C 3 HOH   241 641 254 HOH   HOH A . 
C 3 HOH   242 642 274 HOH   HOH A . 
C 3 HOH   243 643 258 HOH   HOH A . 
C 3 HOH   244 644 165 HOH   HOH A . 
C 3 HOH   245 645 322 HOH   HOH A . 
C 3 HOH   246 646 251 HOH   HOH A . 
C 3 HOH   247 647 221 HOH   HOH A . 
C 3 HOH   248 648 326 HOH   HOH A . 
C 3 HOH   249 649 317 HOH   HOH A . 
C 3 HOH   250 650 205 HOH   HOH A . 
C 3 HOH   251 651 111 HOH   HOH A . 
C 3 HOH   252 652 216 HOH   HOH A . 
C 3 HOH   253 653 315 HOH   HOH A . 
C 3 HOH   254 654 249 HOH   HOH A . 
C 3 HOH   255 655 209 HOH   HOH A . 
C 3 HOH   256 656 132 HOH   HOH A . 
C 3 HOH   257 657 211 HOH   HOH A . 
C 3 HOH   258 658 252 HOH   HOH A . 
C 3 HOH   259 659 123 HOH   HOH A . 
C 3 HOH   260 660 148 HOH   HOH A . 
C 3 HOH   261 661 279 HOH   HOH A . 
C 3 HOH   262 662 61  HOH   HOH A . 
C 3 HOH   263 663 236 HOH   HOH A . 
C 3 HOH   264 664 250 HOH   HOH A . 
C 3 HOH   265 665 212 HOH   HOH A . 
C 3 HOH   266 666 261 HOH   HOH A . 
C 3 HOH   267 667 325 HOH   HOH A . 
C 3 HOH   268 668 270 HOH   HOH A . 
C 3 HOH   269 669 286 HOH   HOH A . 
C 3 HOH   270 670 308 HOH   HOH A . 
C 3 HOH   271 671 168 HOH   HOH A . 
C 3 HOH   272 672 313 HOH   HOH A . 
C 3 HOH   273 673 159 HOH   HOH A . 
C 3 HOH   274 674 226 HOH   HOH A . 
C 3 HOH   275 675 277 HOH   HOH A . 
C 3 HOH   276 676 200 HOH   HOH A . 
C 3 HOH   277 677 220 HOH   HOH A . 
C 3 HOH   278 678 80  HOH   HOH A . 
C 3 HOH   279 679 217 HOH   HOH A . 
C 3 HOH   280 680 102 HOH   HOH A . 
C 3 HOH   281 681 43  HOH   HOH A . 
C 3 HOH   282 682 284 HOH   HOH A . 
C 3 HOH   283 683 289 HOH   HOH A . 
C 3 HOH   284 684 302 HOH   HOH A . 
C 3 HOH   285 685 75  HOH   HOH A . 
C 3 HOH   286 686 275 HOH   HOH A . 
C 3 HOH   287 687 237 HOH   HOH A . 
C 3 HOH   288 688 298 HOH   HOH A . 
C 3 HOH   289 689 183 HOH   HOH A . 
C 3 HOH   290 690 167 HOH   HOH A . 
C 3 HOH   291 691 269 HOH   HOH A . 
C 3 HOH   292 692 122 HOH   HOH A . 
C 3 HOH   293 693 243 HOH   HOH A . 
C 3 HOH   294 694 323 HOH   HOH A . 
C 3 HOH   295 695 230 HOH   HOH A . 
C 3 HOH   296 696 228 HOH   HOH A . 
C 3 HOH   297 697 238 HOH   HOH A . 
C 3 HOH   298 698 139 HOH   HOH A . 
C 3 HOH   299 699 36  HOH   HOH A . 
C 3 HOH   300 700 149 HOH   HOH A . 
C 3 HOH   301 701 214 HOH   HOH A . 
C 3 HOH   302 702 328 HOH   HOH A . 
C 3 HOH   303 703 318 HOH   HOH A . 
C 3 HOH   304 704 171 HOH   HOH A . 
C 3 HOH   305 705 203 HOH   HOH A . 
C 3 HOH   306 706 242 HOH   HOH A . 
C 3 HOH   307 707 231 HOH   HOH A . 
C 3 HOH   308 708 201 HOH   HOH A . 
C 3 HOH   309 709 271 HOH   HOH A . 
C 3 HOH   310 710 290 HOH   HOH A . 
C 3 HOH   311 711 133 HOH   HOH A . 
C 3 HOH   312 712 193 HOH   HOH A . 
C 3 HOH   313 713 202 HOH   HOH A . 
C 3 HOH   314 714 142 HOH   HOH A . 
C 3 HOH   315 715 294 HOH   HOH A . 
C 3 HOH   316 716 291 HOH   HOH A . 
C 3 HOH   317 717 304 HOH   HOH A . 
C 3 HOH   318 718 233 HOH   HOH A . 
C 3 HOH   319 719 213 HOH   HOH A . 
C 3 HOH   320 720 131 HOH   HOH A . 
C 3 HOH   321 721 306 HOH   HOH A . 
C 3 HOH   322 722 129 HOH   HOH A . 
C 3 HOH   323 723 273 HOH   HOH A . 
C 3 HOH   324 724 175 HOH   HOH A . 
C 3 HOH   325 725 247 HOH   HOH A . 
C 3 HOH   326 726 197 HOH   HOH A . 
C 3 HOH   327 727 287 HOH   HOH A . 
C 3 HOH   328 728 189 HOH   HOH A . 
C 3 HOH   329 729 281 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             591513.705 
_cell.length_a           66.136 
_cell.length_b           89.422 
_cell.length_c           100.019 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HAB 
_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                         7HAB 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HAB 
# 
_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   2023-07-03 
_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                     7HAB 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.710 
_reflns.d_resolution_high            1.500 
_reflns.number_obs                   47287 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.600 
_reflns.pdbx_Rmerge_I_obs            0.041 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        29.100 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              11.400 
_reflns.pdbx_Rrim_I_all              0.043 
_reflns.pdbx_Rpim_I_all              0.012 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     538093 
_reflns.pdbx_scaling_rejects         14 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.500 1.580  ? 39581 6238 ? 0.434 ? ? ? 6.300  ? 2.900  ? ? ? ? ? ? 90.700 0.472 0.181 0.904 
1 2 4.740 44.710 ? 19513 1640 ? 0.025 ? ? ? 11.900 ? 77.100 ? ? ? ? ? ? 99.600 0.027 0.008 0.999 
# 
_refine.entry_id                                 7HAB 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.87 
_refine.pdbx_overall_phase_error                 17.1473 
_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                          0.1622 
_refine.B_iso_mean                               27.80 
_refine.ls_number_reflns_R_free                  2299 
_refine.ls_percent_reflns_obs                    98.43 
_refine.ls_R_factor_R_work                       0.1611 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.50 
_refine.ls_number_reflns_obs                     47239 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  44940 
_refine.ls_d_res_low                             36.43 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1848 
_refine.overall_SU_ML                            0.1390 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         14 
_refine_hist.number_atoms_solvent             329 
_refine_hist.number_atoms_total               1987 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        36.43 
# 
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           1899 0.0157 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2563 1.5061 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     289  0.1166 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      331  0.0119 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 263  7.6814 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' 1.50 1.53  2360 0.2164 85.00  0.2365 133 . . . . . 
'X-RAY DIFFRACTION' 1.53 1.57  2609 0.1894 92.93  0.2283 150 . . . . . 
'X-RAY DIFFRACTION' 1.57 1.60  2777 0.1732 98.75  0.1909 137 . . . . . 
'X-RAY DIFFRACTION' 1.60 1.65  2821 0.1626 99.97  0.1842 160 . . . . . 
'X-RAY DIFFRACTION' 1.65 1.70  2838 0.1717 100.00 0.2098 143 . . . . . 
'X-RAY DIFFRACTION' 1.70 1.75  2813 0.1904 99.97  0.2288 148 . . . . . 
'X-RAY DIFFRACTION' 1.75 1.81  2849 0.1801 100.00 0.2092 146 . . . . . 
'X-RAY DIFFRACTION' 1.81 1.89  2823 0.1625 100.00 0.1910 139 . . . . . 
'X-RAY DIFFRACTION' 1.89 1.97  2817 0.1676 98.93  0.1833 139 . . . . . 
'X-RAY DIFFRACTION' 1.97 2.08  2846 0.1663 100.00 0.2078 158 . . . . . 
'X-RAY DIFFRACTION' 2.08 2.21  2836 0.1549 99.97  0.1809 141 . . . . . 
'X-RAY DIFFRACTION' 2.21 2.38  2844 0.1651 99.46  0.1796 128 . . . . . 
'X-RAY DIFFRACTION' 2.38 2.62  2879 0.1626 100.00 0.1938 146 . . . . . 
'X-RAY DIFFRACTION' 2.62 2.99  2910 0.1651 100.00 0.1913 132 . . . . . 
'X-RAY DIFFRACTION' 2.99 3.77  2897 0.1517 99.90  0.1762 152 . . . . . 
'X-RAY DIFFRACTION' 3.77 36.43 3021 0.1515 99.59  0.1652 147 . . . . . 
# 
_struct.entry_id                  7HAB 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr12700' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HAB 
_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              7HAB 
_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 7HAB MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HAB LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HAB GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HAB HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HAB HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HAB HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HAB HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HAB HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HAB HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2 AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3 AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4 AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5 AA5 ILE A 103 ? ALA A 117 ? ILE A 110 ALA A 124 1 ? 15 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 11  ? ALA A 14  ? GLU A 18  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O THR A 83  ? O THR A 90  N ILE A 74  ? N ILE A 81  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HAB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 457 ? ? O A HOH 588 ? ? 1.88 
2  1 ND2 A ASN 105 ? ? O A HOH 401 ? ? 1.90 
3  1 O   A HOH 627 ? ? O A HOH 688 ? ? 1.91 
4  1 O   A HOH 433 ? ? O A HOH 466 ? ? 1.96 
5  1 O   A HOH 667 ? ? O A HOH 695 ? ? 1.96 
6  1 O   A HOH 443 ? ? O A HOH 586 ? ? 2.00 
7  1 OE1 A GLU 158 ? ? O A HOH 402 ? ? 2.02 
8  1 O   A HOH 541 ? ? O A HOH 542 ? ? 2.05 
9  1 N   A ALA 121 ? B O A HOH 403 ? ? 2.09 
10 1 O   A HOH 466 ? ? O A HOH 564 ? ? 2.10 
11 1 O   A HOH 674 ? ? O A HOH 708 ? ? 2.12 
12 1 O   A HOH 641 ? ? O A HOH 687 ? ? 2.15 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 411 ? ? 1_555 O A HOH 496 ? ? 8_544 2.08 
2 1 O A HOH 483 ? ? 1_555 O A HOH 643 ? ? 8_444 2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              182 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              182 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              182 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                123.36 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            3.06 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 38  ? ? -161.76 113.37  
2 1 ASP A 66  ? ? -151.31 88.72   
3 1 ILE A 110 ? A -93.45  59.08   
4 1 ALA A 124 ? B -44.77  -8.62   
5 1 ALA A 166 ? ? 63.46   -140.97 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     699 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
1 ? 'X-RAY DIFFRACTION' refined 12.4063653627  -17.8174844158 -18.6603133015 0.159657222719 0.199552358778 0.200643434024 
0.0123144919401   -0.0282913260311  -0.0356223804386  2.56072732421 1.27271483525 5.27528149401 -0.845530045432 -2.68727249712   
0.0575274212806 0.112153757968   -0.197073428197 -0.0161315878919 0.0283270181463  -0.0640974074568 -0.0598784666903 
0.00893939080667 0.306330955732  -0.0289535101609 
2 ? 'X-RAY DIFFRACTION' refined -5.18218719637 -6.35081753545 -20.8682137904 0.181936541104 0.161881472195 0.212996187566 
-0.00633069905374 -0.00870868334488 -0.0353873193503  1.41112167472 3.5796369081  4.61618939734 -1.21938797451  1.4784106051     
-2.90428250146  -0.046872435044  0.0490042311452 0.142709167104   0.109656875595   -0.0439966027491 0.0609542447473  
-0.317742016401  0.115169062383  0.0582794358812  
3 ? 'X-RAY DIFFRACTION' refined -13.5889889834 -10.8508082193 -28.0422079581 0.183035939345 0.217305939323 0.245918539397 
0.0150534813256   -0.0671002799932  -0.0328726778027  1.5481087047  3.86610615042 5.53868070877 -0.379066696731 0.220273205205   
-3.19242116636  0.117335018907   0.240899081888  -0.0222632891534 -0.246577682818  0.103894545091   0.50239329743    
-0.0961371283841 -0.317492931981 -0.281154100899  
4 ? 'X-RAY DIFFRACTION' refined -6.11084676742 -19.3555699393 -22.0872001962 0.169771099256 0.140355212024 0.196523714276 
-0.00164859079514 -0.0227303599223  -0.0364786061261  1.72597232998 2.97231010542 3.63905165961 -0.374852822935 -0.35151733655   
-2.05314734819  -0.0247109958862 0.0108373932891 -0.188515656659  0.00579289515724 0.112339497843   0.19746523514    
0.194150319174   -0.109487988776 -0.0867084403355 
5 ? 'X-RAY DIFFRACTION' refined 11.3110086651  -6.42469201364 -15.8901595734 0.182711299891 0.213878425748 0.246233589876 
-0.0452754579419  0.00150931472313  -0.0637327599697  2.16567771507 1.90333276651 4.80347591728 0.120294989967  -0.489197534194  
0.248702840312  0.123952077586   -0.348455329432 0.330829964505   0.191677000279   -0.0509921021196 -0.151697341994  
-0.448280769847  0.559549170848  -0.0695171915997 
6 ? 'X-RAY DIFFRACTION' refined 0.994161960224 -19.226834174  -28.1087211835 0.163503770327 0.160275027845 0.191052483358 
0.00553815821423  -0.020616856293   -0.0447560039975  2.43606418067 1.72617177445 1.89281620838 -1.00282970128  0.0757719126044  
-0.207793652076 0.109104669596   0.285981646559  -0.250502303374  -0.172646293785  -0.0803347255197 0.171663520829   0.1698623463 
0.0358012549552 -0.0589310237341 
7 ? 'X-RAY DIFFRACTION' refined -2.18031232878 -23.9320919849 -13.3362275404 0.166806109867 0.134985979162 0.19246652081  
0.00034842314964  -0.0150923553737  -0.00156045247785 2.89195363301 3.08107916912 4.86393497281 -0.637486573169 -0.141902371395  
-1.49614057913  -0.0323469855523 -0.205728143288 -0.275060769735  0.109468513537   -0.0335351939272 -0.0507177726011 
0.365344142342   0.244236587611  0.0145798101331  
8 ? 'X-RAY DIFFRACTION' refined -9.89072107915 -15.3362003969 -5.66427247934 0.172224911005 0.255210519129 0.153584384632 
-0.00207610272593 -0.00914713520562 0.00592201851388  4.57811043433 7.11632331    6.02702506126 -0.33770814108  -0.467870071367  
-1.41348083187  0.0891815425541  -0.348076663124 -0.0741701787154 0.167806424438   0.0905664314189  0.349620577985   
-0.0918358582427 -0.242389174034 -0.0549720055609 
9 ? 'X-RAY DIFFRACTION' refined -13.8894771073 -13.4767552176 -14.7343603152 0.145939742974 0.178217257827 0.138732422292 
0.00580034260073  -0.00424773419848 -0.0240297544858  3.93673574236 3.11159822625 3.75738943315 -0.246968362335 -0.0964834752137 
-1.25469839946  0.020551520281   -0.28916457468  -0.0177113520917 0.37785820813    -0.0104122115613 0.0539851953546  
-0.153942001096  -0.185576599536 0.010020591998   
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 1 'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2 2 'X-RAY DIFFRACTION' A 41  A 26  A 65  A 50  . 
;chain 'A' and (resid 41 through 65 )
;
3 3 'X-RAY DIFFRACTION' A 66  A 51  A 83  A 68  . 
;chain 'A' and (resid 66 through 83 )
;
4 4 'X-RAY DIFFRACTION' A 84  A 69  A 99  A 84  . 
;chain 'A' and (resid 84 through 99 )
;
5 5 'X-RAY DIFFRACTION' A 100 A 85  A 136 A 121 . 
;chain 'A' and (resid 100 through 136 )
;
6 6 'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
7 7 'X-RAY DIFFRACTION' A 183 A 168 A 199 A 184 . 
;chain 'A' and (resid 183 through 199 )
;
8 8 'X-RAY DIFFRACTION' A 200 A 185 A 210 A 195 . 
;chain 'A' and (resid 200 through 210 )
;
9 9 '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 
A1AXC C4   C N N 1   
A1AXC C6   C Y N 2   
A1AXC C11  C Y N 3   
A1AXC C8   C Y N 4   
A1AXC C9   C Y N 5   
A1AXC C10  C Y N 6   
A1AXC C3   C N N 7   
A1AXC C2   C N N 8   
A1AXC C1   C N N 9   
A1AXC C5   C N N 10  
A1AXC C7   C Y N 11  
A1AXC N1   N N N 12  
A1AXC O1   O N N 13  
A1AXC O2   O N N 14  
A1AXC H43  H N N 15  
A1AXC H42  H N N 16  
A1AXC H11  H N N 17  
A1AXC H8   H N N 18  
A1AXC H9   H N N 19  
A1AXC H10  H N N 20  
A1AXC H32  H N N 21  
A1AXC H33  H N N 22  
A1AXC H23  H N N 23  
A1AXC H22  H N N 24  
A1AXC H53  H N N 25  
A1AXC H52  H N N 26  
A1AXC H7   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 
A1AXC O1  C1   doub N N 1   
A1AXC C1  N1   sing N N 2   
A1AXC C1  C6   sing N N 3   
A1AXC N1  C2   sing N N 4   
A1AXC N1  C5   sing N N 5   
A1AXC C2  C3   sing N N 6   
A1AXC C3  O2   sing N N 7   
A1AXC O2  C4   sing N N 8   
A1AXC C4  C5   sing N N 9   
A1AXC C6  C7   doub Y N 10  
A1AXC C6  C11  sing Y N 11  
A1AXC C7  C8   sing Y N 12  
A1AXC C8  C9   doub Y N 13  
A1AXC C9  C10  sing Y N 14  
A1AXC C10 C11  doub Y N 15  
A1AXC C4  H43  sing N N 16  
A1AXC C4  H42  sing N N 17  
A1AXC C11 H11  sing N N 18  
A1AXC C8  H8   sing N N 19  
A1AXC C9  H9   sing N N 20  
A1AXC C10 H10  sing N N 21  
A1AXC C3  H32  sing N N 22  
A1AXC C3  H33  sing N N 23  
A1AXC C2  H23  sing N N 24  
A1AXC C2  H22  sing N N 25  
A1AXC C5  H53  sing N N 26  
A1AXC C5  H52  sing N N 27  
A1AXC C7  H7   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                    7HAB 
_atom_sites.fract_transf_matrix[1][1]   0.015120 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011183 
_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]   0.009998 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU   A 1 9   ? 4.57053   -28.35295 -39.03083 1.000 52.94863  ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.83489   -27.63704 -39.21458 1.000 60.70322  ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 6.10669   -26.73501 -37.99079 1.000 44.97396  ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 5.40957   -25.73978 -37.77929 1.000 50.95720  ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.77355   -26.81512 -40.50766 1.000 67.37147  ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 6.57658   -25.50009 -40.56086 1.000 83.64624  ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 8.09802   -25.67155 -40.56983 1.000 97.17096  ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 8.61607   -26.67853 -40.03842 1.000 100.24663 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 8.78397   -24.76998 -41.11023 1.000 86.60266  ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 7.08099   -27.09668 -37.15764 1.000 37.71535  ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 7.30201   -26.42540 -35.88169 1.000 30.84126  ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.65964   -25.75916 -35.91964 1.000 30.83843  ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.64619   -26.40142 -36.27818 1.000 32.85551  ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 7.31135   -27.42968 -34.72711 1.000 34.43750  ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.54557   -26.73258 -33.39636 1.000 36.65014  ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 6.05246   -28.30084 -34.76766 1.000 39.12393  ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.70478   -24.48665 -35.60671 1.000 25.58461  ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.96118   -23.74078 -35.52487 1.000 23.87429  ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 10.35954  -23.57819 -34.06935 1.000 22.20490  ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.53807   -23.24393 -33.20422 1.000 21.77935  ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.81006   -22.36352 -36.14735 1.000 23.95571  ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.57104   -22.44022 -37.64762 1.000 26.19405  ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 9.39553   -21.06424 -38.23365 1.000 31.90826  ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 8.33984   -20.46375 -37.98110 1.000 34.96437  ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 10.23417  -20.63547 -39.06308 1.000 40.82399  ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.62371  -23.85913 -33.75739 1.000 21.48145  ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 12.16418  -23.77413 -32.42352 1.000 20.25973  ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 13.16752  -22.64481 -32.35441 1.000 19.28384  ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 14.03573  -22.55715 -33.21544 1.000 19.92421  ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.83219  -25.09423 -32.00157 1.000 20.89078  ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.94019  -26.18934 -32.11656 1.000 22.36092  ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 13.36038  -25.01105 -30.59869 1.000 19.94311  ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 13.00811  -21.78811 -31.38033 1.000 18.14584  ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.82802  -20.58972 -31.21175 1.000 19.25673  ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.43285  -20.57759 -29.82892 1.000 20.83186  ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.87202  -21.09548 -28.86834 1.000 19.56566  ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.90022  -19.32540 -31.20715 1.000 18.52587  ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 12.16250  -19.10989 -32.47220 1.000 18.96660  ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.95118  -19.80304 -32.72846 1.000 19.11473  ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.69358  -18.28300 -33.46501 1.000 21.38630  ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 10.31652  -19.61735 -33.97781 1.000 21.38714  ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 12.01481  -18.06135 -34.72454 1.000 25.08023  ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.81790  -18.73122 -34.97854 1.000 23.63242  ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.63315  -20.00230 -29.71573 1.000 18.21804  ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 16.20467  -19.72799 -28.41449 1.000 16.77983  ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.68545  -18.41676 -27.87171 1.000 18.48128  ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.62600  -17.40403 -28.57413 1.000 20.26337  ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.72015  -19.56999 -28.57304 1.000 17.29056  ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.36373  -18.40384 -26.56206 1.000 16.93121  ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 15.15742  -17.09595 -25.94583 1.000 17.54100  ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.45185  -16.28860 -25.98132 1.000 18.11111  ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.56710  -16.83032 -25.84589 1.000 20.86964  ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.75197  -17.23115 -24.45307 1.000 18.04945  ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.36451  -17.80910 -24.23822 1.000 16.48551  ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.20856  -17.04425 -24.52841 1.000 17.24025  ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.22100  -19.06312 -23.72808 1.000 18.01444  ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.91968  -17.58110 -24.31495 1.000 17.56647  ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.95918  -19.63853 -23.54835 1.000 17.00762  ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.82528  -18.88189 -23.80606 1.000 16.69353  ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.26332  -14.97335 -26.06144 1.000 18.21237  ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.42735  -14.11614 -25.79721 1.000 18.96537  ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.91747  -14.39427 -24.39240 1.000 20.64135  ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.12235  -14.73139 -23.49894 1.000 20.31420  ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.98942  -12.66506 -25.85943 1.000 24.16528  ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.60546  -12.18709 -27.24297 1.000 25.89274  ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 16.04416  -10.77557 -27.14849 1.000 36.56063  ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.85145  -10.62078 -27.11330 1.000 35.25609  ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.90941  -9.74292  -27.14209 1.000 35.64535  ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.23441  -14.24748 -24.17806 1.000 21.86393  ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.80088  -14.68219 -22.91577 1.000 21.28859  ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.15279  -13.99188 -21.73819 1.000 20.69514  ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 18.92236  -14.62646 -20.71742 1.000 23.19763  ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.29942  -14.37527 -22.95531 1.000 25.49675  ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.81956  -12.72551 -21.88803 1.000 23.12381  ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.24617  -11.98119 -20.77820 1.000 22.84639  ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.87035  -12.51011 -20.39828 1.000 21.73300  ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.49779  -12.51012 -19.20348 1.000 22.90043  ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.19723  -10.49777 -21.14544 1.000 27.39604  ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.53486  -9.80400  -21.40501 1.000 33.89973  ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.09367  -10.00312 -22.81797 1.000 37.28034  ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.48994  -10.69236 -23.66756 1.000 30.77106  ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.17720  -9.43108  -23.12214 1.000 42.52143  ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.11460  -13.00497 -21.37776 1.000 20.39609  ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.78515  -13.53634 -21.08918 1.000 17.01402  ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.90268  -14.91608 -20.47088 1.000 20.48587  ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.15629  -15.28235 -19.55583 1.000 21.00183  ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.92458  -13.54915 -22.37008 1.000 19.92824  ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.43531  -12.14417 -22.77542 1.000 24.08406  ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.64981  -14.40946 -22.20049 1.000 19.66605  ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.48988  -11.05273 -22.91025 1.000 28.32048  ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.85524  -15.72539 -20.95603 1.000 18.92943  ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.08723  -16.99253 -20.28067 1.000 18.04538  ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.47256  -16.75488 -18.81930 1.000 19.71579  ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.02294  -17.49180 -17.94256 1.000 21.24069  ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.21343  -17.77184 -21.01435 1.000 19.73056  ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.27090  -15.71895 -18.55243 1.000 20.30160  ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.66486  -15.41777 -17.18306 1.000 21.92210  ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.45218  -15.00738 -16.35918 1.000 24.35403  ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.33226  -15.43683 -15.20601 1.000 23.92152  ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.70435  -14.31436 -17.19562 1.000 25.43691  ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 19.42816  -14.15881 -15.88660 1.000 40.51136  ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.47436  -13.04404 -15.96435 1.000 70.78395  ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 21.26980  -12.86851 -15.04264 1.000 68.20474  ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 20.57289  -12.39695 -17.14091 1.000 47.91291  ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.56994  -14.17830 -16.93644 1.000 19.48538  ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.30628  -13.81234 -16.23644 1.000 21.47978  ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.50555  -15.05044 -15.87059 1.000 21.86370  ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 13.02089  -15.20482 -14.72951 1.000 22.26645  ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.46274  -12.90111 -17.14500 1.000 24.37028  ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.04851  -12.54932 -16.61336 1.000 22.98599  ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.26467  -11.61906 -15.40665 1.000 29.11049  ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.30449  -11.85031 -17.68348 1.000 24.51959  ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.33280  -15.95190 -16.83315 1.000 17.71567  ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.54515  -17.13825 -16.58990 1.000 18.59914  ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.18706  -17.99561 -15.50103 1.000 19.47998  ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.46993  -18.52488 -14.64197 1.000 20.50027  ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.34205  -17.93125 -17.87710 1.000 17.57342  ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.42609  -17.12369 -18.82251 1.000 18.67956  ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.36322  -17.89530 -20.50382 1.000 19.48534  ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.24701  -19.25913 -20.13144 1.000 20.91839  ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.52198  -18.20655 -15.53475 1.000 21.24242  ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.17285  -18.96079 -14.46383 1.000 19.11965  ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 14.98220  -18.30592 -13.11589 1.000 23.54850  ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.77058  -18.99299 -12.10796 1.000 25.90655  ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.67387  -19.13446 -14.75376 1.000 29.57495  ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 16.80960  -19.84125 -15.93643 1.000 41.45025  ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.03356  -16.99032 -13.07283 1.000 21.56923  ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.85082  -16.32620 -11.79188 1.000 22.30808  ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.44924  -16.58736 -11.26021 1.000 23.59940  ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.25791  -16.84217 -10.04912 1.000 24.55064  ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.10913  -14.82365 -11.94128 1.000 24.84337  ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 14.97638  -13.96623 -10.69178 1.000 29.49904  ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 15.82097  -12.74945 -10.80459 1.000 34.92484  ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 13.48770  -13.56249 -10.50080 1.000 39.17748  ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.45418  -16.49797 -12.14018 1.000 20.09277  ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.07727  -16.69102 -11.68055 1.000 19.65706  ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.87292  -18.12526 -11.23481 1.000 21.55985  ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.14405  -18.39474 -10.26384 1.000 22.28311  ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.13046  -16.32457 -12.82603 1.000 18.78883  ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.14485  -14.80834 -13.00704 1.000 22.02284  ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.70684   -16.88139 -12.60614 1.000 21.19707  ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.53876   -14.34476 -14.34033 1.000 22.07077  ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.48607  -19.07455 -11.94902 1.000 21.49652  ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.32324  -20.48085 -11.60093 1.000 23.07063  ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.09986  -20.85094 -10.33561 1.000 23.31898  ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.64530  -21.69285 -9.54735  1.000 26.06732  ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.73906  -21.34737 -12.81705 1.000 21.91407  ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.73916  -21.12652 -13.92513 1.000 22.19515  ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.87290  -22.81312 -12.42910 1.000 23.90401  ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.21621  -21.71474 -15.29059 1.000 22.79212  ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.30701  -20.29069 -10.13999 1.000 22.58698  ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.16204  -20.81238 -9.07067  1.000 26.35441  ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.10736  -20.03322 -7.76514  1.000 30.72137  ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.53132  -20.57588 -6.72587  1.000 36.36667  ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.59651  -20.83413 -9.55299  1.000 29.95978  ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.79474  -21.82274 -10.63886 1.000 41.59674  ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.10203  -22.84611 -10.68558 1.000 35.24428  ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.72026  -21.52657 -11.55378 1.000 48.31360  ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.66104  -18.78122 -7.78659  1.000 24.69601  ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.62112  -18.00233 -6.54709  1.000 23.05614  ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.54094  -18.50127 -5.60158  1.000 25.10612  ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.39796  -18.72158 -6.02133  1.000 25.00645  ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.41874  -16.51818 -6.89362  1.000 28.49618  ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.51459  -16.07838 -7.72049  1.000 29.49163  ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.48692  -15.68513 -5.63871  1.000 29.98670  ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.88461  -18.67768 -4.32871  1.000 26.33153  ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.87463  -18.94120 -3.33434  1.000 25.72176  ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.00637  -17.69317 -3.14711  1.000 27.46947  ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.51182  -16.62623 -2.76757  1.000 27.57615  ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.50757  -19.38758 -2.02602  1.000 27.18125  ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.47727  -19.70589 -0.98248  1.000 27.52483  ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.70048  -20.83984 -1.13933  1.000 33.46512  ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.23188  -18.86999 0.09098   1.000 28.45893  ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.68438   -21.13219 -0.22215  1.000 30.75202  ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.22661  -19.15559 0.99572   1.000 31.77489  ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.46800   -20.29262 0.86352   1.000 29.34755  ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.69579   -17.82623 -3.40219  1.000 23.13638  ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.81058   -16.67982 -3.30828  1.000 22.87735  ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.40095   -17.25449 -3.19846  1.000 21.71902  ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.89822   -17.83380 -4.16582  1.000 21.63551  ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 8.96025   -15.80414 -4.56576  1.000 24.35268  ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 7.99939   -14.62326 -4.56809  1.000 22.01548  ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.27280   -13.55533 -3.77715  1.000 27.89613  ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 6.85054   -14.58513 -5.42392  1.000 30.81164  ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.44566   -12.47174 -3.69262  1.000 33.61191  ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.00172   -13.44002 -5.36522  1.000 28.32377  ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.34494   -12.41519 -4.50497  1.000 28.92656  ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.56603   -11.24988 -4.35336  1.000 32.71320  ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.76652   -17.06803 -2.06597  1.000 22.50101  ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.50921   -17.74248 -1.77430  1.000 22.32152  ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.30550   -17.11333 -2.44432  1.000 23.41038  ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.34005   -17.83347 -2.68813  1.000 23.70803  ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.30814   -17.81345 -0.25474  1.000 23.76237  ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.35103   -18.63963 0.31651   1.000 24.98958  ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.34412   -15.83532 -2.81011  1.000 21.06509  ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.14102   -15.09902 -3.23040  1.000 21.23939  ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 2.92160   -15.30246 -4.72157  1.000 20.63983  ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 2.91645   -14.35021 -5.52060  1.000 22.20451  ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.34322   -13.63839 -2.90610  1.000 23.99401  ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.19024   -12.76491 -3.26051  1.000 24.33889  ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.03617   -13.15416 -3.13500  1.000 27.12778  ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.51521   -11.50724 -3.57951  1.000 26.20402  ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.73468   -16.56967 -5.08932  1.000 18.96242  ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.62951   -16.90851 -6.51653  1.000 18.40421  ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.32191   -16.44140 -7.17118  1.000 17.89554  ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.31323   -16.35761 -8.41685  1.000 18.21744  ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.68828   -18.43080 -6.65866  1.000 19.67692  ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.12361   -19.05109 -6.38109  1.000 19.19440  ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.05368   -20.57210 -6.50417  1.000 21.20957  ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.44352   -21.25240 -6.25862  1.000 21.48540  ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.41527   -20.96311 -7.37178  1.000 22.50621  ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.28842   -16.13623 -6.38538  1.000 17.60355  ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -1.01162  -15.86839 -6.98052  1.000 17.56606  ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.97579  -14.64764 -7.90980  1.000 18.40954  ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.92993  -14.45198 -8.67436  1.000 18.85490  ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -2.04783  -15.62079 -5.86913  1.000 19.43207  ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.87757  -14.32516 -5.10694  1.000 19.62758  ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.76041  -14.20359 -3.86498  1.000 25.12275  ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.93853  -15.18585 -3.14279  1.000 30.85317  ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.21028  -13.09651 -3.58441  1.000 35.80641  ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.03942   -13.76467 -7.78669  1.000 19.15799  ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.08048   -12.57417 -8.63342  1.000 18.09329  ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.16631   -12.92302 -10.12175 1.000 17.36635  ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? -0.05591  -12.03589 -10.94624 1.000 18.43201  ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.23431   -11.63019 -8.22109  1.000 21.14911  ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.56016   -12.33214 -8.39947  1.000 21.98525  ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 0.96516   -11.15900 -6.75181  1.000 22.43280  ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.16764   -11.99429 -9.74960  1.000 24.71419  ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.50156   -14.17518 -10.50149 1.000 15.98149  ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.51268   -14.47967 -11.93748 1.000 16.59505  ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.83499  -14.15581 -12.55989 1.000 17.19515  ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.90160  -13.71047 -13.72135 1.000 16.79489  ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.84544   -15.96623 -12.19486 1.000 17.52855  ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.32425  -16.88212 -11.98349 1.000 16.19909  ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.62863  -17.35289 -10.73636 1.000 17.82085  ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.14097  -17.22908 -13.04041 1.000 17.03528  ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.79803  -18.15230 -10.53527 1.000 18.21416  ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.27566  -18.01765 -12.85447 1.000 18.69166  ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.62369  -18.47852 -11.60799 1.000 17.49578  ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.92825  -14.36465 -11.79350 1.000 16.09588  ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.22031  -14.24952 -12.47508 1.000 15.77903  ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.55049  -12.77336 -12.68005 1.000 17.83245  ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.07009  -12.40541 -13.74858 1.000 17.58212  ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.28347  -14.92313 -11.62714 1.000 16.55615  ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.69164  -14.93715 -12.24141 1.000 17.10623  ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.66981  -15.63599 -13.56643 1.000 18.94408  ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.62685  -15.68481 -11.31052 1.000 19.94605  ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.18758  -11.91089 -11.70687 1.000 17.64392  ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.33321  -10.47876 -11.89464 1.000 16.78833  ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.56301  -10.01794 -13.11256 1.000 19.86721  ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -3.05954  -9.20297  -13.92844 1.000 19.02501  ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.84310  -9.71592  -10.64203 1.000 19.91349  ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.79498  -8.25550  -10.82407 1.000 23.80890  ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -2.07319  -7.61573  -9.59018  1.000 28.07243  ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.63358  -7.87597  -9.60153  1.000 31.99273  ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.15091   -7.79617  -8.53871  1.000 34.14844  ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.31804  -7.43683  -7.34834  1.000 33.91451  ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.46308   -8.01339  -8.68251  1.000 34.40560  ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.35537  -10.55326 -13.30039 1.000 16.92314  ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.55024  -10.07025 -14.39450 1.000 17.13992  ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.10187  -10.48516 -15.73940 1.000 17.67860  ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -1.06557  -9.69350  -16.68994 1.000 17.17189  ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.88584   -10.60528 -14.24682 1.000 17.09153  ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.59254   -10.11846 -12.98706 1.000 19.82928  ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.57870   -8.59132  -12.85314 1.000 21.41972  ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.65320   -7.86511  -13.86321 1.000 22.01317  ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.48530   -8.08721  -11.71860 1.000 26.76313  ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.61343  -11.71563 -15.84083 1.000 15.05984  ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.16400  -12.14483 -17.13458 1.000 16.35225  ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.46333  -11.42211 -17.41400 1.000 16.49630  ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.74464  -11.10340 -18.58400 1.000 16.54657  ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.37365  -13.65423 -17.12608 1.000 16.39595  ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.02996  -14.41088 -17.06763 1.000 17.88096  ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.32944  -15.96238 -16.95625 1.000 19.80877  ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.12155  -14.13833 -18.26656 1.000 18.72567  ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.32146  -11.22538 -16.38996 1.000 15.24148  ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.55373  -10.45877 -16.61729 1.000 15.05130  ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.23170  -9.03445  -17.03116 1.000 16.37436  ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.90340  -8.47378  -17.91355 1.000 16.64571  ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.43882  -10.52842 -15.36879 1.000 15.18013  ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -6.99777  -11.94884 -15.30147 1.000 15.26173  ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.58281  -9.47457  -15.40987 1.000 18.70581  ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.72508  -12.16998 -13.91214 1.000 18.07528  ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.17882  -8.43539  -16.43446 1.000 16.62295  ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.81210  -7.09134  -16.83311 1.000 15.32376  ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.34557  -7.09519  -18.29508 1.000 17.09781  ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.68923  -6.17144  -19.05811 1.000 17.75364  ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.68566  -6.62629  -15.90751 1.000 19.58781  ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.19137  -5.35768  -16.30862 1.000 25.85067  ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.57815  -8.10944  -18.69788 1.000 16.87665  ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.16858  -8.16875  -20.09790 1.000 16.74884  ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.37564  -8.28932  -20.99662 1.000 17.16559  ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.41030  -7.67741  -22.06744 1.000 17.45668  ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.23575  -9.36607  -20.32398 1.000 17.08832  ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.10623   -9.15339  -19.77258 1.000 23.59459  ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.45593   -8.07060  -19.29367 1.000 23.65747  ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 0.91934   -10.20071 -19.90147 1.000 25.47646  ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.37162  -9.08134  -20.58604 1.000 15.27620  ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.57311  -9.21569  -21.41826 1.000 16.87586  ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.29595  -7.88404  -21.51570 1.000 16.95854  ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.75617  -7.49500  -22.59955 1.000 16.32897  ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.51618  -10.26440 -20.83214 1.000 16.94171  ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -5.95623  -11.57621 -20.96114 1.000 16.74956  ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.42107  -7.16728  -20.38543 1.000 15.04136  ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -7.06842  -5.85343  -20.41170 1.000 15.76083  ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.31785  -4.91809  -21.36848 1.000 17.50943  ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.95073  -4.19770  -22.14929 1.000 18.01200  ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.12847  -5.30114  -18.97142 1.000 17.63899  ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.64293  -3.95732  -18.98513 1.000 18.87924  ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -4.97188  -4.91129  -21.32659 1.000 16.61474  ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.22526  -4.04254  -22.23930 1.000 16.72412  ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.49185  -4.41525  -23.69784 1.000 18.57555  ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.59363  -3.52525  -24.55252 1.000 18.12902  ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.73009  -4.21374  -21.95116 1.000 16.65248  ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.28823  -3.53073  -20.65492 1.000 22.51367  ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -3.09293  -2.78672  -20.02357 1.000 23.96051  ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -1.10712  -3.75250  -20.21679 1.000 24.12793  ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.61269  -5.72368  -23.99568 1.000 15.47940  ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -4.88848  -6.17544  -25.35922 1.000 16.04511  ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.27550  -5.74668  -25.80766 1.000 16.21955  ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.49218  -5.42851  -26.99131 1.000 16.27714  ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.74973  -7.70454  -25.44568 1.000 16.93915  ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.24546  -5.85422  -24.88929 1.000 15.68682  ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.59402  -5.42057  -25.19715 1.000 16.98022  ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.63499  -3.91677  -25.41991 1.000 17.58711  ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.32937  -3.44485  -26.32410 1.000 17.89039  ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.52206  -5.86588  -24.06918 1.000 16.67813  ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.71472  -7.37313  -24.07552 1.000 15.70639  ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.17056 -7.84702  -22.67676 1.000 18.42450  ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.82961 -7.70034  -25.04938 1.000 17.25411  ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.89398  -3.14601  -24.62097 1.000 16.41594  ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.89719  -1.69627  -24.83971 1.000 17.41433  ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.36841  -1.37092  -26.22808 1.000 18.10117  ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.84500  -0.43129  -26.87249 1.000 18.98356  ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.97257  -1.01630  -23.81797 1.000 17.72488  ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.48134  -0.98926  -22.39194 1.000 19.41404  ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.61207  -1.35549  -22.09669 1.000 22.22525  ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.66549  -0.54961  -21.54582 1.000 22.24619  ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.38836  -2.15427  -26.71599 1.000 17.12783  ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.79573  -1.81641  -28.01752 1.000 18.11716  ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.76555  -2.05643  -29.16222 1.000 17.81364  ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -6.86236  -1.21624  -30.06740 1.000 20.30842  ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.54403  -2.68307  -28.22074 1.000 19.74193  ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.36008  -2.25348  -27.38306 1.000 20.01868  ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.23441  -3.29463  -27.56738 1.000 20.02337  ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.16023  -3.07185  -26.50517 1.000 24.53675  ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 0.00238   -4.07959  -26.64884 1.000 28.69262  ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.52230  -3.16093  -29.14011 1.000 17.63746  ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.50429  -3.36636  -30.21849 1.000 17.83266  ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.67770  -2.40956  -30.06216 1.000 19.21904  ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.19085 -1.91405  -31.07593 1.000 20.36281  ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -8.92509  -4.83277  -30.33383 1.000 19.21223  ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.72011  -5.10440  -31.63627 1.000 19.32574  ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.78236  -5.27975  -29.13315 1.000 20.14661  ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -8.90892  -4.83507  -32.95098 1.000 24.29202  ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.04580 -2.05689  -28.82590 1.000 18.02537  ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.09891 -1.05181  -28.67239 1.000 18.80531  ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.66671 0.26208   -29.30546 1.000 19.42034  ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.42743 0.90604   -30.04696 1.000 21.58823  ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.46189 -0.88812  -27.19386 1.000 22.39242  ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.55150 0.16511   -27.04921 1.000 28.15319  ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -12.98121 0.27235   -25.65746 1.000 34.30558  ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.01948 -0.67466  -25.28018 1.000 39.31032  ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.20696 -1.03234  -24.02142 1.000 45.66804  ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.34171 -0.68528  -23.08385 1.000 36.56724  ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.27868 -1.75141  -23.70114 1.000 37.73000  ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.41344  0.70042   -29.03105 1.000 19.31240  ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -8.98602  1.97856   -29.58145 1.000 20.23723  ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -8.99828  1.94166   -31.10774 1.000 23.74620  ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.47263  2.88381   -31.76124 1.000 23.84628  ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.58025  2.31315   -29.05039 1.000 20.57862  ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.14734  3.69201   -29.53595 1.000 22.47896  ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.68650  4.86660   -29.01334 1.000 22.85861  ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.24602  3.78102   -30.56152 1.000 22.29113  ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.31993  6.10019   -29.48537 1.000 24.32213  ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.84817  5.01408   -31.07445 1.000 23.76602  ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.38357  6.17338   -30.52809 1.000 24.73735  ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -6.00911  7.40471   -31.00126 1.000 26.88096  ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.50535  0.85076   -31.68608 1.000 21.78775  ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.46862  0.79000   -33.14761 1.000 23.98850  ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -9.88079  0.82553   -33.70470 1.000 26.65239  ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.13288 1.41491   -34.77010 1.000 27.67352  ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.78916  -0.49334  -33.61831 1.000 22.50918  ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.26264  -0.38122  -33.43738 1.000 23.93477  ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.51344  -1.52262  -34.07024 1.000 31.66007  ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -6.17851  -2.47253  -34.53330 1.000 32.60844  ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -4.24363  -1.45760  -34.12921 1.000 34.89161  ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.82901 0.20975   -33.00094 1.000 22.37964  ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.20881 0.19312   -33.49248 1.000 23.39868  ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -12.87957 1.55459   -33.44403 1.000 25.13286  ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -13.90766 1.74656   -34.10186 1.000 26.24361  ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.02870 -0.82588  -32.70320 1.000 23.69570  ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.45703 -0.28181  -31.41662 1.000 26.81224  ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.37926 2.50114   -32.65927 1.000 24.93917  ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -13.06365 3.78790   -32.55893 1.000 26.27241  ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -13.02558 4.52787   -33.87174 1.000 30.11120  ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.87846 5.38928   -34.11997 1.000 36.09813  ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.40844 4.68172   -31.48659 1.000 26.26080  ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.51862 4.12629   -30.05421 1.000 26.45531  ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.86068 5.12663   -29.11113 1.000 27.08716  ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.93724 3.85891   -29.65533 1.000 31.59085  ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -12.03601 4.25385   -34.70679 1.000 27.63321  ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -11.96157 4.91013   -36.01801 1.000 30.46767  ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.16155 3.95253   -37.18548 1.000 35.19567  ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.23320 4.39456   -38.33959 1.000 39.99739  ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.62632 5.62861   -36.17868 1.000 34.21987  ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.56991  4.67026   -36.09131 1.000 39.24049  ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.43540 6.69907   -35.12606 1.000 31.33281  ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.30518 2.65913   -36.92280 1.000 31.80061  ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.46013 1.66882   -37.98769 1.000 31.49681  ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.27911 0.53735   -37.39092 1.000 30.90442  ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.73333 -0.40955  -36.81598 1.000 30.07696  ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -11.09336 1.16383   -38.44260 1.000 29.90932  ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.20385 0.13122   -39.55339 1.000 38.26348  ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.33854 -0.16199  -39.94238 1.000 37.02034  ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.17592 -0.33937  -40.06193 1.000 40.27744  ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.60452 0.61207   -37.47047 1.000 34.66611  ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.40443 -0.41756  -36.78481 1.000 31.16311  ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.17972 -1.78791  -37.38167 1.000 29.94857  ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.46357 -2.78924  -36.69858 1.000 31.85224  ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.85659 0.01975   -37.03384 1.000 35.94290  ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.79782 1.40580   -37.50233 1.000 45.10257  ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.39606 1.78989   -37.86881 1.000 39.77687  ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.65843 -1.87303  -38.62593 1.000 30.83556  ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.44108 -3.18849  -39.21335 1.000 31.84732  ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.36279 -3.97100  -38.47282 1.000 29.64582  ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.21897 -5.17306  -38.71162 1.000 29.20291  ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.06240 -3.12466  -40.69182 1.000 34.14126  ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -12.73878 -2.64169  -40.84913 1.000 37.77335  ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.60061 -3.32860  -37.57220 1.000 26.22713  ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.63863 -4.06022  -36.76397 1.000 26.68803  ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.31462 -5.09747  -35.87943 1.000 23.92976  ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.65021 -6.00903  -35.36592 1.000 24.58363  ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.89900 -3.06001  -35.87138 1.000 29.38648  ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -10.01027 -2.07949  -36.64503 1.000 32.27570  ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.63269  -2.65096  -36.83346 1.000 33.90493  ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.68449  -1.73022  -37.62337 1.000 36.19097  ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.31890  -2.38625  -37.63125 1.000 35.30287  ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.61181 -4.93867  -35.60263 1.000 24.58210  ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.34586 -5.87671  -34.77228 1.000 24.52068  ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.15981 -6.85745  -35.58402 1.000 23.95799  ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -15.93639 -7.60729  -34.99136 1.000 29.91848  ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.27403 -5.13716  -33.79701 1.000 25.86883  ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.53518 -4.21888  -32.79973 1.000 26.77202  ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.56933 -3.50130  -31.87831 1.000 30.87015  ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.57688 -5.00997  -31.98075 1.000 25.48879  ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -14.92204 -6.94396  -36.88522 1.000 26.83726  ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.62576 -7.94623  -37.68314 1.000 28.87792  ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.26017 -9.34448  -37.20872 1.000 29.48968  ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.02218 -10.29277 -37.42769 1.000 32.09406  ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.23994 -7.79180  -39.15730 1.000 32.03569  ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -15.94795 -6.61263  -39.83970 1.000 38.54459  ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -16.77334 -5.95534  -39.16411 1.000 35.97349  ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.62719 -6.29363  -41.01181 1.000 40.21446  ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.07135 -9.49582  -36.62199 1.000 26.16373  ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.59964 -10.74126 -36.05463 1.000 25.51543  ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.15135 -11.02902 -34.68787 1.000 30.94810  ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -13.72130 -11.98871 -34.04280 1.000 32.34263  ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.05688 -10.69874 -36.04643 1.000 26.72045  ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.57863 -9.48968  -35.47931 1.000 25.22325  ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.06427 -10.19738 -34.18235 1.000 27.25797  ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.59130 -10.46698 -32.87153 1.000 30.22630  ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -15.91082 -9.16413  -32.17101 1.000 27.87238  ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.00516 -8.39928  -31.87366 1.000 24.78600  ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.18191 -8.88948  -31.89218 1.000 27.73242  ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.52421 -7.62244  -31.26865 1.000 25.08346  ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.35963 -7.65628  -29.75635 1.000 25.09669  ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.23098 -6.59534  -29.15291 1.000 28.58999  ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -18.99342 -7.23716  -31.56199 1.000 31.43131  ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.09512 -6.37475  -32.80400 1.000 41.55008  ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.51040 -6.43247  -33.36809 1.000 53.90596  ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.53921 -6.41918  -34.88913 1.000 62.24652  ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -21.62679 -5.50680  -35.37766 1.000 76.29799  ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.41052 -8.83296  -29.13681 1.000 23.04083  ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.41918 -8.86514  -27.66713 1.000 22.93182  ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -15.99759 -8.74065  -27.14188 1.000 21.68637  ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.10267 -9.36958  -27.67988 1.000 23.53126  ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -17.94008 -10.20734 -27.19765 1.000 30.66700  ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -19.43944 -10.45992 -27.41972 1.000 38.41651  ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -19.83878 -10.58842 -28.88447 1.000 86.93067  ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -19.04930 -11.18315 -29.65691 1.000 88.15940  ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -20.93556 -10.09743 -29.26147 1.000 81.55255  ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -15.84051 -7.95569  -26.09513 1.000 21.55644  ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.54308 -7.66476  -25.46322 1.000 18.31158  ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.62100 -8.16739  -24.03307 1.000 18.08635  ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.31057 -7.58884  -23.17734 1.000 19.88636  ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.32253 -6.16094  -25.50803 1.000 21.03313  ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.22108 -5.58201  -26.93110 1.000 24.36772  ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.80502 -4.12341  -26.78471 1.000 32.37741  ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.16719 -6.25833  -27.78036 1.000 22.02040  ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -13.97690 -9.32006  -23.80295 1.000 16.94325  ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.13153 -9.96671  -22.50917 1.000 17.40010  ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -12.93418 -10.83421 -22.21233 1.000 15.73939  ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.05592 -11.06276 -23.06977 1.000 15.88072  ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.42950 -10.81792 -22.50321 1.000 18.29407  ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.41236 -11.93640 -23.50530 1.000 18.48623  ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.35450 -12.03035 -24.50553 1.000 26.04722  ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.56976 -12.98234 -23.68204 1.000 22.14494  ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.09326 -13.08285 -25.25133 1.000 25.86677  ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.05879 -13.71048 -24.75938 1.000 24.39517  ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -12.91887 -11.33001 -20.97306 1.000 16.33183  ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -11.90357 -12.22806 -20.43919 1.000 15.84486  ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.58714 -13.42702 -19.78596 1.000 16.70290  ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.48294 -13.24158 -18.95015 1.000 17.09773  ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.06839 -11.48966 -19.37900 1.000 16.06270  ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.38697 -10.27296 -19.98281 1.000 16.86533  ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -10.05688 -12.46558 -18.72127 1.000 17.34864  ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.70003  -9.34447  -18.93907 1.000 17.86651  ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.19604 -14.64781 -20.17721 1.000 15.67039  ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.75611 -15.85478 -19.58876 1.000 15.36630  ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.63709 -16.59760 -18.87406 1.000 16.46932  ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.49516 -16.68651 -19.35173 1.000 16.28229  ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.35783 -16.76684 -20.65682 1.000 15.92414  ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.54920 -16.17949 -21.30738 1.000 17.50149  ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.27389 -15.39546 -20.70738 1.000 19.31475  ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.81468 -16.57288 -22.56491 1.000 21.86346  ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -11.94839 -17.15899 -17.70764 1.000 16.02869  ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -10.98649 -17.95820 -16.95100 1.000 14.24787  ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.54727 -19.36016 -16.91809 1.000 14.85795  ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.68548 -19.58435 -16.45905 1.000 16.51133  ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.82076 -17.45291 -15.51839 1.000 15.99604  ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.50316 -15.96868 -15.42900 1.000 16.85558  ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.48660 -15.58364 -13.95547 1.000 18.22322  ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.17393  -15.65226 -16.11879 1.000 16.89152  ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.79117 -20.31076 -17.46007 1.000 16.20554  ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.31496 -21.65855 -17.67596 1.000 17.36904  ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.40302 -22.66160 -16.99873 1.000 18.94084  ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.38462  -23.06305 -17.55290 1.000 18.46173  ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.48195 -21.99874 -19.16486 1.000 18.76009  ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.20005 -20.84928 -19.87684 1.000 19.40860  ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.15902 -23.36323 -19.31559 1.000 19.51983  ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.35433 -21.06362 -21.36630 1.000 21.61468  ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.77459 -23.15106 -15.82804 1.000 18.93431  ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.02219 -24.20801 -15.15889 1.000 19.03984  ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.45883 -25.55149 -15.69773 1.000 21.38923  ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.62739 -25.77978 -15.99092 1.000 22.90241  ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.46163 -24.03961 -13.69602 1.000 20.85006  ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.84597 -23.51689 -13.72843 1.000 22.49194  ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -11.96228 -22.72521 -15.05640 1.000 23.90603  ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.50598  -26.46149 -15.80947 1.000 20.17320  ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.79616  -27.83333 -16.21446 1.000 21.84791  ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -8.97413  -28.76452 -15.34052 1.000 23.49347  ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.76947  -28.91761 -15.55892 1.000 23.67136  ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.54387  -28.06620 -17.69901 1.000 23.95485  ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -9.99904  -29.45119 -18.14065 1.000 27.34321  ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.66189  -30.45598 -17.51717 1.000 29.75350  ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.89480 -29.48420 -19.10670 1.000 35.45458  ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.61101  -29.43273 -14.38698 1.000 23.68014  ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -8.86287  -30.27828 -13.45648 1.000 25.37126  ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.41912  -31.58221 -14.08809 1.000 28.32120  ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.42775  -32.14819 -13.63261 1.000 30.44709  ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.66027  -30.61312 -12.19138 1.000 27.00161  ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -9.85108  -29.37313 -11.27190 1.000 28.19818  ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.66037 -29.73011 -10.01510 1.000 29.85630  ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.01287 -28.49588 -9.19788  1.000 32.30615  ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -12.02884 -27.67568 -9.91104  1.000 39.75295  ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.07885  -32.04137 -15.15866 1.000 29.79475  ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.65568  -33.30973 -15.75390 1.000 32.17155  ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.37409  -33.12806 -16.54866 1.000 30.17744  ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.52267  -34.03448 -16.58702 1.000 34.41741  ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.73936  -33.88666 -16.66192 1.000 39.04170  ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -10.98962 -34.38660 -15.95720 1.000 57.04555  ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -11.74612 -33.29234 -15.22576 1.000 73.92631  ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -12.21640 -33.49835 -14.10216 1.000 78.28998  ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -11.89269 -32.12484 -15.87324 1.000 58.90336  ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.21954  -31.96999 -17.16320 1.000 26.60937  ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.02866  -31.67071 -17.94838 1.000 26.52184  ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.01479  -30.90652 -17.10466 1.000 25.08936  ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -3.88751  -30.69999 -17.56527 1.000 27.14544  ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.37943  -30.75644 -19.12863 1.000 36.12094  ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.31914  -31.40395 -20.14505 1.000 40.16759  ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.52310  -32.63674 -20.13167 1.000 43.14015  ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.90100  -30.61854 -20.93346 1.000 43.85292  ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.39959  -30.49246 -15.89493 1.000 24.00182  ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.52314  -29.68387 -15.01590 1.000 21.34314  ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.09397  -28.38561 -15.68750 1.000 22.08030  ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -2.90102  -27.97715 -15.64513 1.000 22.14592  ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.34371  -30.45577 -14.43296 1.000 24.93564  ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -2.90898  -29.81558 -13.11649 1.000 24.46714  ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.48614  -29.99216 -12.78391 1.000 43.56228  ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -1.24848  -31.39610 -12.65051 1.000 38.56001  ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? -0.06449  -31.99196 -12.70842 1.000 52.40358  ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 1.04299   -31.33091 -13.01858 1.000 39.19798  ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 0.01542   -33.27990 -12.41480 1.000 44.70484  ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.06320  -27.71059 -16.30049 1.000 21.04573  ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.77335  -26.46267 -16.97995 1.000 19.78181  ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.68213  -25.34384 -16.51262 1.000 19.39536  ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.85441  -25.55795 -16.18874 1.000 19.26975  ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -4.89918  -26.54645 -18.49082 1.000 19.32614  ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.23487  -26.96403 -18.85679 1.000 21.87603  ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -3.85278  -27.49140 -19.06538 1.000 20.71893  ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.14442  -24.14165 -16.45156 1.000 16.68481  ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -5.94969  -22.94781 -16.27681 1.000 16.43138  ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.73536  -22.10225 -17.51642 1.000 16.71284  ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.58635  -21.76819 -17.85541 1.000 17.71236  ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.50777  -22.12085 -15.05053 1.000 18.18767  ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.24170  -20.75999 -14.84761 1.000 16.18754  ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.73882  -21.00960 -14.57993 1.000 18.19468  ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.67869  -20.03217 -13.64663 1.000 18.43841  ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.80939  -21.76814 -18.21850 1.000 16.23442  ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.69567  -21.01732 -19.45661 1.000 15.69936  ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.28788  -19.63031 -19.27764 1.000 17.32077  ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.39407  -19.46127 -18.70414 1.000 17.81369  ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.44472  -21.74313 -20.57666 1.000 17.30413  ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.87127  -23.05553 -20.77179 1.000 18.63929  ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.37410  -20.96373 -21.87723 1.000 20.55455  ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.57068  -18.61493 -19.71173 1.000 16.36798  ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.02293  -17.23804 -19.66713 1.000 15.41352  ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.29926  -16.82532 -21.08782 1.000 17.28871  ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.34910  -16.75152 -21.88219 1.000 17.05964  ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -6.03215  -16.30662 -18.98079 1.000 16.54125  ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.80924  -16.74916 -17.52426 1.000 20.93238  ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.56170  -14.87397 -19.02740 1.000 17.93054  ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.65277  -17.68190 -17.26275 1.000 24.95303  ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.56697  -16.56613 -21.45581 1.000 15.66472  ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -8.93016  -16.23883 -22.83795 1.000 15.25543  ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.33158  -14.78607 -22.88076 1.000 16.57163  ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.14566 -14.34348 -22.07216 1.000 18.52988  ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.15762 -17.06199 -23.28978 1.000 17.53198  ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.42919 -16.73196 -24.78050 1.000 20.91931  ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -9.87525  -18.55767 -23.12721 1.000 19.89367  ? 92  VAL   A CG2 1 
ATOM   622  N N   A ASP   A 1 86  ? -8.83736  -14.04588 -23.86349 0.500 16.18821  ? 93  ASP   A N   1 
ATOM   623  N N   B ASP   A 1 86  ? -8.83736  -14.04588 -23.86349 0.500 16.18821  ? 93  ASP   A N   1 
ATOM   624  C CA  A ASP   A 1 86  ? -9.37335  -12.71070 -24.07442 0.500 15.74734  ? 93  ASP   A CA  1 
ATOM   625  C CA  B ASP   A 1 86  ? -9.37335  -12.71070 -24.07442 0.500 15.74734  ? 93  ASP   A CA  1 
ATOM   626  C C   A ASP   A 1 86  ? -9.62242  -12.50326 -25.55682 0.500 16.58596  ? 93  ASP   A C   1 
ATOM   627  C C   B ASP   A 1 86  ? -9.62242  -12.50326 -25.55682 0.500 16.58596  ? 93  ASP   A C   1 
ATOM   628  O O   A ASP   A 1 86  ? -9.05404  -13.19593 -26.40723 0.500 16.50601  ? 93  ASP   A O   1 
ATOM   629  O O   B ASP   A 1 86  ? -9.05404  -13.19593 -26.40723 0.500 16.50601  ? 93  ASP   A O   1 
ATOM   630  C CB  A ASP   A 1 86  ? -8.43154  -11.60919 -23.51530 0.500 17.34171  ? 93  ASP   A CB  1 
ATOM   631  C CB  B ASP   A 1 86  ? -8.43154  -11.60919 -23.51530 0.500 17.34171  ? 93  ASP   A CB  1 
ATOM   632  C CG  A ASP   A 1 86  ? -7.13185  -11.49174 -24.29718 0.500 19.35282  ? 93  ASP   A CG  1 
ATOM   633  C CG  B ASP   A 1 86  ? -7.13185  -11.49174 -24.29718 0.500 19.35282  ? 93  ASP   A CG  1 
ATOM   634  O OD1 A ASP   A 1 86  ? -7.12811  -11.08612 -25.47726 0.500 17.92576  ? 93  ASP   A OD1 1 
ATOM   635  O OD1 B ASP   A 1 86  ? -7.12811  -11.08612 -25.47726 0.500 17.92576  ? 93  ASP   A OD1 1 
ATOM   636  O OD2 A ASP   A 1 86  ? -6.06372  -11.80498 -23.69874 0.500 18.62851  ? 93  ASP   A OD2 1 
ATOM   637  O OD2 B ASP   A 1 86  ? -6.06372  -11.80498 -23.69874 0.500 18.62851  ? 93  ASP   A OD2 1 
ATOM   638  N N   . THR   A 1 87  ? -10.48531 -11.55754 -25.87415 1.000 15.61355  ? 94  THR   A N   1 
ATOM   639  C CA  . THR   A 1 87  ? -10.76035 -11.21261 -27.25583 1.000 16.14435  ? 94  THR   A CA  1 
ATOM   640  C C   . THR   A 1 87  ? -10.12598 -9.87520  -27.63659 1.000 17.92624  ? 94  THR   A C   1 
ATOM   641  O O   . THR   A 1 87  ? -10.69034 -9.03522  -28.35611 1.000 17.65977  ? 94  THR   A O   1 
ATOM   642  C CB  . THR   A 1 87  ? -12.23177 -11.16085 -27.51988 1.000 17.88681  ? 94  THR   A CB  1 
ATOM   643  O OG1 . THR   A 1 87  ? -12.89111 -10.35484 -26.50839 1.000 18.23367  ? 94  THR   A OG1 1 
ATOM   644  C CG2 . THR   A 1 87  ? -12.85507 -12.59959 -27.40485 1.000 19.73818  ? 94  THR   A CG2 1 
ATOM   645  N N   . GLY   A 1 88  ? -8.91527  -9.65116  -27.14315 1.000 16.59277  ? 95  GLY   A N   1 
ATOM   646  C CA  . GLY   A 1 88  ? -8.21352  -8.42995  -27.47912 1.000 18.58138  ? 95  GLY   A CA  1 
ATOM   647  C C   . GLY   A 1 88  ? -7.59479  -8.47309  -28.85602 1.000 17.46562  ? 95  GLY   A C   1 
ATOM   648  O O   . GLY   A 1 88  ? -7.98355  -9.23147  -29.75484 1.000 17.27794  ? 95  GLY   A O   1 
ATOM   649  N N   . ILE   A 1 89  ? -6.59384  -7.60190  -29.02636 1.000 16.33738  ? 96  ILE   A N   1 
ATOM   650  C CA  . ILE   A 1 89  ? -6.01233  -7.39848  -30.37330 1.000 17.73325  ? 96  ILE   A CA  1 
ATOM   651  C C   . ILE   A 1 89  ? -5.25011  -8.60916  -30.88040 1.000 18.07021  ? 96  ILE   A C   1 
ATOM   652  O O   . ILE   A 1 89  ? -5.03419  -8.75192  -32.09100 1.000 19.08397  ? 96  ILE   A O   1 
ATOM   653  C CB  . ILE   A 1 89  ? -5.16475  -6.09978  -30.38175 1.000 18.06095  ? 96  ILE   A CB  1 
ATOM   654  C CG1 . ILE   A 1 89  ? -4.84789  -5.63954  -31.81533 1.000 19.86026  ? 96  ILE   A CG1 1 
ATOM   655  C CG2 . ILE   A 1 89  ? -3.88023  -6.30699  -29.55992 1.000 17.96725  ? 96  ILE   A CG2 1 
ATOM   656  C CD1 . ILE   A 1 89  ? -4.49397  -4.16232  -31.86342 1.000 22.92322  ? 96  ILE   A CD1 1 
ATOM   657  N N   . GLY   A 1 90  ? -4.81391  -9.52319  -29.98730 1.000 17.34771  ? 97  GLY   A N   1 
ATOM   658  C CA  . GLY   A 1 90  ? -4.05195  -10.65891 -30.47135 1.000 16.99066  ? 97  GLY   A CA  1 
ATOM   659  C C   . GLY   A 1 90  ? -2.61986  -10.25766 -30.81477 1.000 16.68916  ? 97  GLY   A C   1 
ATOM   660  O O   . GLY   A 1 90  ? -2.15777  -9.11747  -30.59128 1.000 18.89948  ? 97  GLY   A O   1 
ATOM   661  N N   . MET   A 1 91  ? -1.91370  -11.25742 -31.32469 1.000 16.30799  ? 98  MET   A N   1 
ATOM   662  C CA  . MET   A 1 91  ? -0.48677  -11.08623 -31.67688 1.000 18.46132  ? 98  MET   A CA  1 
ATOM   663  C C   . MET   A 1 91  ? -0.23697  -11.68608 -33.03086 1.000 18.98735  ? 98  MET   A C   1 
ATOM   664  O O   . MET   A 1 91  ? -0.72275  -12.76773 -33.34426 1.000 19.53342  ? 98  MET   A O   1 
ATOM   665  C CB  . MET   A 1 91  ? 0.41254   -11.81945 -30.66389 1.000 17.66994  ? 98  MET   A CB  1 
ATOM   666  C CG  . MET   A 1 91  ? 0.39607   -11.11840 -29.31276 1.000 18.02572  ? 98  MET   A CG  1 
ATOM   667  S SD  . MET   A 1 91  ? 1.44269   -11.86986 -28.04617 1.000 19.79923  ? 98  MET   A SD  1 
ATOM   668  C CE  . MET   A 1 91  ? 0.28011   -13.23949 -27.63569 1.000 22.14422  ? 98  MET   A CE  1 
ATOM   669  N N   . THR   A 1 92  ? 0.59971   -11.01484 -33.81372 1.000 19.21932  ? 99  THR   A N   1 
ATOM   670  C CA  . THR   A 1 92  ? 1.08614   -11.59425 -35.06174 1.000 19.58009  ? 99  THR   A CA  1 
ATOM   671  C C   . THR   A 1 92  ? 2.19444   -12.60167 -34.75930 1.000 20.29228  ? 99  THR   A C   1 
ATOM   672  O O   . THR   A 1 92  ? 2.67198   -12.69812 -33.63989 1.000 20.26072  ? 99  THR   A O   1 
ATOM   673  C CB  . THR   A 1 92  ? 1.66601   -10.49752 -35.97614 1.000 21.01017  ? 99  THR   A CB  1 
ATOM   674  O OG1 . THR   A 1 92  ? 2.81749   -9.90766  -35.31681 1.000 21.59959  ? 99  THR   A OG1 1 
ATOM   675  C CG2 . THR   A 1 92  ? 0.64486   -9.39112  -36.26114 1.000 23.97596  ? 99  THR   A CG2 1 
ATOM   676  N N   . LYS   A 1 93  ? 2.57537   -13.38444 -35.77896 1.000 19.77113  ? 100 LYS   A N   1 
ATOM   677  C CA  . LYS   A 1 93  ? 3.70749   -14.29750 -35.59098 1.000 19.70905  ? 100 LYS   A CA  1 
ATOM   678  C C   . LYS   A 1 93  ? 4.95049   -13.51903 -35.17295 1.000 19.20598  ? 100 LYS   A C   1 
ATOM   679  O O   . LYS   A 1 93  ? 5.65869   -13.93794 -34.26696 1.000 19.96667  ? 100 LYS   A O   1 
ATOM   680  C CB  . LYS   A 1 93  ? 3.96031   -15.03030 -36.91273 1.000 22.23417  ? 100 LYS   A CB  1 
ATOM   681  C CG  . LYS   A 1 93  ? 5.01914   -16.10603 -36.70274 1.000 22.02655  ? 100 LYS   A CG  1 
ATOM   682  C CD  . LYS   A 1 93  ? 5.37643   -16.73717 -38.07213 1.000 24.38605  ? 100 LYS   A CD  1 
ATOM   683  C CE  . LYS   A 1 93  ? 6.27597   -17.96329 -37.82909 1.000 26.01119  ? 100 LYS   A CE  1 
ATOM   684  N NZ  . LYS   A 1 93  ? 7.01057   -18.28605 -39.08981 1.000 29.96347  ? 100 LYS   A NZ  1 
ATOM   685  N N   . ALA   A 1 94  ? 5.19737   -12.35635 -35.81073 1.000 20.88783  ? 101 ALA   A N   1 
ATOM   686  C CA  . ALA   A 1 94  ? 6.34045   -11.53576 -35.41323 1.000 24.68089  ? 101 ALA   A CA  1 
ATOM   687  C C   . ALA   A 1 94  ? 6.24660   -11.10442 -33.96355 1.000 21.24634  ? 101 ALA   A C   1 
ATOM   688  O O   . ALA   A 1 94  ? 7.25233   -11.14163 -33.22926 1.000 23.02255  ? 101 ALA   A O   1 
ATOM   689  C CB  . ALA   A 1 94  ? 6.49451   -10.34107 -36.35315 1.000 24.73958  ? 101 ALA   A CB  1 
ATOM   690  N N   . ASP   A 1 95  ? 5.04293   -10.75275 -33.48632 1.000 19.86363  ? 102 ASP   A N   1 
ATOM   691  C CA  . ASP   A 1 95  ? 4.91787   -10.38097 -32.08052 1.000 19.69084  ? 102 ASP   A CA  1 
ATOM   692  C C   . ASP   A 1 95  ? 5.22546   -11.53559 -31.17660 1.000 19.00942  ? 102 ASP   A C   1 
ATOM   693  O O   . ASP   A 1 95  ? 5.90495   -11.37539 -30.14552 1.000 20.75455  ? 102 ASP   A O   1 
ATOM   694  C CB  . ASP   A 1 95  ? 3.47056   -9.95363  -31.75791 1.000 20.47573  ? 102 ASP   A CB  1 
ATOM   695  C CG  . ASP   A 1 95  ? 3.05373   -8.66032  -32.36756 1.000 22.92407  ? 102 ASP   A CG  1 
ATOM   696  O OD1 . ASP   A 1 95  ? 3.84386   -7.72188  -32.54014 1.000 27.23214  ? 102 ASP   A OD1 1 
ATOM   697  O OD2 . ASP   A 1 95  ? 1.82589   -8.49223  -32.63843 1.000 25.93442  ? 102 ASP   A OD2 1 
ATOM   698  N N   . LEU   A 1 96  ? 4.77334   -12.73529 -31.52325 1.000 18.06890  ? 103 LEU   A N   1 
ATOM   699  C CA  . LEU   A 1 96  ? 5.05082   -13.88968 -30.66932 1.000 19.48787  ? 103 LEU   A CA  1 
ATOM   700  C C   . LEU   A 1 96  ? 6.52200   -14.08111 -30.52617 1.000 20.44175  ? 103 LEU   A C   1 
ATOM   701  O O   . LEU   A 1 96  ? 7.01692   -14.28608 -29.40627 1.000 18.92557  ? 103 LEU   A O   1 
ATOM   702  C CB  . LEU   A 1 96  ? 4.45506   -15.18898 -31.24985 1.000 20.60408  ? 103 LEU   A CB  1 
ATOM   703  C CG  . LEU   A 1 96  ? 2.96197   -15.31873 -31.05031 1.000 19.09950  ? 103 LEU   A CG  1 
ATOM   704  C CD1 . LEU   A 1 96  ? 2.54808   -16.56769 -31.82583 1.000 18.87815  ? 103 LEU   A CD1 1 
ATOM   705  C CD2 . LEU   A 1 96  ? 2.58136   -15.39515 -29.55564 1.000 19.48940  ? 103 LEU   A CD2 1 
ATOM   706  N N   . ILE   A 1 97  ? 7.22821   -14.04828 -31.66287 1.000 18.73510  ? 104 ILE   A N   1 
ATOM   707  C CA  . ILE   A 1 97  ? 8.67932   -14.28843 -31.66633 1.000 19.14943  ? 104 ILE   A CA  1 
ATOM   708  C C   . ILE   A 1 97  ? 9.39834   -13.19987 -30.88461 1.000 19.77746  ? 104 ILE   A C   1 
ATOM   709  O O   . ILE   A 1 97  ? 10.34711  -13.48998 -30.11558 1.000 21.10615  ? 104 ILE   A O   1 
ATOM   710  C CB  . ILE   A 1 97  ? 9.19863   -14.44925 -33.09739 1.000 21.39312  ? 104 ILE   A CB  1 
ATOM   711  C CG1 . ILE   A 1 97  ? 8.61728   -15.73847 -33.67313 1.000 22.54733  ? 104 ILE   A CG1 1 
ATOM   712  C CG2 . ILE   A 1 97  ? 10.74742  -14.48139 -33.14663 1.000 22.04014  ? 104 ILE   A CG2 1 
ATOM   713  C CD1 . ILE   A 1 97  ? 8.73087   -15.81957 -35.20372 1.000 23.68372  ? 104 ILE   A CD1 1 
ATOM   714  N N   . ASN   A 1 98  ? 8.93377   -11.95517 -31.00459 1.000 20.35570  ? 105 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 98  ? 9.52561   -10.80402 -30.31489 1.000 22.80150  ? 105 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 98  ? 8.94455   -10.68376 -28.90130 1.000 19.44181  ? 105 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 98  ? 8.36343   -9.68064  -28.48347 1.000 21.73158  ? 105 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 98  ? 9.28452   -9.51609  -31.10876 1.000 22.76290  ? 105 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 98  ? 10.27085  -9.33960  -32.20574 1.000 39.58123  ? 105 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 98  ? 11.38242  -8.85155  -31.99580 1.000 59.47390  ? 105 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 98  ? 9.87121   -9.72508  -33.40891 1.000 51.47048  ? 105 ASN   A ND2 1 
ATOM   722  N N   . ASN   A 1 99  ? 9.13572   -11.75837 -28.14706 1.000 18.92952  ? 106 ASN   A N   1 
ATOM   723  C CA  . ASN   A 1 99  ? 8.78934   -11.83727 -26.73327 1.000 18.01788  ? 106 ASN   A CA  1 
ATOM   724  C C   . ASN   A 1 99  ? 7.35012   -11.45881 -26.44779 1.000 19.85578  ? 106 ASN   A C   1 
ATOM   725  O O   . ASN   A 1 99  ? 7.03844   -10.72463 -25.51138 1.000 20.02856  ? 106 ASN   A O   1 
ATOM   726  C CB  . ASN   A 1 99  ? 9.73905   -10.97801 -25.90134 1.000 18.06223  ? 106 ASN   A CB  1 
ATOM   727  C CG  . ASN   A 1 99  ? 11.17486  -11.44098 -26.06646 1.000 18.81639  ? 106 ASN   A CG  1 
ATOM   728  O OD1 . ASN   A 1 99  ? 11.49097  -12.63188 -25.88887 1.000 20.30006  ? 106 ASN   A OD1 1 
ATOM   729  N ND2 . ASN   A 1 99  ? 12.07467  -10.51474 -26.40041 1.000 23.47433  ? 106 ASN   A ND2 1 
ATOM   730  N N   . LEU   A 1 100 ? 6.46518   -12.05062 -27.23707 1.000 17.92633  ? 107 LEU   A N   1 
ATOM   731  C CA  . LEU   A 1 100 ? 5.01536   -11.87596 -27.00710 1.000 17.32028  ? 107 LEU   A CA  1 
ATOM   732  C C   . LEU   A 1 100 ? 4.60282   -10.40455 -26.97348 1.000 21.18597  ? 107 LEU   A C   1 
ATOM   733  O O   . LEU   A 1 100 ? 3.81103   -9.96874  -26.12160 1.000 22.29351  ? 107 LEU   A O   1 
ATOM   734  C CB  . LEU   A 1 100 ? 4.51917   -12.61629 -25.78385 1.000 19.20967  ? 107 LEU   A CB  1 
ATOM   735  C CG  . LEU   A 1 100 ? 4.96469   -14.09795 -25.96335 1.000 24.09786  ? 107 LEU   A CG  1 
ATOM   736  C CD1 . LEU   A 1 100 ? 6.14990   -14.54186 -25.12228 1.000 23.33775  ? 107 LEU   A CD1 1 
ATOM   737  C CD2 . LEU   A 1 100 ? 3.90841   -15.10053 -26.02642 1.000 30.72305  ? 107 LEU   A CD2 1 
ATOM   738  N N   . GLY   A 1 101 ? 5.16924   -9.65038  -27.89479 1.000 19.19012  ? 108 GLY   A N   1 
ATOM   739  C CA  . GLY   A 1 101 ? 4.78875   -8.25037  -28.03730 1.000 21.86328  ? 108 GLY   A CA  1 
ATOM   740  C C   . GLY   A 1 101 ? 5.29041   -7.31038  -26.97640 1.000 22.34149  ? 108 GLY   A C   1 
ATOM   741  O O   . GLY   A 1 101 ? 4.72870   -6.20890  -26.82535 1.000 26.82048  ? 108 GLY   A O   1 
ATOM   742  N N   . THR   A 1 102 ? 6.33745   -7.69990  -26.23245 1.000 20.79639  ? 109 THR   A N   1 
ATOM   743  C CA  . THR   A 1 102 ? 6.88294   -6.92413  -25.12359 1.000 20.34707  ? 109 THR   A CA  1 
ATOM   744  C C   . THR   A 1 102 ? 8.26358   -6.42600  -25.48551 1.000 20.18171  ? 109 THR   A C   1 
ATOM   745  O O   . THR   A 1 102 ? 8.90792   -6.93071  -26.40739 1.000 23.32239  ? 109 THR   A O   1 
ATOM   746  C CB  . THR   A 1 102 ? 7.03919   -7.77042  -23.84492 1.000 22.53121  ? 109 THR   A CB  1 
ATOM   747  O OG1 . THR   A 1 102 ? 8.06359   -8.75500  -24.01453 1.000 23.05477  ? 109 THR   A OG1 1 
ATOM   748  C CG2 . THR   A 1 102 ? 5.75665   -8.45702  -23.44536 1.000 26.61814  ? 109 THR   A CG2 1 
ATOM   749  N N   A ILE   A 1 103 ? 8.71141   -5.43011  -24.72966 0.632 18.99731  ? 110 ILE   A N   1 
ATOM   750  N N   B ILE   A 1 103 ? 8.72083   -5.39961  -24.76722 0.368 18.91763  ? 110 ILE   A N   1 
ATOM   751  C CA  A ILE   A 1 103 ? 10.10130  -4.97250  -24.76097 0.632 19.54820  ? 110 ILE   A CA  1 
ATOM   752  C CA  B ILE   A 1 103 ? 10.13571  -5.02202  -24.83231 0.368 19.60951  ? 110 ILE   A CA  1 
ATOM   753  C C   A ILE   A 1 103 ? 10.89317  -5.68309  -23.68409 0.632 19.55264  ? 110 ILE   A C   1 
ATOM   754  C C   B ILE   A 1 103 ? 10.90163  -5.72098  -23.72235 0.368 19.48084  ? 110 ILE   A C   1 
ATOM   755  O O   A ILE   A 1 103 ? 11.52017  -5.06358  -22.80662 0.632 20.17520  ? 110 ILE   A O   1 
ATOM   756  O O   B ILE   A 1 103 ? 11.47814  -5.09281  -22.82012 0.368 20.32852  ? 110 ILE   A O   1 
ATOM   757  C CB  A ILE   A 1 103 ? 10.21176  -3.44569  -24.73482 0.632 24.97420  ? 110 ILE   A CB  1 
ATOM   758  C CB  B ILE   A 1 103 ? 10.40341  -3.50891  -24.92729 0.368 24.76167  ? 110 ILE   A CB  1 
ATOM   759  C CG1 A ILE   A 1 103 ? 9.48746   -2.85700  -23.53750 0.632 24.68082  ? 110 ILE   A CG1 1 
ATOM   760  C CG1 B ILE   A 1 103 ? 9.68765   -2.73248  -23.82087 0.368 23.23876  ? 110 ILE   A CG1 1 
ATOM   761  C CG2 A ILE   A 1 103 ? 9.54329   -2.91148  -26.00916 0.632 24.23407  ? 110 ILE   A CG2 1 
ATOM   762  C CG2 B ILE   A 1 103 ? 9.97034   -3.02681  -26.32707 0.368 20.47716  ? 110 ILE   A CG2 1 
ATOM   763  C CD1 A ILE   A 1 103 ? 9.82164   -1.39026  -23.34778 0.632 27.98317  ? 110 ILE   A CD1 1 
ATOM   764  C CD1 B ILE   A 1 103 ? 10.16350  -1.27337  -23.68257 0.368 25.58669  ? 110 ILE   A CD1 1 
ATOM   765  N N   A ALA   A 1 104 ? 10.90961  -7.00983  -23.78448 0.632 21.26714  ? 111 ALA   A N   1 
ATOM   766  N N   B ALA   A 1 104 ? 10.94530  -7.04611  -23.82639 0.368 21.19907  ? 111 ALA   A N   1 
ATOM   767  C CA  A ALA   A 1 104 ? 11.30493  -7.79026  -22.62410 0.632 19.53036  ? 111 ALA   A CA  1 
ATOM   768  C CA  B ALA   A 1 104 ? 11.44310  -7.86217  -22.72838 0.368 18.56988  ? 111 ALA   A CA  1 
ATOM   769  C C   A ALA   A 1 104 ? 12.77197  -7.67306  -22.29197 0.632 20.64327  ? 111 ALA   A C   1 
ATOM   770  C C   B ALA   A 1 104 ? 12.89403  -7.57455  -22.39204 0.368 21.99339  ? 111 ALA   A C   1 
ATOM   771  O O   A ALA   A 1 104 ? 13.12361  -7.87619  -21.12527 0.632 22.04488  ? 111 ALA   A O   1 
ATOM   772  O O   B ALA   A 1 104 ? 13.27605  -7.61517  -21.21773 0.368 22.14906  ? 111 ALA   A O   1 
ATOM   773  C CB  A ALA   A 1 104 ? 10.86160  -9.25543  -22.75735 0.632 20.42910  ? 111 ALA   A CB  1 
ATOM   774  C CB  B ALA   A 1 104 ? 11.26326  -9.33634  -23.07637 0.368 19.16175  ? 111 ALA   A CB  1 
ATOM   775  N N   A LYS   A 1 105 ? 13.65478  -7.38324  -23.26481 0.632 21.83313  ? 112 LYS   A N   1 
ATOM   776  N N   B LYS   A 1 105 ? 13.74836  -7.33811  -23.38856 0.368 19.97692  ? 112 LYS   A N   1 
ATOM   777  C CA  A LYS   A 1 105 ? 15.05700  -7.23985  -22.89183 0.632 22.05058  ? 112 LYS   A CA  1 
ATOM   778  C CA  B LYS   A 1 105 ? 15.14007  -7.11728  -23.02369 0.368 24.02798  ? 112 LYS   A CA  1 
ATOM   779  C C   A LYS   A 1 105 ? 15.25032  -6.07793  -21.92051 0.632 24.88608  ? 112 LYS   A C   1 
ATOM   780  C C   B LYS   A 1 105 ? 15.27796  -5.86300  -22.16848 0.368 25.81007  ? 112 LYS   A C   1 
ATOM   781  O O   A LYS   A 1 105 ? 15.82374  -6.24752  -20.83522 0.632 25.94471  ? 112 LYS   A O   1 
ATOM   782  O O   B LYS   A 1 105 ? 15.87706  -5.89074  -21.08415 0.368 25.57816  ? 112 LYS   A O   1 
ATOM   783  C CB  A LYS   A 1 105 ? 15.95425  -7.06187  -24.13134 0.632 23.51499  ? 112 LYS   A CB  1 
ATOM   784  C CB  B LYS   A 1 105 ? 16.02487  -7.02673  -24.27140 0.368 22.99344  ? 112 LYS   A CB  1 
ATOM   785  C CG  A LYS   A 1 105 ? 17.40383  -6.90648  -23.79173 0.632 30.83052  ? 112 LYS   A CG  1 
ATOM   786  C CG  B LYS   A 1 105 ? 17.38050  -6.39232  -24.03388 0.368 38.13690  ? 112 LYS   A CG  1 
ATOM   787  C CD  A LYS   A 1 105 ? 18.23177  -6.83437  -25.08499 0.632 35.50152  ? 112 LYS   A CD  1 
ATOM   788  C CD  B LYS   A 1 105 ? 18.30946  -6.60731  -25.24202 0.368 34.03730  ? 112 LYS   A CD  1 
ATOM   789  C CE  A LYS   A 1 105 ? 19.71928  -6.92161  -24.79025 0.632 42.50960  ? 112 LYS   A CE  1 
ATOM   790  C CE  B LYS   A 1 105 ? 19.79196  -6.50725  -24.85065 0.368 41.92717  ? 112 LYS   A CE  1 
ATOM   791  N NZ  A LYS   A 1 105 ? 20.22014  -5.74814  -24.04559 0.632 49.04148  ? 112 LYS   A NZ  1 
ATOM   792  N NZ  B LYS   A 1 105 ? 20.71298  -7.31466  -25.72619 0.368 40.29422  ? 112 LYS   A NZ  1 
ATOM   793  N N   A SER   A 1 106 ? 14.78033  -4.87436  -22.29094 0.632 24.71655  ? 113 SER   A N   1 
ATOM   794  N N   B SER   A 1 106 ? 14.71891  -4.74242  -22.63473 0.368 22.87942  ? 113 SER   A N   1 
ATOM   795  C CA  A SER   A 1 106 ? 14.93544  -3.74853  -21.38009 0.632 24.70979  ? 113 SER   A CA  1 
ATOM   796  C CA  B SER   A 1 106 ? 14.86574  -3.51971  -21.86525 0.368 25.25648  ? 113 SER   A CA  1 
ATOM   797  C C   A SER   A 1 106 ? 14.09551  -3.92122  -20.11337 0.632 23.29810  ? 113 SER   A C   1 
ATOM   798  C C   B SER   A 1 106 ? 13.98944  -3.54293  -20.62731 0.368 21.75456  ? 113 SER   A C   1 
ATOM   799  O O   A SER   A 1 106 ? 14.53055  -3.51002  -19.03075 0.632 26.00855  ? 113 SER   A O   1 
ATOM   800  O O   B SER   A 1 106 ? 14.33623  -2.89231  -19.62853 0.368 21.93674  ? 113 SER   A O   1 
ATOM   801  C CB  A SER   A 1 106 ? 14.67183  -2.41330  -22.09169 0.632 29.39355  ? 113 SER   A CB  1 
ATOM   802  C CB  B SER   A 1 106 ? 14.56843  -2.28566  -22.71831 0.368 28.42531  ? 113 SER   A CB  1 
ATOM   803  O OG  A SER   A 1 106 ? 13.32822  -2.39489  -22.56314 0.632 29.05387  ? 113 SER   A OG  1 
ATOM   804  O OG  B SER   A 1 106 ? 13.18229  -2.23457  -23.03294 0.368 32.00117  ? 113 SER   A OG  1 
ATOM   805  N N   A GLY   A 1 107 ? 12.92377  -4.53898  -20.21385 0.632 24.74654  ? 114 GLY   A N   1 
ATOM   806  N N   B GLY   A 1 107 ? 12.87339  -4.27823  -20.68113 0.368 21.70249  ? 114 GLY   A N   1 
ATOM   807  C CA  A GLY   A 1 107 ? 12.10772  -4.74418  -19.01501 0.632 20.44852  ? 114 GLY   A CA  1 
ATOM   808  C CA  B GLY   A 1 107 ? 12.02202  -4.41843  -19.50731 0.368 30.00266  ? 114 GLY   A CA  1 
ATOM   809  C C   A GLY   A 1 107 ? 12.77443  -5.66340  -18.01832 0.632 27.66758  ? 114 GLY   A C   1 
ATOM   810  C C   B GLY   A 1 107 ? 12.66431  -5.27896  -18.44591 0.368 19.75486  ? 114 GLY   A C   1 
ATOM   811  O O   A GLY   A 1 107 ? 12.75604  -5.41139  -16.81339 0.632 23.23491  ? 114 GLY   A O   1 
ATOM   812  O O   B GLY   A 1 107 ? 12.63279  -4.94817  -17.26066 0.368 26.70154  ? 114 GLY   A O   1 
ATOM   813  N N   A THR   A 1 108 ? 13.41334  -6.72625  -18.50494 0.632 22.51677  ? 115 THR   A N   1 
ATOM   814  N N   B THR   A 1 108 ? 13.31137  -6.37057  -18.86356 0.368 22.36354  ? 115 THR   A N   1 
ATOM   815  C CA  A THR   A 1 108 ? 14.12934  -7.61458  -17.59716 0.632 24.83976  ? 115 THR   A CA  1 
ATOM   816  C CA  B THR   A 1 108 ? 14.02248  -7.19980  -17.90284 0.368 25.45530  ? 115 THR   A CA  1 
ATOM   817  C C   A THR   A 1 108 ? 15.27005  -6.88883  -16.90610 0.632 26.12321  ? 115 THR   A C   1 
ATOM   818  C C   B THR   A 1 108 ? 15.18452  -6.43051  -17.28855 0.368 28.49188  ? 115 THR   A C   1 
ATOM   819  O O   A THR   A 1 108 ? 15.46862  -7.04354  -15.69999 0.632 25.60992  ? 115 THR   A O   1 
ATOM   820  O O   B THR   A 1 108 ? 15.44248  -6.54597  -16.08905 0.368 26.02227  ? 115 THR   A O   1 
ATOM   821  C CB  A THR   A 1 108 ? 14.70709  -8.77606  -18.40191 0.632 22.24766  ? 115 THR   A CB  1 
ATOM   822  C CB  B THR   A 1 108 ? 14.49130  -8.49223  -18.58501 0.368 26.16379  ? 115 THR   A CB  1 
ATOM   823  O OG1 A THR   A 1 108 ? 13.61241  -9.53384  -18.90574 0.632 21.42352  ? 115 THR   A OG1 1 
ATOM   824  O OG1 B THR   A 1 108 ? 13.34828  -9.16951  -19.13762 0.368 20.35352  ? 115 THR   A OG1 1 
ATOM   825  C CG2 A THR   A 1 108 ? 15.59465  -9.64744  -17.55143 0.632 22.96013  ? 115 THR   A CG2 1 
ATOM   826  C CG2 B THR   A 1 108 ? 15.15929  -9.39610  -17.58683 0.368 22.05986  ? 115 THR   A CG2 1 
ATOM   827  N N   A LYS   A 1 109 ? 16.06519  -6.13030  -17.66980 0.632 27.71173  ? 116 LYS   A N   1 
ATOM   828  N N   B LYS   A 1 109 ? 15.87654  -5.61035  -18.08700 0.368 24.76755  ? 116 LYS   A N   1 
ATOM   829  C CA  A LYS   A 1 109 ? 17.16958  -5.38292  -17.08502 0.632 27.58148  ? 116 LYS   A CA  1 
ATOM   830  C CA  B LYS   A 1 109 ? 16.91803  -4.74848  -17.53616 0.368 25.39087  ? 116 LYS   A CA  1 
ATOM   831  C C   A LYS   A 1 109 ? 16.69190  -4.55315  -15.91222 0.632 30.91620  ? 116 LYS   A C   1 
ATOM   832  C C   B LYS   A 1 109 ? 16.33883  -3.75670  -16.52949 0.368 31.83583  ? 116 LYS   A C   1 
ATOM   833  O O   A LYS   A 1 109 ? 17.28234  -4.56367  -14.82509 0.632 29.02591  ? 116 LYS   A O   1 
ATOM   834  O O   B LYS   A 1 109 ? 16.90016  -3.54612  -15.44766 0.368 33.71863  ? 116 LYS   A O   1 
ATOM   835  C CB  A LYS   A 1 109 ? 17.81081  -4.48973  -18.15455 0.632 27.34674  ? 116 LYS   A CB  1 
ATOM   836  C CB  B LYS   A 1 109 ? 17.61750  -4.01076  -18.67283 0.368 31.09456  ? 116 LYS   A CB  1 
ATOM   837  C CG  A LYS   A 1 109 ? 18.93497  -3.52988  -17.68826 0.632 35.10951  ? 116 LYS   A CG  1 
ATOM   838  C CG  B LYS   A 1 109 ? 18.93770  -3.33062  -18.28329 0.368 39.49048  ? 116 LYS   A CG  1 
ATOM   839  C CD  A LYS   A 1 109 ? 19.35789  -2.64092  -18.86823 0.632 37.47408  ? 116 LYS   A CD  1 
ATOM   840  C CD  B LYS   A 1 109 ? 19.39750  -2.35645  -19.36788 0.368 43.10692  ? 116 LYS   A CD  1 
ATOM   841  C CE  A LYS   A 1 109 ? 19.96839  -1.31740  -18.43808 0.632 52.83263  ? 116 LYS   A CE  1 
ATOM   842  C CE  B LYS   A 1 109 ? 20.49842  -1.42624  -18.87330 0.368 46.62043  ? 116 LYS   A CE  1 
ATOM   843  N NZ  A LYS   A 1 109 ? 21.06266  -1.58284  -17.47528 0.632 55.41572  ? 116 LYS   A NZ  1 
ATOM   844  N NZ  B LYS   A 1 109 ? 21.03882  -1.91948  -17.57965 0.368 51.70922  ? 116 LYS   A NZ  1 
ATOM   845  N N   A ALA   A 1 110 ? 15.63590  -3.79238  -16.12621 0.632 25.87094  ? 117 ALA   A N   1 
ATOM   846  N N   B ALA   A 1 110 ? 15.22573  -3.11807  -16.88719 0.368 29.18104  ? 117 ALA   A N   1 
ATOM   847  C CA  A ALA   A 1 110 ? 15.16379  -2.94095  -15.03921 0.632 29.18305  ? 117 ALA   A CA  1 
ATOM   848  C CA  B ALA   A 1 110 ? 14.60557  -2.15001  -15.98847 0.368 28.32631  ? 117 ALA   A CA  1 
ATOM   849  C C   A ALA   A 1 110 ? 14.63888  -3.78652  -13.88612 0.632 24.28814  ? 117 ALA   A C   1 
ATOM   850  C C   B ALA   A 1 110 ? 14.10872  -2.83531  -14.72196 0.368 30.02085  ? 117 ALA   A C   1 
ATOM   851  O O   A ALA   A 1 110 ? 14.82085  -3.43353  -12.71701 0.632 25.01058  ? 117 ALA   A O   1 
ATOM   852  O O   B ALA   A 1 110 ? 14.24695  -2.28752  -13.61257 0.368 30.42394  ? 117 ALA   A O   1 
ATOM   853  C CB  A ALA   A 1 110 ? 14.07351  -2.02079  -15.58317 0.632 27.62851  ? 117 ALA   A CB  1 
ATOM   854  C CB  B ALA   A 1 110 ? 13.45333  -1.47716  -16.72180 0.368 28.35948  ? 117 ALA   A CB  1 
ATOM   855  N N   A PHE   A 1 111 ? 13.93835  -4.87952  -14.18943 0.632 26.39396  ? 118 PHE   A N   1 
ATOM   856  N N   B PHE   A 1 111 ? 13.54600  -4.04346  -14.87325 0.368 30.49326  ? 118 PHE   A N   1 
ATOM   857  C CA  A PHE   A 1 111 ? 13.35780  -5.68012  -13.11500 0.632 22.95214  ? 118 PHE   A CA  1 
ATOM   858  C CA  B PHE   A 1 111 ? 13.12536  -4.85195  -13.73328 0.368 26.40668  ? 118 PHE   A CA  1 
ATOM   859  C C   A PHE   A 1 111 ? 14.45123  -6.28038  -12.24726 0.632 27.27973  ? 118 PHE   A C   1 
ATOM   860  C C   B PHE   A 1 111 ? 14.29545  -5.14996  -12.80083 0.368 27.40493  ? 118 PHE   A C   1 
ATOM   861  O O   A PHE   A 1 111 ? 14.37273  -6.25381  -11.01885 0.632 25.47840  ? 118 PHE   A O   1 
ATOM   862  O O   B PHE   A 1 111 ? 14.18999  -4.93926  -11.59175 0.368 28.12534  ? 118 PHE   A O   1 
ATOM   863  C CB  A PHE   A 1 111 ? 12.50223  -6.75844  -13.75766 0.632 24.16763  ? 118 PHE   A CB  1 
ATOM   864  C CB  B PHE   A 1 111 ? 12.51062  -6.16749  -14.22709 0.368 23.62133  ? 118 PHE   A CB  1 
ATOM   865  C CG  A PHE   A 1 111 ? 11.79712  -7.66978  -12.80574 0.632 24.16749  ? 118 PHE   A CG  1 
ATOM   866  C CG  B PHE   A 1 111 ? 11.87355  -6.98685  -13.14479 0.368 20.34144  ? 118 PHE   A CG  1 
ATOM   867  C CD1 A PHE   A 1 111 ? 11.13242  -7.20512  -11.66456 0.632 21.31500  ? 118 PHE   A CD1 1 
ATOM   868  C CD1 B PHE   A 1 111 ? 11.20859  -6.37343  -12.09128 0.368 22.60913  ? 118 PHE   A CD1 1 
ATOM   869  C CD2 A PHE   A 1 111 ? 11.67165  -9.01073  -13.12699 0.632 22.08820  ? 118 PHE   A CD2 1 
ATOM   870  C CD2 B PHE   A 1 111 ? 11.97783  -8.37256  -13.15133 0.368 25.60395  ? 118 PHE   A CD2 1 
ATOM   871  C CE1 A PHE   A 1 111 ? 10.46478  -8.09104  -10.83268 0.632 22.18137  ? 118 PHE   A CE1 1 
ATOM   872  C CE1 B PHE   A 1 111 ? 10.61260  -7.12651  -11.10204 0.368 24.91597  ? 118 PHE   A CE1 1 
ATOM   873  C CE2 A PHE   A 1 111 ? 10.96152  -9.89175  -12.32438 0.632 23.57325  ? 118 PHE   A CE2 1 
ATOM   874  C CE2 B PHE   A 1 111 ? 11.40374  -9.13579  -12.14804 0.368 26.22303  ? 118 PHE   A CE2 1 
ATOM   875  C CZ  A PHE   A 1 111 ? 10.32853  -9.41031  -11.17381 0.632 21.43552  ? 118 PHE   A CZ  1 
ATOM   876  C CZ  B PHE   A 1 111 ? 10.72066  -8.50108  -11.11197 0.368 18.61490  ? 118 PHE   A CZ  1 
ATOM   877  N N   A MET   A 1 112 ? 15.49255  -6.80786  -12.87009 0.632 26.90759  ? 119 MET   A N   1 
ATOM   878  N N   B MET   A 1 112 ? 15.41710  -5.66582  -13.34531 0.368 27.46463  ? 119 MET   A N   1 
ATOM   879  C CA  A MET   A 1 112 ? 16.57234  -7.40312  -12.08810 0.632 31.74981  ? 119 MET   A CA  1 
ATOM   880  C CA  B MET   A 1 112 ? 16.53414  -6.04797  -12.48559 0.368 30.60769  ? 119 MET   A CA  1 
ATOM   881  C C   A MET   A 1 112 ? 17.30279  -6.36740  -11.24647 0.632 32.41809  ? 119 MET   A C   1 
ATOM   882  C C   B MET   A 1 112 ? 17.10034  -4.82615  -11.78851 0.368 32.15498  ? 119 MET   A C   1 
ATOM   883  O O   A MET   A 1 112 ? 17.67413  -6.64882  -10.09865 0.632 32.99644  ? 119 MET   A O   1 
ATOM   884  O O   B MET   A 1 112 ? 17.32204  -4.84595  -10.57550 0.368 30.28052  ? 119 MET   A O   1 
ATOM   885  C CB  A MET   A 1 112 ? 17.46153  -8.17638  -13.04807 0.632 35.87979  ? 119 MET   A CB  1 
ATOM   886  C CB  B MET   A 1 112 ? 17.62056  -6.81082  -13.26811 0.368 27.69204  ? 119 MET   A CB  1 
ATOM   887  C CG  A MET   A 1 112 ? 16.96835  -9.58868  -13.13432 0.632 28.88485  ? 119 MET   A CG  1 
ATOM   888  C CG  B MET   A 1 112 ? 17.10601  -8.09259  -14.01385 0.368 26.43097  ? 119 MET   A CG  1 
ATOM   889  S SD  A MET   A 1 112 ? 17.98513  -10.46724 -14.25709 0.632 46.76888  ? 119 MET   A SD  1 
ATOM   890  S SD  B MET   A 1 112 ? 16.41734  -9.36237  -12.91076 0.368 30.72572  ? 119 MET   A SD  1 
ATOM   891  C CE  A MET   A 1 112 ? 16.91536  -11.77202 -14.74799 0.632 27.00091  ? 119 MET   A CE  1 
ATOM   892  C CE  B MET   A 1 112 ? 16.45076  -10.83309 -13.93772 0.368 34.58379  ? 119 MET   A CE  1 
ATOM   893  N N   A GLU   A 1 113 ? 17.49473  -5.15155  -11.77096 0.632 33.62408  ? 120 GLU   A N   1 
ATOM   894  N N   B GLU   A 1 113 ? 17.30062  -3.73544  -12.52835 0.368 32.62505  ? 120 GLU   A N   1 
ATOM   895  C CA  A GLU   A 1 113 ? 18.05207  -4.09360  -10.93151 0.632 30.21814  ? 120 GLU   A CA  1 
ATOM   896  C CA  B GLU   A 1 113 ? 17.68643  -2.48082  -11.88711 0.368 29.73756  ? 120 GLU   A CA  1 
ATOM   897  C C   A GLU   A 1 113 ? 17.15251  -3.80194  -9.73640  0.632 33.44426  ? 120 GLU   A C   1 
ATOM   898  C C   B GLU   A 1 113 ? 16.74443  -2.11760  -10.73749 0.368 29.86240  ? 120 GLU   A C   1 
ATOM   899  O O   A GLU   A 1 113 ? 17.63183  -3.62961  -8.60623  0.632 37.07464  ? 120 GLU   A O   1 
ATOM   900  O O   B GLU   A 1 113 ? 17.17747  -1.55814  -9.71772  0.368 33.40253  ? 120 GLU   A O   1 
ATOM   901  C CB  A GLU   A 1 113 ? 18.27970  -2.81595  -11.74533 0.632 37.18861  ? 120 GLU   A CB  1 
ATOM   902  C CB  B GLU   A 1 113 ? 17.73185  -1.35192  -12.92021 0.368 42.85088  ? 120 GLU   A CB  1 
ATOM   903  C CG  A GLU   A 1 113 ? 19.40699  -2.89227  -12.76497 0.632 46.43124  ? 120 GLU   A CG  1 
ATOM   904  C CG  B GLU   A 1 113 ? 18.82597  -1.45728  -13.97065 0.368 41.95267  ? 120 GLU   A CG  1 
ATOM   905  C CD  A GLU   A 1 113 ? 19.49030  -1.65333  -13.66078 0.632 53.83719  ? 120 GLU   A CD  1 
ATOM   906  C CD  B GLU   A 1 113 ? 18.39545  -0.90146  -15.31204 0.368 40.14719  ? 120 GLU   A CD  1 
ATOM   907  O OE1 A GLU   A 1 113 ? 18.79711  -0.65571  -13.36441 0.632 57.24873  ? 120 GLU   A OE1 1 
ATOM   908  O OE1 B GLU   A 1 113 ? 17.17054  -0.87970  -15.57809 0.368 51.37931  ? 120 GLU   A OE1 1 
ATOM   909  O OE2 A GLU   A 1 113 ? 20.27854  -1.66722  -14.63848 0.632 59.54749  ? 120 GLU   A OE2 1 
ATOM   910  O OE2 B GLU   A 1 113 ? 19.27830  -0.47983  -16.09402 0.368 51.16737  ? 120 GLU   A OE2 1 
ATOM   911  N N   A ALA   A 1 114 ? 15.84456  -3.76540  -9.95791  0.632 28.87981  ? 121 ALA   A N   1 
ATOM   912  N N   B ALA   A 1 114 ? 15.44769  -2.37563  -10.90986 0.368 33.26745  ? 121 ALA   A N   1 
ATOM   913  C CA  A ALA   A 1 114 ? 14.90477  -3.40053  -8.90710  0.632 29.67394  ? 121 ALA   A CA  1 
ATOM   914  C CA  B ALA   A 1 114 ? 14.46212  -2.06365  -9.87469  0.368 36.67583  ? 121 ALA   A CA  1 
ATOM   915  C C   A ALA   A 1 114 ? 14.85930  -4.45562  -7.81686  0.632 29.92756  ? 121 ALA   A C   1 
ATOM   916  C C   B ALA   A 1 114 ? 14.64495  -2.93576  -8.64182  0.368 31.25589  ? 121 ALA   A C   1 
ATOM   917  O O   A ALA   A 1 114 ? 14.72762  -4.12178  -6.63223  0.632 34.64567  ? 121 ALA   A O   1 
ATOM   918  O O   B ALA   A 1 114 ? 14.52425  -2.45445  -7.50707  0.368 33.40713  ? 121 ALA   A O   1 
ATOM   919  C CB  A ALA   A 1 114 ? 13.52901  -3.19246  -9.52112  0.632 29.46712  ? 121 ALA   A CB  1 
ATOM   920  C CB  B ALA   A 1 114 ? 13.06988  -2.26479  -10.45895 0.368 31.23397  ? 121 ALA   A CB  1 
ATOM   921  N N   A LEU   A 1 115 ? 14.92475  -5.73446  -8.20797  0.632 28.46043  ? 122 LEU   A N   1 
ATOM   922  N N   B LEU   A 1 115 ? 14.91255  -4.22421  -8.85029  0.368 32.77969  ? 122 LEU   A N   1 
ATOM   923  C CA  A LEU   A 1 115 ? 14.99626  -6.81747  -7.23390  0.632 28.04354  ? 122 LEU   A CA  1 
ATOM   924  C CA  B LEU   A 1 115 ? 15.08055  -5.15107  -7.73512  0.368 33.50876  ? 122 LEU   A CA  1 
ATOM   925  C C   A LEU   A 1 115 ? 16.23709  -6.67220  -6.35985  0.632 39.57284  ? 122 LEU   A C   1 
ATOM   926  C C   B LEU   A 1 115 ? 16.13380  -4.65098  -6.75884  0.368 37.24044  ? 122 LEU   A C   1 
ATOM   927  O O   A LEU   A 1 115 ? 16.19730  -6.94384  -5.15490  0.632 36.79163  ? 122 LEU   A O   1 
ATOM   928  O O   B LEU   A 1 115 ? 15.95615  -4.74357  -5.53616  0.368 37.60960  ? 122 LEU   A O   1 
ATOM   929  C CB  A LEU   A 1 115 ? 15.05829  -8.11936  -8.00762  0.632 26.43284  ? 122 LEU   A CB  1 
ATOM   930  C CB  B LEU   A 1 115 ? 15.41263  -6.54896  -8.26678  0.368 30.06885  ? 122 LEU   A CB  1 
ATOM   931  C CG  A LEU   A 1 115 ? 13.73407  -8.38291  -8.75285  0.632 26.87101  ? 122 LEU   A CG  1 
ATOM   932  C CG  B LEU   A 1 115 ? 14.17034  -7.29902  -8.72492  0.368 35.74901  ? 122 LEU   A CG  1 
ATOM   933  C CD1 A LEU   A 1 115 ? 13.83318  -9.62485  -9.64151  0.632 28.94160  ? 122 LEU   A CD1 1 
ATOM   934  C CD1 B LEU   A 1 115 ? 13.64140  -6.48747  -9.84501  0.368 35.09554  ? 122 LEU   A CD1 1 
ATOM   935  C CD2 A LEU   A 1 115 ? 12.62352  -8.47326  -7.70370  0.632 27.08166  ? 122 LEU   A CD2 1 
ATOM   936  C CD2 B LEU   A 1 115 ? 14.50223  -8.71844  -9.21037  0.368 26.90166  ? 122 LEU   A CD2 1 
ATOM   937  N N   A GLN   A 1 116 ? 17.34957  -6.25003  -6.94716  0.632 36.35822  ? 123 GLN   A N   1 
ATOM   938  N N   B GLN   A 1 116 ? 17.23049  -4.08969  -7.26480  0.368 39.15712  ? 123 GLN   A N   1 
ATOM   939  C CA  A GLN   A 1 116 ? 18.54049  -6.02516  -6.13770  0.632 39.06468  ? 123 GLN   A CA  1 
ATOM   940  C CA  B GLN   A 1 116 ? 18.15122  -3.42201  -6.34733  0.368 39.76180  ? 123 GLN   A CA  1 
ATOM   941  C C   A GLN   A 1 116 ? 18.47528  -4.73372  -5.33123  0.632 37.42161  ? 123 GLN   A C   1 
ATOM   942  C C   B GLN   A 1 116 ? 17.50919  -2.17791  -5.73771  0.368 49.08684  ? 123 GLN   A C   1 
ATOM   943  O O   A GLN   A 1 116 ? 19.28001  -4.55423  -4.40090  0.632 51.92598  ? 123 GLN   A O   1 
ATOM   944  O O   B GLN   A 1 116 ? 17.43731  -2.03521  -4.51076  0.368 48.01180  ? 123 GLN   A O   1 
ATOM   945  C CB  A GLN   A 1 116 ? 19.77089  -6.02555  -7.03770  0.632 37.75152  ? 123 GLN   A CB  1 
ATOM   946  C CB  B GLN   A 1 116 ? 19.47058  -3.06321  -7.02662  0.368 48.68538  ? 123 GLN   A CB  1 
ATOM   947  C CG  A GLN   A 1 116 ? 20.15790  -7.43393  -7.46706  0.632 47.75272  ? 123 GLN   A CG  1 
ATOM   948  C CG  B GLN   A 1 116 ? 19.36476  -2.78255  -8.47692  0.368 42.91539  ? 123 GLN   A CG  1 
ATOM   949  C CD  A GLN   A 1 116 ? 21.66610  -7.67456  -7.40361  0.632 73.22203  ? 123 GLN   A CD  1 
ATOM   950  C CD  B GLN   A 1 116 ? 19.95843  -1.44719  -8.80390  0.368 37.12607  ? 123 GLN   A CD  1 
ATOM   951  O OE1 A GLN   A 1 116 ? 22.43613  -6.78417  -7.02784  0.632 73.06560  ? 123 GLN   A OE1 1 
ATOM   952  O OE1 B GLN   A 1 116 ? 20.05672  -0.57737  -7.93520  0.368 51.73871  ? 123 GLN   A OE1 1 
ATOM   953  N NE2 A GLN   A 1 116 ? 22.09063  -8.88798  -7.75885  0.632 65.37806  ? 123 GLN   A NE2 1 
ATOM   954  N NE2 B GLN   A 1 116 ? 20.40362  -1.27437  -10.04543 0.368 50.41644  ? 123 GLN   A NE2 1 
ATOM   955  N N   A ALA   A 1 117 ? 17.55868  -3.82552  -5.66789  0.632 45.90522  ? 124 ALA   A N   1 
ATOM   956  N N   B ALA   A 1 117 ? 17.04643  -1.25700  -6.58418  0.368 47.77551  ? 124 ALA   A N   1 
ATOM   957  C CA  A ALA   A 1 117 ? 17.34001  -2.58914  -4.92431  0.632 46.22695  ? 124 ALA   A CA  1 
ATOM   958  C CA  B ALA   A 1 117 ? 16.41015  -0.03119  -6.11145  0.368 39.92237  ? 124 ALA   A CA  1 
ATOM   959  C C   A ALA   A 1 117 ? 16.08263  -2.64441  -4.05721  0.632 54.80071  ? 124 ALA   A C   1 
ATOM   960  C C   B ALA   A 1 117 ? 15.42147  -0.32472  -4.99119  0.368 40.32506  ? 124 ALA   A C   1 
ATOM   961  O O   A ALA   A 1 117 ? 15.52470  -1.59530  -3.69888  0.632 54.06724  ? 124 ALA   A O   1 
ATOM   962  O O   B ALA   A 1 117 ? 14.88533  0.59878   -4.37835  0.368 42.71018  ? 124 ALA   A O   1 
ATOM   963  C CB  A ALA   A 1 117 ? 17.30628  -1.38038  -5.86277  0.632 51.97386  ? 124 ALA   A CB  1 
ATOM   964  C CB  B ALA   A 1 117 ? 15.67306  0.65410   -7.26729  0.368 42.77254  ? 124 ALA   A CB  1 
ATOM   965  N N   A GLY   A 1 118 ? 15.61552  -3.84686  -3.71976  0.632 39.93591  ? 125 GLY   A N   1 
ATOM   966  N N   B GLY   A 1 118 ? 15.14647  -1.59892  -4.73222  0.368 35.56295  ? 125 GLY   A N   1 
ATOM   967  C CA  A GLY   A 1 118 ? 14.61903  -4.02339  -2.68646  0.632 40.10376  ? 125 GLY   A CA  1 
ATOM   968  C CA  B GLY   A 1 118 ? 14.19724  -1.97505  -3.70389  0.368 35.15711  ? 125 GLY   A CA  1 
ATOM   969  C C   A GLY   A 1 118 ? 13.30092  -4.55713  -3.17892  0.632 38.91896  ? 125 GLY   A C   1 
ATOM   970  C C   B GLY   A 1 118 ? 12.86514  -2.48495  -4.20651  0.368 39.95590  ? 125 GLY   A C   1 
ATOM   971  O O   A GLY   A 1 118 ? 12.51360  -5.05349  -2.36970  0.632 42.99376  ? 125 GLY   A O   1 
ATOM   972  O O   B GLY   A 1 118 ? 11.93260  -2.61922  -3.40933  0.368 32.74468  ? 125 GLY   A O   1 
ATOM   973  N N   A ALA   A 1 119 ? 13.04080  -4.48859  -4.48403  0.632 32.54452  ? 126 ALA   A N   1 
ATOM   974  N N   B ALA   A 1 119 ? 12.74229  -2.78106  -5.49313  0.368 30.96492  ? 126 ALA   A N   1 
ATOM   975  C CA  A ALA   A 1 119 ? 11.74892  -4.91032  -5.00151  0.632 33.55583  ? 126 ALA   A CA  1 
ATOM   976  C CA  B ALA   A 1 119 ? 11.48264  -3.30063  -5.99729  0.368 33.92125  ? 126 ALA   A CA  1 
ATOM   977  C C   A ALA   A 1 119 ? 11.57683  -6.42193  -4.85689  0.632 33.49405  ? 126 ALA   A C   1 
ATOM   978  C C   B ALA   A 1 119 ? 11.32913  -4.76597  -5.61038  0.368 30.51058  ? 126 ALA   A C   1 
ATOM   979  O O   A ALA   A 1 119 ? 12.53327  -7.16638  -4.60009  0.632 33.47291  ? 126 ALA   A O   1 
ATOM   980  O O   B ALA   A 1 119 ? 12.20607  -5.37750  -4.99124  0.368 31.17205  ? 126 ALA   A O   1 
ATOM   981  C CB  A ALA   A 1 119 ? 11.61544  -4.51465  -6.47097  0.632 34.25808  ? 126 ALA   A CB  1 
ATOM   982  C CB  B ALA   A 1 119 ? 11.40686  -3.14523  -7.50915  0.368 35.72063  ? 126 ALA   A CB  1 
ATOM   983  N N   A ASP   A 1 120 ? 10.33557  -6.88028  -5.06453  0.632 30.30697  ? 127 ASP   A N   1 
ATOM   984  N N   B ASP   A 1 120 ? 10.18810  -5.34103  -5.97493  0.368 29.02986  ? 127 ASP   A N   1 
ATOM   985  C CA  A ASP   A 1 120 ? 10.04739  -8.30158  -5.07376  0.632 27.24544  ? 127 ASP   A CA  1 
ATOM   986  C CA  B ASP   A 1 120 ? 9.94703   -6.75116  -5.75168  0.368 28.24634  ? 127 ASP   A CA  1 
ATOM   987  C C   A ASP   A 1 120 ? 9.35786   -8.69367  -6.37113  0.632 25.61868  ? 127 ASP   A C   1 
ATOM   988  C C   B ASP   A 1 120 ? 9.17796   -7.28818  -6.94701  0.368 25.53709  ? 127 ASP   A C   1 
ATOM   989  O O   A ASP   A 1 120 ? 8.93227   -7.84759  -7.16252  0.632 25.00284  ? 127 ASP   A O   1 
ATOM   990  O O   B ASP   A 1 120 ? 8.66950   -6.52651  -7.77208  0.368 27.12214  ? 127 ASP   A O   1 
ATOM   991  C CB  A ASP   A 1 120 ? 9.15997   -8.74647  -3.91583  0.632 27.50186  ? 127 ASP   A CB  1 
ATOM   992  C CB  B ASP   A 1 120 ? 9.10430   -6.95854  -4.50540  0.368 34.94762  ? 127 ASP   A CB  1 
ATOM   993  C CG  A ASP   A 1 120 ? 7.80505   -8.09790  -3.93461  0.632 34.51034  ? 127 ASP   A CG  1 
ATOM   994  C CG  B ASP   A 1 120 ? 7.68633   -6.49303  -4.71503  0.368 37.92138  ? 127 ASP   A CG  1 
ATOM   995  O OD1 A ASP   A 1 120 ? 7.71122   -6.88075  -3.66361  0.632 40.29348  ? 127 ASP   A OD1 1 
ATOM   996  O OD1 B ASP   A 1 120 ? 7.44781   -5.25187  -4.73764  0.368 47.44773  ? 127 ASP   A OD1 1 
ATOM   997  O OD2 A ASP   A 1 120 ? 6.84008   -8.81955  -4.27354  0.632 33.65278  ? 127 ASP   A OD2 1 
ATOM   998  O OD2 B ASP   A 1 120 ? 6.84302   -7.37071  -4.95016  0.368 32.54600  ? 127 ASP   A OD2 1 
ATOM   999  N N   A ILE   A 1 121 ? 9.24839   -10.01145 -6.57603  0.632 23.29467  ? 128 ILE   A N   1 
ATOM   1000 N N   B ILE   A 1 121 ? 9.13604   -8.61974  -7.05841  0.368 26.82264  ? 128 ILE   A N   1 
ATOM   1001 C CA  A ILE   A 1 121 ? 8.70321   -10.54371 -7.83092  0.632 22.23528  ? 128 ILE   A CA  1 
ATOM   1002 C CA  B ILE   A 1 121 ? 8.36680   -9.26897  -8.11807  0.368 21.95337  ? 128 ILE   A CA  1 
ATOM   1003 C C   A ILE   A 1 121 ? 7.30881   -10.03458 -8.14065  0.632 22.34109  ? 128 ILE   A C   1 
ATOM   1004 C C   B ILE   A 1 121 ? 6.92698   -8.79981  -8.20382  0.368 26.96237  ? 128 ILE   A C   1 
ATOM   1005 O O   A ILE   A 1 121 ? 6.94312   -9.88248  -9.31292  0.632 22.18317  ? 128 ILE   A O   1 
ATOM   1006 O O   B ILE   A 1 121 ? 6.35361   -8.78217  -9.29922  0.368 26.41091  ? 128 ILE   A O   1 
ATOM   1007 C CB  A ILE   A 1 121 ? 8.81668   -12.08061 -7.83518  0.632 24.19031  ? 128 ILE   A CB  1 
ATOM   1008 C CB  B ILE   A 1 121 ? 8.49308   -10.80497 -8.12144  0.368 22.57716  ? 128 ILE   A CB  1 
ATOM   1009 C CG1 A ILE   A 1 121 ? 10.29102  -12.46803 -8.10049  0.632 28.58383  ? 128 ILE   A CG1 1 
ATOM   1010 C CG1 B ILE   A 1 121 ? 8.47865   -11.33938 -9.57161  0.368 33.38105  ? 128 ILE   A CG1 1 
ATOM   1011 C CG2 A ILE   A 1 121 ? 7.81750   -12.71187 -8.77376  0.632 24.18730  ? 128 ILE   A CG2 1 
ATOM   1012 C CG2 B ILE   A 1 121 ? 7.52375   -11.44741 -7.14493  0.368 30.27808  ? 128 ILE   A CG2 1 
ATOM   1013 C CD1 A ILE   A 1 121 ? 10.65570  -13.94998 -7.82241  0.632 25.32665  ? 128 ILE   A CD1 1 
ATOM   1014 C CD1 B ILE   A 1 121 ? 8.31266   -12.84552 -9.71019  0.368 27.29174  ? 128 ILE   A CD1 1 
ATOM   1015 N N   A SER   A 1 122 ? 6.51578   -9.73556  -7.12219  0.632 22.51016  ? 129 SER   A N   1 
ATOM   1016 N N   B SER   A 1 122 ? 6.29339   -8.46801  -7.07498  0.368 31.40562  ? 129 SER   A N   1 
ATOM   1017 C CA  A SER   A 1 122 ? 5.15729   -9.27266  -7.38170  0.632 24.69602  ? 129 SER   A CA  1 
ATOM   1018 C CA  B SER   A 1 122 ? 4.90147   -8.05954  -7.20024  0.368 23.90615  ? 129 SER   A CA  1 
ATOM   1019 C C   A SER   A 1 122 ? 5.13673   -7.99525  -8.20332  0.632 22.21274  ? 129 SER   A C   1 
ATOM   1020 C C   B SER   A 1 122 ? 4.75297   -6.86904  -8.12606  0.368 29.65086  ? 129 SER   A C   1 
ATOM   1021 O O   A SER   A 1 122 ? 4.07382   -7.64612  -8.75190  0.632 26.41692  ? 129 SER   A O   1 
ATOM   1022 O O   B SER   A 1 122 ? 3.62552   -6.56570  -8.53558  0.368 25.24232  ? 129 SER   A O   1 
ATOM   1023 C CB  A SER   A 1 122 ? 4.43120   -9.07032  -6.03968  0.632 23.22565  ? 129 SER   A CB  1 
ATOM   1024 C CB  B SER   A 1 122 ? 4.28434   -7.72281  -5.85337  0.368 27.24279  ? 129 SER   A CB  1 
ATOM   1025 O OG  A SER   A 1 122 ? 4.83923   -7.86635  -5.42498  0.632 27.33159  ? 129 SER   A OG  1 
ATOM   1026 O OG  B SER   A 1 122 ? 4.60310   -6.38552  -5.47958  0.368 35.15446  ? 129 SER   A OG  1 
ATOM   1027 N N   A MET   A 1 123 ? 6.26398   -7.28204  -8.28114  0.632 21.54237  ? 130 MET   A N   1 
ATOM   1028 N N   B MET   A 1 123 ? 5.87323   -6.21980  -8.46448  0.368 24.36181  ? 130 MET   A N   1 
ATOM   1029 C CA  A MET   A 1 123 ? 6.32019   -6.00664  -8.97866  0.632 21.63419  ? 130 MET   A CA  1 
ATOM   1030 C CA  B MET   A 1 123 ? 5.95715   -5.03760  -9.30008  0.368 29.13091  ? 130 MET   A CA  1 
ATOM   1031 C C   A MET   A 1 123 ? 6.58217   -6.16773  -10.47597 0.632 22.03048  ? 130 MET   A C   1 
ATOM   1032 C C   B MET   A 1 123 ? 6.33432   -5.36434  -10.73960 0.368 22.58031  ? 130 MET   A C   1 
ATOM   1033 O O   A MET   A 1 123 ? 6.74740   -5.16608  -11.18853 0.632 23.67182  ? 130 MET   A O   1 
ATOM   1034 O O   B MET   A 1 123 ? 6.47379   -4.44513  -11.55065 0.368 23.57283  ? 130 MET   A O   1 
ATOM   1035 C CB  A MET   A 1 123 ? 7.35709   -5.11366  -8.29506  0.632 25.69154  ? 130 MET   A CB  1 
ATOM   1036 C CB  B MET   A 1 123 ? 6.99207   -4.08545  -8.68352  0.368 29.06694  ? 130 MET   A CB  1 
ATOM   1037 C CG  A MET   A 1 123 ? 6.89332   -4.79593  -6.84472  0.632 30.94745  ? 130 MET   A CG  1 
ATOM   1038 C CG  B MET   A 1 123 ? 6.93159   -4.13337  -7.13695  0.368 28.96270  ? 130 MET   A CG  1 
ATOM   1039 S SD  A MET   A 1 123 ? 8.20333   -4.04356  -5.91999  0.632 32.94334  ? 130 MET   A SD  1 
ATOM   1040 S SD  B MET   A 1 123 ? 7.66204   -2.72032  -6.32384  0.368 39.59272  ? 130 MET   A SD  1 
ATOM   1041 C CE  A MET   A 1 123 ? 8.16685   -2.47553  -6.78921  0.632 32.77416  ? 130 MET   A CE  1 
ATOM   1042 C CE  B MET   A 1 123 ? 7.96376   -1.66218  -7.71505  0.368 39.27453  ? 130 MET   A CE  1 
ATOM   1043 N N   A ILE   A 1 124 ? 6.65377   -7.40865  -10.97000 0.632 19.20818  ? 131 ILE   A N   1 
ATOM   1044 N N   B ILE   A 1 124 ? 6.44868   -6.65672  -11.08763 0.368 23.71570  ? 131 ILE   A N   1 
ATOM   1045 C CA  A ILE   A 1 124 ? 7.09421   -7.67282  -12.34017 0.632 19.36897  ? 131 ILE   A CA  1 
ATOM   1046 C CA  B ILE   A 1 124 ? 6.96803   -7.05462  -12.39842 0.368 19.95192  ? 131 ILE   A CA  1 
ATOM   1047 C C   A ILE   A 1 124 ? 6.33584   -6.88176  -13.41783 0.632 21.35260  ? 131 ILE   A C   1 
ATOM   1048 C C   B ILE   A 1 124 ? 6.14843   -6.41871  -13.51863 0.368 18.19733  ? 131 ILE   A C   1 
ATOM   1049 O O   A ILE   A 1 124 ? 6.90305   -6.54655  -14.48211 0.632 18.22847  ? 131 ILE   A O   1 
ATOM   1050 O O   B ILE   A 1 124 ? 6.69525   -5.96391  -14.53078 0.368 19.47569  ? 131 ILE   A O   1 
ATOM   1051 C CB  A ILE   A 1 124 ? 6.98988   -9.19860  -12.56481 0.632 18.45991  ? 131 ILE   A CB  1 
ATOM   1052 C CB  B ILE   A 1 124 ? 7.02727   -8.59523  -12.52698 0.368 21.49060  ? 131 ILE   A CB  1 
ATOM   1053 C CG1 A ILE   A 1 124 ? 7.60176   -9.57990  -13.91254 0.632 21.21822  ? 131 ILE   A CG1 1 
ATOM   1054 C CG1 B ILE   A 1 124 ? 7.75384   -9.02501  -13.82245 0.368 19.02598  ? 131 ILE   A CG1 1 
ATOM   1055 C CG2 A ILE   A 1 124 ? 5.49831   -9.70999  -12.40758 0.632 19.80184  ? 131 ILE   A CG2 1 
ATOM   1056 C CG2 B ILE   A 1 124 ? 5.60426   -9.20042  -12.42679 0.368 17.30989  ? 131 ILE   A CG2 1 
ATOM   1057 C CD1 A ILE   A 1 124 ? 7.70439   -11.07802 -14.13091 0.632 21.05387  ? 131 ILE   A CD1 1 
ATOM   1058 C CD1 B ILE   A 1 124 ? 7.94837   -10.53187 -13.93035 0.368 22.42641  ? 131 ILE   A CD1 1 
ATOM   1059 N N   A GLY   A 1 125 ? 5.04007   -6.63727  -13.20446 0.632 21.86495  ? 132 GLY   A N   1 
ATOM   1060 N N   B GLY   A 1 125 ? 4.82305   -6.39047  -13.37027 0.368 24.08160  ? 132 GLY   A N   1 
ATOM   1061 C CA  A GLY   A 1 125 ? 4.25592   -5.91075  -14.18772 0.632 24.18496  ? 132 GLY   A CA  1 
ATOM   1062 C CA  B GLY   A 1 125 ? 4.01815   -5.82207  -14.43471 0.368 21.93936  ? 132 GLY   A CA  1 
ATOM   1063 C C   A GLY   A 1 125 ? 4.65482   -4.45454  -14.32960 0.632 24.61657  ? 132 GLY   A C   1 
ATOM   1064 C C   B GLY   A 1 125 ? 4.44703   -4.41740  -14.79989 0.368 24.54887  ? 132 GLY   A C   1 
ATOM   1065 O O   A GLY   A 1 125 ? 4.31906   -3.82815  -15.33843 0.632 25.31179  ? 132 GLY   A O   1 
ATOM   1066 O O   B GLY   A 1 125 ? 4.23361   -3.98348  -15.93580 0.368 21.87052  ? 132 GLY   A O   1 
ATOM   1067 N N   A GLN   A 1 126 ? 5.34912   -3.88830  -13.32853 0.632 21.98767  ? 133 GLN   A N   1 
ATOM   1068 N N   B GLN   A 1 126 ? 5.07190   -3.70937  -13.85623 0.368 26.10437  ? 133 GLN   A N   1 
ATOM   1069 C CA  A GLN   A 1 126 ? 5.81973   -2.53270  -13.52498 0.632 25.11849  ? 133 GLN   A CA  1 
ATOM   1070 C CA  B GLN   A 1 126 ? 5.47369   -2.33310  -14.04861 0.368 27.79563  ? 133 GLN   A CA  1 
ATOM   1071 C C   A GLN   A 1 126 ? 6.94342   -2.46099  -14.52559 0.632 20.18458  ? 133 GLN   A C   1 
ATOM   1072 C C   B GLN   A 1 126 ? 6.57887   -2.23292  -15.08844 0.368 27.36312  ? 133 GLN   A C   1 
ATOM   1073 O O   A GLN   A 1 126 ? 7.36377   -1.33806  -14.86937 0.632 25.77810  ? 133 GLN   A O   1 
ATOM   1074 O O   B GLN   A 1 126 ? 6.73205   -1.19632  -15.74680 0.368 26.66579  ? 133 GLN   A O   1 
ATOM   1075 C CB  A GLN   A 1 126 ? 6.28388   -1.88971  -12.22915 0.632 26.05465  ? 133 GLN   A CB  1 
ATOM   1076 C CB  B GLN   A 1 126 ? 5.95109   -1.82100  -12.68265 0.368 28.84667  ? 133 GLN   A CB  1 
ATOM   1077 C CG  A GLN   A 1 126 ? 5.17968   -1.80320  -11.19209 0.632 31.34030  ? 133 GLN   A CG  1 
ATOM   1078 C CG  B GLN   A 1 126 ? 4.83405   -1.81888  -11.59337 0.368 31.38004  ? 133 GLN   A CG  1 
ATOM   1079 C CD  A GLN   A 1 126 ? 5.63112   -1.04183  -9.97806  0.632 37.99963  ? 133 GLN   A CD  1 
ATOM   1080 C CD  B GLN   A 1 126 ? 5.32068   -1.36798  -10.21181 0.368 35.75198  ? 133 GLN   A CD  1 
ATOM   1081 O OE1 A GLN   A 1 126 ? 6.27667   0.00986   -10.09440 0.632 41.50132  ? 133 GLN   A OE1 1 
ATOM   1082 O OE1 B GLN   A 1 126 ? 6.07271   -0.39650  -10.08933 0.368 41.27192  ? 133 GLN   A OE1 1 
ATOM   1083 N NE2 A GLN   A 1 126 ? 5.32250   -1.56997  -8.80928  0.632 42.39936  ? 133 GLN   A NE2 1 
ATOM   1084 N NE2 B GLN   A 1 126 ? 4.87400   -2.07056  -9.16251  0.368 31.41245  ? 133 GLN   A NE2 1 
ATOM   1085 N N   A PHE   A 1 127 ? 7.39724   -3.63817  -14.99067 0.632 19.72480  ? 134 PHE   A N   1 
ATOM   1086 N N   B PHE   A 1 127 ? 7.32469   -3.30976  -15.27927 0.368 25.67748  ? 134 PHE   A N   1 
ATOM   1087 C CA  A PHE   A 1 127 ? 8.50468   -3.74978  -15.93014 0.632 20.53836  ? 134 PHE   A CA  1 
ATOM   1088 C CA  B PHE   A 1 127 ? 8.41416   -3.31188  -16.23807 0.368 21.88028  ? 134 PHE   A CA  1 
ATOM   1089 C C   A PHE   A 1 127 ? 8.08386   -4.31378  -17.29086 0.632 20.48973  ? 134 PHE   A C   1 
ATOM   1090 C C   B PHE   A 1 127 ? 8.03948   -4.08348  -17.46672 0.368 23.52582  ? 134 PHE   A C   1 
ATOM   1091 O O   A PHE   A 1 127 ? 8.95800   -4.60381  -18.11119 0.632 22.02949  ? 134 PHE   A O   1 
ATOM   1092 O O   B PHE   A 1 127 ? 8.88951   -4.32426  -18.32951 0.368 23.69856  ? 134 PHE   A O   1 
ATOM   1093 C CB  A PHE   A 1 127 ? 9.66896   -4.53910  -15.29227 0.632 20.39279  ? 134 PHE   A CB  1 
ATOM   1094 C CB  B PHE   A 1 127 ? 9.65707   -3.86045  -15.57398 0.368 27.41654  ? 134 PHE   A CB  1 
ATOM   1095 C CG  A PHE   A 1 127 ? 10.10623  -3.94740  -13.95752 0.632 19.58940  ? 134 PHE   A CG  1 
ATOM   1096 C CG  B PHE   A 1 127 ? 9.87930   -3.20509  -14.29734 0.368 27.67642  ? 134 PHE   A CG  1 
ATOM   1097 C CD1 A PHE   A 1 127 ? 11.02230  -2.90457  -13.92416 0.632 24.77224  ? 134 PHE   A CD1 1 
ATOM   1098 C CD1 B PHE   A 1 127 ? 10.38140  -1.91025  -14.26683 0.368 31.23352  ? 134 PHE   A CD1 1 
ATOM   1099 C CD2 A PHE   A 1 127 ? 9.55079   -4.37879  -12.75550 0.632 23.66562  ? 134 PHE   A CD2 1 
ATOM   1100 C CD2 B PHE   A 1 127 ? 9.47197   -3.80456  -13.12705 0.368 23.79586  ? 134 PHE   A CD2 1 
ATOM   1101 C CE1 A PHE   A 1 127 ? 11.41876  -2.31170  -12.73174 0.632 23.33822  ? 134 PHE   A CE1 1 
ATOM   1102 C CE1 B PHE   A 1 127 ? 10.50530  -1.25713  -13.08417 0.368 26.35622  ? 134 PHE   A CE1 1 
ATOM   1103 C CE2 A PHE   A 1 127 ? 9.96295   -3.82067  -11.51171 0.632 22.13187  ? 134 PHE   A CE2 1 
ATOM   1104 C CE2 B PHE   A 1 127 ? 9.61276   -3.15899  -11.94509 0.368 27.04813  ? 134 PHE   A CE2 1 
ATOM   1105 C CZ  A PHE   A 1 127 ? 10.86568  -2.75394  -11.49581 0.632 24.12532  ? 134 PHE   A CZ  1 
ATOM   1106 C CZ  B PHE   A 1 127 ? 10.12329  -1.89105  -11.91268 0.368 30.92313  ? 134 PHE   A CZ  1 
ATOM   1107 N N   . GLY   A 1 128 ? 6.78174   -4.47078  -17.57371 1.000 21.74964  ? 135 GLY   A N   1 
ATOM   1108 C CA  . GLY   A 1 128 ? 6.33582   -4.86573  -18.87655 1.000 21.00716  ? 135 GLY   A CA  1 
ATOM   1109 C C   . GLY   A 1 128 ? 6.57147   -6.31168  -19.23595 1.000 20.23242  ? 135 GLY   A C   1 
ATOM   1110 O O   . GLY   A 1 128 ? 6.45940   -6.66426  -20.41888 1.000 23.75449  ? 135 GLY   A O   1 
ATOM   1111 N N   . VAL   A 1 129 ? 6.95514   -7.12440  -18.25888 1.000 19.02602  ? 136 VAL   A N   1 
ATOM   1112 C CA  . VAL   A 1 129 ? 7.29758   -8.51065  -18.47390 1.000 17.10741  ? 136 VAL   A CA  1 
ATOM   1113 C C   . VAL   A 1 129 ? 6.46065   -9.41490  -17.58552 1.000 17.76491  ? 136 VAL   A C   1 
ATOM   1114 O O   . VAL   A 1 129 ? 6.85096   -10.54966 -17.29010 1.000 17.91344  ? 136 VAL   A O   1 
ATOM   1115 C CB  . VAL   A 1 129 ? 8.81073   -8.76600  -18.32767 1.000 17.85053  ? 136 VAL   A CB  1 
ATOM   1116 C CG1 . VAL   A 1 129 ? 9.51612   -8.09654  -19.51760 1.000 21.53080  ? 136 VAL   A CG1 1 
ATOM   1117 C CG2 . VAL   A 1 129 ? 9.38831   -8.23076  -17.05298 1.000 19.78159  ? 136 VAL   A CG2 1 
ATOM   1118 N N   . GLY   A 1 130 ? 5.26049   -8.94910  -17.23252 1.000 17.85518  ? 137 GLY   A N   1 
ATOM   1119 C CA  . GLY   A 1 130 ? 4.41140   -9.76647  -16.34505 1.000 18.30905  ? 137 GLY   A CA  1 
ATOM   1120 C C   . GLY   A 1 130 ? 3.96446   -11.10456 -16.92479 1.000 17.63847  ? 137 GLY   A C   1 
ATOM   1121 O O   . GLY   A 1 130 ? 3.67699   -12.00072 -16.14068 1.000 18.22173  ? 137 GLY   A O   1 
ATOM   1122 N N   . PHE   A 1 131 ? 3.90953   -11.24863 -18.25384 1.000 16.70383  ? 138 PHE   A N   1 
ATOM   1123 C CA  . PHE   A 1 131 ? 3.57983   -12.54294 -18.82437 1.000 16.27463  ? 138 PHE   A CA  1 
ATOM   1124 C C   . PHE   A 1 131 ? 4.40836   -13.65387 -18.19208 1.000 16.50661  ? 138 PHE   A C   1 
ATOM   1125 O O   . PHE   A 1 131 ? 3.89613   -14.75108 -17.91236 1.000 16.51627  ? 138 PHE   A O   1 
ATOM   1126 C CB  . PHE   A 1 131 ? 3.88155   -12.51868 -20.34182 1.000 16.53249  ? 138 PHE   A CB  1 
ATOM   1127 C CG  . PHE   A 1 131 ? 3.79654   -13.90230 -20.93965 1.000 16.61719  ? 138 PHE   A CG  1 
ATOM   1128 C CD1 . PHE   A 1 131 ? 2.58417   -14.53350 -21.15514 1.000 17.41066  ? 138 PHE   A CD1 1 
ATOM   1129 C CD2 . PHE   A 1 131 ? 4.99163   -14.54903 -21.27004 1.000 16.99473  ? 138 PHE   A CD2 1 
ATOM   1130 C CE1 . PHE   A 1 131 ? 2.52208   -15.84036 -21.65097 1.000 16.99265  ? 138 PHE   A CE1 1 
ATOM   1131 C CE2 . PHE   A 1 131 ? 4.94639   -15.86035 -21.76043 1.000 18.23832  ? 138 PHE   A CE2 1 
ATOM   1132 C CZ  . PHE   A 1 131 ? 3.71835   -16.49896 -21.95869 1.000 19.16122  ? 138 PHE   A CZ  1 
ATOM   1133 N N   . TYR   A 1 132 ? 5.70902   -13.39218 -17.97905 1.000 16.93533  ? 139 TYR   A N   1 
ATOM   1134 C CA  . TYR   A 1 132 ? 6.59992   -14.49049 -17.57303 1.000 15.29783  ? 139 TYR   A CA  1 
ATOM   1135 C C   . TYR   A 1 132 ? 6.34504   -14.94435 -16.14600 1.000 16.99925  ? 139 TYR   A C   1 
ATOM   1136 O O   . TYR   A 1 132 ? 6.82210   -16.02915 -15.78142 1.000 17.71197  ? 139 TYR   A O   1 
ATOM   1137 C CB  . TYR   A 1 132 ? 8.07483   -14.07738 -17.75250 1.000 15.39061  ? 139 TYR   A CB  1 
ATOM   1138 C CG  . TYR   A 1 132 ? 8.36171   -13.78877 -19.24289 1.000 16.52912  ? 139 TYR   A CG  1 
ATOM   1139 C CD1 . TYR   A 1 132 ? 8.64350   -14.84316 -20.12296 1.000 16.52415  ? 139 TYR   A CD1 1 
ATOM   1140 C CD2 . TYR   A 1 132 ? 8.29035   -12.48853 -19.73483 1.000 18.33745  ? 139 TYR   A CD2 1 
ATOM   1141 C CE1 . TYR   A 1 132 ? 8.84018   -14.61334 -21.50245 1.000 17.39096  ? 139 TYR   A CE1 1 
ATOM   1142 C CE2 . TYR   A 1 132 ? 8.48725   -12.23488 -21.12597 1.000 20.49565  ? 139 TYR   A CE2 1 
ATOM   1143 C CZ  . TYR   A 1 132 ? 8.76855   -13.30354 -21.96843 1.000 20.37948  ? 139 TYR   A CZ  1 
ATOM   1144 O OH  . TYR   A 1 132 ? 8.97913   -12.97344 -23.29097 1.000 21.61696  ? 139 TYR   A OH  1 
ATOM   1145 N N   . SER   A 1 133 ? 5.54411   -14.18264 -15.39667 1.000 16.10551  ? 140 SER   A N   1 
ATOM   1146 C CA  . SER   A 1 133 ? 5.08729   -14.65478 -14.07941 1.000 16.58947  ? 140 SER   A CA  1 
ATOM   1147 C C   . SER   A 1 133 ? 4.24356   -15.91137 -14.17440 1.000 14.67239  ? 140 SER   A C   1 
ATOM   1148 O O   . SER   A 1 133 ? 4.03278   -16.57927 -13.15054 1.000 17.66029  ? 140 SER   A O   1 
ATOM   1149 C CB  . SER   A 1 133 ? 4.34934   -13.57133 -13.26922 1.000 18.24858  ? 140 SER   A CB  1 
ATOM   1150 O OG  . SER   A 1 133 ? 3.07022   -13.31924 -13.83691 1.000 17.71391  ? 140 SER   A OG  1 
ATOM   1151 N N   . ALA   A 1 134 ? 3.75726   -16.23601 -15.37744 1.000 16.47699  ? 141 ALA   A N   1 
ATOM   1152 C CA  . ALA   A 1 134 ? 3.08535   -17.54631 -15.53349 1.000 15.86008  ? 141 ALA   A CA  1 
ATOM   1153 C C   . ALA   A 1 134 ? 3.92783   -18.68827 -15.02880 1.000 15.22465  ? 141 ALA   A C   1 
ATOM   1154 O O   . ALA   A 1 134 ? 3.38761   -19.69500 -14.54866 1.000 17.74220  ? 141 ALA   A O   1 
ATOM   1155 C CB  . ALA   A 1 134 ? 2.78567   -17.74855 -17.02407 1.000 17.56394  ? 141 ALA   A CB  1 
ATOM   1156 N N   . TYR   A 1 135 ? 5.28057   -18.55523 -15.13592 1.000 15.22787  ? 142 TYR   A N   1 
ATOM   1157 C CA  . TYR   A 1 135 ? 6.12544   -19.67567 -14.73887 1.000 17.24086  ? 142 TYR   A CA  1 
ATOM   1158 C C   . TYR   A 1 135 ? 6.31177   -19.79364 -13.22523 1.000 17.86185  ? 142 TYR   A C   1 
ATOM   1159 O O   . TYR   A 1 135 ? 6.95466   -20.73702 -12.76833 1.000 19.73009  ? 142 TYR   A O   1 
ATOM   1160 C CB  . TYR   A 1 135 ? 7.49171   -19.58164 -15.45251 1.000 17.57675  ? 142 TYR   A CB  1 
ATOM   1161 C CG  . TYR   A 1 135 ? 7.31562   -19.87712 -16.93888 1.000 17.14373  ? 142 TYR   A CG  1 
ATOM   1162 C CD1 . TYR   A 1 135 ? 7.31910   -21.20840 -17.41660 1.000 18.19810  ? 142 TYR   A CD1 1 
ATOM   1163 C CD2 . TYR   A 1 135 ? 7.03814   -18.83125 -17.84148 1.000 16.16504  ? 142 TYR   A CD2 1 
ATOM   1164 C CE1 . TYR   A 1 135 ? 7.07543   -21.50059 -18.76018 1.000 17.95245  ? 142 TYR   A CE1 1 
ATOM   1165 C CE2 . TYR   A 1 135 ? 6.77876   -19.11463 -19.18801 1.000 16.22358  ? 142 TYR   A CE2 1 
ATOM   1166 C CZ  . TYR   A 1 135 ? 6.82801   -20.44281 -19.62410 1.000 17.72546  ? 142 TYR   A CZ  1 
ATOM   1167 O OH  . TYR   A 1 135 ? 6.57644   -20.67956 -20.96113 1.000 17.12242  ? 142 TYR   A OH  1 
ATOM   1168 N N   . LEU   A 1 136 ? 5.63295   -18.92509 -12.45244 1.000 17.62874  ? 143 LEU   A N   1 
ATOM   1169 C CA  . LEU   A 1 136 ? 5.49074   -19.19181 -11.02588 1.000 16.87037  ? 143 LEU   A CA  1 
ATOM   1170 C C   . LEU   A 1 136 ? 4.67155   -20.43776 -10.76514 1.000 19.78530  ? 143 LEU   A C   1 
ATOM   1171 O O   . LEU   A 1 136 ? 4.84646   -21.09990 -9.73434  1.000 20.46449  ? 143 LEU   A O   1 
ATOM   1172 C CB  . LEU   A 1 136 ? 4.80221   -17.99352 -10.33331 1.000 19.28724  ? 143 LEU   A CB  1 
ATOM   1173 C CG  . LEU   A 1 136 ? 5.63194   -16.69296 -10.30784 1.000 18.48309  ? 143 LEU   A CG  1 
ATOM   1174 C CD1 . LEU   A 1 136 ? 4.77614   -15.50615 -9.84953  1.000 19.00626  ? 143 LEU   A CD1 1 
ATOM   1175 C CD2 . LEU   A 1 136 ? 6.90012   -16.85061 -9.40393  1.000 22.17919  ? 143 LEU   A CD2 1 
ATOM   1176 N N   . VAL   A 1 137 ? 3.70182   -20.71807 -11.64781 1.000 19.09341  ? 144 VAL   A N   1 
ATOM   1177 C CA  . VAL   A 1 137 ? 2.75538   -21.79209 -11.38395 1.000 18.43668  ? 144 VAL   A CA  1 
ATOM   1178 C C   . VAL   A 1 137 ? 2.68874   -22.81688 -12.48560 1.000 18.80033  ? 144 VAL   A C   1 
ATOM   1179 O O   . VAL   A 1 137 ? 2.17738   -23.91485 -12.23250 1.000 20.58583  ? 144 VAL   A O   1 
ATOM   1180 C CB  . VAL   A 1 137 ? 1.34185   -21.25365 -11.09570 1.000 18.73256  ? 144 VAL   A CB  1 
ATOM   1181 C CG1 . VAL   A 1 137 ? 1.33866   -20.33077 -9.82609  1.000 20.25688  ? 144 VAL   A CG1 1 
ATOM   1182 C CG2 . VAL   A 1 137 ? 0.79329   -20.46816 -12.30413 1.000 19.20086  ? 144 VAL   A CG2 1 
ATOM   1183 N N   . ALA   A 1 138 ? 3.20922   -22.51992 -13.67346 1.000 18.13328  ? 145 ALA   A N   1 
ATOM   1184 C CA  . ALA   A 1 138 ? 3.09448   -23.42577 -14.82535 1.000 18.56007  ? 145 ALA   A CA  1 
ATOM   1185 C C   . ALA   A 1 138 ? 4.41996   -24.05480 -15.15889 1.000 19.50598  ? 145 ALA   A C   1 
ATOM   1186 O O   . ALA   A 1 138 ? 5.44050   -23.33976 -15.25074 1.000 22.21910  ? 145 ALA   A O   1 
ATOM   1187 C CB  . ALA   A 1 138 ? 2.62145   -22.64769 -16.04133 1.000 19.83555  ? 145 ALA   A CB  1 
ATOM   1188 N N   . GLU   A 1 139 ? 4.38127   -25.35392 -15.42369 1.000 19.90534  ? 146 GLU   A N   1 
ATOM   1189 C CA  . GLU   A 1 139 ? 5.56259   -26.01712 -15.98517 1.000 20.00261  ? 146 GLU   A CA  1 
ATOM   1190 C C   . GLU   A 1 139 ? 5.67437   -25.80721 -17.47622 1.000 21.65204  ? 146 GLU   A C   1 
ATOM   1191 O O   . GLU   A 1 139 ? 6.76149   -25.93227 -18.02767 1.000 22.33731  ? 146 GLU   A O   1 
ATOM   1192 C CB  . GLU   A 1 139 ? 5.50482   -27.49539 -15.63075 1.000 24.35305  ? 146 GLU   A CB  1 
ATOM   1193 C CG  . GLU   A 1 139 ? 4.40956   -28.21577 -16.28546 1.000 31.63496  ? 146 GLU   A CG  1 
ATOM   1194 C CD  . GLU   A 1 139 ? 4.25615   -29.64852 -15.78351 1.000 65.81785  ? 146 GLU   A CD  1 
ATOM   1195 O OE1 . GLU   A 1 139 ? 3.44813   -30.40279 -16.38407 1.000 65.39834  ? 146 GLU   A OE1 1 
ATOM   1196 O OE2 . GLU   A 1 139 ? 4.92709   -30.00410 -14.78489 1.000 50.39133  ? 146 GLU   A OE2 1 
ATOM   1197 N N   . LYS   A 1 140 ? 4.57484   -25.53983 -18.15261 1.000 19.86949  ? 147 LYS   A N   1 
ATOM   1198 C CA  . LYS   A 1 140 ? 4.55222   -25.30331 -19.58799 1.000 18.78759  ? 147 LYS   A CA  1 
ATOM   1199 C C   . LYS   A 1 140 ? 3.45615   -24.25586 -19.80621 1.000 16.73757  ? 147 LYS   A C   1 
ATOM   1200 O O   . LYS   A 1 140 ? 2.43095   -24.27417 -19.11373 1.000 18.44078  ? 147 LYS   A O   1 
ATOM   1201 C CB  . LYS   A 1 140 ? 4.25831   -26.58951 -20.36547 1.000 19.70299  ? 147 LYS   A CB  1 
ATOM   1202 C CG  . LYS   A 1 140 ? 4.16061   -26.37806 -21.88536 1.000 19.27266  ? 147 LYS   A CG  1 
ATOM   1203 C CD  . LYS   A 1 140 ? 4.13787   -27.73098 -22.53364 1.000 23.18925  ? 147 LYS   A CD  1 
ATOM   1204 C CE  . LYS   A 1 140 ? 2.74773   -28.21091 -22.66079 1.000 27.81385  ? 147 LYS   A CE  1 
ATOM   1205 N NZ  . LYS   A 1 140 ? 2.73102   -29.68528 -23.02840 1.000 40.35811  ? 147 LYS   A NZ  1 
ATOM   1206 N N   . VAL   A 1 141 ? 3.70247   -23.35409 -20.74299 1.000 16.26771  ? 148 VAL   A N   1 
ATOM   1207 C CA  . VAL   A 1 141 ? 2.70888   -22.35601 -21.12500 1.000 16.63818  ? 148 VAL   A CA  1 
ATOM   1208 C C   . VAL   A 1 141 ? 2.51949   -22.45985 -22.63056 1.000 16.48579  ? 148 VAL   A C   1 
ATOM   1209 O O   . VAL   A 1 141 ? 3.50104   -22.50961 -23.38358 1.000 17.01808  ? 148 VAL   A O   1 
ATOM   1210 C CB  . VAL   A 1 141 ? 3.14037   -20.94190 -20.74076 1.000 16.80568  ? 148 VAL   A CB  1 
ATOM   1211 C CG1 . VAL   A 1 141 ? 2.09009   -19.93005 -21.23516 1.000 18.10425  ? 148 VAL   A CG1 1 
ATOM   1212 C CG2 . VAL   A 1 141 ? 3.31725   -20.83636 -19.18589 1.000 17.92292  ? 148 VAL   A CG2 1 
ATOM   1213 N N   . THR   A 1 142 ? 1.25850   -22.51108 -23.07571 1.000 16.87799  ? 149 THR   A N   1 
ATOM   1214 C CA  . THR   A 1 142 ? 0.92252   -22.50054 -24.49555 1.000 18.62341  ? 149 THR   A CA  1 
ATOM   1215 C C   . THR   A 1 142 ? 0.11358   -21.24105 -24.75717 1.000 19.35791  ? 149 THR   A C   1 
ATOM   1216 O O   . THR   A 1 142 ? -0.82977  -20.94778 -24.00036 1.000 19.76451  ? 149 THR   A O   1 
ATOM   1217 C CB  . THR   A 1 142 ? 0.08072   -23.72130 -24.87128 1.000 17.44891  ? 149 THR   A CB  1 
ATOM   1218 O OG1 . THR   A 1 142 ? 0.72158   -24.94397 -24.45206 1.000 21.02299  ? 149 THR   A OG1 1 
ATOM   1219 C CG2 . THR   A 1 142 ? -0.15955  -23.77561 -26.39247 1.000 20.10214  ? 149 THR   A CG2 1 
ATOM   1220 N N   . VAL   A 1 143 ? 0.45177   -20.49562 -25.79440 1.000 16.72391  ? 150 VAL   A N   1 
ATOM   1221 C CA  . VAL   A 1 143 ? -0.25196  -19.25635 -26.10712 1.000 15.55334  ? 150 VAL   A CA  1 
ATOM   1222 C C   . VAL   A 1 143 ? -0.82157  -19.41400 -27.50189 1.000 17.75862  ? 150 VAL   A C   1 
ATOM   1223 O O   . VAL   A 1 143 ? -0.05450  -19.59211 -28.46578 1.000 18.64830  ? 150 VAL   A O   1 
ATOM   1224 C CB  . VAL   A 1 143 ? 0.66594   -18.04660 -25.99846 1.000 15.57156  ? 150 VAL   A CB  1 
ATOM   1225 C CG1 . VAL   A 1 143 ? -0.10553  -16.74715 -26.40586 1.000 19.99983  ? 150 VAL   A CG1 1 
ATOM   1226 C CG2 . VAL   A 1 143 ? 1.27055   -17.88879 -24.58734 1.000 16.61729  ? 150 VAL   A CG2 1 
ATOM   1227 N N   . ILE   A 1 144 ? -2.14151  -19.36048 -27.64415 1.000 16.57611  ? 151 ILE   A N   1 
ATOM   1228 C CA  . ILE   A 1 144 ? -2.78582  -19.44971 -28.95722 1.000 16.34363  ? 151 ILE   A CA  1 
ATOM   1229 C C   . ILE   A 1 144 ? -3.29570  -18.04883 -29.25710 1.000 16.91380  ? 151 ILE   A C   1 
ATOM   1230 O O   . ILE   A 1 144 ? -3.85935  -17.41336 -28.36818 1.000 18.61044  ? 151 ILE   A O   1 
ATOM   1231 C CB  . ILE   A 1 144 ? -3.97125  -20.42050 -28.94625 1.000 19.79771  ? 151 ILE   A CB  1 
ATOM   1232 C CG1 . ILE   A 1 144 ? -3.61542  -21.72596 -28.23412 1.000 28.33729  ? 151 ILE   A CG1 1 
ATOM   1233 C CG2 . ILE   A 1 144 ? -4.50216  -20.60944 -30.38062 1.000 21.23467  ? 151 ILE   A CG2 1 
ATOM   1234 C CD1 . ILE   A 1 144 ? -2.67215  -22.52601 -28.91414 1.000 28.97873  ? 151 ILE   A CD1 1 
ATOM   1235 N N   . THR   A 1 145 ? -3.01347  -17.52179 -30.44147 1.000 17.00817  ? 152 THR   A N   1 
ATOM   1236 C CA  . THR   A 1 145 ? -3.37056  -16.12285 -30.68611 1.000 16.87299  ? 152 THR   A CA  1 
ATOM   1237 C C   . THR   A 1 145 ? -3.77099  -15.92822 -32.12924 1.000 18.36846  ? 152 THR   A C   1 
ATOM   1238 O O   . THR   A 1 145 ? -3.30573  -16.64569 -33.06011 1.000 19.32743  ? 152 THR   A O   1 
ATOM   1239 C CB  . THR   A 1 145 ? -2.18177  -15.22101 -30.29368 1.000 17.10671  ? 152 THR   A CB  1 
ATOM   1240 O OG1 . THR   A 1 145 ? -2.57648  -13.84740 -30.24583 1.000 18.29532  ? 152 THR   A OG1 1 
ATOM   1241 C CG2 . THR   A 1 145 ? -0.97638  -15.41535 -31.23014 1.000 18.33025  ? 152 THR   A CG2 1 
ATOM   1242 N N   . LYS   A 1 146 ? -4.57267  -14.88360 -32.32998 1.000 18.20352  ? 153 LYS   A N   1 
ATOM   1243 C CA  . LYS   A 1 146 ? -5.07149  -14.54381 -33.65582 1.000 17.81874  ? 153 LYS   A CA  1 
ATOM   1244 C C   . LYS   A 1 146 ? -5.21074  -13.03556 -33.69766 1.000 21.33949  ? 153 LYS   A C   1 
ATOM   1245 O O   . LYS   A 1 146 ? -5.99578  -12.45925 -32.92894 1.000 20.38366  ? 153 LYS   A O   1 
ATOM   1246 C CB  . LYS   A 1 146 ? -6.44867  -15.18410 -33.95774 1.000 19.68516  ? 153 LYS   A CB  1 
ATOM   1247 C CG  . LYS   A 1 146 ? -7.08834  -14.78036 -35.28061 1.000 20.77050  ? 153 LYS   A CG  1 
ATOM   1248 C CD  . LYS   A 1 146 ? -6.26292  -15.24949 -36.48920 1.000 22.03190  ? 153 LYS   A CD  1 
ATOM   1249 C CE  . LYS   A 1 146 ? -6.93486  -14.92617 -37.78035 1.000 23.77564  ? 153 LYS   A CE  1 
ATOM   1250 N NZ  . LYS   A 1 146 ? -6.96338  -13.46628 -38.10310 1.000 25.75734  ? 153 LYS   A NZ  1 
ATOM   1251 N N   . HIS   A 1 147 ? -4.46524  -12.40778 -34.57373 1.000 21.19764  ? 154 HIS   A N   1 
ATOM   1252 C CA  . HIS   A 1 147 ? -4.50717  -10.96447 -34.78404 1.000 18.27829  ? 154 HIS   A CA  1 
ATOM   1253 C C   . HIS   A 1 147 ? -5.16904  -10.73915 -36.13110 1.000 21.75547  ? 154 HIS   A C   1 
ATOM   1254 O O   . HIS   A 1 147 ? -5.06429  -11.57338 -37.03042 1.000 24.11292  ? 154 HIS   A O   1 
ATOM   1255 C CB  . HIS   A 1 147 ? -3.04787  -10.45014 -34.80965 1.000 20.46429  ? 154 HIS   A CB  1 
ATOM   1256 C CG  . HIS   A 1 147 ? -2.90316  -8.95699  -34.93567 1.000 21.53989  ? 154 HIS   A CG  1 
ATOM   1257 N ND1 . HIS   A 1 147 ? -3.10510  -8.27117  -36.11113 1.000 23.95578  ? 154 HIS   A ND1 1 
ATOM   1258 C CD2 . HIS   A 1 147 ? -2.48991  -8.03678  -34.01789 1.000 22.87249  ? 154 HIS   A CD2 1 
ATOM   1259 C CE1 . HIS   A 1 147 ? -2.87462  -6.98441  -35.90549 1.000 25.71219  ? 154 HIS   A CE1 1 
ATOM   1260 N NE2 . HIS   A 1 147 ? -2.49036  -6.82167  -34.64773 1.000 24.24383  ? 154 HIS   A NE2 1 
ATOM   1261 N N   . ASN   A 1 148 ? -5.89674  -9.62922  -36.27718 1.000 20.79911  ? 155 ASN   A N   1 
ATOM   1262 C CA  . ASN   A 1 148 ? -6.57797  -9.38968  -37.54322 1.000 22.54917  ? 155 ASN   A CA  1 
ATOM   1263 C C   . ASN   A 1 148 ? -5.64988  -9.44947  -38.76645 1.000 24.34924  ? 155 ASN   A C   1 
ATOM   1264 O O   . ASN   A 1 148 ? -6.11969  -9.80550  -39.87501 1.000 27.94182  ? 155 ASN   A O   1 
ATOM   1265 C CB  . ASN   A 1 148 ? -7.26448  -7.99226  -37.53633 1.000 23.48095  ? 155 ASN   A CB  1 
ATOM   1266 C CG  . ASN   A 1 148 ? -8.52012  -7.96342  -36.75741 1.000 24.89472  ? 155 ASN   A CG  1 
ATOM   1267 O OD1 . ASN   A 1 148 ? -9.18702  -8.96698  -36.58916 1.000 28.14919  ? 155 ASN   A OD1 1 
ATOM   1268 N ND2 . ASN   A 1 148 ? -8.84661  -6.79342  -36.23735 1.000 26.51107  ? 155 ASN   A ND2 1 
ATOM   1269 N N   . ASP   A 1 149 ? -4.35977  -9.11073  -38.60674 1.000 24.96108  ? 156 ASP   A N   1 
ATOM   1270 C CA  . ASP   A 1 149 ? -3.43601  -9.04857  -39.74576 1.000 28.93754  ? 156 ASP   A CA  1 
ATOM   1271 C C   . ASP   A 1 149 ? -2.61408  -10.31316 -39.93992 1.000 34.79830  ? 156 ASP   A C   1 
ATOM   1272 O O   . ASP   A 1 149 ? -1.65757  -10.29073 -40.74225 1.000 34.06847  ? 156 ASP   A O   1 
ATOM   1273 C CB  . ASP   A 1 149 ? -2.47577  -7.86679  -39.56888 1.000 27.96790  ? 156 ASP   A CB  1 
ATOM   1274 C CG  . ASP   A 1 149 ? -3.19604  -6.51511  -39.54957 1.000 29.75587  ? 156 ASP   A CG  1 
ATOM   1275 O OD1 . ASP   A 1 149 ? -4.34573  -6.43100  -40.04663 1.000 33.29373  ? 156 ASP   A OD1 1 
ATOM   1276 O OD2 . ASP   A 1 149 ? -2.60695  -5.56704  -38.97993 1.000 35.78244  ? 156 ASP   A OD2 1 
ATOM   1277 N N   . ASP   A 1 150 ? -2.94065  -11.41511 -39.25523 1.000 26.70720  ? 157 ASP   A N   1 
ATOM   1278 C CA  . ASP   A 1 150 ? -2.14714  -12.64084 -39.41971 1.000 23.87835  ? 157 ASP   A CA  1 
ATOM   1279 C C   . ASP   A 1 150 ? -3.03566  -13.86591 -39.18624 1.000 27.13565  ? 157 ASP   A C   1 
ATOM   1280 O O   . ASP   A 1 150 ? -4.23739  -13.75936 -38.91999 1.000 27.24993  ? 157 ASP   A O   1 
ATOM   1281 C CB  . ASP   A 1 150 ? -0.92073  -12.58034 -38.49992 1.000 25.06396  ? 157 ASP   A CB  1 
ATOM   1282 C CG  . ASP   A 1 150 ? 0.26231   -13.36901 -39.02033 1.000 25.58169  ? 157 ASP   A CG  1 
ATOM   1283 O OD1 . ASP   A 1 150 ? 0.15892   -14.17879 -39.97041 1.000 30.33398  ? 157 ASP   A OD1 1 
ATOM   1284 O OD2 . ASP   A 1 150 ? 1.36459   -13.15460 -38.40152 1.000 25.94093  ? 157 ASP   A OD2 1 
ATOM   1285 N N   . GLU   A 1 151 ? -2.44604  -15.04216 -39.31752 1.000 26.16533  ? 158 GLU   A N   1 
ATOM   1286 C CA  . GLU   A 1 151 ? -3.11038  -16.31032 -39.08487 1.000 28.77040  ? 158 GLU   A CA  1 
ATOM   1287 C C   . GLU   A 1 151 ? -3.00257  -16.69460 -37.62087 1.000 22.45471  ? 158 GLU   A C   1 
ATOM   1288 O O   . GLU   A 1 151 ? -2.30303  -16.06495 -36.85537 1.000 23.04806  ? 158 GLU   A O   1 
ATOM   1289 C CB  . GLU   A 1 151 ? -2.53964  -17.40300 -40.00186 1.000 33.24652  ? 158 GLU   A CB  1 
ATOM   1290 C CG  . GLU   A 1 151 ? -2.35475  -16.89916 -41.44651 1.000 41.57803  ? 158 GLU   A CG  1 
ATOM   1291 C CD  . GLU   A 1 151 ? -3.69362  -16.69163 -42.12411 1.000 71.12647  ? 158 GLU   A CD  1 
ATOM   1292 O OE1 . GLU   A 1 151 ? -4.59917  -17.50673 -41.86883 1.000 80.63153  ? 158 GLU   A OE1 1 
ATOM   1293 O OE2 . GLU   A 1 151 ? -3.86301  -15.70791 -42.88483 1.000 75.93756  ? 158 GLU   A OE2 1 
ATOM   1294 N N   . GLN   A 1 152 ? -3.69824  -17.75151 -37.25274 1.000 23.70060  ? 159 GLN   A N   1 
ATOM   1295 C CA  . GLN   A 1 152 ? -3.69812  -18.22806 -35.87642 1.000 21.30466  ? 159 GLN   A CA  1 
ATOM   1296 C C   . GLN   A 1 152 ? -2.44708  -19.04063 -35.59596 1.000 20.44741  ? 159 GLN   A C   1 
ATOM   1297 O O   . GLN   A 1 152 ? -2.11930  -19.97384 -36.34945 1.000 23.75046  ? 159 GLN   A O   1 
ATOM   1298 C CB  . GLN   A 1 152 ? -4.95919  -19.06900 -35.62701 1.000 21.37726  ? 159 GLN   A CB  1 
ATOM   1299 C CG  . GLN   A 1 152 ? -5.18601  -19.39927 -34.10875 1.000 21.88496  ? 159 GLN   A CG  1 
ATOM   1300 C CD  . GLN   A 1 152 ? -6.61277  -19.87241 -33.87210 1.000 26.11587  ? 159 GLN   A CD  1 
ATOM   1301 O OE1 . GLN   A 1 152 ? -7.52961  -19.18324 -34.24471 1.000 28.01297  ? 159 GLN   A OE1 1 
ATOM   1302 N NE2 . GLN   A 1 152 ? -6.77889  -21.00977 -33.27658 1.000 27.47464  ? 159 GLN   A NE2 1 
ATOM   1303 N N   A TYR   A 1 153 ? -1.76223  -18.70456 -34.50769 0.500 19.44860  ? 160 TYR   A N   1 
ATOM   1304 N N   B TYR   A 1 153 ? -1.76223  -18.70456 -34.50769 0.500 19.44860  ? 160 TYR   A N   1 
ATOM   1305 C CA  A TYR   A 1 153 ? -0.50354  -19.34479 -34.19571 0.500 22.21924  ? 160 TYR   A CA  1 
ATOM   1306 C CA  B TYR   A 1 153 ? -0.50354  -19.34479 -34.19571 0.500 22.21924  ? 160 TYR   A CA  1 
ATOM   1307 C C   A TYR   A 1 153 ? -0.55750  -19.87145 -32.77511 0.500 20.28358  ? 160 TYR   A C   1 
ATOM   1308 C C   B TYR   A 1 153 ? -0.55750  -19.87145 -32.77511 0.500 20.28358  ? 160 TYR   A C   1 
ATOM   1309 O O   A TYR   A 1 153 ? -1.25633  -19.31478 -31.91263 0.500 19.67908  ? 160 TYR   A O   1 
ATOM   1310 O O   B TYR   A 1 153 ? -1.25633  -19.31478 -31.91263 0.500 19.67908  ? 160 TYR   A O   1 
ATOM   1311 C CB  A TYR   A 1 153 ? 0.67763   -18.35298 -34.32165 0.500 20.94940  ? 160 TYR   A CB  1 
ATOM   1312 C CB  B TYR   A 1 153 ? 0.67763   -18.35298 -34.32165 0.500 20.94940  ? 160 TYR   A CB  1 
ATOM   1313 C CG  A TYR   A 1 153 ? 1.10668   -18.15553 -35.74556 0.500 22.92401  ? 160 TYR   A CG  1 
ATOM   1314 C CG  B TYR   A 1 153 ? 1.10668   -18.15553 -35.74556 0.500 22.92401  ? 160 TYR   A CG  1 
ATOM   1315 C CD1 A TYR   A 1 153 ? 1.96055   -19.06723 -36.32189 0.500 25.08403  ? 160 TYR   A CD1 1 
ATOM   1316 C CD1 B TYR   A 1 153 ? 1.96055   -19.06723 -36.32189 0.500 25.08403  ? 160 TYR   A CD1 1 
ATOM   1317 C CD2 A TYR   A 1 153 ? 0.59874   -17.12740 -36.55599 0.500 25.75184  ? 160 TYR   A CD2 1 
ATOM   1318 C CD2 B TYR   A 1 153 ? 0.59874   -17.12740 -36.55599 0.500 25.75184  ? 160 TYR   A CD2 1 
ATOM   1319 C CE1 A TYR   A 1 153 ? 2.37556   -18.95706 -37.63083 0.500 31.68010  ? 160 TYR   A CE1 1 
ATOM   1320 C CE1 B TYR   A 1 153 ? 2.37556   -18.95706 -37.63083 0.500 31.68010  ? 160 TYR   A CE1 1 
ATOM   1321 C CE2 A TYR   A 1 153 ? 1.02534   -17.01689 -37.89375 0.500 26.90647  ? 160 TYR   A CE2 1 
ATOM   1322 C CE2 B TYR   A 1 153 ? 1.02534   -17.01689 -37.89375 0.500 26.90647  ? 160 TYR   A CE2 1 
ATOM   1323 C CZ  A TYR   A 1 153 ? 1.90966   -17.94578 -38.40713 0.500 32.07073  ? 160 TYR   A CZ  1 
ATOM   1324 C CZ  B TYR   A 1 153 ? 1.90966   -17.94578 -38.40713 0.500 32.07073  ? 160 TYR   A CZ  1 
ATOM   1325 O OH  A TYR   A 1 153 ? 2.35629   -17.88763 -39.72212 0.500 34.67343  ? 160 TYR   A OH  1 
ATOM   1326 O OH  B TYR   A 1 153 ? 2.35629   -17.88763 -39.72212 0.500 34.67343  ? 160 TYR   A OH  1 
ATOM   1327 N N   . ALA   A 1 154 ? 0.29276   -20.87115 -32.50761 1.000 19.99599  ? 161 ALA   A N   1 
ATOM   1328 C CA  . ALA   A 1 154 ? 0.55401   -21.39630 -31.16007 1.000 18.52024  ? 161 ALA   A CA  1 
ATOM   1329 C C   . ALA   A 1 154 ? 2.01727   -21.21682 -30.79491 1.000 18.46962  ? 161 ALA   A C   1 
ATOM   1330 O O   . ALA   A 1 154 ? 2.87471   -21.72779 -31.52879 1.000 19.29358  ? 161 ALA   A O   1 
ATOM   1331 C CB  . ALA   A 1 154 ? 0.22944   -22.88964 -31.09671 1.000 22.82766  ? 161 ALA   A CB  1 
ATOM   1332 N N   . TRP   A 1 155 ? 2.28446   -20.52056 -29.69791 1.000 17.17545  ? 162 TRP   A N   1 
ATOM   1333 C CA  . TRP   A 1 155 ? 3.60975   -20.44135 -29.08896 1.000 16.29365  ? 162 TRP   A CA  1 
ATOM   1334 C C   . TRP   A 1 155 ? 3.61899   -21.35619 -27.88178 1.000 17.81724  ? 162 TRP   A C   1 
ATOM   1335 O O   . TRP   A 1 155 ? 2.58988   -21.53593 -27.22404 1.000 17.96248  ? 162 TRP   A O   1 
ATOM   1336 C CB  . TRP   A 1 155 ? 3.80720   -18.98200 -28.65453 1.000 17.56982  ? 162 TRP   A CB  1 
ATOM   1337 C CG  . TRP   A 1 155 ? 5.01590   -18.57307 -27.86505 1.000 16.09055  ? 162 TRP   A CG  1 
ATOM   1338 C CD1 . TRP   A 1 155 ? 6.06056   -17.85582 -28.34523 1.000 15.80069  ? 162 TRP   A CD1 1 
ATOM   1339 C CD2 . TRP   A 1 155 ? 5.26648   -18.79026 -26.45940 1.000 16.81730  ? 162 TRP   A CD2 1 
ATOM   1340 N NE1 . TRP   A 1 155 ? 6.97270   -17.63174 -27.34771 1.000 16.13862  ? 162 TRP   A NE1 1 
ATOM   1341 C CE2 . TRP   A 1 155 ? 6.49966   -18.17416 -26.15703 1.000 15.57707  ? 162 TRP   A CE2 1 
ATOM   1342 C CE3 . TRP   A 1 155 ? 4.54198   -19.43068 -25.41783 1.000 16.58629  ? 162 TRP   A CE3 1 
ATOM   1343 C CZ2 . TRP   A 1 155 ? 7.05218   -18.19530 -24.86248 1.000 16.75979  ? 162 TRP   A CZ2 1 
ATOM   1344 C CZ3 . TRP   A 1 155 ? 5.08445   -19.45720 -24.15179 1.000 17.54420  ? 162 TRP   A CZ3 1 
ATOM   1345 C CH2 . TRP   A 1 155 ? 6.31962   -18.83350 -23.85899 1.000 16.27904  ? 162 TRP   A CH2 1 
ATOM   1346 N N   . GLU   A 1 156 ? 4.76313   -21.98179 -27.57727 1.000 15.54441  ? 163 GLU   A N   1 
ATOM   1347 C CA  . GLU   A 1 156 ? 4.80017   -22.78374 -26.36176 1.000 16.18798  ? 163 GLU   A CA  1 
ATOM   1348 C C   . GLU   A 1 156 ? 6.20543   -22.82219 -25.80775 1.000 16.65737  ? 163 GLU   A C   1 
ATOM   1349 O O   . GLU   A 1 156 ? 7.19400   -22.80383 -26.55562 1.000 17.59173  ? 163 GLU   A O   1 
ATOM   1350 C CB  . GLU   A 1 156 ? 4.35705   -24.19094 -26.72205 1.000 18.95263  ? 163 GLU   A CB  1 
ATOM   1351 C CG  . GLU   A 1 156 ? 4.22415   -25.16507 -25.60136 1.000 23.10769  ? 163 GLU   A CG  1 
ATOM   1352 C CD  . GLU   A 1 156 ? 3.47492   -26.41761 -26.08759 1.000 38.06709  ? 163 GLU   A CD  1 
ATOM   1353 O OE1 . GLU   A 1 156 ? 2.25049   -26.56927 -25.81020 1.000 30.72979  ? 163 GLU   A OE1 1 
ATOM   1354 O OE2 . GLU   A 1 156 ? 4.09355   -27.21846 -26.87310 1.000 31.24828  ? 163 GLU   A OE2 1 
ATOM   1355 N N   . SER   A 1 157 ? 6.31134   -22.90601 -24.48748 1.000 16.60869  ? 164 SER   A N   1 
ATOM   1356 C CA  . SER   A 1 157 ? 7.62451   -23.07592 -23.86834 1.000 16.31729  ? 164 SER   A CA  1 
ATOM   1357 C C   . SER   A 1 157 ? 7.45448   -23.77084 -22.53618 1.000 15.56281  ? 164 SER   A C   1 
ATOM   1358 O O   . SER   A 1 157 ? 6.55039   -23.40144 -21.74090 1.000 16.27208  ? 164 SER   A O   1 
ATOM   1359 C CB  . SER   A 1 157 ? 8.33507   -21.74763 -23.70053 1.000 17.45114  ? 164 SER   A CB  1 
ATOM   1360 O OG  . SER   A 1 157 ? 9.62249   -21.99241 -23.11528 1.000 16.67384  ? 164 SER   A OG  1 
ATOM   1361 N N   . SER   A 1 158 ? 8.37221   -24.71573 -22.26192 1.000 17.99635  ? 165 SER   A N   1 
ATOM   1362 C CA  . SER   A 1 158 ? 8.58050   -25.25154 -20.91479 1.000 18.54521  ? 165 SER   A CA  1 
ATOM   1363 C C   . SER   A 1 158 ? 9.82038   -24.65387 -20.27711 1.000 19.88996  ? 165 SER   A C   1 
ATOM   1364 O O   . SER   A 1 158 ? 10.42652  -25.30777 -19.42490 1.000 22.01953  ? 165 SER   A O   1 
ATOM   1365 C CB  . SER   A 1 158 ? 8.68489   -26.77495 -20.95316 1.000 21.19985  ? 165 SER   A CB  1 
ATOM   1366 O OG  . SER   A 1 158 ? 7.44035   -27.30201 -21.44009 1.000 24.49342  ? 165 SER   A OG  1 
ATOM   1367 N N   . ALA   A 1 159 ? 10.19323  -23.44635 -20.68617 1.000 18.69457  ? 166 ALA   A N   1 
ATOM   1368 C CA  . ALA   A 1 159 ? 11.46831  -22.76220 -20.26553 1.000 19.50854  ? 166 ALA   A CA  1 
ATOM   1369 C C   . ALA   A 1 159 ? 12.64096  -23.59612 -20.77887 1.000 22.42947  ? 166 ALA   A C   1 
ATOM   1370 O O   . ALA   A 1 159 ? 12.56765  -24.11917 -21.89337 1.000 23.65620  ? 166 ALA   A O   1 
ATOM   1371 C CB  . ALA   A 1 159 ? 11.39889  -22.45566 -18.74959 1.000 22.74909  ? 166 ALA   A CB  1 
ATOM   1372 N N   . GLY   A 1 160 ? 13.71513  -23.75454 -20.03528 1.000 24.31130  ? 167 GLY   A N   1 
ATOM   1373 C CA  . GLY   A 1 160 ? 14.83361  -24.47817 -20.62363 1.000 23.54869  ? 167 GLY   A CA  1 
ATOM   1374 C C   . GLY   A 1 160 ? 15.49868  -23.81514 -21.81140 1.000 24.93986  ? 167 GLY   A C   1 
ATOM   1375 O O   . GLY   A 1 160 ? 16.29430  -24.46715 -22.51966 1.000 26.47425  ? 167 GLY   A O   1 
ATOM   1376 N N   . GLY   A 1 161 ? 15.17992  -22.54991 -22.05392 1.000 20.99416  ? 168 GLY   A N   1 
ATOM   1377 C CA  . GLY   A 1 161 ? 15.92934  -21.77557 -23.02403 1.000 18.32903  ? 168 GLY   A CA  1 
ATOM   1378 C C   . GLY   A 1 161 ? 15.32974  -21.68226 -24.40752 1.000 17.29545  ? 168 GLY   A C   1 
ATOM   1379 O O   . GLY   A 1 161 ? 15.93859  -21.02767 -25.27315 1.000 20.59926  ? 168 GLY   A O   1 
ATOM   1380 N N   . SER   A 1 162 ? 14.21401  -22.35151 -24.66937 1.000 17.93562  ? 169 SER   A N   1 
ATOM   1381 C CA  . SER   A 1 162 ? 13.68675  -22.37967 -26.02572 1.000 17.27871  ? 169 SER   A CA  1 
ATOM   1382 C C   . SER   A 1 162 ? 12.16998  -22.29004 -25.97809 1.000 18.55312  ? 169 SER   A C   1 
ATOM   1383 O O   . SER   A 1 162 ? 11.53620  -22.58137 -24.96647 1.000 18.26682  ? 169 SER   A O   1 
ATOM   1384 C CB  . SER   A 1 162 ? 14.07769  -23.63896 -26.81062 1.000 21.57332  ? 169 SER   A CB  1 
ATOM   1385 O OG  . SER   A 1 162 ? 13.47176  -24.81258 -26.23368 1.000 23.29320  ? 169 SER   A OG  1 
ATOM   1386 N N   . PHE   A 1 163 ? 11.62462  -21.85133 -27.10813 1.000 18.43057  ? 170 PHE   A N   1 
ATOM   1387 C CA  . PHE   A 1 163 ? 10.19531  -21.81369 -27.33657 1.000 15.56342  ? 170 PHE   A CA  1 
ATOM   1388 C C   . PHE   A 1 163 ? 9.94736   -22.26235 -28.75312 1.000 17.22807  ? 170 PHE   A C   1 
ATOM   1389 O O   . PHE   A 1 163 ? 10.80795  -22.24761 -29.61859 1.000 18.79900  ? 170 PHE   A O   1 
ATOM   1390 C CB  . PHE   A 1 163 ? 9.54127   -20.41225 -27.07857 1.000 16.90679  ? 170 PHE   A CB  1 
ATOM   1391 C CG  . PHE   A 1 163 ? 10.04846  -19.31835 -28.01649 1.000 16.83134  ? 170 PHE   A CG  1 
ATOM   1392 C CD1 . PHE   A 1 163 ? 11.17741  -18.56177 -27.65137 1.000 17.36944  ? 170 PHE   A CD1 1 
ATOM   1393 C CD2 . PHE   A 1 163 ? 9.36611   -19.00763 -29.18076 1.000 16.81332  ? 170 PHE   A CD2 1 
ATOM   1394 C CE1 . PHE   A 1 163 ? 11.62325  -17.51337 -28.48224 1.000 18.09510  ? 170 PHE   A CE1 1 
ATOM   1395 C CE2 . PHE   A 1 163 ? 9.80161   -18.00635 -30.01463 1.000 18.59142  ? 170 PHE   A CE2 1 
ATOM   1396 C CZ  . PHE   A 1 163 ? 10.91733  -17.21088 -29.66338 1.000 18.62158  ? 170 PHE   A CZ  1 
ATOM   1397 N N   . THR   A 1 164 ? 8.69740   -22.68088 -29.01893 1.000 16.91960  ? 171 THR   A N   1 
ATOM   1398 C CA  . THR   A 1 164 ? 8.26644   -23.08767 -30.34802 1.000 17.51303  ? 171 THR   A CA  1 
ATOM   1399 C C   . THR   A 1 164 ? 7.14182   -22.21532 -30.85657 1.000 17.70690  ? 171 THR   A C   1 
ATOM   1400 O O   . THR   A 1 164 ? 6.35535   -21.68255 -30.06305 1.000 17.85270  ? 171 THR   A O   1 
ATOM   1401 C CB  . THR   A 1 164 ? 7.85143   -24.55159 -30.45402 1.000 19.60508  ? 171 THR   A CB  1 
ATOM   1402 O OG1 . THR   A 1 164 ? 6.73939   -24.82243 -29.61285 1.000 21.66034  ? 171 THR   A OG1 1 
ATOM   1403 C CG2 . THR   A 1 164 ? 8.98868   -25.51959 -30.06250 1.000 20.10002  ? 171 THR   A CG2 1 
ATOM   1404 N N   . VAL   A 1 165 ? 7.08198   -22.08160 -32.16867 1.000 17.47834  ? 172 VAL   A N   1 
ATOM   1405 C CA  . VAL   A 1 165 ? 5.94864   -21.42490 -32.81478 1.000 19.10819  ? 172 VAL   A CA  1 
ATOM   1406 C C   . VAL   A 1 165 ? 5.51733   -22.31582 -33.94662 1.000 20.54468  ? 172 VAL   A C   1 
ATOM   1407 O O   . VAL   A 1 165 ? 6.33612   -22.79314 -34.73521 1.000 20.59278  ? 172 VAL   A O   1 
ATOM   1408 C CB  . VAL   A 1 165 ? 6.31171   -20.01587 -33.34259 1.000 20.11491  ? 172 VAL   A CB  1 
ATOM   1409 C CG1 . VAL   A 1 165 ? 5.12521   -19.35892 -34.06780 1.000 20.78214  ? 172 VAL   A CG1 1 
ATOM   1410 C CG2 . VAL   A 1 165 ? 6.70537   -19.10878 -32.21136 1.000 19.81778  ? 172 VAL   A CG2 1 
ATOM   1411 N N   . ARG   A 1 166 ? 4.19980   -22.51953 -34.08119 1.000 20.67231  ? 173 ARG   A N   1 
ATOM   1412 C CA  . ARG   A 1 166 ? 3.59215   -23.27662 -35.16040 1.000 20.45492  ? 173 ARG   A CA  1 
ATOM   1413 C C   . ARG   A 1 166 ? 2.26220   -22.66928 -35.56474 1.000 21.75772  ? 173 ARG   A C   1 
ATOM   1414 O O   . ARG   A 1 166 ? 1.66572   -21.97933 -34.74020 1.000 21.16098  ? 173 ARG   A O   1 
ATOM   1415 C CB  . ARG   A 1 166 ? 3.42976   -24.75880 -34.81596 1.000 24.98084  ? 173 ARG   A CB  1 
ATOM   1416 C CG  . ARG   A 1 166 ? 2.38507   -25.04038 -33.74800 1.000 28.96634  ? 173 ARG   A CG  1 
ATOM   1417 C CD  . ARG   A 1 166 ? 2.52621   -26.43984 -33.11072 1.000 32.84825  ? 173 ARG   A CD  1 
ATOM   1418 N NE  . ARG   A 1 166 ? 3.72497   -26.41788 -32.25588 1.000 34.73847  ? 173 ARG   A NE  1 
ATOM   1419 C CZ  . ARG   A 1 166 ? 4.31133   -27.47188 -31.69196 1.000 42.39549  ? 173 ARG   A CZ  1 
ATOM   1420 N NH1 . ARG   A 1 166 ? 3.91254   -28.70930 -31.94293 1.000 42.85396  ? 173 ARG   A NH1 1 
ATOM   1421 N NH2 . ARG   A 1 166 ? 5.36025   -27.27897 -30.88864 1.000 40.94697  ? 173 ARG   A NH2 1 
ATOM   1422 N N   . THR   A 1 167 ? 1.84371   -22.88219 -36.81650 1.000 24.99866  ? 174 THR   A N   1 
ATOM   1423 C CA  . THR   A 1 167 ? 0.46523   -22.52657 -37.15617 1.000 23.12669  ? 174 THR   A CA  1 
ATOM   1424 C C   . THR   A 1 167 ? -0.45201  -23.40176 -36.34673 1.000 35.04397  ? 174 THR   A C   1 
ATOM   1425 O O   . THR   A 1 167 ? -0.16387  -24.57645 -36.12117 1.000 32.93249  ? 174 THR   A O   1 
ATOM   1426 C CB  . THR   A 1 167 ? 0.21368   -22.71871 -38.64850 1.000 29.78609  ? 174 THR   A CB  1 
ATOM   1427 O OG1 . THR   A 1 167 ? 1.13195   -21.87347 -39.35943 1.000 36.46860  ? 174 THR   A OG1 1 
ATOM   1428 C CG2 . THR   A 1 167 ? -1.25302  -22.35924 -39.01501 1.000 37.15453  ? 174 THR   A CG2 1 
ATOM   1429 N N   . ASP   A 1 168 ? -1.56743  -22.82949 -35.88697 1.000 25.82700  ? 175 ASP   A N   1 
ATOM   1430 C CA  . ASP   A 1 168 ? -2.47264  -23.57629 -35.04768 1.000 27.06105  ? 175 ASP   A CA  1 
ATOM   1431 C C   . ASP   A 1 168 ? -3.61934  -24.06071 -35.90749 1.000 38.05073  ? 175 ASP   A C   1 
ATOM   1432 O O   . ASP   A 1 168 ? -4.24522  -23.26664 -36.60078 1.000 39.95101  ? 175 ASP   A O   1 
ATOM   1433 C CB  . ASP   A 1 168 ? -2.99001  -22.67904 -33.93737 1.000 26.49586  ? 175 ASP   A CB  1 
ATOM   1434 C CG  . ASP   A 1 168 ? -3.82161  -23.44508 -32.93704 1.000 39.10719  ? 175 ASP   A CG  1 
ATOM   1435 O OD1 . ASP   A 1 168 ? -3.36616  -24.49755 -32.45750 1.000 47.50133  ? 175 ASP   A OD1 1 
ATOM   1436 O OD2 . ASP   A 1 168 ? -4.93416  -23.00229 -32.63115 1.000 34.55698  ? 175 ASP   A OD2 1 
ATOM   1437 N N   . THR   A 1 169 ? -3.83747  -25.35765 -35.89658 1.000 45.95836  ? 176 THR   A N   1 
ATOM   1438 C CA  . THR   A 1 169 ? -4.95330  -25.97902 -36.58095 1.000 69.26996  ? 176 THR   A CA  1 
ATOM   1439 C C   . THR   A 1 169 ? -6.10611  -26.28312 -35.64252 1.000 57.08959  ? 176 THR   A C   1 
ATOM   1440 O O   . THR   A 1 169 ? -7.11355  -26.84177 -36.08888 1.000 56.04616  ? 176 THR   A O   1 
ATOM   1441 C CB  . THR   A 1 169 ? -4.46974  -27.25876 -37.26054 1.000 69.74992  ? 176 THR   A CB  1 
ATOM   1442 O OG1 . THR   A 1 169 ? -3.56348  -27.95060 -36.37702 1.000 61.56068  ? 176 THR   A OG1 1 
ATOM   1443 C CG2 . THR   A 1 169 ? -3.77277  -26.89870 -38.55533 1.000 47.99644  ? 176 THR   A CG2 1 
ATOM   1444 N N   . GLY   A 1 170 ? -5.96929  -25.93959 -34.35850 1.000 55.78837  ? 177 GLY   A N   1 
ATOM   1445 C CA  . GLY   A 1 170 ? -7.02566  -26.05622 -33.37379 1.000 59.19525  ? 177 GLY   A CA  1 
ATOM   1446 C C   . GLY   A 1 170 ? -8.28065  -25.24771 -33.66312 1.000 46.19612  ? 177 GLY   A C   1 
ATOM   1447 O O   . GLY   A 1 170 ? -8.48018  -24.69936 -34.75326 1.000 42.03616  ? 177 GLY   A O   1 
ATOM   1448 N N   . GLU   A 1 171 ? -9.16011  -25.19774 -32.68867 1.000 34.96443  ? 178 GLU   A N   1 
ATOM   1449 C CA  . GLU   A 1 171 ? -10.40935 -24.46159 -32.85008 1.000 39.92499  ? 178 GLU   A CA  1 
ATOM   1450 C C   . GLU   A 1 171 ? -10.13965 -22.99893 -33.19681 1.000 34.25365  ? 178 GLU   A C   1 
ATOM   1451 O O   . GLU   A 1 171 ? -9.42705  -22.32674 -32.44756 1.000 30.47527  ? 178 GLU   A O   1 
ATOM   1452 C CB  . GLU   A 1 171 ? -11.13381 -24.58948 -31.51040 1.000 42.00583  ? 178 GLU   A CB  1 
ATOM   1453 C CG  . GLU   A 1 171 ? -12.60967 -24.36923 -31.55928 1.000 42.07061  ? 178 GLU   A CG  1 
ATOM   1454 C CD  . GLU   A 1 171 ? -13.33014 -25.35681 -32.46109 1.000 42.93523  ? 178 GLU   A CD  1 
ATOM   1455 O OE1 . GLU   A 1 171 ? -13.23468 -26.57295 -32.24363 1.000 42.27190  ? 178 GLU   A OE1 1 
ATOM   1456 O OE2 . GLU   A 1 171 ? -13.99032 -24.88741 -33.40825 1.000 46.23727  ? 178 GLU   A OE2 1 
ATOM   1457 N N   . PRO   A 1 172 ? -10.65992 -22.48061 -34.31357 1.000 34.26151  ? 179 PRO   A N   1 
ATOM   1458 C CA  . PRO   A 1 172 ? -10.40165 -21.07126 -34.65018 1.000 31.92621  ? 179 PRO   A CA  1 
ATOM   1459 C C   . PRO   A 1 172 ? -10.93145 -20.13491 -33.56642 1.000 34.55243  ? 179 PRO   A C   1 
ATOM   1460 O O   . PRO   A 1 172 ? -12.04401 -20.31841 -33.06023 1.000 39.69010  ? 179 PRO   A O   1 
ATOM   1461 C CB  . PRO   A 1 172 ? -11.18125 -20.87745 -35.94808 1.000 40.19800  ? 179 PRO   A CB  1 
ATOM   1462 C CG  . PRO   A 1 172 ? -11.15139 -22.23612 -36.61340 1.000 41.09828  ? 179 PRO   A CG  1 
ATOM   1463 C CD  . PRO   A 1 172 ? -11.11531 -23.26350 -35.48445 1.000 51.28672  ? 179 PRO   A CD  1 
ATOM   1464 N N   . MET   A 1 173 ? -10.16781 -19.07248 -33.26310 1.000 28.80725  ? 180 MET   A N   1 
ATOM   1465 C CA  . MET   A 1 173 ? -10.51007 -18.14479 -32.18684 1.000 30.15120  ? 180 MET   A CA  1 
ATOM   1466 C C   . MET   A 1 173 ? -11.17320 -16.83622 -32.62193 1.000 40.55164  ? 180 MET   A C   1 
ATOM   1467 O O   . MET   A 1 173 ? -11.65972 -16.07996 -31.76011 1.000 38.64891  ? 180 MET   A O   1 
ATOM   1468 C CB  . MET   A 1 173 ? -9.29846  -17.71857 -31.33941 1.000 31.95287  ? 180 MET   A CB  1 
ATOM   1469 C CG  . MET   A 1 173 ? -8.70231  -18.73709 -30.39305 1.000 47.08709  ? 180 MET   A CG  1 
ATOM   1470 S SD  . MET   A 1 173 ? -7.03019  -18.11669 -30.26582 1.000 37.77228  ? 180 MET   A SD  1 
ATOM   1471 C CE  . MET   A 1 173 ? -7.54660  -16.58693 -29.53053 1.000 30.85521  ? 180 MET   A CE  1 
ATOM   1472 N N   . GLY   A 1 174 ? -11.09289 -16.46503 -33.86203 1.000 30.13176  ? 181 GLY   A N   1 
ATOM   1473 C CA  . GLY   A 1 174 ? -11.75035 -15.21313 -34.22803 1.000 24.47753  ? 181 GLY   A CA  1 
ATOM   1474 C C   . GLY   A 1 174 ? -10.75173 -14.07763 -34.10740 1.000 25.23408  ? 181 GLY   A C   1 
ATOM   1475 O O   . GLY   A 1 174 ? -10.32497 -13.52186 -35.12273 1.000 24.58009  ? 181 GLY   A O   1 
ATOM   1476 N N   . ARG   A 1 175 ? -10.42044 -13.71034 -32.87333 1.000 20.00770  ? 182 ARG   A N   1 
ATOM   1477 C CA  . ARG   A 1 175 ? -9.38468  -12.72924 -32.58960 1.000 18.42460  ? 182 ARG   A CA  1 
ATOM   1478 C C   . ARG   A 1 175 ? -9.12703  -12.78960 -31.09306 1.000 19.43147  ? 182 ARG   A C   1 
ATOM   1479 O O   . ARG   A 1 175 ? -10.06729 -12.89477 -30.31350 1.000 21.03135  ? 182 ARG   A O   1 
ATOM   1480 C CB  . ARG   A 1 175 ? -9.90874  -11.31321 -32.93831 1.000 20.78382  ? 182 ARG   A CB  1 
ATOM   1481 C CG  . ARG   A 1 175 ? -8.81272  -10.20026 -32.77262 1.000 20.14649  ? 182 ARG   A CG  1 
ATOM   1482 C CD  . ARG   A 1 175 ? -9.41240  -8.77437  -32.65146 1.000 19.17926  ? 182 ARG   A CD  1 
ATOM   1483 N NE  . ARG   A 1 175 ? -10.33388 -8.68958  -31.51024 1.000 19.98461  ? 182 ARG   A NE  1 
ATOM   1484 C CZ  . ARG   A 1 175 ? -11.64162 -8.53189  -31.61431 1.000 19.51960  ? 182 ARG   A CZ  1 
ATOM   1485 N NH1 . ARG   A 1 175 ? -12.29702 -8.53349  -32.79221 1.000 20.52847  ? 182 ARG   A NH1 1 
ATOM   1486 N NH2 . ARG   A 1 175 ? -12.37941 -8.44496  -30.50872 1.000 20.11512  ? 182 ARG   A NH2 1 
ATOM   1487 N N   . GLY   A 1 176 ? -7.85233  -12.66087 -30.69633 1.000 19.24799  ? 183 GLY   A N   1 
ATOM   1488 C CA  . GLY   A 1 176 ? -7.49009  -12.52712 -29.29758 1.000 17.70602  ? 183 GLY   A CA  1 
ATOM   1489 C C   . GLY   A 1 176 ? -6.40464  -13.49843 -28.92318 1.000 17.12640  ? 183 GLY   A C   1 
ATOM   1490 O O   . GLY   A 1 176 ? -5.64207  -13.95863 -29.79516 1.000 18.37531  ? 183 GLY   A O   1 
ATOM   1491 N N   . THR   A 1 177 ? -6.32511  -13.78883 -27.64881 1.000 16.09411  ? 184 THR   A N   1 
ATOM   1492 C CA  . THR   A 1 177 ? -5.24682  -14.61394 -27.14228 1.000 14.71882  ? 184 THR   A CA  1 
ATOM   1493 C C   . THR   A 1 177 ? -5.74417  -15.54050 -26.07216 1.000 18.25075  ? 184 THR   A C   1 
ATOM   1494 O O   . THR   A 1 177 ? -6.59492  -15.14269 -25.23990 1.000 16.87135  ? 184 THR   A O   1 
ATOM   1495 C CB  . THR   A 1 177 ? -4.14510  -13.69484 -26.56446 1.000 16.98734  ? 184 THR   A CB  1 
ATOM   1496 O OG1 . THR   A 1 177 ? -3.56951  -12.91911 -27.58447 1.000 20.50014  ? 184 THR   A OG1 1 
ATOM   1497 C CG2 . THR   A 1 177 ? -2.99987  -14.47596 -25.81679 1.000 18.59094  ? 184 THR   A CG2 1 
ATOM   1498 N N   . LYS   A 1 178 ? -5.23224  -16.77903 -26.08653 1.000 16.36195  ? 185 LYS   A N   1 
ATOM   1499 C CA  . LYS   A 1 178 ? -5.53559  -17.76056 -25.04668 1.000 16.83726  ? 185 LYS   A CA  1 
ATOM   1500 C C   . LYS   A 1 178 ? -4.23876  -18.19608 -24.42149 1.000 17.15005  ? 185 LYS   A C   1 
ATOM   1501 O O   . LYS   A 1 178 ? -3.34743  -18.65512 -25.15575 1.000 18.06131  ? 185 LYS   A O   1 
ATOM   1502 C CB  . LYS   A 1 178 ? -6.19684  -18.96732 -25.74904 1.000 22.04414  ? 185 LYS   A CB  1 
ATOM   1503 C CG  . LYS   A 1 178 ? -6.56382  -20.08804 -24.94329 1.000 30.76978  ? 185 LYS   A CG  1 
ATOM   1504 C CD  . LYS   A 1 178 ? -7.34613  -21.18287 -25.75489 1.000 35.46988  ? 185 LYS   A CD  1 
ATOM   1505 C CE  . LYS   A 1 178 ? -7.83396  -20.71388 -27.10701 1.000 47.42843  ? 185 LYS   A CE  1 
ATOM   1506 N NZ  . LYS   A 1 178 ? -8.54335  -21.84916 -27.82924 1.000 51.47472  ? 185 LYS   A NZ  1 
ATOM   1507 N N   . VAL   A 1 179 ? -4.08317  -18.01770 -23.12177 1.000 15.74947  ? 186 VAL   A N   1 
ATOM   1508 C CA  . VAL   A 1 179 ? -2.86882  -18.45238 -22.43008 1.000 14.90389  ? 186 VAL   A CA  1 
ATOM   1509 C C   . VAL   A 1 179 ? -3.24151  -19.68016 -21.63711 1.000 17.68455  ? 186 VAL   A C   1 
ATOM   1510 O O   . VAL   A 1 179 ? -4.08909  -19.59900 -20.72224 1.000 17.50706  ? 186 VAL   A O   1 
ATOM   1511 C CB  . VAL   A 1 179 ? -2.36634  -17.36350 -21.47601 1.000 14.84830  ? 186 VAL   A CB  1 
ATOM   1512 C CG1 . VAL   A 1 179 ? -1.16518  -17.93317 -20.65594 1.000 16.54800  ? 186 VAL   A CG1 1 
ATOM   1513 C CG2 . VAL   A 1 179 ? -1.93940  -16.14672 -22.21699 1.000 16.81855  ? 186 VAL   A CG2 1 
ATOM   1514 N N   . ILE   A 1 180 ? -2.67402  -20.82077 -21.99580 1.000 15.84658  ? 187 ILE   A N   1 
ATOM   1515 C CA  . ILE   A 1 180 ? -2.98157  -22.11019 -21.35711 1.000 15.45520  ? 187 ILE   A CA  1 
ATOM   1516 C C   . ILE   A 1 180 ? -1.84667  -22.41273 -20.39516 1.000 15.09423  ? 187 ILE   A C   1 
ATOM   1517 O O   . ILE   A 1 180 ? -0.69360  -22.60246 -20.82905 1.000 17.53010  ? 187 ILE   A O   1 
ATOM   1518 C CB  . ILE   A 1 180 ? -3.11203  -23.21174 -22.40074 1.000 17.82097  ? 187 ILE   A CB  1 
ATOM   1519 C CG1 . ILE   A 1 180 ? -4.14590  -22.83808 -23.47464 1.000 16.86978  ? 187 ILE   A CG1 1 
ATOM   1520 C CG2 . ILE   A 1 180 ? -3.48936  -24.53198 -21.68917 1.000 20.23484  ? 187 ILE   A CG2 1 
ATOM   1521 C CD1 . ILE   A 1 180 ? -4.13307  -23.80072 -24.62320 1.000 23.49413  ? 187 ILE   A CD1 1 
ATOM   1522 N N   . LEU   A 1 181 ? -2.15560  -22.43501 -19.09649 1.000 15.95266  ? 188 LEU   A N   1 
ATOM   1523 C CA  . LEU   A 1 181 ? -1.12235  -22.71328 -18.09269 1.000 14.58274  ? 188 LEU   A CA  1 
ATOM   1524 C C   . LEU   A 1 181 ? -1.21880  -24.18650 -17.73063 1.000 17.96280  ? 188 LEU   A C   1 
ATOM   1525 O O   . LEU   A 1 181 ? -2.23058  -24.62358 -17.14631 1.000 18.66063  ? 188 LEU   A O   1 
ATOM   1526 C CB  . LEU   A 1 181 ? -1.38361  -21.84176 -16.85120 1.000 16.32148  ? 188 LEU   A CB  1 
ATOM   1527 C CG  . LEU   A 1 181 ? -1.45917  -20.34479 -17.11395 1.000 17.31968  ? 188 LEU   A CG  1 
ATOM   1528 C CD1 . LEU   A 1 181 ? -1.92496  -19.63804 -15.79089 1.000 20.17926  ? 188 LEU   A CD1 1 
ATOM   1529 C CD2 . LEU   A 1 181 ? -0.13377  -19.87594 -17.57566 1.000 20.04230  ? 188 LEU   A CD2 1 
ATOM   1530 N N   . HIS   A 1 182 ? -0.16586  -24.96021 -18.02647 1.000 17.16107  ? 189 HIS   A N   1 
ATOM   1531 C CA  . HIS   A 1 182 ? -0.09488  -26.38568 -17.64427 1.000 18.78636  ? 189 HIS   A CA  1 
ATOM   1532 C C   . HIS   A 1 182 ? 0.50501   -26.35567 -16.25044 1.000 18.59587  ? 189 HIS   A C   1 
ATOM   1533 O O   . HIS   A 1 182 ? 1.71252   -26.14685 -16.08976 1.000 20.65411  ? 189 HIS   A O   1 
ATOM   1534 C CB  . HIS   A 1 182 ? 0.75000   -27.17422 -18.66280 1.000 18.05976  ? 189 HIS   A CB  1 
ATOM   1535 C CG  . HIS   A 1 182 ? 0.25566   -27.02050 -20.08684 1.000 23.13883  ? 189 HIS   A CG  1 
ATOM   1536 N ND1 . HIS   A 1 182 ? -0.54931  -27.96634 -20.69322 1.000 29.66833  ? 189 HIS   A ND1 1 
ATOM   1537 C CD2 . HIS   A 1 182 ? 0.38390   -26.00091 -20.98201 1.000 23.73633  ? 189 HIS   A CD2 1 
ATOM   1538 C CE1 . HIS   A 1 182 ? -0.87020  -27.54993 -21.91224 1.000 26.27831  ? 189 HIS   A CE1 1 
ATOM   1539 N NE2 . HIS   A 1 182 ? -0.27868  -26.38491 -22.13326 1.000 27.13936  ? 189 HIS   A NE2 1 
ATOM   1540 N N   . LEU   A 1 183 ? -0.33492  -26.49180 -15.23299 1.000 18.18574  ? 190 LEU   A N   1 
ATOM   1541 C CA  . LEU   A 1 183 ? 0.13005   -26.17085 -13.87520 1.000 18.15098  ? 190 LEU   A CA  1 
ATOM   1542 C C   . LEU   A 1 183 ? 1.06314   -27.21315 -13.32133 1.000 22.44217  ? 190 LEU   A C   1 
ATOM   1543 O O   . LEU   A 1 183 ? 0.96312   -28.41129 -13.61136 1.000 23.40430  ? 190 LEU   A O   1 
ATOM   1544 C CB  . LEU   A 1 183 ? -1.06538  -26.07988 -12.93110 1.000 18.86512  ? 190 LEU   A CB  1 
ATOM   1545 C CG  . LEU   A 1 183 ? -1.99419  -24.90485 -13.28015 1.000 18.68369  ? 190 LEU   A CG  1 
ATOM   1546 C CD1 . LEU   A 1 183 ? -3.18026  -24.91118 -12.27538 1.000 21.93315  ? 190 LEU   A CD1 1 
ATOM   1547 C CD2 . LEU   A 1 183 ? -1.28571  -23.56020 -13.16842 1.000 20.73844  ? 190 LEU   A CD2 1 
ATOM   1548 N N   . LYS   A 1 184 ? 1.97788   -26.73914 -12.48794 1.000 21.79949  ? 191 LYS   A N   1 
ATOM   1549 C CA  . LYS   A 1 184 ? 2.81572   -27.63893 -11.71214 1.000 22.84637  ? 191 LYS   A CA  1 
ATOM   1550 C C   . LYS   A 1 184 ? 1.96299   -28.44903 -10.75014 1.000 24.44545  ? 191 LYS   A C   1 
ATOM   1551 O O   . LYS   A 1 184 ? 0.90277   -28.00538 -10.31493 1.000 23.87265  ? 191 LYS   A O   1 
ATOM   1552 C CB  . LYS   A 1 184 ? 3.84630   -26.82311 -10.90016 1.000 24.47094  ? 191 LYS   A CB  1 
ATOM   1553 C CG  . LYS   A 1 184 ? 4.88945   -26.08807 -11.76272 1.000 26.30931  ? 191 LYS   A CG  1 
ATOM   1554 C CD  . LYS   A 1 184 ? 5.85597   -25.18855 -10.92538 1.000 33.08759  ? 191 LYS   A CD  1 
ATOM   1555 C CE  . LYS   A 1 184 ? 6.17323   -23.77585 -11.43692 1.000 35.12961  ? 191 LYS   A CE  1 
ATOM   1556 N NZ  . LYS   A 1 184 ? 7.40573   -23.00673 -10.77544 1.000 37.61698  ? 191 LYS   A NZ  1 
ATOM   1557 N N   . GLU   A 1 185 ? 2.45368   -29.65281 -10.40935 1.000 27.24513  ? 192 GLU   A N   1 
ATOM   1558 C CA  . GLU   A 1 185 ? 1.66450   -30.58252 -9.60905  1.000 28.64069  ? 192 GLU   A CA  1 
ATOM   1559 C C   . GLU   A 1 185 ? 1.23488   -29.98952 -8.28514  1.000 29.46569  ? 192 GLU   A C   1 
ATOM   1560 O O   . GLU   A 1 185 ? 0.14740   -30.31244 -7.79242  1.000 32.91877  ? 192 GLU   A O   1 
ATOM   1561 C CB  . GLU   A 1 185 ? 2.47240   -31.85761 -9.36145  1.000 35.32908  ? 192 GLU   A CB  1 
ATOM   1562 C CG  . GLU   A 1 185 ? 1.65033   -33.11147 -9.23947  1.000 60.15152  ? 192 GLU   A CG  1 
ATOM   1563 C CD  . GLU   A 1 185 ? 2.50432   -34.36334 -9.39734  1.000 88.62796  ? 192 GLU   A CD  1 
ATOM   1564 O OE1 . GLU   A 1 185 ? 2.37390   -35.05258 -10.43970 1.000 79.91158  ? 192 GLU   A OE1 1 
ATOM   1565 O OE2 . GLU   A 1 185 ? 3.31308   -34.64468 -8.48590  1.000 88.01041  ? 192 GLU   A OE2 1 
ATOM   1566 N N   A ASP   A 1 186 ? 2.05651   -29.13201 -7.68754  0.500 26.44480  ? 193 ASP   A N   1 
ATOM   1567 N N   B ASP   A 1 186 ? 2.05651   -29.13201 -7.68754  0.500 26.44480  ? 193 ASP   A N   1 
ATOM   1568 C CA  A ASP   A 1 186 ? 1.75775   -28.57621 -6.37436  0.500 26.48196  ? 193 ASP   A CA  1 
ATOM   1569 C CA  B ASP   A 1 186 ? 1.75775   -28.57621 -6.37436  0.500 26.48196  ? 193 ASP   A CA  1 
ATOM   1570 C C   A ASP   A 1 186 ? 1.04017   -27.23579 -6.44108  0.500 25.44722  ? 193 ASP   A C   1 
ATOM   1571 C C   B ASP   A 1 186 ? 1.04017   -27.23579 -6.44108  0.500 25.44722  ? 193 ASP   A C   1 
ATOM   1572 O O   A ASP   A 1 186 ? 0.84512   -26.60175 -5.39645  0.500 25.79178  ? 193 ASP   A O   1 
ATOM   1573 O O   B ASP   A 1 186 ? 0.84512   -26.60175 -5.39645  0.500 25.79178  ? 193 ASP   A O   1 
ATOM   1574 C CB  A ASP   A 1 186 ? 3.01285   -28.47198 -5.50717  0.500 30.33884  ? 193 ASP   A CB  1 
ATOM   1575 C CB  B ASP   A 1 186 ? 3.01285   -28.47198 -5.50717  0.500 30.33884  ? 193 ASP   A CB  1 
ATOM   1576 C CG  A ASP   A 1 186 ? 4.06896   -27.56748 -6.09083  0.500 32.49146  ? 193 ASP   A CG  1 
ATOM   1577 C CG  B ASP   A 1 186 ? 4.06896   -27.56748 -6.09083  0.500 32.49146  ? 193 ASP   A CG  1 
ATOM   1578 O OD1 A ASP   A 1 186 ? 3.92368   -27.10524 -7.24131  0.500 38.21973  ? 193 ASP   A OD1 1 
ATOM   1579 O OD1 B ASP   A 1 186 ? 3.92368   -27.10524 -7.24131  0.500 38.21973  ? 193 ASP   A OD1 1 
ATOM   1580 O OD2 A ASP   A 1 186 ? 5.08048   -27.32710 -5.39615  0.500 43.05351  ? 193 ASP   A OD2 1 
ATOM   1581 O OD2 B ASP   A 1 186 ? 5.08048   -27.32710 -5.39615  0.500 43.05351  ? 193 ASP   A OD2 1 
ATOM   1582 N N   . GLN   A 1 187 ? 0.59218   -26.82460 -7.63308  1.000 22.59226  ? 194 GLN   A N   1 
ATOM   1583 C CA  . GLN   A 1 187 ? -0.07732  -25.54499 -7.81156  1.000 21.37009  ? 194 GLN   A CA  1 
ATOM   1584 C C   . GLN   A 1 187 ? -1.52795  -25.71827 -8.24360  1.000 19.36610  ? 194 GLN   A C   1 
ATOM   1585 O O   . GLN   A 1 187 ? -2.10586  -24.81588 -8.87362  1.000 21.47341  ? 194 GLN   A O   1 
ATOM   1586 C CB  . GLN   A 1 187 ? 0.68398   -24.67033 -8.80998  1.000 21.55446  ? 194 GLN   A CB  1 
ATOM   1587 C CG  . GLN   A 1 187 ? 2.13527   -24.44239 -8.33061  1.000 22.24447  ? 194 GLN   A CG  1 
ATOM   1588 C CD  . GLN   A 1 187 ? 2.23593   -23.78254 -6.96488  1.000 26.41081  ? 194 GLN   A CD  1 
ATOM   1589 O OE1 . GLN   A 1 187 ? 1.43116   -22.89920 -6.66203  1.000 26.59499  ? 194 GLN   A OE1 1 
ATOM   1590 N NE2 . GLN   A 1 187 ? 3.26498   -24.12260 -6.17368  1.000 28.21336  ? 194 GLN   A NE2 1 
ATOM   1591 N N   . THR   A 1 188 ? -2.15643  -26.81344 -7.86482  1.000 22.58377  ? 195 THR   A N   1 
ATOM   1592 C CA  . THR   A 1 188 ? -3.52302  -27.03411 -8.36670  1.000 23.72266  ? 195 THR   A CA  1 
ATOM   1593 C C   . THR   A 1 188 ? -4.57255  -26.23892 -7.60749  1.000 23.49295  ? 195 THR   A C   1 
ATOM   1594 O O   . THR   A 1 188 ? -5.75953  -26.29630 -7.97457  1.000 23.79948  ? 195 THR   A O   1 
ATOM   1595 C CB  . THR   A 1 188 ? -3.86793  -28.52737 -8.36241  1.000 26.70961  ? 195 THR   A CB  1 
ATOM   1596 O OG1 . THR   A 1 188 ? -3.80629  -29.04833 -7.02801  1.000 29.16394  ? 195 THR   A OG1 1 
ATOM   1597 C CG2 . THR   A 1 188 ? -2.95430  -29.30204 -9.31638  1.000 25.82342  ? 195 THR   A CG2 1 
ATOM   1598 N N   . GLU   A 1 189 ? -4.19305  -25.52501 -6.54054  1.000 22.62426  ? 196 GLU   A N   1 
ATOM   1599 C CA  . GLU   A 1 189 ? -5.15127  -24.61965 -5.90033  1.000 21.48960  ? 196 GLU   A CA  1 
ATOM   1600 C C   . GLU   A 1 189 ? -5.70974  -23.63228 -6.90524  1.000 21.78910  ? 196 GLU   A C   1 
ATOM   1601 O O   . GLU   A 1 189 ? -6.82244  -23.12570 -6.72298  1.000 22.39692  ? 196 GLU   A O   1 
ATOM   1602 C CB  . GLU   A 1 189 ? -4.50811  -23.87465 -4.72961  1.000 22.72349  ? 196 GLU   A CB  1 
ATOM   1603 C CG  . GLU   A 1 189 ? -3.43282  -22.85304 -5.14848  1.000 23.53734  ? 196 GLU   A CG  1 
ATOM   1604 C CD  . GLU   A 1 189 ? -2.67229  -22.37923 -3.94911  1.000 26.25173  ? 196 GLU   A CD  1 
ATOM   1605 O OE1 . GLU   A 1 189 ? -1.80008  -23.15510 -3.45790  1.000 29.10414  ? 196 GLU   A OE1 1 
ATOM   1606 O OE2 . GLU   A 1 189 ? -3.00790  -21.31525 -3.38099  1.000 26.44264  ? 196 GLU   A OE2 1 
ATOM   1607 N N   . TYR   A 1 190 ? -4.95297  -23.30664 -7.94550  1.000 20.69141  ? 197 TYR   A N   1 
ATOM   1608 C CA  . TYR   A 1 190 ? -5.41768  -22.29590 -8.90088  1.000 18.84672  ? 197 TYR   A CA  1 
ATOM   1609 C C   . TYR   A 1 190 ? -6.43359  -22.84005 -9.87060  1.000 20.73433  ? 197 TYR   A C   1 
ATOM   1610 O O   . TYR   A 1 190 ? -6.78106  -22.11322 -10.82106 1.000 21.87925  ? 197 TYR   A O   1 
ATOM   1611 C CB  . TYR   A 1 190 ? -4.21775  -21.64772 -9.63735  1.000 18.30945  ? 197 TYR   A CB  1 
ATOM   1612 C CG  . TYR   A 1 190 ? -3.29697  -21.02868 -8.60922  1.000 18.33042  ? 197 TYR   A CG  1 
ATOM   1613 C CD1 . TYR   A 1 190 ? -3.72053  -19.90817 -7.87112  1.000 19.80550  ? 197 TYR   A CD1 1 
ATOM   1614 C CD2 . TYR   A 1 190 ? -2.05052  -21.57681 -8.30166  1.000 20.46432  ? 197 TYR   A CD2 1 
ATOM   1615 C CE1 . TYR   A 1 190 ? -2.94194  -19.32321 -6.87905  1.000 20.45843  ? 197 TYR   A CE1 1 
ATOM   1616 C CE2 . TYR   A 1 190 ? -1.24381  -21.01724 -7.27112  1.000 20.44106  ? 197 TYR   A CE2 1 
ATOM   1617 C CZ  . TYR   A 1 190 ? -1.69527  -19.87024 -6.53843  1.000 19.23010  ? 197 TYR   A CZ  1 
ATOM   1618 O OH  . TYR   A 1 190 ? -0.93249  -19.29341 -5.53346  1.000 22.87641  ? 197 TYR   A OH  1 
ATOM   1619 N N   . LEU   A 1 191 ? -6.86425  -24.08969 -9.70482  1.000 19.95830  ? 198 LEU   A N   1 
ATOM   1620 C CA  . LEU   A 1 191 ? -8.02281  -24.59432 -10.44017 1.000 19.33934  ? 198 LEU   A CA  1 
ATOM   1621 C C   . LEU   A 1 191 ? -9.28474  -24.55113 -9.60839  1.000 23.25938  ? 198 LEU   A C   1 
ATOM   1622 O O   . LEU   A 1 191 ? -10.35357 -24.95856 -10.10163 1.000 24.32639  ? 198 LEU   A O   1 
ATOM   1623 C CB  . LEU   A 1 191 ? -7.76409  -26.04450 -10.86690 1.000 21.18808  ? 198 LEU   A CB  1 
ATOM   1624 C CG  . LEU   A 1 191 ? -6.54390  -26.17763 -11.73542 1.000 21.37108  ? 198 LEU   A CG  1 
ATOM   1625 C CD1 . LEU   A 1 191 ? -6.29872  -27.66958 -12.05995 1.000 28.15748  ? 198 LEU   A CD1 1 
ATOM   1626 C CD2 . LEU   A 1 191 ? -6.59211  -25.29838 -13.04167 1.000 25.36298  ? 198 LEU   A CD2 1 
ATOM   1627 N N   . GLU   A 1 192 ? -9.18229  -24.24144 -8.31710  1.000 20.61419  ? 199 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 192 ? -10.35303 -24.25357 -7.45091  1.000 20.96233  ? 199 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 192 ? -11.12810 -22.95115 -7.54800  1.000 25.05311  ? 199 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 192 ? -10.55207 -21.85921 -7.54618  1.000 22.96728  ? 199 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 192 ? -9.93024  -24.47288 -6.00931  1.000 25.76217  ? 199 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 192 ? -9.17159  -25.78653 -5.78871  1.000 30.76220  ? 199 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 192 ? -8.78779  -25.98759 -4.32449  1.000 73.30087  ? 199 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 192 ? -9.63621  -25.74951 -3.43711  1.000 90.92119  ? 199 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 192 ? -7.63637  -26.40218 -4.06335  1.000 77.16445  ? 199 GLU   A OE2 1 
ATOM   1636 N N   . GLU   A 1 193 ? -12.43809 -23.07388 -7.70922  1.000 25.02187  ? 200 GLU   A N   1 
ATOM   1637 C CA  . GLU   A 1 193 ? -13.26998 -21.90173 -7.93395  1.000 22.52800  ? 200 GLU   A CA  1 
ATOM   1638 C C   . GLU   A 1 193 ? -13.07249 -20.87309 -6.82768  1.000 21.44908  ? 200 GLU   A C   1 
ATOM   1639 O O   . GLU   A 1 193 ? -12.95200 -19.66688 -7.09495  1.000 21.93665  ? 200 GLU   A O   1 
ATOM   1640 C CB  . GLU   A 1 193 ? -14.74368 -22.32191 -8.00350  1.000 25.88183  ? 200 GLU   A CB  1 
ATOM   1641 C CG  . GLU   A 1 193 ? -15.58121 -21.20992 -8.51619  1.000 31.32077  ? 200 GLU   A CG  1 
ATOM   1642 C CD  . GLU   A 1 193 ? -17.10603 -21.47161 -8.45416  1.000 66.22797  ? 200 GLU   A CD  1 
ATOM   1643 O OE1 . GLU   A 1 193 ? -17.53963 -22.50938 -7.91265  1.000 47.32034  ? 200 GLU   A OE1 1 
ATOM   1644 O OE2 . GLU   A 1 193 ? -17.87338 -20.64543 -9.01088  1.000 48.10630  ? 200 GLU   A OE2 1 
ATOM   1645 N N   . ARG   A 1 194 ? -13.11310 -21.32610 -5.57138  1.000 23.71045  ? 201 ARG   A N   1 
ATOM   1646 C CA  . ARG   A 1 194 ? -13.05050 -20.34504 -4.48956  1.000 23.96883  ? 201 ARG   A CA  1 
ATOM   1647 C C   . ARG   A 1 194 ? -11.72696 -19.60234 -4.50237  1.000 22.59043  ? 201 ARG   A C   1 
ATOM   1648 O O   . ARG   A 1 194 ? -11.67703 -18.40689 -4.17999  1.000 22.96676  ? 201 ARG   A O   1 
ATOM   1649 C CB  . ARG   A 1 194 ? -13.34066 -20.98499 -3.11716  1.000 28.65265  ? 201 ARG   A CB  1 
ATOM   1650 C CG  . ARG   A 1 194 ? -12.21507 -21.68492 -2.53696  1.000 36.46316  ? 201 ARG   A CG  1 
ATOM   1651 C CD  . ARG   A 1 194 ? -12.79193 -22.62455 -1.48324  1.000 41.14413  ? 201 ARG   A CD  1 
ATOM   1652 N NE  . ARG   A 1 194 ? -11.79763 -23.51094 -0.92108  1.000 44.72958  ? 201 ARG   A NE  1 
ATOM   1653 C CZ  . ARG   A 1 194 ? -11.90506 -23.96997 0.31548   1.000 42.41547  ? 201 ARG   A CZ  1 
ATOM   1654 N NH1 . ARG   A 1 194 ? -12.97021 -23.68950 1.04807   1.000 44.03542  ? 201 ARG   A NH1 1 
ATOM   1655 N NH2 . ARG   A 1 194 ? -10.93481 -24.73226 0.81175   1.000 53.35543  ? 201 ARG   A NH2 1 
ATOM   1656 N N   . ARG   A 1 195 ? -10.64123 -20.27871 -4.90005  1.000 20.44312  ? 202 ARG   A N   1 
ATOM   1657 C CA  . ARG   A 1 195 ? -9.32780  -19.62967 -4.87925  1.000 21.06699  ? 202 ARG   A CA  1 
ATOM   1658 C C   . ARG   A 1 195 ? -9.22062  -18.62350 -6.02239  1.000 19.75333  ? 202 ARG   A C   1 
ATOM   1659 O O   . ARG   A 1 195 ? -8.71031  -17.51216 -5.84658  1.000 18.60001  ? 202 ARG   A O   1 
ATOM   1660 C CB  . ARG   A 1 195 ? -8.24098  -20.71444 -5.03774  1.000 20.92949  ? 202 ARG   A CB  1 
ATOM   1661 C CG  . ARG   A 1 195 ? -6.79460  -20.23141 -4.96637  1.000 21.33051  ? 202 ARG   A CG  1 
ATOM   1662 C CD  . ARG   A 1 195 ? -6.43043  -19.66752 -3.58040  1.000 24.83555  ? 202 ARG   A CD  1 
ATOM   1663 N NE  . ARG   A 1 195 ? -4.99071  -19.41075 -3.52254  1.000 22.85915  ? 202 ARG   A NE  1 
ATOM   1664 C CZ  . ARG   A 1 195 ? -4.43904  -18.21089 -3.35720  1.000 24.76627  ? 202 ARG   A CZ  1 
ATOM   1665 N NH1 . ARG   A 1 195 ? -5.17249  -17.13457 -3.13782  1.000 24.36566  ? 202 ARG   A NH1 1 
ATOM   1666 N NH2 . ARG   A 1 195 ? -3.11172  -18.10050 -3.40589  1.000 22.79987  ? 202 ARG   A NH2 1 
ATOM   1667 N N   . ILE   A 1 196 ? -9.72427  -18.98989 -7.20635  1.000 18.30751  ? 203 ILE   A N   1 
ATOM   1668 C CA  . ILE   A 1 196 ? -9.66482  -18.07926 -8.33857  1.000 18.33342  ? 203 ILE   A CA  1 
ATOM   1669 C C   . ILE   A 1 196 ? -10.50226 -16.86152 -8.04096  1.000 19.65921  ? 203 ILE   A C   1 
ATOM   1670 O O   . ILE   A 1 196 ? -10.06091 -15.73529 -8.29699  1.000 19.63456  ? 203 ILE   A O   1 
ATOM   1671 C CB  . ILE   A 1 196 ? -10.11456 -18.77966 -9.63574  1.000 18.76354  ? 203 ILE   A CB  1 
ATOM   1672 C CG1 . ILE   A 1 196 ? -9.17605  -19.95841 -10.00736 1.000 20.86439  ? 203 ILE   A CG1 1 
ATOM   1673 C CG2 . ILE   A 1 196 ? -10.11179 -17.76259 -10.76087 1.000 21.17831  ? 203 ILE   A CG2 1 
ATOM   1674 C CD1 . ILE   A 1 196 ? -9.85461  -20.96385 -11.00591 1.000 21.14679  ? 203 ILE   A CD1 1 
ATOM   1675 N N   . LYS   A 1 197 ? -11.73762 -17.06740 -7.49743  1.000 19.60059  ? 204 LYS   A N   1 
ATOM   1676 C CA  . LYS   A 1 197 ? -12.60291 -15.93895 -7.17244  1.000 19.85440  ? 204 LYS   A CA  1 
ATOM   1677 C C   . LYS   A 1 197 ? -11.91124 -15.00313 -6.20147  1.000 20.12289  ? 204 LYS   A C   1 
ATOM   1678 O O   . LYS   A 1 197 ? -11.98335 -13.77108 -6.35404  1.000 21.49676  ? 204 LYS   A O   1 
ATOM   1679 C CB  . LYS   A 1 197 ? -13.94080 -16.38473 -6.51943  1.000 20.90231  ? 204 LYS   A CB  1 
ATOM   1680 C CG  . LYS   A 1 197 ? -14.94646 -16.88379 -7.44952  1.000 28.34557  ? 204 LYS   A CG  1 
ATOM   1681 C CD  . LYS   A 1 197 ? -16.16722 -17.40830 -6.60654  1.000 28.84926  ? 204 LYS   A CD  1 
ATOM   1682 C CE  . LYS   A 1 197 ? -17.03148 -18.33114 -7.40945  1.000 47.90900  ? 204 LYS   A CE  1 
ATOM   1683 N NZ  . LYS   A 1 197 ? -18.35220 -18.60880 -6.75467  1.000 62.60306  ? 204 LYS   A NZ  1 
ATOM   1684 N N   . GLU   A 1 198 ? -11.21649 -15.56923 -5.19601  1.000 18.41318  ? 205 GLU   A N   1 
ATOM   1685 C CA  . GLU   A 1 198 ? -10.54060 -14.73536 -4.21054  1.000 19.27129  ? 205 GLU   A CA  1 
ATOM   1686 C C   . GLU   A 1 198 ? -9.44595  -13.89129 -4.84478  1.000 19.02060  ? 205 GLU   A C   1 
ATOM   1687 O O   . GLU   A 1 198 ? -9.31673  -12.70117 -4.53572  1.000 19.25608  ? 205 GLU   A O   1 
ATOM   1688 C CB  . GLU   A 1 198 ? -9.93550  -15.64755 -3.13179  1.000 19.33136  ? 205 GLU   A CB  1 
ATOM   1689 C CG  . GLU   A 1 198 ? -9.01448  -14.93110 -2.16414  1.000 21.08444  ? 205 GLU   A CG  1 
ATOM   1690 C CD  . GLU   A 1 198 ? -8.30086  -15.88442 -1.17247  1.000 23.51146  ? 205 GLU   A CD  1 
ATOM   1691 O OE1 . GLU   A 1 198 ? -7.72444  -16.85120 -1.73766  1.000 23.48364  ? 205 GLU   A OE1 1 
ATOM   1692 O OE2 . GLU   A 1 198 ? -8.32748  -15.63772 0.01894   1.000 23.48223  ? 205 GLU   A OE2 1 
ATOM   1693 N N   . ILE   A 1 199 ? -8.68681  -14.47623 -5.75559  1.000 17.76730  ? 206 ILE   A N   1 
ATOM   1694 C CA  . ILE   A 1 199 ? -7.59673  -13.72813 -6.39018  1.000 18.57464  ? 206 ILE   A CA  1 
ATOM   1695 C C   . ILE   A 1 199 ? -8.15557  -12.62940 -7.28277  1.000 18.03952  ? 206 ILE   A C   1 
ATOM   1696 O O   . ILE   A 1 199 ? -7.59797  -11.52367 -7.33427  1.000 20.05844  ? 206 ILE   A O   1 
ATOM   1697 C CB  . ILE   A 1 199 ? -6.67993  -14.69935 -7.16556  1.000 19.72447  ? 206 ILE   A CB  1 
ATOM   1698 C CG1 . ILE   A 1 199 ? -6.04937  -15.67539 -6.15598  1.000 20.16731  ? 206 ILE   A CG1 1 
ATOM   1699 C CG2 . ILE   A 1 199 ? -5.64001  -13.92234 -8.00707  1.000 21.39720  ? 206 ILE   A CG2 1 
ATOM   1700 C CD1 . ILE   A 1 199 ? -5.54142  -16.90748 -6.90904  1.000 21.59220  ? 206 ILE   A CD1 1 
ATOM   1701 N N   . VAL   A 1 200 ? -9.18270  -12.94732 -8.10220  1.000 17.82549  ? 207 VAL   A N   1 
ATOM   1702 C CA  . VAL   A 1 200 ? -9.74134  -11.92606 -8.96198  1.000 17.41879  ? 207 VAL   A CA  1 
ATOM   1703 C C   . VAL   A 1 200 ? -10.29650 -10.77171 -8.14402  1.000 18.94543  ? 207 VAL   A C   1 
ATOM   1704 O O   . VAL   A 1 200 ? -10.10421 -9.60184  -8.49299  1.000 21.82559  ? 207 VAL   A O   1 
ATOM   1705 C CB  . VAL   A 1 200 ? -10.82719 -12.55648 -9.83670  1.000 18.07459  ? 207 VAL   A CB  1 
ATOM   1706 C CG1 . VAL   A 1 200 ? -11.62978 -11.46574 -10.60030 1.000 19.84145  ? 207 VAL   A CG1 1 
ATOM   1707 C CG2 . VAL   A 1 200 ? -10.16510 -13.52501 -10.80705 1.000 20.46520  ? 207 VAL   A CG2 1 
ATOM   1708 N N   . LYS   A 1 201 ? -10.97923 -11.06724 -7.03764  1.000 17.99897  ? 208 LYS   A N   1 
ATOM   1709 C CA  . LYS   A 1 201 ? -11.54250 -9.99160  -6.21056  1.000 19.30009  ? 208 LYS   A CA  1 
ATOM   1710 C C   . LYS   A 1 201 ? -10.44633 -9.15066  -5.56585  1.000 20.03770  ? 208 LYS   A C   1 
ATOM   1711 O O   . LYS   A 1 201 ? -10.61091 -7.95404  -5.41680  1.000 26.69306  ? 208 LYS   A O   1 
ATOM   1712 C CB  . LYS   A 1 201 ? -12.46754 -10.60326 -5.14419  1.000 23.08643  ? 208 LYS   A CB  1 
ATOM   1713 C CG  . LYS   A 1 201 ? -13.09820 -9.58545  -4.17872  1.000 27.77058  ? 208 LYS   A CG  1 
ATOM   1714 C CD  . LYS   A 1 201 ? -13.85336 -10.28798 -3.09183  1.000 35.48776  ? 208 LYS   A CD  1 
ATOM   1715 C CE  . LYS   A 1 201 ? -14.50233 -9.28709  -2.13675  1.000 39.81716  ? 208 LYS   A CE  1 
ATOM   1716 N NZ  . LYS   A 1 201 ? -15.49768 -9.99496  -1.31901  1.000 64.42334  ? 208 LYS   A NZ  1 
ATOM   1717 N N   . LYS   A 1 202 ? -9.32313  -9.78686  -5.17796  1.000 22.43068  ? 209 LYS   A N   1 
ATOM   1718 C CA  . LYS   A 1 202 ? -8.29189  -9.05507  -4.44294  1.000 21.68576  ? 209 LYS   A CA  1 
ATOM   1719 C C   . LYS   A 1 202 ? -7.49126  -8.16374  -5.38778  1.000 21.43882  ? 209 LYS   A C   1 
ATOM   1720 O O   . LYS   A 1 202 ? -7.10598  -7.03064  -5.03008  1.000 23.73662  ? 209 LYS   A O   1 
ATOM   1721 C CB  . LYS   A 1 202 ? -7.31965  -10.08616 -3.82824  1.000 22.64024  ? 209 LYS   A CB  1 
ATOM   1722 C CG  . LYS   A 1 202 ? -5.99125  -9.49488  -3.27858  1.000 25.85991  ? 209 LYS   A CG  1 
ATOM   1723 C CD  . LYS   A 1 202 ? -5.49100  -10.46616 -2.31295  1.000 38.56817  ? 209 LYS   A CD  1 
ATOM   1724 C CE  . LYS   A 1 202 ? -4.10338  -10.08268 -1.83432  1.000 56.11154  ? 209 LYS   A CE  1 
ATOM   1725 N NZ  . LYS   A 1 202 ? -3.48378  -11.23979 -1.11813  1.000 45.30122  ? 209 LYS   A NZ  1 
ATOM   1726 N N   . HIS   A 1 203 ? -7.20478  -8.67224  -6.60157  1.000 21.27433  ? 210 HIS   A N   1 
ATOM   1727 C CA  . HIS   A 1 203 ? -6.21749  -7.98561  -7.44246  1.000 21.88071  ? 210 HIS   A CA  1 
ATOM   1728 C C   . HIS   A 1 203 ? -6.76448  -7.41835  -8.73842  1.000 21.52189  ? 210 HIS   A C   1 
ATOM   1729 O O   . HIS   A 1 203 ? -6.02433  -6.63457  -9.38458  1.000 24.53056  ? 210 HIS   A O   1 
ATOM   1730 C CB  . HIS   A 1 203 ? -5.11436  -8.97495  -7.86527  1.000 24.54748  ? 210 HIS   A CB  1 
ATOM   1731 C CG  . HIS   A 1 203 ? -4.27105  -9.47078  -6.73609  1.000 27.43988  ? 210 HIS   A CG  1 
ATOM   1732 N ND1 . HIS   A 1 203 ? -3.47751  -8.64898  -5.97418  1.000 31.42362  ? 210 HIS   A ND1 1 
ATOM   1733 C CD2 . HIS   A 1 203 ? -4.15314  -10.71406 -6.20825  1.000 28.23497  ? 210 HIS   A CD2 1 
ATOM   1734 C CE1 . HIS   A 1 203 ? -2.85897  -9.36837  -5.04743  1.000 28.93053  ? 210 HIS   A CE1 1 
ATOM   1735 N NE2 . HIS   A 1 203 ? -3.25017  -10.62562 -5.17244  1.000 32.31218  ? 210 HIS   A NE2 1 
ATOM   1736 N N   . SER   A 1 204 ? -7.97242  -7.79521  -9.17651  1.000 22.98164  ? 211 SER   A N   1 
ATOM   1737 C CA  . SER   A 1 204 ? -8.44994  -7.46301  -10.50892 1.000 21.13566  ? 211 SER   A CA  1 
ATOM   1738 C C   . SER   A 1 204 ? -9.82505  -6.76200  -10.43654 1.000 20.40801  ? 211 SER   A C   1 
ATOM   1739 O O   . SER   A 1 204 ? -10.61294 -6.80789  -11.40076 1.000 23.98572  ? 211 SER   A O   1 
ATOM   1740 C CB  . SER   A 1 204 ? -8.45219  -8.70788  -11.46036 1.000 20.52268  ? 211 SER   A CB  1 
ATOM   1741 O OG  . SER   A 1 204 ? -7.10286  -9.21711  -11.50404 1.000 25.67356  ? 211 SER   A OG  1 
ATOM   1742 N N   . GLN   A 1 205 ? -10.10312 -6.14577  -9.31872  1.000 25.28217  ? 212 GLN   A N   1 
ATOM   1743 C CA  . GLN   A 1 205 ? -11.45524 -5.64729  -9.12469  1.000 33.56824  ? 212 GLN   A CA  1 
ATOM   1744 C C   . GLN   A 1 205 ? -11.77791 -4.45159  -10.02327 1.000 34.66935  ? 212 GLN   A C   1 
ATOM   1745 O O   . GLN   A 1 205 ? -12.96589 -4.17518  -10.24118 1.000 38.29326  ? 212 GLN   A O   1 
ATOM   1746 C CB  . GLN   A 1 205 ? -11.68480 -5.32462  -7.65367  1.000 43.18981  ? 212 GLN   A CB  1 
ATOM   1747 C CG  . GLN   A 1 205 ? -10.86169 -4.20783  -7.18865  1.000 37.49996  ? 212 GLN   A CG  1 
ATOM   1748 C CD  . GLN   A 1 205 ? -9.53254  -4.58015  -6.47833  1.000 74.42349  ? 212 GLN   A CD  1 
ATOM   1749 O OE1 . GLN   A 1 205 ? -8.62814  -5.23782  -7.03362  1.000 37.27559  ? 212 GLN   A OE1 1 
ATOM   1750 N NE2 . GLN   A 1 205 ? -9.40593  -4.09895  -5.23841  1.000 52.06221  ? 212 GLN   A NE2 1 
ATOM   1751 N N   . PHE   A 1 206 ? -10.76796 -3.72478  -10.53428 1.000 26.78486  ? 213 PHE   A N   1 
ATOM   1752 C CA  . PHE   A 1 206 ? -10.99732 -2.54969  -11.37934 1.000 28.07582  ? 213 PHE   A CA  1 
ATOM   1753 C C   . PHE   A 1 206 ? -10.66334 -2.81104  -12.86181 1.000 29.52227  ? 213 PHE   A C   1 
ATOM   1754 O O   . PHE   A 1 206 ? -10.34875 -1.88302  -13.62112 1.000 37.59118  ? 213 PHE   A O   1 
ATOM   1755 C CB  . PHE   A 1 206 ? -10.21931 -1.36191  -10.86945 1.000 32.32554  ? 213 PHE   A CB  1 
ATOM   1756 C CG  . PHE   A 1 206 ? -10.65452 -0.94472  -9.49498  1.000 34.52848  ? 213 PHE   A CG  1 
ATOM   1757 C CD1 . PHE   A 1 206 ? -11.93258 -0.48508  -9.26708  1.000 41.89891  ? 213 PHE   A CD1 1 
ATOM   1758 C CD2 . PHE   A 1 206 ? -9.78971  -1.08724  -8.42627  1.000 34.80152  ? 213 PHE   A CD2 1 
ATOM   1759 C CE1 . PHE   A 1 206 ? -12.34004 -0.12156  -7.98944  1.000 45.74061  ? 213 PHE   A CE1 1 
ATOM   1760 C CE2 . PHE   A 1 206 ? -10.18831 -0.72358  -7.13915  1.000 38.47133  ? 213 PHE   A CE2 1 
ATOM   1761 C CZ  . PHE   A 1 206 ? -11.46622 -0.24226  -6.92640  1.000 41.02297  ? 213 PHE   A CZ  1 
ATOM   1762 N N   . ILE   A 1 207 ? -10.66175 -4.04177  -13.29897 1.000 21.01314  ? 214 ILE   A N   1 
ATOM   1763 C CA  . ILE   A 1 207 ? -10.48470 -4.32000  -14.70591 1.000 18.89344  ? 214 ILE   A CA  1 
ATOM   1764 C C   . ILE   A 1 207 ? -11.79817 -4.06397  -15.44542 1.000 24.08635  ? 214 ILE   A C   1 
ATOM   1765 O O   . ILE   A 1 207 ? -12.86175 -4.55362  -15.02276 1.000 24.51125  ? 214 ILE   A O   1 
ATOM   1766 C CB  . ILE   A 1 207 ? -10.04909 -5.78510  -14.89216 1.000 19.27965  ? 214 ILE   A CB  1 
ATOM   1767 C CG1 . ILE   A 1 207 ? -8.64861  -5.96875  -14.31069 1.000 20.51335  ? 214 ILE   A CG1 1 
ATOM   1768 C CG2 . ILE   A 1 207 ? -10.02599 -6.19887  -16.38973 1.000 19.17803  ? 214 ILE   A CG2 1 
ATOM   1769 C CD1 . ILE   A 1 207 ? -7.51584  -5.20431  -15.01105 1.000 23.75622  ? 214 ILE   A CD1 1 
ATOM   1770 N N   . GLY   A 1 208 ? -11.74729 -3.28968  -16.53429 1.000 20.13984  ? 215 GLY   A N   1 
ATOM   1771 C CA  . GLY   A 1 208 ? -12.95052 -2.78014  -17.14150 1.000 19.64288  ? 215 GLY   A CA  1 
ATOM   1772 C C   . GLY   A 1 208 ? -13.53879 -3.64651  -18.23137 1.000 20.52178  ? 215 GLY   A C   1 
ATOM   1773 O O   . GLY   A 1 208 ? -14.09419 -3.12810  -19.19626 1.000 22.04603  ? 215 GLY   A O   1 
ATOM   1774 N N   . TYR   A 1 209 ? -13.46015 -4.95873  -18.07043 1.000 19.13850  ? 216 TYR   A N   1 
ATOM   1775 C CA  . TYR   A 1 209 ? -14.04317 -5.90005  -19.02611 1.000 19.58313  ? 216 TYR   A CA  1 
ATOM   1776 C C   . TYR   A 1 209 ? -14.61878 -6.99081  -18.14675 1.000 20.80521  ? 216 TYR   A C   1 
ATOM   1777 O O   . TYR   A 1 209 ? -14.07789 -7.26653  -17.07902 1.000 22.02738  ? 216 TYR   A O   1 
ATOM   1778 C CB  . TYR   A 1 209 ? -12.93008 -6.50456  -19.91251 1.000 18.47009  ? 216 TYR   A CB  1 
ATOM   1779 C CG  . TYR   A 1 209 ? -12.33869 -5.44125  -20.78827 1.000 18.60578  ? 216 TYR   A CG  1 
ATOM   1780 C CD1 . TYR   A 1 209 ? -12.99264 -5.00422  -21.96652 1.000 18.34926  ? 216 TYR   A CD1 1 
ATOM   1781 C CD2 . TYR   A 1 209 ? -11.10846 -4.80555  -20.46589 1.000 17.27436  ? 216 TYR   A CD2 1 
ATOM   1782 C CE1 . TYR   A 1 209 ? -12.48590 -4.00327  -22.75266 1.000 19.46488  ? 216 TYR   A CE1 1 
ATOM   1783 C CE2 . TYR   A 1 209 ? -10.60585 -3.79329  -21.24204 1.000 19.17280  ? 216 TYR   A CE2 1 
ATOM   1784 C CZ  . TYR   A 1 209 ? -11.26651 -3.39558  -22.41722 1.000 17.89973  ? 216 TYR   A CZ  1 
ATOM   1785 O OH  . TYR   A 1 209 ? -10.81266 -2.35747  -23.14649 1.000 20.83232  ? 216 TYR   A OH  1 
ATOM   1786 N N   . PRO   A 1 210 ? -15.64927 -7.68751  -18.61373 1.000 20.25133  ? 217 PRO   A N   1 
ATOM   1787 C CA  . PRO   A 1 210 ? -16.21606 -8.80183  -17.85399 1.000 18.71160  ? 217 PRO   A CA  1 
ATOM   1788 C C   . PRO   A 1 210 ? -15.26092 -9.97724  -17.78311 1.000 20.48592  ? 217 PRO   A C   1 
ATOM   1789 O O   . PRO   A 1 210 ? -14.68024 -10.36869 -18.79959 1.000 21.08074  ? 217 PRO   A O   1 
ATOM   1790 C CB  . PRO   A 1 210 ? -17.50028 -9.15696  -18.62913 1.000 20.50130  ? 217 PRO   A CB  1 
ATOM   1791 C CG  . PRO   A 1 210 ? -17.41572 -8.47252  -19.90827 1.000 26.02201  ? 217 PRO   A CG  1 
ATOM   1792 C CD  . PRO   A 1 210 ? -16.36925 -7.34870  -19.84949 1.000 21.75677  ? 217 PRO   A CD  1 
ATOM   1793 N N   . ILE   A 1 211 ? -15.05964 -10.47192 -16.57067 1.000 18.27080  ? 218 ILE   A N   1 
ATOM   1794 C CA  . ILE   A 1 211 ? -14.21268 -11.62392 -16.27581 1.000 16.35457  ? 218 ILE   A CA  1 
ATOM   1795 C C   . ILE   A 1 211 ? -15.15575 -12.72553 -15.83735 1.000 17.29509  ? 218 ILE   A C   1 
ATOM   1796 O O   . ILE   A 1 211 ? -15.75532 -12.64565 -14.76634 1.000 22.20045  ? 218 ILE   A O   1 
ATOM   1797 C CB  . ILE   A 1 211 ? -13.19375 -11.33818 -15.17876 1.000 18.39220  ? 218 ILE   A CB  1 
ATOM   1798 C CG1 . ILE   A 1 211 ? -12.27196 -10.17249 -15.60486 1.000 18.26287  ? 218 ILE   A CG1 1 
ATOM   1799 C CG2 . ILE   A 1 211 ? -12.35609 -12.58624 -14.90315 1.000 19.70786  ? 218 ILE   A CG2 1 
ATOM   1800 C CD1 . ILE   A 1 211 ? -11.40972 -9.63611  -14.44192 1.000 19.80646  ? 218 ILE   A CD1 1 
ATOM   1801 N N   . THR   A 1 212 ? -15.26745 -13.75579 -16.66813 1.000 17.81758  ? 219 THR   A N   1 
ATOM   1802 C CA  . THR   A 1 212 ? -16.19116 -14.86719 -16.38436 1.000 17.23721  ? 219 THR   A CA  1 
ATOM   1803 C C   . THR   A 1 212 ? -15.37124 -16.06656 -15.96009 1.000 15.46923  ? 219 THR   A C   1 
ATOM   1804 O O   . THR   A 1 212 ? -14.55298 -16.53487 -16.75824 1.000 16.77640  ? 219 THR   A O   1 
ATOM   1805 C CB  . THR   A 1 212 ? -16.99689 -15.20670 -17.62364 1.000 17.71630  ? 219 THR   A CB  1 
ATOM   1806 O OG1 . THR   A 1 212 ? -17.77630 -14.05581 -18.00199 1.000 20.29377  ? 219 THR   A OG1 1 
ATOM   1807 C CG2 . THR   A 1 212 ? -18.00528 -16.38239 -17.24631 1.000 18.40609  ? 219 THR   A CG2 1 
ATOM   1808 N N   . LEU   A 1 213 ? -15.57999 -16.54806 -14.76512 1.000 17.68337  ? 220 LEU   A N   1 
ATOM   1809 C CA  . LEU   A 1 213 ? -14.95869 -17.77071 -14.27593 1.000 16.68652  ? 220 LEU   A CA  1 
ATOM   1810 C C   . LEU   A 1 213 ? -15.89001 -18.93797 -14.60370 1.000 18.14147  ? 220 LEU   A C   1 
ATOM   1811 O O   . LEU   A 1 213 ? -17.00818 -19.02461 -14.06866 1.000 19.63753  ? 220 LEU   A O   1 
ATOM   1812 C CB  . LEU   A 1 213 ? -14.74004 -17.64343 -12.77507 1.000 20.18753  ? 220 LEU   A CB  1 
ATOM   1813 C CG  . LEU   A 1 213 ? -14.17647 -18.89282 -12.13121 1.000 19.65479  ? 220 LEU   A CG  1 
ATOM   1814 C CD1 . LEU   A 1 213 ? -12.92178 -19.39249 -12.78869 1.000 20.46687  ? 220 LEU   A CD1 1 
ATOM   1815 C CD2 . LEU   A 1 213 ? -13.92125 -18.56518 -10.61589 1.000 21.80592  ? 220 LEU   A CD2 1 
ATOM   1816 N N   . PHE   A 1 214 ? -15.41560 -19.77570 -15.51490 1.000 17.57668  ? 221 PHE   A N   1 
ATOM   1817 C CA  . PHE   A 1 214 ? -16.15684 -20.95450 -15.90510 1.000 16.71067  ? 221 PHE   A CA  1 
ATOM   1818 C C   . PHE   A 1 214 ? -16.14009 -21.97078 -14.79828 1.000 18.72559  ? 221 PHE   A C   1 
ATOM   1819 O O   . PHE   A 1 214 ? -15.17923 -22.04940 -14.03025 1.000 21.84916  ? 221 PHE   A O   1 
ATOM   1820 C CB  . PHE   A 1 214 ? -15.55914 -21.59633 -17.14973 1.000 17.04894  ? 221 PHE   A CB  1 
ATOM   1821 C CG  . PHE   A 1 214 ? -15.85062 -20.87934 -18.45752 1.000 17.54162  ? 221 PHE   A CG  1 
ATOM   1822 C CD1 . PHE   A 1 214 ? -15.95233 -19.49130 -18.55017 1.000 17.58297  ? 221 PHE   A CD1 1 
ATOM   1823 C CD2 . PHE   A 1 214 ? -15.95546 -21.65211 -19.61939 1.000 17.85253  ? 221 PHE   A CD2 1 
ATOM   1824 C CE1 . PHE   A 1 214 ? -16.14864 -18.84820 -19.79328 1.000 17.66848  ? 221 PHE   A CE1 1 
ATOM   1825 C CE2 . PHE   A 1 214 ? -16.15321 -21.04678 -20.87676 1.000 18.17037  ? 221 PHE   A CE2 1 
ATOM   1826 C CZ  . PHE   A 1 214 ? -16.26245 -19.63839 -20.97600 1.000 18.19423  ? 221 PHE   A CZ  1 
ATOM   1827 N N   . VAL   A 1 215 ? -17.22626 -22.72086 -14.66219 1.000 19.36855  ? 222 VAL   A N   1 
ATOM   1828 C CA  . VAL   A 1 215 ? -17.25061 -23.82548 -13.71623 1.000 22.30113  ? 222 VAL   A CA  1 
ATOM   1829 C C   . VAL   A 1 215 ? -17.14835 -25.15874 -14.42159 1.000 24.68569  ? 222 VAL   A C   1 
ATOM   1830 O O   . VAL   A 1 215 ? -17.21713 -25.24120 -15.66036 1.000 24.63418  ? 222 VAL   A O   1 
ATOM   1831 C CB  . VAL   A 1 215 ? -18.37327 -23.80464 -12.70444 1.000 31.83690  ? 222 VAL   A CB  1 
ATOM   1832 C CG1 . VAL   A 1 215 ? -18.25876 -22.55204 -11.79419 1.000 34.39411  ? 222 VAL   A CG1 1 
ATOM   1833 C CG2 . VAL   A 1 215 ? -19.58857 -23.77040 -13.50688 1.000 26.27343  ? 222 VAL   A CG2 1 
ATOM   1834 N N   . GLU   A 1 216 ? -16.77109 -26.15873 -13.64765 1.000 24.85244  ? 223 GLU   A N   1 
ATOM   1835 C CA  . GLU   A 1 216 ? -16.57479 -27.49899 -14.18596 1.000 27.73134  ? 223 GLU   A CA  1 
ATOM   1836 C C   . GLU   A 1 216 ? -17.67692 -28.44986 -13.76865 1.000 33.02805  ? 223 GLU   A C   1 
ATOM   1837 O O   . GLU   A 1 216 ? -18.17952 -28.37286 -12.63945 1.000 33.51214  ? 223 GLU   A O   1 
ATOM   1838 C CB  . GLU   A 1 216 ? -15.21336 -28.07394 -13.79060 1.000 29.88546  ? 223 GLU   A CB  1 
ATOM   1839 C CG  . GLU   A 1 216 ? -14.10094 -27.13773 -14.08528 1.000 29.67506  ? 223 GLU   A CG  1 
ATOM   1840 C CD  . GLU   A 1 216 ? -12.76960 -27.66401 -13.59860 1.000 36.98431  ? 223 GLU   A CD  1 
ATOM   1841 O OE1 . GLU   A 1 216 ? -12.34542 -28.74368 -14.08249 1.000 31.64852  ? 223 GLU   A OE1 1 
ATOM   1842 O OE2 . GLU   A 1 216 ? -12.19506 -27.00333 -12.69597 1.000 32.23868  ? 223 GLU   A OE2 1 
ATOM   1843 N N   . LYS   A 1 217 ? -17.99226 -29.40133 -14.67313 1.000 34.01075  ? 224 LYS   A N   1 
ATOM   1844 C CA  . LYS   A 1 217 ? -18.87641 -30.52291 -14.38749 1.000 36.38660  ? 224 LYS   A CA  1 
ATOM   1845 C C   . LYS   A 1 217 ? -18.55235 -31.26160 -13.07995 1.000 52.94704  ? 224 LYS   A C   1 
ATOM   1846 O O   . LYS   A 1 217 ? -17.39387 -31.57261 -12.82703 1.000 52.69277  ? 224 LYS   A O   1 
ATOM   1847 C CB  . LYS   A 1 217 ? -18.85610 -31.54562 -15.54610 1.000 44.94870  ? 224 LYS   A CB  1 
ATOM   1848 C CG  . LYS   A 1 217 ? -19.69340 -32.78419 -15.29806 1.000 68.28813  ? 224 LYS   A CG  1 
ATOM   1849 C CD  . LYS   A 1 217 ? -19.96504 -33.54093 -16.59700 1.000 76.78020  ? 224 LYS   A CD  1 
ATOM   1850 C CE  . LYS   A 1 217 ? -18.88453 -34.59032 -16.88393 1.000 87.42043  ? 224 LYS   A CE  1 
ATOM   1851 N NZ  . LYS   A 1 217 ? -17.69253 -34.00711 -17.59426 1.000 73.84017  ? 224 LYS   A NZ  1 
HETATM 1852 C C4  B A1AXC B 2 .   ? 13.03947  -12.53965 -7.52911  0.368 42.16160  ? 301 A1AXC A C4  1 
HETATM 1853 C C6  B A1AXC B 2 .   ? 11.76551  -11.09773 -3.80506  0.368 41.36354  ? 301 A1AXC A C6  1 
HETATM 1854 C C11 B A1AXC B 2 .   ? 12.58382  -12.21207 -3.69577  0.368 43.32702  ? 301 A1AXC A C11 1 
HETATM 1855 C C8  B A1AXC B 2 .   ? 12.23576  -10.53995 -1.51101  0.368 28.23046  ? 301 A1AXC A C8  1 
HETATM 1856 C C9  B A1AXC B 2 .   ? 13.03841  -11.65607 -1.40702  0.368 40.55776  ? 301 A1AXC A C9  1 
HETATM 1857 C C10 B A1AXC B 2 .   ? 13.21897  -12.48433 -2.49537  0.368 41.57775  ? 301 A1AXC A C10 1 
HETATM 1858 C C3  B A1AXC B 2 .   ? 11.04851  -13.66739 -7.11645  0.368 26.37370  ? 301 A1AXC A C3  1 
HETATM 1859 C C2  B A1AXC B 2 .   ? 10.34148  -12.39721 -6.71945  0.368 35.93248  ? 301 A1AXC A C2  1 
HETATM 1860 C C1  B A1AXC B 2 .   ? 11.06790  -10.72814 -5.07762  0.368 27.37978  ? 301 A1AXC A C1  1 
HETATM 1861 C C5  B A1AXC B 2 .   ? 12.45838  -11.21272 -7.09386  0.368 29.68873  ? 301 A1AXC A C5  1 
HETATM 1862 C C7  B A1AXC B 2 .   ? 11.59635  -10.26267 -2.70782  0.368 42.10478  ? 301 A1AXC A C7  1 
HETATM 1863 N N1  B A1AXC B 2 .   ? 11.30903  -11.42588 -6.20847  0.368 38.23363  ? 301 A1AXC A N1  1 
HETATM 1864 O O1  B A1AXC B 2 .   ? 10.33323  -9.73977  -5.07764  0.368 35.88506  ? 301 A1AXC A O1  1 
HETATM 1865 O O2  B A1AXC B 2 .   ? 12.05252  -13.40117 -8.08911  0.368 40.25025  ? 301 A1AXC A O2  1 
HETATM 1866 O O   . HOH   C 3 .   ? 9.76585   -11.04249 -34.77514 1.000 37.89005  ? 401 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? -6.43244  -17.03561 -41.17413 1.000 43.23510  ? 402 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? 15.06745  -0.70314  -12.10068 1.000 44.25188  ? 403 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? 9.11185   -3.20863  -20.35905 1.000 28.93918  ? 404 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? 8.45227   -0.29593  -17.16544 1.000 34.21926  ? 405 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? 5.13422   -9.85590  -2.43356  1.000 44.52761  ? 406 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? 16.15163  1.31884   -15.47891 1.000 51.83584  ? 407 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? 12.32207  -8.83108  -29.75862 1.000 35.40172  ? 408 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? 5.87202   -25.57713 -7.29820  1.000 40.90463  ? 409 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? 15.24734  -0.59100  -19.35774 1.000 40.55113  ? 410 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? 11.88858  -21.77985 -40.56327 1.000 47.48735  ? 411 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? -13.01297 -7.41081  -11.92979 1.000 33.73799  ? 412 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? -16.13294 -25.71111 -17.90593 1.000 26.57358  ? 413 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? 3.45852   -24.29763 -38.57005 1.000 36.90772  ? 414 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? 0.30995   -14.88073 -1.39472  1.000 38.70526  ? 415 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? 13.90596  -11.11150 -29.44252 1.000 38.03589  ? 416 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? -2.73524  -3.16446  -35.30444 1.000 42.56420  ? 417 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? 20.02078  -10.37710 -26.16082 1.000 38.64651  ? 418 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? 0.21271   -22.27185 -2.10964  1.000 41.80629  ? 419 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? 22.32548  -7.56153  -21.75774 1.000 50.08550  ? 420 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? 2.20642   -15.63290 -40.97580 1.000 40.99439  ? 421 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? -3.61154  -13.15591 -42.56065 1.000 45.90990  ? 422 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? 18.44847  -10.94006 -17.36326 1.000 46.02830  ? 423 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? -0.07106  -5.63007  -38.46988 1.000 43.70575  ? 424 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? -1.46289  -29.11098 -5.93165  1.000 31.70864  ? 425 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? -17.88966 -5.10872  -36.98563 1.000 54.39868  ? 426 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? -13.66846 -15.15715 -30.40741 1.000 42.98894  ? 427 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? 7.83025   -23.12502 -14.25755 1.000 27.67257  ? 428 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? -4.42762  0.62555   -22.19801 1.000 30.68785  ? 429 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? 3.13698   -6.15219  -11.06996 1.000 23.28973  ? 430 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? 6.71992   -26.56590 -27.66344 1.000 30.76807  ? 431 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? 5.27474   -29.07816 -8.30764  1.000 45.20015  ? 432 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? 1.84574   -3.91433  -17.01569 1.000 42.63200  ? 433 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? 6.11615   -21.62464 -37.21631 1.000 33.04556  ? 434 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? 5.96220   -21.20531 -0.08733  1.000 28.29409  ? 435 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? -12.25257 -25.83771 -3.64985  1.000 43.45687  ? 436 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? -5.77489  -2.16334  -19.44634 1.000 22.59524  ? 437 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? -13.22934 -0.94972  -20.39919 1.000 30.24990  ? 438 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? -8.01833  -22.77195 -30.26432 1.000 41.85857  ? 439 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? -15.78604 0.09427   -30.23793 1.000 38.58942  ? 440 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? -0.96509  -11.43452 -3.08239  1.000 38.26017  ? 441 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? 16.62933  0.73381   -17.60305 1.000 44.47549  ? 442 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? -3.75276  -14.23729 -0.81142  1.000 43.93239  ? 443 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? 7.73358   -18.83984 -6.49466  1.000 24.14517  ? 444 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? 18.22041  -7.22767  -20.25880 1.000 32.86603  ? 445 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? 0.90078   -29.74256 -16.04034 1.000 37.23045  ? 446 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? 2.95361   -4.02968  -8.94061  1.000 51.56916  ? 447 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? 2.93687   -20.45267 -2.85626  1.000 36.29676  ? 448 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 7.58155   1.29209   -14.55074 1.000 36.44936  ? 449 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? -2.97334  -6.06619  -6.35655  1.000 38.89598  ? 450 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? 9.85657   -14.66567 -25.14510 1.000 19.75173  ? 451 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? 9.20445   -26.39701 -17.08448 1.000 29.05217  ? 452 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? -5.52841  -7.75987  -13.08202 1.000 20.91624  ? 453 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? 10.16201  -23.86431 -9.12017  1.000 44.30008  ? 454 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? 1.42819   -7.82379  -16.52079 1.000 21.42177  ? 455 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? -11.85764 -0.45048  -15.29088 1.000 32.49881  ? 456 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? -1.54093  -30.31759 -19.90987 1.000 56.40607  ? 457 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? -8.07580  1.75220   -36.44343 1.000 36.65425  ? 458 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? 7.76801   -27.74839 -24.06101 1.000 33.24863  ? 459 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 0.40368   -1.56732  -19.86646 1.000 37.14200  ? 460 HOH   A O   1 
HETATM 1926 O O   . HOH   C 3 .   ? -7.41416  -5.69434  -2.72557  1.000 42.25116  ? 461 HOH   A O   1 
HETATM 1927 O O   . HOH   C 3 .   ? -20.45444 -14.14605 -18.13253 1.000 36.52538  ? 462 HOH   A O   1 
HETATM 1928 O O   . HOH   C 3 .   ? -12.89602 -25.04447 -10.95945 1.000 30.37449  ? 463 HOH   A O   1 
HETATM 1929 O O   . HOH   C 3 .   ? -14.49064 -7.20700  -14.42527 1.000 35.49794  ? 464 HOH   A O   1 
HETATM 1930 O O   . HOH   C 3 .   ? -5.29006  -10.44142 -27.32922 1.000 18.37229  ? 465 HOH   A O   1 
HETATM 1931 O O   . HOH   C 3 .   ? 0.46790   -4.99047  -16.13632 1.000 36.45719  ? 466 HOH   A O   1 
HETATM 1932 O O   . HOH   C 3 .   ? -16.95148 -5.49246  -22.76684 1.000 28.15241  ? 467 HOH   A O   1 
HETATM 1933 O O   . HOH   C 3 .   ? -0.24852  -5.46610  -18.31881 1.000 28.73355  ? 468 HOH   A O   1 
HETATM 1934 O O   . HOH   C 3 .   ? -10.65554 -14.63254 0.94066   1.000 25.25269  ? 469 HOH   A O   1 
HETATM 1935 O O   . HOH   C 3 .   ? -6.68165  -27.98393 -21.31892 1.000 42.04574  ? 470 HOH   A O   1 
HETATM 1936 O O   . HOH   C 3 .   ? -16.21059 -12.83161 -19.83933 1.000 20.05859  ? 471 HOH   A O   1 
HETATM 1937 O O   . HOH   C 3 .   ? -2.08852  -13.68945 -35.56784 1.000 20.70844  ? 472 HOH   A O   1 
HETATM 1938 O O   . HOH   C 3 .   ? -2.38623  -10.67952 -26.61862 1.000 30.56595  ? 473 HOH   A O   1 
HETATM 1939 O O   . HOH   C 3 .   ? 9.71947   -17.38281 -7.67704  1.000 21.50261  ? 474 HOH   A O   1 
HETATM 1940 O O   . HOH   C 3 .   ? -4.19716  -4.93058  -8.32179  1.000 44.03245  ? 475 HOH   A O   1 
HETATM 1941 O O   . HOH   C 3 .   ? -5.62433  -28.52124 -5.08138  1.000 51.04572  ? 476 HOH   A O   1 
HETATM 1942 O O   . HOH   C 3 .   ? -6.26505  -11.38019 -10.07975 1.000 24.51575  ? 477 HOH   A O   1 
HETATM 1943 O O   . HOH   C 3 .   ? 12.99100  -13.78007 -29.53627 1.000 26.15059  ? 478 HOH   A O   1 
HETATM 1944 O O   . HOH   C 3 .   ? -12.37125 -27.91989 -30.04032 1.000 36.53492  ? 479 HOH   A O   1 
HETATM 1945 O O   . HOH   C 3 .   ? 13.60627  -14.13326 -26.72476 1.000 20.71790  ? 480 HOH   A O   1 
HETATM 1946 O O   . HOH   C 3 .   ? 11.51302  -28.26669 -30.40223 1.000 34.54625  ? 481 HOH   A O   1 
HETATM 1947 O O   . HOH   C 3 .   ? -3.31652  -12.12101 -8.97830  1.000 32.15555  ? 482 HOH   A O   1 
HETATM 1948 O O   . HOH   C 3 .   ? -20.22050 -27.92032 -10.88111 1.000 56.98272  ? 483 HOH   A O   1 
HETATM 1949 O O   . HOH   C 3 .   ? 11.21382  -7.99865  -27.41218 1.000 24.26993  ? 484 HOH   A O   1 
HETATM 1950 O O   . HOH   C 3 .   ? -1.01160  -25.88528 -32.38468 1.000 46.27914  ? 485 HOH   A O   1 
HETATM 1951 O O   . HOH   C 3 .   ? -17.92902 -3.95020  -28.99935 1.000 45.31996  ? 486 HOH   A O   1 
HETATM 1952 O O   . HOH   C 3 .   ? -19.69278 -19.53542 -14.27123 1.000 21.77988  ? 487 HOH   A O   1 
HETATM 1953 O O   . HOH   C 3 .   ? 1.51584   -26.20253 -2.76815  1.000 44.60766  ? 488 HOH   A O   1 
HETATM 1954 O O   . HOH   C 3 .   ? -1.12782  -7.40661  -23.57075 1.000 24.72357  ? 489 HOH   A O   1 
HETATM 1955 O O   . HOH   C 3 .   ? -8.06315  -24.90453 -19.10499 1.000 20.05115  ? 490 HOH   A O   1 
HETATM 1956 O O   . HOH   C 3 .   ? -6.35029  -7.73347  -34.27760 1.000 20.88790  ? 491 HOH   A O   1 
HETATM 1957 O O   . HOH   C 3 .   ? 3.89813   -29.73876 -25.79155 1.000 49.23904  ? 492 HOH   A O   1 
HETATM 1958 O O   . HOH   C 3 .   ? 11.72222  -27.30305 -34.62154 1.000 24.36539  ? 493 HOH   A O   1 
HETATM 1959 O O   . HOH   C 3 .   ? 0.90337   -21.12669 -4.61313  1.000 26.32944  ? 494 HOH   A O   1 
HETATM 1960 O O   . HOH   C 3 .   ? -3.93633  -3.48536  -15.28664 1.000 33.76864  ? 495 HOH   A O   1 
HETATM 1961 O O   . HOH   C 3 .   ? -20.593   -20.942   -9.369    1.000 44.03212  ? 496 HOH   A O   1 
HETATM 1962 O O   . HOH   C 3 .   ? -6.44690  -4.94806  -39.04027 1.000 44.24946  ? 497 HOH   A O   1 
HETATM 1963 O O   . HOH   C 3 .   ? -3.50984  -10.80530 -24.02467 1.000 25.33421  ? 498 HOH   A O   1 
HETATM 1964 O O   . HOH   C 3 .   ? 3.73907   -7.60411  -36.53221 1.000 37.02273  ? 499 HOH   A O   1 
HETATM 1965 O O   . HOH   C 3 .   ? 6.71232   -29.61737 -20.11985 1.000 36.54809  ? 500 HOH   A O   1 
HETATM 1966 O O   . HOH   C 3 .   ? -8.54699  -11.80998 -36.37116 1.000 26.29397  ? 501 HOH   A O   1 
HETATM 1967 O O   . HOH   C 3 .   ? -13.67025 -17.13839 -2.73951  1.000 27.84286  ? 502 HOH   A O   1 
HETATM 1968 O O   . HOH   C 3 .   ? -10.91459 -14.21353 -37.73678 1.000 35.92402  ? 503 HOH   A O   1 
HETATM 1969 O O   . HOH   C 3 .   ? -9.33744  -2.31593  -17.53504 1.000 21.33136  ? 504 HOH   A O   1 
HETATM 1970 O O   . HOH   C 3 .   ? -6.66702  -3.53621  -7.99735  1.000 49.50313  ? 505 HOH   A O   1 
HETATM 1971 O O   . HOH   C 3 .   ? 8.89791   -15.42424 -27.72046 1.000 17.77018  ? 506 HOH   A O   1 
HETATM 1972 O O   . HOH   C 3 .   ? -8.01722  -3.99092  -10.74777 1.000 27.78779  ? 507 HOH   A O   1 
HETATM 1973 O O   . HOH   C 3 .   ? 14.03248  -15.79931 -1.95474  1.000 31.66290  ? 508 HOH   A O   1 
HETATM 1974 O O   . HOH   C 3 .   ? -7.55690  -24.39064 -23.10561 1.000 28.70573  ? 509 HOH   A O   1 
HETATM 1975 O O   . HOH   C 3 .   ? -14.19533 -22.13097 -33.65345 1.000 43.73348  ? 510 HOH   A O   1 
HETATM 1976 O O   . HOH   C 3 .   ? -8.37800  4.71502   -33.53807 1.000 30.95794  ? 511 HOH   A O   1 
HETATM 1977 O O   . HOH   C 3 .   ? 10.81921  -25.49135 -26.70357 1.000 31.40261  ? 512 HOH   A O   1 
HETATM 1978 O O   . HOH   C 3 .   ? -5.418    -11.388   0.875     1.000 45.93959  ? 513 HOH   A O   1 
HETATM 1979 O O   . HOH   C 3 .   ? 0.74103   -26.95457 -37.24615 1.000 46.60751  ? 514 HOH   A O   1 
HETATM 1980 O O   . HOH   C 3 .   ? -14.52559 -22.80821 -11.43234 1.000 29.71482  ? 515 HOH   A O   1 
HETATM 1981 O O   . HOH   C 3 .   ? -15.12041 -11.16423 -29.80963 1.000 27.04645  ? 516 HOH   A O   1 
HETATM 1982 O O   . HOH   C 3 .   ? 7.99197   -23.25584 -7.20201  1.000 33.78710  ? 517 HOH   A O   1 
HETATM 1983 O O   . HOH   C 3 .   ? -7.60671  -28.38455 -8.06988  1.000 30.82107  ? 518 HOH   A O   1 
HETATM 1984 O O   . HOH   C 3 .   ? -1.52948  -6.32842  -26.02749 1.000 21.96708  ? 519 HOH   A O   1 
HETATM 1985 O O   . HOH   C 3 .   ? 10.42777  -21.17260 -6.94976  1.000 35.19948  ? 520 HOH   A O   1 
HETATM 1986 O O   . HOH   C 3 .   ? 18.06860  -19.20916 -24.46579 1.000 33.09266  ? 521 HOH   A O   1 
HETATM 1987 O O   . HOH   C 3 .   ? -5.72090  -31.18899 -11.63167 1.000 33.36176  ? 522 HOH   A O   1 
HETATM 1988 O O   . HOH   C 3 .   ? 8.67982   -16.06556 -39.43885 1.000 37.94016  ? 523 HOH   A O   1 
HETATM 1989 O O   . HOH   C 3 .   ? -16.00621 -3.13288  -21.24151 1.000 28.66662  ? 524 HOH   A O   1 
HETATM 1990 O O   . HOH   C 3 .   ? -10.34548 -0.76612  -19.97631 1.000 28.07313  ? 525 HOH   A O   1 
HETATM 1991 O O   . HOH   C 3 .   ? 8.50603   -20.40646 -9.20605  1.000 28.54706  ? 526 HOH   A O   1 
HETATM 1992 O O   . HOH   C 3 .   ? -15.76537 6.21860   -32.22010 1.000 43.50547  ? 527 HOH   A O   1 
HETATM 1993 O O   . HOH   C 3 .   ? 10.72594  -25.27678 -23.68856 1.000 24.19488  ? 528 HOH   A O   1 
HETATM 1994 O O   . HOH   C 3 .   ? -14.15900 -12.76614 -7.82192  1.000 24.77640  ? 529 HOH   A O   1 
HETATM 1995 O O   . HOH   C 3 .   ? -6.26980  -5.11283  -35.49189 1.000 24.67775  ? 530 HOH   A O   1 
HETATM 1996 O O   . HOH   C 3 .   ? -4.18136  -4.20570  -37.08143 1.000 38.14687  ? 531 HOH   A O   1 
HETATM 1997 O O   . HOH   C 3 .   ? 15.52171  -20.18766 -18.59562 1.000 23.86800  ? 532 HOH   A O   1 
HETATM 1998 O O   . HOH   C 3 .   ? -8.70026  -17.97224 -36.50599 1.000 42.85039  ? 533 HOH   A O   1 
HETATM 1999 O O   . HOH   C 3 .   ? 14.41537  -15.96149 -30.67508 1.000 30.81147  ? 534 HOH   A O   1 
HETATM 2000 O O   . HOH   C 3 .   ? -7.25762  1.18608   -19.40103 1.000 31.76683  ? 535 HOH   A O   1 
HETATM 2001 O O   . HOH   C 3 .   ? -1.75653  -25.69545 -4.77849  1.000 24.47265  ? 536 HOH   A O   1 
HETATM 2002 O O   . HOH   C 3 .   ? -6.09354  -14.09974 0.80450   1.000 26.70114  ? 537 HOH   A O   1 
HETATM 2003 O O   . HOH   C 3 .   ? -18.83797 -10.94125 -23.71856 1.000 29.97600  ? 538 HOH   A O   1 
HETATM 2004 O O   . HOH   C 3 .   ? 4.20816   -24.08133 -30.64735 1.000 20.53068  ? 539 HOH   A O   1 
HETATM 2005 O O   . HOH   C 3 .   ? -2.15875  -0.53663  -18.57703 1.000 34.52524  ? 540 HOH   A O   1 
HETATM 2006 O O   . HOH   C 3 .   ? 1.11618   -6.16105  -34.08495 1.000 44.75563  ? 541 HOH   A O   1 
HETATM 2007 O O   . HOH   C 3 .   ? 3.04613   -5.45846  -34.04843 1.000 49.42038  ? 542 HOH   A O   1 
HETATM 2008 O O   . HOH   C 3 .   ? 7.44765   -4.63541  -22.13808 1.000 32.34660  ? 543 HOH   A O   1 
HETATM 2009 O O   . HOH   C 3 .   ? 4.93787   -30.48979 -11.49679 1.000 42.59783  ? 544 HOH   A O   1 
HETATM 2010 O O   . HOH   C 3 .   ? -15.19212 -12.23055 -12.01583 1.000 31.21921  ? 545 HOH   A O   1 
HETATM 2011 O O   . HOH   C 3 .   ? -11.83742 -7.60919  -38.24649 1.000 37.58080  ? 546 HOH   A O   1 
HETATM 2012 O O   . HOH   C 3 .   ? -1.17489  -29.86022 -17.52636 1.000 43.77083  ? 547 HOH   A O   1 
HETATM 2013 O O   . HOH   C 3 .   ? -5.78728  -7.20936  -42.37019 1.000 52.63106  ? 548 HOH   A O   1 
HETATM 2014 O O   . HOH   C 3 .   ? -8.86523  -10.42025 -40.29675 1.000 38.89388  ? 549 HOH   A O   1 
HETATM 2015 O O   . HOH   C 3 .   ? -0.22049  -7.05860  -30.91035 1.000 32.65445  ? 550 HOH   A O   1 
HETATM 2016 O O   . HOH   C 3 .   ? -12.29928 -31.94107 -18.81194 1.000 51.56687  ? 551 HOH   A O   1 
HETATM 2017 O O   . HOH   C 3 .   ? 3.55714   -30.01349 -19.20145 1.000 48.02005  ? 552 HOH   A O   1 
HETATM 2018 O O   . HOH   C 3 .   ? 13.32608  -6.68128  -26.12644 1.000 23.17691  ? 553 HOH   A O   1 
HETATM 2019 O O   . HOH   C 3 .   ? -17.09059 -28.69622 -17.28091 1.000 36.32873  ? 554 HOH   A O   1 
HETATM 2020 O O   . HOH   C 3 .   ? -5.88081  -24.33857 -30.29952 1.000 47.02743  ? 555 HOH   A O   1 
HETATM 2021 O O   . HOH   C 3 .   ? 21.969    -13.540   -19.348   1.000 49.08984  ? 556 HOH   A O   1 
HETATM 2022 O O   . HOH   C 3 .   ? -17.67182 -18.84887 -11.29883 1.000 32.27017  ? 557 HOH   A O   1 
HETATM 2023 O O   . HOH   C 3 .   ? 4.59816   -19.46949 -40.51349 1.000 32.11763  ? 558 HOH   A O   1 
HETATM 2024 O O   . HOH   C 3 .   ? -4.56999  0.46536   -30.34295 1.000 29.44413  ? 559 HOH   A O   1 
HETATM 2025 O O   . HOH   C 3 .   ? 3.55972   -6.73562  -17.84338 1.000 22.19300  ? 560 HOH   A O   1 
HETATM 2026 O O   . HOH   C 3 .   ? 18.45242  -16.04176 -13.38752 1.000 33.30140  ? 561 HOH   A O   1 
HETATM 2027 O O   . HOH   C 3 .   ? -7.33010  -13.22107 -40.92819 1.000 49.27146  ? 562 HOH   A O   1 
HETATM 2028 O O   . HOH   C 3 .   ? -10.38191 -11.60808 -2.11579  1.000 23.51915  ? 563 HOH   A O   1 
HETATM 2029 O O   . HOH   C 3 .   ? 0.55059   -5.23168  -14.05036 1.000 36.80362  ? 564 HOH   A O   1 
HETATM 2030 O O   . HOH   C 3 .   ? 6.82203   -25.05587 -5.38792  1.000 50.06348  ? 565 HOH   A O   1 
HETATM 2031 O O   . HOH   C 3 .   ? 13.81373  -20.44872 -20.65964 1.000 20.75484  ? 566 HOH   A O   1 
HETATM 2032 O O   . HOH   C 3 .   ? 17.18440  -24.64873 -25.24207 1.000 32.77370  ? 567 HOH   A O   1 
HETATM 2033 O O   . HOH   C 3 .   ? -5.04179  -14.30543 -22.62195 1.000 17.63919  ? 568 HOH   A O   1 
HETATM 2034 O O   . HOH   C 3 .   ? -7.58949  7.40598   -33.40254 1.000 37.50328  ? 569 HOH   A O   1 
HETATM 2035 O O   . HOH   C 3 .   ? 20.07565  -5.21906  -14.62681 1.000 48.82597  ? 570 HOH   A O   1 
HETATM 2036 O O   . HOH   C 3 .   ? -13.48465 -26.53406 -18.05659 1.000 27.79648  ? 571 HOH   A O   1 
HETATM 2037 O O   . HOH   C 3 .   ? -10.60865 -6.34810  -3.02682  1.000 46.46015  ? 572 HOH   A O   1 
HETATM 2038 O O   . HOH   C 3 .   ? -10.10834 -15.05358 -28.33915 1.000 24.44023  ? 573 HOH   A O   1 
HETATM 2039 O O   . HOH   C 3 .   ? 4.04615   -9.19303  -20.26760 1.000 21.73649  ? 574 HOH   A O   1 
HETATM 2040 O O   . HOH   C 3 .   ? -5.11107  -5.39374  -11.82328 1.000 36.83111  ? 575 HOH   A O   1 
HETATM 2041 O O   . HOH   C 3 .   ? 19.80488  -16.39253 -27.62825 1.000 41.46509  ? 576 HOH   A O   1 
HETATM 2042 O O   . HOH   C 3 .   ? 3.86058   -11.68555 -38.46729 1.000 27.38068  ? 577 HOH   A O   1 
HETATM 2043 O O   . HOH   C 3 .   ? 20.92064  -13.99352 -26.52494 1.000 33.17024  ? 578 HOH   A O   1 
HETATM 2044 O O   . HOH   C 3 .   ? 1.99670   -6.11610  -25.83964 1.000 35.49344  ? 579 HOH   A O   1 
HETATM 2045 O O   . HOH   C 3 .   ? -3.11482  -1.09811  -23.94709 1.000 26.20739  ? 580 HOH   A O   1 
HETATM 2046 O O   . HOH   C 3 .   ? 13.72517  -3.93208  -25.32889 1.000 22.76537  ? 581 HOH   A O   1 
HETATM 2047 O O   . HOH   C 3 .   ? -3.30738  -21.18153 -0.48922  1.000 32.73526  ? 582 HOH   A O   1 
HETATM 2048 O O   . HOH   C 3 .   ? -7.03981  -22.45623 -36.53205 1.000 46.21012  ? 583 HOH   A O   1 
HETATM 2049 O O   . HOH   C 3 .   ? -2.34617  -24.82660 -1.13716  1.000 47.30509  ? 584 HOH   A O   1 
HETATM 2050 O O   . HOH   C 3 .   ? -14.46668 -3.64897  -12.76179 1.000 40.89464  ? 585 HOH   A O   1 
HETATM 2051 O O   . HOH   C 3 .   ? -2.46314  -15.67286 -0.29944  1.000 41.58228  ? 586 HOH   A O   1 
HETATM 2052 O O   . HOH   C 3 .   ? 15.67964  -18.32695 -3.53186  1.000 30.47810  ? 587 HOH   A O   1 
HETATM 2053 O O   . HOH   C 3 .   ? -2.95417  -31.51123 -20.21931 1.000 49.26071  ? 588 HOH   A O   1 
HETATM 2054 O O   . HOH   C 3 .   ? -13.68945 -18.55595 -24.40984 1.000 22.29886  ? 589 HOH   A O   1 
HETATM 2055 O O   . HOH   C 3 .   ? 12.53005  -27.35235 -19.64608 1.000 42.48355  ? 590 HOH   A O   1 
HETATM 2056 O O   . HOH   C 3 .   ? -3.41100  -13.23472 -20.59966 1.000 21.90475  ? 591 HOH   A O   1 
HETATM 2057 O O   . HOH   C 3 .   ? -5.66519  -18.85963 -39.15963 1.000 37.98588  ? 592 HOH   A O   1 
HETATM 2058 O O   . HOH   C 3 .   ? -16.45924 -9.19563  -14.30076 1.000 34.68506  ? 593 HOH   A O   1 
HETATM 2059 O O   . HOH   C 3 .   ? -17.64671 -15.22153 -13.10368 1.000 26.59917  ? 594 HOH   A O   1 
HETATM 2060 O O   . HOH   C 3 .   ? 8.74739   -20.50366 -4.29164  1.000 26.01385  ? 595 HOH   A O   1 
HETATM 2061 O O   . HOH   C 3 .   ? 1.28920   -8.55391  -26.84743 1.000 32.40202  ? 596 HOH   A O   1 
HETATM 2062 O O   . HOH   C 3 .   ? -14.03505 -24.07687 -4.88414  1.000 30.56862  ? 597 HOH   A O   1 
HETATM 2063 O O   . HOH   C 3 .   ? 20.38616  -5.82786  -21.06474 1.000 41.09426  ? 598 HOH   A O   1 
HETATM 2064 O O   . HOH   C 3 .   ? -16.04822 -25.54690 -10.81268 1.000 35.27113  ? 599 HOH   A O   1 
HETATM 2065 O O   . HOH   C 3 .   ? -7.89259  1.44756   -39.33373 1.000 48.97603  ? 600 HOH   A O   1 
HETATM 2066 O O   . HOH   C 3 .   ? -18.10154 -6.11550  -25.42655 1.000 34.82446  ? 601 HOH   A O   1 
HETATM 2067 O O   . HOH   C 3 .   ? 0.51069   -5.61892  -21.90490 1.000 35.56088  ? 602 HOH   A O   1 
HETATM 2068 O O   . HOH   C 3 .   ? -0.05808  -30.33986 -23.90967 1.000 52.92986  ? 603 HOH   A O   1 
HETATM 2069 O O   . HOH   C 3 .   ? 8.57354   -19.89633 -41.45013 1.000 47.33631  ? 604 HOH   A O   1 
HETATM 2070 O O   . HOH   C 3 .   ? 2.20190   -29.90106 -34.10227 1.000 55.46655  ? 605 HOH   A O   1 
HETATM 2071 O O   . HOH   C 3 .   ? 11.39615  -1.70628  -20.17587 1.000 32.66508  ? 606 HOH   A O   1 
HETATM 2072 O O   . HOH   C 3 .   ? 1.38509   -2.92580  -24.23374 1.000 36.24462  ? 607 HOH   A O   1 
HETATM 2073 O O   . HOH   C 3 .   ? 9.78925   -5.89976  -1.37948  1.000 49.94131  ? 608 HOH   A O   1 
HETATM 2074 O O   . HOH   C 3 .   ? -1.44749  -8.59840  -27.70035 1.000 27.07466  ? 609 HOH   A O   1 
HETATM 2075 O O   . HOH   C 3 .   ? -13.53106 -31.05674 -12.53875 1.000 47.68545  ? 610 HOH   A O   1 
HETATM 2076 O O   . HOH   C 3 .   ? -1.01688  -27.34435 -34.85243 1.000 57.64426  ? 611 HOH   A O   1 
HETATM 2077 O O   . HOH   C 3 .   ? -13.45815 -25.93251 -7.87262  1.000 29.62787  ? 612 HOH   A O   1 
HETATM 2078 O O   . HOH   C 3 .   ? -16.82624 -20.31875 -4.75560  1.000 47.10987  ? 613 HOH   A O   1 
HETATM 2079 O O   . HOH   C 3 .   ? -14.05199 -16.28416 -26.02878 1.000 25.86422  ? 614 HOH   A O   1 
HETATM 2080 O O   . HOH   C 3 .   ? 16.66096  -27.48775 -22.46248 1.000 42.45721  ? 615 HOH   A O   1 
HETATM 2081 O O   . HOH   C 3 .   ? -12.76447 -27.04680 -35.21366 1.000 49.53437  ? 616 HOH   A O   1 
HETATM 2082 O O   . HOH   C 3 .   ? -0.04955  -16.75068 -3.42055  1.000 26.99242  ? 617 HOH   A O   1 
HETATM 2083 O O   . HOH   C 3 .   ? -12.98295 -12.29978 -31.00819 1.000 26.30031  ? 618 HOH   A O   1 
HETATM 2084 O O   . HOH   C 3 .   ? 5.60091   -3.35089  -26.17266 1.000 37.56299  ? 619 HOH   A O   1 
HETATM 2085 O O   . HOH   C 3 .   ? 4.01127   -22.95384 -3.43285  1.000 33.70796  ? 620 HOH   A O   1 
HETATM 2086 O O   . HOH   C 3 .   ? 15.59215  -7.00814  -27.74363 1.000 34.47483  ? 621 HOH   A O   1 
HETATM 2087 O O   . HOH   C 3 .   ? -15.885   -4.096    -15.507   1.000 50.26945  ? 622 HOH   A O   1 
HETATM 2088 O O   . HOH   C 3 .   ? -12.25687 -26.99853 -20.36543 1.000 28.28957  ? 623 HOH   A O   1 
HETATM 2089 O O   . HOH   C 3 .   ? 13.18333  -22.51619 -4.67315  1.000 48.55770  ? 624 HOH   A O   1 
HETATM 2090 O O   . HOH   C 3 .   ? -5.53302  -12.18222 -41.84259 1.000 43.99219  ? 625 HOH   A O   1 
HETATM 2091 O O   . HOH   C 3 .   ? -13.55312 -29.19140 -16.95902 1.000 50.07586  ? 626 HOH   A O   1 
HETATM 2092 O O   . HOH   C 3 .   ? 7.17636   -29.53488 -29.63200 1.000 60.04703  ? 627 HOH   A O   1 
HETATM 2093 O O   . HOH   C 3 .   ? -9.38303  -13.46374 -40.13834 1.000 58.94315  ? 628 HOH   A O   1 
HETATM 2094 O O   . HOH   C 3 .   ? 4.68575   -1.88960  -18.28233 1.000 32.01970  ? 629 HOH   A O   1 
HETATM 2095 O O   . HOH   C 3 .   ? 13.90537  0.87153   -13.58823 1.000 34.18258  ? 630 HOH   A O   1 
HETATM 2096 O O   . HOH   C 3 .   ? 17.77552  -15.23444 -29.49276 1.000 49.65622  ? 631 HOH   A O   1 
HETATM 2097 O O   . HOH   C 3 .   ? 2.83144   -10.14375 -23.08537 1.000 29.79786  ? 632 HOH   A O   1 
HETATM 2098 O O   . HOH   C 3 .   ? 4.26758   -4.97752  -22.03621 1.000 48.04033  ? 633 HOH   A O   1 
HETATM 2099 O O   . HOH   C 3 .   ? 3.74603   -0.27634  -16.50151 1.000 39.24600  ? 634 HOH   A O   1 
HETATM 2100 O O   . HOH   C 3 .   ? 1.74024   -18.35548 0.07264   1.000 35.35445  ? 635 HOH   A O   1 
HETATM 2101 O O   . HOH   C 3 .   ? 8.36408   -25.75258 -25.87449 1.000 35.88675  ? 636 HOH   A O   1 
HETATM 2102 O O   . HOH   C 3 .   ? 14.56473  -22.48446 -17.16564 1.000 34.18847  ? 637 HOH   A O   1 
HETATM 2103 O O   . HOH   C 3 .   ? 5.55858   1.70928   -16.61393 1.000 35.62162  ? 638 HOH   A O   1 
HETATM 2104 O O   . HOH   C 3 .   ? 7.17873   2.05425   -12.47375 1.000 39.94721  ? 639 HOH   A O   1 
HETATM 2105 O O   . HOH   C 3 .   ? -1.83359  -26.95060 -24.95757 1.000 38.71048  ? 640 HOH   A O   1 
HETATM 2106 O O   . HOH   C 3 .   ? 3.18718   -6.69951  -20.52058 1.000 38.32042  ? 641 HOH   A O   1 
HETATM 2107 O O   . HOH   C 3 .   ? -17.045   -4.869    -17.470   1.000 37.93914  ? 642 HOH   A O   1 
HETATM 2108 O O   . HOH   C 3 .   ? 10.78784  -17.34325 -38.64294 1.000 43.81051  ? 643 HOH   A O   1 
HETATM 2109 O O   . HOH   C 3 .   ? 2.15720   -25.88747 -29.32346 1.000 39.19599  ? 644 HOH   A O   1 
HETATM 2110 O O   . HOH   C 3 .   ? -12.25397 -20.81155 -29.70354 1.000 49.56691  ? 645 HOH   A O   1 
HETATM 2111 O O   . HOH   C 3 .   ? 4.55816   -21.78137 -39.26219 1.000 54.54545  ? 646 HOH   A O   1 
HETATM 2112 O O   . HOH   C 3 .   ? -1.40356  -5.88288  -12.28340 1.000 46.80627  ? 647 HOH   A O   1 
HETATM 2113 O O   . HOH   C 3 .   ? -16.56400 -13.52292 -29.22762 1.000 54.42496  ? 648 HOH   A O   1 
HETATM 2114 O O   . HOH   C 3 .   ? -11.90525 -27.18353 -5.61737  1.000 56.92040  ? 649 HOH   A O   1 
HETATM 2115 O O   . HOH   C 3 .   ? 0.08738   -18.96198 -1.93287  1.000 37.28074  ? 650 HOH   A O   1 
HETATM 2116 O O   . HOH   C 3 .   ? 18.90127  -8.26247  -17.66268 1.000 38.25597  ? 651 HOH   A O   1 
HETATM 2117 O O   . HOH   C 3 .   ? -6.40934  3.80677   -34.66372 1.000 45.58763  ? 652 HOH   A O   1 
HETATM 2118 O O   . HOH   C 3 .   ? -11.41067 -19.69273 -27.97645 1.000 47.66045  ? 653 HOH   A O   1 
HETATM 2119 O O   . HOH   C 3 .   ? 3.43561   -8.05967  -2.10515  1.000 46.73665  ? 654 HOH   A O   1 
HETATM 2120 O O   . HOH   C 3 .   ? 17.74400  -21.32517 -19.82068 1.000 31.49273  ? 655 HOH   A O   1 
HETATM 2121 O O   . HOH   C 3 .   ? -13.90988 -14.37196 -3.07079  1.000 31.15884  ? 656 HOH   A O   1 
HETATM 2122 O O   . HOH   C 3 .   ? 12.353    -25.153   -38.367   1.000 30.79467  ? 657 HOH   A O   1 
HETATM 2123 O O   . HOH   C 3 .   ? -8.87139  -5.63810  -39.68849 1.000 44.36622  ? 658 HOH   A O   1 
HETATM 2124 O O   . HOH   C 3 .   ? -14.16762 -9.98902  -8.43596  1.000 36.40700  ? 659 HOH   A O   1 
HETATM 2125 O O   . HOH   C 3 .   ? -0.46719  -1.26787  -22.81096 1.000 34.58052  ? 660 HOH   A O   1 
HETATM 2126 O O   . HOH   C 3 .   ? 18.03403  -17.72165 -11.05372 1.000 42.23412  ? 661 HOH   A O   1 
HETATM 2127 O O   . HOH   C 3 .   ? -12.29640 -16.47029 -28.16892 1.000 31.09139  ? 662 HOH   A O   1 
HETATM 2128 O O   . HOH   C 3 .   ? 1.65717   -2.97793  -12.61303 1.000 45.23485  ? 663 HOH   A O   1 
HETATM 2129 O O   . HOH   C 3 .   ? 2.24731   -0.88040  -14.36634 1.000 43.92688  ? 664 HOH   A O   1 
HETATM 2130 O O   . HOH   C 3 .   ? -18.046   -36.929   -19.906   1.000 38.63242  ? 665 HOH   A O   1 
HETATM 2131 O O   . HOH   C 3 .   ? -7.85803  -20.69942 -37.65529 1.000 47.08302  ? 666 HOH   A O   1 
HETATM 2132 O O   . HOH   C 3 .   ? -14.59591 -14.31339 -36.85633 1.000 59.23790  ? 667 HOH   A O   1 
HETATM 2133 O O   . HOH   C 3 .   ? -3.28867  -27.37776 -3.39217  1.000 45.71327  ? 668 HOH   A O   1 
HETATM 2134 O O   . HOH   C 3 .   ? 12.06943  -27.55052 -23.36181 1.000 46.72380  ? 669 HOH   A O   1 
HETATM 2135 O O   . HOH   C 3 .   ? -1.17314  -33.05448 -16.41681 1.000 59.02778  ? 670 HOH   A O   1 
HETATM 2136 O O   . HOH   C 3 .   ? 7.84752   -13.78872 -38.14065 1.000 36.14477  ? 671 HOH   A O   1 
HETATM 2137 O O   . HOH   C 3 .   ? -15.74873 -20.78588 -32.25826 1.000 51.76728  ? 672 HOH   A O   1 
HETATM 2138 O O   . HOH   C 3 .   ? -6.333    6.709     -35.921   1.000 45.65154  ? 673 HOH   A O   1 
HETATM 2139 O O   . HOH   C 3 .   ? -2.31365  -1.10166  -30.83715 1.000 49.09003  ? 674 HOH   A O   1 
HETATM 2140 O O   . HOH   C 3 .   ? -11.60677 -9.70934  -39.60163 1.000 54.96496  ? 675 HOH   A O   1 
HETATM 2141 O O   . HOH   C 3 .   ? 3.61626   -9.05302  -39.03378 1.000 42.26105  ? 676 HOH   A O   1 
HETATM 2142 O O   . HOH   C 3 .   ? -10.61935 -8.94594  -1.58275  1.000 40.21942  ? 677 HOH   A O   1 
HETATM 2143 O O   . HOH   C 3 .   ? -18.61380 -11.81561 -21.11307 1.000 27.75076  ? 678 HOH   A O   1 
HETATM 2144 O O   . HOH   C 3 .   ? 6.33211   -29.82034 -24.90848 1.000 44.20687  ? 679 HOH   A O   1 
HETATM 2145 O O   . HOH   C 3 .   ? 6.62323   -21.52208 -2.72429  1.000 33.48599  ? 680 HOH   A O   1 
HETATM 2146 O O   . HOH   C 3 .   ? -9.73975  -26.16882 -20.95960 1.000 25.59728  ? 681 HOH   A O   1 
HETATM 2147 O O   . HOH   C 3 .   ? 2.292     -0.870    -25.920   1.000 38.73650  ? 682 HOH   A O   1 
HETATM 2148 O O   . HOH   C 3 .   ? 10.58496  -21.30812 -43.03735 1.000 52.36929  ? 683 HOH   A O   1 
HETATM 2149 O O   . HOH   C 3 .   ? -16.52220 -18.64806 -3.12747  1.000 48.85869  ? 684 HOH   A O   1 
HETATM 2150 O O   . HOH   C 3 .   ? 5.82621   -12.83028 -39.82059 1.000 32.95732  ? 685 HOH   A O   1 
HETATM 2151 O O   . HOH   C 3 .   ? -6.702    -23.174   -1.716    1.000 41.76138  ? 686 HOH   A O   1 
HETATM 2152 O O   . HOH   C 3 .   ? 2.92050   -4.64412  -19.96656 1.000 42.34251  ? 687 HOH   A O   1 
HETATM 2153 O O   . HOH   C 3 .   ? 7.98246   -28.74982 -28.09079 1.000 42.05242  ? 688 HOH   A O   1 
HETATM 2154 O O   . HOH   C 3 .   ? 5.45676   -3.19633  -23.57196 1.000 41.03085  ? 689 HOH   A O   1 
HETATM 2155 O O   . HOH   C 3 .   ? -10.430   -22.706   4.373     1.000 45.80449  ? 690 HOH   A O   1 
HETATM 2156 O O   . HOH   C 3 .   ? -4.73963  -9.52336  -43.78567 1.000 55.20348  ? 691 HOH   A O   1 
HETATM 2157 O O   . HOH   C 3 .   ? -6.88624  -30.77825 -9.23435  1.000 34.68953  ? 692 HOH   A O   1 
HETATM 2158 O O   . HOH   C 3 .   ? -10.12189 -29.05469 -30.87131 1.000 46.45203  ? 693 HOH   A O   1 
HETATM 2159 O O   . HOH   C 3 .   ? -4.72783  -24.99163 -1.01393  1.000 58.06422  ? 694 HOH   A O   1 
HETATM 2160 O O   . HOH   C 3 .   ? -13.52695 -13.61499 -38.34048 1.000 51.34215  ? 695 HOH   A O   1 
HETATM 2161 O O   . HOH   C 3 .   ? -16.15112 -13.44155 -3.74693  1.000 46.11881  ? 696 HOH   A O   1 
HETATM 2162 O O   . HOH   C 3 .   ? 1.91085   -5.88536  -36.42862 1.000 40.76045  ? 697 HOH   A O   1 
HETATM 2163 O O   . HOH   C 3 .   ? 11.05437  -27.96548 -27.81214 1.000 40.80762  ? 698 HOH   A O   1 
HETATM 2164 O O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.45581 0.50  21.84546  ? 699 HOH   A O   1 
HETATM 2165 O O   . HOH   C 3 .   ? -11.86229 -20.54475 -25.39806 1.000 36.30432  ? 700 HOH   A O   1 
HETATM 2166 O O   . HOH   C 3 .   ? 16.19000  -3.02878  -26.32631 1.000 40.28912  ? 701 HOH   A O   1 
HETATM 2167 O O   . HOH   C 3 .   ? -19.64823 -8.60951  -24.02066 1.000 56.88684  ? 702 HOH   A O   1 
HETATM 2168 O O   . HOH   C 3 .   ? -6.95734  -26.64144 -23.31455 1.000 51.10881  ? 703 HOH   A O   1 
HETATM 2169 O O   . HOH   C 3 .   ? 11.447    -30.038   -34.196   1.000 39.87556  ? 704 HOH   A O   1 
HETATM 2170 O O   . HOH   C 3 .   ? -16.27588 -12.77472 -6.26412  1.000 43.97589  ? 705 HOH   A O   1 
HETATM 2171 O O   . HOH   C 3 .   ? 20.931    -18.248   -22.233   1.000 44.26447  ? 706 HOH   A O   1 
HETATM 2172 O O   . HOH   C 3 .   ? 4.89215   -14.71537 -41.49857 1.000 45.56082  ? 707 HOH   A O   1 
HETATM 2173 O O   . HOH   C 3 .   ? -0.85855  -2.51460  -31.46399 1.000 45.58214  ? 708 HOH   A O   1 
HETATM 2174 O O   . HOH   C 3 .   ? 12.94068  -25.04003 -15.76753 1.000 48.18180  ? 709 HOH   A O   1 
HETATM 2175 O O   . HOH   C 3 .   ? -17.23561 4.38919   -31.37507 1.000 51.53765  ? 710 HOH   A O   1 
HETATM 2176 O O   . HOH   C 3 .   ? 3.05002   -2.17664  -20.55117 1.000 37.31932  ? 711 HOH   A O   1 
HETATM 2177 O O   . HOH   C 3 .   ? 4.147     -1.910    -27.971   1.000 39.47154  ? 712 HOH   A O   1 
HETATM 2178 O O   . HOH   C 3 .   ? 9.88362   -25.01151 -14.87692 1.000 40.10957  ? 713 HOH   A O   1 
HETATM 2179 O O   . HOH   C 3 .   ? 0.56702   -1.35787  -16.75089 1.000 38.59406  ? 714 HOH   A O   1 
HETATM 2180 O O   . HOH   C 3 .   ? 11.06102  -29.79958 -19.32888 1.000 56.20881  ? 715 HOH   A O   1 
HETATM 2181 O O   . HOH   C 3 .   ? 20.57467  -7.60206  -15.70316 1.000 51.42226  ? 716 HOH   A O   1 
HETATM 2182 O O   . HOH   C 3 .   ? 4.078     -3.341    -33.906   1.000 49.64232  ? 717 HOH   A O   1 
HETATM 2183 O O   . HOH   C 3 .   ? 9.58576   -12.46744 -37.17011 1.000 43.72162  ? 718 HOH   A O   1 
HETATM 2184 O O   . HOH   C 3 .   ? 19.29374  -20.44651 -22.18215 1.000 37.04131  ? 719 HOH   A O   1 
HETATM 2185 O O   . HOH   C 3 .   ? -16.87656 -15.71725 -10.41581 1.000 35.41310  ? 720 HOH   A O   1 
HETATM 2186 O O   . HOH   C 3 .   ? 14.905    -17.239   0.307     1.000 39.36298  ? 721 HOH   A O   1 
HETATM 2187 O O   . HOH   C 3 .   ? -14.47871 -14.26292 -10.25093 1.000 28.83651  ? 722 HOH   A O   1 
HETATM 2188 O O   . HOH   C 3 .   ? 22.008    -18.006   -25.042   1.000 39.87212  ? 723 HOH   A O   1 
HETATM 2189 O O   . HOH   C 3 .   ? -14.69318 -9.53846  -11.33117 1.000 40.86988  ? 724 HOH   A O   1 
HETATM 2190 O O   . HOH   C 3 .   ? -19.59615 -6.01144  -21.55935 1.000 43.33944  ? 725 HOH   A O   1 
HETATM 2191 O O   . HOH   C 3 .   ? 17.32802  -4.74487  -28.16571 1.000 44.48646  ? 726 HOH   A O   1 
HETATM 2192 O O   . HOH   C 3 .   ? -2.95072  -26.33242 -27.42907 1.000 50.81784  ? 727 HOH   A O   1 
HETATM 2193 O O   . HOH   C 3 .   ? -8.95145  -32.72122 -8.63304  1.000 48.56796  ? 728 HOH   A O   1 
HETATM 2194 O O   . HOH   C 3 .   ? -9.82105  -20.56654 -39.69520 1.000 48.64051  ? 729 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   ? 0.65528 0.81621 0.54031 -0.05986 -0.05021 -0.24824 16  GLU A N   
2    C CA  . GLU A 9   ? 0.76414 0.90340 0.63891 -0.02809 -0.05056 -0.23256 16  GLU A CA  
3    C C   . GLU A 9   ? 0.55919 0.69637 0.45325 -0.01386 -0.05286 -0.21422 16  GLU A C   
4    O O   . GLU A 9   ? 0.61216 0.79943 0.52456 -0.00369 -0.06204 -0.20408 16  GLU A O   
5    C CB  . GLU A 9   ? 0.83339 1.02330 0.70312 -0.00403 -0.05993 -0.22769 16  GLU A CB  
6    C CG  . GLU A 9   ? 1.03641 1.23407 0.90770 0.03420  -0.06312 -0.20421 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.23327 1.37198 1.08680 0.04990  -0.05365 -0.19732 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.29281 1.37767 1.13844 0.03444  -0.04361 -0.20589 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.09922 1.24471 0.94657 0.08036  -0.05373 -0.18087 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.48805 0.56747 0.37749 -0.01203 -0.04316 -0.20976 17  VAL A N   
11   C CA  . VAL A 10  ? 0.39706 0.46652 0.30825 -0.00351 -0.04268 -0.18699 17  VAL A CA  
12   C C   . VAL A 10  ? 0.40571 0.45015 0.31586 0.02512  -0.03883 -0.16239 17  VAL A C   
13   O O   . VAL A 10  ? 0.44997 0.45443 0.34396 0.03090  -0.02959 -0.16185 17  VAL A O   
14   C CB  . VAL A 10  ? 0.45796 0.47969 0.37082 -0.02486 -0.03088 -0.19061 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.48102 0.49668 0.41484 -0.01544 -0.03120 -0.16728 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.51295 0.54893 0.42466 -0.05863 -0.02931 -0.21513 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.32608 0.39438 0.25164 0.04240  -0.04399 -0.14325 18  GLU A N   
18   C CA  . GLU A 11  ? 0.31023 0.35862 0.23827 0.06441  -0.03876 -0.12118 18  GLU A CA  
19   C C   . GLU A 11  ? 0.29074 0.31750 0.23545 0.06029  -0.03500 -0.10781 18  GLU A C   
20   O O   . GLU A 11  ? 0.27578 0.31760 0.23413 0.05121  -0.03897 -0.10705 18  GLU A O   
21   C CB  . GLU A 11  ? 0.29932 0.38175 0.22915 0.08552  -0.04240 -0.10912 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.32574 0.43327 0.23624 0.09588  -0.04573 -0.11906 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.38864 0.52669 0.29704 0.12139  -0.04584 -0.10372 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.41300 0.58699 0.32849 0.12364  -0.05120 -0.10232 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.50881 0.63714 0.40518 0.14090  -0.03916 -0.09364 18  GLU A OE2 
26   N N   . THR A 12  ? 0.29269 0.28770 0.23581 0.06758  -0.02713 -0.09738 19  THR A N   
27   C CA  . THR A 12  ? 0.27774 0.25785 0.23419 0.06588  -0.02378 -0.08507 19  THR A CA  
28   C C   . THR A 12  ? 0.25950 0.24768 0.22551 0.08028  -0.02183 -0.06854 19  THR A C   
29   O O   . THR A 12  ? 0.27110 0.25609 0.22984 0.09277  -0.01746 -0.06439 19  THR A O   
30   C CB  . THR A 12  ? 0.30168 0.24441 0.24766 0.06358  -0.01442 -0.08596 19  THR A CB  
31   O OG1 . THR A 12  ? 0.33010 0.25611 0.26340 0.04665  -0.01141 -0.10343 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.28775 0.22387 0.24612 0.06489  -0.01187 -0.07243 19  THR A CG2 
33   N N   . PHE A 13  ? 0.23686 0.23500 0.21760 0.07680  -0.02358 -0.06085 20  PHE A N   
34   C CA  . PHE A 13  ? 0.24568 0.25070 0.23529 0.08408  -0.01945 -0.04858 20  PHE A CA  
35   C C   . PHE A 13  ? 0.26240 0.26464 0.26449 0.07723  -0.01837 -0.04242 20  PHE A C   
36   O O   . PHE A 13  ? 0.24668 0.24484 0.25189 0.06838  -0.02162 -0.04516 20  PHE A O   
37   C CB  . PHE A 13  ? 0.23060 0.25043 0.22287 0.08520  -0.02026 -0.04639 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.23560 0.26952 0.21553 0.09575  -0.02188 -0.05018 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.23352 0.28358 0.20917 0.08980  -0.03027 -0.06263 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.26884 0.30351 0.24023 0.11134  -0.01421 -0.04228 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.25848 0.33248 0.22165 0.10111  -0.03308 -0.06724 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.31461 0.36745 0.27087 0.12619  -0.01539 -0.04417 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.28964 0.36629 0.24199 0.12165  -0.02619 -0.05706 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.22501 0.23306 0.23414 0.08092  -0.01305 -0.03438 21  ALA A N   
45   C CA  . ALA A 14  ? 0.19960 0.21670 0.22125 0.07339  -0.01289 -0.03004 21  ALA A CA  
46   C C   . ALA A 14  ? 0.21790 0.23915 0.24516 0.06433  -0.01141 -0.03034 21  ALA A C   
47   O O   . ALA A 14  ? 0.24253 0.26113 0.26626 0.06707  -0.00477 -0.02879 21  ALA A O   
48   C CB  . ALA A 14  ? 0.19912 0.23026 0.22758 0.07814  -0.00716 -0.02375 21  ALA A CB  
49   N N   . PHE A 15  ? 0.19511 0.21980 0.22840 0.05488  -0.01502 -0.03133 22  PHE A N   
50   C CA  . PHE A 15  ? 0.20139 0.22717 0.23792 0.04573  -0.01043 -0.03188 22  PHE A CA  
51   C C   . PHE A 15  ? 0.20341 0.23860 0.24613 0.03980  -0.00198 -0.03080 22  PHE A C   
52   O O   . PHE A 15  ? 0.22962 0.28321 0.28013 0.04021  -0.00348 -0.02915 22  PHE A O   
53   C CB  . PHE A 15  ? 0.20492 0.23505 0.24582 0.03634  -0.01531 -0.03369 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.18912 0.21134 0.22592 0.03752  -0.02083 -0.03556 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.20171 0.21952 0.23382 0.03905  -0.01869 -0.03662 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.20909 0.22956 0.24582 0.03770  -0.02565 -0.03558 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.20512 0.22561 0.23672 0.03826  -0.02386 -0.03932 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.19935 0.21336 0.23350 0.03461  -0.02847 -0.03904 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.19399 0.21243 0.22785 0.03336  -0.02872 -0.04164 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.21007 0.23343 0.24848 0.03369  0.00879  -0.03188 23  GLN A N   
61   C CA  . GLN A 16  ? 0.21468 0.24627 0.25964 0.01951  0.01927  -0.03478 23  GLN A CA  
62   C C   . GLN A 16  ? 0.22400 0.28059 0.27969 0.00616  0.01177  -0.04000 23  GLN A C   
63   O O   . GLN A 16  ? 0.22128 0.27580 0.27477 0.00590  0.00381  -0.04106 23  GLN A O   
64   C CB  . GLN A 16  ? 0.29353 0.29775 0.32689 0.01282  0.03586  -0.03635 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.32761 0.30920 0.34699 0.02917  0.04713  -0.02891 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.47948 0.42767 0.48199 0.02712  0.06688  -0.02784 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.47042 0.40736 0.46179 0.03978  0.06584  -0.02380 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.47450 0.40621 0.47365 0.01143  0.08738  -0.03138 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.22593 0.31146 0.29334 -0.00460 0.01462  -0.04325 24  ALA A N   
70   C CA  . ALA A 17  ? 0.20314 0.32520 0.28053 -0.01242 0.00536  -0.04696 24  ALA A CA  
71   C C   . ALA A 17  ? 0.20012 0.31415 0.27205 -0.02738 0.00580  -0.05515 24  ALA A C   
72   O O   . ALA A 17  ? 0.22630 0.35609 0.29901 -0.02459 -0.00485 -0.05454 24  ALA A O   
73   C CB  . ALA A 17  ? 0.23795 0.40094 0.32987 -0.02450 0.01028  -0.05126 24  ALA A CB  
74   N N   . GLU A 18  ? 0.24350 0.32859 0.30651 -0.04068 0.02020  -0.06155 25  GLU A N   
75   C CA  . GLU A 18  ? 0.24699 0.31982 0.30125 -0.05518 0.02381  -0.07033 25  GLU A CA  
76   C C   . GLU A 18  ? 0.24198 0.29595 0.28783 -0.03990 0.01502  -0.06367 25  GLU A C   
77   O O   . GLU A 18  ? 0.25570 0.31581 0.29861 -0.04625 0.01014  -0.06813 25  GLU A O   
78   C CB  . GLU A 18  ? 0.32141 0.35689 0.36262 -0.07016 0.04678  -0.07727 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.39601 0.44709 0.44494 -0.09317 0.06028  -0.08742 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.43719 0.48738 0.49191 -0.08152 0.06590  -0.07815 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.35992 0.39786 0.41138 -0.05533 0.05875  -0.06479 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.49681 0.55985 0.55896 -0.10056 0.07916  -0.08556 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.23228 0.26814 0.27454 -0.02072 0.01272  -0.05396 26  ILE A N   
84   C CA  . ILE A 19  ? 0.19502 0.21951 0.23193 -0.00917 0.00514  -0.04920 26  ILE A CA  
85   C C   . ILE A 19  ? 0.22879 0.27580 0.27378 -0.00381 -0.00940 -0.04619 26  ILE A C   
86   O O   . ILE A 19  ? 0.23631 0.28270 0.27897 -0.00330 -0.01460 -0.04562 26  ILE A O   
87   C CB  . ILE A 19  ? 0.24050 0.24616 0.27053 0.00714  0.00806  -0.04247 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.30753 0.28483 0.32273 0.00882  0.02547  -0.04150 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.23676 0.24399 0.26647 0.01678  -0.00222 -0.03932 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.36695 0.33122 0.37788 -0.00507 0.04258  -0.04641 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.20062 0.26555 0.25306 0.00228  -0.01373 -0.04283 27  ALA A N   
92   C CA  . ALA A 20  ? 0.18284 0.26470 0.23810 0.01025  -0.02284 -0.03803 27  ALA A CA  
93   C C   . ALA A 20  ? 0.19519 0.30166 0.25225 0.00095  -0.02587 -0.04171 27  ALA A C   
94   O O   . ALA A 20  ? 0.21523 0.32344 0.26838 0.00702  -0.03088 -0.03757 27  ALA A O   
95   C CB  . ALA A 20  ? 0.19706 0.29528 0.25733 0.02103  -0.02366 -0.03268 27  ALA A CB  
96   N N   . GLN A 21  ? 0.19501 0.32003 0.25633 -0.01506 -0.02142 -0.05053 28  GLN A N   
97   C CA  . GLN A 21  ? 0.20561 0.36007 0.26726 -0.02672 -0.02471 -0.05757 28  GLN A CA  
98   C C   . GLN A 21  ? 0.24876 0.37751 0.29907 -0.03119 -0.02345 -0.06054 28  GLN A C   
99   O O   . GLN A 21  ? 0.23872 0.38452 0.28567 -0.02887 -0.02976 -0.05957 28  GLN A O   
100  C CB  . GLN A 21  ? 0.24054 0.41764 0.30830 -0.04888 -0.01761 -0.07063 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.41438 0.63982 0.48504 -0.06195 -0.02319 -0.08029 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.78706 1.03749 0.86491 -0.09041 -0.01417 -0.09733 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.73525 1.03792 0.81830 -0.10510 -0.01884 -0.10865 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.50740 0.72672 0.58635 -0.09713 -0.00086 -0.09858 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.20244 0.29257 0.24535 -0.03473 -0.01417 -0.06267 29  LEU A N   
106  C CA  . LEU A 22  ? 0.23951 0.30545 0.27118 -0.03484 -0.01159 -0.06324 29  LEU A CA  
107  C C   . LEU A 22  ? 0.24367 0.31060 0.27646 -0.02004 -0.02087 -0.05337 29  LEU A C   
108  O O   . LEU A 22  ? 0.24938 0.31983 0.27681 -0.02061 -0.02336 -0.05328 29  LEU A O   
109  C CB  . LEU A 22  ? 0.29154 0.31993 0.31449 -0.03229 0.00069  -0.06230 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.28513 0.29133 0.29690 -0.02694 0.00467  -0.05995 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.36796 0.36984 0.36827 -0.04324 0.01213  -0.07096 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.31622 0.29550 0.31991 -0.01674 0.01587  -0.05509 29  LEU A CD2 
113  N N   . MET A 23  ? 0.19139 0.25252 0.22921 -0.00781 -0.02410 -0.04579 30  MET A N   
114  C CA  . MET A 23  ? 0.20476 0.26004 0.24188 0.00214  -0.02872 -0.03859 30  MET A CA  
115  C C   . MET A 23  ? 0.20957 0.28523 0.24536 0.00697  -0.03326 -0.03399 30  MET A C   
116  O O   . MET A 23  ? 0.22617 0.29605 0.25670 0.01031  -0.03346 -0.02985 30  MET A O   
117  C CB  . MET A 23  ? 0.19464 0.23857 0.23450 0.01072  -0.02934 -0.03495 30  MET A CB  
118  C CG  . MET A 23  ? 0.21383 0.24354 0.25236 0.01015  -0.02535 -0.03774 30  MET A CG  
119  S SD  . MET A 23  ? 0.22549 0.24958 0.26529 0.01890  -0.02684 -0.03686 30  MET A SD  
120  C CE  . MET A 23  ? 0.24587 0.26384 0.28509 0.01809  -0.02974 -0.03679 30  MET A CE  
121  N N   . SER A 24  ? 0.22166 0.32403 0.26143 0.01006  -0.03583 -0.03297 31  SER A N   
122  C CA  . SER A 24  ? 0.18684 0.31662 0.22300 0.01970  -0.03949 -0.02653 31  SER A CA  
123  C C   . SER A 24  ? 0.23948 0.38505 0.27020 0.01068  -0.04139 -0.03231 31  SER A C   
124  O O   . SER A 24  ? 0.26994 0.42204 0.29236 0.02091  -0.04253 -0.02488 31  SER A O   
125  C CB  . SER A 24  ? 0.30433 0.47204 0.34734 0.02547  -0.04198 -0.02480 31  SER A CB  
126  O OG  . SER A 24  ? 0.46038 0.60970 0.50485 0.03640  -0.03901 -0.01850 31  SER A OG  
127  N N   . LEU A 25  ? 0.21330 0.36090 0.24533 -0.00786 -0.03940 -0.04544 32  LEU A N   
128  C CA  . LEU A 25  ? 0.22164 0.38098 0.24499 -0.01820 -0.03977 -0.05354 32  LEU A CA  
129  C C   . LEU A 25  ? 0.25114 0.37992 0.26560 -0.01214 -0.03718 -0.04764 32  LEU A C   
130  O O   . LEU A 25  ? 0.26209 0.40315 0.26757 -0.00824 -0.03920 -0.04545 32  LEU A O   
131  C CB  . LEU A 25  ? 0.25570 0.41050 0.27774 -0.04146 -0.03302 -0.07039 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.31655 0.47836 0.32592 -0.05670 -0.03065 -0.08334 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.38233 0.55358 0.39108 -0.08245 -0.02334 -0.10222 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.45859 0.57401 0.45596 -0.05388 -0.02292 -0.08080 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.21760 0.31152 0.23432 -0.01098 -0.03235 -0.04515 33  ILE A N   
136  C CA  . ILE A 26  ? 0.22115 0.29330 0.23243 -0.00703 -0.02919 -0.04045 33  ILE A CA  
137  C C   . ILE A 26  ? 0.24512 0.31880 0.25526 0.00599  -0.03107 -0.02861 33  ILE A C   
138  O O   . ILE A 26  ? 0.25820 0.32727 0.26118 0.00891  -0.02865 -0.02439 33  ILE A O   
139  C CB  . ILE A 26  ? 0.21708 0.26413 0.23268 -0.00711 -0.02442 -0.04044 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.26394 0.29977 0.27305 -0.01650 -0.01680 -0.04951 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.25160 0.28638 0.26741 -0.00192 -0.02229 -0.03423 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.27007 0.28723 0.28129 -0.01168 -0.01104 -0.04766 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.24230 0.31758 0.25690 0.01479  -0.03248 -0.02246 34  ILE A N   
144  C CA  . ILE A 27  ? 0.26738 0.33331 0.27589 0.02813  -0.02892 -0.01052 34  ILE A CA  
145  C C   . ILE A 27  ? 0.26526 0.35746 0.26329 0.03986  -0.03028 -0.00334 34  ILE A C   
146  O O   . ILE A 27  ? 0.30739 0.38841 0.29464 0.05032  -0.02414 0.00697  34  ILE A O   
147  C CB  . ILE A 27  ? 0.25592 0.30898 0.26774 0.03493  -0.02687 -0.00687 34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.26431 0.29543 0.28358 0.02478  -0.02551 -0.01368 34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.29006 0.32845 0.28973 0.05091  -0.01873 0.00612  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.27441 0.29551 0.29607 0.02875  -0.02467 -0.01415 34  ILE A CD1 
151  N N   . ASN A 28  ? 0.24240 0.37312 0.24269 0.03913  -0.03714 -0.00819 35  ASN A N   
152  C CA  . ASN A 28  ? 0.28120 0.44860 0.27154 0.05504  -0.03944 0.00019  35  ASN A CA  
153  C C   . ASN A 28  ? 0.33010 0.52450 0.31268 0.04763  -0.04373 -0.00737 35  ASN A C   
154  O O   . ASN A 28  ? 0.39602 0.61935 0.36640 0.06418  -0.04475 0.00169  35  ASN A O   
155  C CB  . ASN A 28  ? 0.31100 0.51859 0.30875 0.06075  -0.04473 -0.00014 35  ASN A CB  
156  C CG  . ASN A 28  ? 0.46594 0.64935 0.46520 0.07474  -0.03892 0.01033  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.40212 0.54603 0.39098 0.08646  -0.02956 0.02139  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.54036 0.74397 0.55136 0.07179  -0.04234 0.00578  35  ASN A ND2 
159  N N   . THR A 29  ? 0.25526 0.44171 0.24137 0.02543  -0.04482 -0.02327 36  THR A N   
160  C CA  . THR A 29  ? 0.23096 0.43904 0.20602 0.01647  -0.04717 -0.03312 36  THR A CA  
161  C C   . THR A 29  ? 0.26848 0.45528 0.23016 0.02723  -0.04192 -0.02297 36  THR A C   
162  O O   . THR A 29  ? 0.28022 0.42523 0.24468 0.02692  -0.03496 -0.01780 36  THR A O   
163  C CB  . THR A 29  ? 0.30377 0.49750 0.28145 -0.00943 -0.04461 -0.05258 36  THR A CB  
164  O OG1 . THR A 29  ? 0.30531 0.52040 0.29483 -0.02054 -0.04721 -0.06179 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.32083 0.53475 0.28378 -0.02149 -0.04532 -0.06618 36  THR A CG2 
166  N N   . PHE A 30  ? 0.27784 0.49756 0.22508 0.03668  -0.04479 -0.02031 37  PHE A N   
167  C CA  . PHE A 30  ? 0.28128 0.48205 0.21399 0.04459  -0.03855 -0.01255 37  PHE A CA  
168  C C   . PHE A 30  ? 0.31173 0.49013 0.24185 0.02402  -0.03553 -0.02788 37  PHE A C   
169  O O   . PHE A 30  ? 0.30784 0.50765 0.23227 0.00794  -0.03935 -0.04574 37  PHE A O   
170  C CB  . PHE A 30  ? 0.29100 0.53593 0.20584 0.06249  -0.04203 -0.00544 37  PHE A CB  
171  C CG  . PHE A 30  ? 0.30804 0.53174 0.20604 0.07260  -0.03367 0.00441  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.39725 0.58082 0.29346 0.08792  -0.02142 0.02396  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.31957 0.55867 0.20307 0.06442  -0.03570 -0.00702 37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.37479 0.53648 0.25717 0.09511  -0.01113 0.03329  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.37386 0.59109 0.24235 0.07427  -0.02660 0.00299  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.35523 0.53590 0.22394 0.09007  -0.01433 0.02393  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.27001 0.40623 0.20284 0.02431  -0.02685 -0.02145 38  TYR A N   
178  C CA  . TYR A 31  ? 0.27551 0.38914 0.20459 0.01046  -0.02149 -0.03250 38  TYR A CA  
179  C C   . TYR A 31  ? 0.26991 0.35469 0.20063 0.01858  -0.01243 -0.01960 38  TYR A C   
180  O O   . TYR A 31  ? 0.26991 0.33674 0.21540 0.01972  -0.00975 -0.01288 38  TYR A O   
181  C CB  . TYR A 31  ? 0.29520 0.39389 0.23620 -0.00411 -0.02097 -0.04370 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.27787 0.34728 0.21134 -0.01297 -0.01132 -0.05181 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.35771 0.42908 0.27314 -0.02454 -0.00781 -0.06676 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.39515 0.43727 0.33828 -0.00888 -0.00461 -0.04484 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.44499 0.48444 0.34767 -0.02957 0.00457  -0.07320 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.37516 0.39336 0.30765 -0.01154 0.00644  -0.04996 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.39159 0.40470 0.30279 -0.02093 0.01190  -0.06331 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.45549 0.43782 0.34965 -0.02160 0.02676  -0.06823 38  TYR A OH  
189  N N   . SER A 32  ? 0.28531 0.36835 0.20128 0.02228  -0.00728 -0.01780 39  SER A N   
190  C CA  . SER A 32  ? 0.28909 0.35240 0.20662 0.03009  0.00250  -0.00446 39  SER A CA  
191  C C   . SER A 32  ? 0.30631 0.34848 0.23470 0.02265  0.00903  -0.00730 39  SER A C   
192  O O   . SER A 32  ? 0.30980 0.34192 0.24908 0.02500  0.01566  0.00233  39  SER A O   
193  C CB  . SER A 32  ? 0.31144 0.38384 0.20758 0.03952  0.00663  0.00029  39  SER A CB  
194  O OG  . SER A 32  ? 0.32218 0.41930 0.20801 0.05290  0.00178  0.00790  39  SER A OG  
195  N N   . ASN A 33  ? 0.27958 0.31584 0.20496 0.01413  0.00906  -0.01989 40  ASN A N   
196  C CA  . ASN A 33  ? 0.28617 0.30562 0.21521 0.01382  0.01800  -0.02001 40  ASN A CA  
197  C C   . ASN A 33  ? 0.27248 0.28925 0.22249 0.01187  0.01585  -0.01835 40  ASN A C   
198  O O   . ASN A 33  ? 0.29540 0.30289 0.24538 0.00974  0.01824  -0.02457 40  ASN A O   
199  C CB  . ASN A 33  ? 0.33178 0.33872 0.24117 0.00849  0.02344  -0.03311 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.34341 0.33125 0.25010 0.01391  0.03574  -0.03127 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.37466 0.36679 0.28928 0.02278  0.04081  -0.02034 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.37910 0.34561 0.27093 0.00900  0.04330  -0.04228 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.26560 0.25294 0.20195 -0.00579 -0.03428 -0.02287 41  LYS A N   
204  C CA  . LYS A 34  ? 0.24207 0.25117 0.20603 -0.00265 -0.02621 -0.02144 41  LYS A CA  
205  C C   . LYS A 34  ? 0.23891 0.23775 0.20329 -0.00051 -0.01592 -0.02864 41  LYS A C   
206  O O   . LYS A 34  ? 0.23276 0.24457 0.21484 -0.00029 -0.01334 -0.02810 41  LYS A O   
207  C CB  . LYS A 34  ? 0.25251 0.27090 0.22423 0.00747  -0.01941 -0.01836 41  LYS A CB  
208  C CG  . LYS A 34  ? 0.23721 0.27564 0.21646 0.01034  -0.02732 -0.00803 41  LYS A CG  
209  C CD  . LYS A 34  ? 0.26388 0.30035 0.24164 0.02373  -0.02058 -0.00674 41  LYS A CD  
210  C CE  . LYS A 34  ? 0.25789 0.31583 0.24262 0.03198  -0.02601 0.00499  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.25269 0.34311 0.25932 0.03807  -0.02507 0.01510  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.24838 0.22691 0.19357 0.00300  -0.00976 -0.03309 42  GLU A N   
213  C CA  . GLU A 35  ? 0.24630 0.22304 0.19808 0.00706  0.00123  -0.03549 42  GLU A CA  
214  C C   . GLU A 35  ? 0.25586 0.23127 0.21235 0.00248  -0.00265 -0.03895 42  GLU A C   
215  O O   . GLU A 35  ? 0.25671 0.23548 0.22421 0.00524  0.00472  -0.03981 42  GLU A O   
216  C CB  . GLU A 35  ? 0.28282 0.24315 0.21236 0.01589  0.01092  -0.03539 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.30663 0.23833 0.20080 0.01881  0.00547  -0.04121 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.39345 0.30578 0.25532 0.03445  0.01737  -0.04003 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.46366 0.38349 0.32513 0.03874  0.02428  -0.03374 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.54712 0.43383 0.37953 0.04417  0.01954  -0.04466 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.27054 0.23935 0.21803 -0.00584 -0.01593 -0.03902 43  ILE A N   
222  C CA  . ILE A 36  ? 0.25738 0.22208 0.20799 -0.01199 -0.02120 -0.04023 43  ILE A CA  
223  C C   . ILE A 36  ? 0.22932 0.22055 0.20997 -0.01257 -0.01651 -0.03670 43  ILE A C   
224  O O   . ILE A 36  ? 0.24213 0.23126 0.22695 -0.01569 -0.01758 -0.03742 43  ILE A O   
225  C CB  . ILE A 36  ? 0.30458 0.25692 0.24207 -0.02548 -0.04111 -0.03657 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.29627 0.28092 0.25814 -0.03274 -0.04859 -0.02496 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.34960 0.26034 0.24241 -0.02181 -0.04757 -0.04313 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.31138 0.32490 0.30274 -0.03894 -0.04987 -0.01531 43  ILE A CD1 
229  N N   . PHE A 37  ? 0.20014 0.21110 0.19598 -0.00781 -0.01210 -0.03299 44  PHE A N   
230  C CA  . PHE A 37  ? 0.19733 0.22351 0.20970 -0.00409 -0.00786 -0.03102 44  PHE A CA  
231  C C   . PHE A 37  ? 0.20825 0.22375 0.22134 -0.00214 -0.00214 -0.03663 44  PHE A C   
232  O O   . PHE A 37  ? 0.19898 0.21955 0.21960 -0.00240 -0.00195 -0.03614 44  PHE A O   
233  C CB  . PHE A 37  ? 0.20525 0.23990 0.22086 0.00564  -0.00429 -0.02856 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.19556 0.21440 0.20554 0.00928  -0.00023 -0.03306 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.22127 0.23225 0.22359 0.00860  0.00071  -0.03275 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.20769 0.21945 0.22012 0.01176  0.00077  -0.03517 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.22941 0.23063 0.23201 0.00911  0.00395  -0.03168 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.23301 0.23216 0.24502 0.01023  0.00033  -0.03474 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.21941 0.21598 0.22937 0.00827  0.00250  -0.03151 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.20031 0.20423 0.20703 0.00057  0.00295  -0.03927 45  LEU A N   
241  C CA  . LEU A 38  ? 0.19389 0.19647 0.20917 0.00262  0.00774  -0.03962 45  LEU A CA  
242  C C   . LEU A 38  ? 0.22414 0.21900 0.23441 0.00208  0.00798  -0.04216 45  LEU A C   
243  O O   . LEU A 38  ? 0.21669 0.21467 0.23668 0.00191  0.00812  -0.04203 45  LEU A O   
244  C CB  . LEU A 38  ? 0.20364 0.20517 0.22025 0.00591  0.01410  -0.03541 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.20300 0.21091 0.23605 0.00621  0.01732  -0.02975 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.22335 0.23093 0.26550 0.00146  0.00855  -0.02995 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.23424 0.24933 0.27429 0.00793  0.02369  -0.01918 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.23363 0.21288 0.22388 0.00191  0.00547  -0.04463 46  ARG A N   
249  C CA  . ARG A 39  ? 0.23300 0.19472 0.21016 0.00145  0.00197  -0.04757 46  ARG A CA  
250  C C   . ARG A 39  ? 0.26449 0.23572 0.25465 -0.00803 -0.00580 -0.04525 46  ARG A C   
251  O O   . ARG A 39  ? 0.25465 0.22117 0.24704 -0.00756 -0.00555 -0.04582 46  ARG A O   
252  C CB  . ARG A 39  ? 0.29371 0.22578 0.23713 0.00123  -0.00565 -0.05103 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.35959 0.26315 0.28189 -0.00120 -0.01466 -0.05410 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.44001 0.30500 0.32161 -0.00513 -0.02980 -0.05735 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.48064 0.35960 0.37534 -0.02410 -0.04617 -0.05052 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.52301 0.38109 0.39338 -0.03127 -0.06153 -0.04985 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.55044 0.36473 0.37343 -0.01991 -0.06314 -0.05810 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.51167 0.39231 0.40328 -0.04930 -0.07671 -0.03880 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.21821 0.20635 0.21844 -0.01478 -0.01137 -0.04020 47  GLU A N   
260  C CA  . GLU A 40  ? 0.21183 0.21443 0.22498 -0.02180 -0.01649 -0.03336 47  GLU A CA  
261  C C   . GLU A 40  ? 0.21049 0.22496 0.23626 -0.01496 -0.00884 -0.03362 47  GLU A C   
262  O O   . GLU A 40  ? 0.20216 0.21839 0.23191 -0.01790 -0.01053 -0.03055 47  GLU A O   
263  C CB  . GLU A 40  ? 0.19980 0.22567 0.22393 -0.02674 -0.02171 -0.02310 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.24286 0.25617 0.25439 -0.03758 -0.03523 -0.02025 47  GLU A CG  
265  C CD  . GLU A 40  ? 0.27781 0.26314 0.27290 -0.04978 -0.04901 -0.02014 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.28001 0.27114 0.28525 -0.05520 -0.05084 -0.01459 47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.36640 0.31787 0.33261 -0.05311 -0.05930 -0.02568 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.17507 0.19333 0.20380 -0.00679 -0.00286 -0.03652 48  LEU A N   
269  C CA  . LEU A 41  ? 0.18938 0.20956 0.22237 -0.00118 -0.00048 -0.03724 48  LEU A CA  
270  C C   . LEU A 41  ? 0.19409 0.20382 0.22888 -0.00195 0.00003  -0.04027 48  LEU A C   
271  O O   . LEU A 41  ? 0.19401 0.20374 0.23095 -0.00088 -0.00128 -0.03956 48  LEU A O   
272  C CB  . LEU A 41  ? 0.19199 0.20923 0.22175 0.00540  0.00027  -0.03876 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.20840 0.23672 0.23428 0.01170  0.00129  -0.03449 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.24117 0.25536 0.25611 0.01931  -0.00013 -0.03726 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.21439 0.25689 0.24021 0.01855  0.00382  -0.02789 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.18126 0.18347 0.21438 -0.00097 0.00304  -0.04197 49  ILE A N   
277  C CA  . ILE A 42  ? 0.17929 0.17661 0.21597 0.00230  0.00566  -0.04146 49  ILE A CA  
278  C C   . ILE A 42  ? 0.20241 0.18922 0.23052 0.00034  0.00259  -0.04280 49  ILE A C   
279  O O   . ILE A 42  ? 0.20448 0.19036 0.23762 0.00223  0.00219  -0.04162 49  ILE A O   
280  C CB  . ILE A 42  ? 0.18232 0.17767 0.21678 0.00893  0.01316  -0.03941 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.17397 0.18222 0.22369 0.00740  0.01364  -0.03367 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.22833 0.21971 0.26270 0.01797  0.01880  -0.03663 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.20824 0.22105 0.25748 0.01440  0.02353  -0.02732 49  ILE A CD1 
284  N N   . SER A 43  ? 0.21316 0.19037 0.22807 -0.00534 -0.00243 -0.04358 50  SER A N   
285  C CA  . SER A 43  ? 0.20466 0.16740 0.21017 -0.01100 -0.00953 -0.04241 50  SER A CA  
286  C C   . SER A 43  ? 0.21648 0.19654 0.23662 -0.01555 -0.01118 -0.03667 50  SER A C   
287  O O   . SER A 43  ? 0.22813 0.19998 0.24644 -0.01628 -0.01339 -0.03528 50  SER A O   
288  C CB  . SER A 43  ? 0.26826 0.21749 0.25850 -0.02084 -0.01997 -0.04091 50  SER A CB  
289  O OG  . SER A 43  ? 0.35595 0.28881 0.33744 -0.03116 -0.03159 -0.03662 50  SER A OG  
290  N N   . ASN A 44  ? 0.20302 0.20465 0.23356 -0.01566 -0.00924 -0.03269 51  ASN A N   
291  C CA  . ASN A 44  ? 0.19435 0.21043 0.23160 -0.01411 -0.00794 -0.02646 51  ASN A CA  
292  C C   . ASN A 44  ? 0.20245 0.21093 0.23883 -0.00721 -0.00608 -0.03118 51  ASN A C   
293  O O   . ASN A 44  ? 0.20640 0.21491 0.24196 -0.00711 -0.00717 -0.02754 51  ASN A O   
294  C CB  . ASN A 44  ? 0.19077 0.22690 0.23162 -0.00792 -0.00373 -0.02171 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.26463 0.31855 0.31331 -0.01519 -0.00653 -0.01083 51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.26667 0.31533 0.31687 -0.02858 -0.01512 -0.00589 51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.28062 0.35461 0.33276 -0.00590 -0.00105 -0.00496 51  ASN A ND2 
298  N N   . SER A 45  ? 0.17965 0.18312 0.21766 -0.00273 -0.00476 -0.03669 52  SER A N   
299  C CA  . SER A 45  ? 0.20038 0.19907 0.24175 0.00063  -0.00717 -0.03751 52  SER A CA  
300  C C   . SER A 45  ? 0.20305 0.19486 0.24644 0.00046  -0.00730 -0.03654 52  SER A C   
301  O O   . SER A 45  ? 0.19560 0.18520 0.23962 0.00167  -0.01068 -0.03462 52  SER A O   
302  C CB  . SER A 45  ? 0.19863 0.19767 0.24741 0.00157  -0.00812 -0.03796 52  SER A CB  
303  O OG  . SER A 45  ? 0.19949 0.19631 0.24061 0.00293  -0.01090 -0.03933 52  SER A OG  
304  N N   . SER A 46  ? 0.18293 0.16658 0.22199 0.00122  -0.00426 -0.03800 53  SER A N   
305  C CA  . SER A 46  ? 0.19901 0.16822 0.23161 0.00541  -0.00424 -0.03759 53  SER A CA  
306  C C   . SER A 46  ? 0.22589 0.18767 0.25172 -0.00138 -0.01035 -0.03508 53  SER A C   
307  O O   . SER A 46  ? 0.23432 0.19001 0.26004 0.00180  -0.01203 -0.03312 53  SER A O   
308  C CB  . SER A 46  ? 0.23447 0.18565 0.25009 0.01082  -0.00089 -0.04085 53  SER A CB  
309  O OG  . SER A 46  ? 0.26356 0.19095 0.26282 0.01833  -0.00174 -0.04133 53  SER A OG  
310  N N   . ASP A 47  ? 0.21430 0.17993 0.23706 -0.01097 -0.01391 -0.03202 54  ASP A N   
311  C CA  . ASP A 47  ? 0.21639 0.18151 0.23754 -0.01902 -0.01930 -0.02409 54  ASP A CA  
312  C C   . ASP A 47  ? 0.23330 0.21178 0.26071 -0.01383 -0.01640 -0.02096 54  ASP A C   
313  O O   . ASP A 47  ? 0.23090 0.20294 0.25498 -0.01553 -0.01938 -0.01607 54  ASP A O   
314  C CB  . ASP A 47  ? 0.20905 0.18889 0.23478 -0.02991 -0.02263 -0.01543 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.29473 0.25279 0.30790 -0.03977 -0.03250 -0.01610 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.33066 0.25568 0.32405 -0.03545 -0.03573 -0.02426 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.30824 0.28033 0.32818 -0.05044 -0.03799 -0.00745 54  ASP A OD2 
318  N N   . ALA A 48  ? 0.18867 0.17978 0.21970 -0.00708 -0.01246 -0.02377 55  ALA A N   
319  C CA  . ALA A 48  ? 0.19673 0.19012 0.22279 -0.00031 -0.01280 -0.02243 55  ALA A CA  
320  C C   . ALA A 48  ? 0.20229 0.18396 0.23002 0.00214  -0.01768 -0.02510 55  ALA A C   
321  O O   . ALA A 48  ? 0.20666 0.18424 0.22756 0.00476  -0.02090 -0.02201 55  ALA A O   
322  C CB  . ALA A 48  ? 0.20893 0.20565 0.22903 0.00691  -0.01160 -0.02615 55  ALA A CB  
323  N N   . LEU A 49  ? 0.19308 0.17251 0.23043 0.00312  -0.01774 -0.02872 56  LEU A N   
324  C CA  . LEU A 49  ? 0.20777 0.18425 0.25315 0.00705  -0.02121 -0.02673 56  LEU A CA  
325  C C   . LEU A 49  ? 0.22161 0.18608 0.26055 0.00832  -0.02105 -0.02441 56  LEU A C   
326  O O   . LEU A 49  ? 0.22600 0.18758 0.26617 0.01140  -0.02549 -0.02088 56  LEU A O   
327  C CB  . LEU A 49  ? 0.19644 0.18091 0.25634 0.01038  -0.01779 -0.02599 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.17906 0.17162 0.24609 0.00662  -0.02263 -0.02549 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.20563 0.20890 0.28551 0.00821  -0.01594 -0.02304 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.19460 0.18945 0.27153 0.00492  -0.03451 -0.01897 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.21389 0.16688 0.24296 0.00511  -0.01878 -0.02570 57  ASP A N   
332  C CA  . ASP A 50  ? 0.23773 0.16961 0.25433 0.00493  -0.02240 -0.02313 57  ASP A CA  
333  C C   . ASP A 50  ? 0.24600 0.18115 0.26061 -0.00089 -0.02660 -0.01648 57  ASP A C   
334  O O   . ASP A 50  ? 0.26338 0.18559 0.27231 0.00164  -0.03030 -0.01312 57  ASP A O   
335  C CB  . ASP A 50  ? 0.25373 0.16547 0.25426 -0.00237 -0.02552 -0.02436 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.28390 0.18035 0.27339 0.00698  -0.02164 -0.03108 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.31396 0.21904 0.31145 0.02075  -0.01386 -0.03236 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.33313 0.20803 0.30409 -0.00019 -0.02772 -0.03284 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.22698 0.17968 0.24412 -0.00584 -0.02474 -0.01314 58  LYS A N   
340  C CA  . LYS A 51  ? 0.23947 0.19751 0.25139 -0.00798 -0.02558 -0.00376 58  LYS A CA  
341  C C   . LYS A 51  ? 0.23799 0.19322 0.24562 0.00086  -0.02821 -0.00520 58  LYS A C   
342  O O   . LYS A 51  ? 0.27436 0.22220 0.27506 0.00082  -0.03117 0.00114  58  LYS A O   
343  C CB  . LYS A 51  ? 0.25214 0.23258 0.26539 -0.00882 -0.01957 0.00231  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.25032 0.23917 0.27113 -0.02125 -0.02028 0.01082  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.23875 0.25720 0.26485 -0.01691 -0.01186 0.01873  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.28751 0.31823 0.32655 -0.03052 -0.01521 0.02754  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.32526 0.39157 0.37336 -0.02348 -0.00543 0.03902  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.23365 0.19206 0.24443 0.00672  -0.02998 -0.01193 59  ILE A N   
349  C CA  . ILE A 52  ? 0.23998 0.19190 0.24568 0.01199  -0.03822 -0.01161 59  ILE A CA  
350  C C   . ILE A 52  ? 0.25538 0.20209 0.27277 0.01364  -0.04229 -0.00957 59  ILE A C   
351  O O   . ILE A 52  ? 0.27396 0.21395 0.28579 0.01634  -0.04878 -0.00529 59  ILE A O   
352  C CB  . ILE A 52  ? 0.25873 0.21000 0.26124 0.01436  -0.04457 -0.01647 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.26950 0.20693 0.25786 0.01754  -0.05847 -0.01489 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.26009 0.21988 0.28551 0.01129  -0.04560 -0.01853 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.34610 0.27288 0.30400 0.02477  -0.05641 -0.01188 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.23587 0.18382 0.26519 0.01487  -0.03753 -0.01151 60  ARG A N   
357  C CA  . ARG A 53  ? 0.24581 0.18751 0.28119 0.02267  -0.03832 -0.00787 60  ARG A CA  
358  C C   . ARG A 53  ? 0.26563 0.18774 0.28451 0.02174  -0.04043 -0.00455 60  ARG A C   
359  O O   . ARG A 53  ? 0.29504 0.21159 0.31362 0.02757  -0.04535 0.00042  60  ARG A O   
360  C CB  . ARG A 53  ? 0.28936 0.23093 0.33051 0.02959  -0.03012 -0.01020 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.36449 0.29843 0.40677 0.04441  -0.02819 -0.00495 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.44295 0.37579 0.48471 0.05719  -0.01780 -0.00584 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.48509 0.45184 0.55669 0.06304  -0.01348 0.00244  60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.56220 0.53657 0.63641 0.07133  -0.00265 0.00285  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.46519 0.41294 0.51126 0.07260  0.00232  -0.00747 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.43945 0.44907 0.54504 0.07738  0.00175  0.01609  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.27188 0.18380 0.27811 0.01278  -0.03852 -0.00467 61  TYR A N   
368  C CA  . TYR A 54  ? 0.29515 0.18688 0.28690 0.00833  -0.04312 0.00190  61  TYR A CA  
369  C C   . TYR A 54  ? 0.33816 0.23707 0.32702 0.00828  -0.04627 0.00884  61  TYR A C   
370  O O   . TYR A 54  ? 0.34684 0.23092 0.32828 0.01149  -0.05124 0.01387  61  TYR A O   
371  C CB  . TYR A 54  ? 0.30392 0.18952 0.28845 -0.00606 -0.04414 0.00567  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.34085 0.20217 0.31109 -0.01467 -0.05251 0.01579  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.36504 0.18696 0.31651 -0.01045 -0.05967 0.01319  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.33249 0.20913 0.30534 -0.02458 -0.05280 0.02945  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.39843 0.19203 0.33367 -0.01954 -0.07022 0.02303  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.36115 0.21819 0.32366 -0.03491 -0.06141 0.04251  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.39438 0.20752 0.33802 -0.03426 -0.07184 0.03875  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.43508 0.22140 0.36487 -0.04595 -0.08349 0.05196  61  TYR A OH  
379  N N   . GLU A 55  ? 0.30701 0.22440 0.29642 0.00731  -0.04362 0.00902  62  GLU A N   
380  C CA  . GLU A 55  ? 0.33884 0.25706 0.31555 0.01074  -0.04629 0.01526  62  GLU A CA  
381  C C   . GLU A 55  ? 0.37442 0.28542 0.35283 0.01843  -0.05554 0.01320  62  GLU A C   
382  O O   . GLU A 55  ? 0.39420 0.29614 0.36113 0.02116  -0.06078 0.01944  62  GLU A O   
383  C CB  . GLU A 55  ? 0.31898 0.25022 0.28605 0.01453  -0.04181 0.01414  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.33184 0.27855 0.29902 0.00898  -0.03164 0.02382  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.43066 0.38992 0.38236 0.01955  -0.02390 0.02600  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.45216 0.39917 0.38763 0.02960  -0.02918 0.01648  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.46381 0.44413 0.41779 0.01861  -0.01355 0.03940  62  GLU A OE2 
388  N N   . SER A 56  ? 0.31249 0.23037 0.30747 0.02150  -0.05833 0.00744  63  SER A N   
389  C CA  . SER A 56  ? 0.32173 0.24097 0.32634 0.02702  -0.06907 0.01065  63  SER A CA  
390  C C   . SER A 56  ? 0.34506 0.25571 0.35417 0.03373  -0.06930 0.01637  63  SER A C   
391  O O   . SER A 56  ? 0.35602 0.26914 0.37198 0.03911  -0.07868 0.02267  63  SER A O   
392  C CB  . SER A 56  ? 0.31236 0.24821 0.33975 0.02687  -0.07193 0.00891  63  SER A CB  
393  O OG  . SER A 56  ? 0.34334 0.28677 0.38864 0.03273  -0.06224 0.00966  63  SER A OG  
394  N N   . LEU A 57  ? 0.34908 0.24627 0.35223 0.03434  -0.06145 0.01509  64  LEU A N   
395  C CA  . LEU A 57  ? 0.37303 0.25284 0.37237 0.04465  -0.06248 0.01954  64  LEU A CA  
396  C C   . LEU A 57  ? 0.43079 0.29739 0.41591 0.04350  -0.07016 0.02677  64  LEU A C   
397  O O   . LEU A 57  ? 0.51033 0.36650 0.49473 0.05441  -0.07401 0.03219  64  LEU A O   
398  C CB  . LEU A 57  ? 0.38720 0.24050 0.37009 0.04438  -0.05714 0.01564  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.38479 0.24509 0.37530 0.04930  -0.04880 0.00852  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.41475 0.23661 0.37783 0.04894  -0.04869 0.00440  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.43653 0.31635 0.44742 0.06717  -0.04427 0.01217  64  LEU A CD2 
402  N N   . THR A 58  ? 0.40359 0.27066 0.37569 0.03300  -0.07106 0.02870  65  THR A N   
403  C CA  . THR A 58  ? 0.44867 0.30443 0.40453 0.03278  -0.07712 0.03748  65  THR A CA  
404  C C   . THR A 58  ? 0.50748 0.37370 0.45609 0.03440  -0.08340 0.03831  65  THR A C   
405  O O   . THR A 58  ? 0.57720 0.43351 0.50901 0.03669  -0.08920 0.04553  65  THR A O   
406  C CB  . THR A 58  ? 0.50500 0.34947 0.44573 0.02145  -0.07307 0.04491  65  THR A CB  
407  O OG1 . THR A 58  ? 0.56157 0.42584 0.50355 0.01451  -0.06544 0.04419  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.47771 0.29756 0.41523 0.01771  -0.07380 0.04462  65  THR A CG2 
409  N N   . ASP A 59  ? 0.50955 0.35653 0.34220 0.07273  -0.06145 0.07386  66  ASP A N   
410  C CA  . ASP A 59  ? 0.48726 0.37657 0.33291 0.07501  -0.07213 0.07170  66  ASP A CA  
411  C C   . ASP A 59  ? 0.45968 0.37754 0.33701 0.07964  -0.07688 0.06049  66  ASP A C   
412  O O   . ASP A 59  ? 0.44184 0.37198 0.32897 0.06850  -0.07524 0.04814  66  ASP A O   
413  C CB  . ASP A 59  ? 0.46690 0.36824 0.30128 0.05864  -0.07041 0.06943  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.56349 0.49430 0.39604 0.06393  -0.07951 0.06537  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.54138 0.48283 0.38239 0.07471  -0.09136 0.06447  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.58990 0.53115 0.40931 0.05796  -0.07509 0.06534  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.49643 0.42782 0.39291 0.09583  -0.08270 0.06750  67  PRO A N   
418  C CA  . PRO A 60  ? 0.43076 0.39161 0.36168 0.09719  -0.08697 0.06101  67  PRO A CA  
419  C C   . PRO A 60  ? 0.40563 0.39200 0.34028 0.08440  -0.10150 0.05032  67  PRO A C   
420  O O   . PRO A 60  ? 0.41666 0.41986 0.37372 0.07859  -0.10415 0.04173  67  PRO A O   
421  C CB  . PRO A 60  ? 0.47742 0.45735 0.43090 0.11702  -0.09247 0.07858  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.61236 0.56135 0.53998 0.12996  -0.08563 0.09174  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.56817 0.48504 0.45812 0.11452  -0.08142 0.08488  67  PRO A CD  
424  N N   . SER A 61  ? 0.42670 0.41073 0.33418 0.08083  -0.10988 0.05080  68  SER A N   
425  C CA  . SER A 61  ? 0.43917 0.43421 0.33667 0.07199  -0.12236 0.03937  68  SER A CA  
426  C C   . SER A 61  ? 0.41383 0.40373 0.30885 0.06266  -0.11056 0.02498  68  SER A C   
427  O O   . SER A 61  ? 0.41015 0.40296 0.29646 0.05777  -0.11807 0.01405  68  SER A O   
428  C CB  . SER A 61  ? 0.48377 0.47081 0.34264 0.07389  -0.13062 0.04275  68  SER A CB  
429  O OG  . SER A 61  ? 0.54238 0.51479 0.37805 0.07282  -0.11358 0.04385  68  SER A OG  
430  N N   . LYS A 62  ? 0.37287 0.35179 0.27185 0.05961  -0.09362 0.02579  69  LYS A N   
431  C CA  . LYS A 62  ? 0.37696 0.35747 0.27959 0.05046  -0.08416 0.01570  69  LYS A CA  
432  C C   . LYS A 62  ? 0.32978 0.32163 0.25781 0.04804  -0.08872 0.00553  69  LYS A C   
433  O O   . LYS A 62  ? 0.33649 0.33136 0.26622 0.04213  -0.08425 -0.00372 69  LYS A O   
434  C CB  . LYS A 62  ? 0.41655 0.38130 0.31870 0.04365  -0.07074 0.02122  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.46473 0.41864 0.34297 0.04013  -0.06602 0.03406  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.48216 0.45173 0.35434 0.03213  -0.05880 0.03570  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.51805 0.48558 0.37145 0.02683  -0.05304 0.05351  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.49685 0.49083 0.35366 0.02115  -0.04305 0.05959  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.32746 0.32822 0.27833 0.05329  -0.09581 0.01023  70  LEU A N   
440  C CA  . LEU A 63  ? 0.31207 0.32837 0.29124 0.04985  -0.10011 0.00522  70  LEU A CA  
441  C C   . LEU A 63  ? 0.29892 0.32978 0.28159 0.04520  -0.12184 0.00471  70  LEU A C   
442  O O   . LEU A 63  ? 0.35997 0.40709 0.36971 0.03964  -0.12888 0.00498  70  LEU A O   
443  C CB  . LEU A 63  ? 0.31854 0.34015 0.32421 0.05932  -0.09150 0.01498  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.34387 0.33751 0.33584 0.06121  -0.07221 0.01334  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.39197 0.38167 0.39929 0.07698  -0.06099 0.02303  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.32961 0.31960 0.31926 0.04850  -0.06671 0.00094  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.34881 0.37063 0.30025 0.04505  -0.13314 0.00399  71  ASP A N   
448  C CA  . ASP A 64  ? 0.37707 0.40121 0.31895 0.03657  -0.15794 0.00173  71  ASP A CA  
449  C C   . ASP A 64  ? 0.39110 0.40337 0.32601 0.02648  -0.15992 -0.01333 71  ASP A C   
450  O O   . ASP A 64  ? 0.42412 0.43601 0.35931 0.01433  -0.18156 -0.01487 71  ASP A O   
451  C CB  . ASP A 64  ? 0.43902 0.44436 0.33384 0.04004  -0.16699 0.00127  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.51514 0.53331 0.41607 0.04778  -0.17414 0.01885  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.46108 0.50248 0.40327 0.05262  -0.17127 0.03186  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.55395 0.55755 0.41647 0.05219  -0.17933 0.02105  71  ASP A OD2 
455  N N   . SER A 65  ? 0.35589 0.35663 0.28159 0.03018  -0.13942 -0.02259 72  SER A N   
456  C CA  . SER A 65  ? 0.35365 0.34243 0.27339 0.02483  -0.13675 -0.03506 72  SER A CA  
457  C C   . SER A 65  ? 0.40243 0.40870 0.36475 0.01794  -0.13348 -0.03369 72  SER A C   
458  O O   . SER A 65  ? 0.42347 0.42087 0.38453 0.01397  -0.12897 -0.04252 72  SER A O   
459  C CB  . SER A 65  ? 0.38039 0.35828 0.27659 0.03405  -0.11544 -0.03975 72  SER A CB  
460  O OG  . SER A 65  ? 0.35014 0.34242 0.26582 0.03660  -0.09963 -0.03083 72  SER A OG  
461  N N   . GLY A 66  ? 0.33571 0.36584 0.33414 0.01949  -0.13272 -0.02124 73  GLY A N   
462  C CA  . GLY A 66  ? 0.35551 0.40209 0.39086 0.01613  -0.12623 -0.01817 73  GLY A CA  
463  C C   . GLY A 66  ? 0.31481 0.37285 0.37136 0.02805  -0.11020 -0.00705 73  GLY A C   
464  O O   . GLY A 66  ? 0.28684 0.32824 0.32668 0.03356  -0.09464 -0.01050 73  GLY A O   
465  N N   . LYS A 67  ? 0.29284 0.37724 0.38362 0.03250  -0.11356 0.00831  74  LYS A N   
466  C CA  . LYS A 67  ? 0.25516 0.34132 0.35658 0.04989  -0.09534 0.01943  74  LYS A CA  
467  C C   . LYS A 67  ? 0.25476 0.33424 0.36456 0.05349  -0.07543 0.01614  74  LYS A C   
468  O O   . LYS A 67  ? 0.30973 0.36946 0.40710 0.06705  -0.05773 0.01888  74  LYS A O   
469  C CB  . LYS A 67  ? 0.31188 0.43390 0.44847 0.06000  -0.10269 0.04252  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.44658 0.56518 0.56695 0.06749  -0.11189 0.05019  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.57542 0.73919 0.73357 0.06984  -0.12974 0.07429  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.68830 0.85126 0.82553 0.06194  -0.15477 0.07626  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.84697 1.04209 1.00991 0.07859  -0.15949 0.10398  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.21989 0.31018 0.34538 0.04184  -0.07867 0.01111  75  GLU A N   
475  C CA  . GLU A 68  ? 0.21675 0.30362 0.35094 0.04669  -0.05982 0.01093  75  GLU A CA  
476  C C   . GLU A 68  ? 0.22396 0.27632 0.32371 0.04148  -0.05012 -0.00533 75  GLU A C   
477  O O   . GLU A 68  ? 0.25470 0.29995 0.33944 0.03008  -0.05907 -0.01603 75  GLU A O   
478  C CB  . GLU A 68  ? 0.29716 0.40784 0.46021 0.03414  -0.06766 0.01324  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.36554 0.52069 0.57343 0.03435  -0.07804 0.03565  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.97540 1.14289 1.18468 0.02491  -0.10442 0.04074  75  GLU A CD  
481  O OE1 . GLU A 68  ? 1.01021 1.15184 1.18761 0.01145  -0.11894 0.02393  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.88544 1.08800 1.12518 0.03258  -0.11005 0.06302  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.23393 0.26518 0.31994 0.05049  -0.03232 -0.00483 76  LEU A N   
484  C CA  . LEU A 69  ? 0.21472 0.21345 0.26758 0.04255  -0.02554 -0.01597 76  LEU A CA  
485  C C   . LEU A 69  ? 0.21179 0.20722 0.26819 0.04199  -0.01469 -0.01792 76  LEU A C   
486  O O   . LEU A 69  ? 0.23988 0.22384 0.29187 0.05629  0.00020  -0.01151 76  LEU A O   
487  C CB  . LEU A 69  ? 0.27167 0.23523 0.29227 0.05083  -0.01764 -0.01310 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.31517 0.28066 0.33004 0.05189  -0.02742 -0.00922 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.44453 0.36505 0.42061 0.05587  -0.01953 -0.00688 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.28292 0.25947 0.29428 0.03645  -0.03942 -0.01613 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.19168 0.19716 0.25493 0.02830  -0.02095 -0.02535 77  HIS A N   
492  C CA  . HIS A 70  ? 0.19473 0.20159 0.26481 0.02716  -0.01231 -0.02563 77  HIS A CA  
493  C C   . HIS A 70  ? 0.17736 0.18150 0.23916 0.01288  -0.01758 -0.03432 77  HIS A C   
494  O O   . HIS A 70  ? 0.18057 0.18701 0.23581 0.00606  -0.02670 -0.03865 77  HIS A O   
495  C CB  . HIS A 70  ? 0.18140 0.22211 0.29158 0.03060  -0.01421 -0.01576 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.17231 0.23110 0.29898 0.01778  -0.03327 -0.01868 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.25360 0.33433 0.40175 0.01750  -0.04623 -0.01001 77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.22362 0.27596 0.34182 0.00607  -0.04191 -0.02862 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.25247 0.33227 0.39808 0.00408  -0.06342 -0.01674 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.24569 0.30764 0.37357 -0.00088 -0.05941 -0.02791 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.18593 0.18682 0.24779 0.01109  -0.00995 -0.03448 78  ILE A N   
502  C CA  . ILE A 71  ? 0.18121 0.18236 0.23846 0.00024  -0.01307 -0.03921 78  ILE A CA  
503  C C   . ILE A 71  ? 0.17931 0.19538 0.25994 -0.00009 -0.01084 -0.03630 78  ILE A C   
504  O O   . ILE A 71  ? 0.18182 0.19890 0.26891 0.00707  0.00019  -0.02986 78  ILE A O   
505  C CB  . ILE A 71  ? 0.20346 0.17852 0.22833 -0.00497 -0.00760 -0.04034 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.22792 0.18471 0.22817 -0.00941 -0.01199 -0.04056 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.21721 0.19976 0.24221 -0.01538 -0.01137 -0.04104 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.26674 0.18641 0.22569 -0.01908 -0.01077 -0.04052 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.15992 0.18494 0.25054 -0.00676 -0.01986 -0.03934 79  ASN A N   
510  C CA  . ASN A 72  ? 0.14710 0.18040 0.25635 -0.01046 -0.02000 -0.03582 79  ASN A CA  
511  C C   . ASN A 72  ? 0.16801 0.19318 0.26456 -0.01452 -0.01857 -0.03882 79  ASN A C   
512  O O   . ASN A 72  ? 0.17134 0.19302 0.25429 -0.01488 -0.02260 -0.04268 79  ASN A O   
513  C CB  . ASN A 72  ? 0.14665 0.18695 0.27144 -0.01584 -0.03429 -0.03582 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.15490 0.21132 0.29875 -0.01396 -0.03879 -0.02830 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.16998 0.23808 0.32581 -0.00595 -0.02732 -0.01915 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.21007 0.26618 0.35446 -0.01983 -0.05565 -0.03036 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.16022 0.18603 0.26277 -0.01615 -0.01174 -0.03398 80  LEU A N   
518  C CA  . LEU A 73  ? 0.14276 0.16302 0.23558 -0.01925 -0.01094 -0.03403 80  LEU A CA  
519  C C   . LEU A 73  ? 0.14478 0.16573 0.25402 -0.02297 -0.01484 -0.03101 80  LEU A C   
520  O O   . LEU A 73  ? 0.15673 0.18589 0.28473 -0.02573 -0.01134 -0.02346 80  LEU A O   
521  C CB  . LEU A 73  ? 0.17247 0.18550 0.24981 -0.01943 -0.00082 -0.03026 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.19614 0.19575 0.24854 -0.01861 0.00175  -0.03285 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.22858 0.20927 0.25455 -0.01897 0.01081  -0.03013 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.19940 0.20111 0.24129 -0.02461 -0.00824 -0.03503 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.16787 0.17885 0.26901 -0.02247 -0.02174 -0.03479 81  ILE A N   
526  C CA  . ILE A 74  ? 0.18512 0.18303 0.29179 -0.02765 -0.02904 -0.03370 81  ILE A CA  
527  C C   . ILE A 74  ? 0.21321 0.19862 0.30784 -0.02373 -0.02549 -0.03153 81  ILE A C   
528  O O   . ILE A 74  ? 0.21662 0.19109 0.29376 -0.01428 -0.02642 -0.03494 81  ILE A O   
529  C CB  . ILE A 74  ? 0.21125 0.19348 0.30807 -0.02844 -0.04216 -0.04100 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.21023 0.20905 0.31816 -0.02997 -0.04574 -0.04148 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.22934 0.18771 0.32462 -0.03921 -0.05356 -0.03936 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.24845 0.23125 0.34156 -0.03135 -0.06017 -0.04839 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.20962 0.19675 0.31304 -0.02857 -0.02020 -0.02355 82  PRO A N   
534  C CA  . PRO A 75  ? 0.21893 0.19282 0.31168 -0.02466 -0.01760 -0.01925 82  PRO A CA  
535  C C   . PRO A 75  ? 0.26085 0.20429 0.34755 -0.02908 -0.02656 -0.02009 82  PRO A C   
536  O O   . PRO A 75  ? 0.27696 0.21664 0.37659 -0.04267 -0.03475 -0.01820 82  PRO A O   
537  C CB  . PRO A 75  ? 0.23454 0.22093 0.33673 -0.02961 -0.00833 -0.00971 82  PRO A CB  
538  C CG  . PRO A 75  ? 0.24420 0.24354 0.36685 -0.03694 -0.00668 -0.00637 82  PRO A CG  
539  C CD  . PRO A 75  ? 0.26044 0.26367 0.38421 -0.03535 -0.01415 -0.01543 82  PRO A CD  
540  N N   . ASN A 76  ? 0.26057 0.18041 0.32551 -0.01774 -0.02565 -0.02070 83  ASN A N   
541  C CA  . ASN A 76  ? 0.30308 0.17820 0.34884 -0.02047 -0.03377 -0.02199 83  ASN A CA  
542  C C   . ASN A 76  ? 0.33262 0.19365 0.36638 -0.00910 -0.02562 -0.01375 83  ASN A C   
543  O O   . ASN A 76  ? 0.34145 0.19962 0.35834 0.01185  -0.01852 -0.01316 83  ASN A O   
544  C CB  . ASN A 76  ? 0.35093 0.19294 0.36630 -0.01235 -0.04160 -0.03381 83  ASN A CB  
545  C CG  . ASN A 76  ? 0.42462 0.20572 0.40858 -0.01931 -0.05361 -0.03680 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.46904 0.22276 0.43869 -0.01399 -0.04953 -0.03113 83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.53783 0.29721 0.51208 -0.03548 -0.07086 -0.04360 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.32269 0.20368 0.37337 -0.02151 0.01517  0.04693  84  LYS A N   
549  C CA  . LYS A 77  ? 0.35491 0.21767 0.39141 -0.01107 0.02154  0.05325  84  LYS A CA  
550  C C   . LYS A 77  ? 0.40757 0.23375 0.43476 -0.01566 0.01789  0.04942  84  LYS A C   
551  O O   . LYS A 77  ? 0.44478 0.25507 0.45700 -0.00230 0.02191  0.05093  84  LYS A O   
552  C CB  . LYS A 77  ? 0.37045 0.24068 0.41481 -0.01073 0.03247  0.07252  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.37775 0.27517 0.41848 0.00113  0.04023  0.07658  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.39514 0.29899 0.44027 0.00407  0.05398  0.09717  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.42214 0.34682 0.45853 0.01654  0.06373  0.10070  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.50168 0.44852 0.56023 0.00979  0.06412  0.10079  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.42962 0.24024 0.46221 -0.03336 0.00986  0.04431  85  GLN A N   
558  C CA  . GLN A 78  ? 0.48071 0.24596 0.49570 -0.03703 0.00736  0.03915  85  GLN A CA  
559  C C   . GLN A 78  ? 0.46661 0.21924 0.46076 -0.02224 0.00584  0.02359  85  GLN A C   
560  O O   . GLN A 78  ? 0.53757 0.25741 0.51273 -0.01112 0.01071  0.02244  85  GLN A O   
561  C CB  . GLN A 78  ? 0.57205 0.31862 0.59273 -0.06307 -0.00316 0.03757  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.78970 0.54402 0.83375 -0.08067 -0.00169 0.05677  85  GLN A CG  
563  C CD  . GLN A 78  ? 0.97662 0.78366 1.04858 -0.07823 0.00379  0.06927  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.02338 0.84303 1.10826 -0.07612 0.01433  0.08744  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.77436 0.61010 0.85360 -0.07724 -0.00188 0.06055  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.41134 0.19011 0.40958 -0.02040 0.00083  0.01376  86  ASP A N   
567  C CA  . ASP A 79  ? 0.41718 0.19079 0.39974 -0.00668 0.00039  0.00139  86  ASP A CA  
568  C C   . ASP A 79  ? 0.38834 0.19072 0.37421 0.01153  0.00548  0.00565  86  ASP A C   
569  O O   . ASP A 79  ? 0.41660 0.22055 0.39425 0.02452  0.00648  0.00011  86  ASP A O   
570  C CB  . ASP A 79  ? 0.53335 0.32068 0.51840 -0.01555 -0.00845 -0.01042 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.59583 0.35629 0.57406 -0.03585 -0.01791 -0.01623 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.65046 0.37242 0.61626 -0.04298 -0.01781 -0.01442 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.63409 0.41276 0.61936 -0.04599 -0.02661 -0.02165 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.36371 0.18822 0.36003 0.01208  0.00843  0.01623  87  ARG A N   
575  C CA  . ARG A 80  ? 0.32214 0.17187 0.31694 0.02560  0.00999  0.01974  87  ARG A CA  
576  C C   . ARG A 80  ? 0.32346 0.19504 0.32045 0.02622  0.00424  0.00923  87  ARG A C   
577  O O   . ARG A 80  ? 0.32164 0.20495 0.31486 0.03659  0.00257  0.00813  87  ARG A O   
578  C CB  . ARG A 80  ? 0.37378 0.21459 0.35907 0.04142  0.01411  0.02728  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.36038 0.22568 0.34358 0.04907  0.01375  0.03594  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.60093 0.47478 0.57945 0.06405  0.01241  0.04174  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.54751 0.39608 0.52152 0.07293  0.01965  0.05088  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.72410 0.57100 0.69599 0.08909  0.02218  0.05777  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.54614 0.41923 0.52397 0.09681  0.01725  0.05700  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.63799 0.45749 0.60309 0.09824  0.03053  0.06798  87  ARG A NH2 
585  N N   . THR A 81  ? 0.30499 0.18448 0.31018 0.01469  0.00091  0.00368  88  THR A N   
586  C CA  . THR A 81  ? 0.28247 0.17977 0.28938 0.01465  -0.00375 -0.00525 88  THR A CA  
587  C C   . THR A 81  ? 0.26903 0.18508 0.28283 0.01017  -0.00304 -0.00310 88  THR A C   
588  O O   . THR A 81  ? 0.26392 0.18147 0.28678 0.00361  0.00025  0.00394  88  THR A O   
589  C CB  . THR A 81  ? 0.28013 0.16794 0.28623 0.00850  -0.00836 -0.01528 88  THR A CB  
590  O OG1 . THR A 81  ? 0.31259 0.19276 0.32584 -0.00585 -0.01116 -0.01398 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.30928 0.17536 0.30259 0.01746  -0.00627 -0.01865 88  THR A CG2 
592  N N   . LEU A 82  ? 0.23161 0.16129 0.24105 0.01420  -0.00517 -0.00758 89  LEU A N   
593  C CA  . LEU A 82  ? 0.22373 0.16519 0.23540 0.01208  -0.00339 -0.00766 89  LEU A CA  
594  C C   . LEU A 82  ? 0.22407 0.17189 0.23905 0.00911  -0.00870 -0.01667 89  LEU A C   
595  O O   . LEU A 82  ? 0.23807 0.18750 0.24742 0.01221  -0.01270 -0.02185 89  LEU A O   
596  C CB  . LEU A 82  ? 0.25053 0.19436 0.24616 0.01887  -0.00134 -0.00580 89  LEU A CB  
597  C CG  . LEU A 82  ? 0.22572 0.17353 0.21580 0.02000  0.00281  -0.00702 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.24553 0.19819 0.24759 0.02006  0.01258  0.00288  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.26538 0.20540 0.22979 0.02550  0.00315  -0.00761 89  LEU A CD2 
600  N N   . THR A 83  ? 0.21227 0.16643 0.23814 0.00316  -0.00889 -0.01643 90  THR A N   
601  C CA  . THR A 83  ? 0.20287 0.16272 0.23091 0.00063  -0.01385 -0.02351 90  THR A CA  
602  C C   . THR A 83  ? 0.21949 0.18979 0.24883 0.00325  -0.01034 -0.02156 90  THR A C   
603  O O   . THR A 83  ? 0.22112 0.19796 0.25776 0.00441  -0.00407 -0.01309 90  THR A O   
604  C CB  . THR A 83  ? 0.22112 0.17861 0.25775 -0.00874 -0.01916 -0.02441 90  THR A CB  
605  O OG1 . THR A 83  ? 0.24705 0.18539 0.27576 -0.00992 -0.02102 -0.02746 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.26048 0.22413 0.29637 -0.01054 -0.02436 -0.03069 90  THR A CG2 
607  N N   . ILE A 84  ? 0.20960 0.18063 0.23167 0.00541  -0.01262 -0.02755 91  ILE A N   
608  C CA  . ILE A 84  ? 0.19761 0.17147 0.21656 0.00874  -0.00887 -0.02665 91  ILE A CA  
609  C C   . ILE A 84  ? 0.21550 0.19786 0.24353 0.00547  -0.01303 -0.02855 91  ILE A C   
610  O O   . ILE A 84  ? 0.21440 0.19527 0.23852 0.00368  -0.01804 -0.03465 91  ILE A O   
611  C CB  . ILE A 84  ? 0.22162 0.18501 0.22186 0.01154  -0.00914 -0.03099 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.28466 0.23919 0.27149 0.01464  -0.00654 -0.02846 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.24364 0.20150 0.23615 0.01541  -0.00412 -0.03070 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.33566 0.29104 0.32140 0.01272  -0.01293 -0.02936 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.18680 0.18068 0.22770 0.00529  -0.01092 -0.02154 92  VAL A N   
616  C CA  . VAL A 85  ? 0.17554 0.17966 0.22443 0.00169  -0.01672 -0.02162 92  VAL A CA  
617  C C   . VAL A 85  ? 0.19143 0.19895 0.23927 0.00945  -0.01058 -0.01731 92  VAL A C   
618  O O   . VAL A 85  ? 0.21435 0.22441 0.26529 0.01674  -0.00138 -0.00908 92  VAL A O   
619  C CB  . VAL A 85  ? 0.19348 0.21204 0.26061 -0.00615 -0.02167 -0.01375 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.23222 0.26027 0.30235 -0.01084 -0.03060 -0.01451 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.22784 0.23529 0.29274 -0.01427 -0.02656 -0.01744 92  VAL A CG2 
622  N N   A ASP A 86  ? 0.18852 0.19516 0.23140 0.00940  -0.01398 -0.02120 93  ASP A N   
623  N N   B ASP A 86  ? 0.18852 0.19516 0.23140 0.00940  -0.01398 -0.02120 93  ASP A N   
624  C CA  A ASP A 86  ? 0.18233 0.19083 0.22517 0.01708  -0.00803 -0.01519 93  ASP A CA  
625  C CA  B ASP A 86  ? 0.18233 0.19083 0.22517 0.01708  -0.00803 -0.01519 93  ASP A CA  
626  C C   A ASP A 86  ? 0.18606 0.20792 0.23621 0.01422  -0.01505 -0.01295 93  ASP A C   
627  C C   B ASP A 86  ? 0.18606 0.20792 0.23621 0.01422  -0.01505 -0.01295 93  ASP A C   
628  O O   A ASP A 86  ? 0.18583 0.20838 0.23294 0.00694  -0.02363 -0.01936 93  ASP A O   
629  O O   B ASP A 86  ? 0.18583 0.20838 0.23294 0.00694  -0.02363 -0.01936 93  ASP A O   
630  C CB  A ASP A 86  ? 0.21685 0.20285 0.23920 0.02115  -0.00298 -0.02088 93  ASP A CB  
631  C CB  B ASP A 86  ? 0.21685 0.20285 0.23920 0.02115  -0.00298 -0.02088 93  ASP A CB  
632  C CG  A ASP A 86  ? 0.24570 0.22774 0.26188 0.01454  -0.01002 -0.02831 93  ASP A CG  
633  C CG  B ASP A 86  ? 0.24570 0.22774 0.26188 0.01454  -0.01002 -0.02831 93  ASP A CG  
634  O OD1 A ASP A 86  ? 0.22398 0.21324 0.24388 0.01408  -0.01257 -0.02662 93  ASP A OD1 
635  O OD1 B ASP A 86  ? 0.22398 0.21324 0.24388 0.01408  -0.01257 -0.02662 93  ASP A OD1 
636  O OD2 A ASP A 86  ? 0.24210 0.21563 0.25007 0.01034  -0.01266 -0.03415 93  ASP A OD2 
637  O OD2 B ASP A 86  ? 0.24210 0.21563 0.25007 0.01034  -0.01266 -0.03415 93  ASP A OD2 
638  N N   . THR A 87  ? 0.16826 0.19946 0.22552 0.02162  -0.01056 -0.00294 94  THR A N   
639  C CA  . THR A 87  ? 0.16886 0.21351 0.23105 0.02029  -0.01731 0.00124  94  THR A CA  
640  C C   . THR A 87  ? 0.20057 0.23110 0.24944 0.02700  -0.01178 0.00034  94  THR A C   
641  O O   . THR A 87  ? 0.19297 0.23197 0.24605 0.03341  -0.01018 0.00974  94  THR A O   
642  C CB  . THR A 87  ? 0.17477 0.24613 0.25872 0.02322  -0.01830 0.01697  94  THR A CB  
643  O OG1 . THR A 87  ? 0.17803 0.24803 0.26674 0.03740  -0.00315 0.02713  94  THR A OG1 
644  C CG2 . THR A 87  ? 0.18795 0.27489 0.28711 0.01084  -0.02794 0.01896  94  THR A CG2 
645  N N   . GLY A 88  ? 0.19605 0.20508 0.22932 0.02477  -0.00935 -0.00948 95  GLY A N   
646  C CA  . GLY A 88  ? 0.23050 0.22396 0.25155 0.02721  -0.00549 -0.00991 95  GLY A CA  
647  C C   . GLY A 88  ? 0.21373 0.21572 0.23416 0.02267  -0.01186 -0.01082 95  GLY A C   
648  O O   . GLY A 88  ? 0.20379 0.22272 0.22998 0.02007  -0.01915 -0.00986 95  GLY A O   
649  N N   . ILE A 89  ? 0.20748 0.19517 0.21810 0.02101  -0.00907 -0.01215 96  ILE A N   
650  C CA  . ILE A 89  ? 0.22323 0.21850 0.23206 0.01937  -0.01154 -0.00976 96  ILE A CA  
651  C C   . ILE A 89  ? 0.22431 0.22957 0.23270 0.01420  -0.01710 -0.01636 96  ILE A C   
652  O O   . ILE A 89  ? 0.23610 0.24927 0.23974 0.01520  -0.01891 -0.01464 96  ILE A O   
653  C CB  . ILE A 89  ? 0.23588 0.21344 0.23691 0.01768  -0.00622 -0.00664 96  ILE A CB  
654  C CG1 . ILE A 89  ? 0.25633 0.24225 0.25602 0.01915  -0.00565 0.00040  96  ILE A CG1 
655  C CG2 . ILE A 89  ? 0.23836 0.20716 0.23715 0.00795  -0.00813 -0.01322 96  ILE A CG2 
656  C CD1 . ILE A 89  ? 0.30384 0.27002 0.29712 0.01895  0.00072  0.00749  96  ILE A CD1 
657  N N   . GLY A 90  ? 0.21541 0.21823 0.22550 0.01035  -0.01877 -0.02344 97  GLY A N   
658  C CA  . GLY A 90  ? 0.21000 0.21820 0.21737 0.00867  -0.02143 -0.02856 97  GLY A CA  
659  C C   . GLY A 90  ? 0.20595 0.21555 0.21260 0.00774  -0.01752 -0.02621 97  GLY A C   
660  O O   . GLY A 90  ? 0.23465 0.23983 0.24362 0.00471  -0.01490 -0.02126 97  GLY A O   
661  N N   . MET A 91  ? 0.20068 0.21517 0.20377 0.01028  -0.01669 -0.02885 98  MET A N   
662  C CA  . MET A 91  ? 0.22396 0.24664 0.23085 0.01144  -0.01115 -0.02344 98  MET A CA  
663  C C   . MET A 91  ? 0.23413 0.25939 0.22792 0.01966  -0.00671 -0.02331 98  MET A C   
664  O O   . MET A 91  ? 0.24832 0.26523 0.22863 0.02327  -0.00900 -0.03080 98  MET A O   
665  C CB  . MET A 91  ? 0.20954 0.23640 0.22545 0.01016  -0.01130 -0.02432 98  MET A CB  
666  C CG  . MET A 91  ? 0.21323 0.23524 0.23642 0.00118  -0.01614 -0.02400 98  MET A CG  
667  S SD  . MET A 91  ? 0.22988 0.25959 0.26281 -0.00170 -0.01933 -0.02281 98  MET A SD  
668  C CE  . MET A 91  ? 0.26662 0.28443 0.29033 0.00442  -0.02024 -0.03263 98  MET A CE  
669  N N   . THR A 92  ? 0.23351 0.26787 0.22887 0.02233  0.00020  -0.01432 99  THR A N   
670  C CA  . THR A 92  ? 0.24289 0.27879 0.22228 0.03302  0.00791  -0.01280 99  THR A CA  
671  C C   . THR A 92  ? 0.24862 0.29004 0.23236 0.04023  0.01504  -0.01173 99  THR A C   
672  O O   . THR A 92  ? 0.23940 0.28842 0.24199 0.03532  0.01270  -0.00988 99  THR A O   
673  C CB  . THR A 92  ? 0.25668 0.30323 0.23838 0.03480  0.01551  -0.00018 99  THR A CB  
674  O OG1 . THR A 92  ? 0.25048 0.31267 0.25753 0.02875  0.01917  0.01065  99  THR A OG1 
675  C CG2 . THR A 92  ? 0.29714 0.33808 0.27576 0.02971  0.01004  0.00172  99  THR A CG2 
676  N N   . LYS A 93  ? 0.25803 0.26379 0.22940 0.04085  -0.02436 -0.00301 100 LYS A N   
677  C CA  . LYS A 93  ? 0.26420 0.25530 0.22935 0.03768  -0.01535 -0.00932 100 LYS A CA  
678  C C   . LYS A 93  ? 0.25732 0.24229 0.23012 0.04190  -0.00572 -0.00235 100 LYS A C   
679  O O   . LYS A 93  ? 0.26511 0.24589 0.24764 0.04121  -0.00028 -0.00579 100 LYS A O   
680  C CB  . LYS A 93  ? 0.30640 0.29309 0.24530 0.03646  -0.01495 -0.01440 100 LYS A CB  
681  C CG  . LYS A 93  ? 0.31146 0.28228 0.24317 0.03694  -0.00557 -0.02247 100 LYS A CG  
682  C CD  . LYS A 93  ? 0.35318 0.31755 0.25583 0.03790  -0.00281 -0.02853 100 LYS A CD  
683  C CE  . LYS A 93  ? 0.38309 0.32843 0.27680 0.04179  0.00626  -0.03848 100 LYS A CE  
684  N NZ  . LYS A 93  ? 0.44295 0.38440 0.31113 0.04724  0.01362  -0.04287 100 LYS A NZ  
685  N N   . ALA A 94  ? 0.28055 0.26523 0.24787 0.04532  -0.00397 0.00798  101 ALA A N   
686  C CA  . ALA A 94  ? 0.32791 0.30756 0.30230 0.04448  0.00547  0.01406  101 ALA A CA  
687  C C   . ALA A 94  ? 0.27774 0.25600 0.27353 0.04292  0.00531  0.01311  101 ALA A C   
688  O O   . ALA A 94  ? 0.29642 0.27618 0.30216 0.03960  0.01174  0.01115  101 ALA A O   
689  C CB  . ALA A 94  ? 0.33567 0.30855 0.29577 0.04572  0.00785  0.02626  101 ALA A CB  
690  N N   . ASP A 95  ? 0.25725 0.23665 0.26082 0.04573  -0.00212 0.01338  102 ASP A N   
691  C CA  . ASP A 95  ? 0.24965 0.22765 0.27086 0.04450  -0.00125 0.01093  102 ASP A CA  
692  C C   . ASP A 95  ? 0.23678 0.21961 0.26587 0.04026  -0.00005 0.00238  102 ASP A C   
693  O O   . ASP A 95  ? 0.25600 0.23784 0.29474 0.03761  0.00391  0.00082  102 ASP A O   
694  C CB  . ASP A 95  ? 0.25514 0.23896 0.28389 0.05035  -0.00851 0.01119  102 ASP A CB  
695  C CG  . ASP A 95  ? 0.29150 0.26648 0.31304 0.05933  -0.01032 0.02094  102 ASP A CG  
696  O OD1 . ASP A 95  ? 0.35503 0.31113 0.36854 0.05852  -0.00419 0.02780  102 ASP A OD1 
697  O OD2 . ASP A 95  ? 0.32489 0.31188 0.34862 0.06817  -0.01824 0.02242  102 ASP A OD2 
698  N N   . LEU A 96  ? 0.22609 0.21197 0.24848 0.03896  -0.00350 -0.00330 103 LEU A N   
699  C CA  . LEU A 96  ? 0.24454 0.22691 0.26900 0.03592  -0.00183 -0.00992 103 LEU A CA  
700  C C   . LEU A 96  ? 0.25761 0.23772 0.28137 0.03877  0.00495  -0.00938 103 LEU A C   
701  O O   . LEU A 96  ? 0.23534 0.21623 0.26752 0.03884  0.00665  -0.01063 103 LEU A O   
702  C CB  . LEU A 96  ? 0.26495 0.24231 0.27561 0.03221  -0.00513 -0.01658 103 LEU A CB  
703  C CG  . LEU A 96  ? 0.24094 0.22801 0.25674 0.02562  -0.01202 -0.01956 103 LEU A CG  
704  C CD1 . LEU A 96  ? 0.24654 0.22628 0.24446 0.01813  -0.01482 -0.02725 103 LEU A CD1 
705  C CD2 . LEU A 96  ? 0.24062 0.22968 0.27021 0.02170  -0.01068 -0.02087 103 LEU A CD2 
706  N N   . ILE A 97  ? 0.23915 0.22019 0.25251 0.04158  0.00882  -0.00760 104 ILE A N   
707  C CA  . ILE A 97  ? 0.24190 0.22910 0.25659 0.04554  0.01631  -0.00774 104 ILE A CA  
708  C C   . ILE A 97  ? 0.24092 0.23879 0.27174 0.04147  0.01924  -0.00339 104 ILE A C   
709  O O   . ILE A 97  ? 0.25090 0.25975 0.29129 0.04338  0.02180  -0.00514 104 ILE A O   
710  C CB  . ILE A 97  ? 0.27486 0.26389 0.27408 0.04868  0.02142  -0.00739 104 ILE A CB  
711  C CG1 . ILE A 97  ? 0.30018 0.27549 0.28102 0.05171  0.01872  -0.01517 104 ILE A CG1 
712  C CG2 . ILE A 97  ? 0.27575 0.28079 0.28089 0.05297  0.03087  -0.00694 104 ILE A CG2 
713  C CD1 . ILE A 97  ? 0.32169 0.29652 0.28167 0.05323  0.02173  -0.01608 104 ILE A CD1 
714  N N   . ASN A 98  ? 0.24901 0.24272 0.28170 0.03614  0.01826  0.00187  105 ASN A N   
715  C CA  . ASN A 98  ? 0.27555 0.27191 0.31889 0.02898  0.02146  0.00474  105 ASN A CA  
716  C C   . ASN A 98  ? 0.23063 0.22377 0.28431 0.02768  0.01688  0.00085  105 ASN A C   
717  O O   . ASN A 98  ? 0.26244 0.24522 0.31804 0.02488  0.01581  0.00214  105 ASN A O   
718  C CB  . ASN A 98  ? 0.28233 0.26585 0.31671 0.02491  0.02370  0.01257  105 ASN A CB  
719  C CG  . ASN A 98  ? 0.49616 0.48602 0.52173 0.02115  0.03157  0.01731  105 ASN A CG  
720  O OD1 . ASN A 98  ? 0.74241 0.74250 0.77483 0.01188  0.03854  0.01819  105 ASN A OD1 
721  N ND2 . ASN A 98  ? 0.65312 0.63984 0.66269 0.02681  0.03084  0.01996  105 ASN A ND2 
722  N N   . ASN A 99  ? 0.22043 0.22065 0.27815 0.03105  0.01496  -0.00393 106 ASN A N   
723  C CA  . ASN A 99  ? 0.20656 0.20670 0.27134 0.02947  0.01175  -0.00747 106 ASN A CA  
724  C C   . ASN A 99  ? 0.23327 0.22337 0.29779 0.02910  0.00840  -0.00833 106 ASN A C   
725  O O   . ASN A 99  ? 0.23440 0.22232 0.30428 0.02620  0.00833  -0.01030 106 ASN A O   
726  C CB  . ASN A 99  ? 0.20086 0.21067 0.27475 0.02231  0.01380  -0.00838 106 ASN A CB  
727  C CG  . ASN A 99  ? 0.20170 0.23264 0.28059 0.02355  0.01654  -0.00814 106 ASN A CG  
728  O OD1 . ASN A 99  ? 0.21876 0.25638 0.29617 0.03305  0.01502  -0.00916 106 ASN A OD1 
729  N ND2 . ASN A 99  ? 0.25526 0.29715 0.33951 0.01429  0.02121  -0.00670 106 ASN A ND2 
730  N N   . LEU A 100 ? 0.21207 0.19892 0.27013 0.03227  0.00567  -0.00808 107 LEU A N   
731  C CA  . LEU A 100 ? 0.20332 0.19042 0.26435 0.03269  0.00194  -0.00951 107 LEU A CA  
732  C C   . LEU A 100 ? 0.25218 0.23527 0.31752 0.03541  0.00251  -0.00672 107 LEU A C   
733  O O   . LEU A 100 ? 0.26336 0.24816 0.33553 0.03694  0.00223  -0.00956 107 LEU A O   
734  C CB  . LEU A 100 ? 0.22519 0.21497 0.28972 0.02938  0.00133  -0.01406 107 LEU A CB  
735  C CG  . LEU A 100 ? 0.29256 0.27637 0.34668 0.02842  0.00127  -0.01543 107 LEU A CG  
736  C CD1 . LEU A 100 ? 0.28411 0.26590 0.33672 0.03059  0.00343  -0.01503 107 LEU A CD1 
737  C CD2 . LEU A 100 ? 0.37949 0.36030 0.42754 0.02316  -0.00091 -0.01859 107 LEU A CD2 
738  N N   . GLY A 101 ? 0.23164 0.20695 0.29055 0.03648  0.00448  -0.00110 108 GLY A N   
739  C CA  . GLY A 101 ? 0.27068 0.23268 0.32735 0.04054  0.00549  0.00329  108 GLY A CA  
740  C C   . GLY A 101 ? 0.27978 0.22964 0.33946 0.03562  0.01014  0.00040  108 GLY A C   
741  O O   . GLY A 101 ? 0.34308 0.27644 0.39953 0.04101  0.01130  0.00174  108 GLY A O   
742  N N   . THR A 102 ? 0.25631 0.21338 0.32048 0.02640  0.01253  -0.00399 109 THR A N   
743  C CA  . THR A 102 ? 0.25231 0.20230 0.31849 0.01849  0.01572  -0.00904 109 THR A CA  
744  C C   . THR A 102 ? 0.25147 0.20028 0.31506 0.00671  0.02015  -0.00679 109 THR A C   
745  O O   . THR A 102 ? 0.28778 0.24762 0.35075 0.00587  0.02133  -0.00221 109 THR A O   
746  C CB  . THR A 102 ? 0.27223 0.23834 0.34551 0.01583  0.01363  -0.01604 109 THR A CB  
747  O OG1 . THR A 102 ? 0.27224 0.25547 0.34827 0.01338  0.01265  -0.01485 109 THR A OG1 
748  C CG2 . THR A 102 ? 0.32126 0.29289 0.39722 0.02338  0.01081  -0.01823 109 THR A CG2 
749  N N   A ILE A 103 ? 0.24122 0.17787 0.30272 -0.00369 0.02333  -0.01123 110 ILE A N   
750  N N   B ILE A 103 ? 0.24054 0.17654 0.30171 -0.00382 0.02349  -0.01098 110 ILE A N   
751  C CA  A ILE A 103 ? 0.24589 0.18875 0.30811 -0.02049 0.02752  -0.01184 110 ILE A CA  
752  C CA  B ILE A 103 ? 0.24618 0.19026 0.30863 -0.02033 0.02755  -0.01138 110 ILE A CA  
753  C C   A ILE A 103 ? 0.23192 0.20507 0.30592 -0.02612 0.02405  -0.01911 110 ILE A C   
754  C C   B ILE A 103 ? 0.23072 0.20456 0.30491 -0.02579 0.02403  -0.01885 110 ILE A C   
755  O O   A ILE A 103 ? 0.23882 0.21424 0.31350 -0.03996 0.02459  -0.02604 110 ILE A O   
756  O O   B ILE A 103 ? 0.24085 0.21605 0.31549 -0.03923 0.02449  -0.02587 110 ILE A O   
757  C CB  A ILE A 103 ? 0.33039 0.23900 0.37951 -0.03217 0.03331  -0.01222 110 ILE A CB  
758  C CB  B ILE A 103 ? 0.32634 0.23844 0.37606 -0.03363 0.03384  -0.01092 110 ILE A CB  
759  C CG1 A ILE A 103 ? 0.33480 0.22361 0.37934 -0.03000 0.03244  -0.02135 110 ILE A CG1 
760  C CG1 B ILE A 103 ? 0.31780 0.20441 0.36076 -0.03261 0.03367  -0.01929 110 ILE A CG1 
761  C CG2 A ILE A 103 ? 0.33493 0.21586 0.36999 -0.02287 0.03598  -0.00120 110 ILE A CG2 
762  C CG2 B ILE A 103 ? 0.28474 0.17267 0.32063 -0.02708 0.03727  0.00083  110 ILE A CG2 
763  C CD1 A ILE A 103 ? 0.39470 0.24541 0.42313 -0.04465 0.03893  -0.02459 110 ILE A CD1 
764  C CD1 B ILE A 103 ? 0.36503 0.21507 0.39208 -0.04973 0.04053  -0.02204 110 ILE A CD1 
765  N N   A ALA A 104 ? 0.24381 0.23945 0.32479 -0.01539 0.02014  -0.01742 111 ALA A N   
766  N N   B ALA A 104 ? 0.24255 0.23915 0.32377 -0.01527 0.02018  -0.01718 111 ALA A N   
767  C CA  A ALA A 104 ? 0.21215 0.23002 0.29990 -0.01437 0.01526  -0.02261 111 ALA A CA  
768  C CA  B ALA A 104 ? 0.19873 0.21951 0.28734 -0.01436 0.01541  -0.02205 111 ALA A CA  
769  C C   A ALA A 104 ? 0.21361 0.26035 0.31039 -0.02570 0.01509  -0.02524 111 ALA A C   
770  C C   B ALA A 104 ? 0.23024 0.27791 0.32750 -0.02736 0.01578  -0.02503 111 ALA A C   
771  O O   A ALA A 104 ? 0.22499 0.28786 0.32475 -0.02830 0.01021  -0.03059 111 ALA A O   
772  O O   B ALA A 104 ? 0.22621 0.28892 0.32644 -0.03211 0.01129  -0.03100 111 ALA A O   
773  C CB  A ALA A 104 ? 0.22101 0.24631 0.30889 0.00060  0.01168  -0.01961 111 ALA A CB  
774  C CB  B ALA A 104 ? 0.20230 0.23377 0.29200 0.00029  0.01253  -0.01832 111 ALA A CB  
775  N N   A LYS A 105 ? 0.22322 0.28177 0.32457 -0.03280 0.02015  -0.02160 112 LYS A N   
776  N N   B LYS A 105 ? 0.19924 0.25883 0.30096 -0.03374 0.02087  -0.02112 112 LYS A N   
777  C CA  A LYS A 105 ? 0.20957 0.30487 0.32338 -0.04541 0.02000  -0.02512 112 LYS A CA  
778  C CA  B LYS A 105 ? 0.23462 0.32980 0.34854 -0.04748 0.02109  -0.02478 112 LYS A CA  
779  C C   A LYS A 105 ? 0.24904 0.33676 0.35975 -0.06589 0.01931  -0.03340 112 LYS A C   
780  C C   B LYS A 105 ? 0.26262 0.34588 0.37217 -0.06869 0.02132  -0.03253 112 LYS A C   
781  O O   A LYS A 105 ? 0.25140 0.36580 0.36859 -0.07084 0.01309  -0.03989 112 LYS A O   
782  O O   B LYS A 105 ? 0.24921 0.35754 0.36510 -0.07629 0.01570  -0.03972 112 LYS A O   
783  C CB  A LYS A 105 ? 0.22043 0.33293 0.34010 -0.05206 0.02782  -0.02011 112 LYS A CB  
784  C CB  B LYS A 105 ? 0.21347 0.32685 0.33333 -0.05285 0.02879  -0.01952 112 LYS A CB  
785  C CG  A LYS A 105 ? 0.29173 0.45140 0.42829 -0.06632 0.02826  -0.02416 112 LYS A CG  
786  C CG  B LYS A 105 ? 0.38903 0.53810 0.52190 -0.07464 0.03154  -0.02369 112 LYS A CG  
787  C CD  A LYS A 105 ? 0.34183 0.52247 0.48460 -0.07168 0.03814  -0.01883 112 LYS A CD  
788  C CD  B LYS A 105 ? 0.32415 0.50305 0.46607 -0.07624 0.04015  -0.01835 112 LYS A CD  
789  C CE  A LYS A 105 ? 0.40248 0.64473 0.56796 -0.08215 0.03851  -0.02294 112 LYS A CE  
790  C CE  B LYS A 105 ? 0.39694 0.63513 0.56097 -0.09125 0.04061  -0.02336 112 LYS A CE  
791  N NZ  A LYS A 105 ? 0.48226 0.73052 0.65057 -0.11263 0.03807  -0.03011 112 LYS A NZ  
792  N NZ  B LYS A 105 ? 0.35573 0.64031 0.53496 -0.07972 0.04646  -0.01974 112 LYS A NZ  
793  N N   A SER A 106 ? 0.26416 0.31304 0.36192 -0.07759 0.02546  -0.03351 113 SER A N   
794  N N   B SER A 106 ? 0.24372 0.28613 0.33946 -0.07788 0.02751  -0.03142 113 SER A N   
795  C CA  A SER A 106 ? 0.27197 0.30500 0.36189 -0.09762 0.02592  -0.04318 113 SER A CA  
796  C CA  B SER A 106 ? 0.28343 0.30590 0.37030 -0.09865 0.02914  -0.04009 113 SER A CA  
797  C C   A SER A 106 ? 0.26007 0.28183 0.34333 -0.08878 0.01987  -0.05072 113 SER A C   
798  C C   B SER A 106 ? 0.24680 0.25355 0.32623 -0.09095 0.02367  -0.04809 113 SER A C   
799  O O   A SER A 106 ? 0.29227 0.32265 0.37329 -0.10283 0.01657  -0.06107 113 SER A O   
800  O O   B SER A 106 ? 0.25121 0.25661 0.32568 -0.10706 0.02217  -0.05878 113 SER A O   
801  C CB  A SER A 106 ? 0.35257 0.33875 0.42550 -0.11082 0.03506  -0.04083 113 SER A CB  
802  C CB  B SER A 106 ? 0.34484 0.32077 0.41442 -0.10924 0.03835  -0.03571 113 SER A CB  
803  O OG  A SER A 106 ? 0.36470 0.31336 0.42586 -0.09058 0.03613  -0.03476 113 SER A OG  
804  O OG  B SER A 106 ? 0.40686 0.34491 0.46413 -0.08892 0.03842  -0.03087 113 SER A OG  
805  N N   A GLY A 107 ? 0.28479 0.29107 0.36440 -0.06756 0.01855  -0.04638 114 GLY A N   
806  N N   B GLY A 107 ? 0.25006 0.24682 0.32772 -0.06862 0.02125  -0.04390 114 GLY A N   
807  C CA  A GLY A 107 ? 0.23476 0.23413 0.30806 -0.06010 0.01467  -0.05309 114 GLY A CA  
808  C CA  B GLY A 107 ? 0.36018 0.34807 0.43171 -0.06107 0.01754  -0.05088 114 GLY A CA  
809  C C   A GLY A 107 ? 0.31112 0.34879 0.39133 -0.05945 0.00678  -0.05601 114 GLY A C   
810  C C   B GLY A 107 ? 0.21545 0.24094 0.29420 -0.06158 0.00990  -0.05503 114 GLY A C   
811  O O   A GLY A 107 ? 0.25681 0.29637 0.32964 -0.06579 0.00361  -0.06493 114 GLY A O   
812  O O   B GLY A 107 ? 0.30604 0.33109 0.37740 -0.06861 0.00724  -0.06446 114 GLY A O   
813  N N   A THR A 108 ? 0.23182 0.29982 0.32390 -0.05065 0.00354  -0.04857 115 THR A N   
814  N N   B THR A 108 ? 0.23363 0.29151 0.32458 -0.05328 0.00633  -0.04809 115 THR A N   
815  C CA  A THR A 108 ? 0.24752 0.35167 0.34460 -0.04636 -0.00467 -0.04934 115 THR A CA  
816  C CA  B THR A 108 ? 0.25893 0.35298 0.35527 -0.05049 -0.00175 -0.04991 115 THR A CA  
817  C C   A THR A 108 ? 0.25303 0.38480 0.35474 -0.06634 -0.00840 -0.05793 115 THR A C   
818  C C   B THR A 108 ? 0.28727 0.40703 0.38826 -0.07171 -0.00463 -0.05845 115 THR A C   
819  O O   A THR A 108 ? 0.24278 0.39083 0.33945 -0.06850 -0.01563 -0.06348 115 THR A O   
820  O O   B THR A 108 ? 0.25140 0.38879 0.34853 -0.07514 -0.01176 -0.06470 115 THR A O   
821  C CB  A THR A 108 ? 0.20303 0.33122 0.31105 -0.03129 -0.00590 -0.04012 115 THR A CB  
822  C CB  B THR A 108 ? 0.25646 0.37477 0.36288 -0.03386 -0.00379 -0.04059 115 THR A CB  
823  O OG1 A THR A 108 ? 0.20381 0.30576 0.30442 -0.01550 -0.00363 -0.03407 115 THR A OG1 
824  O OG1 B THR A 108 ? 0.19421 0.28562 0.29350 -0.01853 -0.00128 -0.03467 115 THR A OG1 
825  C CG2 A THR A 108 ? 0.19753 0.36427 0.31058 -0.02348 -0.01467 -0.03931 115 THR A CG2 
826  C CG2 B THR A 108 ? 0.19266 0.34400 0.30152 -0.02580 -0.01266 -0.04032 115 THR A CG2 
827  N N   A LYS A 109 ? 0.26741 0.40769 0.37782 -0.08264 -0.00367 -0.05896 116 LYS A N   
828  N N   B LYS A 109 ? 0.23719 0.35942 0.34445 -0.08835 0.00098  -0.05907 116 LYS A N   
829  C CA  A LYS A 109 ? 0.25430 0.42353 0.37014 -0.10697 -0.00671 -0.06836 116 LYS A CA  
830  C CA  B LYS A 109 ? 0.23657 0.38095 0.34722 -0.11463 -0.00075 -0.06887 116 LYS A CA  
831  C C   A LYS A 109 ? 0.31097 0.45503 0.40868 -0.12032 -0.00865 -0.08072 116 LYS A C   
832  C C   B LYS A 109 ? 0.33639 0.44590 0.42733 -0.12835 -0.00057 -0.08110 116 LYS A C   
833  O O   A LYS A 109 ? 0.27728 0.45118 0.37439 -0.12954 -0.01715 -0.08892 116 LYS A O   
834  O O   B LYS A 109 ? 0.35340 0.48564 0.44211 -0.14202 -0.00740 -0.09145 116 LYS A O   
835  C CB  A LYS A 109 ? 0.24994 0.41709 0.37202 -0.12717 0.00229  -0.06764 116 LYS A CB  
836  C CB  B LYS A 109 ? 0.30623 0.45161 0.42362 -0.13258 0.00803  -0.06626 116 LYS A CB  
837  C CG  A LYS A 109 ? 0.33876 0.53059 0.46466 -0.15932 0.00138  -0.07812 116 LYS A CG  
838  C CG  B LYS A 109 ? 0.39708 0.57981 0.52357 -0.16209 0.00645  -0.07500 116 LYS A CG  
839  C CD  A LYS A 109 ? 0.37572 0.54873 0.49939 -0.17555 0.01296  -0.07318 116 LYS A CD  
840  C CD  B LYS A 109 ? 0.45112 0.61377 0.57298 -0.17999 0.01773  -0.07055 116 LYS A CD  
841  C CE  A LYS A 109 ? 0.58083 0.73671 0.68986 -0.20165 0.01510  -0.08068 116 LYS A CE  
842  C CE  B LYS A 109 ? 0.49266 0.66836 0.61034 -0.20379 0.01679  -0.07716 116 LYS A CE  
843  N NZ  A LYS A 109 ? 0.59197 0.80186 0.71171 -0.20686 0.00523  -0.08673 116 LYS A NZ  
844  N NZ  B LYS A 109 ? 0.54053 0.75905 0.66513 -0.20069 0.00436  -0.08457 116 LYS A NZ  
845  N N   A ALA A 110 ? 0.27049 0.36048 0.35201 -0.12074 -0.00082 -0.08278 117 ALA A N   
846  N N   B ALA A 110 ? 0.32601 0.38128 0.40145 -0.12393 0.00717  -0.08064 117 ALA A N   
847  C CA  A ALA A 110 ? 0.32832 0.39033 0.39017 -0.13190 -0.00063 -0.09627 117 ALA A CA  
848  C CA  B ALA A 110 ? 0.33486 0.35194 0.38947 -0.13307 0.00940  -0.09308 117 ALA A CA  
849  C C   A ALA A 110 ? 0.26409 0.33908 0.31967 -0.11647 -0.00783 -0.09802 117 ALA A C   
850  C C   B ALA A 110 ? 0.35373 0.38409 0.40283 -0.12091 0.00233  -0.09812 117 ALA A C   
851  O O   A ALA A 110 ? 0.27537 0.35615 0.31877 -0.12794 -0.01233 -0.10994 117 ALA A O   
852  O O   B ALA A 110 ? 0.36423 0.39187 0.39987 -0.13446 -0.00019 -0.11160 117 ALA A O   
853  C CB  A ALA A 110 ? 0.33416 0.33530 0.38030 -0.12878 0.00996  -0.09660 117 ALA A CB  
854  C CB  B ALA A 110 ? 0.35845 0.31929 0.39979 -0.12287 0.01888  -0.08912 117 ALA A CB  
855  N N   A PHE A 111 ? 0.28881 0.36499 0.34904 -0.09221 -0.00830 -0.08666 118 PHE A N   
856  N N   B PHE A 111 ? 0.35294 0.39621 0.40945 -0.09714 -0.00046 -0.08763 118 PHE A N   
857  C CA  A PHE A 111 ? 0.24633 0.32895 0.29679 -0.07942 -0.01315 -0.08677 118 PHE A CA  
858  C CA  B PHE A 111 ? 0.29884 0.35588 0.34861 -0.08597 -0.00643 -0.08922 118 PHE A CA  
859  C C   A PHE A 111 ? 0.28471 0.41384 0.33795 -0.08274 -0.02472 -0.08759 118 PHE A C   
860  C C   B PHE A 111 ? 0.29600 0.39718 0.34808 -0.09631 -0.01694 -0.09397 118 PHE A C   
861  O O   A PHE A 111 ? 0.26493 0.40002 0.30311 -0.08640 -0.02962 -0.09486 118 PHE A O   
862  O O   B PHE A 111 ? 0.30968 0.41239 0.34657 -0.10238 -0.02069 -0.10371 118 PHE A O   
863  C CB  A PHE A 111 ? 0.26302 0.33727 0.31797 -0.05713 -0.01078 -0.07396 118 PHE A CB  
864  C CB  B PHE A 111 ? 0.25934 0.32191 0.31625 -0.06272 -0.00713 -0.07572 118 PHE A CB  
865  C CG  A PHE A 111 ? 0.26638 0.34210 0.30978 -0.04511 -0.01339 -0.07150 118 PHE A CG  
866  C CG  B PHE A 111 ? 0.22010 0.28690 0.26588 -0.05204 -0.01050 -0.07528 118 PHE A CG  
867  C CD1 A PHE A 111 ? 0.24028 0.30315 0.26645 -0.04958 -0.01135 -0.08119 118 PHE A CD1 
868  C CD1 B PHE A 111 ? 0.25993 0.31016 0.28895 -0.05715 -0.00780 -0.08608 118 PHE A CD1 
869  C CD2 A PHE A 111 ? 0.23614 0.32017 0.28295 -0.02905 -0.01581 -0.05922 118 PHE A CD2 
870  C CD2 B PHE A 111 ? 0.27963 0.36472 0.32849 -0.03727 -0.01545 -0.06421 118 PHE A CD2 
871  C CE1 A PHE A 111 ? 0.25464 0.31951 0.26865 -0.03989 -0.01208 -0.07734 118 PHE A CE1 
872  C CE1 B PHE A 111 ? 0.29165 0.34668 0.30836 -0.04889 -0.00932 -0.08486 118 PHE A CE1 
873  C CE2 A PHE A 111 ? 0.26103 0.34050 0.29414 -0.02006 -0.01653 -0.05518 118 PHE A CE2 
874  C CE2 B PHE A 111 ? 0.29233 0.37715 0.32688 -0.02956 -0.01752 -0.06215 118 PHE A CE2 
875  C CZ  A PHE A 111 ? 0.24205 0.31319 0.25921 -0.02619 -0.01423 -0.06382 118 PHE A CZ  
876  C CZ  B PHE A 111 ? 0.20549 0.27745 0.22434 -0.03633 -0.01430 -0.07224 118 PHE A CZ  
877  N N   A MET A 112 ? 0.26187 0.42692 0.33357 -0.08033 -0.02926 -0.08030 119 MET A N   
878  N N   B MET A 112 ? 0.27720 0.41837 0.34795 -0.09688 -0.02202 -0.08725 119 MET A N   
879  C CA  A MET A 112 ? 0.30466 0.52036 0.38133 -0.07942 -0.04150 -0.07990 119 MET A CA  
880  C CA  B MET A 112 ? 0.29834 0.49039 0.37423 -0.10236 -0.03378 -0.09024 119 MET A CA  
881  C C   A MET A 112 ? 0.30806 0.54336 0.38033 -0.10612 -0.04673 -0.09512 119 MET A C   
882  C C   B MET A 112 ? 0.31908 0.51547 0.38720 -0.13204 -0.03567 -0.10673 119 MET A C   
883  O O   A MET A 112 ? 0.30905 0.57234 0.37233 -0.10671 -0.05740 -0.09890 119 MET A O   
884  O O   B MET A 112 ? 0.29312 0.50793 0.34947 -0.13742 -0.04426 -0.11461 119 MET A O   
885  C CB  A MET A 112 ? 0.33799 0.58821 0.43706 -0.06743 -0.04329 -0.06918 119 MET A CB  
886  C CB  B MET A 112 ? 0.23801 0.47617 0.33799 -0.09416 -0.03766 -0.08032 119 MET A CB  
887  C CG  A MET A 112 ? 0.25367 0.49604 0.34778 -0.03866 -0.04481 -0.05601 119 MET A CG  
888  C CG  B MET A 112 ? 0.22383 0.45267 0.32775 -0.06475 -0.03531 -0.06529 119 MET A CG  
889  S SD  A MET A 112 ? 0.46097 0.73842 0.57761 -0.02181 -0.04521 -0.04574 119 MET A SD  
890  S SD  B MET A 112 ? 0.28645 0.50907 0.37193 -0.04155 -0.04255 -0.05844 119 MET A SD  
891  C CE  A MET A 112 ? 0.22897 0.46474 0.33220 0.00481  -0.04059 -0.03361 119 MET A CE  
892  C CE  B MET A 112 ? 0.33233 0.55577 0.42593 -0.01334 -0.04096 -0.04275 119 MET A CE  
893  N N   A GLU A 113 ? 0.32831 0.54620 0.40305 -0.12966 -0.03945 -0.10423 120 GLU A N   
894  N N   B GLU A 113 ? 0.33190 0.50580 0.40191 -0.15179 -0.02709 -0.11165 120 GLU A N   
895  C CA  A GLU A 113 ? 0.28970 0.50678 0.35168 -0.15272 -0.04106 -0.11659 120 GLU A CA  
896  C CA  B GLU A 113 ? 0.30726 0.46221 0.36042 -0.17339 -0.02498 -0.12238 120 GLU A CA  
897  C C   A GLU A 113 ? 0.34947 0.53703 0.38424 -0.15342 -0.04158 -0.12717 120 GLU A C   
898  C C   B GLU A 113 ? 0.32881 0.45013 0.35570 -0.17215 -0.02463 -0.13350 120 GLU A C   
899  O O   A GLU A 113 ? 0.39353 0.59877 0.41637 -0.16050 -0.04865 -0.13340 120 GLU A O   
900  O O   B GLU A 113 ? 0.37674 0.50267 0.38973 -0.18470 -0.02846 -0.14283 120 GLU A O   
901  C CB  A GLU A 113 ? 0.38887 0.57402 0.45011 -0.17302 -0.03006 -0.12019 120 GLU A CB  
902  C CB  B GLU A 113 ? 0.48728 0.60312 0.53774 -0.18794 -0.01316 -0.12179 120 GLU A CB  
903  C CG  A GLU A 113 ? 0.48697 0.70606 0.57115 -0.17817 -0.02856 -0.11185 120 GLU A CG  
904  C CG  B GLU A 113 ? 0.45760 0.60683 0.52958 -0.19477 -0.01152 -0.11280 120 GLU A CG  
905  C CD  A GLU A 113 ? 0.59550 0.77592 0.67415 -0.19766 -0.01651 -0.11332 120 GLU A CD  
906  C CD  B GLU A 113 ? 0.44911 0.55692 0.51937 -0.19716 0.00068  -0.10607 120 GLU A CD  
907  O OE1 A GLU A 113 ? 0.66390 0.79142 0.71987 -0.20688 -0.01056 -0.12127 120 GLU A OE1 
908  O OE1 B GLU A 113 ? 0.60957 0.67316 0.66945 -0.18507 0.00592  -0.10502 120 GLU A OE1 
909  O OE2 A GLU A 113 ? 0.65510 0.85746 0.74998 -0.20247 -0.01267 -0.10610 120 GLU A OE2 
910  O OE2 B GLU A 113 ? 0.58210 0.70191 0.66012 -0.21056 0.00532  -0.10159 120 GLU A OE2 
911  N N   A ALA A 114 ? 0.30984 0.45335 0.33411 -0.14407 -0.03327 -0.12867 121 ALA A N   
912  N N   B ALA A 114 ? 0.38584 0.47290 0.40528 -0.15732 -0.01881 -0.13341 121 ALA A N   
913  C CA  A ALA A 114 ? 0.33914 0.45149 0.33684 -0.14318 -0.03020 -0.13943 121 ALA A CA  
914  C CA  B ALA A 114 ? 0.44767 0.50357 0.44228 -0.15275 -0.01587 -0.14368 121 ALA A CA  
915  C C   A ALA A 114 ? 0.33528 0.47803 0.32380 -0.12973 -0.03989 -0.13512 121 ALA A C   
916  C C   B ALA A 114 ? 0.36852 0.46288 0.35618 -0.14732 -0.02699 -0.14534 121 ALA A C   
917  O O   A ALA A 114 ? 0.40332 0.54380 0.36926 -0.13729 -0.04236 -0.14649 121 ALA A O   
918  O O   B ALA A 114 ? 0.40594 0.49129 0.37209 -0.15316 -0.02766 -0.15527 121 ALA A O   
919  C CB  A ALA A 114 ? 0.35514 0.41639 0.34808 -0.12762 -0.01700 -0.13552 121 ALA A CB  
920  C CB  B ALA A 114 ? 0.39188 0.40987 0.38500 -0.13068 -0.00604 -0.13695 121 ALA A CB  
921  N N   A LEU A 115 ? 0.30472 0.46991 0.30674 -0.10825 -0.04419 -0.11752 122 LEU A N   
922  N N   B LEU A 115 ? 0.37033 0.50169 0.37346 -0.13024 -0.03443 -0.13060 122 LEU A N   
923  C CA  A LEU A 115 ? 0.29454 0.48583 0.28516 -0.09441 -0.05379 -0.11014 122 LEU A CA  
924  C CA  B LEU A 115 ? 0.37197 0.53594 0.36527 -0.12079 -0.04515 -0.12753 122 LEU A CA  
925  C C   A LEU A 115 ? 0.42531 0.66503 0.41325 -0.10814 -0.06844 -0.11753 122 LEU A C   
926  C C   B LEU A 115 ? 0.41176 0.60591 0.39730 -0.13903 -0.05476 -0.13739 122 LEU A C   
927  O O   A LEU A 115 ? 0.39354 0.64489 0.35949 -0.10663 -0.07558 -0.11994 122 LEU A O   
928  O O   B LEU A 115 ? 0.42259 0.62016 0.38625 -0.13835 -0.05914 -0.14223 122 LEU A O   
929  C CB  A LEU A 115 ? 0.26547 0.46757 0.27129 -0.07087 -0.05539 -0.09060 122 LEU A CB  
930  C CB  B LEU A 115 ? 0.31281 0.50617 0.32350 -0.09830 -0.05102 -0.10800 122 LEU A CB  
931  C CG  A LEU A 115 ? 0.28568 0.44397 0.29133 -0.05843 -0.04255 -0.08385 122 LEU A CG  
932  C CG  B LEU A 115 ? 0.39680 0.55681 0.40470 -0.07672 -0.04222 -0.09625 122 LEU A CG  
933  C CD1 A LEU A 115 ? 0.30575 0.46957 0.32433 -0.03828 -0.04343 -0.06683 122 LEU A CD1 
934  C CD1 B LEU A 115 ? 0.39671 0.52246 0.41430 -0.08135 -0.03070 -0.09877 122 LEU A CD1 
935  C CD2 A LEU A 115 ? 0.30413 0.44019 0.28466 -0.05574 -0.03802 -0.08732 122 LEU A CD2 
936  C CD2 B LEU A 115 ? 0.27408 0.45483 0.29323 -0.05526 -0.04743 -0.07837 122 LEU A CD2 
937  N N   A GLN A 116 ? 0.36885 0.63414 0.37845 -0.11929 -0.07096 -0.11791 123 GLN A N   
938  N N   B GLN A 116 ? 0.42459 0.63644 0.42676 -0.15290 -0.05578 -0.13721 123 GLN A N   
939  C CA  A GLN A 116 ? 0.39087 0.69310 0.40031 -0.12838 -0.08021 -0.12018 123 GLN A CA  
940  C CA  B GLN A 116 ? 0.42871 0.65942 0.42264 -0.17014 -0.06152 -0.14570 123 GLN A CA  
941  C C   A GLN A 116 ? 0.38480 0.66266 0.37439 -0.15188 -0.07636 -0.13700 123 GLN A C   
942  C C   B GLN A 116 ? 0.57196 0.75327 0.53984 -0.18508 -0.05303 -0.16134 123 GLN A C   
943  O O   A GLN A 116 ? 0.56118 0.86738 0.54439 -0.16030 -0.08492 -0.14128 123 GLN A O   
944  O O   B GLN A 116 ? 0.56470 0.74801 0.51152 -0.18845 -0.05736 -0.16955 123 GLN A O   
945  C CB  A GLN A 116 ? 0.35247 0.69055 0.39137 -0.13121 -0.08155 -0.11408 123 GLN A CB  
946  C CB  B GLN A 116 ? 0.52364 0.78591 0.54027 -0.18354 -0.06299 -0.14309 123 GLN A CB  
947  C CG  A GLN A 116 ? 0.46225 0.83475 0.51739 -0.10339 -0.08823 -0.09709 123 GLN A CG  
948  C CG  B GLN A 116 ? 0.45187 0.69391 0.48481 -0.18546 -0.05277 -0.13777 123 GLN A CG  
949  C CD  A GLN A 116 ? 0.76070 1.18749 0.83391 -0.10115 -0.09575 -0.09240 123 GLN A CD  
950  C CD  B GLN A 116 ? 0.38525 0.60947 0.41591 -0.21150 -0.04569 -0.14573 123 GLN A CD  
951  O OE1 A GLN A 116 ? 0.75264 1.19612 0.82740 -0.12310 -0.09689 -0.10228 123 GLN A OE1 
952  O OE1 B GLN A 116 ? 0.58180 0.79063 0.59341 -0.22792 -0.04586 -0.15799 123 GLN A OE1 
953  N NE2 A GLN A 116 ? 0.64851 1.10162 0.73394 -0.07380 -0.10033 -0.07775 123 GLN A NE2 
954  N NE2 B GLN A 116 ? 0.54690 0.77354 0.59515 -0.21617 -0.03927 -0.13877 123 GLN A NE2 
955  N N   A ALA A 117 ? 0.51327 0.73854 0.49238 -0.16110 -0.06366 -0.14648 124 ALA A N   
956  N N   B ALA A 117 ? 0.57101 0.70596 0.53828 -0.19233 -0.04069 -0.16492 124 ALA A N   
957  C CA  A ALA A 117 ? 0.53601 0.72796 0.49244 -0.17908 -0.05818 -0.16231 124 ALA A CA  
958  C CA  B ALA A 117 ? 0.49758 0.57975 0.43954 -0.20198 -0.03150 -0.17850 124 ALA A CA  
959  C C   A ALA A 117 ? 0.66471 0.82406 0.59341 -0.16977 -0.05332 -0.16878 124 ALA A C   
960  C C   B ALA A 117 ? 0.51477 0.58385 0.43355 -0.18970 -0.03108 -0.18493 124 ALA A C   
961  O O   A ALA A 117 ? 0.67576 0.79303 0.58553 -0.17853 -0.04424 -0.18157 124 ALA A O   
962  O O   B ALA A 117 ? 0.56548 0.59606 0.46125 -0.19439 -0.02421 -0.19719 124 ALA A O   
963  C CB  A ALA A 117 ? 0.62071 0.77264 0.58142 -0.19426 -0.04634 -0.16786 124 ALA A CB  
964  C CB  B ALA A 117 ? 0.55080 0.58043 0.49393 -0.19884 -0.01812 -0.17629 124 ALA A CB  
965  N N   A GLY A 118 ? 0.47205 0.64889 0.39644 -0.15103 -0.05822 -0.15964 125 GLY A N   
966  N N   B GLY A 118 ? 0.44311 0.54216 0.36595 -0.17306 -0.03745 -0.17639 125 GLY A N   
967  C CA  A GLY A 118 ? 0.48996 0.64802 0.38578 -0.14347 -0.05456 -0.16458 125 GLY A CA  
968  C CA  B GLY A 118 ? 0.44895 0.53832 0.34854 -0.16153 -0.03573 -0.18060 125 GLY A CA  
969  C C   A GLY A 118 ? 0.48457 0.61620 0.37798 -0.12745 -0.04414 -0.16050 125 GLY A C   
970  C C   B GLY A 118 ? 0.51812 0.58229 0.41773 -0.14267 -0.02564 -0.17623 125 GLY A C   
971  O O   A GLY A 118 ? 0.54497 0.67185 0.41675 -0.11820 -0.04131 -0.16015 125 GLY A O   
972  O O   B GLY A 118 ? 0.43808 0.48858 0.31749 -0.13380 -0.01999 -0.18087 125 GLY A O   
973  N N   A ALA A 119 ? 0.40204 0.51764 0.31686 -0.12401 -0.03764 -0.15660 126 ALA A N   
974  N N   B ALA A 119 ? 0.39827 0.45818 0.32007 -0.13647 -0.02255 -0.16761 126 ALA A N   
975  C CA  A ALA A 119 ? 0.42343 0.50936 0.34218 -0.10415 -0.02535 -0.14680 126 ALA A CA  
976  C CA  B ALA A 119 ? 0.44160 0.48015 0.36711 -0.11618 -0.01288 -0.16033 126 ALA A CA  
977  C C   A ALA A 119 ? 0.41488 0.52229 0.33545 -0.08531 -0.03028 -0.12748 126 ALA A C   
978  C C   B ALA A 119 ? 0.38775 0.45663 0.31489 -0.09945 -0.01914 -0.14443 126 ALA A C   
979  O O   A ALA A 119 ? 0.40205 0.54490 0.32487 -0.08312 -0.04331 -0.11883 126 ALA A O   
980  O O   B ALA A 119 ? 0.38512 0.49073 0.30854 -0.10247 -0.03175 -0.14075 126 ALA A O   
981  C CB  A ALA A 119 ? 0.43159 0.49583 0.37424 -0.10164 -0.01830 -0.14171 126 ALA A CB  
982  C CB  B ALA A 119 ? 0.46202 0.48390 0.41131 -0.11071 -0.00756 -0.15026 126 ALA A CB  
983  N N   A ASP A 120 ? 0.38234 0.46739 0.30179 -0.07126 -0.01945 -0.12037 127 ASP A N   
984  N N   B ASP A 120 ? 0.37296 0.42579 0.30425 -0.08161 -0.01033 -0.13455 127 ASP A N   
985  C CA  A ASP A 120 ? 0.34053 0.43497 0.25970 -0.05585 -0.02147 -0.10187 127 ASP A CA  
986  C CA  B ASP A 120 ? 0.35710 0.42837 0.28776 -0.06734 -0.01395 -0.11830 127 ASP A CA  
987  C C   A ASP A 120 ? 0.31852 0.39562 0.25926 -0.04490 -0.01387 -0.09153 127 ASP A C   
988  C C   B ASP A 120 ? 0.32098 0.37804 0.27127 -0.05338 -0.00697 -0.10553 127 ASP A C   
989  O O   A ASP A 120 ? 0.31273 0.37080 0.26646 -0.04688 -0.00639 -0.09806 127 ASP A O   
990  O O   B ASP A 120 ? 0.34489 0.37943 0.30621 -0.05271 0.00093  -0.10978 127 ASP A O   
991  C CB  A ASP A 120 ? 0.35444 0.44390 0.24661 -0.05270 -0.01588 -0.10163 127 ASP A CB  
992  C CB  B ASP A 120 ? 0.45206 0.51944 0.35635 -0.06503 -0.00861 -0.12283 127 ASP A CB  
993  C CG  A ASP A 120 ? 0.45226 0.51635 0.34263 -0.05202 0.00026  -0.11139 127 ASP A CG  
994  C CG  B ASP A 120 ? 0.49877 0.53838 0.40369 -0.05826 0.00729  -0.12847 127 ASP A CG  
995  O OD1 A ASP A 120 ? 0.53173 0.58327 0.41596 -0.06037 0.00508  -0.12934 127 ASP A OD1 
996  O OD1 B ASP A 120 ? 0.62804 0.64534 0.52942 -0.06370 0.01426  -0.14444 127 ASP A OD1 
997  O OD2 A ASP A 120 ? 0.44204 0.49888 0.33773 -0.04278 0.00824  -0.10119 127 ASP A OD2 
998  O OD2 B ASP A 120 ? 0.42886 0.46876 0.33899 -0.04721 0.01265  -0.11654 127 ASP A OD2 
999  N N   A ILE A 121 ? 0.28745 0.36898 0.22866 -0.03303 -0.01619 -0.07500 128 ILE A N   
1000 N N   B ILE A 121 ? 0.33269 0.40149 0.28496 -0.04220 -0.01064 -0.08953 128 ILE A N   
1001 C CA  A ILE A 121 ? 0.27250 0.34032 0.23202 -0.02400 -0.01095 -0.06520 128 ILE A CA  
1002 C CA  B ILE A 121 ? 0.27026 0.32647 0.23740 -0.03110 -0.00470 -0.07834 128 ILE A CA  
1003 C C   A ILE A 121 ? 0.27910 0.32668 0.24308 -0.02389 0.00197  -0.07104 128 ILE A C   
1004 C C   B ILE A 121 ? 0.34015 0.37670 0.30760 -0.02848 0.00816  -0.08419 128 ILE A C   
1005 O O   A ILE A 121 ? 0.27422 0.31204 0.25660 -0.01989 0.00557  -0.06875 128 ILE A O   
1006 O O   B ILE A 121 ? 0.33092 0.35743 0.31515 -0.02244 0.01263  -0.08010 128 ILE A O   
1007 C CB  A ILE A 121 ? 0.29918 0.36880 0.25114 -0.01287 -0.01510 -0.04814 128 ILE A CB  
1008 C CB  B ILE A 121 ? 0.27708 0.34095 0.23980 -0.02103 -0.00945 -0.06166 128 ILE A CB  
1009 C CG1 A ILE A 121 ? 0.34497 0.43684 0.30424 -0.00689 -0.02768 -0.04180 128 ILE A CG1 
1010 C CG1 B ILE A 121 ? 0.40956 0.46644 0.39233 -0.01297 -0.00874 -0.05209 128 ILE A CG1 
1011 C CG2 A ILE A 121 ? 0.30271 0.35284 0.26346 -0.00748 -0.00692 -0.04084 128 ILE A CG2 
1012 C CG2 B ILE A 121 ? 0.38397 0.44128 0.32517 -0.01989 -0.00344 -0.05839 128 ILE A CG2 
1013 C CD1 A ILE A 121 ? 0.30849 0.40095 0.25286 0.00776  -0.03387 -0.02521 128 ILE A CD1 
1014 C CD1 B ILE A 121 ? 0.33686 0.38810 0.31200 -0.00304 -0.01000 -0.03727 128 ILE A CD1 
1015 N N   A SER A 122 ? 0.28791 0.33203 0.23534 -0.02710 0.00911  -0.07888 129 SER A N   
1016 N N   B SER A 122 ? 0.40327 0.43768 0.35233 -0.03149 0.01432  -0.09345 129 SER A N   
1017 C CA  A SER A 122 ? 0.31733 0.34948 0.27152 -0.02395 0.02179  -0.08459 129 SER A CA  
1018 C CA  B SER A 122 ? 0.31087 0.33347 0.26398 -0.02590 0.02729  -0.09885 129 SER A CA  
1019 C C   A SER A 122 ? 0.28556 0.30370 0.25472 -0.02325 0.02459  -0.09431 129 SER A C   
1020 C C   B SER A 122 ? 0.38485 0.38913 0.35261 -0.02315 0.03101  -0.10663 129 SER A C   
1021 O O   A SER A 122 ? 0.33794 0.34774 0.31804 -0.01594 0.03315  -0.09617 129 SER A O   
1022 O O   B SER A 122 ? 0.32835 0.32557 0.30517 -0.01392 0.04008  -0.10842 129 SER A O   
1023 C CB  A SER A 122 ? 0.30515 0.33987 0.23746 -0.02713 0.03011  -0.09347 129 SER A CB  
1024 C CB  B SER A 122 ? 0.36013 0.38413 0.29084 -0.02871 0.03534  -0.11019 129 SER A CB  
1025 O OG  A SER A 122 ? 0.36269 0.39181 0.28398 -0.03306 0.03023  -0.11000 129 SER A OG  
1026 O OG  B SER A 122 ? 0.46798 0.47823 0.38950 -0.03390 0.03701  -0.12771 129 SER A OG  
1027 N N   A MET A 123 ? 0.27792 0.29396 0.24663 -0.03104 0.01777  -0.10020 130 MET A N   
1028 N N   B MET A 123 ? 0.31926 0.31746 0.28892 -0.03108 0.02413  -0.11033 130 MET A N   
1029 C CA  A MET A 123 ? 0.28351 0.27865 0.25984 -0.03315 0.02132  -0.10902 130 MET A CA  
1030 C CA  B MET A 123 ? 0.38507 0.35949 0.36228 -0.03182 0.02725  -0.11656 130 MET A CA  
1031 C C   A MET A 123 ? 0.28256 0.27452 0.27998 -0.02876 0.01869  -0.09811 130 MET A C   
1032 C C   B MET A 123 ? 0.29495 0.27041 0.29260 -0.02843 0.02300  -0.10365 130 MET A C   
1033 O O   A MET A 123 ? 0.30830 0.28079 0.31034 -0.03113 0.02111  -0.10220 130 MET A O   
1034 O O   B MET A 123 ? 0.31296 0.26748 0.31522 -0.02956 0.02535  -0.10576 130 MET A O   
1035 C CB  A MET A 123 ? 0.34037 0.33289 0.30289 -0.04862 0.01677  -0.12213 130 MET A CB  
1036 C CB  B MET A 123 ? 0.39187 0.35823 0.35431 -0.04832 0.02363  -0.13008 130 MET A CB  
1037 C CG  A MET A 123 ? 0.41600 0.40643 0.35343 -0.05193 0.02150  -0.13576 130 MET A CG  
1038 C CG  B MET A 123 ? 0.39534 0.37114 0.33397 -0.05413 0.02384  -0.14112 130 MET A CG  
1039 S SD  A MET A 123 ? 0.44588 0.44179 0.36403 -0.07336 0.01281  -0.15102 130 MET A SD  
1040 S SD  B MET A 123 ? 0.54446 0.50042 0.45946 -0.07361 0.02368  -0.16375 130 MET A SD  
1041 C CE  A MET A 123 ? 0.45700 0.40995 0.37832 -0.07942 0.02080  -0.16275 130 MET A CE  
1042 C CE  B MET A 123 ? 0.54726 0.46956 0.47543 -0.07756 0.02689  -0.16378 130 MET A CE  
1043 N N   A ILE A 124 ? 0.23865 0.24586 0.24531 -0.02286 0.01428  -0.08434 131 ILE A N   
1044 N N   B ILE A 124 ? 0.29971 0.29504 0.30634 -0.02373 0.01785  -0.09027 131 ILE A N   
1045 C CA  A ILE A 124 ? 0.23510 0.24248 0.25835 -0.01957 0.01108  -0.07478 131 ILE A CA  
1046 C CA  B ILE A 124 ? 0.24563 0.24407 0.26839 -0.02108 0.01361  -0.07934 131 ILE A CA  
1047 C C   A ILE A 124 ? 0.26375 0.25099 0.29656 -0.01375 0.01733  -0.07524 131 ILE A C   
1048 C C   B ILE A 124 ? 0.22664 0.20565 0.25913 -0.01327 0.01962  -0.07796 131 ILE A C   
1049 O O   A ILE A 124 ? 0.22331 0.20468 0.26461 -0.01520 0.01574  -0.07110 131 ILE A O   
1050 O O   B ILE A 124 ? 0.24335 0.21383 0.28281 -0.01534 0.01847  -0.07455 131 ILE A O   
1051 C CB  A ILE A 124 ? 0.21868 0.23832 0.24440 -0.01219 0.00768  -0.06205 131 ILE A CB  
1052 C CB  B ILE A 124 ? 0.25849 0.27382 0.28423 -0.01485 0.00897  -0.06680 131 ILE A CB  
1053 C CG1 A ILE A 124 ? 0.24835 0.27001 0.28784 -0.00837 0.00423  -0.05348 131 ILE A CG1 
1054 C CG1 B ILE A 124 ? 0.22127 0.24092 0.26071 -0.01181 0.00477  -0.05755 131 ILE A CG1 
1055 C CG2 A ILE A 124 ? 0.23792 0.25287 0.26159 -0.00656 0.01482  -0.06023 131 ILE A CG2 
1056 C CG2 B ILE A 124 ? 0.20700 0.21908 0.23163 -0.00778 0.01535  -0.06387 131 ILE A CG2 
1057 C CD1 A ILE A 124 ? 0.24490 0.27253 0.28251 -0.00092 0.00080  -0.04253 131 ILE A CD1 
1058 C CD1 B ILE A 124 ? 0.26155 0.29102 0.29953 -0.00449 0.00054  -0.04663 131 ILE A CD1 
1059 N N   A GLY A 125 ? 0.27317 0.25282 0.30478 -0.00574 0.02450  -0.07896 132 GLY A N   
1060 N N   B GLY A 125 ? 0.30238 0.27732 0.33530 -0.00370 0.02613  -0.07982 132 GLY A N   
1061 C CA  A GLY A 125 ? 0.30501 0.26888 0.34504 0.00387  0.02913  -0.07823 132 GLY A CA  
1062 C CA  B GLY A 125 ? 0.27648 0.23817 0.31895 0.00687  0.03003  -0.07735 132 GLY A CA  
1063 C C   A GLY A 125 ? 0.32246 0.25805 0.35481 0.00065  0.03214  -0.08598 132 GLY A C   
1064 C C   B GLY A 125 ? 0.32116 0.25405 0.35754 0.00472  0.03246  -0.08284 132 GLY A C   
1065 O O   A GLY A 125 ? 0.33584 0.25359 0.37230 0.00843  0.03428  -0.08211 132 GLY A O   
1066 O O   B GLY A 125 ? 0.29000 0.20913 0.33184 0.01172  0.03308  -0.07674 132 GLY A O   
1067 N N   A GLN A 126 ? 0.29623 0.22483 0.31437 -0.01146 0.03229  -0.09695 133 GLN A N   
1068 N N   B GLN A 126 ? 0.34943 0.27093 0.37149 -0.00634 0.03370  -0.09413 133 GLN A N   
1069 C CA  A GLN A 126 ? 0.35027 0.24615 0.35796 -0.01883 0.03550  -0.10460 133 GLN A CA  
1070 C CA  B GLN A 126 ? 0.38619 0.27297 0.39694 -0.01230 0.03742  -0.10140 133 GLN A CA  
1071 C C   A GLN A 126 ? 0.28568 0.18110 0.30014 -0.02997 0.03081  -0.09670 133 GLN A C   
1072 C C   B GLN A 126 ? 0.37976 0.26378 0.39613 -0.02342 0.03306  -0.09314 133 GLN A C   
1073 O O   A GLN A 126 ? 0.36998 0.23465 0.37482 -0.03892 0.03435  -0.10081 133 GLN A O   
1074 O O   B GLN A 126 ? 0.38432 0.23562 0.39324 -0.02608 0.03708  -0.09314 133 GLN A O   
1075 C CB  A GLN A 126 ? 0.37152 0.25856 0.35988 -0.03241 0.03684  -0.12067 133 GLN A CB  
1076 C CB  B GLN A 126 ? 0.40753 0.28848 0.40004 -0.02587 0.03857  -0.11707 133 GLN A CB  
1077 C CG  A GLN A 126 ? 0.44263 0.32766 0.42051 -0.02155 0.04400  -0.13062 133 GLN A CG  
1078 C CG  B GLN A 126 ? 0.44211 0.32473 0.42546 -0.01478 0.04539  -0.12688 133 GLN A CG  
1079 C CD  A GLN A 126 ? 0.53967 0.41044 0.49371 -0.03529 0.04599  -0.14854 133 GLN A CD  
1080 C CD  B GLN A 126 ? 0.50640 0.38440 0.46761 -0.02884 0.04618  -0.14337 133 GLN A CD  
1081 O OE1 A GLN A 126 ? 0.59780 0.43918 0.53987 -0.04742 0.04646  -0.15561 133 GLN A OE1 
1082 O OE1 B GLN A 126 ? 0.58963 0.44181 0.53670 -0.04342 0.04631  -0.15344 133 GLN A OE1 
1083 N NE2 A GLN A 126 ? 0.59159 0.48314 0.53625 -0.03509 0.04663  -0.15446 133 GLN A NE2 
1084 N NE2 B GLN A 126 ? 0.44525 0.34741 0.40086 -0.02627 0.04708  -0.14647 133 GLN A NE2 
1085 N N   A PHE A 127 ? 0.26475 0.19124 0.29346 -0.02933 0.02426  -0.08569 134 PHE A N   
1086 N N   B PHE A 127 ? 0.34371 0.26026 0.37166 -0.02868 0.02592  -0.08537 134 PHE A N   
1087 C CA  A PHE A 127 ? 0.26923 0.20458 0.30655 -0.03831 0.02063  -0.07810 134 PHE A CA  
1088 C CA  B PHE A 127 ? 0.29129 0.21351 0.32655 -0.03852 0.02296  -0.07808 134 PHE A CA  
1089 C C   A PHE A 127 ? 0.26426 0.20147 0.31278 -0.02569 0.02069  -0.06490 134 PHE A C   
1090 C C   B PHE A 127 ? 0.30518 0.23600 0.35269 -0.02567 0.02179  -0.06466 134 PHE A C   
1091 O O   A PHE A 127 ? 0.27734 0.22649 0.33319 -0.03078 0.01851  -0.05800 134 PHE A O   
1092 O O   B PHE A 127 ? 0.30160 0.24283 0.35601 -0.03096 0.01995  -0.05758 134 PHE A O   
1093 C CB  A PHE A 127 ? 0.25378 0.22529 0.29577 -0.04839 0.01281  -0.07855 134 PHE A CB  
1094 C CB  B PHE A 127 ? 0.34936 0.30418 0.38817 -0.05230 0.01601  -0.08065 134 PHE A CB  
1095 C CG  A PHE A 127 ? 0.24755 0.22047 0.27629 -0.06260 0.01115  -0.09241 134 PHE A CG  
1096 C CG  B PHE A 127 ? 0.35911 0.30878 0.38369 -0.06467 0.01585  -0.09490 134 PHE A CG  
1097 C CD1 A PHE A 127 ? 0.31782 0.28221 0.34120 -0.08313 0.01172  -0.10082 134 PHE A CD1 
1098 C CD1 B PHE A 127 ? 0.41664 0.34021 0.42988 -0.08221 0.01970  -0.10453 134 PHE A CD1 
1099 C CD2 A PHE A 127 ? 0.29997 0.28042 0.31879 -0.05752 0.00991  -0.09773 134 PHE A CD2 
1100 C CD2 B PHE A 127 ? 0.30722 0.27168 0.32524 -0.05960 0.01322  -0.09942 134 PHE A CD2 
1101 C CE1 A PHE A 127 ? 0.30458 0.26891 0.31325 -0.09885 0.00976  -0.11565 134 PHE A CE1 
1102 C CE1 B PHE A 127 ? 0.36377 0.27772 0.35992 -0.09453 0.02004  -0.12013 134 PHE A CE1 
1103 C CE2 A PHE A 127 ? 0.28524 0.26753 0.28813 -0.07124 0.00796  -0.11169 134 PHE A CE2 
1104 C CE2 B PHE A 127 ? 0.35607 0.31437 0.35726 -0.07081 0.01349  -0.11386 134 PHE A CE2 
1105 C CZ  A PHE A 127 ? 0.31541 0.28846 0.31278 -0.09192 0.00759  -0.12174 134 PHE A CZ  
1106 C CZ  B PHE A 127 ? 0.41709 0.35046 0.40738 -0.08815 0.01659  -0.12519 134 PHE A CZ  
1107 N N   . GLY A 128 ? 0.28231 0.21165 0.33243 -0.00987 0.02319  -0.06194 135 GLY A N   
1108 C CA  . GLY A 128 ? 0.26999 0.20034 0.32785 0.00039  0.02241  -0.05117 135 GLY A CA  
1109 C C   . GLY A 128 ? 0.24832 0.20525 0.31517 0.00255  0.01737  -0.04408 135 GLY A C   
1110 O O   . GLY A 128 ? 0.29119 0.24927 0.36210 0.00790  0.01630  -0.03613 135 GLY A O   
1111 N N   . VAL A 129 ? 0.22715 0.20205 0.29371 -0.00126 0.01433  -0.04674 136 VAL A N   
1112 C CA  . VAL A 129 ? 0.19560 0.18852 0.26588 0.00187  0.01008  -0.04023 136 VAL A CA  
1113 C C   . VAL A 129 ? 0.20344 0.20217 0.26937 0.00559  0.00980  -0.04089 136 VAL A C   
1114 O O   . VAL A 129 ? 0.20338 0.21143 0.26582 0.00680  0.00648  -0.03668 136 VAL A O   
1115 C CB  . VAL A 129 ? 0.19864 0.20855 0.27104 -0.00458 0.00622  -0.03935 136 VAL A CB  
1116 C CG1 . VAL A 129 ? 0.24443 0.25138 0.32226 -0.00911 0.00846  -0.03639 136 VAL A CG1 
1117 C CG2 . VAL A 129 ? 0.22235 0.23959 0.28968 -0.01432 0.00434  -0.04740 136 VAL A CG2 
1118 N N   . GLY A 130 ? 0.22781 0.20670 0.24390 -0.01370 -0.01420 -0.03703 137 GLY A N   
1119 C CA  . GLY A 130 ? 0.23692 0.21663 0.24211 -0.00548 -0.01156 -0.03641 137 GLY A CA  
1120 C C   . GLY A 130 ? 0.22580 0.21126 0.23312 -0.00342 -0.00688 -0.02909 137 GLY A C   
1121 O O   . GLY A 130 ? 0.23429 0.22250 0.23555 0.00195  -0.00502 -0.02703 137 GLY A O   
1122 N N   . PHE A 131 ? 0.21094 0.19759 0.22614 -0.00713 -0.00517 -0.02527 138 PHE A N   
1123 C CA  . PHE A 131 ? 0.20340 0.19408 0.22088 -0.00539 -0.00263 -0.02104 138 PHE A CA  
1124 C C   . PHE A 131 ? 0.20515 0.20152 0.22050 -0.00241 -0.00381 -0.02069 138 PHE A C   
1125 O O   . PHE A 131 ? 0.20602 0.20126 0.22026 0.00108  -0.00134 -0.01730 138 PHE A O   
1126 C CB  . PHE A 131 ? 0.20365 0.19735 0.22717 -0.00873 -0.00248 -0.01926 138 PHE A CB  
1127 C CG  . PHE A 131 ? 0.20310 0.20012 0.22816 -0.00648 -0.00170 -0.01794 138 PHE A CG  
1128 C CD1 . PHE A 131 ? 0.21373 0.20738 0.24042 -0.00515 -0.00046 -0.01676 138 PHE A CD1 
1129 C CD2 . PHE A 131 ? 0.20514 0.20899 0.23159 -0.00563 -0.00266 -0.01856 138 PHE A CD2 
1130 C CE1 . PHE A 131 ? 0.20751 0.20125 0.23688 -0.00376 -0.00098 -0.01722 138 PHE A CE1 
1131 C CE2 . PHE A 131 ? 0.22071 0.22459 0.24768 -0.00229 -0.00241 -0.01887 138 PHE A CE2 
1132 C CZ  . PHE A 131 ? 0.23416 0.23145 0.26243 -0.00183 -0.00199 -0.01873 138 PHE A CZ  
1133 N N   . TYR A 132 ? 0.20799 0.21087 0.22460 -0.00380 -0.00772 -0.02351 139 TYR A N   
1134 C CA  . TYR A 132 ? 0.18501 0.19533 0.20090 0.00038  -0.00926 -0.02248 139 TYR A CA  
1135 C C   . TYR A 132 ? 0.21035 0.21931 0.21623 0.00681  -0.00953 -0.02149 139 TYR A C   
1136 O O   . TYR A 132 ? 0.21884 0.23133 0.22280 0.01210  -0.00966 -0.01827 139 TYR A O   
1137 C CB  . TYR A 132 ? 0.18000 0.20186 0.20292 -0.00260 -0.01363 -0.02536 139 TYR A CB  
1138 C CG  . TYR A 132 ? 0.19025 0.21552 0.22225 -0.00744 -0.01106 -0.02359 139 TYR A CG  
1139 C CD1 . TYR A 132 ? 0.18798 0.21791 0.22195 -0.00384 -0.00847 -0.02124 139 TYR A CD1 
1140 C CD2 . TYR A 132 ? 0.21249 0.23491 0.24934 -0.01422 -0.01085 -0.02398 139 TYR A CD2 
1141 C CE1 . TYR A 132 ? 0.19600 0.23021 0.23456 -0.00604 -0.00543 -0.01950 139 TYR A CE1 
1142 C CE2 . TYR A 132 ? 0.23660 0.26270 0.27945 -0.01720 -0.00716 -0.02003 139 TYR A CE2 
1143 C CZ  . TYR A 132 ? 0.23282 0.26610 0.27541 -0.01263 -0.00448 -0.01803 139 TYR A CZ  
1144 O OH  . TYR A 132 ? 0.24577 0.28418 0.29139 -0.01407 -0.00057 -0.01421 139 TYR A OH  
1145 N N   . SER A 133 ? 0.20324 0.20674 0.20196 0.00780  -0.00872 -0.02332 140 SER A N   
1146 C CA  . SER A 133 ? 0.21355 0.21644 0.20034 0.01561  -0.00670 -0.02056 140 SER A CA  
1147 C C   . SER A 133 ? 0.18986 0.18903 0.17859 0.01833  0.00004  -0.01156 140 SER A C   
1148 O O   . SER A 133 ? 0.23036 0.23000 0.21065 0.02518  0.00306  -0.00591 140 SER A O   
1149 C CB  . SER A 133 ? 0.23916 0.23770 0.21650 0.01800  -0.00619 -0.02497 140 SER A CB  
1150 O OG  . SER A 133 ? 0.23283 0.22513 0.21508 0.01603  -0.00030 -0.02206 140 SER A OG  
1151 N N   . ALA A 134 ? 0.21027 0.20571 0.21007 0.01317  0.00219  -0.01001 141 ALA A N   
1152 C CA  . ALA A 134 ? 0.20222 0.19302 0.20738 0.01421  0.00683  -0.00286 141 ALA A CA  
1153 C C   . ALA A 134 ? 0.19516 0.18618 0.19713 0.01974  0.00627  0.00139  141 ALA A C   
1154 O O   . ALA A 134 ? 0.22860 0.21419 0.23133 0.02271  0.01104  0.00948  141 ALA A O   
1155 C CB  . ALA A 134 ? 0.22094 0.20903 0.23738 0.00840  0.00588  -0.00526 141 ALA A CB  
1156 N N   . TYR A 135 ? 0.19356 0.19141 0.19362 0.02137  0.00069  -0.00305 142 TYR A N   
1157 C CA  . TYR A 135 ? 0.21942 0.21836 0.21730 0.02828  -0.00028 0.00119  142 TYR A CA  
1158 C C   . TYR A 135 ? 0.23047 0.23308 0.21512 0.03665  -0.00022 0.00608  142 TYR A C   
1159 O O   . TYR A 135 ? 0.25501 0.25835 0.23629 0.04419  -0.00081 0.01144  142 TYR A O   
1160 C CB  . TYR A 135 ? 0.21880 0.22720 0.22184 0.02813  -0.00570 -0.00451 142 TYR A CB  
1161 C CG  . TYR A 135 ? 0.21154 0.21560 0.22424 0.02360  -0.00433 -0.00722 142 TYR A CG  
1162 C CD1 . TYR A 135 ? 0.22649 0.22220 0.24275 0.02756  -0.00268 -0.00490 142 TYR A CD1 
1163 C CD2 . TYR A 135 ? 0.19697 0.20341 0.21382 0.01625  -0.00472 -0.01206 142 TYR A CD2 
1164 C CE1 . TYR A 135 ? 0.22282 0.21403 0.24526 0.02466  -0.00240 -0.00933 142 TYR A CE1 
1165 C CE2 . TYR A 135 ? 0.19690 0.20026 0.21926 0.01381  -0.00367 -0.01436 142 TYR A CE2 
1166 C CZ  . TYR A 135 ? 0.21748 0.21412 0.24188 0.01825  -0.00300 -0.01395 142 TYR A CZ  
1167 O OH  . TYR A 135 ? 0.20965 0.20378 0.23714 0.01688  -0.00322 -0.01843 142 TYR A OH  
1168 N N   . LEU A 136 ? 0.23001 0.23384 0.20596 0.03692  0.00127  0.00508  143 LEU A N   
1169 C CA  . LEU A 136 ? 0.22473 0.23088 0.18539 0.04657  0.00362  0.01153  143 LEU A CA  
1170 C C   . LEU A 136 ? 0.26397 0.26125 0.22653 0.04979  0.01264  0.02519  143 LEU A C   
1171 O O   . LEU A 136 ? 0.27595 0.27437 0.22723 0.05940  0.01520  0.03439  143 LEU A O   
1172 C CB  . LEU A 136 ? 0.25806 0.26649 0.20827 0.04732  0.00446  0.00662  143 LEU A CB  
1173 C CG  . LEU A 136 ? 0.24676 0.26163 0.19389 0.04469  -0.00529 -0.00717 143 LEU A CG  
1174 C CD1 . LEU A 136 ? 0.25710 0.26900 0.19605 0.04498  -0.00384 -0.01323 143 LEU A CD1 
1175 C CD2 . LEU A 136 ? 0.29341 0.31944 0.22986 0.05254  -0.01375 -0.01000 143 LEU A CD2 
1176 N N   . VAL A 137 ? 0.25319 0.24197 0.23030 0.04179  0.01754  0.02718  144 VAL A N   
1177 C CA  . VAL A 137 ? 0.24568 0.22583 0.22900 0.04226  0.02638  0.04008  144 VAL A CA  
1178 C C   . VAL A 137 ? 0.24844 0.21712 0.24877 0.03625  0.02596  0.04073  144 VAL A C   
1179 O O   . VAL A 137 ? 0.27204 0.23088 0.27924 0.03677  0.03194  0.05177  144 VAL A O   
1180 C CB  . VAL A 137 ? 0.24777 0.23003 0.23395 0.03924  0.03390  0.04360  144 VAL A CB  
1181 C CG1 . VAL A 137 ? 0.27061 0.26285 0.23621 0.04826  0.03539  0.04303  144 VAL A CG1 
1182 C CG2 . VAL A 137 ? 0.24936 0.23177 0.24842 0.02937  0.03075  0.03350  144 VAL A CG2 
1183 N N   . ALA A 138 ? 0.23766 0.20675 0.24457 0.03117  0.01930  0.02956  145 ALA A N   
1184 C CA  . ALA A 138 ? 0.24199 0.20025 0.26296 0.02640  0.01793  0.02719  145 ALA A CA  
1185 C C   . ALA A 138 ? 0.25539 0.21204 0.27370 0.03241  0.01317  0.02405  145 ALA A C   
1186 O O   . ALA A 138 ? 0.28798 0.25651 0.29974 0.03499  0.00827  0.01754  145 ALA A O   
1187 C CB  . ALA A 138 ? 0.25452 0.21589 0.28325 0.01810  0.01458  0.01707  145 ALA A CB  
1188 N N   . GLU A 139 ? 0.26282 0.20493 0.28856 0.03407  0.01445  0.02797  146 GLU A N   
1189 C CA  . GLU A 139 ? 0.26517 0.20453 0.29031 0.04062  0.01006  0.02324  146 GLU A CA  
1190 C C   . GLU A 139 ? 0.28370 0.22390 0.31508 0.03590  0.00566  0.01049  146 GLU A C   
1191 O O   . GLU A 139 ? 0.29141 0.23685 0.32045 0.04160  0.00232  0.00465  146 GLU A O   
1192 C CB  . GLU A 139 ? 0.32515 0.24560 0.35455 0.04594  0.01317  0.03238  146 GLU A CB  
1193 C CG  . GLU A 139 ? 0.41824 0.32116 0.46258 0.03758  0.01478  0.03170  146 GLU A CG  
1194 C CD  . GLU A 139 ? 0.85631 0.73737 0.90710 0.04147  0.01880  0.04297  146 GLU A CD  
1195 O OE1 . GLU A 139 ? 0.85162 0.71525 0.91797 0.03399  0.01876  0.04113  146 GLU A OE1 
1196 O OE2 . GLU A 139 ? 0.66419 0.54536 0.70509 0.05192  0.02153  0.05379  146 GLU A OE2 
1197 N N   . LYS A 140 ? 0.25971 0.19630 0.29894 0.02679  0.00578  0.00653  147 LYS A N   
1198 C CA  . LYS A 140 ? 0.24429 0.18264 0.28691 0.02324  0.00140  -0.00517 147 LYS A CA  
1199 C C   . LYS A 140 ? 0.21492 0.16027 0.26076 0.01447  0.00178  -0.00650 147 LYS A C   
1200 O O   . LYS A 140 ? 0.23568 0.17788 0.28711 0.01024  0.00546  0.00038  147 LYS A O   
1201 C CB  . LYS A 140 ? 0.25907 0.17953 0.31003 0.02347  -0.00090 -0.01001 147 LYS A CB  
1202 C CG  . LYS A 140 ? 0.25260 0.17570 0.30398 0.02143  -0.00615 -0.02327 147 LYS A CG  
1203 C CD  . LYS A 140 ? 0.30674 0.21087 0.36348 0.02444  -0.00961 -0.03016 147 LYS A CD  
1204 C CE  . LYS A 140 ? 0.36472 0.25627 0.43582 0.01475  -0.01157 -0.03097 147 LYS A CE  
1205 N NZ  . LYS A 140 ? 0.52903 0.39643 0.60797 0.01700  -0.01511 -0.03668 147 LYS A NZ  
1206 N N   . VAL A 141 ? 0.20666 0.16228 0.24916 0.01285  -0.00121 -0.01404 148 VAL A N   
1207 C CA  . VAL A 141 ? 0.20848 0.17003 0.25366 0.00622  -0.00156 -0.01568 148 VAL A CA  
1208 C C   . VAL A 141 ? 0.20599 0.16748 0.25291 0.00504  -0.00630 -0.02495 148 VAL A C   
1209 O O   . VAL A 141 ? 0.21356 0.17896 0.25409 0.00986  -0.00802 -0.03013 148 VAL A O   
1210 C CB  . VAL A 141 ? 0.20907 0.18277 0.24670 0.00602  -0.00049 -0.01442 148 VAL A CB  
1211 C CG1 . VAL A 141 ? 0.22327 0.20094 0.26367 0.00079  -0.00086 -0.01588 148 VAL A CG1 
1212 C CG2 . VAL A 141 ? 0.22453 0.19906 0.25740 0.00876  0.00291  -0.00711 148 VAL A CG2 
1213 N N   . THR A 142 ? 0.20888 0.16793 0.26448 -0.00049 -0.00849 -0.02706 149 THR A N   
1214 C CA  . THR A 142 ? 0.23032 0.19145 0.28584 -0.00098 -0.01440 -0.03650 149 THR A CA  
1215 C C   . THR A 142 ? 0.23590 0.20790 0.29171 -0.00446 -0.01467 -0.03495 149 THR A C   
1216 O O   . THR A 142 ? 0.23786 0.21099 0.30211 -0.00872 -0.01211 -0.02921 149 THR A O   
1217 C CB  . THR A 142 ? 0.21531 0.16456 0.28311 -0.00438 -0.01921 -0.04201 149 THR A CB  
1218 O OG1 . THR A 142 ? 0.26487 0.19971 0.33420 -0.00102 -0.01818 -0.04169 149 THR A OG1 
1219 C CG2 . THR A 142 ? 0.24910 0.20122 0.31347 -0.00290 -0.02728 -0.05439 149 THR A CG2 
1220 N N   . VAL A 143 ? 0.20282 0.18307 0.24954 -0.00168 -0.01689 -0.03886 150 VAL A N   
1221 C CA  . VAL A 143 ? 0.18535 0.17435 0.23125 -0.00340 -0.01712 -0.03637 150 VAL A CA  
1222 C C   . VAL A 143 ? 0.21245 0.20547 0.25683 -0.00175 -0.02413 -0.04403 150 VAL A C   
1223 O O   . VAL A 143 ? 0.22661 0.22187 0.26007 0.00364  -0.02599 -0.04922 150 VAL A O   
1224 C CB  . VAL A 143 ? 0.18680 0.18175 0.22310 -0.00146 -0.01285 -0.03157 150 VAL A CB  
1225 C CG1 . VAL A 143 ? 0.24129 0.24198 0.27664 -0.00223 -0.01314 -0.02847 150 VAL A CG1 
1226 C CG2 . VAL A 143 ? 0.20081 0.19298 0.23760 -0.00250 -0.00803 -0.02621 150 VAL A CG2 
1227 N N   . ILE A 144 ? 0.19299 0.18899 0.24783 -0.00530 -0.02824 -0.04509 151 ILE A N   
1228 C CA  . ILE A 144 ? 0.18845 0.19073 0.24180 -0.00319 -0.03688 -0.05318 151 ILE A CA  
1229 C C   . ILE A 144 ? 0.19345 0.20643 0.24277 -0.00115 -0.03604 -0.04721 151 ILE A C   
1230 O O   . ILE A 144 ? 0.21179 0.22598 0.26934 -0.00412 -0.03169 -0.03995 151 ILE A O   
1231 C CB  . ILE A 144 ? 0.22675 0.22678 0.29869 -0.00911 -0.04386 -0.05916 151 ILE A CB  
1232 C CG1 . ILE A 144 ? 0.33692 0.32220 0.41757 -0.01282 -0.04217 -0.06073 151 ILE A CG1 
1233 C CG2 . ILE A 144 ? 0.24375 0.25090 0.31217 -0.00590 -0.05536 -0.07059 151 ILE A CG2 
1234 C CD1 . ILE A 144 ? 0.35152 0.32848 0.42106 -0.00751 -0.04540 -0.06979 151 ILE A CD1 
1235 N N   . THR A 145 ? 0.19707 0.21700 0.23217 0.00522  -0.03891 -0.04910 152 THR A N   
1236 C CA  . THR A 145 ? 0.19451 0.22179 0.22480 0.00812  -0.03686 -0.04107 152 THR A CA  
1237 C C   . THR A 145 ? 0.21354 0.25093 0.23345 0.01513  -0.04436 -0.04509 152 THR A C   
1238 O O   . THR A 145 ? 0.22878 0.26782 0.23776 0.01979  -0.04894 -0.05350 152 THR A O   
1239 C CB  . THR A 145 ? 0.20183 0.22541 0.22275 0.00900  -0.02763 -0.03245 152 THR A CB  
1240 O OG1 . THR A 145 ? 0.21666 0.24208 0.23640 0.01038  -0.02479 -0.02390 152 THR A OG1 
1241 C CG2 . THR A 145 ? 0.22132 0.24777 0.22738 0.01428  -0.02619 -0.03413 152 THR A CG2 
1242 N N   . LYS A 146 ? 0.20882 0.25317 0.22966 0.01775  -0.04525 -0.03871 153 LYS A N   
1243 C CA  . LYS A 146 ? 0.20372 0.25958 0.21373 0.02602  -0.05271 -0.04042 153 LYS A CA  
1244 C C   . LYS A 146 ? 0.24955 0.30702 0.25424 0.03045  -0.04728 -0.02724 153 LYS A C   
1245 O O   . LYS A 146 ? 0.23342 0.29002 0.25104 0.02801  -0.04565 -0.02243 153 LYS A O   
1246 C CB  . LYS A 146 ? 0.21950 0.28498 0.24347 0.02478  -0.06498 -0.04979 153 LYS A CB  
1247 C CG  . LYS A 146 ? 0.23204 0.31220 0.24494 0.03454  -0.07468 -0.05193 153 LYS A CG  
1248 C CD  . LYS A 146 ? 0.25518 0.33746 0.24448 0.04273  -0.07836 -0.05925 153 LYS A CD  
1249 C CE  . LYS A 146 ? 0.27639 0.37455 0.25242 0.05374  -0.08902 -0.06208 153 LYS A CE  
1250 N NZ  . LYS A 146 ? 0.30374 0.40685 0.26807 0.06197  -0.08277 -0.04548 153 LYS A NZ  
1251 N N   . HIS A 147 ? 0.25325 0.31257 0.23959 0.03745  -0.04384 -0.02094 154 HIS A N   
1252 C CA  . HIS A 147 ? 0.21872 0.27703 0.19874 0.04236  -0.03847 -0.00708 154 HIS A CA  
1253 C C   . HIS A 147 ? 0.26263 0.33439 0.22959 0.05361  -0.04635 -0.00639 154 HIS A C   
1254 O O   . HIS A 147 ? 0.29319 0.37381 0.24918 0.05835  -0.05317 -0.01560 154 HIS A O   
1255 C CB  . HIS A 147 ? 0.25206 0.30324 0.22224 0.04133  -0.02756 0.00170  154 HIS A CB  
1256 C CG  . HIS A 147 ? 0.26891 0.31439 0.23512 0.04415  -0.02058 0.01709  154 HIS A CG  
1257 N ND1 . HIS A 147 ? 0.30210 0.35428 0.25383 0.05436  -0.02098 0.02632  154 HIS A ND1 
1258 C CD2 . HIS A 147 ? 0.28751 0.31942 0.26212 0.03807  -0.01294 0.02477  154 HIS A CD2 
1259 C CE1 . HIS A 147 ? 0.32746 0.36888 0.28060 0.05396  -0.01334 0.04025  154 HIS A CE1 
1260 N NE2 . HIS A 147 ? 0.30842 0.33699 0.27575 0.04375  -0.00887 0.03844  154 HIS A NE2 
1261 N N   . ASN A 148 ? 0.24987 0.32328 0.21712 0.05926  -0.04635 0.00369  155 ASN A N   
1262 C CA  . ASN A 148 ? 0.27162 0.35955 0.22560 0.07161  -0.05476 0.00524  155 ASN A CA  
1263 C C   . ASN A 148 ? 0.30111 0.39453 0.22952 0.08024  -0.05254 0.00846  155 ASN A C   
1264 O O   . ASN A 148 ? 0.34631 0.45471 0.26064 0.09054  -0.06259 0.00277  155 ASN A O   
1265 C CB  . ASN A 148 ? 0.28363 0.36958 0.23896 0.07848  -0.05234 0.01966  155 ASN A CB  
1266 C CG  . ASN A 148 ? 0.29313 0.38277 0.26999 0.07607  -0.05775 0.01550  155 ASN A CG  
1267 O OD1 . ASN A 148 ? 0.32653 0.42661 0.31640 0.07171  -0.06665 0.00255  155 ASN A OD1 
1268 N ND2 . ASN A 148 ? 0.31484 0.39529 0.29717 0.07881  -0.05172 0.02678  155 ASN A ND2 
1269 N N   . ASP A 149 ? 0.31410 0.39790 0.23640 0.07694  -0.03991 0.01722  156 ASP A N   
1270 C CA  . ASP A 149 ? 0.36979 0.46090 0.26881 0.08589  -0.03480 0.02353  156 ASP A CA  
1271 C C   . ASP A 149 ? 0.44468 0.53995 0.33755 0.08456  -0.03552 0.01006  156 ASP A C   
1272 O O   . ASP A 149 ? 0.43927 0.54096 0.31422 0.09156  -0.02843 0.01567  156 ASP A O   
1273 C CB  . ASP A 149 ? 0.36121 0.44192 0.25953 0.08337  -0.01970 0.04303  156 ASP A CB  
1274 C CG  . ASP A 149 ? 0.38534 0.45897 0.28628 0.08731  -0.01807 0.05806  156 ASP A CG  
1275 O OD1 . ASP A 149 ? 0.42875 0.51119 0.32507 0.09655  -0.02799 0.05622  156 ASP A OD1 
1276 O OD2 . ASP A 149 ? 0.46380 0.52251 0.37326 0.08083  -0.00758 0.07058  156 ASP A OD2 
1277 N N   . ASP A 150 ? 0.33859 0.43046 0.24570 0.07674  -0.04300 -0.00655 157 ASP A N   
1278 C CA  . ASP A 150 ? 0.30431 0.39709 0.20586 0.07655  -0.04374 -0.01959 157 ASP A CA  
1279 C C   . ASP A 150 ? 0.34199 0.43412 0.25492 0.07261  -0.05768 -0.03910 157 ASP A C   
1280 O O   . ASP A 150 ? 0.33834 0.43245 0.26458 0.06961  -0.06618 -0.04178 157 ASP A O   
1281 C CB  . ASP A 150 ? 0.31949 0.40221 0.23061 0.06753  -0.03110 -0.01362 157 ASP A CB  
1282 C CG  . ASP A 150 ? 0.32857 0.41633 0.22709 0.07265  -0.02661 -0.01896 157 ASP A CG  
1283 O OD1 . ASP A 150 ? 0.39141 0.48726 0.27388 0.08253  -0.03376 -0.03082 157 ASP A OD1 
1284 O OD2 . ASP A 150 ? 0.33197 0.41574 0.23793 0.06674  -0.01562 -0.01151 157 ASP A OD2 
1285 N N   . GLU A 151 ? 0.33182 0.42150 0.24085 0.07294  -0.05994 -0.05253 158 GLU A N   
1286 C CA  . GLU A 151 ? 0.36217 0.44736 0.28361 0.06795  -0.07220 -0.07110 158 GLU A CA  
1287 C C   . GLU A 151 ? 0.27886 0.34966 0.22466 0.05407  -0.06721 -0.07026 158 GLU A C   
1288 O O   . GLU A 151 ? 0.28684 0.35206 0.23681 0.04962  -0.05544 -0.05802 158 GLU A O   
1289 C CB  . GLU A 151 ? 0.42429 0.51118 0.32775 0.07701  -0.07765 -0.08693 158 GLU A CB  
1290 C CG  . GLU A 151 ? 0.53461 0.63745 0.40772 0.09355  -0.07870 -0.08454 158 GLU A CG  
1291 C CD  . GLU A 151 ? 0.90586 1.02016 0.77647 0.09828  -0.09372 -0.09018 158 GLU A CD  
1292 O OE1 . GLU A 151 ? 1.02157 1.13270 0.90936 0.09135  -0.10726 -0.10555 158 GLU A OE1 
1293 O OE2 . GLU A 151 ? 0.96827 1.09524 0.82176 0.10860  -0.09211 -0.07841 158 GLU A OE2 
1294 N N   . GLN A 152 ? 0.29119 0.35627 0.25305 0.04744  -0.07666 -0.08346 159 GLN A N   
1295 C CA  . GLN A 152 ? 0.25776 0.30979 0.24194 0.03533  -0.07215 -0.08205 159 GLN A CA  
1296 C C   . GLN A 152 ? 0.25224 0.29336 0.23131 0.03581  -0.06605 -0.08576 159 GLN A C   
1297 O O   . GLN A 152 ? 0.29820 0.33724 0.26697 0.04194  -0.07202 -0.09905 159 GLN A O   
1298 C CB  . GLN A 152 ? 0.25185 0.30258 0.25781 0.02760  -0.08382 -0.09277 159 GLN A CB  
1299 C CG  . GLN A 152 ? 0.25374 0.29345 0.28433 0.01522  -0.07751 -0.08706 159 GLN A CG  
1300 C CD  . GLN A 152 ? 0.29749 0.34154 0.35326 0.00707  -0.08687 -0.09240 159 GLN A CD  
1301 O OE1 . GLN A 152 ? 0.31544 0.37375 0.37518 0.00893  -0.09198 -0.09023 159 GLN A OE1 
1302 N NE2 . GLN A 152 ? 0.31256 0.34525 0.38611 -0.00147 -0.08870 -0.09821 159 GLN A NE2 
1303 N N   A TYR A 153 ? 0.23948 0.27391 0.22557 0.03034  -0.05501 -0.07507 160 TYR A N   
1304 N N   B TYR A 153 ? 0.23948 0.27391 0.22557 0.03034  -0.05501 -0.07507 160 TYR A N   
1305 C CA  A TYR A 153 ? 0.27842 0.30549 0.26031 0.03195  -0.04868 -0.07648 160 TYR A CA  
1306 C CA  B TYR A 153 ? 0.27842 0.30549 0.26031 0.03195  -0.04868 -0.07648 160 TYR A CA  
1307 C C   A TYR A 153 ? 0.25181 0.26642 0.25246 0.02246  -0.04562 -0.07404 160 TYR A C   
1308 C C   B TYR A 153 ? 0.25181 0.26642 0.25246 0.02246  -0.04562 -0.07404 160 TYR A C   
1309 O O   A TYR A 153 ? 0.24004 0.25414 0.25354 0.01527  -0.04362 -0.06639 160 TYR A O   
1310 O O   B TYR A 153 ? 0.24004 0.25414 0.25354 0.01527  -0.04362 -0.06639 160 TYR A O   
1311 C CB  A TYR A 153 ? 0.26378 0.29848 0.23372 0.03630  -0.03746 -0.06441 160 TYR A CB  
1312 C CB  B TYR A 153 ? 0.26378 0.29848 0.23372 0.03630  -0.03746 -0.06441 160 TYR A CB  
1313 C CG  A TYR A 153 ? 0.29201 0.33852 0.24048 0.04806  -0.03766 -0.06636 160 TYR A CG  
1314 C CG  B TYR A 153 ? 0.29201 0.33852 0.24048 0.04806  -0.03766 -0.06636 160 TYR A CG  
1315 C CD1 A TYR A 153 ? 0.32297 0.37003 0.26007 0.05645  -0.03736 -0.07554 160 TYR A CD1 
1316 C CD1 B TYR A 153 ? 0.32297 0.37003 0.26007 0.05645  -0.03736 -0.07554 160 TYR A CD1 
1317 C CD2 A TYR A 153 ? 0.32770 0.38492 0.26583 0.05264  -0.03845 -0.05943 160 TYR A CD2 
1318 C CD2 B TYR A 153 ? 0.32770 0.38492 0.26583 0.05264  -0.03845 -0.05943 160 TYR A CD2 
1319 C CE1 A TYR A 153 ? 0.40977 0.46914 0.32479 0.06920  -0.03666 -0.07774 160 TYR A CE1 
1320 C CE1 B TYR A 153 ? 0.40977 0.46914 0.32479 0.06920  -0.03666 -0.07774 160 TYR A CE1 
1321 C CE2 A TYR A 153 ? 0.34588 0.41515 0.26130 0.06533  -0.03787 -0.06034 160 TYR A CE2 
1322 C CE2 B TYR A 153 ? 0.34588 0.41515 0.26130 0.06533  -0.03787 -0.06034 160 TYR A CE2 
1323 C CZ  A TYR A 153 ? 0.41466 0.48549 0.31839 0.07352  -0.03676 -0.06981 160 TYR A CZ  
1324 C CZ  B TYR A 153 ? 0.41466 0.48549 0.31839 0.07352  -0.03676 -0.06981 160 TYR A CZ  
1325 O OH  A TYR A 153 ? 0.45137 0.53563 0.33044 0.08793  -0.03517 -0.07109 160 TYR A OH  
1326 O OH  B TYR A 153 ? 0.45137 0.53563 0.33044 0.08793  -0.03517 -0.07109 160 TYR A OH  
1327 N N   . ALA A 154 ? 0.25139 0.25679 0.25158 0.02425  -0.04383 -0.07908 161 ALA A N   
1328 C CA  . ALA A 154 ? 0.23204 0.22598 0.24567 0.01804  -0.03920 -0.07461 161 ALA A CA  
1329 C C   . ALA A 154 ? 0.23308 0.22929 0.23940 0.02237  -0.03052 -0.06862 161 ALA A C   
1330 O O   . ALA A 154 ? 0.24652 0.24452 0.24202 0.03087  -0.03029 -0.07477 161 ALA A O   
1331 C CB  . ALA A 154 ? 0.28860 0.26756 0.31119 0.01666  -0.04572 -0.08551 161 ALA A CB  
1332 N N   . TRP A 155 ? 0.21426 0.21164 0.22669 0.01734  -0.02409 -0.05783 162 TRP A N   
1333 C CA  . TRP A 155 ? 0.20282 0.20281 0.21345 0.01961  -0.01744 -0.05249 162 TRP A CA  
1334 C C   . TRP A 155 ? 0.22296 0.21089 0.24313 0.01709  -0.01707 -0.05155 162 TRP A C   
1335 O O   . TRP A 155 ? 0.22418 0.20451 0.25381 0.01101  -0.01872 -0.04982 162 TRP A O   
1336 C CB  . TRP A 155 ? 0.21594 0.22452 0.22711 0.01532  -0.01238 -0.04230 162 TRP A CB  
1337 C CG  . TRP A 155 ? 0.19481 0.20854 0.20802 0.01469  -0.00694 -0.03614 162 TRP A CG  
1338 C CD1 . TRP A 155 ? 0.18813 0.21412 0.19810 0.01656  -0.00251 -0.03200 162 TRP A CD1 
1339 C CD2 . TRP A 155 ? 0.20344 0.21220 0.22334 0.01180  -0.00580 -0.03301 162 TRP A CD2 
1340 N NE1 . TRP A 155 ? 0.18907 0.21866 0.20547 0.01417  0.00009  -0.02789 162 TRP A NE1 
1341 C CE2 . TRP A 155 ? 0.18401 0.20309 0.20476 0.01194  -0.00232 -0.02877 162 TRP A CE2 
1342 C CE3 . TRP A 155 ? 0.20230 0.20008 0.22783 0.00930  -0.00716 -0.03254 162 TRP A CE3 
1343 C CZ2 . TRP A 155 ? 0.19748 0.21659 0.22272 0.01057  -0.00194 -0.02599 162 TRP A CZ2 
1344 C CZ3 . TRP A 155 ? 0.21391 0.21114 0.24155 0.00901  -0.00516 -0.02816 162 TRP A CZ3 
1345 C CH2 . TRP A 155 ? 0.19467 0.20253 0.22132 0.00994  -0.00344 -0.02573 162 TRP A CH2 
1346 N N   . GLU A 156 ? 0.19509 0.18210 0.21343 0.02259  -0.01442 -0.05166 163 GLU A N   
1347 C CA  . GLU A 156 ? 0.20448 0.18020 0.23038 0.02144  -0.01351 -0.04826 163 GLU A CA  
1348 C C   . GLU A 156 ? 0.20888 0.19159 0.23243 0.02710  -0.00956 -0.04419 163 GLU A C   
1349 O O   . GLU A 156 ? 0.21921 0.21194 0.23725 0.03380  -0.00815 -0.04714 163 GLU A O   
1350 C CB  . GLU A 156 ? 0.24375 0.20319 0.27317 0.02378  -0.01814 -0.05643 163 GLU A CB  
1351 C CG  . GLU A 156 ? 0.29852 0.24275 0.33672 0.02266  -0.01697 -0.05173 163 GLU A CG  
1352 C CD  . GLU A 156 ? 0.49174 0.41721 0.53743 0.02158  -0.02265 -0.06035 163 GLU A CD  
1353 O OE1 . GLU A 156 ? 0.39696 0.31565 0.45498 0.01261  -0.02464 -0.05870 163 GLU A OE1 
1354 O OE2 . GLU A 156 ? 0.40965 0.32814 0.44950 0.02991  -0.02571 -0.07026 163 GLU A OE2 
1355 N N   . SER A 157 ? 0.20795 0.18735 0.23576 0.02539  -0.00773 -0.03716 164 SER A N   
1356 C CA  . SER A 157 ? 0.20209 0.18901 0.22888 0.03163  -0.00572 -0.03374 164 SER A CA  
1357 C C   . SER A 157 ? 0.19518 0.17145 0.22469 0.03265  -0.00520 -0.02750 164 SER A C   
1358 O O   . SER A 157 ? 0.20496 0.17698 0.23633 0.02647  -0.00426 -0.02241 164 SER A O   
1359 C CB  . SER A 157 ? 0.21050 0.21558 0.23699 0.02860  -0.00395 -0.03011 164 SER A CB  
1360 O OG  . SER A 157 ? 0.19676 0.21182 0.22495 0.03467  -0.00341 -0.02772 164 SER A OG  
1361 N N   . SER A 158 ? 0.22700 0.20080 0.25598 0.04183  -0.00509 -0.02680 165 SER A N   
1362 C CA  . SER A 158 ? 0.23571 0.20419 0.26473 0.04572  -0.00410 -0.01847 165 SER A CA  
1363 C C   . SER A 158 ? 0.24695 0.23498 0.27379 0.05020  -0.00463 -0.01541 165 SER A C   
1364 O O   . SER A 158 ? 0.27465 0.26198 0.30001 0.05829  -0.00497 -0.01018 165 SER A O   
1365 C CB  . SER A 158 ? 0.27492 0.22486 0.30573 0.05378  -0.00425 -0.01855 165 SER A CB  
1366 O OG  . SER A 158 ? 0.32105 0.25243 0.35716 0.04728  -0.00501 -0.02185 165 SER A OG  
1367 N N   . ALA A 159 ? 0.22580 0.23094 0.25356 0.04507  -0.00510 -0.01824 166 ALA A N   
1368 C CA  . ALA A 159 ? 0.22800 0.25494 0.25830 0.04717  -0.00673 -0.01711 166 ALA A CA  
1369 C C   . ALA A 159 ? 0.26114 0.29650 0.29457 0.05817  -0.00640 -0.01894 166 ALA A C   
1370 O O   . ALA A 159 ? 0.27871 0.30866 0.31147 0.06155  -0.00440 -0.02382 166 ALA A O   
1371 C CB  . ALA A 159 ? 0.26983 0.29812 0.29642 0.04672  -0.00908 -0.01183 166 ALA A CB  
1372 N N   . GLY A 160 ? 0.27933 0.32868 0.31570 0.06516  -0.00866 -0.01594 167 GLY A N   
1373 C CA  . GLY A 160 ? 0.26456 0.32472 0.30546 0.07665  -0.00762 -0.01782 167 GLY A CA  
1374 C C   . GLY A 160 ? 0.27330 0.35326 0.32105 0.07462  -0.00456 -0.02175 167 GLY A C   
1375 O O   . GLY A 160 ? 0.28910 0.37747 0.33933 0.08538  -0.00196 -0.02413 167 GLY A O   
1376 N N   . GLY A 161 ? 0.22006 0.30707 0.27056 0.06213  -0.00402 -0.02176 168 GLY A N   
1377 C CA  . GLY A 161 ? 0.17620 0.28500 0.23522 0.05934  -0.00023 -0.02215 168 GLY A CA  
1378 C C   . GLY A 161 ? 0.16754 0.26970 0.21990 0.05825  0.00473  -0.02520 168 GLY A C   
1379 O O   . GLY A 161 ? 0.20123 0.32211 0.25933 0.05677  0.00948  -0.02354 168 GLY A O   
1380 N N   . SER A 162 ? 0.18736 0.26548 0.22863 0.05962  0.00377  -0.02922 169 SER A N   
1381 C CA  . SER A 162 ? 0.18324 0.25665 0.21662 0.06082  0.00669  -0.03389 169 SER A CA  
1382 C C   . SER A 162 ? 0.20889 0.26035 0.23569 0.05301  0.00349  -0.03599 169 SER A C   
1383 O O   . SER A 162 ? 0.20977 0.24692 0.23736 0.04956  0.00027  -0.03435 169 SER A O   
1384 C CB  . SER A 162 ? 0.24096 0.31057 0.26816 0.07538  0.00810  -0.04076 169 SER A CB  
1385 O OG  . SER A 162 ? 0.27223 0.31684 0.29596 0.07936  0.00375  -0.04434 169 SER A OG  
1386 N N   . PHE A 163 ? 0.20930 0.26108 0.22989 0.05104  0.00491  -0.03871 170 PHE A N   
1387 C CA  . PHE A 163 ? 0.18036 0.21525 0.19573 0.04529  0.00142  -0.04189 170 PHE A CA  
1388 C C   . PHE A 163 ? 0.20530 0.23882 0.21046 0.05232  0.00107  -0.04991 170 PHE A C   
1389 O O   . PHE A 163 ? 0.22197 0.26993 0.22238 0.06034  0.00523  -0.05105 170 PHE A O   
1390 C CB  . PHE A 163 ? 0.19560 0.23324 0.21353 0.03379  0.00172  -0.03587 170 PHE A CB  
1391 C CG  . PHE A 163 ? 0.18947 0.24387 0.20617 0.03256  0.00634  -0.03174 170 PHE A CG  
1392 C CD1 . PHE A 163 ? 0.18767 0.25863 0.21367 0.02967  0.01006  -0.02520 170 PHE A CD1 
1393 C CD2 . PHE A 163 ? 0.19242 0.24627 0.20014 0.03362  0.00660  -0.03342 170 PHE A CD2 
1394 C CE1 . PHE A 163 ? 0.19143 0.27686 0.21924 0.02699  0.01548  -0.01901 170 PHE A CE1 
1395 C CE2 . PHE A 163 ? 0.21076 0.27903 0.21660 0.03311  0.01197  -0.02706 170 PHE A CE2 
1396 C CZ  . PHE A 163 ? 0.20245 0.28579 0.21929 0.02895  0.01719  -0.01883 170 PHE A CZ  
1397 N N   . THR A 164 ? 0.20807 0.22502 0.20978 0.04965  -0.00431 -0.05609 171 THR A N   
1398 C CA  . THR A 164 ? 0.22007 0.23454 0.21081 0.05587  -0.00735 -0.06601 171 THR A CA  
1399 C C   . THR A 164 ? 0.22316 0.23878 0.21084 0.04888  -0.01019 -0.06512 171 THR A C   
1400 O O   . THR A 164 ? 0.22396 0.23440 0.21997 0.03896  -0.01149 -0.05958 171 THR A O   
1401 C CB  . THR A 164 ? 0.25360 0.24776 0.24355 0.06099  -0.01350 -0.07764 171 THR A CB  
1402 O OG1 . THR A 164 ? 0.28167 0.25920 0.28212 0.05101  -0.01799 -0.07635 171 THR A OG1 
1403 C CG2 . THR A 164 ? 0.26036 0.25155 0.25180 0.07108  -0.01080 -0.07898 171 THR A CG2 
1404 N N   . VAL A 165 ? 0.22198 0.24541 0.19671 0.05568  -0.01094 -0.07038 172 VAL A N   
1405 C CA  . VAL A 165 ? 0.24392 0.26839 0.21371 0.05192  -0.01540 -0.07109 172 VAL A CA  
1406 C C   . VAL A 165 ? 0.26775 0.28755 0.22530 0.06073  -0.02287 -0.08597 172 VAL A C   
1407 O O   . VAL A 165 ? 0.27054 0.29632 0.21557 0.07270  -0.02065 -0.09208 172 VAL A O   
1408 C CB  . VAL A 165 ? 0.25279 0.29486 0.21663 0.05175  -0.00855 -0.05966 172 VAL A CB  
1409 C CG1 . VAL A 165 ? 0.26308 0.30635 0.22020 0.05031  -0.01360 -0.05975 172 VAL A CG1 
1410 C CG2 . VAL A 165 ? 0.24384 0.28826 0.22089 0.04219  -0.00299 -0.04737 172 VAL A CG2 
1411 N N   . ARG A 166 ? 0.27122 0.28189 0.23234 0.05549  -0.03230 -0.09276 173 ARG A N   
1412 C CA  . ARG A 166 ? 0.27331 0.27963 0.22426 0.06216  -0.04246 -0.10887 173 ARG A CA  
1413 C C   . ARG A 166 ? 0.28786 0.29861 0.24023 0.05679  -0.05029 -0.10955 173 ARG A C   
1414 O O   . ARG A 166 ? 0.27565 0.28648 0.24189 0.04638  -0.04838 -0.09908 173 ARG A O   
1415 C CB  . ARG A 166 ? 0.33478 0.31989 0.29449 0.06179  -0.04928 -0.12198 173 ARG A CB  
1416 C CG  . ARG A 166 ? 0.38238 0.35344 0.36477 0.04757  -0.05347 -0.11917 173 ARG A CG  
1417 C CD  . ARG A 166 ? 0.43531 0.38357 0.42921 0.04646  -0.05584 -0.12579 173 ARG A CD  
1418 N NE  . ARG A 166 ? 0.45897 0.40787 0.45306 0.04982  -0.04522 -0.11497 173 ARG A NE  
1419 C CZ  . ARG A 166 ? 0.55959 0.49253 0.55871 0.05350  -0.04381 -0.11682 173 ARG A CZ  
1420 N NH1 . ARG A 166 ? 0.57099 0.48251 0.57475 0.05479  -0.05168 -0.12988 173 ARG A NH1 
1421 N NH2 . ARG A 166 ? 0.53921 0.47770 0.53889 0.05662  -0.03489 -0.10568 173 ARG A NH2 
1422 N N   . THR A 167 ? 0.33225 0.34828 0.26931 0.06529  -0.05889 -0.12169 174 THR A N   
1423 C CA  . THR A 167 ? 0.30570 0.32563 0.24738 0.06033  -0.06926 -0.12482 174 THR A CA  
1424 C C   . THR A 167 ? 0.45394 0.45767 0.41990 0.04839  -0.07726 -0.13180 174 THR A C   
1425 O O   . THR A 167 ? 0.43079 0.41840 0.40209 0.04838  -0.08001 -0.14195 174 THR A O   
1426 C CB  . THR A 167 ? 0.39439 0.42348 0.31386 0.07295  -0.07897 -0.13869 174 THR A CB  
1427 O OG1 . THR A 167 ? 0.48108 0.52649 0.37807 0.08446  -0.06870 -0.12866 174 THR A OG1 
1428 C CG2 . THR A 167 ? 0.48328 0.51933 0.40909 0.06841  -0.09160 -0.14245 174 THR A CG2 
1429 N N   . ASP A 168 ? 0.33046 0.33835 0.31250 0.03846  -0.08023 -0.12530 175 ASP A N   
1430 C CA  . ASP A 168 ? 0.34144 0.33704 0.34971 0.02611  -0.08558 -0.12856 175 ASP A CA  
1431 C C   . ASP A 168 ? 0.47777 0.47648 0.49150 0.02498  -0.10190 -0.14424 175 ASP A C   
1432 O O   . ASP A 168 ? 0.49851 0.51399 0.50545 0.02841  -0.10716 -0.14359 175 ASP A O   
1433 C CB  . ASP A 168 ? 0.32734 0.32773 0.35166 0.01660  -0.07790 -0.11176 175 ASP A CB  
1434 C CG  . ASP A 168 ? 0.48155 0.47090 0.53345 0.00427  -0.07989 -0.11153 175 ASP A CG  
1435 O OD1 . ASP A 168 ? 0.59140 0.56393 0.64950 0.00214  -0.07854 -0.11507 175 ASP A OD1 
1436 O OD2 . ASP A 168 ? 0.41568 0.41361 0.48372 -0.00269 -0.08217 -0.10683 175 ASP A OD2 
1437 N N   . THR A 169 ? 0.57945 0.56182 0.60494 0.02096  -0.11020 -0.15825 176 THR A N   
1438 C CA  . THR A 169 ? 0.87039 0.85473 0.90682 0.01718  -0.12193 -0.16733 176 THR A CA  
1439 C C   . THR A 169 ? 0.70581 0.68679 0.77654 0.00104  -0.12342 -0.16164 176 THR A C   
1440 O O   . THR A 169 ? 0.68730 0.67037 0.77183 -0.00415 -0.13292 -0.16858 176 THR A O   
1441 C CB  . THR A 169 ? 0.88433 0.85367 0.91218 0.02320  -0.12601 -0.18045 176 THR A CB  
1442 O OG1 . THR A 169 ? 0.78576 0.73542 0.81784 0.02175  -0.11726 -0.17691 176 THR A OG1 
1443 C CG2 . THR A 169 ? 0.61591 0.59670 0.61104 0.04012  -0.12736 -0.18721 176 THR A CG2 
1444 N N   . GLY A 170 ? 0.68603 0.66285 0.77082 -0.00656 -0.11372 -0.14886 177 GLY A N   
1445 C CA  . GLY A 170 ? 0.71839 0.69595 0.83481 -0.02060 -0.11182 -0.13967 177 GLY A CA  
1446 C C   . GLY A 170 ? 0.54220 0.54251 0.67053 -0.02402 -0.11803 -0.13740 177 GLY A C   
1447 O O   . GLY A 170 ? 0.48994 0.50483 0.60241 -0.01568 -0.12615 -0.14417 177 GLY A O   
1448 N N   . GLU A 171 ? 0.38920 0.39374 0.54555 -0.03526 -0.11365 -0.12684 178 GLU A N   
1449 C CA  . GLU A 171 ? 0.43926 0.46700 0.61070 -0.03821 -0.11849 -0.12340 178 GLU A CA  
1450 C C   . GLU A 171 ? 0.36856 0.41300 0.51993 -0.02774 -0.11712 -0.11858 178 GLU A C   
1451 O O   . GLU A 171 ? 0.32621 0.36610 0.46561 -0.02450 -0.10263 -0.10475 178 GLU A O   
1452 C CB  . GLU A 171 ? 0.45491 0.48378 0.65734 -0.05021 -0.10902 -0.10939 178 GLU A CB  
1453 C CG  . GLU A 171 ? 0.44056 0.49036 0.66757 -0.05617 -0.11348 -0.10639 178 GLU A CG  
1454 C CD  . GLU A 171 ? 0.44900 0.49802 0.68432 -0.06020 -0.12604 -0.11905 178 GLU A CD  
1455 O OE1 . GLU A 171 ? 0.44370 0.47419 0.68825 -0.06711 -0.12559 -0.12209 178 GLU A OE1 
1456 O OE2 . GLU A 171 ? 0.48579 0.55305 0.71797 -0.05576 -0.13684 -0.12592 178 GLU A OE2 
1457 N N   . PRO A 172 ? 0.36580 0.42777 0.50822 -0.02062 -0.12874 -0.12597 179 PRO A N   
1458 C CA  . PRO A 172 ? 0.33970 0.41438 0.45897 -0.00895 -0.12328 -0.11584 179 PRO A CA  
1459 C C   . PRO A 172 ? 0.36550 0.44791 0.49942 -0.01236 -0.11153 -0.09819 179 PRO A C   
1460 O O   . PRO A 172 ? 0.41729 0.50985 0.58090 -0.02074 -0.11389 -0.09623 179 PRO A O   
1461 C CB  . PRO A 172 ? 0.43959 0.53352 0.55423 -0.00216 -0.14024 -0.12714 179 PRO A CB  
1462 C CG  . PRO A 172 ? 0.45588 0.53688 0.56878 -0.00468 -0.14772 -0.14192 179 PRO A CG  
1463 C CD  . PRO A 172 ? 0.58283 0.64535 0.72048 -0.01847 -0.14103 -0.13989 179 PRO A CD  
1464 N N   . MET A 173 ? 0.30062 0.37977 0.41415 -0.00516 -0.09922 -0.08570 180 MET A N   
1465 C CA  . MET A 173 ? 0.31340 0.39596 0.43625 -0.00657 -0.08746 -0.07051 180 MET A CA  
1466 C C   . MET A 173 ? 0.44123 0.54012 0.55943 0.00216  -0.08892 -0.06358 180 MET A C   
1467 O O   . MET A 173 ? 0.41238 0.51526 0.54084 0.00197  -0.08061 -0.05277 180 MET A O   
1468 C CB  . MET A 173 ? 0.34670 0.41344 0.45393 -0.00531 -0.07275 -0.06081 180 MET A CB  
1469 C CG  . MET A 173 ? 0.54123 0.59215 0.65571 -0.01306 -0.06651 -0.06112 180 MET A CG  
1470 S SD  . MET A 173 ? 0.43680 0.47559 0.52279 -0.00641 -0.05642 -0.05551 180 MET A SD  
1471 C CE  . MET A 173 ? 0.34624 0.39201 0.43411 -0.00397 -0.04823 -0.04231 180 MET A CE  
1472 N N   . GLY A 174 ? 0.31281 0.41942 0.41264 0.01159  -0.09740 -0.06798 181 GLY A N   
1473 C CA  . GLY A 174 ? 0.23775 0.35857 0.33372 0.02091  -0.09833 -0.05944 181 GLY A CA  
1474 C C   . GLY A 174 ? 0.25916 0.36821 0.33141 0.02802  -0.08599 -0.04712 181 GLY A C   
1475 O O   . GLY A 174 ? 0.25768 0.36903 0.30723 0.03792  -0.08820 -0.04507 181 GLY A O   
1476 N N   . ARG A 175 ? 0.19489 0.29226 0.27306 0.02320  -0.07330 -0.03864 182 ARG A N   
1477 C CA  . ARG A 175 ? 0.18545 0.26915 0.24545 0.02692  -0.06195 -0.02860 182 ARG A CA  
1478 C C   . ARG A 175 ? 0.19844 0.27067 0.26920 0.01931  -0.05141 -0.02477 182 ARG A C   
1479 O O   . ARG A 175 ? 0.21022 0.28855 0.30033 0.01608  -0.05037 -0.02371 182 ARG A O   
1480 C CB  . ARG A 175 ? 0.21547 0.30453 0.26970 0.03690  -0.06089 -0.01838 182 ARG A CB  
1481 C CG  . ARG A 175 ? 0.21864 0.29153 0.25530 0.04006  -0.04989 -0.00761 182 ARG A CG  
1482 C CD  . ARG A 175 ? 0.20681 0.27827 0.24365 0.04811  -0.04642 0.00333  182 ARG A CD  
1483 N NE  . ARG A 175 ? 0.20963 0.28341 0.26628 0.04571  -0.04391 0.00297  182 ARG A NE  
1484 C CZ  . ARG A 175 ? 0.19376 0.28349 0.26440 0.05099  -0.04938 0.00320  182 ARG A CZ  
1485 N NH1 . ARG A 175 ? 0.20170 0.30793 0.27035 0.05849  -0.06004 0.00223  182 ARG A NH1 
1486 N NH2 . ARG A 175 ? 0.19445 0.28707 0.28276 0.04936  -0.04469 0.00392  182 ARG A NH2 
1487 N N   . GLY A 176 ? 0.25171 0.28589 0.19374 0.03332  -0.02800 0.03546  183 GLY A N   
1488 C CA  . GLY A 176 ? 0.22852 0.25088 0.19334 0.02665  -0.02134 0.03102  183 GLY A CA  
1489 C C   . GLY A 176 ? 0.22257 0.24050 0.18765 0.01876  -0.01654 0.01934  183 GLY A C   
1490 O O   . GLY A 176 ? 0.24366 0.26354 0.19098 0.02099  -0.01257 0.01811  183 GLY A O   
1491 N N   . THR A 177 ? 0.20523 0.21801 0.18827 0.01229  -0.01577 0.01213  184 THR A N   
1492 C CA  . THR A 177 ? 0.18775 0.19746 0.17404 0.00698  -0.01096 0.00401  184 THR A CA  
1493 C C   . THR A 177 ? 0.22910 0.23760 0.22675 0.00186  -0.01657 -0.00660 184 THR A C   
1494 O O   . THR A 177 ? 0.20734 0.21613 0.21756 0.00056  -0.01917 -0.00540 184 THR A O   
1495 C CB  . THR A 177 ? 0.21494 0.21852 0.21199 0.00225  -0.00158 0.01165  184 THR A CB  
1496 O OG1 . THR A 177 ? 0.26198 0.26709 0.24984 0.00469  0.00540  0.02401  184 THR A OG1 
1497 C CG2 . THR A 177 ? 0.23051 0.23836 0.23750 -0.00276 0.00202  0.00577  184 THR A CG2 
1498 N N   . LYS A 178 ? 0.20814 0.21380 0.19974 0.00078  -0.01689 -0.01577 185 LYS A N   
1499 C CA  . LYS A 178 ? 0.21282 0.21337 0.21355 -0.00458 -0.02066 -0.02370 185 LYS A CA  
1500 C C   . LYS A 178 ? 0.21667 0.21358 0.22137 -0.00329 -0.01345 -0.02492 185 LYS A C   
1501 O O   . LYS A 178 ? 0.23213 0.22870 0.22542 0.00332  -0.00827 -0.02612 185 LYS A O   
1502 C CB  . LYS A 178 ? 0.28575 0.28029 0.27154 -0.00676 -0.02961 -0.03312 185 LYS A CB  
1503 C CG  . LYS A 178 ? 0.39773 0.38244 0.38894 -0.01388 -0.03380 -0.03978 185 LYS A CG  
1504 C CD  . LYS A 178 ? 0.46670 0.44029 0.44070 -0.02082 -0.04572 -0.04962 185 LYS A CD  
1505 C CE  . LYS A 178 ? 0.62052 0.60348 0.57806 -0.01892 -0.05334 -0.04976 185 LYS A CE  
1506 N NZ  . LYS A 178 ? 0.68337 0.65211 0.62033 -0.02910 -0.06814 -0.06195 185 LYS A NZ  
1507 N N   . VAL A 179 ? 0.19410 0.19099 0.21332 -0.00751 -0.01253 -0.02357 186 VAL A N   
1508 C CA  . VAL A 179 ? 0.18068 0.17972 0.20588 -0.00626 -0.00830 -0.02303 186 VAL A CA  
1509 C C   . VAL A 179 ? 0.21926 0.20857 0.24410 -0.00679 -0.01158 -0.02843 186 VAL A C   
1510 O O   . VAL A 179 ? 0.21565 0.20283 0.24671 -0.01233 -0.01477 -0.02842 186 VAL A O   
1511 C CB  . VAL A 179 ? 0.17422 0.17840 0.21154 -0.01237 -0.00741 -0.01767 186 VAL A CB  
1512 C CG1 . VAL A 179 ? 0.18991 0.20315 0.23569 -0.01193 -0.00656 -0.01615 186 VAL A CG1 
1513 C CG2 . VAL A 179 ? 0.19761 0.20587 0.23555 -0.01462 -0.00384 -0.01046 186 VAL A CG2 
1514 N N   . ILE A 180 ? 0.20175 0.18293 0.21742 0.00017  -0.00948 -0.03208 187 ILE A N   
1515 C CA  . ILE A 180 ? 0.20393 0.16776 0.21554 -0.00000 -0.01197 -0.03602 187 ILE A CA  
1516 C C   . ILE A 180 ? 0.19448 0.16461 0.21442 0.00661  -0.00792 -0.03039 187 ILE A C   
1517 O O   . ILE A 180 ? 0.22287 0.20104 0.24215 0.01780  -0.00201 -0.02786 187 ILE A O   
1518 C CB  . ILE A 180 ? 0.24856 0.18999 0.23856 0.00491  -0.01285 -0.04474 187 ILE A CB  
1519 C CG1 . ILE A 180 ? 0.23991 0.18108 0.21999 -0.00209 -0.01976 -0.04982 187 ILE A CG1 
1520 C CG2 . ILE A 180 ? 0.28938 0.20505 0.27440 0.00192  -0.01575 -0.04757 187 ILE A CG2 
1521 C CD1 . ILE A 180 ? 0.34162 0.25844 0.29262 0.00271  -0.02188 -0.06083 187 ILE A CD1 
1522 N N   . LEU A 181 ? 0.20252 0.17327 0.23034 0.00107  -0.01072 -0.02692 188 LEU A N   
1523 C CA  . LEU A 181 ? 0.18002 0.15978 0.21428 0.00702  -0.00967 -0.02040 188 LEU A CA  
1524 C C   . LEU A 181 ? 0.23347 0.19062 0.25842 0.01364  -0.00874 -0.01981 188 LEU A C   
1525 O O   . LEU A 181 ? 0.24839 0.19059 0.27004 0.00562  -0.01112 -0.01981 188 LEU A O   
1526 C CB  . LEU A 181 ? 0.19643 0.18646 0.23724 -0.00188 -0.01360 -0.01732 188 LEU A CB  
1527 C CG  . LEU A 181 ? 0.20410 0.20448 0.24949 -0.00950 -0.01471 -0.01873 188 LEU A CG  
1528 C CD1 . LEU A 181 ? 0.24183 0.24068 0.28421 -0.01599 -0.01784 -0.01893 188 LEU A CD1 
1529 C CD2 . LEU A 181 ? 0.22945 0.24828 0.28379 -0.00792 -0.01379 -0.01454 188 LEU A CD2 
1530 N N   . HIS A 182 ? 0.22545 0.17990 0.24669 0.02911  -0.00411 -0.01736 189 HIS A N   
1531 C CA  . HIS A 182 ? 0.25935 0.18559 0.26886 0.03902  -0.00209 -0.01518 189 HIS A CA  
1532 C C   . HIS A 182 ? 0.24720 0.19195 0.26741 0.04242  -0.00430 -0.00332 189 HIS A C   
1533 O O   . HIS A 182 ? 0.26043 0.23256 0.29177 0.05354  -0.00328 0.00392  189 HIS A O   
1534 C CB  . HIS A 182 ? 0.25906 0.17140 0.25573 0.05892  0.00566  -0.01826 189 HIS A CB  
1535 C CG  . HIS A 182 ? 0.33317 0.23166 0.31435 0.05578  0.00675  -0.03080 189 HIS A CG  
1536 N ND1 . HIS A 182 ? 0.43882 0.29336 0.39508 0.05254  0.00442  -0.04188 189 HIS A ND1 
1537 C CD2 . HIS A 182 ? 0.33161 0.25350 0.31676 0.05314  0.00826  -0.03329 189 HIS A CD2 
1538 C CE1 . HIS A 182 ? 0.40015 0.25421 0.34410 0.04939  0.00344  -0.05163 189 HIS A CE1 
1539 N NE2 . HIS A 182 ? 0.39206 0.28648 0.35264 0.05174  0.00716  -0.04560 189 HIS A NE2 
1540 N N   . LEU A 183 ? 0.24598 0.18128 0.26371 0.03215  -0.00777 -0.00011 190 LEU A N   
1541 C CA  . LEU A 183 ? 0.23650 0.19328 0.25988 0.03287  -0.01168 0.00973  190 LEU A CA  
1542 C C   . LEU A 183 ? 0.29288 0.24661 0.31321 0.05076  -0.01040 0.02121  190 LEU A C   
1543 O O   . LEU A 183 ? 0.31996 0.24061 0.32868 0.06071  -0.00532 0.02285  190 LEU A O   
1544 C CB  . LEU A 183 ? 0.25063 0.19811 0.26805 0.02002  -0.01286 0.01138  190 LEU A CB  
1545 C CG  . LEU A 183 ? 0.24383 0.20008 0.26598 0.00595  -0.01371 0.00259  190 LEU A CG  
1546 C CD1 . LEU A 183 ? 0.28813 0.23971 0.30551 -0.00258 -0.01165 0.00685  190 LEU A CD1 
1547 C CD2 . LEU A 183 ? 0.25914 0.24119 0.28763 0.00391  -0.01789 -0.00027 190 LEU A CD2 
1548 N N   . LYS A 184 ? 0.27061 0.25767 0.30000 0.05474  -0.01616 0.02960  191 LYS A N   
1549 C CA  . LYS A 184 ? 0.28294 0.27456 0.31055 0.07249  -0.01713 0.04412  191 LYS A CA  
1550 C C   . LYS A 184 ? 0.31933 0.28031 0.32917 0.07062  -0.01593 0.05111  191 LYS A C   
1551 O O   . LYS A 184 ? 0.31664 0.27031 0.32010 0.05397  -0.01659 0.04683  191 LYS A O   
1552 C CB  . LYS A 184 ? 0.28302 0.32268 0.32408 0.07163  -0.02792 0.05163  191 LYS A CB  
1553 C CG  . LYS A 184 ? 0.28599 0.36332 0.35033 0.07273  -0.02893 0.05027  191 LYS A CG  
1554 C CD  . LYS A 184 ? 0.35040 0.47662 0.43016 0.06429  -0.04335 0.05724  191 LYS A CD  
1555 C CE  . LYS A 184 ? 0.36224 0.51426 0.45826 0.04443  -0.04854 0.04990  191 LYS A CE  
1556 N NZ  . LYS A 184 ? 0.36929 0.57407 0.48591 0.03432  -0.06477 0.05869  191 LYS A NZ  
1557 N N   . GLU A 185 ? 0.36309 0.30693 0.36517 0.08971  -0.01271 0.06412  192 GLU A N   
1558 C CA  . GLU A 185 ? 0.39865 0.30672 0.38285 0.08826  -0.00941 0.07378  192 GLU A CA  
1559 C C   . GLU A 185 ? 0.40453 0.33237 0.38266 0.07691  -0.01494 0.08018  192 GLU A C   
1560 O O   . GLU A 185 ? 0.45981 0.36439 0.42656 0.06589  -0.01022 0.08377  192 GLU A O   
1561 C CB  . GLU A 185 ? 0.49264 0.38118 0.46852 0.11436  -0.00563 0.08967  192 GLU A CB  
1562 C CG  . GLU A 185 ? 0.83350 0.66260 0.78938 0.11365  0.00194  0.09600  192 GLU A CG  
1563 C CD  . GLU A 185 ? 1.20817 1.00594 1.15334 0.14339  0.00799  0.10766  192 GLU A CD  
1564 O OE1 . GLU A 185 ? 1.11473 0.87068 1.05086 0.14652  0.01440  0.09626  192 GLU A OE1 
1565 O OE2 . GLU A 185 ? 1.19275 1.01259 1.13865 0.16065  0.00495  0.12504  192 GLU A OE2 
1566 N N   A ASP A 186 ? 0.35007 0.32058 0.33414 0.07861  -0.02482 0.08194  193 ASP A N   
1567 N N   B ASP A 186 ? 0.35007 0.32058 0.33414 0.07861  -0.02482 0.08194  193 ASP A N   
1568 C CA  A ASP A 186 ? 0.35011 0.33610 0.31998 0.07052  -0.03100 0.08639  193 ASP A CA  
1569 C CA  B ASP A 186 ? 0.35011 0.33610 0.31998 0.07052  -0.03100 0.08639  193 ASP A CA  
1570 C C   A ASP A 186 ? 0.33376 0.32957 0.30355 0.05068  -0.03278 0.06993  193 ASP A C   
1571 C C   B ASP A 186 ? 0.33376 0.32957 0.30355 0.05068  -0.03278 0.06993  193 ASP A C   
1572 O O   A ASP A 186 ? 0.33967 0.34704 0.29326 0.04503  -0.03776 0.06992  193 ASP A O   
1573 O O   B ASP A 186 ? 0.33967 0.34704 0.29326 0.04503  -0.03776 0.06992  193 ASP A O   
1574 C CB  A ASP A 186 ? 0.38693 0.40960 0.35621 0.08249  -0.04378 0.09806  193 ASP A CB  
1575 C CB  B ASP A 186 ? 0.38693 0.40960 0.35621 0.08249  -0.04378 0.09806  193 ASP A CB  
1576 C CG  A ASP A 186 ? 0.39323 0.45585 0.38544 0.07990  -0.05367 0.09031  193 ASP A CG  
1577 C CG  B ASP A 186 ? 0.39323 0.45585 0.38544 0.07990  -0.05367 0.09031  193 ASP A CG  
1578 O OD1 A ASP A 186 ? 0.46187 0.52109 0.46921 0.07246  -0.04861 0.07732  193 ASP A OD1 
1579 O OD1 B ASP A 186 ? 0.46187 0.52109 0.46921 0.07246  -0.04861 0.07732  193 ASP A OD1 
1580 O OD2 A ASP A 186 ? 0.51319 0.61361 0.50904 0.08461  -0.06731 0.09899  193 ASP A OD2 
1581 O OD2 B ASP A 186 ? 0.51319 0.61361 0.50904 0.08461  -0.06731 0.09899  193 ASP A OD2 
1582 N N   . GLN A 187 ? 0.29585 0.28346 0.27909 0.04194  -0.02810 0.05633  194 GLN A N   
1583 C CA  . GLN A 187 ? 0.27795 0.27212 0.26189 0.02656  -0.02875 0.04216  194 GLN A CA  
1584 C C   . GLN A 187 ? 0.26035 0.23141 0.24406 0.01766  -0.01847 0.03805  194 GLN A C   
1585 O O   . GLN A 187 ? 0.28389 0.25775 0.27425 0.00848  -0.01715 0.02658  194 GLN A O   
1586 C CB  . GLN A 187 ? 0.26826 0.28098 0.26973 0.02301  -0.03384 0.03205  194 GLN A CB  
1587 C CG  . GLN A 187 ? 0.26403 0.30928 0.27188 0.02833  -0.04566 0.03843  194 GLN A CG  
1588 C CD  . GLN A 187 ? 0.31902 0.37626 0.30821 0.02178  -0.05632 0.03871  194 GLN A CD  
1589 O OE1 . GLN A 187 ? 0.33006 0.37561 0.30482 0.01068  -0.05529 0.02807  194 GLN A OE1 
1590 N NE2 . GLN A 187 ? 0.33412 0.41590 0.32195 0.02952  -0.06738 0.05014  194 GLN A NE2 
1591 N N   . THR A 188 ? 0.31024 0.26062 0.28722 0.01921  -0.01171 0.04896  195 THR A N   
1592 C CA  . THR A 188 ? 0.32803 0.26237 0.31095 0.00724  -0.00383 0.04662  195 THR A CA  
1593 C C   . THR A 188 ? 0.32254 0.26972 0.30037 -0.00018 0.00151  0.04675  195 THR A C   
1594 O O   . THR A 188 ? 0.32396 0.26843 0.31188 -0.01017 0.00791  0.04682  195 THR A O   
1595 C CB  . THR A 188 ? 0.37718 0.28069 0.35698 0.00720  0.00130  0.05862  195 THR A CB  
1596 O OG1 . THR A 188 ? 0.41395 0.31559 0.37856 0.01313  0.00444  0.07554  195 THR A OG1 
1597 C CG2 . THR A 188 ? 0.37219 0.25543 0.35356 0.01755  -0.00150 0.05539  195 THR A CG2 
1598 N N   . GLU A 189 ? 0.31222 0.27403 0.27337 0.00508  -0.00094 0.04719  196 GLU A N   
1599 C CA  . GLU A 189 ? 0.29804 0.26905 0.24942 0.00218  0.00600  0.04418  196 GLU A CA  
1600 C C   . GLU A 189 ? 0.29524 0.27098 0.26167 -0.00371 0.00686  0.03054  196 GLU A C   
1601 O O   . GLU A 189 ? 0.30059 0.28262 0.26777 -0.00503 0.01605  0.03048  196 GLU A O   
1602 C CB  . GLU A 189 ? 0.31998 0.29954 0.24387 0.00877  0.00041  0.04144  196 GLU A CB  
1603 C CG  . GLU A 189 ? 0.32764 0.31421 0.25247 0.00691  -0.01322 0.02668  196 GLU A CG  
1604 C CD  . GLU A 189 ? 0.36926 0.36262 0.26557 0.01012  -0.02317 0.02527  196 GLU A CD  
1605 O OE1 . GLU A 189 ? 0.40398 0.40553 0.29632 0.01572  -0.03102 0.03629  196 GLU A OE1 
1606 O OE2 . GLU A 189 ? 0.38091 0.36956 0.25424 0.00879  -0.02285 0.01446  196 GLU A OE2 
1607 N N   . TYR A 190 ? 0.27756 0.25297 0.25565 -0.00523 -0.00146 0.02077  197 TYR A N   
1608 C CA  . TYR A 190 ? 0.24931 0.22823 0.23854 -0.00946 -0.00104 0.00964  197 TYR A CA  
1609 C C   . TYR A 190 ? 0.26754 0.24466 0.27561 -0.01573 0.00336  0.01175  197 TYR A C   
1610 O O   . TYR A 190 ? 0.27721 0.25874 0.29537 -0.01809 0.00228  0.00423  197 TYR A O   
1611 C CB  . TYR A 190 ? 0.24017 0.22181 0.23370 -0.00984 -0.01061 0.00057  197 TYR A CB  
1612 C CG  . TYR A 190 ? 0.24455 0.23123 0.22069 -0.00829 -0.01799 -0.00159 197 TYR A CG  
1613 C CD1 . TYR A 190 ? 0.27134 0.25310 0.22808 -0.00887 -0.01673 -0.00883 197 TYR A CD1 
1614 C CD2 . TYR A 190 ? 0.26848 0.26431 0.24476 -0.00531 -0.02665 0.00380  197 TYR A CD2 
1615 C CE1 . TYR A 190 ? 0.28714 0.26873 0.22146 -0.01004 -0.02590 -0.01328 197 TYR A CE1 
1616 C CE2 . TYR A 190 ? 0.27084 0.27552 0.23031 -0.00649 -0.03689 0.00232  197 TYR A CE2 
1617 C CZ  . TYR A 190 ? 0.26649 0.26180 0.20237 -0.01066 -0.03764 -0.00761 197 TYR A CZ  
1618 O OH  . TYR A 190 ? 0.31897 0.31793 0.23229 -0.01439 -0.05021 -0.01191 197 TYR A OH  
1619 N N   . LEU A 191 ? 0.25904 0.22824 0.27104 -0.01968 0.00665  0.02209  198 LEU A N   
1620 C CA  . LEU A 191 ? 0.24537 0.21475 0.27469 -0.03045 0.00915  0.02495  198 LEU A CA  
1621 C C   . LEU A 191 ? 0.28783 0.27330 0.32262 -0.03404 0.01956  0.03622  198 LEU A C   
1622 O O   . LEU A 191 ? 0.29211 0.28594 0.34624 -0.04567 0.02110  0.04161  198 LEU A O   
1623 C CB  . LEU A 191 ? 0.27682 0.22154 0.30669 -0.03609 0.00578  0.02916  198 LEU A CB  
1624 C CG  . LEU A 191 ? 0.28559 0.21657 0.30985 -0.02862 -0.00132 0.01939  198 LEU A CG  
1625 C CD1 . LEU A 191 ? 0.38463 0.28256 0.40267 -0.02990 -0.00250 0.02313  198 LEU A CD1 
1626 C CD2 . LEU A 191 ? 0.33034 0.27080 0.36254 -0.03027 -0.00595 0.00632  198 LEU A CD2 
1627 N N   . GLU A 192 ? 0.25824 0.24907 0.27593 -0.02532 0.02668  0.04194  199 GLU A N   
1628 C CA  . GLU A 192 ? 0.25579 0.26435 0.27634 -0.02568 0.04018  0.05500  199 GLU A CA  
1629 C C   . GLU A 192 ? 0.29903 0.32851 0.32436 -0.01814 0.04675  0.04910  199 GLU A C   
1630 O O   . GLU A 192 ? 0.28008 0.30319 0.28938 -0.00820 0.04348  0.03580  199 GLU A O   
1631 C CB  . GLU A 192 ? 0.32719 0.33118 0.32047 -0.01665 0.04632  0.06382  199 GLU A CB  
1632 C CG  . GLU A 192 ? 0.39985 0.38238 0.38659 -0.01998 0.04125  0.07349  199 GLU A CG  
1633 C CD  . GLU A 192 ? 0.94876 0.93016 0.90618 -0.00962 0.04655  0.08481  199 GLU A CD  
1634 O OE1 . GLU A 192 ? 1.16975 1.16630 1.11854 -0.00628 0.06024  0.09448  199 GLU A OE1 
1635 O OE2 . GLU A 192 ? 1.00716 0.97510 0.94963 -0.00333 0.03741  0.08535  199 GLU A OE2 
1636 N N   . GLU A 193 ? 0.30312 0.30621 0.34139 -0.07103 -0.06336 0.03968  200 GLU A N   
1637 C CA  . GLU A 193 ? 0.25006 0.29560 0.31030 -0.07012 -0.06548 0.03900  200 GLU A CA  
1638 C C   . GLU A 193 ? 0.22507 0.30217 0.28772 -0.05514 -0.04482 0.04555  200 GLU A C   
1639 O O   . GLU A 193 ? 0.22848 0.31935 0.28567 -0.04242 -0.04241 0.03788  200 GLU A O   
1640 C CB  . GLU A 193 ? 0.26926 0.33955 0.37458 -0.09280 -0.07593 0.04958  200 GLU A CB  
1641 C CG  . GLU A 193 ? 0.31556 0.42759 0.44689 -0.08778 -0.08383 0.04891  200 GLU A CG  
1642 C CD  . GLU A 193 ? 0.72124 0.87884 0.91629 -0.10812 -0.09293 0.06379  200 GLU A CD  
1643 O OE1 . GLU A 193 ? 0.47379 0.63039 0.69379 -0.13013 -0.08936 0.07579  200 GLU A OE1 
1644 O OE2 . GLU A 193 ? 0.46948 0.66487 0.69347 -0.10252 -0.10508 0.06538  200 GLU A OE2 
1645 N N   . ARG A 194 ? 0.25044 0.33405 0.31640 -0.05748 -0.02975 0.06016  201 ARG A N   
1646 C CA  . ARG A 194 ? 0.24812 0.35650 0.30609 -0.04465 -0.01082 0.06341  201 ARG A CA  
1647 C C   . ARG A 194 ? 0.24651 0.34141 0.27042 -0.02977 -0.01235 0.04947  201 ARG A C   
1648 O O   . ARG A 194 ? 0.25001 0.35731 0.26531 -0.02022 -0.00407 0.04215  201 ARG A O   
1649 C CB  . ARG A 194 ? 0.30630 0.42075 0.36163 -0.04966 0.00667  0.08313  201 ARG A CB  
1650 C CG  . ARG A 194 ? 0.42611 0.51217 0.44716 -0.04526 0.00413  0.08816  201 ARG A CG  
1651 C CD  . ARG A 194 ? 0.48563 0.57003 0.50763 -0.05561 0.01855  0.11365  201 ARG A CD  
1652 N NE  . ARG A 194 ? 0.55217 0.60475 0.54260 -0.05037 0.01342  0.12507  201 ARG A NE  
1653 C CZ  . ARG A 194 ? 0.53164 0.58095 0.49901 -0.05093 0.02727  0.14812  201 ARG A CZ  
1654 N NH1 . ARG A 194 ? 0.54151 0.61643 0.51521 -0.05802 0.05107  0.16062  201 ARG A NH1 
1655 N NH2 . ARG A 194 ? 0.68970 0.71035 0.62722 -0.04211 0.01860  0.16094  201 ARG A NH2 
1656 N N   . ARG A 195 ? 0.23335 0.30217 0.24123 -0.02773 -0.02197 0.04552  202 ARG A N   
1657 C CA  . ARG A 195 ? 0.24861 0.31483 0.23701 -0.01633 -0.02310 0.03550  202 ARG A CA  
1658 C C   . ARG A 195 ? 0.23212 0.29752 0.22090 -0.01307 -0.02584 0.02116  202 ARG A C   
1659 O O   . ARG A 195 ? 0.21794 0.29021 0.19856 -0.00842 -0.02172 0.01377  202 ARG A O   
1660 C CB  . ARG A 195 ? 0.25605 0.30105 0.23813 -0.01109 -0.02935 0.03865  202 ARG A CB  
1661 C CG  . ARG A 195 ? 0.25999 0.31365 0.23682 -0.00030 -0.03132 0.03279  202 ARG A CG  
1662 C CD  . ARG A 195 ? 0.30132 0.37603 0.26629 0.00025  -0.03247 0.03774  202 ARG A CD  
1663 N NE  . ARG A 195 ? 0.26970 0.35833 0.24051 0.00674  -0.04044 0.03460  202 ARG A NE  
1664 C CZ  . ARG A 195 ? 0.28871 0.39388 0.25841 0.00193  -0.04319 0.02364  202 ARG A CZ  
1665 N NH1 . ARG A 195 ? 0.28973 0.39177 0.24429 -0.00544 -0.03725 0.01376  202 ARG A NH1 
1666 N NH2 . ARG A 195 ? 0.25111 0.37595 0.23924 0.00465  -0.05158 0.02325  202 ARG A NH2 
1667 N N   . ILE A 196 ? 0.21656 0.26892 0.21013 -0.01717 -0.03405 0.01760  203 ILE A N   
1668 C CA  . ILE A 196 ? 0.22143 0.26873 0.20643 -0.01302 -0.03711 0.00800  203 ILE A CA  
1669 C C   . ILE A 196 ? 0.22778 0.29521 0.22397 -0.00988 -0.03261 0.00982  203 ILE A C   
1670 O O   . ILE A 196 ? 0.23267 0.29543 0.21792 -0.00331 -0.02767 0.00423  203 ILE A O   
1671 C CB  . ILE A 196 ? 0.23701 0.26254 0.21338 -0.01851 -0.05086 0.00350  203 ILE A CB  
1672 C CG1 . ILE A 196 ? 0.28056 0.27395 0.23824 -0.01640 -0.05031 -0.00198 203 ILE A CG1 
1673 C CG2 . ILE A 196 ? 0.27554 0.29497 0.23417 -0.01267 -0.05409 -0.00231 203 ILE A CG2 
1674 C CD1 . ILE A 196 ? 0.29982 0.26078 0.24288 -0.02696 -0.06634 -0.00885 203 ILE A CD1 
1675 N N   . LYS A 197 ? 0.21144 0.30046 0.23282 -0.01392 -0.03166 0.01902  204 LYS A N   
1676 C CA  . LYS A 197 ? 0.20245 0.31229 0.23964 -0.00497 -0.02285 0.02167  204 LYS A CA  
1677 C C   . LYS A 197 ? 0.21533 0.31849 0.23075 0.00338  -0.00697 0.01473  204 LYS A C   
1678 O O   . LYS A 197 ? 0.23714 0.33299 0.24665 0.01348  -0.00114 0.00910  204 LYS A O   
1679 C CB  . LYS A 197 ? 0.19192 0.33490 0.26738 -0.00938 -0.01670 0.03514  204 LYS A CB  
1680 C CG  . LYS A 197 ? 0.26936 0.42911 0.37852 -0.01888 -0.03538 0.04197  204 LYS A CG  
1681 C CD  . LYS A 197 ? 0.24584 0.44640 0.40390 -0.02742 -0.02425 0.05868  204 LYS A CD  
1682 C CE  . LYS A 197 ? 0.46950 0.68537 0.66546 -0.04840 -0.04842 0.06588  204 LYS A CE  
1683 N NZ  . LYS A 197 ? 0.61650 0.88513 0.87700 -0.05758 -0.03714 0.08527  204 LYS A NZ  
1684 N N   . GLU A 198 ? 0.19974 0.30051 0.19936 -0.00119 -0.00227 0.01513  205 GLU A N   
1685 C CA  . GLU A 198 ? 0.22214 0.31530 0.19478 0.00276  0.00662  0.00634  205 GLU A CA  
1686 C C   . GLU A 198 ? 0.22931 0.30415 0.18923 0.00191  0.00044  -0.00559 205 GLU A C   
1687 O O   . GLU A 198 ? 0.24175 0.30303 0.18686 0.00483  0.00705  -0.01562 205 GLU A O   
1688 C CB  . GLU A 198 ? 0.22769 0.32350 0.18331 -0.00246 0.00531  0.01241  205 GLU A CB  
1689 C CG  . GLU A 198 ? 0.26394 0.35153 0.18564 -0.00260 0.00462  0.00185  205 GLU A CG  
1690 C CD  . GLU A 198 ? 0.29958 0.39179 0.20196 -0.00588 -0.00378 0.01148  205 GLU A CD  
1691 O OE1 . GLU A 198 ? 0.29238 0.38663 0.21326 -0.00707 -0.01473 0.01990  205 GLU A OE1 
1692 O OE2 . GLU A 198 ? 0.31167 0.40151 0.17903 -0.00511 0.00067  0.01033  205 GLU A OE2 
1693 N N   . ILE A 199 ? 0.21299 0.28379 0.17829 -0.00221 -0.00929 -0.00450 206 ILE A N   
1694 C CA  . ILE A 199 ? 0.22923 0.28812 0.18841 -0.00480 -0.01024 -0.01207 206 ILE A CA  
1695 C C   . ILE A 199 ? 0.22887 0.27134 0.18521 0.00003  -0.00584 -0.01378 206 ILE A C   
1696 O O   . ILE A 199 ? 0.26293 0.28899 0.21021 -0.00287 -0.00089 -0.01993 206 ILE A O   
1697 C CB  . ILE A 199 ? 0.24114 0.30136 0.20694 -0.00588 -0.01500 -0.00906 206 ILE A CB  
1698 C CG1 . ILE A 199 ? 0.24048 0.31497 0.21081 -0.00647 -0.02034 -0.00428 206 ILE A CG1 
1699 C CG2 . ILE A 199 ? 0.26483 0.31785 0.23032 -0.00867 -0.00963 -0.01319 206 ILE A CG2 
1700 C CD1 . ILE A 199 ? 0.25770 0.32686 0.23584 -0.00097 -0.02203 0.00028  206 ILE A CD1 
1701 N N   . VAL A 200 ? 0.22291 0.26727 0.18711 0.00592  -0.01046 -0.00681 207 VAL A N   
1702 C CA  . VAL A 200 ? 0.22392 0.25378 0.18414 0.01403  -0.01004 -0.00410 207 VAL A CA  
1703 C C   . VAL A 200 ? 0.24491 0.26843 0.20650 0.02304  0.00108  -0.00709 207 VAL A C   
1704 O O   . VAL A 200 ? 0.29458 0.29085 0.24384 0.02758  0.00671  -0.00882 207 VAL A O   
1705 C CB  . VAL A 200 ? 0.22487 0.26568 0.19620 0.01762  -0.02387 0.00457  207 VAL A CB  
1706 C CG1 . VAL A 200 ? 0.25009 0.28244 0.22136 0.03086  -0.02762 0.01224  207 VAL A CG1 
1707 C CG2 . VAL A 200 ? 0.26491 0.29413 0.21854 0.01025  -0.03264 0.00250  207 VAL A CG2 
1708 N N   . LYS A 201 ? 0.22293 0.26553 0.19541 0.02661  0.00766  -0.00746 208 LYS A N   
1709 C CA  . LYS A 201 ? 0.24490 0.27640 0.21201 0.03943  0.02366  -0.01305 208 LYS A CA  
1710 C C   . LYS A 201 ? 0.27628 0.27453 0.21053 0.03123  0.02910  -0.02913 208 LYS A C   
1711 O O   . LYS A 201 ? 0.37594 0.34214 0.29613 0.03990  0.03938  -0.03676 208 LYS A O   
1712 C CB  . LYS A 201 ? 0.27810 0.33935 0.25973 0.04473  0.03488  -0.00870 208 LYS A CB  
1713 C CG  . LYS A 201 ? 0.34537 0.39416 0.31562 0.06236  0.05841  -0.01632 208 LYS A CG  
1714 C CD  . LYS A 201 ? 0.43016 0.50951 0.40870 0.06564  0.07486  -0.01017 208 LYS A CD  
1715 C CE  . LYS A 201 ? 0.49601 0.56006 0.45680 0.08745  0.10457  -0.01946 208 LYS A CE  
1716 N NZ  . LYS A 201 ? 0.78716 0.89162 0.76902 0.09372  0.12625  -0.00650 208 LYS A NZ  
1717 N N   . LYS A 202 ? 0.30761 0.31269 0.23196 0.01424  0.02036  -0.03394 209 LYS A N   
1718 C CA  . LYS A 202 ? 0.31441 0.29648 0.21307 0.00175  0.01938  -0.04943 209 LYS A CA  
1719 C C   . LYS A 202 ? 0.31942 0.27540 0.21976 -0.00773 0.01746  -0.05142 209 LYS A C   
1720 O O   . LYS A 202 ? 0.36687 0.28690 0.24811 -0.01532 0.02105  -0.06434 209 LYS A O   
1721 C CB  . LYS A 202 ? 0.31805 0.32598 0.21619 -0.01178 0.00606  -0.04873 209 LYS A CB  
1722 C CG  . LYS A 202 ? 0.36685 0.36466 0.25105 -0.03078 -0.00514 -0.06196 209 LYS A CG  
1723 C CD  . LYS A 202 ? 0.52113 0.54583 0.39845 -0.03530 -0.01821 -0.05908 209 LYS A CD  
1724 C CE  . LYS A 202 ? 0.74228 0.77202 0.61768 -0.05576 -0.03734 -0.06859 209 LYS A CE  
1725 N NZ  . LYS A 202 ? 0.59240 0.65750 0.47134 -0.05616 -0.05491 -0.05834 209 LYS A NZ  
1726 N N   . HIS A 203 ? 0.30699 0.27569 0.22564 -0.00901 0.01327  -0.03892 210 HIS A N   
1727 C CA  . HIS A 203 ? 0.32066 0.27034 0.24037 -0.02148 0.01532  -0.03750 210 HIS A CA  
1728 C C   . HIS A 203 ? 0.32592 0.25148 0.24033 -0.01053 0.02172  -0.02529 210 HIS A C   
1729 O O   . HIS A 203 ? 0.37408 0.27456 0.28341 -0.02109 0.02849  -0.02173 210 HIS A O   
1730 C CB  . HIS A 203 ? 0.33765 0.31889 0.27615 -0.03164 0.01021  -0.03201 210 HIS A CB  
1731 C CG  . HIS A 203 ? 0.36234 0.36986 0.31039 -0.04320 -0.00020 -0.03932 210 HIS A CG  
1732 N ND1 . HIS A 203 ? 0.41603 0.41592 0.36201 -0.06165 -0.00600 -0.05067 210 HIS A ND1 
1733 C CD2 . HIS A 203 ? 0.35923 0.39769 0.31588 -0.03869 -0.00892 -0.03571 210 HIS A CD2 
1734 C CE1 . HIS A 203 ? 0.37146 0.40286 0.32491 -0.06748 -0.02074 -0.05298 210 HIS A CE1 
1735 N NE2 . HIS A 203 ? 0.40470 0.45846 0.36455 -0.05192 -0.02111 -0.04243 210 HIS A NE2 
1736 N N   . SER A 204 ? 0.35914 0.29404 0.22002 -0.04435 -0.08044 -0.07891 211 SER A N   
1737 C CA  . SER A 204 ? 0.32772 0.25825 0.21709 -0.03725 -0.06806 -0.07490 211 SER A CA  
1738 C C   . SER A 204 ? 0.33236 0.23983 0.20323 -0.02307 -0.05124 -0.08698 211 SER A C   
1739 O O   . SER A 204 ? 0.36919 0.28191 0.26025 -0.01221 -0.03821 -0.08066 211 SER A O   
1740 C CB  . SER A 204 ? 0.29900 0.25991 0.22086 -0.03127 -0.06176 -0.05658 211 SER A CB  
1741 O OG  . SER A 204 ? 0.35142 0.33218 0.29188 -0.04147 -0.07601 -0.04589 211 SER A OG  
1742 N N   . GLN A 205 ? 0.41435 0.29906 0.24720 -0.02212 -0.05164 -0.10383 212 GLN A N   
1743 C CA  . GLN A 205 ? 0.53029 0.39912 0.34603 -0.00437 -0.03255 -0.11379 212 GLN A CA  
1744 C C   . GLN A 205 ? 0.54854 0.38959 0.37914 0.00162  -0.02642 -0.11870 212 GLN A C   
1745 O O   . GLN A 205 ? 0.59515 0.43287 0.42695 0.01989  -0.00894 -0.11994 212 GLN A O   
1746 C CB  . GLN A 205 ? 0.67472 0.52588 0.44042 -0.00201 -0.03180 -0.13204 212 GLN A CB  
1747 C CG  . GLN A 205 ? 0.61571 0.43961 0.36951 -0.01522 -0.04478 -0.14745 212 GLN A CG  
1748 C CD  . GLN A 205 ? 1.07931 0.92022 0.82822 -0.03535 -0.06735 -0.14506 212 GLN A CD  
1749 O OE1 . GLN A 205 ? 0.59333 0.45516 0.36782 -0.04682 -0.08131 -0.12973 212 GLN A OE1 
1750 N NE2 . GLN A 205 ? 0.80869 0.64276 0.52667 -0.03841 -0.07079 -0.16048 212 GLN A NE2 
1751 N N   . PHE A 206 ? 0.45026 0.27311 0.29433 -0.01300 -0.04000 -0.11921 213 PHE A N   
1752 C CA  . PHE A 206 ? 0.47197 0.26469 0.33010 -0.00850 -0.03483 -0.12055 213 PHE A CA  
1753 C C   . PHE A 206 ? 0.46833 0.28428 0.36910 -0.01135 -0.03508 -0.09870 213 PHE A C   
1754 O O   . PHE A 206 ? 0.57240 0.36717 0.48873 -0.01554 -0.03679 -0.09437 213 PHE A O   
1755 C CB  . PHE A 206 ? 0.54621 0.29507 0.38693 -0.02346 -0.04766 -0.13694 213 PHE A CB  
1756 C CG  . PHE A 206 ? 0.58947 0.32632 0.39613 -0.01796 -0.04174 -0.15635 213 PHE A CG  
1757 C CD1 . PHE A 206 ? 0.69139 0.41458 0.48600 0.00475  -0.02171 -0.16459 213 PHE A CD1 
1758 C CD2 . PHE A 206 ? 0.59597 0.34150 0.38482 -0.03433 -0.05632 -0.16478 213 PHE A CD2 
1759 C CE1 . PHE A 206 ? 0.75331 0.46801 0.51661 0.01042  -0.01539 -0.18278 213 PHE A CE1 
1760 C CE2 . PHE A 206 ? 0.65743 0.39284 0.41146 -0.02896 -0.05151 -0.18376 213 PHE A CE2 
1761 C CZ  . PHE A 206 ? 0.69976 0.41877 0.44016 -0.00673 -0.03040 -0.19333 213 PHE A CZ  
1762 N N   . ILE A 207 ? 0.34115 0.19785 0.25941 -0.00996 -0.03356 -0.08469 214 ILE A N   
1763 C CA  . ILE A 207 ? 0.29621 0.17425 0.24741 -0.00943 -0.03133 -0.06702 214 ILE A CA  
1764 C C   . ILE A 207 ? 0.35922 0.23832 0.31763 0.00933  -0.01667 -0.06251 214 ILE A C   
1765 O O   . ILE A 207 ? 0.36363 0.25424 0.31344 0.02180  -0.00721 -0.06591 214 ILE A O   
1766 C CB  . ILE A 207 ? 0.28394 0.20056 0.24805 -0.01306 -0.03449 -0.05661 214 ILE A CB  
1767 C CG1 . ILE A 207 ? 0.29777 0.21910 0.26254 -0.03016 -0.05012 -0.05641 214 ILE A CG1 
1768 C CG2 . ILE A 207 ? 0.26594 0.20518 0.25756 -0.00929 -0.02961 -0.04145 214 ILE A CG2 
1769 C CD1 . ILE A 207 ? 0.33289 0.25012 0.31961 -0.04398 -0.05841 -0.04898 214 ILE A CD1 
1770 N N   . GLY A 208 ? 0.30640 0.17671 0.28211 0.01129  -0.01487 -0.05260 215 GLY A N   
1771 C CA  . GLY A 208 ? 0.29922 0.16644 0.28068 0.02978  -0.00337 -0.04766 215 GLY A CA  
1772 C C   . GLY A 208 ? 0.29098 0.19781 0.29094 0.03704  0.00068  -0.03346 215 GLY A C   
1773 O O   . GLY A 208 ? 0.30533 0.21496 0.31735 0.04721  0.00501  -0.02226 215 GLY A O   
1774 N N   . TYR A 209 ? 0.26357 0.19922 0.26438 0.03207  -0.00143 -0.03390 216 TYR A N   
1775 C CA  . TYR A 209 ? 0.25323 0.22293 0.26791 0.03650  0.00073  -0.02461 216 TYR A CA  
1776 C C   . TYR A 209 ? 0.26568 0.25085 0.27397 0.03660  0.00317  -0.03113 216 TYR A C   
1777 O O   . TYR A 209 ? 0.28879 0.26461 0.28354 0.02970  0.00037  -0.03862 216 TYR A O   
1778 C CB  . TYR A 209 ? 0.23116 0.21524 0.25538 0.02592  -0.00542 -0.01699 216 TYR A CB  
1779 C CG  . TYR A 209 ? 0.23425 0.20674 0.26595 0.02444  -0.00618 -0.00685 216 TYR A CG  
1780 C CD1 . TYR A 209 ? 0.22556 0.20725 0.26438 0.03426  -0.00248 0.00503  216 TYR A CD1 
1781 C CD2 . TYR A 209 ? 0.22324 0.17675 0.25635 0.01193  -0.01150 -0.00651 216 TYR A CD2 
1782 C CE1 . TYR A 209 ? 0.24145 0.21165 0.28649 0.03320  -0.00205 0.01799  216 TYR A CE1 
1783 C CE2 . TYR A 209 ? 0.24807 0.18976 0.29064 0.00867  -0.01125 0.00547  216 TYR A CE2 
1784 C CZ  . TYR A 209 ? 0.22757 0.17688 0.27566 0.01971  -0.00558 0.01898  216 TYR A CZ  
1785 O OH  . TYR A 209 ? 0.26639 0.20212 0.32302 0.01690  -0.00438 0.03400  216 TYR A OH  
1786 N N   . PRO A 210 ? 0.24654 0.25765 0.26526 0.04222  0.00690  -0.02655 217 PRO A N   
1787 C CA  . PRO A 210 ? 0.22231 0.24940 0.23924 0.03971  0.00968  -0.02927 217 PRO A CA  
1788 C C   . PRO A 210 ? 0.24400 0.27467 0.25970 0.02738  0.00283  -0.02930 217 PRO A C   
1789 O O   . PRO A 210 ? 0.24667 0.28361 0.27069 0.02339  -0.00207 -0.02575 217 PRO A O   
1790 C CB  . PRO A 210 ? 0.22959 0.28517 0.26419 0.04571  0.01266  -0.02249 217 PRO A CB  
1791 C CG  . PRO A 210 ? 0.29623 0.35364 0.33884 0.05028  0.00895  -0.01595 217 PRO A CG  
1792 C CD  . PRO A 210 ? 0.25570 0.28229 0.28867 0.05051  0.00782  -0.01712 217 PRO A CD  
1793 N N   . ILE A 211 ? 0.22163 0.24745 0.22513 0.02329  0.00334  -0.03269 218 ILE A N   
1794 C CA  . ILE A 211 ? 0.19682 0.22500 0.19958 0.01426  -0.00250 -0.03041 218 ILE A CA  
1795 C C   . ILE A 211 ? 0.20298 0.24505 0.20910 0.01290  0.00258  -0.02664 218 ILE A C   
1796 O O   . ILE A 211 ? 0.26848 0.31169 0.26335 0.01528  0.00903  -0.02684 218 ILE A O   
1797 C CB  . ILE A 211 ? 0.23303 0.24676 0.21903 0.00956  -0.00818 -0.03365 218 ILE A CB  
1798 C CG1 . ILE A 211 ? 0.23586 0.23540 0.22265 0.00719  -0.01414 -0.03657 218 ILE A CG1 
1799 C CG2 . ILE A 211 ? 0.24649 0.26646 0.23585 0.00320  -0.01428 -0.02751 218 ILE A CG2 
1800 C CD1 . ILE A 211 ? 0.26672 0.25075 0.23509 0.00021  -0.02225 -0.04264 218 ILE A CD1 
1801 N N   . THR A 212 ? 0.20169 0.25314 0.22216 0.00845  0.00016  -0.02336 219 THR A N   
1802 C CA  . THR A 212 ? 0.18789 0.25066 0.21639 0.00340  0.00369  -0.01864 219 THR A CA  
1803 C C   . THR A 212 ? 0.16961 0.22209 0.19606 -0.00301 -0.00025 -0.01456 219 THR A C   
1804 O O   . THR A 212 ? 0.18676 0.23222 0.21845 -0.00394 -0.00566 -0.01664 219 THR A O   
1805 C CB  . THR A 212 ? 0.18351 0.26059 0.22903 0.00100  0.00174  -0.01934 219 THR A CB  
1806 O OG1 . THR A 212 ? 0.21057 0.30014 0.26036 0.00945  0.00497  -0.01965 219 THR A OG1 
1807 C CG2 . THR A 212 ? 0.18428 0.27295 0.24212 -0.00857 0.00430  -0.01357 219 THR A CG2 
1808 N N   . LEU A 213 ? 0.20031 0.25254 0.21903 -0.00555 0.00346  -0.00772 220 LEU A N   
1809 C CA  . LEU A 213 ? 0.19095 0.23354 0.20952 -0.01048 0.00034  0.00048  220 LEU A CA  
1810 C C   . LEU A 213 ? 0.20299 0.24815 0.23815 -0.01897 0.00315  0.00565  220 LEU A C   
1811 O O   . LEU A 213 ? 0.21605 0.27500 0.25509 -0.02302 0.01051  0.01195  220 LEU A O   
1812 C CB  . LEU A 213 ? 0.24219 0.28437 0.24048 -0.00936 0.00233  0.00769  220 LEU A CB  
1813 C CG  . LEU A 213 ? 0.23831 0.27245 0.23603 -0.01295 -0.00077 0.02106  220 LEU A CG  
1814 C CD1 . LEU A 213 ? 0.24903 0.27168 0.25693 -0.01056 -0.00967 0.02062  220 LEU A CD1 
1815 C CD2 . LEU A 213 ? 0.27347 0.31119 0.24387 -0.01106 -0.00048 0.02806  220 LEU A CD2 
1816 N N   . PHE A 214 ? 0.19683 0.22898 0.24202 -0.02164 -0.00230 0.00213  221 PHE A N   
1817 C CA  . PHE A 214 ? 0.18289 0.20935 0.24269 -0.03227 -0.00241 0.00411  221 PHE A CA  
1818 C C   . PHE A 214 ? 0.21200 0.22751 0.27197 -0.03758 0.00062  0.01952  221 PHE A C   
1819 O O   . PHE A 214 ? 0.25816 0.26515 0.30686 -0.03097 -0.00042 0.02706  221 PHE A O   
1820 C CB  . PHE A 214 ? 0.19164 0.20029 0.25585 -0.03190 -0.00840 -0.00696 221 PHE A CB  
1821 C CG  . PHE A 214 ? 0.19371 0.21452 0.25827 -0.03007 -0.01172 -0.02039 221 PHE A CG  
1822 C CD1 . PHE A 214 ? 0.18956 0.22938 0.24914 -0.02286 -0.01033 -0.02172 221 PHE A CD1 
1823 C CD2 . PHE A 214 ? 0.20065 0.20982 0.26785 -0.03506 -0.01667 -0.03181 221 PHE A CD2 
1824 C CE1 . PHE A 214 ? 0.18719 0.23778 0.24636 -0.01992 -0.01366 -0.03035 221 PHE A CE1 
1825 C CE2 . PHE A 214 ? 0.20201 0.22368 0.26470 -0.03277 -0.02070 -0.04309 221 PHE A CE2 
1826 C CZ  . PHE A 214 ? 0.19572 0.24006 0.25552 -0.02500 -0.01918 -0.04038 221 PHE A CZ  
1827 N N   . VAL A 215 ? 0.21442 0.23319 0.28830 -0.05041 0.00387  0.02680  222 VAL A N   
1828 C CA  . VAL A 215 ? 0.25527 0.26024 0.33184 -0.05735 0.00722  0.04469  222 VAL A CA  
1829 C C   . VAL A 215 ? 0.29109 0.26500 0.38185 -0.06652 0.00198  0.04241  222 VAL A C   
1830 O O   . VAL A 215 ? 0.29105 0.25730 0.38763 -0.06910 -0.00411 0.02483  222 VAL A O   
1831 C CB  . VAL A 215 ? 0.36712 0.39510 0.44744 -0.06530 0.01734  0.06085  222 VAL A CB  
1832 C CG1 . VAL A 215 ? 0.39993 0.44957 0.45732 -0.05248 0.02393  0.06176  222 VAL A CG1 
1833 C CG2 . VAL A 215 ? 0.28313 0.32936 0.38578 -0.07688 0.01725  0.05464  222 VAL A CG2 
1834 N N   . GLU A 216 ? 0.30034 0.25214 0.39179 -0.06826 0.00375  0.05916  223 GLU A N   
1835 C CA  . GLU A 216 ? 0.34593 0.25833 0.44941 -0.07498 -0.00017 0.05788  223 GLU A CA  
1836 C C   . GLU A 216 ? 0.40943 0.31460 0.53089 -0.09606 0.00309  0.07325  223 GLU A C   
1837 O O   . GLU A 216 ? 0.40893 0.33408 0.53030 -0.10051 0.01100  0.09503  223 GLU A O   
1838 C CB  . GLU A 216 ? 0.38471 0.26989 0.48091 -0.05960 -0.00135 0.06664  223 GLU A CB  
1839 C CG  . GLU A 216 ? 0.38187 0.28024 0.46541 -0.04119 -0.00438 0.05569  223 GLU A CG  
1840 C CD  . GLU A 216 ? 0.48071 0.36222 0.56230 -0.02550 -0.00617 0.06810  223 GLU A CD  
1841 O OE1 . GLU A 216 ? 0.42169 0.26771 0.51310 -0.02123 -0.00634 0.06669  223 GLU A OE1 
1842 O OE2 . GLU A 216 ? 0.41696 0.32083 0.48713 -0.01763 -0.00781 0.07945  223 GLU A OE2 
1843 N N   . LYS A 217 ? 0.42759 0.30157 0.56310 -0.10944 -0.00287 0.06204  224 LYS A N   
1844 C CA  . LYS A 217 ? 0.45690 0.31234 0.61329 -0.13265 -0.00203 0.07631  224 LYS A CA  
1845 C C   . LYS A 217 ? 0.67222 0.51073 0.82880 -0.13107 0.00566  0.10795  224 LYS A C   
1846 O O   . LYS A 217 ? 0.68165 0.49412 0.82632 -0.11317 0.00529  0.11259  224 LYS A O   
1847 C CB  . LYS A 217 ? 0.57878 0.38694 0.74213 -0.14328 -0.01145 0.05559  224 LYS A CB  
1848 C CG  . LYS A 217 ? 0.87832 0.66632 1.05000 -0.16319 -0.00960 0.06428  224 LYS A CG  
1849 C CD  . LYS A 217 ? 0.99823 0.75352 1.16555 -0.17490 -0.01873 0.03581  224 LYS A CD  
1850 C CE  . LYS A 217 ? 1.15924 0.85210 1.31024 -0.16154 -0.01832 0.02777  224 LYS A CE  
1851 N NZ  . LYS A 217 ? 0.99519 0.68020 1.13021 -0.13621 -0.02043 0.00887  224 LYS A NZ  
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