data_7HBN
# 
_entry.id   7HBN 
# 
_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   7HBN         pdb_00007hbn 10.2210/pdb7hbn/pdb 
WWPDB D_1001407269 ?            ?                   
# 
_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                        7HBN 
_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 '{2-[(oxan-4-yl)oxy]phenyl}methanol' 208.254   1   ?        ? ? ? 
3 water       nat water                                18.015    266 ?        ? ? ? 
# 
_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 '{2-[(oxan-4-yl)oxy]phenyl}methanol' A1ABL 
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 
A1ABL non-polymer         . '{2-[(oxan-4-yl)oxy]phenyl}methanol' ? 'C12 H16 O3'     208.254 
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        A1ABL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ABL 
_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 A1ABL 1   301 301 A1ABL C6Y A . 
C 3 HOH   1   401 219 HOH   HOH A . 
C 3 HOH   2   402 200 HOH   HOH A . 
C 3 HOH   3   403 254 HOH   HOH A . 
C 3 HOH   4   404 56  HOH   HOH A . 
C 3 HOH   5   405 162 HOH   HOH A . 
C 3 HOH   6   406 241 HOH   HOH A . 
C 3 HOH   7   407 244 HOH   HOH A . 
C 3 HOH   8   408 223 HOH   HOH A . 
C 3 HOH   9   409 75  HOH   HOH A . 
C 3 HOH   10  410 257 HOH   HOH A . 
C 3 HOH   11  411 70  HOH   HOH A . 
C 3 HOH   12  412 24  HOH   HOH A . 
C 3 HOH   13  413 131 HOH   HOH A . 
C 3 HOH   14  414 148 HOH   HOH A . 
C 3 HOH   15  415 90  HOH   HOH A . 
C 3 HOH   16  416 41  HOH   HOH A . 
C 3 HOH   17  417 21  HOH   HOH A . 
C 3 HOH   18  418 35  HOH   HOH A . 
C 3 HOH   19  419 96  HOH   HOH A . 
C 3 HOH   20  420 8   HOH   HOH A . 
C 3 HOH   21  421 25  HOH   HOH A . 
C 3 HOH   22  422 84  HOH   HOH A . 
C 3 HOH   23  423 183 HOH   HOH A . 
C 3 HOH   24  424 140 HOH   HOH A . 
C 3 HOH   25  425 154 HOH   HOH A . 
C 3 HOH   26  426 128 HOH   HOH A . 
C 3 HOH   27  427 72  HOH   HOH A . 
C 3 HOH   28  428 54  HOH   HOH A . 
C 3 HOH   29  429 43  HOH   HOH A . 
C 3 HOH   30  430 209 HOH   HOH A . 
C 3 HOH   31  431 246 HOH   HOH A . 
C 3 HOH   32  432 17  HOH   HOH A . 
C 3 HOH   33  433 85  HOH   HOH A . 
C 3 HOH   34  434 76  HOH   HOH A . 
C 3 HOH   35  435 36  HOH   HOH A . 
C 3 HOH   36  436 4   HOH   HOH A . 
C 3 HOH   37  437 42  HOH   HOH A . 
C 3 HOH   38  438 60  HOH   HOH A . 
C 3 HOH   39  439 100 HOH   HOH A . 
C 3 HOH   40  440 29  HOH   HOH A . 
C 3 HOH   41  441 93  HOH   HOH A . 
C 3 HOH   42  442 38  HOH   HOH A . 
C 3 HOH   43  443 184 HOH   HOH A . 
C 3 HOH   44  444 258 HOH   HOH A . 
C 3 HOH   45  445 13  HOH   HOH A . 
C 3 HOH   46  446 6   HOH   HOH A . 
C 3 HOH   47  447 12  HOH   HOH A . 
C 3 HOH   48  448 27  HOH   HOH A . 
C 3 HOH   49  449 112 HOH   HOH A . 
C 3 HOH   50  450 7   HOH   HOH A . 
C 3 HOH   51  451 22  HOH   HOH A . 
C 3 HOH   52  452 201 HOH   HOH A . 
C 3 HOH   53  453 59  HOH   HOH A . 
C 3 HOH   54  454 23  HOH   HOH A . 
C 3 HOH   55  455 45  HOH   HOH A . 
C 3 HOH   56  456 87  HOH   HOH A . 
C 3 HOH   57  457 152 HOH   HOH A . 
C 3 HOH   58  458 191 HOH   HOH A . 
C 3 HOH   59  459 32  HOH   HOH A . 
C 3 HOH   60  460 228 HOH   HOH A . 
C 3 HOH   61  461 5   HOH   HOH A . 
C 3 HOH   62  462 179 HOH   HOH A . 
C 3 HOH   63  463 40  HOH   HOH A . 
C 3 HOH   64  464 18  HOH   HOH A . 
C 3 HOH   65  465 97  HOH   HOH A . 
C 3 HOH   66  466 66  HOH   HOH A . 
C 3 HOH   67  467 33  HOH   HOH A . 
C 3 HOH   68  468 11  HOH   HOH A . 
C 3 HOH   69  469 119 HOH   HOH A . 
C 3 HOH   70  470 31  HOH   HOH A . 
C 3 HOH   71  471 53  HOH   HOH A . 
C 3 HOH   72  472 46  HOH   HOH A . 
C 3 HOH   73  473 63  HOH   HOH A . 
C 3 HOH   74  474 15  HOH   HOH A . 
C 3 HOH   75  475 101 HOH   HOH A . 
C 3 HOH   76  476 126 HOH   HOH A . 
C 3 HOH   77  477 34  HOH   HOH A . 
C 3 HOH   78  478 130 HOH   HOH A . 
C 3 HOH   79  479 117 HOH   HOH A . 
C 3 HOH   80  480 49  HOH   HOH A . 
C 3 HOH   81  481 79  HOH   HOH A . 
C 3 HOH   82  482 67  HOH   HOH A . 
C 3 HOH   83  483 165 HOH   HOH A . 
C 3 HOH   84  484 10  HOH   HOH A . 
C 3 HOH   85  485 175 HOH   HOH A . 
C 3 HOH   86  486 9   HOH   HOH A . 
C 3 HOH   87  487 28  HOH   HOH A . 
C 3 HOH   88  488 19  HOH   HOH A . 
C 3 HOH   89  489 68  HOH   HOH A . 
C 3 HOH   90  490 37  HOH   HOH A . 
C 3 HOH   91  491 30  HOH   HOH A . 
C 3 HOH   92  492 107 HOH   HOH A . 
C 3 HOH   93  493 14  HOH   HOH A . 
C 3 HOH   94  494 61  HOH   HOH A . 
C 3 HOH   95  495 225 HOH   HOH A . 
C 3 HOH   96  496 197 HOH   HOH A . 
C 3 HOH   97  497 65  HOH   HOH A . 
C 3 HOH   98  498 173 HOH   HOH A . 
C 3 HOH   99  499 16  HOH   HOH A . 
C 3 HOH   100 500 83  HOH   HOH A . 
C 3 HOH   101 501 104 HOH   HOH A . 
C 3 HOH   102 502 115 HOH   HOH A . 
C 3 HOH   103 503 120 HOH   HOH A . 
C 3 HOH   104 504 108 HOH   HOH A . 
C 3 HOH   105 505 133 HOH   HOH A . 
C 3 HOH   106 506 122 HOH   HOH A . 
C 3 HOH   107 507 64  HOH   HOH A . 
C 3 HOH   108 508 169 HOH   HOH A . 
C 3 HOH   109 509 151 HOH   HOH A . 
C 3 HOH   110 510 50  HOH   HOH A . 
C 3 HOH   111 511 149 HOH   HOH A . 
C 3 HOH   112 512 187 HOH   HOH A . 
C 3 HOH   113 513 167 HOH   HOH A . 
C 3 HOH   114 514 263 HOH   HOH A . 
C 3 HOH   115 515 71  HOH   HOH A . 
C 3 HOH   116 516 116 HOH   HOH A . 
C 3 HOH   117 517 127 HOH   HOH A . 
C 3 HOH   118 518 2   HOH   HOH A . 
C 3 HOH   119 519 132 HOH   HOH A . 
C 3 HOH   120 520 52  HOH   HOH A . 
C 3 HOH   121 521 39  HOH   HOH A . 
C 3 HOH   122 522 103 HOH   HOH A . 
C 3 HOH   123 523 213 HOH   HOH A . 
C 3 HOH   124 524 121 HOH   HOH A . 
C 3 HOH   125 525 48  HOH   HOH A . 
C 3 HOH   126 526 110 HOH   HOH A . 
C 3 HOH   127 527 129 HOH   HOH A . 
C 3 HOH   128 528 91  HOH   HOH A . 
C 3 HOH   129 529 62  HOH   HOH A . 
C 3 HOH   130 530 199 HOH   HOH A . 
C 3 HOH   131 531 80  HOH   HOH A . 
C 3 HOH   132 532 248 HOH   HOH A . 
C 3 HOH   133 533 134 HOH   HOH A . 
C 3 HOH   134 534 95  HOH   HOH A . 
C 3 HOH   135 535 58  HOH   HOH A . 
C 3 HOH   136 536 26  HOH   HOH A . 
C 3 HOH   137 537 123 HOH   HOH A . 
C 3 HOH   138 538 1   HOH   HOH A . 
C 3 HOH   139 539 111 HOH   HOH A . 
C 3 HOH   140 540 216 HOH   HOH A . 
C 3 HOH   141 541 82  HOH   HOH A . 
C 3 HOH   142 542 156 HOH   HOH A . 
C 3 HOH   143 543 143 HOH   HOH A . 
C 3 HOH   144 544 226 HOH   HOH A . 
C 3 HOH   145 545 203 HOH   HOH A . 
C 3 HOH   146 546 242 HOH   HOH A . 
C 3 HOH   147 547 217 HOH   HOH A . 
C 3 HOH   148 548 73  HOH   HOH A . 
C 3 HOH   149 549 3   HOH   HOH A . 
C 3 HOH   150 550 196 HOH   HOH A . 
C 3 HOH   151 551 157 HOH   HOH A . 
C 3 HOH   152 552 137 HOH   HOH A . 
C 3 HOH   153 553 142 HOH   HOH A . 
C 3 HOH   154 554 77  HOH   HOH A . 
C 3 HOH   155 555 166 HOH   HOH A . 
C 3 HOH   156 556 20  HOH   HOH A . 
C 3 HOH   157 557 194 HOH   HOH A . 
C 3 HOH   158 558 188 HOH   HOH A . 
C 3 HOH   159 559 214 HOH   HOH A . 
C 3 HOH   160 560 147 HOH   HOH A . 
C 3 HOH   161 561 105 HOH   HOH A . 
C 3 HOH   162 562 92  HOH   HOH A . 
C 3 HOH   163 563 125 HOH   HOH A . 
C 3 HOH   164 564 163 HOH   HOH A . 
C 3 HOH   165 565 233 HOH   HOH A . 
C 3 HOH   166 566 57  HOH   HOH A . 
C 3 HOH   167 567 158 HOH   HOH A . 
C 3 HOH   168 568 136 HOH   HOH A . 
C 3 HOH   169 569 98  HOH   HOH A . 
C 3 HOH   170 570 259 HOH   HOH A . 
C 3 HOH   171 571 44  HOH   HOH A . 
C 3 HOH   172 572 51  HOH   HOH A . 
C 3 HOH   173 573 256 HOH   HOH A . 
C 3 HOH   174 574 247 HOH   HOH A . 
C 3 HOH   175 575 229 HOH   HOH A . 
C 3 HOH   176 576 205 HOH   HOH A . 
C 3 HOH   177 577 189 HOH   HOH A . 
C 3 HOH   178 578 227 HOH   HOH A . 
C 3 HOH   179 579 124 HOH   HOH A . 
C 3 HOH   180 580 177 HOH   HOH A . 
C 3 HOH   181 581 171 HOH   HOH A . 
C 3 HOH   182 582 89  HOH   HOH A . 
C 3 HOH   183 583 113 HOH   HOH A . 
C 3 HOH   184 584 206 HOH   HOH A . 
C 3 HOH   185 585 239 HOH   HOH A . 
C 3 HOH   186 586 94  HOH   HOH A . 
C 3 HOH   187 587 232 HOH   HOH A . 
C 3 HOH   188 588 180 HOH   HOH A . 
C 3 HOH   189 589 218 HOH   HOH A . 
C 3 HOH   190 590 231 HOH   HOH A . 
C 3 HOH   191 591 168 HOH   HOH A . 
C 3 HOH   192 592 153 HOH   HOH A . 
C 3 HOH   193 593 114 HOH   HOH A . 
C 3 HOH   194 594 210 HOH   HOH A . 
C 3 HOH   195 595 139 HOH   HOH A . 
C 3 HOH   196 596 202 HOH   HOH A . 
C 3 HOH   197 597 78  HOH   HOH A . 
C 3 HOH   198 598 172 HOH   HOH A . 
C 3 HOH   199 599 207 HOH   HOH A . 
C 3 HOH   200 600 141 HOH   HOH A . 
C 3 HOH   201 601 69  HOH   HOH A . 
C 3 HOH   202 602 160 HOH   HOH A . 
C 3 HOH   203 603 212 HOH   HOH A . 
C 3 HOH   204 604 266 HOH   HOH A . 
C 3 HOH   205 605 170 HOH   HOH A . 
C 3 HOH   206 606 138 HOH   HOH A . 
C 3 HOH   207 607 150 HOH   HOH A . 
C 3 HOH   208 608 155 HOH   HOH A . 
C 3 HOH   209 609 264 HOH   HOH A . 
C 3 HOH   210 610 161 HOH   HOH A . 
C 3 HOH   211 611 164 HOH   HOH A . 
C 3 HOH   212 612 47  HOH   HOH A . 
C 3 HOH   213 613 86  HOH   HOH A . 
C 3 HOH   214 614 204 HOH   HOH A . 
C 3 HOH   215 615 145 HOH   HOH A . 
C 3 HOH   216 616 185 HOH   HOH A . 
C 3 HOH   217 617 159 HOH   HOH A . 
C 3 HOH   218 618 195 HOH   HOH A . 
C 3 HOH   219 619 220 HOH   HOH A . 
C 3 HOH   220 620 182 HOH   HOH A . 
C 3 HOH   221 621 208 HOH   HOH A . 
C 3 HOH   222 622 109 HOH   HOH A . 
C 3 HOH   223 623 99  HOH   HOH A . 
C 3 HOH   224 624 221 HOH   HOH A . 
C 3 HOH   225 625 240 HOH   HOH A . 
C 3 HOH   226 626 55  HOH   HOH A . 
C 3 HOH   227 627 190 HOH   HOH A . 
C 3 HOH   228 628 222 HOH   HOH A . 
C 3 HOH   229 629 192 HOH   HOH A . 
C 3 HOH   230 630 215 HOH   HOH A . 
C 3 HOH   231 631 102 HOH   HOH A . 
C 3 HOH   232 632 265 HOH   HOH A . 
C 3 HOH   233 633 174 HOH   HOH A . 
C 3 HOH   234 634 245 HOH   HOH A . 
C 3 HOH   235 635 176 HOH   HOH A . 
C 3 HOH   236 636 261 HOH   HOH A . 
C 3 HOH   237 637 146 HOH   HOH A . 
C 3 HOH   238 638 74  HOH   HOH A . 
C 3 HOH   239 639 198 HOH   HOH A . 
C 3 HOH   240 640 211 HOH   HOH A . 
C 3 HOH   241 641 224 HOH   HOH A . 
C 3 HOH   242 642 255 HOH   HOH A . 
C 3 HOH   243 643 238 HOH   HOH A . 
C 3 HOH   244 644 144 HOH   HOH A . 
C 3 HOH   245 645 243 HOH   HOH A . 
C 3 HOH   246 646 118 HOH   HOH A . 
C 3 HOH   247 647 186 HOH   HOH A . 
C 3 HOH   248 648 81  HOH   HOH A . 
C 3 HOH   249 649 106 HOH   HOH A . 
C 3 HOH   250 650 230 HOH   HOH A . 
C 3 HOH   251 651 88  HOH   HOH A . 
C 3 HOH   252 652 181 HOH   HOH A . 
C 3 HOH   253 653 260 HOH   HOH A . 
C 3 HOH   254 654 251 HOH   HOH A . 
C 3 HOH   255 655 178 HOH   HOH A . 
C 3 HOH   256 656 236 HOH   HOH A . 
C 3 HOH   257 657 235 HOH   HOH A . 
C 3 HOH   258 658 193 HOH   HOH A . 
C 3 HOH   259 659 252 HOH   HOH A . 
C 3 HOH   260 660 234 HOH   HOH A . 
C 3 HOH   261 661 262 HOH   HOH A . 
C 3 HOH   262 662 249 HOH   HOH A . 
C 3 HOH   263 663 135 HOH   HOH A . 
C 3 HOH   264 664 250 HOH   HOH A . 
C 3 HOH   265 665 237 HOH   HOH A . 
C 3 HOH   266 666 253 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             591809.463 
_cell.length_a           66.060 
_cell.length_b           89.390 
_cell.length_c           100.220 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HBN 
_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                         7HBN 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HBN 
# 
_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   2023-07-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HBN 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             66.710 
_reflns.d_resolution_high            1.990 
_reflns.number_obs                   20590 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.300 
_reflns.pdbx_Rmerge_I_obs            0.149 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.600 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              10.800 
_reflns.pdbx_Rrim_I_all              0.156 
_reflns.pdbx_Rpim_I_all              0.046 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     223194 
_reflns.pdbx_scaling_rejects         328 
_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 1.990 2.040  ? 9142 1486 ? 0.987 ? ? ? 6.200 ? 2.200  ? ? ? ? ? ? 99.200 1.078 0.419 0.621 
1 2 8.900 66.710 ? 2565 269  ? 0.043 ? ? ? 9.500 ? 33.800 ? ? ? ? ? ? 97.500 0.045 0.014 0.998 
# 
_refine.entry_id                                 7HBN 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.ls_percent_reflns_R_free                 4.75 
_refine.pdbx_overall_phase_error                 22.0290 
_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                          0.1849 
_refine.B_iso_mean                               33.41 
_refine.ls_number_reflns_R_free                  974 
_refine.ls_percent_reflns_obs                    98.91 
_refine.ls_R_factor_R_work                       0.1839 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.99 
_refine.ls_number_reflns_obs                     20520 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.ls_number_reflns_R_work                  19546 
_refine.ls_d_res_low                             66.71 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2051 
_refine.overall_SU_ML                            0.2446 
_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         15 
_refine_hist.number_atoms_solvent             266 
_refine_hist.number_atoms_total               1925 
_refine_hist.d_res_high                       1.99 
_refine_hist.d_res_low                        66.71 
# 
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           1686 0.0020 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2271 0.5537 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     260  0.0410 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      288  0.0045 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 231  7.6603 ? ? ? 
# 
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' 1.99 2.09  2773 0.2718 99.18 0.2867 126 . . . . . 
'X-RAY DIFFRACTION' 2.10 2.23  2779 0.2172 99.56 0.2617 136 . . . . . 
'X-RAY DIFFRACTION' 2.23 2.40  2640 0.2734 94.61 0.2850 117 . . . . . 
'X-RAY DIFFRACTION' 2.40 2.64  2786 0.2042 99.86 0.2402 144 . . . . . 
'X-RAY DIFFRACTION' 2.64 3.02  2808 0.1858 99.93 0.2067 145 . . . . . 
'X-RAY DIFFRACTION' 3.02 3.81  2812 0.1659 99.63 0.2006 153 . . . . . 
'X-RAY DIFFRACTION' 3.81 66.71 2948 0.1468 99.49 0.1576 153 . . . . . 
# 
_struct.entry_id                  7HBN 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13145' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HBN 
_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              7HBN 
_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 7HBN MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HBN LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HBN GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HBN HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HBN HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HBN HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HBN HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HBN HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HBN HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2 AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3 AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4 AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5 AA5 ILE A 103 ? ALA A 117 ? ILE A 110 ALA A 124 1 ? 15 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLN A 187 ? LEU A 191 ? GLN A 194 LEU A 198 5 ? 5  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 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 VAL A 85  ? O VAL A 92  N ASN A 72  ? N ASN A 79  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HBN 
_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 OE1 A GLU 200 ? ? O A HOH 401 ? ? 2.00 
2 1 O   A HOH 608 ? ? O A HOH 639 ? ? 2.08 
3 1 O   A HOH 545 ? ? O A HOH 621 ? ? 2.10 
4 1 NZ  A LYS 116 ? ? O A HOH 402 ? ? 2.14 
# 
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 629 ? ? 1_555 O A HOH 652 ? ? 8_444 2.08 
2 1 O A HOH 498 ? ? 1_555 O A HOH 618 ? ? 2_555 2.13 
3 1 O A HOH 495 ? ? 1_555 O A HOH 495 ? ? 2_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 TYR A 38  ? ? -160.10 109.68  
2 1 ALA A 166 ? ? 62.84   -141.46 
# 
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 12.3552559585  -17.8772077867 -18.7174559814 0.183962165671 0.224806745938 0.25605078687  
0.0103490199101   -0.0287415538934   -0.0341006272052 3.30143452174 1.92398369943 6.27209693906 -1.22539588046   -3.79383474587  
0.27946581425   0.126422049583  -0.386999378807 0.0310121112057 -0.0110661750588 0.0166061839244 -0.0708686525605 -0.100366490343 
0.618879470963   -0.130853462259  
2 ? 'X-RAY DIFFRACTION' refined -5.15815454712 -6.29810841854 -20.8721940015 0.182333685398 0.161100269049 0.225402508424 
-0.0143620656918  0.006483800322     -0.0344006985251 2.68154005164 5.26150941757 7.61309883501 -2.21736407308   3.34327415616   
-4.76998413023  -0.134254537864 0.0895003253238 0.25244701395   0.0459222540348  -0.144467462492 -0.0579723407051 -0.271920197922 
0.289432449996   0.223720663625   
3 ? 'X-RAY DIFFRACTION' refined -10.0557761904 -15.0069552581 -25.2067690127 0.162307862474 0.195585063583 0.252133475542 
-0.00322038121543 -0.0531863543758   -0.0370062673176 1.639413483   3.80650394784 5.09000029466 0.0826945780806  -0.402165847273 
-2.36514453794  0.0557426325074 0.111484731116  -0.113153737093 -0.200400677583  0.104497689079  0.341529645227   0.116150037453  
-0.239546074539  -0.222537401647  
4 ? 'X-RAY DIFFRACTION' refined 10.7019341576  -7.47845255122 -17.8416546836 0.164929930189 0.231125273232 0.307580919524 
-0.00822504813232 0.0230321907335    -0.0369317534705 3.43222469846 3.97632649834 9.00822843152 1.10729779486    -0.200126984655 
1.89164932538   0.124833848704  -0.498055280223 0.449082471038  0.0294590554784  -0.222471429096 -0.0949079589161 -0.525015360639 
0.337978310873   0.10048637343    
5 ? 'X-RAY DIFFRACTION' refined 0.973158278456 -19.2867506547 -27.8654084113 0.214994026252 0.153365820824 0.261938824376 
-0.0219277690451  -0.0193541389089   -0.0333422415546 3.30927509501 1.77965519244 2.82281719461 -1.52830794507   0.342114365344  
-0.479418513019 0.110774867958  0.2437627808    -0.327082354166 -0.226372225243  -0.040816310046 0.156408994929   0.263976305406  
0.0433050989821  -0.0925632654366 
6 ? 'X-RAY DIFFRACTION' refined -5.56870462352 -20.2137069295 -10.4009604315 0.174639270292 0.182466060062 0.201086006224 
-0.0230731165864  -0.0153755694701   0.0114843038578  3.55412549028 2.71610674688 4.83010618181 -0.994807295288  -0.134944764654 
-0.744406382072 -0.039685398658 -0.450163622416 -0.172828187841 0.197369547746   0.0973485202624 0.0886902155033  0.224109687395  
-0.038301892267  -0.0568965264314 
7 ? 'X-RAY DIFFRACTION' refined -13.9216244038 -13.4145182376 -14.6964882621 0.150099305783 0.209200515661 0.178519031127 
-0.0105572022925  -0.000738616587165 -0.0432064504219 5.31587587932 4.16910877463 4.69887192796 0.00681508814558 0.180242706605  
-1.55002214826  0.197701967754  -0.353230532083 0.044541949854  0.620533584792   -0.151514993836 -0.194030711273  -0.273436711525 
-0.0461038683532 0.00549841673814 
# 
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 210 A 195 . 
;chain 'A' and (resid 183 through 210 )
;
7 7 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       666 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.98 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
A1ABL C10  C N N 1   
A1ABL C15  C N N 2   
A1ABL C02  C N N 3   
A1ABL C03  C Y N 4   
A1ABL C04  C Y N 5   
A1ABL C05  C Y N 6   
A1ABL C06  C Y N 7   
A1ABL C07  C Y N 8   
A1ABL C08  C Y N 9   
A1ABL C11  C N N 10  
A1ABL C12  C N N 11  
A1ABL C14  C N N 12  
A1ABL O01  O N N 13  
A1ABL O09  O N N 14  
A1ABL O13  O N N 15  
A1ABL H101 H N N 16  
A1ABL H151 H N N 17  
A1ABL H152 H N N 18  
A1ABL H021 H N N 19  
A1ABL H022 H N N 20  
A1ABL H041 H N N 21  
A1ABL H051 H N N 22  
A1ABL H061 H N N 23  
A1ABL H071 H N N 24  
A1ABL H111 H N N 25  
A1ABL H112 H N N 26  
A1ABL H121 H N N 27  
A1ABL H122 H N N 28  
A1ABL H141 H N N 29  
A1ABL H142 H N N 30  
A1ABL H011 H N N 31  
ALA   N    N N N 32  
ALA   CA   C N S 33  
ALA   C    C N N 34  
ALA   O    O N N 35  
ALA   CB   C N N 36  
ALA   OXT  O N N 37  
ALA   H    H N N 38  
ALA   H2   H N N 39  
ALA   HA   H N N 40  
ALA   HB1  H N N 41  
ALA   HB2  H N N 42  
ALA   HB3  H N N 43  
ALA   HXT  H N N 44  
ARG   N    N N N 45  
ARG   CA   C N S 46  
ARG   C    C N N 47  
ARG   O    O N N 48  
ARG   CB   C N N 49  
ARG   CG   C N N 50  
ARG   CD   C N N 51  
ARG   NE   N N N 52  
ARG   CZ   C N N 53  
ARG   NH1  N N N 54  
ARG   NH2  N N N 55  
ARG   OXT  O N N 56  
ARG   H    H N N 57  
ARG   H2   H N N 58  
ARG   HA   H N N 59  
ARG   HB2  H N N 60  
ARG   HB3  H N N 61  
ARG   HG2  H N N 62  
ARG   HG3  H N N 63  
ARG   HD2  H N N 64  
ARG   HD3  H N N 65  
ARG   HE   H N N 66  
ARG   HH11 H N N 67  
ARG   HH12 H N N 68  
ARG   HH21 H N N 69  
ARG   HH22 H N N 70  
ARG   HXT  H N N 71  
ASN   N    N N N 72  
ASN   CA   C N S 73  
ASN   C    C N N 74  
ASN   O    O N N 75  
ASN   CB   C N N 76  
ASN   CG   C N N 77  
ASN   OD1  O N N 78  
ASN   ND2  N N N 79  
ASN   OXT  O N N 80  
ASN   H    H N N 81  
ASN   H2   H N N 82  
ASN   HA   H N N 83  
ASN   HB2  H N N 84  
ASN   HB3  H N N 85  
ASN   HD21 H N N 86  
ASN   HD22 H N N 87  
ASN   HXT  H N N 88  
ASP   N    N N N 89  
ASP   CA   C N S 90  
ASP   C    C N N 91  
ASP   O    O N N 92  
ASP   CB   C N N 93  
ASP   CG   C N N 94  
ASP   OD1  O N N 95  
ASP   OD2  O N N 96  
ASP   OXT  O N N 97  
ASP   H    H N N 98  
ASP   H2   H N N 99  
ASP   HA   H N N 100 
ASP   HB2  H N N 101 
ASP   HB3  H N N 102 
ASP   HD2  H N N 103 
ASP   HXT  H N N 104 
GLN   N    N N N 105 
GLN   CA   C N S 106 
GLN   C    C N N 107 
GLN   O    O N N 108 
GLN   CB   C N N 109 
GLN   CG   C N N 110 
GLN   CD   C N N 111 
GLN   OE1  O N N 112 
GLN   NE2  N N N 113 
GLN   OXT  O N N 114 
GLN   H    H N N 115 
GLN   H2   H N N 116 
GLN   HA   H N N 117 
GLN   HB2  H N N 118 
GLN   HB3  H N N 119 
GLN   HG2  H N N 120 
GLN   HG3  H N N 121 
GLN   HE21 H N N 122 
GLN   HE22 H N N 123 
GLN   HXT  H N N 124 
GLU   N    N N N 125 
GLU   CA   C N S 126 
GLU   C    C N N 127 
GLU   O    O N N 128 
GLU   CB   C N N 129 
GLU   CG   C N N 130 
GLU   CD   C N N 131 
GLU   OE1  O N N 132 
GLU   OE2  O N N 133 
GLU   OXT  O N N 134 
GLU   H    H N N 135 
GLU   H2   H N N 136 
GLU   HA   H N N 137 
GLU   HB2  H N N 138 
GLU   HB3  H N N 139 
GLU   HG2  H N N 140 
GLU   HG3  H N N 141 
GLU   HE2  H N N 142 
GLU   HXT  H N N 143 
GLY   N    N N N 144 
GLY   CA   C N N 145 
GLY   C    C N N 146 
GLY   O    O N N 147 
GLY   OXT  O N N 148 
GLY   H    H N N 149 
GLY   H2   H N N 150 
GLY   HA2  H N N 151 
GLY   HA3  H N N 152 
GLY   HXT  H N N 153 
HIS   N    N N N 154 
HIS   CA   C N S 155 
HIS   C    C N N 156 
HIS   O    O N N 157 
HIS   CB   C N N 158 
HIS   CG   C Y N 159 
HIS   ND1  N Y N 160 
HIS   CD2  C Y N 161 
HIS   CE1  C Y N 162 
HIS   NE2  N Y N 163 
HIS   OXT  O N N 164 
HIS   H    H N N 165 
HIS   H2   H N N 166 
HIS   HA   H N N 167 
HIS   HB2  H N N 168 
HIS   HB3  H N N 169 
HIS   HD1  H N N 170 
HIS   HD2  H N N 171 
HIS   HE1  H N N 172 
HIS   HE2  H N N 173 
HIS   HXT  H N N 174 
HOH   O    O N N 175 
HOH   H1   H N N 176 
HOH   H2   H N N 177 
ILE   N    N N N 178 
ILE   CA   C N S 179 
ILE   C    C N N 180 
ILE   O    O N N 181 
ILE   CB   C N S 182 
ILE   CG1  C N N 183 
ILE   CG2  C N N 184 
ILE   CD1  C N N 185 
ILE   OXT  O N N 186 
ILE   H    H N N 187 
ILE   H2   H N N 188 
ILE   HA   H N N 189 
ILE   HB   H N N 190 
ILE   HG12 H N N 191 
ILE   HG13 H N N 192 
ILE   HG21 H N N 193 
ILE   HG22 H N N 194 
ILE   HG23 H N N 195 
ILE   HD11 H N N 196 
ILE   HD12 H N N 197 
ILE   HD13 H N N 198 
ILE   HXT  H N N 199 
LEU   N    N N N 200 
LEU   CA   C N S 201 
LEU   C    C N N 202 
LEU   O    O N N 203 
LEU   CB   C N N 204 
LEU   CG   C N N 205 
LEU   CD1  C N N 206 
LEU   CD2  C N N 207 
LEU   OXT  O N N 208 
LEU   H    H N N 209 
LEU   H2   H N N 210 
LEU   HA   H N N 211 
LEU   HB2  H N N 212 
LEU   HB3  H N N 213 
LEU   HG   H N N 214 
LEU   HD11 H N N 215 
LEU   HD12 H N N 216 
LEU   HD13 H N N 217 
LEU   HD21 H N N 218 
LEU   HD22 H N N 219 
LEU   HD23 H N N 220 
LEU   HXT  H N N 221 
LYS   N    N N N 222 
LYS   CA   C N S 223 
LYS   C    C N N 224 
LYS   O    O N N 225 
LYS   CB   C N N 226 
LYS   CG   C N N 227 
LYS   CD   C N N 228 
LYS   CE   C N N 229 
LYS   NZ   N N N 230 
LYS   OXT  O N N 231 
LYS   H    H N N 232 
LYS   H2   H N N 233 
LYS   HA   H N N 234 
LYS   HB2  H N N 235 
LYS   HB3  H N N 236 
LYS   HG2  H N N 237 
LYS   HG3  H N N 238 
LYS   HD2  H N N 239 
LYS   HD3  H N N 240 
LYS   HE2  H N N 241 
LYS   HE3  H N N 242 
LYS   HZ1  H N N 243 
LYS   HZ2  H N N 244 
LYS   HZ3  H N N 245 
LYS   HXT  H N N 246 
MET   N    N N N 247 
MET   CA   C N S 248 
MET   C    C N N 249 
MET   O    O N N 250 
MET   CB   C N N 251 
MET   CG   C N N 252 
MET   SD   S N N 253 
MET   CE   C N N 254 
MET   OXT  O N N 255 
MET   H    H N N 256 
MET   H2   H N N 257 
MET   HA   H N N 258 
MET   HB2  H N N 259 
MET   HB3  H N N 260 
MET   HG2  H N N 261 
MET   HG3  H N N 262 
MET   HE1  H N N 263 
MET   HE2  H N N 264 
MET   HE3  H N N 265 
MET   HXT  H N N 266 
PHE   N    N N N 267 
PHE   CA   C N S 268 
PHE   C    C N N 269 
PHE   O    O N N 270 
PHE   CB   C N N 271 
PHE   CG   C Y N 272 
PHE   CD1  C Y N 273 
PHE   CD2  C Y N 274 
PHE   CE1  C Y N 275 
PHE   CE2  C Y N 276 
PHE   CZ   C Y N 277 
PHE   OXT  O N N 278 
PHE   H    H N N 279 
PHE   H2   H N N 280 
PHE   HA   H N N 281 
PHE   HB2  H N N 282 
PHE   HB3  H N N 283 
PHE   HD1  H N N 284 
PHE   HD2  H N N 285 
PHE   HE1  H N N 286 
PHE   HE2  H N N 287 
PHE   HZ   H N N 288 
PHE   HXT  H N N 289 
PRO   N    N N N 290 
PRO   CA   C N S 291 
PRO   C    C N N 292 
PRO   O    O N N 293 
PRO   CB   C N N 294 
PRO   CG   C N N 295 
PRO   CD   C N N 296 
PRO   OXT  O N N 297 
PRO   H    H N N 298 
PRO   HA   H N N 299 
PRO   HB2  H N N 300 
PRO   HB3  H N N 301 
PRO   HG2  H N N 302 
PRO   HG3  H N N 303 
PRO   HD2  H N N 304 
PRO   HD3  H N N 305 
PRO   HXT  H N N 306 
SER   N    N N N 307 
SER   CA   C N S 308 
SER   C    C N N 309 
SER   O    O N N 310 
SER   CB   C N N 311 
SER   OG   O N N 312 
SER   OXT  O N N 313 
SER   H    H N N 314 
SER   H2   H N N 315 
SER   HA   H N N 316 
SER   HB2  H N N 317 
SER   HB3  H N N 318 
SER   HG   H N N 319 
SER   HXT  H N N 320 
THR   N    N N N 321 
THR   CA   C N S 322 
THR   C    C N N 323 
THR   O    O N N 324 
THR   CB   C N R 325 
THR   OG1  O N N 326 
THR   CG2  C N N 327 
THR   OXT  O N N 328 
THR   H    H N N 329 
THR   H2   H N N 330 
THR   HA   H N N 331 
THR   HB   H N N 332 
THR   HG1  H N N 333 
THR   HG21 H N N 334 
THR   HG22 H N N 335 
THR   HG23 H N N 336 
THR   HXT  H N N 337 
TRP   N    N N N 338 
TRP   CA   C N S 339 
TRP   C    C N N 340 
TRP   O    O N N 341 
TRP   CB   C N N 342 
TRP   CG   C Y N 343 
TRP   CD1  C Y N 344 
TRP   CD2  C Y N 345 
TRP   NE1  N Y N 346 
TRP   CE2  C Y N 347 
TRP   CE3  C Y N 348 
TRP   CZ2  C Y N 349 
TRP   CZ3  C Y N 350 
TRP   CH2  C Y N 351 
TRP   OXT  O N N 352 
TRP   H    H N N 353 
TRP   H2   H N N 354 
TRP   HA   H N N 355 
TRP   HB2  H N N 356 
TRP   HB3  H N N 357 
TRP   HD1  H N N 358 
TRP   HE1  H N N 359 
TRP   HE3  H N N 360 
TRP   HZ2  H N N 361 
TRP   HZ3  H N N 362 
TRP   HH2  H N N 363 
TRP   HXT  H N N 364 
TYR   N    N N N 365 
TYR   CA   C N S 366 
TYR   C    C N N 367 
TYR   O    O N N 368 
TYR   CB   C N N 369 
TYR   CG   C Y N 370 
TYR   CD1  C Y N 371 
TYR   CD2  C Y N 372 
TYR   CE1  C Y N 373 
TYR   CE2  C Y N 374 
TYR   CZ   C Y N 375 
TYR   OH   O N N 376 
TYR   OXT  O N N 377 
TYR   H    H N N 378 
TYR   H2   H N N 379 
TYR   HA   H N N 380 
TYR   HB2  H N N 381 
TYR   HB3  H N N 382 
TYR   HD1  H N N 383 
TYR   HD2  H N N 384 
TYR   HE1  H N N 385 
TYR   HE2  H N N 386 
TYR   HH   H N N 387 
TYR   HXT  H N N 388 
VAL   N    N N N 389 
VAL   CA   C N S 390 
VAL   C    C N N 391 
VAL   O    O N N 392 
VAL   CB   C N N 393 
VAL   CG1  C N N 394 
VAL   CG2  C N N 395 
VAL   OXT  O N N 396 
VAL   H    H N N 397 
VAL   H2   H N N 398 
VAL   HA   H N N 399 
VAL   HB   H N N 400 
VAL   HG11 H N N 401 
VAL   HG12 H N N 402 
VAL   HG13 H N N 403 
VAL   HG21 H N N 404 
VAL   HG22 H N N 405 
VAL   HG23 H N N 406 
VAL   HXT  H N N 407 
# 
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 
A1ABL O01 C02  sing N N 1   
A1ABL C04 C05  doub Y N 2   
A1ABL C04 C03  sing Y N 3   
A1ABL C05 C06  sing Y N 4   
A1ABL C02 C03  sing N N 5   
A1ABL C03 C08  doub Y N 6   
A1ABL C06 C07  doub Y N 7   
A1ABL C08 C07  sing Y N 8   
A1ABL C08 O09  sing N N 9   
A1ABL O09 C10  sing N N 10  
A1ABL C12 C11  sing N N 11  
A1ABL C12 O13  sing N N 12  
A1ABL C11 C10  sing N N 13  
A1ABL C10 C15  sing N N 14  
A1ABL O13 C14  sing N N 15  
A1ABL C14 C15  sing N N 16  
A1ABL C10 H101 sing N N 17  
A1ABL C15 H151 sing N N 18  
A1ABL C15 H152 sing N N 19  
A1ABL C02 H021 sing N N 20  
A1ABL C02 H022 sing N N 21  
A1ABL C04 H041 sing N N 22  
A1ABL C05 H051 sing N N 23  
A1ABL C06 H061 sing N N 24  
A1ABL C07 H071 sing N N 25  
A1ABL C11 H111 sing N N 26  
A1ABL C11 H112 sing N N 27  
A1ABL C12 H121 sing N N 28  
A1ABL C12 H122 sing N N 29  
A1ABL C14 H141 sing N N 30  
A1ABL C14 H142 sing N N 31  
A1ABL O01 H011 sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
GLN   N   CA   sing N N 102 
GLN   N   H    sing N N 103 
GLN   N   H2   sing N N 104 
GLN   CA  C    sing N N 105 
GLN   CA  CB   sing N N 106 
GLN   CA  HA   sing N N 107 
GLN   C   O    doub N N 108 
GLN   C   OXT  sing N N 109 
GLN   CB  CG   sing N N 110 
GLN   CB  HB2  sing N N 111 
GLN   CB  HB3  sing N N 112 
GLN   CG  CD   sing N N 113 
GLN   CG  HG2  sing N N 114 
GLN   CG  HG3  sing N N 115 
GLN   CD  OE1  doub N N 116 
GLN   CD  NE2  sing N N 117 
GLN   NE2 HE21 sing N N 118 
GLN   NE2 HE22 sing N N 119 
GLN   OXT HXT  sing N N 120 
GLU   N   CA   sing N N 121 
GLU   N   H    sing N N 122 
GLU   N   H2   sing N N 123 
GLU   CA  C    sing N N 124 
GLU   CA  CB   sing N N 125 
GLU   CA  HA   sing N N 126 
GLU   C   O    doub N N 127 
GLU   C   OXT  sing N N 128 
GLU   CB  CG   sing N N 129 
GLU   CB  HB2  sing N N 130 
GLU   CB  HB3  sing N N 131 
GLU   CG  CD   sing N N 132 
GLU   CG  HG2  sing N N 133 
GLU   CG  HG3  sing N N 134 
GLU   CD  OE1  doub N N 135 
GLU   CD  OE2  sing N N 136 
GLU   OE2 HE2  sing N N 137 
GLU   OXT HXT  sing N N 138 
GLY   N   CA   sing N N 139 
GLY   N   H    sing N N 140 
GLY   N   H2   sing N N 141 
GLY   CA  C    sing N N 142 
GLY   CA  HA2  sing N N 143 
GLY   CA  HA3  sing N N 144 
GLY   C   O    doub N N 145 
GLY   C   OXT  sing N N 146 
GLY   OXT HXT  sing N N 147 
HIS   N   CA   sing N N 148 
HIS   N   H    sing N N 149 
HIS   N   H2   sing N N 150 
HIS   CA  C    sing N N 151 
HIS   CA  CB   sing N N 152 
HIS   CA  HA   sing N N 153 
HIS   C   O    doub N N 154 
HIS   C   OXT  sing N N 155 
HIS   CB  CG   sing N N 156 
HIS   CB  HB2  sing N N 157 
HIS   CB  HB3  sing N N 158 
HIS   CG  ND1  sing Y N 159 
HIS   CG  CD2  doub Y N 160 
HIS   ND1 CE1  doub Y N 161 
HIS   ND1 HD1  sing N N 162 
HIS   CD2 NE2  sing Y N 163 
HIS   CD2 HD2  sing N N 164 
HIS   CE1 NE2  sing Y N 165 
HIS   CE1 HE1  sing N N 166 
HIS   NE2 HE2  sing N N 167 
HIS   OXT HXT  sing N N 168 
HOH   O   H1   sing N N 169 
HOH   O   H2   sing N N 170 
ILE   N   CA   sing N N 171 
ILE   N   H    sing N N 172 
ILE   N   H2   sing N N 173 
ILE   CA  C    sing N N 174 
ILE   CA  CB   sing N N 175 
ILE   CA  HA   sing N N 176 
ILE   C   O    doub N N 177 
ILE   C   OXT  sing N N 178 
ILE   CB  CG1  sing N N 179 
ILE   CB  CG2  sing N N 180 
ILE   CB  HB   sing N N 181 
ILE   CG1 CD1  sing N N 182 
ILE   CG1 HG12 sing N N 183 
ILE   CG1 HG13 sing N N 184 
ILE   CG2 HG21 sing N N 185 
ILE   CG2 HG22 sing N N 186 
ILE   CG2 HG23 sing N N 187 
ILE   CD1 HD11 sing N N 188 
ILE   CD1 HD12 sing N N 189 
ILE   CD1 HD13 sing N N 190 
ILE   OXT HXT  sing N N 191 
LEU   N   CA   sing N N 192 
LEU   N   H    sing N N 193 
LEU   N   H2   sing N N 194 
LEU   CA  C    sing N N 195 
LEU   CA  CB   sing N N 196 
LEU   CA  HA   sing N N 197 
LEU   C   O    doub N N 198 
LEU   C   OXT  sing N N 199 
LEU   CB  CG   sing N N 200 
LEU   CB  HB2  sing N N 201 
LEU   CB  HB3  sing N N 202 
LEU   CG  CD1  sing N N 203 
LEU   CG  CD2  sing N N 204 
LEU   CG  HG   sing N N 205 
LEU   CD1 HD11 sing N N 206 
LEU   CD1 HD12 sing N N 207 
LEU   CD1 HD13 sing N N 208 
LEU   CD2 HD21 sing N N 209 
LEU   CD2 HD22 sing N N 210 
LEU   CD2 HD23 sing N N 211 
LEU   OXT HXT  sing N N 212 
LYS   N   CA   sing N N 213 
LYS   N   H    sing N N 214 
LYS   N   H2   sing N N 215 
LYS   CA  C    sing N N 216 
LYS   CA  CB   sing N N 217 
LYS   CA  HA   sing N N 218 
LYS   C   O    doub N N 219 
LYS   C   OXT  sing N N 220 
LYS   CB  CG   sing N N 221 
LYS   CB  HB2  sing N N 222 
LYS   CB  HB3  sing N N 223 
LYS   CG  CD   sing N N 224 
LYS   CG  HG2  sing N N 225 
LYS   CG  HG3  sing N N 226 
LYS   CD  CE   sing N N 227 
LYS   CD  HD2  sing N N 228 
LYS   CD  HD3  sing N N 229 
LYS   CE  NZ   sing N N 230 
LYS   CE  HE2  sing N N 231 
LYS   CE  HE3  sing N N 232 
LYS   NZ  HZ1  sing N N 233 
LYS   NZ  HZ2  sing N N 234 
LYS   NZ  HZ3  sing N N 235 
LYS   OXT HXT  sing N N 236 
MET   N   CA   sing N N 237 
MET   N   H    sing N N 238 
MET   N   H2   sing N N 239 
MET   CA  C    sing N N 240 
MET   CA  CB   sing N N 241 
MET   CA  HA   sing N N 242 
MET   C   O    doub N N 243 
MET   C   OXT  sing N N 244 
MET   CB  CG   sing N N 245 
MET   CB  HB2  sing N N 246 
MET   CB  HB3  sing N N 247 
MET   CG  SD   sing N N 248 
MET   CG  HG2  sing N N 249 
MET   CG  HG3  sing N N 250 
MET   SD  CE   sing N N 251 
MET   CE  HE1  sing N N 252 
MET   CE  HE2  sing N N 253 
MET   CE  HE3  sing N N 254 
MET   OXT HXT  sing N N 255 
PHE   N   CA   sing N N 256 
PHE   N   H    sing N N 257 
PHE   N   H2   sing N N 258 
PHE   CA  C    sing N N 259 
PHE   CA  CB   sing N N 260 
PHE   CA  HA   sing N N 261 
PHE   C   O    doub N N 262 
PHE   C   OXT  sing N N 263 
PHE   CB  CG   sing N N 264 
PHE   CB  HB2  sing N N 265 
PHE   CB  HB3  sing N N 266 
PHE   CG  CD1  doub Y N 267 
PHE   CG  CD2  sing Y N 268 
PHE   CD1 CE1  sing Y N 269 
PHE   CD1 HD1  sing N N 270 
PHE   CD2 CE2  doub Y N 271 
PHE   CD2 HD2  sing N N 272 
PHE   CE1 CZ   doub Y N 273 
PHE   CE1 HE1  sing N N 274 
PHE   CE2 CZ   sing Y N 275 
PHE   CE2 HE2  sing N N 276 
PHE   CZ  HZ   sing N N 277 
PHE   OXT HXT  sing N N 278 
PRO   N   CA   sing N N 279 
PRO   N   CD   sing N N 280 
PRO   N   H    sing N N 281 
PRO   CA  C    sing N N 282 
PRO   CA  CB   sing N N 283 
PRO   CA  HA   sing N N 284 
PRO   C   O    doub N N 285 
PRO   C   OXT  sing N N 286 
PRO   CB  CG   sing N N 287 
PRO   CB  HB2  sing N N 288 
PRO   CB  HB3  sing N N 289 
PRO   CG  CD   sing N N 290 
PRO   CG  HG2  sing N N 291 
PRO   CG  HG3  sing N N 292 
PRO   CD  HD2  sing N N 293 
PRO   CD  HD3  sing N N 294 
PRO   OXT HXT  sing N N 295 
SER   N   CA   sing N N 296 
SER   N   H    sing N N 297 
SER   N   H2   sing N N 298 
SER   CA  C    sing N N 299 
SER   CA  CB   sing N N 300 
SER   CA  HA   sing N N 301 
SER   C   O    doub N N 302 
SER   C   OXT  sing N N 303 
SER   CB  OG   sing N N 304 
SER   CB  HB2  sing N N 305 
SER   CB  HB3  sing N N 306 
SER   OG  HG   sing N N 307 
SER   OXT HXT  sing N N 308 
THR   N   CA   sing N N 309 
THR   N   H    sing N N 310 
THR   N   H2   sing N N 311 
THR   CA  C    sing N N 312 
THR   CA  CB   sing N N 313 
THR   CA  HA   sing N N 314 
THR   C   O    doub N N 315 
THR   C   OXT  sing N N 316 
THR   CB  OG1  sing N N 317 
THR   CB  CG2  sing N N 318 
THR   CB  HB   sing N N 319 
THR   OG1 HG1  sing N N 320 
THR   CG2 HG21 sing N N 321 
THR   CG2 HG22 sing N N 322 
THR   CG2 HG23 sing N N 323 
THR   OXT HXT  sing N N 324 
TRP   N   CA   sing N N 325 
TRP   N   H    sing N N 326 
TRP   N   H2   sing N N 327 
TRP   CA  C    sing N N 328 
TRP   CA  CB   sing N N 329 
TRP   CA  HA   sing N N 330 
TRP   C   O    doub N N 331 
TRP   C   OXT  sing N N 332 
TRP   CB  CG   sing N N 333 
TRP   CB  HB2  sing N N 334 
TRP   CB  HB3  sing N N 335 
TRP   CG  CD1  doub Y N 336 
TRP   CG  CD2  sing Y N 337 
TRP   CD1 NE1  sing Y N 338 
TRP   CD1 HD1  sing N N 339 
TRP   CD2 CE2  doub Y N 340 
TRP   CD2 CE3  sing Y N 341 
TRP   NE1 CE2  sing Y N 342 
TRP   NE1 HE1  sing N N 343 
TRP   CE2 CZ2  sing Y N 344 
TRP   CE3 CZ3  doub Y N 345 
TRP   CE3 HE3  sing N N 346 
TRP   CZ2 CH2  doub Y N 347 
TRP   CZ2 HZ2  sing N N 348 
TRP   CZ3 CH2  sing Y N 349 
TRP   CZ3 HZ3  sing N N 350 
TRP   CH2 HH2  sing N N 351 
TRP   OXT HXT  sing N N 352 
TYR   N   CA   sing N N 353 
TYR   N   H    sing N N 354 
TYR   N   H2   sing N N 355 
TYR   CA  C    sing N N 356 
TYR   CA  CB   sing N N 357 
TYR   CA  HA   sing N N 358 
TYR   C   O    doub N N 359 
TYR   C   OXT  sing N N 360 
TYR   CB  CG   sing N N 361 
TYR   CB  HB2  sing N N 362 
TYR   CB  HB3  sing N N 363 
TYR   CG  CD1  doub Y N 364 
TYR   CG  CD2  sing Y N 365 
TYR   CD1 CE1  sing Y N 366 
TYR   CD1 HD1  sing N N 367 
TYR   CD2 CE2  doub Y N 368 
TYR   CD2 HD2  sing N N 369 
TYR   CE1 CZ   doub Y N 370 
TYR   CE1 HE1  sing N N 371 
TYR   CE2 CZ   sing Y N 372 
TYR   CE2 HE2  sing N N 373 
TYR   CZ  OH   sing N N 374 
TYR   OH  HH   sing N N 375 
TYR   OXT HXT  sing N N 376 
VAL   N   CA   sing N N 377 
VAL   N   H    sing N N 378 
VAL   N   H2   sing N N 379 
VAL   CA  C    sing N N 380 
VAL   CA  CB   sing N N 381 
VAL   CA  HA   sing N N 382 
VAL   C   O    doub N N 383 
VAL   C   OXT  sing N N 384 
VAL   CB  CG1  sing N N 385 
VAL   CB  CG2  sing N N 386 
VAL   CB  HB   sing N N 387 
VAL   CG1 HG11 sing N N 388 
VAL   CG1 HG12 sing N N 389 
VAL   CG1 HG13 sing N N 390 
VAL   CG2 HG21 sing N N 391 
VAL   CG2 HG22 sing N N 392 
VAL   CG2 HG23 sing N N 393 
VAL   OXT HXT  sing N N 394 
# 
_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                    7HBN 
_atom_sites.fract_transf_matrix[1][1]   0.015138 
_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]   0.011187 
_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 
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   ? 4.36736   -28.17206 -39.17868 1.000 49.49539 ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 5.72022   -27.63642 -39.25285 1.000 59.31139 ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 5.99352   -26.77171 -38.03786 1.000 51.63289 ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 5.32954   -25.75711 -37.83607 1.000 58.51780 ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 5.90197   -26.83213 -40.54585 1.000 69.36902 ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 6.97563   -25.74744 -40.48175 1.000 77.90442 ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 6.75539   -24.65568 -41.51487 1.000 99.72516 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 6.16901   -24.94698 -42.57703 1.000 91.53746 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 7.12892   -23.49379 -41.25846 1.000 87.98538 ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 6.96649   -27.18376 -37.22862 1.000 40.69086 ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 7.26041   -26.56102 -35.94203 1.000 33.54384 ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 8.62100   -25.88188 -36.01415 1.000 37.31217 ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 9.61986   -26.51471 -36.37658 1.000 40.88760 ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 7.23220   -27.59532 -34.80387 1.000 33.81255 ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 7.49388   -26.92617 -33.46431 1.000 34.73535 ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 5.90300   -28.32987 -34.79354 1.000 46.10761 ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 8.66312   -24.60275 -35.64961 1.000 28.70183 ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 9.90309   -23.84018 -35.58317 1.000 31.19311 ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 10.31526  -23.68112 -34.12539 1.000 32.41492 ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 9.51095   -23.24857 -33.29394 1.000 24.17602 ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 9.73321   -22.46748 -36.23556 1.000 26.87221 ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 9.64713   -22.49688 -37.75223 1.000 33.54369 ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 9.23423   -21.15635 -38.33359 1.000 47.91992 ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 8.06255   -20.76311 -38.14873 1.000 49.68728 ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 10.07950  -20.49414 -38.97267 1.000 43.71818 ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 11.56025  -24.03317 -33.81818 1.000 23.99321 ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 12.10158  -23.91769 -32.47070 1.000 22.50151 ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 13.05500  -22.73386 -32.40558 1.000 25.44550 ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 13.96450  -22.61663 -33.23387 1.000 24.82902 ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 12.82364  -25.19960 -32.05301 1.000 25.86631 ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 11.97717  -26.32710 -32.30663 1.000 27.14100 ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 13.17538  -25.15528 -30.57202 1.000 24.07354 ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 12.84301  -21.86408 -31.42283 1.000 23.75976 ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 13.63807  -20.66179 -31.23711 1.000 22.15254 ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 14.31924  -20.70080 -29.87856 1.000 36.42717 ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 13.79417  -21.27370 -28.92047 1.000 25.52249 ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 12.77642  -19.39880 -31.30786 1.000 21.22777 ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 12.08262  -19.19645 -32.62060 1.000 23.64091 ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 10.86080  -19.79948 -32.87091 1.000 24.49877 ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 12.62821  -18.36865 -33.58735 1.000 25.33818 ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 10.20973  -19.60532 -34.07277 1.000 23.94541 ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 11.97936  -18.16547 -34.78951 1.000 30.02938 ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 10.76913  -18.78756 -35.03332 1.000 33.49287 ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 15.48318  -20.06662 -29.79656 1.000 28.08196 ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 16.14930  -19.85047 -28.52200 1.000 29.18389 ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 15.69371  -18.51907 -27.93988 1.000 27.18442 ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 15.62412  -17.51589 -28.65638 1.000 21.91036 ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 17.66868  -19.86389 -28.69272 1.000 24.46367 ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 15.35836  -18.51787 -26.65148 1.000 20.77815 ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 15.13146  -17.26028 -25.95410 1.000 19.72865 ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 16.39608  -16.41284 -25.99401 1.000 26.61891 ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 17.51523  -16.93334 -26.00271 1.000 20.90999 ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 14.73493  -17.50864 -24.49497 1.000 20.19116 ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 13.31480  -17.96525 -24.30860 1.000 25.40765 ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 12.25750  -17.12006 -24.59873 1.000 22.78662 ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 13.03843  -19.23276 -23.82083 1.000 19.16424 ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 10.94964  -17.53366 -24.41754 1.000 24.14156 ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 11.73527  -19.65279 -23.64039 1.000 20.79333 ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 10.68859  -18.80220 -23.93914 1.000 22.16204 ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 16.21816  -15.09370 -26.02501 1.000 23.12591 ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 17.34873  -14.22113 -25.74603 1.000 28.00067 ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 17.87880  -14.51754 -24.34798 1.000 25.59492 ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 17.12843  -14.90410 -23.44702 1.000 26.65665 ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 16.95424  -12.74765 -25.86448 1.000 30.79483 ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 16.59301  -12.29588 -27.27166 1.000 31.97013 ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 15.89096  -10.95019 -27.28420 1.000 41.28057 ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 14.67018  -10.87157 -27.15710 1.000 46.18207 ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 16.66585  -9.88054  -27.43128 1.000 44.14520 ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 19.19279  -14.34774 -24.17741 1.000 26.91510 ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 19.83749  -14.74391 -22.92806 1.000 24.98578 ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 19.20223  -14.05622 -21.72501 1.000 27.22544 ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 19.02517  -14.67544 -20.66927 1.000 29.19599 ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 21.33460  -14.44233 -22.99305 1.000 31.21256 ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 18.83698  -12.78120 -21.86926 1.000 30.50666 ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 18.24717  -12.05197 -20.75125 1.000 30.98667 ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 16.86451  -12.58892 -20.39913 1.000 29.56071 ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 16.48788  -12.61826 -19.22120 1.000 27.71507 ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.18224  -10.55731 -21.07095 1.000 35.83087 ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 19.53133  -9.91620  -21.39166 1.000 47.20500 ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 19.97996  -10.12515 -22.82805 1.000 53.48712 ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 19.31160  -10.87707 -23.56873 1.000 43.48295 ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.00678  -9.52983  -23.21844 1.000 64.67101 ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 16.09387  -13.02078 -21.40078 1.000 26.20851 ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 14.76567  -13.56000 -21.12080 1.000 30.13388 ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 14.88077  -14.94027 -20.48216 1.000 25.63219 ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 14.11056  -15.28863 -19.57828 1.000 22.82544 ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 13.89984  -13.58620 -22.39895 1.000 23.45259 ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 13.36925  -12.18984 -22.76371 1.000 26.38898 ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 12.72236  -14.53923 -22.23868 1.000 19.99980 ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.41316  -11.13325 -23.08886 1.000 28.91459 ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 15.85264  -15.74117 -20.92720 1.000 22.71074 ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 16.09929  -17.02835 -20.28550 1.000 26.24499 ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 16.51524  -16.84566 -18.83121 1.000 30.85468 ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 16.12760  -17.63631 -17.96251 1.000 23.72990 ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 17.16542  -17.80609 -21.05829 1.000 24.08292 ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 17.30650  -15.80730 -18.54739 1.000 28.46095 ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 17.68027  -15.51559 -17.16654 1.000 30.44002 ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 16.46971  -15.09739 -16.34120 1.000 29.69887 ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 16.33317  -15.50319 -15.18074 1.000 30.70568 ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 18.74917  -14.42476 -17.12758 1.000 33.55451 ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 19.55156  -14.39393 -15.83770 1.000 50.28525 ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 20.60006  -13.29977 -15.83041 1.000 69.53103 ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 20.56801  -12.38763 -16.65737 1.000 57.09305 ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 21.53479  -13.38182 -14.88921 1.000 71.46361 ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 15.58840  -14.27513 -16.91824 1.000 26.51827 ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 14.36350  -13.89305 -16.22203 1.000 34.24250 ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 13.51780  -15.11272 -15.88941 1.000 33.56409 ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 12.96001  -15.21399 -14.79054 1.000 29.22577 ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 13.56026  -12.90966 -17.07280 1.000 27.31043 ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 12.15735  -12.58107 -16.55764 1.000 34.52270 ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 12.23504  -11.66388 -15.35181 1.000 31.66299 ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 11.30758  -11.96116 -17.65646 1.000 32.18316 ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 13.42503  -16.05667 -16.82438 1.000 25.02364 ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 12.55403  -17.20832 -16.63397 1.000 21.22931 ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 13.10200  -18.13802 -15.55686 1.000 30.97431 ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 12.33978  -18.67008 -14.74172 1.000 31.45824 ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 12.39140  -17.94231 -17.96319 1.000 17.84393 ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 11.28793  -17.35825 -18.82881 1.000 25.03603 ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 11.26919  -18.02581 -20.50106 1.000 26.40336 ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 10.25575  -19.47903 -20.25766 1.000 25.09227 ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 14.42429  -18.33462 -15.52779 1.000 28.83219 ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 15.02069  -19.18909 -14.50660 1.000 27.63546 ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 14.95056  -18.54834 -13.12683 1.000 32.02350 ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 14.82153  -19.25890 -12.12440 1.000 34.00600 ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 16.46882  -19.51530 -14.87099 1.000 32.55478 ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 17.15974  -18.35886 -15.30793 1.000 53.64968 ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.03569  -17.21772 -13.05102 1.000 26.27813 ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 14.87093  -16.54568 -11.76625 1.000 32.94412 ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 13.45185  -16.72798 -11.24253 1.000 36.35495 ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.24987  -16.98363 -10.04972 1.000 26.88342 ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.23521  -15.06199 -11.90647 1.000 28.76974 ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 15.17938  -14.02508 -10.76917 1.000 39.90227 ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 15.76890  -12.71667 -11.27003 1.000 48.82959 ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 13.77861  -13.75513 -10.22381 1.000 33.96849 ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 12.45570  -16.59838 -12.12115 1.000 27.25435 ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.06927  -16.80270 -11.71253 1.000 30.51696 ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 10.85890  -18.24004 -11.25317 1.000 33.40101 ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.13583  -18.50282 -10.28338 1.000 31.57318 ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 10.11983  -16.42479 -12.86563 1.000 24.58988 ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 10.06433  -14.90691 -13.03567 1.000 28.09457 ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 8.72132   -16.98139 -12.62846 1.000 29.03039 ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 9.52549   -14.46451 -14.37824 1.000 34.78609 ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 11.51022  -19.18920 -11.92377 1.000 26.77344 ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 11.30346  -20.59844 -11.61424 1.000 35.22311 ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.04917  -21.00924 -10.34696 1.000 39.19531 ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 11.54886  -21.83123 -9.56942  1.000 35.48215 ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 11.71988  -21.45559 -12.82368 1.000 35.17931 ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 10.67064  -21.35092 -13.93089 1.000 27.90768 ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.92912  -22.91225 -12.42892 1.000 31.53783 ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 11.12964  -21.91510 -15.24907 1.000 30.99649 ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.22757  -20.43568 -10.09585 1.000 38.53161 ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.11169  -20.94438 -9.05453  1.000 30.40359 ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.06976  -20.15279 -7.75322  1.000 44.08495 ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 14.41518  -20.70853 -6.70539  1.000 41.46703 ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 15.55652  -20.97952 -9.56389  1.000 38.66475 ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 15.75075  -21.97789 -10.68392 1.000 44.48105 ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 15.17257  -23.06518 -10.66820 1.000 42.20057 ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 16.56261  -21.61229 -11.66794 1.000 58.34523 ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 13.67102  -18.88349 -7.78397  1.000 35.54299 ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.66176  -18.07807 -6.56772  1.000 36.68536 ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.56184  -18.54737 -5.62386  1.000 35.44074 ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.41806  -18.75499 -6.04092  1.000 34.59413 ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.46147  -16.59937 -6.90382  1.000 30.05828 ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 14.48765  -16.16902 -7.80638  1.000 37.81491 ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.51282  -15.74899 -5.64262  1.000 36.14315 ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.90614  -18.71994 -4.34934  1.000 32.00166 ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.88548  -18.99396 -3.34688  1.000 32.07407 ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 11.03973  -17.74562 -3.13693  1.000 38.96927 ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.54842  -16.70540 -2.70479  1.000 34.38433 ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.50864  -19.44119 -2.02869  1.000 35.33970 ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.49151  -19.74913 -0.96677  1.000 35.66559 ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.70054  -20.88373 -1.05578  1.000 42.11777 ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 11.30244  -18.88937 0.10254   1.000 37.14361 ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.75211   -21.16628 -0.08633  1.000 38.87968 ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 10.35498  -19.16529 1.07500   1.000 45.33559 ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.57963   -20.30513 0.97971   1.000 36.90964 ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.74844   -17.85044 -3.43953  1.000 30.81182 ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.86448   -16.69073 -3.39275  1.000 28.09639 ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.43507   -17.20879 -3.29419  1.000 26.69533 ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.91138   -17.76860 -4.26189  1.000 26.51911 ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 9.07232   -15.81617 -4.62419  1.000 28.68898 ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.05606   -14.72043 -4.77672  1.000 32.95135 ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.12308   -13.57388 -3.99747  1.000 35.00792 ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 7.03275   -14.82651 -5.70542  1.000 34.10295 ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.19126   -12.56861 -4.13191  1.000 36.37016 ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.09951   -13.82757 -5.84857  1.000 32.91307 ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.18349   -12.70261 -5.06040  1.000 31.21179 ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.25147   -11.70775 -5.20152  1.000 53.83338 ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.81199   -17.02305 -2.12920  1.000 29.29972 ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.55694   -17.70019 -1.82452  1.000 29.19455 ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.33697   -17.03507 -2.44983  1.000 25.41801 ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.31467   -17.70451 -2.63287  1.000 32.75890 ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.36761   -17.78403 -0.30813  1.000 29.04480 ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 6.34923   -18.62108 0.27610   1.000 30.94412 ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.41229   -15.74603 -2.78027  1.000 25.22001 ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.24714   -14.99955 -3.25501  1.000 24.27963 ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 3.03028   -15.23725 -4.75399  1.000 26.40406 ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 3.07857   -14.32860 -5.58320  1.000 29.60914 ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.41877   -13.52038 -2.93240  1.000 30.06872 ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.19769   -12.69505 -3.28927  1.000 34.20884 ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 1.06284   -13.15451 -3.16096  1.000 33.55929 ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.42605   -11.46285 -3.72894  1.000 32.42798 ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.77152   -16.50383 -5.09247  1.000 23.71107 ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.66448   -16.89415 -6.49439  1.000 22.84489 ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.35990   -16.44640 -7.13992  1.000 23.93478 ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.28491   -16.40228 -8.37215  1.000 28.23956 ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 2.79734   -18.41193 -6.63919  1.000 26.67537 ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.16690   -18.98032 -6.29592  1.000 22.41943 ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.14461   -20.50303 -6.37304  1.000 33.41737 ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 5.53465   -21.10415 -6.22427  1.000 31.91060 ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 6.39143   -20.85216 -7.41567  1.000 26.91150 ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.33615   -16.11397 -6.34721  1.000 24.94657 ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.98199  -15.83528 -6.91051  1.000 21.89904 ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.98720  -14.62116 -7.82964  1.000 24.50205 ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.93148  -14.45744 -8.60979  1.000 23.92838 ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -2.01018  -15.61506 -5.79987  1.000 23.01897 ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.76094  -14.36572 -4.97569  1.000 22.74045 ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.68303  -14.26115 -3.77987  1.000 33.46671 ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -2.86665  -15.27616 -3.07526  1.000 37.70299 ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.22574  -13.16086 -3.54775  1.000 40.66005 ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.03582   -13.76498 -7.75690  1.000 24.50550 ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.06808   -12.55902 -8.57687  1.000 22.58911 ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.18042   -12.85001 -10.06505 1.000 23.03035 ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? 0.03061   -11.92721 -10.87373 1.000 23.76428 ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.21707   -11.63057 -8.12704  1.000 28.31024 ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.58103   -12.31912 -8.26165  1.000 29.12999 ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 0.97978   -11.14468 -6.70355  1.000 32.87414 ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.31589   -12.02170 -9.56270  1.000 29.30755 ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 0.44144   -14.10255 -10.45142 1.000 19.01804 ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 0.48670   -14.43742 -11.87229 1.000 24.17552 ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.83257  -14.09795 -12.55643 1.000 25.38118 ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.84693  -13.64598 -13.70744 1.000 20.62967 ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 0.81964   -15.92174 -12.05941 1.000 21.49272 ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? -0.36026  -16.84072 -11.86287 1.000 22.84773 ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? -0.68114  -17.31830 -10.60461 1.000 26.90692 ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? -1.14960  -17.22432 -12.93829 1.000 25.22701 ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -1.76736  -18.15829 -10.41929 1.000 23.84058 ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -2.23958  -18.05877 -12.75680 1.000 17.05151 ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -2.54413  -18.52934 -11.49728 1.000 20.02187 ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.95352  -14.30120 -11.85851 1.000 24.22931 ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -3.25639  -14.10394 -12.48405 1.000 17.62100 ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -3.54036  -12.62587 -12.71204 1.000 25.19616 ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -4.09270  -12.24842 -13.75311 1.000 23.72877 ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -4.35245  -14.74194 -11.63192 1.000 16.06682 ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -5.72931  -14.77028 -12.29783 1.000 18.94318 ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -5.67475  -15.57931 -13.58436 1.000 19.47804 ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -6.77508  -15.33847 -11.35328 1.000 20.00059 ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -3.17208  -11.77612 -11.74888 1.000 23.24576 ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -3.28372  -10.33487 -11.94975 1.000 21.61239 ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -2.48911  -9.89213  -13.17126 1.000 23.69429 ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -2.94937  -9.04914  -13.95068 1.000 25.70381 ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.80269  -9.59029  -10.70204 1.000 22.05120 ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.67061  -8.08330  -10.88290 1.000 29.12616 ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -1.98277  -7.43301  -9.69333  1.000 34.13450 ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.55743  -7.74025  -9.64881  1.000 36.51632 ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.18646   -7.68990  -8.55165  1.000 45.18917 ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.32997  -7.35293  -7.38103  1.000 34.70344 ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.48131   -7.98414  -8.63092  1.000 39.53238 ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -1.30176  -10.47069 -13.36687 1.000 23.51288 ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? -0.44276  -10.04970 -14.46794 1.000 27.24461 ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -1.02020  -10.46442 -15.81550 1.000 22.86116 ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -0.97574  -9.69081  -16.77968 1.000 21.38214 ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 0.96242   -10.62453 -14.28379 1.000 22.51742 ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 1.67227   -10.15581 -13.01841 1.000 26.17143 ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 1.63359   -8.64914  -12.84011 1.000 35.95170 ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 1.77336   -7.92252  -13.84585 1.000 35.61315 ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.46504   -8.18968  -11.68981 1.000 44.37170 ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -1.56244  -11.68120 -15.90602 1.000 20.13660 ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -2.13077  -12.13485 -17.17215 1.000 27.30240 ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -3.42798  -11.40111 -17.49332 1.000 24.46961 ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -3.67961  -11.05638 -18.65452 1.000 22.21201 ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -2.35877  -13.64559 -17.13775 1.000 25.55473 ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? -1.11022  -14.50012 -16.90458 1.000 19.19761 ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? -1.47572  -15.97286 -16.82870 1.000 21.28045 ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? -0.07499  -14.25142 -17.99422 1.000 19.77217 ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -4.26365  -11.15518 -16.48022 1.000 19.97716 ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -5.49996  -10.40848 -16.70039 1.000 24.60469 ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -5.18786  -8.98129  -17.13095 1.000 21.38089 ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.85339  -8.42210  -18.01201 1.000 24.16107 ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -6.38040  -10.44364 -15.43591 1.000 19.87759 ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -6.98730  -11.83599 -15.24437 1.000 19.29911 ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -7.48190  -9.39139  -15.50722 1.000 27.38387 ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -7.62768  -12.04158 -13.88416 1.000 25.86491 ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -4.16296  -8.37317  -16.52705 1.000 23.24585 ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.78327  -7.01684  -16.90868 1.000 22.33194 ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -3.26415  -6.97371  -18.34106 1.000 22.89407 ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -3.53857  -6.01847  -19.07645 1.000 19.90184 ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.73902  -6.46797  -15.93534 1.000 24.42044 ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -1.88817  -5.53169  -16.57297 1.000 41.07211 ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -2.51276  -7.99796  -18.75636 1.000 21.12652 ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -2.11288  -8.09495  -20.15731 1.000 27.22593 ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -3.32827  -8.21126  -21.06628 1.000 26.51290 ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -3.39428  -7.55956  -22.11531 1.000 21.28567 ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -1.18380  -9.29053  -20.36502 1.000 23.93917 ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 0.22579   -9.02441  -19.88929 1.000 28.93905 ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 0.59766   -7.88228  -19.61742 1.000 28.45654 ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 1.02724   -10.08043 -19.79981 1.000 26.80457 ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -4.29838  -9.04435  -20.68091 1.000 17.62735 ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -5.52215  -9.17470  -21.46479 1.000 20.43931 ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -6.25983  -7.84461  -21.55395 1.000 26.39372 ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -6.76503  -7.47548  -22.62108 1.000 21.21360 ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -6.42333  -10.24797 -20.85103 1.000 21.29976 ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -5.87923  -11.54527 -21.03021 1.000 20.53534 ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -6.32575  -7.10840  -20.44054 1.000 21.41707 ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -6.98464  -5.80637  -20.44665 1.000 23.21351 ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -6.28869  -4.83798  -21.39546 1.000 25.78247 ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.95035  -4.09047  -22.12564 1.000 22.63206 ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -7.02437  -5.23501  -19.02952 1.000 18.73924 ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.71428  -3.99745  -18.99860 1.000 26.44766 ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -4.95270  -4.83533  -21.39735 1.000 22.17383 ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -4.21518  -3.97342  -22.31666 1.000 18.18967 ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -4.47278  -4.36361  -23.76662 1.000 29.05554 ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -4.59553  -3.49505  -24.63903 1.000 23.27155 ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -2.72052  -4.02835  -22.00174 1.000 20.79763 ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -2.38479  -3.40950  -20.65638 1.000 41.26691 ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -3.31070  -2.91551  -19.97744 1.000 36.85219 ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -1.19407  -3.41871  -20.27616 1.000 31.75065 ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -4.55592  -5.66776  -24.04286 1.000 20.63784 ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -4.84464  -6.12423  -25.39894 1.000 22.97670 ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -6.26097  -5.74793  -25.81883 1.000 22.66449 ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -6.50319  -5.41582  -26.98502 1.000 19.33760 ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -4.63840  -7.63575  -25.49938 1.000 19.08328 ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -7.21032  -5.79177  -24.88225 1.000 20.48511 ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -8.56920  -5.36228  -25.19229 1.000 21.71913 ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -8.63846  -3.85381  -25.39454 1.000 25.15750 ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -9.40459  -3.37052  -26.23720 1.000 23.29321 ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -9.52370  -5.80418  -24.08512 1.000 24.36897 ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -9.77882  -7.30892  -24.00652 1.000 20.24531 ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -10.23469 -7.69945  -22.61315 1.000 23.23593 ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -10.81548 -7.71452  -25.03832 1.000 25.52128 ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -7.84956  -3.09362  -24.62859 1.000 20.37757 ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -7.78345  -1.65017  -24.84154 1.000 22.95496 ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -7.28765  -1.32206  -26.24432 1.000 25.66977 ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -7.75615  -0.36272  -26.86968 1.000 20.75838 ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.87349  -0.99994  -23.79755 1.000 21.56518 ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -7.50376  -0.94773  -22.41940 1.000 28.07751 ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.67952  -1.34572  -22.27939 1.000 26.61496 ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.81811  -0.50545  -21.47338 1.000 28.27349 ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -6.33972  -2.11133  -26.75517 1.000 23.83621 ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -5.74654  -1.82058  -28.05637 1.000 26.95334 ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -6.75858  -2.00006  -29.18123 1.000 25.70564 ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -6.86722  -1.14802  -30.07137 1.000 23.66119 ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -4.52297  -2.70861  -28.28491 1.000 26.09852 ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -3.29710  -2.30020  -27.48311 1.000 29.54730 ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -2.20740  -3.35654  -27.57964 1.000 29.01453 ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -1.11138  -3.13033  -26.55155 1.000 39.83511 ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 0.10888   -3.92607  -26.86843 1.000 39.05515 ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -7.50816  -3.10551  -29.16323 1.000 22.40953 ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -8.48098  -3.33491  -30.22720 1.000 22.07284 ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -9.65699  -2.37383  -30.10629 1.000 28.29801 ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -10.23479 -1.96387  -31.12078 1.000 28.21181 ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -8.94203  -4.80634  -30.24190 1.000 20.55731 ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -9.72135  -5.10635  -31.52689 1.000 23.47087 ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -9.77699  -5.14142  -29.00947 1.000 18.02942 ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -8.94992  -4.80432  -32.79498 1.000 30.43173 ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -10.02683 -1.98331  -28.88322 1.000 22.68734 ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -11.09956 -1.00584  -28.73133 1.000 24.94987 ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -10.69543 0.34534   -29.30248 1.000 25.38770 ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -11.48827 0.99669   -29.99341 1.000 25.87231 ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -11.50267 -0.86267  -27.26365 1.000 25.48207 ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -12.70984 0.04929   -27.08549 1.000 34.75028 ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -13.06466 0.28649   -25.62937 1.000 49.00183 ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -14.10067 -0.62776  -25.16436 1.000 46.92621 ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -14.23958 -1.02709  -23.90795 1.000 51.46317 ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -13.41302 -0.62098  -22.95846 1.000 48.13488 ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -15.23638 -1.85004  -23.59517 1.000 45.22609 ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -9.46468  0.78545   -29.02595 1.000 22.81990 ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -9.00597  2.05696   -29.57593 1.000 21.77504 ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -8.98736  2.02623   -31.09887 1.000 28.55602 ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -9.37986  3.00078   -31.75154 1.000 27.79758 ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -7.61903  2.41215   -29.04106 1.000 22.60832 ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -7.19318  3.79958   -29.46053 1.000 36.73357 ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -7.75483  4.92599   -28.87423 1.000 29.21772 ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -6.26877  3.98319   -30.48048 1.000 28.74722 ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -7.38434  6.19679   -29.26983 1.000 28.53247 ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -5.89346  5.24894   -30.88449 1.000 28.65015 ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -6.45425  6.35115   -30.27613 1.000 32.43930 ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -6.08429  7.61323   -30.67438 1.000 39.96833 ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -8.53295  0.91611   -31.68467 1.000 27.65827 ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -8.50456  0.81847   -33.13969 1.000 29.67559 ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -9.90795  0.81785   -33.72885 1.000 29.50013 ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -10.12297 1.36881   -34.81477 1.000 35.35259 ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -7.74146  -0.43373  -33.56985 1.000 26.66420 ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -6.22966  -0.28418  -33.50114 1.000 46.78883 ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -5.49636  -1.44958  -34.13820 1.000 54.73121 ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -6.16591  -2.32696  -34.72353 1.000 47.35318 ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -4.24969  -1.48428  -34.06008 1.000 50.37668 ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -10.87383 0.22235   -33.02778 1.000 29.03173 ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -12.24953 0.20492   -33.50732 1.000 29.93351 ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -12.91615 1.57272   -33.44291 1.000 35.66069 ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -13.97505 1.75276   -34.05395 1.000 32.75138 ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -13.06999 -0.80496  -32.70349 1.000 30.08304 ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -13.29257 -0.34407  -31.38193 1.000 31.77192 ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -12.32871 2.53340   -32.72344 1.000 34.03763 ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -12.94071 3.85318   -32.60907 1.000 39.76826 ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -12.96764 4.58191   -33.94625 1.000 42.85990 ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -13.90315 5.34401   -34.21532 1.000 48.21517 ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -12.19775 4.69000   -31.56702 1.000 35.12611 ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -12.31177 4.23593   -30.11014 1.000 33.93335 ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.54636 5.17886   -29.19453 1.000 32.48139 ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.76809 4.13740   -29.68507 1.000 35.25397 ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -11.96014 4.36754   -34.79070 1.000 41.97097 ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -11.89968 4.98880   -36.10627 1.000 52.96499 ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -12.10395 3.99916   -37.24464 1.000 51.67534 ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -12.15432 4.41596   -38.40702 1.000 50.26715 ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -10.56183 5.71685   -36.29210 1.000 56.72425 ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -9.48661  4.77014   -36.24835 1.000 55.14270 ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -10.36565 6.76422   -35.20370 1.000 41.27807 ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -12.22128 2.70467   -36.94816 1.000 47.82051 ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -12.46167 1.69405   -37.97720 1.000 41.50936 ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -13.28523 0.57933   -37.35418 1.000 37.46942 ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -12.73885 -0.39951  -36.82629 1.000 35.31309 ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -11.15346 1.15526   -38.55503 1.000 37.98540 ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -11.36888 0.17651   -39.70002 1.000 49.84620 ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -12.53333 -0.07535  -40.07420 1.000 48.37401 ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -10.36369 -0.34163  -40.23280 1.000 47.33374 ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -14.61689 0.70600   -37.37601 1.000 46.20787 ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -15.46571 -0.34550  -36.78649 1.000 33.27198 ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -15.21731 -1.73106  -37.35871 1.000 40.96239 ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -15.44384 -2.72608  -36.65827 1.000 36.74563 ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -16.89354 0.12764   -37.09832 1.000 44.18723 ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -16.78334 1.53896   -37.58491 1.000 47.11191 ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -15.35176 1.96137   -37.60175 1.000 47.11978 ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -14.75690 -1.82918  -38.61026 1.000 39.34751 ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -14.53828 -3.13361  -39.22742 1.000 32.04905 ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -13.46723 -3.94494  -38.50965 1.000 42.94978 ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -13.37045 -5.15653  -38.73332 1.000 37.17209 ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -14.16020 -2.96634  -40.70001 1.000 33.09870 ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -12.88171 -2.37144  -40.83413 1.000 37.63317 ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -12.66216 -3.30970  -37.65409 1.000 27.95300 ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -11.68661 -4.04859  -36.86255 1.000 30.74651 ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -12.34913 -5.04839  -35.92416 1.000 35.80857 ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -11.68074 -5.97393  -35.44965 1.000 30.13844 ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -10.81947 -3.07668  -36.06211 1.000 35.18904 ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -9.97329  -2.15197  -36.92147 1.000 41.28170 ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -8.53422  -2.62946  -37.00037 1.000 41.76548 ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -7.68577  -1.68655  -37.83766 1.000 35.48965 ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -6.25308  -2.09341  -37.83984 1.000 53.06983 ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -13.64257 -4.88365  -35.64609 1.000 28.16192 ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -14.39468 -5.80584  -34.80770 1.000 30.09903 ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -15.20261 -6.81318  -35.61585 1.000 31.55434 ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -16.03619 -7.52163  -35.04292 1.000 31.97427 ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -15.32022 -5.03120  -33.86731 1.000 34.74751 ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -14.63992 -4.07814  -32.88374 1.000 37.42487 ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -15.66185 -3.46500  -31.94173 1.000 32.27265 ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -13.54574 -4.79617  -32.10458 1.000 29.35431 ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -14.98080 -6.89178  -36.93175 1.000 28.62749 ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -15.64903 -7.91679  -37.72816 1.000 32.93855 ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -15.26952 -9.31632  -37.26395 1.000 31.11244 ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -16.04781 -10.26150 -37.43526 1.000 36.43514 ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -15.31252 -7.74269  -39.20937 1.000 31.43474 ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -15.97082 -6.51853  -39.81947 1.000 50.24617 ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -16.84167 -5.91330  -39.15871 1.000 47.30420 ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -15.61725 -6.16379  -40.96427 1.000 52.60590 ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -14.08571 -9.46634  -36.67469 1.000 29.42684 ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -13.62996 -10.74085 -36.13839 1.000 27.65825 ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -14.20130 -11.04237 -34.75973 1.000 38.14797 ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -13.84622 -12.06960 -34.17201 1.000 39.28148 ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -12.10115 -10.75826 -36.07471 1.000 31.50488 ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -11.60730 -9.54016  -35.54104 1.000 31.15498 ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -15.06613 -10.17977 -34.23186 1.000 33.64385 ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -15.63575 -10.37897 -32.91438 1.000 34.00172 ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -15.95362 -9.07493  -32.21176 1.000 35.57525 ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -15.05337 -8.27370  -31.93776 1.000 34.14181 ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -17.23527 -8.85176  -31.91039 1.000 34.16926 ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -17.64522 -7.59341  -31.29671 1.000 38.18826 ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -17.49043 -7.60874  -29.78018 1.000 31.81031 ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -17.33841 -6.54469  -29.17009 1.000 31.22577 ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -19.09332 -7.27658  -31.67159 1.000 43.23346 ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -19.28185 -6.85963  -33.12416 1.000 49.45715 ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -20.73343 -6.50754  -33.41343 1.000 59.18176 ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -20.89589 -5.06058  -33.84310 1.000 58.84637 ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -21.94259 -4.93371  -34.89629 1.000 72.60917 ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -17.51903 -8.78568  -29.15829 1.000 25.96815 ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -17.44453 -8.87817  -27.70617 1.000 31.72686 ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -16.01150 -8.69545  -27.22087 1.000 30.22628 ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -15.06720 -9.24012  -27.79962 1.000 34.99218 ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -17.98920 -10.22283 -27.21836 1.000 32.09741 ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -19.49336 -10.41746 -27.40363 1.000 37.72954 ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -19.89804 -10.59861 -28.85439 1.000 71.27874 ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -19.27779 -11.43446 -29.54580 1.000 74.90829 ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -20.83432 -9.90382  -29.30464 1.000 70.00706 ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -15.86010 -7.92742  -26.14370 1.000 25.75863 ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -14.56634 -7.63396  -25.52892 1.000 26.38700 ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -14.62586 -8.14611  -24.09287 1.000 25.51849 ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -15.20306 -7.48743  -23.22234 1.000 23.73814 ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -14.27173 -6.13613  -25.57076 1.000 28.25762 ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -14.14896 -5.46962  -26.94348 1.000 27.62077 ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -13.72415 -4.01393  -26.79691 1.000 39.50908 ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -13.18126 -6.23028  -27.83642 1.000 22.41706 ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -14.03548 -9.31186  -23.83197 1.000 22.40898 ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -14.19630 -9.93568  -22.52598 1.000 20.25794 ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -12.97078 -10.76751 -22.17258 1.000 20.32236 ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -12.05779 -10.95733 -22.98087 1.000 22.01426 ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -15.45944 -10.80485 -22.47754 1.000 25.16349 ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -15.48116 -11.90311 -23.49606 1.000 21.74857 ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -16.40666 -11.95246 -24.51545 1.000 33.28874 ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -14.69701 -12.99689 -23.64766 1.000 37.69587 ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -16.19054 -13.02701 -25.25306 1.000 27.71680 ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -15.15785 -13.67724 -24.74868 1.000 33.75817 ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -12.97623 -11.26842 -20.93788 1.000 18.34589 ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -11.93522 -12.13580 -20.40031 1.000 23.28403 ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -12.60859 -13.34392 -19.76528 1.000 22.84726 ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -13.50016 -13.18721 -18.92409 1.000 21.56454 ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -11.06467 -11.40884 -19.35704 1.000 26.70263 ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -10.44533 -10.14226 -19.94946 1.000 22.02403 ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -9.99531  -12.34860 -18.80754 1.000 19.34733 ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -9.50792  -9.42266  -19.00142 1.000 21.51556 ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -12.18304 -14.54282 -20.15780 1.000 18.07761 ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -12.68568 -15.77903 -19.57376 1.000 22.98167 ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -11.56386 -16.51769 -18.85714 1.000 23.56787 ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -10.43241 -16.58207 -19.34956 1.000 20.76706 ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -13.30811 -16.69933 -20.63596 1.000 22.67853 ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -14.50580 -16.07618 -21.32475 1.000 27.70922 ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -15.25275 -15.30377 -20.72370 1.000 27.68399 ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -14.70076 -16.41888 -22.59189 1.000 25.53293 ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -11.88641 -17.07023 -17.69122 1.000 22.91789 ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -10.99264 -17.94926 -16.94764 1.000 18.27482 ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -11.59908 -19.34533 -16.94613 1.000 20.26386 ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -12.69358 -19.54947 -16.40927 1.000 19.25220 ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -10.77898 -17.44620 -15.51968 1.000 21.31813 ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -10.44109 -15.96286 -15.36013 1.000 18.92712 ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -10.41496 -15.57823 -13.88960 1.000 18.51676 ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -9.11300  -15.64423 -16.02912 1.000 18.46874 ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -10.89672 -20.29549 -17.54684 1.000 20.07625 ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -11.40536 -21.64305 -17.75866 1.000 24.41101 ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -10.47397 -22.62684 -17.06279 1.000 27.72097 ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -9.41660  -22.97681 -17.58830 1.000 22.33451 ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -11.53458 -21.96754 -19.25788 1.000 22.87688 ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -12.26773 -20.83699 -19.98475 1.000 23.74283 ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -12.24729 -23.29725 -19.45479 1.000 23.07597 ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -12.33964 -21.01822 -21.48640 1.000 24.35872 ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -10.83436 -23.09469 -15.87187 1.000 24.63767 ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -10.06539 -24.16589 -15.23693 1.000 21.95097 ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -10.52594 -25.53388 -15.71319 1.000 24.51766 ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -11.69985 -25.75448 -16.02136 1.000 24.14576 ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -10.36363 -23.96885 -13.74691 1.000 21.02144 ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -11.76550 -23.43019 -13.73647 1.000 27.99408 ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -11.94146 -22.62809 -15.01713 1.000 23.33456 ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -9.57211  -26.45963 -15.77736 1.000 22.46932 ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -9.84754  -27.83430 -16.18742 1.000 24.67848 ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -9.00021  -28.75137 -15.31732 1.000 25.07172 ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -7.77953  -28.81749 -15.48936 1.000 27.74954 ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -9.54598  -28.04145 -17.67346 1.000 28.36189 ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -10.01618 -29.39249 -18.18608 1.000 40.11244 ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -9.73591  -30.43246 -17.59054 1.000 32.24021 ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -10.73950 -29.37971 -19.29937 1.000 36.81945 ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -9.64605  -29.45459 -14.38480 1.000 26.88510 ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -8.91898  -30.30352 -13.44766 1.000 33.30042 ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -8.41799  -31.58803 -14.09463 1.000 39.06875 ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -7.41480  -32.14940 -13.64063 1.000 37.70248 ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -9.80353  -30.63627 -12.24464 1.000 29.36231 ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -10.02909 -29.46801 -11.29820 1.000 33.50117 ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -10.85937 -29.88857 -10.09571 1.000 40.39201 ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -11.10935 -28.71943 -9.15682  1.000 35.91521 ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -11.70837 -27.55443 -9.86373  1.000 41.91385 ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -9.09494  -32.07022 -15.13961 1.000 35.39477 ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -8.64491  -33.28507 -15.81223 1.000 45.32914 ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -7.34190  -33.04247 -16.56275 1.000 38.66808 ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -6.39805  -33.83493 -16.46298 1.000 41.88967 ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -9.72908  -33.79460 -16.76205 1.000 41.14857 ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -10.82495 -34.59930 -16.08264 1.000 56.08967 ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -11.74409 -33.73987 -15.23702 1.000 73.02678 ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -12.26086 -32.72152 -15.69910 1.000 67.50128 ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -11.95620 -34.14906 -13.99112 1.000 69.18044 ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -7.27572  -31.95273 -17.32614 1.000 33.24056 ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -6.05532  -31.57435 -18.02363 1.000 35.41855 ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -5.05464  -30.87285 -17.11700 1.000 34.73764 ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -3.89362  -30.71689 -17.51139 1.000 35.77746 ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -6.39009  -30.66269 -19.20750 1.000 32.91993 ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -7.22187  -31.36029 -20.26615 1.000 54.35525 ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -7.34099  -32.60329 -20.21194 1.000 51.65738 ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -7.75855  -30.66303 -21.15291 1.000 42.09449 ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -5.47712  -30.46284 -15.92005 1.000 27.54235 ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -4.66986  -29.64646 -15.01337 1.000 27.79791 ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -4.17090  -28.38463 -15.71429 1.000 30.94120 ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -2.98215  -28.05659 -15.69695 1.000 28.50139 ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -3.50741  -30.44728 -14.42290 1.000 29.36999 ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -3.12017  -29.99102 -13.02387 1.000 27.84771 ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? -1.64650  -30.21149 -12.73660 1.000 40.54118 ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? -1.31882  -31.62231 -12.57650 1.000 46.22551 ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? -0.10716  -32.13170 -12.74983 1.000 52.37453 ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 0.91848   -31.37230 -13.09967 1.000 40.18157 ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 0.08119   -33.43483 -12.56432 1.000 57.43165 ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -5.10236  -27.66841 -16.34134 1.000 23.52307 ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -4.78765  -26.43322 -17.04323 1.000 24.69781 ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -5.69913  -25.31265 -16.56867 1.000 23.02012 ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -6.87952  -25.53519 -16.28227 1.000 23.21900 ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -4.92787  -26.58277 -18.56717 1.000 24.98976 ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -6.28344  -26.91192 -18.89683 1.000 27.87928 ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -3.99479  -27.66524 -19.09525 1.000 30.18601 ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -5.13697  -24.10964 -16.48417 1.000 21.94262 ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -5.89742  -22.88065 -16.29756 1.000 21.74915 ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -5.69994  -22.02548 -17.53884 1.000 23.09328 ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -4.56112  -21.72488 -17.91291 1.000 21.26257 ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -5.45171  -22.12489 -15.04359 1.000 24.33418 ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -6.17939  -20.79915 -14.79978 1.000 21.35927 ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -7.68381  -21.01458 -14.71665 1.000 21.90421 ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -5.65894  -20.11063 -13.54523 1.000 24.28297 ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -6.80022  -21.64165 -18.17736 1.000 20.78447 ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -6.75740  -20.92262 -19.44190 1.000 19.81045 ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -7.33800  -19.52753 -19.26314 1.000 23.86186 ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -8.45096  -19.37325 -18.74733 1.000 23.54248 ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -7.52087  -21.68263 -20.52715 1.000 23.67496 ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -6.90529  -22.95918 -20.73967 1.000 25.12965 ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -7.50093  -20.90828 -21.82180 1.000 22.12411 ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -6.58152  -18.51929 -19.68817 1.000 19.65102 ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -7.01408  -17.12617 -19.66733 1.000 23.55612 ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -7.26200  -16.70889 -21.11056 1.000 22.97138 ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -6.31529  -16.54979 -21.89245 1.000 24.30166 ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -5.98228  -16.20993 -18.99333 1.000 18.62008 ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -5.80484  -16.58273 -17.51847 1.000 27.68594 ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -6.39248  -14.74940 -19.13558 1.000 21.76552 ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -4.70993  -17.59961 -17.25644 1.000 32.05584 ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -8.53179  -16.53167 -21.46667 1.000 21.47122 ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -8.93971  -16.17220 -22.81951 1.000 24.60611 ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -9.35006  -14.70819 -22.82774 1.000 30.36132 ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -10.07327 -14.25463 -21.93209 1.000 25.47427 ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -10.09561 -17.05744 -23.31822 1.000 22.09391 ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -10.43301 -16.72278 -24.76420 1.000 19.69769 ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -9.74679  -18.52833 -23.17619 1.000 22.50948 ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -8.88920  -13.97259 -23.83685 1.000 28.99202 ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -9.35410  -12.61947 -24.09217 1.000 22.99225 ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -9.62263  -12.46008 -25.58153 1.000 28.25450 ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -9.07118  -13.18324 -26.41574 1.000 24.90498 ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -8.34840  -11.56181 -23.59258 1.000 24.46122 ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -7.05720  -11.52733 -24.40685 1.000 32.47070 ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -7.09588  -11.21154 -25.61713 1.000 25.80774 ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -5.99020  -11.80778 -23.82156 1.000 26.55436 ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -10.49032 -11.50743 -25.90648 1.000 21.51741 ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -10.80446 -11.16109 -27.28757 1.000 24.68481 ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -10.14840 -9.83992  -27.68046 1.000 29.90312 ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -10.73085 -9.01889  -28.39348 1.000 22.32314 ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -12.31338 -11.09958 -27.49884 1.000 26.38137 ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -12.90549 -10.27662 -26.48665 1.000 23.25098 ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -12.91359 -12.49462 -27.42556 1.000 27.18846 ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -8.92232  -9.62656  -27.21225 1.000 21.89964 ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -8.18445  -8.41567  -27.50021 1.000 19.21076 ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -7.63489  -8.39722  -28.91187 1.000 19.38035 ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -8.08568  -9.12544  -29.79953 1.000 19.90877 ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -6.62199  -7.55040  -29.11075 1.000 20.39414 ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -6.09737  -7.31701  -30.45294 1.000 23.78799 ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -5.35360  -8.54024  -30.98078 1.000 22.45041 ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -5.26504  -8.74285  -32.19837 1.000 24.16057 ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -5.20418  -6.06102  -30.45059 1.000 26.16714 ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -4.83978  -5.64672  -31.87893 1.000 25.19479 ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -3.95638  -6.28909  -29.60827 1.000 20.47536 ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -4.54170  -4.17191  -32.02331 1.000 36.43358 ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -4.81929  -9.37681  -30.09496 1.000 22.61429 ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -4.05829  -10.53092 -30.52472 1.000 23.97138 ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -2.63247  -10.16863 -30.89485 1.000 25.78785 ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -2.17364  -9.03614  -30.73942 1.000 24.17884 ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? -1.91634  -11.16554 -31.40567 1.000 25.77146 ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? -0.50942  -11.00367 -31.73898 1.000 25.30266 ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? -0.21669  -11.64618 -33.08517 1.000 24.54949 ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? -0.71233  -12.73593 -33.38331 1.000 27.92338 ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 0.39232   -11.62713 -30.66446 1.000 24.81031 ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 0.49163   -10.81228 -29.38658 1.000 24.91120 ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 1.46063   -11.65115 -28.11928 1.000 29.84458 ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 0.30709   -12.91657 -27.59353 1.000 18.57821 ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 0.59107   -10.96634 -33.89419 1.000 25.77057 ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 1.08193   -11.56385 -35.12470 1.000 29.50760 ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 2.18819   -12.57017 -34.80829 1.000 27.25070 ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 2.66051   -12.68055 -33.67222 1.000 24.72150 ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 1.60420   -10.48830 -36.07766 1.000 28.55764 ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 2.77732   -9.88294  -35.51778 1.000 26.66113 ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 0.54841   -9.41675  -36.29532 1.000 27.08349 ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 2.59721   -13.32205 -35.83448 1.000 28.11636 ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 3.70870   -14.25244 -35.66000 1.000 25.50857 ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 4.97388   -13.52027 -35.23566 1.000 27.13067 ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 5.69009   -13.97338 -34.33500 1.000 24.80386 ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 3.95874   -15.03590 -36.94753 1.000 29.19330 ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 4.93327   -16.18902 -36.77165 1.000 30.63764 ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 5.24299   -16.86668 -38.09730 1.000 34.81125 ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 6.13897   -18.07736 -37.89453 1.000 38.73943 ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 6.86307   -18.44655 -39.14171 1.000 38.56222 ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 5.26325   -12.38340 -35.87428 1.000 28.46572 ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 6.42459   -11.59031 -35.48633 1.000 27.98490 ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 6.30877   -11.11580 -34.04384 1.000 33.21587 ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 7.30405   -11.08809 -33.31017 1.000 28.13533 ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 6.58858   -10.40229 -36.43369 1.000 30.20427 ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 5.09808   -10.74529 -33.61829 1.000 26.85625 ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 4.88524   -10.34014 -32.23227 1.000 28.13863 ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 5.18067   -11.48954 -31.27634 1.000 25.72362 ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 5.86316   -11.30879 -30.26131 1.000 26.53719 ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 3.45051   -9.84319  -32.04885 1.000 30.11040 ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 3.25388   -8.42301  -32.54630 1.000 41.33428 ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 4.25060   -7.78262  -32.94490 1.000 43.97071 ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 2.09661   -7.95058  -32.54801 1.000 48.09914 ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 4.66909   -12.68335 -31.58922 1.000 25.02933 ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 4.91371   -13.85305 -30.75038 1.000 24.90455 ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 6.40532   -14.12575 -30.61064 1.000 31.49713 ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 6.91341   -14.32110 -29.50009 1.000 25.64122 ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 4.20935   -15.07367 -31.34101 1.000 22.74033 ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 2.74554   -15.33251 -30.99572 1.000 30.11428 ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 2.30680   -16.65142 -31.61116 1.000 27.91309 ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 2.53637   -15.34557 -29.49324 1.000 21.87687 ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 7.12252   -14.14557 -31.73620 1.000 26.32425 ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 8.55585   -14.42127 -31.70905 1.000 28.67143 ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 9.29189   -13.32943 -30.94325 1.000 24.00596 ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 10.21651  -13.60516 -30.16885 1.000 28.85479 ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 9.08916   -14.57003 -33.14607 1.000 26.63783 ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 8.51784   -15.83200 -33.79452 1.000 24.81061 ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 10.61252  -14.61209 -33.15648 1.000 24.89530 ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 8.71002   -15.88583 -35.29458 1.000 24.71297 ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 8.88023   -12.07567 -31.12972 1.000 22.95093 ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 9.51157   -10.93704 -30.46509 1.000 24.72459 ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 8.95679   -10.76899 -29.04533 1.000 25.78662 ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 8.39949   -9.73720  -28.66972 1.000 30.81409 ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 9.32052   -9.67853  -31.30209 1.000 33.46732 ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 10.18456  -8.52948  -30.83374 1.000 50.41906 ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 11.16265  -8.72417  -30.10932 1.000 51.19387 ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 9.83359   -7.31978  -31.25536 1.000 45.92247 ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 9.11281   -11.83717 -28.25891 1.000 24.25718 ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 8.78297   -11.85060 -26.83006 1.000 27.00547 ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 7.32830   -11.46279 -26.56582 1.000 28.90012 ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 7.02962   -10.69708 -25.64669 1.000 25.76940 ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.74109   -10.95870 -26.03898 1.000 24.35414 ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 11.18257  -11.41396 -26.15665 1.000 26.29661 ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.49919  -12.57279 -25.88839 1.000 23.03752 ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 12.06426  -10.50420 -26.55624 1.000 25.15871 ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 6.41958   -12.01021 -27.37369 1.000 24.36167 ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 4.97375   -11.88433 -27.16877 1.000 22.33819 ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 4.54909   -10.42736 -26.98545 1.000 24.08196 ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 3.84435   -10.07065 -26.03929 1.000 24.18574 ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 4.51456   -12.74580 -25.98845 1.000 19.03709 ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 4.92140   -14.22130 -26.05979 1.000 22.82981 ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 6.10431   -14.51479 -25.14627 1.000 28.66842 ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 3.75170   -15.12735 -25.72551 1.000 25.11180 ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 4.98913   -9.57694  -27.91058 1.000 21.74183 ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 4.53942   -8.19837  -27.92853 1.000 22.35197 ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 5.06878   -7.31742  -26.81988 1.000 29.48425 ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 4.49575   -6.25564  -26.56255 1.000 25.95254 ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 6.14721   -7.71838  -26.15354 1.000 26.78724 ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 6.72522   -6.93445  -25.07379 1.000 28.29169 ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 8.15867   -6.54752  -25.41302 1.000 30.04457 ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 8.81673   -7.17685  -26.24586 1.000 27.81995 ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 6.70441   -7.70242  -23.74393 1.000 29.61992 ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 7.74612   -8.68613  -23.74405 1.000 28.53844 ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 5.36448   -8.39090  -23.53861 1.000 25.57264 ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 8.63260   -5.48978  -24.75608 1.000 26.23185 ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 10.03274  -5.08807  -24.82966 1.000 24.34055 ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 10.78682  -5.80697  -23.71755 1.000 29.48446 ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.34013  -5.17613  -22.80916 1.000 24.87721 ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.18394  -3.55842  -24.73395 1.000 26.63142 ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.34596   -2.99959  -23.58094 1.000 27.62304 ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.77798   -2.90373  -26.04350 1.000 32.21232 ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 9.76490   -1.61346  -23.14837 1.000 38.49899 ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 10.82491  -7.13982  -23.79943 1.000 21.28882 ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.24794  -7.95144  -22.66373 1.000 26.88397 ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 12.72355  -7.77126  -22.33163 1.000 24.48677 ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.11144  -7.93143  -21.16920 1.000 25.26154 ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 10.94442  -9.42475  -22.93250 1.000 25.16703 ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 13.56097  -7.44628  -23.31972 1.000 27.01671 ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 14.99086  -7.32069  -23.04882 1.000 29.40962 ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.27063  -6.15886  -22.10176 1.000 37.06026 ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 15.92245  -6.33032  -21.06514 1.000 36.67679 ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 15.77014  -7.15210  -24.35384 1.000 25.93979 ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 17.25864  -7.44175  -24.20839 1.000 44.83913 ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 18.00580  -7.25928  -25.51892 1.000 37.32893 ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 18.80437  -5.96529  -25.51882 1.000 66.21803 ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 19.97563  -6.04209  -24.60001 1.000 62.15475 ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 14.78258  -4.96356  -22.44141 1.000 26.87108 ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 14.99572  -3.81180  -21.57151 1.000 28.57629 ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.15410  -3.90247  -20.30491 1.000 36.25444 ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 14.56272  -3.39606  -19.25398 1.000 32.07190 ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 14.68514  -2.51720  -22.32191 1.000 30.27124 ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 13.35644  -2.51877  -22.81218 1.000 39.92780 ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 12.98348  -4.53768  -20.38277 1.000 29.94098 ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.16359  -4.70241  -19.19349 1.000 29.90745 ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 12.79283  -5.63378  -18.17500 1.000 31.22605 ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 12.72447  -5.38510  -16.96820 1.000 31.30694 ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.41184  -6.71969  -18.64499 1.000 24.88334 ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.10914  -7.62807  -17.73951 1.000 32.07163 ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.29340  -6.93735  -17.07766 1.000 33.22806 ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.54907  -7.12994  -15.88241 1.000 35.11282 ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.57437  -8.87084  -18.50105 1.000 28.92329 ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.43407  -9.63259  -18.91709 1.000 35.85747 ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.46659  -9.73940  -17.62738 1.000 30.50095 ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.02172  -6.12005  -17.84116 1.000 30.90753 ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.17981  -5.42263  -17.29531 1.000 35.08740 ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 16.77663  -4.49059  -16.15792 1.000 45.51686 ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.42945  -4.46366  -15.10906 1.000 46.38225 ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 17.89079  -4.66569  -18.41740 1.000 35.37935 ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 19.17069  -3.95749  -18.02042 1.000 54.63602 ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 19.35189  -2.69401  -18.84453 1.000 58.31886 ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 20.36698  -1.75991  -18.21969 1.000 62.67679 ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 19.69664  -0.57957  -17.61148 1.000 68.41783 ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 15.68667  -3.73964  -16.33381 1.000 38.72208 ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 15.20621  -2.87458  -15.25951 1.000 42.04221 ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 14.65749  -3.68853  -14.09107 1.000 35.71295 ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 14.86892  -3.33252  -12.92553 1.000 37.02082 ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 14.14162  -1.91621  -15.79373 1.000 37.52808 ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 13.95473  -4.78606  -14.38397 1.000 30.89953 ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.37734  -5.61129  -13.32601 1.000 31.65094 ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.45757  -6.20893  -12.43083 1.000 41.99352 ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.30634  -6.25017  -11.20431 1.000 36.47971 ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.51662  -6.71222  -13.94815 1.000 23.06750 ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.82891  -7.59783  -12.94589 1.000 33.33382 ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.25279  -7.06859  -11.80306 1.000 33.23695 ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.74646  -8.96381  -13.15875 1.000 28.00009 ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.61474  -7.88681  -10.88840 1.000 33.50202 ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.11155  -9.78717  -12.24847 1.000 27.49173 ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.54431  -9.24783  -11.11202 1.000 31.49813 ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.56013  -6.66940  -13.02369 1.000 39.10927 ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.59887  -7.32195  -12.23517 1.000 50.07870 ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.40941  -6.32147  -11.42139 1.000 42.98769 ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 17.90611  -6.66458  -10.34259 1.000 48.46368 ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.50836  -8.14137  -13.14812 1.000 46.09767 ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 17.16257  -9.61796  -13.16836 1.000 32.20583 ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 18.08859  -10.53574 -14.40707 1.000 78.09346 ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 16.89976  -11.79715 -14.83845 1.000 43.86841 ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.56299  -5.09118  -11.91626 1.000 42.00296 ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 18.18489  -4.05142  -11.10397 1.000 48.43174 ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.29761  -3.65581  -9.93307  1.000 51.13338 ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 17.80550  -3.28636  -8.86871  1.000 47.06829 ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.50848  -2.82847  -11.96259 1.000 48.26308 ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.38175  -3.12039  -13.16651 1.000 68.84681 ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 19.64275  -1.88645  -14.00638 1.000 87.81175 ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 20.41832  -1.98064  -14.98133 1.000 94.25646 ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 19.06044  -0.82580  -13.69997 1.000 87.31640 ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 15.97761  -3.72593  -10.10655 1.000 42.00845 ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 15.07795  -3.41709  -9.00255  1.000 35.22137 ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 15.10760  -4.51450  -7.94649  1.000 46.72831 ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 15.03999  -4.22792  -6.74565  1.000 55.80473 ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.65922  -3.20623  -9.52743  1.000 39.91133 ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.21666  -5.77604  -8.37420  1.000 37.30790 ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.23666  -6.88413  -7.42360  1.000 41.08129 ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.45004  -6.80478  -6.50631  1.000 57.31200 ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.33134  -6.99176  -5.28980  1.000 53.66833 ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.21301  -8.21697  -8.17104  1.000 41.93389 ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.90898  -8.55711  -8.89232  1.000 36.93000 ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 14.03777  -9.87145  -9.64702  1.000 39.99719 ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.75370  -8.61043  -7.90308  1.000 39.89135 ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.62697  -6.52432  -7.06880  1.000 53.36978 ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.81290  -6.34330  -6.24243  1.000 60.09649 ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.73901  -5.07477  -5.40277  1.000 66.52512 ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.50978  -4.93479  -4.44687  1.000 62.45781 ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 20.06865  -6.33962  -7.12283  1.000 60.49879 ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.22113  -5.12921  -8.04468  1.000 71.26227 ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 20.85553  -3.92779  -7.36538  1.000 91.93442 ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 21.57721  -4.06631  -6.37722  1.000 93.43033 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 20.58769  -2.73906  -7.89632  1.000 86.39233 ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.82632  -4.15712  -5.72957  1.000 67.39188 ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.69643  -2.88931  -5.02345  1.000 60.73054 ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 16.47450  -2.84853  -4.11020  1.000 79.38985 ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 16.01947  -1.76120  -3.74041  1.000 71.97249 ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 17.65003  -1.73021  -6.01879  1.000 49.26519 ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 15.92716  -4.00534  -3.74406  1.000 65.68368 ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 14.86290  -4.09460  -2.76015  1.000 65.32115 ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.53549  -4.59968  -3.29013  1.000 64.87182 ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.71385  -5.08517  -2.49931  1.000 48.62062 ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.28554  -4.50323  -4.59399  1.000 48.10891 ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 12.00122  -4.92348  -5.13479  1.000 49.01730 ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.82527  -6.43596  -4.99789  1.000 46.61045 ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.76727  -7.18087  -4.71187  1.000 47.83006 ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 11.86956  -4.50586  -6.59908  1.000 37.48083 ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.58942  -6.88668  -5.20275  1.000 43.39907 ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 10.25059  -8.30099  -5.16951  1.000 36.55248 ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.54353   -8.67415  -6.46856  1.000 38.33222 ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.27231   -7.82567  -7.32354  1.000 35.79534 ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 9.38860   -8.64049  -3.94709  1.000 42.79529 ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 8.01808   -8.00272  -4.00297  1.000 52.76065 ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 7.92833   -6.76586  -3.85752  1.000 66.71063 ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 7.02898   -8.74236  -4.18622  1.000 57.28837 ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.23580   -9.96550  -6.60694  1.000 32.58779 ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.74912   -10.48983 -7.87943  1.000 31.39370 ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.34563   -9.97582  -8.19421  1.000 34.38013 ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 6.97854   -9.84136  -9.36852  1.000 32.06288 ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.82506   -12.03015 -7.85654  1.000 37.34604 ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.28736  -12.47825 -7.94036  1.000 35.78896 ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.02168   -12.65099 -8.99088  1.000 29.34060 ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.49636  -13.95673 -7.69646  1.000 40.20696 ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.55182   -9.64397  -7.16976  1.000 32.83120 ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.19923   -9.14080  -7.40541  1.000 46.52392 ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.18437   -7.85171  -8.21725  1.000 38.61030 ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.14184   -7.49912  -8.78045  1.000 39.53916 ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.47626   -8.90591  -6.07805  1.000 33.08546 ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.94318   -7.72662  -5.44765  1.000 38.35016 ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.30803   -7.14362  -8.28745  1.000 30.58959 ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.41378   -5.88932  -9.01865  1.000 33.35918 ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.74554   -6.09117  -10.49294 1.000 35.09473 ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 7.01798   -5.11012  -11.19200 1.000 30.05488 ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.47253   -5.00054  -8.36119  1.000 35.59051 ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 7.44168   -5.05715  -6.83852  1.000 47.63064 ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 8.35391   -3.73205  -6.02732  1.000 49.27071 ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 7.89586   -2.32650  -7.03817  1.000 52.93210 ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.70911   -7.33649  -10.97853 1.000 26.48755 ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.16000   -7.64993  -12.33380 1.000 27.23870 ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.35722   -6.89415  -13.38679 1.000 30.86282 ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 6.89644   -6.51726  -14.43539 1.000 25.53851 ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.10067   -9.17527  -12.56380 1.000 31.50033 ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.68252   -9.54169  -13.93202 1.000 28.59738 ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.67192   -9.69428  -12.41610 1.000 26.31991 ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 7.91719   -11.02588 -14.11777 1.000 27.36864 ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.07011   -6.65073  -13.13118 1.000 26.57736 ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.22809   -5.99079  -14.11385 1.000 33.97820 ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.61697   -4.55486  -14.39714 1.000 37.54198 ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.30123   -4.03582  -15.47311 1.000 39.02226 ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.29717   -3.89698  -13.45679 1.000 32.83505 ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.74069   -2.52482  -13.66966 1.000 41.01232 ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.88372   -2.42365  -14.66935 1.000 31.08374 ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.24426   -1.30899  -15.06028 1.000 32.39396 ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.16385   -1.89953  -12.34079 1.000 30.90163 ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.09358   -1.95679  -11.26759 1.000 39.21956 ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 5.56269   -1.37051  -9.95341  1.000 44.76925 ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.30963   -0.39072  -9.92897  1.000 44.65612 ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.12408   -1.96571  -8.84980  1.000 50.78812 ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.45719   -3.54966  -15.08855 1.000 29.90277 ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.55300   -3.56659  -16.04663 1.000 32.33812 ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.15221   -4.19734  -17.37366 1.000 30.26451 ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 9.01547   -4.42927  -18.22552 1.000 28.90126 ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.76237   -4.28604  -15.44335 1.000 23.47327 ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.13122  -3.79039  -14.07173 1.000 29.30070 ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 11.02058  -2.73926  -13.91706 1.000 43.13497 ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 9.57542   -4.36079  -12.93925 1.000 33.27508 ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 11.35589  -2.27317  -12.65770 1.000 43.73177 ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 9.90478   -3.89733  -11.67652 1.000 31.94943 ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 10.79634  -2.85287  -11.53695 1.000 38.23987 ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 6.86486   -4.47744  -17.56799 1.000 25.46163 ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.37152   -4.91470  -18.85816 1.000 22.00036 ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 6.65158   -6.35432  -19.21715 1.000 25.19273 ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 6.50486   -6.72547  -20.38512 1.000 30.23909 ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.04225   -7.18455  -18.25234 1.000 28.16583 ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.35243   -8.58399  -18.52427 1.000 26.45031 ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 6.51053   -9.47690  -17.62192 1.000 25.14395 ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 6.93785   -10.57158 -17.23731 1.000 23.08562 ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 8.85502   -8.86249  -18.33895 1.000 24.08801 ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 9.65400   -8.17827  -19.43058 1.000 26.00827 ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.31825   -8.38940  -16.96942 1.000 25.17455 ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.30138   -9.01917  -17.29082 1.000 25.38645 ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 4.44141   -9.75463  -16.38000 1.000 25.29954 ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 3.97251   -11.09584 -16.90530 1.000 27.99662 ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 3.57893   -11.95705 -16.10978 1.000 22.05985 ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 3.99905   -11.29526 -18.22673 1.000 23.11049 ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 3.58952   -12.58176 -18.78565 1.000 24.60158 ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 4.40384   -13.72677 -18.20189 1.000 22.65007 ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 3.86991   -14.81319 -17.94878 1.000 19.86908 ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 3.72626   -12.57325 -20.30870 1.000 22.83976 ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 3.73993   -13.94891 -20.91840 1.000 26.92837 ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 2.55997   -14.65246 -21.10064 1.000 20.51318 ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 4.93538   -14.54647 -21.29236 1.000 23.24624 ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 2.57034   -15.92373 -21.65357 1.000 19.93649 ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 4.95294   -15.81845 -21.84374 1.000 19.31186 ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 3.76805   -16.50613 -22.02475 1.000 19.80439 ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 5.70014   -13.50279 -17.98346 1.000 21.28970 ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 6.59069   -14.57798 -17.57139 1.000 20.28976 ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 6.36294   -15.01071 -16.13135 1.000 22.94535 ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 6.89745   -16.04808 -15.72487 1.000 23.72383 ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 8.04058   -14.14754 -17.78372 1.000 21.68070 ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 8.34099   -13.86377 -19.23661 1.000 23.13171 ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 8.59671   -14.89712 -20.12923 1.000 23.50789 ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 8.33600   -12.56316 -19.72353 1.000 21.98939 ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 8.85860   -14.64046 -21.46680 1.000 24.72795 ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 8.59846   -12.29627 -21.05700 1.000 32.27395 ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 8.85739   -13.33793 -21.92374 1.000 24.31980 ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 9.11417   -13.07209 -23.25047 1.000 24.97234 ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 5.57686   -14.25625 -15.35887 1.000 22.99643 ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 5.15738   -14.72195 -14.04308 1.000 26.53855 ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 4.27064   -15.95541 -14.12632 1.000 24.52958 ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 4.02382   -16.59138 -13.09559 1.000 22.67553 ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 4.42197   -13.60869 -13.29435 1.000 20.59809 ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 3.14086   -13.38115 -13.85304 1.000 22.69484 ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 3.78255   -16.29987 -15.32261 1.000 23.28441 ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 3.04187   -17.54287 -15.50328 1.000 21.86215 ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 3.84646   -18.74870 -15.04165 1.000 18.68140 ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 3.27377   -19.73360 -14.56134 1.000 23.83950 ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 2.64858   -17.70819 -16.97184 1.000 18.02050 ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 5.17129   -18.68828 -15.16533 1.000 21.88460 ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 6.03145   -19.79583 -14.77515 1.000 23.85612 ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 6.24427   -19.87596 -13.26963 1.000 22.22566 ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 7.05846   -20.68609 -12.81381 1.000 24.88688 ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 7.36888   -19.69744 -15.51191 1.000 23.95269 ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 7.20494   -19.95795 -16.99013 1.000 22.73911 ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 7.23319   -21.25254 -17.49247 1.000 22.46465 ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 6.98290   -18.91358 -17.87856 1.000 17.46213 ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 7.06493   -21.50011 -18.84118 1.000 21.74783 ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 6.81297   -19.15021 -19.23173 1.000 20.12783 ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 6.85497   -20.44560 -19.70639 1.000 24.58303 ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 6.68733   -20.69254 -21.04985 1.000 19.71542 ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 5.53023   -19.05854 -12.49177 1.000 29.30662 ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 5.46847   -19.28899 -11.05406 1.000 26.94452 ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 4.61079   -20.50446 -10.72359 1.000 23.11648 ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 4.80626   -21.13322 -9.67728  1.000 25.95777 ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 4.91940   -18.05374 -10.34060 1.000 23.51012 ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 5.77575   -16.78799 -10.31068 1.000 22.86300 ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 4.94820   -15.59714 -9.85107  1.000 22.37091 ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 6.98182   -16.98248 -9.39981  1.000 22.34514 ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 3.66938   -20.85813 -11.60083 1.000 20.82356 ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 2.68863   -21.89524 -11.29448 1.000 24.70416 ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 2.60357   -22.92917 -12.41140 1.000 25.09243 ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 2.02934   -24.00713 -12.22463 1.000 31.42604 ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 1.30235   -21.27769 -11.02842 1.000 27.69881 ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 1.33550   -20.40222 -9.78157  1.000 28.08053 ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 0.83617   -20.47765 -12.23556 1.000 24.27958 ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 3.16395   -22.61939 -13.57619 1.000 30.16276 ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 3.04564   -23.47729 -14.74886 1.000 24.69603 ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 4.39843   -24.07354 -15.11305 1.000 20.45274 ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 5.40673   -23.36001 -15.15325 1.000 29.62540 ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 2.47872   -22.70091 -15.94003 1.000 21.05896 ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 4.41528   -25.38319 -15.37463 1.000 21.52438 ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 5.59553   -26.03191 -15.93232 1.000 24.65417 ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 5.69509   -25.84477 -17.43689 1.000 28.95370 ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 6.75548   -26.10497 -18.01452 1.000 29.75796 ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 5.58941   -27.53050 -15.61557 1.000 25.56645 ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 4.20413   -28.14980 -15.54821 1.000 40.78579 ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 4.23812   -29.66809 -15.55871 1.000 64.34000 ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 4.99982   -30.25200 -14.75869 1.000 66.95422 ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 3.50625   -30.27689 -16.36948 1.000 73.40891 ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 4.61772   -25.39995 -18.07390 1.000 25.16131 ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 4.55654   -25.24192 -19.51671 1.000 23.76279 ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 3.42069   -24.28373 -19.83255 1.000 21.69631 ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 2.34692   -24.37486 -19.23285 1.000 25.20903 ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 4.33657   -26.59079 -20.20739 1.000 21.51743 ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 4.14178   -26.51108 -21.70686 1.000 25.35350 ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 4.08082   -27.90622 -22.29122 1.000 32.80430 ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 2.79206   -28.11982 -23.05737 1.000 41.42597 ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 2.40877   -29.55826 -23.08198 1.000 40.46354 ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 3.66604   -23.36435 -20.76207 1.000 18.93042 ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 2.68894   -22.35315 -21.14624 1.000 19.08541 ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 2.48405   -22.42181 -22.65189 1.000 26.14569 ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 3.45500   -22.40257 -23.41716 1.000 19.98960 ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 3.13186   -20.93744 -20.72822 1.000 22.49446 ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 2.12076   -19.90137 -21.20441 1.000 19.48642 ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 3.31660   -20.85694 -19.21784 1.000 16.57696 ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 1.22568   -22.50535 -23.07251 1.000 23.82124 ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 0.85262   -22.44966 -24.47878 1.000 25.52983 ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 0.05686   -21.17724 -24.73060 1.000 22.48354 ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? -0.90419  -20.88781 -24.00917 1.000 27.76005 ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? 0.02983   -23.67376 -24.88757 1.000 26.82509 ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 0.70854   -24.86752 -24.48002 1.000 28.42817 ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? -0.17088  -23.69927 -26.39582 1.000 25.87207 ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 0.46083   -20.41971 -25.74539 1.000 20.48222 ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? -0.20468  -19.17843 -26.11951 1.000 21.01190 ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? -0.76759  -19.35914 -27.52147 1.000 23.45836 ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? -0.01036  -19.50799 -28.48952 1.000 26.42772 ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 0.74068   -17.97205 -26.05606 1.000 21.91162 ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? 0.01357   -16.71312 -26.50052 1.000 18.27478 ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 1.28863   -17.80316 -24.64770 1.000 19.03425 ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? -2.09231  -19.35980 -27.63031 1.000 20.15222 ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -2.78427  -19.37310 -28.91297 1.000 22.28016 ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -3.29999  -17.96591 -29.16878 1.000 24.31277 ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -3.94624  -17.36865 -28.29825 1.000 22.76245 ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -3.93686  -20.39103 -28.91927 1.000 26.60191 ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -3.50746  -21.70427 -28.25859 1.000 31.45133 ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -4.41676  -20.63448 -30.34216 1.000 28.78050 ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? -2.84027  -22.67924 -29.19629 1.000 36.28917 ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -3.01477  -17.42699 -30.35189 1.000 22.12616 ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -3.34684  -16.03938 -30.63620 1.000 26.65003 ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -3.77720  -15.88122 -32.08783 1.000 26.37642 ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -3.35378  -16.63331 -32.97066 1.000 25.09265 ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? -2.16358  -15.10632 -30.32104 1.000 24.52496 ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -2.61758  -13.74719 -30.26653 1.000 25.33823 ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? -1.06761  -15.23900 -31.36786 1.000 23.82385 ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -4.64027  -14.89354 -32.31768 1.000 19.26428 ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -5.11020  -14.54788 -33.65377 1.000 19.91876 ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -5.21559  -13.03537 -33.74966 1.000 25.09247 ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -5.98369  -12.41601 -33.00719 1.000 27.05292 ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -6.46165  -15.20134 -33.96302 1.000 21.41972 ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -7.08352  -14.74728 -35.28001 1.000 23.11743 ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -6.37813  -15.35535 -36.48234 1.000 24.76255 ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -7.14374  -15.07874 -37.77009 1.000 25.76287 ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -7.16602  -13.63082 -38.12009 1.000 25.11307 ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -4.44020  -12.44915 -34.65375 1.000 22.53333 ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -4.47345  -11.02454 -34.93938 1.000 25.22126 ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -5.15925  -10.81921 -36.28467 1.000 30.07729 ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -5.09929  -11.68622 -37.16126 1.000 31.60203 ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -3.04979  -10.44649 -34.95164 1.000 25.48393 ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -2.99078  -8.95313  -35.04672 1.000 24.79531 ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -3.19759  -8.26983  -36.22519 1.000 28.62775 ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -2.73010  -8.01243  -34.10810 1.000 25.44107 ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -3.07824  -6.97248  -36.00695 1.000 33.59960 ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -2.79378  -6.78957  -34.73027 1.000 25.47871 ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -5.83277  -9.67433  -36.43888 1.000 26.47248 ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -6.57149  -9.41891  -37.67427 1.000 28.12973 ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -5.67609  -9.49764  -38.90535 1.000 28.21828 ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -6.14886  -9.84853  -39.99228 1.000 29.86205 ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -7.25679  -8.05242  -37.61650 1.000 27.94837 ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -8.50843  -8.05975  -36.76261 1.000 32.97080 ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -9.13878  -9.09885  -36.56968 1.000 36.27377 ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -8.88497  -6.88959  -36.25841 1.000 28.03232 ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -4.38932  -9.19001  -38.75839 1.000 27.18093 ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -3.46837  -9.11188  -39.88338 1.000 29.70633 ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? -2.63959  -10.37714 -40.07101 1.000 31.84556 ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? -1.65362  -10.34947 -40.81462 1.000 38.66685 ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? -2.53684  -7.91035  -39.71188 1.000 31.83999 ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -3.28026  -6.59092  -39.72180 1.000 37.30830 ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -4.39908  -6.54061  -40.27510 1.000 40.96697 ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -2.74859  -5.60564  -39.16938 1.000 38.24121 ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? -3.00557  -11.48027 -39.42405 1.000 26.86245 ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? -2.20539  -12.69611 -39.50873 1.000 27.44241 ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? -3.10344  -13.89778 -39.23867 1.000 34.34089 ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -4.29261  -13.75758 -38.94071 1.000 32.64986 ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? -1.02344  -12.64178 -38.53441 1.000 28.43862 ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 0.18434   -13.40591 -39.03906 1.000 36.89690 ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 0.03087   -14.20304 -39.98907 1.000 30.02863 ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 1.28916   -13.20450 -38.49146 1.000 36.49325 ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? -2.51935  -15.08886 -39.35376 1.000 31.56862 ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? -3.22195  -16.33301 -39.08910 1.000 33.89385 ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? -3.09451  -16.70962 -37.61353 1.000 30.10060 ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? -2.41580  -16.04420 -36.82753 1.000 23.99325 ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? -2.68889  -17.44886 -39.98846 1.000 38.32156 ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? -2.47283  -17.04428 -41.44115 1.000 48.24136 ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? -3.70084  -16.40453 -42.06574 1.000 76.31264 ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? -4.82950  -16.84692 -41.76064 1.000 84.70813 ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? -3.53886  -15.45477 -42.86031 1.000 87.90872 ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -3.75852  -17.79768 -37.23361 1.000 24.35583 ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -3.71956  -18.27816 -35.85975 1.000 29.49466 ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? -2.44614  -19.08316 -35.62652 1.000 26.82832 ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? -2.16207  -20.03645 -36.35955 1.000 24.32984 ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -4.95164  -19.13223 -35.56681 1.000 28.72318 ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -5.21067  -19.38570 -34.09203 1.000 25.16607 ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -6.64339  -19.80432 -33.82615 1.000 32.28592 ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -7.58210  -19.07759 -34.14907 1.000 30.21772 ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -6.81883  -20.98030 -33.23529 1.000 36.39035 ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? -1.67971  -18.69893 -34.60700 1.000 21.46618 ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? -0.41857  -19.35142 -34.28724 1.000 22.83175 ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? -0.41003  -19.83136 -32.84390 1.000 26.89828 ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? -1.11043  -19.28813 -31.98463 1.000 24.45276 ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 0.77527   -18.41701 -34.51993 1.000 27.49521 ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 1.10907   -18.21655 -35.97811 1.000 30.19619 ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 0.47538   -17.23695 -36.72888 1.000 27.43603 ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 2.05014   -19.01962 -36.60759 1.000 28.18348 ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 0.77650   -17.05727 -38.06781 1.000 32.27827 ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 2.35692   -18.84951 -37.94229 1.000 33.93052 ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 1.71860   -17.86644 -38.66769 1.000 41.13420 ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 2.02474   -17.69450 -39.99835 1.000 58.95057 ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 0.40332   -20.85411 -32.58886 1.000 21.10701 ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 0.54365   -21.45277 -31.26777 1.000 21.35317 ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 1.98486   -21.30149 -30.80343 1.000 33.30353 ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 2.90920   -21.79745 -31.45828 1.000 22.19637 ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 0.13613   -22.92752 -31.28405 1.000 28.74808 ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 2.16776   -20.61524 -29.68035 1.000 19.90484 ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 3.45989   -20.45860 -29.02867 1.000 18.58525 ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 3.50013   -21.37063 -27.80931 1.000 24.46054 ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 2.49996   -21.50994 -27.09929 1.000 25.81063 ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 3.66462   -18.99090 -28.63441 1.000 20.72855 ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 4.91616   -18.64234 -27.87290 1.000 23.54582 ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 6.01009   -17.98843 -28.36274 1.000 19.66827 ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 5.16958   -18.85049 -26.47415 1.000 25.29037 ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 6.94030   -17.80912 -27.36939 1.000 25.94732 ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 6.44929   -18.32800 -26.20064 1.000 23.76307 ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 4.44632   -19.44147 -25.43223 1.000 21.83921 ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 7.02134   -18.38033 -24.93233 1.000 21.74576 ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 5.01709   -19.49379 -24.17438 1.000 19.78221 ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 6.28983   -18.96470 -23.93460 1.000 20.58433 ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 4.64743   -22.00646 -27.57486 1.000 18.21171 ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 4.75794   -22.94950 -26.46932 1.000 19.13194 ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 6.17393   -22.95337 -25.91527 1.000 23.97711 ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 7.14300   -22.84601 -26.66998 1.000 21.11066 ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 4.37572   -24.36845 -26.90125 1.000 24.08521 ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 3.88590   -25.23780 -25.75756 1.000 35.77273 ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 3.28152   -26.54185 -26.23475 1.000 55.43303 ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 3.99289   -27.31438 -26.91100 1.000 47.96221 ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 2.09313   -26.79055 -25.93964 1.000 46.63084 ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 6.28458   -23.09737 -24.59513 1.000 22.50902 ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 7.58951   -23.20304 -23.95578 1.000 23.71967 ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 7.44051   -23.85449 -22.59037 1.000 20.13115 ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 6.54786   -23.49010 -21.81778 1.000 22.79231 ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 8.25231   -21.82968 -23.80969 1.000 19.83665 ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 9.54229   -21.95764 -23.23610 1.000 22.16129 ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 8.31608   -24.81853 -22.30428 1.000 22.99094 ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 8.50970   -25.35001 -20.96198 1.000 20.28194 ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 9.75563   -24.76784 -20.30651 1.000 25.53959 ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 10.41210  -25.44340 -19.50581 1.000 25.84798 ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 8.59156   -26.87564 -20.99663 1.000 27.09015 ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 7.38021   -27.44498 -21.46124 1.000 27.16683 ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 10.08806  -23.52637 -20.64223 1.000 26.98411 ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 11.33019  -22.85287 -20.22885 1.000 29.53240 ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 12.49112  -23.64563 -20.83602 1.000 29.29793 ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 12.38482  -24.11284 -21.98039 1.000 33.60688 ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 11.37502  -22.68776 -18.72414 1.000 29.68443 ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 13.59917  -23.81461 -20.11929 1.000 25.86125 ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 14.72809  -24.52641 -20.68098 1.000 25.58729 ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 15.43683  -23.81742 -21.81095 1.000 28.78197 ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 16.23724  -24.44524 -22.51034 1.000 29.17326 ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 15.15665  -22.53380 -22.02564 1.000 22.00485 ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 15.89110  -21.73330 -22.98088 1.000 27.32703 ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 15.35594  -21.72390 -24.39671 1.000 26.91833 ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 15.99115  -21.12079 -25.27186 1.000 22.78575 ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 14.21434  -22.35772 -24.65982 1.000 23.05512 ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 13.68944  -22.41404 -26.01566 1.000 22.23710 ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 12.16866  -22.36289 -25.99776 1.000 27.44589 ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 11.52147  -22.71491 -25.00835 1.000 20.17545 ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 14.15821  -23.67698 -26.75249 1.000 23.45462 ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 13.54355  -24.83605 -26.21958 1.000 26.42915 ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 11.60594  -21.90981 -27.11745 1.000 22.50709 ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 10.17060  -21.96045 -27.34813 1.000 20.52215 ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 9.92538   -22.37995 -28.79032 1.000 26.20956 ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 10.81284  -22.29276 -29.64250 1.000 23.99930 ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 9.48667   -20.61430 -27.05648 1.000 22.08354 ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 9.94651   -19.48331 -27.94006 1.000 24.72285 ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 11.06136  -18.73161 -27.60750 1.000 24.33983 ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 9.24643   -19.15720 -29.09192 1.000 24.15726 ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 11.47769  -17.68584 -28.41230 1.000 28.59595 ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 9.65737   -18.11315 -29.89985 1.000 19.32046 ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 10.77270  -17.37329 -29.55708 1.000 23.82677 ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 8.70880   -22.84637 -29.05712 1.000 20.57487 ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 8.31108   -23.24742 -30.39672 1.000 21.60147 ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 7.13980   -22.40022 -30.87099 1.000 20.93318 ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 6.34600   -21.89755 -30.06842 1.000 25.92041 ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 7.92506   -24.73355 -30.46328 1.000 22.78820 ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 6.71467   -24.95033 -29.72734 1.000 22.94027 ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 9.03778   -25.60866 -29.89791 1.000 23.57901 ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 7.04818   -22.24245 -32.18926 1.000 24.68977 ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 5.94454   -21.54499 -32.83571 1.000 25.45394 ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 5.47563   -22.39772 -34.00443 1.000 30.48154 ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 6.29315   -22.85175 -34.81296 1.000 25.95591 ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 6.35126   -20.13869 -33.31955 1.000 21.38390 ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 5.21881   -19.50191 -34.11378 1.000 23.46334 ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 6.74499   -19.25322 -32.14223 1.000 19.97765 ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 4.16742   -22.62567 -34.08620 1.000 23.31248 ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 3.58476   -23.37371 -35.18872 1.000 30.15903 ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 2.23360   -22.77349 -35.54144 1.000 27.80927 ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 1.60210   -22.08925 -34.73198 1.000 23.50877 ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 3.41030   -24.86139 -34.85279 1.000 28.62012 ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 2.41795   -25.12380 -33.72853 1.000 35.40620 ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 2.60744   -26.50195 -33.11157 1.000 34.01643 ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 3.52783   -26.48295 -31.98071 1.000 40.93871 ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 4.16152   -27.55045 -31.51425 1.000 49.62421 ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 3.98451   -28.74772 -32.04884 1.000 46.89980 ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 4.99257   -27.41358 -30.48487 1.000 57.44877 ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 1.79831   -23.03705 -36.77009 1.000 26.60338 ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 0.43621   -22.70577 -37.15969 1.000 33.91592 ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? -0.54033  -23.54605 -36.34869 1.000 32.17898 ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? -0.39479  -24.76798 -36.25184 1.000 39.84162 ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 0.23627   -22.94927 -38.65613 1.000 34.74100 ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 0.97944   -21.97747 -39.40235 1.000 32.13713 ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? -1.23460  -22.84362 -39.02350 1.000 46.95933 ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? -1.52664  -22.88798 -35.74848 1.000 26.93071 ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? -2.49624  -23.58353 -34.91348 1.000 33.11223 ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? -3.60036  -24.16769 -35.78598 1.000 46.96915 ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -4.29681  -23.43263 -36.49480 1.000 44.35886 ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? -3.08200  -22.63967 -33.86723 1.000 29.83634 ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -3.97878  -23.35713 -32.87917 1.000 42.06753 ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -3.57224  -24.42393 -32.37364 1.000 50.20879 ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -5.09434  -22.86183 -32.61786 1.000 45.88877 ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? -3.75223  -25.48776 -35.74068 1.000 46.18646 ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -4.83997  -26.17110 -36.42475 1.000 69.95501 ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -6.03611  -26.41291 -35.51706 1.000 61.49533 ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -7.00406  -27.05018 -35.94555 1.000 62.69793 ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -4.35433  -27.50752 -36.99638 1.000 78.79981 ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? -3.45173  -28.12733 -36.07055 1.000 64.54867 ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? -3.64619  -27.29133 -38.32600 1.000 53.15996 ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -5.99264  -25.91895 -34.28218 1.000 64.73532 ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -7.06745  -26.13357 -33.33517 1.000 62.01996 ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -8.29903  -25.29305 -33.60386 1.000 53.68478 ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -8.53326  -24.85757 -34.73565 1.000 46.16473 ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -9.08546  -25.05644 -32.56291 1.000 52.97534 ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -10.35326 -24.34785 -32.69557 1.000 47.15892 ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -10.11349 -22.89230 -33.07847 1.000 35.84145 ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -9.37649  -22.19163 -32.37264 1.000 33.17297 ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -11.13099 -24.43599 -31.38309 1.000 46.86778 ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -12.62880 -24.24241 -31.52558 1.000 51.16961 ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -13.24965 -25.21812 -32.50570 1.000 58.65374 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -13.02380 -26.43738 -32.35799 1.000 53.49799 ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -13.96306 -24.76424 -33.42389 1.000 56.70817 ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -10.68240 -22.40597 -34.18317 1.000 42.89607 ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -10.49441 -20.99480 -34.55188 1.000 37.37102 ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -11.00570 -20.05863 -33.46538 1.000 40.61481 ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -12.01717 -20.32579 -32.81357 1.000 49.37903 ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -11.30660 -20.84096 -35.84474 1.000 33.96974 ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -11.73165 -22.20612 -36.25834 1.000 48.84061 ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -11.25803 -23.21557 -35.26966 1.000 47.75732 ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -10.29521 -18.94161 -33.28216 1.000 36.37176 ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -10.61054 -17.98522 -32.22926 1.000 37.34411 ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -11.27677 -16.70917 -32.71963 1.000 36.95991 ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -11.87441 -15.99755 -31.90624 1.000 49.65137 ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -9.34015  -17.59147 -31.46231 1.000 38.31799 ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -8.46065  -18.75257 -31.05746 1.000 61.19215 ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -7.01961  -18.19123 -30.13579 1.000 65.26353 ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -7.73666  -16.90546 -29.11820 1.000 38.72748 ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -11.18083 -16.39290 -34.00724 1.000 29.99575 ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -11.69902 -15.13331 -34.50357 1.000 34.51398 ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -10.72321 -13.99711 -34.28018 1.000 28.31920 ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -10.16170 -13.45454 -35.23684 1.000 30.58464 ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -10.51205 -13.63355 -33.01598 1.000 24.11838 ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -9.52462  -12.63077 -32.64143 1.000 25.09637 ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -9.30290  -12.70582 -31.13902 1.000 29.62733 ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -10.25548 -12.89008 -30.37770 1.000 28.92301 ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -9.97218  -11.21517 -33.03287 1.000 21.53708 ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -8.88490  -10.16275 -32.85129 1.000 22.74381 ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -9.45699  -8.76008  -32.70046 1.000 21.14699 ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -10.35682 -8.65272  -31.55765 1.000 20.99985 ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -11.67645 -8.55333  -31.64597 1.000 24.68780 ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -12.29232 -8.52992  -32.81737 1.000 24.26962 ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -12.39678 -8.47096  -30.53085 1.000 21.97724 ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -8.04988  -12.56169 -30.72068 1.000 24.01424 ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -7.71118  -12.53654 -29.31751 1.000 21.25269 ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -6.56126  -13.46238 -29.01227 1.000 27.41211 ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -5.84767  -13.93307 -29.90552 1.000 26.43813 ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -6.37526  -13.73131 -27.72271 1.000 24.66936 ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -5.25432  -14.53109 -27.25715 1.000 20.72984 ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -5.72582  -15.46730 -26.15548 1.000 32.60388 ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -6.59222  -15.11124 -25.34954 1.000 23.81134 ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -4.10793  -13.63945 -26.75259 1.000 23.36581 ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -3.63130  -12.82706 -27.83097 1.000 23.96257 ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -2.95169  -14.47979 -26.23649 1.000 24.50757 ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -5.15241  -16.66834 -26.13887 1.000 20.71505 ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -5.47599  -17.70239 -25.16611 1.000 22.56354 ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -4.18313  -18.16603 -24.51210 1.000 23.29732 ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -3.28182  -18.65553 -25.19999 1.000 23.73888 ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -6.19477  -18.86659 -25.85249 1.000 32.22297 ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -6.34431  -20.11386 -25.01122 1.000 42.88752 ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -6.82928  -21.32950 -25.81585 1.000 54.89205 ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -7.83260  -21.01924 -26.93787 1.000 47.21157 ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -8.86411  -19.97400 -26.64631 1.000 57.59896 ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -4.08412  -18.00197 -23.19556 1.000 22.21429 ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -2.90795  -18.41678 -22.43739 1.000 17.82193 ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -3.28397  -19.66294 -21.64756 1.000 25.19491 ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -4.07723  -19.59574 -20.70015 1.000 19.48359 ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -2.39436  -17.30559 -21.51169 1.000 17.38764 ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? -1.19578  -17.80012 -20.70964 1.000 15.69760 ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -2.02478  -16.07303 -22.31627 1.000 19.74874 ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -2.71646  -20.80111 -22.03399 1.000 21.71792 ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -2.98632  -22.07979 -21.38751 1.000 20.19738 ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? -1.84390  -22.37677 -20.42802 1.000 24.21238 ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? -0.69557  -22.55405 -20.85285 1.000 20.61507 ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -3.14864  -23.20836 -22.41683 1.000 20.34099 ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -4.23410  -22.85070 -23.43291 1.000 20.81952 ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -3.46871  -24.52389 -21.71874 1.000 20.98826 ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -4.16702  -23.66718 -24.70455 1.000 28.58695 ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -2.15631  -22.43244 -19.13581 1.000 18.35357 ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? -1.17315  -22.71567 -18.09628 1.000 21.26110 ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? -1.28120  -24.18358 -17.70483 1.000 22.03994 ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -2.25679  -24.59025 -17.06850 1.000 23.79772 ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? -1.38876  -21.81922 -16.87933 1.000 18.72802 ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? -1.46421  -20.31329 -17.11663 1.000 24.83342 ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -1.68547  -19.59413 -15.80168 1.000 23.80278 ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? -0.19653  -19.82560 -17.78794 1.000 23.19332 ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? -0.28023  -24.97484 -18.07973 1.000 20.40484 ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? -0.18047  -26.35911 -17.62192 1.000 23.71764 ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 0.46826   -26.33636 -16.24366 1.000 21.43245 ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 1.68907   -26.21998 -16.11678 1.000 23.57564 ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 0.60097   -27.20506 -18.62165 1.000 20.54917 ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 0.19664   -26.98060 -20.04764 1.000 27.78444 ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? -0.50524  -27.91628 -20.77719 1.000 30.54314 ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 0.39677   -25.93018 -20.87945 1.000 26.20502 ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? -0.72306  -27.45060 -21.99439 1.000 33.84608 ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? -0.18592  -26.24705 -22.08244 1.000 31.07240 ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? -0.35846  -26.44330 -15.20655 1.000 22.39750 ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 0.06632   -26.11628 -13.85278 1.000 24.58062 ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 1.00940   -27.16774 -13.28061 1.000 24.46983 ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 0.94704   -28.35166 -13.62405 1.000 28.51883 ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? -1.14879  -25.97084 -12.93681 1.000 23.29629 ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -2.07217  -24.78428 -13.21485 1.000 24.80646 ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -3.22588  -24.76737 -12.23037 1.000 20.94227 ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? -1.29632  -23.48082 -13.15153 1.000 24.47756 ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 1.88852   -26.71340 -12.38898 1.000 26.33375 ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 2.73718   -27.61700 -11.63027 1.000 35.74335 ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 1.88305   -28.51625 -10.74104 1.000 31.34446 ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 0.74724   -28.18877 -10.38723 1.000 34.44658 ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 3.73261   -26.83041 -10.77664 1.000 33.96281 ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 4.87552   -26.19727 -11.55533 1.000 31.66640 ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 5.44494   -25.00059 -10.80516 1.000 42.13619 ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 6.57984   -24.34420 -11.57375 1.000 47.12783 ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 7.19728   -23.22197 -10.80849 1.000 57.49558 ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 2.45505   -29.66507 -10.37185 1.000 35.58941 ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 1.70618   -30.66175 -9.61291  1.000 36.22633 ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 1.21960   -30.11724 -8.27546  1.000 34.39450 ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 0.14745   -30.50965 -7.80092  1.000 44.18177 ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 2.56920   -31.90518 -9.39681  1.000 47.85304 ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 1.83614   -33.07711 -8.76922  1.000 60.46440 ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 2.61887   -34.37215 -8.87034  1.000 85.86113 ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 2.93932   -34.78665 -10.00454 1.000 94.08140 ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 2.91597   -34.97404 -7.81671  1.000 84.34105 ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 1.98018   -29.21446 -7.65604  1.000 33.17900 ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 1.64405   -28.68499 -6.34164  1.000 35.42560 ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 0.97074   -27.31718 -6.41011  1.000 28.83398 ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 0.92610   -26.60633 -5.40082  1.000 34.04718 ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 2.89651   -28.61447 -5.46435  1.000 34.28655 ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 3.99716   -27.76925 -6.07895  1.000 50.19440 ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 3.87555   -27.39564 -7.26462  1.000 53.68822 ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 4.98758   -27.47790 -5.37428  1.000 53.94579 ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 0.44215   -26.93403 -7.57266  1.000 26.77586 ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? -0.17996  -25.62686 -7.74732  1.000 24.09927 ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -1.61164  -25.74608 -8.25922  1.000 23.52988 ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -2.13044  -24.82370 -8.89035  1.000 27.49476 ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 0.65159   -24.75353 -8.68672  1.000 25.09357 ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 2.09137   -24.55713 -8.23742  1.000 27.38577 ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 2.20019   -23.76418 -6.94965  1.000 28.38407 ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 1.41561   -22.84825 -6.70070  1.000 31.56443 ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 3.17567   -24.11647 -6.12028  1.000 30.56846 ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -2.26519  -26.87348 -7.98731  1.000 27.00073 ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -3.62385  -27.10205 -8.46413  1.000 34.91036 ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -4.67400  -26.31916 -7.68493  1.000 29.36293 ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -5.86147  -26.41744 -8.01337  1.000 34.48553 ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -3.95712  -28.59566 -8.41376  1.000 31.72680 ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -3.90146  -29.05532 -7.05701  1.000 31.79323 ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -2.97054  -29.39114 -9.26141  1.000 34.10216 ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -4.27477  -25.55165 -6.66661  1.000 27.91016 ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -5.23411  -24.71025 -5.95804  1.000 34.74866 ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -5.82348  -23.64613 -6.87310  1.000 24.45994 ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -6.95208  -23.19065 -6.65299  1.000 27.45505 ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -4.56881  -24.05622 -4.74608  1.000 30.06058 ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -3.59745  -22.93881 -5.10075  1.000 25.73571 ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.82405  -22.42922 -3.90157  1.000 36.89927 ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -1.86131  -23.10478 -3.48330  1.000 38.00525 ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -3.17596  -21.34874 -3.38081  1.000 36.40532 ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -5.08359  -23.24408 -7.90278  1.000 27.74876 ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -5.54304  -22.23801 -8.84852  1.000 29.19336 ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -6.49762  -22.80739 -9.88865  1.000 28.14862 ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -6.83270  -22.11353 -10.85463 1.000 28.27980 ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -4.33495  -21.57193 -9.51067  1.000 23.35330 ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -3.41161  -20.95333 -8.48599  1.000 20.08288 ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -3.81717  -19.85664 -7.73848  1.000 22.35611 ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -2.15429  -21.48779 -8.23508  1.000 20.41010 ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.99102  -19.29497 -6.78571  1.000 22.11908 ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -1.31763  -20.92961 -7.28076  1.000 27.05015 ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -1.74384  -19.83157 -6.56069  1.000 25.20971 ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.92628  -19.26517 -5.60901  1.000 30.01189 ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -6.93151  -24.05500 -9.70710  1.000 25.44689 ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -8.05025  -24.62314 -10.44218 1.000 25.11028 ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -9.34350  -24.61000 -9.63923  1.000 28.02157 ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -10.40082 -24.92094 -10.19452 1.000 27.84974 ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -7.73771  -26.06551 -10.86387 1.000 23.56570 ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -6.53748  -26.28544 -11.78316 1.000 24.23723 ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -6.36393  -27.76339 -12.08931 1.000 31.60498 ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -6.71020  -25.49098 -13.06425 1.000 30.08943 ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -9.28420  -24.26666 -8.35518  1.000 25.10899 ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -10.45884 -24.25498 -7.49573  1.000 27.89508 ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -11.20139 -22.93369 -7.63938  1.000 31.32456 ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -10.58608 -21.86409 -7.69824  1.000 27.03239 ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -10.05884 -24.48225 -6.03701  1.000 30.27496 ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -9.25576  -25.75400 -5.80944  1.000 38.56427 ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -8.93993  -25.99467 -4.34507  1.000 68.87751 ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -9.50711  -25.28624 -3.48595  1.000 81.80898 ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -8.12107  -26.89211 -4.05269  1.000 69.99284 ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -12.53338 -23.01920 -7.68443  1.000 26.09140 ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -13.35148 -21.84286 -7.96449  1.000 28.37097 ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -13.15307 -20.75810 -6.91224  1.000 27.64017 ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.95476 -19.58475 -7.24664  1.000 25.87529 ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -14.82681 -22.23425 -8.04624  1.000 30.47069 ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -15.74269 -21.06489 -8.37357  1.000 45.83592 ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -17.20104 -21.46500 -8.46995  1.000 72.27673 ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -17.57404 -22.50232 -7.88339  1.000 50.46434 ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -17.97424 -20.74355 -9.13470  1.000 73.09671 ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -13.21224 -21.12887 -5.63006  1.000 29.79871 ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -13.17165 -20.11574 -4.58021  1.000 32.42586 ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.80343 -19.45393 -4.48539  1.000 30.21092 ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.70595 -18.29658 -4.06007  1.000 29.12506 ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.55627 -20.72416 -3.23226  1.000 31.84541 ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.69881 -21.89227 -2.78946  1.000 38.41810 ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -13.11104 -22.34887 -1.39572  1.000 46.18953 ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -12.20188 -23.34819 -0.84829  1.000 46.90638 ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.27832 -23.83229 0.38381   1.000 49.37385 ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.22597 -23.44340 1.22174   1.000 43.29555 ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.38092 -24.72760 0.78601   1.000 52.34923 ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.74086 -20.16379 -4.87139  1.000 23.51499 ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -9.41400  -19.55860 -4.85816  1.000 25.26788 ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -9.25485  -18.56748 -6.00456  1.000 23.30653 ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.66302  -17.49628 -5.82886  1.000 25.29677 ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -8.34153  -20.64666 -4.92443  1.000 28.84677 ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.91091  -20.12545 -4.97888  1.000 28.79650 ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.43728  -19.67054 -3.60422  1.000 26.32222 ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -5.00701  -19.38827 -3.57868  1.000 25.14354 ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.47940  -18.19641 -3.33430  1.000 29.81446 ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.23890  -17.13766 -3.10701  1.000 21.52109 ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -3.15573  -18.06391 -3.31808  1.000 26.65505 ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.78370  -18.90303 -7.18388  1.000 23.81435 ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -9.71295  -17.98343 -8.31615  1.000 22.04326 ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -10.54750 -16.73672 -8.04807  1.000 26.35324 ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -10.10794 -15.61281 -8.32103  1.000 23.48977 ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -10.15163 -18.68764 -9.61343  1.000 26.25051 ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -9.22715  -19.86673 -9.92588  1.000 22.68249 ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -10.16462 -17.70728 -10.77652 1.000 21.34904 ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -9.79866  -20.82538 -10.94905 1.000 31.61190 ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.76252 -16.91108 -7.51342  1.000 27.32944 ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.59997 -15.75738 -7.19095  1.000 26.26700 ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.91014 -14.83909 -6.19239  1.000 27.80284 ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.96456 -13.61011 -6.32540  1.000 29.08699 ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.95116 -16.20607 -6.63025  1.000 25.06665 ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.84792 -16.93888 -7.60732  1.000 37.55906 ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -16.20752 -17.21580 -6.98085  1.000 43.49773 ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -16.16213 -18.41357 -6.04727  1.000 59.44175 ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -17.44611 -19.16986 -6.04916  1.000 65.95490 ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -11.26326 -15.42119 -5.17905  1.000 22.29941 ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.55541 -14.62106 -4.18575  1.000 25.05725 ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.45397  -13.78835 -4.82881  1.000 22.43782 ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.27806  -12.61106 -4.49381  1.000 22.99718 ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.97568  -15.53302 -3.10386  1.000 26.14168 ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -9.04993  -14.83576 -2.12377  1.000 28.50618 ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.33996  -15.81249 -1.20877  1.000 29.62460 ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.81644  -16.82500 -1.71879  1.000 26.25499 ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.30482  -15.56975 0.01659   1.000 28.40394 ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.70562  -14.38232 -5.75932  1.000 21.73220 ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.59645  -13.67401 -6.39036  1.000 25.72322 ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -8.11013  -12.56723 -7.30371  1.000 24.26610 ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.57128  -11.45349 -7.31405  1.000 25.08475 ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.70161  -14.66931 -7.14962  1.000 22.29041 ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -6.04465  -15.64641 -6.17411  1.000 25.76342 ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.65322  -13.93925 -7.95497  1.000 24.51341 ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -5.52933  -16.89527 -6.83744  1.000 30.60784 ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -9.15661  -12.85203 -8.08229  1.000 20.76097 ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.70850  -11.84706 -8.98758  1.000 19.92579 ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.24341 -10.65660 -8.20147  1.000 23.09125 ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -9.99507  -9.49657  -8.55387  1.000 31.14770 ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.79571 -12.47652 -9.87866  1.000 23.41351 ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.62906 -11.39522 -10.55668 1.000 18.71822 ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -10.16615 -13.40349 -10.90695 1.000 20.25175 ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.97944 -10.92369 -7.12088  1.000 22.56532 ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.52115 -9.84399  -6.30264  1.000 25.58537 ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.41481 -9.04814  -5.61992  1.000 29.11742 ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.55415 -7.83582  -5.42445  1.000 30.30548 ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.49134 -10.42156 -5.26959  1.000 25.13519 ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -12.93129 -9.45433  -4.18230  1.000 32.90969 ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -13.84177 -10.14417 -3.17729  1.000 35.12400 ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -14.48862 -9.14527  -2.23235  1.000 36.67420 ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -15.47286 -9.79979  -1.32552  1.000 48.22300 ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.30403  -9.70285  -5.27798  1.000 30.33753 ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.23003  -9.04066  -4.54554  1.000 31.78367 ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.38139  -8.15177  -5.44964  1.000 28.70141 ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.00401  -7.04324  -5.05403  1.000 27.02539 ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.35409  -10.09002 -3.85763  1.000 28.81821 ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.06556  -9.55390  -3.25000  1.000 37.73942 ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.39098  -10.61726 -2.39591  1.000 42.78805 ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.42852  -10.00555 -1.38990  1.000 60.84083 ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.28631  -10.91810 -1.09677  1.000 63.47570 ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.07919  -8.60882  -6.66548  1.000 24.93789 ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.09589  -7.94617  -7.50959  1.000 31.56674 ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.64367  -7.39137  -8.81754  1.000 32.51954 ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -5.93560  -6.62343  -9.47915  1.000 32.94999 ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -4.94529  -8.91165  -7.83700  1.000 34.02622 ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.15561  -9.34037  -6.64007  1.000 33.11033 ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.33472  -8.48058  -5.94223  1.000 31.68982 ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -4.06161  -10.53897 -6.01689  1.000 34.86950 ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.76818  -9.13117  -4.94144  1.000 42.16350 ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.19302  -10.38173 -4.96391  1.000 33.45752 ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.86674  -7.74647  -9.21525  1.000 29.72506 ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.38226  -7.36406  -10.52523 1.000 27.81537 ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.77532  -6.75203  -10.42902 1.000 32.95050 ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.57798 -6.88005  -11.35665 1.000 28.76308 ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.39714  -8.56558  -11.47056 1.000 30.48272 ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -7.12248  -9.18480  -11.52676 1.000 35.39263 ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.07702 -6.07095  -9.32138  1.000 30.76969 ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.43005 -5.56366  -9.12069  1.000 46.71356 ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.75284 -4.37040  -10.01248 1.000 42.92490 ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -12.93369 -4.05973  -10.20029 1.000 40.73183 ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -11.64662 -5.18718  -7.65200  1.000 37.27690 ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -10.75976 -4.06286  -7.13848  1.000 58.48310 ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -9.41860  -4.54659  -6.61342  1.000 69.33017 ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -8.80406  -5.45326  -7.17680  1.000 49.40356 ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -8.95877  -3.93905  -5.52427  1.000 63.29500 ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.74352 -3.69795  -10.56915 1.000 36.53422 ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -10.96353 -2.51425  -11.39276 1.000 38.93081 ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.63479 -2.74722  -12.86488 1.000 33.10693 ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.33007 -1.79188  -13.58547 1.000 43.95854 ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.15772 -1.33033  -10.85653 1.000 36.63630 ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.59697 -0.86555  -9.49807  1.000 54.42305 ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -9.76264  -1.00334  -8.40086  1.000 45.77965 ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -11.84997 -0.30535  -9.31485  1.000 52.16950 ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -10.16648 -0.57881  -7.14740  1.000 63.66172 ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -12.26035 0.11865   -8.06475  1.000 44.93986 ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.41726 -0.01865  -6.97956  1.000 47.24911 ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.69065 -3.98951  -13.32897 1.000 32.49597 ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.50368 -4.27352  -14.74731 1.000 26.78813 ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.79519 -3.93893  -15.48162 1.000 30.15131 ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.88004 -4.38562  -15.09026 1.000 31.24107 ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -10.09430 -5.73853  -14.96231 1.000 28.00184 ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.73709  -6.01140  -14.30726 1.000 25.57815 ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -10.03710 -6.06572  -16.44646 1.000 29.58230 ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.58352  -5.27047  -14.95181 1.000 26.43154 ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.68450 -3.14373  -16.54314 1.000 26.53544 ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.85445 -2.60508  -17.21102 1.000 27.96134 ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -13.49721 -3.52024  -18.23343 1.000 30.97642 ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -14.09756 -3.04890  -19.20360 1.000 30.51567 ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -13.39086 -4.82746  -18.02861 1.000 29.43421 ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -13.96890 -5.80470  -18.93542 1.000 32.15210 ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -14.55701 -6.94455  -18.12022 1.000 21.34463 ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -14.05116 -7.25864  -17.03642 1.000 30.27526 ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.92040 -6.34720  -19.91944 1.000 19.38855 ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -12.33276 -5.27900  -20.81183 1.000 26.61473 ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -13.00386 -4.84954  -21.94904 1.000 24.12250 ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -11.11212 -4.68924  -20.50844 1.000 24.35189 ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -12.47077 -3.86819  -22.76518 1.000 24.23368 ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -10.57138 -3.70650  -21.31689 1.000 25.91199 ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -11.25613 -3.29938  -22.44339 1.000 23.80974 ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -10.72476 -2.32248  -23.25285 1.000 27.15271 ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -15.62720 -7.57329  -18.60659 1.000 25.65276 ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -16.24027 -8.66975  -17.84178 1.000 28.38060 ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -15.30220 -9.86504  -17.75248 1.000 30.86553 ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -14.82306 -10.37705 -18.76718 1.000 30.77318 ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -17.50914 -9.00562  -18.63541 1.000 28.83121 ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -17.31991 -8.40810  -19.98356 1.000 33.51431 ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -16.34007 -7.28289  -19.86364 1.000 31.05614 ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -15.03420 -10.29714 -16.52494 1.000 26.86341 ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -14.21624 -11.47283 -16.25593 1.000 22.30468 ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -15.16253 -12.58833 -15.84101 1.000 26.88721 ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -15.79824 -12.51449 -14.78233 1.000 26.99396 ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -13.16010 -11.20803 -15.17492 1.000 24.60415 ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -12.24828 -10.04908 -15.58446 1.000 21.98450 ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -12.34443 -12.46409 -14.91542 1.000 26.93113 ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -11.32327 -9.58626  -14.48088 1.000 23.56093 ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -15.26427 -13.61918 -16.67213 1.000 22.56958 ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -16.15608 -14.74450 -16.42631 1.000 22.68148 ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -15.32638 -15.94748 -16.00411 1.000 20.86964 ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -14.46071 -16.40526 -16.75811 1.000 20.48311 ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -16.98323 -15.07573 -17.66828 1.000 25.47382 ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -17.73145 -13.92057 -18.06446 1.000 25.30380 ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -17.94269 -16.22620 -17.38061 1.000 21.85002 ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -15.58826 -16.45208 -14.80232 1.000 21.10712 ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -14.94250 -17.66323 -14.31000 1.000 25.03813 ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -15.83201 -18.85397 -14.65082 1.000 29.38007 ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -16.92123 -19.00711 -14.08817 1.000 23.05462 ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -14.68957 -17.57111 -12.80718 1.000 22.92719 ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -14.13187 -18.82678 -12.13331 1.000 28.95512 ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -12.85610 -19.29708 -12.81723 1.000 21.07942 ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.88182 -18.56959 -10.65772 1.000 25.99051 ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -15.37552 -19.68499 -15.58268 1.000 26.09072 ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -16.11013 -20.88761 -15.94488 1.000 26.87631 ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -16.10617 -21.87828 -14.78471 1.000 27.62525 ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -15.16232 -21.93828 -13.99347 1.000 23.77709 ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -15.49150 -21.54745 -17.18161 1.000 22.73564 ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -15.80431 -20.85208 -18.48463 1.000 26.54013 ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -15.96424 -19.47649 -18.54657 1.000 19.31601 ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -15.91464 -21.58452 -19.65628 1.000 22.04565 ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -16.24209 -18.84672 -19.74709 1.000 21.15539 ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -16.19355 -20.96128 -20.86109 1.000 25.48638 ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -16.35698 -19.58988 -20.90610 1.000 25.44435 ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -17.17492 -22.66160 -14.68760 1.000 20.74292 ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -17.25581 -23.74305 -13.71638 1.000 26.28519 ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -17.18868 -25.06854 -14.46477 1.000 26.09071 ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -17.37367 -25.13617 -15.68332 1.000 30.72495 ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -18.52702 -23.65614 -12.84539 1.000 40.09305 ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -18.54954 -22.34831 -12.06980 1.000 52.55718 ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -19.76290 -23.76741 -13.70562 1.000 23.27378 ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -16.90609 -26.13619 -13.72231 1.000 26.64230 ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -16.74521 -27.45940 -14.30548 1.000 37.89452 ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -17.82099 -28.40819 -13.79130 1.000 48.12070 ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -18.46958 -28.15804 -12.77151 1.000 46.92035 ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -15.35322 -28.03777 -14.01057 1.000 36.78336 ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -14.24512 -26.99811 -13.93036 1.000 41.20155 ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -12.93259 -27.58488 -13.44009 1.000 61.78964 ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -12.55338 -28.67663 -13.91798 1.000 44.13187 ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -12.27907 -26.95446 -12.57984 1.000 46.48934 ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -17.99875 -29.50693 -14.52032 1.000 48.06780 ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -19.00519 -30.51214 -14.19603 1.000 57.79890 ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -18.74373 -31.15078 -12.83418 1.000 59.43999 ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -17.59713 -31.26645 -12.40083 1.000 60.92693 ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -19.04448 -31.59175 -15.28212 1.000 58.53271 ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -19.80371 -32.85053 -14.88644 1.000 82.31797 ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -20.06591 -33.74119 -16.09309 1.000 66.15298 ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -20.11601 -35.21098 -15.70170 1.000 74.46476 ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -19.32908 -35.49488 -14.46942 1.000 75.16535 ? 224 LYS   A NZ  1 
HETATM 1645 C C10 . A1ABL B 2 .   ? 0.67030   -8.44479  -24.83003 0.688 35.38788 ? 301 A1ABL A C10 1 
HETATM 1646 C C15 . A1ABL B 2 .   ? 0.04438   -8.64523  -26.19289 0.897 35.30376 ? 301 A1ABL A C15 1 
HETATM 1647 C C02 . A1ABL B 2 .   ? -2.61613  -10.60149 -23.73814 1.000 26.26974 ? 301 A1ABL A C02 1 
HETATM 1648 C C03 . A1ABL B 2 .   ? -1.28961  -11.31284 -23.81202 1.000 22.84398 ? 301 A1ABL A C03 1 
HETATM 1649 C C04 . A1ABL B 2 .   ? -1.21721  -12.70445 -23.83795 0.782 27.49501 ? 301 A1ABL A C04 1 
HETATM 1650 C C05 . A1ABL B 2 .   ? 0.00010   -13.35764 -23.91399 1.000 22.64819 ? 301 A1ABL A C05 1 
HETATM 1651 C C06 . A1ABL B 2 .   ? 1.16403   -12.62769 -23.97315 0.834 24.34047 ? 301 A1ABL A C06 1 
HETATM 1652 C C07 . A1ABL B 2 .   ? 1.12579   -11.24611 -23.95513 1.000 28.45474 ? 301 A1ABL A C07 1 
HETATM 1653 C C08 . A1ABL B 2 .   ? -0.09571  -10.59170 -23.88548 1.000 27.23740 ? 301 A1ABL A C08 1 
HETATM 1654 C C11 . A1ABL B 2 .   ? 0.63351   -6.98921  -24.42139 1.000 39.54009 ? 301 A1ABL A C11 1 
HETATM 1655 C C12 . A1ABL B 2 .   ? -0.77522  -6.48689  -24.63139 1.000 33.98287 ? 301 A1ABL A C12 1 
HETATM 1656 C C14 . A1ABL B 2 .   ? -0.25112  -7.30219  -26.81788 0.739 31.61516 ? 301 A1ABL A C14 1 
HETATM 1657 O O01 . A1ABL B 2 .   ? -3.58629  -11.18384 -24.59845 1.000 31.82767 ? 301 A1ABL A O01 1 
HETATM 1658 O O09 . A1ABL B 2 .   ? -0.11659  -9.21651  -23.85768 1.000 28.91282 ? 301 A1ABL A O09 1 
HETATM 1659 O O13 . A1ABL B 2 .   ? -1.14917  -6.54657  -26.00787 1.000 34.42821 ? 301 A1ABL A O13 1 
HETATM 1660 O O   . HOH   C 3 .   ? -17.88870 -24.23446 -8.84014  1.000 53.44845 ? 401 HOH   A O   1 
HETATM 1661 O O   . HOH   C 3 .   ? 19.37309  1.35277   -16.76304 1.000 52.48101 ? 402 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? 0.62310   -28.47925 -25.21591 1.000 51.35162 ? 403 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? 6.15091   -21.03788 -0.02903  1.000 32.83087 ? 404 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? 21.37762  -13.31913 -18.78137 1.000 57.09273 ? 405 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? -4.00762  -26.24217 -30.75338 1.000 50.68477 ? 406 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? -1.72980  -29.93678 -20.01542 1.000 55.37108 ? 407 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? 7.41058   -30.32355 -15.36651 1.000 57.31543 ? 408 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? 0.74372   -20.86709 -4.67441  1.000 36.48603 ? 409 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? -12.95395 -7.46852  -11.85480 1.000 42.69832 ? 410 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? -13.30822 -0.74180  -20.45627 1.000 34.97892 ? 411 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -8.65332  -11.91049 -36.54252 1.000 26.29400 ? 412 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? -8.17081  1.96745   -36.31260 1.000 42.19509 ? 413 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? 0.52435   -14.83059 -1.32662  1.000 39.68649 ? 414 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? 5.97678   -22.02016 -37.40785 1.000 36.65501 ? 415 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? 11.68365  -27.44984 -34.59288 1.000 32.20282 ? 416 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? -0.30304  -5.32930  -18.59041 1.000 25.00503 ? 417 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? 7.80990   -23.02964 -14.28635 1.000 35.37215 ? 418 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 3.48826   -24.19654 -38.73948 1.000 39.65709 ? 419 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? -6.39458  -7.74153  -34.28758 1.000 22.66880 ? 420 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? -16.32082 -12.70043 -19.85260 1.000 24.21304 ? 421 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? 7.56107   -27.80914 -24.01563 1.000 33.67781 ? 422 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -8.08637  -22.71713 -30.17725 1.000 47.56531 ? 423 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? 3.51790   -7.72285  -36.78400 1.000 33.88665 ? 424 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? 7.57953   1.25064   -14.64026 1.000 41.97454 ? 425 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? 9.76124   -23.74621 -9.48131  1.000 53.54969 ? 426 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? -3.33290  -12.10907 -9.14658  1.000 38.53385 ? 427 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? 11.49936  -28.07093 -30.39809 1.000 31.91742 ? 428 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? 7.73346   -18.75274 -6.56296  1.000 29.78502 ? 429 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? 4.68899   -1.28156  -6.34408  1.000 53.71512 ? 430 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 1.42768   -26.14200 -2.85190  1.000 52.54506 ? 431 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? -16.18419 -25.44053 -18.02161 1.000 25.98399 ? 432 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 3.50682   -29.60314 -25.68368 1.000 50.74179 ? 433 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? 6.83416   -26.71291 -27.76141 1.000 36.81674 ? 434 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? 10.81215  -14.79390 -1.03220  1.000 30.60569 ? 435 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? -8.05611  -24.81144 -19.24115 1.000 24.46128 ? 436 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? -8.45870  4.71953   -33.54454 1.000 31.06851 ? 437 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? -7.74166  -28.28436 -8.00484  1.000 36.09671 ? 438 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? 4.66802   -30.62084 -11.47813 1.000 44.52237 ? 439 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? 1.37564   -7.78305  -16.46787 1.000 25.38095 ? 440 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? -14.49764 -11.82595 0.08912   1.000 38.66951 ? 441 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? 10.55636  -25.33181 -23.64788 1.000 30.61611 ? 442 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? 0.59459   -5.53603  -13.78840 1.000 39.09126 ? 443 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? -7.43169  -28.01915 -21.18005 1.000 51.76959 ? 444 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? 15.45304  -20.13101 -18.63171 1.000 29.49395 ? 445 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -2.09590  -13.71029 -35.56081 1.000 25.13832 ? 446 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? -5.77958  -2.08224  -19.36973 1.000 25.01747 ? 447 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? 9.22739   -26.46519 -17.05306 1.000 30.87714 ? 448 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -0.39640  -7.04276  -31.04250 1.000 32.15918 ? 449 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? 9.83083   -14.66311 -25.29495 1.000 24.39511 ? 450 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? -16.07601 -3.08684  -21.35597 1.000 37.50038 ? 451 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? -5.09602  -10.51537 -27.27987 1.000 23.31864 ? 452 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? 17.99036  -19.20394 -24.63051 1.000 33.71419 ? 453 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? -15.02538 -11.02731 -29.81985 1.000 28.13276 ? 454 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? -1.46671  -29.15325 -5.89769  1.000 41.85250 ? 455 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? -18.81165 -10.99728 -23.72661 1.000 37.77090 ? 456 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? 19.741    -16.465   -27.468   1.000 44.65288 ? 457 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? -2.86595  -3.31942  -35.49455 1.000 46.98213 ? 458 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? 9.76581   -17.36478 -7.67918  1.000 29.29231 ? 459 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? 5.55927   -29.25959 -8.29977  1.000 48.00982 ? 460 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? 4.19329   -24.18879 -30.68114 1.000 22.81668 ? 461 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? 0.96072   -6.84918  -5.03881  1.000 52.58635 ? 462 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -10.34637 -11.59525 -2.20558  1.000 29.81743 ? 463 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? 13.67789  -13.98493 -26.73773 1.000 25.68826 ? 464 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? 10.35543  -21.52037 -7.13192  1.000 44.78563 ? 465 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? -13.07227 -24.87924 -10.78127 1.000 39.37484 ? 466 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? -9.20515  -2.14978  -17.63460 1.000 25.32297 ? 467 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? 3.64978   -6.86121  -17.65566 1.000 26.80647 ? 468 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? 18.33840  -7.25987  -20.16123 1.000 41.10975 ? 469 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? -16.99868 -5.45489  -22.78668 1.000 29.79277 ? 470 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? -14.48770 -22.64499 -11.42597 1.000 33.61045 ? 471 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? 2.80646   -5.09045  -28.39060 1.000 37.66122 ? 472 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? 3.19354   -20.45205 -2.73317  1.000 35.72294 ? 473 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? 11.17930  -7.97211  -27.41218 1.000 27.23839 ? 474 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? -14.16189 -6.90462  -14.30069 1.000 43.21529 ? 475 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? 13.97115  -11.18828 -29.81871 1.000 48.00688 ? 476 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? -14.07047 -12.72384 -7.89856  1.000 28.91020 ? 477 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? -8.83190  -10.37315 -40.47816 1.000 48.88314 ? 478 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? -0.97304  -11.26938 -3.01399  1.000 39.36404 ? 479 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? 3.13436   -6.05052  -11.08520 1.000 37.03348 ? 480 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -7.98358  -4.02329  -10.74811 1.000 36.39745 ? 481 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? -9.85919  -0.54823  -19.88553 1.000 39.84586 ? 482 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? 10.56155  -17.74786 -39.02329 1.000 47.09089 ? 483 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? -5.38430  -7.59268  -13.02040 1.000 21.23150 ? 484 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -15.06498 -5.84983  -9.97969  1.000 45.95297 ? 485 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? -4.94979  -14.13100 -22.67344 1.000 21.95228 ? 486 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? -13.84602 -17.04537 -2.76581  1.000 26.47079 ? 487 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? 8.79892   -15.45706 -27.77218 1.000 22.18594 ? 488 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -6.12914  -13.98309 0.78066   1.000 31.22530 ? 489 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? -5.81322  -31.16602 -11.56556 1.000 36.50147 ? 490 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? -3.09533  -13.05330 -20.54727 1.000 24.46121 ? 491 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? 8.45684   -20.60519 -9.45845  1.000 35.26251 ? 492 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 13.76709  -20.45063 -20.73703 1.000 25.48132 ? 493 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? 12.97025  -13.78377 -29.58109 1.000 32.96824 ? 494 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 0.18817   -1.06045  -19.56544 1.000 43.72856 ? 495 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? -6.41505  -5.18257  -38.83547 1.000 48.44552 ? 496 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? -1.77353  -25.68789 -4.63326  1.000 31.90586 ? 497 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? 15.04963  -0.55692  -12.40237 1.000 49.20885 ? 498 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? 13.22285  -25.27029 -35.74818 1.000 26.47608 ? 499 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? 14.08955  -15.56773 -2.16494  1.000 38.84286 ? 500 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? -11.19130 -14.29415 -37.74286 1.000 47.07569 ? 501 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? 6.76215   -29.85447 -20.09597 1.000 39.09774 ? 502 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? -4.62626  0.56037   -30.42882 1.000 43.78698 ? 503 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? -7.76162  -24.32614 -23.08262 1.000 42.47562 ? 504 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -2.84947  -15.49752 -0.23344  1.000 42.97713 ? 505 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? -6.06541  -11.28143 -9.90534  1.000 31.82300 ? 506 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? 14.39253  -15.81315 -30.58851 1.000 36.84299 ? 507 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? -7.10846  1.37611   -19.33623 1.000 40.28495 ? 508 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? -0.00625  -5.71299  -38.33830 1.000 41.73590 ? 509 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -6.28390  -5.02903  -35.67747 1.000 30.10384 ? 510 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? 5.92864   -25.39461 -7.16928  1.000 45.91008 ? 511 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? -1.62044  -32.76975 -7.90808  1.000 50.85075 ? 512 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? 20.59751  -10.70046 -26.13060 1.000 45.51867 ? 513 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? -19.42705 -9.96153  -33.40705 1.000 55.40080 ? 514 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 10.82130  -25.55103 -26.81588 1.000 36.70256 ? 515 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? 4.40928   -19.17027 -40.64751 1.000 42.25705 ? 516 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? 9.71771   -11.06605 -34.87980 1.000 42.23539 ? 517 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? -0.24914  -12.46992 -20.78683 1.000 25.22409 ? 518 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? 3.12428   -5.50208  -5.70235  1.000 46.49495 ? 519 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? -17.58886 -15.24083 -13.11223 1.000 28.58658 ? 520 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? -13.03379 -12.37332 -30.99907 1.000 25.41875 ? 521 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? 3.82713   -11.82341 -38.67879 1.000 34.88032 ? 522 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? 16.48573  -27.32170 -22.73406 1.000 46.55311 ? 523 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? -7.65068  -13.38053 -40.96543 1.000 50.93757 ? 524 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? 4.00344   -9.18987  -20.21980 1.000 28.83521 ? 525 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? 20.944    -16.776   -20.098   1.000 44.45212 ? 526 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? 2.23148   -26.04610 -29.42116 1.000 44.96461 ? 527 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? -10.15848 -15.06254 -28.34477 1.000 35.89783 ? 528 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? 7.66849   -23.45495 -7.18918  1.000 44.92203 ? 529 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? -17.91630 -18.70158 -11.21008 1.000 49.54702 ? 530 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? 8.82714   -20.44857 -4.40145  1.000 36.57674 ? 531 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? 12.17452  -21.64168 -40.65421 1.000 54.48241 ? 532 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -11.76998 -7.56269  -38.30442 1.000 41.38513 ? 533 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? -3.15378  -21.32238 -0.45799  1.000 41.92112 ? 534 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? -13.47487 -26.42197 -18.25087 1.000 32.74040 ? 535 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? 13.11062  -6.76911  -26.13308 1.000 24.33257 ? 536 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? -3.27912  -0.93761  -24.08720 1.000 41.60512 ? 537 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? 13.64796  -4.01174  -25.32923 1.000 22.44141 ? 538 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? -16.04910 0.14054   -30.43443 1.000 45.72336 ? 539 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? -8.82056  -18.18120 -36.68407 1.000 44.34739 ? 540 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? -14.17542 -16.07870 -26.17407 1.000 34.56625 ? 541 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? -6.00574  -18.77385 -38.89558 1.000 37.81174 ? 542 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -4.12069  0.42652   -22.26288 1.000 33.67874 ? 543 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? 1.82815   -6.47478  -29.98974 1.000 44.82772 ? 544 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? -15.14018 -12.12794 -11.91582 1.000 37.99548 ? 545 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? 18.38930  -16.50151 -13.28958 1.000 47.38774 ? 546 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? -7.99396  -24.74586 -37.66490 1.000 52.38452 ? 547 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? -1.09222  -26.09238 -32.35509 1.000 42.24223 ? 548 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? -13.71107 -18.53538 -24.46062 1.000 25.00322 ? 549 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? 18.76365  -22.25341 -25.42245 1.000 48.55009 ? 550 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? 15.78685  -18.84709 -3.51542  1.000 41.02463 ? 551 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? -16.21160 -8.93461  -14.12121 1.000 41.69436 ? 552 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? 6.92460   -29.67079 -30.02237 1.000 43.56554 ? 553 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? 8.68809   -16.09572 -39.59166 1.000 45.34687 ? 554 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? 3.08265   -4.18687  -8.74391  1.000 48.95016 ? 555 HOH   A O   1 
HETATM 1815 O O   . HOH   C 3 .   ? -13.72568 -25.78145 -7.93256  1.000 31.99805 ? 556 HOH   A O   1 
HETATM 1816 O O   . HOH   C 3 .   ? -1.38647  -4.23501  -33.94677 1.000 45.80567 ? 557 HOH   A O   1 
HETATM 1817 O O   . HOH   C 3 .   ? -20.734   -14.148   -18.376   1.000 45.04444 ? 558 HOH   A O   1 
HETATM 1818 O O   . HOH   C 3 .   ? 5.80436   -30.68350 -38.27527 1.000 56.00895 ? 559 HOH   A O   1 
HETATM 1819 O O   . HOH   C 3 .   ? 0.91509   -8.83162  -3.72032  1.000 40.50374 ? 560 HOH   A O   1 
HETATM 1820 O O   . HOH   C 3 .   ? 3.67652   -30.27807 -19.40334 1.000 45.80537 ? 561 HOH   A O   1 
HETATM 1821 O O   . HOH   C 3 .   ? 7.20024   -7.62485  -33.65981 1.000 36.90413 ? 562 HOH   A O   1 
HETATM 1822 O O   . HOH   C 3 .   ? 10.98558  -11.62716 -4.74627  1.000 39.01446 ? 563 HOH   A O   1 
HETATM 1823 O O   . HOH   C 3 .   ? -5.11107  -31.85436 -7.22946  1.000 50.81810 ? 564 HOH   A O   1 
HETATM 1824 O O   . HOH   C 3 .   ? 3.32664   -23.83884 -3.07976  1.000 41.74460 ? 565 HOH   A O   1 
HETATM 1825 O O   . HOH   C 3 .   ? 21.01739  -13.93899 -26.59796 1.000 34.08004 ? 566 HOH   A O   1 
HETATM 1826 O O   . HOH   C 3 .   ? -3.23195  -5.43977  -6.31033  1.000 40.98180 ? 567 HOH   A O   1 
HETATM 1827 O O   . HOH   C 3 .   ? 8.42335   -20.15100 -41.53332 1.000 42.22941 ? 568 HOH   A O   1 
HETATM 1828 O O   . HOH   C 3 .   ? -14.05307 -23.99311 -4.86902  1.000 38.29886 ? 569 HOH   A O   1 
HETATM 1829 O O   . HOH   C 3 .   ? -2.173    -0.462    -18.487   1.000 57.82436 ? 570 HOH   A O   1 
HETATM 1830 O O   . HOH   C 3 .   ? -0.08322  -16.66300 -3.31672  1.000 28.65403 ? 571 HOH   A O   1 
HETATM 1831 O O   . HOH   C 3 .   ? -12.20038 -26.82050 -20.29887 1.000 30.00659 ? 572 HOH   A O   1 
HETATM 1832 O O   . HOH   C 3 .   ? 3.18955   -6.32005  -20.35120 1.000 40.63714 ? 573 HOH   A O   1 
HETATM 1833 O O   . HOH   C 3 .   ? 11.74569  -1.91755  -3.76777  1.000 54.09757 ? 574 HOH   A O   1 
HETATM 1834 O O   . HOH   C 3 .   ? 1.39227   -9.59012  -40.94948 1.000 54.61393 ? 575 HOH   A O   1 
HETATM 1835 O O   . HOH   C 3 .   ? -16.910   -28.557   -17.319   1.000 48.28267 ? 576 HOH   A O   1 
HETATM 1836 O O   . HOH   C 3 .   ? 5.44485   -10.37918 -2.00146  1.000 49.08022 ? 577 HOH   A O   1 
HETATM 1837 O O   . HOH   C 3 .   ? -1.63051  -26.91430 -25.06381 1.000 49.66721 ? 578 HOH   A O   1 
HETATM 1838 O O   . HOH   C 3 .   ? 1.81793   -18.47007 0.10883   1.000 37.47042 ? 579 HOH   A O   1 
HETATM 1839 O O   . HOH   C 3 .   ? 1.17753   -4.51968  -16.54553 1.000 48.99845 ? 580 HOH   A O   1 
HETATM 1840 O O   . HOH   C 3 .   ? -16.31209 -25.22963 -10.66504 1.000 39.51317 ? 581 HOH   A O   1 
HETATM 1841 O O   . HOH   C 3 .   ? -4.70718  -5.01791  -12.10559 1.000 43.06607 ? 582 HOH   A O   1 
HETATM 1842 O O   . HOH   C 3 .   ? -5.72175  -12.43233 -42.06532 1.000 44.19017 ? 583 HOH   A O   1 
HETATM 1843 O O   . HOH   C 3 .   ? 17.855    -15.210   -29.643   1.000 49.29744 ? 584 HOH   A O   1 
HETATM 1844 O O   . HOH   C 3 .   ? -0.34813  -1.59223  -22.98561 1.000 57.13628 ? 585 HOH   A O   1 
HETATM 1845 O O   . HOH   C 3 .   ? 11.44422  -1.52591  -20.10561 1.000 36.48622 ? 586 HOH   A O   1 
HETATM 1846 O O   . HOH   C 3 .   ? 15.29259  -12.92369 -7.16036  1.000 50.69308 ? 587 HOH   A O   1 
HETATM 1847 O O   . HOH   C 3 .   ? 4.84285   -1.86984  -18.41830 1.000 47.54619 ? 588 HOH   A O   1 
HETATM 1848 O O   . HOH   C 3 .   ? 0.88881   -5.87564  -34.99522 1.000 51.68324 ? 589 HOH   A O   1 
HETATM 1849 O O   . HOH   C 3 .   ? -16.49074 -18.25587 -2.83575  1.000 52.97335 ? 590 HOH   A O   1 
HETATM 1850 O O   . HOH   C 3 .   ? -6.99063  -1.96953  -12.52663 1.000 42.49394 ? 591 HOH   A O   1 
HETATM 1851 O O   . HOH   C 3 .   ? -6.975    -23.546   -1.767    1.000 46.15021 ? 592 HOH   A O   1 
HETATM 1852 O O   . HOH   C 3 .   ? -0.03626  -19.15836 -2.10027  1.000 34.50655 ? 593 HOH   A O   1 
HETATM 1853 O O   . HOH   C 3 .   ? 4.09854   -8.49180  -2.09256  1.000 53.88382 ? 594 HOH   A O   1 
HETATM 1854 O O   . HOH   C 3 .   ? -15.179   -23.325   -30.413   1.000 38.35417 ? 595 HOH   A O   1 
HETATM 1855 O O   . HOH   C 3 .   ? -4.517    -3.398    -15.450   1.000 48.94495 ? 596 HOH   A O   1 
HETATM 1856 O O   . HOH   C 3 .   ? 14.56808  -22.45508 -16.95053 1.000 43.06622 ? 597 HOH   A O   1 
HETATM 1857 O O   . HOH   C 3 .   ? -2.19498  -1.04972  -31.15080 1.000 47.97229 ? 598 HOH   A O   1 
HETATM 1858 O O   . HOH   C 3 .   ? -13.95577 -29.27905 -17.17867 1.000 50.69714 ? 599 HOH   A O   1 
HETATM 1859 O O   . HOH   C 3 .   ? 12.17140  -25.29922 -38.60736 1.000 41.25692 ? 600 HOH   A O   1 
HETATM 1860 O O   . HOH   C 3 .   ? -9.90458  -26.23058 -20.86803 1.000 37.32923 ? 601 HOH   A O   1 
HETATM 1861 O O   . HOH   C 3 .   ? -18.16840 -5.18455  -25.60948 1.000 43.68934 ? 602 HOH   A O   1 
HETATM 1862 O O   . HOH   C 3 .   ? 5.280     -2.741    -26.099   1.000 48.02181 ? 603 HOH   A O   1 
HETATM 1863 O O   . HOH   C 3 .   ? 1.80011   -3.15916  -12.76385 1.000 54.91264 ? 604 HOH   A O   1 
HETATM 1864 O O   . HOH   C 3 .   ? -14.30691 -9.79344  -8.20712  1.000 46.07355 ? 605 HOH   A O   1 
HETATM 1865 O O   . HOH   C 3 .   ? 20.40862  -5.80196  -20.94313 1.000 54.07379 ? 606 HOH   A O   1 
HETATM 1866 O O   . HOH   C 3 .   ? -6.418    6.923     -36.268   1.000 47.88690 ? 607 HOH   A O   1 
HETATM 1867 O O   . HOH   C 3 .   ? -14.16495 -14.17854 -3.12195  1.000 40.85325 ? 608 HOH   A O   1 
HETATM 1868 O O   . HOH   C 3 .   ? -3.47932  -27.11042 -3.27080  1.000 47.11783 ? 609 HOH   A O   1 
HETATM 1869 O O   . HOH   C 3 .   ? 3.86559   -0.42816  -16.66083 1.000 46.61342 ? 610 HOH   A O   1 
HETATM 1870 O O   . HOH   C 3 .   ? 3.42089   -8.95226  -39.17375 1.000 40.45134 ? 611 HOH   A O   1 
HETATM 1871 O O   . HOH   C 3 .   ? -12.28444 -16.32897 -28.07333 1.000 34.96491 ? 612 HOH   A O   1 
HETATM 1872 O O   . HOH   C 3 .   ? -18.59012 -11.65101 -21.10823 1.000 35.50762 ? 613 HOH   A O   1 
HETATM 1873 O O   . HOH   C 3 .   ? 7.92969   -13.89690 -38.28874 1.000 40.69656 ? 614 HOH   A O   1 
HETATM 1874 O O   . HOH   C 3 .   ? 19.14628  -8.49554  -17.71230 1.000 42.57107 ? 615 HOH   A O   1 
HETATM 1875 O O   . HOH   C 3 .   ? 6.24637   -29.87014 -24.95766 1.000 48.89421 ? 616 HOH   A O   1 
HETATM 1876 O O   . HOH   C 3 .   ? 11.02179  -1.09010  -17.39447 1.000 45.83122 ? 617 HOH   A O   1 
HETATM 1877 O O   . HOH   C 3 .   ? -14.272   -0.874    -13.771   1.000 50.99202 ? 618 HOH   A O   1 
HETATM 1878 O O   . HOH   C 3 .   ? 16.13037  1.60821   -15.11741 1.000 53.24884 ? 619 HOH   A O   1 
HETATM 1879 O O   . HOH   C 3 .   ? -6.09404  3.75740   -34.17558 1.000 46.14544 ? 620 HOH   A O   1 
HETATM 1880 O O   . HOH   C 3 .   ? -15.17576 -10.07477 -11.48169 1.000 43.93084 ? 621 HOH   A O   1 
HETATM 1881 O O   . HOH   C 3 .   ? -6.91207  -30.82835 -9.31186  1.000 42.44920 ? 622 HOH   A O   1 
HETATM 1882 O O   . HOH   C 3 .   ? 6.74647   -21.62496 -2.58363  1.000 33.99530 ? 623 HOH   A O   1 
HETATM 1883 O O   . HOH   C 3 .   ? -8.62393  -5.46244  -40.18305 1.000 49.38778 ? 624 HOH   A O   1 
HETATM 1884 O O   . HOH   C 3 .   ? 24.16679  -12.28251 -23.22480 1.000 56.15281 ? 625 HOH   A O   1 
HETATM 1885 O O   . HOH   C 3 .   ? 5.92786   -13.01517 -39.96576 1.000 37.16352 ? 626 HOH   A O   1 
HETATM 1886 O O   . HOH   C 3 .   ? -4.17561  2.62945   -33.02489 1.000 48.65863 ? 627 HOH   A O   1 
HETATM 1887 O O   . HOH   C 3 .   ? -14.29983 -14.22902 -37.83346 1.000 53.17260 ? 628 HOH   A O   1 
HETATM 1888 O O   . HOH   C 3 .   ? -11.087   -22.951   -24.486   1.000 52.95088 ? 629 HOH   A O   1 
HETATM 1889 O O   . HOH   C 3 .   ? 4.84638   -14.82681 -41.54719 1.000 50.78019 ? 630 HOH   A O   1 
HETATM 1890 O O   . HOH   C 3 .   ? 13.76425  -11.38372 -5.09560  1.000 44.29018 ? 631 HOH   A O   1 
HETATM 1891 O O   . HOH   C 3 .   ? -16.677   -3.519    -12.400   1.000 55.29307 ? 632 HOH   A O   1 
HETATM 1892 O O   . HOH   C 3 .   ? -21.422   -14.341   -15.744   1.000 40.34671 ? 633 HOH   A O   1 
HETATM 1893 O O   . HOH   C 3 .   ? -18.676   -15.854   -26.252   1.000 52.40250 ? 634 HOH   A O   1 
HETATM 1894 O O   . HOH   C 3 .   ? 23.224    -15.496   -19.398   1.000 55.11892 ? 635 HOH   A O   1 
HETATM 1895 O O   . HOH   C 3 .   ? 9.47577   -12.56737 -37.34345 1.000 51.60645 ? 636 HOH   A O   1 
HETATM 1896 O O   . HOH   C 3 .   ? 16.34148  -3.16165  -26.22848 1.000 42.36844 ? 637 HOH   A O   1 
HETATM 1897 O O   . HOH   C 3 .   ? 3.997     -2.041    -28.044   1.000 42.10561 ? 638 HOH   A O   1 
HETATM 1898 O O   . HOH   C 3 .   ? -16.03832 -13.54604 -3.77796  1.000 48.52524 ? 639 HOH   A O   1 
HETATM 1899 O O   . HOH   C 3 .   ? -10.31311 -8.56170  -0.94320  1.000 45.96050 ? 640 HOH   A O   1 
HETATM 1900 O O   . HOH   C 3 .   ? -4.16646  -27.88958 -23.56627 1.000 46.47413 ? 641 HOH   A O   1 
HETATM 1901 O O   . HOH   C 3 .   ? -7.72519  -24.28613 -25.65366 1.000 51.68691 ? 642 HOH   A O   1 
HETATM 1902 O O   . HOH   C 3 .   ? 23.49261  -12.28630 -20.51733 1.000 58.12480 ? 643 HOH   A O   1 
HETATM 1903 O O   . HOH   C 3 .   ? 10.80388  -28.23705 -27.70325 1.000 45.31309 ? 644 HOH   A O   1 
HETATM 1904 O O   . HOH   C 3 .   ? 19.40045  -20.69957 -21.93017 1.000 48.45124 ? 645 HOH   A O   1 
HETATM 1905 O O   . HOH   C 3 .   ? 9.51360   -25.32999 -14.22565 1.000 44.85699 ? 646 HOH   A O   1 
HETATM 1906 O O   . HOH   C 3 .   ? 0.63321   -0.99087  -16.74016 1.000 48.74643 ? 647 HOH   A O   1 
HETATM 1907 O O   . HOH   C 3 .   ? -12.30178 -13.26584 -0.94924  1.000 36.90744 ? 648 HOH   A O   1 
HETATM 1908 O O   . HOH   C 3 .   ? -14.53456 -14.06837 -10.25535 1.000 36.91661 ? 649 HOH   A O   1 
HETATM 1909 O O   . HOH   C 3 .   ? 15.278    -17.046   0.264     1.000 47.84082 ? 650 HOH   A O   1 
HETATM 1910 O O   . HOH   C 3 .   ? -17.19710 -15.64180 -10.30287 1.000 39.07000 ? 651 HOH   A O   1 
HETATM 1911 O O   . HOH   C 3 .   ? 20.83284  -20.39301 -26.74815 1.000 48.00537 ? 652 HOH   A O   1 
HETATM 1912 O O   . HOH   C 3 .   ? 21.84528  -2.25018  -22.10931 1.000 56.88560 ? 653 HOH   A O   1 
HETATM 1913 O O   . HOH   C 3 .   ? -9.02212  -33.00630 -9.08266  1.000 52.45199 ? 654 HOH   A O   1 
HETATM 1914 O O   . HOH   C 3 .   ? 22.16628  -18.19064 -25.04341 1.000 52.12491 ? 655 HOH   A O   1 
HETATM 1915 O O   . HOH   C 3 .   ? -8.78838  -10.67366 -0.00551  1.000 47.37199 ? 656 HOH   A O   1 
HETATM 1916 O O   . HOH   C 3 .   ? -10.496   -11.661   2.074     1.000 46.32259 ? 657 HOH   A O   1 
HETATM 1917 O O   . HOH   C 3 .   ? -2.58915  -26.46235 -27.96085 1.000 46.34912 ? 658 HOH   A O   1 
HETATM 1918 O O   . HOH   C 3 .   ? -16.87210 2.96614   -41.22119 1.000 52.24811 ? 659 HOH   A O   1 
HETATM 1919 O O   . HOH   C 3 .   ? -20.76341 -10.20204 -19.51480 1.000 47.54978 ? 660 HOH   A O   1 
HETATM 1920 O O   . HOH   C 3 .   ? 16.83860  -14.43874 -3.67765  1.000 51.00638 ? 661 HOH   A O   1 
HETATM 1921 O O   . HOH   C 3 .   ? -8.933    0.862     -3.749    1.000 56.70697 ? 662 HOH   A O   1 
HETATM 1922 O O   . HOH   C 3 .   ? -19.67364 -5.66691  -21.43620 1.000 46.50892 ? 663 HOH   A O   1 
HETATM 1923 O O   . HOH   C 3 .   ? -18.90434 2.36812   -39.98868 1.000 45.56141 ? 664 HOH   A O   1 
HETATM 1924 O O   . HOH   C 3 .   ? -7.997    -29.739   -26.410   1.000 51.05587 ? 665 HOH   A O   1 
HETATM 1925 O O   . HOH   C 3 .   ? 24.63550  -3.56854  -21.79369 1.000 51.39244 ? 666 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   ? 0.63153 0.74927 0.49980 -0.05275 -0.09299 -0.28554 16  GLU A N   
2    C CA  . GLU A 9   ? 0.77768 0.85115 0.62473 -0.01953 -0.08895 -0.26743 16  GLU A CA  
3    C C   . GLU A 9   ? 0.67476 0.73702 0.55004 -0.00231 -0.08784 -0.23338 16  GLU A C   
4    O O   . GLU A 9   ? 0.73844 0.85462 0.63034 0.01241  -0.10200 -0.22078 16  GLU A O   
5    C CB  . GLU A 9   ? 0.90089 1.01347 0.72134 0.01339  -0.10162 -0.25957 16  GLU A CB  
6    C CG  . GLU A 9   ? 1.02042 1.10569 0.83391 0.05443  -0.09724 -0.22153 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.28599 1.42442 1.07868 0.09083  -0.10967 -0.20997 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.17305 1.35522 0.94974 0.08768  -0.11824 -0.22825 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.13749 1.27086 0.93469 0.12067  -0.10563 -0.17695 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.55795 0.55144 0.43667 -0.00272 -0.06906 -0.21712 17  VAL A N   
11   C CA  . VAL A 10  ? 0.46296 0.44314 0.36841 0.00691  -0.06561 -0.18845 17  VAL A CA  
12   C C   . VAL A 10  ? 0.52364 0.47413 0.41992 0.03656  -0.05866 -0.15935 17  VAL A C   
13   O O   . VAL A 10  ? 0.58985 0.49671 0.46698 0.04138  -0.04506 -0.15795 17  VAL A O   
14   C CB  . VAL A 10  ? 0.47662 0.41270 0.39540 -0.01705 -0.04881 -0.19323 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.48155 0.41255 0.42569 -0.00611 -0.04745 -0.16527 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.62045 0.58274 0.54869 -0.05238 -0.05077 -0.22602 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.40257 0.37575 0.31222 0.05521  -0.06490 -0.13694 18  GLU A N   
18   C CA  . GLU A 11  ? 0.44285 0.39288 0.34947 0.07692  -0.05584 -0.11185 18  GLU A CA  
19   C C   . GLU A 11  ? 0.45517 0.38926 0.38719 0.07147  -0.04924 -0.09658 18  GLU A C   
20   O O   . GLU A 11  ? 0.33766 0.29198 0.28893 0.06446  -0.05540 -0.09457 18  GLU A O   
21   C CB  . GLU A 11  ? 0.38164 0.36001 0.27937 0.10064  -0.06073 -0.09882 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.47164 0.46506 0.33781 0.11558  -0.06475 -0.10781 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.64755 0.67187 0.50133 0.14379  -0.06710 -0.09284 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.65263 0.72091 0.51435 0.14585  -0.07825 -0.09555 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.60745 0.61137 0.44227 0.16586  -0.05482 -0.07696 18  GLU A OE2 
26   N N   . THR A 12  ? 0.35902 0.26249 0.29012 0.07654  -0.03669 -0.08581 19  THR A N   
27   C CA  . THR A 12  ? 0.33511 0.23252 0.28733 0.07437  -0.03094 -0.07178 19  THR A CA  
28   C C   . THR A 12  ? 0.36739 0.27383 0.32559 0.08661  -0.02675 -0.05523 19  THR A C   
29   O O   . THR A 12  ? 0.36636 0.26503 0.31200 0.09828  -0.01944 -0.05059 19  THR A O   
30   C CB  . THR A 12  ? 0.38981 0.25591 0.33708 0.07374  -0.01771 -0.07065 19  THR A CB  
31   O OG1 . THR A 12  ? 0.41649 0.26271 0.35203 0.05889  -0.01483 -0.08972 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.35886 0.22947 0.32635 0.07357  -0.01395 -0.05711 19  THR A CG2 
33   N N   . PHE A 13  ? 0.33516 0.25609 0.31152 0.08182  -0.02875 -0.04806 20  PHE A N   
34   C CA  . PHE A 13  ? 0.31064 0.23790 0.29316 0.08585  -0.02105 -0.03717 20  PHE A CA  
35   C C   . PHE A 13  ? 0.48138 0.41857 0.48412 0.07761  -0.01801 -0.03189 20  PHE A C   
36   O O   . PHE A 13  ? 0.33939 0.27901 0.35134 0.07097  -0.02323 -0.03354 20  PHE A O   
37   C CB  . PHE A 13  ? 0.29765 0.23142 0.27749 0.08798  -0.02167 -0.03474 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.33475 0.27094 0.29256 0.10232  -0.02483 -0.03719 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.34084 0.29425 0.29575 0.10050  -0.03860 -0.04806 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.36566 0.29183 0.30525 0.11768  -0.01269 -0.02918 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.33527 0.30515 0.26940 0.11527  -0.04374 -0.05180 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.43073 0.36439 0.34586 0.13630  -0.01546 -0.02946 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.46662 0.42695 0.37900 0.13588  -0.03278 -0.04118 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.37015 0.31736 0.37947 0.07767  -0.00852 -0.02641 21  ALA A N   
45   C CA  . ALA A 14  ? 0.36964 0.34084 0.39838 0.06847  -0.00672 -0.02418 21  ALA A CA  
46   C C   . ALA A 14  ? 0.34191 0.31501 0.37596 0.05549  -0.00358 -0.02701 21  ALA A C   
47   O O   . ALA A 14  ? 0.28350 0.24151 0.30748 0.05577  0.00652  -0.02680 21  ALA A O   
48   C CB  . ALA A 14  ? 0.30006 0.29306 0.33639 0.07152  0.00261  -0.02044 21  ALA A CB  
49   N N   . PHE A 15  ? 0.25255 0.23892 0.29800 0.04649  -0.00898 -0.02861 22  PHE A N   
50   C CA  . PHE A 15  ? 0.23802 0.22490 0.28668 0.03242  -0.00233 -0.03273 22  PHE A CA  
51   C C   . PHE A 15  ? 0.31834 0.31978 0.37327 0.01967  0.01212  -0.03785 22  PHE A C   
52   O O   . PHE A 15  ? 0.23247 0.26363 0.29838 0.02033  0.01175  -0.03786 22  PHE A O   
53   C CB  . PHE A 15  ? 0.23510 0.23820 0.29387 0.02535  -0.01032 -0.03432 22  PHE A CB  
54   C CG  . PHE A 15  ? 0.30796 0.29470 0.36271 0.03114  -0.01909 -0.03163 22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.28376 0.25213 0.32990 0.03186  -0.01594 -0.03141 22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.22612 0.21699 0.28504 0.03678  -0.02717 -0.02871 22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.30165 0.26709 0.34854 0.03602  -0.02422 -0.03005 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.25098 0.22967 0.30941 0.03715  -0.03244 -0.02895 22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.27182 0.24339 0.32685 0.03566  -0.03274 -0.03051 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.28373 0.26414 0.33081 0.00802  0.02814  -0.04241 23  GLN A N   
61   C CA  . GLN A 16  ? 0.33754 0.33312 0.39324 -0.01415 0.04527  -0.05318 23  GLN A CA  
62   C C   . GLN A 16  ? 0.28408 0.32917 0.35924 -0.02923 0.03500  -0.06255 23  GLN A C   
63   O O   . GLN A 16  ? 0.29608 0.34536 0.37139 -0.02550 0.02192  -0.06069 23  GLN A O   
64   C CB  . GLN A 16  ? 0.39316 0.34544 0.43147 -0.02585 0.07048  -0.05762 23  GLN A CB  
65   C CG  . GLN A 16  ? 0.43081 0.33837 0.44554 -0.00675 0.08599  -0.04629 23  GLN A CG  
66   C CD  . GLN A 16  ? 0.57394 0.43075 0.56377 -0.00765 0.11255  -0.04449 23  GLN A CD  
67   O OE1 . GLN A 16  ? 0.64597 0.48614 0.62259 0.00907  0.10671  -0.03575 23  GLN A OE1 
68   N NE2 . GLN A 16  ? 0.62117 0.45255 0.60359 -0.02706 0.14534  -0.05273 23  GLN A NE2 
69   N N   . ALA A 17  ? 0.28071 0.36949 0.37245 -0.04517 0.04145  -0.07259 24  ALA A N   
70   C CA  . ALA A 17  ? 0.22853 0.38211 0.33871 -0.05414 0.02938  -0.08066 24  ALA A CA  
71   C C   . ALA A 17  ? 0.25993 0.40943 0.36508 -0.07223 0.02973  -0.09234 24  ALA A C   
72   O O   . ALA A 17  ? 0.27244 0.45490 0.38197 -0.06544 0.01365  -0.09058 24  ALA A O   
73   C CB  . ALA A 17  ? 0.28130 0.49262 0.41202 -0.07269 0.03868  -0.09341 24  ALA A CB  
74   N N   . GLU A 18  ? 0.32108 0.42517 0.41287 -0.09259 0.05117  -0.10285 25  GLU A N   
75   C CA  . GLU A 18  ? 0.33393 0.42690 0.41652 -0.11035 0.05589  -0.11499 25  GLU A CA  
76   C C   . GLU A 18  ? 0.32940 0.39333 0.40044 -0.08632 0.04119  -0.09899 25  GLU A C   
77   O O   . GLU A 18  ? 0.30124 0.38057 0.37123 -0.09127 0.03343  -0.10399 25  GLU A O   
78   C CB  . GLU A 18  ? 0.41930 0.45787 0.48425 -0.13510 0.08974  -0.12824 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.55108 0.61422 0.62828 -0.16660 0.11069  -0.14825 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.63547 0.68224 0.71456 -0.15133 0.11902  -0.13499 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.51892 0.54304 0.59020 -0.11603 0.10475  -0.11178 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 0.77042 0.82836 0.85842 -0.17665 0.14127  -0.14966 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.30224 0.32881 0.36475 -0.06131 0.03768  -0.08119 26  ILE A N   
84   C CA  . ILE A 19  ? 0.36066 0.36781 0.41648 -0.04213 0.02469  -0.06860 26  ILE A CA  
85   C C   . ILE A 19  ? 0.28606 0.33248 0.35537 -0.02981 0.00289  -0.06226 26  ILE A C   
86   O O   . ILE A 19  ? 0.25062 0.29788 0.31877 -0.02499 -0.00532 -0.05872 26  ILE A O   
87   C CB  . ILE A 19  ? 0.29356 0.26082 0.33671 -0.02148 0.02736  -0.05525 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.35368 0.27391 0.37507 -0.02377 0.05207  -0.05523 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.24912 0.21646 0.29432 -0.00384 0.00951  -0.04489 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.39322 0.29755 0.40785 -0.04380 0.07880  -0.06641 26  ILE A CD1 
91   N N   . ALA A 20  ? 0.23566 0.31191 0.31533 -0.02227 -0.00309 -0.05912 27  ALA A N   
92   C CA  . ALA A 20  ? 0.26688 0.37648 0.35383 -0.00649 -0.01705 -0.05075 27  ALA A CA  
93   C C   . ALA A 20  ? 0.30823 0.46367 0.40043 -0.01596 -0.02103 -0.05873 27  ALA A C   
94   O O   . ALA A 20  ? 0.21531 0.38122 0.30510 -0.00180 -0.02941 -0.05015 27  ALA A O   
95   C CB  . ALA A 20  ? 0.22971 0.36214 0.32319 0.00627  -0.01789 -0.04471 27  ALA A CB  
96   N N   . GLN A 21  ? 0.26674 0.45033 0.36432 -0.04091 -0.01306 -0.07657 28  GLN A N   
97   C CA  . GLN A 21  ? 0.27429 0.50769 0.37461 -0.05412 -0.01722 -0.08944 28  GLN A CA  
98   C C   . GLN A 21  ? 0.28200 0.47868 0.36774 -0.05798 -0.01610 -0.09058 28  GLN A C   
99   O O   . GLN A 21  ? 0.28585 0.51211 0.36872 -0.05092 -0.02525 -0.08909 28  GLN A O   
100  C CB  . GLN A 21  ? 0.29862 0.56841 0.40789 -0.08790 -0.00559 -0.11440 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.48005 0.83301 0.59755 -0.10003 -0.01427 -0.13044 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.71039 1.09635 0.83513 -0.13812 0.00042  -0.15845 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.56981 0.90715 0.69232 -0.16102 0.02108  -0.16884 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.71295 1.16601 0.83633 -0.13884 -0.00504 -0.16616 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.26636 0.40052 0.34070 -0.06571 -0.00325 -0.09145 29  LEU A N   
106  C CA  . LEU A 22  ? 0.38082 0.47903 0.44121 -0.06501 -0.00033 -0.08942 29  LEU A CA  
107  C C   . LEU A 22  ? 0.37239 0.46822 0.43467 -0.03888 -0.01475 -0.07046 29  LEU A C   
108  O O   . LEU A 22  ? 0.31801 0.41804 0.37440 -0.03621 -0.01792 -0.06920 29  LEU A O   
109  C CB  . LEU A 22  ? 0.31871 0.35377 0.36519 -0.06827 0.01763  -0.08790 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.42720 0.42463 0.45988 -0.06016 0.02176  -0.08063 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.39556 0.39245 0.41504 -0.08155 0.03328  -0.09757 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.41868 0.36511 0.43902 -0.04884 0.03579  -0.07054 29  LEU A CD2 
113  N N   . MET A 23  ? 0.26520 0.35171 0.33387 -0.02101 -0.02079 -0.05697 30  MET A N   
114  C CA  . MET A 23  ? 0.22115 0.29514 0.29033 -0.00143 -0.02837 -0.04201 30  MET A CA  
115  C C   . MET A 23  ? 0.33157 0.44382 0.40149 0.01105  -0.03475 -0.03600 30  MET A C   
116  O O   . MET A 23  ? 0.34228 0.44556 0.40743 0.02083  -0.03545 -0.02768 30  MET A O   
117  C CB  . MET A 23  ? 0.18436 0.23698 0.25664 0.00982  -0.02997 -0.03413 30  MET A CB  
118  C CG  . MET A 23  ? 0.28892 0.30527 0.35706 0.00797  -0.02615 -0.03401 30  MET A CG  
119  S SD  . MET A 23  ? 0.31132 0.31251 0.37937 0.01801  -0.02864 -0.03038 30  MET A SD  
120  C CE  . MET A 23  ? 0.29643 0.28854 0.36841 0.02617  -0.03434 -0.02455 30  MET A CE  
121  N N   . SER A 24  ? 0.28734 0.44586 0.36229 0.01341  -0.03760 -0.03877 31  SER A N   
122  C CA  . SER A 24  ? 0.25787 0.46213 0.33002 0.03242  -0.04243 -0.03014 31  SER A CA  
123  C C   . SER A 24  ? 0.30540 0.54037 0.37098 0.02290  -0.04504 -0.04003 31  SER A C   
124  O O   . SER A 24  ? 0.32764 0.58046 0.38398 0.04296  -0.04713 -0.02870 31  SER A O   
125  C CB  . SER A 24  ? 0.29957 0.55737 0.38000 0.04049  -0.04480 -0.02980 31  SER A CB  
126  O OG  . SER A 24  ? 0.55589 0.83571 0.64685 0.01265  -0.04321 -0.04983 31  SER A OG  
127  N N   . LEU A 25  ? 0.23163 0.46892 0.29790 -0.00675 -0.04177 -0.06117 32  LEU A N   
128  C CA  . LEU A 25  ? 0.31267 0.57075 0.36830 -0.01933 -0.04196 -0.07411 32  LEU A CA  
129  C C   . LEU A 25  ? 0.37642 0.58442 0.42049 -0.00909 -0.03875 -0.06222 32  LEU A C   
130  O O   . LEU A 25  ? 0.25336 0.48161 0.28648 0.00074  -0.04153 -0.05900 32  LEU A O   
131  C CB  . LEU A 25  ? 0.26055 0.51716 0.31540 -0.05682 -0.03217 -0.10151 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.40215 0.67144 0.44252 -0.08212 -0.02642 -0.12471 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.51817 0.77812 0.55901 -0.12085 -0.00999 -0.15199 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.35237 0.56312 0.37515 -0.07666 -0.01961 -0.11718 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.28029 0.42860 0.32664 -0.00998 -0.03250 -0.05547 33  ILE A N   
136  C CA  . ILE A 26  ? 0.33681 0.44545 0.37724 -0.00094 -0.02891 -0.04432 33  ILE A CA  
137  C C   . ILE A 26  ? 0.37127 0.48591 0.41191 0.02452  -0.03221 -0.02545 33  ILE A C   
138  O O   . ILE A 26  ? 0.35355 0.46018 0.38590 0.03323  -0.02903 -0.01799 33  ILE A O   
139  C CB  . ILE A 26  ? 0.27638 0.33626 0.32166 -0.00459 -0.02293 -0.04119 33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.33089 0.37029 0.36628 -0.02417 -0.01130 -0.05555 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.34104 0.37389 0.38810 0.00724  -0.02118 -0.02791 33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.42721 0.43035 0.46415 -0.02255 -0.00430 -0.05145 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.28204 0.40628 0.32896 0.03790  -0.03470 -0.01680 34  ILE A N   
144  C CA  . ILE A 27  ? 0.39378 0.50871 0.43582 0.06304  -0.03013 0.00219  34  ILE A CA  
145  C C   . ILE A 27  ? 0.43292 0.59489 0.46144 0.08307  -0.03118 0.00958  34  ILE A C   
146  O O   . ILE A 27  ? 0.39463 0.54230 0.41124 0.10326  -0.02264 0.02529  34  ILE A O   
147  C CB  . ILE A 27  ? 0.39620 0.49639 0.44406 0.07149  -0.02792 0.00860  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.31656 0.37021 0.37360 0.05755  -0.02595 0.00419  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 0.35629 0.44987 0.39214 0.10045  -0.01741 0.02804  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.35863 0.39990 0.41919 0.06032  -0.02527 0.00453  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.40417 0.62638 0.43347 0.07807  -0.04007 -0.00203 35  ASN A N   
152  C CA  . ASN A 28  ? 0.28434 0.56942 0.30144 0.10272  -0.04325 0.00593  35  ASN A CA  
153  C C   . ASN A 28  ? 0.44865 0.77222 0.45415 0.09367  -0.04873 -0.00711 35  ASN A C   
154  O O   . ASN A 28  ? 0.40648 0.77339 0.39568 0.12071  -0.04956 0.00413  35  ASN A O   
155  C CB  . ASN A 28  ? 0.36493 0.71223 0.39192 0.10627  -0.05033 0.00121  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.44808 0.76269 0.47931 0.12438  -0.04275 0.01785  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.43881 0.70677 0.45784 0.14832  -0.03039 0.03848  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.61177 0.94664 0.65844 0.11134  -0.04698 0.00765  35  ASN A ND2 
159  N N   . THR A 29  ? 0.34456 0.65218 0.35373 0.05905  -0.05001 -0.02981 36  THR A N   
160  C CA  . THR A 29  ? 0.35318 0.69317 0.34752 0.04672  -0.05283 -0.04627 36  THR A CA  
161  C C   . THR A 29  ? 0.35475 0.66026 0.33157 0.06676  -0.04585 -0.02927 36  THR A C   
162  O O   . THR A 29  ? 0.36506 0.60315 0.34621 0.06744  -0.03665 -0.01782 36  THR A O   
163  C CB  . THR A 29  ? 0.27658 0.59155 0.27395 0.00503  -0.04842 -0.07401 36  THR A CB  
164  O OG1 . THR A 29  ? 0.36022 0.70277 0.37380 -0.01483 -0.05070 -0.08951 36  THR A OG1 
165  C CG2 . THR A 29  ? 0.34997 0.69540 0.32790 -0.01149 -0.04849 -0.09537 36  THR A CG2 
166  N N   . PHE A 30  ? 0.30044 0.65786 0.25762 0.08356  -0.04971 -0.02799 37  PHE A N   
167  C CA  . PHE A 30  ? 0.31845 0.64419 0.25602 0.10018  -0.04097 -0.01424 37  PHE A CA  
168  C C   . PHE A 30  ? 0.42020 0.70677 0.35368 0.06820  -0.03640 -0.03412 37  PHE A C   
169  O O   . PHE A 30  ? 0.35344 0.67478 0.27823 0.04315  -0.04112 -0.06145 37  PHE A O   
170  C CB  . PHE A 30  ? 0.34495 0.74019 0.25760 0.12979  -0.04566 -0.00743 37  PHE A CB  
171  C CG  . PHE A 30  ? 0.36813 0.72937 0.25763 0.14968  -0.03409 0.00855  37  PHE A CG  
172  C CD1 . PHE A 30  ? 0.46987 0.77317 0.35725 0.17768  -0.01723 0.03959  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 0.38650 0.76939 0.25540 0.13756  -0.03699 -0.00929 37  PHE A CD2 
174  C CE1 . PHE A 30  ? 0.44644 0.71685 0.31395 0.19463  -0.00323 0.05454  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 0.50855 0.85871 0.35529 0.15723  -0.02481 0.00656  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 0.42006 0.71489 0.26745 0.18625  -0.00778 0.03943  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.33879 0.55445 0.27747 0.06874  -0.02483 -0.02133 38  TYR A N   
178  C CA  . TYR A 31  ? 0.32000 0.49280 0.25473 0.04429  -0.01695 -0.03525 38  TYR A CA  
179  C C   . TYR A 31  ? 0.31943 0.43752 0.25735 0.05889  -0.00476 -0.01356 38  TYR A C   
180  O O   . TYR A 31  ? 0.32086 0.40724 0.27951 0.06162  -0.00166 -0.00153 38  TYR A O   
181  C CB  . TYR A 31  ? 0.32911 0.48146 0.27949 0.01639  -0.01651 -0.05154 38  TYR A CB  
182  C CG  . TYR A 31  ? 0.40338 0.50078 0.34785 -0.00042 -0.00291 -0.05877 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.43796 0.53339 0.35879 -0.01976 0.00519  -0.08027 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.42852 0.47857 0.38867 0.00423  0.00363  -0.04464 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.47761 0.51643 0.38787 -0.03001 0.02266  -0.08381 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.43057 0.43663 0.38335 -0.00396 0.01770  -0.04740 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.42104 0.41729 0.34758 -0.01912 0.02876  -0.06519 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.72829 0.67449 0.64264 -0.02237 0.04758  -0.06496 38  TYR A OH  
189  N N   . SER A 32  ? 0.36145 0.47269 0.27912 0.06660  0.00273  -0.01047 39  SER A N   
190  C CA  . SER A 32  ? 0.37244 0.44358 0.29323 0.08356  0.01601  0.01182  39  SER A CA  
191  C C   . SER A 32  ? 0.33532 0.35940 0.27105 0.06887  0.02513  0.01099  39  SER A C   
192  O O   . SER A 32  ? 0.43205 0.42951 0.38313 0.07746  0.03452  0.02755  39  SER A O   
193  C CB  . SER A 32  ? 0.37610 0.45990 0.26757 0.10111  0.02228  0.01766  39  SER A CB  
194  O OG  . SER A 32  ? 0.38948 0.52026 0.26599 0.12524  0.01626  0.02593  39  SER A OG  
195  N N   . ASN A 33  ? 0.33760 0.35246 0.26818 0.04782  0.02535  -0.00770 40  ASN A N   
196  C CA  . ASN A 33  ? 0.33701 0.31092 0.27458 0.04150  0.03718  -0.00548 40  ASN A CA  
197  C C   . ASN A 33  ? 0.35760 0.32173 0.32391 0.03753  0.03311  -0.00093 40  ASN A C   
198  O O   . ASN A 33  ? 0.40284 0.35241 0.36976 0.02615  0.03567  -0.01001 40  ASN A O   
199  C CB  . ASN A 33  ? 0.42410 0.38250 0.33587 0.02460  0.04612  -0.02548 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.49123 0.40596 0.40259 0.02628  0.06314  -0.01901 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.48180 0.38735 0.40595 0.04167  0.06881  -0.00049 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.48269 0.37124 0.37819 0.01150  0.07443  -0.03380 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.31779 0.32067 0.26245 0.00679  -0.02253 -0.00532 41  LYS A N   
204  C CA  . LYS A 34  ? 0.29099 0.31412 0.26289 0.01275  -0.00923 -0.00355 41  LYS A CA  
205  C C   . LYS A 34  ? 0.31044 0.32063 0.27835 0.01231  0.00241  -0.01487 41  LYS A C   
206  O O   . LYS A 34  ? 0.35594 0.37633 0.34071 0.01474  0.00835  -0.01488 41  LYS A O   
207  C CB  . LYS A 34  ? 0.33909 0.36360 0.31085 0.02674  -0.00142 0.00090  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.27450 0.32098 0.25636 0.03485  -0.00928 0.01554  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.42412 0.45450 0.39109 0.05337  -0.00381 0.01654  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.39242 0.44989 0.37014 0.07070  -0.00795 0.03317  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.30731 0.40569 0.30951 0.08880  0.00022  0.04651  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.33733 0.32865 0.28188 0.01297  0.00677  -0.02165 42  GLU A N   
213  C CA  . GLU A 35  ? 0.29814 0.28813 0.24580 0.01521  0.01948  -0.02581 42  GLU A CA  
214  C C   . GLU A 35  ? 0.32868 0.31760 0.28468 0.01137  0.01596  -0.03221 42  GLU A C   
215  O O   . GLU A 35  ? 0.31674 0.30933 0.28310 0.01259  0.02492  -0.03402 42  GLU A O   
216  C CB  . GLU A 35  ? 0.32361 0.30595 0.24506 0.02458  0.02888  -0.02492 42  GLU A CB  
217  C CG  . GLU A 35  ? 0.34276 0.29720 0.22408 0.03260  0.01943  -0.03481 42  GLU A CG  
218  C CD  . GLU A 35  ? 0.49493 0.44040 0.33625 0.05402  0.03279  -0.03244 42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.54348 0.50408 0.38499 0.05661  0.04172  -0.02027 42  GLU A OE1 
220  O OE2 . GLU A 35  ? 0.60561 0.52802 0.41127 0.07180  0.03483  -0.04076 42  GLU A OE2 
221  N N   . ILE A 36  ? 0.33115 0.31518 0.28477 0.00378  -0.00059 -0.03180 43  ILE A N   
222  C CA  . ILE A 36  ? 0.30622 0.28555 0.26651 -0.00350 -0.00839 -0.03391 43  ILE A CA  
223  C C   . ILE A 36  ? 0.29157 0.29838 0.28509 -0.00447 0.00096  -0.02816 43  ILE A C   
224  O O   . ILE A 36  ? 0.29884 0.30447 0.29963 -0.00978 -0.00218 -0.02862 43  ILE A O   
225  C CB  . ILE A 36  ? 0.38555 0.35175 0.33837 -0.01867 -0.03697 -0.02673 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.37121 0.37742 0.35818 -0.02658 -0.04343 -0.00653 43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.47764 0.39499 0.37643 -0.01325 -0.05154 -0.03727 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.34530 0.39350 0.37475 -0.03399 -0.04327 0.01251  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.23127 0.25504 0.23629 0.00371  0.01058  -0.02308 44  PHE A N   
230  C CA  . PHE A 37  ? 0.28797 0.32448 0.30611 0.01120  0.01886  -0.02005 44  PHE A CA  
231  C C   . PHE A 37  ? 0.30984 0.33022 0.32431 0.00966  0.02405  -0.02976 44  PHE A C   
232  O O   . PHE A 37  ? 0.24537 0.27119 0.26727 0.01066  0.02584  -0.02872 44  PHE A O   
233  C CB  . PHE A 37  ? 0.25719 0.29225 0.26719 0.02726  0.02426  -0.01708 44  PHE A CB  
234  C CG  . PHE A 37  ? 0.29018 0.29472 0.28321 0.02711  0.02469  -0.02480 44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.34635 0.34359 0.33240 0.02183  0.02270  -0.02353 44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.33027 0.31381 0.31443 0.02999  0.02364  -0.02875 44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.31594 0.29478 0.29511 0.01690  0.02078  -0.02086 44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.23825 0.19612 0.21351 0.02222  0.01622  -0.02759 44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.27454 0.23464 0.25157 0.01447  0.01534  -0.02103 44  PHE A CZ  
240  N N   . LEU A 38  ? 0.30277 0.30950 0.30833 0.00817  0.02694  -0.03473 45  LEU A N   
241  C CA  . LEU A 38  ? 0.21901 0.22100 0.22950 0.00664  0.03091  -0.03666 45  LEU A CA  
242  C C   . LEU A 38  ? 0.31519 0.31584 0.32630 0.00542  0.03035  -0.04165 45  LEU A C   
243  O O   . LEU A 38  ? 0.29370 0.29440 0.31349 0.00414  0.03092  -0.04252 45  LEU A O   
244  C CB  . LEU A 38  ? 0.19873 0.20274 0.20899 0.00599  0.03539  -0.02963 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.22761 0.23809 0.25405 0.00119  0.03612  -0.02158 45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.24132 0.23185 0.26691 -0.00498 0.02345  -0.02176 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.23108 0.26107 0.26778 -0.00069 0.04163  -0.00303 45  LEU A CD2 
248  N N   . ARG A 39  ? 0.29950 0.28967 0.29406 0.00648  0.02511  -0.04525 46  ARG A N   
249  C CA  . ARG A 39  ? 0.28854 0.26078 0.27185 0.00588  0.01697  -0.05065 46  ARG A CA  
250  C C   . ARG A 39  ? 0.30510 0.28707 0.30811 -0.00600 0.00899  -0.04493 46  ARG A C   
251  O O   . ARG A 39  ? 0.33225 0.30703 0.33735 -0.00734 0.00702  -0.04675 46  ARG A O   
252  C CB  . ARG A 39  ? 0.31658 0.25726 0.26401 0.00822  0.00249  -0.05562 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.42632 0.32969 0.35065 0.00450  -0.01732 -0.06058 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.52105 0.37658 0.39933 0.00258  -0.04359 -0.06461 46  ARG A CD  
255  N NE  . ARG A 39  ? 0.53736 0.41038 0.43972 -0.02195 -0.06247 -0.04978 46  ARG A NE  
256  C CZ  . ARG A 39  ? 0.66555 0.51144 0.53999 -0.02825 -0.08535 -0.04792 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 0.57243 0.36333 0.38281 -0.00874 -0.09195 -0.06352 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.57222 0.44851 0.48132 -0.05148 -0.10202 -0.02732 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.29043 0.29418 0.30877 -0.01151 0.00629  -0.03425 47  GLU A N   
260  C CA  . GLU A 40  ? 0.32295 0.34969 0.36253 -0.01855 0.00246  -0.02013 47  GLU A CA  
261  C C   . GLU A 40  ? 0.26332 0.29750 0.30781 -0.00846 0.01615  -0.02223 47  GLU A C   
262  O O   . GLU A 40  ? 0.24000 0.28007 0.29236 -0.01259 0.01428  -0.01609 47  GLU A O   
263  C CB  . GLU A 40  ? 0.24591 0.30649 0.30316 -0.01962 0.00013  -0.00147 47  GLU A CB  
264  C CG  . GLU A 40  ? 0.29674 0.34799 0.34967 -0.03472 -0.02152 0.00489  47  GLU A CG  
265  C CD  . GLU A 40  ? 0.43533 0.45428 0.47640 -0.05404 -0.04725 0.00604  47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.42095 0.45242 0.47976 -0.06324 -0.05115 0.01807  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.56851 0.54251 0.57490 -0.05793 -0.06566 -0.00480 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.23414 0.26157 0.26939 0.00326  0.02543  -0.02928 48  LEU A N   
269  C CA  . LEU A 41  ? 0.33033 0.34902 0.35802 0.01205  0.03000  -0.03206 48  LEU A CA  
270  C C   . LEU A 41  ? 0.29835 0.30284 0.32854 0.00473  0.02704  -0.03899 48  LEU A C   
271  O O   . LEU A 41  ? 0.27146 0.27253 0.29997 0.00639  0.02639  -0.03827 48  LEU A O   
272  C CB  . LEU A 41  ? 0.32085 0.32045 0.32966 0.02279  0.03011  -0.03586 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.23967 0.24991 0.23984 0.03830  0.03431  -0.02907 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.28797 0.26154 0.25906 0.04850  0.02817  -0.03481 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.23888 0.27433 0.23804 0.05596  0.04316  -0.01677 48  LEU A CD2 
276  N N   . ILE A 42  ? 0.24258 0.24170 0.27477 0.00082  0.02673  -0.04322 49  ILE A N   
277  C CA  . ILE A 42  ? 0.30099 0.29575 0.33812 0.00039  0.02678  -0.04516 49  ILE A CA  
278  C C   . ILE A 42  ? 0.26319 0.25114 0.29805 -0.00213 0.02157  -0.04694 49  ILE A C   
279  O O   . ILE A 42  ? 0.29821 0.28253 0.33727 -0.00204 0.02001  -0.04694 49  ILE A O   
280  C CB  . ILE A 42  ? 0.23984 0.23932 0.27609 0.00633  0.03285  -0.04363 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.22562 0.23515 0.27251 0.00241  0.03377  -0.03377 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.33396 0.33458 0.37192 0.01532  0.03622  -0.04289 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.30263 0.32897 0.35115 0.00942  0.04335  -0.02465 49  ILE A CD1 
284  N N   . SER A 43  ? 0.29086 0.27371 0.31866 -0.00730 0.01402  -0.04566 50  SER A N   
285  C CA  . SER A 43  ? 0.28525 0.25401 0.30925 -0.01588 0.00065  -0.04245 50  SER A CA  
286  C C   . SER A 43  ? 0.27958 0.26936 0.32092 -0.02180 0.00214  -0.03055 50  SER A C   
287  O O   . SER A 43  ? 0.24495 0.22492 0.28630 -0.02637 -0.00439 -0.02802 50  SER A O   
288  C CB  . SER A 43  ? 0.32053 0.27448 0.33285 -0.02666 -0.01723 -0.03785 50  SER A CB  
289  O OG  . SER A 43  ? 0.52764 0.48255 0.55036 -0.04492 -0.03501 -0.02209 50  SER A OG  
290  N N   . ASN A 44  ? 0.24525 0.26194 0.29552 -0.01705 0.01152  -0.02209 51  ASN A N   
291  C CA  . ASN A 44  ? 0.31450 0.35062 0.36934 -0.01130 0.01831  -0.01038 51  ASN A CA  
292  C C   . ASN A 44  ? 0.31659 0.33181 0.35897 -0.00431 0.02068  -0.02178 51  ASN A C   
293  O O   . ASN A 44  ? 0.25002 0.26668 0.29206 -0.00515 0.01949  -0.01541 51  ASN A O   
294  C CB  . ASN A 44  ? 0.26552 0.32641 0.31765 0.00508  0.03031  -0.00124 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.30766 0.40829 0.38360 -0.00204 0.02791  0.02256  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.29344 0.40030 0.38748 -0.02421 0.01248  0.03571  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.27294 0.39796 0.34755 0.01646  0.03924  0.03125  51  ASN A ND2 
298  N N   . SER A 45  ? 0.21242 0.21042 0.24692 0.00012  0.02124  -0.03420 52  SER A N   
299  C CA  . SER A 45  ? 0.25568 0.23632 0.28460 0.00123  0.01666  -0.03925 52  SER A CA  
300  C C   . SER A 45  ? 0.32839 0.30624 0.36822 -0.00485 0.01238  -0.03982 52  SER A C   
301  O O   . SER A 45  ? 0.26608 0.23672 0.30323 -0.00478 0.00797  -0.03830 52  SER A O   
302  C CB  . SER A 45  ? 0.26960 0.24081 0.29888 -0.00004 0.01290  -0.04251 52  SER A CB  
303  O OG  . SER A 45  ? 0.27199 0.22871 0.27955 0.00752  0.01076  -0.04337 52  SER A OG  
304  N N   . SER A 46  ? 0.26461 0.24077 0.30837 -0.00650 0.01182  -0.04262 53  SER A N   
305  C CA  . SER A 46  ? 0.29305 0.25469 0.33427 -0.00471 0.00614  -0.04471 53  SER A CA  
306  C C   . SER A 46  ? 0.32860 0.28338 0.36763 -0.01390 -0.00281 -0.03776 53  SER A C   
307  O O   . SER A 46  ? 0.29265 0.23666 0.33061 -0.01263 -0.00767 -0.03729 53  SER A O   
308  C CB  . SER A 46  ? 0.24704 0.19225 0.27272 0.00268  0.00437  -0.05088 53  SER A CB  
309  O OG  . SER A 46  ? 0.35851 0.27811 0.36827 0.01317  -0.00203 -0.05472 53  SER A OG  
310  N N   . ASP A 47  ? 0.27777 0.24458 0.32015 -0.02377 -0.00562 -0.02722 54  ASP A N   
311  C CA  . ASP A 47  ? 0.22308 0.19656 0.27148 -0.03544 -0.01380 -0.01025 54  ASP A CA  
312  C C   . ASP A 47  ? 0.35643 0.34358 0.40397 -0.02711 -0.00386 -0.00562 54  ASP A C   
313  O O   . ASP A 47  ? 0.28503 0.26704 0.33214 -0.03227 -0.01012 0.00285  54  ASP A O   
314  C CB  . ASP A 47  ? 0.24207 0.24315 0.30500 -0.04777 -0.01783 0.01035  54  ASP A CB  
315  C CG  . ASP A 47  ? 0.51303 0.48680 0.56813 -0.06094 -0.03830 0.00807  54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.48027 0.40995 0.50999 -0.05365 -0.04571 -0.01168 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.37994 0.37574 0.45071 -0.07574 -0.04803 0.02821  54  ASP A OD2 
318  N N   . ALA A 48  ? 0.24981 0.24538 0.28895 -0.01319 0.00812  -0.01116 55  ALA A N   
319  C CA  . ALA A 48  ? 0.28721 0.27812 0.30768 -0.00095 0.01226  -0.01007 55  ALA A CA  
320  C C   . ALA A 48  ? 0.29264 0.25811 0.31040 -0.00379 0.00208  -0.02020 55  ALA A C   
321  O O   . ALA A 48  ? 0.25721 0.21486 0.26267 -0.00079 -0.00122 -0.01575 55  ALA A O   
322  C CB  . ALA A 48  ? 0.24766 0.23281 0.24461 0.01663  0.01925  -0.01601 55  ALA A CB  
323  N N   . LEU A 49  ? 0.26347 0.22132 0.29355 -0.00722 -0.00203 -0.02994 56  LEU A N   
324  C CA  . LEU A 49  ? 0.28002 0.22788 0.31733 -0.00765 -0.01030 -0.03209 56  LEU A CA  
325  C C   . LEU A 49  ? 0.32532 0.26533 0.36522 -0.00997 -0.01525 -0.02903 56  LEU A C   
326  O O   . LEU A 49  ? 0.30440 0.23640 0.34423 -0.00887 -0.02236 -0.02657 56  LEU A O   
327  C CB  . LEU A 49  ? 0.30494 0.26166 0.35932 -0.00559 -0.00885 -0.03440 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.25285 0.21006 0.30632 -0.00878 -0.01253 -0.03289 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.27785 0.25460 0.35041 -0.00769 -0.00573 -0.02969 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.32359 0.26911 0.37699 -0.01471 -0.03000 -0.02612 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.26690 0.20210 0.30526 -0.01452 -0.01665 -0.02798 57  ASP A N   
332  C CA  . ASP A 50  ? 0.30932 0.22210 0.34076 -0.01966 -0.02941 -0.02342 57  ASP A CA  
333  C C   . ASP A 50  ? 0.34132 0.26153 0.37249 -0.02821 -0.03234 -0.00878 57  ASP A C   
334  O O   . ASP A 50  ? 0.28685 0.18878 0.31310 -0.02978 -0.04255 -0.00524 57  ASP A O   
335  C CB  . ASP A 50  ? 0.30077 0.19556 0.32305 -0.02868 -0.04033 -0.02161 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.39594 0.26869 0.40219 -0.01296 -0.03978 -0.03703 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.37218 0.25550 0.38357 0.00507  -0.02784 -0.04387 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.41358 0.25981 0.40087 -0.01809 -0.05278 -0.03858 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.30846 0.25616 0.34105 -0.02919 -0.02196 0.00175  58  LYS A N   
340  C CA  . LYS A 51  ? 0.34441 0.30731 0.37239 -0.03084 -0.01969 0.02114  58  LYS A CA  
341  C C   . LYS A 51  ? 0.33989 0.28650 0.35031 -0.02010 -0.02082 0.01401  58  LYS A C   
342  O O   . LYS A 51  ? 0.31755 0.25807 0.32340 -0.02415 -0.02738 0.02491  58  LYS A O   
343  C CB  . LYS A 51  ? 0.32109 0.32203 0.34851 -0.02262 -0.00331 0.03638  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.34675 0.37610 0.39981 -0.03899 -0.00665 0.05723  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.32398 0.39876 0.37968 -0.02311 0.01333  0.07252  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.44046 0.54534 0.52775 -0.04143 0.00630  0.09253  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.40636 0.57287 0.50469 -0.02356 0.02757  0.12061  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.30519 0.24149 0.30478 -0.00930 -0.01908 -0.00140 59  ILE A N   
349  C CA  . ILE A 52  ? 0.31428 0.22928 0.29510 -0.00335 -0.02848 -0.00543 59  ILE A CA  
350  C C   . ILE A 52  ? 0.39013 0.29474 0.39032 -0.00992 -0.04099 -0.00784 59  ILE A C   
351  O O   . ILE A 52  ? 0.39666 0.28821 0.38704 -0.00920 -0.05086 -0.00379 59  ILE A O   
352  C CB  . ILE A 52  ? 0.30722 0.20534 0.26853 0.00437  -0.03320 -0.01621 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.36582 0.23119 0.29477 0.00889  -0.05056 -0.01705 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.26271 0.16744 0.25489 -0.00392 -0.03740 -0.02300 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.46935 0.32811 0.35880 0.02354  -0.04365 -0.00841 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.31027 0.21912 0.33263 -0.01143 -0.04021 -0.01339 60  ARG A N   
357  C CA  . ARG A 53  ? 0.33808 0.23787 0.37203 -0.00706 -0.04853 -0.01369 60  ARG A CA  
358  C C   . ARG A 53  ? 0.35386 0.23405 0.37671 -0.01169 -0.05692 -0.00647 60  ARG A C   
359  O O   . ARG A 53  ? 0.36420 0.23278 0.38604 -0.00792 -0.06649 -0.00302 60  ARG A O   
360  C CB  . ARG A 53  ? 0.33934 0.24372 0.38515 0.00270  -0.04265 -0.02025 60  ARG A CB  
361  C CG  . ARG A 53  ? 0.45632 0.35543 0.50861 0.01942  -0.04687 -0.01832 60  ARG A CG  
362  C CD  . ARG A 53  ? 0.63740 0.53733 0.68711 0.04021  -0.03746 -0.02356 60  ARG A CD  
363  N NE  . ARG A 53  ? 0.58619 0.53004 0.66676 0.04968  -0.02702 -0.01417 60  ARG A NE  
364  C CZ  . ARG A 53  ? 0.63687 0.59814 0.72036 0.06353  -0.01328 -0.01433 60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.61586 0.54641 0.66664 0.07104  -0.01004 -0.02798 60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.52927 0.54001 0.64911 0.06824  -0.00556 0.00339  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.32424 0.20153 0.34128 -0.02245 -0.05691 0.00012  61  TYR A N   
368  C CA  . TYR A 54  ? 0.32023 0.17799 0.32913 -0.03375 -0.07079 0.01413  61  TYR A CA  
369  C C   . TYR A 54  ? 0.40489 0.27304 0.40706 -0.03545 -0.06962 0.02731  61  TYR A C   
370  O O   . TYR A 54  ? 0.40437 0.25187 0.39994 -0.03814 -0.08245 0.03441  61  TYR A O   
371  C CB  . TYR A 54  ? 0.32861 0.18993 0.34047 -0.05212 -0.07634 0.02853  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.51860 0.35315 0.52396 -0.07042 -0.09940 0.04831  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.45030 0.22596 0.43388 -0.06813 -0.12283 0.03866  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.40343 0.26931 0.41953 -0.08659 -0.09845 0.07944  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.45820 0.19643 0.42947 -0.08730 -0.15097 0.05763  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.41036 0.25366 0.42455 -0.10846 -0.12319 0.10392  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.48908 0.26333 0.48013 -0.11153 -0.15245 0.09190  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.59682 0.34197 0.57983 -0.13319 -0.18193 0.11503  61  TYR A OH  
379  N N   . GLU A 55  ? 0.38741 0.28091 0.38256 -0.02989 -0.05529 0.03041  62  GLU A N   
380  C CA  . GLU A 55  ? 0.41949 0.31523 0.39282 -0.02393 -0.05352 0.04165  62  GLU A CA  
381  C C   . GLU A 55  ? 0.42860 0.29907 0.39320 -0.01735 -0.06653 0.03012  62  GLU A C   
382  O O   . GLU A 55  ? 0.51159 0.37105 0.46061 -0.01691 -0.07399 0.03995  62  GLU A O   
383  C CB  . GLU A 55  ? 0.38225 0.29787 0.33301 -0.00892 -0.03616 0.04456  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.61989 0.57704 0.58084 -0.01174 -0.02109 0.07073  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.72481 0.70206 0.65267 0.01576  -0.00007 0.07713  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.65700 0.59979 0.54241 0.03540  -0.00278 0.05829  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.64939 0.67437 0.59032 0.01945  0.01653  0.10354  62  GLU A OE2 
388  N N   . SER A 56  ? 0.41947 0.28592 0.39768 -0.01345 -0.07060 0.01445  63  SER A N   
389  C CA  . SER A 56  ? 0.43354 0.28802 0.41577 -0.01040 -0.08609 0.01175  63  SER A CA  
390  C C   . SER A 56  ? 0.50396 0.34968 0.50130 -0.00919 -0.09515 0.01619  63  SER A C   
391  O O   . SER A 56  ? 0.46720 0.30787 0.46933 -0.00581 -0.10860 0.01998  63  SER A O   
392  C CB  . SER A 56  ? 0.42464 0.29065 0.42773 -0.00932 -0.08851 0.00443  63  SER A CB  
393  O OG  . SER A 56  ? 0.43123 0.31313 0.46283 -0.00498 -0.07976 0.00131  63  SER A OG  
394  N N   . LEU A 57  ? 0.48514 0.32270 0.48543 -0.01117 -0.09236 0.01696  64  LEU A N   
395  C CA  . LEU A 57  ? 0.56603 0.37871 0.56627 -0.00442 -0.10465 0.01886  64  LEU A CA  
396  C C   . LEU A 57  ? 0.61557 0.41196 0.60095 -0.01065 -0.11711 0.03183  64  LEU A C   
397  O O   . LEU A 57  ? 0.68859 0.46844 0.67494 -0.00068 -0.12912 0.03349  64  LEU A O   
398  C CB  . LEU A 57  ? 0.51910 0.30619 0.50934 -0.00699 -0.10811 0.01626  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.50030 0.29293 0.49608 0.00529  -0.09807 0.00239  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.50492 0.25357 0.47565 0.00175  -0.11101 -0.00025 64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.50825 0.31368 0.51756 0.03227  -0.09276 -0.00278 64  LEU A CD2 
402  N N   . THR A 58  ? 0.60659 0.41100 0.57712 -0.02313 -0.11276 0.04400  65  THR A N   
403  C CA  . THR A 58  ? 0.75542 0.54902 0.70799 -0.02779 -0.12170 0.06019  65  THR A CA  
404  C C   . THR A 58  ? 0.74386 0.54573 0.67384 -0.02051 -0.11806 0.06068  65  THR A C   
405  O O   . THR A 58  ? 0.73709 0.52811 0.64473 -0.02022 -0.12511 0.07330  65  THR A O   
406  C CB  . THR A 58  ? 0.80309 0.60086 0.75131 -0.04525 -0.12127 0.08376  65  THR A CB  
407  O OG1 . THR A 58  ? 0.77054 0.60575 0.71889 -0.04622 -0.10114 0.09116  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.61466 0.38236 0.57136 -0.05569 -0.13709 0.08332  65  THR A CG2 
409  N N   . ASP A 59  ? 0.71389 0.53639 0.56668 0.11960  -0.03264 0.09685  66  ASP A N   
410  C CA  . ASP A 59  ? 0.61577 0.48093 0.48047 0.11305  -0.05265 0.09776  66  ASP A CA  
411  C C   . ASP A 59  ? 0.53580 0.44609 0.44178 0.11432  -0.06237 0.09347  66  ASP A C   
412  O O   . ASP A 59  ? 0.50112 0.42339 0.41723 0.09822  -0.06282 0.07640  66  ASP A O   
413  C CB  . ASP A 59  ? 0.57994 0.44018 0.42315 0.08966  -0.05331 0.08430  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.72163 0.61078 0.56152 0.08413  -0.07194 0.08404  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.68922 0.60442 0.54435 0.09398  -0.08852 0.09488  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.69786 0.58283 0.51778 0.06966  -0.06986 0.07406  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.62826 0.56642 0.56101 0.13370  -0.06974 0.11127  67  PRO A N   
418  C CA  . PRO A 60  ? 0.43421 0.41978 0.41020 0.13253  -0.07930 0.11082  67  PRO A CA  
419  C C   . PRO A 60  ? 0.52247 0.53339 0.50053 0.10858  -0.09946 0.09841  67  PRO A C   
420  O O   . PRO A 60  ? 0.45231 0.48725 0.45660 0.09953  -0.10294 0.08998  67  PRO A O   
421  C CB  . PRO A 60  ? 0.55233 0.57048 0.55610 0.15644  -0.08713 0.13884  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.61294 0.59121 0.58589 0.17561  -0.07611 0.15245  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.64677 0.56944 0.57413 0.16037  -0.06303 0.13391  67  PRO A CD  
424  N N   . SER A 61  ? 0.51611 0.51690 0.46202 0.09871  -0.11146 0.09719  68  SER A N   
425  C CA  . SER A 61  ? 0.42270 0.43616 0.35886 0.07809  -0.12913 0.08483  68  SER A CA  
426  C C   . SER A 61  ? 0.56656 0.56657 0.49877 0.06418  -0.11686 0.06165  68  SER A C   
427  O O   . SER A 61  ? 0.49222 0.49995 0.42020 0.04977  -0.12821 0.05035  68  SER A O   
428  C CB  . SER A 61  ? 0.45676 0.45234 0.34850 0.07323  -0.13957 0.08774  68  SER A CB  
429  O OG  . SER A 61  ? 0.53706 0.49566 0.39717 0.07217  -0.11949 0.07963  68  SER A OG  
430  N N   . LYS A 62  ? 0.38453 0.36224 0.31532 0.06764  -0.09496 0.05537  69  LYS A N   
431  C CA  . LYS A 62  ? 0.42098 0.39310 0.35414 0.05561  -0.08473 0.03720  69  LYS A CA  
432  C C   . LYS A 62  ? 0.46526 0.46320 0.43211 0.05253  -0.09014 0.03231  69  LYS A C   
433  O O   . LYS A 62  ? 0.39317 0.39059 0.36136 0.04199  -0.08693 0.01818  69  LYS A O   
434  C CB  . LYS A 62  ? 0.48862 0.43403 0.41437 0.05692  -0.06447 0.03472  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.58595 0.50425 0.47831 0.05477  -0.05746 0.03955  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.59745 0.51176 0.47769 0.03968  -0.04918 0.02856  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.53544 0.42709 0.38592 0.03574  -0.04051 0.03646  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.75783 0.65426 0.60432 0.02217  -0.02987 0.03026  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.35066 0.37314 0.34622 0.06247  -0.09716 0.04608  70  LEU A N   
440  C CA  . LEU A 63  ? 0.35379 0.40543 0.38441 0.05867  -0.10230 0.04560  70  LEU A CA  
441  C C   . LEU A 63  ? 0.36049 0.43919 0.39925 0.04625  -0.12801 0.05036  70  LEU A C   
442  O O   . LEU A 63  ? 0.34491 0.45323 0.41674 0.04119  -0.13547 0.05527  70  LEU A O   
443  C CB  . LEU A 63  ? 0.39794 0.46362 0.45869 0.07772  -0.09063 0.06032  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.44869 0.47878 0.49451 0.08776  -0.06598 0.05434  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.37228 0.41182 0.44212 0.10944  -0.05223 0.06839  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.35426 0.36992 0.39115 0.07186  -0.05926 0.03429  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.33825 0.40522 0.34424 0.03931  -0.14220 0.04973  71  ASP A N   
448  C CA  . ASP A 64  ? 0.38941 0.47148 0.39062 0.02239  -0.16937 0.05140  71  ASP A CA  
449  C C   . ASP A 64  ? 0.37062 0.44338 0.36813 0.00520  -0.17112 0.03341  71  ASP A C   
450  O O   . ASP A 64  ? 0.43009 0.51836 0.43592 -0.01129 -0.19233 0.03594  71  ASP A O   
451  C CB  . ASP A 64  ? 0.39398 0.45340 0.34700 0.01828  -0.18159 0.05100  71  ASP A CB  
452  C CG  . ASP A 64  ? 0.62611 0.69939 0.58362 0.03324  -0.18733 0.07346  71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.56410 0.66838 0.56487 0.04728  -0.18419 0.09097  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.67705 0.72883 0.59290 0.03300  -0.19334 0.07488  71  ASP A OD2 
455  N N   . SER A 65  ? 0.36187 0.40936 0.34685 0.00781  -0.15009 0.01708  72  SER A N   
456  C CA  . SER A 65  ? 0.34446 0.38047 0.32596 -0.00374 -0.14803 0.00157  72  SER A CA  
457  C C   . SER A 65  ? 0.45432 0.51499 0.48014 -0.00389 -0.14279 0.00530  72  SER A C   
458  O O   . SER A 65  ? 0.47195 0.52312 0.49745 -0.01227 -0.13980 -0.00576 72  SER A O   
459  C CB  . SER A 65  ? 0.41204 0.41843 0.36657 0.00129  -0.12757 -0.01305 72  SER A CB  
460  O OG  . SER A 65  ? 0.40307 0.41163 0.36905 0.01353  -0.10985 -0.00822 72  SER A OG  
461  N N   . GLY A 66  ? 0.37587 0.46548 0.43696 0.00733  -0.13956 0.02166  73  GLY A N   
462  C CA  . GLY A 66  ? 0.35968 0.47224 0.46000 0.01019  -0.13074 0.02705  73  GLY A CA  
463  C C   . GLY A 66  ? 0.36999 0.49187 0.48983 0.03200  -0.11264 0.03909  73  GLY A C   
464  O O   . GLY A 66  ? 0.36830 0.46184 0.46709 0.04142  -0.09576 0.03149  73  GLY A O   
465  N N   . LYS A 67  ? 0.32646 0.48668 0.48514 0.04002  -0.11542 0.05927  74  LYS A N   
466  C CA  . LYS A 67  ? 0.37157 0.53545 0.54395 0.06574  -0.09555 0.07256  74  LYS A CA  
467  C C   . LYS A 67  ? 0.29074 0.44610 0.47181 0.07315  -0.07251 0.06702  74  LYS A C   
468  O O   . LYS A 67  ? 0.29492 0.42734 0.46418 0.09250  -0.05152 0.06852  74  LYS A O   
469  C CB  . LYS A 67  ? 0.40590 0.61875 0.61802 0.07658  -0.10554 0.10086  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.48783 0.70523 0.68609 0.07565  -0.12597 0.11043  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.58165 0.84815 0.81884 0.08649  -0.13353 0.13834  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.58479 0.83950 0.81161 0.11443  -0.12285 0.15237  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.74514 1.03064 0.98303 0.11127  -0.14173 0.16878  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.20799 0.37532 0.40336 0.05766  -0.07601 0.06062  75  GLU A N   
475  C CA  . GLU A 68  ? 0.28081 0.44185 0.48281 0.06393  -0.05540 0.05712  75  GLU A CA  
476  C C   . GLU A 68  ? 0.29069 0.40492 0.45285 0.06048  -0.04450 0.03563  75  GLU A C   
477  O O   . GLU A 68  ? 0.36332 0.46150 0.50472 0.04563  -0.05498 0.02168  75  GLU A O   
478  C CB  . GLU A 68  ? 0.26625 0.45622 0.49709 0.04741  -0.06349 0.06019  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.30267 0.54851 0.58237 0.04830  -0.07250 0.08623  75  GLU A CG  
480  C CD  . GLU A 68  ? 0.71965 0.98503 1.00358 0.03520  -0.10113 0.09389  75  GLU A CD  
481  O OE1 . GLU A 68  ? 0.78194 1.02514 1.03909 0.01301  -0.11933 0.07804  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.68831 0.98112 0.99052 0.04738  -0.10228 0.11269  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.24535 0.33780 0.39556 0.07440  -0.02311 0.03449  76  LEU A N   
484  C CA  . LEU A 69  ? 0.27940 0.33025 0.39294 0.06899  -0.01421 0.01750  76  LEU A CA  
485  C C   . LEU A 69  ? 0.26794 0.31702 0.38463 0.06846  -0.00222 0.01460  76  LEU A C   
486  O O   . LEU A 69  ? 0.24971 0.28948 0.36274 0.08492  0.01602  0.02145  76  LEU A O   
487  C CB  . LEU A 69  ? 0.32569 0.33954 0.40843 0.08228  -0.00194 0.01805  76  LEU A CB  
488  C CG  . LEU A 69  ? 0.32217 0.33151 0.39579 0.08424  -0.01129 0.02234  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.50090 0.46292 0.53735 0.09435  0.00260  0.02171  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.25730 0.27055 0.32389 0.06416  -0.02762 0.01145  76  LEU A CD2 
491  N N   . HIS A 70  ? 0.22590 0.28021 0.34533 0.05177  -0.01060 0.00532  77  HIS A N   
492  C CA  . HIS A 70  ? 0.19627 0.25271 0.32073 0.05058  -0.00108 0.00514  77  HIS A CA  
493  C C   . HIS A 70  ? 0.20692 0.24970 0.31554 0.03490  -0.00763 -0.00831 77  HIS A C   
494  O O   . HIS A 70  ? 0.23363 0.27041 0.33240 0.02610  -0.01841 -0.01621 77  HIS A O   
495  C CB  . HIS A 70  ? 0.23141 0.32822 0.39647 0.04996  -0.00407 0.01925  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.17679 0.29217 0.35739 0.03229  -0.02606 0.01786  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.30508 0.44963 0.51011 0.03023  -0.03950 0.02992  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.38594 0.49025 0.55608 0.01633  -0.03686 0.00634  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.23502 0.37996 0.43813 0.01122  -0.05856 0.02376  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.32744 0.44623 0.50898 0.00451  -0.05546 0.00928  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.18366 0.22323 0.29017 0.03362  0.00057  -0.00861 78  ILE A N   
502  C CA  . ILE A 71  ? 0.25287 0.28377 0.34805 0.02167  -0.00457 -0.01716 78  ILE A CA  
503  C C   . ILE A 71  ? 0.23467 0.28276 0.35066 0.01792  -0.00368 -0.01088 78  ILE A C   
504  O O   . ILE A 71  ? 0.21386 0.26825 0.33724 0.02567  0.00938  -0.00208 78  ILE A O   
505  C CB  . ILE A 71  ? 0.31736 0.31896 0.37826 0.02120  0.00329  -0.02327 78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.27268 0.25320 0.31093 0.02139  0.00241  -0.02784 78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.22646 0.22747 0.28118 0.00982  -0.00408 -0.02798 78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.28973 0.23792 0.28985 0.01411  0.00532  -0.03380 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.17057 0.22303 0.29326 0.00704  -0.01553 -0.01436 79  ASN A N   
510  C CA  . ASN A 72  ? 0.22494 0.28605 0.36221 0.00027  -0.01604 -0.00870 79  ASN A CA  
511  C C   . ASN A 72  ? 0.24396 0.28828 0.36322 -0.00366 -0.01681 -0.01453 79  ASN A C   
512  O O   . ASN A 72  ? 0.21606 0.25076 0.32223 -0.00465 -0.02333 -0.02218 79  ASN A O   
513  C CB  . ASN A 72  ? 0.21064 0.28411 0.36693 -0.01040 -0.03027 -0.00581 79  ASN A CB  
514  C CG  . ASN A 72  ? 0.25798 0.35691 0.43793 -0.00821 -0.03300 0.00446  79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.24829 0.36242 0.44116 0.00287  -0.01988 0.01463  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.22803 0.33074 0.41136 -0.01745 -0.04966 0.00315  79  ASN A ND2 
517  N N   . LEU A 73  ? 0.23562 0.27945 0.35570 -0.00463 -0.00921 -0.00837 80  LEU A N   
518  C CA  . LEU A 73  ? 0.18578 0.21663 0.29195 -0.00783 -0.01089 -0.00986 80  LEU A CA  
519  C C   . LEU A 73  ? 0.20567 0.23788 0.32638 -0.01598 -0.01434 -0.00353 80  LEU A C   
520  O O   . LEU A 73  ? 0.18391 0.22773 0.31986 -0.01899 -0.00730 0.00664  80  LEU A O   
521  C CB  . LEU A 73  ? 0.23435 0.25583 0.31981 -0.00380 -0.00018 -0.00750 80  LEU A CB  
522  C CG  . LEU A 73  ? 0.21499 0.22562 0.27853 0.00125  0.00457  -0.01297 80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.22573 0.21828 0.25954 0.00347  0.01531  -0.01091 80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.21354 0.22053 0.26766 -0.00287 -0.00728 -0.02062 80  LEU A CD2 
525  N N   . ILE A 74  ? 0.20999 0.22842 0.32440 -0.01929 -0.02373 -0.00825 81  ILE A N   
526  C CA  . ILE A 74  ? 0.26682 0.27427 0.38641 -0.02935 -0.02917 -0.00433 81  ILE A CA  
527  C C   . ILE A 74  ? 0.32152 0.30772 0.42403 -0.02555 -0.02763 -0.00318 81  ILE A C   
528  O O   . ILE A 74  ? 0.26267 0.23445 0.35149 -0.01840 -0.03131 -0.00906 81  ILE A O   
529  C CB  . ILE A 74  ? 0.25095 0.24925 0.36901 -0.03570 -0.04146 -0.01120 81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.24873 0.27100 0.38239 -0.03627 -0.04427 -0.01096 81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.25940 0.23990 0.37748 -0.05151 -0.04907 -0.00692 81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.26230 0.27492 0.38830 -0.04259 -0.05783 -0.01777 81  ILE A CD1 
533  N N   . PRO A 75  ? 0.28274 0.26771 0.38568 -0.02814 -0.02075 0.00648  82  PRO A N   
534  C CA  . PRO A 75  ? 0.26138 0.22442 0.34824 -0.02443 -0.02029 0.01049  82  PRO A CA  
535  C C   . PRO A 75  ? 0.30395 0.23988 0.38772 -0.03459 -0.02526 0.01278  82  PRO A C   
536  O O   . PRO A 75  ? 0.29324 0.23314 0.39104 -0.05022 -0.02825 0.01652  82  PRO A O   
537  C CB  . PRO A 75  ? 0.24787 0.21900 0.33185 -0.02402 -0.01038 0.02054  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.32274 0.31385 0.42706 -0.03182 -0.00392 0.02525  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.25536 0.25924 0.37200 -0.03178 -0.01069 0.01610  82  PRO A CD  
540  N N   . ASN A 76  ? 0.29421 0.20130 0.35823 -0.02581 -0.02641 0.01199  83  ASN A N   
541  C CA  . ASN A 76  ? 0.34101 0.20694 0.38972 -0.03384 -0.03006 0.01307  83  ASN A CA  
542  C C   . ASN A 76  ? 0.35987 0.20197 0.39077 -0.02097 -0.02429 0.02163  83  ASN A C   
543  O O   . ASN A 76  ? 0.39899 0.23616 0.41921 -0.00121 -0.02238 0.01996  83  ASN A O   
544  C CB  . ASN A 76  ? 0.40110 0.24259 0.43393 -0.03214 -0.03696 0.00029  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.57588 0.36449 0.58373 -0.04550 -0.04253 -0.00080 83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.49350 0.24802 0.48346 -0.04176 -0.03790 0.00595  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.53953 0.31733 0.54212 -0.06247 -0.05377 -0.00871 83  ASN A ND2 
548  N N   . LYS A 77  ? 0.38708 0.21763 0.41680 -0.03140 -0.02095 0.03340  84  LYS A N   
549  C CA  . LYS A 77  ? 0.48147 0.29011 0.49368 -0.01898 -0.01562 0.04443  84  LYS A CA  
550  C C   . LYS A 77  ? 0.58239 0.33555 0.56650 -0.01131 -0.01622 0.04284  84  LYS A C   
551  O O   . LYS A 77  ? 0.57512 0.31276 0.54464 0.00941  -0.01142 0.05063  84  LYS A O   
552  C CB  . LYS A 77  ? 0.42933 0.24051 0.44579 -0.03268 -0.01008 0.05880  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.46211 0.31766 0.49312 -0.03169 -0.00430 0.06270  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.55001 0.40451 0.58019 -0.04221 0.00491  0.07859  84  LYS A CD  
555  C CE  . LYS A 77  ? 0.48021 0.36962 0.51478 -0.03877 0.01380  0.08139  84  LYS A CE  
556  N NZ  . LYS A 77  ? 0.53872 0.45848 0.59534 -0.04220 0.01409  0.07145  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.55056 0.27085 0.52343 -0.02710 -0.02220 0.03394  85  GLN A N   
558  C CA  . GLN A 78  ? 0.71131 0.36534 0.64566 -0.01954 -0.02134 0.03014  85  GLN A CA  
559  C C   . GLN A 78  ? 0.63121 0.28364 0.55437 0.01044  -0.01617 0.02218  85  GLN A C   
560  O O   . GLN A 78  ? 0.69069 0.30987 0.59105 0.03490  -0.00743 0.02782  85  GLN A O   
561  C CB  . GLN A 78  ? 0.67647 0.29214 0.59485 -0.04875 -0.03206 0.02174  85  GLN A CB  
562  C CG  . GLN A 78  ? 0.87254 0.46779 0.79082 -0.07744 -0.03554 0.03412  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.04939 0.71146 1.01384 -0.09301 -0.03526 0.04506  85  GLN A CD  
564  O OE1 . GLN A 78  ? 0.95467 0.66293 0.94714 -0.10077 -0.04064 0.03979  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 0.99799 0.66292 0.96763 -0.09548 -0.02715 0.06150  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.54457 0.23390 0.48452 0.01033  -0.02001 0.01132  86  ASP A N   
567  C CA  . ASP A 79  ? 0.57047 0.26911 0.50616 0.03707  -0.01377 0.00626  86  ASP A CA  
568  C C   . ASP A 79  ? 0.53497 0.28734 0.49757 0.05542  -0.00942 0.01785  86  ASP A C   
569  O O   . ASP A 79  ? 0.54364 0.30852 0.50722 0.07939  -0.00303 0.01994  86  ASP A O   
570  C CB  . ASP A 79  ? 0.53146 0.24700 0.47236 0.02760  -0.02011 -0.00839 86  ASP A CB  
571  C CG  . ASP A 79  ? 0.83252 0.49266 0.74007 0.00941  -0.02759 -0.02000 86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.82980 0.42938 0.70357 0.00740  -0.02584 -0.01853 86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.67112 0.34531 0.58297 -0.00415 -0.03646 -0.02994 86  ASP A OD2 
574  N N   . ARG A 80  ? 0.42691 0.21048 0.40910 0.04385  -0.01275 0.02663  87  ARG A N   
575  C CA  . ARG A 80  ? 0.40694 0.24003 0.40922 0.05353  -0.01313 0.03622  87  ARG A CA  
576  C C   . ARG A 80  ? 0.42792 0.30061 0.44710 0.05596  -0.01578 0.02794  87  ARG A C   
577  O O   . ARG A 80  ? 0.38492 0.28480 0.41320 0.07224  -0.01471 0.03473  87  ARG A O   
578  C CB  . ARG A 80  ? 0.43145 0.25814 0.42634 0.07804  -0.00823 0.05220  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.39559 0.26016 0.40234 0.07744  -0.01299 0.06653  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.54645 0.43392 0.56001 0.10287  -0.01269 0.08312  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.63818 0.48466 0.63352 0.12304  -0.00481 0.09560  87  ARG A NE  
582  C CZ  . ARG A 80  ? 0.71249 0.56589 0.71162 0.15304  0.00091  0.11014  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.53217 0.43768 0.55687 0.16423  -0.00117 0.11542  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.79908 0.60650 0.77656 0.17286  0.00988  0.12176  87  ARG A NH2 
585  N N   . THR A 81  ? 0.33015 0.20829 0.35533 0.03881  -0.01967 0.01550  88  THR A N   
586  C CA  . THR A 81  ? 0.33019 0.23998 0.36824 0.03873  -0.02203 0.00758  88  THR A CA  
587  C C   . THR A 81  ? 0.29606 0.23092 0.34768 0.02140  -0.02583 0.00445  88  THR A C   
588  O O   . THR A 81  ? 0.30125 0.22652 0.35445 0.00773  -0.02613 0.00446  88  THR A O   
589  C CB  . THR A 81  ? 0.34541 0.23248 0.37160 0.04024  -0.02154 -0.00465 88  THR A CB  
590  O OG1 . THR A 81  ? 0.39217 0.25533 0.41179 0.02071  -0.02703 -0.01127 88  THR A OG1 
591  C CG2 . THR A 81  ? 0.42903 0.28368 0.43423 0.06215  -0.01327 -0.00214 88  THR A CG2 
592  N N   . LEU A 82  ? 0.26901 0.23506 0.32966 0.02244  -0.02764 0.00343  89  LEU A N   
593  C CA  . LEU A 82  ? 0.25879 0.24147 0.32612 0.01054  -0.02876 -0.00151 89  LEU A CA  
594  C C   . LEU A 82  ? 0.27112 0.26327 0.34305 0.01124  -0.03072 -0.01051 89  LEU A C   
595  O O   . LEU A 82  ? 0.24334 0.24821 0.31633 0.01906  -0.03140 -0.00931 89  LEU A O   
596  C CB  . LEU A 82  ? 0.28752 0.28681 0.35025 0.00836  -0.02960 0.00453  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.24833 0.25453 0.30870 -0.00032 -0.02744 -0.00094 89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.25559 0.25426 0.32241 -0.00549 -0.02076 -0.00104 89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.28993 0.30008 0.33262 -0.00400 -0.02913 0.00347  89  LEU A CD2 
600  N N   . THR A 83  ? 0.24129 0.23063 0.31780 0.00309  -0.03166 -0.01693 90  THR A N   
601  C CA  . THR A 83  ? 0.22700 0.22107 0.30463 0.00353  -0.03415 -0.02463 90  THR A CA  
602  C C   . THR A 83  ? 0.27095 0.28075 0.35494 -0.00174 -0.03334 -0.02597 90  THR A C   
603  O O   . THR A 83  ? 0.26375 0.27602 0.35473 -0.00693 -0.03088 -0.02310 90  THR A O   
604  C CB  . THR A 83  ? 0.28432 0.25818 0.35704 -0.00104 -0.03848 -0.02986 90  THR A CB  
605  O OG1 . THR A 83  ? 0.31681 0.26416 0.37384 0.00628  -0.03693 -0.02990 90  THR A OG1 
606  C CG2 . THR A 83  ? 0.26434 0.24229 0.33399 -0.00053 -0.04172 -0.03687 90  THR A CG2 
607  N N   . ILE A 84  ? 0.21551 0.23473 0.29641 0.00055  -0.03380 -0.02864 91  ILE A N   
608  C CA  . ILE A 84  ? 0.26355 0.28816 0.34331 -0.00268 -0.03216 -0.03050 91  ILE A CA  
609  C C   . ILE A 84  ? 0.25529 0.28040 0.33712 -0.00163 -0.03508 -0.03516 91  ILE A C   
610  O O   . ILE A 84  ? 0.27309 0.30028 0.34999 0.00110  -0.03622 -0.03709 91  ILE A O   
611  C CB  . ILE A 84  ? 0.20344 0.23203 0.27201 -0.00540 -0.03226 -0.02897 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.32192 0.34774 0.38228 -0.00781 -0.03150 -0.02382 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.24860 0.27070 0.30770 -0.00816 -0.02963 -0.03211 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.37278 0.40780 0.43740 -0.00466 -0.03586 -0.01740 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.23315 0.25949 0.32317 -0.00348 -0.03610 -0.03468 92  VAL A N   
616  C CA  . VAL A 85  ? 0.27233 0.29968 0.36291 -0.00350 -0.04150 -0.03720 92  VAL A CA  
617  C C   . VAL A 85  ? 0.34345 0.37571 0.43443 -0.00028 -0.03748 -0.03497 92  VAL A C   
618  O O   . VAL A 85  ? 0.27878 0.31390 0.37522 0.00217  -0.03068 -0.03022 92  VAL A O   
619  C CB  . VAL A 85  ? 0.23710 0.26495 0.33742 -0.00995 -0.04935 -0.03516 92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.20862 0.23605 0.30376 -0.01158 -0.05827 -0.03733 92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.25042 0.26179 0.34305 -0.01358 -0.05188 -0.03749 92  VAL A CG2 
622  N N   . ASP A 86  ? 0.33008 0.35961 0.41187 0.00139  -0.03960 -0.03751 93  ASP A N   
623  C CA  . ASP A 86  ? 0.25562 0.28363 0.33435 0.00561  -0.03644 -0.03456 93  ASP A CA  
624  C C   . ASP A 86  ? 0.32213 0.35242 0.39899 0.00651  -0.04414 -0.03432 93  ASP A C   
625  O O   . ASP A 86  ? 0.28349 0.31045 0.35234 0.00368  -0.04964 -0.03885 93  ASP A O   
626  C CB  . ASP A 86  ? 0.28456 0.29960 0.34526 0.00417  -0.03045 -0.03633 93  ASP A CB  
627  C CG  . ASP A 86  ? 0.38839 0.40450 0.44085 -0.00018 -0.03356 -0.03864 93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.30543 0.32115 0.35399 0.00194  -0.03593 -0.03843 93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.31279 0.33283 0.36332 -0.00524 -0.03319 -0.03859 93  ASP A OD2 
630  N N   . THR A 87  ? 0.23440 0.26791 0.31526 0.01236  -0.04350 -0.02802 94  THR A N   
631  C CA  . THR A 87  ? 0.27530 0.31096 0.35165 0.01378  -0.05183 -0.02538 94  THR A CA  
632  C C   . THR A 87  ? 0.35278 0.37316 0.41024 0.01808  -0.04575 -0.02496 94  THR A C   
633  O O   . THR A 87  ? 0.25782 0.27756 0.31279 0.02453  -0.04764 -0.01812 94  THR A O   
634  C CB  . THR A 87  ? 0.28277 0.33859 0.38101 0.01750  -0.05802 -0.01414 94  THR A CB  
635  O OG1 . THR A 87  ? 0.23865 0.29739 0.34739 0.02866  -0.04488 -0.00654 94  THR A OG1 
636  C CG2 . THR A 87  ? 0.28306 0.35275 0.39722 0.00672  -0.06848 -0.01359 94  THR A CG2 
637  N N   . GLY A 88  ? 0.25959 0.26842 0.30408 0.01327  -0.03938 -0.03023 95  GLY A N   
638  C CA  . GLY A 88  ? 0.23725 0.22981 0.26287 0.01187  -0.03443 -0.02890 95  GLY A CA  
639  C C   . GLY A 88  ? 0.24249 0.23620 0.25767 0.01048  -0.03828 -0.02838 95  GLY A C   
640  O O   . GLY A 88  ? 0.24601 0.24757 0.26286 0.01279  -0.04580 -0.02910 95  GLY A O   
641  N N   . ILE A 89  ? 0.26365 0.24701 0.26423 0.00473  -0.03316 -0.02652 96  ILE A N   
642  C CA  . ILE A 89  ? 0.31128 0.29384 0.29872 0.00450  -0.03325 -0.02351 96  ILE A CA  
643  C C   . ILE A 89  ? 0.28894 0.28578 0.27829 0.00458  -0.03302 -0.02739 96  ILE A C   
644  O O   . ILE A 89  ? 0.31632 0.31061 0.29106 0.00847  -0.03357 -0.02687 96  ILE A O   
645  C CB  . ILE A 89  ? 0.35099 0.31931 0.32393 -0.00436 -0.02690 -0.01795 96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.34489 0.31020 0.30220 -0.00329 -0.02509 -0.01214 96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.27254 0.25226 0.25317 -0.01704 -0.02406 -0.01814 96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.50126 0.44286 0.44019 -0.01022 -0.02063 -0.00434 96  ILE A CD1 
649  N N   . GLY A 90  ? 0.28279 0.29092 0.28553 0.00227  -0.03116 -0.03066 97  GLY A N   
650  C CA  . GLY A 90  ? 0.29704 0.31433 0.29943 0.00669  -0.02754 -0.03280 97  GLY A CA  
651  C C   . GLY A 90  ? 0.31596 0.34623 0.31763 0.00451  -0.01763 -0.02514 97  GLY A C   
652  O O   . GLY A 90  ? 0.29481 0.32698 0.29689 -0.00526 -0.01589 -0.01834 97  GLY A O   
653  N N   . MET A 91  ? 0.31397 0.35194 0.31329 0.01389  -0.01000 -0.02486 98  MET A N   
654  C CA  . MET A 91  ? 0.29848 0.35858 0.30433 0.01511  0.00243  -0.01376 98  MET A CA  
655  C C   . MET A 91  ? 0.29972 0.35067 0.28238 0.03033  0.01371  -0.01452 98  MET A C   
656  O O   . MET A 91  ? 0.35509 0.38533 0.32054 0.04099  0.01278  -0.02426 98  MET A O   
657  C CB  . MET A 91  ? 0.27441 0.36158 0.30669 0.01529  0.00518  -0.00739 98  MET A CB  
658  C CG  . MET A 91  ? 0.26690 0.36415 0.31546 -0.00299 -0.00444 -0.00346 98  MET A CG  
659  S SD  . MET A 91  ? 0.30907 0.43906 0.38583 -0.00310 -0.00543 0.00541  98  MET A SD  
660  C CE  . MET A 91  ? 0.17729 0.28208 0.24652 0.00920  -0.00981 -0.00895 98  MET A CE  
661  N N   . THR A 92  ? 0.31308 0.37529 0.29080 0.03020  0.02487  -0.00390 99  THR A N   
662  C CA  . THR A 92  ? 0.37135 0.42584 0.32397 0.04714  0.04068  -0.00241 99  THR A CA  
663  C C   . THR A 92  ? 0.32910 0.40736 0.29895 0.06260  0.05655  0.00528  99  THR A C   
664  O O   . THR A 92  ? 0.27577 0.38290 0.28063 0.05738  0.05327  0.01205  99  THR A O   
665  C CB  . THR A 92  ? 0.36044 0.42165 0.30297 0.04273  0.05011  0.00928  99  THR A CB  
666  O OG1 . THR A 92  ? 0.31065 0.41356 0.28879 0.03262  0.05749  0.02695  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.35441 0.39251 0.28213 0.02951  0.03478  0.00472  99  THR A CG2 
668  N N   . LYS A 93  ? 0.41488 0.37008 0.28333 0.04804  -0.05757 0.00813  100 LYS A N   
669  C CA  . LYS A 93  ? 0.39441 0.32075 0.25405 0.03118  -0.02720 0.00731  100 LYS A CA  
670  C C   . LYS A 93  ? 0.42214 0.31995 0.28875 0.03933  -0.01115 0.02264  100 LYS A C   
671  O O   . LYS A 93  ? 0.38450 0.28243 0.27550 0.03601  0.00718  0.02022  100 LYS A O   
672  C CB  . LYS A 93  ? 0.46633 0.36862 0.27426 0.01642  -0.01994 0.00402  100 LYS A CB  
673  C CG  . LYS A 93  ? 0.49643 0.37162 0.29604 0.00488  0.01015  -0.00287 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.57710 0.42418 0.32139 -0.00694 0.02005  -0.00888 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.63970 0.45662 0.37560 -0.01092 0.04914  -0.01941 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.66387 0.45172 0.34959 -0.01493 0.06644  -0.02382 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.45608 0.32819 0.29729 0.04809  -0.01875 0.03859  101 ALA A N   
678  C CA  . ALA A 94  ? 0.45673 0.30423 0.30234 0.04797  -0.00327 0.05120  101 ALA A CA  
679  C C   . ALA A 94  ? 0.50061 0.36636 0.39508 0.05673  -0.00592 0.04743  101 ALA A C   
680  O O   . ALA A 94  ? 0.42926 0.29553 0.34423 0.05049  0.01172  0.04865  101 ALA A O   
681  C CB  . ALA A 94  ? 0.51504 0.31983 0.31275 0.05057  -0.01229 0.06971  101 ALA A CB  
682  N N   . ASP A 95  ? 0.40609 0.29379 0.32053 0.07164  -0.02801 0.04054  102 ASP A N   
683  C CA  . ASP A 95  ? 0.40086 0.30920 0.35908 0.07938  -0.02891 0.03291  102 ASP A CA  
684  C C   . ASP A 95  ? 0.35163 0.28718 0.33857 0.06527  -0.01171 0.02215  102 ASP A C   
685  O O   . ASP A 95  ? 0.35436 0.29109 0.36283 0.06283  -0.00090 0.02259  102 ASP A O   
686  C CB  . ASP A 95  ? 0.40978 0.34814 0.38614 0.10047  -0.05406 0.02275  102 ASP A CB  
687  C CG  . ASP A 95  ? 0.57382 0.47223 0.52446 0.12475  -0.07309 0.03495  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.63774 0.47967 0.55328 0.11777  -0.06411 0.05201  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.64716 0.57011 0.61029 0.15096  -0.09700 0.02687  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.33922 0.29154 0.32024 0.05461  -0.01014 0.01264  103 LEU A N   
691  C CA  . LEU A 96  ? 0.33087 0.29121 0.32418 0.04125  0.00536  0.00493  103 LEU A CA  
692  C C   . LEU A 96  ? 0.42462 0.35997 0.41215 0.04083  0.02456  0.01431  103 LEU A C   
693  O O   . LEU A 96  ? 0.34148 0.28338 0.34938 0.04113  0.03225  0.01440  103 LEU A O   
694  C CB  . LEU A 96  ? 0.30921 0.27321 0.28161 0.02537  0.00548  -0.00631 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.38188 0.39057 0.37175 0.01492  -0.00697 -0.02301 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.36670 0.36746 0.32641 -0.01008 -0.00211 -0.03454 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.25932 0.29064 0.28126 0.01080  -0.00074 -0.02892 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.37591 0.28880 0.33550 0.04053  0.03219  0.02102  104 ILE A N   
699  C CA  . ILE A 97  ? 0.40838 0.31274 0.36826 0.04198  0.05176  0.02594  104 ILE A CA  
700  C C   . ILE A 97  ? 0.33663 0.25277 0.32271 0.04406  0.05300  0.03318  104 ILE A C   
701  O O   . ILE A 97  ? 0.38585 0.31719 0.39331 0.04651  0.06302  0.03297  104 ILE A O   
702  C CB  . ILE A 97  ? 0.40123 0.28643 0.32446 0.03837  0.06221  0.02832  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.39288 0.26271 0.28710 0.03381  0.06413  0.01708  104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.37366 0.26661 0.30563 0.04077  0.08372  0.03081  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.41267 0.26375 0.26256 0.02780  0.07032  0.01682  104 ILE A CD1 
706  N N   . ASN A 98  ? 0.32792 0.23472 0.30939 0.04382  0.04120  0.03888  105 ASN A N   
707  C CA  . ASN A 98  ? 0.34560 0.25145 0.34237 0.04055  0.04254  0.04378  105 ASN A CA  
708  C C   . ASN A 98  ? 0.34181 0.26717 0.37079 0.04601  0.03365  0.03568  105 ASN A C   
709  O O   . ASN A 98  ? 0.40753 0.32318 0.44009 0.05089  0.02244  0.03418  105 ASN A O   
710  C CB  . ASN A 98  ? 0.47959 0.34796 0.44405 0.03846  0.03451  0.05400  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.69871 0.55183 0.66516 0.02608  0.04116  0.05895  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.68987 0.57197 0.68329 0.01589  0.05429  0.05465  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.66878 0.47356 0.60250 0.02663  0.03087  0.06770  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.30897 0.25706 0.35563 0.04635  0.03945  0.02996  106 ASN A N   
715  C CA  . ASN A 99  ? 0.32896 0.29727 0.39985 0.04690  0.03520  0.02290  106 ASN A CA  
716  C C   . ASN A 99  ? 0.34868 0.32409 0.42531 0.05136  0.02211  0.01344  106 ASN A C   
717  O O   . ASN A 99  ? 0.30034 0.28546 0.39331 0.05373  0.01752  0.00662  106 ASN A O   
718  C CB  . ASN A 99  ? 0.28730 0.26385 0.37420 0.04176  0.03820  0.02430  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.30494 0.29682 0.39738 0.03856  0.05042  0.02956  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.25880 0.26240 0.35412 0.04641  0.05437  0.02973  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.29080 0.28230 0.38282 0.02721  0.05679  0.03290  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.29497 0.27145 0.35921 0.05251  0.01643  0.01010  107 LEU A N   
723  C CA  . LEU A 100 ? 0.25635 0.25937 0.33303 0.05647  0.00421  -0.00292 107 LEU A CA  
724  C C   . LEU A 100 ? 0.27490 0.27708 0.36303 0.07376  -0.00812 -0.00614 107 LEU A C   
725  O O   . LEU A 100 ? 0.25918 0.28870 0.37106 0.07925  -0.01136 -0.01990 107 LEU A O   
726  C CB  . LEU A 100 ? 0.20084 0.23083 0.29165 0.04354  0.01110  -0.01377 107 LEU A CB  
727  C CG  . LEU A 100 ? 0.26202 0.27456 0.33085 0.02859  0.02280  -0.00974 107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.34112 0.33917 0.40899 0.02914  0.03247  -0.00076 107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.28511 0.31842 0.35060 0.00942  0.02420  -0.02312 107 LEU A CD2 
730  N N   . GLY A 101 ? 0.26545 0.23004 0.33060 0.08230  -0.01372 0.00609  108 GLY A N   
731  C CA  . GLY A 101 ? 0.28131 0.22488 0.34308 0.10252  -0.02769 0.00518  108 GLY A CA  
732  C C   . GLY A 101 ? 0.37323 0.30131 0.44573 0.10140  -0.02139 0.00091  108 GLY A C   
733  O O   . GLY A 101 ? 0.33408 0.24529 0.40672 0.12130  -0.03219 -0.00621 108 GLY A O   
734  N N   . THR A 102 ? 0.33500 0.26813 0.41466 0.08070  -0.00552 0.00352  109 THR A N   
735  C CA  . THR A 102 ? 0.35445 0.27835 0.44215 0.07395  -0.00008 -0.00236 109 THR A CA  
736  C C   . THR A 102 ? 0.39208 0.28746 0.46202 0.05417  0.01031  0.01039  109 THR A C   
737  O O   . THR A 102 ? 0.36632 0.26408 0.42663 0.04523  0.01770  0.02177  109 THR A O   
738  C CB  . THR A 102 ? 0.34747 0.31641 0.46154 0.06481  0.00714  -0.01374 109 THR A CB  
739  O OG1 . THR A 102 ? 0.32968 0.31113 0.44352 0.04983  0.01717  -0.00350 109 THR A OG1 
740  C CG2 . THR A 102 ? 0.27831 0.28528 0.40805 0.07349  0.00256  -0.02606 109 THR A CG2 
741  N N   . ILE A 103 ? 0.35349 0.22459 0.41861 0.04517  0.01239  0.00540  110 ILE A N   
742  C CA  . ILE A 103 ? 0.33702 0.19599 0.39182 0.01780  0.02421  0.01220  110 ILE A CA  
743  C C   . ILE A 103 ? 0.37267 0.28837 0.45924 0.00503  0.03106  0.00516  110 ILE A C   
744  O O   . ILE A 103 ? 0.31161 0.23080 0.40281 -0.01103 0.03318  -0.00388 110 ILE A O   
745  C CB  . ILE A 103 ? 0.39727 0.19277 0.42182 0.00843  0.02291  0.00954  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.40818 0.19828 0.44309 0.02418  0.01499  -0.00965 110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.50522 0.23397 0.48473 0.01853  0.01627  0.02398  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.57601 0.30495 0.58183 0.00828  0.01750  -0.01751 110 ILE A CD1 
749  N N   . ALA A 104 ? 0.25023 0.20565 0.35300 0.01238  0.03324  0.00936  111 ALA A N   
750  C CA  . ALA A 104 ? 0.29836 0.29945 0.42365 0.01000  0.03434  0.00460  111 ALA A CA  
751  C C   . ALA A 104 ? 0.25444 0.28446 0.39148 -0.00829 0.04039  0.00535  111 ALA A C   
752  O O   . ALA A 104 ? 0.24868 0.31147 0.39968 -0.01291 0.03669  -0.00101 111 ALA A O   
753  C CB  . ALA A 104 ? 0.27007 0.28826 0.39790 0.02313  0.03521  0.01046  111 ALA A CB  
754  N N   . LYS A 105 ? 0.29016 0.31523 0.42112 -0.02080 0.04962  0.01188  112 LYS A N   
755  C CA  . LYS A 105 ? 0.29889 0.36986 0.44868 -0.04071 0.05669  0.00916  112 LYS A CA  
756  C C   . LYS A 105 ? 0.39760 0.46446 0.54606 -0.06559 0.05363  -0.00257 112 LYS A C   
757  O O   . LYS A 105 ? 0.36877 0.48592 0.53886 -0.07272 0.04890  -0.01036 112 LYS A O   
758  C CB  . LYS A 105 ? 0.25805 0.32823 0.39932 -0.05485 0.07159  0.01578  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.46190 0.60652 0.63526 -0.06830 0.08085  0.01066  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.36786 0.51833 0.53214 -0.08639 0.10038  0.01415  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.73614 0.88774 0.89210 -0.13352 0.11093  0.00794  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.63908 0.88175 0.84077 -0.14819 0.11058  -0.00599 112 LYS A NZ  
763  N N   . SER A 106 ? 0.30033 0.30255 0.41810 -0.07798 0.05488  -0.00440 113 SER A N   
764  C CA  . SER A 106 ? 0.33206 0.31439 0.43932 -0.10288 0.05342  -0.01827 113 SER A CA  
765  C C   . SER A 106 ? 0.42565 0.41217 0.53968 -0.08631 0.04226  -0.03070 113 SER A C   
766  O O   . SER A 106 ? 0.36703 0.36839 0.48316 -0.10584 0.04008  -0.04514 113 SER A O   
767  C CB  . SER A 106 ? 0.39829 0.29214 0.45974 -0.11676 0.05777  -0.01582 113 SER A CB  
768  O OG  . SER A 106 ? 0.54370 0.38673 0.58664 -0.08224 0.04901  -0.00979 113 SER A OG  
769  N N   . GLY A 107 ? 0.34804 0.32586 0.46372 -0.05455 0.03636  -0.02738 114 GLY A N   
770  C CA  . GLY A 107 ? 0.34143 0.33173 0.46318 -0.04246 0.02977  -0.04052 114 GLY A CA  
771  C C   . GLY A 107 ? 0.33063 0.38408 0.47173 -0.04723 0.02645  -0.04102 114 GLY A C   
772  O O   . GLY A 107 ? 0.32780 0.39518 0.46654 -0.05537 0.02272  -0.05461 114 GLY A O   
773  N N   . THR A 108 ? 0.23378 0.32240 0.38927 -0.03974 0.02698  -0.02654 115 THR A N   
774  C CA  . THR A 108 ? 0.30246 0.44508 0.47103 -0.03759 0.02032  -0.02392 115 THR A CA  
775  C C   . THR A 108 ? 0.30098 0.48178 0.47975 -0.06314 0.01700  -0.03352 115 THR A C   
776  O O   . THR A 108 ? 0.31354 0.52803 0.49256 -0.06707 0.00717  -0.03939 115 THR A O   
777  C CB  . THR A 108 ? 0.25232 0.41543 0.43120 -0.01838 0.02189  -0.00816 115 THR A CB  
778  O OG1 . THR A 108 ? 0.35577 0.48596 0.52069 -0.00011 0.02362  -0.00187 115 THR A OG1 
779  C CG2 . THR A 108 ? 0.25135 0.46652 0.44103 -0.00968 0.01186  -0.00391 115 THR A CG2 
780  N N   . LYS A 109 ? 0.27158 0.44824 0.45452 -0.08482 0.02521  -0.03577 116 LYS A N   
781  C CA  . LYS A 109 ? 0.30679 0.52589 0.50048 -0.11770 0.02380  -0.04787 116 LYS A CA  
782  C C   . LYS A 109 ? 0.45422 0.64821 0.62700 -0.13689 0.01885  -0.06634 116 LYS A C   
783  O O   . LYS A 109 ? 0.44575 0.69052 0.62604 -0.15230 0.00923  -0.07670 116 LYS A O   
784  C CB  . LYS A 109 ? 0.31456 0.52228 0.50741 -0.14508 0.03823  -0.04742 116 LYS A CB  
785  C CG  . LYS A 109 ? 0.53630 0.79683 0.74279 -0.18818 0.04020  -0.06182 116 LYS A CG  
786  C CD  . LYS A 109 ? 0.61483 0.81179 0.78923 -0.22486 0.05575  -0.06479 116 LYS A CD  
787  C CE  . LYS A 109 ? 0.66780 0.88216 0.83147 -0.25950 0.05420  -0.07894 116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.78201 0.91457 0.90298 -0.27961 0.05381  -0.09255 116 LYS A NZ  
789  N N   . ALA A 110 ? 0.40267 0.52068 0.54790 -0.13302 0.02414  -0.07221 117 ALA A N   
790  C CA  . ALA A 110 ? 0.46192 0.55065 0.58485 -0.14548 0.02179  -0.09349 117 ALA A CA  
791  C C   . ALA A 110 ? 0.36905 0.49319 0.49469 -0.12776 0.01292  -0.09696 117 ALA A C   
792  O O   . ALA A 110 ? 0.38319 0.52544 0.49800 -0.14566 0.00778  -0.11368 117 ALA A O   
793  C CB  . ALA A 110 ? 0.44419 0.44339 0.53831 -0.13552 0.02873  -0.09963 117 ALA A CB  
794  N N   . PHE A 111 ? 0.30314 0.43419 0.43672 -0.09702 0.01192  -0.08183 118 PHE A N   
795  C CA  . PHE A 111 ? 0.30699 0.46228 0.43331 -0.08526 0.00636  -0.08278 118 PHE A CA  
796  C C   . PHE A 111 ? 0.41675 0.63232 0.54650 -0.09459 -0.00671 -0.07814 118 PHE A C   
797  O O   . PHE A 111 ? 0.34801 0.57931 0.45874 -0.10245 -0.01282 -0.08770 118 PHE A O   
798  C CB  . PHE A 111 ? 0.20008 0.34654 0.32984 -0.05801 0.00930  -0.06669 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.33058 0.49181 0.44414 -0.05202 0.00733  -0.06622 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.33517 0.49671 0.43097 -0.06345 0.00989  -0.08640 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.26213 0.43035 0.37140 -0.03732 0.00500  -0.04650 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.34139 0.51598 0.41555 -0.06375 0.01117  -0.08561 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.26343 0.43431 0.34682 -0.03811 0.00511  -0.04418 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.31799 0.49495 0.38384 -0.05306 0.00875  -0.06312 118 PHE A CZ  
805  N N   . MET A 112 ? 0.35972 0.61368 0.51257 -0.09208 -0.01179 -0.06461 119 MET A N   
806  C CA  . MET A 112 ? 0.47419 0.79398 0.63459 -0.09131 -0.02843 -0.05915 119 MET A CA  
807  C C   . MET A 112 ? 0.37220 0.72811 0.53303 -0.12627 -0.03560 -0.07947 119 MET A C   
808  O O   . MET A 112 ? 0.42807 0.83191 0.58142 -0.12880 -0.05267 -0.08096 119 MET A O   
809  C CB  . MET A 112 ? 0.40108 0.75907 0.59135 -0.07159 -0.03087 -0.04232 119 MET A CB  
810  C CG  . MET A 112 ? 0.23201 0.58060 0.41107 -0.03456 -0.03668 -0.02144 119 MET A CG  
811  S SD  . MET A 112 ? 0.79259 1.17126 1.00335 -0.00545 -0.03462 -0.00653 119 MET A SD  
812  C CE  . MET A 112 ? 0.39353 0.70117 0.57210 0.02418  -0.02839 0.01103  119 MET A CE  
813  N N   . GLU A 113 ? 0.36787 0.69716 0.53089 -0.15532 -0.02386 -0.09499 120 GLU A N   
814  C CA  . GLU A 113 ? 0.44872 0.79188 0.59959 -0.19280 -0.02751 -0.11691 120 GLU A CA  
815  C C   . GLU A 113 ? 0.50453 0.81771 0.62060 -0.20106 -0.02917 -0.13581 120 GLU A C   
816  O O   . GLU A 113 ? 0.45207 0.78671 0.54960 -0.21771 -0.03717 -0.14682 120 GLU A O   
817  C CB  . GLU A 113 ? 0.46356 0.76072 0.60949 -0.22070 -0.01178 -0.12558 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.70556 1.03065 0.87965 -0.21764 -0.00573 -0.10990 120 GLU A CG  
819  C CD  . GLU A 113 ? 0.96998 1.24014 1.12633 -0.24975 0.01081  -0.11652 120 GLU A CD  
820  O OE1 . GLU A 113 ? 1.03880 1.33106 1.21146 -0.25430 0.01869  -0.10670 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 0.99928 1.19836 1.11999 -0.26866 0.01659  -0.13162 120 GLU A OE2 
822  N N   . ALA A 114 ? 0.41468 0.66712 0.51433 -0.17835 -0.01808 -0.13453 121 ALA A N   
823  C CA  . ALA A 114 ? 0.34755 0.57594 0.41476 -0.18088 -0.01543 -0.15367 121 ALA A CA  
824  C C   . ALA A 114 ? 0.48117 0.75892 0.53537 -0.17159 -0.02907 -0.14358 121 ALA A C   
825  O O   . ALA A 114 ? 0.60219 0.89117 0.62696 -0.18909 -0.03340 -0.16110 121 ALA A O   
826  C CB  . ALA A 114 ? 0.43014 0.59532 0.49099 -0.15691 0.00036  -0.15737 121 ALA A CB  
827  N N   . LEU A 115 ? 0.34985 0.64988 0.41780 -0.14470 -0.03589 -0.11536 122 LEU A N   
828  C CA  . LEU A 115 ? 0.39593 0.72550 0.43947 -0.13359 -0.04983 -0.10097 122 LEU A CA  
829  C C   . LEU A 115 ? 0.58253 0.97448 0.62059 -0.15047 -0.07247 -0.10480 122 LEU A C   
830  O O   . LEU A 115 ? 0.54495 0.94981 0.54440 -0.15908 -0.08236 -0.10907 122 LEU A O   
831  C CB  . LEU A 115 ? 0.40405 0.73112 0.45812 -0.10065 -0.05279 -0.07045 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.35908 0.63340 0.41069 -0.08589 -0.03390 -0.06572 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.39834 0.66621 0.45516 -0.05815 -0.03737 -0.03792 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.41556 0.67046 0.42967 -0.09510 -0.02478 -0.07717 122 LEU A CD2 
835  N N   . GLN A 116 ? 0.50501 0.94244 0.58036 -0.15753 -0.08095 -0.10459 123 GLN A N   
836  C CA  . GLN A 116 ? 0.57437 1.06183 0.64719 -0.16791 -0.09707 -0.10717 123 GLN A CA  
837  C C   . GLN A 116 ? 0.67179 1.13768 0.71817 -0.20377 -0.08920 -0.13482 123 GLN A C   
838  O O   . GLN A 116 ? 0.61171 1.11574 0.64567 -0.21526 -0.10279 -0.13930 123 GLN A O   
839  C CB  . GLN A 116 ? 0.55040 1.07985 0.66843 -0.16206 -0.09893 -0.09972 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.69114 1.19027 0.82623 -0.18964 -0.07786 -0.11509 123 GLN A CG  
841  C CD  . GLN A 116 ? 0.95603 1.46051 1.07655 -0.22792 -0.07615 -0.13735 123 GLN A CD  
842  O OE1 . GLN A 116 ? 0.96027 1.51534 1.07432 -0.23248 -0.09242 -0.14004 123 GLN A OE1 
843  N NE2 . GLN A 116 ? 0.90766 1.35571 1.01915 -0.25520 -0.05709 -0.15287 123 GLN A NE2 
844  N N   . ALA A 117 ? 0.70708 1.11033 0.74318 -0.21858 -0.06818 -0.15386 124 ALA A N   
845  C CA  . ALA A 117 ? 0.64351 1.01251 0.65147 -0.24792 -0.05808 -0.18125 124 ALA A CA  
846  C C   . ALA A 117 ? 0.90485 1.23872 0.87288 -0.24621 -0.04967 -0.19597 124 ALA A C   
847  O O   . ALA A 117 ? 0.83370 1.12113 0.77979 -0.26195 -0.03526 -0.22111 124 ALA A O   
848  C CB  . ALA A 117 ? 0.51342 0.82694 0.53149 -0.26328 -0.04012 -0.19382 124 ALA A CB  
849  N N   . GLY A 118 ? 0.72965 1.08175 0.68429 -0.22700 -0.05669 -0.18105 125 GLY A N   
850  C CA  . GLY A 118 ? 0.74627 1.07666 0.65899 -0.22833 -0.04684 -0.19338 125 GLY A CA  
851  C C   . GLY A 118 ? 0.75069 1.05113 0.66301 -0.21031 -0.03102 -0.19348 125 GLY A C   
852  O O   . GLY A 118 ? 0.55734 0.85486 0.43516 -0.20911 -0.02341 -0.19546 125 GLY A O   
853  N N   . ALA A 119 ? 0.53471 0.80809 0.48512 -0.19272 -0.02202 -0.18617 126 ALA A N   
854  C CA  . ALA A 119 ? 0.55428 0.79621 0.51195 -0.16826 -0.00421 -0.18103 126 ALA A CA  
855  C C   . ALA A 119 ? 0.52177 0.78253 0.46668 -0.15388 -0.01054 -0.15032 126 ALA A C   
856  O O   . ALA A 119 ? 0.53042 0.82099 0.46592 -0.15294 -0.03081 -0.12832 126 ALA A O   
857  C CB  . ALA A 119 ? 0.40642 0.61447 0.40322 -0.15124 0.00313  -0.17588 126 ALA A CB  
858  N N   . ASP A 120 ? 0.48829 0.73009 0.43059 -0.14227 0.00666  -0.15007 127 ASP A N   
859  C CA  . ASP A 120 ? 0.40786 0.65047 0.33050 -0.13390 0.00555  -0.12280 127 ASP A CA  
860  C C   . ASP A 120 ? 0.42624 0.64776 0.38245 -0.11369 0.01648  -0.11324 127 ASP A C   
861  O O   . ASP A 120 ? 0.38656 0.59520 0.37830 -0.10395 0.02345  -0.12680 127 ASP A O   
862  C CB  . ASP A 120 ? 0.50172 0.74919 0.37512 -0.15240 0.01776  -0.13343 127 ASP A CB  
863  C CG  . ASP A 120 ? 0.62396 0.86884 0.51186 -0.15384 0.04461  -0.16501 127 ASP A CG  
864  O OD1 . ASP A 120 ? 0.79663 1.03984 0.69823 -0.15528 0.05087  -0.19604 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 0.68235 0.92746 0.56688 -0.15337 0.05940  -0.16043 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.36292 0.57496 0.30031 -0.10859 0.01700  -0.08937 128 ILE A N   
867  C CA  . ILE A 121 ? 0.34498 0.53847 0.30937 -0.09195 0.02349  -0.07750 128 ILE A CA  
868  C C   . ILE A 121 ? 0.37478 0.57161 0.35990 -0.09280 0.04390  -0.10232 128 ILE A C   
869  O O   . ILE A 121 ? 0.33699 0.52506 0.35619 -0.07685 0.04666  -0.10184 128 ILE A O   
870  C CB  . ILE A 121 ? 0.43939 0.61181 0.36778 -0.08980 0.01885  -0.04747 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.42065 0.59362 0.34555 -0.07305 -0.00454 -0.02324 128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.33946 0.49126 0.28410 -0.08215 0.03021  -0.04144 128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.50373 0.64406 0.37989 -0.06519 -0.01306 0.00662  128 ILE A CD1 
874  N N   . SER A 122 ? 0.35552 0.57048 0.32144 -0.10930 0.05778  -0.12619 129 SER A N   
875  C CA  . SER A 122 ? 0.51427 0.74717 0.50626 -0.10513 0.07693  -0.15426 129 SER A CA  
876  C C   . SER A 122 ? 0.40336 0.62592 0.43774 -0.08108 0.07405  -0.17177 129 SER A C   
877  O O   . SER A 122 ? 0.40129 0.63570 0.46531 -0.06522 0.08340  -0.18908 129 SER A O   
878  C CB  . SER A 122 ? 0.34400 0.60487 0.30823 -0.12630 0.09436  -0.18153 129 SER A CB  
879  O OG  . SER A 122 ? 0.41250 0.67116 0.37348 -0.12580 0.09159  -0.20415 129 SER A OG  
880  N N   . MET A 123 ? 0.30899 0.50960 0.34368 -0.07899 0.06071  -0.16782 130 MET A N   
881  C CA  . MET A 123 ? 0.34497 0.51794 0.40458 -0.06200 0.05816  -0.18146 130 MET A CA  
882  C C   . MET A 123 ? 0.36606 0.51728 0.45010 -0.04523 0.04916  -0.15784 130 MET A C   
883  O O   . MET A 123 ? 0.30982 0.42760 0.40453 -0.03480 0.04533  -0.16224 130 MET A O   
884  C CB  . MET A 123 ? 0.38429 0.54226 0.42573 -0.07815 0.05094  -0.19123 130 MET A CB  
885  C CG  . MET A 123 ? 0.54022 0.72290 0.54663 -0.10080 0.05588  -0.20803 130 MET A CG  
886  S SD  . MET A 123 ? 0.57479 0.73898 0.55830 -0.12205 0.05076  -0.23349 130 MET A SD  
887  C CE  . MET A 123 ? 0.63345 0.73871 0.63902 -0.09895 0.05781  -0.25414 130 MET A CE  
888  N N   . ILE A 124 ? 0.25276 0.41517 0.33848 -0.04426 0.04698  -0.13368 131 ILE A N   
889  C CA  . ILE A 124 ? 0.26295 0.40644 0.36556 -0.03123 0.03931  -0.11126 131 ILE A CA  
890  C C   . ILE A 124 ? 0.30742 0.43273 0.43250 -0.00990 0.04104  -0.12117 131 ILE A C   
891  O O   . ILE A 124 ? 0.24711 0.34398 0.37926 -0.00122 0.03456  -0.10916 131 ILE A O   
892  C CB  . ILE A 124 ? 0.31763 0.46919 0.41005 -0.03378 0.03903  -0.08856 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.28276 0.41516 0.38865 -0.02065 0.03256  -0.06769 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.24613 0.41623 0.33768 -0.03746 0.05130  -0.10019 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.27478 0.40200 0.36311 -0.02131 0.03118  -0.04560 131 ILE A CD1 
896  N N   . GLY A 125 ? 0.24349 0.38786 0.37846 -0.00027 0.04932  -0.14353 132 GLY A N   
897  C CA  . GLY A 125 ? 0.33364 0.46725 0.49013 0.02722  0.04658  -0.15275 132 GLY A CA  
898  C C   . GLY A 125 ? 0.39775 0.48015 0.54852 0.04153  0.04090  -0.16119 132 GLY A C   
899  O O   . GLY A 125 ? 0.42432 0.47718 0.58117 0.06510  0.03317  -0.15709 132 GLY A O   
900  N N   . GLN A 126 ? 0.34996 0.41546 0.48216 0.02561  0.04388  -0.17269 133 GLN A N   
901  C CA  . GLN A 126 ? 0.47943 0.48317 0.59568 0.03111  0.04040  -0.18168 133 GLN A CA  
902  C C   . GLN A 126 ? 0.36950 0.33513 0.47641 0.01933  0.03266  -0.15514 133 GLN A C   
903  O O   . GLN A 126 ? 0.41357 0.31708 0.50018 0.01955  0.03060  -0.15845 133 GLN A O   
904  C CB  . GLN A 126 ? 0.36009 0.35890 0.45514 0.01012  0.04680  -0.20473 133 GLN A CB  
905  C CG  . GLN A 126 ? 0.45054 0.48973 0.54990 0.01769  0.05856  -0.23442 133 GLN A CG  
906  C CD  . GLN A 126 ? 0.53224 0.56527 0.60352 -0.00613 0.06505  -0.25792 133 GLN A CD  
907  O OE1 . GLN A 126 ? 0.55623 0.53525 0.60525 -0.01689 0.06169  -0.26468 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 0.59246 0.67849 0.65877 -0.01895 0.07523  -0.27129 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.34050 0.33810 0.45757 0.00826  0.03007  -0.13040 134 PHE A N   
910  C CA  . PHE A 127 ? 0.37988 0.35616 0.49266 -0.00316 0.02615  -0.10780 134 PHE A CA  
911  C C   . PHE A 127 ? 0.35154 0.32507 0.47330 0.01505  0.02292  -0.08861 134 PHE A C   
912  O O   . PHE A 127 ? 0.33800 0.30314 0.45697 0.00607  0.02241  -0.06973 134 PHE A O   
913  C CB  . PHE A 127 ? 0.25258 0.27047 0.36883 -0.02846 0.02526  -0.09782 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.32605 0.35656 0.43068 -0.04871 0.02574  -0.11705 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.51437 0.51935 0.60521 -0.07264 0.02562  -0.12628 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.36569 0.43141 0.46720 -0.04859 0.02738  -0.12711 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.52266 0.53985 0.59910 -0.09444 0.02519  -0.14668 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.35078 0.42788 0.43527 -0.06858 0.02747  -0.14577 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.44194 0.49601 0.51499 -0.09063 0.02541  -0.15635 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.28255 0.26945 0.41542 0.03849  0.02144  -0.09560 135 GLY A N   
921  C CA  . GLY A 128 ? 0.23877 0.22104 0.37610 0.05531  0.01595  -0.08136 135 GLY A CA  
922  C C   . GLY A 128 ? 0.26579 0.28124 0.41018 0.04576  0.01811  -0.06423 135 GLY A C   
923  O O   . GLY A 128 ? 0.33368 0.33976 0.47551 0.05397  0.01440  -0.05135 135 GLY A O   
924  N N   . VAL A 129 ? 0.29203 0.33948 0.43866 0.02983  0.02326  -0.06373 136 VAL A N   
925  C CA  . VAL A 129 ? 0.26540 0.32968 0.40991 0.02408  0.02505  -0.04739 136 VAL A CA  
926  C C   . VAL A 129 ? 0.23988 0.33347 0.38200 0.01713  0.02991  -0.05518 136 VAL A C   
927  O O   . VAL A 129 ? 0.21681 0.31531 0.34503 0.00758  0.03192  -0.04350 136 VAL A O   
928  C CB  . VAL A 129 ? 0.23609 0.30269 0.37645 0.01327  0.02486  -0.03385 136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.26797 0.31137 0.40886 0.01316  0.02468  -0.02553 136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.24536 0.32798 0.38317 0.00018  0.02384  -0.04434 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.31203 0.28144 0.37110 -0.01925 -0.03383 -0.05489 137 GLY A N   
932  C CA  . GLY A 130 ? 0.31278 0.29066 0.35783 -0.00496 -0.03109 -0.05269 137 GLY A CA  
933  C C   . GLY A 130 ? 0.34453 0.32920 0.39001 -0.00394 -0.02194 -0.03938 137 GLY A C   
934  O O   . GLY A 130 ? 0.26806 0.26325 0.30686 0.00585  -0.01896 -0.03451 137 GLY A O   
935  N N   . PHE A 131 ? 0.28221 0.26061 0.33527 -0.01330 -0.01774 -0.03323 138 PHE A N   
936  C CA  . PHE A 131 ? 0.29979 0.28130 0.35366 -0.01279 -0.01155 -0.02392 138 PHE A CA  
937  C C   . PHE A 131 ? 0.27083 0.26420 0.32556 -0.00806 -0.01087 -0.02216 138 PHE A C   
938  O O   . PHE A 131 ? 0.23572 0.23055 0.28866 -0.00313 -0.00693 -0.01469 138 PHE A O   
939  C CB  . PHE A 131 ? 0.27791 0.25293 0.33697 -0.02137 -0.00896 -0.02083 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.32860 0.30585 0.38870 -0.02077 -0.00543 -0.01605 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.24915 0.22215 0.30811 -0.01934 -0.00373 -0.01128 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.27860 0.26243 0.34222 -0.02124 -0.00451 -0.01695 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.24209 0.21237 0.30303 -0.01947 -0.00255 -0.00913 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.22979 0.21156 0.29241 -0.01846 -0.00224 -0.01469 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.23963 0.21212 0.30072 -0.01810 -0.00195 -0.01161 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.24907 0.25140 0.30844 -0.00958 -0.01487 -0.02798 139 TYR A N   
947  C CA  . TYR A 132 ? 0.23167 0.24691 0.29234 -0.00365 -0.01429 -0.02582 139 TYR A CA  
948  C C   . TYR A 132 ? 0.26534 0.28971 0.31677 0.00890  -0.01545 -0.02428 139 TYR A C   
949  O O   . TYR A 132 ? 0.27259 0.30576 0.32305 0.01651  -0.01378 -0.01927 139 TYR A O   
950  C CB  . TYR A 132 ? 0.24153 0.26943 0.31281 -0.00884 -0.01850 -0.03184 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.25853 0.28193 0.33844 -0.01901 -0.01473 -0.02944 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.26284 0.28757 0.34278 -0.01658 -0.00895 -0.02410 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.24410 0.26076 0.33063 -0.02939 -0.01675 -0.03202 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.27706 0.30106 0.36142 -0.02275 -0.00487 -0.02162 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.37272 0.38775 0.46579 -0.03697 -0.01177 -0.02671 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.27075 0.29164 0.36165 -0.03287 -0.00561 -0.02160 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.27736 0.30000 0.37147 -0.03741 -0.00012 -0.01615 139 TYR A OH  
958  N N   . SER A 133 ? 0.26917 0.29223 0.31236 0.01344  -0.01768 -0.02760 140 SER A N   
959  C CA  . SER A 133 ? 0.31422 0.34827 0.34585 0.02798  -0.01638 -0.02313 140 SER A CA  
960  C C   . SER A 133 ? 0.28970 0.32037 0.32194 0.03098  -0.00694 -0.00691 140 SER A C   
961  O O   . SER A 133 ? 0.26513 0.30636 0.29008 0.04307  -0.00340 0.00200  140 SER A O   
962  C CB  . SER A 133 ? 0.24261 0.27647 0.26355 0.03441  -0.02002 -0.03078 140 SER A CB  
963  O OG  . SER A 133 ? 0.27262 0.29522 0.29447 0.03111  -0.01440 -0.02487 140 SER A OG  
964  N N   . ALA A 134 ? 0.27557 0.29223 0.31690 0.02036  -0.00329 -0.00260 141 ALA A N   
965  C CA  . ALA A 134 ? 0.25782 0.26853 0.30430 0.02013  0.00332  0.01096  141 ALA A CA  
966  C C   . ALA A 134 ? 0.21665 0.23032 0.26284 0.02754  0.00526  0.01795  141 ALA A C   
967  O O   . ALA A 134 ? 0.28190 0.29377 0.33012 0.03201  0.01095  0.03194  141 ALA A O   
968  C CB  . ALA A 134 ? 0.21124 0.20682 0.26664 0.00788  0.00344  0.00956  141 ALA A CB  
969  N N   . TYR A 135 ? 0.25566 0.27485 0.30101 0.02930  0.00094  0.00992  142 TYR A N   
970  C CA  . TYR A 135 ? 0.27961 0.30276 0.32406 0.03875  0.00232  0.01601  142 TYR A CA  
971  C C   . TYR A 135 ? 0.25635 0.29773 0.29039 0.05390  0.00217  0.02138  142 TYR A C   
972  O O   . TYR A 135 ? 0.28859 0.33691 0.32010 0.06456  0.00255  0.02665  142 TYR A O   
973  C CB  . TYR A 135 ? 0.27771 0.30562 0.32676 0.03640  -0.00176 0.00621  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.26576 0.27689 0.32134 0.02652  0.00006  0.00376  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.26672 0.26307 0.32376 0.03002  0.00318  0.00909  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.19869 0.20734 0.25745 0.01518  -0.00178 -0.00399 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.26158 0.24331 0.32143 0.02333  0.00332  0.00422  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.23563 0.23204 0.29710 0.00881  -0.00028 -0.00604 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.29630 0.28030 0.35744 0.01332  0.00174  -0.00316 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.23855 0.21117 0.29938 0.00928  0.00171  -0.00786 142 TYR A OH  
981  N N   . LEU A 136 ? 0.34568 0.39603 0.37181 0.05749  0.00157  0.02006  143 LEU A N   
982  C CA  . LEU A 136 ? 0.31417 0.38244 0.32716 0.07485  0.00334  0.02814  143 LEU A CA  
983  C C   . LEU A 136 ? 0.26689 0.32925 0.28218 0.07972  0.01438  0.05097  143 LEU A C   
984  O O   . LEU A 136 ? 0.30163 0.37686 0.30779 0.09542  0.01814  0.06349  143 LEU A O   
985  C CB  . LEU A 136 ? 0.27073 0.35025 0.27229 0.07990  -0.00045 0.01874  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.26145 0.34712 0.26012 0.07727  -0.01310 -0.00379 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.25848 0.34467 0.24684 0.08087  -0.01616 -0.01333 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.25026 0.35754 0.24121 0.09023  -0.02047 -0.00901 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.23959 0.28340 0.26821 0.06638  0.01923  0.05742  144 VAL A N   
990  C CA  . VAL A 137 ? 0.28799 0.32619 0.32446 0.06713  0.02909  0.07959  144 VAL A CA  
991  C C   . VAL A 137 ? 0.29638 0.30762 0.34941 0.05420  0.02982  0.08334  144 VAL A C   
992  O O   . VAL A 137 ? 0.37659 0.37748 0.43997 0.05319  0.03645  0.10170  144 VAL A O   
993  C CB  . VAL A 137 ? 0.32200 0.36971 0.36072 0.06478  0.03391  0.08530  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.32484 0.39845 0.34365 0.08227  0.03369  0.08222  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.27970 0.31591 0.32690 0.04895  0.02867  0.07067  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.36358 0.36298 0.41949 0.04468  0.02290  0.06631  145 ALA A N   
997  C CA  . ALA A 138 ? 0.29871 0.27278 0.36685 0.03395  0.02171  0.06513  145 ALA A CA  
998  C C   . ALA A 138 ? 0.24894 0.21552 0.31265 0.04080  0.01864  0.05855  145 ALA A C   
999  O O   . ALA A 138 ? 0.36284 0.34397 0.41882 0.04508  0.01448  0.04659  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.25280 0.22109 0.32625 0.01980  0.01714  0.05192  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.26782 0.21185 0.33816 0.04196  0.02045  0.06657  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.31223 0.24581 0.37870 0.04955  0.01759  0.05906  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.37004 0.29137 0.43870 0.04013  0.01227  0.04193  146 GLU A C   
1004 O O   . GLU A 139 ? 0.38236 0.30240 0.44591 0.04756  0.01018  0.03291  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.33030 0.23977 0.40134 0.05696  0.02115  0.07379  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.52447 0.41429 0.61091 0.04513  0.02432  0.08768  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.83127 0.68745 0.92590 0.04887  0.02581  0.09919  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 0.86663 0.72367 0.95366 0.06549  0.02996  0.11085  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.95077 0.77879 1.05965 0.03568  0.02188  0.09608  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.32167 0.23728 0.39706 0.02592  0.01037  0.03804  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.30739 0.21255 0.38294 0.01824  0.00516  0.02300  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.27716 0.18968 0.35752 0.00537  0.00369  0.02092  147 LYS A C   
1013 O O   . LYS A 140 ? 0.31847 0.23124 0.40812 -0.00020 0.00593  0.03190  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.28767 0.16133 0.36857 0.01766  0.00190  0.02108  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.34053 0.20374 0.41905 0.01169  -0.00477 0.00431  147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.44511 0.27469 0.52661 0.01412  -0.00990 -0.00078 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.55578 0.36970 0.64852 -0.00072 -0.01766 -0.00685 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.55177 0.32939 0.65627 -0.00300 -0.02271 -0.00537 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.24139 0.16187 0.31602 0.00189  0.00080  0.00870  148 VAL A N   
1020 C CA  . VAL A 141 ? 0.24012 0.16785 0.31718 -0.00777 -0.00077 0.00638  148 VAL A CA  
1021 C C   . VAL A 141 ? 0.33346 0.25137 0.40858 -0.01252 -0.00604 -0.00504 148 VAL A C   
1022 O O   . VAL A 141 ? 0.25819 0.17682 0.32450 -0.00710 -0.00665 -0.01354 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.27878 0.22650 0.34941 -0.00632 0.00082  0.00429  148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.23900 0.19048 0.31092 -0.01408 -0.00075 0.00217  148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.20039 0.15978 0.26968 0.00078  0.00417  0.01282  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.30314 0.21543 0.38653 -0.02140 -0.00986 -0.00489 149 THR A N   
1027 C CA  . THR A 142 ? 0.32766 0.23461 0.40774 -0.02510 -0.01645 -0.01637 149 THR A CA  
1028 C C   . THR A 142 ? 0.28406 0.20628 0.36394 -0.03013 -0.01669 -0.01541 149 THR A C   
1029 O O   . THR A 142 ? 0.34507 0.27458 0.43510 -0.03482 -0.01520 -0.00676 149 THR A O   
1030 C CB  . THR A 142 ? 0.34676 0.23422 0.43825 -0.03122 -0.02380 -0.01949 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.37285 0.24167 0.46562 -0.02566 -0.02294 -0.01800 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.33892 0.22164 0.42246 -0.03152 -0.03262 -0.03511 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.26070 0.18871 0.32882 -0.02754 -0.01768 -0.02277 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.26433 0.20384 0.33019 -0.03021 -0.01786 -0.02136 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.29754 0.23520 0.35857 -0.03077 -0.02520 -0.03004 150 VAL A C   
1036 O O   . VAL A 143 ? 0.33992 0.27595 0.38827 -0.02472 -0.02608 -0.03761 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.27563 0.22414 0.33277 -0.02668 -0.01220 -0.01953 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.22830 0.18332 0.28274 -0.02836 -0.01256 -0.01717 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.23668 0.18866 0.29787 -0.02534 -0.00771 -0.01404 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.25118 0.19236 0.32216 -0.03668 -0.03069 -0.02900 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.27850 0.22283 0.34521 -0.03674 -0.03956 -0.03761 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.30101 0.26021 0.36256 -0.03451 -0.03720 -0.03177 151 ILE A C   
1043 O O   . ILE A 144 ? 0.27576 0.24217 0.34694 -0.03709 -0.03369 -0.02275 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.32845 0.26864 0.41366 -0.04571 -0.04938 -0.04106 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.39289 0.31412 0.48799 -0.04910 -0.04934 -0.04131 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.35782 0.29964 0.43607 -0.04418 -0.06170 -0.05505 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.46384 0.36706 0.54792 -0.04398 -0.05670 -0.05688 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.27721 0.24107 0.32241 -0.02780 -0.03853 -0.03600 152 THR A N   
1049 C CA  . THR A 145 ? 0.33329 0.30743 0.37186 -0.02400 -0.03509 -0.02839 152 THR A CA  
1050 C C   . THR A 145 ? 0.33128 0.31418 0.35672 -0.01743 -0.04193 -0.03377 152 THR A C   
1051 O O   . THR A 145 ? 0.31926 0.30018 0.33397 -0.01299 -0.04674 -0.04409 152 THR A O   
1052 C CB  . THR A 145 ? 0.30989 0.28116 0.34079 -0.02115 -0.02457 -0.02115 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.31956 0.29448 0.34871 -0.01916 -0.02140 -0.01245 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.30555 0.27812 0.32153 -0.01483 -0.02199 -0.02437 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.23799 0.23130 0.26267 -0.01459 -0.04268 -0.02710 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.24710 0.25225 0.25747 -0.00584 -0.04869 -0.02947 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.31387 0.32268 0.31684 0.00064  -0.04119 -0.01550 153 LYS A C   
1058 O O   . LYS A 146 ? 0.33451 0.34500 0.34838 -0.00107 -0.04009 -0.00888 153 LYS A O   
1059 C CB  . LYS A 146 ? 0.25847 0.27528 0.28010 -0.00893 -0.06277 -0.03807 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.27939 0.31301 0.28595 0.00195  -0.07063 -0.04047 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.30768 0.34086 0.29233 0.01067  -0.07548 -0.05253 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.31872 0.37217 0.28798 0.02266  -0.08623 -0.05720 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.31205 0.37446 0.26767 0.03374  -0.07652 -0.03919 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.28725 0.29693 0.27198 0.00900  -0.03548 -0.01015 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.32391 0.33364 0.30074 0.01572  -0.02834 0.00482  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.38550 0.41151 0.34580 0.02838  -0.03455 0.00565  154 HIS A C   
1067 O O   . HIS A 147 ? 0.40514 0.44118 0.35441 0.03325  -0.04174 -0.00547 154 HIS A O   
1068 C CB  . HIS A 147 ? 0.33200 0.33252 0.30376 0.01487  -0.01595 0.01440  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.32656 0.31998 0.29556 0.01834  -0.00805 0.03122  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.37775 0.37919 0.33078 0.03000  -0.00587 0.04229  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.33666 0.31350 0.31648 0.01234  -0.00238 0.03871  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.44436 0.43204 0.40023 0.03013  0.00153  0.05754  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.34143 0.31296 0.31368 0.01914  0.00296  0.05416  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.34005 0.36845 0.29734 0.03550  -0.03267 0.01793  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.36036 0.40710 0.30133 0.04972  -0.03914 0.02016  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.36692 0.42082 0.28442 0.05998  -0.03485 0.02311  155 ASN A C   
1077 O O   . ASN A 148 ? 0.38690 0.45980 0.28793 0.07193  -0.04383 0.01678  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.35913 0.40379 0.29899 0.05810  -0.03521 0.03630  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.41474 0.46503 0.37297 0.05510  -0.04251 0.03191  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.44794 0.51172 0.41859 0.04857  -0.05313 0.01807  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.35464 0.39482 0.31565 0.06045  -0.03669 0.04433  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.35818 0.40040 0.27417 0.05636  -0.02161 0.03239  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.39366 0.44620 0.28885 0.06728  -0.01381 0.04019  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.42072 0.47809 0.31118 0.06625  -0.01569 0.02437  156 ASP A C   
1085 O O   . ASP A 149 ? 0.50885 0.57556 0.38475 0.07470  -0.00635 0.03148  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.42330 0.46378 0.32270 0.06420  0.00287  0.06335  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.49527 0.52731 0.39496 0.06908  0.00535  0.08043  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.54111 0.58552 0.42993 0.08088  -0.00368 0.07827  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.50962 0.52220 0.42116 0.06150  0.01536  0.09525  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.35545 0.40699 0.25821 0.05721  -0.02674 0.00453  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.36434 0.41491 0.26344 0.05698  -0.02871 -0.01074 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.45003 0.49663 0.35813 0.05126  -0.04593 -0.03293 157 ASP A C   
1093 O O   . ASP A 150 ? 0.42406 0.47258 0.34390 0.04618  -0.05499 -0.03477 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.37615 0.41398 0.29041 0.04598  -0.01661 -0.00421 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.48493 0.52940 0.38758 0.05353  -0.01154 -0.00996 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.40130 0.45510 0.28456 0.06642  -0.01963 -0.02400 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.47731 0.51912 0.39015 0.04771  -0.00015 -0.00136 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.41802 0.45933 0.32212 0.05237  -0.05027 -0.04910 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.44674 0.47899 0.36208 0.04518  -0.06644 -0.06994 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.39582 0.40958 0.33829 0.02802  -0.06287 -0.06777 158 GLU A C   
1101 O O   . GLU A 151 ? 0.31755 0.32654 0.26754 0.02310  -0.04941 -0.05330 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.50971 0.54120 0.40514 0.05729  -0.07418 -0.08982 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.63916 0.69213 0.50167 0.07886  -0.07354 -0.08971 158 GLU A CG  
1104 C CD  . GLU A 151 ? 0.99075 1.06096 0.84782 0.08343  -0.08332 -0.08762 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.09216 1.15957 0.96680 0.07301  -0.09900 -0.09925 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.13840 1.22669 0.97505 0.09774  -0.07496 -0.07275 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.32128 0.32498 0.27915 0.01892  -0.07566 -0.08212 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.38343 0.37123 0.36600 0.00434  -0.07254 -0.07892 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.35640 0.32921 0.33374 0.00730  -0.06696 -0.08417 159 GLN A C   
1110 O O   . GLN A 152 ? 0.33105 0.29711 0.29627 0.01501  -0.07510 -0.10056 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.36758 0.35173 0.37205 -0.00735 -0.08735 -0.08865 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.31658 0.29121 0.34841 -0.02190 -0.08235 -0.07906 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.39587 0.37742 0.45343 -0.03401 -0.09400 -0.08106 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.36198 0.36364 0.42252 -0.03294 -0.09792 -0.07717 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.44617 0.41221 0.52429 -0.04543 -0.09928 -0.08564 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.28720 0.25543 0.27299 0.00272  -0.05404 -0.07144 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.30881 0.26728 0.29141 0.00656  -0.04764 -0.07386 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.35770 0.30270 0.36161 -0.00455 -0.04526 -0.06896 160 TYR A C   
1119 O O   . TYR A 153 ? 0.32087 0.26843 0.33980 -0.01398 -0.04349 -0.05917 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.36732 0.33888 0.33850 0.01408  -0.03363 -0.06232 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.40486 0.39069 0.35177 0.02913  -0.03309 -0.06589 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.36844 0.36792 0.30608 0.03259  -0.03327 -0.05878 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.38411 0.37107 0.31566 0.04243  -0.03198 -0.07572 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.43269 0.44799 0.34575 0.04865  -0.03190 -0.06004 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.45965 0.46324 0.36631 0.05911  -0.03051 -0.07844 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.54910 0.56752 0.44630 0.06200  -0.03027 -0.06994 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.77733 0.81499 0.64753 0.08076  -0.02790 -0.07062 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.28897 0.22074 0.29226 -0.00087 -0.04474 -0.07526 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.29067 0.20956 0.31108 -0.00812 -0.04202 -0.06975 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.44216 0.36558 0.45765 -0.00115 -0.03100 -0.06385 161 ALA A C   
1131 O O   . ALA A 154 ? 0.30602 0.22900 0.30834 0.01054  -0.02981 -0.07133 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.38950 0.28556 0.41724 -0.01029 -0.05265 -0.08138 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.26673 0.19676 0.29280 -0.00715 -0.02368 -0.05134 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.24756 0.18457 0.27403 -0.00281 -0.01519 -0.04566 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.32242 0.24714 0.35983 -0.00436 -0.01550 -0.04274 162 TRP A C   
1136 O O   . TRP A 155 ? 0.33803 0.25604 0.38661 -0.01240 -0.01810 -0.03804 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.26836 0.22092 0.29831 -0.00785 -0.00878 -0.03551 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.29885 0.26214 0.33364 -0.00641 -0.00216 -0.03009 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.24502 0.22446 0.27782 -0.00360 0.00381  -0.02702 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.31814 0.28052 0.36226 -0.00807 -0.00134 -0.02625 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.31821 0.30694 0.36073 -0.00469 0.00678  -0.02326 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.29236 0.27076 0.33977 -0.00622 0.00330  -0.02347 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.27571 0.22788 0.32620 -0.01030 -0.00381 -0.02373 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.26238 0.24675 0.31710 -0.00553 0.00367  -0.02084 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.24613 0.20395 0.30155 -0.00810 -0.00157 -0.01909 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.25066 0.22434 0.30711 -0.00528 0.00122  -0.01894 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.24450 0.16849 0.27897 0.00468  -0.01215 -0.04389 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.25756 0.16914 0.30023 0.00611  -0.01200 -0.03954 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.31512 0.23982 0.35608 0.01559  -0.00583 -0.03601 163 GLU A C   
1150 O O   . GLU A 156 ? 0.27755 0.21393 0.31063 0.02405  -0.00307 -0.04067 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.32933 0.21436 0.37144 0.00935  -0.01897 -0.04789 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.47849 0.34645 0.53426 0.00518  -0.01951 -0.03889 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.73621 0.57346 0.79653 0.00373  -0.02824 -0.04687 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.65004 0.47292 0.69939 0.01558  -0.03131 -0.05840 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.62262 0.45053 0.69861 -0.00906 -0.03242 -0.04197 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.29351 0.21959 0.34214 0.01532  -0.00363 -0.02710 164 SER A N   
1157 C CA  . SER A 157 ? 0.30409 0.24466 0.35249 0.02519  0.00040  -0.02397 164 SER A CA  
1158 C C   . SER A 157 ? 0.25917 0.19295 0.31277 0.02823  0.00105  -0.01452 164 SER A C   
1159 O O   . SER A 157 ? 0.29128 0.22464 0.35008 0.02054  0.00106  -0.00751 164 SER A O   
1160 C CB  . SER A 157 ? 0.24477 0.21277 0.29616 0.02099  0.00328  -0.02225 164 SER A CB  
1161 O OG  . SER A 157 ? 0.26721 0.25345 0.32138 0.02990  0.00556  -0.02030 164 SER A OG  
1162 N N   . SER A 158 ? 0.29745 0.22751 0.34860 0.04153  0.00232  -0.01322 165 SER A N   
1163 C CA  . SER A 158 ? 0.26211 0.19263 0.31589 0.04863  0.00427  -0.00206 165 SER A CA  
1164 C C   . SER A 158 ? 0.31836 0.28029 0.37173 0.05666  0.00589  -0.00087 165 SER A C   
1165 O O   . SER A 158 ? 0.32137 0.28737 0.37336 0.06971  0.00706  0.00549  165 SER A O   
1166 C CB  . SER A 158 ? 0.35822 0.26070 0.41038 0.05934  0.00390  0.00034  165 SER A CB  
1167 O OG  . SER A 158 ? 0.36744 0.24032 0.42445 0.04942  0.00048  -0.00064 165 SER A OG  
1168 N N   . ALA A 159 ? 0.32836 0.31258 0.38434 0.04887  0.00534  -0.00646 166 ALA A N   
1169 C CA  . ALA A 159 ? 0.34835 0.36482 0.40893 0.05280  0.00503  -0.00774 166 ALA A CA  
1170 C C   . ALA A 159 ? 0.34321 0.36740 0.40257 0.06699  0.00732  -0.01028 166 ALA A C   
1171 O O   . ALA A 159 ? 0.40429 0.41426 0.45836 0.06944  0.00901  -0.01544 166 ALA A O   
1172 C CB  . ALA A 159 ? 0.34610 0.37459 0.40718 0.05658  0.00286  -0.00173 166 ALA A CB  
1173 N N   . GLY A 160 ? 0.29039 0.33869 0.35353 0.07833  0.00691  -0.00766 167 GLY A N   
1174 C CA  . GLY A 160 ? 0.28315 0.34320 0.34585 0.09404  0.00969  -0.00956 167 GLY A CA  
1175 C C   . GLY A 160 ? 0.31344 0.39733 0.38282 0.08988  0.01276  -0.01481 167 GLY A C   
1176 O O   . GLY A 160 ? 0.31640 0.40891 0.38314 0.10437  0.01657  -0.01687 167 GLY A O   
1177 N N   . GLY A 161 ? 0.22135 0.31578 0.29895 0.07183  0.01194  -0.01590 168 GLY A N   
1178 C CA  . GLY A 161 ? 0.27656 0.39760 0.36414 0.06633  0.01597  -0.01663 168 GLY A CA  
1179 C C   . GLY A 161 ? 0.27975 0.38575 0.35728 0.06458  0.02064  -0.01937 168 GLY A C   
1180 O O   . GLY A 161 ? 0.21712 0.34717 0.30147 0.06242  0.02605  -0.01725 168 GLY A O   
1181 N N   . SER A 162 ? 0.24791 0.31753 0.31055 0.06544  0.01855  -0.02331 169 SER A N   
1182 C CA  . SER A 162 ? 0.24577 0.30244 0.29671 0.06588  0.02080  -0.02820 169 SER A CA  
1183 C C   . SER A 162 ? 0.32466 0.34907 0.36909 0.05462  0.01566  -0.03069 169 SER A C   
1184 O O   . SER A 162 ? 0.23777 0.24472 0.28408 0.05118  0.01159  -0.02866 169 SER A O   
1185 C CB  . SER A 162 ? 0.26825 0.31728 0.30563 0.08689  0.02269  -0.03492 169 SER A CB  
1186 O OG  . SER A 162 ? 0.31997 0.33422 0.34999 0.09310  0.01731  -0.03857 169 SER A OG  
1187 N N   . PHE A 163 ? 0.26589 0.28619 0.30308 0.04994  0.01638  -0.03376 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.25177 0.24522 0.28276 0.04153  0.01087  -0.03747 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.33152 0.31745 0.34687 0.04982  0.00994  -0.04655 170 PHE A C   
1190 O O   . PHE A 163 ? 0.29913 0.30479 0.30794 0.06039  0.01556  -0.04747 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.26727 0.26577 0.30603 0.02506  0.01054  -0.03142 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.29335 0.31286 0.33315 0.02138  0.01589  -0.02730 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.27550 0.32077 0.32853 0.01830  0.02063  -0.02055 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.29140 0.30592 0.32054 0.02058  0.01581  -0.02901 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.32174 0.38534 0.37943 0.01313  0.02650  -0.01357 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.22356 0.25708 0.25346 0.01807  0.02216  -0.02167 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.26766 0.32467 0.31298 0.01354  0.02816  -0.01288 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.27068 0.23058 0.28049 0.04568  0.00245  -0.05334 171 THR A N   
1199 C CA  . THR A 164 ? 0.29195 0.24320 0.28561 0.05330  -0.00175 -0.06500 171 THR A CA  
1200 C C   . THR A 164 ? 0.28397 0.23450 0.27690 0.04119  -0.00553 -0.06413 171 THR A C   
1201 O O   . THR A 164 ? 0.34461 0.29039 0.34985 0.02728  -0.00730 -0.05729 171 THR A O   
1202 C CB  . THR A 164 ? 0.31958 0.23867 0.30759 0.06091  -0.01052 -0.07763 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.32445 0.22197 0.32520 0.04597  -0.01733 -0.07522 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.33024 0.24693 0.31873 0.07488  -0.00680 -0.07708 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.33455 0.29217 0.31138 0.04905  -0.00648 -0.07083 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.34542 0.30376 0.31795 0.04177  -0.01113 -0.07122 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.41900 0.36609 0.37307 0.05303  -0.02101 -0.08880 172 VAL A C   
1208 O O   . VAL A 165 ? 0.36501 0.31916 0.30203 0.07042  -0.01859 -0.09648 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.28576 0.27058 0.25615 0.04048  -0.00135 -0.05812 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.31463 0.30001 0.27686 0.03730  -0.00643 -0.05855 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.25892 0.25128 0.24885 0.02789  0.00530  -0.04403 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.33212 0.26362 0.29003 0.04402  -0.03275 -0.09599 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.42761 0.34845 0.36985 0.05263  -0.04567 -0.11525 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.39512 0.32049 0.34102 0.04224  -0.05417 -0.11534 173 ARG A C   
1215 O O   . ARG A 166 ? 0.33358 0.26208 0.29756 0.02736  -0.05163 -0.10230 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.41705 0.30529 0.36509 0.05296  -0.05654 -0.13007 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.49979 0.37041 0.47507 0.03271  -0.06172 -0.12351 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.48972 0.32835 0.47439 0.03308  -0.06666 -0.12982 173 ARG A CD  
1219 N NE  . ARG A 166 ? 0.57398 0.41492 0.56658 0.03448  -0.05399 -0.11467 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 0.69080 0.50991 0.68478 0.04236  -0.05378 -0.11719 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 0.66825 0.45659 0.65714 0.04878  -0.06548 -0.13469 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.78499 0.61242 0.78539 0.04470  -0.04257 -0.10252 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.38532 0.31300 0.31249 0.05240  -0.06481 -0.13102 174 THR A N   
1224 C CA  . THR A 167 ? 0.47513 0.40695 0.40658 0.04399  -0.07662 -0.13480 174 THR A CA  
1225 C C   . THR A 167 ? 0.45202 0.36068 0.40995 0.02661  -0.08854 -0.14052 174 THR A C   
1226 O O   . THR A 167 ? 0.55636 0.43997 0.51747 0.02751  -0.09679 -0.15447 174 THR A O   
1227 C CB  . THR A 167 ? 0.49202 0.43207 0.39592 0.06084  -0.08778 -0.15333 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.45741 0.42474 0.33892 0.07588  -0.07448 -0.14191 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.64307 0.58670 0.55447 0.05186  -0.10405 -0.16100 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.37611 0.29308 0.35405 0.01140  -0.08868 -0.12833 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.44987 0.35136 0.45689 -0.00612 -0.09731 -0.12869 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.62500 0.52418 0.63543 -0.00960 -0.11782 -0.14745 175 ASP A C   
1233 O O   . ASP A 168 ? 0.58678 0.50809 0.59057 -0.00728 -0.12310 -0.14847 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.39716 0.31245 0.42404 -0.01858 -0.08806 -0.10761 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.54543 0.44927 0.60368 -0.03553 -0.09308 -0.10321 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.65359 0.53400 0.72012 -0.03825 -0.09388 -0.10606 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.58299 0.50235 0.65823 -0.04518 -0.09562 -0.09551 175 ASP A OD2 
1238 N N   . THR A 169 ? 0.62054 0.49242 0.64191 -0.01484 -0.13028 -0.16252 176 THR A N   
1239 C CA  . THR A 169 ? 0.91874 0.78997 0.94926 -0.02156 -0.14672 -0.17509 176 THR A CA  
1240 C C   . THR A 169 ? 0.79823 0.67147 0.86684 -0.04411 -0.14800 -0.16133 176 THR A C   
1241 O O   . THR A 169 ? 0.80890 0.68274 0.89060 -0.05265 -0.16011 -0.16882 176 THR A O   
1242 C CB  . THR A 169 ? 1.04290 0.88902 1.06211 -0.01325 -0.15297 -0.19117 176 THR A CB  
1243 O OG1 . THR A 169 ? 0.86866 0.69100 0.89290 -0.01311 -0.14214 -0.18312 176 THR A OG1 
1244 C CG2 . THR A 169 ? 0.72793 0.58327 0.70863 0.01073  -0.15640 -0.20813 176 THR A CG2 
1245 N N   . GLY A 170 ? 0.83229 0.70875 0.91862 -0.05300 -0.13545 -0.14122 177 GLY A N   
1246 C CA  . GLY A 170 ? 0.78446 0.66697 0.90504 -0.07155 -0.13337 -0.12516 177 GLY A CA  
1247 C C   . GLY A 170 ? 0.66403 0.57794 0.79780 -0.07831 -0.13998 -0.12200 177 GLY A C   
1248 O O   . GLY A 170 ? 0.56951 0.49758 0.68696 -0.07003 -0.15091 -0.13606 177 GLY A O   
1249 N N   . GLU A 171 ? 0.64109 0.56867 0.80306 -0.09112 -0.13295 -0.10282 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.55069 0.51091 0.73023 -0.09763 -0.13860 -0.09772 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.40695 0.38814 0.56673 -0.08469 -0.13604 -0.09654 178 GLU A C   
1252 O O   . GLU A 171 ? 0.37808 0.35755 0.52479 -0.07733 -0.11837 -0.08231 178 GLU A O   
1253 C CB  . GLU A 171 ? 0.53234 0.50398 0.74444 -0.11101 -0.12823 -0.07514 178 GLU A CB  
1254 C CG  . GLU A 171 ? 0.56759 0.57121 0.80541 -0.12072 -0.13564 -0.07094 178 GLU A CG  
1255 C CD  . GLU A 171 ? 0.66232 0.66111 0.90515 -0.12766 -0.15218 -0.08821 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 0.60443 0.57581 0.85244 -0.13451 -0.15317 -0.09175 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 0.63019 0.65282 0.87165 -0.12549 -0.16483 -0.09827 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.49300 0.49479 0.64207 -0.07794 -0.14791 -0.10727 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.42521 0.44665 0.54807 -0.06182 -0.13835 -0.09891 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.45545 0.49425 0.59347 -0.06442 -0.12419 -0.07617 179 PRO A C   
1261 O O   . PRO A 172 ? 0.55095 0.60380 0.72144 -0.07696 -0.12679 -0.06846 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.37702 0.42056 0.49312 -0.05600 -0.15649 -0.11337 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.56318 0.59539 0.69714 -0.06804 -0.17670 -0.13375 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.55445 0.55636 0.70374 -0.08011 -0.16697 -0.12735 179 PRO A CD  
1265 N N   . MET A 173 ? 0.40960 0.44798 0.52438 -0.05188 -0.10924 -0.06546 180 MET A N   
1266 C CA  . MET A 173 ? 0.41545 0.46487 0.53858 -0.05088 -0.09566 -0.04661 180 MET A CA  
1267 C C   . MET A 173 ? 0.40620 0.47831 0.51980 -0.03934 -0.09537 -0.04030 180 MET A C   
1268 O O   . MET A 173 ? 0.55894 0.64396 0.68363 -0.03794 -0.08768 -0.02695 180 MET A O   
1269 C CB  . MET A 173 ? 0.43953 0.46918 0.54720 -0.04620 -0.07959 -0.03883 180 MET A CB  
1270 C CG  . MET A 173 ? 0.73606 0.74228 0.84668 -0.05285 -0.07848 -0.04432 180 MET A CG  
1271 S SD  . MET A 173 ? 0.79796 0.78897 0.89278 -0.04655 -0.06120 -0.03510 180 MET A SD  
1272 C CE  . MET A 173 ? 0.45395 0.46154 0.55598 -0.04388 -0.05176 -0.01909 180 MET A CE  
1273 N N   . GLY A 174 ? 0.32352 0.40095 0.41523 -0.02881 -0.10294 -0.04884 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.37875 0.47457 0.45805 -0.01527 -0.10132 -0.04052 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.31296 0.39331 0.36973 -0.00498 -0.08515 -0.02870 181 GLY A C   
1276 O O   . GLY A 174 ? 0.35089 0.42877 0.38242 0.00654  -0.08362 -0.02848 181 GLY A O   
1277 N N   . ARG A 175 ? 0.25976 0.33047 0.32617 -0.00898 -0.07332 -0.01854 182 ARG A N   
1278 C CA  . ARG A 175 ? 0.28355 0.33642 0.33358 -0.00262 -0.05967 -0.00943 182 ARG A CA  
1279 C C   . ARG A 175 ? 0.33951 0.38281 0.40338 -0.00960 -0.05098 -0.00438 182 ARG A C   
1280 O O   . ARG A 175 ? 0.31966 0.37651 0.40277 -0.01294 -0.05198 -0.00076 182 ARG A O   
1281 C CB  . ARG A 175 ? 0.24034 0.29950 0.27847 0.01101  -0.05638 0.00107  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.26821 0.30539 0.29056 0.01595  -0.04414 0.00982  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.24986 0.28591 0.26772 0.02748  -0.03971 0.02142  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.23991 0.28363 0.27436 0.02735  -0.03924 0.02288  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.27550 0.34302 0.31950 0.03387  -0.04501 0.02504  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.26603 0.35159 0.30452 0.04090  -0.05338 0.02484  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.23298 0.30985 0.29220 0.03479  -0.04231 0.02776  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.34341 0.33807 0.23095 0.07175  -0.02376 0.05202  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.30175 0.28615 0.21961 0.05785  -0.01824 0.04657  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.38107 0.36012 0.30034 0.04885  -0.01246 0.03592  183 GLY A C   
1291 O O   . GLY A 176 ? 0.37557 0.35599 0.27297 0.05505  -0.00800 0.03513  183 GLY A O   
1292 N N   . THR A 177 ? 0.33972 0.31428 0.28332 0.03674  -0.01200 0.02818  184 THR A N   
1293 C CA  . THR A 177 ? 0.28920 0.26049 0.23795 0.03025  -0.00643 0.02040  184 THR A CA  
1294 C C   . THR A 177 ? 0.43498 0.40550 0.39832 0.02063  -0.01602 0.00734  184 THR A C   
1295 O O   . THR A 177 ? 0.31746 0.29079 0.29648 0.01565  -0.02068 0.00747  184 THR A O   
1296 C CB  . THR A 177 ? 0.31851 0.28611 0.28317 0.02466  0.00828  0.03027  184 THR A CB  
1297 O OG1 . THR A 177 ? 0.33050 0.29812 0.28185 0.03171  0.01924  0.04552  184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.32828 0.30122 0.30168 0.02016  0.01265  0.02339  184 THR A CG2 
1299 N N   . LYS A 178 ? 0.28824 0.25413 0.24471 0.01995  -0.01755 -0.00260 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.31022 0.27036 0.27673 0.01121  -0.02519 -0.01248 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.31855 0.27501 0.29163 0.01175  -0.01689 -0.01339 185 LYS A C   
1302 O O   . LYS A 178 ? 0.32966 0.28374 0.28857 0.02127  -0.01139 -0.01532 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.44137 0.39332 0.38964 0.01068  -0.03814 -0.02429 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.57922 0.51690 0.53341 0.00131  -0.04420 -0.03299 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.74470 0.66442 0.67653 -0.00079 -0.05680 -0.04704 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.64768 0.57974 0.56641 -0.00087 -0.06883 -0.05062 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.76247 0.72266 0.70337 -0.00550 -0.07203 -0.04000 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.29714 0.25649 0.29041 0.00386  -0.01585 -0.01175 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.23781 0.19975 0.23960 0.00477  -0.01051 -0.01161 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.33542 0.28548 0.33639 0.00189  -0.01762 -0.01732 186 VAL A C   
1311 O O   . VAL A 179 ? 0.25927 0.21047 0.27054 -0.00693 -0.02182 -0.01646 186 VAL A O   
1312 C CB  . VAL A 179 ? 0.22173 0.19567 0.24326 -0.00213 -0.00537 -0.00589 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.19357 0.17773 0.22513 -0.00109 -0.00296 -0.00590 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.24971 0.22844 0.27221 -0.00190 0.00254  0.00188  186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.30034 0.23728 0.28756 0.01059  -0.01762 -0.02214 187 ILE A N   
1316 C CA  . ILE A 180 ? 0.28928 0.20598 0.27216 0.00876  -0.02337 -0.02587 187 ILE A CA  
1317 C C   . ILE A 180 ? 0.33478 0.25852 0.32666 0.01597  -0.01806 -0.02053 187 ILE A C   
1318 O O   . ILE A 180 ? 0.28824 0.21850 0.27654 0.02985  -0.01154 -0.02003 187 ILE A O   
1319 C CB  . ILE A 180 ? 0.30886 0.19757 0.26643 0.01518  -0.02808 -0.03630 187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.31799 0.20714 0.26591 0.00839  -0.03591 -0.04210 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.32840 0.18761 0.28145 0.01071  -0.03378 -0.03871 187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.43436 0.30060 0.35121 0.01753  -0.04022 -0.05508 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.25570 0.18265 0.25900 0.00812  -0.02064 -0.01566 188 LEU A N   
1324 C CA  . LEU A 181 ? 0.28666 0.22396 0.29720 0.01505  -0.01831 -0.00972 188 LEU A CA  
1325 C C   . LEU A 181 ? 0.31040 0.21874 0.30827 0.02069  -0.02107 -0.00799 188 LEU A C   
1326 O O   . LEU A 181 ? 0.33750 0.23208 0.33462 0.00962  -0.02498 -0.00502 188 LEU A O   
1327 C CB  . LEU A 181 ? 0.24272 0.20092 0.26793 0.00501  -0.01943 -0.00557 188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.31055 0.28656 0.34645 -0.00266 -0.01724 -0.00763 188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.29060 0.27929 0.33451 -0.01019 -0.01908 -0.00688 188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.28197 0.27467 0.32460 0.00312  -0.01196 -0.00679 188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.29615 0.19483 0.28431 0.03869  -0.01781 -0.00848 189 HIS A N   
1332 C CA  . HIS A 182 ? 0.35356 0.21952 0.32808 0.04814  -0.01924 -0.00490 189 HIS A CA  
1333 C C   . HIS A 182 ? 0.31340 0.20176 0.29917 0.05373  -0.01887 0.00738  189 HIS A C   
1334 O O   . HIS A 182 ? 0.32938 0.24386 0.32252 0.06966  -0.01582 0.01094  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.32716 0.17061 0.28300 0.06981  -0.01521 -0.01152 189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.42670 0.25987 0.36911 0.06741  -0.01533 -0.02472 189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.48542 0.27201 0.40308 0.06541  -0.02076 -0.03619 189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.39500 0.25767 0.34300 0.06654  -0.01130 -0.02779 189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.52917 0.32073 0.43609 0.06493  -0.02112 -0.04678 189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.47291 0.31004 0.39765 0.06651  -0.01437 -0.04026 189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.32696 0.20979 0.31426 0.04085  -0.02212 0.01450  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.34231 0.25363 0.33800 0.04289  -0.02309 0.02461  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.34657 0.24979 0.33338 0.06441  -0.02271 0.03539  190 LEU A C   
1344 O O   . LEU A 183 ? 0.41728 0.27835 0.38795 0.07411  -0.02119 0.03785  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.32691 0.23549 0.32275 0.02563  -0.02435 0.03018  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.33686 0.26206 0.34361 0.00843  -0.02448 0.02193  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.28713 0.21434 0.29424 -0.00399 -0.02341 0.02937  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.31708 0.27740 0.33556 0.01000  -0.02477 0.01584  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.35367 0.29673 0.35017 0.07234  -0.02510 0.04148  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.47492 0.41916 0.46400 0.09440  -0.02633 0.05488  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.43703 0.34576 0.40816 0.09123  -0.02607 0.06838  191 LYS A C   
1352 O O   . LYS A 184 ? 0.47873 0.38102 0.44906 0.07043  -0.02562 0.06831  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.42807 0.42988 0.43248 0.09927  -0.03218 0.05769  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.37890 0.41980 0.40448 0.10582  -0.03149 0.05024  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.48676 0.58241 0.53182 0.09439  -0.03945 0.04701  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.52715 0.66510 0.59840 0.09616  -0.03794 0.04213  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.63457 0.82373 0.72627 0.08156  -0.04791 0.03814  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.50273 0.38958 0.45992 0.11360  -0.02518 0.08207  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.53106 0.37600 0.46937 0.11134  -0.02302 0.09857  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.49777 0.37318 0.43589 0.09982  -0.02486 0.10897  192 GLU A C   
1361 O O   . GLU A 185 ? 0.63327 0.48305 0.56239 0.08499  -0.02075 0.11906  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.69313 0.51005 0.61502 0.14227  -0.02153 0.11352  192 GLU A CB  
1363 C CG  . GLU A 185 ? 0.87912 0.63923 0.77902 0.14027  -0.01763 0.13285  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.21559 0.94280 1.10394 0.16418  -0.01585 0.13919  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.32809 1.03063 1.21594 0.17129  -0.01390 0.12384  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.19806 0.92830 1.07822 0.17449  -0.01628 0.15754  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.46071 0.39173 0.40821 0.10557  -0.03087 0.10624  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.48135 0.44225 0.42241 0.09885  -0.03359 0.11344  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.38527 0.37174 0.33855 0.07572  -0.03435 0.09603  193 ASP A C   
1370 O O   . ASP A 186 ? 0.44226 0.46100 0.39037 0.07263  -0.03810 0.09526  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.45324 0.45766 0.39183 0.12048  -0.04251 0.12088  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.63229 0.67998 0.59489 0.12360  -0.04958 0.10455  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.67508 0.71228 0.65254 0.11356  -0.04549 0.09025  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 0.66259 0.75752 0.62959 0.13534  -0.05952 0.10703  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.36008 0.33102 0.32626 0.06149  -0.03110 0.08183  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.31581 0.30660 0.29325 0.04313  -0.03119 0.06644  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.31724 0.28064 0.29615 0.02599  -0.02463 0.06542  194 GLN A C   
1378 O O   . GLN A 187 ? 0.36119 0.33198 0.35151 0.01403  -0.02405 0.05226  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.31577 0.32666 0.31101 0.04266  -0.03479 0.05062  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.33032 0.37841 0.33181 0.05616  -0.04232 0.05124  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.33367 0.41485 0.32995 0.05181  -0.04961 0.04873  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.37432 0.45645 0.36854 0.03710  -0.04850 0.03899  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.35356 0.46237 0.34554 0.06672  -0.05764 0.05689  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.37482 0.30766 0.34342 0.02416  -0.02002 0.08052  195 THR A N   
1385 C CA  . THR A 188 ? 0.48022 0.39172 0.45449 0.00510  -0.01532 0.08090  195 THR A CA  
1386 C C   . THR A 188 ? 0.39952 0.33829 0.37784 -0.00676 -0.01038 0.08285  195 THR A C   
1387 O O   . THR A 188 ? 0.46330 0.39567 0.45132 -0.02283 -0.00638 0.08441  195 THR A O   
1388 C CB  . THR A 188 ? 0.45829 0.32520 0.42199 0.00341  -0.01213 0.09718  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.46224 0.33397 0.41179 0.01056  -0.00781 0.11808  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.50187 0.33581 0.45805 0.01892  -0.01585 0.09293  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.37295 0.34378 0.34373 0.00146  -0.01095 0.08197  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.45115 0.44719 0.42195 -0.00546 -0.00507 0.08058  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.31253 0.31633 0.30051 -0.01474 -0.00541 0.06314  196 GLU A C   
1394 O O   . GLU A 189 ? 0.34402 0.36148 0.33767 -0.02168 0.00136  0.06384  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.38798 0.41254 0.34165 0.00675  -0.00789 0.07822  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.32616 0.36618 0.28550 0.01013  -0.01756 0.05712  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.46459 0.53141 0.40601 0.02002  -0.02428 0.05321  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.47939 0.55201 0.41263 0.03132  -0.03073 0.06247  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.45579 0.53759 0.38986 0.01777  -0.02392 0.04005  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.35351 0.35099 0.34983 -0.01314 -0.01213 0.04946  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.36590 0.36757 0.37575 -0.01969 -0.01260 0.03539  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.35437 0.33968 0.37547 -0.03052 -0.01167 0.03760  197 TYR A C   
1403 O O   . TYR A 190 ? 0.35207 0.33947 0.38297 -0.03401 -0.01345 0.02762  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.29002 0.29380 0.30350 -0.01452 -0.01876 0.02289  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.24450 0.26852 0.25003 -0.00797 -0.02268 0.01864  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.27056 0.30842 0.27045 -0.00948 -0.02146 0.01020  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.24761 0.27784 0.25004 0.00087  -0.02841 0.02236  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.26545 0.32005 0.25493 -0.00550 -0.02759 0.00319  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.32564 0.38014 0.32201 0.00505  -0.03500 0.01764  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.30125 0.36646 0.29015 0.00026  -0.03541 0.00694  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.35771 0.44505 0.33756 0.00243  -0.04440 -0.00103 197 TYR A OH  
1412 N N   . LEU A 191 ? 0.32669 0.29469 0.34549 -0.03654 -0.00980 0.05082  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.32227 0.27893 0.35287 -0.05196 -0.01010 0.05344  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.34838 0.32754 0.38877 -0.06241 -0.00215 0.06558  198 LEU A C   
1415 O O   . LEU A 191 ? 0.34010 0.32151 0.39656 -0.07781 -0.00301 0.06788  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.31878 0.23509 0.34152 -0.05553 -0.01358 0.05924  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.33827 0.23163 0.35100 -0.04295 -0.01955 0.04812  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.45096 0.29802 0.45186 -0.04407 -0.02161 0.05355  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.40717 0.30837 0.42772 -0.04542 -0.02422 0.03191  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.30783 0.30731 0.33889 -0.05425 0.00538  0.07334  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.33198 0.35783 0.37007 -0.06077 0.01620  0.08686  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.36071 0.41903 0.41046 -0.05671 0.01943  0.07583  199 GLU A C   
1423 O O   . GLU A 192 ? 0.30822 0.36950 0.34939 -0.04405 0.01638  0.06048  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.36675 0.40025 0.38330 -0.05027 0.02377  0.10022  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.48762 0.48792 0.48972 -0.04900 0.02104  0.11375  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.87560 0.88726 0.85417 -0.03713 0.02825  0.13016  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 1.02997 1.07523 1.00317 -0.03262 0.03699  0.13178  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 0.90311 0.89027 0.86603 -0.02979 0.02537  0.14160  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.27936 0.36210 0.34990 -0.06760 0.02580  0.08474  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.29317 0.40713 0.37767 -0.06117 0.02882  0.07595  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.28468 0.41516 0.35036 -0.04107 0.03752  0.06975  200 GLU A C   
1432 O O   . GLU A 193 ? 0.26384 0.39371 0.32559 -0.02895 0.03489  0.05351  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.29906 0.44612 0.41257 -0.07571 0.03493  0.08993  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.47569 0.65972 0.60614 -0.06534 0.03820  0.08305  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.78449 1.01211 0.94958 -0.07988 0.04337  0.09812  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 0.50324 0.73753 0.67665 -0.09695 0.04990  0.11649  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.77836 1.03525 0.96373 -0.07452 0.04087  0.09314  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.31290 0.45541 0.36390 -0.03712 0.04800  0.08248  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.34766 0.50757 0.37680 -0.01745 0.05647  0.07477  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.33631 0.47083 0.34074 -0.00705 0.04575  0.05555  201 ARG A C   
1441 O O   . ARG A 194 ? 0.32635 0.46490 0.31537 0.00719  0.04752  0.03981  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.33783 0.51916 0.35300 -0.01480 0.07065  0.09434  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.43413 0.59230 0.43329 -0.02110 0.06662  0.10824  201 ARG A CG  
1444 C CD  . ARG A 194 ? 0.53096 0.71246 0.51157 -0.01539 0.08243  0.12947  201 ARG A CD  
1445 N NE  . ARG A 194 ? 0.55500 0.71341 0.51382 -0.01561 0.07847  0.14361  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 0.58971 0.76178 0.52449 -0.00841 0.09003  0.16399  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 0.50185 0.71233 0.43085 -0.00111 0.10781  0.17252  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 0.64208 0.79031 0.55665 -0.00593 0.08453  0.17737  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.26128 0.36989 0.26229 -0.01393 0.03465  0.05621  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.29423 0.38680 0.27904 -0.00672 0.02378  0.03944  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.26901 0.34976 0.26677 -0.00771 0.01735  0.02219  202 ARG A C   
1452 O O   . ARG A 195 ? 0.29981 0.37513 0.28622 -0.00102 0.01336  0.00565  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.34708 0.42208 0.32689 -0.01025 0.01554  0.04777  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.35212 0.41961 0.32240 -0.00458 0.00357  0.03288  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.32433 0.40785 0.26794 0.00603  0.00219  0.02805  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.31137 0.39421 0.24977 0.00831  -0.01145 0.01685  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.37156 0.45874 0.30251 0.00901  -0.01858 -0.00358 202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.26951 0.35517 0.19303 0.01088  -0.01289 -0.01661 202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.32933 0.42232 0.26111 0.00781  -0.03179 -0.01113 202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.26987 0.34520 0.28976 -0.01682 0.01580  0.02609  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.24740 0.31286 0.27728 -0.01612 0.01087  0.01332  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.29818 0.37605 0.32708 -0.00513 0.01814  0.00576  203 ILE A C   
1463 O O   . ILE A 196 ? 0.26882 0.33222 0.29147 0.00101  0.01544  -0.00808 203 ILE A O   
1464 C CB  . ILE A 196 ? 0.29622 0.35585 0.34533 -0.02685 0.00641  0.01911  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.25924 0.29822 0.30436 -0.03369 -0.00025 0.02352  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.23412 0.28682 0.29023 -0.02363 0.00239  0.00885  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.37110 0.40085 0.42915 -0.04559 -0.00444 0.02897  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.29957 0.40373 0.33509 -0.00190 0.02846  0.01564  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.28218 0.40041 0.31544 0.01384  0.03747  0.00903  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.31633 0.42055 0.31951 0.02642  0.03881  -0.00677 204 LYS A C   
1471 O O   . LYS A 197 ? 0.33997 0.42989 0.33531 0.03805  0.03982  -0.02103 204 LYS A O   
1472 C CB  . LYS A 197 ? 0.24944 0.40703 0.29595 0.01612  0.05044  0.02458  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.39004 0.56716 0.46987 0.00208  0.04795  0.03801  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.44357 0.66790 0.54125 0.00380  0.06211  0.05393  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.64431 0.87664 0.73757 -0.00895 0.06866  0.07086  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.70169 0.97645 0.82785 -0.02291 0.07685  0.09179  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.25235 0.35845 0.23648 0.02448  0.03798  -0.00462 205 GLU A N   
1478 C CA  . GLU A 198 ? 0.30133 0.39654 0.25420 0.03436  0.03590  -0.02167 205 GLU A CA  
1479 C C   . GLU A 198 ? 0.27924 0.34307 0.23022 0.02893  0.02307  -0.03943 205 GLU A C   
1480 O O   . GLU A 198 ? 0.29801 0.34434 0.23144 0.03682  0.02222  -0.05810 205 GLU A O   
1481 C CB  . GLU A 198 ? 0.31768 0.42420 0.25138 0.03264  0.03440  -0.01334 205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.36164 0.45944 0.26203 0.03971  0.02690  -0.03233 205 GLU A CG  
1483 C CD  . GLU A 198 ? 0.37728 0.48828 0.26003 0.03868  0.02216  -0.02171 205 GLU A CD  
1484 O OE1 . GLU A 198 ? 0.32991 0.43870 0.22896 0.02843  0.01630  -0.00735 205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.36898 0.49142 0.21882 0.05030  0.02432  -0.02770 205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.26743 0.32250 0.23579 0.01529  0.01384  -0.03375 206 ILE A N   
1487 C CA  . ILE A 199 ? 0.32509 0.35685 0.29543 0.00811  0.00342  -0.04677 206 ILE A CA  
1488 C C   . ILE A 199 ? 0.31009 0.32300 0.28891 0.01182  0.00672  -0.05337 206 ILE A C   
1489 O O   . ILE A 199 ? 0.33147 0.32039 0.30124 0.01132  0.00310  -0.06839 206 ILE A O   
1490 C CB  . ILE A 199 ? 0.27626 0.30855 0.26213 -0.00348 -0.00443 -0.03706 206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.31931 0.36608 0.29351 -0.00350 -0.00860 -0.03051 206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.30753 0.32278 0.30109 -0.01135 -0.01207 -0.04674 206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.37615 0.42302 0.36379 -0.00904 -0.01223 -0.01680 206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.25662 0.27944 0.25276 0.01504  0.01281  -0.04161 207 VAL A N   
1495 C CA  . VAL A 200 ? 0.24848 0.25666 0.25195 0.02212  0.01569  -0.04451 207 VAL A CA  
1496 C C   . VAL A 200 ? 0.29855 0.29542 0.28339 0.03896  0.02315  -0.05717 207 VAL A C   
1497 O O   . VAL A 200 ? 0.41364 0.37857 0.39126 0.04307  0.02234  -0.06773 207 VAL A O   
1498 C CB  . VAL A 200 ? 0.27796 0.30804 0.30361 0.02294  0.01853  -0.02928 207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.21897 0.24283 0.24941 0.03723  0.02298  -0.03015 207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.23461 0.26207 0.27280 0.00805  0.00994  -0.02200 207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.28747 0.30771 0.26219 0.04981  0.03165  -0.05588 208 LYS A N   
1502 C CA  . LYS A 201 ? 0.33666 0.34666 0.28880 0.07007  0.04045  -0.06957 208 LYS A CA  
1503 C C   . LYS A 201 ? 0.40270 0.37738 0.32625 0.06647  0.03261  -0.09193 208 LYS A C   
1504 O O   . LYS A 201 ? 0.43460 0.37733 0.33954 0.07900  0.03554  -0.10827 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.31961 0.36902 0.26639 0.08237  0.05296  -0.06123 208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.43112 0.47302 0.34628 0.10610  0.06332  -0.07739 208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.44511 0.53345 0.35599 0.11752  0.07793  -0.06515 208 LYS A CD  
1508 C CE  . LYS A 201 ? 0.47614 0.56141 0.35590 0.14726  0.09178  -0.08041 208 LYS A CE  
1509 N NZ  . LYS A 201 ? 0.60513 0.74328 0.48384 0.16007  0.10963  -0.06477 208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.41785 0.39679 0.33805 0.04944  0.02168  -0.09326 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.45234 0.40734 0.34796 0.04298  0.01130  -0.11472 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.42264 0.34015 0.32773 0.02892  0.00258  -0.12374 209 LYS A C   
1513 O O   . LYS A 202 ? 0.41983 0.30233 0.30469 0.02823  -0.00160 -0.14465 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.40753 0.38850 0.29893 0.03186  0.00198  -0.11020 209 LYS A CB  
1515 C CG  . LYS A 202 ? 0.53128 0.49762 0.40502 0.02017  -0.01354 -0.13053 209 LYS A CG  
1516 C CD  . LYS A 202 ? 0.58698 0.58646 0.45231 0.01661  -0.02164 -0.12391 209 LYS A CD  
1517 C CE  . LYS A 202 ? 0.82657 0.82069 0.66441 0.01113  -0.03688 -0.14751 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 0.84746 0.87221 0.69212 0.00097  -0.05096 -0.13942 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.36380 0.28604 0.29768 0.01723  0.00029  -0.10832 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.45318 0.34810 0.39811 0.00092  -0.00707 -0.11236 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.46724 0.34187 0.42648 0.00567  -0.00006 -0.10221 210 HIS A C   
1522 O O   . HIS A 203 ? 0.48058 0.32631 0.44506 -0.00606 -0.00321 -0.10474 210 HIS A O   
1523 C CB  . HIS A 203 ? 0.47002 0.38935 0.43347 -0.01688 -0.01646 -0.10333 210 HIS A CB  
1524 C CG  . HIS A 203 ? 0.45633 0.39500 0.40672 -0.02249 -0.02642 -0.11249 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 0.44833 0.37126 0.38448 -0.03278 -0.03687 -0.13290 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.46826 0.44028 0.41635 -0.01910 -0.02852 -0.10339 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 0.57512 0.52633 0.50058 -0.03424 -0.04607 -0.13633 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.45316 0.43314 0.38494 -0.02474 -0.04027 -0.11726 210 HIS A NE2 
1529 N N   . SER A 204 ? 0.43697 0.36509 0.32735 -0.13145 -0.12080 -0.10233 211 SER A N   
1530 C CA  . SER A 204 ? 0.40170 0.32644 0.32872 -0.11508 -0.09623 -0.09806 211 SER A CA  
1531 C C   . SER A 204 ? 0.49113 0.37879 0.38205 -0.09737 -0.06963 -0.11635 211 SER A C   
1532 O O   . SER A 204 ? 0.42729 0.32442 0.34116 -0.07698 -0.04724 -0.10878 211 SER A O   
1533 C CB  . SER A 204 ? 0.40505 0.37581 0.37734 -0.09860 -0.08739 -0.07486 211 SER A CB  
1534 O OG  . SER A 204 ? 0.44298 0.45024 0.45153 -0.10955 -0.10901 -0.05751 211 SER A OG  
1535 N N   . GLN A 205 ? 0.49592 0.34310 0.33009 -0.10382 -0.07177 -0.14094 212 GLN A N   
1536 C CA  . GLN A 205 ? 0.71925 0.53604 0.51961 -0.08233 -0.04336 -0.15821 212 GLN A CA  
1537 C C   . GLN A 205 ? 0.67546 0.45724 0.49825 -0.07277 -0.02816 -0.16390 212 GLN A C   
1538 O O   . GLN A 205 ? 0.65438 0.42364 0.46961 -0.04821 -0.00157 -0.16969 212 GLN A O   
1539 C CB  . GLN A 205 ? 0.62680 0.42115 0.36840 -0.08347 -0.04637 -0.17980 212 GLN A CB  
1540 C CG  . GLN A 205 ? 0.90720 0.67156 0.64333 -0.10044 -0.06608 -0.19590 212 GLN A CG  
1541 C CD  . GLN A 205 ? 1.03206 0.82556 0.77662 -0.12546 -0.09901 -0.18558 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 0.75431 0.58689 0.53590 -0.13243 -0.11037 -0.16140 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 0.97170 0.74889 0.68434 -0.13719 -0.11415 -0.20389 212 GLN A NE2 
1544 N N   . PHE A 206 ? 0.58853 0.35722 0.44238 -0.09129 -0.04412 -0.15892 213 PHE A N   
1545 C CA  . PHE A 206 ? 0.62443 0.35509 0.49967 -0.08485 -0.03165 -0.15993 213 PHE A CA  
1546 C C   . PHE A 206 ? 0.51678 0.28633 0.45480 -0.08079 -0.02754 -0.12895 213 PHE A C   
1547 O O   . PHE A 206 ? 0.65388 0.39881 0.61753 -0.08604 -0.02609 -0.12164 213 PHE A O   
1548 C CB  . PHE A 206 ? 0.61262 0.29937 0.48003 -0.10665 -0.05006 -0.17552 213 PHE A CB  
1549 C CG  . PHE A 206 ? 0.86296 0.52430 0.68057 -0.09985 -0.04945 -0.20388 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 0.75687 0.42956 0.55299 -0.12069 -0.07319 -0.21426 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 0.85203 0.48390 0.64627 -0.07102 -0.02432 -0.21858 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 1.00800 0.65744 0.75342 -0.11510 -0.07193 -0.24159 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 0.78207 0.39449 0.53094 -0.06411 -0.02189 -0.24534 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 0.81849 0.43726 0.53950 -0.08698 -0.04550 -0.25820 213 PHE A CZ  
1555 N N   . ILE A 207 ? 0.48236 0.30933 0.44301 -0.07170 -0.02508 -0.11070 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.38098 0.24539 0.39146 -0.06387 -0.01779 -0.08525 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.42492 0.28287 0.43782 -0.03676 0.00689  -0.08182 214 ILE A C   
1558 O O   . ILE A 207 ? 0.44403 0.30727 0.43571 -0.01933 0.01934  -0.08986 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.37098 0.29183 0.40114 -0.06271 -0.02443 -0.07146 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.33364 0.26725 0.37096 -0.08745 -0.05038 -0.06948 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.36511 0.32240 0.43648 -0.05088 -0.01344 -0.05051 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.32968 0.26796 0.40664 -0.10593 -0.05981 -0.05640 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.37221 0.22263 0.41338 -0.03370 0.01357  -0.06665 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.39248 0.23271 0.43722 -0.00838 0.03372  -0.06075 215 GLY A CA  
1565 C C   . GLY A 208 ? 0.40588 0.30058 0.47050 0.00969  0.04324  -0.04369 215 GLY A C   
1566 O O   . GLY A 208 ? 0.39299 0.29287 0.47359 0.02572  0.05441  -0.02836 215 GLY A O   
1567 N N   . TYR A 209 ? 0.37411 0.30744 0.43681 0.00685  0.03734  -0.04587 216 TYR A N   
1568 C CA  . TYR A 209 ? 0.38802 0.36795 0.46567 0.02024  0.04319  -0.03470 216 TYR A CA  
1569 C C   . TYR A 209 ? 0.25141 0.24716 0.31242 0.02217  0.04211  -0.04576 216 TYR A C   
1570 O O   . TYR A 209 ? 0.37461 0.35826 0.41745 0.00947  0.03267  -0.05629 216 TYR A O   
1571 C CB  . TYR A 209 ? 0.20676 0.22044 0.30948 0.01244  0.03667  -0.02025 216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.29453 0.30047 0.41625 0.00896  0.03989  -0.00324 216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.25635 0.27386 0.38633 0.02453  0.05093  0.01272  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.26769 0.25703 0.40054 -0.01175 0.03053  -0.00016 216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.25465 0.26492 0.40120 0.02072  0.05467  0.03334  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.28277 0.26519 0.43658 -0.01808 0.03422  0.01936  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.25126 0.24276 0.41064 -0.00119 0.04740  0.03704  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.28921 0.27386 0.46860 -0.00794 0.05187  0.06134  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.29447 0.31855 0.36166 0.03594  0.05015  -0.04149 217 PRO A N   
1580 C CA  . PRO A 210 ? 0.32788 0.36700 0.38345 0.03496  0.04989  -0.04816 217 PRO A CA  
1581 C C   . PRO A 210 ? 0.35299 0.40668 0.41308 0.02192  0.03591  -0.04705 217 PRO A C   
1582 O O   . PRO A 210 ? 0.33835 0.41291 0.41798 0.02247  0.03184  -0.04016 217 PRO A O   
1583 C CB  . PRO A 210 ? 0.31802 0.38843 0.38900 0.04910  0.05864  -0.04056 217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.36832 0.44788 0.45719 0.05627  0.05907  -0.02879 217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.34978 0.39489 0.43532 0.05094  0.05805  -0.02816 217 PRO A CD  
1586 N N   . ILE A 211 ? 0.31272 0.35511 0.35285 0.01209  0.02928  -0.05342 218 ILE A N   
1587 C CA  . ILE A 211 ? 0.24941 0.30338 0.29469 0.00235  0.01547  -0.04959 218 ILE A CA  
1588 C C   . ILE A 211 ? 0.30525 0.37157 0.34477 0.00375  0.01873  -0.04749 218 ILE A C   
1589 O O   . ILE A 211 ? 0.31743 0.37571 0.33251 0.00198  0.02426  -0.05044 218 ILE A O   
1590 C CB  . ILE A 211 ? 0.28998 0.32623 0.31864 -0.01179 0.00143  -0.05296 218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.25737 0.28100 0.29695 -0.01795 -0.00293 -0.05372 218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.31050 0.36255 0.35021 -0.01798 -0.01335 -0.04440 218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.28992 0.29415 0.31113 -0.03565 -0.01953 -0.05980 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.23732 0.32218 0.29804 0.00610  0.01612  -0.04266 219 THR A N   
1595 C CA  . THR A 212 ? 0.23504 0.32964 0.29711 0.00362  0.01725  -0.03897 219 THR A CA  
1596 C C   . THR A 212 ? 0.21281 0.30146 0.27868 -0.00370 0.00376  -0.03339 219 THR A C   
1597 O O   . THR A 212 ? 0.20107 0.29198 0.28522 -0.00033 -0.00330 -0.03391 219 THR A O   
1598 C CB  . THR A 212 ? 0.25718 0.37168 0.33903 0.00951  0.02131  -0.03955 219 THR A CB  
1599 O OG1 . THR A 212 ? 0.25217 0.37501 0.33424 0.01900  0.03256  -0.04025 219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.20641 0.32990 0.29390 0.00185  0.02047  -0.03512 219 THR A CG2 
1601 N N   . LEU A 213 ? 0.22371 0.30593 0.27233 -0.01171 0.00162  -0.02639 220 LEU A N   
1602 C CA  . LEU A 213 ? 0.27440 0.34939 0.32754 -0.01757 -0.01162 -0.01580 220 LEU A CA  
1603 C C   . LEU A 213 ? 0.32373 0.40051 0.39207 -0.02094 -0.00978 -0.01052 220 LEU A C   
1604 O O   . LEU A 213 ? 0.24437 0.32765 0.30396 -0.02779 -0.00145 -0.00404 220 LEU A O   
1605 C CB  . LEU A 213 ? 0.26048 0.32780 0.28285 -0.02607 -0.01714 -0.00729 220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.33812 0.39889 0.36315 -0.03168 -0.03167 0.01033  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.22851 0.28805 0.28436 -0.02442 -0.04519 0.01165  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.31444 0.37230 0.30078 -0.04047 -0.03840 0.01921  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.27616 0.34735 0.36782 -0.01662 -0.01677 -0.01403 221 PHE A N   
1610 C CA  . PHE A 214 ? 0.28372 0.34767 0.38979 -0.02271 -0.01886 -0.01213 221 PHE A CA  
1611 C C   . PHE A 214 ? 0.29998 0.34778 0.40187 -0.03292 -0.02571 0.00709  221 PHE A C   
1612 O O   . PHE A 214 ? 0.25663 0.29666 0.35012 -0.03084 -0.03385 0.01752  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.22825 0.28218 0.35342 -0.01348 -0.02451 -0.02488 221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.26975 0.34174 0.39691 -0.00636 -0.01783 -0.04104 221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.17480 0.26662 0.29250 -0.00241 -0.00919 -0.04172 221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.21201 0.27796 0.34766 -0.00319 -0.02096 -0.05547 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.19176 0.30075 0.31129 0.00481  -0.00403 -0.05122 221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.25018 0.33616 0.38203 0.00311  -0.01629 -0.06799 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.24405 0.35345 0.36927 0.00730  -0.00794 -0.06322 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.21108 0.25643 0.32062 -0.04558 -0.02376 0.01460  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.28728 0.31466 0.39678 -0.05724 -0.02990 0.03710  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.28619 0.28315 0.42199 -0.06004 -0.04023 0.03396  222 VAL A C   
1623 O O   . VAL A 215 ? 0.34118 0.33636 0.48988 -0.05639 -0.04086 0.01260  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.45904 0.50630 0.55801 -0.07264 -0.01797 0.05331  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.62011 0.68974 0.68709 -0.06641 -0.00605 0.05168  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.23279 0.29695 0.35457 -0.08144 -0.01201 0.04514  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.30059 0.27028 0.44141 -0.06614 -0.04901 0.05533  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.44876 0.37723 0.61383 -0.06731 -0.05943 0.05272  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.57985 0.49336 0.75515 -0.09230 -0.06089 0.07372  223 GLU A C   
1630 O O   . GLU A 216 ? 0.56113 0.49784 0.72379 -0.10586 -0.05330 0.09722  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.44138 0.34256 0.61367 -0.04973 -0.07020 0.06214  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.49173 0.41996 0.65378 -0.03136 -0.06956 0.05649  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.75350 0.66575 0.92847 -0.01584 -0.08205 0.07352  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.53382 0.40971 0.73328 -0.00538 -0.08747 0.07177  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.55650 0.49215 0.71773 -0.01358 -0.08737 0.08811  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.58505 0.45855 0.78276 -0.09885 -0.06997 0.06441  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.70945 0.56227 0.92437 -0.12678 -0.07403 0.08329  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.73702 0.57219 0.94924 -0.13317 -0.07664 0.12497  224 LYS A C   
1639 O O   . LYS A 217 ? 0.76370 0.58233 0.96892 -0.11357 -0.08254 0.13464  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.72908 0.53030 0.96460 -0.13092 -0.08630 0.06000  224 LYS A CB  
1641 C CG  . LYS A 217 ? 1.03667 0.81121 1.27983 -0.15179 -0.08924 0.07754  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.84307 0.57942 1.09103 -0.15572 -0.09714 0.04534  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.96336 0.64621 1.21975 -0.16513 -0.10289 0.06062  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.97645 0.64590 1.23359 -0.15366 -0.10226 0.09693  224 LYS A NZ  
# 
