data_7HA1
# 
_entry.id   7HA1 
# 
_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   7HA1         pdb_00007ha1 10.2210/pdb7ha1/pdb 
WWPDB D_1001407212 ?            ?                   
# 
_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                        7HA1 
_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 5-bromo-3,3-dimethyl-1,3-dihydro-2H-indol-2-one 240.096   1   ?        ? ? ? 
3 water       nat water                                           18.015    348 ?        ? ? ? 
# 
_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 5-bromo-3,3-dimethyl-1,3-dihydro-2H-indol-2-one A1AX6 
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 
A1AX6 non-polymer         . 5-bromo-3,3-dimethyl-1,3-dihydro-2H-indol-2-one ? 'C10 H10 Br N O' 240.096 
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        A1AX6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AX6 
_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 A1AX6 1   301 301 A1AX6 DDM A . 
C 3 HOH   1   401 335 HOH   HOH A . 
C 3 HOH   2   402 341 HOH   HOH A . 
C 3 HOH   3   403 259 HOH   HOH A . 
C 3 HOH   4   404 246 HOH   HOH A . 
C 3 HOH   5   405 173 HOH   HOH A . 
C 3 HOH   6   406 290 HOH   HOH A . 
C 3 HOH   7   407 162 HOH   HOH A . 
C 3 HOH   8   408 249 HOH   HOH A . 
C 3 HOH   9   409 296 HOH   HOH A . 
C 3 HOH   10  410 73  HOH   HOH A . 
C 3 HOH   11  411 142 HOH   HOH A . 
C 3 HOH   12  412 269 HOH   HOH A . 
C 3 HOH   13  413 343 HOH   HOH A . 
C 3 HOH   14  414 307 HOH   HOH A . 
C 3 HOH   15  415 81  HOH   HOH A . 
C 3 HOH   16  416 89  HOH   HOH A . 
C 3 HOH   17  417 45  HOH   HOH A . 
C 3 HOH   18  418 325 HOH   HOH A . 
C 3 HOH   19  419 42  HOH   HOH A . 
C 3 HOH   20  420 185 HOH   HOH A . 
C 3 HOH   21  421 133 HOH   HOH A . 
C 3 HOH   22  422 337 HOH   HOH A . 
C 3 HOH   23  423 164 HOH   HOH A . 
C 3 HOH   24  424 119 HOH   HOH A . 
C 3 HOH   25  425 64  HOH   HOH A . 
C 3 HOH   26  426 36  HOH   HOH A . 
C 3 HOH   27  427 195 HOH   HOH A . 
C 3 HOH   28  428 126 HOH   HOH A . 
C 3 HOH   29  429 237 HOH   HOH A . 
C 3 HOH   30  430 58  HOH   HOH A . 
C 3 HOH   31  431 149 HOH   HOH A . 
C 3 HOH   32  432 114 HOH   HOH A . 
C 3 HOH   33  433 125 HOH   HOH A . 
C 3 HOH   34  434 15  HOH   HOH A . 
C 3 HOH   35  435 139 HOH   HOH A . 
C 3 HOH   36  436 46  HOH   HOH A . 
C 3 HOH   37  437 233 HOH   HOH A . 
C 3 HOH   38  438 282 HOH   HOH A . 
C 3 HOH   39  439 92  HOH   HOH A . 
C 3 HOH   40  440 177 HOH   HOH A . 
C 3 HOH   41  441 11  HOH   HOH A . 
C 3 HOH   42  442 115 HOH   HOH A . 
C 3 HOH   43  443 55  HOH   HOH A . 
C 3 HOH   44  444 80  HOH   HOH A . 
C 3 HOH   45  445 268 HOH   HOH A . 
C 3 HOH   46  446 47  HOH   HOH A . 
C 3 HOH   47  447 127 HOH   HOH A . 
C 3 HOH   48  448 103 HOH   HOH A . 
C 3 HOH   49  449 100 HOH   HOH A . 
C 3 HOH   50  450 16  HOH   HOH A . 
C 3 HOH   51  451 26  HOH   HOH A . 
C 3 HOH   52  452 97  HOH   HOH A . 
C 3 HOH   53  453 321 HOH   HOH A . 
C 3 HOH   54  454 183 HOH   HOH A . 
C 3 HOH   55  455 238 HOH   HOH A . 
C 3 HOH   56  456 141 HOH   HOH A . 
C 3 HOH   57  457 263 HOH   HOH A . 
C 3 HOH   58  458 6   HOH   HOH A . 
C 3 HOH   59  459 44  HOH   HOH A . 
C 3 HOH   60  460 21  HOH   HOH A . 
C 3 HOH   61  461 347 HOH   HOH A . 
C 3 HOH   62  462 156 HOH   HOH A . 
C 3 HOH   63  463 60  HOH   HOH A . 
C 3 HOH   64  464 56  HOH   HOH A . 
C 3 HOH   65  465 12  HOH   HOH A . 
C 3 HOH   66  466 1   HOH   HOH A . 
C 3 HOH   67  467 338 HOH   HOH A . 
C 3 HOH   68  468 324 HOH   HOH A . 
C 3 HOH   69  469 14  HOH   HOH A . 
C 3 HOH   70  470 318 HOH   HOH A . 
C 3 HOH   71  471 94  HOH   HOH A . 
C 3 HOH   72  472 38  HOH   HOH A . 
C 3 HOH   73  473 59  HOH   HOH A . 
C 3 HOH   74  474 87  HOH   HOH A . 
C 3 HOH   75  475 40  HOH   HOH A . 
C 3 HOH   76  476 9   HOH   HOH A . 
C 3 HOH   77  477 330 HOH   HOH A . 
C 3 HOH   78  478 25  HOH   HOH A . 
C 3 HOH   79  479 61  HOH   HOH A . 
C 3 HOH   80  480 93  HOH   HOH A . 
C 3 HOH   81  481 86  HOH   HOH A . 
C 3 HOH   82  482 145 HOH   HOH A . 
C 3 HOH   83  483 18  HOH   HOH A . 
C 3 HOH   84  484 240 HOH   HOH A . 
C 3 HOH   85  485 286 HOH   HOH A . 
C 3 HOH   86  486 71  HOH   HOH A . 
C 3 HOH   87  487 75  HOH   HOH A . 
C 3 HOH   88  488 101 HOH   HOH A . 
C 3 HOH   89  489 4   HOH   HOH A . 
C 3 HOH   90  490 19  HOH   HOH A . 
C 3 HOH   91  491 178 HOH   HOH A . 
C 3 HOH   92  492 27  HOH   HOH A . 
C 3 HOH   93  493 339 HOH   HOH A . 
C 3 HOH   94  494 10  HOH   HOH A . 
C 3 HOH   95  495 72  HOH   HOH A . 
C 3 HOH   96  496 17  HOH   HOH A . 
C 3 HOH   97  497 23  HOH   HOH A . 
C 3 HOH   98  498 99  HOH   HOH A . 
C 3 HOH   99  499 287 HOH   HOH A . 
C 3 HOH   100 500 255 HOH   HOH A . 
C 3 HOH   101 501 161 HOH   HOH A . 
C 3 HOH   102 502 231 HOH   HOH A . 
C 3 HOH   103 503 117 HOH   HOH A . 
C 3 HOH   104 504 280 HOH   HOH A . 
C 3 HOH   105 505 102 HOH   HOH A . 
C 3 HOH   106 506 53  HOH   HOH A . 
C 3 HOH   107 507 52  HOH   HOH A . 
C 3 HOH   108 508 293 HOH   HOH A . 
C 3 HOH   109 509 65  HOH   HOH A . 
C 3 HOH   110 510 39  HOH   HOH A . 
C 3 HOH   111 511 50  HOH   HOH A . 
C 3 HOH   112 512 336 HOH   HOH A . 
C 3 HOH   113 513 166 HOH   HOH A . 
C 3 HOH   114 514 203 HOH   HOH A . 
C 3 HOH   115 515 43  HOH   HOH A . 
C 3 HOH   116 516 327 HOH   HOH A . 
C 3 HOH   117 517 5   HOH   HOH A . 
C 3 HOH   118 518 91  HOH   HOH A . 
C 3 HOH   119 519 68  HOH   HOH A . 
C 3 HOH   120 520 107 HOH   HOH A . 
C 3 HOH   121 521 41  HOH   HOH A . 
C 3 HOH   122 522 20  HOH   HOH A . 
C 3 HOH   123 523 331 HOH   HOH A . 
C 3 HOH   124 524 85  HOH   HOH A . 
C 3 HOH   125 525 8   HOH   HOH A . 
C 3 HOH   126 526 95  HOH   HOH A . 
C 3 HOH   127 527 3   HOH   HOH A . 
C 3 HOH   128 528 169 HOH   HOH A . 
C 3 HOH   129 529 74  HOH   HOH A . 
C 3 HOH   130 530 224 HOH   HOH A . 
C 3 HOH   131 531 37  HOH   HOH A . 
C 3 HOH   132 532 201 HOH   HOH A . 
C 3 HOH   133 533 303 HOH   HOH A . 
C 3 HOH   134 534 192 HOH   HOH A . 
C 3 HOH   135 535 35  HOH   HOH A . 
C 3 HOH   136 536 140 HOH   HOH A . 
C 3 HOH   137 537 216 HOH   HOH A . 
C 3 HOH   138 538 179 HOH   HOH A . 
C 3 HOH   139 539 67  HOH   HOH A . 
C 3 HOH   140 540 106 HOH   HOH A . 
C 3 HOH   141 541 104 HOH   HOH A . 
C 3 HOH   142 542 191 HOH   HOH A . 
C 3 HOH   143 543 78  HOH   HOH A . 
C 3 HOH   144 544 143 HOH   HOH A . 
C 3 HOH   145 545 138 HOH   HOH A . 
C 3 HOH   146 546 30  HOH   HOH A . 
C 3 HOH   147 547 174 HOH   HOH A . 
C 3 HOH   148 548 33  HOH   HOH A . 
C 3 HOH   149 549 159 HOH   HOH A . 
C 3 HOH   150 550 66  HOH   HOH A . 
C 3 HOH   151 551 273 HOH   HOH A . 
C 3 HOH   152 552 48  HOH   HOH A . 
C 3 HOH   153 553 319 HOH   HOH A . 
C 3 HOH   154 554 24  HOH   HOH A . 
C 3 HOH   155 555 63  HOH   HOH A . 
C 3 HOH   156 556 314 HOH   HOH A . 
C 3 HOH   157 557 158 HOH   HOH A . 
C 3 HOH   158 558 148 HOH   HOH A . 
C 3 HOH   159 559 31  HOH   HOH A . 
C 3 HOH   160 560 297 HOH   HOH A . 
C 3 HOH   161 561 245 HOH   HOH A . 
C 3 HOH   162 562 187 HOH   HOH A . 
C 3 HOH   163 563 244 HOH   HOH A . 
C 3 HOH   164 564 121 HOH   HOH A . 
C 3 HOH   165 565 29  HOH   HOH A . 
C 3 HOH   166 566 124 HOH   HOH A . 
C 3 HOH   167 567 186 HOH   HOH A . 
C 3 HOH   168 568 157 HOH   HOH A . 
C 3 HOH   169 569 227 HOH   HOH A . 
C 3 HOH   170 570 189 HOH   HOH A . 
C 3 HOH   171 571 62  HOH   HOH A . 
C 3 HOH   172 572 306 HOH   HOH A . 
C 3 HOH   173 573 82  HOH   HOH A . 
C 3 HOH   174 574 49  HOH   HOH A . 
C 3 HOH   175 575 84  HOH   HOH A . 
C 3 HOH   176 576 69  HOH   HOH A . 
C 3 HOH   177 577 264 HOH   HOH A . 
C 3 HOH   178 578 110 HOH   HOH A . 
C 3 HOH   179 579 332 HOH   HOH A . 
C 3 HOH   180 580 132 HOH   HOH A . 
C 3 HOH   181 581 265 HOH   HOH A . 
C 3 HOH   182 582 51  HOH   HOH A . 
C 3 HOH   183 583 295 HOH   HOH A . 
C 3 HOH   184 584 251 HOH   HOH A . 
C 3 HOH   185 585 32  HOH   HOH A . 
C 3 HOH   186 586 181 HOH   HOH A . 
C 3 HOH   187 587 13  HOH   HOH A . 
C 3 HOH   188 588 300 HOH   HOH A . 
C 3 HOH   189 589 136 HOH   HOH A . 
C 3 HOH   190 590 88  HOH   HOH A . 
C 3 HOH   191 591 301 HOH   HOH A . 
C 3 HOH   192 592 250 HOH   HOH A . 
C 3 HOH   193 593 105 HOH   HOH A . 
C 3 HOH   194 594 22  HOH   HOH A . 
C 3 HOH   195 595 79  HOH   HOH A . 
C 3 HOH   196 596 180 HOH   HOH A . 
C 3 HOH   197 597 144 HOH   HOH A . 
C 3 HOH   198 598 239 HOH   HOH A . 
C 3 HOH   199 599 223 HOH   HOH A . 
C 3 HOH   200 600 155 HOH   HOH A . 
C 3 HOH   201 601 226 HOH   HOH A . 
C 3 HOH   202 602 34  HOH   HOH A . 
C 3 HOH   203 603 131 HOH   HOH A . 
C 3 HOH   204 604 2   HOH   HOH A . 
C 3 HOH   205 605 184 HOH   HOH A . 
C 3 HOH   206 606 130 HOH   HOH A . 
C 3 HOH   207 607 129 HOH   HOH A . 
C 3 HOH   208 608 108 HOH   HOH A . 
C 3 HOH   209 609 257 HOH   HOH A . 
C 3 HOH   210 610 28  HOH   HOH A . 
C 3 HOH   211 611 83  HOH   HOH A . 
C 3 HOH   212 612 320 HOH   HOH A . 
C 3 HOH   213 613 346 HOH   HOH A . 
C 3 HOH   214 614 122 HOH   HOH A . 
C 3 HOH   215 615 317 HOH   HOH A . 
C 3 HOH   216 616 7   HOH   HOH A . 
C 3 HOH   217 617 217 HOH   HOH A . 
C 3 HOH   218 618 329 HOH   HOH A . 
C 3 HOH   219 619 123 HOH   HOH A . 
C 3 HOH   220 620 150 HOH   HOH A . 
C 3 HOH   221 621 152 HOH   HOH A . 
C 3 HOH   222 622 232 HOH   HOH A . 
C 3 HOH   223 623 165 HOH   HOH A . 
C 3 HOH   224 624 167 HOH   HOH A . 
C 3 HOH   225 625 218 HOH   HOH A . 
C 3 HOH   226 626 98  HOH   HOH A . 
C 3 HOH   227 627 135 HOH   HOH A . 
C 3 HOH   228 628 188 HOH   HOH A . 
C 3 HOH   229 629 285 HOH   HOH A . 
C 3 HOH   230 630 160 HOH   HOH A . 
C 3 HOH   231 631 272 HOH   HOH A . 
C 3 HOH   232 632 278 HOH   HOH A . 
C 3 HOH   233 633 120 HOH   HOH A . 
C 3 HOH   234 634 214 HOH   HOH A . 
C 3 HOH   235 635 230 HOH   HOH A . 
C 3 HOH   236 636 312 HOH   HOH A . 
C 3 HOH   237 637 171 HOH   HOH A . 
C 3 HOH   238 638 215 HOH   HOH A . 
C 3 HOH   239 639 275 HOH   HOH A . 
C 3 HOH   240 640 304 HOH   HOH A . 
C 3 HOH   241 641 220 HOH   HOH A . 
C 3 HOH   242 642 76  HOH   HOH A . 
C 3 HOH   243 643 147 HOH   HOH A . 
C 3 HOH   244 644 109 HOH   HOH A . 
C 3 HOH   245 645 219 HOH   HOH A . 
C 3 HOH   246 646 271 HOH   HOH A . 
C 3 HOH   247 647 200 HOH   HOH A . 
C 3 HOH   248 648 206 HOH   HOH A . 
C 3 HOH   249 649 111 HOH   HOH A . 
C 3 HOH   250 650 289 HOH   HOH A . 
C 3 HOH   251 651 308 HOH   HOH A . 
C 3 HOH   252 652 57  HOH   HOH A . 
C 3 HOH   253 653 196 HOH   HOH A . 
C 3 HOH   254 654 118 HOH   HOH A . 
C 3 HOH   255 655 194 HOH   HOH A . 
C 3 HOH   256 656 322 HOH   HOH A . 
C 3 HOH   257 657 172 HOH   HOH A . 
C 3 HOH   258 658 294 HOH   HOH A . 
C 3 HOH   259 659 209 HOH   HOH A . 
C 3 HOH   260 660 334 HOH   HOH A . 
C 3 HOH   261 661 208 HOH   HOH A . 
C 3 HOH   262 662 225 HOH   HOH A . 
C 3 HOH   263 663 315 HOH   HOH A . 
C 3 HOH   264 664 211 HOH   HOH A . 
C 3 HOH   265 665 283 HOH   HOH A . 
C 3 HOH   266 666 221 HOH   HOH A . 
C 3 HOH   267 667 54  HOH   HOH A . 
C 3 HOH   268 668 292 HOH   HOH A . 
C 3 HOH   269 669 247 HOH   HOH A . 
C 3 HOH   270 670 128 HOH   HOH A . 
C 3 HOH   271 671 210 HOH   HOH A . 
C 3 HOH   272 672 204 HOH   HOH A . 
C 3 HOH   273 673 90  HOH   HOH A . 
C 3 HOH   274 674 228 HOH   HOH A . 
C 3 HOH   275 675 182 HOH   HOH A . 
C 3 HOH   276 676 134 HOH   HOH A . 
C 3 HOH   277 677 274 HOH   HOH A . 
C 3 HOH   278 678 326 HOH   HOH A . 
C 3 HOH   279 679 279 HOH   HOH A . 
C 3 HOH   280 680 276 HOH   HOH A . 
C 3 HOH   281 681 242 HOH   HOH A . 
C 3 HOH   282 682 311 HOH   HOH A . 
C 3 HOH   283 683 260 HOH   HOH A . 
C 3 HOH   284 684 235 HOH   HOH A . 
C 3 HOH   285 685 212 HOH   HOH A . 
C 3 HOH   286 686 333 HOH   HOH A . 
C 3 HOH   287 687 256 HOH   HOH A . 
C 3 HOH   288 688 291 HOH   HOH A . 
C 3 HOH   289 689 190 HOH   HOH A . 
C 3 HOH   290 690 305 HOH   HOH A . 
C 3 HOH   291 691 205 HOH   HOH A . 
C 3 HOH   292 692 344 HOH   HOH A . 
C 3 HOH   293 693 261 HOH   HOH A . 
C 3 HOH   294 694 70  HOH   HOH A . 
C 3 HOH   295 695 193 HOH   HOH A . 
C 3 HOH   296 696 313 HOH   HOH A . 
C 3 HOH   297 697 310 HOH   HOH A . 
C 3 HOH   298 698 340 HOH   HOH A . 
C 3 HOH   299 699 266 HOH   HOH A . 
C 3 HOH   300 700 198 HOH   HOH A . 
C 3 HOH   301 701 77  HOH   HOH A . 
C 3 HOH   302 702 262 HOH   HOH A . 
C 3 HOH   303 703 112 HOH   HOH A . 
C 3 HOH   304 704 252 HOH   HOH A . 
C 3 HOH   305 705 316 HOH   HOH A . 
C 3 HOH   306 706 284 HOH   HOH A . 
C 3 HOH   307 707 302 HOH   HOH A . 
C 3 HOH   308 708 270 HOH   HOH A . 
C 3 HOH   309 709 328 HOH   HOH A . 
C 3 HOH   310 710 154 HOH   HOH A . 
C 3 HOH   311 711 146 HOH   HOH A . 
C 3 HOH   312 712 197 HOH   HOH A . 
C 3 HOH   313 713 243 HOH   HOH A . 
C 3 HOH   314 714 213 HOH   HOH A . 
C 3 HOH   315 715 345 HOH   HOH A . 
C 3 HOH   316 716 176 HOH   HOH A . 
C 3 HOH   317 717 202 HOH   HOH A . 
C 3 HOH   318 718 248 HOH   HOH A . 
C 3 HOH   319 719 153 HOH   HOH A . 
C 3 HOH   320 720 207 HOH   HOH A . 
C 3 HOH   321 721 281 HOH   HOH A . 
C 3 HOH   322 722 323 HOH   HOH A . 
C 3 HOH   323 723 222 HOH   HOH A . 
C 3 HOH   324 724 199 HOH   HOH A . 
C 3 HOH   325 725 348 HOH   HOH A . 
C 3 HOH   326 726 163 HOH   HOH A . 
C 3 HOH   327 727 299 HOH   HOH A . 
C 3 HOH   328 728 241 HOH   HOH A . 
C 3 HOH   329 729 168 HOH   HOH A . 
C 3 HOH   330 730 113 HOH   HOH A . 
C 3 HOH   331 731 229 HOH   HOH A . 
C 3 HOH   332 732 116 HOH   HOH A . 
C 3 HOH   333 733 175 HOH   HOH A . 
C 3 HOH   334 734 277 HOH   HOH A . 
C 3 HOH   335 735 151 HOH   HOH A . 
C 3 HOH   336 736 342 HOH   HOH A . 
C 3 HOH   337 737 234 HOH   HOH A . 
C 3 HOH   338 738 137 HOH   HOH A . 
C 3 HOH   339 739 96  HOH   HOH A . 
C 3 HOH   340 740 236 HOH   HOH A . 
C 3 HOH   341 741 254 HOH   HOH A . 
C 3 HOH   342 742 258 HOH   HOH A . 
C 3 HOH   343 743 309 HOH   HOH A . 
C 3 HOH   344 744 267 HOH   HOH A . 
C 3 HOH   345 745 288 HOH   HOH A . 
C 3 HOH   346 746 253 HOH   HOH A . 
C 3 HOH   347 747 170 HOH   HOH A . 
C 3 HOH   348 748 298 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             591239.512 
_cell.length_a           65.930 
_cell.length_b           89.480 
_cell.length_c           100.220 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HA1 
_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                         7HA1 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HA1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2024-01-13 
_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   0.97919 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97919 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HA1 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             31.300 
_reflns.d_resolution_high            1.460 
_reflns.number_obs                   51301 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.300 
_reflns.pdbx_Rmerge_I_obs            0.061 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        20.300 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              11.200 
_reflns.pdbx_Rrim_I_all              0.064 
_reflns.pdbx_Rpim_I_all              0.018 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     574631 
_reflns.pdbx_scaling_rejects         792 
_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 1.460 1.500  ? 23973 3486 ? 1.150 ? ? ? 6.900  ? 1.600  ? ? ? ? ? ? 92.400 1.244 0.459 0.699 
1 2 6.530 31.300 ? 6467  649  ? 0.047 ? ? ? 10.000 ? 44.200 ? ? ? ? ? ? 98.500 0.050 0.015 0.998 
# 
_refine.entry_id                                 7HA1 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.94 
_refine.pdbx_overall_phase_error                 21.0891 
_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                          0.1754 
_refine.B_iso_mean                               28.55 
_refine.ls_number_reflns_R_free                  2531 
_refine.ls_percent_reflns_obs                    99.20 
_refine.ls_R_factor_R_work                       0.1743 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.46 
_refine.ls_number_reflns_obs                     51279 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  48748 
_refine.ls_d_res_low                             24.80 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1960 
_refine.overall_SU_ML                            0.1770 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         13 
_refine_hist.number_atoms_solvent             348 
_refine_hist.number_atoms_total               2005 
_refine_hist.d_res_high                       1.46 
_refine_hist.d_res_low                        24.80 
# 
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           1684 0.0040 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2273 0.7255 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     260  0.0689 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      289  0.0065 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 226  5.4069 ? ? ? 
# 
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' 1.46 1.49  2426 0.3328 91.10  0.3609 124 . . . . . 
'X-RAY DIFFRACTION' 1.49 1.52  2642 0.2599 97.27  0.2800 134 . . . . . 
'X-RAY DIFFRACTION' 1.52 1.55  2702 0.2244 99.93  0.2440 135 . . . . . 
'X-RAY DIFFRACTION' 1.55 1.59  2693 0.2192 99.96  0.2273 155 . . . . . 
'X-RAY DIFFRACTION' 1.59 1.63  2700 0.2147 100.00 0.2213 154 . . . . . 
'X-RAY DIFFRACTION' 1.63 1.67  2676 0.2139 100.00 0.2482 142 . . . . . 
'X-RAY DIFFRACTION' 1.67 1.72  2683 0.2176 100.00 0.2741 157 . . . . . 
'X-RAY DIFFRACTION' 1.72 1.78  2710 0.2066 99.97  0.2527 152 . . . . . 
'X-RAY DIFFRACTION' 1.78 1.84  2728 0.1987 100.00 0.2212 125 . . . . . 
'X-RAY DIFFRACTION' 1.84 1.91  2734 0.1954 99.72  0.1979 122 . . . . . 
'X-RAY DIFFRACTION' 1.91 2.00  2720 0.1955 99.72  0.2012 135 . . . . . 
'X-RAY DIFFRACTION' 2.00 2.11  2726 0.1833 99.97  0.2121 132 . . . . . 
'X-RAY DIFFRACTION' 2.11 2.24  2726 0.1677 99.90  0.2030 137 . . . . . 
'X-RAY DIFFRACTION' 2.24 2.41  2743 0.1781 99.52  0.2113 140 . . . . . 
'X-RAY DIFFRACTION' 2.41 2.65  2722 0.1739 99.69  0.1893 154 . . . . . 
'X-RAY DIFFRACTION' 2.65 3.04  2747 0.1698 99.62  0.1624 137 . . . . . 
'X-RAY DIFFRACTION' 3.04 3.82  2784 0.1530 99.76  0.1682 145 . . . . . 
'X-RAY DIFFRACTION' 3.82 24.80 2886 0.1525 99.35  0.1887 151 . . . . . 
# 
_struct.entry_id                  7HA1 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with FL0092' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HA1 
_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              7HA1 
_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 7HA1 MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HA1 LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HA1 GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HA1 HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HA1 HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HA1 HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HA1 HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HA1 HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HA1 HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2  AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3  AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4  AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5  AA5 ASN A 99  ? THR A 102 ? ASN A 106 THR A 109 5 ? 4  
HELX_P HELX_P6  AA6 ILE A 103 ? GLN A 116 ? ILE A 110 GLN A 123 1 ? 14 
HELX_P HELX_P7  AA7 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P8  AA8 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P9  AA9 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P10 AB1 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 11  ? ALA A 14  ? GLU A 18  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 TYR A 153 ? SER A 157 ? TYR A 160 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N THR A 142 ? N THR A 149 O ILE A 180 ? O ILE A 187 
AA1 5 6 O LEU A 181 ? O LEU A 188 N LEU A 82  ? N LEU A 89  
AA1 6 7 O THR A 83  ? O THR A 90  N ILE A 74  ? N ILE A 81  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HA1 
_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 636 ? ? O A HOH 663 ? ? 1.80 
2  1 O   A HOH 480 ? ? O A HOH 628 ? ? 1.83 
3  1 O   A HOH 592 ? ? O A HOH 665 ? ? 1.85 
4  1 OD1 A ASP 102 ? ? O A HOH 401 ? ? 1.86 
5  1 O   A HOH 632 ? ? O A HOH 658 ? ? 1.87 
6  1 O   A HOH 572 ? ? O A HOH 686 ? ? 1.94 
7  1 O   A HOH 437 ? ? O A HOH 634 ? ? 1.97 
8  1 OE2 A GLU 120 ? ? O A HOH 402 ? ? 2.00 
9  1 O   A HOH 418 ? ? O A HOH 470 ? ? 2.10 
10 1 O   A HOH 641 ? ? O A HOH 727 ? ? 2.15 
11 1 O   A HOH 453 ? ? O A HOH 632 ? ? 2.16 
12 1 O   A HOH 635 ? ? O A HOH 690 ? ? 2.16 
13 1 O   A HOH 572 ? ? O A HOH 687 ? ? 2.18 
# 
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 682 ? ? 1_555 O A HOH 743 ? ? 8_444 1.91 
2 1 O A HOH 412 ? ? 1_555 O A HOH 612 ? ? 3_555 1.99 
3 1 O A HOH 454 ? ? 1_555 O A HOH 706 ? ? 3_555 2.15 
# 
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 ALA A 166 ? ? 63.47   -144.21 
2 1 ARG A 182 ? ? -171.70 138.14  
# 
_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     701 
_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 12.3607669217  -17.9231763668 -18.7384871289 0.176805983081 0.206441044588 0.20914575658  
0.00226223696923   -0.0254540356062  -0.0259287384421 2.50712820899 0.881058764009 4.73013571076 -0.697300381643 -2.80905478237   
0.473401322393  0.118124706809   -0.303328984311 -0.0165929083456 0.0126136201287 -0.0601589473071 -0.0496780754055  
-0.0488729917539 0.214977670465   -0.0936003481624  
2 ? 'X-RAY DIFFRACTION' refined -5.21244798572 -6.2670199564  -20.9027289615 0.184397549568 0.159072255347 0.19902025687  
-0.00723137662386  -0.00387211952276 -0.0348198144014 1.56985553264 3.90337048766  6.3712343437  -1.48768560897  2.21898703134    
-4.02817457254  -0.0788359626455 0.0883230444172 0.124002544386   0.207602201751  -0.108286490147  0.00538010964821  
-0.494299251417  0.281227792402   0.134960416828    
3 ? 'X-RAY DIFFRACTION' refined -10.1243919534 -14.979459374  -25.1866012667 0.149762771366 0.135090782907 0.197368806405 
-0.000154295932928 -0.0371696685166  -0.0412288771917 1.65754213743 2.93362836675  3.62226043189 -0.291204472755 -0.0766530020879 
-1.58236230112  0.0488655835327  0.0890516527446 -0.124311664722  -0.121151331642 0.0558847120084  0.255617693733    
0.0619896689446  -0.198167446082  -0.140382709823   
4 ? 'X-RAY DIFFRACTION' refined 10.7098430675  -7.50651162656 -17.9062879358 0.178698509232 0.245217783329 0.262268041795 
-0.0411247771114   0.0170997900636   -0.0572006633519 3.40493977074 2.38418767232  4.66888690251 0.265580272412  -1.76538040289   
0.420631628903  0.193502662817   -0.550083473886 0.404366976547   0.167005914951  -0.0488139852986 -0.133943760815   
-0.412873158533  0.854393413931   -0.135830675807   
5 ? 'X-RAY DIFFRACTION' refined 0.886330698851 -19.2972349464 -27.8929813355 0.15796844202  0.127356033476 0.18394083776  
0.00127777679417   -0.0148902124426  -0.0339374741875 2.41853021602 1.78300911985  1.56660760659 -1.10414662042  0.145910944216   
-0.411108993017 0.15622124282    0.215825938495  -0.251772225648  -0.176349449339 -0.0698571286204 0.150131426265    
0.159208337077   0.0587877355354  -0.106642557613   
6 ? 'X-RAY DIFFRACTION' refined -2.57556683895 -23.6786975777 -13.7218857911 0.180160369802 0.154820074175 0.197166149403 
0.00429898506432   -0.0100317158911  0.0106971925874  2.69181271237 3.30339416026  4.61355781128 -0.51727208131  0.0716453830077  
-1.68928203825  0.0134675160233  -0.241973871478 -0.26203389321   0.192901354865  -0.0178176923719 -0.00678685745222 
0.236893575687   0.110169656224   -0.0146113101967  
7 ? 'X-RAY DIFFRACTION' refined -12.1016821652 -14.2323086012 -10.4826782659 0.150762985485 0.197994413732 0.169210326266 
0.00286688783764   0.0106227327974   -0.0170489117169 3.02325534882 1.98169783918  4.41540805787 -0.674315347312 0.658692854301   
-0.867794391958 0.0319230717716  -0.26924418358  -0.101243906032  0.185500866102  -0.0121496248968 0.0726681852805   
-0.0814932717746 -0.0771458355759 -0.00388427545494 
# 
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 99  A 84  . 
;chain 'A' and (resid 66 through 99 )
;
4 4 'X-RAY DIFFRACTION' A 100 A 85  A 136 A 121 . 
;chain 'A' and (resid 100 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 182 A 167 . 
;chain 'A' and (resid 137 through 182 )
;
6 6 'X-RAY DIFFRACTION' A 183 A 168 A 199 A 184 . 
;chain 'A' and (resid 183 through 199 )
;
7 7 'X-RAY DIFFRACTION' A 200 A 185 A 224 A 209 . 
;chain 'A' and (resid 200 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 
A1AX6 C2   C  N N 1   
A1AX6 C3   C  N N 2   
A1AX6 C1   C  N N 3   
A1AX6 C4   C  N N 4   
A1AX6 C5   C  Y N 5   
A1AX6 C6   C  Y N 6   
A1AX6 C10  C  Y N 7   
A1AX6 C7   C  Y N 8   
A1AX6 C8   C  Y N 9   
A1AX6 C9   C  Y N 10  
A1AX6 N1   N  N N 11  
A1AX6 O1   O  N N 12  
A1AX6 BR1  BR N N 13  
A1AX6 H32  H  N N 14  
A1AX6 H31  H  N N 15  
A1AX6 H33  H  N N 16  
A1AX6 H11  H  N N 17  
A1AX6 H13  H  N N 18  
A1AX6 H12  H  N N 19  
A1AX6 H6   H  N N 20  
A1AX6 H7   H  N N 21  
A1AX6 H9   H  N N 22  
A1AX6 HN1  H  N N 23  
ALA   N    N  N N 24  
ALA   CA   C  N S 25  
ALA   C    C  N N 26  
ALA   O    O  N N 27  
ALA   CB   C  N N 28  
ALA   OXT  O  N N 29  
ALA   H    H  N N 30  
ALA   H2   H  N N 31  
ALA   HA   H  N N 32  
ALA   HB1  H  N N 33  
ALA   HB2  H  N N 34  
ALA   HB3  H  N N 35  
ALA   HXT  H  N N 36  
ARG   N    N  N N 37  
ARG   CA   C  N S 38  
ARG   C    C  N N 39  
ARG   O    O  N N 40  
ARG   CB   C  N N 41  
ARG   CG   C  N N 42  
ARG   CD   C  N N 43  
ARG   NE   N  N N 44  
ARG   CZ   C  N N 45  
ARG   NH1  N  N N 46  
ARG   NH2  N  N N 47  
ARG   OXT  O  N N 48  
ARG   H    H  N N 49  
ARG   H2   H  N N 50  
ARG   HA   H  N N 51  
ARG   HB2  H  N N 52  
ARG   HB3  H  N N 53  
ARG   HG2  H  N N 54  
ARG   HG3  H  N N 55  
ARG   HD2  H  N N 56  
ARG   HD3  H  N N 57  
ARG   HE   H  N N 58  
ARG   HH11 H  N N 59  
ARG   HH12 H  N N 60  
ARG   HH21 H  N N 61  
ARG   HH22 H  N N 62  
ARG   HXT  H  N N 63  
ASN   N    N  N N 64  
ASN   CA   C  N S 65  
ASN   C    C  N N 66  
ASN   O    O  N N 67  
ASN   CB   C  N N 68  
ASN   CG   C  N N 69  
ASN   OD1  O  N N 70  
ASN   ND2  N  N N 71  
ASN   OXT  O  N N 72  
ASN   H    H  N N 73  
ASN   H2   H  N N 74  
ASN   HA   H  N N 75  
ASN   HB2  H  N N 76  
ASN   HB3  H  N N 77  
ASN   HD21 H  N N 78  
ASN   HD22 H  N N 79  
ASN   HXT  H  N N 80  
ASP   N    N  N N 81  
ASP   CA   C  N S 82  
ASP   C    C  N N 83  
ASP   O    O  N N 84  
ASP   CB   C  N N 85  
ASP   CG   C  N N 86  
ASP   OD1  O  N N 87  
ASP   OD2  O  N N 88  
ASP   OXT  O  N N 89  
ASP   H    H  N N 90  
ASP   H2   H  N N 91  
ASP   HA   H  N N 92  
ASP   HB2  H  N N 93  
ASP   HB3  H  N N 94  
ASP   HD2  H  N N 95  
ASP   HXT  H  N N 96  
GLN   N    N  N N 97  
GLN   CA   C  N S 98  
GLN   C    C  N N 99  
GLN   O    O  N N 100 
GLN   CB   C  N N 101 
GLN   CG   C  N N 102 
GLN   CD   C  N N 103 
GLN   OE1  O  N N 104 
GLN   NE2  N  N N 105 
GLN   OXT  O  N N 106 
GLN   H    H  N N 107 
GLN   H2   H  N N 108 
GLN   HA   H  N N 109 
GLN   HB2  H  N N 110 
GLN   HB3  H  N N 111 
GLN   HG2  H  N N 112 
GLN   HG3  H  N N 113 
GLN   HE21 H  N N 114 
GLN   HE22 H  N N 115 
GLN   HXT  H  N N 116 
GLU   N    N  N N 117 
GLU   CA   C  N S 118 
GLU   C    C  N N 119 
GLU   O    O  N N 120 
GLU   CB   C  N N 121 
GLU   CG   C  N N 122 
GLU   CD   C  N N 123 
GLU   OE1  O  N N 124 
GLU   OE2  O  N N 125 
GLU   OXT  O  N N 126 
GLU   H    H  N N 127 
GLU   H2   H  N N 128 
GLU   HA   H  N N 129 
GLU   HB2  H  N N 130 
GLU   HB3  H  N N 131 
GLU   HG2  H  N N 132 
GLU   HG3  H  N N 133 
GLU   HE2  H  N N 134 
GLU   HXT  H  N N 135 
GLY   N    N  N N 136 
GLY   CA   C  N N 137 
GLY   C    C  N N 138 
GLY   O    O  N N 139 
GLY   OXT  O  N N 140 
GLY   H    H  N N 141 
GLY   H2   H  N N 142 
GLY   HA2  H  N N 143 
GLY   HA3  H  N N 144 
GLY   HXT  H  N N 145 
HIS   N    N  N N 146 
HIS   CA   C  N S 147 
HIS   C    C  N N 148 
HIS   O    O  N N 149 
HIS   CB   C  N N 150 
HIS   CG   C  Y N 151 
HIS   ND1  N  Y N 152 
HIS   CD2  C  Y N 153 
HIS   CE1  C  Y N 154 
HIS   NE2  N  Y N 155 
HIS   OXT  O  N N 156 
HIS   H    H  N N 157 
HIS   H2   H  N N 158 
HIS   HA   H  N N 159 
HIS   HB2  H  N N 160 
HIS   HB3  H  N N 161 
HIS   HD1  H  N N 162 
HIS   HD2  H  N N 163 
HIS   HE1  H  N N 164 
HIS   HE2  H  N N 165 
HIS   HXT  H  N N 166 
HOH   O    O  N N 167 
HOH   H1   H  N N 168 
HOH   H2   H  N N 169 
ILE   N    N  N N 170 
ILE   CA   C  N S 171 
ILE   C    C  N N 172 
ILE   O    O  N N 173 
ILE   CB   C  N S 174 
ILE   CG1  C  N N 175 
ILE   CG2  C  N N 176 
ILE   CD1  C  N N 177 
ILE   OXT  O  N N 178 
ILE   H    H  N N 179 
ILE   H2   H  N N 180 
ILE   HA   H  N N 181 
ILE   HB   H  N N 182 
ILE   HG12 H  N N 183 
ILE   HG13 H  N N 184 
ILE   HG21 H  N N 185 
ILE   HG22 H  N N 186 
ILE   HG23 H  N N 187 
ILE   HD11 H  N N 188 
ILE   HD12 H  N N 189 
ILE   HD13 H  N N 190 
ILE   HXT  H  N N 191 
LEU   N    N  N N 192 
LEU   CA   C  N S 193 
LEU   C    C  N N 194 
LEU   O    O  N N 195 
LEU   CB   C  N N 196 
LEU   CG   C  N N 197 
LEU   CD1  C  N N 198 
LEU   CD2  C  N N 199 
LEU   OXT  O  N N 200 
LEU   H    H  N N 201 
LEU   H2   H  N N 202 
LEU   HA   H  N N 203 
LEU   HB2  H  N N 204 
LEU   HB3  H  N N 205 
LEU   HG   H  N N 206 
LEU   HD11 H  N N 207 
LEU   HD12 H  N N 208 
LEU   HD13 H  N N 209 
LEU   HD21 H  N N 210 
LEU   HD22 H  N N 211 
LEU   HD23 H  N N 212 
LEU   HXT  H  N N 213 
LYS   N    N  N N 214 
LYS   CA   C  N S 215 
LYS   C    C  N N 216 
LYS   O    O  N N 217 
LYS   CB   C  N N 218 
LYS   CG   C  N N 219 
LYS   CD   C  N N 220 
LYS   CE   C  N N 221 
LYS   NZ   N  N N 222 
LYS   OXT  O  N N 223 
LYS   H    H  N N 224 
LYS   H2   H  N N 225 
LYS   HA   H  N N 226 
LYS   HB2  H  N N 227 
LYS   HB3  H  N N 228 
LYS   HG2  H  N N 229 
LYS   HG3  H  N N 230 
LYS   HD2  H  N N 231 
LYS   HD3  H  N N 232 
LYS   HE2  H  N N 233 
LYS   HE3  H  N N 234 
LYS   HZ1  H  N N 235 
LYS   HZ2  H  N N 236 
LYS   HZ3  H  N N 237 
LYS   HXT  H  N N 238 
MET   N    N  N N 239 
MET   CA   C  N S 240 
MET   C    C  N N 241 
MET   O    O  N N 242 
MET   CB   C  N N 243 
MET   CG   C  N N 244 
MET   SD   S  N N 245 
MET   CE   C  N N 246 
MET   OXT  O  N N 247 
MET   H    H  N N 248 
MET   H2   H  N N 249 
MET   HA   H  N N 250 
MET   HB2  H  N N 251 
MET   HB3  H  N N 252 
MET   HG2  H  N N 253 
MET   HG3  H  N N 254 
MET   HE1  H  N N 255 
MET   HE2  H  N N 256 
MET   HE3  H  N N 257 
MET   HXT  H  N N 258 
PHE   N    N  N N 259 
PHE   CA   C  N S 260 
PHE   C    C  N N 261 
PHE   O    O  N N 262 
PHE   CB   C  N N 263 
PHE   CG   C  Y N 264 
PHE   CD1  C  Y N 265 
PHE   CD2  C  Y N 266 
PHE   CE1  C  Y N 267 
PHE   CE2  C  Y N 268 
PHE   CZ   C  Y N 269 
PHE   OXT  O  N N 270 
PHE   H    H  N N 271 
PHE   H2   H  N N 272 
PHE   HA   H  N N 273 
PHE   HB2  H  N N 274 
PHE   HB3  H  N N 275 
PHE   HD1  H  N N 276 
PHE   HD2  H  N N 277 
PHE   HE1  H  N N 278 
PHE   HE2  H  N N 279 
PHE   HZ   H  N N 280 
PHE   HXT  H  N N 281 
PRO   N    N  N N 282 
PRO   CA   C  N S 283 
PRO   C    C  N N 284 
PRO   O    O  N N 285 
PRO   CB   C  N N 286 
PRO   CG   C  N N 287 
PRO   CD   C  N N 288 
PRO   OXT  O  N N 289 
PRO   H    H  N N 290 
PRO   HA   H  N N 291 
PRO   HB2  H  N N 292 
PRO   HB3  H  N N 293 
PRO   HG2  H  N N 294 
PRO   HG3  H  N N 295 
PRO   HD2  H  N N 296 
PRO   HD3  H  N N 297 
PRO   HXT  H  N N 298 
SER   N    N  N N 299 
SER   CA   C  N S 300 
SER   C    C  N N 301 
SER   O    O  N N 302 
SER   CB   C  N N 303 
SER   OG   O  N N 304 
SER   OXT  O  N N 305 
SER   H    H  N N 306 
SER   H2   H  N N 307 
SER   HA   H  N N 308 
SER   HB2  H  N N 309 
SER   HB3  H  N N 310 
SER   HG   H  N N 311 
SER   HXT  H  N N 312 
THR   N    N  N N 313 
THR   CA   C  N S 314 
THR   C    C  N N 315 
THR   O    O  N N 316 
THR   CB   C  N R 317 
THR   OG1  O  N N 318 
THR   CG2  C  N N 319 
THR   OXT  O  N N 320 
THR   H    H  N N 321 
THR   H2   H  N N 322 
THR   HA   H  N N 323 
THR   HB   H  N N 324 
THR   HG1  H  N N 325 
THR   HG21 H  N N 326 
THR   HG22 H  N N 327 
THR   HG23 H  N N 328 
THR   HXT  H  N N 329 
TRP   N    N  N N 330 
TRP   CA   C  N S 331 
TRP   C    C  N N 332 
TRP   O    O  N N 333 
TRP   CB   C  N N 334 
TRP   CG   C  Y N 335 
TRP   CD1  C  Y N 336 
TRP   CD2  C  Y N 337 
TRP   NE1  N  Y N 338 
TRP   CE2  C  Y N 339 
TRP   CE3  C  Y N 340 
TRP   CZ2  C  Y N 341 
TRP   CZ3  C  Y N 342 
TRP   CH2  C  Y N 343 
TRP   OXT  O  N N 344 
TRP   H    H  N N 345 
TRP   H2   H  N N 346 
TRP   HA   H  N N 347 
TRP   HB2  H  N N 348 
TRP   HB3  H  N N 349 
TRP   HD1  H  N N 350 
TRP   HE1  H  N N 351 
TRP   HE3  H  N N 352 
TRP   HZ2  H  N N 353 
TRP   HZ3  H  N N 354 
TRP   HH2  H  N N 355 
TRP   HXT  H  N N 356 
TYR   N    N  N N 357 
TYR   CA   C  N S 358 
TYR   C    C  N N 359 
TYR   O    O  N N 360 
TYR   CB   C  N N 361 
TYR   CG   C  Y N 362 
TYR   CD1  C  Y N 363 
TYR   CD2  C  Y N 364 
TYR   CE1  C  Y N 365 
TYR   CE2  C  Y N 366 
TYR   CZ   C  Y N 367 
TYR   OH   O  N N 368 
TYR   OXT  O  N N 369 
TYR   H    H  N N 370 
TYR   H2   H  N N 371 
TYR   HA   H  N N 372 
TYR   HB2  H  N N 373 
TYR   HB3  H  N N 374 
TYR   HD1  H  N N 375 
TYR   HD2  H  N N 376 
TYR   HE1  H  N N 377 
TYR   HE2  H  N N 378 
TYR   HH   H  N N 379 
TYR   HXT  H  N N 380 
VAL   N    N  N N 381 
VAL   CA   C  N S 382 
VAL   C    C  N N 383 
VAL   O    O  N N 384 
VAL   CB   C  N N 385 
VAL   CG1  C  N N 386 
VAL   CG2  C  N N 387 
VAL   OXT  O  N N 388 
VAL   H    H  N N 389 
VAL   H2   H  N N 390 
VAL   HA   H  N N 391 
VAL   HB   H  N N 392 
VAL   HG11 H  N N 393 
VAL   HG12 H  N N 394 
VAL   HG13 H  N N 395 
VAL   HG21 H  N N 396 
VAL   HG22 H  N N 397 
VAL   HG23 H  N N 398 
VAL   HXT  H  N N 399 
# 
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 
A1AX6 C1  C2   sing N N 1   
A1AX6 C2  C3   sing N N 2   
A1AX6 C2  C4   sing N N 3   
A1AX6 C2  C10  sing N N 4   
A1AX6 C4  O1   doub N N 5   
A1AX6 C4  N1   sing N N 6   
A1AX6 N1  C5   sing N N 7   
A1AX6 C5  C6   doub Y N 8   
A1AX6 C5  C10  sing Y N 9   
A1AX6 C6  C7   sing Y N 10  
A1AX6 C7  C8   doub Y N 11  
A1AX6 C8  BR1  sing N N 12  
A1AX6 C8  C9   sing Y N 13  
A1AX6 C9  C10  doub Y N 14  
A1AX6 C3  H32  sing N N 15  
A1AX6 C3  H31  sing N N 16  
A1AX6 C3  H33  sing N N 17  
A1AX6 C1  H11  sing N N 18  
A1AX6 C1  H13  sing N N 19  
A1AX6 C1  H12  sing N N 20  
A1AX6 C6  H6   sing N N 21  
A1AX6 C7  H7   sing N N 22  
A1AX6 C9  H9   sing N N 23  
A1AX6 N1  HN1  sing N N 24  
ALA   N   CA   sing N N 25  
ALA   N   H    sing N N 26  
ALA   N   H2   sing N N 27  
ALA   CA  C    sing N N 28  
ALA   CA  CB   sing N N 29  
ALA   CA  HA   sing N N 30  
ALA   C   O    doub N N 31  
ALA   C   OXT  sing N N 32  
ALA   CB  HB1  sing N N 33  
ALA   CB  HB2  sing N N 34  
ALA   CB  HB3  sing N N 35  
ALA   OXT HXT  sing N N 36  
ARG   N   CA   sing N N 37  
ARG   N   H    sing N N 38  
ARG   N   H2   sing N N 39  
ARG   CA  C    sing N N 40  
ARG   CA  CB   sing N N 41  
ARG   CA  HA   sing N N 42  
ARG   C   O    doub N N 43  
ARG   C   OXT  sing N N 44  
ARG   CB  CG   sing N N 45  
ARG   CB  HB2  sing N N 46  
ARG   CB  HB3  sing N N 47  
ARG   CG  CD   sing N N 48  
ARG   CG  HG2  sing N N 49  
ARG   CG  HG3  sing N N 50  
ARG   CD  NE   sing N N 51  
ARG   CD  HD2  sing N N 52  
ARG   CD  HD3  sing N N 53  
ARG   NE  CZ   sing N N 54  
ARG   NE  HE   sing N N 55  
ARG   CZ  NH1  sing N N 56  
ARG   CZ  NH2  doub N N 57  
ARG   NH1 HH11 sing N N 58  
ARG   NH1 HH12 sing N N 59  
ARG   NH2 HH21 sing N N 60  
ARG   NH2 HH22 sing N N 61  
ARG   OXT HXT  sing N N 62  
ASN   N   CA   sing N N 63  
ASN   N   H    sing N N 64  
ASN   N   H2   sing N N 65  
ASN   CA  C    sing N N 66  
ASN   CA  CB   sing N N 67  
ASN   CA  HA   sing N N 68  
ASN   C   O    doub N N 69  
ASN   C   OXT  sing N N 70  
ASN   CB  CG   sing N N 71  
ASN   CB  HB2  sing N N 72  
ASN   CB  HB3  sing N N 73  
ASN   CG  OD1  doub N N 74  
ASN   CG  ND2  sing N N 75  
ASN   ND2 HD21 sing N N 76  
ASN   ND2 HD22 sing N N 77  
ASN   OXT HXT  sing N N 78  
ASP   N   CA   sing N N 79  
ASP   N   H    sing N N 80  
ASP   N   H2   sing N N 81  
ASP   CA  C    sing N N 82  
ASP   CA  CB   sing N N 83  
ASP   CA  HA   sing N N 84  
ASP   C   O    doub N N 85  
ASP   C   OXT  sing N N 86  
ASP   CB  CG   sing N N 87  
ASP   CB  HB2  sing N N 88  
ASP   CB  HB3  sing N N 89  
ASP   CG  OD1  doub N N 90  
ASP   CG  OD2  sing N N 91  
ASP   OD2 HD2  sing N N 92  
ASP   OXT HXT  sing N N 93  
GLN   N   CA   sing N N 94  
GLN   N   H    sing N N 95  
GLN   N   H2   sing N N 96  
GLN   CA  C    sing N N 97  
GLN   CA  CB   sing N N 98  
GLN   CA  HA   sing N N 99  
GLN   C   O    doub N N 100 
GLN   C   OXT  sing N N 101 
GLN   CB  CG   sing N N 102 
GLN   CB  HB2  sing N N 103 
GLN   CB  HB3  sing N N 104 
GLN   CG  CD   sing N N 105 
GLN   CG  HG2  sing N N 106 
GLN   CG  HG3  sing N N 107 
GLN   CD  OE1  doub N N 108 
GLN   CD  NE2  sing N N 109 
GLN   NE2 HE21 sing N N 110 
GLN   NE2 HE22 sing N N 111 
GLN   OXT HXT  sing N N 112 
GLU   N   CA   sing N N 113 
GLU   N   H    sing N N 114 
GLU   N   H2   sing N N 115 
GLU   CA  C    sing N N 116 
GLU   CA  CB   sing N N 117 
GLU   CA  HA   sing N N 118 
GLU   C   O    doub N N 119 
GLU   C   OXT  sing N N 120 
GLU   CB  CG   sing N N 121 
GLU   CB  HB2  sing N N 122 
GLU   CB  HB3  sing N N 123 
GLU   CG  CD   sing N N 124 
GLU   CG  HG2  sing N N 125 
GLU   CG  HG3  sing N N 126 
GLU   CD  OE1  doub N N 127 
GLU   CD  OE2  sing N N 128 
GLU   OE2 HE2  sing N N 129 
GLU   OXT HXT  sing N N 130 
GLY   N   CA   sing N N 131 
GLY   N   H    sing N N 132 
GLY   N   H2   sing N N 133 
GLY   CA  C    sing N N 134 
GLY   CA  HA2  sing N N 135 
GLY   CA  HA3  sing N N 136 
GLY   C   O    doub N N 137 
GLY   C   OXT  sing N N 138 
GLY   OXT HXT  sing N N 139 
HIS   N   CA   sing N N 140 
HIS   N   H    sing N N 141 
HIS   N   H2   sing N N 142 
HIS   CA  C    sing N N 143 
HIS   CA  CB   sing N N 144 
HIS   CA  HA   sing N N 145 
HIS   C   O    doub N N 146 
HIS   C   OXT  sing N N 147 
HIS   CB  CG   sing N N 148 
HIS   CB  HB2  sing N N 149 
HIS   CB  HB3  sing N N 150 
HIS   CG  ND1  sing Y N 151 
HIS   CG  CD2  doub Y N 152 
HIS   ND1 CE1  doub Y N 153 
HIS   ND1 HD1  sing N N 154 
HIS   CD2 NE2  sing Y N 155 
HIS   CD2 HD2  sing N N 156 
HIS   CE1 NE2  sing Y N 157 
HIS   CE1 HE1  sing N N 158 
HIS   NE2 HE2  sing N N 159 
HIS   OXT HXT  sing N N 160 
HOH   O   H1   sing N N 161 
HOH   O   H2   sing N N 162 
ILE   N   CA   sing N N 163 
ILE   N   H    sing N N 164 
ILE   N   H2   sing N N 165 
ILE   CA  C    sing N N 166 
ILE   CA  CB   sing N N 167 
ILE   CA  HA   sing N N 168 
ILE   C   O    doub N N 169 
ILE   C   OXT  sing N N 170 
ILE   CB  CG1  sing N N 171 
ILE   CB  CG2  sing N N 172 
ILE   CB  HB   sing N N 173 
ILE   CG1 CD1  sing N N 174 
ILE   CG1 HG12 sing N N 175 
ILE   CG1 HG13 sing N N 176 
ILE   CG2 HG21 sing N N 177 
ILE   CG2 HG22 sing N N 178 
ILE   CG2 HG23 sing N N 179 
ILE   CD1 HD11 sing N N 180 
ILE   CD1 HD12 sing N N 181 
ILE   CD1 HD13 sing N N 182 
ILE   OXT HXT  sing N N 183 
LEU   N   CA   sing N N 184 
LEU   N   H    sing N N 185 
LEU   N   H2   sing N N 186 
LEU   CA  C    sing N N 187 
LEU   CA  CB   sing N N 188 
LEU   CA  HA   sing N N 189 
LEU   C   O    doub N N 190 
LEU   C   OXT  sing N N 191 
LEU   CB  CG   sing N N 192 
LEU   CB  HB2  sing N N 193 
LEU   CB  HB3  sing N N 194 
LEU   CG  CD1  sing N N 195 
LEU   CG  CD2  sing N N 196 
LEU   CG  HG   sing N N 197 
LEU   CD1 HD11 sing N N 198 
LEU   CD1 HD12 sing N N 199 
LEU   CD1 HD13 sing N N 200 
LEU   CD2 HD21 sing N N 201 
LEU   CD2 HD22 sing N N 202 
LEU   CD2 HD23 sing N N 203 
LEU   OXT HXT  sing N N 204 
LYS   N   CA   sing N N 205 
LYS   N   H    sing N N 206 
LYS   N   H2   sing N N 207 
LYS   CA  C    sing N N 208 
LYS   CA  CB   sing N N 209 
LYS   CA  HA   sing N N 210 
LYS   C   O    doub N N 211 
LYS   C   OXT  sing N N 212 
LYS   CB  CG   sing N N 213 
LYS   CB  HB2  sing N N 214 
LYS   CB  HB3  sing N N 215 
LYS   CG  CD   sing N N 216 
LYS   CG  HG2  sing N N 217 
LYS   CG  HG3  sing N N 218 
LYS   CD  CE   sing N N 219 
LYS   CD  HD2  sing N N 220 
LYS   CD  HD3  sing N N 221 
LYS   CE  NZ   sing N N 222 
LYS   CE  HE2  sing N N 223 
LYS   CE  HE3  sing N N 224 
LYS   NZ  HZ1  sing N N 225 
LYS   NZ  HZ2  sing N N 226 
LYS   NZ  HZ3  sing N N 227 
LYS   OXT HXT  sing N N 228 
MET   N   CA   sing N N 229 
MET   N   H    sing N N 230 
MET   N   H2   sing N N 231 
MET   CA  C    sing N N 232 
MET   CA  CB   sing N N 233 
MET   CA  HA   sing N N 234 
MET   C   O    doub N N 235 
MET   C   OXT  sing N N 236 
MET   CB  CG   sing N N 237 
MET   CB  HB2  sing N N 238 
MET   CB  HB3  sing N N 239 
MET   CG  SD   sing N N 240 
MET   CG  HG2  sing N N 241 
MET   CG  HG3  sing N N 242 
MET   SD  CE   sing N N 243 
MET   CE  HE1  sing N N 244 
MET   CE  HE2  sing N N 245 
MET   CE  HE3  sing N N 246 
MET   OXT HXT  sing N N 247 
PHE   N   CA   sing N N 248 
PHE   N   H    sing N N 249 
PHE   N   H2   sing N N 250 
PHE   CA  C    sing N N 251 
PHE   CA  CB   sing N N 252 
PHE   CA  HA   sing N N 253 
PHE   C   O    doub N N 254 
PHE   C   OXT  sing N N 255 
PHE   CB  CG   sing N N 256 
PHE   CB  HB2  sing N N 257 
PHE   CB  HB3  sing N N 258 
PHE   CG  CD1  doub Y N 259 
PHE   CG  CD2  sing Y N 260 
PHE   CD1 CE1  sing Y N 261 
PHE   CD1 HD1  sing N N 262 
PHE   CD2 CE2  doub Y N 263 
PHE   CD2 HD2  sing N N 264 
PHE   CE1 CZ   doub Y N 265 
PHE   CE1 HE1  sing N N 266 
PHE   CE2 CZ   sing Y N 267 
PHE   CE2 HE2  sing N N 268 
PHE   CZ  HZ   sing N N 269 
PHE   OXT HXT  sing N N 270 
PRO   N   CA   sing N N 271 
PRO   N   CD   sing N N 272 
PRO   N   H    sing N N 273 
PRO   CA  C    sing N N 274 
PRO   CA  CB   sing N N 275 
PRO   CA  HA   sing N N 276 
PRO   C   O    doub N N 277 
PRO   C   OXT  sing N N 278 
PRO   CB  CG   sing N N 279 
PRO   CB  HB2  sing N N 280 
PRO   CB  HB3  sing N N 281 
PRO   CG  CD   sing N N 282 
PRO   CG  HG2  sing N N 283 
PRO   CG  HG3  sing N N 284 
PRO   CD  HD2  sing N N 285 
PRO   CD  HD3  sing N N 286 
PRO   OXT HXT  sing N N 287 
SER   N   CA   sing N N 288 
SER   N   H    sing N N 289 
SER   N   H2   sing N N 290 
SER   CA  C    sing N N 291 
SER   CA  CB   sing N N 292 
SER   CA  HA   sing N N 293 
SER   C   O    doub N N 294 
SER   C   OXT  sing N N 295 
SER   CB  OG   sing N N 296 
SER   CB  HB2  sing N N 297 
SER   CB  HB3  sing N N 298 
SER   OG  HG   sing N N 299 
SER   OXT HXT  sing N N 300 
THR   N   CA   sing N N 301 
THR   N   H    sing N N 302 
THR   N   H2   sing N N 303 
THR   CA  C    sing N N 304 
THR   CA  CB   sing N N 305 
THR   CA  HA   sing N N 306 
THR   C   O    doub N N 307 
THR   C   OXT  sing N N 308 
THR   CB  OG1  sing N N 309 
THR   CB  CG2  sing N N 310 
THR   CB  HB   sing N N 311 
THR   OG1 HG1  sing N N 312 
THR   CG2 HG21 sing N N 313 
THR   CG2 HG22 sing N N 314 
THR   CG2 HG23 sing N N 315 
THR   OXT HXT  sing N N 316 
TRP   N   CA   sing N N 317 
TRP   N   H    sing N N 318 
TRP   N   H2   sing N N 319 
TRP   CA  C    sing N N 320 
TRP   CA  CB   sing N N 321 
TRP   CA  HA   sing N N 322 
TRP   C   O    doub N N 323 
TRP   C   OXT  sing N N 324 
TRP   CB  CG   sing N N 325 
TRP   CB  HB2  sing N N 326 
TRP   CB  HB3  sing N N 327 
TRP   CG  CD1  doub Y N 328 
TRP   CG  CD2  sing Y N 329 
TRP   CD1 NE1  sing Y N 330 
TRP   CD1 HD1  sing N N 331 
TRP   CD2 CE2  doub Y N 332 
TRP   CD2 CE3  sing Y N 333 
TRP   NE1 CE2  sing Y N 334 
TRP   NE1 HE1  sing N N 335 
TRP   CE2 CZ2  sing Y N 336 
TRP   CE3 CZ3  doub Y N 337 
TRP   CE3 HE3  sing N N 338 
TRP   CZ2 CH2  doub Y N 339 
TRP   CZ2 HZ2  sing N N 340 
TRP   CZ3 CH2  sing Y N 341 
TRP   CZ3 HZ3  sing N N 342 
TRP   CH2 HH2  sing N N 343 
TRP   OXT HXT  sing N N 344 
TYR   N   CA   sing N N 345 
TYR   N   H    sing N N 346 
TYR   N   H2   sing N N 347 
TYR   CA  C    sing N N 348 
TYR   CA  CB   sing N N 349 
TYR   CA  HA   sing N N 350 
TYR   C   O    doub N N 351 
TYR   C   OXT  sing N N 352 
TYR   CB  CG   sing N N 353 
TYR   CB  HB2  sing N N 354 
TYR   CB  HB3  sing N N 355 
TYR   CG  CD1  doub Y N 356 
TYR   CG  CD2  sing Y N 357 
TYR   CD1 CE1  sing Y N 358 
TYR   CD1 HD1  sing N N 359 
TYR   CD2 CE2  doub Y N 360 
TYR   CD2 HD2  sing N N 361 
TYR   CE1 CZ   doub Y N 362 
TYR   CE1 HE1  sing N N 363 
TYR   CE2 CZ   sing Y N 364 
TYR   CE2 HE2  sing N N 365 
TYR   CZ  OH   sing N N 366 
TYR   OH  HH   sing N N 367 
TYR   OXT HXT  sing N N 368 
VAL   N   CA   sing N N 369 
VAL   N   H    sing N N 370 
VAL   N   H2   sing N N 371 
VAL   CA  C    sing N N 372 
VAL   CA  CB   sing N N 373 
VAL   CA  HA   sing N N 374 
VAL   C   O    doub N N 375 
VAL   C   OXT  sing N N 376 
VAL   CB  CG1  sing N N 377 
VAL   CB  CG2  sing N N 378 
VAL   CB  HB   sing N N 379 
VAL   CG1 HG11 sing N N 380 
VAL   CG1 HG12 sing N N 381 
VAL   CG1 HG13 sing N N 382 
VAL   CG2 HG21 sing N N 383 
VAL   CG2 HG22 sing N N 384 
VAL   CG2 HG23 sing N N 385 
VAL   OXT HXT  sing N N 386 
# 
_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                    7HA1 
_atom_sites.fract_transf_matrix[1][1]   0.015168 
_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]   0.011176 
_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]   0.009978 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
BR ? ? 25.79822 9.11301 ? ? 1.35700  25.34896 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLU   A 1 9   ? 4.39924   -28.52896 -39.14778 1.000 46.80125 ? 16  GLU   A N   1 
ATOM   2    C  CA  . GLU   A 1 9   ? 5.61717   -27.73885 -39.29331 1.000 50.03678 ? 16  GLU   A CA  1 
ATOM   3    C  C   . GLU   A 1 9   ? 5.82660   -26.87077 -38.05226 1.000 45.61763 ? 16  GLU   A C   1 
ATOM   4    O  O   . GLU   A 1 9   ? 5.10869   -25.89466 -37.83238 1.000 41.17676 ? 16  GLU   A O   1 
ATOM   5    C  CB  . GLU   A 1 9   ? 5.53602   -26.86822 -40.55044 1.000 58.58181 ? 16  GLU   A CB  1 
ATOM   6    C  CG  . GLU   A 1 9   ? 6.58959   -25.77088 -40.64280 1.000 63.35381 ? 16  GLU   A CG  1 
ATOM   7    C  CD  . GLU   A 1 9   ? 8.00966   -26.31288 -40.68606 1.000 76.14858 ? 16  GLU   A CD  1 
ATOM   8    O  OE1 . GLU   A 1 9   ? 8.94798   -25.54382 -40.38698 1.000 68.15704 ? 16  GLU   A OE1 1 
ATOM   9    O  OE2 . GLU   A 1 9   ? 8.19245   -27.49863 -41.04020 1.000 75.56705 ? 16  GLU   A OE2 1 
ATOM   10   N  N   . VAL   A 1 10  ? 6.81449   -27.23420 -37.23942 1.000 32.83539 ? 17  VAL   A N   1 
ATOM   11   C  CA  . VAL   A 1 10  ? 7.06653   -26.59337 -35.95452 1.000 27.21730 ? 17  VAL   A CA  1 
ATOM   12   C  C   . VAL   A 1 10  ? 8.43723   -25.93566 -36.00757 1.000 29.15215 ? 17  VAL   A C   1 
ATOM   13   O  O   . VAL   A 1 10  ? 9.43092   -26.59417 -36.33668 1.000 29.64053 ? 17  VAL   A O   1 
ATOM   14   C  CB  . VAL   A 1 10  ? 7.01086   -27.61713 -34.80618 1.000 31.68847 ? 17  VAL   A CB  1 
ATOM   15   C  CG1 . VAL   A 1 10  ? 7.32509   -26.94769 -33.47648 1.000 32.53923 ? 17  VAL   A CG1 1 
ATOM   16   C  CG2 . VAL   A 1 10  ? 5.65770   -28.30624 -34.77008 1.000 39.25142 ? 17  VAL   A CG2 1 
ATOM   17   N  N   . GLU   A 1 11  ? 8.49380   -24.64582 -35.68297 1.000 23.51238 ? 18  GLU   A N   1 
ATOM   18   C  CA  . GLU   A 1 11  ? 9.75479   -23.91511 -35.60600 1.000 21.89601 ? 18  GLU   A CA  1 
ATOM   19   C  C   . GLU   A 1 11  ? 10.16390  -23.74834 -34.14919 1.000 20.54251 ? 18  GLU   A C   1 
ATOM   20   O  O   . GLU   A 1 11  ? 9.34459   -23.35833 -33.30693 1.000 20.42563 ? 18  GLU   A O   1 
ATOM   21   C  CB  . GLU   A 1 11  ? 9.64466   -22.54377 -36.27565 1.000 21.80673 ? 18  GLU   A CB  1 
ATOM   22   C  CG  . GLU   A 1 11  ? 9.31350   -22.60232 -37.76123 1.000 24.52685 ? 18  GLU   A CG  1 
ATOM   23   C  CD  . GLU   A 1 11  ? 9.05332   -21.22943 -38.34780 1.000 34.40421 ? 18  GLU   A CD  1 
ATOM   24   O  OE1 . GLU   A 1 11  ? 7.92520   -20.72316 -38.19113 1.000 35.19965 ? 18  GLU   A OE1 1 
ATOM   25   O  OE2 . GLU   A 1 11  ? 9.96155   -20.67106 -38.99846 1.000 37.90748 ? 18  GLU   A OE2 1 
ATOM   26   N  N   . THR   A 1 12  ? 11.43014  -24.03902 -33.85486 1.000 19.71533 ? 19  THR   A N   1 
ATOM   27   C  CA  . THR   A 1 12  ? 11.98142  -23.94011 -32.51095 1.000 18.72195 ? 19  THR   A CA  1 
ATOM   28   C  C   . THR   A 1 12  ? 12.97614  -22.78913 -32.46514 1.000 18.82391 ? 19  THR   A C   1 
ATOM   29   O  O   . THR   A 1 12  ? 13.84150  -22.67929 -33.33960 1.000 18.41748 ? 19  THR   A O   1 
ATOM   30   C  CB  . THR   A 1 12  ? 12.65458  -25.25364 -32.09891 1.000 19.10113 ? 19  THR   A CB  1 
ATOM   31   O  OG1 . THR   A 1 12  ? 11.72386  -26.33865 -32.23033 1.000 20.43545 ? 19  THR   A OG1 1 
ATOM   32   C  CG2 . THR   A 1 12  ? 13.15592  -25.18431 -30.65690 1.000 18.41531 ? 19  THR   A CG2 1 
ATOM   33   N  N   . PHE   A 1 13  ? 12.83603  -21.92856 -31.45971 1.000 17.64844 ? 20  PHE   A N   1 
ATOM   34   C  CA  . PHE   A 1 13  ? 13.64944  -20.73114 -31.30656 1.000 17.23527 ? 20  PHE   A CA  1 
ATOM   35   C  C   . PHE   A 1 13  ? 14.29385  -20.73359 -29.92802 1.000 20.68433 ? 20  PHE   A C   1 
ATOM   36   O  O   . PHE   A 1 13  ? 13.73475  -21.26281 -28.96262 1.000 18.22413 ? 20  PHE   A O   1 
ATOM   37   C  CB  . PHE   A 1 13  ? 12.78221  -19.45674 -31.35906 1.000 18.56043 ? 20  PHE   A CB  1 
ATOM   38   C  CG  . PHE   A 1 13  ? 12.02951  -19.26643 -32.64789 1.000 18.05791 ? 20  PHE   A CG  1 
ATOM   39   C  CD1 . PHE   A 1 13  ? 10.81958  -19.91143 -32.86788 1.000 19.35950 ? 20  PHE   A CD1 1 
ATOM   40   C  CD2 . PHE   A 1 13  ? 12.52767  -18.43197 -33.63705 1.000 20.68118 ? 20  PHE   A CD2 1 
ATOM   41   C  CE1 . PHE   A 1 13  ? 10.12796  -19.73777 -34.05718 1.000 21.77066 ? 20  PHE   A CE1 1 
ATOM   42   C  CE2 . PHE   A 1 13  ? 11.83320  -18.24462 -34.82967 1.000 23.00670 ? 20  PHE   A CE2 1 
ATOM   43   C  CZ  . PHE   A 1 13  ? 10.63046  -18.90047 -35.03502 1.000 22.34457 ? 20  PHE   A CZ  1 
ATOM   44   N  N   . ALA   A 1 14  ? 15.46178  -20.10673 -29.82731 1.000 17.60969 ? 21  ALA   A N   1 
ATOM   45   C  CA  . ALA   A 1 14  ? 16.08800  -19.88968 -28.53471 1.000 18.98004 ? 21  ALA   A CA  1 
ATOM   46   C  C   . ALA   A 1 14  ? 15.60546  -18.56145 -27.97402 1.000 17.50272 ? 21  ALA   A C   1 
ATOM   47   O  O   . ALA   A 1 14  ? 15.52648  -17.56671 -28.69846 1.000 19.21357 ? 21  ALA   A O   1 
ATOM   48   C  CB  . ALA   A 1 14  ? 17.60737  -19.83389 -28.69363 1.000 19.07814 ? 21  ALA   A CB  1 
ATOM   49   N  N   . PHE   A 1 15  ? 15.28373  -18.53773 -26.67706 1.000 16.76377 ? 22  PHE   A N   1 
ATOM   50   C  CA  . PHE   A 1 15  ? 15.09225  -17.25308 -26.02518 1.000 17.89721 ? 22  PHE   A CA  1 
ATOM   51   C  C   . PHE   A 1 15  ? 16.38211  -16.44542 -26.06153 1.000 19.68685 ? 22  PHE   A C   1 
ATOM   52   O  O   . PHE   A 1 15  ? 17.48767  -16.99394 -25.97032 1.000 20.57202 ? 22  PHE   A O   1 
ATOM   53   C  CB  . PHE   A 1 15  ? 14.68665  -17.41103 -24.55425 1.000 17.04260 ? 22  PHE   A CB  1 
ATOM   54   C  CG  . PHE   A 1 15  ? 13.29855  -17.96350 -24.34443 1.000 15.89850 ? 22  PHE   A CG  1 
ATOM   55   C  CD1 . PHE   A 1 15  ? 12.17899  -17.18073 -24.61097 1.000 17.11051 ? 22  PHE   A CD1 1 
ATOM   56   C  CD2 . PHE   A 1 15  ? 13.11610  -19.22342 -23.80534 1.000 16.40075 ? 22  PHE   A CD2 1 
ATOM   57   C  CE1 . PHE   A 1 15  ? 10.89685  -17.67314 -24.39911 1.000 17.24111 ? 22  PHE   A CE1 1 
ATOM   58   C  CE2 . PHE   A 1 15  ? 11.83788  -19.72376 -23.58568 1.000 16.88738 ? 22  PHE   A CE2 1 
ATOM   59   C  CZ  . PHE   A 1 15  ? 10.72911  -18.94242 -23.87896 1.000 16.92794 ? 22  PHE   A CZ  1 
ATOM   60   N  N   . GLN   A 1 16  ? 16.23668  -15.12771 -26.17809 1.000 18.89399 ? 23  GLN   A N   1 
ATOM   61   C  CA  . GLN   A 1 16  ? 17.36415  -14.25228 -25.89085 1.000 19.74744 ? 23  GLN   A CA  1 
ATOM   62   C  C   . GLN   A 1 16  ? 17.87986  -14.56093 -24.49350 1.000 21.00354 ? 23  GLN   A C   1 
ATOM   63   O  O   . GLN   A 1 16  ? 17.11622  -14.94330 -23.60431 1.000 19.77499 ? 23  GLN   A O   1 
ATOM   64   C  CB  . GLN   A 1 16  ? 16.92517  -12.79222 -25.95714 1.000 23.76336 ? 23  GLN   A CB  1 
ATOM   65   C  CG  . GLN   A 1 16  ? 16.60236  -12.31840 -27.35399 1.000 25.38774 ? 23  GLN   A CG  1 
ATOM   66   C  CD  . GLN   A 1 16  ? 16.01492  -10.92425 -27.36181 1.000 34.64621 ? 23  GLN   A CD  1 
ATOM   67   O  OE1 . GLN   A 1 16  ? 14.79836  -10.75762 -27.35406 1.000 36.18775 ? 23  GLN   A OE1 1 
ATOM   68   N  NE2 . GLN   A 1 16  ? 16.87707  -9.91326  -27.37949 1.000 34.07507 ? 23  GLN   A NE2 1 
ATOM   69   N  N   . ALA   A 1 17  ? 19.19188  -14.40417 -24.30446 1.000 22.35226 ? 24  ALA   A N   1 
ATOM   70   C  CA  . ALA   A 1 17  ? 19.81542  -14.81408 -23.04877 1.000 22.96125 ? 24  ALA   A CA  1 
ATOM   71   C  C   . ALA   A 1 17  ? 19.16625  -14.13049 -21.85405 1.000 21.06387 ? 24  ALA   A C   1 
ATOM   72   O  O   . ALA   A 1 17  ? 18.93240  -14.76411 -20.81756 1.000 22.59688 ? 24  ALA   A O   1 
ATOM   73   C  CB  . ALA   A 1 17  ? 21.31574  -14.51801 -23.09203 1.000 24.75390 ? 24  ALA   A CB  1 
ATOM   74   N  N   . GLU   A 1 18  ? 18.83477  -12.84652 -21.99463 1.000 22.50437 ? 25  GLU   A N   1 
ATOM   75   C  CA  . GLU   A 1 18  ? 18.25582  -12.10034 -20.88385 1.000 22.58917 ? 25  GLU   A CA  1 
ATOM   76   C  C   . GLU   A 1 18  ? 16.87729  -12.62667 -20.50041 1.000 21.60908 ? 25  GLU   A C   1 
ATOM   77   O  O   . GLU   A 1 18  ? 16.51142  -12.59254 -19.31666 1.000 22.19415 ? 25  GLU   A O   1 
ATOM   78   C  CB  . GLU   A 1 18  ? 18.19441  -10.61200 -21.22934 1.000 25.48192 ? 25  GLU   A CB  1 
ATOM   79   C  CG  . GLU   A 1 18  ? 19.55848  -9.95055  -21.43409 1.000 29.89010 ? 25  GLU   A CG  1 
ATOM   80   C  CD  . GLU   A 1 18  ? 20.14252  -10.18014 -22.81964 1.000 39.89761 ? 25  GLU   A CD  1 
ATOM   81   O  OE1 . GLU   A 1 18  ? 19.47348  -10.80722 -23.66781 1.000 32.37247 ? 25  GLU   A OE1 1 
ATOM   82   O  OE2 . GLU   A 1 18  ? 21.27775  -9.72147  -23.06469 1.000 47.90079 ? 25  GLU   A OE2 1 
ATOM   83   N  N   . ILE   A 1 19  ? 16.10361  -13.10650 -21.47840 1.000 21.19745 ? 26  ILE   A N   1 
ATOM   84   C  CA  . ILE   A 1 19  ? 14.78027  -13.65397 -21.19140 1.000 20.55619 ? 26  ILE   A CA  1 
ATOM   85   C  C   . ILE   A 1 19  ? 14.90107  -15.03013 -20.54596 1.000 19.33212 ? 26  ILE   A C   1 
ATOM   86   O  O   . ILE   A 1 19  ? 14.15454  -15.36854 -19.61884 1.000 20.19576 ? 26  ILE   A O   1 
ATOM   87   C  CB  . ILE   A 1 19  ? 13.88991  -13.67143 -22.45630 1.000 18.92360 ? 26  ILE   A CB  1 
ATOM   88   C  CG1 . ILE   A 1 19  ? 13.37973  -12.26824 -22.84058 1.000 24.24999 ? 26  ILE   A CG1 1 
ATOM   89   C  CG2 . ILE   A 1 19  ? 12.67008  -14.58223 -22.25617 1.000 19.03081 ? 26  ILE   A CG2 1 
ATOM   90   C  CD1 . ILE   A 1 19  ? 14.42493  -11.17253 -23.02309 1.000 27.29666 ? 26  ILE   A CD1 1 
ATOM   91   N  N   . ALA   A 1 20  ? 15.84545  -15.84877 -21.01994 1.000 18.10785 ? 27  ALA   A N   1 
ATOM   92   C  CA  . ALA   A 1 20  ? 16.08354  -17.12872 -20.36297 1.000 20.09197 ? 27  ALA   A CA  1 
ATOM   93   C  C   . ALA   A 1 20  ? 16.49218  -16.92080 -18.90941 1.000 19.73857 ? 27  ALA   A C   1 
ATOM   94   O  O   . ALA   A 1 20  ? 16.06512  -17.66845 -18.02096 1.000 21.78641 ? 27  ALA   A O   1 
ATOM   95   C  CB  . ALA   A 1 20  ? 17.16050  -17.91363 -21.11366 1.000 21.51595 ? 27  ALA   A CB  1 
ATOM   96   N  N   . GLN   A 1 21  ? 17.30015  -15.89134 -18.64719 1.000 21.39515 ? 28  GLN   A N   1 
ATOM   97   C  CA  . GLN   A 1 21  ? 17.68775  -15.58619 -17.27440 1.000 21.30091 ? 28  GLN   A CA  1 
ATOM   98   C  C   . GLN   A 1 21  ? 16.48138  -15.16679 -16.44180 1.000 24.65401 ? 28  GLN   A C   1 
ATOM   99   O  O   . GLN   A 1 21  ? 16.34173  -15.59709 -15.29268 1.000 25.55781 ? 28  GLN   A O   1 
ATOM   100  C  CB  . GLN   A 1 21  ? 18.77003  -14.50656 -17.26755 1.000 24.56286 ? 28  GLN   A CB  1 
ATOM   101  C  CG  . GLN   A 1 21  ? 19.45618  -14.30746 -15.92628 1.000 39.15084 ? 28  GLN   A CG  1 
ATOM   102  C  CD  . GLN   A 1 21  ? 20.42102  -13.13477 -15.94010 1.000 55.95880 ? 28  GLN   A CD  1 
ATOM   103  O  OE1 . GLN   A 1 21  ? 21.01930  -12.79419 -14.91872 1.000 58.80234 ? 28  GLN   A OE1 1 
ATOM   104  N  NE2 . GLN   A 1 21  ? 20.58122  -12.51415 -17.10545 1.000 48.43204 ? 28  GLN   A NE2 1 
ATOM   105  N  N   . LEU   A 1 22  ? 15.59980  -14.33503 -17.00693 1.000 20.04807 ? 29  LEU   A N   1 
ATOM   106  C  CA  . LEU   A 1 22  ? 14.38020  -13.94449 -16.29612 1.000 22.42883 ? 29  LEU   A CA  1 
ATOM   107  C  C   . LEU   A 1 22  ? 13.54158  -15.16363 -15.94117 1.000 22.25967 ? 29  LEU   A C   1 
ATOM   108  O  O   . LEU   A 1 22  ? 13.05176  -15.29848 -14.81026 1.000 22.94264 ? 29  LEU   A O   1 
ATOM   109  C  CB  . LEU   A 1 22  ? 13.56585  -12.98080 -17.16344 1.000 23.12032 ? 29  LEU   A CB  1 
ATOM   110  C  CG  . LEU   A 1 22  ? 12.16156  -12.64922 -16.64673 1.000 23.21296 ? 29  LEU   A CG  1 
ATOM   111  C  CD1 . LEU   A 1 22  ? 12.27125  -11.81756 -15.38197 1.000 26.18845 ? 29  LEU   A CD1 1 
ATOM   112  C  CD2 . LEU   A 1 22  ? 11.35303  -11.91653 -17.69739 1.000 24.92540 ? 29  LEU   A CD2 1 
ATOM   113  N  N   . MET   A 1 23  ? 13.35687  -16.06856 -16.90312 1.000 18.64350 ? 30  MET   A N   1 
ATOM   114  C  CA  . MET   A 1 23  ? 12.54178  -17.24875 -16.65711 1.000 19.14897 ? 30  MET   A CA  1 
ATOM   115  C  C   . MET   A 1 23  ? 13.15266  -18.14316 -15.57890 1.000 20.87537 ? 30  MET   A C   1 
ATOM   116  O  O   . MET   A 1 23  ? 12.43805  -18.64404 -14.70339 1.000 21.17820 ? 30  MET   A O   1 
ATOM   117  C  CB  . MET   A 1 23  ? 12.30324  -18.01786 -17.95788 1.000 17.89265 ? 30  MET   A CB  1 
ATOM   118  C  CG  . MET   A 1 23  ? 11.33005  -17.31333 -18.89975 1.000 20.06589 ? 30  MET   A CG  1 
ATOM   119  S  SD  . MET   A 1 23  ? 11.31905  -17.99451 -20.56589 1.000 19.16264 ? 30  MET   A SD  1 
ATOM   120  C  CE  . MET   A 1 23  ? 10.14001  -19.31483 -20.30638 1.000 20.56185 ? 30  MET   A CE  1 
ATOM   121  N  N   . SER   A 1 24  ? 14.47416  -18.34233 -15.60923 1.000 21.48254 ? 31  SER   A N   1 
ATOM   122  C  CA  . SER   A 1 24  ? 15.09289  -19.17081 -14.57644 1.000 21.33583 ? 31  SER   A CA  1 
ATOM   123  C  C   . SER   A 1 24  ? 14.97139  -18.53108 -13.19740 1.000 24.51119 ? 31  SER   A C   1 
ATOM   124  O  O   . SER   A 1 24  ? 14.78078  -19.23572 -12.20070 1.000 26.77602 ? 31  SER   A O   1 
ATOM   125  C  CB  . SER   A 1 24  ? 16.54229  -19.49062 -14.93806 1.000 33.09839 ? 31  SER   A CB  1 
ATOM   126  O  OG  . SER   A 1 24  ? 17.33858  -18.32339 -14.96019 1.000 46.55769 ? 31  SER   A OG  1 
ATOM   127  N  N   . LEU   A 1 25  ? 15.05069  -17.19879 -13.11585 1.000 22.56273 ? 32  LEU   A N   1 
ATOM   128  C  CA  . LEU   A 1 25  ? 14.87167  -16.53834 -11.82587 1.000 24.35832 ? 32  LEU   A CA  1 
ATOM   129  C  C   . LEU   A 1 25  ? 13.45096  -16.73131 -11.30764 1.000 25.11338 ? 32  LEU   A C   1 
ATOM   130  O  O   . LEU   A 1 25  ? 13.24491  -16.96631 -10.11106 1.000 26.18176 ? 32  LEU   A O   1 
ATOM   131  C  CB  . LEU   A 1 25  ? 15.22652  -15.05187 -11.93628 1.000 27.20391 ? 32  LEU   A CB  1 
ATOM   132  C  CG  . LEU   A 1 25  ? 14.91309  -14.05767 -10.80015 1.000 33.05953 ? 32  LEU   A CG  1 
ATOM   133  C  CD1 . LEU   A 1 25  ? 15.82436  -12.84738 -10.92340 1.000 38.85122 ? 32  LEU   A CD1 1 
ATOM   134  C  CD2 . LEU   A 1 25  ? 13.46158  -13.58183 -10.76895 1.000 38.72073 ? 32  LEU   A CD2 1 
ATOM   135  N  N   . ILE   A 1 26  ? 12.45933  -16.63051 -12.19392 1.000 20.91503 ? 33  ILE   A N   1 
ATOM   136  C  CA  . ILE   A 1 26  ? 11.07345  -16.82104 -11.77739 1.000 23.25980 ? 33  ILE   A CA  1 
ATOM   137  C  C   . ILE   A 1 26  ? 10.85209  -18.25093 -11.30277 1.000 23.94370 ? 33  ILE   A C   1 
ATOM   138  O  O   . ILE   A 1 26  ? 10.13322  -18.49643 -10.32278 1.000 23.41568 ? 33  ILE   A O   1 
ATOM   139  C  CB  . ILE   A 1 26  ? 10.12960  -16.43298 -12.92978 1.000 20.45380 ? 33  ILE   A CB  1 
ATOM   140  C  CG1 . ILE   A 1 26  ? 10.09916  -14.91398 -13.09440 1.000 22.79256 ? 33  ILE   A CG1 1 
ATOM   141  C  CG2 . ILE   A 1 26  ? 8.72123   -16.98074 -12.69290 1.000 21.67377 ? 33  ILE   A CG2 1 
ATOM   142  C  CD1 . ILE   A 1 26  ? 9.48576   -14.44492 -14.38974 1.000 23.23341 ? 33  ILE   A CD1 1 
ATOM   143  N  N   . ILE   A 1 27  ? 11.48737  -19.21347 -11.96890 1.000 23.82216 ? 34  ILE   A N   1 
ATOM   144  C  CA  . ILE   A 1 27  ? 11.28099  -20.61903 -11.64175 1.000 24.66646 ? 34  ILE   A CA  1 
ATOM   145  C  C   . ILE   A 1 27  ? 12.03150  -21.00985 -10.37399 1.000 26.96040 ? 34  ILE   A C   1 
ATOM   146  O  O   . ILE   A 1 27  ? 11.54413  -21.82112 -9.57888  1.000 29.97414 ? 34  ILE   A O   1 
ATOM   147  C  CB  . ILE   A 1 27  ? 11.66238  -21.49914 -12.84836 1.000 24.64952 ? 34  ILE   A CB  1 
ATOM   148  C  CG1 . ILE   A 1 27  ? 10.64195  -21.31944 -13.97260 1.000 24.10403 ? 34  ILE   A CG1 1 
ATOM   149  C  CG2 . ILE   A 1 27  ? 11.78416  -22.96503 -12.45281 1.000 27.72142 ? 34  ILE   A CG2 1 
ATOM   150  C  CD1 . ILE   A 1 27  ? 11.14585  -21.78420 -15.32285 1.000 24.46075 ? 34  ILE   A CD1 1 
ATOM   151  N  N   . ASN   A 1 28  ? 13.21245  -20.42922 -10.14817 1.000 24.53571 ? 35  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 28  ? 14.10611  -20.93037 -9.10867  1.000 28.44345 ? 35  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 28  ? 14.08808  -20.12198 -7.81606  1.000 34.47269 ? 35  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 28  ? 14.46707  -20.66373 -6.77047  1.000 37.92880 ? 35  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 28  ? 15.53874  -21.00341 -9.64246  1.000 31.89596 ? 35  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 28  ? 15.71593  -22.11144 -10.65260 1.000 38.78071 ? 35  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 28  ? 15.15944  -23.20046 -10.50189 1.000 41.20261 ? 35  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 28  ? 16.48552  -21.83682 -11.70189 1.000 49.17441 ? 35  ASN   A ND2 1 
ATOM   159  N  N   . THR   A 1 29  ? 13.67749  -18.85662 -7.84798  1.000 27.77888 ? 36  THR   A N   1 
ATOM   160  C  CA  . THR   A 1 29  ? 13.68240  -18.04747 -6.63336  1.000 28.20948 ? 36  THR   A CA  1 
ATOM   161  C  C   . THR   A 1 29  ? 12.59467  -18.52578 -5.67795  1.000 27.71650 ? 36  THR   A C   1 
ATOM   162  O  O   . THR   A 1 29  ? 11.45902  -18.77835 -6.09154  1.000 28.43876 ? 36  THR   A O   1 
ATOM   163  C  CB  . THR   A 1 29  ? 13.44222  -16.57756 -6.98288  1.000 29.80502 ? 36  THR   A CB  1 
ATOM   164  O  OG1 . THR   A 1 29  ? 14.48602  -16.10928 -7.84445  1.000 33.02591 ? 36  THR   A OG1 1 
ATOM   165  C  CG2 . THR   A 1 29  ? 13.42558  -15.72025 -5.72152  1.000 32.36339 ? 36  THR   A CG2 1 
ATOM   166  N  N   . PHE   A 1 30  ? 12.93624  -18.65548 -4.39716  1.000 27.47876 ? 37  PHE   A N   1 
ATOM   167  C  CA  . PHE   A 1 30  ? 11.90925  -18.92463 -3.40060  1.000 28.33198 ? 37  PHE   A CA  1 
ATOM   168  C  C   . PHE   A 1 30  ? 11.05212  -17.68000 -3.21437  1.000 31.03557 ? 37  PHE   A C   1 
ATOM   169  O  O   . PHE   A 1 30  ? 11.55505  -16.62250 -2.81752  1.000 29.47129 ? 37  PHE   A O   1 
ATOM   170  C  CB  . PHE   A 1 30  ? 12.52011  -19.34566 -2.06892  1.000 28.89764 ? 37  PHE   A CB  1 
ATOM   171  C  CG  . PHE   A 1 30  ? 11.48755  -19.65154 -1.02497  1.000 29.34135 ? 37  PHE   A CG  1 
ATOM   172  C  CD1 . PHE   A 1 30  ? 10.70233  -20.78728 -1.12638  1.000 33.76609 ? 37  PHE   A CD1 1 
ATOM   173  C  CD2 . PHE   A 1 30  ? 11.26460  -18.78060 0.02845   1.000 30.81676 ? 37  PHE   A CD2 1 
ATOM   174  C  CE1 . PHE   A 1 30  ? 9.73242   -21.06425 -0.18035  1.000 30.64956 ? 37  PHE   A CE1 1 
ATOM   175  C  CE2 . PHE   A 1 30  ? 10.29758  -19.05244 0.97457   1.000 32.93645 ? 37  PHE   A CE2 1 
ATOM   176  C  CZ  . PHE   A 1 30  ? 9.53141   -20.19673 0.87200   1.000 30.05326 ? 37  PHE   A CZ  1 
ATOM   177  N  N   . TYR   A 1 31  ? 9.75632   -17.80681 -3.49225  1.000 26.42872 ? 38  TYR   A N   1 
ATOM   178  C  CA  . TYR   A 1 31  ? 8.86245   -16.65461 -3.45328  1.000 24.98806 ? 38  TYR   A CA  1 
ATOM   179  C  C   . TYR   A 1 31  ? 7.44392   -17.19119 -3.30760  1.000 23.44732 ? 38  TYR   A C   1 
ATOM   180  O  O   . TYR   A 1 31  ? 6.91902   -17.80696 -4.23612  1.000 23.72661 ? 38  TYR   A O   1 
ATOM   181  C  CB  . TYR   A 1 31  ? 9.01893   -15.83242 -4.72918  1.000 26.24149 ? 38  TYR   A CB  1 
ATOM   182  C  CG  . TYR   A 1 31  ? 8.08328   -14.65897 -4.78950  1.000 24.15749 ? 38  TYR   A CG  1 
ATOM   183  C  CD1 . TYR   A 1 31  ? 8.33083   -13.52429 -4.03090  1.000 28.53385 ? 38  TYR   A CD1 1 
ATOM   184  C  CD2 . TYR   A 1 31  ? 6.95328   -14.68125 -5.59916  1.000 30.50327 ? 38  TYR   A CD2 1 
ATOM   185  C  CE1 . TYR   A 1 31  ? 7.48191   -12.44882 -4.06331  1.000 38.81764 ? 38  TYR   A CE1 1 
ATOM   186  C  CE2 . TYR   A 1 31  ? 6.09383   -13.60080 -5.63864  1.000 27.29675 ? 38  TYR   A CE2 1 
ATOM   187  C  CZ  . TYR   A 1 31  ? 6.36955   -12.49037 -4.86921  1.000 32.10860 ? 38  TYR   A CZ  1 
ATOM   188  O  OH  . TYR   A 1 31  ? 5.52673   -11.41054 -4.89903  1.000 51.76407 ? 38  TYR   A OH  1 
ATOM   189  N  N   . SER   A 1 32  ? 6.82821   -16.96069 -2.14915  1.000 24.18903 ? 39  SER   A N   1 
ATOM   190  C  CA  . SER   A 1 32  ? 5.57647   -17.63583 -1.82570  1.000 23.98542 ? 39  SER   A CA  1 
ATOM   191  C  C   . SER   A 1 32  ? 4.35546   -16.99882 -2.47880  1.000 23.69795 ? 39  SER   A C   1 
ATOM   192  O  O   . SER   A 1 32  ? 3.35103   -17.68858 -2.67723  1.000 25.46894 ? 39  SER   A O   1 
ATOM   193  C  CB  . SER   A 1 32  ? 5.37842   -17.67832 -0.30851  1.000 25.33159 ? 39  SER   A CB  1 
ATOM   194  O  OG  . SER   A 1 32  ? 6.36798   -18.49339 0.30498   1.000 26.61822 ? 39  SER   A OG  1 
ATOM   195  N  N   . ASN   A 1 33  ? 4.42062   -15.71587 -2.83373  1.000 24.44076 ? 40  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 33  ? 3.24733   -14.95960 -3.27859  1.000 23.82287 ? 40  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 33  ? 2.98880   -15.18152 -4.77547  1.000 21.16570 ? 40  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 33  ? 2.98716   -14.25864 -5.58991  1.000 21.56768 ? 40  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 33  ? 3.45489   -13.48930 -2.93099  1.000 25.55686 ? 40  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 33  ? 2.27955   -12.61231 -3.30531  1.000 26.87309 ? 40  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 33  ? 1.12499   -13.02440 -3.21920  1.000 28.51540 ? 40  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 33  ? 2.57274   -11.38128 -3.70308  1.000 29.48495 ? 40  ASN   A ND2 1 
ATOM   203  N  N   . LYS   A 1 34  ? 2.75461   -16.45071 -5.12765  1.000 19.40703 ? 41  LYS   A N   1 
ATOM   204  C  CA  . LYS   A 1 34  ? 2.64036   -16.83988 -6.53201  1.000 19.72726 ? 41  LYS   A CA  1 
ATOM   205  C  C   . LYS   A 1 34  ? 1.34617   -16.36319 -7.18176  1.000 19.33724 ? 41  LYS   A C   1 
ATOM   206  O  O   . LYS   A 1 34  ? 1.29784   -16.25097 -8.41473  1.000 18.51058 ? 41  LYS   A O   1 
ATOM   207  C  CB  . LYS   A 1 34  ? 2.72335   -18.36228 -6.65589  1.000 20.86839 ? 41  LYS   A CB  1 
ATOM   208  C  CG  . LYS   A 1 34  ? 4.09718   -18.96683 -6.34126  1.000 20.72865 ? 41  LYS   A CG  1 
ATOM   209  C  CD  . LYS   A 1 34  ? 4.05167   -20.48390 -6.48052  1.000 22.92766 ? 41  LYS   A CD  1 
ATOM   210  C  CE  . LYS   A 1 34  ? 5.40195   -21.12747 -6.21753  1.000 23.69385 ? 41  LYS   A CE  1 
ATOM   211  N  NZ  . LYS   A 1 34  ? 6.35212   -20.89896 -7.33766  1.000 23.75055 ? 41  LYS   A NZ  1 
ATOM   212  N  N   . GLU   A 1 35  ? 0.30907   -16.07188 -6.39123  1.000 18.12369 ? 42  GLU   A N   1 
ATOM   213  C  CA  . GLU   A 1 35  ? -1.00594  -15.77663 -6.95426  1.000 18.13918 ? 42  GLU   A CA  1 
ATOM   214  C  C   . GLU   A 1 35  ? -1.00113  -14.56624 -7.88016  1.000 18.47683 ? 42  GLU   A C   1 
ATOM   215  O  O   . GLU   A 1 35  ? -1.94746  -14.39677 -8.65699  1.000 18.98401 ? 42  GLU   A O   1 
ATOM   216  C  CB  . GLU   A 1 35  ? -2.02618  -15.54702 -5.83583  1.000 19.41192 ? 42  GLU   A CB  1 
ATOM   217  C  CG  . GLU   A 1 35  ? -1.82287  -14.24301 -5.08409  1.000 19.21153 ? 42  GLU   A CG  1 
ATOM   218  C  CD  . GLU   A 1 35  ? -2.70776  -14.13046 -3.85507  1.000 26.53444 ? 42  GLU   A CD  1 
ATOM   219  O  OE1 . GLU   A 1 35  ? -2.85489  -15.13832 -3.13931  1.000 31.04899 ? 42  GLU   A OE1 1 
ATOM   220  O  OE2 . GLU   A 1 35  ? -3.24800  -13.03479 -3.60824  1.000 36.29825 ? 42  GLU   A OE2 1 
ATOM   221  N  N   . ILE   A 1 36  ? 0.02951   -13.71903 -7.82287  1.000 18.40217 ? 43  ILE   A N   1 
ATOM   222  C  CA  . ILE   A 1 36  ? 0.06257   -12.52828 -8.65830  1.000 18.81303 ? 43  ILE   A CA  1 
ATOM   223  C  C   . ILE   A 1 36  ? 0.13774   -12.84105 -10.14631 1.000 17.85973 ? 43  ILE   A C   1 
ATOM   224  O  O   . ILE   A 1 36  ? -0.10882  -11.94518 -10.95970 1.000 17.76138 ? 43  ILE   A O   1 
ATOM   225  C  CB  . ILE   A 1 36  ? 1.19335   -11.56366 -8.23339  1.000 23.64088 ? 43  ILE   A CB  1 
ATOM   226  C  CG1 . ILE   A 1 36  ? 2.55710   -12.23133 -8.41139  1.000 22.39495 ? 43  ILE   A CG1 1 
ATOM   227  C  CG2 . ILE   A 1 36  ? 0.98610   -11.09725 -6.79007  1.000 26.00186 ? 43  ILE   A CG2 1 
ATOM   228  C  CD1 . ILE   A 1 36  ? 3.26122   -11.84774 -9.70665  1.000 26.79275 ? 43  ILE   A CD1 1 
ATOM   229  N  N   . PHE   A 1 37  ? 0.48018   -14.08072 -10.52781 1.000 17.08634 ? 44  PHE   A N   1 
ATOM   230  C  CA  . PHE   A 1 37  ? 0.49037   -14.42726 -11.94755 1.000 18.09556 ? 44  PHE   A CA  1 
ATOM   231  C  C   . PHE   A 1 37  ? -0.85422  -14.10311 -12.59295 1.000 16.15830 ? 44  PHE   A C   1 
ATOM   232  O  O   . PHE   A 1 37  ? -0.90940  -13.66756 -13.74778 1.000 17.14517 ? 44  PHE   A O   1 
ATOM   233  C  CB  . PHE   A 1 37  ? 0.81295   -15.91318 -12.17110 1.000 17.28205 ? 44  PHE   A CB  1 
ATOM   234  C  CG  . PHE   A 1 37  ? -0.37516  -16.82602 -11.96999 1.000 17.22819 ? 44  PHE   A CG  1 
ATOM   235  C  CD1 . PHE   A 1 37  ? -0.71884  -17.27437 -10.70852 1.000 18.64692 ? 44  PHE   A CD1 1 
ATOM   236  C  CD2 . PHE   A 1 37  ? -1.18723  -17.18796 -13.04559 1.000 19.39783 ? 44  PHE   A CD2 1 
ATOM   237  C  CE1 . PHE   A 1 37  ? -1.82605  -18.09411 -10.51762 1.000 18.51041 ? 44  PHE   A CE1 1 
ATOM   238  C  CE2 . PHE   A 1 37  ? -2.30782  -17.99411 -12.85654 1.000 19.55767 ? 44  PHE   A CE2 1 
ATOM   239  C  CZ  . PHE   A 1 37  ? -2.62654  -18.44730 -11.59141 1.000 18.59118 ? 44  PHE   A CZ  1 
ATOM   240  N  N   . LEU   A 1 38  ? -1.94947  -14.30092 -11.85279 1.000 14.83118 ? 45  LEU   A N   1 
ATOM   241  C  CA  . LEU   A 1 38  ? -3.25457  -14.14092 -12.48441 1.000 15.35062 ? 45  LEU   A CA  1 
ATOM   242  C  C   . LEU   A 1 38  ? -3.56869  -12.66829 -12.70157 1.000 17.76683 ? 45  LEU   A C   1 
ATOM   243  O  O   . LEU   A 1 38  ? -4.10566  -12.29210 -13.75373 1.000 18.30837 ? 45  LEU   A O   1 
ATOM   244  C  CB  . LEU   A 1 38  ? -4.32957  -14.83535 -11.65216 1.000 15.99084 ? 45  LEU   A CB  1 
ATOM   245  C  CG  . LEU   A 1 38  ? -5.74519  -14.83515 -12.24136 1.000 17.35039 ? 45  LEU   A CG  1 
ATOM   246  C  CD1 . LEU   A 1 38  ? -5.75319  -15.53229 -13.58718 1.000 19.86382 ? 45  LEU   A CD1 1 
ATOM   247  C  CD2 . LEU   A 1 38  ? -6.70006  -15.53500 -11.29118 1.000 20.73611 ? 45  LEU   A CD2 1 
ATOM   248  N  N   . ARG   A 1 39  ? -3.21357  -11.82066 -11.72967 1.000 16.35285 ? 46  ARG   A N   1 
ATOM   249  C  CA  . ARG   A 1 39  ? -3.34843  -10.38148 -11.91703 1.000 18.04954 ? 46  ARG   A CA  1 
ATOM   250  C  C   . ARG   A 1 39  ? -2.56752  -9.92072  -13.13743 1.000 19.79177 ? 46  ARG   A C   1 
ATOM   251  O  O   . ARG   A 1 39  ? -3.05085  -9.09395  -13.92167 1.000 19.27947 ? 46  ARG   A O   1 
ATOM   252  C  CB  . ARG   A 1 39  ? -2.85327  -9.64759  -10.67053 1.000 22.00063 ? 46  ARG   A CB  1 
ATOM   253  C  CG  . ARG   A 1 39  ? -2.76002  -8.14211  -10.81819 1.000 22.12967 ? 46  ARG   A CG  1 
ATOM   254  C  CD  . ARG   A 1 39  ? -2.06855  -7.51769  -9.60650  1.000 26.31664 ? 46  ARG   A CD  1 
ATOM   255  N  NE  . ARG   A 1 39  ? -0.62785  -7.74958  -9.62474  1.000 30.10844 ? 46  ARG   A NE  1 
ATOM   256  C  CZ  . ARG   A 1 39  ? 0.16225   -7.65300  -8.56409  1.000 28.87966 ? 46  ARG   A CZ  1 
ATOM   257  N  NH1 . ARG   A 1 39  ? -0.31623  -7.34093  -7.36979  1.000 30.10618 ? 46  ARG   A NH1 1 
ATOM   258  N  NH2 . ARG   A 1 39  ? 1.46697   -7.87526  -8.70429  1.000 33.77703 ? 46  ARG   A NH2 1 
ATOM   259  N  N   . GLU   A 1 40  ? -1.36124  -10.46108 -13.32550 1.000 16.80100 ? 47  GLU   A N   1 
ATOM   260  C  CA  . GLU   A 1 40  ? -0.52571  -10.01159 -14.43103 1.000 17.08327 ? 47  GLU   A CA  1 
ATOM   261  C  C   . GLU   A 1 40  ? -1.11893  -10.41775 -15.77179 1.000 18.49828 ? 47  GLU   A C   1 
ATOM   262  O  O   . GLU   A 1 40  ? -1.12278  -9.62178  -16.71747 1.000 18.00175 ? 47  GLU   A O   1 
ATOM   263  C  CB  . GLU   A 1 40  ? 0.89781   -10.55598 -14.28189 1.000 17.15702 ? 47  GLU   A CB  1 
ATOM   264  C  CG  . GLU   A 1 40  ? 1.62773   -10.07243 -13.03666 1.000 19.60101 ? 47  GLU   A CG  1 
ATOM   265  C  CD  . GLU   A 1 40  ? 1.59869   -8.56072  -12.86244 1.000 24.96877 ? 47  GLU   A CD  1 
ATOM   266  O  OE1 . GLU   A 1 40  ? 1.66610   -7.82530  -13.86953 1.000 24.25512 ? 47  GLU   A OE1 1 
ATOM   267  O  OE2 . GLU   A 1 40  ? 1.49728   -8.10416  -11.70357 1.000 29.76922 ? 47  GLU   A OE2 1 
ATOM   268  N  N   . LEU   A 1 41  ? -1.64095  -11.64375 -15.86884 1.000 16.18025 ? 48  LEU   A N   1 
ATOM   269  C  CA  . LEU   A 1 41  ? -2.21506  -12.09326 -17.13851 1.000 16.84309 ? 48  LEU   A CA  1 
ATOM   270  C  C   . LEU   A 1 41  ? -3.52117  -11.37275 -17.44362 1.000 17.85745 ? 48  LEU   A C   1 
ATOM   271  O  O   . LEU   A 1 41  ? -3.80366  -11.05443 -18.60727 1.000 17.93392 ? 48  LEU   A O   1 
ATOM   272  C  CB  . LEU   A 1 41  ? -2.42929  -13.60550 -17.13123 1.000 17.08705 ? 48  LEU   A CB  1 
ATOM   273  C  CG  . LEU   A 1 41  ? -1.14323  -14.43215 -17.04578 1.000 19.08950 ? 48  LEU   A CG  1 
ATOM   274  C  CD1 . LEU   A 1 41  ? -1.44924  -15.91838 -16.89745 1.000 20.76959 ? 48  LEU   A CD1 1 
ATOM   275  C  CD2 . LEU   A 1 41  ? -0.22565  -14.18243 -18.23883 1.000 19.59281 ? 48  LEU   A CD2 1 
ATOM   276  N  N   . ILE   A 1 42  ? -4.34301  -11.12850 -16.42074 1.000 14.64384 ? 49  ILE   A N   1 
ATOM   277  C  CA  . ILE   A 1 42  ? -5.57085  -10.36930 -16.63105 1.000 15.64284 ? 49  ILE   A CA  1 
ATOM   278  C  C   . ILE   A 1 42  ? -5.25295  -8.94235  -17.05180 1.000 17.42757 ? 49  ILE   A C   1 
ATOM   279  O  O   . ILE   A 1 42  ? -5.91624  -8.37453  -17.92855 1.000 17.44056 ? 49  ILE   A O   1 
ATOM   280  C  CB  . ILE   A 1 42  ? -6.46175  -10.43567 -15.37550 1.000 16.33424 ? 49  ILE   A CB  1 
ATOM   281  C  CG1 . ILE   A 1 42  ? -7.04841  -11.84045 -15.23228 1.000 17.49960 ? 49  ILE   A CG1 1 
ATOM   282  C  CG2 . ILE   A 1 42  ? -7.57143  -9.37511  -15.42179 1.000 18.01154 ? 49  ILE   A CG2 1 
ATOM   283  C  CD1 . ILE   A 1 42  ? -7.82113  -12.05228 -13.93835 1.000 19.28503 ? 49  ILE   A CD1 1 
ATOM   284  N  N   . SER   A 1 43  ? -4.21687  -8.34308  -16.45426 1.000 16.86177 ? 50  SER   A N   1 
ATOM   285  C  CA  . SER   A 1 43  ? -3.81497  -7.00309  -16.85903 1.000 16.41429 ? 50  SER   A CA  1 
ATOM   286  C  C   . SER   A 1 43  ? -3.36084  -6.98743  -18.31783 1.000 17.52000 ? 50  SER   A C   1 
ATOM   287  O  O   . SER   A 1 43  ? -3.70079  -6.06906  -19.07605 1.000 17.63973 ? 50  SER   A O   1 
ATOM   288  C  CB  . SER   A 1 43  ? -2.70608  -6.50190  -15.93015 1.000 20.73348 ? 50  SER   A CB  1 
ATOM   289  O  OG  . SER   A 1 43  ? -2.17160  -5.27000  -16.38183 1.000 26.90850 ? 50  SER   A OG  1 
ATOM   290  N  N   . ASN   A 1 44  ? -2.59422  -7.99747  -18.73052 1.000 17.42540 ? 51  ASN   A N   1 
ATOM   291  C  CA  . ASN   A 1 44  ? -2.18646  -8.07454  -20.13157 1.000 16.91141 ? 51  ASN   A CA  1 
ATOM   292  C  C   . ASN   A 1 44  ? -3.39343  -8.20834  -21.05151 1.000 16.15686 ? 51  ASN   A C   1 
ATOM   293  O  O   . ASN   A 1 44  ? -3.43588  -7.58695  -22.12042 1.000 17.27328 ? 51  ASN   A O   1 
ATOM   294  C  CB  . ASN   A 1 44  ? -1.23633  -9.25115  -20.33945 1.000 17.90869 ? 51  ASN   A CB  1 
ATOM   295  C  CG  . ASN   A 1 44  ? 0.12448   -9.00260  -19.76129 1.000 26.11318 ? 51  ASN   A CG  1 
ATOM   296  O  OD1 . ASN   A 1 44  ? 0.42885   -7.90094  -19.30336 1.000 23.33522 ? 51  ASN   A OD1 1 
ATOM   297  N  ND2 . ASN   A 1 44  ? 0.96329   -10.02592 -19.78686 1.000 26.32882 ? 51  ASN   A ND2 1 
ATOM   298  N  N   . SER   A 1 45  ? -4.37905  -9.02146  -20.65914 1.000 15.06145 ? 52  SER   A N   1 
ATOM   299  C  CA  . SER   A 1 45  ? -5.59606  -9.14014  -21.45816 1.000 16.52064 ? 52  SER   A CA  1 
ATOM   300  C  C   . SER   A 1 45  ? -6.31962  -7.80431  -21.54903 1.000 15.64085 ? 52  SER   A C   1 
ATOM   301  O  O   . SER   A 1 45  ? -6.79530  -7.41932  -22.62446 1.000 16.62234 ? 52  SER   A O   1 
ATOM   302  C  CB  . SER   A 1 45  ? -6.52429  -10.18893 -20.84578 1.000 15.13084 ? 52  SER   A CB  1 
ATOM   303  O  OG  . SER   A 1 45  ? -6.00533  -11.49402 -21.00639 1.000 18.03855 ? 52  SER   A OG  1 
ATOM   304  N  N   . SER   A 1 46  ? -6.42211  -7.08625  -20.42608 1.000 15.49293 ? 53  SER   A N   1 
ATOM   305  C  CA  . SER   A 1 46  ? -7.06105  -5.77385  -20.44417 1.000 17.13633 ? 53  SER   A CA  1 
ATOM   306  C  C   . SER   A 1 46  ? -6.34048  -4.82942  -21.40025 1.000 16.43494 ? 53  SER   A C   1 
ATOM   307  O  O   . SER   A 1 46  ? -6.98225  -4.09476  -22.15985 1.000 17.50117 ? 53  SER   A O   1 
ATOM   308  C  CB  . SER   A 1 46  ? -7.11082  -5.19687  -19.02432 1.000 17.90356 ? 53  SER   A CB  1 
ATOM   309  O  OG  . SER   A 1 46  ? -7.66569  -3.89075  -19.01021 1.000 19.89684 ? 53  SER   A OG  1 
ATOM   310  N  N   . ASP   A 1 47  ? -5.00243  -4.85564  -21.39632 1.000 16.48843 ? 54  ASP   A N   1 
ATOM   311  C  CA  . ASP   A 1 47  ? -4.24293  -3.98875  -22.28978 1.000 19.21083 ? 54  ASP   A CA  1 
ATOM   312  C  C   . ASP   A 1 47  ? -4.53137  -4.33099  -23.74806 1.000 16.87117 ? 54  ASP   A C   1 
ATOM   313  O  O   . ASP   A 1 47  ? -4.64602  -3.43663  -24.59593 1.000 17.75342 ? 54  ASP   A O   1 
ATOM   314  C  CB  . ASP   A 1 47  ? -2.75203  -4.15745  -21.99532 1.000 17.39251 ? 54  ASP   A CB  1 
ATOM   315  C  CG  . ASP   A 1 47  ? -2.30740  -3.41316  -20.74441 1.000 23.00991 ? 54  ASP   A CG  1 
ATOM   316  O  OD1 . ASP   A 1 47  ? -3.10494  -2.63524  -20.17281 1.000 23.91647 ? 54  ASP   A OD1 1 
ATOM   317  O  OD2 . ASP   A 1 47  ? -1.15021  -3.62301  -20.31698 1.000 26.77162 ? 54  ASP   A OD2 1 
ATOM   318  N  N   . ALA   A 1 48  ? -4.67098  -5.62230  -24.05491 1.000 15.58657 ? 55  ALA   A N   1 
ATOM   319  C  CA  . ALA   A 1 48  ? -4.92369  -6.03471  -25.43033 1.000 17.33423 ? 55  ALA   A CA  1 
ATOM   320  C  C   . ALA   A 1 48  ? -6.33711  -5.67641  -25.86462 1.000 15.85508 ? 55  ALA   A C   1 
ATOM   321  O  O   . ALA   A 1 48  ? -6.56973  -5.35505  -27.03610 1.000 16.66795 ? 55  ALA   A O   1 
ATOM   322  C  CB  . ALA   A 1 48  ? -4.69265  -7.53410  -25.57357 1.000 16.60792 ? 55  ALA   A CB  1 
ATOM   323  N  N   . LEU   A 1 49  ? -7.29455  -5.75682  -24.93738 1.000 15.85784 ? 56  LEU   A N   1 
ATOM   324  C  CA  . LEU   A 1 49  ? -8.65765  -5.32648  -25.22426 1.000 16.81441 ? 56  LEU   A CA  1 
ATOM   325  C  C   . LEU   A 1 49  ? -8.71985  -3.81740  -25.43963 1.000 17.29312 ? 56  LEU   A C   1 
ATOM   326  O  O   . LEU   A 1 49  ? -9.44126  -3.34362  -26.32757 1.000 17.88353 ? 56  LEU   A O   1 
ATOM   327  C  CB  . LEU   A 1 49  ? -9.57683  -5.76659  -24.08404 1.000 17.28466 ? 56  LEU   A CB  1 
ATOM   328  C  CG  . LEU   A 1 49  ? -9.82482  -7.27777  -24.07961 1.000 15.65600 ? 56  LEU   A CG  1 
ATOM   329  C  CD1 . LEU   A 1 49  ? -10.26487 -7.75558  -22.70204 1.000 18.90882 ? 56  LEU   A CD1 1 
ATOM   330  C  CD2 . LEU   A 1 49  ? -10.88810 -7.63333  -25.11426 1.000 17.32659 ? 56  LEU   A CD2 1 
ATOM   331  N  N   . ASP   A 1 50  ? -7.95902  -3.04655  -24.65294 1.000 16.10855 ? 57  ASP   A N   1 
ATOM   332  C  CA  . ASP   A 1 50  ? -7.89669  -1.60155  -24.87061 1.000 17.11732 ? 57  ASP   A CA  1 
ATOM   333  C  C   . ASP   A 1 50  ? -7.41968  -1.28634  -26.28337 1.000 17.30097 ? 57  ASP   A C   1 
ATOM   334  O  O   . ASP   A 1 50  ? -7.92160  -0.35500  -26.92423 1.000 18.43605 ? 57  ASP   A O   1 
ATOM   335  C  CB  . ASP   A 1 50  ? -6.93223  -0.94468  -23.87871 1.000 18.05901 ? 57  ASP   A CB  1 
ATOM   336  C  CG  . ASP   A 1 50  ? -7.46589  -0.88087  -22.45580 1.000 21.66838 ? 57  ASP   A CG  1 
ATOM   337  O  OD1 . ASP   A 1 50  ? -8.64220  -1.21417  -22.20986 1.000 23.72187 ? 57  ASP   A OD1 1 
ATOM   338  O  OD2 . ASP   A 1 50  ? -6.68867  -0.45835  -21.57324 1.000 23.84819 ? 57  ASP   A OD2 1 
ATOM   339  N  N   . LYS   A 1 51  ? -6.43770  -2.04737  -26.77521 1.000 17.01898 ? 58  LYS   A N   1 
ATOM   340  C  CA  . LYS   A 1 51  ? -5.84343  -1.76228  -28.07828 1.000 17.66545 ? 58  LYS   A CA  1 
ATOM   341  C  C   . LYS   A 1 51  ? -6.84621  -1.96785  -29.20686 1.000 17.45007 ? 58  LYS   A C   1 
ATOM   342  O  O   . LYS   A 1 51  ? -6.95711  -1.12631  -30.10800 1.000 19.41114 ? 58  LYS   A O   1 
ATOM   343  C  CB  . LYS   A 1 51  ? -4.60363  -2.63503  -28.28737 1.000 19.50436 ? 58  LYS   A CB  1 
ATOM   344  C  CG  . LYS   A 1 51  ? -3.39660  -2.19734  -27.47786 1.000 21.98873 ? 58  LYS   A CG  1 
ATOM   345  C  CD  . LYS   A 1 51  ? -2.24421  -3.18379  -27.65415 1.000 23.50955 ? 58  LYS   A CD  1 
ATOM   346  C  CE  . LYS   A 1 51  ? -1.18479  -3.00185  -26.57495 1.000 29.51544 ? 58  LYS   A CE  1 
ATOM   347  N  NZ  . LYS   A 1 51  ? -0.08199  -3.99672  -26.72263 1.000 34.66628 ? 58  LYS   A NZ  1 
ATOM   348  N  N   . ILE   A 1 52  ? -7.58061  -3.08246  -29.18806 1.000 17.13128 ? 59  ILE   A N   1 
ATOM   349  C  CA  . ILE   A 1 52  ? -8.55758  -3.30056  -30.25362 1.000 17.49402 ? 59  ILE   A CA  1 
ATOM   350  C  C   . ILE   A 1 52  ? -9.71595  -2.32198  -30.12449 1.000 19.29315 ? 59  ILE   A C   1 
ATOM   351  O  O   . ILE   A 1 52  ? -10.25764 -1.85882  -31.13445 1.000 20.03439 ? 59  ILE   A O   1 
ATOM   352  C  CB  . ILE   A 1 52  ? -9.01053  -4.77165  -30.34603 1.000 17.84516 ? 59  ILE   A CB  1 
ATOM   353  C  CG1 . ILE   A 1 52  ? -9.83846  -5.00220  -31.61601 1.000 19.65921 ? 59  ILE   A CG1 1 
ATOM   354  C  CG2 . ILE   A 1 52  ? -9.80920  -5.18266  -29.11314 1.000 19.69509 ? 59  ILE   A CG2 1 
ATOM   355  C  CD1 . ILE   A 1 52  ? -9.08660  -4.71587  -32.90564 1.000 22.92803 ? 59  ILE   A CD1 1 
ATOM   356  N  N   . ARG   A 1 53  ? -10.09055 -1.95593  -28.89726 1.000 18.17140 ? 60  ARG   A N   1 
ATOM   357  C  CA  . ARG   A 1 53  ? -11.13496 -0.94908  -28.73316 1.000 18.44201 ? 60  ARG   A CA  1 
ATOM   358  C  C   . ARG   A 1 53  ? -10.72427 0.37505   -29.35744 1.000 19.69130 ? 60  ARG   A C   1 
ATOM   359  O  O   . ARG   A 1 53  ? -11.50605 0.99620   -30.08748 1.000 20.82069 ? 60  ARG   A O   1 
ATOM   360  C  CB  . ARG   A 1 53  ? -11.49668 -0.76936  -27.25791 1.000 22.63946 ? 60  ARG   A CB  1 
ATOM   361  C  CG  . ARG   A 1 53  ? -12.63227 0.22956   -27.06518 1.000 28.66639 ? 60  ARG   A CG  1 
ATOM   362  C  CD  . ARG   A 1 53  ? -13.00793 0.39078   -25.61192 1.000 35.66250 ? 60  ARG   A CD  1 
ATOM   363  N  NE  . ARG   A 1 53  ? -14.07329 -0.52418  -25.22063 1.000 43.13165 ? 60  ARG   A NE  1 
ATOM   364  C  CZ  . ARG   A 1 53  ? -14.26047 -0.96257  -23.98408 1.000 44.70117 ? 60  ARG   A CZ  1 
ATOM   365  N  NH1 . ARG   A 1 53  ? -13.43861 -0.62830  -23.00283 1.000 41.49548 ? 60  ARG   A NH1 1 
ATOM   366  N  NH2 . ARG   A 1 53  ? -15.29590 -1.75724  -23.72628 1.000 35.08093 ? 60  ARG   A NH2 1 
ATOM   367  N  N   . TYR   A 1 54  ? -9.49630  0.83031   -29.08575 1.000 18.76784 ? 61  TYR   A N   1 
ATOM   368  C  CA  . TYR   A 1 54  ? -9.04357  2.09531   -29.64919 1.000 19.94352 ? 61  TYR   A CA  1 
ATOM   369  C  C   . TYR   A 1 54  ? -9.05743  2.05427   -31.17555 1.000 20.93251 ? 61  TYR   A C   1 
ATOM   370  O  O   . TYR   A 1 54  ? -9.52720  2.99313   -31.82641 1.000 22.29144 ? 61  TYR   A O   1 
ATOM   371  C  CB  . TYR   A 1 54  ? -7.64462  2.44129   -29.14180 1.000 20.65444 ? 61  TYR   A CB  1 
ATOM   372  C  CG  . TYR   A 1 54  ? -7.19328  3.80115   -29.62171 1.000 23.37860 ? 61  TYR   A CG  1 
ATOM   373  C  CD1 . TYR   A 1 54  ? -7.73026  4.96302   -29.08332 1.000 23.81995 ? 61  TYR   A CD1 1 
ATOM   374  C  CD2 . TYR   A 1 54  ? -6.27889  3.92171   -30.66055 1.000 24.16241 ? 61  TYR   A CD2 1 
ATOM   375  C  CE1 . TYR   A 1 54  ? -7.33653  6.20941   -29.53514 1.000 25.69907 ? 61  TYR   A CE1 1 
ATOM   376  C  CE2 . TYR   A 1 54  ? -5.88261  5.16281   -31.12450 1.000 26.26409 ? 61  TYR   A CE2 1 
ATOM   377  C  CZ  . TYR   A 1 54  ? -6.41405  6.30173   -30.55901 1.000 27.86866 ? 61  TYR   A CZ  1 
ATOM   378  O  OH  . TYR   A 1 54  ? -6.01804  7.53621   -31.01415 1.000 31.90471 ? 61  TYR   A OH  1 
ATOM   379  N  N   . GLU   A 1 55  ? -8.52746  0.97670   -31.76288 1.000 20.09154 ? 62  GLU   A N   1 
ATOM   380  C  CA  . GLU   A 1 55  ? -8.54367  0.85434   -33.22123 1.000 22.08795 ? 62  GLU   A CA  1 
ATOM   381  C  C   . GLU   A 1 55  ? -9.96319  0.88482   -33.76700 1.000 24.25509 ? 62  GLU   A C   1 
ATOM   382  O  O   . GLU   A 1 55  ? -10.21559 1.47526   -34.82391 1.000 25.39557 ? 62  GLU   A O   1 
ATOM   383  C  CB  . GLU   A 1 55  ? -7.82182  -0.41892  -33.66267 1.000 23.23568 ? 62  GLU   A CB  1 
ATOM   384  C  CG  . GLU   A 1 55  ? -6.32492  -0.38251  -33.41437 1.000 24.61263 ? 62  GLU   A CG  1 
ATOM   385  C  CD  . GLU   A 1 55  ? -5.58087  -1.47834  -34.15289 1.000 35.23838 ? 62  GLU   A CD  1 
ATOM   386  O  OE1 . GLU   A 1 55  ? -6.24422  -2.35757  -34.73947 1.000 31.79865 ? 62  GLU   A OE1 1 
ATOM   387  O  OE2 . GLU   A 1 55  ? -4.33136  -1.44760  -34.16474 1.000 37.81151 ? 62  GLU   A OE2 1 
ATOM   388  N  N   . SER   A 1 56  ? -10.90848 0.27524   -33.05179 1.000 20.97400 ? 63  SER   A N   1 
ATOM   389  C  CA  . SER   A 1 56  ? -12.28640 0.23046   -33.52791 1.000 23.42315 ? 63  SER   A CA  1 
ATOM   390  C  C   . SER   A 1 56  ? -12.96209 1.59630   -33.51005 1.000 24.64332 ? 63  SER   A C   1 
ATOM   391  O  O   . SER   A 1 56  ? -13.98501 1.77050   -34.17657 1.000 25.26483 ? 63  SER   A O   1 
ATOM   392  C  CB  . SER   A 1 56  ? -13.10232 -0.76149  -32.69915 1.000 22.86870 ? 63  SER   A CB  1 
ATOM   393  O  OG  . SER   A 1 56  ? -13.48434 -0.20491  -31.44848 1.000 24.93761 ? 63  SER   A OG  1 
ATOM   394  N  N   . LEU   A 1 57  ? -12.42478 2.56576   -32.76414 1.000 22.15800 ? 64  LEU   A N   1 
ATOM   395  C  CA  . LEU   A 1 57  ? -13.07117 3.87276   -32.67965 1.000 26.45018 ? 64  LEU   A CA  1 
ATOM   396  C  C   . LEU   A 1 57  ? -13.04122 4.61015   -34.01156 1.000 28.87378 ? 64  LEU   A C   1 
ATOM   397  O  O   . LEU   A 1 57  ? -13.94867 5.39664   -34.30203 1.000 32.17837 ? 64  LEU   A O   1 
ATOM   398  C  CB  . LEU   A 1 57  ? -12.42278 4.72347   -31.58571 1.000 25.79826 ? 64  LEU   A CB  1 
ATOM   399  C  CG  . LEU   A 1 57  ? -12.54140 4.21188   -30.14909 1.000 27.30890 ? 64  LEU   A CG  1 
ATOM   400  C  CD1 . LEU   A 1 57  ? -11.86717 5.18502   -29.19818 1.000 27.42735 ? 64  LEU   A CD1 1 
ATOM   401  C  CD2 . LEU   A 1 57  ? -13.99391 4.00409   -29.76350 1.000 27.57718 ? 64  LEU   A CD2 1 
ATOM   402  N  N   . THR   A 1 58  ? -12.01558 4.37878   -34.82780 1.000 29.32883 ? 65  THR   A N   1 
ATOM   403  C  CA  . THR   A 1 58  ? -11.92070 4.99928   -36.14062 1.000 28.64585 ? 65  THR   A CA  1 
ATOM   404  C  C   . THR   A 1 58  ? -12.15550 4.02313   -37.28503 1.000 32.94376 ? 65  THR   A C   1 
ATOM   405  O  O   . THR   A 1 58  ? -12.24873 4.46421   -38.43737 1.000 37.10780 ? 65  THR   A O   1 
ATOM   406  C  CB  . THR   A 1 58  ? -10.55205 5.67031   -36.32113 1.000 38.39573 ? 65  THR   A CB  1 
ATOM   407  O  OG1 . THR   A 1 58  ? -9.51557  4.69310   -36.16599 1.000 39.35602 ? 65  THR   A OG1 1 
ATOM   408  C  CG2 . THR   A 1 58  ? -10.36324 6.78196   -35.29937 1.000 33.05600 ? 65  THR   A CG2 1 
ATOM   409  N  N   . ASP   A 1 59  ? -12.25415 2.73150   -37.00376 1.000 31.35863 ? 66  ASP   A N   1 
ATOM   410  C  CA  . ASP   A 1 59  ? -12.46120 1.71879   -38.04328 1.000 28.20011 ? 66  ASP   A CA  1 
ATOM   411  C  C   . ASP   A 1 59  ? -13.29328 0.60877   -37.43337 1.000 28.33677 ? 66  ASP   A C   1 
ATOM   412  O  O   . ASP   A 1 59  ? -12.75657 -0.35532  -36.86085 1.000 29.20926 ? 66  ASP   A O   1 
ATOM   413  C  CB  . ASP   A 1 59  ? -11.13167 1.18875   -38.57527 1.000 31.08534 ? 66  ASP   A CB  1 
ATOM   414  C  CG  . ASP   A 1 59  ? -11.30382 0.19766   -39.71689 1.000 37.21604 ? 66  ASP   A CG  1 
ATOM   415  O  OD1 . ASP   A 1 59  ? -12.45530 -0.09178  -40.09942 1.000 37.33673 ? 66  ASP   A OD1 1 
ATOM   416  O  OD2 . ASP   A 1 59  ? -10.27796 -0.28694  -40.23955 1.000 40.17703 ? 66  ASP   A OD2 1 
ATOM   417  N  N   . PRO   A 1 60  ? -14.62130 0.70558   -37.50790 1.000 33.42702 ? 67  PRO   A N   1 
ATOM   418  C  CA  . PRO   A 1 60  ? -15.47471 -0.32704  -36.90070 1.000 30.16884 ? 67  PRO   A CA  1 
ATOM   419  C  C   . PRO   A 1 60  ? -15.25734 -1.72121  -37.46615 1.000 27.89659 ? 67  PRO   A C   1 
ATOM   420  O  O   . PRO   A 1 60  ? -15.54476 -2.70155  -36.76684 1.000 28.60435 ? 67  PRO   A O   1 
ATOM   421  C  CB  . PRO   A 1 60  ? -16.90324 0.16642   -37.16348 1.000 36.28200 ? 67  PRO   A CB  1 
ATOM   422  C  CG  . PRO   A 1 60  ? -16.78733 1.58820   -37.56031 1.000 46.19709 ? 67  PRO   A CG  1 
ATOM   423  C  CD  . PRO   A 1 60  ? -15.38143 1.87903   -37.97957 1.000 37.15508 ? 67  PRO   A CD  1 
ATOM   424  N  N   . SER   A 1 61  ? -14.76440 -1.84656  -38.70376 1.000 32.70357 ? 68  SER   A N   1 
ATOM   425  C  CA  . SER   A 1 61  ? -14.53173 -3.16769  -39.27815 1.000 29.62901 ? 68  SER   A CA  1 
ATOM   426  C  C   . SER   A 1 61  ? -13.46083 -3.94887  -38.53103 1.000 27.82841 ? 68  SER   A C   1 
ATOM   427  O  O   . SER   A 1 61  ? -13.34487 -5.16151  -38.73783 1.000 27.79824 ? 68  SER   A O   1 
ATOM   428  C  CB  . SER   A 1 61  ? -14.16953 -3.07163  -40.76379 1.000 28.97815 ? 68  SER   A CB  1 
ATOM   429  O  OG  . SER   A 1 61  ? -12.87962 -2.51494  -40.94850 1.000 34.14063 ? 68  SER   A OG  1 
ATOM   430  N  N   . LYS   A 1 62  ? -12.68148 -3.29256  -37.66659 1.000 25.72182 ? 69  LYS   A N   1 
ATOM   431  C  CA  . LYS   A 1 62  ? -11.73056 -4.01446  -36.83274 1.000 25.61375 ? 69  LYS   A CA  1 
ATOM   432  C  C   . LYS   A 1 62  ? -12.41120 -5.02604  -35.92054 1.000 25.43481 ? 69  LYS   A C   1 
ATOM   433  O  O   . LYS   A 1 62  ? -11.75238 -5.95671  -35.44248 1.000 23.19954 ? 69  LYS   A O   1 
ATOM   434  C  CB  . LYS   A 1 62  ? -10.92128 -3.02719  -35.99327 1.000 27.58724 ? 69  LYS   A CB  1 
ATOM   435  C  CG  . LYS   A 1 62  ? -10.07228 -2.07181  -36.80732 1.000 30.46868 ? 69  LYS   A CG  1 
ATOM   436  C  CD  . LYS   A 1 62  ? -8.63637  -2.54780  -36.84826 1.000 33.05442 ? 69  LYS   A CD  1 
ATOM   437  C  CE  . LYS   A 1 62  ? -7.78823  -1.70235  -37.77160 1.000 30.53647 ? 69  LYS   A CE  1 
ATOM   438  N  NZ  . LYS   A 1 62  ? -6.38274  -2.19704  -37.77917 1.000 40.09139 ? 69  LYS   A NZ  1 
ATOM   439  N  N   . LEU   A 1 63  ? -13.70317 -4.85835  -35.64916 1.000 23.80648 ? 70  LEU   A N   1 
ATOM   440  C  CA  . LEU   A 1 63  ? -14.44459 -5.78792  -34.81108 1.000 25.17953 ? 70  LEU   A CA  1 
ATOM   441  C  C   . LEU   A 1 63  ? -15.25355 -6.79512  -35.61711 1.000 25.04155 ? 70  LEU   A C   1 
ATOM   442  O  O   . LEU   A 1 63  ? -16.07635 -7.51086  -35.03918 1.000 26.90741 ? 70  LEU   A O   1 
ATOM   443  C  CB  . LEU   A 1 63  ? -15.34841 -5.03370  -33.82976 1.000 24.29526 ? 70  LEU   A CB  1 
ATOM   444  C  CG  . LEU   A 1 63  ? -14.62390 -4.09513  -32.86311 1.000 26.56614 ? 70  LEU   A CG  1 
ATOM   445  C  CD1 . LEU   A 1 63  ? -15.62386 -3.39014  -31.95191 1.000 29.21147 ? 70  LEU   A CD1 1 
ATOM   446  C  CD2 . LEU   A 1 63  ? -13.60765 -4.87329  -32.04941 1.000 25.99683 ? 70  LEU   A CD2 1 
ATOM   447  N  N   . ASP   A 1 64  ? -15.03250 -6.87685  -36.93284 1.000 25.34405 ? 71  ASP   A N   1 
ATOM   448  C  CA  . ASP   A 1 64  ? -15.72405 -7.88737  -37.72889 1.000 29.74919 ? 71  ASP   A CA  1 
ATOM   449  C  C   . ASP   A 1 64  ? -15.36572 -9.29460  -37.27354 1.000 27.59585 ? 71  ASP   A C   1 
ATOM   450  O  O   . ASP   A 1 64  ? -16.15122 -10.22687 -37.48000 1.000 30.42884 ? 71  ASP   A O   1 
ATOM   451  C  CB  . ASP   A 1 64  ? -15.39235 -7.72016  -39.21475 1.000 30.01013 ? 71  ASP   A CB  1 
ATOM   452  C  CG  . ASP   A 1 64  ? -16.08968 -6.52522  -39.84076 1.000 35.56255 ? 71  ASP   A CG  1 
ATOM   453  O  OD1 . ASP   A 1 64  ? -16.98124 -5.94338  -39.18714 1.000 36.81771 ? 71  ASP   A OD1 1 
ATOM   454  O  OD2 . ASP   A 1 64  ? -15.74914 -6.16964  -40.99008 1.000 38.61859 ? 71  ASP   A OD2 1 
ATOM   455  N  N   . SER   A 1 65  ? -14.19745 -9.45910  -36.66065 1.000 23.13386 ? 72  SER   A N   1 
ATOM   456  C  CA  . SER   A 1 65  ? -13.73569 -10.71750 -36.09699 1.000 23.98733 ? 72  SER   A CA  1 
ATOM   457  C  C   . SER   A 1 65  ? -14.27569 -10.97306 -34.69438 1.000 28.52540 ? 72  SER   A C   1 
ATOM   458  O  O   . SER   A 1 65  ? -13.81339 -11.90494 -34.02786 1.000 30.10376 ? 72  SER   A O   1 
ATOM   459  C  CB  . SER   A 1 65  ? -12.20544 -10.72425 -36.07269 1.000 23.79879 ? 72  SER   A CB  1 
ATOM   460  O  OG  . SER   A 1 65  ? -11.71732 -9.52341  -35.49052 1.000 23.20853 ? 72  SER   A OG  1 
ATOM   461  N  N   . GLY   A 1 66  ? -15.22734 -10.16663 -34.22995 1.000 25.15896 ? 73  GLY   A N   1 
ATOM   462  C  CA  . GLY   A 1 66  ? -15.80006 -10.33991 -32.90928 1.000 30.31397 ? 73  GLY   A CA  1 
ATOM   463  C  C   . GLY   A 1 66  ? -16.04938 -9.02424  -32.19842 1.000 26.18567 ? 73  GLY   A C   1 
ATOM   464  O  O   . GLY   A 1 66  ? -15.10780 -8.27656  -31.92152 1.000 22.48093 ? 73  GLY   A O   1 
ATOM   465  N  N   . LYS   A 1 67  ? -17.31384 -8.73132  -31.88851 1.000 26.80977 ? 74  LYS   A N   1 
ATOM   466  C  CA  . LYS   A 1 67  ? -17.66095 -7.46914  -31.24628 1.000 26.72965 ? 74  LYS   A CA  1 
ATOM   467  C  C   . LYS   A 1 67  ? -17.48130 -7.49945  -29.73276 1.000 23.67014 ? 74  LYS   A C   1 
ATOM   468  O  O   . LYS   A 1 67  ? -17.30089 -6.43969  -29.12518 1.000 28.90569 ? 74  LYS   A O   1 
ATOM   469  C  CB  . LYS   A 1 67  ? -19.11328 -7.09654  -31.56548 1.000 28.55138 ? 74  LYS   A CB  1 
ATOM   470  C  CG  . LYS   A 1 67  ? -19.37992 -6.80812  -33.03273 1.000 39.70687 ? 74  LYS   A CG  1 
ATOM   471  C  CD  . LYS   A 1 67  ? -20.28289 -5.59222  -33.19991 1.000 46.66365 ? 74  LYS   A CD  1 
ATOM   472  C  CE  . LYS   A 1 67  ? -20.22912 -5.05386  -34.62042 1.000 59.17102 ? 74  LYS   A CE  1 
ATOM   473  N  NZ  . LYS   A 1 67  ? -20.26958 -6.15086  -35.62757 1.000 62.92816 ? 74  LYS   A NZ  1 
ATOM   474  N  N   . GLU   A 1 68  ? -17.53830 -8.67307  -29.11201 1.000 22.70970 ? 75  GLU   A N   1 
ATOM   475  C  CA  . GLU   A 1 68  ? -17.52944 -8.75348  -27.65727 1.000 23.94846 ? 75  GLU   A CA  1 
ATOM   476  C  C   . GLU   A 1 68  ? -16.10643 -8.62224  -27.13379 1.000 20.98003 ? 75  GLU   A C   1 
ATOM   477  O  O   . GLU   A 1 68  ? -15.19157 -9.26340  -27.64885 1.000 23.52553 ? 75  GLU   A O   1 
ATOM   478  C  CB  . GLU   A 1 68  ? -18.12738 -10.08174 -27.19537 1.000 29.80198 ? 75  GLU   A CB  1 
ATOM   479  C  CG  . GLU   A 1 68  ? -19.63374 -10.20181 -27.39866 1.000 35.89505 ? 75  GLU   A CG  1 
ATOM   480  C  CD  . GLU   A 1 68  ? -20.01902 -10.47933 -28.84093 1.000 58.21762 ? 75  GLU   A CD  1 
ATOM   481  O  OE1 . GLU   A 1 68  ? -21.10394 -10.02731 -29.26645 1.000 63.21012 ? 75  GLU   A OE1 1 
ATOM   482  O  OE2 . GLU   A 1 68  ? -19.23935 -11.15451 -29.54673 1.000 51.07291 ? 75  GLU   A OE2 1 
ATOM   483  N  N   . LEU   A 1 69  ? -15.93000 -7.79668  -26.10525 1.000 20.51860 ? 76  LEU   A N   1 
ATOM   484  C  CA  . LEU   A 1 69  ? -14.63060 -7.54885  -25.48347 1.000 18.72791 ? 76  LEU   A CA  1 
ATOM   485  C  C   . LEU   A 1 69  ? -14.69573 -8.06983  -24.05112 1.000 16.91506 ? 76  LEU   A C   1 
ATOM   486  O  O   . LEU   A 1 69  ? -15.33690 -7.45480  -23.18975 1.000 19.47058 ? 76  LEU   A O   1 
ATOM   487  C  CB  . LEU   A 1 69  ? -14.33147 -6.05143  -25.51073 1.000 19.80865 ? 76  LEU   A CB  1 
ATOM   488  C  CG  . LEU   A 1 69  ? -14.29088 -5.39586  -26.89793 1.000 22.36167 ? 76  LEU   A CG  1 
ATOM   489  C  CD1 . LEU   A 1 69  ? -13.84573 -3.94345  -26.79752 1.000 31.07081 ? 76  LEU   A CD1 1 
ATOM   490  C  CD2 . LEU   A 1 69  ? -13.37017 -6.16529  -27.83446 1.000 22.18070 ? 76  LEU   A CD2 1 
ATOM   491  N  N   . HIS   A 1 70  ? -14.02720 -9.19465  -23.79022 1.000 15.94825 ? 77  HIS   A N   1 
ATOM   492  C  CA  . HIS   A 1 70  ? -14.21036 -9.88045  -22.51724 1.000 17.96231 ? 77  HIS   A CA  1 
ATOM   493  C  C   . HIS   A 1 70  ? -13.00669 -10.75458 -22.19711 1.000 15.54267 ? 77  HIS   A C   1 
ATOM   494  O  O   . HIS   A 1 70  ? -12.14410 -11.01103 -23.04303 1.000 14.60409 ? 77  HIS   A O   1 
ATOM   495  C  CB  . HIS   A 1 70  ? -15.49901 -10.71505 -22.52799 1.000 18.26752 ? 77  HIS   A CB  1 
ATOM   496  C  CG  . HIS   A 1 70  ? -15.49072 -11.83119 -23.53062 1.000 17.77308 ? 77  HIS   A CG  1 
ATOM   497  N  ND1 . HIS   A 1 70  ? -16.45296 -11.95018 -24.50955 1.000 26.50908 ? 77  HIS   A ND1 1 
ATOM   498  C  CD2 . HIS   A 1 70  ? -14.66360 -12.89235 -23.68629 1.000 21.41358 ? 77  HIS   A CD2 1 
ATOM   499  C  CE1 . HIS   A 1 70  ? -16.20256 -13.02068 -25.24241 1.000 23.64447 ? 77  HIS   A CE1 1 
ATOM   500  N  NE2 . HIS   A 1 70  ? -15.12619 -13.61272 -24.76223 1.000 24.36564 ? 77  HIS   A NE2 1 
ATOM   501  N  N   . ILE   A 1 71  ? -12.98895 -11.23266 -20.95180 1.000 17.29738 ? 78  ILE   A N   1 
ATOM   502  C  CA  . ILE   A 1 71  ? -11.96264 -12.11385 -20.41386 1.000 16.06899 ? 78  ILE   A CA  1 
ATOM   503  C  C   . ILE   A 1 71  ? -12.65947 -13.30530 -19.77094 1.000 15.04743 ? 78  ILE   A C   1 
ATOM   504  O  O   . ILE   A 1 71  ? -13.55228 -13.12425 -18.93498 1.000 16.96678 ? 78  ILE   A O   1 
ATOM   505  C  CB  . ILE   A 1 71  ? -11.11010 -11.38583 -19.35553 1.000 16.38757 ? 78  ILE   A CB  1 
ATOM   506  C  CG1 . ILE   A 1 71  ? -10.45442 -10.13741 -19.95410 1.000 17.37710 ? 78  ILE   A CG1 1 
ATOM   507  C  CG2 . ILE   A 1 71  ? -10.08348 -12.33738 -18.75820 1.000 16.43067 ? 78  ILE   A CG2 1 
ATOM   508  C  CD1 . ILE   A 1 71  ? -9.74159  -9.25918  -18.92843 1.000 18.55046 ? 78  ILE   A CD1 1 
ATOM   509  N  N   . ASN   A 1 72  ? -12.25805 -14.51485 -20.15633 1.000 15.62999 ? 79  ASN   A N   1 
ATOM   510  C  CA  . ASN   A 1 72  ? -12.79144 -15.74090 -19.57632 1.000 15.33522 ? 79  ASN   A CA  1 
ATOM   511  C  C   . ASN   A 1 72  ? -11.67786 -16.50257 -18.86898 1.000 17.13468 ? 79  ASN   A C   1 
ATOM   512  O  O   . ASN   A 1 72  ? -10.55818 -16.60992 -19.38489 1.000 15.53664 ? 79  ASN   A O   1 
ATOM   513  C  CB  . ASN   A 1 72  ? -13.43152 -16.64181 -20.64668 1.000 15.54726 ? 79  ASN   A CB  1 
ATOM   514  C  CG  . ASN   A 1 72  ? -14.65806 -16.02112 -21.27638 1.000 18.25505 ? 79  ASN   A CG  1 
ATOM   515  O  OD1 . ASN   A 1 72  ? -15.35207 -15.22208 -20.65417 1.000 18.38792 ? 79  ASN   A OD1 1 
ATOM   516  N  ND2 . ASN   A 1 72  ? -14.94797 -16.41028 -22.51260 1.000 21.51411 ? 79  ASN   A ND2 1 
ATOM   517  N  N   . LEU   A 1 73  ? -11.98718 -17.03589 -17.68629 1.000 15.65098 ? 80  LEU   A N   1 
ATOM   518  C  CA  . LEU   A 1 73  ? -11.06397 -17.86891 -16.92145 1.000 14.80087 ? 80  LEU   A CA  1 
ATOM   519  C  C   . LEU   A 1 73  ? -11.63745 -19.27840 -16.89746 1.000 15.56293 ? 80  LEU   A C   1 
ATOM   520  O  O   . LEU   A 1 73  ? -12.75859 -19.48769 -16.41966 1.000 16.45438 ? 80  LEU   A O   1 
ATOM   521  C  CB  . LEU   A 1 73  ? -10.89884 -17.34580 -15.49502 1.000 16.01939 ? 80  LEU   A CB  1 
ATOM   522  C  CG  . LEU   A 1 73  ? -10.56235 -15.86206 -15.36668 1.000 15.90041 ? 80  LEU   A CG  1 
ATOM   523  C  CD1 . LEU   A 1 73  ? -10.52149 -15.46344 -13.90036 1.000 18.04706 ? 80  LEU   A CD1 1 
ATOM   524  C  CD2 . LEU   A 1 73  ? -9.24586  -15.54701 -16.06551 1.000 17.51124 ? 80  LEU   A CD2 1 
ATOM   525  N  N   . ILE   A 1 74  ? -10.88692 -20.23304 -17.43381 1.000 16.42394 ? 81  ILE   A N   1 
ATOM   526  C  CA  . ILE   A 1 74  ? -11.40111 -21.58510 -17.64014 1.000 16.80829 ? 81  ILE   A CA  1 
ATOM   527  C  C   . ILE   A 1 74  ? -10.50668 -22.60816 -16.95373 1.000 18.68620 ? 81  ILE   A C   1 
ATOM   528  O  O   . ILE   A 1 74  ? -9.47397  -23.01192 -17.50974 1.000 17.61966 ? 81  ILE   A O   1 
ATOM   529  C  CB  . ILE   A 1 74  ? -11.57089 -21.90908 -19.13272 1.000 19.66896 ? 81  ILE   A CB  1 
ATOM   530  C  CG1 . ILE   A 1 74  ? -12.33402 -20.78704 -19.84737 1.000 19.50706 ? 81  ILE   A CG1 1 
ATOM   531  C  CG2 . ILE   A 1 74  ? -12.27713 -23.24289 -19.29433 1.000 19.52267 ? 81  ILE   A CG2 1 
ATOM   532  C  CD1 . ILE   A 1 74  ? -12.49080 -21.00688 -21.34795 1.000 21.97157 ? 81  ILE   A CD1 1 
ATOM   533  N  N   . PRO   A 1 75  ? -10.86458 -23.05691 -15.75726 1.000 17.21957 ? 82  PRO   A N   1 
ATOM   534  C  CA  . PRO   A 1 75  ? -10.11165 -24.13723 -15.12075 1.000 18.95074 ? 82  PRO   A CA  1 
ATOM   535  C  C   . PRO   A 1 75  ? -10.57170 -25.48652 -15.64858 1.000 20.77785 ? 82  PRO   A C   1 
ATOM   536  O  O   . PRO   A 1 75  ? -11.74403 -25.68943 -15.96704 1.000 22.54069 ? 82  PRO   A O   1 
ATOM   537  C  CB  . PRO   A 1 75  ? -10.48430 -23.99126 -13.63948 1.000 20.07233 ? 82  PRO   A CB  1 
ATOM   538  C  CG  . PRO   A 1 75  ? -11.84848 -23.32527 -13.64532 1.000 21.59120 ? 82  PRO   A CG  1 
ATOM   539  C  CD  . PRO   A 1 75  ? -12.05681 -22.66206 -14.98744 1.000 20.13408 ? 82  PRO   A CD  1 
ATOM   540  N  N   . ASN   A 1 76  ? -9.62133  -26.41670 -15.74965 1.000 20.70969 ? 83  ASN   A N   1 
ATOM   541  C  CA  . ASN   A 1 76  ? -9.91903  -27.79052 -16.16007 1.000 21.81579 ? 83  ASN   A CA  1 
ATOM   542  C  C   . ASN   A 1 76  ? -9.08832  -28.72516 -15.28563 1.000 23.41608 ? 83  ASN   A C   1 
ATOM   543  O  O   . ASN   A 1 76  ? -7.88373  -28.87624 -15.50361 1.000 24.67455 ? 83  ASN   A O   1 
ATOM   544  C  CB  . ASN   A 1 76  ? -9.63544  -28.01075 -17.64259 1.000 25.18971 ? 83  ASN   A CB  1 
ATOM   545  C  CG  . ASN   A 1 76  ? -10.14070 -29.35670 -18.13867 1.000 32.72891 ? 83  ASN   A CG  1 
ATOM   546  O  OD1 . ASN   A 1 76  ? -9.81388  -30.40239 -17.57695 1.000 29.60119 ? 83  ASN   A OD1 1 
ATOM   547  N  ND2 . ASN   A 1 76  ? -10.95821 -29.33361 -19.18564 1.000 38.05757 ? 83  ASN   A ND2 1 
ATOM   548  N  N   . LYS   A 1 77  ? -9.73959  -29.36500 -14.31163 1.000 25.55329 ? 84  LYS   A N   1 
ATOM   549  C  CA  . LYS   A 1 77  ? -9.01369  -30.22838 -13.38336 1.000 27.43161 ? 84  LYS   A CA  1 
ATOM   550  C  C   . LYS   A 1 77  ? -8.54355  -31.51970 -14.03882 1.000 29.88150 ? 84  LYS   A C   1 
ATOM   551  O  O   . LYS   A 1 77  ? -7.53935  -32.09571 -13.60586 1.000 30.99809 ? 84  LYS   A O   1 
ATOM   552  C  CB  . LYS   A 1 77  ? -9.86445  -30.53871 -12.15147 1.000 28.18615 ? 84  LYS   A CB  1 
ATOM   553  C  CG  . LYS   A 1 77  ? -9.99095  -29.37613 -11.18418 1.000 30.12758 ? 84  LYS   A CG  1 
ATOM   554  C  CD  . LYS   A 1 77  ? -10.96225 -29.70339 -10.05912 1.000 30.29125 ? 84  LYS   A CD  1 
ATOM   555  C  CE  . LYS   A 1 77  ? -11.24354 -28.48186 -9.20107  1.000 35.61807 ? 84  LYS   A CE  1 
ATOM   556  N  NZ  . LYS   A 1 77  ? -12.42228 -27.71986 -9.69893  1.000 51.85417 ? 84  LYS   A NZ  1 
ATOM   557  N  N   . GLN   A 1 78  ? -9.24846  -32.00097 -15.06684 1.000 32.58900 ? 85  GLN   A N   1 
ATOM   558  C  CA  . GLN   A 1 78  ? -8.82816  -33.23514 -15.72046 1.000 36.63849 ? 85  GLN   A CA  1 
ATOM   559  C  C   . GLN   A 1 78  ? -7.53138  -33.04228 -16.49547 1.000 31.94754 ? 85  GLN   A C   1 
ATOM   560  O  O   . GLN   A 1 78  ? -6.66335  -33.92240 -16.49822 1.000 35.41391 ? 85  GLN   A O   1 
ATOM   561  C  CB  . GLN   A 1 78  ? -9.93067  -33.80019 -16.62365 1.000 40.11815 ? 85  GLN   A CB  1 
ATOM   562  C  CG  . GLN   A 1 78  ? -11.17084 -34.35139 -15.90721 1.000 51.50423 ? 85  GLN   A CG  1 
ATOM   563  C  CD  . GLN   A 1 78  ? -11.86137 -33.34907 -14.99780 1.000 62.41401 ? 85  GLN   A CD  1 
ATOM   564  O  OE1 . GLN   A 1 78  ? -12.22769 -33.66827 -13.86611 1.000 60.43623 ? 85  GLN   A OE1 1 
ATOM   565  N  NE2 . GLN   A 1 78  ? -12.08057 -32.13981 -15.50806 1.000 56.17861 ? 85  GLN   A NE2 1 
ATOM   566  N  N   . ASP   A 1 79  ? -7.38138  -31.89306 -17.15299 1.000 29.03161 ? 86  ASP   A N   1 
ATOM   567  C  CA  . ASP   A 1 79  ? -6.16856  -31.56748 -17.88899 1.000 29.24171 ? 86  ASP   A CA  1 
ATOM   568  C  C   . ASP   A 1 79  ? -5.13736  -30.84795 -17.03049 1.000 27.47664 ? 86  ASP   A C   1 
ATOM   569  O  O   . ASP   A 1 79  ? -4.00607  -30.65070 -17.48799 1.000 26.59069 ? 86  ASP   A O   1 
ATOM   570  C  CB  . ASP   A 1 79  ? -6.51002  -30.68293 -19.09395 1.000 33.45026 ? 86  ASP   A CB  1 
ATOM   571  C  CG  . ASP   A 1 79  ? -7.46750  -31.35420 -20.06176 1.000 42.78137 ? 86  ASP   A CG  1 
ATOM   572  O  OD1 . ASP   A 1 79  ? -7.68251  -32.57859 -19.94172 1.000 45.22665 ? 86  ASP   A OD1 1 
ATOM   573  O  OD2 . ASP   A 1 79  ? -8.01237  -30.65135 -20.93995 1.000 42.23219 ? 86  ASP   A OD2 1 
ATOM   574  N  N   . ARG   A 1 80  ? -5.49918  -30.47512 -15.80229 1.000 24.81267 ? 87  ARG   A N   1 
ATOM   575  C  CA  . ARG   A 1 80  ? -4.67651  -29.62820 -14.93512 1.000 21.85290 ? 87  ARG   A CA  1 
ATOM   576  C  C   . ARG   A 1 80  ? -4.21629  -28.35692 -15.64506 1.000 21.60542 ? 87  ARG   A C   1 
ATOM   577  O  O   . ARG   A 1 80  ? -3.03084  -28.00495 -15.64317 1.000 23.64000 ? 87  ARG   A O   1 
ATOM   578  C  CB  . ARG   A 1 80  ? -3.50218  -30.37857 -14.30155 1.000 24.58719 ? 87  ARG   A CB  1 
ATOM   579  C  CG  . ARG   A 1 80  ? -3.07169  -29.74684 -12.98120 1.000 25.20029 ? 87  ARG   A CG  1 
ATOM   580  C  CD  . ARG   A 1 80  ? -1.65578  -30.10059 -12.56224 1.000 37.02882 ? 87  ARG   A CD  1 
ATOM   581  N  NE  . ARG   A 1 80  ? -1.40494  -31.53360 -12.54018 1.000 43.82234 ? 87  ARG   A NE  1 
ATOM   582  C  CZ  . ARG   A 1 80  ? -0.21334  -32.08361 -12.73179 1.000 48.48102 ? 87  ARG   A CZ  1 
ATOM   583  N  NH1 . ARG   A 1 80  ? 0.85808   -31.34510 -12.97603 1.000 39.28086 ? 87  ARG   A NH1 1 
ATOM   584  N  NH2 . ARG   A 1 80  ? -0.09116  -33.40578 -12.66844 1.000 49.60270 ? 87  ARG   A NH2 1 
ATOM   585  N  N   . THR   A 1 81  ? -5.17134  -27.65233 -16.25065 1.000 20.37122 ? 88  THR   A N   1 
ATOM   586  C  CA  . THR   A 1 81  ? -4.88282  -26.40981 -16.95162 1.000 19.45954 ? 88  THR   A CA  1 
ATOM   587  C  C   . THR   A 1 81  ? -5.79981  -25.29926 -16.47254 1.000 19.93744 ? 88  THR   A C   1 
ATOM   588  O  O   . THR   A 1 81  ? -6.96967  -25.53476 -16.15711 1.000 20.43078 ? 88  THR   A O   1 
ATOM   589  C  CB  . THR   A 1 81  ? -5.02629  -26.53867 -18.48024 1.000 18.61812 ? 88  THR   A CB  1 
ATOM   590  O  OG1 . THR   A 1 81  ? -6.37097  -26.92043 -18.80817 1.000 22.37890 ? 88  THR   A OG1 1 
ATOM   591  C  CG2 . THR   A 1 81  ? -4.04225  -27.55575 -19.04004 1.000 23.66544 ? 88  THR   A CG2 1 
ATOM   592  N  N   . LEU   A 1 82  ? -5.25751  -24.08761 -16.42112 1.000 16.44091 ? 89  LEU   A N   1 
ATOM   593  C  CA  . LEU   A 1 82  ? -6.04004  -22.87014 -16.25444 1.000 16.80874 ? 89  LEU   A CA  1 
ATOM   594  C  C   . LEU   A 1 82  ? -5.81551  -22.02154 -17.49516 1.000 18.31224 ? 89  LEU   A C   1 
ATOM   595  O  O   . LEU   A 1 82  ? -4.67226  -21.69875 -17.82802 1.000 18.19452 ? 89  LEU   A O   1 
ATOM   596  C  CB  . LEU   A 1 82  ? -5.61038  -22.09391 -15.00696 1.000 18.53041 ? 89  LEU   A CB  1 
ATOM   597  C  CG  . LEU   A 1 82  ? -6.31297  -20.74201 -14.81336 1.000 16.68275 ? 89  LEU   A CG  1 
ATOM   598  C  CD1 . LEU   A 1 82  ? -7.81040  -20.94937 -14.59263 1.000 18.98737 ? 89  LEU   A CD1 1 
ATOM   599  C  CD2 . LEU   A 1 82  ? -5.71567  -19.98493 -13.63568 1.000 18.81813 ? 89  LEU   A CD2 1 
ATOM   600  N  N   . THR   A 1 83  ? -6.89501  -21.67886 -18.18884 1.000 16.09485 ? 90  THR   A N   1 
ATOM   601  C  CA  . THR   A 1 83  ? -6.80889  -20.94185 -19.44167 1.000 17.24893 ? 90  THR   A CA  1 
ATOM   602  C  C   . THR   A 1 83  ? -7.39904  -19.55080 -19.25373 1.000 16.77971 ? 90  THR   A C   1 
ATOM   603  O  O   . THR   A 1 83  ? -8.49869  -19.40636 -18.70255 1.000 17.80730 ? 90  THR   A O   1 
ATOM   604  C  CB  . THR   A 1 83  ? -7.56421  -21.68351 -20.54441 1.000 17.97473 ? 90  THR   A CB  1 
ATOM   605  O  OG1 . THR   A 1 83  ? -6.96993  -22.97197 -20.75194 1.000 18.34696 ? 90  THR   A OG1 1 
ATOM   606  C  CG2 . THR   A 1 83  ? -7.49647  -20.89850 -21.83861 1.000 19.56177 ? 90  THR   A CG2 1 
ATOM   607  N  N   . ILE   A 1 84  ? -6.66809  -18.53009 -19.69115 1.000 16.55668 ? 91  ILE   A N   1 
ATOM   608  C  CA  . ILE   A 1 84  ? -7.12905  -17.14466 -19.67028 1.000 16.38956 ? 91  ILE   A CA  1 
ATOM   609  C  C   . ILE   A 1 84  ? -7.36876  -16.73602 -21.11568 1.000 19.37015 ? 91  ILE   A C   1 
ATOM   610  O  O   . ILE   A 1 84  ? -6.42136  -16.65876 -21.91176 1.000 17.84721 ? 91  ILE   A O   1 
ATOM   611  C  CB  . ILE   A 1 84  ? -6.13123  -16.19735 -18.98561 1.000 18.49398 ? 91  ILE   A CB  1 
ATOM   612  C  CG1 . ILE   A 1 84  ? -5.88948  -16.59187 -17.52112 1.000 21.77219 ? 91  ILE   A CG1 1 
ATOM   613  C  CG2 . ILE   A 1 84  ? -6.63406  -14.75434 -19.06510 1.000 17.87562 ? 91  ILE   A CG2 1 
ATOM   614  C  CD1 . ILE   A 1 84  ? -4.76770  -17.58697 -17.30390 1.000 27.68698 ? 91  ILE   A CD1 1 
ATOM   615  N  N   . VAL   A 1 85  ? -8.62430  -16.47201 -21.46420 1.000 15.84248 ? 92  VAL   A N   1 
ATOM   616  C  CA  . VAL   A 1 85  ? -9.02358  -16.15606 -22.83033 1.000 16.04940 ? 92  VAL   A CA  1 
ATOM   617  C  C   . VAL   A 1 85  ? -9.44133  -14.69702 -22.87741 1.000 17.66560 ? 92  VAL   A C   1 
ATOM   618  O  O   . VAL   A 1 85  ? -10.22875 -14.24730 -22.03573 1.000 18.64250 ? 92  VAL   A O   1 
ATOM   619  C  CB  . VAL   A 1 85  ? -10.19957 -17.03747 -23.28649 1.000 18.75222 ? 92  VAL   A CB  1 
ATOM   620  C  CG1 . VAL   A 1 85  ? -10.53349 -16.75424 -24.75144 1.000 23.07173 ? 92  VAL   A CG1 1 
ATOM   621  C  CG2 . VAL   A 1 85  ? -9.90785  -18.51133 -23.05763 1.000 21.54158 ? 92  VAL   A CG2 1 
ATOM   622  N  N   . ASP   A 1 86  ? -8.95807  -13.96409 -23.87736 1.000 17.55208 ? 93  ASP   A N   1 
ATOM   623  C  CA  . ASP   A 1 86  ? -9.45720  -12.61739 -24.10279 1.000 16.98217 ? 93  ASP   A CA  1 
ATOM   624  C  C   . ASP   A 1 86  ? -9.70794  -12.43660 -25.59246 1.000 18.07162 ? 93  ASP   A C   1 
ATOM   625  O  O   . ASP   A 1 86  ? -9.13874  -13.13939 -26.43350 1.000 17.55559 ? 93  ASP   A O   1 
ATOM   626  C  CB  . ASP   A 1 86  ? -8.52027  -11.51593 -23.55569 1.000 16.82715 ? 93  ASP   A CB  1 
ATOM   627  C  CG  . ASP   A 1 86  ? -7.19943  -11.42542 -24.30525 1.000 20.27728 ? 93  ASP   A CG  1 
ATOM   628  O  OD1 . ASP   A 1 86  ? -7.21084  -11.03888 -25.49357 1.000 18.73946 ? 93  ASP   A OD1 1 
ATOM   629  O  OD2 . ASP   A 1 86  ? -6.14617  -11.75106 -23.71212 1.000 20.63237 ? 93  ASP   A OD2 1 
ATOM   630  N  N   . THR   A 1 87  ? -10.58790 -11.49374 -25.90717 1.000 16.05095 ? 94  THR   A N   1 
ATOM   631  C  CA  . THR   A 1 87  ? -10.87526 -11.11787 -27.28723 1.000 14.98710 ? 94  THR   A CA  1 
ATOM   632  C  C   . THR   A 1 87  ? -10.19836 -9.80553  -27.66692 1.000 18.95205 ? 94  THR   A C   1 
ATOM   633  O  O   . THR   A 1 87  ? -10.75685 -8.98297  -28.39327 1.000 18.04186 ? 94  THR   A O   1 
ATOM   634  C  CB  . THR   A 1 87  ? -12.38025 -11.07434 -27.52148 1.000 16.64933 ? 94  THR   A CB  1 
ATOM   635  O  OG1 . THR   A 1 87  ? -13.00045 -10.25399 -26.52528 1.000 17.91828 ? 94  THR   A OG1 1 
ATOM   636  C  CG2 . THR   A 1 87  ? -12.95640 -12.48445 -27.43846 1.000 18.43898 ? 94  THR   A CG2 1 
ATOM   637  N  N   . GLY   A 1 88  ? -8.98039  -9.58361  -27.17645 1.000 17.10770 ? 95  GLY   A N   1 
ATOM   638  C  CA  . GLY   A 1 88  ? -8.23382  -8.38824  -27.50207 1.000 18.20942 ? 95  GLY   A CA  1 
ATOM   639  C  C   . GLY   A 1 88  ? -7.66069  -8.41004  -28.90650 1.000 17.27909 ? 95  GLY   A C   1 
ATOM   640  O  O   . GLY   A 1 88  ? -8.08573  -9.16946  -29.77919 1.000 17.09411 ? 95  GLY   A O   1 
ATOM   641  N  N   . ILE   A 1 89  ? -6.66002  -7.55116  -29.11215 1.000 17.07869 ? 96  ILE   A N   1 
ATOM   642  C  CA  . ILE   A 1 89  ? -6.09845  -7.33960  -30.44441 1.000 18.03213 ? 96  ILE   A CA  1 
ATOM   643  C  C   . ILE   A 1 89  ? -5.34748  -8.55805  -30.97290 1.000 17.37395 ? 96  ILE   A C   1 
ATOM   644  O  O   . ILE   A 1 89  ? -5.18932  -8.70391  -32.19193 1.000 18.70862 ? 96  ILE   A O   1 
ATOM   645  C  CB  . ILE   A 1 89  ? -5.23398  -6.06166  -30.44082 1.000 17.14999 ? 96  ILE   A CB  1 
ATOM   646  C  CG1 . ILE   A 1 89  ? -4.92375  -5.60443  -31.87110 1.000 19.92484 ? 96  ILE   A CG1 1 
ATOM   647  C  CG2 . ILE   A 1 89  ? -3.95464  -6.27346  -29.62337 1.000 17.62067 ? 96  ILE   A CG2 1 
ATOM   648  C  CD1 . ILE   A 1 89  ? -4.49921  -4.15317  -31.94975 1.000 24.18699 ? 96  ILE   A CD1 1 
ATOM   649  N  N   . GLY   A 1 90  ? -4.88287  -9.44485  -30.09343 1.000 17.37108 ? 97  GLY   A N   1 
ATOM   650  C  CA  . GLY   A 1 90  ? -4.12810  -10.59728 -30.53618 1.000 16.85840 ? 97  GLY   A CA  1 
ATOM   651  C  C   . GLY   A 1 90  ? -2.70854  -10.22909 -30.91919 1.000 16.51780 ? 97  GLY   A C   1 
ATOM   652  O  O   . GLY   A 1 90  ? -2.25790  -9.08976  -30.78934 1.000 20.06004 ? 97  GLY   A O   1 
ATOM   653  N  N   . MET   A 1 91  ? -1.98893  -11.23194 -31.40112 1.000 16.86677 ? 98  MET   A N   1 
ATOM   654  C  CA  . MET   A 1 91  ? -0.59055  -11.06766 -31.77054 1.000 17.39141 ? 98  MET   A CA  1 
ATOM   655  C  C   . MET   A 1 91  ? -0.33634  -11.70333 -33.12198 1.000 18.34541 ? 98  MET   A C   1 
ATOM   656  O  O   . MET   A 1 91  ? -0.85220  -12.78505 -33.41389 1.000 20.06982 ? 98  MET   A O   1 
ATOM   657  C  CB  . MET   A 1 91  ? 0.33995   -11.73043 -30.74099 1.000 19.75418 ? 98  MET   A CB  1 
ATOM   658  C  CG  . MET   A 1 91  ? 0.49683   -10.94160 -29.44172 1.000 19.79837 ? 98  MET   A CG  1 
ATOM   659  S  SD  . MET   A 1 91  ? 1.38734   -11.85115 -28.15472 1.000 20.68779 ? 98  MET   A SD  1 
ATOM   660  C  CE  . MET   A 1 91  ? 0.21162   -13.16662 -27.81735 1.000 23.09940 ? 98  MET   A CE  1 
ATOM   661  N  N   . THR   A 1 92  ? 0.47276   -11.03125 -33.93894 1.000 18.38236 ? 99  THR   A N   1 
ATOM   662  C  CA  . THR   A 1 92  ? 0.95615   -11.62309 -35.17349 1.000 19.72243 ? 99  THR   A CA  1 
ATOM   663  C  C   . THR   A 1 92  ? 2.06048   -12.62392 -34.85629 1.000 20.47512 ? 99  THR   A C   1 
ATOM   664  O  O   . THR   A 1 92  ? 2.57133   -12.68799 -33.73598 1.000 20.41852 ? 99  THR   A O   1 
ATOM   665  C  CB  . THR   A 1 92  ? 1.52011   -10.54408 -36.09472 1.000 23.05609 ? 99  THR   A CB  1 
ATOM   666  O  OG1 . THR   A 1 92  ? 2.67587   -9.95851  -35.48000 1.000 23.45353 ? 99  THR   A OG1 1 
ATOM   667  C  CG2 . THR   A 1 92  ? 0.47999   -9.46040  -36.35365 1.000 24.06145 ? 99  THR   A CG2 1 
ATOM   668  N  N   . LYS   A 1 93  ? 2.42931   -13.41647 -35.86499 1.000 19.73841 ? 100 LYS   A N   1 
ATOM   669  C  CA  . LYS   A 1 93  ? 3.55338   -14.33261 -35.69874 1.000 18.40492 ? 100 LYS   A CA  1 
ATOM   670  C  C   . LYS   A 1 93  ? 4.80771   -13.57888 -35.28809 1.000 20.07595 ? 100 LYS   A C   1 
ATOM   671  O  O   . LYS   A 1 93  ? 5.54527   -14.02412 -34.40000 1.000 19.16573 ? 100 LYS   A O   1 
ATOM   672  C  CB  . LYS   A 1 93  ? 3.80602   -15.11719 -36.98692 1.000 21.82472 ? 100 LYS   A CB  1 
ATOM   673  C  CG  . LYS   A 1 93  ? 4.85367   -16.21268 -36.81873 1.000 24.15555 ? 100 LYS   A CG  1 
ATOM   674  C  CD  . LYS   A 1 93  ? 5.18179   -16.88637 -38.15070 1.000 25.25158 ? 100 LYS   A CD  1 
ATOM   675  C  CE  . LYS   A 1 93  ? 6.11276   -18.06863 -37.93645 1.000 27.51450 ? 100 LYS   A CE  1 
ATOM   676  N  NZ  . LYS   A 1 93  ? 6.79369   -18.47280 -39.20002 1.000 29.84317 ? 100 LYS   A NZ  1 
ATOM   677  N  N   . ALA   A 1 94  ? 5.05594   -12.42448 -35.91321 1.000 21.04034 ? 101 ALA   A N   1 
ATOM   678  C  CA  . ALA   A 1 94  ? 6.22277   -11.62407 -35.55871 1.000 21.55041 ? 101 ALA   A CA  1 
ATOM   679  C  C   . ALA   A 1 94  ? 6.16658   -11.17488 -34.10191 1.000 22.59046 ? 101 ALA   A C   1 
ATOM   680  O  O   . ALA   A 1 94  ? 7.18689   -11.20739 -33.40321 1.000 23.26265 ? 101 ALA   A O   1 
ATOM   681  C  CB  . ALA   A 1 94  ? 6.35549   -10.42861 -36.50113 1.000 23.54757 ? 101 ALA   A CB  1 
ATOM   682  N  N   . ASP   A 1 95  ? 4.98244   -10.76045 -33.62589 1.000 20.75141 ? 102 ASP   A N   1 
ATOM   683  C  CA  . ASP   A 1 95  ? 4.82183   -10.42261 -32.20908 1.000 21.22555 ? 102 ASP   A CA  1 
ATOM   684  C  C   . ASP   A 1 95  ? 5.17662   -11.59345 -31.31119 1.000 19.66563 ? 102 ASP   A C   1 
ATOM   685  O  O   . ASP   A 1 95  ? 5.88436   -11.43084 -30.30752 1.000 21.50922 ? 102 ASP   A O   1 
ATOM   686  C  CB  . ASP   A 1 95  ? 3.39138   -9.96236  -31.88608 1.000 22.70336 ? 102 ASP   A CB  1 
ATOM   687  C  CG  . ASP   A 1 95  ? 2.98954   -8.68700  -32.59258 1.000 28.43611 ? 102 ASP   A CG  1 
ATOM   688  O  OD1 . ASP   A 1 95  ? 3.81813   -7.75624  -32.67283 1.000 29.61668 ? 102 ASP   A OD1 1 
ATOM   689  O  OD2 . ASP   A 1 95  ? 1.80998   -8.57952  -32.99571 1.000 30.28588 ? 102 ASP   A OD2 1 
ATOM   690  N  N   . LEU   A 1 96  ? 4.65605   -12.78554 -31.62347 1.000 18.54358 ? 103 LEU   A N   1 
ATOM   691  C  CA  . LEU   A 1 96  ? 4.92732   -13.94614 -30.78569 1.000 20.82057 ? 103 LEU   A CA  1 
ATOM   692  C  C   . LEU   A 1 96  ? 6.41913   -14.17397 -30.65002 1.000 20.33615 ? 103 LEU   A C   1 
ATOM   693  O  O   . LEU   A 1 96  ? 6.93208   -14.35089 -29.54167 1.000 20.16242 ? 103 LEU   A O   1 
ATOM   694  C  CB  . LEU   A 1 96  ? 4.28854   -15.20202 -31.36712 1.000 22.18878 ? 103 LEU   A CB  1 
ATOM   695  C  CG  . LEU   A 1 96  ? 2.79579   -15.38106 -31.18503 1.000 20.11421 ? 103 LEU   A CG  1 
ATOM   696  C  CD1 . LEU   A 1 96  ? 2.38221   -16.63786 -31.92558 1.000 20.42546 ? 103 LEU   A CD1 1 
ATOM   697  C  CD2 . LEU   A 1 96  ? 2.44219   -15.45551 -29.70010 1.000 20.54152 ? 103 LEU   A CD2 1 
ATOM   698  N  N   . ILE   A 1 97  ? 7.12992   -14.16048 -31.78042 1.000 19.41921 ? 104 ILE   A N   1 
ATOM   699  C  CA  . ILE   A 1 97  ? 8.56478   -14.42404 -31.76947 1.000 20.20516 ? 104 ILE   A CA  1 
ATOM   700  C  C   . ILE   A 1 97  ? 9.30434   -13.33544 -31.00840 1.000 20.05473 ? 104 ILE   A C   1 
ATOM   701  O  O   . ILE   A 1 97  ? 10.26227  -13.61542 -30.27495 1.000 21.36329 ? 104 ILE   A O   1 
ATOM   702  C  CB  . ILE   A 1 97  ? 9.08503   -14.59124 -33.20823 1.000 21.49313 ? 104 ILE   A CB  1 
ATOM   703  C  CG1 . ILE   A 1 97  ? 8.47571   -15.84384 -33.84011 1.000 22.30926 ? 104 ILE   A CG1 1 
ATOM   704  C  CG2 . ILE   A 1 97  ? 10.61179  -14.64609 -33.23376 1.000 21.73463 ? 104 ILE   A CG2 1 
ATOM   705  C  CD1 . ILE   A 1 97  ? 8.62117   -15.89353 -35.35225 1.000 24.30314 ? 104 ILE   A CD1 1 
ATOM   706  N  N   . ASN   A 1 98  ? 8.85622   -12.08765 -31.14540 1.000 20.40926 ? 105 ASN   A N   1 
ATOM   707  C  CA  . ASN   A 1 98  ? 9.45903   -10.93974 -30.47071 1.000 22.96430 ? 105 ASN   A CA  1 
ATOM   708  C  C   . ASN   A 1 98  ? 8.91220   -10.79778 -29.04608 1.000 18.80282 ? 105 ASN   A C   1 
ATOM   709  O  O   . ASN   A 1 98  ? 8.36415   -9.76853  -28.64847 1.000 21.37749 ? 105 ASN   A O   1 
ATOM   710  C  CB  . ASN   A 1 98  ? 9.23114   -9.67442  -31.28811 1.000 22.81613 ? 105 ASN   A CB  1 
ATOM   711  C  CG  . ASN   A 1 98  ? 10.22638  -8.58087  -30.96416 1.000 38.44722 ? 105 ASN   A CG  1 
ATOM   712  O  OD1 . ASN   A 1 98  ? 11.21931  -8.80886  -30.26856 1.000 37.07767 ? 105 ASN   A OD1 1 
ATOM   713  N  ND2 . ASN   A 1 98  ? 9.96530   -7.38078  -31.46946 1.000 42.57674 ? 105 ASN   A ND2 1 
ATOM   714  N  N   . ASN   A 1 99  ? 9.06890   -11.88265 -28.28400 1.000 20.24191 ? 106 ASN   A N   1 
ATOM   715  C  CA  . ASN   A 1 99  ? 8.75387   -11.91997 -26.85349 1.000 19.11787 ? 106 ASN   A CA  1 
ATOM   716  C  C   . ASN   A 1 99  ? 7.30430   -11.55301 -26.56390 1.000 20.33994 ? 106 ASN   A C   1 
ATOM   717  O  O   . ASN   A 1 99  ? 7.00845   -10.78365 -25.64731 1.000 19.63629 ? 106 ASN   A O   1 
ATOM   718  C  CB  . ASN   A 1 99  ? 9.72065   -11.05994 -26.04343 1.000 18.91695 ? 106 ASN   A CB  1 
ATOM   719  C  CG  . ASN   A 1 99  ? 11.15157  -11.50445 -26.21249 1.000 19.34109 ? 106 ASN   A CG  1 
ATOM   720  O  OD1 . ASN   A 1 99  ? 11.47309  -12.67892 -26.02600 1.000 21.52024 ? 106 ASN   A OD1 1 
ATOM   721  N  ND2 . ASN   A 1 99  ? 12.01722  -10.57571 -26.58643 1.000 23.68252 ? 106 ASN   A ND2 1 
ATOM   722  N  N   . LEU   A 1 100 ? 6.39531   -12.12102 -27.35541 1.000 18.50560 ? 107 LEU   A N   1 
ATOM   723  C  CA  . LEU   A 1 100 ? 4.95775   -11.94649 -27.14554 1.000 19.80821 ? 107 LEU   A CA  1 
ATOM   724  C  C   . LEU   A 1 100 ? 4.56759   -10.46978 -27.06686 1.000 19.18718 ? 107 LEU   A C   1 
ATOM   725  O  O   . LEU   A 1 100 ? 3.78459   -10.04492 -26.21097 1.000 20.34283 ? 107 LEU   A O   1 
ATOM   726  C  CB  . LEU   A 1 100 ? 4.45885   -12.75771 -25.94841 1.000 20.78759 ? 107 LEU   A CB  1 
ATOM   727  C  CG  . LEU   A 1 100 ? 4.88817   -14.22902 -26.05221 1.000 21.49283 ? 107 LEU   A CG  1 
ATOM   728  C  CD1 . LEU   A 1 100 ? 6.07491   -14.54516 -25.14788 1.000 21.34271 ? 107 LEU   A CD1 1 
ATOM   729  C  CD2 . LEU   A 1 100 ? 3.73544   -15.17557 -25.78269 1.000 28.84631 ? 107 LEU   A CD2 1 
ATOM   730  N  N   . GLY   A 1 101 ? 5.12597   -9.67537  -27.97712 1.000 18.83364 ? 108 GLY   A N   1 
ATOM   731  C  CA  . GLY   A 1 101 ? 4.75378   -8.27907  -28.09977 1.000 20.38232 ? 108 GLY   A CA  1 
ATOM   732  C  C   . GLY   A 1 101 ? 5.28488   -7.36279  -27.02213 1.000 21.15008 ? 108 GLY   A C   1 
ATOM   733  O  O   . GLY   A 1 101 ? 4.78297   -6.24433  -26.87354 1.000 25.85570 ? 108 GLY   A O   1 
ATOM   734  N  N   . THR   A 1 102 ? 6.29374   -7.79650  -26.27170 1.000 21.42953 ? 109 THR   A N   1 
ATOM   735  C  CA  . THR   A 1 102 ? 6.85834   -7.02770  -25.17452 1.000 22.52486 ? 109 THR   A CA  1 
ATOM   736  C  C   . THR   A 1 102 ? 8.25406   -6.54654  -25.53985 1.000 21.18986 ? 109 THR   A C   1 
ATOM   737  O  O   . THR   A 1 102 ? 8.90166   -7.07336  -26.45011 1.000 22.64457 ? 109 THR   A O   1 
ATOM   738  C  CB  . THR   A 1 102 ? 6.94387   -7.87363  -23.89521 1.000 21.97036 ? 109 THR   A CB  1 
ATOM   739  O  OG1 . THR   A 1 102 ? 8.00180   -8.83412  -24.02140 1.000 23.59281 ? 109 THR   A OG1 1 
ATOM   740  C  CG2 . THR   A 1 102 ? 5.63077   -8.59985  -23.63245 1.000 28.36519 ? 109 THR   A CG2 1 
ATOM   741  N  N   . ILE   A 1 103 ? 8.71137   -5.52960  -24.81489 1.000 19.31838 ? 110 ILE   A N   1 
ATOM   742  C  CA  . ILE   A 1 103 ? 10.10919  -5.11690  -24.88257 1.000 20.78666 ? 110 ILE   A CA  1 
ATOM   743  C  C   . ILE   A 1 103 ? 10.87168  -5.82476  -23.76967 1.000 19.92661 ? 110 ILE   A C   1 
ATOM   744  O  O   . ILE   A 1 103 ? 11.43750  -5.19199  -22.86815 1.000 21.48095 ? 110 ILE   A O   1 
ATOM   745  C  CB  . ILE   A 1 103 ? 10.27879  -3.58498  -24.88368 1.000 33.27013 ? 110 ILE   A CB  1 
ATOM   746  C  CG1 . ILE   A 1 103 ? 9.54880   -2.93397  -23.71133 1.000 29.72810 ? 110 ILE   A CG1 1 
ATOM   747  C  CG2 . ILE   A 1 103 ? 9.77318   -2.99972  -26.19665 1.000 25.60044 ? 110 ILE   A CG2 1 
ATOM   748  C  CD1 . ILE   A 1 103 ? 9.97955   -1.50250  -23.46965 1.000 34.55111 ? 110 ILE   A CD1 1 
ATOM   749  N  N   . ALA   A 1 104 ? 10.91209  -7.15697  -23.85627 1.000 20.37565 ? 111 ALA   A N   1 
ATOM   750  C  CA  . ALA   A 1 104 ? 11.33508  -7.96998  -22.72452 1.000 21.13294 ? 111 ALA   A CA  1 
ATOM   751  C  C   . ALA   A 1 104 ? 12.80905  -7.79146  -22.38844 1.000 22.02514 ? 111 ALA   A C   1 
ATOM   752  O  O   . ALA   A 1 104 ? 13.18084  -7.91520  -21.21802 1.000 23.50692 ? 111 ALA   A O   1 
ATOM   753  C  CB  . ALA   A 1 104 ? 11.00629  -9.44204  -22.97160 1.000 22.63297 ? 111 ALA   A CB  1 
ATOM   754  N  N   . LYS   A 1 105 ? 13.66310  -7.50091  -23.37496 1.000 21.69315 ? 112 LYS   A N   1 
ATOM   755  C  CA  . LYS   A 1 105 ? 15.08267  -7.33714  -23.06894 1.000 25.93960 ? 112 LYS   A CA  1 
ATOM   756  C  C   . LYS   A 1 105 ? 15.30086  -6.15079  -22.13496 1.000 27.00605 ? 112 LYS   A C   1 
ATOM   757  O  O   . LYS   A 1 105 ? 15.90583  -6.28966  -21.06507 1.000 28.75097 ? 112 LYS   A O   1 
ATOM   758  C  CB  . LYS   A 1 105 ? 15.89475  -7.18510  -24.36058 1.000 24.59483 ? 112 LYS   A CB  1 
ATOM   759  C  CG  . LYS   A 1 105 ? 17.24147  -6.49535  -24.20557 1.000 43.94934 ? 112 LYS   A CG  1 
ATOM   760  C  CD  . LYS   A 1 105 ? 18.27174  -7.07163  -25.18424 1.000 34.86223 ? 112 LYS   A CD  1 
ATOM   761  C  CE  . LYS   A 1 105 ? 19.69513  -6.74287  -24.75812 1.000 40.26818 ? 112 LYS   A CE  1 
ATOM   762  N  NZ  . LYS   A 1 105 ? 20.70209  -7.23411  -25.74581 1.000 50.62713 ? 112 LYS   A NZ  1 
ATOM   763  N  N   . SER   A 1 106 ? 14.79172  -4.97278  -22.51057 1.000 27.41713 ? 113 SER   A N   1 
ATOM   764  C  CA  . SER   A 1 106 ? 14.97548  -3.80192  -21.65881 1.000 27.74091 ? 113 SER   A CA  1 
ATOM   765  C  C   . SER   A 1 106 ? 14.13894  -3.89691  -20.38957 1.000 26.46161 ? 113 SER   A C   1 
ATOM   766  O  O   . SER   A 1 106 ? 14.56992  -3.41913  -19.33435 1.000 29.23269 ? 113 SER   A O   1 
ATOM   767  C  CB  . SER   A 1 106 ? 14.65552  -2.51387  -22.42177 1.000 30.86875 ? 113 SER   A CB  1 
ATOM   768  O  OG  . SER   A 1 106 ? 13.31549  -2.50495  -22.88357 1.000 32.81752 ? 113 SER   A OG  1 
ATOM   769  N  N   . GLY   A 1 107 ? 12.95511  -4.51037  -20.46900 1.000 25.98244 ? 114 GLY   A N   1 
ATOM   770  C  CA  . GLY   A 1 107 ? 12.14665  -4.69139  -19.27194 1.000 23.01602 ? 114 GLY   A CA  1 
ATOM   771  C  C   . GLY   A 1 107 ? 12.81730  -5.58401  -18.24719 1.000 27.76519 ? 114 GLY   A C   1 
ATOM   772  O  O   . GLY   A 1 107 ? 12.79306  -5.29705  -17.04582 1.000 27.19842 ? 114 GLY   A O   1 
ATOM   773  N  N   . THR   A 1 108 ? 13.43398  -6.67654  -18.70620 1.000 24.39717 ? 115 THR   A N   1 
ATOM   774  C  CA  . THR   A 1 108 ? 14.15816  -7.55645  -17.79331 1.000 29.40379 ? 115 THR   A CA  1 
ATOM   775  C  C   . THR   A 1 108 ? 15.32129  -6.83085  -17.12972 1.000 30.17322 ? 115 THR   A C   1 
ATOM   776  O  O   . THR   A 1 108 ? 15.53856  -6.97268  -15.92110 1.000 29.85473 ? 115 THR   A O   1 
ATOM   777  C  CB  . THR   A 1 108 ? 14.65660  -8.78923  -18.54554 1.000 26.23156 ? 115 THR   A CB  1 
ATOM   778  O  OG1 . THR   A 1 108 ? 13.53045  -9.54192  -19.00772 1.000 23.26100 ? 115 THR   A OG1 1 
ATOM   779  C  CG2 . THR   A 1 108 ? 15.50716  -9.66247  -17.63913 1.000 28.29865 ? 115 THR   A CG2 1 
ATOM   780  N  N   . LYS   A 1 109 ? 16.08581  -6.05671  -17.90699 1.000 28.47244 ? 116 LYS   A N   1 
ATOM   781  C  CA  . LYS   A 1 109 ? 17.18576  -5.27867  -17.34518 1.000 32.00845 ? 116 LYS   A CA  1 
ATOM   782  C  C   . LYS   A 1 109 ? 16.69886  -4.38054  -16.21379 1.000 33.90723 ? 116 LYS   A C   1 
ATOM   783  O  O   . LYS   A 1 109 ? 17.29386  -4.34457  -15.13027 1.000 36.93703 ? 116 LYS   A O   1 
ATOM   784  C  CB  . LYS   A 1 109 ? 17.84016  -4.44747  -18.44987 1.000 31.91948 ? 116 LYS   A CB  1 
ATOM   785  C  CG  . LYS   A 1 109 ? 18.88711  -3.45336  -17.96430 1.000 44.63918 ? 116 LYS   A CG  1 
ATOM   786  C  CD  . LYS   A 1 109 ? 19.57142  -2.76761  -19.13778 1.000 41.47518 ? 116 LYS   A CD  1 
ATOM   787  C  CE  . LYS   A 1 109 ? 20.89685  -2.14617  -18.72713 1.000 53.97576 ? 116 LYS   A CE  1 
ATOM   788  N  NZ  . LYS   A 1 109 ? 21.61889  -2.98585  -17.73344 1.000 64.33762 ? 116 LYS   A NZ  1 
ATOM   789  N  N   . ALA   A 1 110 ? 15.60632  -3.65224  -16.44612 1.000 31.59909 ? 117 ALA   A N   1 
ATOM   790  C  CA  . ALA   A 1 110 ? 15.08649  -2.76311  -15.41239 1.000 37.26855 ? 117 ALA   A CA  1 
ATOM   791  C  C   . ALA   A 1 110 ? 14.57948  -3.54775  -14.20774 1.000 34.47666 ? 117 ALA   A C   1 
ATOM   792  O  O   . ALA   A 1 110 ? 14.79090  -3.13930  -13.05963 1.000 35.96229 ? 117 ALA   A O   1 
ATOM   793  C  CB  . ALA   A 1 110 ? 13.97797  -1.88894  -15.99280 1.000 34.91142 ? 117 ALA   A CB  1 
ATOM   794  N  N   . PHE   A 1 111 ? 13.90897  -4.67525  -14.45250 1.000 31.06960 ? 118 PHE   A N   1 
ATOM   795  C  CA  . PHE   A 1 111 ? 13.35243  -5.47777  -13.36721 1.000 27.70327 ? 118 PHE   A CA  1 
ATOM   796  C  C   . PHE   A 1 111 ? 14.45028  -6.02041  -12.45949 1.000 33.55375 ? 118 PHE   A C   1 
ATOM   797  O  O   . PHE   A 1 111 ? 14.37854  -5.89058  -11.23232 1.000 34.22450 ? 118 PHE   A O   1 
ATOM   798  C  CB  . PHE   A 1 111 ? 12.52233  -6.60937  -13.97490 1.000 25.89703 ? 118 PHE   A CB  1 
ATOM   799  C  CG  . PHE   A 1 111 ? 11.84038  -7.49053  -12.97031 1.000 26.69860 ? 118 PHE   A CG  1 
ATOM   800  C  CD1 . PHE   A 1 111 ? 11.24058  -6.95857  -11.83897 1.000 25.57414 ? 118 PHE   A CD1 1 
ATOM   801  C  CD2 . PHE   A 1 111 ? 11.74706  -8.85521  -13.19060 1.000 26.87216 ? 118 PHE   A CD2 1 
ATOM   802  C  CE1 . PHE   A 1 111 ? 10.59663  -7.77762  -10.93044 1.000 26.56237 ? 118 PHE   A CE1 1 
ATOM   803  C  CE2 . PHE   A 1 111 ? 11.09743  -9.67833  -12.29008 1.000 27.92718 ? 118 PHE   A CE2 1 
ATOM   804  C  CZ  . PHE   A 1 111 ? 10.51733  -9.13674  -11.15685 1.000 25.20559 ? 118 PHE   A CZ  1 
ATOM   805  N  N   . MET   A 1 112 ? 15.48759  -6.62226  -13.04473 1.000 34.79168 ? 119 MET   A N   1 
ATOM   806  C  CA  . MET   A 1 112 ? 16.52795  -7.23039  -12.22129 1.000 42.65118 ? 119 MET   A CA  1 
ATOM   807  C  C   . MET   A 1 112 ? 17.32100  -6.19133  -11.43764 1.000 49.71763 ? 119 MET   A C   1 
ATOM   808  O  O   . MET   A 1 112 ? 17.76477  -6.47202  -10.31807 1.000 44.53715 ? 119 MET   A O   1 
ATOM   809  C  CB  . MET   A 1 112 ? 17.43517  -8.12083  -13.06797 1.000 47.69931 ? 119 MET   A CB  1 
ATOM   810  C  CG  . MET   A 1 112 ? 16.90370  -9.54316  -13.20914 1.000 32.02589 ? 119 MET   A CG  1 
ATOM   811  S  SD  . MET   A 1 112 ? 17.98784  -10.52772 -14.25585 1.000 67.97258 ? 119 MET   A SD  1 
ATOM   812  C  CE  . MET   A 1 112 ? 16.87459  -11.82252 -14.77647 1.000 36.06436 ? 119 MET   A CE  1 
ATOM   813  N  N   . GLU   A 1 113 ? 17.50546  -4.99231  -11.99589 1.000 40.59364 ? 120 GLU   A N   1 
ATOM   814  C  CA  . GLU   A 1 113 ? 18.11208  -3.91733  -11.21834 1.000 50.81542 ? 120 GLU   A CA  1 
ATOM   815  C  C   . GLU   A 1 113 ? 17.23302  -3.53961  -10.03495 1.000 47.62276 ? 120 GLU   A C   1 
ATOM   816  O  O   . GLU   A 1 113 ? 17.73720  -3.26012  -8.94076  1.000 46.61478 ? 120 GLU   A O   1 
ATOM   817  C  CB  . GLU   A 1 113 ? 18.37077  -2.69746  -12.10106 1.000 50.34583 ? 120 GLU   A CB  1 
ATOM   818  C  CG  . GLU   A 1 113 ? 19.69183  -2.73172  -12.84710 1.000 61.64855 ? 120 GLU   A CG  1 
ATOM   819  C  CD  . GLU   A 1 113 ? 19.73909  -1.73247  -13.98763 1.000 74.67944 ? 120 GLU   A CD  1 
ATOM   820  O  OE1 . GLU   A 1 113 ? 18.75018  -0.99207  -14.17432 1.000 66.85865 ? 120 GLU   A OE1 1 
ATOM   821  O  OE2 . GLU   A 1 113 ? 20.77042  -1.67703  -14.69069 1.000 77.82326 ? 120 GLU   A OE2 1 
ATOM   822  N  N   . ALA   A 1 114 ? 15.91335  -3.53305  -10.23321 1.000 41.21917 ? 121 ALA   A N   1 
ATOM   823  C  CA  . ALA   A 1 114 ? 15.00482  -3.20066  -9.14125  1.000 38.80440 ? 121 ALA   A CA  1 
ATOM   824  C  C   . ALA   A 1 114 ? 15.01959  -4.27237  -8.05836  1.000 39.73129 ? 121 ALA   A C   1 
ATOM   825  O  O   . ALA   A 1 114 ? 14.89332  -3.95824  -6.86946  1.000 46.24566 ? 121 ALA   A O   1 
ATOM   826  C  CB  . ALA   A 1 114 ? 13.59151  -2.98668  -9.67909  1.000 41.80806 ? 121 ALA   A CB  1 
ATOM   827  N  N   . LEU   A 1 115 ? 15.17907  -5.54067  -8.44718  1.000 41.38330 ? 122 LEU   A N   1 
ATOM   828  C  CA  . LEU   A 1 115 ? 15.16305  -6.62744  -7.47175  1.000 38.16090 ? 122 LEU   A CA  1 
ATOM   829  C  C   . LEU   A 1 115 ? 16.33677  -6.52421  -6.50963  1.000 52.37822 ? 122 LEU   A C   1 
ATOM   830  O  O   . LEU   A 1 115 ? 16.17746  -6.69347  -5.29584  1.000 52.57429 ? 122 LEU   A O   1 
ATOM   831  C  CB  . LEU   A 1 115 ? 15.17490  -7.97717  -8.18420  1.000 42.11812 ? 122 LEU   A CB  1 
ATOM   832  C  CG  . LEU   A 1 115 ? 13.86828  -8.35003  -8.87119  1.000 36.52767 ? 122 LEU   A CG  1 
ATOM   833  C  CD1 . LEU   A 1 115 ? 14.05109  -9.59592  -9.71787  1.000 41.35989 ? 122 LEU   A CD1 1 
ATOM   834  C  CD2 . LEU   A 1 115 ? 12.78457  -8.55383  -7.82134  1.000 36.00988 ? 122 LEU   A CD2 1 
ATOM   835  N  N   . GLN   A 1 116 ? 17.53086  -6.26002  -7.03570  1.000 52.23169 ? 123 GLN   A N   1 
ATOM   836  C  CA  . GLN   A 1 116 ? 18.67734  -6.05414  -6.16267  1.000 60.06125 ? 123 GLN   A CA  1 
ATOM   837  C  C   . GLN   A 1 116 ? 18.63987  -4.70116  -5.46004  1.000 62.16009 ? 123 GLN   A C   1 
ATOM   838  O  O   . GLN   A 1 116 ? 19.51100  -4.42934  -4.62705  1.000 65.37427 ? 123 GLN   A O   1 
ATOM   839  C  CB  . GLN   A 1 116 ? 19.98110  -6.23512  -6.94590  1.000 62.70247 ? 123 GLN   A CB  1 
ATOM   840  C  CG  . GLN   A 1 116 ? 20.33413  -7.68730  -7.26389  1.000 66.60598 ? 123 GLN   A CG  1 
ATOM   841  C  CD  . GLN   A 1 116 ? 21.82342  -7.96627  -7.13324  1.000 89.57878 ? 123 GLN   A CD  1 
ATOM   842  O  OE1 . GLN   A 1 116 ? 22.61935  -7.05600  -6.89692  1.000 92.48220 ? 123 GLN   A OE1 1 
ATOM   843  N  NE2 . GLN   A 1 116 ? 22.20605  -9.22829  -7.28981  1.000 86.44832 ? 123 GLN   A NE2 1 
ATOM   844  N  N   . ALA   A 1 117 ? 17.64575  -3.86269  -5.75933  1.000 61.57749 ? 124 ALA   A N   1 
ATOM   845  C  CA  . ALA   A 1 117 ? 17.49253  -2.54864  -5.14916  1.000 55.98133 ? 124 ALA   A CA  1 
ATOM   846  C  C   . ALA   A 1 117 ? 16.23277  -2.45036  -4.29320  1.000 70.40916 ? 124 ALA   A C   1 
ATOM   847  O  O   . ALA   A 1 117 ? 15.67760  -1.35700  -4.13135  1.000 65.58253 ? 124 ALA   A O   1 
ATOM   848  C  CB  . ALA   A 1 117 ? 17.51689  -1.45754  -6.21969  1.000 53.83419 ? 124 ALA   A CB  1 
ATOM   849  N  N   . GLY   A 1 118 ? 15.76221  -3.57819  -3.75665  1.000 61.64727 ? 125 GLY   A N   1 
ATOM   850  C  CA  . GLY   A 1 118 ? 14.65145  -3.61097  -2.83029  1.000 57.79567 ? 125 GLY   A CA  1 
ATOM   851  C  C   . GLY   A 1 118 ? 13.41415  -4.32402  -3.33997  1.000 53.55579 ? 125 GLY   A C   1 
ATOM   852  O  O   . GLY   A 1 118 ? 12.69589  -4.93321  -2.53599  1.000 51.05311 ? 125 GLY   A O   1 
ATOM   853  N  N   . ALA   A 1 119 ? 13.14771  -4.27937  -4.64425  1.000 42.58603 ? 126 ALA   A N   1 
ATOM   854  C  CA  . ALA   A 1 119 ? 11.87377  -4.74399  -5.17723  1.000 39.14388 ? 126 ALA   A CA  1 
ATOM   855  C  C   . ALA   A 1 119 ? 11.72406  -6.25650  -5.01842  1.000 44.41353 ? 126 ALA   A C   1 
ATOM   856  O  O   . ALA   A 1 119 ? 12.67681  -6.98447  -4.72509  1.000 42.31710 ? 126 ALA   A O   1 
ATOM   857  C  CB  . ALA   A 1 119 ? 11.74086  -4.36623  -6.65182  1.000 40.53078 ? 126 ALA   A CB  1 
ATOM   858  N  N   . ASP   A 1 120 ? 10.49347  -6.72450  -5.22491  1.000 39.66583 ? 127 ASP   A N   1 
ATOM   859  C  CA  . ASP   A 1 120 ? 10.15643  -8.13728  -5.15784  1.000 38.96597 ? 127 ASP   A CA  1 
ATOM   860  C  C   . ASP   A 1 120 ? 9.48038   -8.56170  -6.45791  1.000 32.20187 ? 127 ASP   A C   1 
ATOM   861  O  O   . ASP   A 1 120 ? 9.11638   -7.73455  -7.29855  1.000 30.62590 ? 127 ASP   A O   1 
ATOM   862  C  CB  . ASP   A 1 120 ? 9.26038   -8.45094  -3.94888  1.000 38.13262 ? 127 ASP   A CB  1 
ATOM   863  C  CG  . ASP   A 1 120 ? 7.79159   -8.16821  -4.21625  1.000 50.42009 ? 127 ASP   A CG  1 
ATOM   864  O  OD1 . ASP   A 1 120 ? 7.48131   -7.12134  -4.82274  1.000 57.97418 ? 127 ASP   A OD1 1 
ATOM   865  O  OD2 . ASP   A 1 120 ? 6.94645   -9.00214  -3.82853  1.000 50.75155 ? 127 ASP   A OD2 1 
ATOM   866  N  N   . ILE   A 1 121 ? 9.31075   -9.87727  -6.61114  1.000 30.22698 ? 128 ILE   A N   1 
ATOM   867  C  CA  . ILE   A 1 121 ? 8.78522   -10.43497 -7.85734  1.000 27.00787 ? 128 ILE   A CA  1 
ATOM   868  C  C   . ILE   A 1 121 ? 7.39329   -9.90154  -8.18486  1.000 30.74125 ? 128 ILE   A C   1 
ATOM   869  O  O   . ILE   A 1 121 ? 7.02158   -9.79950  -9.36218  1.000 29.48363 ? 128 ILE   A O   1 
ATOM   870  C  CB  . ILE   A 1 121 ? 8.87959   -11.97820 -7.82905  1.000 29.32023 ? 128 ILE   A CB  1 
ATOM   871  C  CG1 . ILE   A 1 121 ? 10.33479  -12.41123 -8.06252  1.000 38.02790 ? 128 ILE   A CG1 1 
ATOM   872  C  CG2 . ILE   A 1 121 ? 7.93321   -12.63254 -8.83012  1.000 30.98018 ? 128 ILE   A CG2 1 
ATOM   873  C  CD1 . ILE   A 1 121 ? 10.61923  -13.85964 -7.72562  1.000 39.26123 ? 128 ILE   A CD1 1 
ATOM   874  N  N   . SER   A 1 122 ? 6.61903   -9.50863  -7.16903  1.000 32.03504 ? 129 SER   A N   1 
ATOM   875  C  CA  . SER   A 1 122 ? 5.25414   -9.04713  -7.41954  1.000 28.79790 ? 129 SER   A CA  1 
ATOM   876  C  C   . SER   A 1 122 ? 5.19836   -7.76752  -8.24824  1.000 31.14871 ? 129 SER   A C   1 
ATOM   877  O  O   . SER   A 1 122 ? 4.13246   -7.43427  -8.77655  1.000 32.48102 ? 129 SER   A O   1 
ATOM   878  C  CB  . SER   A 1 122 ? 4.50065   -8.83618  -6.10403  1.000 28.63353 ? 129 SER   A CB  1 
ATOM   879  O  OG  . SER   A 1 122 ? 4.90410   -7.64040  -5.46543  1.000 33.54889 ? 129 SER   A OG  1 
ATOM   880  N  N   . MET   A 1 123 ? 6.30391   -7.03728  -8.36819  1.000 27.49216 ? 130 MET   A N   1 
ATOM   881  C  CA  . MET   A 1 123 ? 6.33001   -5.79396  -9.12763  1.000 27.36008 ? 130 MET   A CA  1 
ATOM   882  C  C   . MET   A 1 123 ? 6.68285   -6.00129  -10.59628 1.000 25.07434 ? 130 MET   A C   1 
ATOM   883  O  O   . MET   A 1 123 ? 6.86175   -5.02009  -11.32572 1.000 26.88560 ? 130 MET   A O   1 
ATOM   884  C  CB  . MET   A 1 123 ? 7.26999   -4.79319  -8.45414  1.000 32.96205 ? 130 MET   A CB  1 
ATOM   885  C  CG  . MET   A 1 123 ? 6.94125   -4.62436  -6.97148  1.000 31.90512 ? 130 MET   A CG  1 
ATOM   886  S  SD  . MET   A 1 123 ? 8.21837   -3.80958  -6.00709  1.000 43.77872 ? 130 MET   A SD  1 
ATOM   887  C  CE  . MET   A 1 123 ? 8.39599   -2.28703  -6.93453  1.000 46.27358 ? 130 MET   A CE  1 
ATOM   888  N  N   . ILE   A 1 124 ? 6.73289   -7.25807  -11.04419 1.000 22.70746 ? 131 ILE   A N   1 
ATOM   889  C  CA  . ILE   A 1 124 ? 7.17233   -7.59908  -12.39803 1.000 22.22084 ? 131 ILE   A CA  1 
ATOM   890  C  C   . ILE   A 1 124 ? 6.39288   -6.83193  -13.46367 1.000 21.89072 ? 131 ILE   A C   1 
ATOM   891  O  O   . ILE   A 1 124 ? 6.95117   -6.42821  -14.49446 1.000 21.28199 ? 131 ILE   A O   1 
ATOM   892  C  CB  . ILE   A 1 124 ? 7.09145   -9.12568  -12.60035 1.000 21.39828 ? 131 ILE   A CB  1 
ATOM   893  C  CG1 . ILE   A 1 124 ? 7.70730   -9.53303  -13.94569 1.000 21.60492 ? 131 ILE   A CG1 1 
ATOM   894  C  CG2 . ILE   A 1 124 ? 5.64557   -9.62334  -12.44443 1.000 22.95135 ? 131 ILE   A CG2 1 
ATOM   895  C  CD1 . ILE   A 1 124 ? 7.83288   -11.02987 -14.11756 1.000 23.98786 ? 131 ILE   A CD1 1 
ATOM   896  N  N   . GLY   A 1 125 ? 5.09477   -6.62048  -13.24033 1.000 22.17646 ? 132 GLY   A N   1 
ATOM   897  C  CA  . GLY   A 1 125 ? 4.26625   -5.97399  -14.24514 1.000 24.08756 ? 132 GLY   A CA  1 
ATOM   898  C  C   . GLY   A 1 125 ? 4.66051   -4.54236  -14.54388 1.000 24.99793 ? 132 GLY   A C   1 
ATOM   899  O  O   . GLY   A 1 125 ? 4.38099   -4.04773  -15.64233 1.000 28.97320 ? 132 GLY   A O   1 
ATOM   900  N  N   . GLN   A 1 126 ? 5.30184   -3.86309  -13.58968 1.000 24.46950 ? 133 GLN   A N   1 
ATOM   901  C  CA  . GLN   A 1 126 ? 5.76256   -2.49692  -13.79665 1.000 30.87230 ? 133 GLN   A CA  1 
ATOM   902  C  C   . GLN   A 1 126 ? 6.88407   -2.41322  -14.81898 1.000 30.92316 ? 133 GLN   A C   1 
ATOM   903  O  O   . GLN   A 1 126 ? 7.22715   -1.30771  -15.25253 1.000 32.04884 ? 133 GLN   A O   1 
ATOM   904  C  CB  . GLN   A 1 126 ? 6.25202   -1.92119  -12.47014 1.000 31.60241 ? 133 GLN   A CB  1 
ATOM   905  C  CG  . GLN   A 1 126 ? 5.16525   -1.80882  -11.41527 1.000 35.38755 ? 133 GLN   A CG  1 
ATOM   906  C  CD  . GLN   A 1 126 ? 5.65586   -1.13304  -10.15683 1.000 43.99464 ? 133 GLN   A CD  1 
ATOM   907  O  OE1 . GLN   A 1 126 ? 6.30975   -0.09039  -10.21326 1.000 44.09880 ? 133 GLN   A OE1 1 
ATOM   908  N  NE2 . GLN   A 1 126 ? 5.34504   -1.72433  -9.00887  1.000 47.99192 ? 133 GLN   A NE2 1 
ATOM   909  N  N   . PHE   A 1 127 ? 7.45981   -3.54884  -15.20430 1.000 25.82557 ? 134 PHE   A N   1 
ATOM   910  C  CA  . PHE   A 1 127 ? 8.56950   -3.59731  -16.14566 1.000 25.75790 ? 134 PHE   A CA  1 
ATOM   911  C  C   . PHE   A 1 127 ? 8.17711   -4.23493  -17.47123 1.000 24.78598 ? 134 PHE   A C   1 
ATOM   912  O  O   . PHE   A 1 127 ? 9.05054   -4.53888  -18.29060 1.000 26.34826 ? 134 PHE   A O   1 
ATOM   913  C  CB  . PHE   A 1 127 ? 9.75742   -4.31287  -15.50285 1.000 25.23619 ? 134 PHE   A CB  1 
ATOM   914  C  CG  . PHE   A 1 127 ? 10.13423  -3.74497  -14.16439 1.000 25.40535 ? 134 PHE   A CG  1 
ATOM   915  C  CD1 . PHE   A 1 127 ? 10.96065  -2.63722  -14.07172 1.000 34.64481 ? 134 PHE   A CD1 1 
ATOM   916  C  CD2 . PHE   A 1 127 ? 9.61725   -4.28635  -12.99961 1.000 26.30222 ? 134 PHE   A CD2 1 
ATOM   917  C  CE1 . PHE   A 1 127 ? 11.29234  -2.10136  -12.83747 1.000 34.32713 ? 134 PHE   A CE1 1 
ATOM   918  C  CE2 . PHE   A 1 127 ? 9.94450   -3.75697  -11.76071 1.000 27.15597 ? 134 PHE   A CE2 1 
ATOM   919  C  CZ  . PHE   A 1 127 ? 10.78242  -2.66211  -11.68003 1.000 34.63066 ? 134 PHE   A CZ  1 
ATOM   920  N  N   . GLY   A 1 128 ? 6.88581   -4.45046  -17.69993 1.000 23.91031 ? 135 GLY   A N   1 
ATOM   921  C  CA  . GLY   A 1 128 ? 6.41381   -4.89478  -18.99203 1.000 23.25371 ? 135 GLY   A CA  1 
ATOM   922  C  C   . GLY   A 1 128 ? 6.64459   -6.35262  -19.30746 1.000 21.74709 ? 135 GLY   A C   1 
ATOM   923  O  O   . GLY   A 1 128 ? 6.46960   -6.74728  -20.46480 1.000 25.47581 ? 135 GLY   A O   1 
ATOM   924  N  N   . VAL   A 1 129 ? 7.02247   -7.16805  -18.32225 1.000 19.71291 ? 136 VAL   A N   1 
ATOM   925  C  CA  . VAL   A 1 129 ? 7.31810   -8.57949  -18.55641 1.000 18.50786 ? 136 VAL   A CA  1 
ATOM   926  C  C   . VAL   A 1 129 ? 6.47011   -9.46755  -17.65309 1.000 18.85775 ? 136 VAL   A C   1 
ATOM   927  O  O   . VAL   A 1 129 ? 6.87377   -10.58022 -17.29725 1.000 18.98674 ? 136 VAL   A O   1 
ATOM   928  C  CB  . VAL   A 1 129 ? 8.82196   -8.86613  -18.39249 1.000 19.27077 ? 136 VAL   A CB  1 
ATOM   929  C  CG1 . VAL   A 1 129 ? 9.59702   -8.23801  -19.53954 1.000 21.27980 ? 136 VAL   A CG1 1 
ATOM   930  C  CG2 . VAL   A 1 129 ? 9.33248   -8.31727  -17.07902 1.000 22.62843 ? 136 VAL   A CG2 1 
ATOM   931  N  N   . GLY   A 1 130 ? 5.27431   -8.98826  -17.30381 1.000 17.82660 ? 137 GLY   A N   1 
ATOM   932  C  CA  . GLY   A 1 130 ? 4.40249   -9.73872  -16.41421 1.000 18.29424 ? 137 GLY   A CA  1 
ATOM   933  C  C   . GLY   A 1 130 ? 3.97164   -11.09538 -16.94268 1.000 18.63898 ? 137 GLY   A C   1 
ATOM   934  O  O   . GLY   A 1 130 ? 3.66450   -11.99331 -16.15338 1.000 18.17163 ? 137 GLY   A O   1 
ATOM   935  N  N   . PHE   A 1 131 ? 3.93195   -11.26564 -18.27192 1.000 17.85922 ? 138 PHE   A N   1 
ATOM   936  C  CA  . PHE   A 1 131 ? 3.57623   -12.56806 -18.83641 1.000 16.74167 ? 138 PHE   A CA  1 
ATOM   937  C  C   . PHE   A 1 131 ? 4.39773   -13.69083 -18.21446 1.000 16.83921 ? 138 PHE   A C   1 
ATOM   938  O  O   . PHE   A 1 131 ? 3.87091   -14.77200 -17.91719 1.000 16.24349 ? 138 PHE   A O   1 
ATOM   939  C  CB  . PHE   A 1 131 ? 3.80020   -12.57537 -20.35196 1.000 20.37712 ? 138 PHE   A CB  1 
ATOM   940  C  CG  . PHE   A 1 131 ? 3.78123   -13.95716 -20.95060 1.000 17.82591 ? 138 PHE   A CG  1 
ATOM   941  C  CD1 . PHE   A 1 131 ? 2.58933   -14.64289 -21.10903 1.000 18.68833 ? 138 PHE   A CD1 1 
ATOM   942  C  CD2 . PHE   A 1 131 ? 4.96817   -14.58892 -21.31280 1.000 17.44381 ? 138 PHE   A CD2 1 
ATOM   943  C  CE1 . PHE   A 1 131 ? 2.56392   -15.91904 -21.64129 1.000 18.19610 ? 138 PHE   A CE1 1 
ATOM   944  C  CE2 . PHE   A 1 131 ? 4.95291   -15.87051 -21.84414 1.000 19.55752 ? 138 PHE   A CE2 1 
ATOM   945  C  CZ  . PHE   A 1 131 ? 3.74779   -16.53703 -22.00890 1.000 20.07616 ? 138 PHE   A CZ  1 
ATOM   946  N  N   . TYR   A 1 132 ? 5.69581   -13.45395 -18.01178 1.000 17.01279 ? 139 TYR   A N   1 
ATOM   947  C  CA  . TYR   A 1 132 ? 6.58228   -14.53028 -17.59216 1.000 16.86122 ? 139 TYR   A CA  1 
ATOM   948  C  C   . TYR   A 1 132 ? 6.32390   -14.98166 -16.16163 1.000 17.14400 ? 139 TYR   A C   1 
ATOM   949  O  O   . TYR   A 1 132 ? 6.80225   -16.05417 -15.77586 1.000 18.55807 ? 139 TYR   A O   1 
ATOM   950  C  CB  . TYR   A 1 132 ? 8.04818   -14.13384 -17.82308 1.000 17.00327 ? 139 TYR   A CB  1 
ATOM   951  C  CG  . TYR   A 1 132 ? 8.32460   -13.85901 -19.28809 1.000 17.68778 ? 139 TYR   A CG  1 
ATOM   952  C  CD1 . TYR   A 1 132 ? 8.59842   -14.89455 -20.17561 1.000 18.57909 ? 139 TYR   A CD1 1 
ATOM   953  C  CD2 . TYR   A 1 132 ? 8.27613   -12.56407 -19.78703 1.000 19.11064 ? 139 TYR   A CD2 1 
ATOM   954  C  CE1 . TYR   A 1 132 ? 8.82439   -14.64027 -21.53300 1.000 17.45083 ? 139 TYR   A CE1 1 
ATOM   955  C  CE2 . TYR   A 1 132 ? 8.50464   -12.30132 -21.12880 1.000 20.87558 ? 139 TYR   A CE2 1 
ATOM   956  C  CZ  . TYR   A 1 132 ? 8.77313   -13.33734 -21.99391 1.000 19.26226 ? 139 TYR   A CZ  1 
ATOM   957  O  OH  . TYR   A 1 132 ? 8.99006   -13.04940 -23.32260 1.000 20.94118 ? 139 TYR   A OH  1 
ATOM   958  N  N   . SER   A 1 133 ? 5.54704   -14.21585 -15.38745 1.000 17.88485 ? 140 SER   A N   1 
ATOM   959  C  CA  . SER   A 1 133 ? 5.10508   -14.68195 -14.07747 1.000 17.63443 ? 140 SER   A CA  1 
ATOM   960  C  C   . SER   A 1 133 ? 4.24793   -15.93624 -14.17084 1.000 16.45393 ? 140 SER   A C   1 
ATOM   961  O  O   . SER   A 1 133 ? 4.03552   -16.59830 -13.14925 1.000 18.14527 ? 140 SER   A O   1 
ATOM   962  C  CB  . SER   A 1 133 ? 4.33851   -13.58998 -13.32050 1.000 19.49831 ? 140 SER   A CB  1 
ATOM   963  O  OG  . SER   A 1 133 ? 3.06432   -13.35998 -13.89540 1.000 18.97805 ? 140 SER   A OG  1 
ATOM   964  N  N   . ALA   A 1 134 ? 3.75775   -16.28048 -15.36712 1.000 16.69514 ? 141 ALA   A N   1 
ATOM   965  C  CA  . ALA   A 1 134 ? 3.05524   -17.54819 -15.54231 1.000 15.82536 ? 141 ALA   A CA  1 
ATOM   966  C  C   . ALA   A 1 134 ? 3.88041   -18.72535 -15.04553 1.000 16.76495 ? 141 ALA   A C   1 
ATOM   967  O  O   . ALA   A 1 134 ? 3.32156   -19.71415 -14.55596 1.000 17.60585 ? 141 ALA   A O   1 
ATOM   968  C  CB  . ALA   A 1 134 ? 2.69091   -17.74395 -17.01971 1.000 15.94151 ? 141 ALA   A CB  1 
ATOM   969  N  N   . TYR   A 1 135 ? 5.21437   -18.63197 -15.14123 1.000 16.12697 ? 142 TYR   A N   1 
ATOM   970  C  CA  . TYR   A 1 135 ? 6.07908   -19.73854 -14.75488 1.000 17.44508 ? 142 TYR   A CA  1 
ATOM   971  C  C   . TYR   A 1 135 ? 6.24376   -19.85871 -13.24292 1.000 18.35976 ? 142 TYR   A C   1 
ATOM   972  O  O   . TYR   A 1 135 ? 6.94077   -20.76682 -12.78085 1.000 19.80285 ? 142 TYR   A O   1 
ATOM   973  C  CB  . TYR   A 1 135 ? 7.42003   -19.64091 -15.50026 1.000 15.39169 ? 142 TYR   A CB  1 
ATOM   974  C  CG  . TYR   A 1 135 ? 7.22294   -19.94891 -16.96678 1.000 16.38348 ? 142 TYR   A CG  1 
ATOM   975  C  CD1 . TYR   A 1 135 ? 7.20464   -21.26025 -17.42624 1.000 17.58153 ? 142 TYR   A CD1 1 
ATOM   976  C  CD2 . TYR   A 1 135 ? 6.96065   -18.92768 -17.87639 1.000 16.26492 ? 142 TYR   A CD2 1 
ATOM   977  C  CE1 . TYR   A 1 135 ? 6.97885   -21.54678 -18.76787 1.000 17.30324 ? 142 TYR   A CE1 1 
ATOM   978  C  CE2 . TYR   A 1 135 ? 6.73011   -19.20216 -19.21642 1.000 16.38801 ? 142 TYR   A CE2 1 
ATOM   979  C  CZ  . TYR   A 1 135 ? 6.74176   -20.51115 -19.65270 1.000 16.33049 ? 142 TYR   A CZ  1 
ATOM   980  O  OH  . TYR   A 1 135 ? 6.51033   -20.78002 -20.98826 1.000 17.65335 ? 142 TYR   A OH  1 
ATOM   981  N  N   . LEU   A 1 136 ? 5.59965   -18.98033 -12.46793 1.000 18.34332 ? 143 LEU   A N   1 
ATOM   982  C  CA  . LEU   A 1 136 ? 5.47849   -19.21083 -11.03377 1.000 18.39408 ? 143 LEU   A CA  1 
ATOM   983  C  C   . LEU   A 1 136 ? 4.61094   -20.42759 -10.74902 1.000 19.16691 ? 143 LEU   A C   1 
ATOM   984  O  O   . LEU   A 1 136 ? 4.80963   -21.11512 -9.74431  1.000 21.27527 ? 143 LEU   A O   1 
ATOM   985  C  CB  . LEU   A 1 136 ? 4.85586   -17.98627 -10.35758 1.000 19.41769 ? 143 LEU   A CB  1 
ATOM   986  C  CG  . LEU   A 1 136 ? 5.67026   -16.68937 -10.33875 1.000 19.61261 ? 143 LEU   A CG  1 
ATOM   987  C  CD1 . LEU   A 1 136 ? 4.82285   -15.52088 -9.85957  1.000 19.73465 ? 143 LEU   A CD1 1 
ATOM   988  C  CD2 . LEU   A 1 136 ? 6.90750   -16.85076 -9.46888  1.000 21.90352 ? 143 LEU   A CD2 1 
ATOM   989  N  N   . VAL   A 1 137 ? 3.64109   -20.70639 -11.61827 1.000 18.74674 ? 144 VAL   A N   1 
ATOM   990  C  CA  . VAL   A 1 137 ? 2.67278   -21.76140 -11.35799 1.000 21.26969 ? 144 VAL   A CA  1 
ATOM   991  C  C   . VAL   A 1 137 ? 2.60703   -22.80706 -12.46416 1.000 19.45954 ? 144 VAL   A C   1 
ATOM   992  O  O   . VAL   A 1 137 ? 2.07116   -23.90056 -12.22374 1.000 20.80075 ? 144 VAL   A O   1 
ATOM   993  C  CB  . VAL   A 1 137 ? 1.26554   -21.19599 -11.05725 1.000 17.71524 ? 144 VAL   A CB  1 
ATOM   994  C  CG1 . VAL   A 1 137 ? 1.29003   -20.31195 -9.81598  1.000 20.08900 ? 144 VAL   A CG1 1 
ATOM   995  C  CG2 . VAL   A 1 137 ? 0.71849   -20.42919 -12.25442 1.000 18.60632 ? 144 VAL   A CG2 1 
ATOM   996  N  N   . ALA   A 1 138 ? 3.14164   -22.53984 -13.65294 1.000 19.00483 ? 145 ALA   A N   1 
ATOM   997  C  CA  . ALA   A 1 138 ? 2.99004   -23.43060 -14.79392 1.000 18.86395 ? 145 ALA   A CA  1 
ATOM   998  C  C   . ALA   A 1 138 ? 4.32341   -24.06139 -15.16311 1.000 19.87780 ? 145 ALA   A C   1 
ATOM   999  O  O   . ALA   A 1 138 ? 5.35229   -23.37792 -15.21427 1.000 22.71747 ? 145 ALA   A O   1 
ATOM   1000 C  CB  . ALA   A 1 138 ? 2.44298   -22.67271 -16.00544 1.000 20.84557 ? 145 ALA   A CB  1 
ATOM   1001 N  N   . GLU   A 1 139 ? 4.29351   -25.36620 -15.42705 1.000 19.01102 ? 146 GLU   A N   1 
ATOM   1002 C  CA  . GLU   A 1 139 ? 5.45941   -26.04538 -15.98259 1.000 20.14406 ? 146 GLU   A CA  1 
ATOM   1003 C  C   . GLU   A 1 139 ? 5.55695   -25.87474 -17.48960 1.000 20.29466 ? 146 GLU   A C   1 
ATOM   1004 O  O   . GLU   A 1 139 ? 6.65299   -25.97671 -18.04973 1.000 20.64203 ? 146 GLU   A O   1 
ATOM   1005 C  CB  . GLU   A 1 139 ? 5.42686   -27.53191 -15.61917 1.000 24.71976 ? 146 GLU   A CB  1 
ATOM   1006 C  CG  . GLU   A 1 139 ? 4.34446   -28.32475 -16.32958 1.000 35.22765 ? 146 GLU   A CG  1 
ATOM   1007 C  CD  . GLU   A 1 139 ? 4.17307   -29.72413 -15.76369 1.000 50.99604 ? 146 GLU   A CD  1 
ATOM   1008 O  OE1 . GLU   A 1 139 ? 3.41370   -30.51770 -16.36246 1.000 48.12116 ? 146 GLU   A OE1 1 
ATOM   1009 O  OE2 . GLU   A 1 139 ? 4.79930   -30.03135 -14.72589 1.000 51.97159 ? 146 GLU   A OE2 1 
ATOM   1010 N  N   . LYS   A 1 140 ? 4.43694   -25.60978 -18.15162 1.000 20.20787 ? 147 LYS   A N   1 
ATOM   1011 C  CA  . LYS   A 1 140 ? 4.41162   -25.35392 -19.58053 1.000 18.11797 ? 147 LYS   A CA  1 
ATOM   1012 C  C   . LYS   A 1 140 ? 3.32649   -24.32130 -19.81936 1.000 17.43337 ? 147 LYS   A C   1 
ATOM   1013 O  O   . LYS   A 1 140 ? 2.30593   -24.31985 -19.12698 1.000 18.18787 ? 147 LYS   A O   1 
ATOM   1014 C  CB  . LYS   A 1 140 ? 4.10950   -26.63571 -20.36319 1.000 19.42879 ? 147 LYS   A CB  1 
ATOM   1015 C  CG  . LYS   A 1 140 ? 4.09397   -26.46762 -21.87562 1.000 21.10368 ? 147 LYS   A CG  1 
ATOM   1016 C  CD  . LYS   A 1 140 ? 4.02034   -27.82069 -22.55484 1.000 25.48120 ? 147 LYS   A CD  1 
ATOM   1017 C  CE  . LYS   A 1 140 ? 2.59017   -28.30479 -22.68031 1.000 27.35401 ? 147 LYS   A CE  1 
ATOM   1018 N  NZ  . LYS   A 1 140 ? 2.52347   -29.70841 -23.18775 1.000 38.92848 ? 147 LYS   A NZ  1 
ATOM   1019 N  N   . VAL   A 1 141 ? 3.56617   -23.42611 -20.76840 1.000 15.20250 ? 148 VAL   A N   1 
ATOM   1020 C  CA  . VAL   A 1 141 ? 2.59417   -22.41210 -21.15696 1.000 16.56598 ? 148 VAL   A CA  1 
ATOM   1021 C  C   . VAL   A 1 141 ? 2.39934   -22.49095 -22.66078 1.000 18.07279 ? 148 VAL   A C   1 
ATOM   1022 O  O   . VAL   A 1 141 ? 3.38045   -22.48841 -23.41656 1.000 16.19720 ? 148 VAL   A O   1 
ATOM   1023 C  CB  . VAL   A 1 141 ? 3.04177   -20.99879 -20.74414 1.000 17.50431 ? 148 VAL   A CB  1 
ATOM   1024 C  CG1 . VAL   A 1 141 ? 2.02684   -19.95598 -21.23299 1.000 18.49051 ? 148 VAL   A CG1 1 
ATOM   1025 C  CG2 . VAL   A 1 141 ? 3.23668   -20.91521 -19.22640 1.000 16.49846 ? 148 VAL   A CG2 1 
ATOM   1026 N  N   . THR   A 1 142 ? 1.14323   -22.55747 -23.09555 1.000 17.02988 ? 149 THR   A N   1 
ATOM   1027 C  CA  . THR   A 1 142 ? 0.78145   -22.50297 -24.50551 1.000 16.97318 ? 149 THR   A CA  1 
ATOM   1028 C  C   . THR   A 1 142 ? -0.01113  -21.22761 -24.74632 1.000 18.83798 ? 149 THR   A C   1 
ATOM   1029 O  O   . THR   A 1 142 ? -0.93772  -20.91780 -23.98858 1.000 18.98964 ? 149 THR   A O   1 
ATOM   1030 C  CB  . THR   A 1 142 ? -0.06682  -23.71372 -24.90636 1.000 18.91995 ? 149 THR   A CB  1 
ATOM   1031 O  OG1 . THR   A 1 142 ? 0.57524   -24.93008 -24.49931 1.000 22.32824 ? 149 THR   A OG1 1 
ATOM   1032 C  CG2 . THR   A 1 142 ? -0.29535  -23.73535 -26.41587 1.000 21.46410 ? 149 THR   A CG2 1 
ATOM   1033 N  N   . VAL   A 1 143 ? 0.35430   -20.47978 -25.77979 1.000 16.18357 ? 150 VAL   A N   1 
ATOM   1034 C  CA  . VAL   A 1 143 ? -0.33452  -19.23947 -26.12821 1.000 17.01693 ? 150 VAL   A CA  1 
ATOM   1035 C  C   . VAL   A 1 143 ? -0.89825  -19.39575 -27.53445 1.000 16.59342 ? 150 VAL   A C   1 
ATOM   1036 O  O   . VAL   A 1 143 ? -0.13369  -19.54085 -28.49968 1.000 18.88774 ? 150 VAL   A O   1 
ATOM   1037 C  CB  . VAL   A 1 143 ? 0.59844   -18.01990 -26.03141 1.000 16.33323 ? 150 VAL   A CB  1 
ATOM   1038 C  CG1 . VAL   A 1 143 ? -0.12204  -16.74271 -26.46600 1.000 21.71273 ? 150 VAL   A CG1 1 
ATOM   1039 C  CG2 . VAL   A 1 143 ? 1.17847   -17.87432 -24.61275 1.000 17.44522 ? 150 VAL   A CG2 1 
ATOM   1040 N  N   . ILE   A 1 144 ? -2.22796  -19.37808 -27.65457 1.000 15.90570 ? 151 ILE   A N   1 
ATOM   1041 C  CA  . ILE   A 1 144 ? -2.92113  -19.41431 -28.94284 1.000 16.26796 ? 151 ILE   A CA  1 
ATOM   1042 C  C   . ILE   A 1 144 ? -3.39840  -18.00015 -29.23390 1.000 17.56130 ? 151 ILE   A C   1 
ATOM   1043 O  O   . ILE   A 1 144 ? -3.99735  -17.35556 -28.36388 1.000 17.32072 ? 151 ILE   A O   1 
ATOM   1044 C  CB  . ILE   A 1 144 ? -4.12873  -20.36749 -28.90451 1.000 18.82526 ? 151 ILE   A CB  1 
ATOM   1045 C  CG1 . ILE   A 1 144 ? -3.78437  -21.69318 -28.22825 1.000 28.07832 ? 151 ILE   A CG1 1 
ATOM   1046 C  CG2 . ILE   A 1 144 ? -4.64846  -20.60893 -30.32209 1.000 21.59656 ? 151 ILE   A CG2 1 
ATOM   1047 C  CD1 . ILE   A 1 144 ? -2.84229  -22.55010 -29.01236 1.000 26.62470 ? 151 ILE   A CD1 1 
ATOM   1048 N  N   . THR   A 1 145 ? -3.14746  -17.51047 -30.44460 1.000 17.11009 ? 152 THR   A N   1 
ATOM   1049 C  CA  . THR   A 1 145 ? -3.43958  -16.11002 -30.72564 1.000 17.32224 ? 152 THR   A CA  1 
ATOM   1050 C  C   . THR   A 1 145 ? -3.86332  -15.90931 -32.17631 1.000 17.80547 ? 152 THR   A C   1 
ATOM   1051 O  O   . THR   A 1 145 ? -3.43583  -16.63702 -33.08020 1.000 18.96533 ? 152 THR   A O   1 
ATOM   1052 C  CB  . THR   A 1 145 ? -2.26018  -15.19884 -30.32862 1.000 16.95173 ? 152 THR   A CB  1 
ATOM   1053 O  OG1 . THR   A 1 145 ? -2.69677  -13.83388 -30.29385 1.000 19.00113 ? 152 THR   A OG1 1 
ATOM   1054 C  CG2 . THR   A 1 145 ? -1.09501  -15.34648 -31.30460 1.000 19.02801 ? 152 THR   A CG2 1 
ATOM   1055 N  N   . LYS   A 1 146 ? -4.72329  -14.91036 -32.38012 1.000 17.37686 ? 153 LYS   A N   1 
ATOM   1056 C  CA  . LYS   A 1 146 ? -5.20927  -14.53820 -33.70463 1.000 17.25337 ? 153 LYS   A CA  1 
ATOM   1057 C  C   . LYS   A 1 146 ? -5.33903  -13.02493 -33.74468 1.000 18.71364 ? 153 LYS   A C   1 
ATOM   1058 O  O   . LYS   A 1 146 ? -6.10623  -12.44426 -32.96948 1.000 18.54401 ? 153 LYS   A O   1 
ATOM   1059 C  CB  . LYS   A 1 146 ? -6.55901  -15.20006 -34.00029 1.000 19.01328 ? 153 LYS   A CB  1 
ATOM   1060 C  CG  . LYS   A 1 146 ? -7.21723  -14.77047 -35.31375 1.000 20.14994 ? 153 LYS   A CG  1 
ATOM   1061 C  CD  . LYS   A 1 146 ? -6.41873  -15.23848 -36.52150 1.000 20.56209 ? 153 LYS   A CD  1 
ATOM   1062 C  CE  . LYS   A 1 146 ? -7.16273  -14.93283 -37.81758 1.000 23.73774 ? 153 LYS   A CE  1 
ATOM   1063 N  NZ  . LYS   A 1 146 ? -7.11307  -13.48951 -38.17004 1.000 23.08459 ? 153 LYS   A NZ  1 
ATOM   1064 N  N   . HIS   A 1 147 ? -4.57540  -12.39980 -34.63225 1.000 18.92765 ? 154 HIS   A N   1 
ATOM   1065 C  CA  . HIS   A 1 147 ? -4.60583  -10.97094 -34.89274 1.000 17.47003 ? 154 HIS   A CA  1 
ATOM   1066 C  C   . HIS   A 1 147 ? -5.28002  -10.76069 -36.24418 1.000 21.04683 ? 154 HIS   A C   1 
ATOM   1067 O  O   . HIS   A 1 147 ? -5.17540  -11.60566 -37.13853 1.000 21.61966 ? 154 HIS   A O   1 
ATOM   1068 C  CB  . HIS   A 1 147 ? -3.15983  -10.45153 -34.92902 1.000 18.47468 ? 154 HIS   A CB  1 
ATOM   1069 C  CG  . HIS   A 1 147 ? -3.02992  -8.96609  -35.05876 1.000 21.13668 ? 154 HIS   A CG  1 
ATOM   1070 N  ND1 . HIS   A 1 147 ? -3.22959  -8.29780  -36.24674 1.000 22.93259 ? 154 HIS   A ND1 1 
ATOM   1071 C  CD2 . HIS   A 1 147 ? -2.68057  -8.02237  -34.15160 1.000 22.07603 ? 154 HIS   A CD2 1 
ATOM   1072 C  CE1 . HIS   A 1 147 ? -3.02667  -7.00558  -36.06323 1.000 24.36146 ? 154 HIS   A CE1 1 
ATOM   1073 N  NE2 . HIS   A 1 147 ? -2.68977  -6.81259  -34.80024 1.000 24.25792 ? 154 HIS   A NE2 1 
ATOM   1074 N  N   . ASN   A 1 148 ? -5.99451  -9.63900  -36.38805 1.000 19.87855 ? 155 ASN   A N   1 
ATOM   1075 C  CA  . ASN   A 1 148 ? -6.70415  -9.37427  -37.64189 1.000 21.26797 ? 155 ASN   A CA  1 
ATOM   1076 C  C   . ASN   A 1 148 ? -5.80237  -9.47226  -38.87036 1.000 23.77017 ? 155 ASN   A C   1 
ATOM   1077 O  O   . ASN   A 1 148 ? -6.27474  -9.82310  -39.95927 1.000 26.12341 ? 155 ASN   A O   1 
ATOM   1078 C  CB  . ASN   A 1 148 ? -7.37915  -7.99667  -37.62050 1.000 22.72666 ? 155 ASN   A CB  1 
ATOM   1079 C  CG  . ASN   A 1 148 ? -8.64343  -7.97245  -36.79367 1.000 23.82555 ? 155 ASN   A CG  1 
ATOM   1080 O  OD1 . ASN   A 1 148 ? -9.32827  -8.98481  -36.65830 1.000 26.51379 ? 155 ASN   A OD1 1 
ATOM   1081 N  ND2 . ASN   A 1 148 ? -8.98433  -6.80004  -36.26777 1.000 25.37369 ? 155 ASN   A ND2 1 
ATOM   1082 N  N   . ASP   A 1 149 ? -4.51321  -9.16525  -38.72680 1.000 23.49351 ? 156 ASP   A N   1 
ATOM   1083 C  CA  . ASP   A 1 149 ? -3.60695  -9.08782  -39.86558 1.000 26.27398 ? 156 ASP   A CA  1 
ATOM   1084 C  C   . ASP   A 1 149 ? -2.80352  -10.36299 -40.08960 1.000 30.18318 ? 156 ASP   A C   1 
ATOM   1085 O  O   . ASP   A 1 149 ? -1.89114  -10.36091 -40.92067 1.000 30.84406 ? 156 ASP   A O   1 
ATOM   1086 C  CB  . ASP   A 1 149 ? -2.64953  -7.90266  -39.71370 1.000 27.65343 ? 156 ASP   A CB  1 
ATOM   1087 C  CG  . ASP   A 1 149 ? -3.36652  -6.57158  -39.66975 1.000 29.21179 ? 156 ASP   A CG  1 
ATOM   1088 O  OD1 . ASP   A 1 149 ? -4.51440  -6.49413  -40.15227 1.000 30.55468 ? 156 ASP   A OD1 1 
ATOM   1089 O  OD2 . ASP   A 1 149 ? -2.77217  -5.60020  -39.15799 1.000 35.42843 ? 156 ASP   A OD2 1 
ATOM   1090 N  N   . ASP   A 1 150 ? -3.10461  -11.44628 -39.37569 1.000 25.98649 ? 157 ASP   A N   1 
ATOM   1091 C  CA  . ASP   A 1 150 ? -2.31166  -12.66328 -39.50934 1.000 23.84111 ? 157 ASP   A CA  1 
ATOM   1092 C  C   . ASP   A 1 150 ? -3.20133  -13.87994 -39.27197 1.000 28.98567 ? 157 ASP   A C   1 
ATOM   1093 O  O   . ASP   A 1 150 ? -4.39875  -13.75974 -38.99418 1.000 25.69152 ? 157 ASP   A O   1 
ATOM   1094 C  CB  . ASP   A 1 150 ? -1.10151  -12.62415 -38.56671 1.000 24.73044 ? 157 ASP   A CB  1 
ATOM   1095 C  CG  . ASP   A 1 150 ? 0.09021   -13.40570 -39.09677 1.000 25.48502 ? 157 ASP   A CG  1 
ATOM   1096 O  OD1 . ASP   A 1 150 ? -0.05866  -14.16900 -40.07711 1.000 30.66520 ? 157 ASP   A OD1 1 
ATOM   1097 O  OD2 . ASP   A 1 150 ? 1.19130   -13.24450 -38.52336 1.000 26.31804 ? 157 ASP   A OD2 1 
ATOM   1098 N  N   . GLU   A 1 151 ? -2.60385  -15.06204 -39.39725 1.000 24.45226 ? 158 GLU   A N   1 
ATOM   1099 C  CA  . GLU   A 1 151 ? -3.28743  -16.32329 -39.15877 1.000 26.69786 ? 158 GLU   A CA  1 
ATOM   1100 C  C   . GLU   A 1 151 ? -3.18214  -16.70669 -37.68443 1.000 21.76565 ? 158 GLU   A C   1 
ATOM   1101 O  O   . GLU   A 1 151 ? -2.49959  -16.05525 -36.89687 1.000 21.54819 ? 158 GLU   A O   1 
ATOM   1102 C  CB  . GLU   A 1 151 ? -2.68215  -17.42478 -40.02927 1.000 31.83149 ? 158 GLU   A CB  1 
ATOM   1103 C  CG  . GLU   A 1 151 ? -2.67034  -17.11009 -41.51847 1.000 37.58925 ? 158 GLU   A CG  1 
ATOM   1104 C  CD  . GLU   A 1 151 ? -4.04679  -16.77132 -42.05380 1.000 55.87196 ? 158 GLU   A CD  1 
ATOM   1105 O  OE1 . GLU   A 1 151 ? -4.16762  -15.77251 -42.79498 1.000 66.12462 ? 158 GLU   A OE1 1 
ATOM   1106 O  OE2 . GLU   A 1 151 ? -5.00775  -17.50278 -41.73434 1.000 66.72120 ? 158 GLU   A OE2 1 
ATOM   1107 N  N   . GLN   A 1 152 ? -3.85958  -17.79102 -37.31766 1.000 22.44814 ? 159 GLN   A N   1 
ATOM   1108 C  CA  . GLN   A 1 152 ? -3.86247  -18.24695 -35.93331 1.000 21.04167 ? 159 GLN   A CA  1 
ATOM   1109 C  C   . GLN   A 1 152 ? -2.61498  -19.07721 -35.65681 1.000 20.75094 ? 159 GLN   A C   1 
ATOM   1110 O  O   . GLN   A 1 152 ? -2.29636  -20.00384 -36.40885 1.000 23.12384 ? 159 GLN   A O   1 
ATOM   1111 C  CB  . GLN   A 1 152 ? -5.11400  -19.07802 -35.65420 1.000 20.09743 ? 159 GLN   A CB  1 
ATOM   1112 C  CG  . GLN   A 1 152 ? -5.34834  -19.34241 -34.16526 1.000 20.94713 ? 159 GLN   A CG  1 
ATOM   1113 C  CD  . GLN   A 1 152 ? -6.76527  -19.79621 -33.88229 1.000 24.91788 ? 159 GLN   A CD  1 
ATOM   1114 O  OE1 . GLN   A 1 152 ? -7.72044  -19.11283 -34.23619 1.000 28.44511 ? 159 GLN   A OE1 1 
ATOM   1115 N  NE2 . GLN   A 1 152 ? -6.90771  -20.94968 -33.24196 1.000 26.01899 ? 159 GLN   A NE2 1 
ATOM   1116 N  N   . TYR   A 1 153 ? -1.91909  -18.74832 -34.57023 1.000 17.98917 ? 160 TYR   A N   1 
ATOM   1117 C  CA  . TYR   A 1 153 ? -0.65236  -19.37719 -34.23075 1.000 20.42092 ? 160 TYR   A CA  1 
ATOM   1118 C  C   . TYR   A 1 153 ? -0.67100  -19.87961 -32.79548 1.000 20.88164 ? 160 TYR   A C   1 
ATOM   1119 O  O   . TYR   A 1 153 ? -1.40299  -19.36086 -31.94722 1.000 19.15271 ? 160 TYR   A O   1 
ATOM   1120 C  CB  . TYR   A 1 153 ? 0.51532   -18.39266 -34.39290 1.000 19.83491 ? 160 TYR   A CB  1 
ATOM   1121 C  CG  . TYR   A 1 153 ? 0.94295   -18.22119 -35.82779 1.000 21.71829 ? 160 TYR   A CG  1 
ATOM   1122 C  CD1 . TYR   A 1 153 ? 1.81408   -19.12556 -36.41701 1.000 24.06689 ? 160 TYR   A CD1 1 
ATOM   1123 C  CD2 . TYR   A 1 153 ? 0.44844   -17.18248 -36.60840 1.000 25.50971 ? 160 TYR   A CD2 1 
ATOM   1124 C  CE1 . TYR   A 1 153 ? 2.20578   -18.99191 -37.73866 1.000 28.31566 ? 160 TYR   A CE1 1 
ATOM   1125 C  CE2 . TYR   A 1 153 ? 0.83564   -17.04067 -37.93456 1.000 28.46335 ? 160 TYR   A CE2 1 
ATOM   1126 C  CZ  . TYR   A 1 153 ? 1.71244   -17.95041 -38.49001 1.000 30.95522 ? 160 TYR   A CZ  1 
ATOM   1127 O  OH  . TYR   A 1 153 ? 2.10557   -17.81967 -39.80209 1.000 37.79251 ? 160 TYR   A OH  1 
ATOM   1128 N  N   . ALA   A 1 154 ? 0.17157   -20.87829 -32.53088 1.000 19.73231 ? 161 ALA   A N   1 
ATOM   1129 C  CA  . ALA   A 1 154 ? 0.39188   -21.42241 -31.19576 1.000 18.11189 ? 161 ALA   A CA  1 
ATOM   1130 C  C   . ALA   A 1 154 ? 1.86598   -21.28424 -30.83297 1.000 18.30911 ? 161 ALA   A C   1 
ATOM   1131 O  O   . ALA   A 1 154 ? 2.73347   -21.79944 -31.54561 1.000 18.59152 ? 161 ALA   A O   1 
ATOM   1132 C  CB  . ALA   A 1 154 ? -0.00879  -22.89736 -31.14571 1.000 22.34623 ? 161 ALA   A CB  1 
ATOM   1133 N  N   . TRP   A 1 155 ? 2.13528   -20.59568 -29.73158 1.000 16.92969 ? 162 TRP   A N   1 
ATOM   1134 C  CA  . TRP   A 1 155 ? 3.45251   -20.48873 -29.11327 1.000 15.49992 ? 162 TRP   A CA  1 
ATOM   1135 C  C   . TRP   A 1 155 ? 3.46139   -21.40128 -27.89641 1.000 17.85465 ? 162 TRP   A C   1 
ATOM   1136 O  O   . TRP   A 1 155 ? 2.43622   -21.55489 -27.22755 1.000 16.71713 ? 162 TRP   A O   1 
ATOM   1137 C  CB  . TRP   A 1 155 ? 3.64134   -19.02778 -28.68321 1.000 17.36322 ? 162 TRP   A CB  1 
ATOM   1138 C  CG  . TRP   A 1 155 ? 4.88693   -18.63589 -27.90754 1.000 14.53352 ? 162 TRP   A CG  1 
ATOM   1139 C  CD1 . TRP   A 1 155 ? 5.94764   -17.92947 -28.39045 1.000 15.33671 ? 162 TRP   A CD1 1 
ATOM   1140 C  CD2 . TRP   A 1 155 ? 5.14451   -18.83999 -26.50541 1.000 15.84733 ? 162 TRP   A CD2 1 
ATOM   1141 N  NE1 . TRP   A 1 155 ? 6.86721   -17.71084 -27.38779 1.000 16.23563 ? 162 TRP   A NE1 1 
ATOM   1142 C  CE2 . TRP   A 1 155 ? 6.39459   -18.25481 -26.22147 1.000 16.77132 ? 162 TRP   A CE2 1 
ATOM   1143 C  CE3 . TRP   A 1 155 ? 4.44386   -19.46806 -25.46824 1.000 16.22311 ? 162 TRP   A CE3 1 
ATOM   1144 C  CZ2 . TRP   A 1 155 ? 6.96688   -18.29512 -24.94911 1.000 16.13418 ? 162 TRP   A CZ2 1 
ATOM   1145 C  CZ3 . TRP   A 1 155 ? 5.01299   -19.49712 -24.20188 1.000 16.79719 ? 162 TRP   A CZ3 1 
ATOM   1146 C  CH2 . TRP   A 1 155 ? 6.26085   -18.91367 -23.95438 1.000 17.01310 ? 162 TRP   A CH2 1 
ATOM   1147 N  N   . GLU   A 1 156 ? 4.60204   -22.03212 -27.61526 1.000 16.24274 ? 163 GLU   A N   1 
ATOM   1148 C  CA  . GLU   A 1 156 ? 4.66083   -22.91550 -26.45787 1.000 16.26679 ? 163 GLU   A CA  1 
ATOM   1149 C  C   . GLU   A 1 156 ? 6.06895   -22.92463 -25.88246 1.000 15.51915 ? 163 GLU   A C   1 
ATOM   1150 O  O   . GLU   A 1 156 ? 7.05264   -22.89170 -26.62980 1.000 17.00324 ? 163 GLU   A O   1 
ATOM   1151 C  CB  . GLU   A 1 156 ? 4.26192   -24.34234 -26.84198 1.000 19.39099 ? 163 GLU   A CB  1 
ATOM   1152 C  CG  . GLU   A 1 156 ? 4.03544   -25.28866 -25.68202 1.000 21.22639 ? 163 GLU   A CG  1 
ATOM   1153 C  CD  . GLU   A 1 156 ? 3.28284   -26.53442 -26.11191 1.000 33.34472 ? 163 GLU   A CD  1 
ATOM   1154 O  OE1 . GLU   A 1 156 ? 3.88186   -27.37144 -26.82315 1.000 33.17938 ? 163 GLU   A OE1 1 
ATOM   1155 O  OE2 . GLU   A 1 156 ? 2.08996   -26.67080 -25.76023 1.000 29.63880 ? 163 GLU   A OE2 1 
ATOM   1156 N  N   . SER   A 1 157 ? 6.16730   -22.98638 -24.55644 1.000 15.50760 ? 164 SER   A N   1 
ATOM   1157 C  CA  . SER   A 1 157 ? 7.47262   -23.16634 -23.93837 1.000 15.49905 ? 164 SER   A CA  1 
ATOM   1158 C  C   . SER   A 1 157 ? 7.33022   -23.83159 -22.58012 1.000 15.03238 ? 164 SER   A C   1 
ATOM   1159 O  O   . SER   A 1 157 ? 6.43270   -23.49470 -21.79791 1.000 15.09443 ? 164 SER   A O   1 
ATOM   1160 C  CB  . SER   A 1 157 ? 8.22750   -21.84297 -23.79379 1.000 16.75582 ? 164 SER   A CB  1 
ATOM   1161 O  OG  . SER   A 1 157 ? 9.48351   -22.06656 -23.16133 1.000 16.77572 ? 164 SER   A OG  1 
ATOM   1162 N  N   . SER   A 1 158 ? 8.22489   -24.78501 -22.31371 1.000 17.48040 ? 165 SER   A N   1 
ATOM   1163 C  CA  . SER   A 1 158 ? 8.43951   -25.33170 -20.98196 1.000 19.99446 ? 165 SER   A CA  1 
ATOM   1164 C  C   . SER   A 1 158 ? 9.69309   -24.75737 -20.34246 1.000 17.15330 ? 165 SER   A C   1 
ATOM   1165 O  O   . SER   A 1 158 ? 10.30703  -25.41397 -19.49433 1.000 22.34371 ? 165 SER   A O   1 
ATOM   1166 C  CB  . SER   A 1 158 ? 8.52135   -26.85775 -21.04198 1.000 21.48389 ? 165 SER   A CB  1 
ATOM   1167 O  OG  . SER   A 1 158 ? 7.28890   -27.40501 -21.48411 1.000 24.02359 ? 165 SER   A OG  1 
ATOM   1168 N  N   . ALA   A 1 159 ? 10.07696  -23.54435 -20.74064 1.000 18.44927 ? 166 ALA   A N   1 
ATOM   1169 C  CA  . ALA   A 1 159 ? 11.33578  -22.92562 -20.34048 1.000 20.65072 ? 166 ALA   A CA  1 
ATOM   1170 C  C   . ALA   A 1 159 ? 12.49784  -23.75305 -20.87923 1.000 22.95576 ? 166 ALA   A C   1 
ATOM   1171 O  O   . ALA   A 1 159 ? 12.40601  -24.30124 -21.98020 1.000 25.11732 ? 166 ALA   A O   1 
ATOM   1172 C  CB  . ALA   A 1 159 ? 11.39804  -22.70666 -18.82510 1.000 25.69137 ? 166 ALA   A CB  1 
ATOM   1173 N  N   . GLY   A 1 160 ? 13.58928  -23.85709 -20.13148 1.000 24.59521 ? 167 GLY   A N   1 
ATOM   1174 C  CA  . GLY   A 1 160 ? 14.71177  -24.60525 -20.66006 1.000 24.29465 ? 167 GLY   A CA  1 
ATOM   1175 C  C   . GLY   A 1 160 ? 15.38468  -23.97272 -21.85464 1.000 24.56637 ? 167 GLY   A C   1 
ATOM   1176 O  O   . GLY   A 1 160 ? 16.17993  -24.63685 -22.52932 1.000 25.42640 ? 167 GLY   A O   1 
ATOM   1177 N  N   . GLY   A 1 161 ? 15.06725  -22.71800 -22.15731 1.000 19.50393 ? 168 GLY   A N   1 
ATOM   1178 C  CA  . GLY   A 1 161 ? 15.81523  -21.94198 -23.11816 1.000 17.61924 ? 168 GLY   A CA  1 
ATOM   1179 C  C   . GLY   A 1 161 ? 15.23024  -21.86603 -24.50958 1.000 16.70394 ? 168 GLY   A C   1 
ATOM   1180 O  O   . GLY   A 1 161 ? 15.82127  -21.20163 -25.36529 1.000 19.98406 ? 168 GLY   A O   1 
ATOM   1181 N  N   . SER   A 1 162 ? 14.09733  -22.51369 -24.77031 1.000 18.36278 ? 169 SER   A N   1 
ATOM   1182 C  CA  . SER   A 1 162 ? 13.55438  -22.50913 -26.11803 1.000 17.25857 ? 169 SER   A CA  1 
ATOM   1183 C  C   . SER   A 1 162 ? 12.04305  -22.39539 -26.07010 1.000 17.83136 ? 169 SER   A C   1 
ATOM   1184 O  O   . SER   A 1 162 ? 11.40409  -22.69090 -25.05616 1.000 18.36028 ? 169 SER   A O   1 
ATOM   1185 C  CB  . SER   A 1 162 ? 13.92918  -23.76987 -26.90878 1.000 20.36016 ? 169 SER   A CB  1 
ATOM   1186 O  OG  . SER   A 1 162 ? 13.37317  -24.93544 -26.31853 1.000 23.76994 ? 169 SER   A OG  1 
ATOM   1187 N  N   . PHE   A 1 163 ? 11.48876  -21.96602 -27.20191 1.000 17.41252 ? 170 PHE   A N   1 
ATOM   1188 C  CA  . PHE   A 1 163 ? 10.05264  -21.94251 -27.41544 1.000 16.77304 ? 170 PHE   A CA  1 
ATOM   1189 C  C   . PHE   A 1 163 ? 9.77248   -22.39193 -28.84004 1.000 17.65646 ? 170 PHE   A C   1 
ATOM   1190 O  O   . PHE   A 1 163 ? 10.65096  -22.36461 -29.70196 1.000 18.18250 ? 170 PHE   A O   1 
ATOM   1191 C  CB  . PHE   A 1 163 ? 9.44301   -20.55458 -27.14376 1.000 18.28696 ? 170 PHE   A CB  1 
ATOM   1192 C  CG  . PHE   A 1 163 ? 9.93303   -19.45743 -28.06376 1.000 16.00271 ? 170 PHE   A CG  1 
ATOM   1193 C  CD1 . PHE   A 1 163 ? 11.05667  -18.71203 -27.73601 1.000 17.37808 ? 170 PHE   A CD1 1 
ATOM   1194 C  CD2 . PHE   A 1 163 ? 9.23815   -19.13880 -29.22360 1.000 16.31825 ? 170 PHE   A CD2 1 
ATOM   1195 C  CE1 . PHE   A 1 163 ? 11.49474  -17.68256 -28.56382 1.000 18.01214 ? 170 PHE   A CE1 1 
ATOM   1196 C  CE2 . PHE   A 1 163 ? 9.66125   -18.11213 -30.05500 1.000 16.13200 ? 170 PHE   A CE2 1 
ATOM   1197 C  CZ  . PHE   A 1 163 ? 10.79633  -17.38268 -29.72732 1.000 18.80049 ? 170 PHE   A CZ  1 
ATOM   1198 N  N   . THR   A 1 164 ? 8.54064   -22.82984 -29.08259 1.000 17.49998 ? 171 THR   A N   1 
ATOM   1199 C  CA  . THR   A 1 164 ? 8.12759   -23.23121 -30.42058 1.000 17.97246 ? 171 THR   A CA  1 
ATOM   1200 C  C   . THR   A 1 164 ? 6.99093   -22.34868 -30.91257 1.000 15.96550 ? 171 THR   A C   1 
ATOM   1201 O  O   . THR   A 1 164 ? 6.21945   -21.80058 -30.11702 1.000 16.31687 ? 171 THR   A O   1 
ATOM   1202 C  CB  . THR   A 1 164 ? 7.69586   -24.70459 -30.49205 1.000 18.73246 ? 171 THR   A CB  1 
ATOM   1203 O  OG1 . THR   A 1 164 ? 6.55664   -24.91712 -29.64935 1.000 22.01650 ? 171 THR   A OG1 1 
ATOM   1204 C  CG2 . THR   A 1 164 ? 8.83029   -25.63257 -30.06654 1.000 19.24435 ? 171 THR   A CG2 1 
ATOM   1205 N  N   . VAL   A 1 165 ? 6.89191   -22.22547 -32.23610 1.000 16.89043 ? 172 VAL   A N   1 
ATOM   1206 C  CA  . VAL   A 1 165 ? 5.77447   -21.55645 -32.89028 1.000 18.59898 ? 172 VAL   A CA  1 
ATOM   1207 C  C   . VAL   A 1 165 ? 5.30044   -22.44567 -34.02869 1.000 19.74712 ? 172 VAL   A C   1 
ATOM   1208 O  O   . VAL   A 1 165 ? 6.11414   -22.97353 -34.79253 1.000 20.91972 ? 172 VAL   A O   1 
ATOM   1209 C  CB  . VAL   A 1 165 ? 6.14915   -20.15391 -33.41584 1.000 19.41376 ? 172 VAL   A CB  1 
ATOM   1210 C  CG1 . VAL   A 1 165 ? 4.97014   -19.52144 -34.14577 1.000 21.18198 ? 172 VAL   A CG1 1 
ATOM   1211 C  CG2 . VAL   A 1 165 ? 6.59319   -19.24869 -32.28262 1.000 19.34678 ? 172 VAL   A CG2 1 
ATOM   1212 N  N   . ARG   A 1 166 ? 3.98443   -22.61678 -34.13824 1.000 19.59798 ? 173 ARG   A N   1 
ATOM   1213 C  CA  . ARG   A 1 166 ? 3.40776   -23.35506 -35.24885 1.000 20.30722 ? 173 ARG   A CA  1 
ATOM   1214 C  C   . ARG   A 1 166 ? 2.06815   -22.72837 -35.60303 1.000 19.37237 ? 173 ARG   A C   1 
ATOM   1215 O  O   . ARG   A 1 166 ? 1.43216   -22.08171 -34.77006 1.000 19.86176 ? 173 ARG   A O   1 
ATOM   1216 C  CB  . ARG   A 1 166 ? 3.21645   -24.83897 -34.90567 1.000 25.74008 ? 173 ARG   A CB  1 
ATOM   1217 C  CG  . ARG   A 1 166 ? 2.23274   -25.09053 -33.77322 1.000 27.91511 ? 173 ARG   A CG  1 
ATOM   1218 C  CD  . ARG   A 1 166 ? 2.39864   -26.48032 -33.18051 1.000 35.93172 ? 173 ARG   A CD  1 
ATOM   1219 N  NE  . ARG   A 1 166 ? 3.49801   -26.51949 -32.22178 1.000 40.74960 ? 173 ARG   A NE  1 
ATOM   1220 C  CZ  . ARG   A 1 166 ? 4.04185   -27.63047 -31.74304 1.000 46.33841 ? 173 ARG   A CZ  1 
ATOM   1221 N  NH1 . ARG   A 1 166 ? 3.60474   -28.82606 -32.10360 1.000 37.57161 ? 173 ARG   A NH1 1 
ATOM   1222 N  NH2 . ARG   A 1 166 ? 5.05256   -27.53923 -30.88300 1.000 41.27801 ? 173 ARG   A NH2 1 
ATOM   1223 N  N   . THR   A 1 167 ? 1.64585   -22.92175 -36.85114 1.000 22.60734 ? 174 THR   A N   1 
ATOM   1224 C  CA  . THR   A 1 167 ? 0.27158   -22.59265 -37.20375 1.000 21.61584 ? 174 THR   A CA  1 
ATOM   1225 C  C   . THR   A 1 167 ? -0.66663  -23.47588 -36.39462 1.000 27.62109 ? 174 THR   A C   1 
ATOM   1226 O  O   . THR   A 1 167 ? -0.41088  -24.66702 -36.20089 1.000 30.95449 ? 174 THR   A O   1 
ATOM   1227 C  CB  . THR   A 1 167 ? 0.03594   -22.80888 -38.69974 1.000 27.35691 ? 174 THR   A CB  1 
ATOM   1228 O  OG1 . THR   A 1 167 ? 1.01778   -22.08354 -39.44987 1.000 35.39942 ? 174 THR   A OG1 1 
ATOM   1229 C  CG2 . THR   A 1 167 ? -1.34980  -22.32169 -39.09537 1.000 34.42240 ? 174 THR   A CG2 1 
ATOM   1230 N  N   . ASP   A 1 168 ? -1.74298  -22.88347 -35.88808 1.000 25.47784 ? 175 ASP   A N   1 
ATOM   1231 C  CA  . ASP   A 1 168 ? -2.65337  -23.60024 -35.00876 1.000 26.57209 ? 175 ASP   A CA  1 
ATOM   1232 C  C   . ASP   A 1 168 ? -3.77828  -24.20002 -35.83966 1.000 35.11808 ? 175 ASP   A C   1 
ATOM   1233 O  O   . ASP   A 1 168 ? -4.50781  -23.47324 -36.52105 1.000 36.70964 ? 175 ASP   A O   1 
ATOM   1234 C  CB  . ASP   A 1 168 ? -3.21948  -22.67366 -33.93558 1.000 25.29379 ? 175 ASP   A CB  1 
ATOM   1235 C  CG  . ASP   A 1 168 ? -4.09257  -23.41019 -32.93872 1.000 37.71890 ? 175 ASP   A CG  1 
ATOM   1236 O  OD1 . ASP   A 1 168 ? -3.69673  -24.51353 -32.50460 1.000 39.45557 ? 175 ASP   A OD1 1 
ATOM   1237 O  OD2 . ASP   A 1 168 ? -5.17326  -22.89203 -32.59304 1.000 34.19701 ? 175 ASP   A OD2 1 
ATOM   1238 N  N   . THR   A 1 169 ? -3.90885  -25.52151 -35.78518 1.000 45.32742 ? 176 THR   A N   1 
ATOM   1239 C  CA  . THR   A 1 169 ? -4.99295  -26.23407 -36.44322 1.000 55.43916 ? 176 THR   A CA  1 
ATOM   1240 C  C   . THR   A 1 169 ? -6.20146  -26.42213 -35.53805 1.000 53.79580 ? 176 THR   A C   1 
ATOM   1241 O  O   . THR   A 1 169 ? -7.21932  -26.95896 -35.98985 1.000 53.65443 ? 176 THR   A O   1 
ATOM   1242 C  CB  . THR   A 1 169 ? -4.50034  -27.60212 -36.92715 1.000 56.91136 ? 176 THR   A CB  1 
ATOM   1243 O  OG1 . THR   A 1 169 ? -3.67141  -28.19490 -35.91724 1.000 55.73083 ? 176 THR   A OG1 1 
ATOM   1244 C  CG2 . THR   A 1 169 ? -3.70210  -27.45313 -38.21117 1.000 50.09801 ? 176 THR   A CG2 1 
ATOM   1245 N  N   . GLY   A 1 170 ? -6.11378  -25.99599 -34.28159 1.000 50.30215 ? 177 GLY   A N   1 
ATOM   1246 C  CA  . GLY   A 1 170 ? -7.19899  -26.15580 -33.34270 1.000 53.35606 ? 177 GLY   A CA  1 
ATOM   1247 C  C   . GLY   A 1 170 ? -8.38989  -25.27237 -33.66787 1.000 45.01594 ? 177 GLY   A C   1 
ATOM   1248 O  O   . GLY   A 1 170 ? -8.52918  -24.71853 -34.75441 1.000 44.17497 ? 177 GLY   A O   1 
ATOM   1249 N  N   . GLU   A 1 171 ? -9.25817  -25.14702 -32.67371 1.000 40.03552 ? 178 GLU   A N   1 
ATOM   1250 C  CA  . GLU   A 1 171 ? -10.51098 -24.41107 -32.79052 1.000 38.60812 ? 178 GLU   A CA  1 
ATOM   1251 C  C   . GLU   A 1 171 ? -10.25955 -22.95773 -33.17998 1.000 37.29688 ? 178 GLU   A C   1 
ATOM   1252 O  O   . GLU   A 1 171 ? -9.50773  -22.26264 -32.47971 1.000 30.48747 ? 178 GLU   A O   1 
ATOM   1253 C  CB  . GLU   A 1 171 ? -11.18798 -24.46465 -31.42208 1.000 42.75741 ? 178 GLU   A CB  1 
ATOM   1254 C  CG  . GLU   A 1 171 ? -12.69212 -24.33641 -31.45162 1.000 42.86887 ? 178 GLU   A CG  1 
ATOM   1255 C  CD  . GLU   A 1 171 ? -13.35064 -25.28987 -32.42961 1.000 41.14796 ? 178 GLU   A CD  1 
ATOM   1256 O  OE1 . GLU   A 1 171 ? -13.06830 -26.50739 -32.39460 1.000 40.31786 ? 178 GLU   A OE1 1 
ATOM   1257 O  OE2 . GLU   A 1 171 ? -14.14120 -24.80422 -33.25422 1.000 46.42370 ? 178 GLU   A OE2 1 
ATOM   1258 N  N   . PRO   A 1 172 ? -10.82118 -22.47533 -34.29036 1.000 34.56346 ? 179 PRO   A N   1 
ATOM   1259 C  CA  . PRO   A 1 172 ? -10.65712 -21.05985 -34.64025 1.000 35.55148 ? 179 PRO   A CA  1 
ATOM   1260 C  C   . PRO   A 1 172 ? -11.11512 -20.14229 -33.51255 1.000 37.67844 ? 179 PRO   A C   1 
ATOM   1261 O  O   . PRO   A 1 172 ? -12.09748 -20.41964 -32.82371 1.000 43.45228 ? 179 PRO   A O   1 
ATOM   1262 C  CB  . PRO   A 1 172 ? -11.57125 -20.91110 -35.85448 1.000 39.96032 ? 179 PRO   A CB  1 
ATOM   1263 C  CG  . PRO   A 1 172 ? -11.43178 -22.23097 -36.57000 1.000 46.61318 ? 179 PRO   A CG  1 
ATOM   1264 C  CD  . PRO   A 1 172 ? -11.07204 -23.27913 -35.50228 1.000 45.75467 ? 179 PRO   A CD  1 
ATOM   1265 N  N   . MET   A 1 173 ? -10.41107 -19.01389 -33.36520 1.000 28.02718 ? 180 MET   A N   1 
ATOM   1266 C  CA  . MET   A 1 173 ? -10.61378 -18.09964 -32.24884 1.000 29.39693 ? 180 MET   A CA  1 
ATOM   1267 C  C   . MET   A 1 173 ? -11.33538 -16.81693 -32.63681 1.000 39.78291 ? 180 MET   A C   1 
ATOM   1268 O  O   . MET   A 1 173 ? -11.90742 -16.17017 -31.75616 1.000 37.51540 ? 180 MET   A O   1 
ATOM   1269 C  CB  . MET   A 1 173 ? -9.25861  -17.69670 -31.65700 1.000 36.44401 ? 180 MET   A CB  1 
ATOM   1270 C  CG  . MET   A 1 173 ? -8.59819  -18.74376 -30.83618 1.000 43.77747 ? 180 MET   A CG  1 
ATOM   1271 S  SD  . MET   A 1 173 ? -6.99179  -18.10197 -30.40164 1.000 41.35356 ? 180 MET   A SD  1 
ATOM   1272 C  CE  . MET   A 1 173 ? -7.36949  -16.35598 -30.26374 1.000 33.73889 ? 180 MET   A CE  1 
ATOM   1273 N  N   . GLY   A 1 174 ? -11.32092 -16.42722 -33.90852 1.000 31.86011 ? 181 GLY   A N   1 
ATOM   1274 C  CA  . GLY   A 1 174 ? -11.88875 -15.15200 -34.30104 1.000 28.62062 ? 181 GLY   A CA  1 
ATOM   1275 C  C   . GLY   A 1 174 ? -10.87679 -14.03135 -34.16537 1.000 24.03622 ? 181 GLY   A C   1 
ATOM   1276 O  O   . GLY   A 1 174 ? -10.40138 -13.48902 -35.16879 1.000 23.62321 ? 181 GLY   A O   1 
ATOM   1277 N  N   . ARG   A 1 175 ? -10.53075 -13.69032 -32.92282 1.000 19.73501 ? 182 ARG   A N   1 
ATOM   1278 C  CA  . ARG   A 1 175 ? -9.52442  -12.68297 -32.61111 1.000 19.17838 ? 182 ARG   A CA  1 
ATOM   1279 C  C   . ARG   A 1 175 ? -9.25789  -12.71794 -31.11420 1.000 17.84282 ? 182 ARG   A C   1 
ATOM   1280 O  O   . ARG   A 1 175 ? -10.19585 -12.81964 -30.32062 1.000 21.16263 ? 182 ARG   A O   1 
ATOM   1281 C  CB  . ARG   A 1 175 ? -10.00813 -11.27524 -32.99695 1.000 18.97035 ? 182 ARG   A CB  1 
ATOM   1282 C  CG  . ARG   A 1 175 ? -8.93951  -10.18805 -32.81733 1.000 18.77522 ? 182 ARG   A CG  1 
ATOM   1283 C  CD  . ARG   A 1 175 ? -9.55188  -8.78986  -32.70804 1.000 18.41928 ? 182 ARG   A CD  1 
ATOM   1284 N  NE  . ARG   A 1 175 ? -10.44798 -8.67451  -31.56229 1.000 18.72242 ? 182 ARG   A NE  1 
ATOM   1285 C  CZ  . ARG   A 1 175 ? -11.76352 -8.53321  -31.64715 1.000 19.67397 ? 182 ARG   A CZ  1 
ATOM   1286 N  NH1 . ARG   A 1 175 ? -12.38544 -8.50366  -32.81726 1.000 19.37196 ? 182 ARG   A NH1 1 
ATOM   1287 N  NH2 . ARG   A 1 175 ? -12.48025 -8.44039  -30.52991 1.000 19.83523 ? 182 ARG   A NH2 1 
ATOM   1288 N  N   . GLY   A 1 176 ? -7.98366  -12.61628 -30.73490 1.000 19.30052 ? 183 GLY   A N   1 
ATOM   1289 C  CA  . GLY   A 1 176 ? -7.63537  -12.49006 -29.33818 1.000 17.98740 ? 183 GLY   A CA  1 
ATOM   1290 C  C   . GLY   A 1 176 ? -6.51588  -13.43459 -28.97250 1.000 17.88415 ? 183 GLY   A C   1 
ATOM   1291 O  O   . GLY   A 1 176 ? -5.73070  -13.86120 -29.82633 1.000 17.70254 ? 183 GLY   A O   1 
ATOM   1292 N  N   . THR   A 1 177 ? -6.43969  -13.76842 -27.68599 1.000 17.08123 ? 184 THR   A N   1 
ATOM   1293 C  CA  . THR   A 1 177 ? -5.34910  -14.57340 -27.15792 1.000 15.42175 ? 184 THR   A CA  1 
ATOM   1294 C  C   . THR   A 1 177 ? -5.86776  -15.49662 -26.06488 1.000 18.25872 ? 184 THR   A C   1 
ATOM   1295 O  O   . THR   A 1 177 ? -6.69623  -15.08867 -25.24685 1.000 17.37449 ? 184 THR   A O   1 
ATOM   1296 C  CB  . THR   A 1 177 ? -4.24513  -13.66416 -26.59780 1.000 17.70687 ? 184 THR   A CB  1 
ATOM   1297 O  OG1 . THR   A 1 177 ? -3.69219  -12.88006 -27.66238 1.000 20.28093 ? 184 THR   A OG1 1 
ATOM   1298 C  CG2 . THR   A 1 177 ? -3.12813  -14.48458 -25.95698 1.000 18.97703 ? 184 THR   A CG2 1 
ATOM   1299 N  N   . LYS   A 1 178 ? -5.37557  -16.74008 -26.07405 1.000 16.52480 ? 185 LYS   A N   1 
ATOM   1300 C  CA  . LYS   A 1 178 ? -5.61593  -17.74040 -25.03442 1.000 16.71269 ? 185 LYS   A CA  1 
ATOM   1301 C  C   . LYS   A 1 178 ? -4.27569  -18.13031 -24.42910 1.000 16.66327 ? 185 LYS   A C   1 
ATOM   1302 O  O   . LYS   A 1 178 ? -3.38422  -18.58869 -25.14913 1.000 17.87490 ? 185 LYS   A O   1 
ATOM   1303 C  CB  . LYS   A 1 178 ? -6.26479  -18.99279 -25.63251 1.000 22.16764 ? 185 LYS   A CB  1 
ATOM   1304 C  CG  . LYS   A 1 178 ? -7.73168  -18.82872 -25.93625 1.000 39.22268 ? 185 LYS   A CG  1 
ATOM   1305 C  CD  . LYS   A 1 178 ? -8.41988  -20.14994 -26.25582 1.000 38.96847 ? 185 LYS   A CD  1 
ATOM   1306 C  CE  . LYS   A 1 178 ? -7.47045  -21.11535 -26.94076 1.000 48.43648 ? 185 LYS   A CE  1 
ATOM   1307 N  NZ  . LYS   A 1 178 ? -8.15727  -22.36312 -27.37075 1.000 56.92104 ? 185 LYS   A NZ  1 
ATOM   1308 N  N   . VAL   A 1 179 ? -4.13529  -17.94735 -23.11788 1.000 17.13816 ? 186 VAL   A N   1 
ATOM   1309 C  CA  . VAL   A 1 179 ? -2.94295  -18.38792 -22.39884 1.000 15.55197 ? 186 VAL   A CA  1 
ATOM   1310 C  C   . VAL   A 1 179 ? -3.33671  -19.62765 -21.60920 1.000 17.48062 ? 186 VAL   A C   1 
ATOM   1311 O  O   . VAL   A 1 179 ? -4.17043  -19.54806 -20.69545 1.000 18.15040 ? 186 VAL   A O   1 
ATOM   1312 C  CB  . VAL   A 1 179 ? -2.39825  -17.29419 -21.46957 1.000 16.23987 ? 186 VAL   A CB  1 
ATOM   1313 C  CG1 . VAL   A 1 179 ? -1.22643  -17.84080 -20.63259 1.000 17.41720 ? 186 VAL   A CG1 1 
ATOM   1314 C  CG2 . VAL   A 1 179 ? -1.98776  -16.07071 -22.27317 1.000 18.50347 ? 186 VAL   A CG2 1 
ATOM   1315 N  N   . ILE   A 1 180 ? -2.76195  -20.77059 -21.97758 1.000 16.66422 ? 187 ILE   A N   1 
ATOM   1316 C  CA  . ILE   A 1 180 ? -3.06531  -22.05614 -21.35393 1.000 15.20506 ? 187 ILE   A CA  1 
ATOM   1317 C  C   . ILE   A 1 180 ? -1.92904  -22.37214 -20.39054 1.000 15.30613 ? 187 ILE   A C   1 
ATOM   1318 O  O   . ILE   A 1 180 ? -0.78970  -22.59227 -20.81281 1.000 16.63451 ? 187 ILE   A O   1 
ATOM   1319 C  CB  . ILE   A 1 180 ? -3.21675  -23.16590 -22.40187 1.000 17.66471 ? 187 ILE   A CB  1 
ATOM   1320 C  CG1 . ILE   A 1 180 ? -4.24397  -22.76979 -23.46866 1.000 18.92998 ? 187 ILE   A CG1 1 
ATOM   1321 C  CG2 . ILE   A 1 180 ? -3.58061  -24.49435 -21.73987 1.000 18.99897 ? 187 ILE   A CG2 1 
ATOM   1322 C  CD1 . ILE   A 1 180 ? -4.27634  -23.72156 -24.65164 1.000 22.76714 ? 187 ILE   A CD1 1 
ATOM   1323 N  N   . LEU   A 1 181 ? -2.22976  -22.39916 -19.09498 1.000 14.55543 ? 188 LEU   A N   1 
ATOM   1324 C  CA  . LEU   A 1 181 ? -1.23419  -22.69343 -18.06959 1.000 15.58884 ? 188 LEU   A CA  1 
ATOM   1325 C  C   . LEU   A 1 181 ? -1.34186  -24.16789 -17.70149 1.000 17.86153 ? 188 LEU   A C   1 
ATOM   1326 O  O   . LEU   A 1 181 ? -2.34298  -24.59529 -17.11848 1.000 18.20461 ? 188 LEU   A O   1 
ATOM   1327 C  CB  . LEU   A 1 181 ? -1.46784  -21.82637 -16.83492 1.000 15.40803 ? 188 LEU   A CB  1 
ATOM   1328 C  CG  . LEU   A 1 181 ? -1.54439  -20.32696 -17.08774 1.000 18.42355 ? 188 LEU   A CG  1 
ATOM   1329 C  CD1 . LEU   A 1 181 ? -1.95073  -19.62682 -15.80249 1.000 21.02974 ? 188 LEU   A CD1 1 
ATOM   1330 C  CD2 . LEU   A 1 181 ? -0.22925  -19.79851 -17.60476 1.000 21.49028 ? 188 LEU   A CD2 1 
ATOM   1331 N  N   . HIS   A 1 182 ? -0.30954  -24.94438 -18.03132 1.000 19.23125 ? 189 HIS   A N   1 
ATOM   1332 C  CA  . HIS   A 1 182 ? -0.22701  -26.34499 -17.61942 1.000 18.30509 ? 189 HIS   A CA  1 
ATOM   1333 C  C   . HIS   A 1 182 ? 0.40606   -26.33370 -16.23445 1.000 18.58670 ? 189 HIS   A C   1 
ATOM   1334 O  O   . HIS   A 1 182 ? 1.61732   -26.17064 -16.09495 1.000 20.01327 ? 189 HIS   A O   1 
ATOM   1335 C  CB  . HIS   A 1 182 ? 0.58681   -27.15029 -18.62956 1.000 17.52280 ? 189 HIS   A CB  1 
ATOM   1336 C  CG  . HIS   A 1 182 ? 0.09145   -27.02496 -20.04053 1.000 22.26007 ? 189 HIS   A CG  1 
ATOM   1337 N  ND1 . HIS   A 1 182 ? -0.73335  -27.96081 -20.62835 1.000 27.48642 ? 189 HIS   A ND1 1 
ATOM   1338 C  CD2 . HIS   A 1 182 ? 0.28334   -26.05739 -20.96913 1.000 22.73650 ? 189 HIS   A CD2 1 
ATOM   1339 C  CE1 . HIS   A 1 182 ? -1.01760  -27.58124 -21.86257 1.000 26.94645 ? 189 HIS   A CE1 1 
ATOM   1340 N  NE2 . HIS   A 1 182 ? -0.40951  -26.43155 -22.09629 1.000 26.61732 ? 189 HIS   A NE2 1 
ATOM   1341 N  N   . LEU   A 1 183 ? -0.42239  -26.46857 -15.20444 1.000 18.03568 ? 190 LEU   A N   1 
ATOM   1342 C  CA  . LEU   A 1 183 ? 0.01615   -26.15513 -13.84850 1.000 19.22561 ? 190 LEU   A CA  1 
ATOM   1343 C  C   . LEU   A 1 183 ? 0.96192   -27.20670 -13.28113 1.000 22.66166 ? 190 LEU   A C   1 
ATOM   1344 O  O   . LEU   A 1 183 ? 0.86394   -28.40066 -13.58050 1.000 23.95619 ? 190 LEU   A O   1 
ATOM   1345 C  CB  . LEU   A 1 183 ? -1.19073  -26.01469 -12.92131 1.000 20.11599 ? 190 LEU   A CB  1 
ATOM   1346 C  CG  . LEU   A 1 183 ? -2.13375  -24.85587 -13.23953 1.000 17.96144 ? 190 LEU   A CG  1 
ATOM   1347 C  CD1 . LEU   A 1 183 ? -3.29256  -24.83582 -12.25185 1.000 22.23917 ? 190 LEU   A CD1 1 
ATOM   1348 C  CD2 . LEU   A 1 183 ? -1.38558  -23.54147 -13.19206 1.000 21.87658 ? 190 LEU   A CD2 1 
ATOM   1349 N  N   . LYS   A 1 184 ? 1.88358   -26.73961 -12.43825 1.000 21.32091 ? 191 LYS   A N   1 
ATOM   1350 C  CA  . LYS   A 1 184 ? 2.71119   -27.63813 -11.64823 1.000 23.17276 ? 191 LYS   A CA  1 
ATOM   1351 C  C   . LYS   A 1 184 ? 1.83530   -28.46911 -10.71653 1.000 25.52328 ? 191 LYS   A C   1 
ATOM   1352 O  O   . LYS   A 1 184 ? 0.75056   -28.04532 -10.30468 1.000 24.52628 ? 191 LYS   A O   1 
ATOM   1353 C  CB  . LYS   A 1 184 ? 3.72088   -26.83924 -10.81937 1.000 23.70797 ? 191 LYS   A CB  1 
ATOM   1354 C  CG  . LYS   A 1 184 ? 4.79537   -26.12178 -11.63161 1.000 28.18074 ? 191 LYS   A CG  1 
ATOM   1355 C  CD  . LYS   A 1 184 ? 5.44164   -25.00762 -10.80489 1.000 30.15269 ? 191 LYS   A CD  1 
ATOM   1356 C  CE  . LYS   A 1 184 ? 6.40070   -24.16942 -11.63241 1.000 35.73295 ? 191 LYS   A CE  1 
ATOM   1357 N  NZ  . LYS   A 1 184 ? 7.27154   -23.28671 -10.79417 1.000 37.76279 ? 191 LYS   A NZ  1 
ATOM   1358 N  N   . GLU   A 1 185 ? 2.32581   -29.66738 -10.38529 1.000 27.27101 ? 192 GLU   A N   1 
ATOM   1359 C  CA  . GLU   A 1 185 ? 1.55489   -30.61358 -9.58275  1.000 32.33113 ? 192 GLU   A CA  1 
ATOM   1360 C  C   . GLU   A 1 185 ? 1.11040   -30.01753 -8.25550  1.000 29.09844 ? 192 GLU   A C   1 
ATOM   1361 O  O   . GLU   A 1 185 ? 0.02065   -30.33920 -7.76625  1.000 32.66934 ? 192 GLU   A O   1 
ATOM   1362 C  CB  . GLU   A 1 185 ? 2.39597   -31.86054 -9.31388  1.000 35.20398 ? 192 GLU   A CB  1 
ATOM   1363 C  CG  . GLU   A 1 185 ? 1.61134   -33.15287 -9.25593  1.000 52.40696 ? 192 GLU   A CG  1 
ATOM   1364 C  CD  . GLU   A 1 185 ? 2.50923   -34.35025 -9.01904  1.000 64.59871 ? 192 GLU   A CD  1 
ATOM   1365 O  OE1 . GLU   A 1 185 ? 3.69963   -34.14164 -8.70246  1.000 62.39485 ? 192 GLU   A OE1 1 
ATOM   1366 O  OE2 . GLU   A 1 185 ? 2.02631   -35.49566 -9.14018  1.000 74.67328 ? 192 GLU   A OE2 1 
ATOM   1367 N  N   . ASP   A 1 186 ? 1.93588   -29.17088 -7.64820  1.000 26.27314 ? 193 ASP   A N   1 
ATOM   1368 C  CA  . ASP   A 1 186 ? 1.64030   -28.62095 -6.33294  1.000 27.50406 ? 193 ASP   A CA  1 
ATOM   1369 C  C   . ASP   A 1 186 ? 0.95505   -27.26037 -6.39308  1.000 26.82042 ? 193 ASP   A C   1 
ATOM   1370 O  O   . ASP   A 1 186 ? 0.83841   -26.59212 -5.36069  1.000 26.66400 ? 193 ASP   A O   1 
ATOM   1371 C  CB  . ASP   A 1 186 ? 2.90842   -28.57251 -5.47586  1.000 32.02325 ? 193 ASP   A CB  1 
ATOM   1372 C  CG  . ASP   A 1 186 ? 3.93377   -27.59174 -6.00268  1.000 34.95182 ? 193 ASP   A CG  1 
ATOM   1373 O  OD1 . ASP   A 1 186 ? 3.86271   -27.23161 -7.19733  1.000 40.62468 ? 193 ASP   A OD1 1 
ATOM   1374 O  OD2 . ASP   A 1 186 ? 4.82139   -27.18754 -5.22354  1.000 45.24040 ? 193 ASP   A OD2 1 
ATOM   1375 N  N   . GLN   A 1 187 ? 0.48109   -26.84855 -7.56916  1.000 23.04836 ? 194 GLN   A N   1 
ATOM   1376 C  CA  . GLN   A 1 187 ? -0.14763  -25.54714 -7.75778  1.000 23.14185 ? 194 GLN   A CA  1 
ATOM   1377 C  C   . GLN   A 1 187 ? -1.60098  -25.68141 -8.20435  1.000 20.73230 ? 194 GLN   A C   1 
ATOM   1378 O  O   . GLN   A 1 187 ? -2.14609  -24.78375 -8.85087  1.000 21.59793 ? 194 GLN   A O   1 
ATOM   1379 C  CB  . GLN   A 1 187 ? 0.65423   -24.68628 -8.73568  1.000 23.46242 ? 194 GLN   A CB  1 
ATOM   1380 C  CG  . GLN   A 1 187 ? 2.09737   -24.43579 -8.29541  1.000 23.17649 ? 194 GLN   A CG  1 
ATOM   1381 C  CD  . GLN   A 1 187 ? 2.19740   -23.75445 -6.94118  1.000 28.71470 ? 194 GLN   A CD  1 
ATOM   1382 O  OE1 . GLN   A 1 187 ? 1.40936   -22.86343 -6.62060  1.000 28.34842 ? 194 GLN   A OE1 1 
ATOM   1383 N  NE2 . GLN   A 1 187 ? 3.18658   -24.15608 -6.14746  1.000 29.21426 ? 194 GLN   A NE2 1 
ATOM   1384 N  N   . THR   A 1 188 ? -2.24965  -26.79165 -7.85022  1.000 23.68319 ? 195 THR   A N   1 
ATOM   1385 C  CA  . THR   A 1 188 ? -3.61682  -27.02198 -8.30765  1.000 25.01301 ? 195 THR   A CA  1 
ATOM   1386 C  C   . THR   A 1 188 ? -4.66163  -26.20907 -7.55277  1.000 26.70023 ? 195 THR   A C   1 
ATOM   1387 O  O   . THR   A 1 188 ? -5.84295  -26.27447 -7.91298  1.000 26.65242 ? 195 THR   A O   1 
ATOM   1388 C  CB  . THR   A 1 188 ? -3.97352  -28.51231 -8.27293  1.000 26.04091 ? 195 THR   A CB  1 
ATOM   1389 O  OG1 . THR   A 1 188 ? -3.87936  -29.00243 -6.92969  1.000 31.45892 ? 195 THR   A OG1 1 
ATOM   1390 C  CG2 . THR   A 1 188 ? -3.04425  -29.30625 -9.18066  1.000 28.98162 ? 195 THR   A CG2 1 
ATOM   1391 N  N   . GLU   A 1 189 ? -4.27081  -25.44659 -6.52723  1.000 24.39382 ? 196 GLU   A N   1 
ATOM   1392 C  CA  . GLU   A 1 189 ? -5.23409  -24.56453 -5.87472  1.000 23.14877 ? 196 GLU   A CA  1 
ATOM   1393 C  C   . GLU   A 1 189 ? -5.79834  -23.53666 -6.84648  1.000 23.05591 ? 196 GLU   A C   1 
ATOM   1394 O  O   . GLU   A 1 189 ? -6.90776  -23.03552 -6.64314  1.000 23.21078 ? 196 GLU   A O   1 
ATOM   1395 C  CB  . GLU   A 1 189 ? -4.59947  -23.85256 -4.67967  1.000 23.77956 ? 196 GLU   A CB  1 
ATOM   1396 C  CG  . GLU   A 1 189 ? -3.54475  -22.82728 -5.05967  1.000 24.15153 ? 196 GLU   A CG  1 
ATOM   1397 C  CD  . GLU   A 1 189 ? -2.75665  -22.35331 -3.86090  1.000 28.61780 ? 196 GLU   A CD  1 
ATOM   1398 O  OE1 . GLU   A 1 189 ? -1.83343  -23.08036 -3.43286  1.000 31.52186 ? 196 GLU   A OE1 1 
ATOM   1399 O  OE2 . GLU   A 1 189 ? -3.06811  -21.26231 -3.33709  1.000 29.77557 ? 196 GLU   A OE2 1 
ATOM   1400 N  N   . TYR   A 1 190 ? -5.05831  -23.20889 -7.90147  1.000 21.33145 ? 197 TYR   A N   1 
ATOM   1401 C  CA  . TYR   A 1 190 ? -5.49362  -22.21466 -8.87266  1.000 18.57904 ? 197 TYR   A CA  1 
ATOM   1402 C  C   . TYR   A 1 190 ? -6.50441  -22.76392 -9.86552  1.000 22.58000 ? 197 TYR   A C   1 
ATOM   1403 O  O   . TYR   A 1 190 ? -6.86866  -22.06161 -10.81549 1.000 21.44016 ? 197 TYR   A O   1 
ATOM   1404 C  CB  . TYR   A 1 190 ? -4.27578  -21.58183 -9.55830  1.000 19.97088 ? 197 TYR   A CB  1 
ATOM   1405 C  CG  . TYR   A 1 190 ? -3.36836  -20.95249 -8.53144  1.000 19.17984 ? 197 TYR   A CG  1 
ATOM   1406 C  CD1 . TYR   A 1 190 ? -3.78201  -19.83697 -7.81490  1.000 20.91023 ? 197 TYR   A CD1 1 
ATOM   1407 C  CD2 . TYR   A 1 190 ? -2.12838  -21.50797 -8.22055  1.000 21.95848 ? 197 TYR   A CD2 1 
ATOM   1408 C  CE1 . TYR   A 1 190 ? -2.98047  -19.26581 -6.84340  1.000 23.34564 ? 197 TYR   A CE1 1 
ATOM   1409 C  CE2 . TYR   A 1 190 ? -1.31336  -20.94029 -7.24648  1.000 22.68348 ? 197 TYR   A CE2 1 
ATOM   1410 C  CZ  . TYR   A 1 190 ? -1.74638  -19.81526 -6.55649  1.000 21.72491 ? 197 TYR   A CZ  1 
ATOM   1411 O  OH  . TYR   A 1 190 ? -0.96164  -19.23442 -5.58090  1.000 24.41319 ? 197 TYR   A OH  1 
ATOM   1412 N  N   . LEU   A 1 191 ? -6.95956  -23.99878 -9.65806  1.000 20.41778 ? 198 LEU   A N   1 
ATOM   1413 C  CA  . LEU   A 1 191 ? -8.09870  -24.55267 -10.37172 1.000 20.91624 ? 198 LEU   A CA  1 
ATOM   1414 C  C   . LEU   A 1 191 ? -9.37204  -24.53142 -9.54008  1.000 23.94139 ? 198 LEU   A C   1 
ATOM   1415 O  O   . LEU   A 1 191 ? -10.43739 -24.87698 -10.06010 1.000 25.26870 ? 198 LEU   A O   1 
ATOM   1416 C  CB  . LEU   A 1 191 ? -7.80974  -26.00162 -10.78328 1.000 23.43861 ? 198 LEU   A CB  1 
ATOM   1417 C  CG  . LEU   A 1 191 ? -6.61400  -26.19922 -11.71203 1.000 22.10606 ? 198 LEU   A CG  1 
ATOM   1418 C  CD1 . LEU   A 1 191 ? -6.40647  -27.67452 -12.02892 1.000 28.87591 ? 198 LEU   A CD1 1 
ATOM   1419 C  CD2 . LEU   A 1 191 ? -6.79889  -25.38114 -12.98268 1.000 25.37606 ? 198 LEU   A CD2 1 
ATOM   1420 N  N   . GLU   A 1 192 ? -9.28842  -24.16459 -8.26216  1.000 21.02969 ? 199 GLU   A N   1 
ATOM   1421 C  CA  . GLU   A 1 192 ? -10.44416 -24.18010 -7.37599  1.000 23.43110 ? 199 GLU   A CA  1 
ATOM   1422 C  C   . GLU   A 1 192 ? -11.21140 -22.86974 -7.49086  1.000 26.99413 ? 199 GLU   A C   1 
ATOM   1423 O  O   . GLU   A 1 192 ? -10.61838 -21.78566 -7.46832  1.000 23.39792 ? 199 GLU   A O   1 
ATOM   1424 C  CB  . GLU   A 1 192 ? -10.01037 -24.41988 -5.93023  1.000 27.72386 ? 199 GLU   A CB  1 
ATOM   1425 C  CG  . GLU   A 1 192 ? -9.25485  -25.72566 -5.72695  1.000 32.20615 ? 199 GLU   A CG  1 
ATOM   1426 C  CD  . GLU   A 1 192 ? -8.99713  -26.03064 -4.26463  1.000 65.65865 ? 199 GLU   A CD  1 
ATOM   1427 O  OE1 . GLU   A 1 192 ? -7.88607  -26.50091 -3.93879  1.000 75.01342 ? 199 GLU   A OE1 1 
ATOM   1428 O  OE2 . GLU   A 1 192 ? -9.90649  -25.79886 -3.43959  1.000 71.77684 ? 199 GLU   A OE2 1 
ATOM   1429 N  N   . GLU   A 1 193 ? -12.53483 -22.97677 -7.61278  1.000 23.36535 ? 200 GLU   A N   1 
ATOM   1430 C  CA  . GLU   A 1 193 ? -13.35087 -21.80036 -7.88040  1.000 23.14653 ? 200 GLU   A CA  1 
ATOM   1431 C  C   . GLU   A 1 193 ? -13.17464 -20.73911 -6.79668  1.000 20.12081 ? 200 GLU   A C   1 
ATOM   1432 O  O   . GLU   A 1 193 ? -13.01957 -19.55210 -7.10319  1.000 22.32985 ? 200 GLU   A O   1 
ATOM   1433 C  CB  . GLU   A 1 193 ? -14.81865 -22.21277 -8.00621  1.000 25.45844 ? 200 GLU   A CB  1 
ATOM   1434 C  CG  . GLU   A 1 193 ? -15.74712 -21.07820 -8.38660  1.000 34.68866 ? 200 GLU   A CG  1 
ATOM   1435 C  CD  . GLU   A 1 193 ? -17.21302 -21.48043 -8.38554  1.000 54.47273 ? 200 GLU   A CD  1 
ATOM   1436 O  OE1 . GLU   A 1 193 ? -17.52547 -22.61772 -7.97331  1.000 49.59307 ? 200 GLU   A OE1 1 
ATOM   1437 O  OE2 . GLU   A 1 193 ? -18.05350 -20.65994 -8.81059  1.000 45.67017 ? 200 GLU   A OE2 1 
ATOM   1438 N  N   . ARG   A 1 194 ? -13.18969 -21.14099 -5.52201  1.000 23.69930 ? 201 ARG   A N   1 
ATOM   1439 C  CA  . ARG   A 1 194 ? -13.12210 -20.13279 -4.46862  1.000 23.11233 ? 201 ARG   A CA  1 
ATOM   1440 C  C   . ARG   A 1 194 ? -11.77096 -19.43261 -4.45051  1.000 22.17435 ? 201 ARG   A C   1 
ATOM   1441 O  O   . ARG   A 1 194 ? -11.69397 -18.25363 -4.08899  1.000 22.37127 ? 201 ARG   A O   1 
ATOM   1442 C  CB  . ARG   A 1 194 ? -13.43501 -20.72941 -3.09778  1.000 29.70707 ? 201 ARG   A CB  1 
ATOM   1443 C  CG  . ARG   A 1 194 ? -12.66178 -21.97539 -2.74479  1.000 35.43756 ? 201 ARG   A CG  1 
ATOM   1444 C  CD  . ARG   A 1 194 ? -13.02149 -22.40573 -1.33004  1.000 36.74032 ? 201 ARG   A CD  1 
ATOM   1445 N  NE  . ARG   A 1 194 ? -12.02245 -23.28989 -0.74443  1.000 44.46762 ? 201 ARG   A NE  1 
ATOM   1446 C  CZ  . ARG   A 1 194 ? -12.19680 -23.95486 0.38916   1.000 37.27628 ? 201 ARG   A CZ  1 
ATOM   1447 N  NH1 . ARG   A 1 194 ? -13.31630 -23.84859 1.08531   1.000 44.36838 ? 201 ARG   A NH1 1 
ATOM   1448 N  NH2 . ARG   A 1 194 ? -11.22203 -24.74076 0.83692   1.000 51.59710 ? 201 ARG   A NH2 1 
ATOM   1449 N  N   . ARG   A 1 195 ? -10.70395 -20.13696 -4.83677  1.000 20.49196 ? 202 ARG   A N   1 
ATOM   1450 C  CA  . ARG   A 1 195 ? -9.38183  -19.51885 -4.85960  1.000 20.90067 ? 202 ARG   A CA  1 
ATOM   1451 C  C   . ARG   A 1 195 ? -9.26922  -18.51061 -5.99564  1.000 20.55868 ? 202 ARG   A C   1 
ATOM   1452 O  O   . ARG   A 1 195 ? -8.75696  -17.40215 -5.80025  1.000 19.62183 ? 202 ARG   A O   1 
ATOM   1453 C  CB  . ARG   A 1 195 ? -8.30260  -20.59962 -4.96852  1.000 21.25071 ? 202 ARG   A CB  1 
ATOM   1454 C  CG  . ARG   A 1 195 ? -6.86374  -20.08782 -4.95898  1.000 21.30150 ? 202 ARG   A CG  1 
ATOM   1455 C  CD  . ARG   A 1 195 ? -6.46561  -19.53900 -3.59570  1.000 23.45594 ? 202 ARG   A CD  1 
ATOM   1456 N  NE  . ARG   A 1 195 ? -5.02964  -19.28898 -3.51504  1.000 23.58296 ? 202 ARG   A NE  1 
ATOM   1457 C  CZ  . ARG   A 1 195 ? -4.47376  -18.10141 -3.30880  1.000 22.86796 ? 202 ARG   A CZ  1 
ATOM   1458 N  NH1 . ARG   A 1 195 ? -5.20482  -17.01768 -3.10811  1.000 23.55846 ? 202 ARG   A NH1 1 
ATOM   1459 N  NH2 . ARG   A 1 195 ? -3.14766  -18.00027 -3.30055  1.000 23.17163 ? 202 ARG   A NH2 1 
ATOM   1460 N  N   . ILE   A 1 196 ? -9.75574  -18.87132 -7.18778  1.000 18.43991 ? 203 ILE   A N   1 
ATOM   1461 C  CA  . ILE   A 1 196 ? -9.72241  -17.94531 -8.31759  1.000 18.27421 ? 203 ILE   A CA  1 
ATOM   1462 C  C   . ILE   A 1 196 ? -10.55354 -16.70687 -8.01370  1.000 17.94007 ? 203 ILE   A C   1 
ATOM   1463 O  O   . ILE   A 1 196 ? -10.11474 -15.57240 -8.24049  1.000 19.49831 ? 203 ILE   A O   1 
ATOM   1464 C  CB  . ILE   A 1 196 ? -10.18532 -18.64218 -9.61143  1.000 18.33796 ? 203 ILE   A CB  1 
ATOM   1465 C  CG1 . ILE   A 1 196 ? -9.27430  -19.82080 -9.96191  1.000 20.41422 ? 203 ILE   A CG1 1 
ATOM   1466 C  CG2 . ILE   A 1 196 ? -10.24344 -17.63815 -10.75719 1.000 20.60961 ? 203 ILE   A CG2 1 
ATOM   1467 C  CD1 . ILE   A 1 196 ? -9.91658  -20.79893 -10.94703 1.000 21.68961 ? 203 ILE   A CD1 1 
ATOM   1468 N  N   . LYS   A 1 197 ? -11.76859 -16.90388 -7.47849  1.000 19.35712 ? 204 LYS   A N   1 
ATOM   1469 C  CA  . LYS   A 1 197 ? -12.61917 -15.77124 -7.12357  1.000 18.49043 ? 204 LYS   A CA  1 
ATOM   1470 C  C   . LYS   A 1 197 ? -11.91978 -14.83634 -6.15172  1.000 18.25282 ? 204 LYS   A C   1 
ATOM   1471 O  O   . LYS   A 1 197 ? -11.99313 -13.61121 -6.29602  1.000 21.27832 ? 204 LYS   A O   1 
ATOM   1472 C  CB  . LYS   A 1 197 ? -13.93015 -16.24728 -6.49366  1.000 21.82368 ? 204 LYS   A CB  1 
ATOM   1473 C  CG  . LYS   A 1 197 ? -14.97321 -16.73123 -7.46577  1.000 29.18487 ? 204 LYS   A CG  1 
ATOM   1474 C  CD  . LYS   A 1 197 ? -16.29937 -16.91942 -6.73809  1.000 39.97641 ? 204 LYS   A CD  1 
ATOM   1475 C  CE  . LYS   A 1 197 ? -17.05512 -18.11979 -7.25803  1.000 47.25344 ? 204 LYS   A CE  1 
ATOM   1476 N  NZ  . LYS   A 1 197 ? -18.27040 -18.42718 -6.45288  1.000 53.24765 ? 204 LYS   A NZ  1 
ATOM   1477 N  N   . GLU   A 1 198 ? -11.25648 -15.40239 -5.13862  1.000 18.92628 ? 205 GLU   A N   1 
ATOM   1478 C  CA  . GLU   A 1 198 ? -10.55681 -14.58757 -4.15129  1.000 19.56136 ? 205 GLU   A CA  1 
ATOM   1479 C  C   . GLU   A 1 198 ? -9.46924  -13.74694 -4.80786  1.000 19.38733 ? 205 GLU   A C   1 
ATOM   1480 O  O   . GLU   A 1 198 ? -9.32161  -12.55901 -4.50127  1.000 19.70482 ? 205 GLU   A O   1 
ATOM   1481 C  CB  . GLU   A 1 198 ? -9.95319  -15.49972 -3.08397  1.000 20.41294 ? 205 GLU   A CB  1 
ATOM   1482 C  CG  . GLU   A 1 198 ? -9.07092  -14.79587 -2.06021  1.000 21.41563 ? 205 GLU   A CG  1 
ATOM   1483 C  CD  . GLU   A 1 198 ? -8.35518  -15.77734 -1.15293  1.000 25.28690 ? 205 GLU   A CD  1 
ATOM   1484 O  OE1 . GLU   A 1 198 ? -7.76293  -16.73639 -1.69344  1.000 25.31103 ? 205 GLU   A OE1 1 
ATOM   1485 O  OE2 . GLU   A 1 198 ? -8.37092  -15.58571 0.08273   1.000 25.99469 ? 205 GLU   A OE2 1 
ATOM   1486 N  N   . ILE   A 1 199 ? -8.70770  -14.34830 -5.71903  1.000 16.98458 ? 206 ILE   A N   1 
ATOM   1487 C  CA  . ILE   A 1 199 ? -7.61721  -13.63124 -6.37232  1.000 18.99891 ? 206 ILE   A CA  1 
ATOM   1488 C  C   . ILE   A 1 199 ? -8.15221  -12.52193 -7.27049  1.000 18.67021 ? 206 ILE   A C   1 
ATOM   1489 O  O   . ILE   A 1 199 ? -7.60546  -11.41216 -7.30162  1.000 20.88057 ? 206 ILE   A O   1 
ATOM   1490 C  CB  . ILE   A 1 199 ? -6.73370  -14.62577 -7.14278  1.000 19.81850 ? 206 ILE   A CB  1 
ATOM   1491 C  CG1 . ILE   A 1 199 ? -6.09503  -15.62008 -6.17485  1.000 22.13023 ? 206 ILE   A CG1 1 
ATOM   1492 C  CG2 . ILE   A 1 199 ? -5.68610  -13.89897 -7.96612  1.000 19.68089 ? 206 ILE   A CG2 1 
ATOM   1493 C  CD1 . ILE   A 1 199 ? -5.55991  -16.84927 -6.86321  1.000 22.50264 ? 206 ILE   A CD1 1 
ATOM   1494 N  N   . VAL   A 1 200 ? -9.20697  -12.80738 -8.03641  1.000 18.37823 ? 207 VAL   A N   1 
ATOM   1495 C  CA  . VAL   A 1 200 ? -9.78453  -11.79125 -8.90900  1.000 17.06909 ? 207 VAL   A CA  1 
ATOM   1496 C  C   . VAL   A 1 200 ? -10.31054 -10.61626 -8.09694  1.000 20.28501 ? 207 VAL   A C   1 
ATOM   1497 O  O   . VAL   A 1 200 ? -10.08804 -9.45142  -8.44742  1.000 20.98193 ? 207 VAL   A O   1 
ATOM   1498 C  CB  . VAL   A 1 200 ? -10.86999 -12.41817 -9.79875  1.000 17.64896 ? 207 VAL   A CB  1 
ATOM   1499 C  CG1 . VAL   A 1 200 ? -11.62958 -11.33710 -10.55729 1.000 21.94616 ? 207 VAL   A CG1 1 
ATOM   1500 C  CG2 . VAL   A 1 200 ? -10.22967 -13.40351 -10.76189 1.000 19.23015 ? 207 VAL   A CG2 1 
ATOM   1501 N  N   . LYS   A 1 201 ? -10.99495 -10.89830 -6.98562  1.000 19.41908 ? 208 LYS   A N   1 
ATOM   1502 C  CA  . LYS   A 1 201 ? -11.53313 -9.82226  -6.15974  1.000 20.69490 ? 208 LYS   A CA  1 
ATOM   1503 C  C   . LYS   A 1 201 ? -10.41717 -9.00181  -5.52084  1.000 20.97810 ? 208 LYS   A C   1 
ATOM   1504 O  O   . LYS   A 1 201 ? -10.53369 -7.77894  -5.38945  1.000 27.70452 ? 208 LYS   A O   1 
ATOM   1505 C  CB  . LYS   A 1 201 ? -12.46055 -10.40891 -5.09156  1.000 22.77673 ? 208 LYS   A CB  1 
ATOM   1506 C  CG  . LYS   A 1 201 ? -13.11300 -9.39267  -4.17656  1.000 29.69986 ? 208 LYS   A CG  1 
ATOM   1507 C  CD  . LYS   A 1 201 ? -13.90502 -10.09241 -3.08356  1.000 36.83020 ? 208 LYS   A CD  1 
ATOM   1508 C  CE  . LYS   A 1 201 ? -14.52618 -9.09742  -2.12149  1.000 42.77327 ? 208 LYS   A CE  1 
ATOM   1509 N  NZ  . LYS   A 1 201 ? -15.58869 -9.73135  -1.29476  1.000 55.06639 ? 208 LYS   A NZ  1 
ATOM   1510 N  N   . LYS   A 1 202 ? -9.32776  -9.66051  -5.11932  1.000 22.10545 ? 209 LYS   A N   1 
ATOM   1511 C  CA  . LYS   A 1 202 ? -8.23767  -8.96848  -4.43630  1.000 23.00939 ? 209 LYS   A CA  1 
ATOM   1512 C  C   . LYS   A 1 202 ? -7.44177  -8.07595  -5.38570  1.000 22.52245 ? 209 LYS   A C   1 
ATOM   1513 O  O   . LYS   A 1 202 ? -7.07465  -6.95107  -5.02470  1.000 24.87872 ? 209 LYS   A O   1 
ATOM   1514 C  CB  . LYS   A 1 202 ? -7.31582  -9.99939  -3.78489  1.000 24.55627 ? 209 LYS   A CB  1 
ATOM   1515 C  CG  . LYS   A 1 202 ? -6.11375  -9.41205  -3.06197  1.000 28.03515 ? 209 LYS   A CG  1 
ATOM   1516 C  CD  . LYS   A 1 202 ? -5.31612  -10.50871 -2.37775  1.000 34.59945 ? 209 LYS   A CD  1 
ATOM   1517 C  CE  . LYS   A 1 202 ? -4.12000  -9.94598  -1.63139  1.000 42.91036 ? 209 LYS   A CE  1 
ATOM   1518 N  NZ  . LYS   A 1 202 ? -3.36078  -11.01763 -0.92884  1.000 49.20045 ? 209 LYS   A NZ  1 
ATOM   1519 N  N   . HIS   A 1 203 ? -7.15851  -8.55623  -6.59819  1.000 21.02406 ? 210 HIS   A N   1 
ATOM   1520 C  CA  . HIS   A 1 203 ? -6.17680  -7.91477  -7.46462  1.000 24.22548 ? 210 HIS   A CA  1 
ATOM   1521 C  C   . HIS   A 1 203 ? -6.73060  -7.33279  -8.75837  1.000 23.72721 ? 210 HIS   A C   1 
ATOM   1522 O  O   . HIS   A 1 203 ? -6.03134  -6.53589  -9.39681  1.000 27.22451 ? 210 HIS   A O   1 
ATOM   1523 C  CB  . HIS   A 1 203 ? -5.05790  -8.90371  -7.83291  1.000 25.92906 ? 210 HIS   A CB  1 
ATOM   1524 C  CG  . HIS   A 1 203 ? -4.26471  -9.39376  -6.66198  1.000 25.54150 ? 210 HIS   A CG  1 
ATOM   1525 N  ND1 . HIS   A 1 203 ? -3.42883  -8.57738  -5.93146  1.000 29.76226 ? 210 HIS   A ND1 1 
ATOM   1526 C  CD2 . HIS   A 1 203 ? -4.17268  -10.62379 -6.10174  1.000 30.84317 ? 210 HIS   A CD2 1 
ATOM   1527 C  CE1 . HIS   A 1 203 ? -2.85667  -9.28222  -4.97093  1.000 33.49820 ? 210 HIS   A CE1 1 
ATOM   1528 N  NE2 . HIS   A 1 203 ? -3.29304  -10.52675 -5.05130  1.000 30.75061 ? 210 HIS   A NE2 1 
ATOM   1529 N  N   . SER   A 1 204 ? -7.94479  -7.70182  -9.17281  1.000 20.94448 ? 211 SER   A N   1 
ATOM   1530 C  CA  . SER   A 1 204 ? -8.45088  -7.32943  -10.49040 1.000 20.81145 ? 211 SER   A CA  1 
ATOM   1531 C  C   . SER   A 1 204 ? -9.84008  -6.70446  -10.41595 1.000 21.50598 ? 211 SER   A C   1 
ATOM   1532 O  O   . SER   A 1 204 ? -10.58744 -6.74212  -11.39974 1.000 23.56789 ? 211 SER   A O   1 
ATOM   1533 C  CB  . SER   A 1 204 ? -8.43821  -8.53490  -11.43799 1.000 21.30670 ? 211 SER   A CB  1 
ATOM   1534 O  OG  . SER   A 1 204 ? -7.13394  -9.09939  -11.51460 1.000 24.91146 ? 211 SER   A OG  1 
ATOM   1535 N  N   . GLN   A 1 205 ? -10.18093 -6.09958  -9.28010  1.000 24.04949 ? 212 GLN   A N   1 
ATOM   1536 C  CA  . GLN   A 1 205 ? -11.53715 -5.61110  -9.06386  1.000 28.62384 ? 212 GLN   A CA  1 
ATOM   1537 C  C   . GLN   A 1 205 ? -11.89933 -4.42651  -9.95410  1.000 29.50942 ? 212 GLN   A C   1 
ATOM   1538 O  O   . GLN   A 1 205 ? -13.09129 -4.16178  -10.14581 1.000 39.37032 ? 212 GLN   A O   1 
ATOM   1539 C  CB  . GLN   A 1 205 ? -11.72697 -5.26833  -7.58528  1.000 36.07115 ? 212 GLN   A CB  1 
ATOM   1540 C  CG  . GLN   A 1 205 ? -10.82100 -4.15457  -7.11710  1.000 40.38783 ? 212 GLN   A CG  1 
ATOM   1541 C  CD  . GLN   A 1 205 ? -9.58979  -4.67105  -6.39342  1.000 51.48930 ? 212 GLN   A CD  1 
ATOM   1542 O  OE1 . GLN   A 1 205 ? -8.59077  -5.03537  -7.02258  1.000 34.54051 ? 212 GLN   A OE1 1 
ATOM   1543 N  NE2 . GLN   A 1 205 ? -9.64951  -4.69500  -5.06575  1.000 50.02423 ? 212 GLN   A NE2 1 
ATOM   1544 N  N   . PHE   A 1 206 ? -10.91775 -3.71650  -10.51344 1.000 24.21226 ? 213 PHE   A N   1 
ATOM   1545 C  CA  . PHE   A 1 206 ? -11.18794 -2.53440  -11.32278 1.000 26.27207 ? 213 PHE   A CA  1 
ATOM   1546 C  C   . PHE   A 1 206 ? -10.91764 -2.73789  -12.81220 1.000 30.48090 ? 213 PHE   A C   1 
ATOM   1547 O  O   . PHE   A 1 206 ? -10.84316 -1.75439  -13.55441 1.000 39.01155 ? 213 PHE   A O   1 
ATOM   1548 C  CB  . PHE   A 1 206 ? -10.41693 -1.31990  -10.79786 1.000 37.28700 ? 213 PHE   A CB  1 
ATOM   1549 C  CG  . PHE   A 1 206 ? -10.79792 -0.92181  -9.40179  1.000 37.99267 ? 213 PHE   A CG  1 
ATOM   1550 C  CD1 . PHE   A 1 206 ? -12.03931 -0.37003  -9.14017  1.000 39.73522 ? 213 PHE   A CD1 1 
ATOM   1551 C  CD2 . PHE   A 1 206 ? -9.90411  -1.07634  -8.35523  1.000 39.82324 ? 213 PHE   A CD2 1 
ATOM   1552 C  CE1 . PHE   A 1 206 ? -12.39223 0.00005   -7.85491  1.000 45.20069 ? 213 PHE   A CE1 1 
ATOM   1553 C  CE2 . PHE   A 1 206 ? -10.25060 -0.70702  -7.06789  1.000 41.95161 ? 213 PHE   A CE2 1 
ATOM   1554 C  CZ  . PHE   A 1 206 ? -11.49584 -0.16746  -6.81845  1.000 42.48767 ? 213 PHE   A CZ  1 
ATOM   1555 N  N   . ILE   A 1 207 ? -10.76425 -3.98142  -13.26844 1.000 21.73011 ? 214 ILE   A N   1 
ATOM   1556 C  CA  . ILE   A 1 207 ? -10.57550 -4.24038  -14.69434 1.000 19.83720 ? 214 ILE   A CA  1 
ATOM   1557 C  C   . ILE   A 1 207 ? -11.87127 -3.93134  -15.43696 1.000 23.53853 ? 214 ILE   A C   1 
ATOM   1558 O  O   . ILE   A 1 207 ? -12.95236 -4.39790  -15.05444 1.000 24.13440 ? 214 ILE   A O   1 
ATOM   1559 C  CB  . ILE   A 1 207 ? -10.12508 -5.69406  -14.91654 1.000 20.05618 ? 214 ILE   A CB  1 
ATOM   1560 C  CG1 . ILE   A 1 207 ? -8.72183  -5.91901  -14.34209 1.000 19.32014 ? 214 ILE   A CG1 1 
ATOM   1561 C  CG2 . ILE   A 1 207 ? -10.13811 -6.05004  -16.39675 1.000 20.83635 ? 214 ILE   A CG2 1 
ATOM   1562 C  CD1 . ILE   A 1 207 ? -7.63473  -5.09208  -15.01702 1.000 22.73656 ? 214 ILE   A CD1 1 
ATOM   1563 N  N   . GLY   A 1 208 ? -11.76840 -3.14381  -16.50482 1.000 20.00547 ? 215 GLY   A N   1 
ATOM   1564 C  CA  . GLY   A 1 208 ? -12.93842 -2.61344  -17.18228 1.000 23.13242 ? 215 GLY   A CA  1 
ATOM   1565 C  C   . GLY   A 1 208 ? -13.54484 -3.49271  -18.25520 1.000 20.85677 ? 215 GLY   A C   1 
ATOM   1566 O  O   . GLY   A 1 208 ? -14.09650 -2.98343  -19.23481 1.000 22.08403 ? 215 GLY   A O   1 
ATOM   1567 N  N   . TYR   A 1 209 ? -13.45245 -4.80709  -18.08463 1.000 20.52069 ? 216 TYR   A N   1 
ATOM   1568 C  CA  . TYR   A 1 209 ? -14.03263 -5.77556  -18.99924 1.000 19.55905 ? 216 TYR   A CA  1 
ATOM   1569 C  C   . TYR   A 1 209 ? -14.61253 -6.90940  -18.15631 1.000 19.83376 ? 216 TYR   A C   1 
ATOM   1570 O  O   . TYR   A 1 209 ? -14.09247 -7.19830  -17.07815 1.000 22.04240 ? 216 TYR   A O   1 
ATOM   1571 C  CB  . TYR   A 1 209 ? -12.95978 -6.33472  -19.94807 1.000 18.59486 ? 216 TYR   A CB  1 
ATOM   1572 C  CG  . TYR   A 1 209 ? -12.37406 -5.25835  -20.82533 1.000 19.17388 ? 216 TYR   A CG  1 
ATOM   1573 C  CD1 . TYR   A 1 209 ? -13.03341 -4.83710  -21.97346 1.000 19.68746 ? 216 TYR   A CD1 1 
ATOM   1574 C  CD2 . TYR   A 1 209 ? -11.17595 -4.63395  -20.48544 1.000 18.81138 ? 216 TYR   A CD2 1 
ATOM   1575 C  CE1 . TYR   A 1 209 ? -12.51704 -3.83992  -22.76508 1.000 19.50373 ? 216 TYR   A CE1 1 
ATOM   1576 C  CE2 . TYR   A 1 209 ? -10.64819 -3.63529  -21.27457 1.000 19.45869 ? 216 TYR   A CE2 1 
ATOM   1577 C  CZ  . TYR   A 1 209 ? -11.32331 -3.24303  -22.41662 1.000 20.16135 ? 216 TYR   A CZ  1 
ATOM   1578 O  OH  . TYR   A 1 209 ? -10.82381 -2.24347  -23.20872 1.000 23.52060 ? 216 TYR   A OH  1 
ATOM   1579 N  N   . PRO   A 1 210 ? -15.68175 -7.54498  -18.62716 1.000 18.63892 ? 217 PRO   A N   1 
ATOM   1580 C  CA  . PRO   A 1 210 ? -16.27002 -8.64708  -17.84722 1.000 19.27270 ? 217 PRO   A CA  1 
ATOM   1581 C  C   . PRO   A 1 210 ? -15.31258 -9.82706  -17.76491 1.000 21.39041 ? 217 PRO   A C   1 
ATOM   1582 O  O   . PRO   A 1 210 ? -14.77620 -10.28185 -18.77640 1.000 21.00936 ? 217 PRO   A O   1 
ATOM   1583 C  CB  . PRO   A 1 210 ? -17.54062 -9.01056  -18.62890 1.000 20.79268 ? 217 PRO   A CB  1 
ATOM   1584 C  CG  . PRO   A 1 210 ? -17.41160 -8.37636  -19.95704 1.000 25.66168 ? 217 PRO   A CG  1 
ATOM   1585 C  CD  . PRO   A 1 210 ? -16.43056 -7.24468  -19.85670 1.000 21.83436 ? 217 PRO   A CD  1 
ATOM   1586 N  N   . ILE   A 1 211 ? -15.09400 -10.30730 -16.54470 1.000 19.06578 ? 218 ILE   A N   1 
ATOM   1587 C  CA  . ILE   A 1 211 ? -14.26310 -11.47385 -16.26868 1.000 17.22159 ? 218 ILE   A CA  1 
ATOM   1588 C  C   . ILE   A 1 211 ? -15.21305 -12.57519 -15.82526 1.000 18.04307 ? 218 ILE   A C   1 
ATOM   1589 O  O   . ILE   A 1 211 ? -15.84388 -12.47172 -14.76438 1.000 22.82810 ? 218 ILE   A O   1 
ATOM   1590 C  CB  . ILE   A 1 211 ? -13.22435 -11.18374 -15.17846 1.000 18.37526 ? 218 ILE   A CB  1 
ATOM   1591 C  CG1 . ILE   A 1 211 ? -12.27831 -10.05870 -15.60676 1.000 17.54123 ? 218 ILE   A CG1 1 
ATOM   1592 C  CG2 . ILE   A 1 211 ? -12.42473 -12.43557 -14.86752 1.000 18.88709 ? 218 ILE   A CG2 1 
ATOM   1593 C  CD1 . ILE   A 1 211 ? -11.44893 -9.51192  -14.44802 1.000 19.52241 ? 218 ILE   A CD1 1 
ATOM   1594 N  N   . THR   A 1 212 ? -15.33885 -13.62011 -16.63638 1.000 18.31313 ? 219 THR   A N   1 
ATOM   1595 C  CA  . THR   A 1 212 ? -16.25907 -14.71547 -16.35228 1.000 17.23157 ? 219 THR   A CA  1 
ATOM   1596 C  C   . THR   A 1 212 ? -15.43674 -15.92287 -15.93371 1.000 16.30253 ? 219 THR   A C   1 
ATOM   1597 O  O   . THR   A 1 212 ? -14.59822 -16.40314 -16.70493 1.000 16.71006 ? 219 THR   A O   1 
ATOM   1598 C  CB  . THR   A 1 212 ? -17.10798 -15.05776 -17.57813 1.000 18.61031 ? 219 THR   A CB  1 
ATOM   1599 O  OG1 . THR   A 1 212 ? -17.84897 -13.90381 -17.99649 1.000 20.25094 ? 219 THR   A OG1 1 
ATOM   1600 C  CG2 . THR   A 1 212 ? -18.09315 -16.18987 -17.24618 1.000 18.97639 ? 219 THR   A CG2 1 
ATOM   1601 N  N   . LEU   A 1 213 ? -15.67430 -16.40509 -14.71892 1.000 18.20341 ? 220 LEU   A N   1 
ATOM   1602 C  CA  . LEU   A 1 213 ? -15.05069 -17.62404 -14.22168 1.000 17.67462 ? 220 LEU   A CA  1 
ATOM   1603 C  C   . LEU   A 1 213 ? -15.96252 -18.79847 -14.56187 1.000 18.97260 ? 220 LEU   A C   1 
ATOM   1604 O  O   . LEU   A 1 213 ? -17.05862 -18.92528 -14.00281 1.000 20.26318 ? 220 LEU   A O   1 
ATOM   1605 C  CB  . LEU   A 1 213 ? -14.82210 -17.52689 -12.71437 1.000 20.36312 ? 220 LEU   A CB  1 
ATOM   1606 C  CG  . LEU   A 1 213 ? -14.26352 -18.77062 -12.02190 1.000 21.73084 ? 220 LEU   A CG  1 
ATOM   1607 C  CD1 . LEU   A 1 213 ? -12.99145 -19.27688 -12.69456 1.000 18.81023 ? 220 LEU   A CD1 1 
ATOM   1608 C  CD2 . LEU   A 1 213 ? -14.01369 -18.46812 -10.54030 1.000 22.61091 ? 220 LEU   A CD2 1 
ATOM   1609 N  N   . PHE   A 1 214 ? -15.51001 -19.64918 -15.48076 1.000 17.03438 ? 221 PHE   A N   1 
ATOM   1610 C  CA  . PHE   A 1 214 ? -16.26615 -20.83531 -15.85602 1.000 18.31358 ? 221 PHE   A CA  1 
ATOM   1611 C  C   . PHE   A 1 214 ? -16.22395 -21.84710 -14.71767 1.000 20.62957 ? 221 PHE   A C   1 
ATOM   1612 O  O   . PHE   A 1 214 ? -15.25457 -21.91381 -13.95457 1.000 21.04334 ? 221 PHE   A O   1 
ATOM   1613 C  CB  . PHE   A 1 214 ? -15.65641 -21.50162 -17.09669 1.000 18.49151 ? 221 PHE   A CB  1 
ATOM   1614 C  CG  . PHE   A 1 214 ? -15.92186 -20.78543 -18.40621 1.000 17.97663 ? 221 PHE   A CG  1 
ATOM   1615 C  CD1 . PHE   A 1 214 ? -16.03370 -19.40331 -18.47593 1.000 16.97581 ? 221 PHE   A CD1 1 
ATOM   1616 C  CD2 . PHE   A 1 214 ? -16.02843 -21.52047 -19.58023 1.000 19.14634 ? 221 PHE   A CD2 1 
ATOM   1617 C  CE1 . PHE   A 1 214 ? -16.26044 -18.76539 -19.69597 1.000 17.57282 ? 221 PHE   A CE1 1 
ATOM   1618 C  CE2 . PHE   A 1 214 ? -16.25691 -20.89463 -20.80123 1.000 19.12993 ? 221 PHE   A CE2 1 
ATOM   1619 C  CZ  . PHE   A 1 214 ? -16.37957 -19.51608 -20.85888 1.000 18.21147 ? 221 PHE   A CZ  1 
ATOM   1620 N  N   . VAL   A 1 215 ? -17.28182 -22.64161 -14.60642 1.000 21.53989 ? 222 VAL   A N   1 
ATOM   1621 C  CA  . VAL   A 1 215 ? -17.33119 -23.72727 -13.64115 1.000 22.96054 ? 222 VAL   A CA  1 
ATOM   1622 C  C   . VAL   A 1 215 ? -17.19974 -25.05406 -14.37554 1.000 23.81036 ? 222 VAL   A C   1 
ATOM   1623 O  O   . VAL   A 1 215 ? -17.32707 -25.13503 -15.59865 1.000 25.10555 ? 222 VAL   A O   1 
ATOM   1624 C  CB  . VAL   A 1 215 ? -18.58768 -23.67272 -12.75115 1.000 35.75643 ? 222 VAL   A CB  1 
ATOM   1625 C  CG1 . VAL   A 1 215 ? -18.52314 -22.46237 -11.82175 1.000 40.64306 ? 222 VAL   A CG1 1 
ATOM   1626 C  CG2 . VAL   A 1 215 ? -19.81373 -23.59936 -13.60852 1.000 30.32595 ? 222 VAL   A CG2 1 
ATOM   1627 N  N   . GLU   A 1 216 ? -16.92960 -26.10819 -13.61628 1.000 26.89993 ? 223 GLU   A N   1 
ATOM   1628 C  CA  . GLU   A 1 216 ? -16.70145 -27.42765 -14.17546 1.000 29.04602 ? 223 GLU   A CA  1 
ATOM   1629 C  C   . GLU   A 1 216 ? -17.84616 -28.36445 -13.81708 1.000 34.37627 ? 223 GLU   A C   1 
ATOM   1630 O  O   . GLU   A 1 216 ? -18.52669 -28.18187 -12.80544 1.000 38.85632 ? 223 GLU   A O   1 
ATOM   1631 C  CB  . GLU   A 1 216 ? -15.37299 -27.99183 -13.66811 1.000 31.80105 ? 223 GLU   A CB  1 
ATOM   1632 C  CG  . GLU   A 1 216 ? -14.18747 -27.12942 -14.03766 1.000 32.65136 ? 223 GLU   A CG  1 
ATOM   1633 C  CD  . GLU   A 1 216 ? -12.87661 -27.70051 -13.54521 1.000 39.63321 ? 223 GLU   A CD  1 
ATOM   1634 O  OE1 . GLU   A 1 216 ? -12.39779 -28.68049 -14.15294 1.000 35.11770 ? 223 GLU   A OE1 1 
ATOM   1635 O  OE2 . GLU   A 1 216 ? -12.31794 -27.15432 -12.56811 1.000 37.55432 ? 223 GLU   A OE2 1 
ATOM   1636 N  N   . LYS   A 1 217 ? -18.05298 -29.36636 -14.67176 1.000 34.60396 ? 224 LYS   A N   1 
ATOM   1637 C  CA  . LYS   A 1 217 ? -19.03331 -30.42194 -14.42876 1.000 46.27893 ? 224 LYS   A CA  1 
ATOM   1638 C  C   . LYS   A 1 217 ? -18.87338 -31.01116 -13.03029 1.000 58.58819 ? 224 LYS   A C   1 
ATOM   1639 O  O   . LYS   A 1 217 ? -17.76288 -31.27783 -12.58548 1.000 52.06624 ? 224 LYS   A O   1 
ATOM   1640 C  CB  . LYS   A 1 217 ? -18.88809 -31.55263 -15.45208 1.000 46.00297 ? 224 LYS   A CB  1 
ATOM   1641 C  CG  . LYS   A 1 217 ? -19.94193 -32.64764 -15.27297 1.000 59.67613 ? 224 LYS   A CG  1 
ATOM   1642 C  CD  . LYS   A 1 217 ? -20.14002 -33.48303 -16.53051 1.000 64.67196 ? 224 LYS   A CD  1 
ATOM   1643 C  CE  . LYS   A 1 217 ? -19.08969 -34.59284 -16.61331 1.000 74.51349 ? 224 LYS   A CE  1 
ATOM   1644 N  NZ  . LYS   A 1 217 ? -17.82747 -34.14514 -17.27102 1.000 75.03322 ? 224 LYS   A NZ  1 
HETATM 1645 C  C2  . A1AX6 B 2 .   ? 0.36182   -11.59534 -23.34882 1.000 40.61865 ? 301 A1AX6 A C2  1 
HETATM 1646 C  C3  . A1AX6 B 2 .   ? 1.30694   -10.44300 -22.96805 1.000 46.65137 ? 301 A1AX6 A C3  1 
HETATM 1647 C  C1  . A1AX6 B 2 .   ? 1.12538   -12.75936 -24.00330 1.000 35.51694 ? 301 A1AX6 A C1  1 
HETATM 1648 C  C4  . A1AX6 B 2 .   ? -0.34277  -12.11786 -22.08572 0.496 40.08598 ? 301 A1AX6 A C4  1 
HETATM 1649 C  C5  . A1AX6 B 2 .   ? -1.98206  -11.37543 -23.49158 1.000 42.37491 ? 301 A1AX6 A C5  1 
HETATM 1650 C  C6  . A1AX6 B 2 .   ? -3.22518  -11.06207 -24.01304 1.000 27.72523 ? 301 A1AX6 A C6  1 
HETATM 1651 C  C10 . A1AX6 B 2 .   ? -0.80540  -11.13035 -24.19116 1.000 45.42221 ? 301 A1AX6 A C10 1 
HETATM 1652 C  C7  . A1AX6 B 2 .   ? -3.25394  -10.48301 -25.27168 0.447 40.52075 ? 301 A1AX6 A C7  1 
HETATM 1653 C  C8  . A1AX6 B 2 .   ? -2.08220  -10.23561 -25.95616 1.000 49.43842 ? 301 A1AX6 A C8  1 
HETATM 1654 C  C9  . A1AX6 B 2 .   ? -0.83632  -10.55167 -25.43508 0.783 46.63545 ? 301 A1AX6 A C9  1 
HETATM 1655 N  N1  . A1AX6 B 2 .   ? -1.67629  -11.96570 -22.25527 1.000 36.94613 ? 301 A1AX6 A N1  1 
HETATM 1656 O  O1  . A1AX6 B 2 .   ? 0.20864   -12.59706 -21.11422 1.000 38.90607 ? 301 A1AX6 A O1  1 
HETATM 1657 BR BR1 . A1AX6 B 2 .   ? -2.17302  -9.43034  -27.67321 0.669 94.69846 ? 301 A1AX6 A BR1 1 
HETATM 1658 O  O   . HOH   C 3 .   ? 5.27827   -7.46061  -33.79465 1.000 48.97273 ? 401 HOH   A O   1 
HETATM 1659 O  O   . HOH   C 3 .   ? 21.65771  -3.43000  -15.07643 1.000 52.48355 ? 402 HOH   A O   1 
HETATM 1660 O  O   . HOH   C 3 .   ? -17.47055 -24.72418 -8.78685  1.000 46.81627 ? 403 HOH   A O   1 
HETATM 1661 O  O   . HOH   C 3 .   ? -17.82264 -4.97225  -37.21570 1.000 46.44167 ? 404 HOH   A O   1 
HETATM 1662 O  O   . HOH   C 3 .   ? 5.68173   -25.71298 -7.29577  1.000 42.61388 ? 405 HOH   A O   1 
HETATM 1663 O  O   . HOH   C 3 .   ? -12.28560 -25.91290 -3.45292  1.000 51.16816 ? 406 HOH   A O   1 
HETATM 1664 O  O   . HOH   C 3 .   ? 1.95126   -15.79514 -41.10718 1.000 42.25145 ? 407 HOH   A O   1 
HETATM 1665 O  O   . HOH   C 3 .   ? -20.42749 -20.71098 -9.27109  1.000 42.00863 ? 408 HOH   A O   1 
HETATM 1666 O  O   . HOH   C 3 .   ? -17.55504 -10.85584 -2.17842  1.000 59.84177 ? 409 HOH   A O   1 
HETATM 1667 O  O   . HOH   C 3 .   ? 5.85285   -21.76176 -37.44420 1.000 28.96028 ? 410 HOH   A O   1 
HETATM 1668 O  O   . HOH   C 3 .   ? 13.85060  -11.35535 -29.53992 1.000 41.05843 ? 411 HOH   A O   1 
HETATM 1669 O  O   . HOH   C 3 .   ? 5.02995   -9.89698  -2.54624  1.000 44.26062 ? 412 HOH   A O   1 
HETATM 1670 O  O   . HOH   C 3 .   ? 7.21410   -30.52209 -15.05366 1.000 52.74226 ? 413 HOH   A O   1 
HETATM 1671 O  O   . HOH   C 3 .   ? 11.610    -21.592   -40.626   1.000 48.34947 ? 414 HOH   A O   1 
HETATM 1672 O  O   . HOH   C 3 .   ? -13.32121 -0.72791  -20.51287 1.000 33.62487 ? 415 HOH   A O   1 
HETATM 1673 O  O   . HOH   C 3 .   ? 3.30879   -24.38505 -38.70719 1.000 36.69746 ? 416 HOH   A O   1 
HETATM 1674 O  O   . HOH   C 3 .   ? -1.59707  -29.05526 -5.89332  1.000 33.76949 ? 417 HOH   A O   1 
HETATM 1675 O  O   . HOH   C 3 .   ? -6.40805  -24.00342 -30.68228 1.000 52.70140 ? 418 HOH   A O   1 
HETATM 1676 O  O   . HOH   C 3 .   ? -16.17942 -25.45423 -17.84354 1.000 25.64681 ? 419 HOH   A O   1 
HETATM 1677 O  O   . HOH   C 3 .   ? 20.16031  -3.30150  -8.10613  1.000 53.32101 ? 420 HOH   A O   1 
HETATM 1678 O  O   . HOH   C 3 .   ? -15.83035 0.19810   -30.47014 1.000 40.33652 ? 421 HOH   A O   1 
HETATM 1679 O  O   . HOH   C 3 .   ? -11.96533 -0.25462  -15.36138 1.000 42.08306 ? 422 HOH   A O   1 
HETATM 1680 O  O   . HOH   C 3 .   ? 9.34455   -3.30650  -20.57067 1.000 36.18225 ? 423 HOH   A O   1 
HETATM 1681 O  O   . HOH   C 3 .   ? -13.07270 -7.25069  -12.01045 1.000 35.63480 ? 424 HOH   A O   1 
HETATM 1682 O  O   . HOH   C 3 .   ? 7.75440   -23.26080 -14.19947 1.000 29.52597 ? 425 HOH   A O   1 
HETATM 1683 O  O   . HOH   C 3 .   ? 7.74392   -18.84612 -6.51686  1.000 24.04410 ? 426 HOH   A O   1 
HETATM 1684 O  O   . HOH   C 3 .   ? -0.22344  -5.74398  -38.59832 1.000 42.84544 ? 427 HOH   A O   1 
HETATM 1685 O  O   . HOH   C 3 .   ? -2.78465  -6.08679  -6.47374  1.000 38.18185 ? 428 HOH   A O   1 
HETATM 1686 O  O   . HOH   C 3 .   ? 20.28460  -10.74969 -26.17269 1.000 41.35399 ? 429 HOH   A O   1 
HETATM 1687 O  O   . HOH   C 3 .   ? 11.23722  -28.38753 -30.64251 1.000 32.26488 ? 430 HOH   A O   1 
HETATM 1688 O  O   . HOH   C 3 .   ? -4.31355  0.50111   -22.20231 1.000 36.01871 ? 431 HOH   A O   1 
HETATM 1689 O  O   . HOH   C 3 .   ? -2.88621  -3.28911  -35.39023 1.000 42.18539 ? 432 HOH   A O   1 
HETATM 1690 O  O   . HOH   C 3 .   ? 6.55848   -26.71589 -27.71152 1.000 33.85355 ? 433 HOH   A O   1 
HETATM 1691 O  O   . HOH   C 3 .   ? -16.26812 -12.72420 -19.76053 1.000 20.28860 ? 434 HOH   A O   1 
HETATM 1692 O  O   . HOH   C 3 .   ? 0.46831   -1.59926  -19.78085 1.000 40.08078 ? 435 HOH   A O   1 
HETATM 1693 O  O   . HOH   C 3 .   ? 0.84066   -20.94281 -4.64212  1.000 28.71802 ? 436 HOH   A O   1 
HETATM 1694 O  O   . HOH   C 3 .   ? -3.90950  -13.12653 -42.74712 1.000 48.53692 ? 437 HOH   A O   1 
HETATM 1695 O  O   . HOH   C 3 .   ? -7.43433  -27.94654 -21.01928 1.000 44.42694 ? 438 HOH   A O   1 
HETATM 1696 O  O   . HOH   C 3 .   ? 3.57089   -29.77163 -25.71483 1.000 41.35322 ? 439 HOH   A O   1 
HETATM 1697 O  O   . HOH   C 3 .   ? 18.21924  -7.32143  -20.24309 1.000 35.54842 ? 440 HOH   A O   1 
HETATM 1698 O  O   . HOH   C 3 .   ? -5.74153  -2.10249  -19.46432 1.000 24.03249 ? 441 HOH   A O   1 
HETATM 1699 O  O   . HOH   C 3 .   ? 7.66575   1.29316   -14.81643 1.000 34.84931 ? 442 HOH   A O   1 
HETATM 1700 O  O   . HOH   C 3 .   ? 6.06243   -21.12268 -0.07686  1.000 29.05251 ? 443 HOH   A O   1 
HETATM 1701 O  O   . HOH   C 3 .   ? -12.98806 -24.92057 -10.86625 1.000 32.37328 ? 444 HOH   A O   1 
HETATM 1702 O  O   . HOH   C 3 .   ? -6.68461  -3.50493  -8.11157  1.000 46.68880 ? 445 HOH   A O   1 
HETATM 1703 O  O   . HOH   C 3 .   ? -0.31411  -5.39780  -18.30745 1.000 27.36418 ? 446 HOH   A O   1 
HETATM 1704 O  O   . HOH   C 3 .   ? -0.97488  -11.36192 -3.12756  1.000 34.08294 ? 447 HOH   A O   1 
HETATM 1705 O  O   . HOH   C 3 .   ? -0.32575  -7.24957  -31.04119 1.000 31.83160 ? 448 HOH   A O   1 
HETATM 1706 O  O   . HOH   C 3 .   ? 7.61277   -27.93972 -24.09067 1.000 34.00084 ? 449 HOH   A O   1 
HETATM 1707 O  O   . HOH   C 3 .   ? 9.82656   -14.71550 -25.25263 1.000 20.87885 ? 450 HOH   A O   1 
HETATM 1708 O  O   . HOH   C 3 .   ? 3.22975   -6.14267  -11.10921 1.000 24.64722 ? 451 HOH   A O   1 
HETATM 1709 O  O   . HOH   C 3 .   ? 2.98998   -20.35111 -2.77900  1.000 36.15701 ? 452 HOH   A O   1 
HETATM 1710 O  O   . HOH   C 3 .   ? 1.24080   -6.70152  -5.27193  1.000 44.77909 ? 453 HOH   A O   1 
HETATM 1711 O  O   . HOH   C 3 .   ? 0.43908   -22.27036 -2.23938  1.000 43.20634 ? 454 HOH   A O   1 
HETATM 1712 O  O   . HOH   C 3 .   ? -3.31258  -12.04085 -9.04798  1.000 33.82811 ? 455 HOH   A O   1 
HETATM 1713 O  O   . HOH   C 3 .   ? 3.52947   -7.71533  -36.70214 1.000 36.00006 ? 456 HOH   A O   1 
HETATM 1714 O  O   . HOH   C 3 .   ? 0.62487   -26.89945 -37.29555 1.000 46.12882 ? 457 HOH   A O   1 
HETATM 1715 O  O   . HOH   C 3 .   ? -2.24790  -13.66925 -35.67121 1.000 19.94243 ? 458 HOH   A O   1 
HETATM 1716 O  O   . HOH   C 3 .   ? -8.71597  -11.80517 -36.42703 1.000 25.13070 ? 459 HOH   A O   1 
HETATM 1717 O  O   . HOH   C 3 .   ? 11.16482  -8.09761  -27.50409 1.000 24.09577 ? 460 HOH   A O   1 
HETATM 1718 O  O   . HOH   C 3 .   ? -6.79257  -35.07617 -19.43884 1.000 52.89108 ? 461 HOH   A O   1 
HETATM 1719 O  O   . HOH   C 3 .   ? -20.53433 -14.14648 -18.23746 1.000 37.30683 ? 462 HOH   A O   1 
HETATM 1720 O  O   . HOH   C 3 .   ? -17.03544 -5.38986  -22.76126 1.000 27.81103 ? 463 HOH   A O   1 
HETATM 1721 O  O   . HOH   C 3 .   ? 9.14258   -26.45326 -17.09678 1.000 30.78020 ? 464 HOH   A O   1 
HETATM 1722 O  O   . HOH   C 3 .   ? -6.43524  -7.75013  -34.40018 1.000 20.38181 ? 465 HOH   A O   1 
HETATM 1723 O  O   . HOH   C 3 .   ? -5.41228  -10.43427 -27.42898 1.000 19.24543 ? 466 HOH   A O   1 
HETATM 1724 O  O   . HOH   C 3 .   ? 0.26126   -28.65924 -25.53163 1.000 50.61772 ? 467 HOH   A O   1 
HETATM 1725 O  O   . HOH   C 3 .   ? 5.17394   -29.24493 -8.45449  1.000 42.86549 ? 468 HOH   A O   1 
HETATM 1726 O  O   . HOH   C 3 .   ? 10.61068  -25.33978 -23.73259 1.000 23.81240 ? 469 HOH   A O   1 
HETATM 1727 O  O   . HOH   C 3 .   ? -8.02053  -22.72647 -30.25557 1.000 44.08367 ? 470 HOH   A O   1 
HETATM 1728 O  O   . HOH   C 3 .   ? -14.52446 -6.93830  -14.40891 1.000 32.69696 ? 471 HOH   A O   1 
HETATM 1729 O  O   . HOH   C 3 .   ? -1.48775  -6.25521  -26.16872 1.000 23.97712 ? 472 HOH   A O   1 
HETATM 1730 O  O   . HOH   C 3 .   ? -10.71629 -14.54493 0.97907   1.000 27.77200 ? 473 HOH   A O   1 
HETATM 1731 O  O   . HOH   C 3 .   ? 8.44382   -16.33464 -39.52834 1.000 37.24646 ? 474 HOH   A O   1 
HETATM 1732 O  O   . HOH   C 3 .   ? 9.74363   -17.43929 -7.72614  1.000 24.03907 ? 475 HOH   A O   1 
HETATM 1733 O  O   . HOH   C 3 .   ? -3.50170  -13.15910 -20.62645 1.000 21.63659 ? 476 HOH   A O   1 
HETATM 1734 O  O   . HOH   C 3 .   ? 1.59683   -26.21576 -2.76894  1.000 43.82025 ? 477 HOH   A O   1 
HETATM 1735 O  O   . HOH   C 3 .   ? 1.47525   -7.84883  -16.59340 1.000 22.01686 ? 478 HOH   A O   1 
HETATM 1736 O  O   . HOH   C 3 .   ? -18.83529 -10.87878 -23.70852 1.000 29.63519 ? 479 HOH   A O   1 
HETATM 1737 O  O   . HOH   C 3 .   ? 0.66823   -5.28350  -13.96353 1.000 38.92741 ? 480 HOH   A O   1 
HETATM 1738 O  O   . HOH   C 3 .   ? -10.21143 -0.65159  -20.04244 1.000 33.17306 ? 481 HOH   A O   1 
HETATM 1739 O  O   . HOH   C 3 .   ? 0.33349   -14.91517 -1.40416  1.000 39.59409 ? 482 HOH   A O   1 
HETATM 1740 O  O   . HOH   C 3 .   ? -9.30120  -2.27513  -17.52322 1.000 23.22419 ? 483 HOH   A O   1 
HETATM 1741 O  O   . HOH   C 3 .   ? -7.36355  -5.58050  -2.66981  1.000 45.70769 ? 484 HOH   A O   1 
HETATM 1742 O  O   . HOH   C 3 .   ? 22.42593  -7.67726  -21.64679 1.000 48.31753 ? 485 HOH   A O   1 
HETATM 1743 O  O   . HOH   C 3 .   ? -8.44028  4.77122   -33.64306 1.000 31.58426 ? 486 HOH   A O   1 
HETATM 1744 O  O   . HOH   C 3 .   ? -7.69747  -28.29675 -7.91088  1.000 33.82253 ? 487 HOH   A O   1 
HETATM 1745 O  O   . HOH   C 3 .   ? 14.03115  -15.69702 -2.07760  1.000 33.75001 ? 488 HOH   A O   1 
HETATM 1746 O  O   . HOH   C 3 .   ? -8.17337  -24.86760 -19.08185 1.000 19.73333 ? 489 HOH   A O   1 
HETATM 1747 O  O   . HOH   C 3 .   ? 13.58353  -14.23494 -26.85600 1.000 22.52598 ? 490 HOH   A O   1 
HETATM 1748 O  O   . HOH   C 3 .   ? -6.52261  -4.88798  -39.17544 1.000 41.27378 ? 491 HOH   A O   1 
HETATM 1749 O  O   . HOH   C 3 .   ? 11.55395  -27.40582 -34.78502 1.000 25.02479 ? 492 HOH   A O   1 
HETATM 1750 O  O   . HOH   C 3 .   ? -1.58808  -30.35369 -19.57006 1.000 47.68316 ? 493 HOH   A O   1 
HETATM 1751 O  O   . HOH   C 3 .   ? -5.48171  -7.59042  -13.12102 1.000 21.56161 ? 494 HOH   A O   1 
HETATM 1752 O  O   . HOH   C 3 .   ? -10.98879 -14.14069 -37.78070 1.000 36.21053 ? 495 HOH   A O   1 
HETATM 1753 O  O   . HOH   C 3 .   ? 15.51921  -20.25985 -18.78825 1.000 25.06875 ? 496 HOH   A O   1 
HETATM 1754 O  O   . HOH   C 3 .   ? -19.762   -19.424   -14.226   1.000 21.25305 ? 497 HOH   A O   1 
HETATM 1755 O  O   . HOH   C 3 .   ? -6.25943  -11.29251 -10.08518 1.000 25.84503 ? 498 HOH   A O   1 
HETATM 1756 O  O   . HOH   C 3 .   ? -19.87078 -12.95334 -16.36968 1.000 44.93730 ? 499 HOH   A O   1 
HETATM 1757 O  O   . HOH   C 3 .   ? -1.84162  -32.38209 -7.78879  1.000 50.68608 ? 500 HOH   A O   1 
HETATM 1758 O  O   . HOH   C 3 .   ? -8.12624  1.78288   -36.60863 1.000 35.30847 ? 501 HOH   A O   1 
HETATM 1759 O  O   . HOH   C 3 .   ? -4.15621  -4.74932  -8.42063  1.000 38.89409 ? 502 HOH   A O   1 
HETATM 1760 O  O   . HOH   C 3 .   ? 6.51117   -29.68149 -20.11141 1.000 38.38221 ? 503 HOH   A O   1 
HETATM 1761 O  O   . HOH   C 3 .   ? -2.08161  -0.52915  -18.69237 1.000 38.19107 ? 504 HOH   A O   1 
HETATM 1762 O  O   . HOH   C 3 .   ? 0.75509   -29.68927 -16.03486 1.000 36.17872 ? 505 HOH   A O   1 
HETATM 1763 O  O   . HOH   C 3 .   ? -5.87758  -31.22287 -11.56203 1.000 31.92313 ? 506 HOH   A O   1 
HETATM 1764 O  O   . HOH   C 3 .   ? 12.93301  -13.98553 -29.61742 1.000 27.01766 ? 507 HOH   A O   1 
HETATM 1765 O  O   . HOH   C 3 .   ? -15.74716 6.41065   -32.44636 1.000 42.79575 ? 508 HOH   A O   1 
HETATM 1766 O  O   . HOH   C 3 .   ? 10.72947  -25.68019 -26.73992 1.000 31.42744 ? 509 HOH   A O   1 
HETATM 1767 O  O   . HOH   C 3 .   ? -1.12957  -7.37804  -23.65706 1.000 26.04499 ? 510 HOH   A O   1 
HETATM 1768 O  O   . HOH   C 3 .   ? -14.60787 -22.72381 -11.37546 1.000 29.43639 ? 511 HOH   A O   1 
HETATM 1769 O  O   . HOH   C 3 .   ? -19.36272 -10.31443 -32.91523 1.000 42.71942 ? 512 HOH   A O   1 
HETATM 1770 O  O   . HOH   C 3 .   ? -17.87928 -3.71605  -29.00916 1.000 45.04170 ? 513 HOH   A O   1 
HETATM 1771 O  O   . HOH   C 3 .   ? 19.83059  -16.73132 -27.46311 1.000 39.22209 ? 514 HOH   A O   1 
HETATM 1772 O  O   . HOH   C 3 .   ? -13.71818 -16.98342 -2.64809  1.000 26.62426 ? 515 HOH   A O   1 
HETATM 1773 O  O   . HOH   C 3 .   ? -9.841    -24.325   3.229     1.000 52.80858 ? 516 HOH   A O   1 
HETATM 1774 O  O   . HOH   C 3 .   ? 8.80086   -15.50021 -27.80737 1.000 18.98671 ? 517 HOH   A O   1 
HETATM 1775 O  O   . HOH   C 3 .   ? 17.98510  -19.42804 -24.68239 1.000 31.57341 ? 518 HOH   A O   1 
HETATM 1776 O  O   . HOH   C 3 .   ? -8.12483  -3.85621  -10.72958 1.000 29.06783 ? 519 HOH   A O   1 
HETATM 1777 O  O   . HOH   C 3 .   ? -3.31362  -21.06292 -0.54880  1.000 35.75180 ? 520 HOH   A O   1 
HETATM 1778 O  O   . HOH   C 3 .   ? -16.07760 -3.02649  -21.22513 1.000 30.11307 ? 521 HOH   A O   1 
HETATM 1779 O  O   . HOH   C 3 .   ? -10.39306 -11.49652 -2.12840  1.000 23.81203 ? 522 HOH   A O   1 
HETATM 1780 O  O   . HOH   C 3 .   ? 2.31181   -34.78987 -11.84860 1.000 57.63708 ? 523 HOH   A O   1 
HETATM 1781 O  O   . HOH   C 3 .   ? -6.17316  -13.97950 0.79557   1.000 29.45853 ? 524 HOH   A O   1 
HETATM 1782 O  O   . HOH   C 3 .   ? 4.05386   -24.17531 -30.70238 1.000 20.93808 ? 525 HOH   A O   1 
HETATM 1783 O  O   . HOH   C 3 .   ? 8.40268   -20.51402 -9.22726  1.000 30.78288 ? 526 HOH   A O   1 
HETATM 1784 O  O   . HOH   C 3 .   ? -5.14371  -14.25828 -22.64338 1.000 17.42006 ? 527 HOH   A O   1 
HETATM 1785 O  O   . HOH   C 3 .   ? 10.43780  -21.46704 -7.01322  1.000 37.43917 ? 528 HOH   A O   1 
HETATM 1786 O  O   . HOH   C 3 .   ? -4.68956  0.50842   -30.46693 1.000 29.63103 ? 529 HOH   A O   1 
HETATM 1787 O  O   . HOH   C 3 .   ? -4.31726  -4.25712  -37.21996 1.000 46.01724 ? 530 HOH   A O   1 
HETATM 1788 O  O   . HOH   C 3 .   ? -15.25627 -11.09206 -29.79387 1.000 26.44808 ? 531 HOH   A O   1 
HETATM 1789 O  O   . HOH   C 3 .   ? -17.24367 -28.73915 -17.29974 1.000 38.53600 ? 532 HOH   A O   1 
HETATM 1790 O  O   . HOH   C 3 .   ? -20.32635 -27.56554 -10.71919 1.000 51.34409 ? 533 HOH   A O   1 
HETATM 1791 O  O   . HOH   C 3 .   ? -10.55103 -6.42665  -2.90507  1.000 41.58293 ? 534 HOH   A O   1 
HETATM 1792 O  O   . HOH   C 3 .   ? -13.53664 -26.51503 -17.99455 1.000 27.07802 ? 535 HOH   A O   1 
HETATM 1793 O  O   . HOH   C 3 .   ? -12.22266 -27.88074 -30.06881 1.000 35.70070 ? 536 HOH   A O   1 
HETATM 1794 O  O   . HOH   C 3 .   ? 1.63630   -3.27031  -24.59287 1.000 41.60734 ? 537 HOH   A O   1 
HETATM 1795 O  O   . HOH   C 3 .   ? 3.48056   -30.15438 -19.17074 1.000 46.48833 ? 538 HOH   A O   1 
HETATM 1796 O  O   . HOH   C 3 .   ? -7.72863  -24.27134 -23.15185 1.000 29.18444 ? 539 HOH   A O   1 
HETATM 1797 O  O   . HOH   C 3 .   ? 8.06030   -23.14241 -7.05726  1.000 35.44738 ? 540 HOH   A O   1 
HETATM 1798 O  O   . HOH   C 3 .   ? -1.31036  -26.04357 -32.43457 1.000 39.87178 ? 541 HOH   A O   1 
HETATM 1799 O  O   . HOH   C 3 .   ? -4.00667  -14.07704 -0.77377  1.000 44.81990 ? 542 HOH   A O   1 
HETATM 1800 O  O   . HOH   C 3 .   ? 14.34064  -16.05822 -30.79495 1.000 32.16772 ? 543 HOH   A O   1 
HETATM 1801 O  O   . HOH   C 3 .   ? 4.71731   -30.67371 -11.56104 1.000 40.41149 ? 544 HOH   A O   1 
HETATM 1802 O  O   . HOH   C 3 .   ? 15.67727  -0.81116  -19.63174 1.000 36.67713 ? 545 HOH   A O   1 
HETATM 1803 O  O   . HOH   C 3 .   ? -6.38118  -5.06401  -35.62808 1.000 23.89243 ? 546 HOH   A O   1 
HETATM 1804 O  O   . HOH   C 3 .   ? -3.40452  -3.27671  -40.68655 1.000 50.34409 ? 547 HOH   A O   1 
HETATM 1805 O  O   . HOH   C 3 .   ? -14.23889 -12.59504 -7.75809  1.000 25.20279 ? 548 HOH   A O   1 
HETATM 1806 O  O   . HOH   C 3 .   ? -1.33421  -4.48886  -33.79580 1.000 37.85636 ? 549 HOH   A O   1 
HETATM 1807 O  O   . HOH   C 3 .   ? -15.20169 -11.96979 -12.01015 1.000 29.46112 ? 550 HOH   A O   1 
HETATM 1808 O  O   . HOH   C 3 .   ? -5.85179  -28.26474 -4.93984  1.000 47.13234 ? 551 HOH   A O   1 
HETATM 1809 O  O   . HOH   C 3 .   ? 3.70092   -11.84496 -38.58827 1.000 27.15351 ? 552 HOH   A O   1 
HETATM 1810 O  O   . HOH   C 3 .   ? -14.41091 -21.97885 -33.71794 1.000 40.03829 ? 553 HOH   A O   1 
HETATM 1811 O  O   . HOH   C 3 .   ? 3.60453   -6.71486  -17.86922 1.000 23.85621 ? 554 HOH   A O   1 
HETATM 1812 O  O   . HOH   C 3 .   ? 8.80852   -20.40568 -4.29120  1.000 28.10003 ? 555 HOH   A O   1 
HETATM 1813 O  O   . HOH   C 3 .   ? -14.77646 -29.37764 -9.80608  1.000 51.83789 ? 556 HOH   A O   1 
HETATM 1814 O  O   . HOH   C 3 .   ? 9.64104   -11.06416 -34.90607 1.000 37.14674 ? 557 HOH   A O   1 
HETATM 1815 O  O   . HOH   C 3 .   ? -1.23596  -29.88188 -17.28803 1.000 38.65730 ? 558 HOH   A O   1 
HETATM 1816 O  O   . HOH   C 3 .   ? -1.83269  -25.65912 -4.72086  1.000 24.34099 ? 559 HOH   A O   1 
HETATM 1817 O  O   . HOH   C 3 .   ? -0.18309  -30.30253 -24.00330 1.000 49.64356 ? 560 HOH   A O   1 
HETATM 1818 O  O   . HOH   C 3 .   ? -12.544   -27.259   -35.135   1.000 47.17402 ? 561 HOH   A O   1 
HETATM 1819 O  O   . HOH   C 3 .   ? 18.49043  -16.11361 -13.43057 1.000 37.81838 ? 562 HOH   A O   1 
HETATM 1820 O  O   . HOH   C 3 .   ? -14.58043 -3.87094  -12.72513 1.000 42.19899 ? 563 HOH   A O   1 
HETATM 1821 O  O   . HOH   C 3 .   ? 10.91836  -11.42476 -4.76749  1.000 35.25647 ? 564 HOH   A O   1 
HETATM 1822 O  O   . HOH   C 3 .   ? 4.05081   -9.17943  -20.27577 1.000 22.88996 ? 565 HOH   A O   1 
HETATM 1823 O  O   . HOH   C 3 .   ? -7.21264  1.30722   -19.33764 1.000 35.52196 ? 566 HOH   A O   1 
HETATM 1824 O  O   . HOH   C 3 .   ? -5.83572  -18.85743 -39.15174 1.000 38.10565 ? 567 HOH   A O   1 
HETATM 1825 O  O   . HOH   C 3 .   ? -9.06450  -10.41069 -40.49359 1.000 42.53328 ? 568 HOH   A O   1 
HETATM 1826 O  O   . HOH   C 3 .   ? -8.72371  -18.18357 -36.79688 1.000 36.92510 ? 569 HOH   A O   1 
HETATM 1827 O  O   . HOH   C 3 .   ? -3.95447  -3.25497  -15.28721 1.000 43.46797 ? 570 HOH   A O   1 
HETATM 1828 O  O   . HOH   C 3 .   ? -3.06558  -1.06175  -24.04637 1.000 28.34624 ? 571 HOH   A O   1 
HETATM 1829 O  O   . HOH   C 3 .   ? 6.75658   -29.73614 -30.02625 1.000 52.60661 ? 572 HOH   A O   1 
HETATM 1830 O  O   . HOH   C 3 .   ? 4.33740   -19.46441 -40.68932 1.000 33.94283 ? 573 HOH   A O   1 
HETATM 1831 O  O   . HOH   C 3 .   ? -13.52090 -25.83033 -7.77443  1.000 29.80204 ? 574 HOH   A O   1 
HETATM 1832 O  O   . HOH   C 3 .   ? 20.88838  -14.13970 -26.66443 1.000 32.35101 ? 575 HOH   A O   1 
HETATM 1833 O  O   . HOH   C 3 .   ? -10.26212 -15.07345 -28.31403 1.000 26.69931 ? 576 HOH   A O   1 
HETATM 1834 O  O   . HOH   C 3 .   ? -2.39185  -24.83417 -1.15028  1.000 46.86113 ? 577 HOH   A O   1 
HETATM 1835 O  O   . HOH   C 3 .   ? -5.20796  -5.22029  -11.88537 1.000 37.48086 ? 578 HOH   A O   1 
HETATM 1836 O  O   . HOH   C 3 .   ? 4.71268   -33.66887 -11.41434 1.000 59.24520 ? 579 HOH   A O   1 
HETATM 1837 O  O   . HOH   C 3 .   ? -17.73513 -18.65170 -11.15998 1.000 35.76069 ? 580 HOH   A O   1 
HETATM 1838 O  O   . HOH   C 3 .   ? -15.81716 -3.82290  -15.33409 1.000 49.31157 ? 581 HOH   A O   1 
HETATM 1839 O  O   . HOH   C 3 .   ? -17.75812 -15.14978 -13.07622 1.000 26.54365 ? 582 HOH   A O   1 
HETATM 1840 O  O   . HOH   C 3 .   ? -0.85918  -13.76614 -42.87474 1.000 46.18029 ? 583 HOH   A O   1 
HETATM 1841 O  O   . HOH   C 3 .   ? 2.02425   -6.24652  -25.86211 1.000 39.55757 ? 584 HOH   A O   1 
HETATM 1842 O  O   . HOH   C 3 .   ? -12.28358 -26.94260 -20.26770 1.000 28.59947 ? 585 HOH   A O   1 
HETATM 1843 O  O   . HOH   C 3 .   ? -7.93706  -13.59839 -40.99093 1.000 47.71412 ? 586 HOH   A O   1 
HETATM 1844 O  O   . HOH   C 3 .   ? 13.70337  -20.52113 -20.74752 1.000 21.96375 ? 587 HOH   A O   1 
HETATM 1845 O  O   . HOH   C 3 .   ? 20.06116  -5.30375  -14.81434 1.000 47.04156 ? 588 HOH   A O   1 
HETATM 1846 O  O   . HOH   C 3 .   ? -16.45234 -9.04806  -14.24248 1.000 33.44755 ? 589 HOH   A O   1 
HETATM 1847 O  O   . HOH   C 3 .   ? 15.77068  -18.34174 -3.57371  1.000 31.40043 ? 590 HOH   A O   1 
HETATM 1848 O  O   . HOH   C 3 .   ? 0.92213   -9.52559  -40.46317 1.000 48.55944 ? 591 HOH   A O   1 
HETATM 1849 O  O   . HOH   C 3 .   ? -7.28352  -22.40902 -36.60768 1.000 44.09041 ? 592 HOH   A O   1 
HETATM 1850 O  O   . HOH   C 3 .   ? 17.02916  -24.78977 -25.37659 1.000 31.43436 ? 593 HOH   A O   1 
HETATM 1851 O  O   . HOH   C 3 .   ? 13.26891  -6.82372  -26.24824 1.000 23.89405 ? 594 HOH   A O   1 
HETATM 1852 O  O   . HOH   C 3 .   ? -14.22971 -16.13239 -26.07716 1.000 25.81272 ? 595 HOH   A O   1 
HETATM 1853 O  O   . HOH   C 3 .   ? 7.27359   -4.52543  -22.38738 1.000 41.28380 ? 596 HOH   A O   1 
HETATM 1854 O  O   . HOH   C 3 .   ? -14.04849 -11.63207 0.43484   1.000 39.37255 ? 597 HOH   A O   1 
HETATM 1855 O  O   . HOH   C 3 .   ? 12.38504  -27.56613 -19.71256 1.000 43.56427 ? 598 HOH   A O   1 
HETATM 1856 O  O   . HOH   C 3 .   ? 1.26299   -8.54396  -26.83987 1.000 37.63642 ? 599 HOH   A O   1 
HETATM 1857 O  O   . HOH   C 3 .   ? 12.03464  -1.68034  -3.60199  1.000 51.93878 ? 600 HOH   A O   1 
HETATM 1858 O  O   . HOH   C 3 .   ? 21.959    -13.619   -19.548   1.000 46.83887 ? 601 HOH   A O   1 
HETATM 1859 O  O   . HOH   C 3 .   ? 0.02657   -16.68549 -3.45385  1.000 26.56466 ? 602 HOH   A O   1 
HETATM 1860 O  O   . HOH   C 3 .   ? -16.22938 -25.46370 -10.75172 1.000 33.72453 ? 603 HOH   A O   1 
HETATM 1861 O  O   . HOH   C 3 .   ? 13.66929  -4.06254  -25.44721 1.000 20.30323 ? 604 HOH   A O   1 
HETATM 1862 O  O   . HOH   C 3 .   ? 8.69688   -19.86365 -41.62365 1.000 44.91844 ? 605 HOH   A O   1 
HETATM 1863 O  O   . HOH   C 3 .   ? 0.94118   -5.96721  -34.26358 1.000 45.32773 ? 606 HOH   A O   1 
HETATM 1864 O  O   . HOH   C 3 .   ? 3.96506   -22.97076 -3.46609  1.000 36.33175 ? 607 HOH   A O   1 
HETATM 1865 O  O   . HOH   C 3 .   ? 2.97580   -5.03711  -28.99373 1.000 42.40629 ? 608 HOH   A O   1 
HETATM 1866 O  O   . HOH   C 3 .   ? -5.36986  -31.65862 -6.91776  1.000 49.35463 ? 609 HOH   A O   1 
HETATM 1867 O  O   . HOH   C 3 .   ? -13.11025 -12.18329 -31.00056 1.000 25.33956 ? 610 HOH   A O   1 
HETATM 1868 O  O   . HOH   C 3 .   ? -14.09286 -24.00333 -4.90399  1.000 32.84167 ? 611 HOH   A O   1 
HETATM 1869 O  O   . HOH   C 3 .   ? -5.662    -11.108   1.094     1.000 52.70385 ? 612 HOH   A O   1 
HETATM 1870 O  O   . HOH   C 3 .   ? -2.33473  -8.71864  -43.48264 1.000 48.83847 ? 613 HOH   A O   1 
HETATM 1871 O  O   . HOH   C 3 .   ? -18.12564 -5.75476  -25.40928 1.000 33.85091 ? 614 HOH   A O   1 
HETATM 1872 O  O   . HOH   C 3 .   ? 15.45648  -7.24583  -27.96516 1.000 35.36312 ? 615 HOH   A O   1 
HETATM 1873 O  O   . HOH   C 3 .   ? -13.77880 -18.53149 -24.41650 1.000 23.27894 ? 616 HOH   A O   1 
HETATM 1874 O  O   . HOH   C 3 .   ? -19.08566 -13.39514 -27.42583 1.000 44.02186 ? 617 HOH   A O   1 
HETATM 1875 O  O   . HOH   C 3 .   ? -12.39048 -32.07180 -19.05118 1.000 53.33171 ? 618 HOH   A O   1 
HETATM 1876 O  O   . HOH   C 3 .   ? -7.572    7.565     -33.692   1.000 37.21591 ? 619 HOH   A O   1 
HETATM 1877 O  O   . HOH   C 3 .   ? 16.48663  -27.71549 -22.36882 1.000 43.32671 ? 620 HOH   A O   1 
HETATM 1878 O  O   . HOH   C 3 .   ? 7.14672   1.84652   -12.49280 1.000 40.17094 ? 621 HOH   A O   1 
HETATM 1879 O  O   . HOH   C 3 .   ? 3.16981   -3.94039  -9.08634  1.000 44.54634 ? 622 HOH   A O   1 
HETATM 1880 O  O   . HOH   C 3 .   ? 5.65886   -3.34660  -26.15971 1.000 39.23154 ? 623 HOH   A O   1 
HETATM 1881 O  O   . HOH   C 3 .   ? 1.47558   -3.97471  -16.75526 1.000 39.10755 ? 624 HOH   A O   1 
HETATM 1882 O  O   . HOH   C 3 .   ? 17.52830  -15.40184 -29.76264 1.000 42.74693 ? 625 HOH   A O   1 
HETATM 1883 O  O   . HOH   C 3 .   ? 11.44904  -1.75501  -20.32304 1.000 39.49013 ? 626 HOH   A O   1 
HETATM 1884 O  O   . HOH   C 3 .   ? 0.43635   -5.76314  -22.00593 1.000 35.29459 ? 627 HOH   A O   1 
HETATM 1885 O  O   . HOH   C 3 .   ? -0.62279  -5.87278  -12.80947 1.000 47.95566 ? 628 HOH   A O   1 
HETATM 1886 O  O   . HOH   C 3 .   ? 10.46078  -17.51849 -38.84708 1.000 48.10918 ? 629 HOH   A O   1 
HETATM 1887 O  O   . HOH   C 3 .   ? 1.82647   -18.36008 0.05132   1.000 35.66452 ? 630 HOH   A O   1 
HETATM 1888 O  O   . HOH   C 3 .   ? -3.78829  -33.02746 -10.98762 1.000 50.47507 ? 631 HOH   A O   1 
HETATM 1889 O  O   . HOH   C 3 .   ? 1.13367   -8.53619  -4.14595  1.000 36.47040 ? 632 HOH   A O   1 
HETATM 1890 O  O   . HOH   C 3 .   ? 8.22675   -25.81928 -25.91571 1.000 34.83778 ? 633 HOH   A O   1 
HETATM 1891 O  O   . HOH   C 3 .   ? -5.50495  -12.22530 -42.01968 1.000 45.76593 ? 634 HOH   A O   1 
HETATM 1892 O  O   . HOH   C 3 .   ? 3.20051   -6.76636  -20.59815 1.000 35.35438 ? 635 HOH   A O   1 
HETATM 1893 O  O   . HOH   C 3 .   ? -18.05731 -34.08547 -10.93767 1.000 64.34816 ? 636 HOH   A O   1 
HETATM 1894 O  O   . HOH   C 3 .   ? -2.06031  -15.74848 0.00000   1.000 41.60697 ? 637 HOH   A O   1 
HETATM 1895 O  O   . HOH   C 3 .   ? 4.32372   -21.90513 -39.33173 1.000 46.52291 ? 638 HOH   A O   1 
HETATM 1896 O  O   . HOH   C 3 .   ? -2.00476  -26.91290 -25.19276 1.000 44.94425 ? 639 HOH   A O   1 
HETATM 1897 O  O   . HOH   C 3 .   ? -14.02499 -0.64371  -13.52623 1.000 35.58915 ? 640 HOH   A O   1 
HETATM 1898 O  O   . HOH   C 3 .   ? -17.13427 -4.69360  -17.52627 1.000 37.03524 ? 641 HOH   A O   1 
HETATM 1899 O  O   . HOH   C 3 .   ? 14.38222  -22.41848 -17.17222 1.000 33.14795 ? 642 HOH   A O   1 
HETATM 1900 O  O   . HOH   C 3 .   ? 4.64722   -1.91315  -18.32099 1.000 38.28823 ? 643 HOH   A O   1 
HETATM 1901 O  O   . HOH   C 3 .   ? 1.90071   -25.78327 -29.26742 1.000 33.43573 ? 644 HOH   A O   1 
HETATM 1902 O  O   . HOH   C 3 .   ? -15.341   -23.218   -30.308   1.000 35.92120 ? 645 HOH   A O   1 
HETATM 1903 O  O   . HOH   C 3 .   ? 12.04643  -27.61841 -23.25820 1.000 47.39254 ? 646 HOH   A O   1 
HETATM 1904 O  O   . HOH   C 3 .   ? 0.07830   -18.97115 -1.92392  1.000 37.17376 ? 647 HOH   A O   1 
HETATM 1905 O  O   . HOH   C 3 .   ? -0.34866  -1.06851  -22.72139 1.000 43.12450 ? 648 HOH   A O   1 
HETATM 1906 O  O   . HOH   C 3 .   ? -13.92638 -14.18427 -3.03215  1.000 32.53760 ? 649 HOH   A O   1 
HETATM 1907 O  O   . HOH   C 3 .   ? 2.72521   -4.53893  -31.43228 1.000 52.30557 ? 650 HOH   A O   1 
HETATM 1908 O  O   . HOH   C 3 .   ? 3.43735   -8.00481  -2.15571  1.000 49.88797 ? 651 HOH   A O   1 
HETATM 1909 O  O   . HOH   C 3 .   ? -12.45540 -16.33990 -28.15965 1.000 32.51814 ? 652 HOH   A O   1 
HETATM 1910 O  O   . HOH   C 3 .   ? 5.51094   1.55281   -16.71468 1.000 38.25125 ? 653 HOH   A O   1 
HETATM 1911 O  O   . HOH   C 3 .   ? 12.15976  -25.32119 -38.40747 1.000 31.67070 ? 654 HOH   A O   1 
HETATM 1912 O  O   . HOH   C 3 .   ? -9.03274  -5.67818  -39.74680 1.000 41.53839 ? 655 HOH   A O   1 
HETATM 1913 O  O   . HOH   C 3 .   ? 14.791    -7.999    -30.196   1.000 41.03508 ? 656 HOH   A O   1 
HETATM 1914 O  O   . HOH   C 3 .   ? 1.80024   -2.98281  -12.84989 1.000 43.76399 ? 657 HOH   A O   1 
HETATM 1915 O  O   . HOH   C 3 .   ? -0.16189  -9.00785  -2.87948  1.000 48.85476 ? 658 HOH   A O   1 
HETATM 1916 O  O   . HOH   C 3 .   ? -11.46680 -9.45150  -39.67902 1.000 47.14285 ? 659 HOH   A O   1 
HETATM 1917 O  O   . HOH   C 3 .   ? -3.21478  0.96364   -36.82529 1.000 55.07750 ? 660 HOH   A O   1 
HETATM 1918 O  O   . HOH   C 3 .   ? 15.61203  -12.58923 -7.08735  1.000 49.91645 ? 661 HOH   A O   1 
HETATM 1919 O  O   . HOH   C 3 .   ? -14.53471 -29.03775 -17.25797 1.000 45.14919 ? 662 HOH   A O   1 
HETATM 1920 O  O   . HOH   C 3 .   ? -16.28197 -34.19565 -10.64934 1.000 67.71101 ? 663 HOH   A O   1 
HETATM 1921 O  O   . HOH   C 3 .   ? 7.74633   -13.92447 -38.16726 1.000 35.61189 ? 664 HOH   A O   1 
HETATM 1922 O  O   . HOH   C 3 .   ? -7.83746  -20.93600 -37.58875 1.000 46.90220 ? 665 HOH   A O   1 
HETATM 1923 O  O   . HOH   C 3 .   ? 3.43910   -9.13051  -39.13035 1.000 40.67656 ? 666 HOH   A O   1 
HETATM 1924 O  O   . HOH   C 3 .   ? -9.82821  -26.06382 -20.81806 1.000 28.93905 ? 667 HOH   A O   1 
HETATM 1925 O  O   . HOH   C 3 .   ? 16.072    1.462     -15.403   1.000 48.70660 ? 668 HOH   A O   1 
HETATM 1926 O  O   . HOH   C 3 .   ? 2.22752   -0.96422  -26.05895 1.000 43.15837 ? 669 HOH   A O   1 
HETATM 1927 O  O   . HOH   C 3 .   ? 19.10725  -8.47302  -17.73162 1.000 42.29390 ? 670 HOH   A O   1 
HETATM 1928 O  O   . HOH   C 3 .   ? 11.11327  -1.36653  -17.42424 1.000 38.07768 ? 671 HOH   A O   1 
HETATM 1929 O  O   . HOH   C 3 .   ? -3.40644  -26.96539 -3.04553  1.000 47.80697 ? 672 HOH   A O   1 
HETATM 1930 O  O   . HOH   C 3 .   ? -18.70206 -11.64917 -21.08927 1.000 27.84931 ? 673 HOH   A O   1 
HETATM 1931 O  O   . HOH   C 3 .   ? -10.50633 -8.73473  -1.47963  1.000 39.41662 ? 674 HOH   A O   1 
HETATM 1932 O  O   . HOH   C 3 .   ? -6.132    6.706     -35.996   1.000 47.71221 ? 675 HOH   A O   1 
HETATM 1933 O  O   . HOH   C 3 .   ? 6.66794   -21.43907 -2.69659  1.000 35.28495 ? 676 HOH   A O   1 
HETATM 1934 O  O   . HOH   C 3 .   ? -2.30864  -0.89162  -30.78424 1.000 46.30714 ? 677 HOH   A O   1 
HETATM 1935 O  O   . HOH   C 3 .   ? -5.247    -25.230   -1.244    1.000 56.97772 ? 678 HOH   A O   1 
HETATM 1936 O  O   . HOH   C 3 .   ? 3.62999   -0.18754  -16.56096 1.000 44.18336 ? 679 HOH   A O   1 
HETATM 1937 O  O   . HOH   C 3 .   ? -16.46304 -18.22791 -2.90175  1.000 47.95498 ? 680 HOH   A O   1 
HETATM 1938 O  O   . HOH   C 3 .   ? 6.18969   -30.02330 -24.73324 1.000 51.77789 ? 681 HOH   A O   1 
HETATM 1939 O  O   . HOH   C 3 .   ? -10.75921 -22.71747 -24.30750 1.000 52.65037 ? 682 HOH   A O   1 
HETATM 1940 O  O   . HOH   C 3 .   ? -6.03803  3.56656   -34.41140 1.000 42.70301 ? 683 HOH   A O   1 
HETATM 1941 O  O   . HOH   C 3 .   ? -6.837    -23.310   -1.667    1.000 43.74713 ? 684 HOH   A O   1 
HETATM 1942 O  O   . HOH   C 3 .   ? 5.50696   -3.30130  -23.66646 1.000 44.87333 ? 685 HOH   A O   1 
HETATM 1943 O  O   . HOH   C 3 .   ? 8.48726   -29.76652 -30.89957 1.000 52.01512 ? 686 HOH   A O   1 
HETATM 1944 O  O   . HOH   C 3 .   ? 7.87764   -29.00550 -28.30260 1.000 46.44083 ? 687 HOH   A O   1 
HETATM 1945 O  O   . HOH   C 3 .   ? 2.29528   -0.78739  -14.28467 1.000 47.18496 ? 688 HOH   A O   1 
HETATM 1946 O  O   . HOH   C 3 .   ? 17.15094  0.38834   -17.70167 1.000 43.30567 ? 689 HOH   A O   1 
HETATM 1947 O  O   . HOH   C 3 .   ? 2.92534   -4.70954  -20.01152 1.000 43.89011 ? 690 HOH   A O   1 
HETATM 1948 O  O   . HOH   C 3 .   ? -10.03880 -28.95827 -31.03416 1.000 43.24119 ? 691 HOH   A O   1 
HETATM 1949 O  O   . HOH   C 3 .   ? -5.52936  1.72591   -36.79359 1.000 54.11137 ? 692 HOH   A O   1 
HETATM 1950 O  O   . HOH   C 3 .   ? -13.92520 -13.61170 -38.35706 1.000 47.88805 ? 693 HOH   A O   1 
HETATM 1951 O  O   . HOH   C 3 .   ? 5.76606   -13.00679 -39.95662 1.000 30.75988 ? 694 HOH   A O   1 
HETATM 1952 O  O   . HOH   C 3 .   ? -10.593   -22.508   4.300     1.000 42.92578 ? 695 HOH   A O   1 
HETATM 1953 O  O   . HOH   C 3 .   ? -10.79023 -16.99217 -38.02525 1.000 47.13405 ? 696 HOH   A O   1 
HETATM 1954 O  O   . HOH   C 3 .   ? 10.09458  -29.06741 -24.12834 1.000 47.51008 ? 697 HOH   A O   1 
HETATM 1955 O  O   . HOH   C 3 .   ? 14.38218  -28.34456 -23.52126 1.000 51.96171 ? 698 HOH   A O   1 
HETATM 1956 O  O   . HOH   C 3 .   ? 10.37965  -21.22306 -43.18368 1.000 50.58588 ? 699 HOH   A O   1 
HETATM 1957 O  O   . HOH   C 3 .   ? -0.57386  -26.49825 -30.34919 1.000 44.97197 ? 700 HOH   A O   1 
HETATM 1958 O  O   . HOH   C 3 .   ? -0.00000  -0.00000  -18.33480 0.50  27.36232 ? 701 HOH   A O   1 
HETATM 1959 O  O   . HOH   C 3 .   ? 8.332     -8.382    0.202     1.000 51.09730 ? 702 HOH   A O   1 
HETATM 1960 O  O   . HOH   C 3 .   ? -7.05018  -30.81394 -9.22284  1.000 37.02661 ? 703 HOH   A O   1 
HETATM 1961 O  O   . HOH   C 3 .   ? 20.857    -18.361   -22.263   1.000 42.65307 ? 704 HOH   A O   1 
HETATM 1962 O  O   . HOH   C 3 .   ? -17.23495 4.50666   -31.59889 1.000 49.74116 ? 705 HOH   A O   1 
HETATM 1963 O  O   . HOH   C 3 .   ? -1.925    -23.134   0.953     1.000 45.74451 ? 706 HOH   A O   1 
HETATM 1964 O  O   . HOH   C 3 .   ? 2.06913   -32.02293 -26.89212 1.000 51.52237 ? 707 HOH   A O   1 
HETATM 1965 O  O   . HOH   C 3 .   ? 11.29914  -29.68303 -19.12403 1.000 55.14305 ? 708 HOH   A O   1 
HETATM 1966 O  O   . HOH   C 3 .   ? -12.22824 -19.16221 -28.53792 1.000 48.59740 ? 709 HOH   A O   1 
HETATM 1967 O  O   . HOH   C 3 .   ? 20.28905  -5.84020  -21.21241 1.000 42.82150 ? 710 HOH   A O   1 
HETATM 1968 O  O   . HOH   C 3 .   ? 10.82186  -28.15551 -27.92797 1.000 36.19321 ? 711 HOH   A O   1 
HETATM 1969 O  O   . HOH   C 3 .   ? 11.385    -30.145   -34.445   1.000 37.61303 ? 712 HOH   A O   1 
HETATM 1970 O  O   . HOH   C 3 .   ? -4.28167  -28.09170 -23.43157 1.000 41.56162 ? 713 HOH   A O   1 
HETATM 1971 O  O   . HOH   C 3 .   ? 4.73032   -14.77700 -41.65561 1.000 45.84661 ? 714 HOH   A O   1 
HETATM 1972 O  O   . HOH   C 3 .   ? 20.59851  -7.13893  -16.06598 1.000 50.99259 ? 715 HOH   A O   1 
HETATM 1973 O  O   . HOH   C 3 .   ? 9.52218   -25.31333 -14.73999 1.000 45.57963 ? 716 HOH   A O   1 
HETATM 1974 O  O   . HOH   C 3 .   ? 1.92237   -5.74884  -36.71723 1.000 48.03219 ? 717 HOH   A O   1 
HETATM 1975 O  O   . HOH   C 3 .   ? -16.11346 -13.48827 -3.65855  1.000 44.17240 ? 718 HOH   A O   1 
HETATM 1976 O  O   . HOH   C 3 .   ? 8.710     -10.752   -0.095    1.000 42.99368 ? 719 HOH   A O   1 
HETATM 1977 O  O   . HOH   C 3 .   ? 3.08138   -2.13710  -20.27039 1.000 43.87532 ? 720 HOH   A O   1 
HETATM 1978 O  O   . HOH   C 3 .   ? 21.877    -17.923   -25.052   1.000 40.88187 ? 721 HOH   A O   1 
HETATM 1979 O  O   . HOH   C 3 .   ? 1.02530   -28.92742 -36.02811 1.000 60.20937 ? 722 HOH   A O   1 
HETATM 1980 O  O   . HOH   C 3 .   ? 16.19502  -3.28281  -26.44710 1.000 36.74009 ? 723 HOH   A O   1 
HETATM 1981 O  O   . HOH   C 3 .   ? 4.786     2.827     -13.295   1.000 54.68611 ? 724 HOH   A O   1 
HETATM 1982 O  O   . HOH   C 3 .   ? -1.04408  -10.32902 -45.35395 1.000 53.21565 ? 725 HOH   A O   1 
HETATM 1983 O  O   . HOH   C 3 .   ? 4.040     -1.993    -28.220   1.000 37.60372 ? 726 HOH   A O   1 
HETATM 1984 O  O   . HOH   C 3 .   ? -18.97945 -4.44732  -18.60145 1.000 54.60627 ? 727 HOH   A O   1 
HETATM 1985 O  O   . HOH   C 3 .   ? -16.42682 -12.64709 -6.22275  1.000 39.24549 ? 728 HOH   A O   1 
HETATM 1986 O  O   . HOH   C 3 .   ? -14.73617 -9.56689  -11.36325 1.000 36.50527 ? 729 HOH   A O   1 
HETATM 1987 O  O   . HOH   C 3 .   ? 0.57509   -1.31176  -16.67991 1.000 43.22615 ? 730 HOH   A O   1 
HETATM 1988 O  O   . HOH   C 3 .   ? 19.31226  -20.56130 -22.36094 1.000 37.05228 ? 731 HOH   A O   1 
HETATM 1989 O  O   . HOH   C 3 .   ? -16.91208 -15.52876 -10.30924 1.000 33.13024 ? 732 HOH   A O   1 
HETATM 1990 O  O   . HOH   C 3 .   ? -19.49898 -5.89929  -21.76929 1.000 41.40013 ? 733 HOH   A O   1 
HETATM 1991 O  O   . HOH   C 3 .   ? -12.29775 -13.08841 -0.93959  1.000 30.84173 ? 734 HOH   A O   1 
HETATM 1992 O  O   . HOH   C 3 .   ? -14.56451 -14.10010 -10.17998 1.000 26.75433 ? 735 HOH   A O   1 
HETATM 1993 O  O   . HOH   C 3 .   ? -20.49353 -10.23837 -16.67329 1.000 56.22625 ? 736 HOH   A O   1 
HETATM 1994 O  O   . HOH   C 3 .   ? 9.53027   -12.63269 -37.39923 1.000 45.92045 ? 737 HOH   A O   1 
HETATM 1995 O  O   . HOH   C 3 .   ? -10.447   -11.804   2.025     1.000 33.02503 ? 738 HOH   A O   1 
HETATM 1996 O  O   . HOH   C 3 .   ? 13.71883  -11.58253 -5.19335  1.000 38.52876 ? 739 HOH   A O   1 
HETATM 1997 O  O   . HOH   C 3 .   ? 14.559    -12.949   -2.938    1.000 41.73169 ? 740 HOH   A O   1 
HETATM 1998 O  O   . HOH   C 3 .   ? -19.06804 -8.12088  -15.10969 1.000 48.66202 ? 741 HOH   A O   1 
HETATM 1999 O  O   . HOH   C 3 .   ? -12.10378 -20.54418 -25.38721 1.000 39.30266 ? 742 HOH   A O   1 
HETATM 2000 O  O   . HOH   C 3 .   ? 20.575    -21.103   -26.165   1.000 43.66687 ? 743 HOH   A O   1 
HETATM 2001 O  O   . HOH   C 3 .   ? -2.29775  -26.50173 -28.18075 1.000 52.09790 ? 744 HOH   A O   1 
HETATM 2002 O  O   . HOH   C 3 .   ? -18.41631 -1.80793  -30.42712 1.000 49.78149 ? 745 HOH   A O   1 
HETATM 2003 O  O   . HOH   C 3 .   ? 9.53426   -0.89406  -3.61794  1.000 55.26522 ? 746 HOH   A O   1 
HETATM 2004 O  O   . HOH   C 3 .   ? -9.26316  -32.81124 -8.80968  1.000 49.21707 ? 747 HOH   A O   1 
HETATM 2005 O  O   . HOH   C 3 .   ? -10.01719 -20.58686 -39.64829 1.000 46.87094 ? 748 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   ? 0.51557 0.76084 0.50182 -0.07656 -0.01607 -0.23911 16  GLU A N   
2    C CA  . GLU A 9   ? 0.57046 0.78664 0.54407 -0.04859 -0.02364 -0.22316 16  GLU A CA  
3    C C   . GLU A 9   ? 0.51829 0.71491 0.50006 -0.03318 -0.02841 -0.19937 16  GLU A C   
4    O O   . GLU A 9   ? 0.44524 0.68597 0.43332 -0.01836 -0.03858 -0.19224 16  GLU A O   
5    C CB  . GLU A 9   ? 0.66436 0.93023 0.63125 -0.02194 -0.03502 -0.21852 16  GLU A CB  
6    C CG  . GLU A 9   ? 0.73657 0.97683 0.69376 0.01258  -0.04052 -0.19264 16  GLU A CG  
7    C CD  . GLU A 9   ? 0.92445 1.09402 0.87483 0.01167  -0.03050 -0.18291 16  GLU A CD  
8    O OE1 . GLU A 9   ? 0.83435 0.97095 0.78436 0.03269  -0.03078 -0.15761 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 0.92614 1.07448 0.87059 -0.01005 -0.02072 -0.20135 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.37858 0.50898 0.36003 -0.03481 -0.01931 -0.18419 17  VAL A N   
11   C CA  . VAL A 10  ? 0.31202 0.41993 0.30219 -0.02488 -0.02123 -0.16189 17  VAL A CA  
12   C C   . VAL A 10  ? 0.35015 0.42202 0.33548 -0.00117 -0.02235 -0.13785 17  VAL A C   
13   O O   . VAL A 10  ? 0.37159 0.40513 0.34949 -0.00191 -0.01445 -0.13570 17  VAL A O   
14   C CB  . VAL A 10  ? 0.38043 0.44915 0.37443 -0.04758 -0.00840 -0.16519 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.39492 0.44475 0.39667 -0.03617 -0.01123 -0.14250 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.46308 0.56606 0.46223 -0.07581 -0.00390 -0.19184 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.27363 0.35740 0.26234 0.01901  -0.02993 -0.12071 18  GLU A N   
18   C CA  . GLU A 11  ? 0.26453 0.31702 0.25040 0.03724  -0.02896 -0.10006 18  GLU A CA  
19   C C   . GLU A 11  ? 0.25325 0.27948 0.24779 0.03402  -0.02678 -0.08703 18  GLU A C   
20   O O   . GLU A 11  ? 0.24424 0.28638 0.24546 0.03060  -0.02983 -0.08663 18  GLU A O   
21   C CB  . GLU A 11  ? 0.25757 0.33383 0.23716 0.06126  -0.03377 -0.09046 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.28528 0.39294 0.25368 0.07012  -0.03634 -0.10061 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.40570 0.53733 0.36417 0.09830  -0.03813 -0.08846 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.40228 0.57386 0.36129 0.10540  -0.04244 -0.09030 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.46037 0.57107 0.40887 0.11472  -0.03326 -0.07665 18  GLU A OE2 
26   N N   . THR A 12  ? 0.25470 0.24567 0.24872 0.03630  -0.02152 -0.07655 19  THR A N   
27   C CA  . THR A 12  ? 0.24608 0.21821 0.24706 0.03486  -0.01962 -0.06445 19  THR A CA  
28   C C   . THR A 12  ? 0.24845 0.21627 0.25051 0.04867  -0.02073 -0.05083 19  THR A C   
29   O O   . THR A 12  ? 0.24753 0.20742 0.24483 0.05717  -0.01834 -0.04765 19  THR A O   
30   C CB  . THR A 12  ? 0.26193 0.20334 0.26048 0.02774  -0.01054 -0.06311 19  THR A CB  
31   O OG1 . THR A 12  ? 0.28109 0.21955 0.27582 0.01139  -0.00453 -0.07849 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.25473 0.18582 0.25914 0.02899  -0.00917 -0.05014 19  THR A CG2 
33   N N   . PHE A 13  ? 0.23011 0.20277 0.23768 0.04911  -0.02259 -0.04442 20  PHE A N   
34   C CA  . PHE A 13  ? 0.22623 0.19452 0.23411 0.05704  -0.02039 -0.03531 20  PHE A CA  
35   C C   . PHE A 13  ? 0.26887 0.23233 0.28472 0.05037  -0.01971 -0.02953 20  PHE A C   
36   O O   . PHE A 13  ? 0.23555 0.20168 0.25521 0.04301  -0.02176 -0.03060 20  PHE A O   
37   C CB  . PHE A 13  ? 0.24083 0.22041 0.24397 0.06436  -0.02008 -0.03457 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.23258 0.22754 0.22600 0.07600  -0.02105 -0.03850 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.24043 0.26049 0.23465 0.07209  -0.02696 -0.04860 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.27164 0.25975 0.25440 0.09081  -0.01487 -0.03274 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.26540 0.31115 0.25063 0.08379  -0.02894 -0.05352 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.29846 0.30592 0.26978 0.10554  -0.01564 -0.03485 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.27859 0.31887 0.25153 0.10253  -0.02384 -0.04557 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.23030 0.19043 0.24835 0.05251  -0.01604 -0.02424 21  ALA A N   
45   C CA  . ALA A 14  ? 0.24305 0.20965 0.26846 0.04614  -0.01586 -0.02090 21  ALA A CA  
46   C C   . ALA A 14  ? 0.22415 0.19275 0.24812 0.04236  -0.01328 -0.02298 21  ALA A C   
47   O O   . ALA A 14  ? 0.25102 0.21114 0.26786 0.04715  -0.00693 -0.02358 21  ALA A O   
48   C CB  . ALA A 14  ? 0.24144 0.21227 0.27117 0.04762  -0.01219 -0.01732 21  ALA A CB  
49   N N   . PHE A 15  ? 0.21071 0.18745 0.23879 0.03523  -0.01585 -0.02335 22  PHE A N   
50   C CA  . PHE A 15  ? 0.22615 0.20213 0.25173 0.03004  -0.01065 -0.02617 22  PHE A CA  
51   C C   . PHE A 15  ? 0.24827 0.22444 0.27530 0.02392  -0.00252 -0.02862 22  PHE A C   
52   O O   . PHE A 15  ? 0.25218 0.24246 0.28699 0.02155  -0.00465 -0.02761 22  PHE A O   
53   C CB  . PHE A 15  ? 0.21019 0.19755 0.23980 0.02252  -0.01469 -0.02689 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.19598 0.18373 0.22436 0.02484  -0.01956 -0.02645 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.21461 0.19892 0.23659 0.02931  -0.01695 -0.02835 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.19938 0.19194 0.23183 0.02294  -0.02429 -0.02394 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.21286 0.20628 0.23595 0.02993  -0.02138 -0.02962 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.20522 0.19903 0.23739 0.02108  -0.02629 -0.02587 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.20523 0.20349 0.23447 0.02342  -0.02601 -0.02967 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.24618 0.20709 0.26462 0.02140  0.00914  -0.03216 23  GLN A N   
61   C CA  . GLN A 16  ? 0.25631 0.21782 0.27618 0.00818  0.02029  -0.03892 23  GLN A CA  
62   C C   . GLN A 16  ? 0.25879 0.24977 0.28948 -0.00488 0.01364  -0.04393 23  GLN A C   
63   O O   . GLN A 16  ? 0.24044 0.23903 0.27189 -0.00415 0.00581  -0.04233 23  GLN A O   
64   C CB  . GLN A 16  ? 0.32181 0.25452 0.32657 0.00584  0.03818  -0.04277 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.35623 0.26167 0.34672 0.02198  0.04868  -0.03623 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.49141 0.36318 0.46181 0.02576  0.06961  -0.03636 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.51620 0.38207 0.47670 0.04050  0.06871  -0.03046 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.49409 0.34345 0.45716 0.01258  0.09095  -0.04341 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.26596 0.27839 0.30494 -0.01623 0.01711  -0.05017 24  ALA A N   
70   C CA  . ALA A 17  ? 0.25666 0.30968 0.30608 -0.02497 0.00928  -0.05414 24  ALA A CA  
71   C C   . ALA A 17  ? 0.23403 0.28777 0.27852 -0.03615 0.01164  -0.06189 24  ALA A C   
72   O O   . ALA A 17  ? 0.24446 0.32163 0.29249 -0.03407 0.00121  -0.05908 24  ALA A O   
73   C CB  . ALA A 17  ? 0.26573 0.34981 0.32500 -0.03745 0.01475  -0.06293 24  ALA A CB  
74   N N   . GLU A 18  ? 0.26578 0.28996 0.29933 -0.04618 0.02751  -0.07057 25  GLU A N   
75   C CA  . GLU A 18  ? 0.27052 0.29094 0.29683 -0.05755 0.03301  -0.07931 25  GLU A CA  
76   C C   . GLU A 18  ? 0.26276 0.27357 0.28472 -0.04295 0.02293  -0.06890 25  GLU A C   
77   O O   . GLU A 18  ? 0.26566 0.29053 0.28708 -0.04900 0.01932  -0.07271 25  GLU A O   
78   C CB  . GLU A 18  ? 0.32553 0.30616 0.33651 -0.06904 0.05755  -0.08954 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.37695 0.36690 0.39183 -0.09095 0.07224  -0.10468 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.50642 0.48548 0.52403 -0.08155 0.07540  -0.09722 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.41752 0.38022 0.43226 -0.05797 0.06661  -0.08113 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.60271 0.59203 0.62528 -0.09926 0.08754  -0.10901 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.26522 0.25604 0.28414 -0.02505 0.01891  -0.05727 26  ILE A N   
84   C CA  . ILE A 19  ? 0.25887 0.24646 0.27571 -0.01369 0.01016  -0.04957 26  ILE A CA  
85   C C   . ILE A 19  ? 0.23063 0.24554 0.25836 -0.01122 -0.00499 -0.04392 26  ILE A C   
86   O O   . ILE A 19  ? 0.23925 0.26132 0.26678 -0.01086 -0.01009 -0.04197 26  ILE A O   
87   C CB  . ILE A 19  ? 0.24774 0.21375 0.25753 0.00285  0.01179  -0.04208 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.33087 0.26679 0.32373 0.00746  0.02950  -0.04349 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.24487 0.22036 0.25785 0.01145  0.00028  -0.03631 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.37854 0.29476 0.36385 -0.00420 0.04808  -0.05140 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.20824 0.23624 0.24354 -0.00780 -0.01000 -0.04007 27  ALA A N   
92   C CA  . ALA A 20  ? 0.22429 0.27366 0.26545 -0.00231 -0.01956 -0.03272 27  ALA A CA  
93   C C   . ALA A 20  ? 0.20933 0.28843 0.25222 -0.01041 -0.02145 -0.03685 27  ALA A C   
94   O O   . ALA A 20  ? 0.23238 0.32120 0.27420 -0.00511 -0.02667 -0.03042 27  ALA A O   
95   C CB  . ALA A 20  ? 0.23771 0.29572 0.28408 0.00503  -0.02135 -0.02741 27  ALA A CB  
96   N N   . GLN A 21  ? 0.22481 0.31901 0.26910 -0.02441 -0.01556 -0.04881 28  GLN A N   
97   C CA  . GLN A 21  ? 0.21174 0.34064 0.25695 -0.03489 -0.01707 -0.05669 28  GLN A CA  
98   C C   . GLN A 21  ? 0.26220 0.37551 0.29902 -0.03804 -0.01563 -0.05871 28  GLN A C   
99   O O   . GLN A 21  ? 0.26594 0.40315 0.30199 -0.03628 -0.02159 -0.05634 28  GLN A O   
100  C CB  . GLN A 21  ? 0.24571 0.39357 0.29400 -0.05463 -0.00809 -0.07385 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.41203 0.61198 0.46354 -0.06722 -0.01097 -0.08520 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.61823 0.83550 0.67245 -0.09345 0.00135  -0.10758 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.63771 0.90193 0.69457 -0.10914 0.00097  -0.12244 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.53564 0.71636 0.58820 -0.09925 0.01391  -0.11117 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.21930 0.29413 0.24831 -0.03997 -0.00677 -0.06169 29  LEU A N   
106  C CA  . LEU A 22  ? 0.25716 0.31721 0.27782 -0.03990 -0.00447 -0.06214 29  LEU A CA  
107  C C   . LEU A 22  ? 0.25241 0.31737 0.27598 -0.02697 -0.01520 -0.04927 29  LEU A C   
108  O O   . LEU A 22  ? 0.25820 0.33443 0.27908 -0.02817 -0.01771 -0.04873 29  LEU A O   
109  C CB  . LEU A 22  ? 0.28274 0.30259 0.29314 -0.03665 0.00770  -0.06325 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.29175 0.29673 0.29351 -0.03092 0.01040  -0.06069 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.33033 0.34021 0.32450 -0.04541 0.01797  -0.07240 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.32782 0.30023 0.31901 -0.01921 0.02128  -0.05699 29  LEU A CD2 
113  N N   . MET A 23  ? 0.20857 0.26340 0.23640 -0.01585 -0.01957 -0.03989 30  MET A N   
114  C CA  . MET A 23  ? 0.21494 0.26850 0.24413 -0.00730 -0.02522 -0.03015 30  MET A CA  
115  C C   . MET A 23  ? 0.22843 0.30630 0.25844 -0.00409 -0.02955 -0.02376 30  MET A C   
116  O O   . MET A 23  ? 0.23283 0.31225 0.25960 -0.00158 -0.03021 -0.01874 30  MET A O   
117  C CB  . MET A 23  ? 0.20348 0.24096 0.23540 0.00042  -0.02637 -0.02514 30  MET A CB  
118  C CG  . MET A 23  ? 0.23765 0.25814 0.26662 0.00237  -0.02301 -0.02882 30  MET A CG  
119  S SD  . MET A 23  ? 0.22908 0.23898 0.26004 0.00987  -0.02438 -0.02684 30  MET A SD  
120  C CE  . MET A 23  ? 0.24535 0.25690 0.27900 0.00896  -0.02718 -0.02486 30  MET A CE  
121  N N   . SER A 24  ? 0.22767 0.32761 0.26095 -0.00227 -0.03139 -0.02301 31  SER A N   
122  C CA  . SER A 24  ? 0.21655 0.34611 0.24800 0.00634  -0.03461 -0.01462 31  SER A CA  
123  C C   . SER A 24  ? 0.24968 0.40445 0.27719 -0.00115 -0.03578 -0.02113 31  SER A C   
124  O O   . SER A 24  ? 0.27583 0.44394 0.29760 0.00806  -0.03710 -0.01193 31  SER A O   
125  C CB  . SER A 24  ? 0.35497 0.51151 0.39112 0.01265  -0.03633 -0.01211 31  SER A CB  
126  O OG  . SER A 24  ? 0.51567 0.69598 0.55732 -0.00233 -0.03593 -0.02723 31  SER A OG  
127  N N   . LEU A 25  ? 0.22376 0.38179 0.25174 -0.01764 -0.03289 -0.03707 32  LEU A N   
128  C CA  . LEU A 25  ? 0.24150 0.42022 0.26379 -0.02713 -0.03229 -0.04604 32  LEU A CA  
129  C C   . LEU A 25  ? 0.26123 0.41586 0.27711 -0.02282 -0.03113 -0.03981 32  LEU A C   
130  O O   . LEU A 25  ? 0.27008 0.44438 0.28032 -0.02030 -0.03308 -0.03722 32  LEU A O   
131  C CB  . LEU A 25  ? 0.27847 0.45560 0.29955 -0.04805 -0.02430 -0.06633 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.35286 0.53820 0.36505 -0.06329 -0.01877 -0.08112 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.42337 0.61783 0.43497 -0.08645 -0.00850 -0.10322 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.44182 0.58423 0.44516 -0.06150 -0.01215 -0.07911 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.22039 0.33734 0.23694 -0.02127 -0.02770 -0.03758 33  ILE A N   
136  C CA  . ILE A 26  ? 0.25692 0.35717 0.26967 -0.01796 -0.02621 -0.03278 33  ILE A CA  
137  C C   . ILE A 26  ? 0.26414 0.36908 0.27654 -0.00686 -0.02888 -0.01861 33  ILE A C   
138  O O   . ILE A 26  ? 0.25826 0.36584 0.26559 -0.00524 -0.02750 -0.01468 33  ILE A O   
139  C CB  . ILE A 26  ? 0.23083 0.30113 0.24520 -0.01682 -0.02236 -0.03395 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.26677 0.32473 0.27452 -0.02446 -0.01402 -0.04549 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.24900 0.31096 0.26354 -0.01232 -0.02204 -0.02796 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.28105 0.31411 0.28760 -0.01819 -0.00885 -0.04472 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.26229 0.36503 0.27782 0.00152  -0.03007 -0.01032 34  ILE A N   
144  C CA  . ILE A 27  ? 0.27682 0.37249 0.28791 0.01299  -0.02690 0.00394  34  ILE A CA  
145  C C   . ILE A 27  ? 0.29840 0.42464 0.30133 0.02319  -0.02760 0.01224  34  ILE A C   
146  O O   . ILE A 27  ? 0.34134 0.46197 0.33557 0.03179  -0.02214 0.02336  34  ILE A O   
147  C CB  . ILE A 27  ? 0.28203 0.35865 0.29589 0.01915  -0.02452 0.00943  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.28168 0.33277 0.30140 0.01072  -0.02330 0.00205  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.32768 0.39346 0.33214 0.03291  -0.01640 0.02500  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.28973 0.32702 0.31264 0.01356  -0.02267 0.00218  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.25504 0.41738 0.25983 0.02243  -0.03312 0.00647  35  ASN A N   
152  C CA  . ASN A 28  ? 0.29340 0.49669 0.29063 0.03656  -0.03481 0.01545  35  ASN A CA  
153  C C   . ASN A 28  ? 0.35944 0.59841 0.35196 0.02914  -0.03844 0.00609  35  ASN A C   
154  O O   . ASN A 28  ? 0.39554 0.66731 0.37828 0.04395  -0.03892 0.01612  35  ASN A O   
155  C CB  . ASN A 28  ? 0.32496 0.55926 0.32769 0.04263  -0.03861 0.01531  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.42249 0.62649 0.42451 0.05698  -0.03318 0.02922  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.46625 0.64115 0.45810 0.07026  -0.02468 0.04431  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.54986 0.75723 0.56131 0.05306  -0.03565 0.02321  35  ASN A ND2 
159  N N   . THR A 29  ? 0.27523 0.50846 0.27178 0.00848  -0.03918 -0.01226 36  THR A N   
160  C CA  . THR A 29  ? 0.27233 0.53696 0.26254 -0.00111 -0.04061 -0.02407 36  THR A CA  
161  C C   . THR A 29  ? 0.27370 0.52566 0.25373 0.00729  -0.03754 -0.01347 36  THR A C   
162  O O   . THR A 29  ? 0.29667 0.50604 0.27783 0.00736  -0.03275 -0.00787 36  THR A O   
163  C CB  . THR A 29  ? 0.29691 0.54550 0.29005 -0.02473 -0.03676 -0.04580 36  THR A CB  
164  O OG1 . THR A 29  ? 0.33146 0.59037 0.33301 -0.03417 -0.03683 -0.05625 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.32297 0.59949 0.30720 -0.03734 -0.03552 -0.06080 36  THR A CG2 
166  N N   . PHE A 30  ? 0.26021 0.55363 0.23023 0.01437  -0.03985 -0.01130 37  PHE A N   
167  C CA  . PHE A 30  ? 0.27823 0.56093 0.23732 0.02014  -0.03569 -0.00342 37  PHE A CA  
168  C C   . PHE A 30  ? 0.31827 0.58329 0.27765 -0.00035 -0.03322 -0.02131 37  PHE A C   
169  O O   . PHE A 30  ? 0.29043 0.58143 0.24791 -0.01569 -0.03474 -0.04052 37  PHE A O   
170  C CB  . PHE A 30  ? 0.27248 0.60737 0.21813 0.03562  -0.03829 0.00417  37  PHE A CB  
171  C CG  . PHE A 30  ? 0.28646 0.60916 0.21922 0.04281  -0.03250 0.01358  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.35775 0.63980 0.28541 0.05761  -0.02290 0.03454  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.29904 0.64763 0.22423 0.03228  -0.03442 -0.00032 37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.32623 0.59587 0.24245 0.06265  -0.01551 0.04279  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.33378 0.67066 0.24699 0.03929  -0.02849 0.00871  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.31151 0.60956 0.22081 0.05475  -0.01911 0.03086  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.27382 0.49588 0.23447 -0.00083 -0.02749 -0.01587 38  TYR A N   
178  C CA  . TYR A 31  ? 0.26271 0.46417 0.22255 -0.01536 -0.02307 -0.02977 38  TYR A CA  
179  C C   . TYR A 31  ? 0.25270 0.42620 0.21199 -0.00915 -0.01760 -0.01844 38  TYR A C   
180  O O   . TYR A 31  ? 0.26184 0.40986 0.22980 -0.00590 -0.01573 -0.01081 38  TYR A O   
181  C CB  . TYR A 31  ? 0.28338 0.46186 0.25182 -0.02638 -0.02136 -0.04112 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.26732 0.41925 0.23131 -0.03586 -0.01313 -0.05212 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.32332 0.48436 0.27648 -0.04899 -0.00763 -0.06911 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.35664 0.47670 0.32565 -0.03094 -0.00921 -0.04615 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.46628 0.59731 0.41130 -0.05462 0.00366  -0.07757 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.32533 0.42401 0.28781 -0.03418 -0.00006 -0.05355 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.39016 0.49031 0.33951 -0.04487 0.00740  -0.06812 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.65164 0.72451 0.59065 -0.04536 0.02018  -0.07406 38  TYR A OH  
189  N N   . SER A 32  ? 0.26277 0.44422 0.21208 -0.00902 -0.01440 -0.01899 39  SER A N   
190  C CA  . SER A 32  ? 0.26666 0.42944 0.21523 -0.00279 -0.00819 -0.00712 39  SER A CA  
191  C C   . SER A 32  ? 0.26925 0.40587 0.22529 -0.00978 -0.00354 -0.01316 39  SER A C   
192  O O   . SER A 32  ? 0.29439 0.41711 0.25621 -0.00716 0.00110  -0.00490 39  SER A O   
193  C CB  . SER A 32  ? 0.28171 0.46504 0.21573 0.00214  -0.00576 -0.00384 39  SER A CB  
194  O OG  . SER A 32  ? 0.29158 0.50294 0.21685 0.01520  -0.00869 0.00681  39  SER A OG  
195  N N   . ASN A 33  ? 0.28097 0.41177 0.23590 -0.01800 -0.00263 -0.02739 40  ASN A N   
196  C CA  . ASN A 33  ? 0.27923 0.38981 0.23612 -0.01903 0.00396  -0.03142 40  ASN A CA  
197  C C   . ASN A 33  ? 0.24618 0.34189 0.21613 -0.01667 0.00265  -0.02888 40  ASN A C   
198  O O   . ASN A 33  ? 0.25594 0.33827 0.22526 -0.01719 0.00585  -0.03578 40  ASN A O   
199  C CB  . ASN A 33  ? 0.30741 0.41208 0.25156 -0.02627 0.01045  -0.04644 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.33243 0.41512 0.27350 -0.02192 0.02047  -0.04835 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.35084 0.43542 0.29720 -0.01456 0.02187  -0.03993 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.37560 0.43807 0.30662 -0.02583 0.02976  -0.05947 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.24111 0.27612 0.22016 -0.02666 -0.03117 -0.00067 41  LYS A N   
204  C CA  . LYS A 34  ? 0.22666 0.28865 0.23423 -0.01692 -0.02091 -0.00067 41  LYS A CA  
205  C C   . LYS A 34  ? 0.23015 0.27181 0.23277 -0.01154 -0.01136 -0.01278 41  LYS A C   
206  O O   . LYS A 34  ? 0.20975 0.26562 0.22795 -0.00803 -0.00773 -0.01282 41  LYS A O   
207  C CB  . LYS A 34  ? 0.23101 0.30918 0.25271 -0.00059 -0.01259 0.00018  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.21485 0.32466 0.24808 0.00151  -0.01861 0.01552  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.24171 0.35266 0.27677 0.02255  -0.01105 0.01360  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.23654 0.38173 0.28198 0.03167  -0.01414 0.03056  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.21650 0.40531 0.28060 0.04298  -0.01025 0.04644  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.23206 0.24397 0.21258 -0.00819 -0.00635 -0.02033 42  GLU A N   
213  C CA  . GLU A 35  ? 0.23471 0.23741 0.21709 0.00013  0.00464  -0.02646 42  GLU A CA  
214  C C   . GLU A 35  ? 0.24235 0.23834 0.22135 -0.00518 0.00071  -0.02912 42  GLU A C   
215  O O   . GLU A 35  ? 0.24547 0.24206 0.23378 0.00133  0.00866  -0.03239 42  GLU A O   
216  C CB  . GLU A 35  ? 0.26679 0.24666 0.22411 0.00993  0.01343  -0.02773 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.29300 0.23328 0.20367 0.00934  0.00595  -0.03201 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.40589 0.32157 0.28073 0.02792  0.01750  -0.03178 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.45475 0.38601 0.33896 0.03252  0.02452  -0.02572 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.55541 0.43479 0.38896 0.04069  0.02005  -0.03623 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.24738 0.23744 0.21438 -0.01927 -0.01400 -0.02474 43  ILE A N   
222  C CA  . ILE A 36  ? 0.25770 0.23788 0.21922 -0.02733 -0.02080 -0.02456 43  ILE A CA  
223  C C   . ILE A 36  ? 0.22278 0.23747 0.21834 -0.02437 -0.01417 -0.02156 43  ILE A C   
224  O O   . ILE A 36  ? 0.22453 0.23223 0.21809 -0.02789 -0.01606 -0.02240 43  ILE A O   
225  C CB  . ILE A 36  ? 0.33107 0.29521 0.27197 -0.04936 -0.04473 -0.01465 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.28748 0.30115 0.26228 -0.06021 -0.05198 0.00341  43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.39653 0.30636 0.28505 -0.04930 -0.05474 -0.02099 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.31978 0.37316 0.32506 -0.06876 -0.05514 0.01906  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.19492 0.24012 0.21417 -0.01548 -0.00743 -0.01827 44  PHE A N   
230  C CA  . PHE A 37  ? 0.19474 0.26086 0.23195 -0.00638 -0.00133 -0.01712 44  PHE A CA  
231  C C   . PHE A 37  ? 0.17776 0.22403 0.21215 -0.00152 0.00434  -0.02746 44  PHE A C   
232  O O   . PHE A 37  ? 0.18647 0.23875 0.22622 -0.00027 0.00500  -0.02696 44  PHE A O   
233  C CB  . PHE A 37  ? 0.17666 0.25798 0.22200 0.00951  0.00393  -0.01582 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.18554 0.24299 0.22606 0.01679  0.00713  -0.02578 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.20850 0.25553 0.24447 0.01382  0.00708  -0.02644 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.21713 0.26251 0.25739 0.02409  0.00758  -0.03104 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.21102 0.24373 0.24856 0.01670  0.00817  -0.02827 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.22577 0.25161 0.26573 0.02412  0.00460  -0.03348 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.21380 0.23703 0.25555 0.01967  0.00530  -0.03018 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.16939 0.19692 0.19721 0.00201  0.00882  -0.03324 45  LEU A N   
241  C CA  . LEU A 38  ? 0.17666 0.19659 0.21000 0.00720  0.01382  -0.03657 45  LEU A CA  
242  C C   . LEU A 38  ? 0.21659 0.22165 0.23682 0.00467  0.01363  -0.03876 45  LEU A C   
243  O O   . LEU A 38  ? 0.22055 0.22680 0.24829 0.00640  0.01451  -0.03987 45  LEU A O   
244  C CB  . LEU A 38  ? 0.18421 0.20152 0.22185 0.01232  0.01944  -0.03345 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.19519 0.21611 0.24793 0.01561  0.02254  -0.02851 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.22332 0.24459 0.28683 0.01272  0.01303  -0.02977 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.23134 0.26190 0.29465 0.01859  0.02783  -0.01647 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.21451 0.19820 0.20862 0.00081  0.00958  -0.03948 46  ARG A N   
249  C CA  . ARG A 39  ? 0.25353 0.20926 0.22301 -0.00180 0.00412  -0.04183 46  ARG A CA  
250  C C   . ARG A 39  ? 0.26627 0.23641 0.24932 -0.01441 -0.00450 -0.03731 46  ARG A C   
251  O O   . ARG A 39  ? 0.26468 0.22419 0.24366 -0.01350 -0.00483 -0.03894 46  ARG A O   
252  C CB  . ARG A 39  ? 0.33073 0.24766 0.25753 -0.00633 -0.00673 -0.04297 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.35991 0.23237 0.24855 -0.01249 -0.02068 -0.04478 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.44673 0.26926 0.28392 -0.02169 -0.04046 -0.04485 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.48045 0.32646 0.33706 -0.04922 -0.05959 -0.03212 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.48304 0.30337 0.31089 -0.06262 -0.07902 -0.02741 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.53758 0.29926 0.30706 -0.04909 -0.08188 -0.03774 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.52370 0.37948 0.38020 -0.08819 -0.09602 -0.00932 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.21307 0.21202 0.21327 -0.02369 -0.01001 -0.02857 47  GLU A N   
260  C CA  . GLU A 40  ? 0.20397 0.22653 0.21859 -0.03317 -0.01589 -0.01750 47  GLU A CA  
261  C C   . GLU A 40  ? 0.21151 0.24922 0.24212 -0.02007 -0.00507 -0.02147 47  GLU A C   
262  O O   . GLU A 40  ? 0.20451 0.24346 0.23602 -0.02413 -0.00749 -0.01776 47  GLU A O   
263  C CB  . GLU A 40  ? 0.18626 0.24713 0.21850 -0.04041 -0.02099 -0.00091 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.22760 0.27327 0.24388 -0.05930 -0.03851 0.00730  47  GLU A CG  
265  C CD  . GLU A 40  ? 0.31971 0.32286 0.30613 -0.07891 -0.05829 0.00973  47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.30604 0.31592 0.29962 -0.08609 -0.06195 0.01715  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.40882 0.36474 0.35754 -0.08572 -0.07168 0.00405  47  GLU A OE2 
268  N N   . LEU A 41  ? 0.17759 0.22085 0.21633 -0.00584 0.00353  -0.02812 48  LEU A N   
269  C CA  . LEU A 41  ? 0.18330 0.22909 0.22757 0.00522  0.00767  -0.03190 48  LEU A CA  
270  C C   . LEU A 41  ? 0.20373 0.22925 0.24552 0.00453  0.00805  -0.03799 48  LEU A C   
271  O O   . LEU A 41  ? 0.20425 0.22987 0.24729 0.00701  0.00738  -0.03824 48  LEU A O   
272  C CB  . LEU A 41  ? 0.18696 0.23075 0.23152 0.01734  0.00918  -0.03577 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.20610 0.27000 0.24921 0.02644  0.01096  -0.02897 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.23649 0.28305 0.26961 0.03875  0.00887  -0.03448 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.20473 0.29282 0.24689 0.03650  0.01490  -0.01918 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.16973 0.18004 0.20663 0.00462  0.01042  -0.04081 49  ILE A N   
277  C CA  . ILE A 42  ? 0.18730 0.18481 0.22224 0.00925  0.01345  -0.04201 49  ILE A CA  
278  C C   . ILE A 42  ? 0.22062 0.20234 0.23921 0.00401  0.00894  -0.04241 49  ILE A C   
279  O O   . ILE A 42  ? 0.22141 0.19909 0.24216 0.00712  0.00925  -0.04258 49  ILE A O   
280  C CB  . ILE A 42  ? 0.19995 0.19066 0.23002 0.01780  0.02104  -0.04007 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.20085 0.21012 0.25394 0.01917  0.02233  -0.03427 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.22837 0.20688 0.24911 0.02929  0.02718  -0.03785 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.22171 0.23587 0.27516 0.02784  0.03181  -0.02621 49  ILE A CD1 
284  N N   . SER A 43  ? 0.22300 0.19349 0.22417 -0.00661 0.00112  -0.04029 50  SER A N   
285  C CA  . SER A 43  ? 0.23018 0.18028 0.21321 -0.01729 -0.00961 -0.03694 50  SER A CA  
286  C C   . SER A 43  ? 0.22817 0.20575 0.23176 -0.02251 -0.01056 -0.02995 50  SER A C   
287  O O   . SER A 43  ? 0.23634 0.20093 0.23296 -0.02440 -0.01394 -0.02909 50  SER A O   
288  C CB  . SER A 43  ? 0.29794 0.23043 0.25941 -0.03399 -0.02500 -0.03080 50  SER A CB  
289  O OG  . SER A 43  ? 0.38820 0.30067 0.33353 -0.05113 -0.04187 -0.02238 50  SER A OG  
290  N N   . ASN A 44  ? 0.20819 0.22166 0.23223 -0.02103 -0.00665 -0.02412 51  ASN A N   
291  C CA  . ASN A 44  ? 0.18933 0.22820 0.22502 -0.01778 -0.00401 -0.01653 51  ASN A CA  
292  C C   . ASN A 44  ? 0.18421 0.21052 0.21915 -0.00593 0.00051  -0.02645 51  ASN A C   
293  O O   . ASN A 44  ? 0.19821 0.22635 0.23175 -0.00649 -0.00075 -0.02256 51  ASN A O   
294  C CB  . ASN A 44  ? 0.18656 0.26020 0.23369 -0.00789 0.00226  -0.00897 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.27798 0.37971 0.33449 -0.02109 -0.00338 0.00982  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.24796 0.33867 0.30001 -0.04249 -0.01662 0.01827  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.26621 0.40153 0.33263 -0.00831 0.00395  0.01880  51  ASN A ND2 
298  N N   . SER A 45  ? 0.17297 0.18879 0.21050 0.00275  0.00367  -0.03577 52  SER A N   
299  C CA  . SER A 45  ? 0.19366 0.19972 0.23433 0.00928  0.00289  -0.03996 52  SER A CA  
300  C C   . SER A 45  ? 0.18906 0.18016 0.22506 0.00688  0.00223  -0.03964 52  SER A C   
301  O O   . SER A 45  ? 0.20219 0.19061 0.23877 0.00877  -0.00022 -0.03891 52  SER A O   
302  C CB  . SER A 45  ? 0.17399 0.17701 0.22390 0.01326  0.00257  -0.04202 52  SER A CB  
303  O OG  . SER A 45  ? 0.21140 0.21630 0.25769 0.01755  -0.00064 -0.04346 52  SER A OG  
304  N N   . SER A 46  ? 0.19640 0.17153 0.22073 0.00560  0.00355  -0.04044 53  SER A N   
305  C CA  . SER A 46  ? 0.23129 0.18117 0.23864 0.00912  0.00244  -0.04073 53  SER A CA  
306  C C   . SER A 46  ? 0.22763 0.17085 0.22597 -0.00221 -0.00625 -0.03679 53  SER A C   
307  O O   . SER A 46  ? 0.24617 0.17847 0.24032 0.00162  -0.00754 -0.03633 53  SER A O   
308  C CB  . SER A 46  ? 0.26025 0.18057 0.23943 0.01420  0.00326  -0.04332 53  SER A CB  
309  O OG  . SER A 46  ? 0.30785 0.19131 0.25683 0.02297  0.00098  -0.04450 53  SER A OG  
310  N N   . ASP A 47  ? 0.22412 0.17950 0.22287 -0.01653 -0.01250 -0.02986 54  ASP A N   
311  C CA  . ASP A 47  ? 0.25824 0.21741 0.25428 -0.02997 -0.02128 -0.01854 54  ASP A CA  
312  C C   . ASP A 47  ? 0.21647 0.19783 0.22672 -0.02138 -0.01494 -0.01719 54  ASP A C   
313  O O   . ASP A 47  ? 0.23230 0.20571 0.23654 -0.02554 -0.01957 -0.01212 54  ASP A O   
314  C CB  . ASP A 47  ? 0.22371 0.20898 0.22815 -0.04604 -0.02782 -0.00326 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.31420 0.26534 0.29474 -0.06272 -0.04406 -0.00025 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.35391 0.25312 0.30169 -0.05832 -0.04964 -0.01128 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.35092 0.32500 0.34128 -0.07812 -0.05224 0.01462  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.18951 0.19093 0.21177 -0.00890 -0.00688 -0.02187 55  ALA A N   
319  C CA  . ALA A 48  ? 0.20862 0.21872 0.23128 0.00152  -0.00451 -0.02193 55  ALA A CA  
320  C C   . ALA A 48  ? 0.19744 0.18607 0.21891 0.00574  -0.00773 -0.02899 55  ALA A C   
321  O O   . ALA A 48  ? 0.21008 0.19675 0.22647 0.00861  -0.01017 -0.02681 55  ALA A O   
322  C CB  . ALA A 48  ? 0.19627 0.21682 0.21793 0.01505  -0.00038 -0.02583 55  ALA A CB  
323  N N   . LEU A 49  ? 0.19941 0.17655 0.22657 0.00804  -0.00700 -0.03426 56  LEU A N   
324  C CA  . LEU A 49  ? 0.21321 0.18037 0.24529 0.01383  -0.00864 -0.03421 56  LEU A CA  
325  C C   . LEU A 49  ? 0.23050 0.17870 0.24786 0.01230  -0.01036 -0.03192 56  LEU A C   
326  O O   . LEU A 49  ? 0.23907 0.18293 0.25749 0.01615  -0.01333 -0.02960 56  LEU A O   
327  C CB  . LEU A 49  ? 0.21402 0.18450 0.25822 0.02031  -0.00396 -0.03330 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.18368 0.16777 0.24340 0.01887  -0.00806 -0.03220 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.21789 0.21131 0.28925 0.02211  -0.00157 -0.02826 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.20039 0.18628 0.27165 0.01815  -0.01917 -0.02589 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.22718 0.15830 0.22657 0.00532  -0.01215 -0.03151 57  ASP A N   
332  C CA  . ASP A 50  ? 0.25811 0.15850 0.23377 0.00092  -0.01980 -0.02848 57  ASP A CA  
333  C C   . ASP A 50  ? 0.25458 0.16767 0.23512 -0.00810 -0.02475 -0.02090 57  ASP A C   
334  O O   . ASP A 50  ? 0.27886 0.17308 0.24855 -0.00635 -0.02930 -0.01883 57  ASP A O   
335  C CB  . ASP A 50  ? 0.28773 0.16085 0.23758 -0.01220 -0.02945 -0.02634 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.35102 0.19432 0.27797 0.00127  -0.02594 -0.03433 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.37241 0.22195 0.30696 0.02267  -0.01335 -0.03804 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.39781 0.21134 0.29698 -0.00966 -0.03725 -0.03373 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.23583 0.18126 0.22956 -0.01427 -0.02259 -0.01499 58  LYS A N   
340  C CA  . LYS A 51  ? 0.23783 0.20070 0.23267 -0.01877 -0.02413 -0.00363 58  LYS A CA  
341  C C   . LYS A 51  ? 0.23610 0.19590 0.23103 -0.00587 -0.02252 -0.00919 58  LYS A C   
342  O O   . LYS A 51  ? 0.26579 0.21853 0.25321 -0.00857 -0.02679 -0.00294 58  LYS A O   
343  C CB  . LYS A 51  ? 0.24445 0.24697 0.24966 -0.01871 -0.01776 0.00671  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.26998 0.28552 0.27997 -0.03768 -0.02390 0.02229  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.26786 0.33264 0.29275 -0.03109 -0.01397 0.03588  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.33505 0.41578 0.37063 -0.05052 -0.02194 0.05126  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.37614 0.51192 0.42910 -0.03919 -0.00983 0.06775  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.22871 0.19141 0.23079 0.00566  -0.01983 -0.01868 59  ILE A N   
349  C CA  . ILE A 52  ? 0.23632 0.19184 0.23654 0.01363  -0.02479 -0.02114 59  ILE A CA  
350  C C   . ILE A 52  ? 0.26295 0.20244 0.26766 0.01447  -0.02835 -0.02055 59  ILE A C   
351  O O   . ILE A 52  ? 0.27588 0.20883 0.27651 0.01669  -0.03380 -0.01752 59  ILE A O   
352  C CB  . ILE A 52  ? 0.24022 0.19579 0.24202 0.02093  -0.02873 -0.02730 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.27146 0.21267 0.26283 0.02537  -0.04068 -0.02721 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.25650 0.21378 0.27805 0.01922  -0.02854 -0.02937 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.32229 0.26103 0.28784 0.03206  -0.03927 -0.02424 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.25017 0.18170 0.25856 0.01643  -0.02447 -0.02223 60  ARG A N   
357  C CA  . ARG A 53  ? 0.26037 0.17514 0.26520 0.02565  -0.02457 -0.01956 60  ARG A CA  
358  C C   . ARG A 53  ? 0.29174 0.18238 0.27405 0.02037  -0.03039 -0.01643 60  ARG A C   
359  O O   . ARG A 53  ? 0.30938 0.19192 0.28978 0.02706  -0.03371 -0.01278 60  ARG A O   
360  C CB  . ARG A 53  ? 0.31848 0.22328 0.31843 0.03600  -0.01691 -0.02128 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.40386 0.29164 0.39370 0.05566  -0.01333 -0.01633 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.50150 0.37689 0.47662 0.07430  -0.00269 -0.01671 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.57011 0.48756 0.58114 0.08674  0.00706  -0.00584 60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.58691 0.51302 0.59851 0.09857  0.01813  -0.00343 60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.57063 0.46115 0.54486 0.09996  0.01981  -0.01448 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.43684 0.40884 0.48723 0.10740  0.02543  0.01346  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.28884 0.16893 0.25533 0.00618  -0.03417 -0.01440 61  TYR A N   
368  C CA  . TYR A 54  ? 0.31891 0.17463 0.26422 -0.00444 -0.04428 -0.00661 61  TYR A CA  
369  C C   . TYR A 54  ? 0.32212 0.19726 0.27596 -0.00595 -0.04530 -0.00009 61  TYR A C   
370  O O   . TYR A 54  ? 0.35014 0.20493 0.29190 -0.00443 -0.05139 0.00370  61  TYR A O   
371  C CB  . TYR A 54  ? 0.33319 0.18388 0.26770 -0.02597 -0.05284 0.00207  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.38546 0.20596 0.29687 -0.04245 -0.06905 0.01484  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.42474 0.18301 0.29730 -0.03859 -0.08105 0.01048  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.38054 0.23271 0.30482 -0.05876 -0.07237 0.03338  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.46994 0.19087 0.31564 -0.05580 -0.10059 0.02296  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.42162 0.24860 0.32770 -0.07746 -0.08957 0.04961  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.47824 0.23609 0.34456 -0.07830 -0.10581 0.04360  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.54875 0.27212 0.39136 -0.09926 -0.12755 0.06052  61  TYR A OH  
379  N N   . GLU A 55  ? 0.29544 0.20481 0.26313 -0.00590 -0.03966 0.00132  62  GLU A N   
380  C CA  . GLU A 55  ? 0.31767 0.23907 0.28251 -0.00196 -0.04022 0.00658  62  GLU A CA  
381  C C   . GLU A 55  ? 0.34915 0.25674 0.31569 0.00902  -0.04492 0.00058  62  GLU A C   
382  O O   . GLU A 55  ? 0.36896 0.26957 0.32639 0.00977  -0.04995 0.00596  62  GLU A O   
383  C CB  . GLU A 55  ? 0.32263 0.27182 0.28840 0.00524  -0.03293 0.00699  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.32968 0.30693 0.29856 -0.00329 -0.02689 0.02159  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.45757 0.46295 0.41837 0.01336  -0.01640 0.02644  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.42450 0.41429 0.36942 0.03010  -0.01742 0.01381  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.47622 0.51744 0.44301 0.01093  -0.00873 0.04554  62  GLU A OE2 
388  N N   . SER A 56  ? 0.30271 0.21057 0.28364 0.01661  -0.04421 -0.00654 63  SER A N   
389  C CA  . SER A 56  ? 0.33088 0.23687 0.32222 0.02480  -0.05074 -0.00486 63  SER A CA  
390  C C   . SER A 56  ? 0.35419 0.24212 0.34003 0.03091  -0.05174 0.00026  63  SER A C   
391  O O   . SER A 56  ? 0.35860 0.24873 0.35261 0.03751  -0.05790 0.00609  63  SER A O   
392  C CB  . SER A 56  ? 0.31118 0.23189 0.32584 0.02914  -0.05037 -0.00558 63  SER A CB  
393  O OG  . SER A 56  ? 0.33576 0.25495 0.35681 0.03726  -0.04109 -0.00420 63  SER A OG  
394  N N   . LEU A 57  ? 0.33644 0.20143 0.30403 0.02934  -0.04866 -0.00062 64  LEU A N   
395  C CA  . LEU A 57  ? 0.40724 0.24114 0.35660 0.04007  -0.05122 0.00286  64  LEU A CA  
396  C C   . LEU A 57  ? 0.44480 0.26872 0.38355 0.03449  -0.06012 0.00928  64  LEU A C   
397  O O   . LEU A 57  ? 0.49424 0.30208 0.42632 0.04762  -0.06290 0.01358  64  LEU A O   
398  C CB  . LEU A 57  ? 0.42305 0.21702 0.34015 0.03816  -0.05256 -0.00046 64  LEU A CB  
399  C CG  . LEU A 57  ? 0.44210 0.23607 0.35944 0.04847  -0.04348 -0.00682 64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.47754 0.21599 0.34858 0.04537  -0.05142 -0.01028 64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.43480 0.24484 0.36816 0.07630  -0.03247 -0.00317 64  LEU A CD2 
402  N N   . THR A 58  ? 0.44749 0.28331 0.38357 0.01835  -0.06315 0.01245  65  THR A N   
403  C CA  . THR A 58  ? 0.44408 0.27498 0.36935 0.01361  -0.07010 0.02084  65  THR A CA  
404  C C   . THR A 58  ? 0.48746 0.34287 0.42138 0.01735  -0.07078 0.02063  65  THR A C   
405  O O   . THR A 58  ? 0.54561 0.39620 0.46811 0.01711  -0.07645 0.02718  65  THR A O   
406  C CB  . THR A 58  ? 0.57444 0.40018 0.48424 -0.00583 -0.07397 0.03203  65  THR A CB  
407  O OG1 . THR A 58  ? 0.57131 0.43125 0.49279 -0.01262 -0.06620 0.03400  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.52880 0.31095 0.41622 -0.01305 -0.08279 0.03325  65  THR A CG2 
409  N N   . ASP A 59  ? 0.49803 0.33072 0.36274 0.10411  -0.02533 0.07314  66  ASP A N   
410  C CA  . ASP A 59  ? 0.44590 0.31159 0.31399 0.10175  -0.03718 0.07266  66  ASP A CA  
411  C C   . ASP A 59  ? 0.42798 0.32574 0.32295 0.10239  -0.04498 0.06425  66  ASP A C   
412  O O   . ASP A 59  ? 0.43298 0.33979 0.33705 0.08989  -0.04438 0.05127  66  ASP A O   
413  C CB  . ASP A 59  ? 0.48722 0.35181 0.34208 0.08546  -0.03458 0.06665  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.55917 0.44791 0.40696 0.08465  -0.04554 0.06506  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.55225 0.45984 0.40654 0.09344  -0.05818 0.06854  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.60122 0.48961 0.43572 0.07529  -0.04158 0.06091  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.48077 0.39807 0.39123 0.11682  -0.05222 0.07308  67  PRO A N   
418  C CA  . PRO A 60  ? 0.41855 0.36922 0.35851 0.11577  -0.05944 0.06786  67  PRO A CA  
419  C C   . PRO A 60  ? 0.38223 0.35439 0.32333 0.10053  -0.07224 0.05803  67  PRO A C   
420  O O   . PRO A 60  ? 0.37824 0.36861 0.33999 0.09342  -0.07526 0.04986  67  PRO A O   
421  C CB  . PRO A 60  ? 0.48325 0.45531 0.43999 0.13454  -0.06595 0.08427  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.62616 0.56765 0.56147 0.14886  -0.05791 0.09653  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.53309 0.44126 0.43737 0.13583  -0.05177 0.09028  67  PRO A CD  
424  N N   . SER A 61  ? 0.45302 0.42021 0.36936 0.09595  -0.07898 0.05873  68  SER A N   
425  C CA  . SER A 61  ? 0.41242 0.39166 0.32169 0.08321  -0.09007 0.04802  68  SER A CA  
426  C C   . SER A 61  ? 0.39231 0.36242 0.30262 0.07113  -0.08033 0.03291  68  SER A C   
427  O O   . SER A 61  ? 0.39025 0.36791 0.29805 0.06191  -0.08782 0.02270  68  SER A O   
428  C CB  . SER A 61  ? 0.41842 0.38908 0.29353 0.08338  -0.09662 0.05190  68  SER A CB  
429  O OG  . SER A 61  ? 0.49939 0.44489 0.35290 0.08163  -0.08110 0.05148  68  SER A OG  
430  N N   . LYS A 62  ? 0.37083 0.32321 0.28327 0.07079  -0.06491 0.03169  69  LYS A N   
431  C CA  . LYS A 62  ? 0.36890 0.31745 0.28685 0.06004  -0.05722 0.01952  69  LYS A CA  
432  C C   . LYS A 62  ? 0.35253 0.31900 0.29487 0.05648  -0.06238 0.01218  69  LYS A C   
433  O O   . LYS A 62  ? 0.32309 0.28991 0.26848 0.04769  -0.05991 0.00197  69  LYS A O   
434  C CB  . LYS A 62  ? 0.40148 0.32867 0.31803 0.05873  -0.04333 0.02112  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.45177 0.35989 0.34602 0.05815  -0.03688 0.02925  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.48669 0.39356 0.37566 0.04643  -0.02966 0.02399  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.46591 0.35936 0.33498 0.04465  -0.02252 0.03443  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.58465 0.48415 0.45449 0.03432  -0.01402 0.03191  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.32021 0.30286 0.28146 0.06380  -0.06849 0.01900  70  LEU A N   
440  C CA  . LEU A 63  ? 0.32226 0.32516 0.30929 0.05984  -0.07280 0.01519  70  LEU A CA  
441  C C   . LEU A 63  ? 0.31150 0.33596 0.30401 0.05350  -0.09104 0.01526  70  LEU A C   
442  O O   . LEU A 63  ? 0.31996 0.36506 0.33734 0.04914  -0.09683 0.01576  70  LEU A O   
443  C CB  . LEU A 63  ? 0.30160 0.31180 0.30971 0.07173  -0.06548 0.02389  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.34304 0.32532 0.34104 0.07625  -0.04883 0.02167  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.37049 0.35606 0.38336 0.09143  -0.04034 0.02988  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.33929 0.31326 0.33521 0.06331  -0.04391 0.00892  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.32554 0.34414 0.29327 0.05167  -0.10060 0.01512  71  ASP A N   
448  C CA  . ASP A 64  ? 0.37762 0.40995 0.34276 0.04278  -0.12051 0.01301  71  ASP A CA  
449  C C   . ASP A 64  ? 0.35154 0.37894 0.31804 0.02926  -0.12234 -0.00091 71  ASP A C   
450  O O   . ASP A 64  ? 0.38075 0.42047 0.35494 0.01892  -0.13871 -0.00251 71  ASP A O   
451  C CB  . ASP A 64  ? 0.39753 0.41689 0.32582 0.04394  -0.12877 0.01352  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.46474 0.49365 0.39282 0.05629  -0.13364 0.02997  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.46379 0.51245 0.42266 0.06440  -0.13270 0.04113  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.51844 0.53459 0.41430 0.05953  -0.13734 0.03276  71  ASP A OD2 
455  N N   . SER A 65  ? 0.30341 0.31275 0.26283 0.02857  -0.10677 -0.00977 72  SER A N   
456  C CA  . SER A 65  ? 0.31615 0.31819 0.27707 0.01898  -0.10530 -0.02152 72  SER A CA  
457  C C   . SER A 65  ? 0.35751 0.37430 0.35202 0.01628  -0.10112 -0.01956 72  SER A C   
458  O O   . SER A 65  ? 0.37900 0.38852 0.37629 0.00977  -0.09722 -0.02763 72  SER A O   
459  C CB  . SER A 65  ? 0.32732 0.30850 0.26842 0.02142  -0.09017 -0.02873 72  SER A CB  
460  O OG  . SER A 65  ? 0.31765 0.29791 0.26626 0.02814  -0.07668 -0.02228 72  SER A OG  
461  N N   . GLY A 66  ? 0.30039 0.33680 0.31874 0.02299  -0.10040 -0.00806 73  GLY A N   
462  C CA  . GLY A 66  ? 0.35088 0.40205 0.39886 0.02286  -0.09398 -0.00452 73  GLY A CA  
463  C C   . GLY A 66  ? 0.29428 0.34831 0.35235 0.03742  -0.08060 0.00457  73  GLY A C   
464  O O   . GLY A 66  ? 0.26025 0.29229 0.30162 0.04257  -0.06862 0.00112  73  GLY A O   
465  N N   . LYS A 67  ? 0.28452 0.36470 0.36943 0.04416  -0.08230 0.01693  74  LYS A N   
466  C CA  . LYS A 67  ? 0.28187 0.36096 0.37278 0.06169  -0.06818 0.02605  74  LYS A CA  
467  C C   . LYS A 67  ? 0.24352 0.31513 0.34071 0.06443  -0.05199 0.02274  74  LYS A C   
468  O O   . LYS A 67  ? 0.31957 0.37268 0.40604 0.07730  -0.03805 0.02435  74  LYS A O   
469  C CB  . LYS A 67  ? 0.28441 0.39775 0.40266 0.07193  -0.07467 0.04329  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.42637 0.54673 0.53557 0.07254  -0.09103 0.04938  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.50548 0.64041 0.62712 0.09378  -0.08728 0.06718  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.67217 0.80239 0.77368 0.09689  -0.10025 0.07244  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.71781 0.85972 0.81346 0.07772  -0.12302 0.06713  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.22348 0.30534 0.33404 0.05266  -0.05380 0.01835  75  GLU A N   
475  C CA  . GLU A 68  ? 0.23832 0.31662 0.35500 0.05602  -0.03901 0.01750  75  GLU A CA  
476  C C   . GLU A 68  ? 0.22149 0.26566 0.30999 0.05209  -0.03150 0.00455  75  GLU A C   
477  O O   . GLU A 68  ? 0.26114 0.29520 0.33752 0.04064  -0.03872 -0.00443 75  GLU A O   
478  C CB  . GLU A 68  ? 0.29626 0.39816 0.43792 0.04397  -0.04396 0.01979  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.34780 0.49063 0.52541 0.04648  -0.04976 0.03618  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.62417 0.78162 0.80621 0.03753  -0.07125 0.03890  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.66922 0.85770 0.87478 0.04495  -0.07677 0.05400  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.54737 0.68522 0.70794 0.02407  -0.08253 0.02657  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.22524 0.25179 0.30259 0.06197  -0.01716 0.00430  76  LEU A N   
484  C CA  . LEU A 69  ? 0.22136 0.21725 0.27297 0.05699  -0.01167 -0.00613 76  LEU A CA  
485  C C   . LEU A 69  ? 0.19783 0.19308 0.25178 0.05622  -0.00296 -0.00790 76  LEU A C   
486  O O   . LEU A 69  ? 0.23244 0.22333 0.28402 0.06877  0.00909  -0.00324 76  LEU A O   
487  C CB  . LEU A 69  ? 0.25212 0.21990 0.28062 0.06700  -0.00457 -0.00551 76  LEU A CB  
488  C CG  . LEU A 69  ? 0.28683 0.25262 0.31019 0.06954  -0.01145 -0.00142 76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.41770 0.34815 0.41470 0.07686  -0.00378 -0.00106 76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.28418 0.25414 0.30445 0.05509  -0.02222 -0.00741 76  LEU A CD2 
491  N N   . HIS A 70  ? 0.18422 0.18171 0.24002 0.04332  -0.00787 -0.01399 77  HIS A N   
492  C CA  . HIS A 70  ? 0.20703 0.20798 0.26747 0.04195  -0.00104 -0.01343 77  HIS A CA  
493  C C   . HIS A 70  ? 0.18273 0.17390 0.23392 0.02979  -0.00573 -0.02142 77  HIS A C   
494  O O   . HIS A 70  ? 0.17371 0.16093 0.22026 0.02279  -0.01389 -0.02651 77  HIS A O   
495  C CB  . HIS A 70  ? 0.19025 0.22243 0.28140 0.04165  -0.00200 -0.00376 77  HIS A CB  
496  C CG  . HIS A 70  ? 0.17496 0.22041 0.27993 0.02818  -0.01683 -0.00527 77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.27141 0.33954 0.39627 0.02677  -0.02631 0.00179  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.22599 0.26263 0.32500 0.01620  -0.02400 -0.01283 77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.23471 0.30291 0.36076 0.01301  -0.03948 -0.00315 77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.25575 0.30392 0.36611 0.00778  -0.03700 -0.01205 77  HIS A NE2 
501  N N   . ILE A 71  ? 0.20662 0.19535 0.25525 0.02913  0.00065  -0.02092 78  ILE A N   
502  C CA  . ILE A 71  ? 0.19572 0.17753 0.23730 0.02010  -0.00272 -0.02564 78  ILE A CA  
503  C C   . ILE A 71  ? 0.17270 0.16848 0.23055 0.01725  -0.00030 -0.01993 78  ILE A C   
504  O O   . ILE A 71  ? 0.19367 0.19552 0.25547 0.02386  0.00971  -0.01331 78  ILE A O   
505  C CB  . ILE A 71  ? 0.21596 0.17556 0.23113 0.02113  0.00168  -0.02975 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.23939 0.18244 0.23842 0.02131  -0.00093 -0.03397 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.21841 0.17625 0.22963 0.01284  -0.00295 -0.03189 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.27290 0.18940 0.24254 0.01988  0.00129  -0.03810 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.17638 0.17530 0.24218 0.00822  -0.00813 -0.02162 79  ASN A N   
510  C CA  . ASN A 72  ? 0.16557 0.17238 0.24472 0.00288  -0.00704 -0.01590 79  ASN A CA  
511  C C   . ASN A 72  ? 0.19716 0.19042 0.26346 -0.00044 -0.00782 -0.01870 79  ASN A C   
512  O O   . ASN A 72  ? 0.18284 0.16734 0.24014 -0.00191 -0.01377 -0.02489 79  ASN A O   
513  C CB  . ASN A 72  ? 0.15852 0.17580 0.25640 -0.00575 -0.01686 -0.01440 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.18016 0.21761 0.29584 -0.00340 -0.01815 -0.00823 79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.17643 0.22453 0.29769 0.00578  -0.00799 -0.00132 79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.21732 0.25964 0.34048 -0.01067 -0.03069 -0.01000 79  ASN A ND2 
517  N N   . LEU A 73  ? 0.17824 0.17192 0.24451 -0.00051 -0.00105 -0.01232 80  LEU A N   
518  C CA  . LEU A 73  ? 0.17473 0.15743 0.23021 -0.00279 -0.00208 -0.01204 80  LEU A CA  
519  C C   . LEU A 73  ? 0.17858 0.16355 0.24919 -0.00985 -0.00325 -0.00563 80  LEU A C   
520  O O   . LEU A 73  ? 0.18188 0.17788 0.26544 -0.01175 0.00318  0.00324  80  LEU A O   
521  C CB  . LEU A 73  ? 0.19873 0.17488 0.23506 0.00247  0.00608  -0.00922 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.20658 0.17406 0.22350 0.00793  0.00779  -0.01523 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.24639 0.20152 0.23779 0.01250  0.01545  -0.01315 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.23098 0.19275 0.24161 0.00414  -0.00259 -0.02250 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.19380 0.16754 0.26269 -0.01349 -0.01067 -0.00916 81  ILE A N   
526  C CA  . ILE A 74  ? 0.19730 0.16475 0.27659 -0.02190 -0.01393 -0.00493 81  ILE A CA  
527  C C   . ILE A 74  ? 0.23036 0.18105 0.29858 -0.02017 -0.01336 -0.00216 81  ILE A C   
528  O O   . ILE A 74  ? 0.22400 0.16210 0.28336 -0.01627 -0.01805 -0.00786 81  ILE A O   
529  C CB  . ILE A 74  ? 0.23377 0.19600 0.31756 -0.02755 -0.02396 -0.01208 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.22244 0.20290 0.31584 -0.02720 -0.02570 -0.01372 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.23272 0.18428 0.32477 -0.03964 -0.02891 -0.00772 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.25554 0.23074 0.34854 -0.03260 -0.03706 -0.02078 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.21182 0.16250 0.27995 -0.02130 -0.00669 0.00795  82  PRO A N   
534  C CA  . PRO A 75  ? 0.24277 0.17642 0.30086 -0.01937 -0.00671 0.01288  82  PRO A CA  
535  C C   . PRO A 75  ? 0.26953 0.18536 0.33458 -0.02853 -0.01072 0.01535  82  PRO A C   
536  O O   . PRO A 75  ? 0.28488 0.20634 0.36522 -0.03992 -0.01176 0.01871  82  PRO A O   
537  C CB  . PRO A 75  ? 0.25669 0.19677 0.30919 -0.01762 0.00270  0.02372  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.26479 0.22349 0.33209 -0.02169 0.00932  0.02717  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.24014 0.20681 0.31806 -0.02339 0.00243  0.01714  82  PRO A CD  
540  N N   . ASN A 76  ? 0.28010 0.17337 0.33340 -0.02353 -0.01351 0.01439  83  ASN A N   
541  C CA  . ASN A 76  ? 0.30397 0.16912 0.35580 -0.03120 -0.01711 0.01617  83  ASN A CA  
542  C C   . ASN A 76  ? 0.33494 0.18073 0.37403 -0.02272 -0.01348 0.02464  83  ASN A C   
543  O O   . ASN A 76  ? 0.35735 0.19470 0.38547 -0.00925 -0.01442 0.02106  83  ASN A O   
544  C CB  . ASN A 76  ? 0.35477 0.20269 0.39963 -0.03118 -0.02496 0.00309  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.46419 0.27671 0.50265 -0.04247 -0.03050 0.00293  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.43638 0.22310 0.46522 -0.04021 -0.02775 0.00965  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.53170 0.34068 0.57364 -0.05556 -0.03949 -0.00419 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.36281 0.20340 0.40470 -0.02993 -0.00877 0.03775  84  LYS A N   
549  C CA  . LYS A 77  ? 0.39697 0.21960 0.42570 -0.02132 -0.00520 0.04827  84  LYS A CA  
550  C C   . LYS A 77  ? 0.44531 0.22756 0.46249 -0.01860 -0.00884 0.04617  84  LYS A C   
551  O O   . LYS A 77  ? 0.46839 0.23624 0.47316 -0.00422 -0.00693 0.05173  84  LYS A O   
552  C CB  . LYS A 77  ? 0.40383 0.23088 0.43623 -0.02945 0.00238  0.06437  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.41818 0.27665 0.44988 -0.02477 0.00896  0.06807  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.41787 0.28082 0.45224 -0.03214 0.01927  0.08469  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.47815 0.36804 0.50713 -0.02645 0.02769  0.08643  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.66907 0.58212 0.71903 -0.03407 0.03189  0.08366  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.48595 0.24754 0.50474 -0.03155 -0.01450 0.03872  85  GLN A N   
558  C CA  . GLN A 78  ? 0.55934 0.27326 0.55949 -0.02855 -0.01759 0.03483  85  GLN A CA  
559  C C   . GLN A 78  ? 0.50619 0.21468 0.49298 -0.00757 -0.01736 0.02388  85  GLN A C   
560  O O   . GLN A 78  ? 0.56575 0.24388 0.53594 0.00752  -0.01417 0.02621  85  GLN A O   
561  C CB  . GLN A 78  ? 0.61168 0.30068 0.61195 -0.05050 -0.02618 0.02888  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.75158 0.43912 0.76623 -0.07300 -0.02631 0.04341  85  GLN A CG  
563  C CD  . GLN A 78  ? 0.86399 0.60325 0.90421 -0.07742 -0.01972 0.05398  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.83514 0.57979 0.88137 -0.08127 -0.01197 0.07033  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.76900 0.54368 0.82186 -0.07616 -0.02179 0.04518  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.45674 0.19508 0.45124 -0.00523 -0.01947 0.01358  86  ASP A N   
567  C CA  . ASP A 79  ? 0.46126 0.20250 0.44729 0.01369  -0.01773 0.00537  86  ASP A CA  
568  C C   . ASP A 79  ? 0.42434 0.20038 0.41927 0.02799  -0.01363 0.01340  86  ASP A C   
569  O O   . ASP A 79  ? 0.41145 0.19496 0.40392 0.04437  -0.01134 0.01098  86  ASP A O   
570  C CB  . ASP A 79  ? 0.50942 0.26375 0.49779 0.00773  -0.02252 -0.00857 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.64275 0.36326 0.61949 -0.00756 -0.03008 -0.01743 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.69181 0.37176 0.65484 -0.01190 -0.03110 -0.01470 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.63053 0.36358 0.61051 -0.01620 -0.03620 -0.02656 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.38063 0.17759 0.38455 0.02177  -0.01280 0.02364  87  ARG A N   
575  C CA  . ARG A 80  ? 0.33046 0.16039 0.33947 0.03030  -0.01230 0.03001  87  ARG A CA  
576  C C   . ARG A 80  ? 0.31575 0.17330 0.33185 0.03223  -0.01475 0.02024  87  ARG A C   
577  O O   . ARG A 80  ? 0.33502 0.20969 0.35350 0.04394  -0.01549 0.02252  87  ARG A O   
578  C CB  . ARG A 80  ? 0.36908 0.19311 0.37201 0.04728  -0.01075 0.04165  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.36687 0.21926 0.37137 0.04875  -0.01304 0.05231  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.51346 0.37555 0.51792 0.06661  -0.01502 0.06338  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.61295 0.44263 0.60947 0.07877  -0.01069 0.07197  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.67117 0.50130 0.66959 0.09922  -0.00938 0.07934  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.53816 0.40430 0.55003 0.10819  -0.01257 0.08038  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.70115 0.49498 0.68854 0.11124  -0.00425 0.08733  87  ARG A NH2 
585  N N   . THR A 81  ? 0.29635 0.16006 0.31760 0.02012  -0.01631 0.01112  88  THR A N   
586  C CA  . THR A 81  ? 0.27562 0.16173 0.30202 0.02051  -0.01829 0.00252  88  THR A CA  
587  C C   . THR A 81  ? 0.27347 0.17838 0.30568 0.00981  -0.01852 0.00163  88  THR A C   
588  O O   . THR A 81  ? 0.28000 0.18035 0.31593 0.00033  -0.01686 0.00428  88  THR A O   
589  C CB  . THR A 81  ? 0.27059 0.14325 0.29356 0.02055  -0.01961 -0.00893 88  THR A CB  
590  O OG1 . THR A 81  ? 0.32308 0.18070 0.34652 0.00669  -0.02250 -0.01230 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.34536 0.19617 0.35764 0.03522  -0.01659 -0.00916 88  THR A CG2 
592  N N   . LEU A 82  ? 0.22206 0.14753 0.25509 0.01171  -0.01993 -0.00103 89  LEU A N   
593  C CA  . LEU A 82  ? 0.22188 0.16023 0.25655 0.00477  -0.01920 -0.00442 89  LEU A CA  
594  C C   . LEU A 82  ? 0.23749 0.18292 0.27537 0.00511  -0.02165 -0.01350 89  LEU A C   
595  O O   . LEU A 82  ? 0.23383 0.18663 0.27085 0.01045  -0.02358 -0.01440 89  LEU A O   
596  C CB  . LEU A 82  ? 0.24345 0.19188 0.26874 0.00554  -0.01926 0.00021  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.21935 0.17450 0.24003 0.00143  -0.01695 -0.00417 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.24722 0.20057 0.27365 -0.00214 -0.00982 -0.00135 89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.25168 0.20867 0.25465 0.00171  -0.01889 -0.00175 89  LEU A CD2 
600  N N   . THR A 83  ? 0.20766 0.15319 0.25067 -0.00056 -0.02164 -0.01831 90  THR A N   
601  C CA  . THR A 83  ? 0.22054 0.17045 0.26439 -0.00013 -0.02414 -0.02596 90  THR A CA  
602  C C   . THR A 83  ? 0.21034 0.17193 0.25528 -0.00258 -0.02274 -0.02697 90  THR A C   
603  O O   . THR A 83  ? 0.22070 0.18558 0.27031 -0.00565 -0.01962 -0.02360 90  THR A O   
604  C CB  . THR A 83  ? 0.23306 0.17120 0.27870 -0.00415 -0.02756 -0.03053 90  THR A CB  
605  O OG1 . THR A 83  ? 0.24662 0.16547 0.28500 -0.00019 -0.02786 -0.03083 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.25277 0.19499 0.29550 -0.00299 -0.03033 -0.03761 90  THR A CG2 
607  N N   . ILE A 84  ? 0.20715 0.17427 0.24766 -0.00050 -0.02390 -0.03030 91  ILE A N   
608  C CA  . ILE A 84  ? 0.20471 0.17600 0.24201 -0.00156 -0.02250 -0.03198 91  ILE A CA  
609  C C   . ILE A 84  ? 0.24093 0.21390 0.28115 -0.00118 -0.02488 -0.03646 91  ILE A C   
610  O O   . ILE A 84  ? 0.22247 0.19593 0.25971 0.00054  -0.02652 -0.03866 91  ILE A O   
611  C CB  . ILE A 84  ? 0.23498 0.20645 0.26125 -0.00227 -0.02341 -0.03145 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.28006 0.24871 0.29847 -0.00282 -0.02290 -0.02681 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.23138 0.19840 0.24942 -0.00272 -0.02147 -0.03412 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.35217 0.32543 0.37437 -0.00136 -0.02669 -0.02241 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.19311 0.16926 0.23957 -0.00210 -0.02476 -0.03623 92  VAL A N   
616  C CA  . VAL A 85  ? 0.19450 0.17276 0.24255 -0.00201 -0.02890 -0.03925 92  VAL A CA  
617  C C   . VAL A 85  ? 0.21465 0.19625 0.26032 0.00133  -0.02622 -0.03794 92  VAL A C   
618  O O   . VAL A 85  ? 0.22500 0.20948 0.27385 0.00372  -0.02123 -0.03409 92  VAL A O   
619  C CB  . VAL A 85  ? 0.22415 0.20537 0.28298 -0.00681 -0.03387 -0.03811 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.27951 0.26168 0.33543 -0.00736 -0.04090 -0.04143 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.26337 0.23374 0.32137 -0.01068 -0.03577 -0.03891 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.21632 0.19573 0.25484 0.00286  -0.02817 -0.04026 93  ASP A N   
623  C CA  . ASP A 86  ? 0.21061 0.18910 0.24553 0.00683  -0.02609 -0.03826 93  ASP A CA  
624  C C   . ASP A 86  ? 0.22373 0.20521 0.25770 0.00799  -0.03140 -0.03873 93  ASP A C   
625  O O   . ASP A 86  ? 0.21918 0.19916 0.24870 0.00591  -0.03521 -0.04214 93  ASP A O   
626  C CB  . ASP A 86  ? 0.21721 0.18400 0.23814 0.00647  -0.02245 -0.03878 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.26288 0.22896 0.27860 0.00269  -0.02482 -0.03992 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.24406 0.21074 0.25721 0.00439  -0.02608 -0.03942 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.26724 0.23449 0.28221 -0.00142 -0.02514 -0.03976 93  ASP A OD2 
630  N N   . THR A 87  ? 0.19661 0.18094 0.23231 0.01304  -0.03103 -0.03470 94  THR A N   
631  C CA  . THR A 87  ? 0.18354 0.17041 0.21550 0.01515  -0.03672 -0.03338 94  THR A CA  
632  C C   . THR A 87  ? 0.24269 0.21740 0.26000 0.01854  -0.03274 -0.03189 94  THR A C   
633  O O   . THR A 87  ? 0.23229 0.20677 0.24644 0.02408  -0.03417 -0.02728 94  THR A O   
634  C CB  . THR A 87  ? 0.19433 0.19680 0.24147 0.01850  -0.04118 -0.02711 94  THR A CB  
635  O OG1 . THR A 87  ? 0.20779 0.21180 0.26123 0.02636  -0.03236 -0.02157 94  THR A OG1 
636  C CG2 . THR A 87  ? 0.20869 0.22221 0.26969 0.01044  -0.04816 -0.02799 94  THR A CG2 
637  N N   . GLY A 88  ? 0.22541 0.19030 0.23431 0.01439  -0.02847 -0.03426 95  GLY A N   
638  C CA  . GLY A 88  ? 0.24786 0.20021 0.24380 0.01360  -0.02556 -0.03178 95  GLY A CA  
639  C C   . GLY A 88  ? 0.23737 0.19253 0.22663 0.01313  -0.02738 -0.03030 95  GLY A C   
640  O O   . GLY A 88  ? 0.23219 0.19527 0.22203 0.01552  -0.03196 -0.03185 95  GLY A O   
641  N N   . ILE A 89  ? 0.24050 0.18738 0.22104 0.00901  -0.02382 -0.02680 96  ILE A N   
642  C CA  . ILE A 89  ? 0.25490 0.20349 0.22675 0.00964  -0.02261 -0.02280 96  ILE A CA  
643  C C   . ILE A 89  ? 0.24188 0.20277 0.21548 0.00983  -0.02149 -0.02570 96  ILE A C   
644  O O   . ILE A 89  ? 0.26210 0.22413 0.22461 0.01390  -0.02038 -0.02423 96  ILE A O   
645  C CB  . ILE A 89  ? 0.25016 0.18694 0.21452 0.00314  -0.01841 -0.01603 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.28913 0.22556 0.24237 0.00546  -0.01568 -0.00912 96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.25121 0.19440 0.22389 -0.00734 -0.01681 -0.01560 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.35207 0.27095 0.29598 -0.00054 -0.01255 -0.00067 96  ILE A CD1 
649  N N   . GLY A 90  ? 0.23609 0.20377 0.22016 0.00722  -0.02101 -0.02941 97  GLY A N   
650  C CA  . GLY A 90  ? 0.22682 0.20262 0.21110 0.01039  -0.01808 -0.03144 97  GLY A CA  
651  C C   . GLY A 90  ? 0.21894 0.20410 0.20457 0.00877  -0.01038 -0.02387 97  GLY A C   
652  O O   . GLY A 90  ? 0.26328 0.24821 0.25070 0.00172  -0.00895 -0.01697 97  GLY A O   
653  N N   . MET A 91  ? 0.22113 0.21394 0.20580 0.01555  -0.00477 -0.02426 98  MET A N   
654  C CA  . MET A 91  ? 0.22030 0.22923 0.21126 0.01644  0.00486  -0.01465 98  MET A CA  
655  C C   . MET A 91  ? 0.23905 0.24569 0.21230 0.02904  0.01342  -0.01535 98  MET A C   
656  O O   . MET A 91  ? 0.26966 0.26346 0.22944 0.03720  0.01169  -0.02482 98  MET A O   
657  C CB  . MET A 91  ? 0.23796 0.26358 0.24903 0.01538  0.00629  -0.01131 98  MET A CB  
658  C CG  . MET A 91  ? 0.23247 0.26220 0.25757 0.00125  -0.00125 -0.00790 98  MET A CG  
659  S SD  . MET A 91  ? 0.23066 0.27916 0.27623 0.00049  -0.00346 -0.00433 98  MET A SD  
660  C CE  . MET A 91  ? 0.27081 0.30050 0.30636 0.01013  -0.00642 -0.01722 98  MET A CE  
661  N N   . THR A 92  ? 0.23701 0.25368 0.20776 0.03004  0.02292  -0.00496 99  THR A N   
662  C CA  . THR A 92  ? 0.26041 0.27658 0.21237 0.04415  0.03490  -0.00369 99  THR A CA  
663  C C   . THR A 92  ? 0.25971 0.29282 0.22543 0.05394  0.04538  0.00014  99  THR A C   
664  O O   . THR A 92  ? 0.24422 0.29456 0.23703 0.04762  0.04251  0.00472  99  THR A O   
665  C CB  . THR A 92  ? 0.30157 0.32609 0.24837 0.04237  0.04404  0.00920  99  THR A CB  
666  O OG1 . THR A 92  ? 0.28758 0.33915 0.26439 0.03300  0.04937  0.02361  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.32419 0.33147 0.25856 0.03404  0.03402  0.00785  99  THR A CG2 
668  N N   . LYS A 93  ? 0.25914 0.25899 0.23184 0.04891  -0.02603 0.00698  100 LYS A N   
669  C CA  . LYS A 93  ? 0.24809 0.23471 0.21651 0.04340  -0.01207 -0.00262 100 LYS A CA  
670  C C   . LYS A 93  ? 0.27225 0.24626 0.24428 0.04644  -0.00245 0.00873  100 LYS A C   
671  O O   . LYS A 93  ? 0.25867 0.22582 0.24372 0.04626  0.00623  0.00429  100 LYS A O   
672  C CB  . LYS A 93  ? 0.29839 0.29106 0.23979 0.03742  -0.00913 -0.01224 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.33364 0.31159 0.27257 0.03508  0.00717  -0.02397 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.35635 0.33727 0.26582 0.02952  0.01322  -0.03472 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.39096 0.35415 0.30031 0.03073  0.03144  -0.04754 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.42950 0.39383 0.31058 0.02803  0.04207  -0.05560 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.28906 0.26113 0.24924 0.04875  -0.00356 0.02390  101 ALA A N   
678  C CA  . ALA A 94  ? 0.29782 0.25904 0.26196 0.04684  0.00698  0.03293  101 ALA A CA  
679  C C   . ALA A 94  ? 0.30507 0.25853 0.29474 0.04737  0.00729  0.03265  101 ALA A C   
680  O O   . ALA A 94  ? 0.30987 0.26369 0.31032 0.04317  0.01578  0.02992  101 ALA A O   
681  C CB  . ALA A 94  ? 0.33251 0.28597 0.27622 0.04755  0.00783  0.05029  101 ALA A CB  
682  N N   . ASP A 95  ? 0.27931 0.23008 0.27908 0.05268  -0.00183 0.03457  102 ASP A N   
683  C CA  . ASP A 95  ? 0.28039 0.22416 0.30192 0.05267  -0.00053 0.03147  102 ASP A CA  
684  C C   . ASP A 95  ? 0.25461 0.20524 0.28735 0.04973  0.00289  0.01899  102 ASP A C   
685  O O   . ASP A 95  ? 0.27496 0.22416 0.31813 0.04674  0.00818  0.01727  102 ASP A O   
686  C CB  . ASP A 95  ? 0.29554 0.23945 0.32764 0.06063  -0.00936 0.03343  102 ASP A CB  
687  C CG  . ASP A 95  ? 0.37493 0.30807 0.39744 0.06902  -0.01206 0.04935  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.39941 0.31220 0.41369 0.06568  -0.00312 0.05834  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.39366 0.33884 0.41823 0.07932  -0.02240 0.05327  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.23922 0.19671 0.26864 0.05026  0.00028  0.01015  103 LEU A N   
691  C CA  . LEU A 96  ? 0.26611 0.22227 0.30271 0.04960  0.00575  0.00089  103 LEU A CA  
692  C C   . LEU A 96  ? 0.25972 0.21800 0.29496 0.05060  0.01478  0.00248  103 LEU A C   
693  O O   . LEU A 96  ? 0.25324 0.21360 0.29924 0.05245  0.01794  0.00217  103 LEU A O   
694  C CB  . LEU A 96  ? 0.28616 0.24235 0.31456 0.04726  0.00565  -0.00988 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.25524 0.21719 0.29182 0.04382  -0.00180 -0.01613 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.26305 0.22487 0.28815 0.03641  0.00040  -0.02977 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.25682 0.21312 0.31054 0.04422  0.00102  -0.01726 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.25119 0.21351 0.27314 0.04984  0.01895  0.00440  104 ILE A N   
699  C CA  . ILE A 97  ? 0.25737 0.22904 0.28129 0.05170  0.02873  0.00501  104 ILE A CA  
700  C C   . ILE A 97  ? 0.24810 0.22875 0.28514 0.04709  0.02955  0.01120  104 ILE A C   
701  O O   . ILE A 97  ? 0.25560 0.25152 0.30459 0.04932  0.03377  0.01007  104 ILE A O   
702  C CB  . ILE A 97  ? 0.27855 0.25380 0.28429 0.05052  0.03497  0.00457  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.29639 0.26288 0.28838 0.05278  0.03631  -0.00653 104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.27393 0.26569 0.28620 0.05221  0.04634  0.00592  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.32880 0.29811 0.29650 0.04922  0.03991  -0.00885 104 ILE A CD1 
706  N N   . ASN A 98  ? 0.25634 0.22804 0.29107 0.04081  0.02587  0.01739  105 ASN A N   
707  C CA  . ASN A 98  ? 0.28502 0.25821 0.32931 0.03216  0.02882  0.02055  105 ASN A CA  
708  C C   . ASN A 98  ? 0.22892 0.19901 0.28649 0.03242  0.02396  0.01602  105 ASN A C   
709  O O   . ASN A 98  ? 0.26583 0.22110 0.32531 0.02822  0.02279  0.01753  105 ASN A O   
710  C CB  . ASN A 98  ? 0.29314 0.24868 0.32509 0.02634  0.03081  0.03004  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.48953 0.44460 0.52669 0.01234  0.03993  0.03173  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.45987 0.43787 0.51105 0.00602  0.04353  0.02481  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.55424 0.48376 0.57973 0.00719  0.04424  0.04113  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.24088 0.22280 0.30542 0.03868  0.02284  0.01087  106 ASN A N   
715  C CA  . ASN A 99  ? 0.22297 0.20669 0.29673 0.03888  0.01973  0.00692  106 ASN A CA  
716  C C   . ASN A 99  ? 0.24479 0.20949 0.31854 0.03965  0.01537  0.00560  106 ASN A C   
717  O O   . ASN A 99  ? 0.23563 0.19564 0.31483 0.03508  0.01521  0.00282  106 ASN A O   
718  C CB  . ASN A 99  ? 0.21240 0.21191 0.29444 0.02853  0.02177  0.00464  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.20572 0.23552 0.29364 0.02904  0.02535  0.00525  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.22846 0.27109 0.31811 0.04175  0.02511  0.00647  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.25584 0.29659 0.34740 0.01576  0.03041  0.00473  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.22596 0.18293 0.29424 0.04498  0.01245  0.00599  107 LEU A N   
723  C CA  . LEU A 100 ? 0.24377 0.19241 0.31644 0.04713  0.00785  0.00404  107 LEU A CA  
724  C C   . LEU A 100 ? 0.23818 0.17645 0.31439 0.04600  0.00731  0.00795  107 LEU A C   
725  O O   . LEU A 100 ? 0.25183 0.18609 0.33502 0.04650  0.00717  0.00444  107 LEU A O   
726  C CB  . LEU A 100 ? 0.25395 0.20398 0.33190 0.04764  0.00893  -0.00196 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.26482 0.21579 0.33603 0.05060  0.01248  -0.00378 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.26019 0.21893 0.33181 0.05376  0.01634  -0.00125 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.36069 0.30588 0.42946 0.04850  0.01313  -0.00918 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.23871 0.17055 0.30633 0.04408  0.00912  0.01543  108 GLY A N   
731  C CA  . GLY A 101 ? 0.26492 0.17787 0.33164 0.04502  0.01118  0.02185  108 GLY A CA  
732  C C   . GLY A 101 ? 0.27674 0.17802 0.34885 0.03580  0.01896  0.01684  108 GLY A C   
733  O O   . GLY A 101 ? 0.34374 0.22235 0.41631 0.03772  0.02317  0.01945  108 GLY A O   
734  N N   . THR A 102 ? 0.27396 0.19082 0.34945 0.02635  0.02139  0.00930  109 THR A N   
735  C CA  . THR A 102 ? 0.28745 0.20143 0.36697 0.01404  0.02742  0.00091  109 THR A CA  
736  C C   . THR A 102 ? 0.26919 0.19023 0.34570 -0.00048 0.03376  0.00118  109 THR A C   
737  O O   . THR A 102 ? 0.28409 0.21894 0.35735 0.00076  0.03338  0.00706  109 THR A O   
738  C CB  . THR A 102 ? 0.27130 0.20666 0.35682 0.01366  0.02396  -0.00812 109 THR A CB  
739  O OG1 . THR A 102 ? 0.28264 0.24520 0.36858 0.01367  0.02149  -0.00672 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.35225 0.28455 0.44095 0.02581  0.01958  -0.00822 109 THR A CG2 
741  N N   . ILE A 103 ? 0.24796 0.16031 0.32574 -0.01611 0.04121  -0.00718 110 ILE A N   
742  C CA  . ILE A 103 ? 0.26059 0.18923 0.33998 -0.03532 0.04776  -0.01155 110 ILE A CA  
743  C C   . ILE A 103 ? 0.23195 0.20381 0.32135 -0.04056 0.04171  -0.02224 110 ILE A C   
744  O O   . ILE A 103 ? 0.24709 0.22957 0.33952 -0.05857 0.04503  -0.03498 110 ILE A O   
745  C CB  . ILE A 103 ? 0.43244 0.32604 0.50563 -0.05342 0.06147  -0.01538 110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.39497 0.26645 0.46811 -0.05643 0.06457  -0.02743 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.35241 0.20769 0.41260 -0.04499 0.06753  0.00115  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.46902 0.30776 0.53600 -0.07965 0.08084  -0.03709 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.22811 0.22513 0.32094 -0.02463 0.03326  -0.01689 111 ALA A N   
750  C CA  . ALA A 104 ? 0.22402 0.25624 0.32270 -0.02139 0.02625  -0.02225 111 ALA A CA  
751  C C   . ALA A 104 ? 0.21745 0.29335 0.32605 -0.03571 0.02668  -0.02867 111 ALA A C   
752  O O   . ALA A 104 ? 0.22549 0.33071 0.33695 -0.04006 0.02124  -0.03634 111 ALA A O   
753  C CB  . ALA A 104 ? 0.24103 0.28023 0.33869 0.00030  0.02048  -0.01336 111 ALA A CB  
754  N N   . LYS A 105 ? 0.20822 0.29394 0.32208 -0.04386 0.03304  -0.02600 112 LYS A N   
755  C CA  . LYS A 105 ? 0.24032 0.37671 0.36855 -0.05896 0.03386  -0.03348 112 LYS A CA  
756  C C   . LYS A 105 ? 0.25325 0.39118 0.38167 -0.08624 0.03703  -0.04973 112 LYS A C   
757  O O   . LYS A 105 ? 0.25808 0.44054 0.39378 -0.09319 0.02974  -0.05949 112 LYS A O   
758  C CB  . LYS A 105 ? 0.21866 0.36339 0.35243 -0.06490 0.04338  -0.02831 112 LYS A CB  
759  C CG  . LYS A 105 ? 0.44403 0.63222 0.59363 -0.09108 0.04952  -0.03912 112 LYS A CG  
760  C CD  . LYS A 105 ? 0.31192 0.53790 0.47479 -0.08563 0.05488  -0.03293 112 LYS A CD  
761  C CE  . LYS A 105 ? 0.34998 0.64288 0.53714 -0.10691 0.05692  -0.04480 112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.46295 0.79493 0.66572 -0.10177 0.06502  -0.03959 112 LYS A NZ  
763  N N   . SER A 106 ? 0.27843 0.36656 0.39674 -0.10141 0.04840  -0.05298 113 SER A N   
764  C CA  . SER A 106 ? 0.28601 0.36614 0.40188 -0.12942 0.05521  -0.07113 113 SER A CA  
765  C C   . SER A 106 ? 0.27515 0.34737 0.38290 -0.12353 0.04827  -0.07962 113 SER A C   
766  O O   . SER A 106 ? 0.30295 0.39723 0.41054 -0.14402 0.04785  -0.09761 113 SER A O   
767  C CB  . SER A 106 ? 0.34938 0.36933 0.45417 -0.14474 0.07267  -0.07052 113 SER A CB  
768  O OG  . SER A 106 ? 0.39592 0.36297 0.48803 -0.12225 0.07319  -0.05756 113 SER A OG  
769  N N   . GLY A 107 ? 0.28080 0.32512 0.38130 -0.09785 0.04348  -0.06840 114 GLY A N   
770  C CA  . GLY A 107 ? 0.24732 0.28700 0.34018 -0.09177 0.03861  -0.07561 114 GLY A CA  
771  C C   . GLY A 107 ? 0.28732 0.38458 0.38305 -0.08905 0.02608  -0.07890 114 GLY A C   
772  O O   . GLY A 107 ? 0.27837 0.38856 0.36649 -0.10012 0.02412  -0.09283 114 GLY A O   
773  N N   . THR A 108 ? 0.22992 0.36229 0.33477 -0.07294 0.01812  -0.06574 115 THR A N   
774  C CA  . THR A 108 ? 0.27353 0.46245 0.38123 -0.06541 0.00619  -0.06468 115 THR A CA  
775  C C   . THR A 108 ? 0.26437 0.50284 0.37924 -0.09202 0.00392  -0.08154 115 THR A C   
776  O O   . THR A 108 ? 0.25072 0.52467 0.35895 -0.09560 -0.00486 -0.08911 115 THR A O   
777  C CB  . THR A 108 ? 0.22251 0.43411 0.34005 -0.04133 0.00165  -0.04731 115 THR A CB  
778  O OG1 . THR A 108 ? 0.20231 0.37059 0.31090 -0.01998 0.00337  -0.03511 115 THR A OG1 
779  C CG2 . THR A 108 ? 0.22738 0.49899 0.34886 -0.02950 -0.01004 -0.04310 115 THR A CG2 
780  N N   . LYS A 109 ? 0.23686 0.48091 0.36405 -0.11257 0.01212  -0.08800 116 LYS A N   
781  C CA  . LYS A 109 ? 0.26266 0.55463 0.39888 -0.14414 0.01204  -0.10752 116 LYS A CA  
782  C C   . LYS A 109 ? 0.30045 0.57019 0.41767 -0.16433 0.01502  -0.12717 116 LYS A C   
783  O O   . LYS A 109 ? 0.32756 0.63876 0.43712 -0.17106 0.00704  -0.13664 116 LYS A O   
784  C CB  . LYS A 109 ? 0.26419 0.54034 0.40827 -0.16274 0.02592  -0.10945 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.42052 0.71575 0.55982 -0.18925 0.03001  -0.12595 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.38341 0.66332 0.52914 -0.20386 0.04405  -0.12432 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.52637 0.84897 0.67550 -0.22668 0.04541  -0.13909 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.63006 1.02734 0.78714 -0.21631 0.02761  -0.14106 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.29866 0.49796 0.40400 -0.16918 0.02783  -0.13118 117 ALA A N   
790  C CA  . ALA A 110 ? 0.38724 0.55676 0.47203 -0.18323 0.03441  -0.14878 117 ALA A CA  
791  C C   . ALA A 110 ? 0.34608 0.54274 0.42114 -0.17253 0.02173  -0.15190 117 ALA A C   
792  O O   . ALA A 110 ? 0.36443 0.57800 0.42397 -0.18454 0.02079  -0.16613 117 ALA A O   
793  C CB  . ALA A 110 ? 0.38794 0.47528 0.46325 -0.18159 0.05141  -0.14761 117 ALA A CB  
794  N N   . PHE A 111 ? 0.30589 0.49445 0.38016 -0.13869 0.01465  -0.12954 118 PHE A N   
795  C CA  . PHE A 111 ? 0.26373 0.46626 0.32261 -0.12232 0.00569  -0.12549 118 PHE A CA  
796  C C   . PHE A 111 ? 0.31254 0.59200 0.37035 -0.12532 -0.01001 -0.12770 118 PHE A C   
797  O O   . PHE A 111 ? 0.32018 0.62045 0.35974 -0.13458 -0.01440 -0.14007 118 PHE A O   
798  C CB  . PHE A 111 ? 0.24883 0.42595 0.30918 -0.08874 0.00367  -0.10097 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.26322 0.44465 0.30655 -0.07171 -0.00168 -0.09389 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.25857 0.42989 0.28325 -0.08355 0.00273  -0.10955 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.26258 0.45201 0.30643 -0.04419 -0.00818 -0.07166 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.27620 0.45024 0.28281 -0.06883 -0.00001 -0.10176 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.28281 0.46981 0.30849 -0.02980 -0.01012 -0.06337 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.25670 0.43744 0.26355 -0.04235 -0.00622 -0.07773 118 PHE A CZ  
805  N N   . MET A 112 ? 0.30634 0.63240 0.38318 -0.11656 -0.01853 -0.11577 119 MET A N   
806  C CA  . MET A 112 ? 0.37855 0.78468 0.45732 -0.11272 -0.03517 -0.11386 119 MET A CA  
807  C C   . MET A 112 ? 0.46341 0.89194 0.53370 -0.14156 -0.03216 -0.13471 119 MET A C   
808  O O   . MET A 112 ? 0.38741 0.86005 0.44476 -0.13893 -0.04172 -0.13534 119 MET A O   
809  C CB  . MET A 112 ? 0.42291 0.86533 0.52412 -0.09033 -0.04094 -0.09388 119 MET A CB  
810  C CG  . MET A 112 ? 0.23116 0.65893 0.32674 -0.05022 -0.04525 -0.06702 119 MET A CG  
811  S SD  . MET A 112 ? 0.66538 1.13010 0.78716 -0.02422 -0.04798 -0.04722 119 MET A SD  
812  C CE  . MET A 112 ? 0.28612 0.68845 0.39571 0.01236  -0.04216 -0.02316 119 MET A CE  
813  N N   . GLU A 113 ? 0.35691 0.75306 0.43240 -0.16769 -0.01746 -0.15016 120 GLU A N   
814  C CA  . GLU A 113 ? 0.48593 0.89399 0.55083 -0.19606 -0.01113 -0.17160 120 GLU A CA  
815  C C   . GLU A 113 ? 0.46160 0.84679 0.50106 -0.20372 -0.00782 -0.18503 120 GLU A C   
816  O O   . GLU A 113 ? 0.44049 0.86273 0.46793 -0.21651 -0.01106 -0.19699 120 GLU A O   
817  C CB  . GLU A 113 ? 0.49154 0.85816 0.56321 -0.21985 0.00683  -0.18292 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.61408 1.02241 0.70587 -0.22468 0.00530  -0.17893 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.79455 1.15128 0.89165 -0.24179 0.02360  -0.18303 120 GLU A CD  
820  O OE1 . GLU A 113 ? 0.72279 1.01007 0.80747 -0.24741 0.03733  -0.18745 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.81981 1.20473 0.93239 -0.24809 0.02512  -0.18071 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.40303 0.72880 0.43431 -0.19577 -0.00054 -0.18360 121 ALA A N   
823  C CA  . ALA A 114 ? 0.38904 0.68943 0.39593 -0.20057 0.00504  -0.19600 121 ALA A CA  
824  C C   . ALA A 114 ? 0.38882 0.74023 0.38055 -0.18484 -0.01194 -0.18736 121 ALA A C   
825  O O   . ALA A 114 ? 0.47493 0.83626 0.44593 -0.19486 -0.01057 -0.19934 121 ALA A O   
826  C CB  . ALA A 114 ? 0.45303 0.67853 0.45696 -0.19186 0.01811  -0.19490 121 ALA A CB  
827  N N   . LEU A 115 ? 0.39652 0.77902 0.39684 -0.15842 -0.02692 -0.16462 122 LEU A N   
828  C CA  . LEU A 115 ? 0.34823 0.77151 0.33020 -0.13727 -0.04153 -0.14984 122 LEU A CA  
829  C C   . LEU A 115 ? 0.50842 0.99506 0.48666 -0.14534 -0.05003 -0.15322 122 LEU A C   
830  O O   . LEU A 115 ? 0.51263 1.01799 0.46696 -0.14464 -0.05445 -0.15471 122 LEU A O   
831  C CB  . LEU A 115 ? 0.38996 0.82744 0.38290 -0.10347 -0.05281 -0.12129 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.34494 0.70593 0.33702 -0.08458 -0.03951 -0.10778 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.40120 0.76253 0.40775 -0.05146 -0.04392 -0.07824 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.35754 0.69187 0.31881 -0.07989 -0.03444 -0.10853 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.48724 1.00906 0.48827 -0.15309 -0.05188 -0.15458 123 GLN A N   
836  C CA  . GLN A 116 ? 0.56581 1.15096 0.56529 -0.16408 -0.05889 -0.16160 123 GLN A CA  
837  C C   . GLN A 116 ? 0.60091 1.17312 0.58776 -0.20075 -0.04689 -0.19184 123 GLN A C   
838  O O   . GLN A 116 ? 0.62507 1.25072 0.60813 -0.21436 -0.05205 -0.20176 123 GLN A O   
839  C CB  . GLN A 116 ? 0.57535 1.20462 0.60245 -0.16023 -0.06336 -0.15439 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.61147 1.27084 0.64841 -0.12032 -0.07614 -0.12345 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.87318 1.60460 0.92580 -0.11509 -0.08475 -0.11854 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.89758 1.66052 0.95580 -0.14366 -0.08196 -0.13922 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.82319 1.57898 0.88246 -0.07822 -0.09372 -0.09150 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.61916 1.12127 0.59923 -0.21539 -0.03011 -0.20620 124 ALA A N   
845  C CA  . ALA A 117 ? 0.56110 1.03767 0.52827 -0.24696 -0.01453 -0.23369 124 ALA A CA  
846  C C   . ALA A 117 ? 0.76602 1.20190 0.70730 -0.24518 -0.00778 -0.24024 124 ALA A C   
847  O O   . ALA A 117 ? 0.72434 1.11018 0.65732 -0.26433 0.01075  -0.25976 124 ALA A O   
848  C CB  . ALA A 117 ? 0.54679 0.97090 0.52776 -0.26531 0.00406  -0.24503 124 ALA A CB  
849  N N   . GLY A 118 ? 0.65374 1.10745 0.58112 -0.22071 -0.02078 -0.22297 125 GLY A N   
850  C CA  . GLY A 118 ? 0.62401 1.04815 0.52381 -0.21801 -0.01508 -0.22791 125 GLY A CA  
851  C C   . GLY A 118 ? 0.58806 0.96393 0.48288 -0.19413 -0.01194 -0.21318 125 GLY A C   
852  O O   . GLY A 118 ? 0.56551 0.93871 0.43557 -0.18154 -0.01381 -0.20644 125 GLY A O   
853  N N   . ALA A 119 ? 0.45448 0.79302 0.37057 -0.18794 -0.00638 -0.20790 126 ALA A N   
854  C CA  . ALA A 119 ? 0.42937 0.71590 0.34202 -0.16977 0.00062  -0.19959 126 ALA A CA  
855  C C   . ALA A 119 ? 0.49062 0.80670 0.39020 -0.14145 -0.01455 -0.17487 126 ALA A C   
856  O O   . ALA A 119 ? 0.44475 0.81858 0.34453 -0.13085 -0.03149 -0.15913 126 ALA A O   
857  C CB  . ALA A 119 ? 0.45172 0.69686 0.39141 -0.16945 0.00850  -0.19825 126 ALA A CB  
858  N N   . ASP A 120 ? 0.44866 0.71583 0.34263 -0.12331 -0.00420 -0.16427 127 ASP A N   
859  C CA  . ASP A 120 ? 0.44114 0.71148 0.32791 -0.09187 -0.01008 -0.13265 127 ASP A CA  
860  C C   . ASP A 120 ? 0.36291 0.58414 0.27648 -0.07270 -0.00230 -0.11531 127 ASP A C   
861  O O   . ASP A 120 ? 0.34867 0.53253 0.28244 -0.08159 0.00775  -0.12659 127 ASP A O   
862  C CB  . ASP A 120 ? 0.44545 0.70615 0.29726 -0.08884 -0.00260 -0.13318 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.62053 0.81709 0.47811 -0.08628 0.01846  -0.13855 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.72088 0.88422 0.59766 -0.09914 0.02920  -0.15714 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.63483 0.81512 0.47837 -0.07075 0.02503  -0.12319 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.33893 0.55953 0.25002 -0.04612 -0.00646 -0.08735 128 ILE A N   
867  C CA  . ILE A 121 ? 0.30330 0.48512 0.23775 -0.02892 -0.00107 -0.07133 128 ILE A CA  
868  C C   . ILE A 121 ? 0.36590 0.49424 0.30789 -0.03318 0.01554  -0.08141 128 ILE A C   
869  O O   . ILE A 121 ? 0.35171 0.45118 0.31735 -0.02793 0.01955  -0.07783 128 ILE A O   
870  C CB  . ILE A 121 ? 0.33356 0.52121 0.25926 -0.00186 -0.00597 -0.04191 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.42459 0.66202 0.35828 0.00812  -0.02182 -0.03019 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.36578 0.50491 0.30641 0.01182  0.00421  -0.02982 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.44159 0.69037 0.35979 0.03667  -0.02672 -0.00120 128 ILE A CD1 
874  N N   . SER A 122 ? 0.39218 0.51033 0.31467 -0.04224 0.02547  -0.09472 129 SER A N   
875  C CA  . SER A 122 ? 0.36258 0.43630 0.29530 -0.04268 0.04199  -0.10350 129 SER A CA  
876  C C   . SER A 122 ? 0.39309 0.44235 0.34807 -0.05342 0.04772  -0.11999 129 SER A C   
877  O O   . SER A 122 ? 0.41634 0.43076 0.38704 -0.04753 0.05896  -0.12215 129 SER A O   
878  C CB  . SER A 122 ? 0.36997 0.44108 0.27690 -0.05043 0.05372  -0.11637 129 SER A CB  
879  O OG  . SER A 122 ? 0.43322 0.51281 0.32867 -0.07189 0.05658  -0.14285 129 SER A OG  
880  N N   . MET A 123 ? 0.34017 0.40760 0.29682 -0.06892 0.04115  -0.13107 130 MET A N   
881  C CA  . MET A 123 ? 0.34269 0.38087 0.31600 -0.08081 0.04921  -0.14540 130 MET A CA  
882  C C   . MET A 123 ? 0.30835 0.33844 0.30592 -0.07086 0.04334  -0.12912 130 MET A C   
883  O O   . MET A 123 ? 0.33526 0.34187 0.34440 -0.08024 0.04942  -0.13685 130 MET A O   
884  C CB  . MET A 123 ? 0.41164 0.46860 0.37217 -0.10869 0.04950  -0.16993 130 MET A CB  
885  C CG  . MET A 123 ? 0.40422 0.47235 0.33568 -0.11965 0.05509  -0.18774 130 MET A CG  
886  S SD  . MET A 123 ? 0.54627 0.65629 0.46084 -0.15110 0.04941  -0.21056 130 MET A SD  
887  C CE  . MET A 123 ? 0.58524 0.64907 0.52387 -0.16445 0.06410  -0.21905 130 MET A CE  
888  N N   . ILE A 124 ? 0.27193 0.31616 0.27469 -0.05201 0.03398  -0.10683 131 ILE A N   
889  C CA  . ILE A 124 ? 0.26011 0.30225 0.28193 -0.04269 0.02814  -0.09209 131 ILE A CA  
890  C C   . ILE A 124 ? 0.26487 0.26446 0.30242 -0.04039 0.03732  -0.09329 131 ILE A C   
891  O O   . ILE A 124 ? 0.25539 0.24910 0.30413 -0.04335 0.03616  -0.08983 131 ILE A O   
892  C CB  . ILE A 124 ? 0.24608 0.29977 0.26719 -0.02180 0.02109  -0.07052 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.24239 0.29854 0.27996 -0.01315 0.01561  -0.05774 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.27571 0.30140 0.29493 -0.01115 0.02953  -0.06625 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.27034 0.33593 0.30516 0.00633  0.01064  -0.03885 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.27735 0.24940 0.31585 -0.03387 0.04694  -0.09701 132 GLY A N   
897  C CA  . GLY A 125 ? 0.30795 0.24511 0.36215 -0.02611 0.05395  -0.09471 132 GLY A CA  
898  C C   . GLY A 125 ? 0.32749 0.23958 0.38273 -0.03933 0.06237  -0.10630 132 GLY A C   
899  O O   . GLY A 125 ? 0.38282 0.26915 0.44888 -0.03200 0.06534  -0.09844 132 GLY A O   
900  N N   . GLN A 126 ? 0.32333 0.24121 0.36519 -0.05967 0.06712  -0.12495 133 GLN A N   
901  C CA  . GLN A 126 ? 0.41345 0.30637 0.45319 -0.07567 0.07694  -0.13553 133 GLN A CA  
902  C C   . GLN A 126 ? 0.40976 0.30837 0.45681 -0.08553 0.07236  -0.13005 133 GLN A C   
903  O O   . GLN A 126 ? 0.43190 0.30906 0.47675 -0.09405 0.08030  -0.12965 133 GLN A O   
904  C CB  . GLN A 126 ? 0.42371 0.33098 0.44606 -0.09728 0.08146  -0.15648 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.47750 0.37625 0.49082 -0.09034 0.08945  -0.16332 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.58874 0.49962 0.58324 -0.11241 0.09495  -0.18396 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.59430 0.49503 0.58622 -0.12862 0.10122  -0.19204 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.63702 0.57013 0.61632 -0.11370 0.09352  -0.19239 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.33055 0.26755 0.38316 -0.07732 0.05763  -0.11507 134 PHE A N   
910  C CA  . PHE A 127 ? 0.32163 0.27498 0.38208 -0.08398 0.05274  -0.10711 134 PHE A CA  
911  C C   . PHE A 127 ? 0.30955 0.25234 0.37987 -0.06264 0.04839  -0.08537 134 PHE A C   
912  O O   . PHE A 127 ? 0.32133 0.28228 0.39750 -0.06411 0.04390  -0.07667 134 PHE A O   
913  C CB  . PHE A 127 ? 0.29580 0.30811 0.35495 -0.09261 0.04049  -0.10986 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.29586 0.32703 0.34239 -0.11479 0.04227  -0.13241 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.41291 0.44476 0.45867 -0.14460 0.04986  -0.15139 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.30687 0.35272 0.33978 -0.10815 0.03812  -0.13600 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.40736 0.45818 0.43873 -0.16496 0.05156  -0.17248 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.31651 0.38177 0.33352 -0.12948 0.03957  -0.15810 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.41004 0.47906 0.42670 -0.15994 0.04571  -0.17913 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.30594 0.22397 0.37857 -0.04384 0.04995  -0.07791 135 GLY A N   
921  C CA  . GLY A 128 ? 0.29868 0.20612 0.37873 -0.02654 0.04619  -0.06044 135 GLY A CA  
922  C C   . GLY A 128 ? 0.26855 0.20639 0.35135 -0.01500 0.03488  -0.04904 135 GLY A C   
923  O O   . GLY A 128 ? 0.31619 0.24905 0.40273 -0.00459 0.03178  -0.03702 135 GLY A O   
924  N N   . VAL A 129 ? 0.23451 0.20146 0.31303 -0.01581 0.02959  -0.05215 136 VAL A N   
925  C CA  . VAL A 129 ? 0.21155 0.20109 0.29057 -0.00324 0.02171  -0.04061 136 VAL A CA  
926  C C   . VAL A 129 ? 0.21768 0.20824 0.29059 0.00590  0.02116  -0.03941 136 VAL A C   
927  O O   . VAL A 129 ? 0.21495 0.22412 0.28234 0.01369  0.01685  -0.03204 136 VAL A O   
928  C CB  . VAL A 129 ? 0.20859 0.23557 0.28803 -0.00910 0.01642  -0.04001 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.23179 0.25792 0.31883 -0.01707 0.01901  -0.03848 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.24606 0.29483 0.31889 -0.02404 0.01566  -0.05319 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.23082 0.20062 0.24589 -0.02373 -0.00233 -0.04147 137 GLY A N   
932  C CA  . GLY A 130 ? 0.24105 0.21169 0.24236 -0.01595 -0.00062 -0.03987 137 GLY A CA  
933  C C   . GLY A 130 ? 0.24303 0.21940 0.24577 -0.01376 0.00331  -0.03103 137 GLY A C   
934  O O   . GLY A 130 ? 0.23832 0.21836 0.23376 -0.00842 0.00388  -0.02791 137 GLY A O   
935  N N   . PHE A 131 ? 0.23002 0.20664 0.24191 -0.01724 0.00586  -0.02682 138 PHE A N   
936  C CA  . PHE A 131 ? 0.21402 0.19414 0.22795 -0.01528 0.00760  -0.02095 138 PHE A CA  
937  C C   . PHE A 131 ? 0.21344 0.20026 0.22611 -0.01264 0.00444  -0.02029 138 PHE A C   
938  O O   . PHE A 131 ? 0.20649 0.19320 0.21749 -0.00913 0.00564  -0.01547 138 PHE A O   
939  C CB  . PHE A 131 ? 0.25724 0.23842 0.27858 -0.01800 0.00885  -0.01912 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.22335 0.20744 0.24652 -0.01559 0.00823  -0.01649 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.23542 0.21584 0.25881 -0.01388 0.00898  -0.01352 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.21533 0.20580 0.24166 -0.01477 0.00645  -0.01738 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.22820 0.20843 0.25474 -0.01213 0.00694  -0.01271 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.24183 0.23227 0.26900 -0.01131 0.00539  -0.01647 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.25059 0.23449 0.27773 -0.01033 0.00509  -0.01476 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.21259 0.20567 0.22814 -0.01430 0.00028  -0.02427 139 TYR A N   
947  C CA  . TYR A 132 ? 0.20788 0.20891 0.22386 -0.01087 -0.00298 -0.02300 139 TYR A CA  
948  C C   . TYR A 132 ? 0.21484 0.21672 0.21984 -0.00498 -0.00458 -0.02171 139 TYR A C   
949  O O   . TYR A 132 ? 0.23141 0.23816 0.23555 -0.00043 -0.00622 -0.01801 139 TYR A O   
950  C CB  . TYR A 132 ? 0.20330 0.21415 0.22860 -0.01411 -0.00707 -0.02680 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.20815 0.22038 0.24353 -0.01792 -0.00331 -0.02506 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.21729 0.23319 0.25544 -0.01438 -0.00116 -0.02176 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.22541 0.23436 0.26634 -0.02380 -0.00154 -0.02639 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.20027 0.21871 0.24408 -0.01558 0.00295  -0.02000 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.24446 0.25580 0.29291 -0.02582 0.00315  -0.02261 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.22206 0.23915 0.27067 -0.02119 0.00552  -0.01951 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.24070 0.26145 0.29351 -0.02115 0.01068  -0.01567 139 TYR A OH  
958  N N   . SER A 133 ? 0.22889 0.22607 0.22458 -0.00351 -0.00341 -0.02383 140 SER A N   
959  C CA  . SER A 133 ? 0.22953 0.22831 0.21218 0.00419  -0.00265 -0.02054 140 SER A CA  
960  C C   . SER A 133 ? 0.21450 0.21136 0.19931 0.00724  0.00316  -0.00952 140 SER A C   
961  O O   . SER A 133 ? 0.23773 0.23751 0.21420 0.01409  0.00487  -0.00320 140 SER A O   
962  C CB  . SER A 133 ? 0.25854 0.25260 0.22970 0.00693  -0.00113 -0.02522 140 SER A CB  
963  O OG  . SER A 133 ? 0.25298 0.24039 0.22771 0.00561  0.00593  -0.02100 140 SER A OG  
964  N N   . ALA A 134 ? 0.21533 0.20742 0.21160 0.00255  0.00581  -0.00688 141 ALA A N   
965  C CA  . ALA A 134 ? 0.20320 0.19226 0.20583 0.00388  0.00913  0.00213  141 ALA A CA  
966  C C   . ALA A 134 ? 0.21434 0.20617 0.21648 0.00852  0.00682  0.00666  141 ALA A C   
967  O O   . ALA A 134 ? 0.22518 0.21456 0.22920 0.01184  0.01014  0.01627  141 ALA A O   
968  C CB  . ALA A 134 ? 0.20246 0.18652 0.21673 -0.00148 0.00894  0.00066  141 ALA A CB  
969  N N   . TYR A 135 ? 0.20459 0.20216 0.20601 0.00909  0.00145  0.00102  142 TYR A N   
970  C CA  . TYR A 135 ? 0.21995 0.22102 0.22187 0.01467  -0.00118 0.00524  142 TYR A CA  
971  C C   . TYR A 135 ? 0.23377 0.24102 0.22280 0.02236  -0.00189 0.00990  142 TYR A C   
972  O O   . TYR A 135 ? 0.25116 0.26208 0.23918 0.02859  -0.00409 0.01497  142 TYR A O   
973  C CB  . TYR A 135 ? 0.18953 0.19726 0.19802 0.01328  -0.00603 -0.00151 142 TYR A CB  
974  C CG  . TYR A 135 ? 0.20096 0.20237 0.21917 0.00958  -0.00423 -0.00340 142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.21656 0.21127 0.24018 0.01312  -0.00395 0.00018  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.19883 0.19956 0.21960 0.00347  -0.00296 -0.00875 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.21312 0.20155 0.24277 0.01118  -0.00355 -0.00361 142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.20010 0.19620 0.22638 0.00192  -0.00165 -0.01050 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.20013 0.19045 0.22991 0.00602  -0.00243 -0.00887 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.21753 0.20309 0.25013 0.00588  -0.00247 -0.01273 142 TYR A OH  
981  N N   . LEU A 136 ? 0.23688 0.24537 0.21472 0.02361  0.00005  0.00847  143 LEU A N   
982  C CA  . LEU A 136 ? 0.24087 0.25477 0.20326 0.03321  0.00120  0.01469  143 LEU A CA  
983  C C   . LEU A 136 ? 0.25105 0.26026 0.21694 0.03715  0.00902  0.03042  143 LEU A C   
984  O O   . LEU A 136 ? 0.27926 0.29305 0.23605 0.04624  0.01021  0.03980  143 LEU A O   
985  C CB  . LEU A 136 ? 0.25808 0.27301 0.20669 0.03501  0.00256  0.00877  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.26100 0.27891 0.20529 0.03184  -0.00600 -0.00691 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.26782 0.28160 0.20040 0.03361  -0.00349 -0.01305 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.28928 0.31824 0.22471 0.03805  -0.01525 -0.01082 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.24387 0.24436 0.22406 0.03047  0.01403  0.03407  144 VAL A N   
990  C CA  . VAL A 137 ? 0.27468 0.27038 0.26309 0.03207  0.02144  0.04921  144 VAL A CA  
991  C C   . VAL A 137 ? 0.24871 0.23368 0.25699 0.02600  0.01998  0.05121  144 VAL A C   
992  O O   . VAL A 137 ? 0.26426 0.24341 0.28266 0.02712  0.02424  0.06407  144 VAL A O   
993  C CB  . VAL A 137 ? 0.22923 0.22630 0.21757 0.03131  0.02957  0.05417  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.26374 0.27020 0.22935 0.04049  0.03163  0.05262  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.23849 0.23111 0.23735 0.02197  0.02808  0.04450  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.24202 0.22377 0.25631 0.02030  0.01417  0.03930  145 ALA A N   
997  C CA  . ALA A 138 ? 0.23849 0.20946 0.26879 0.01568  0.01198  0.03824  145 ALA A CA  
998  C C   . ALA A 138 ? 0.25173 0.22163 0.28191 0.01963  0.00655  0.03378  145 ALA A C   
999  O O   . ALA A 138 ? 0.28727 0.26628 0.30961 0.02122  0.00299  0.02588  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.26239 0.23132 0.29833 0.00810  0.01036  0.02854  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.24089 0.19959 0.28185 0.02124  0.00590  0.03898  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.25563 0.21149 0.29826 0.02596  0.00111  0.03380  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.25731 0.20893 0.30486 0.02189  -0.00255 0.02109  146 GLU A C   
1004 O O   . GLU A 139 ? 0.26117 0.21646 0.30667 0.02625  -0.00550 0.01429  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.31491 0.25794 0.36639 0.03095  0.00178  0.04431  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.44815 0.37382 0.51652 0.02475  0.00151  0.04544  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.64879 0.56014 0.72869 0.02847  0.00321  0.05873  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.61211 0.50695 0.70932 0.02317  0.00124  0.05879  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.66199 0.57831 0.73439 0.03683  0.00590  0.06921  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.25608 0.20195 0.30978 0.01473  -0.00223 0.01832  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.22995 0.17327 0.28518 0.01201  -0.00584 0.00660  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.21994 0.16711 0.27535 0.00486  -0.00414 0.00537  147 LYS A C   
1013 O O   . LYS A 140 ? 0.22806 0.17409 0.28892 0.00152  -0.00100 0.01344  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.24852 0.17528 0.31441 0.01291  -0.01034 0.00337  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.27119 0.19549 0.33516 0.01262  -0.01499 -0.00987 147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.32985 0.23639 0.40193 0.01588  -0.02101 -0.01555 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.35241 0.24695 0.43996 0.00795  -0.02484 -0.01417 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.50231 0.37613 0.60067 0.01038  -0.03199 -0.01987 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.19164 0.14455 0.24144 0.00350  -0.00530 -0.00330 148 VAL A N   
1020 C CA  . VAL A 141 ? 0.20789 0.16397 0.25758 -0.00193 -0.00413 -0.00485 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.22787 0.18041 0.27840 -0.00211 -0.00857 -0.01369 148 VAL A C   
1022 O O   . VAL A 141 ? 0.20537 0.16055 0.24950 0.00232  -0.00971 -0.01981 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.21930 0.18621 0.25958 -0.00273 -0.00068 -0.00536 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.23127 0.19958 0.27171 -0.00703 0.00071  -0.00667 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.20663 0.17754 0.24270 -0.00082 0.00222  0.00138  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.21344 0.16184 0.27178 -0.00630 -0.01111 -0.01413 149 THR A N   
1027 C CA  . THR A 142 ? 0.21367 0.16044 0.27079 -0.00583 -0.01656 -0.02296 149 THR A CA  
1028 C C   . THR A 142 ? 0.23533 0.19011 0.29032 -0.00906 -0.01439 -0.02152 149 THR A C   
1029 O O   . THR A 142 ? 0.23406 0.19082 0.29664 -0.01321 -0.01163 -0.01475 149 THR A O   
1030 C CB  . THR A 142 ? 0.23774 0.17292 0.30821 -0.00786 -0.02411 -0.02620 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.28297 0.20775 0.35766 -0.00488 -0.02543 -0.02563 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.27211 0.20586 0.33756 -0.00512 -0.03183 -0.03800 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.20343 0.16330 0.24816 -0.00609 -0.01469 -0.02667 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.21274 0.17899 0.25483 -0.00778 -0.01263 -0.02478 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.20818 0.17447 0.24782 -0.00496 -0.01952 -0.03157 150 VAL A C   
1036 O O   . VAL A 143 ? 0.24051 0.20774 0.26940 0.00102  -0.02107 -0.03740 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.20511 0.17782 0.23766 -0.00666 -0.00603 -0.02244 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.27272 0.24925 0.30301 -0.00752 -0.00385 -0.01994 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.21856 0.19184 0.25244 -0.00881 -0.00160 -0.01798 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.19599 0.16292 0.24543 -0.00824 -0.02382 -0.03081 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.20054 0.16965 0.24793 -0.00538 -0.03212 -0.03749 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.21575 0.19363 0.25786 -0.00421 -0.02801 -0.03231 151 ILE A C   
1043 O O   . ILE A 144 ? 0.20920 0.18965 0.25925 -0.00816 -0.02286 -0.02482 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.22786 0.19333 0.29408 -0.01037 -0.04135 -0.04008 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.34527 0.29957 0.42200 -0.01338 -0.04307 -0.04098 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.26377 0.23080 0.32600 -0.00619 -0.05320 -0.05067 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.33329 0.27904 0.39929 -0.00706 -0.04855 -0.05184 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.21326 0.19554 0.24131 0.00244  -0.02972 -0.03564 152 THR A N   
1049 C CA  . THR A 145 ? 0.21563 0.20457 0.23797 0.00451  -0.02448 -0.02887 152 THR A CA  
1050 C C   . THR A 145 ? 0.22329 0.21833 0.23491 0.01216  -0.03105 -0.03267 152 THR A C   
1051 O O   . THR A 145 ? 0.24158 0.23624 0.24277 0.01812  -0.03693 -0.04101 152 THR A O   
1052 C CB  . THR A 145 ? 0.21359 0.20233 0.22816 0.00469  -0.01354 -0.02285 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.23890 0.23013 0.25293 0.00481  -0.00821 -0.01537 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.24366 0.23509 0.24422 0.01138  -0.01205 -0.02568 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.21543 0.21629 0.22853 0.01338  -0.03016 -0.02663 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.21503 0.22360 0.21692 0.02193  -0.03604 -0.02797 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.23377 0.24560 0.23166 0.02459  -0.02713 -0.01633 153 LYS A C   
1058 O O   . LYS A 146 ? 0.22752 0.23910 0.23797 0.02039  -0.02436 -0.01073 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.23171 0.24489 0.24582 0.02078  -0.04967 -0.03447 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.24641 0.26984 0.24936 0.03040  -0.05779 -0.03604 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.25919 0.28322 0.23886 0.04060  -0.06227 -0.04449 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.29989 0.33533 0.26670 0.05156  -0.07246 -0.04719 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.29315 0.33509 0.24886 0.05839  -0.06211 -0.03265 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.24122 0.25572 0.22223 0.03219  -0.02191 -0.01207 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.22380 0.23981 0.20016 0.03599  -0.01352 0.00000  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.27014 0.29597 0.23357 0.04730  -0.02025 0.00092  154 HIS A C   
1067 O O   . HIS A 147 ? 0.27968 0.31079 0.23098 0.05384  -0.02852 -0.00778 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.23993 0.25299 0.20904 0.03612  -0.00185 0.00637  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.27454 0.28555 0.24301 0.03784  0.00800  0.01984  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.29937 0.31676 0.25520 0.04820  0.00965  0.02821  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.28593 0.28797 0.26489 0.03093  0.01646  0.02634  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.31791 0.32927 0.27844 0.04697  0.01942  0.04060  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.31516 0.31647 0.29006 0.03621  0.02311  0.03861  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.25405 0.28210 0.21915 0.05079  -0.01741 0.01086  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.27222 0.31117 0.22469 0.06282  -0.02438 0.01304  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.31009 0.35457 0.23850 0.07383  -0.02231 0.01421  155 ASN A C   
1077 O O   . ASN A 148 ? 0.34138 0.39613 0.25506 0.08471  -0.03241 0.00936  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.28936 0.32835 0.24580 0.06654  -0.01865 0.02661  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.29610 0.33631 0.27286 0.06134  -0.02395 0.02466  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.32482 0.37123 0.31136 0.05778  -0.03540 0.01420  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.31507 0.34960 0.29942 0.06153  -0.01549 0.03520  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.30963 0.34912 0.23389 0.07201  -0.00956 0.02059  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.34955 0.39643 0.25230 0.08349  -0.00386 0.02565  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.40142 0.45019 0.29521 0.08527  -0.00759 0.01257  156 ASP A C   
1085 O O   . ASP A 149 ? 0.41320 0.46888 0.28986 0.09502  -0.00068 0.01674  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.36725 0.41007 0.27339 0.08141  0.01337  0.04301  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.38624 0.42513 0.29854 0.08241  0.01782  0.05690  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.40313 0.44769 0.31012 0.08979  0.00878  0.05592  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.46423 0.49416 0.38774 0.07608  0.02977  0.06847  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.34638 0.38925 0.25175 0.07700  -0.01741 -0.00207 157 ASP A N   
1091 C CA  . ASP A 150 ? 0.32188 0.36358 0.22039 0.07885  -0.02064 -0.01446 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.38582 0.42294 0.29257 0.07481  -0.03741 -0.03148 157 ASP A C   
1093 O O   . ASP A 150 ? 0.33982 0.37717 0.25917 0.07005  -0.04569 -0.03258 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.33134 0.36709 0.24121 0.06985  -0.00861 -0.00989 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.34397 0.38368 0.24066 0.07764  -0.00535 -0.01525 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.41425 0.45822 0.29267 0.08949  -0.01381 -0.02583 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.35197 0.39111 0.25689 0.07253  0.00536  -0.00935 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.33151 0.36464 0.23292 0.07700  -0.04221 -0.04427 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.35897 0.38471 0.27072 0.07232  -0.05777 -0.06054 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.29181 0.30681 0.22838 0.05711  -0.05418 -0.05914 158 GLU A C   
1101 O O   . GLU A 151 ? 0.28748 0.30110 0.23015 0.05146  -0.04101 -0.04812 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.43085 0.45481 0.32379 0.08362  -0.06494 -0.07571 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.50972 0.54559 0.37290 0.10168  -0.06782 -0.07765 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.73897 0.78192 0.60199 0.10391  -0.08112 -0.07988 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 0.87020 0.92505 0.71719 0.11384  -0.07613 -0.06891 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 0.87235 0.90979 0.75296 0.09584  -0.09648 -0.09156 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.29806 0.30551 0.24935 0.05079  -0.06654 -0.07039 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.27577 0.27380 0.24992 0.03770  -0.06345 -0.06796 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.27638 0.26601 0.24604 0.03912  -0.05917 -0.07260 159 GLN A C   
1110 O O   . GLN A 152 ? 0.31149 0.29687 0.27025 0.04695  -0.06704 -0.08528 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.25806 0.25216 0.25339 0.02998  -0.07733 -0.07545 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.26275 0.25035 0.28279 0.01696  -0.07208 -0.06835 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.30421 0.29332 0.34923 0.00880  -0.08263 -0.07005 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.34389 0.34395 0.39294 0.00960  -0.08628 -0.06693 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.31529 0.29418 0.37913 0.00107  -0.08724 -0.07378 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.23944 0.22682 0.21725 0.03249  -0.04746 -0.06309 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.27292 0.25535 0.24763 0.03434  -0.04205 -0.06500 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.27512 0.24909 0.26920 0.02371  -0.04023 -0.06155 160 TYR A C   
1119 O O   . TYR A 153 ? 0.24861 0.22332 0.25578 0.01529  -0.03798 -0.05398 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.26611 0.25784 0.22968 0.03877  -0.02856 -0.05546 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.29444 0.29467 0.23608 0.05246  -0.02789 -0.05832 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.32845 0.32797 0.25802 0.06260  -0.02888 -0.06716 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.34276 0.35195 0.27455 0.05697  -0.02608 -0.05187 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.38675 0.39557 0.29355 0.07739  -0.02732 -0.06961 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.38460 0.40299 0.29389 0.07134  -0.02467 -0.05303 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.42040 0.43912 0.31663 0.08171  -0.02508 -0.06207 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.51172 0.54105 0.38318 0.09802  -0.02260 -0.06294 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.26290 0.22950 0.25734 0.02582  -0.04046 -0.06647 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.23982 0.19910 0.24925 0.01839  -0.03764 -0.06196 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.24299 0.20644 0.24623 0.02210  -0.02832 -0.05792 161 ALA A C   
1131 O O   . ALA A 154 ? 0.24994 0.21378 0.24267 0.03133  -0.02848 -0.06419 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.29481 0.23988 0.31436 0.01750  -0.04791 -0.07090 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.22191 0.18937 0.23197 0.01564  -0.02079 -0.04813 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.20232 0.17470 0.21190 0.01686  -0.01370 -0.04386 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.23133 0.19537 0.25169 0.01319  -0.01540 -0.04203 162 TRP A C   
1136 O O   . TRP A 155 ? 0.21578 0.17397 0.24543 0.00690  -0.01778 -0.03906 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.22266 0.20424 0.23282 0.01189  -0.00618 -0.03532 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.18337 0.17210 0.19674 0.01052  -0.00013 -0.03051 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.19061 0.19045 0.20167 0.01297  0.00582  -0.02757 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.19813 0.18513 0.21886 0.00617  0.00011  -0.02744 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.19764 0.20287 0.21638 0.00949  0.00835  -0.02417 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.20570 0.20313 0.22840 0.00604  0.00450  -0.02458 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.20377 0.18267 0.22996 0.00294  -0.00278 -0.02599 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.19505 0.19494 0.22304 0.00343  0.00426  -0.02227 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.20926 0.19049 0.23846 0.00142  -0.00129 -0.02214 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.20857 0.20015 0.23770 0.00193  0.00133  -0.02126 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.21093 0.17549 0.23073 0.01803  -0.01367 -0.04260 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.21080 0.16762 0.23965 0.01612  -0.01490 -0.03917 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.19881 0.16413 0.22671 0.02017  -0.01047 -0.03586 163 GLU A C   
1150 O O   . GLU A 156 ? 0.21686 0.18992 0.23927 0.02705  -0.00832 -0.03920 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.25410 0.19545 0.28722 0.01951  -0.02225 -0.04591 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.27688 0.20763 0.32199 0.01664  -0.02333 -0.03988 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.43327 0.34611 0.48758 0.01657  -0.03163 -0.04605 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.43540 0.33986 0.48541 0.02481  -0.03576 -0.05518 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.38395 0.29123 0.45096 0.00852  -0.03423 -0.04218 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.19675 0.16236 0.23011 0.01686  -0.00911 -0.02893 164 SER A N   
1157 C CA  . SER A 157 ? 0.19363 0.16769 0.22758 0.02142  -0.00711 -0.02622 164 SER A CA  
1158 C C   . SER A 157 ? 0.18804 0.15659 0.22653 0.02095  -0.00808 -0.01939 164 SER A C   
1159 O O   . SER A 157 ? 0.18926 0.15517 0.22910 0.01518  -0.00724 -0.01427 164 SER A O   
1160 C CB  . SER A 157 ? 0.20445 0.19492 0.23728 0.01845  -0.00311 -0.02414 164 SER A CB  
1161 O OG  . SER A 157 ? 0.20015 0.20088 0.23638 0.02255  -0.00280 -0.02188 164 SER A OG  
1162 N N   . SER A 158 ? 0.21873 0.18638 0.25906 0.02849  -0.00915 -0.01847 165 SER A N   
1163 C CA  . SER A 158 ? 0.25009 0.21681 0.29280 0.03061  -0.00932 -0.01019 165 SER A CA  
1164 C C   . SER A 158 ? 0.20866 0.19361 0.24948 0.03352  -0.00867 -0.00828 165 SER A C   
1165 O O   . SER A 158 ? 0.27335 0.26049 0.31512 0.03962  -0.00993 -0.00300 165 SER A O   
1166 C CB  . SER A 158 ? 0.27234 0.22389 0.32005 0.03770  -0.01175 -0.00921 165 SER A CB  
1167 O OG  . SER A 158 ? 0.30849 0.24263 0.36167 0.03324  -0.01395 -0.01085 165 SER A OG  
1168 N N   . ALA A 159 ? 0.22105 0.21921 0.26073 0.02920  -0.00724 -0.01204 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.24171 0.25869 0.28424 0.03041  -0.00778 -0.01179 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.26702 0.29079 0.31440 0.04009  -0.00776 -0.01303 166 ALA A C   
1171 O O   . ALA A 159 ? 0.29713 0.31370 0.34352 0.04451  -0.00606 -0.01718 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.30485 0.32673 0.34457 0.02965  -0.01061 -0.00700 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.28137 0.31963 0.33350 0.04461  -0.01008 -0.01012 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.27267 0.31959 0.33083 0.05499  -0.00932 -0.01081 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.26952 0.33058 0.33330 0.05493  -0.00478 -0.01453 167 GLY A C   
1176 O O   . GLY A 160 ? 0.27726 0.34443 0.34440 0.06519  -0.00233 -0.01572 167 GLY A O   
1177 N N   . GLY A 161 ? 0.20345 0.26946 0.26814 0.04472  -0.00272 -0.01558 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.17123 0.25423 0.24399 0.04366  0.00254  -0.01574 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.16504 0.24004 0.22960 0.04539  0.00813  -0.01867 168 GLY A C   
1180 O O   . GLY A 161 ? 0.19981 0.28958 0.26992 0.04554  0.01415  -0.01679 168 GLY A O   
1181 N N   . SER A 162 ? 0.19728 0.25068 0.24974 0.04691  0.00617  -0.02265 169 SER A N   
1182 C CA  . SER A 162 ? 0.18863 0.23542 0.23170 0.05018  0.00949  -0.02696 169 SER A CA  
1183 C C   . SER A 162 ? 0.20490 0.23252 0.24009 0.04308  0.00586  -0.02944 169 SER A C   
1184 O O   . SER A 162 ? 0.21480 0.23162 0.25119 0.03837  0.00154  -0.02796 169 SER A O   
1185 C CB  . SER A 162 ? 0.23161 0.27333 0.26866 0.06459  0.00982  -0.03258 169 SER A CB  
1186 O OG  . SER A 162 ? 0.28218 0.30388 0.31708 0.06712  0.00351  -0.03553 169 SER A OG  
1187 N N   . PHE A 163 ? 0.20291 0.22842 0.23027 0.04341  0.00812  -0.03229 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.20233 0.21189 0.22308 0.03862  0.00415  -0.03554 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.21887 0.22390 0.22810 0.04749  0.00348  -0.04298 170 PHE A C   
1190 O O   . PHE A 163 ? 0.22322 0.23992 0.22771 0.05655  0.00850  -0.04379 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.21975 0.23264 0.24243 0.02787  0.00620  -0.03062 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.18669 0.21317 0.20818 0.02815  0.01284  -0.02721 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.19532 0.23766 0.22731 0.02529  0.01764  -0.02136 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.19492 0.21881 0.20629 0.03092  0.01394  -0.02891 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.19850 0.25300 0.23288 0.02457  0.02481  -0.01581 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.18885 0.22512 0.19898 0.03185  0.02127  -0.02313 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.21350 0.26466 0.23617 0.02829  0.02743  -0.01580 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.22359 0.21273 0.22859 0.04557  -0.00304 -0.04858 171 THR A N   
1199 C CA  . THR A 164 ? 0.23548 0.21936 0.22803 0.05389  -0.00641 -0.05782 171 THR A CA  
1200 C C   . THR A 164 ? 0.21165 0.19520 0.19977 0.04796  -0.00810 -0.05721 171 THR A C   
1201 O O   . THR A 164 ? 0.21428 0.19497 0.21072 0.03721  -0.00894 -0.05182 171 THR A O   
1202 C CB  . THR A 164 ? 0.25158 0.21601 0.24416 0.05869  -0.01544 -0.06792 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.29378 0.24528 0.29746 0.04766  -0.02116 -0.06577 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.25717 0.22061 0.25342 0.06681  -0.01369 -0.06831 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.22688 0.21421 0.20066 0.05668  -0.00847 -0.06264 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.25080 0.23770 0.21818 0.05413  -0.01188 -0.06342 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.27257 0.25140 0.22633 0.06453  -0.02120 -0.07733 172 VAL A C   
1208 O O   . VAL A 165 ? 0.29060 0.27246 0.23180 0.07763  -0.01958 -0.08360 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.25760 0.26081 0.21922 0.05483  -0.00206 -0.05339 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.28286 0.28542 0.23654 0.05438  -0.00614 -0.05383 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.24992 0.25889 0.22627 0.04388  0.00502  -0.04201 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.27284 0.24215 0.22964 0.05931  -0.03144 -0.08280 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.28835 0.25032 0.23292 0.06820  -0.04300 -0.09768 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.27546 0.23957 0.22104 0.06275  -0.04995 -0.09751 173 ARG A C   
1215 O O   . ARG A 166 ? 0.27619 0.24183 0.23663 0.05074  -0.04758 -0.08768 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.36050 0.30271 0.31479 0.06759  -0.05350 -0.10933 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.38343 0.31521 0.36201 0.05202  -0.05836 -0.10454 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.48699 0.39993 0.47832 0.05099  -0.06387 -0.11015 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.54568 0.46142 0.54120 0.05114  -0.05310 -0.10013 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.61865 0.52103 0.62097 0.05427  -0.05453 -0.10263 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.51269 0.39510 0.51976 0.05676  -0.06597 -0.11505 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.55143 0.46022 0.55673 0.05516  -0.04504 -0.09264 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.32170 0.28686 0.25041 0.07305  -0.05884 -0.10886 174 THR A N   
1224 C CA  . THR A 167 ? 0.30764 0.27387 0.23979 0.06853  -0.06930 -0.11148 174 THR A CA  
1225 C C   . THR A 167 ? 0.38024 0.33167 0.33757 0.05593  -0.08035 -0.11661 174 THR A C   
1226 O O   . THR A 167 ? 0.42537 0.36198 0.38878 0.05649  -0.08640 -0.12627 174 THR A O   
1227 C CB  . THR A 167 ? 0.38725 0.35702 0.29517 0.08355  -0.07937 -0.12523 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.49212 0.47645 0.37644 0.09682  -0.06687 -0.11848 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.47379 0.44882 0.38529 0.07972  -0.09019 -0.12637 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.34627 0.30184 0.31993 0.04484  -0.08193 -0.10873 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.35442 0.29947 0.35573 0.03190  -0.08936 -0.10918 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.46200 0.40360 0.46872 0.03212  -0.10800 -0.12341 175 ASP A C   
1233 O O   . ASP A 168 ? 0.48011 0.43393 0.48076 0.03468  -0.11277 -0.12358 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.33016 0.28304 0.34786 0.02064  -0.08024 -0.09267 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.48058 0.42510 0.52747 0.00814  -0.08479 -0.08989 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.50437 0.43497 0.55980 0.00626  -0.08694 -0.09367 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.42829 0.38061 0.49042 0.00089  -0.08553 -0.08285 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.59232 0.51829 0.61163 0.02958  -0.11776 -0.13346 176 THR A N   
1239 C CA  . THR A 169 ? 0.71691 0.64158 0.74794 0.02741  -0.13176 -0.14109 176 THR A CA  
1240 C C   . THR A 169 ? 0.68447 0.60915 0.75037 0.01151  -0.13446 -0.13227 176 THR A C   
1241 O O   . THR A 169 ? 0.67775 0.60292 0.75796 0.00807  -0.14590 -0.13737 176 THR A O   
1242 C CB  . THR A 169 ? 0.74154 0.65192 0.76892 0.03355  -0.13731 -0.15186 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.72785 0.62621 0.76346 0.02997  -0.12834 -0.14572 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.66496 0.58008 0.65846 0.05131  -0.13814 -0.16230 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.63536 0.56053 0.71537 0.00247  -0.12369 -0.11874 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.66245 0.59000 0.77484 -0.01114 -0.12296 -0.10743 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.54822 0.49267 0.66951 -0.01441 -0.12844 -0.10511 177 GLY A C   
1248 O O   . GLY A 170 ? 0.54061 0.49382 0.64402 -0.00613 -0.13597 -0.11380 177 GLY A O   
1249 N N   . GLU A 171 ? 0.47385 0.42432 0.62300 -0.02553 -0.12361 -0.09172 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.44472 0.41280 0.60941 -0.02964 -0.12765 -0.08683 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.43113 0.41281 0.57317 -0.02166 -0.12277 -0.08445 178 GLU A C   
1252 O O   . GLU A 171 ? 0.34935 0.33104 0.47800 -0.01946 -0.10618 -0.07342 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.48588 0.45829 0.68042 -0.04072 -0.11729 -0.06939 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.47337 0.46126 0.69419 -0.04661 -0.12226 -0.06385 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.45029 0.43459 0.67856 -0.04685 -0.13797 -0.07606 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.44353 0.41188 0.67648 -0.04877 -0.14096 -0.08065 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.51228 0.51008 0.74153 -0.04447 -0.14785 -0.08130 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.39566 0.38894 0.52865 -0.01522 -0.13377 -0.09200 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.41160 0.41781 0.52138 -0.00599 -0.12455 -0.08427 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.43086 0.44599 0.55476 -0.01148 -0.10966 -0.06605 179 PRO A C   
1261 O O   . PRO A 172 ? 0.49194 0.51272 0.64633 -0.02074 -0.11104 -0.05994 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.46371 0.48259 0.57202 -0.00039 -0.14175 -0.09391 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.55245 0.55894 0.65970 0.00039  -0.15769 -0.11240 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.54090 0.53022 0.66734 -0.01012 -0.15057 -0.10872 179 PRO A CD  
1265 N N   . MET A 173 ? 0.31538 0.33226 0.41727 -0.00502 -0.09546 -0.05747 180 MET A N   
1266 C CA  . MET A 173 ? 0.32868 0.35009 0.43818 -0.00827 -0.08042 -0.04231 180 MET A CA  
1267 C C   . MET A 173 ? 0.45686 0.49199 0.56272 -0.00226 -0.07845 -0.03539 180 MET A C   
1268 O O   . MET A 173 ? 0.42201 0.46281 0.54059 -0.00485 -0.06936 -0.02445 180 MET A O   
1269 C CB  . MET A 173 ? 0.42768 0.43909 0.51794 -0.00624 -0.06600 -0.03776 180 MET A CB  
1270 C CG  . MET A 173 ? 0.52234 0.52178 0.61922 -0.01218 -0.06342 -0.03921 180 MET A CG  
1271 S SD  . MET A 173 ? 0.50191 0.49438 0.57495 -0.00794 -0.04926 -0.03527 180 MET A SD  
1272 C CE  . MET A 173 ? 0.40454 0.40609 0.47130 -0.00461 -0.03969 -0.02489 180 MET A CE  
1273 N N   . GLY A 174 ? 0.36072 0.40128 0.44854 0.00708  -0.08613 -0.04092 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.31783 0.36988 0.39974 0.01446  -0.08311 -0.03268 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.26947 0.31475 0.32905 0.02002  -0.06768 -0.02418 181 GLY A C   
1276 O O   . GLY A 174 ? 0.27118 0.31795 0.30844 0.02959  -0.06779 -0.02423 181 GLY A O   
1277 N N   . ARG A 175 ? 0.21526 0.25337 0.28121 0.01426  -0.05456 -0.01669 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.21635 0.24624 0.26610 0.01699  -0.04080 -0.00977 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.19852 0.22096 0.25847 0.00936  -0.03088 -0.00584 182 ARG A C   
1280 O O   . ARG A 175 ? 0.23287 0.26013 0.31109 0.00559  -0.03013 -0.00229 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.21388 0.24881 0.25809 0.02460  -0.03618 -0.00057 182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.21970 0.24443 0.24924 0.02688  -0.02314 0.00645  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.21455 0.23954 0.24576 0.03209  -0.01660 0.01663  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.21201 0.23836 0.26099 0.02841  -0.01383 0.01868  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.21572 0.25385 0.27795 0.03187  -0.01839 0.02154  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.20882 0.25840 0.26883 0.03873  -0.02780 0.02177  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.21174 0.25206 0.28985 0.02931  -0.01355 0.02438  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.25010 0.27117 0.21205 0.04819  -0.02286 0.03765  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.23043 0.24239 0.21063 0.04391  -0.01495 0.03283  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.23142 0.23869 0.20941 0.03568  -0.01070 0.02191  183 GLY A C   
1291 O O   . GLY A 176 ? 0.23471 0.24155 0.19636 0.03597  -0.00832 0.02045  183 GLY A O   
1292 N N   . THR A 177 ? 0.21713 0.22166 0.21022 0.03065  -0.00872 0.01531  184 THR A N   
1293 C CA  . THR A 177 ? 0.19680 0.19802 0.19113 0.02475  -0.00469 0.00757  184 THR A CA  
1294 C C   . THR A 177 ? 0.22810 0.23154 0.23411 0.02044  -0.00876 -0.00018 184 THR A C   
1295 O O   . THR A 177 ? 0.21258 0.21792 0.22965 0.02111  -0.00901 0.00178  184 THR A O   
1296 C CB  . THR A 177 ? 0.22690 0.21975 0.22613 0.02092  0.00381  0.01229  184 THR A CB  
1297 O OG1 . THR A 177 ? 0.26306 0.25476 0.25276 0.02280  0.00881  0.02227  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.23956 0.23638 0.24511 0.01581  0.00643  0.00692  184 THR A CG2 
1299 N N   . LYS A 178 ? 0.20815 0.20989 0.20983 0.01780  -0.01039 -0.00774 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.20817 0.20809 0.21875 0.01286  -0.01301 -0.01327 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.20872 0.20417 0.22024 0.01311  -0.00693 -0.01523 185 LYS A C   
1302 O O   . LYS A 178 ? 0.22784 0.22154 0.22979 0.01774  -0.00373 -0.01689 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.28126 0.27744 0.28356 0.00936  -0.02246 -0.01952 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.49061 0.49935 0.50032 0.00528  -0.03214 -0.01586 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.49075 0.49420 0.49568 -0.00473 -0.04471 -0.02194 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.62803 0.60635 0.60598 -0.00252 -0.04504 -0.03283 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.74492 0.70742 0.71040 -0.01378 -0.05950 -0.04085 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.21125 0.20680 0.23311 0.00972  -0.00513 -0.01418 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.18984 0.18590 0.21516 0.00930  -0.00251 -0.01430 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.21567 0.20617 0.24234 0.00802  -0.00567 -0.01729 186 VAL A C   
1311 O O   . VAL A 179 ? 0.22268 0.21311 0.25384 0.00414  -0.00681 -0.01622 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.19633 0.19374 0.22697 0.00448  -0.00099 -0.01081 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.20708 0.21106 0.24364 0.00280  -0.00188 -0.00938 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.22529 0.22317 0.25459 0.00317  0.00196  -0.00590 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.20939 0.19335 0.23043 0.01263  -0.00563 -0.01996 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.19560 0.16709 0.21504 0.01142  -0.00868 -0.02158 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.19372 0.16930 0.21854 0.01595  -0.00597 -0.01701 187 ILE A C   
1318 O O   . ILE A 180 ? 0.20902 0.18932 0.23370 0.02501  -0.00210 -0.01563 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.23844 0.19052 0.24222 0.01477  -0.01150 -0.02844 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.25664 0.20917 0.25345 0.00951  -0.01732 -0.03226 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.26307 0.19481 0.26400 0.01106  -0.01540 -0.02901 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.32100 0.25056 0.29348 0.01248  -0.02183 -0.04159 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.18219 0.15920 0.21166 0.01094  -0.00767 -0.01314 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.19223 0.17506 0.22501 0.01435  -0.00803 -0.00744 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.22842 0.19403 0.25621 0.01843  -0.00885 -0.00501 188 LEU A C   
1326 O O   . LEU A 181 ? 0.23685 0.19258 0.26227 0.01147  -0.01016 -0.00328 188 LEU A O   
1327 C CB  . LEU A 181 ? 0.18756 0.17765 0.22022 0.00731  -0.00985 -0.00499 188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.22377 0.21970 0.25654 0.00242  -0.00932 -0.00803 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.26104 0.25345 0.28455 -0.00216 -0.01027 -0.00831 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.25584 0.26463 0.29607 0.00260  -0.01033 -0.00572 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.24739 0.20923 0.27408 0.03056  -0.00694 -0.00314 189 HIS A N   
1332 C CA  . HIS A 182 ? 0.24544 0.18504 0.26502 0.03740  -0.00726 0.00066  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.24180 0.19654 0.26787 0.03922  -0.00979 0.01169  189 HIS A C   
1334 O O   . HIS A 182 ? 0.24995 0.22534 0.28512 0.04854  -0.00994 0.01753  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.24289 0.16837 0.25452 0.05431  -0.00233 -0.00248 189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.31153 0.22375 0.31050 0.05318  -0.00082 -0.01425 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.39672 0.27146 0.37618 0.04972  -0.00430 -0.02276 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.31089 0.24137 0.31163 0.05352  0.00233  -0.01811 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.39468 0.26664 0.36252 0.04890  -0.00438 -0.03238 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.37503 0.28085 0.35546 0.05239  0.00075  -0.02890 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.23840 0.18678 0.26009 0.02990  -0.01207 0.01590  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.24820 0.21264 0.26965 0.02904  -0.01569 0.02469  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.29295 0.25439 0.31370 0.04220  -0.01773 0.03618  190 LEU A C   
1344 O O   . LEU A 183 ? 0.31993 0.25496 0.33534 0.05009  -0.01489 0.03882  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.26417 0.22299 0.27716 0.01812  -0.01444 0.02703  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.23389 0.20020 0.24836 0.00877  -0.01165 0.01857  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.29079 0.25588 0.29832 0.00244  -0.00710 0.02387  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.27781 0.26089 0.29251 0.00816  -0.01481 0.01357  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.26614 0.25310 0.29085 0.04433  -0.02401 0.04347  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.28867 0.27888 0.31291 0.05691  -0.02802 0.05788  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.33258 0.29738 0.33981 0.05409  -0.02670 0.06565  191 LYS A C   
1352 O O   . LYS A 184 ? 0.32521 0.28385 0.32283 0.04066  -0.02436 0.06187  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.28129 0.30775 0.31175 0.05451  -0.03900 0.06436  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.31981 0.37793 0.37300 0.05629  -0.04105 0.06275  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.33360 0.42233 0.38974 0.04260  -0.05506 0.06509  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.38499 0.50601 0.46669 0.03842  -0.05703 0.06505  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.39794 0.55075 0.48612 0.02378  -0.07465 0.07074  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.36036 0.31120 0.36461 0.06841  -0.02687 0.07867  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.43922 0.36150 0.42771 0.06598  -0.02452 0.08951  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.39766 0.33528 0.37267 0.05516  -0.02777 0.09561  192 GLU A C   
1361 O O   . GLU A 185 ? 0.45233 0.37277 0.41619 0.04566  -0.02192 0.10025  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.48154 0.38841 0.46765 0.08634  -0.02549 0.10528  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.72045 0.57802 0.69276 0.08573  -0.01986 0.11266  192 GLU A CG  
1364 C CD  . GLU A 185 ? 0.88337 0.72017 0.85092 0.10962  -0.02012 0.12875  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 0.84099 0.71133 0.81841 0.12651  -0.02544 0.13720  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.03190 0.81880 0.98654 0.11125  -0.01570 0.13412  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.35152 0.32099 0.32574 0.05600  -0.03704 0.09638  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.37114 0.35050 0.32339 0.04826  -0.04129 0.10072  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.36229 0.34883 0.30794 0.03413  -0.03903 0.08429  193 ASP A C   
1370 O O   . ASP A 186 ? 0.36581 0.35908 0.28823 0.02922  -0.04293 0.08382  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.42129 0.42619 0.36926 0.05616  -0.05611 0.11205  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.44162 0.47800 0.40840 0.05319  -0.06651 0.10314  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.50729 0.54312 0.49314 0.05092  -0.06017 0.09125  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.56463 0.62736 0.52693 0.05185  -0.08197 0.10938  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.31075 0.29270 0.27228 0.02915  -0.03264 0.07103  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.31191 0.29826 0.26911 0.01896  -0.02977 0.05659  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.28490 0.25736 0.24547 0.01370  -0.01704 0.05343  194 GLN A C   
1378 O O   . GLN A 187 ? 0.29309 0.26818 0.25935 0.00875  -0.01327 0.04198  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.30567 0.30602 0.27978 0.01696  -0.03542 0.04588  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.29335 0.31654 0.27071 0.01859  -0.04959 0.05105  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.37162 0.39818 0.32123 0.01156  -0.05922 0.05091  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.37803 0.39172 0.30736 0.00427  -0.05523 0.04031  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.37350 0.41682 0.31969 0.01527  -0.07234 0.06270  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.32743 0.28649 0.28594 0.01390  -0.01105 0.06554  195 THR A N   
1385 C CA  . THR A 188 ? 0.34362 0.29513 0.31163 0.00570  -0.00121 0.06554  195 THR A CA  
1386 C C   . THR A 188 ? 0.36477 0.32770 0.32202 0.00203  0.00841  0.06597  195 THR A C   
1387 O O   . THR A 188 ? 0.35869 0.32486 0.32912 -0.00456 0.01683  0.06800  195 THR A O   
1388 C CB  . THR A 188 ? 0.36237 0.29283 0.33424 0.00337  0.00109  0.07944  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.43758 0.36640 0.39131 0.00672  0.00312  0.09581  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.40313 0.31559 0.38245 0.01078  -0.00577 0.07651  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.34155 0.31103 0.27427 0.00670  0.00721  0.06431  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.32889 0.30487 0.24579 0.00770  0.01871  0.06197  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.32118 0.30212 0.25272 0.00646  0.02240  0.04832  196 GLU A C   
1394 O O   . GLU A 189 ? 0.32098 0.30954 0.25139 0.00898  0.03538  0.04937  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.35011 0.32394 0.22946 0.01310  0.01416  0.05829  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.35696 0.32887 0.23182 0.01139  0.00004  0.04208  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.42747 0.39537 0.26450 0.01248  -0.01056 0.03970  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.46291 0.43687 0.29790 0.01286  -0.02254 0.04955  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.45580 0.41278 0.26275 0.01379  -0.00754 0.02812  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.29535 0.27418 0.24097 0.00443  0.01242  0.03755  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.25560 0.23734 0.21298 0.00392  0.01472  0.02626  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.29494 0.28344 0.27956 -0.00054 0.01941  0.03031  197 TYR A C   
1403 O O   . TYR A 190 ? 0.27509 0.26795 0.27158 -0.00054 0.01967  0.02294  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.27357 0.25214 0.23308 0.00254  0.00302  0.01559  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.27375 0.24784 0.20716 0.00265  -0.00468 0.01194  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.30812 0.27178 0.21459 0.00487  -0.00040 0.00418  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.30726 0.28664 0.24043 0.00137  -0.01680 0.01681  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.35222 0.30652 0.22829 0.00245  -0.01027 -0.00104 197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.32473 0.30326 0.23388 -0.00135 -0.02757 0.01430  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.32778 0.29152 0.20615 -0.00248 -0.02537 0.00426  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.37407 0.33138 0.22214 -0.00763 -0.03877 -0.00046 197 TYR A OH  
1412 N N   . LEU A 191 ? 0.26481 0.25283 0.25814 -0.00566 0.02160  0.04273  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.26062 0.25608 0.27802 -0.01424 0.02461  0.04869  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.29118 0.30536 0.31312 -0.01529 0.03838  0.06209  198 LEU A C   
1415 O O   . LEU A 191 ? 0.29477 0.32368 0.34165 -0.02431 0.04059  0.06961  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.29620 0.27356 0.32080 -0.02244 0.01705  0.05431  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.28587 0.24641 0.30765 -0.01825 0.00651  0.04302  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.37998 0.31466 0.40251 -0.02265 0.00140  0.04829  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.32149 0.28942 0.35327 -0.01873 0.00341  0.03049  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.26168 0.27763 0.25973 -0.00659 0.04746  0.06633  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.28518 0.32091 0.28418 -0.00431 0.06434  0.08122  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.32418 0.37681 0.32467 0.00737  0.07537  0.07501  199 GLU A C   
1423 O O   . GLU A 192 ? 0.29078 0.32947 0.26877 0.01769  0.07311  0.05936  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.35357 0.38093 0.31889 0.00224  0.07031  0.08901  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.41707 0.42689 0.37973 -0.00577 0.06037  0.09841  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.85306 0.85883 0.78284 0.00074  0.06682  0.11075  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 0.98277 0.97172 0.89567 0.00258  0.05498  0.11097  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.92837 0.95016 0.84866 0.00558  0.08428  0.12159  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.28602 0.28146 0.32030 -0.01861 -0.00266 0.05335  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.27363 0.29229 0.31354 -0.02196 0.00316  0.04439  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.23101 0.27359 0.25990 -0.01757 0.00987  0.04479  200 GLU A C   
1432 O O   . GLU A 193 ? 0.25678 0.30893 0.28273 -0.01260 0.01168  0.03244  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.29671 0.32057 0.35002 -0.03601 0.00497  0.05108  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.40245 0.45199 0.46357 -0.03630 0.01047  0.04262  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.64187 0.70782 0.72003 -0.05038 0.01255  0.05194  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.58144 0.63804 0.66483 -0.06314 0.01021  0.06659  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.51963 0.60870 0.60692 -0.04901 0.01603  0.04588  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.27689 0.32670 0.29687 -0.01921 0.01294  0.05882  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.26718 0.33880 0.27218 -0.01442 0.01865  0.05687  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.25947 0.32934 0.25371 -0.00628 0.01278  0.04617  201 ARG A C   
1441 O O   . ARG A 194 ? 0.26220 0.34245 0.24535 -0.00329 0.01468  0.03595  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.35033 0.43345 0.34496 -0.01714 0.02348  0.07513  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.42988 0.49546 0.42112 -0.01712 0.01701  0.09011  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.44585 0.52636 0.42375 -0.01956 0.02289  0.11001  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.55166 0.61898 0.51893 -0.01439 0.01593  0.12364  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.46253 0.53613 0.41767 -0.01635 0.01907  0.14561  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.54571 0.64190 0.49818 -0.02408 0.03024  0.15681  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.65174 0.71165 0.59707 -0.00899 0.01136  0.15807  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.24138 0.29845 0.23877 -0.00254 0.00520  0.04843  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.24619 0.30955 0.23839 0.00338  -0.00075 0.04067  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.23968 0.30218 0.23928 0.00285  -0.00092 0.02537  202 ARG A C   
1452 O O   . ARG A 195 ? 0.22732 0.29830 0.21993 0.00189  -0.00275 0.01696  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.25200 0.30792 0.24751 0.01085  -0.00760 0.04910  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.24754 0.31943 0.24239 0.01667  -0.01421 0.04447  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.27375 0.36467 0.25279 0.01478  -0.01735 0.04739  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.26812 0.37819 0.24974 0.01862  -0.02618 0.04646  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.25515 0.38099 0.23274 0.01152  -0.03100 0.03658  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.26973 0.38912 0.23626 0.00308  -0.02783 0.02534  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.24901 0.39745 0.23396 0.01308  -0.03985 0.03829  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.21267 0.26329 0.22467 0.00251  0.00005  0.02202  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.20881 0.25927 0.22625 0.00269  0.00043  0.00998  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.20485 0.26079 0.21600 -0.00040 0.00524  0.00344  203 ILE A C   
1463 O O   . ILE A 196 ? 0.22593 0.28247 0.23245 -0.00065 0.00410  -0.00469 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.21036 0.24790 0.23850 0.00384  -0.00034 0.00743  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.23960 0.26642 0.26962 0.01126  -0.00529 0.01108  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.23731 0.27720 0.26857 0.00470  0.00065  -0.00289 203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.26113 0.26709 0.29589 0.01150  -0.00784 0.00848  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.22162 0.28159 0.23228 -0.00234 0.01079  0.00781  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.21077 0.27778 0.21400 -0.00038 0.01660  0.00154  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.21405 0.28174 0.19773 0.00173  0.01500  -0.00435 204 LYS A C   
1471 O O   . LYS A 197 ? 0.25752 0.31843 0.23253 0.00424  0.01524  -0.01506 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.24728 0.32809 0.25384 -0.00169 0.02405  0.01024  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.33302 0.41695 0.35892 -0.00574 0.02512  0.01275  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.46023 0.56742 0.49128 -0.00782 0.03366  0.02217  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.54458 0.65465 0.59618 -0.01986 0.03134  0.03275  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.60800 0.74714 0.66803 -0.02540 0.04003  0.04653  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.22362 0.29720 0.19829 0.00073  0.01215  0.00260  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.23789 0.31351 0.19184 0.00126  0.00801  -0.00381 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.23796 0.30508 0.19360 -0.00309 -0.00023 -0.01317 205 GLU A C   
1480 O O   . GLU A 198 ? 0.24991 0.30839 0.19040 -0.00473 -0.00317 -0.02437 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.24762 0.33429 0.19369 0.00124  0.00463  0.00774  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.26583 0.35782 0.19004 0.00049  -0.00306 0.00129  205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.31218 0.41787 0.23073 0.00181  -0.00816 0.01484  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.30662 0.41271 0.24237 0.00255  -0.01142 0.02490  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.32581 0.44114 0.22073 0.00404  -0.00917 0.01522  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.20113 0.26996 0.17425 -0.00497 -0.00397 -0.00838 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.22499 0.29367 0.20320 -0.01040 -0.01056 -0.01341 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.22580 0.27924 0.20434 -0.01214 -0.00771 -0.02212 206 ILE A C   
1489 O O   . ILE A 199 ? 0.25870 0.30432 0.23034 -0.01913 -0.01278 -0.02859 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.22588 0.30512 0.22201 -0.00774 -0.01290 -0.00529 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.25166 0.34386 0.24533 -0.00387 -0.01719 0.00434  206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.21865 0.30531 0.22382 -0.01342 -0.01716 -0.00780 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.25041 0.34606 0.25852 0.00481  -0.01752 0.01251  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.22113 0.26942 0.20774 -0.00670 -0.00085 -0.02143 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.20903 0.24417 0.19535 -0.00564 0.00164  -0.02778 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.26098 0.28233 0.22743 -0.00359 0.00242  -0.03674 207 VAL A C   
1497 O O   . VAL A 200 ? 0.27836 0.28176 0.23709 -0.00635 -0.00061 -0.04299 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.21141 0.24893 0.21023 0.00015  0.00712  -0.02500 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.27022 0.29689 0.26674 0.00428  0.00963  -0.03031 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.22491 0.26808 0.23767 -0.00044 0.00477  -0.02013 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.25142 0.27927 0.20715 0.00196  0.00655  -0.03715 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.27963 0.29456 0.21213 0.00831  0.00828  -0.04768 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.29439 0.29447 0.20822 -0.00010 -0.00201 -0.05618 208 LYS A C   
1504 O O   . LYS A 201 ? 0.39430 0.36878 0.28957 0.00161  -0.00477 -0.06781 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.30260 0.33529 0.22753 0.01684  0.01644  -0.04427 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.40236 0.42590 0.30020 0.02853  0.02044  -0.05602 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.48617 0.53596 0.37725 0.03627  0.02988  -0.04930 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.57383 0.61748 0.43388 0.05188  0.03513  -0.06240 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.71872 0.79627 0.57728 0.06204  0.04856  -0.05294 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.30229 0.31715 0.22047 -0.00921 -0.00899 -0.05048 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.32129 0.32903 0.22393 -0.01983 -0.02105 -0.05770 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.31748 0.30990 0.22838 -0.03262 -0.02842 -0.05987 209 LYS A C   
1513 O O   . LYS A 202 ? 0.36117 0.33022 0.25389 -0.04107 -0.03720 -0.07050 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.32988 0.36485 0.23830 -0.02421 -0.02668 -0.04832 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.37749 0.41428 0.27344 -0.03695 -0.04147 -0.05418 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.44826 0.51642 0.34995 -0.03698 -0.04657 -0.04298 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.55421 0.63106 0.44513 -0.05051 -0.06330 -0.04836 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.62100 0.73155 0.51685 -0.04754 -0.06888 -0.03604 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.28611 0.29020 0.22251 -0.03480 -0.02533 -0.04968 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.32384 0.32514 0.27148 -0.04875 -0.03165 -0.04663 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.32121 0.30510 0.27522 -0.04610 -0.02574 -0.04494 210 HIS A C   
1522 O O   . HIS A 203 ? 0.36698 0.34234 0.32509 -0.05890 -0.03064 -0.04204 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.32582 0.36249 0.29688 -0.05316 -0.03380 -0.03453 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.31529 0.37278 0.28239 -0.05691 -0.04213 -0.03341 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.37255 0.42893 0.32934 -0.07234 -0.05508 -0.03882 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.37382 0.45308 0.34501 -0.04747 -0.04063 -0.02665 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.41222 0.49336 0.36720 -0.07117 -0.06123 -0.03562 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.37028 0.46454 0.33356 -0.05530 -0.05206 -0.02734 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.28636 0.26737 0.24207 -0.03114 -0.01606 -0.04496 211 SER A N   
1530 C CA  . SER A 204 ? 0.28523 0.25685 0.24866 -0.02692 -0.01117 -0.04135 211 SER A CA  
1531 C C   . SER A 204 ? 0.30561 0.25587 0.25565 -0.01310 -0.00589 -0.04833 211 SER A C   
1532 O O   . SER A 204 ? 0.32869 0.27994 0.28684 -0.00459 -0.00069 -0.04458 211 SER A O   
1533 C CB  . SER A 204 ? 0.27600 0.27333 0.26023 -0.02199 -0.00611 -0.03253 211 SER A CB  
1534 O OG  . SER A 204 ? 0.31040 0.32958 0.30654 -0.03028 -0.00998 -0.02608 211 SER A OG  
1535 N N   . GLN A 205 ? 0.35084 0.28364 0.27930 -0.00920 -0.00754 -0.05877 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.41737 0.33701 0.33319 0.00869  -0.00082 -0.06550 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.44125 0.32962 0.35036 0.01378  -0.00146 -0.06661 212 GLN A C   
1538 O O   . GLN A 205 ? 0.56807 0.45359 0.47423 0.03177  0.00513  -0.06844 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.52353 0.43333 0.41368 0.01431  -0.00183 -0.07753 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.59750 0.47199 0.46507 0.00266  -0.01352 -0.08773 212 GLN A CG  
1541 C CD  . GLN A 205 ? 0.73211 0.62338 0.60087 -0.01472 -0.02262 -0.08672 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.50549 0.41214 0.39475 -0.03020 -0.02743 -0.07668 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.72100 0.61274 0.56695 -0.01052 -0.02490 -0.09665 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.38159 0.24897 0.28939 -0.00143 -0.00915 -0.06350 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.42260 0.25444 0.32118 0.00196  -0.01065 -0.06205 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.46465 0.31035 0.38314 -0.00338 -0.00874 -0.04701 213 PHE A C   
1547 O O   . PHE A 206 ? 0.58462 0.40151 0.49612 -0.00561 -0.01127 -0.04162 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.58462 0.37162 0.46050 -0.01182 -0.02163 -0.06954 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.61013 0.37534 0.45808 -0.00248 -0.02416 -0.08747 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.64562 0.38941 0.47473 0.02333  -0.01803 -0.09681 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.63516 0.40373 0.47421 -0.01776 -0.03287 -0.09506 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 0.73064 0.45624 0.53054 0.03511  -0.01903 -0.11434 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.67874 0.42780 0.48743 -0.00786 -0.03546 -0.11272 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.69985 0.42670 0.48780 0.01918  -0.02787 -0.12286 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.33297 0.21943 0.27324 -0.00468 -0.00459 -0.04003 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.29902 0.20071 0.25400 -0.00622 -0.00218 -0.02790 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.34885 0.24425 0.30126 0.01213  0.00214  -0.02652 214 ILE A C   
1558 O O   . ILE A 207 ? 0.35149 0.25940 0.30611 0.02633  0.00615  -0.03211 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.28207 0.22370 0.25627 -0.00898 0.00028  -0.02419 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.26754 0.22007 0.24647 -0.02550 -0.00454 -0.02250 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.28308 0.24094 0.26766 -0.00542 0.00342  -0.01502 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.31195 0.25893 0.29301 -0.04135 -0.00816 -0.01281 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.31061 0.19018 0.25933 0.01157  0.00119  -0.01716 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.35550 0.22486 0.29857 0.03005  0.00341  -0.01461 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.31019 0.21451 0.26776 0.03890  0.00646  -0.00905 215 GLY A C   
1566 O O   . GLY A 208 ? 0.32860 0.22813 0.28236 0.04913  0.00636  -0.00148 215 GLY A O   
1567 N N   . TYR A 209 ? 0.29021 0.22711 0.26238 0.03523  0.00792  -0.01279 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.26410 0.23090 0.24816 0.04161  0.00854  -0.01092 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.25679 0.24454 0.25226 0.04266  0.00964  -0.01892 216 TYR A C   
1570 O O   . TYR A 209 ? 0.28570 0.27085 0.28096 0.03523  0.01043  -0.02323 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.24571 0.22691 0.23390 0.03237  0.00825  -0.00476 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.26147 0.22733 0.23972 0.02919  0.00834  0.00697  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.26978 0.23632 0.24193 0.04008  0.00786  0.01432  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.26266 0.21432 0.23777 0.01395  0.00808  0.01238  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.27607 0.22722 0.23776 0.03673  0.00838  0.02815  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.27834 0.21548 0.24552 0.00778  0.00815  0.02608  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.29025 0.22587 0.24992 0.01963  0.00894  0.03468  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.34113 0.26106 0.29149 0.01333  0.00943  0.05131  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.23121 0.24048 0.23651 0.05042  0.00886  -0.01964 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.22847 0.25756 0.24625 0.04807  0.00963  -0.02426 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.25191 0.28614 0.27469 0.03627  0.00808  -0.02556 217 PRO A C   
1582 O O   . PRO A 210 ? 0.24585 0.28367 0.26874 0.03427  0.00533  -0.02452 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.23640 0.28849 0.26514 0.05548  0.00664  -0.02306 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.30256 0.34916 0.32332 0.06142  0.00345  -0.01863 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.26897 0.28634 0.27429 0.06051  0.00621  -0.01500 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.22168 0.25636 0.24637 0.03085  0.01011  -0.02761 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.19560 0.23398 0.22477 0.02249  0.00855  -0.02778 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.19784 0.24951 0.23821 0.02026  0.00801  -0.02760 218 ILE A C   
1589 O O   . ILE A 211 ? 0.25592 0.31374 0.29770 0.02073  0.01189  -0.02636 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.21558 0.24508 0.23751 0.01705  0.00985  -0.02778 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.21217 0.22891 0.22541 0.01453  0.00901  -0.02632 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.21825 0.25392 0.24546 0.01189  0.00800  -0.02632 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.24332 0.25030 0.24815 0.00736  0.00786  -0.02782 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.19764 0.25346 0.24472 0.01745  0.00305  -0.02862 219 THR A N   
1595 C CA  . THR A 212 ? 0.17685 0.24207 0.23580 0.01114  0.00031  -0.02725 219 THR A CA  
1596 C C   . THR A 212 ? 0.16932 0.22278 0.22732 0.00509  -0.00195 -0.02644 219 THR A C   
1597 O O   . THR A 212 ? 0.17987 0.22277 0.23227 0.00755  -0.00567 -0.03041 219 THR A O   
1598 C CB  . THR A 212 ? 0.18932 0.26306 0.25473 0.01090  -0.00679 -0.03028 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.20585 0.29183 0.27177 0.01949  -0.00509 -0.02935 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.18577 0.26931 0.26594 -0.00048 -0.01137 -0.02768 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.19114 0.24737 0.25314 -0.00063 0.00083  -0.02050 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.18901 0.23243 0.25012 -0.00558 -0.00185 -0.01696 220 LEU A CA  
1603 C C   . LEU A 213 ? 0.20326 0.24307 0.27455 -0.01537 -0.00835 -0.01520 220 LEU A C   
1604 O O   . LEU A 213 ? 0.21069 0.26595 0.29327 -0.02374 -0.00652 -0.00819 220 LEU A O   
1605 C CB  . LEU A 213 ? 0.22274 0.27076 0.28021 -0.00714 0.00390  -0.00941 220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.24469 0.28046 0.30053 -0.01117 0.00141  -0.00207 220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.21520 0.23442 0.26509 -0.00427 -0.00363 -0.00670 220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.25525 0.30013 0.30374 -0.01095 0.00706  0.00535  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.18677 0.20692 0.25354 -0.01451 -0.01618 -0.02163 221 PHE A N   
1610 C CA  . PHE A 214 ? 0.20506 0.21269 0.27808 -0.02582 -0.02548 -0.02213 221 PHE A CA  
1611 C C   . PHE A 214 ? 0.23804 0.23216 0.31363 -0.03495 -0.02537 -0.01069 221 PHE A C   
1612 O O   . PHE A 214 ? 0.24844 0.23520 0.31591 -0.02796 -0.02083 -0.00599 221 PHE A O   
1613 C CB  . PHE A 214 ? 0.21961 0.20271 0.28028 -0.01912 -0.03432 -0.03469 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.21036 0.20554 0.26713 -0.01279 -0.03714 -0.04490 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.18870 0.20851 0.24779 -0.00659 -0.02965 -0.04270 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.23401 0.21212 0.28134 -0.01199 -0.04819 -0.05694 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.19483 0.22432 0.24854 0.00010  -0.03250 -0.04945 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.23174 0.22271 0.27240 -0.00516 -0.05125 -0.06542 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.20979 0.22767 0.25450 0.00080  -0.04309 -0.06022 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.24616 0.23867 0.33359 -0.05170 -0.03115 -0.00462 222 VAL A N   
1621 C CA  . VAL A 215 ? 0.26919 0.24449 0.35872 -0.06313 -0.03237 0.00887  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.29647 0.22885 0.37936 -0.06934 -0.04629 0.00267  222 VAL A C   
1623 O O   . VAL A 215 ? 0.31768 0.23997 0.39624 -0.06757 -0.05529 -0.01237 222 VAL A O   
1624 C CB  . VAL A 215 ? 0.41480 0.42084 0.52294 -0.07977 -0.02712 0.02483  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.46590 0.50557 0.57278 -0.06883 -0.01273 0.02970  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.33394 0.35938 0.45893 -0.09202 -0.03409 0.02077  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.34642 0.25029 0.42537 -0.07548 -0.04867 0.01415  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.39439 0.24677 0.46246 -0.07907 -0.06232 0.00845  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.46153 0.30137 0.54324 -0.10794 -0.07053 0.02191  223 GLU A C   
1630 O O   . GLU A 216 ? 0.50298 0.37280 0.60058 -0.12187 -0.06251 0.04124  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.44543 0.26692 0.49594 -0.06097 -0.06042 0.01177  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.45408 0.29215 0.49438 -0.03514 -0.05315 0.00035  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.55458 0.37031 0.58099 -0.01627 -0.05196 0.00471  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.51617 0.28972 0.52842 -0.00598 -0.06067 -0.00378 223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.51919 0.36009 0.54761 -0.01020 -0.04303 0.01568  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.48159 0.27727 0.55593 -0.11723 -0.08691 0.01139  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.63335 0.40605 0.71898 -0.14819 -0.09844 0.02374  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.79239 0.55370 0.87999 -0.15561 -0.09154 0.05021  224 LYS A C   
1639 O O   . LYS A 217 ? 0.72472 0.45953 0.79403 -0.13525 -0.08745 0.05247  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.65661 0.36899 0.72230 -0.14919 -0.11621 0.00572  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.83104 0.53135 0.90503 -0.17650 -0.12273 0.01606  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.91259 0.57483 0.96981 -0.17825 -0.13815 -0.00647 224 LYS A CD  
1643 C CE  . LYS A 217 ? 1.06975 0.66468 1.09674 -0.16009 -0.14250 -0.01374 224 LYS A CE  
1644 N NZ  . LYS A 217 ? 1.08834 0.67060 1.09199 -0.12501 -0.14009 -0.03338 224 LYS A NZ  
# 
