data_9BXL
# 
_entry.id   9BXL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9BXL         pdb_00009bxl 10.2210/pdb9bxl/pdb 
WWPDB D_1000281066 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-01-08 
2 'Structure model' 1 1 2025-02-05 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_DOI'    
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_citation.year'                    
5 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BXL 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              katherine.davis@emory.edu 
_pdbx_contact_author.name_first         Katherine 
_pdbx_contact_author.name_last          Davis 
_pdbx_contact_author.name_mi            M 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0258-8907 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ireland, K.A.' 1 0000-0003-0986-5142 
'Davis, K.M.'   2 0000-0002-0258-8907 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structural and functional analysis of SAM-dependent N-methyltransferases involved in ovoselenol and ovothiol biosynthesis.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2024.12.020 
_citation.pdbx_database_id_PubMed   39862859 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ireland, K.A.'        1 ? 
primary 'Kayrouz, C.M.'        2 ? 
primary 'Abbott, M.L.'         3 ? 
primary 'Seyedsayamdost, M.R.' 4 ? 
primary 'Davis, K.M.'          5 ? 
# 
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 '5-thiohistidine N-methyltransferase OvoM' 31352.225 2   ? ? ? ? 
2 non-polymer syn S-ADENOSYLMETHIONINE                       398.437   2   ? ? ? ? 
3 non-polymer syn 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL   122.143   2   ? ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                             62.068    3   ? ? ? ? 
5 water       nat water                                      18.015    290 ? ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMIFKEKNIYETDESVSQYCDFQYGEDCFGVLNFALACATKAIGYTKETPKNRALDLGCAT
GRASFELARSYKHVDGVDYSQAFVDAATELQKNGCIGYSQNGEGELKNYKVIDREGYAFRDSFTKVEFFQGDACNLTPQF
KEYDLIMATNLIDRLYEPRLFLENIHKRINEKGYLILTSPYTWREEYTAKKFWIGGYVDENGKEVSTLEGLKEILEIHFE
LVATEDIPFVIRETSRKFQHTISQMSVWKVIST
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMIFKEKNIYETDESVSQYCDFQYGEDCFGVLNFALACATKAIGYTKETPKNRALDLGCAT
GRASFELARSYKHVDGVDYSQAFVDAATELQKNGCIGYSQNGEGELKNYKVIDREGYAFRDSFTKVEFFQGDACNLTPQF
KEYDLIMATNLIDRLYEPRLFLENIHKRINEKGYLILTSPYTWREEYTAKKFWIGGYVDENGKEVSTLEGLKEILEIHFE
LVATEDIPFVIRETSRKFQHTISQMSVWKVIST
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 S-ADENOSYLMETHIONINE                     SAM 
3 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL TRS 
4 1,2-ETHANEDIOL                           EDO 
5 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   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  ILE n 
1 23  PHE n 
1 24  LYS n 
1 25  GLU n 
1 26  LYS n 
1 27  ASN n 
1 28  ILE n 
1 29  TYR n 
1 30  GLU n 
1 31  THR n 
1 32  ASP n 
1 33  GLU n 
1 34  SER n 
1 35  VAL n 
1 36  SER n 
1 37  GLN n 
1 38  TYR n 
1 39  CYS n 
1 40  ASP n 
1 41  PHE n 
1 42  GLN n 
1 43  TYR n 
1 44  GLY n 
1 45  GLU n 
1 46  ASP n 
1 47  CYS n 
1 48  PHE n 
1 49  GLY n 
1 50  VAL n 
1 51  LEU n 
1 52  ASN n 
1 53  PHE n 
1 54  ALA n 
1 55  LEU n 
1 56  ALA n 
1 57  CYS n 
1 58  ALA n 
1 59  THR n 
1 60  LYS n 
1 61  ALA n 
1 62  ILE n 
1 63  GLY n 
1 64  TYR n 
1 65  THR n 
1 66  LYS n 
1 67  GLU n 
1 68  THR n 
1 69  PRO n 
1 70  LYS n 
1 71  ASN n 
1 72  ARG n 
1 73  ALA n 
1 74  LEU n 
1 75  ASP n 
1 76  LEU n 
1 77  GLY n 
1 78  CYS n 
1 79  ALA n 
1 80  THR n 
1 81  GLY n 
1 82  ARG n 
1 83  ALA n 
1 84  SER n 
1 85  PHE n 
1 86  GLU n 
1 87  LEU n 
1 88  ALA n 
1 89  ARG n 
1 90  SER n 
1 91  TYR n 
1 92  LYS n 
1 93  HIS n 
1 94  VAL n 
1 95  ASP n 
1 96  GLY n 
1 97  VAL n 
1 98  ASP n 
1 99  TYR n 
1 100 SER n 
1 101 GLN n 
1 102 ALA n 
1 103 PHE n 
1 104 VAL n 
1 105 ASP n 
1 106 ALA n 
1 107 ALA n 
1 108 THR n 
1 109 GLU n 
1 110 LEU n 
1 111 GLN n 
1 112 LYS n 
1 113 ASN n 
1 114 GLY n 
1 115 CYS n 
1 116 ILE n 
1 117 GLY n 
1 118 TYR n 
1 119 SER n 
1 120 GLN n 
1 121 ASN n 
1 122 GLY n 
1 123 GLU n 
1 124 GLY n 
1 125 GLU n 
1 126 LEU n 
1 127 LYS n 
1 128 ASN n 
1 129 TYR n 
1 130 LYS n 
1 131 VAL n 
1 132 ILE n 
1 133 ASP n 
1 134 ARG n 
1 135 GLU n 
1 136 GLY n 
1 137 TYR n 
1 138 ALA n 
1 139 PHE n 
1 140 ARG n 
1 141 ASP n 
1 142 SER n 
1 143 PHE n 
1 144 THR n 
1 145 LYS n 
1 146 VAL n 
1 147 GLU n 
1 148 PHE n 
1 149 PHE n 
1 150 GLN n 
1 151 GLY n 
1 152 ASP n 
1 153 ALA n 
1 154 CYS n 
1 155 ASN n 
1 156 LEU n 
1 157 THR n 
1 158 PRO n 
1 159 GLN n 
1 160 PHE n 
1 161 LYS n 
1 162 GLU n 
1 163 TYR n 
1 164 ASP n 
1 165 LEU n 
1 166 ILE n 
1 167 MET n 
1 168 ALA n 
1 169 THR n 
1 170 ASN n 
1 171 LEU n 
1 172 ILE n 
1 173 ASP n 
1 174 ARG n 
1 175 LEU n 
1 176 TYR n 
1 177 GLU n 
1 178 PRO n 
1 179 ARG n 
1 180 LEU n 
1 181 PHE n 
1 182 LEU n 
1 183 GLU n 
1 184 ASN n 
1 185 ILE n 
1 186 HIS n 
1 187 LYS n 
1 188 ARG n 
1 189 ILE n 
1 190 ASN n 
1 191 GLU n 
1 192 LYS n 
1 193 GLY n 
1 194 TYR n 
1 195 LEU n 
1 196 ILE n 
1 197 LEU n 
1 198 THR n 
1 199 SER n 
1 200 PRO n 
1 201 TYR n 
1 202 THR n 
1 203 TRP n 
1 204 ARG n 
1 205 GLU n 
1 206 GLU n 
1 207 TYR n 
1 208 THR n 
1 209 ALA n 
1 210 LYS n 
1 211 LYS n 
1 212 PHE n 
1 213 TRP n 
1 214 ILE n 
1 215 GLY n 
1 216 GLY n 
1 217 TYR n 
1 218 VAL n 
1 219 ASP n 
1 220 GLU n 
1 221 ASN n 
1 222 GLY n 
1 223 LYS n 
1 224 GLU n 
1 225 VAL n 
1 226 SER n 
1 227 THR n 
1 228 LEU n 
1 229 GLU n 
1 230 GLY n 
1 231 LEU n 
1 232 LYS n 
1 233 GLU n 
1 234 ILE n 
1 235 LEU n 
1 236 GLU n 
1 237 ILE n 
1 238 HIS n 
1 239 PHE n 
1 240 GLU n 
1 241 LEU n 
1 242 VAL n 
1 243 ALA n 
1 244 THR n 
1 245 GLU n 
1 246 ASP n 
1 247 ILE n 
1 248 PRO n 
1 249 PHE n 
1 250 VAL n 
1 251 ILE n 
1 252 ARG n 
1 253 GLU n 
1 254 THR n 
1 255 SER n 
1 256 ARG n 
1 257 LYS n 
1 258 PHE n 
1 259 GLN n 
1 260 HIS n 
1 261 THR n 
1 262 ILE n 
1 263 SER n 
1 264 GLN n 
1 265 MET n 
1 266 SER n 
1 267 VAL n 
1 268 TRP n 
1 269 LYS n 
1 270 VAL n 
1 271 ILE n 
1 272 SER n 
1 273 THR 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                   273 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    STB_99 
_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      'Sulfuricurvum sp.' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2025608 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                  ?                 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                 ?                 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                               ?                 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                          ?                 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                                 ?                 'C3 H7 N O2 S'    121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                           'ETHYLENE GLYCOL' 'C2 H6 O2'        62.068  
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 
SAM non-polymer         . S-ADENOSYLMETHIONINE                     ?                 'C15 H22 N6 O5 S' 398.437 
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 
TRS non-polymer         . 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL 'TRIS BUFFER'     'C4 H12 N O3 1'   122.143 
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   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  LEU 14  -6  ?   ?   ?   A . n 
A 1 15  VAL 15  -5  ?   ?   ?   A . n 
A 1 16  PRO 16  -4  ?   ?   ?   A . n 
A 1 17  ARG 17  -3  ?   ?   ?   A . n 
A 1 18  GLY 18  -2  ?   ?   ?   A . n 
A 1 19  SER 19  -1  ?   ?   ?   A . n 
A 1 20  HIS 20  0   ?   ?   ?   A . n 
A 1 21  MET 21  1   ?   ?   ?   A . n 
A 1 22  ILE 22  2   ?   ?   ?   A . n 
A 1 23  PHE 23  3   ?   ?   ?   A . n 
A 1 24  LYS 24  4   ?   ?   ?   A . n 
A 1 25  GLU 25  5   ?   ?   ?   A . n 
A 1 26  LYS 26  6   ?   ?   ?   A . n 
A 1 27  ASN 27  7   7   ASN ASN A . n 
A 1 28  ILE 28  8   8   ILE ILE A . n 
A 1 29  TYR 29  9   9   TYR TYR A . n 
A 1 30  GLU 30  10  10  GLU GLU A . n 
A 1 31  THR 31  11  11  THR THR A . n 
A 1 32  ASP 32  12  12  ASP ASP A . n 
A 1 33  GLU 33  13  13  GLU GLU A . n 
A 1 34  SER 34  14  14  SER SER A . n 
A 1 35  VAL 35  15  15  VAL VAL A . n 
A 1 36  SER 36  16  16  SER SER A . n 
A 1 37  GLN 37  17  17  GLN GLN A . n 
A 1 38  TYR 38  18  18  TYR TYR A . n 
A 1 39  CYS 39  19  19  CYS CYS A . n 
A 1 40  ASP 40  20  20  ASP ASP A . n 
A 1 41  PHE 41  21  21  PHE PHE A . n 
A 1 42  GLN 42  22  22  GLN GLN A . n 
A 1 43  TYR 43  23  23  TYR TYR A . n 
A 1 44  GLY 44  24  24  GLY GLY A . n 
A 1 45  GLU 45  25  25  GLU GLU A . n 
A 1 46  ASP 46  26  26  ASP ASP A . n 
A 1 47  CYS 47  27  27  CYS CYS A . n 
A 1 48  PHE 48  28  28  PHE PHE A . n 
A 1 49  GLY 49  29  29  GLY GLY A . n 
A 1 50  VAL 50  30  30  VAL VAL A . n 
A 1 51  LEU 51  31  31  LEU LEU A . n 
A 1 52  ASN 52  32  32  ASN ASN A . n 
A 1 53  PHE 53  33  33  PHE PHE A . n 
A 1 54  ALA 54  34  34  ALA ALA A . n 
A 1 55  LEU 55  35  35  LEU LEU A . n 
A 1 56  ALA 56  36  36  ALA ALA A . n 
A 1 57  CYS 57  37  37  CYS CYS A . n 
A 1 58  ALA 58  38  38  ALA ALA A . n 
A 1 59  THR 59  39  39  THR THR A . n 
A 1 60  LYS 60  40  40  LYS LYS A . n 
A 1 61  ALA 61  41  41  ALA ALA A . n 
A 1 62  ILE 62  42  42  ILE ILE A . n 
A 1 63  GLY 63  43  43  GLY GLY A . n 
A 1 64  TYR 64  44  44  TYR TYR A . n 
A 1 65  THR 65  45  45  THR THR A . n 
A 1 66  LYS 66  46  46  LYS LYS A . n 
A 1 67  GLU 67  47  47  GLU GLU A . n 
A 1 68  THR 68  48  48  THR THR A . n 
A 1 69  PRO 69  49  49  PRO PRO A . n 
A 1 70  LYS 70  50  50  LYS LYS A . n 
A 1 71  ASN 71  51  51  ASN ASN A . n 
A 1 72  ARG 72  52  52  ARG ARG A . n 
A 1 73  ALA 73  53  53  ALA ALA A . n 
A 1 74  LEU 74  54  54  LEU LEU A . n 
A 1 75  ASP 75  55  55  ASP ASP A . n 
A 1 76  LEU 76  56  56  LEU LEU A . n 
A 1 77  GLY 77  57  57  GLY GLY A . n 
A 1 78  CYS 78  58  58  CYS CYS A . n 
A 1 79  ALA 79  59  59  ALA ALA A . n 
A 1 80  THR 80  60  60  THR THR A . n 
A 1 81  GLY 81  61  61  GLY GLY A . n 
A 1 82  ARG 82  62  62  ARG ARG A . n 
A 1 83  ALA 83  63  63  ALA ALA A . n 
A 1 84  SER 84  64  64  SER SER A . n 
A 1 85  PHE 85  65  65  PHE PHE A . n 
A 1 86  GLU 86  66  66  GLU GLU A . n 
A 1 87  LEU 87  67  67  LEU LEU A . n 
A 1 88  ALA 88  68  68  ALA ALA A . n 
A 1 89  ARG 89  69  69  ARG ARG A . n 
A 1 90  SER 90  70  70  SER SER A . n 
A 1 91  TYR 91  71  71  TYR TYR A . n 
A 1 92  LYS 92  72  72  LYS LYS A . n 
A 1 93  HIS 93  73  73  HIS HIS A . n 
A 1 94  VAL 94  74  74  VAL VAL A . n 
A 1 95  ASP 95  75  75  ASP ASP A . n 
A 1 96  GLY 96  76  76  GLY GLY A . n 
A 1 97  VAL 97  77  77  VAL VAL A . n 
A 1 98  ASP 98  78  78  ASP ASP A . n 
A 1 99  TYR 99  79  79  TYR TYR A . n 
A 1 100 SER 100 80  80  SER SER A . n 
A 1 101 GLN 101 81  81  GLN GLN A . n 
A 1 102 ALA 102 82  82  ALA ALA A . n 
A 1 103 PHE 103 83  83  PHE PHE A . n 
A 1 104 VAL 104 84  84  VAL VAL A . n 
A 1 105 ASP 105 85  85  ASP ASP A . n 
A 1 106 ALA 106 86  86  ALA ALA A . n 
A 1 107 ALA 107 87  87  ALA ALA A . n 
A 1 108 THR 108 88  88  THR THR A . n 
A 1 109 GLU 109 89  89  GLU GLU A . n 
A 1 110 LEU 110 90  90  LEU LEU A . n 
A 1 111 GLN 111 91  91  GLN GLN A . n 
A 1 112 LYS 112 92  92  LYS LYS A . n 
A 1 113 ASN 113 93  93  ASN ASN A . n 
A 1 114 GLY 114 94  94  GLY GLY A . n 
A 1 115 CYS 115 95  95  CYS CYS A . n 
A 1 116 ILE 116 96  96  ILE ILE A . n 
A 1 117 GLY 117 97  97  GLY GLY A . n 
A 1 118 TYR 118 98  98  TYR TYR A . n 
A 1 119 SER 119 99  99  SER SER A . n 
A 1 120 GLN 120 100 100 GLN GLN A . n 
A 1 121 ASN 121 101 101 ASN ASN A . n 
A 1 122 GLY 122 102 102 GLY GLY A . n 
A 1 123 GLU 123 103 103 GLU GLU A . n 
A 1 124 GLY 124 104 104 GLY GLY A . n 
A 1 125 GLU 125 105 105 GLU GLU A . n 
A 1 126 LEU 126 106 106 LEU LEU A . n 
A 1 127 LYS 127 107 107 LYS LYS A . n 
A 1 128 ASN 128 108 108 ASN ASN A . n 
A 1 129 TYR 129 109 109 TYR TYR A . n 
A 1 130 LYS 130 110 110 LYS LYS A . n 
A 1 131 VAL 131 111 111 VAL VAL A . n 
A 1 132 ILE 132 112 112 ILE ILE A . n 
A 1 133 ASP 133 113 113 ASP ASP A . n 
A 1 134 ARG 134 114 114 ARG ARG A . n 
A 1 135 GLU 135 115 115 GLU GLU A . n 
A 1 136 GLY 136 116 116 GLY GLY A . n 
A 1 137 TYR 137 117 117 TYR TYR A . n 
A 1 138 ALA 138 118 118 ALA ALA A . n 
A 1 139 PHE 139 119 119 PHE PHE A . n 
A 1 140 ARG 140 120 120 ARG ARG A . n 
A 1 141 ASP 141 121 121 ASP ASP A . n 
A 1 142 SER 142 122 122 SER SER A . n 
A 1 143 PHE 143 123 123 PHE PHE A . n 
A 1 144 THR 144 124 124 THR THR A . n 
A 1 145 LYS 145 125 125 LYS LYS A . n 
A 1 146 VAL 146 126 126 VAL VAL A . n 
A 1 147 GLU 147 127 127 GLU GLU A . n 
A 1 148 PHE 148 128 128 PHE PHE A . n 
A 1 149 PHE 149 129 129 PHE PHE A . n 
A 1 150 GLN 150 130 130 GLN GLN A . n 
A 1 151 GLY 151 131 131 GLY GLY A . n 
A 1 152 ASP 152 132 132 ASP ASP A . n 
A 1 153 ALA 153 133 133 ALA ALA A . n 
A 1 154 CYS 154 134 134 CYS CYS A . n 
A 1 155 ASN 155 135 135 ASN ASN A . n 
A 1 156 LEU 156 136 136 LEU LEU A . n 
A 1 157 THR 157 137 137 THR THR A . n 
A 1 158 PRO 158 138 138 PRO PRO A . n 
A 1 159 GLN 159 139 139 GLN GLN A . n 
A 1 160 PHE 160 140 140 PHE PHE A . n 
A 1 161 LYS 161 141 141 LYS LYS A . n 
A 1 162 GLU 162 142 142 GLU GLU A . n 
A 1 163 TYR 163 143 143 TYR TYR A . n 
A 1 164 ASP 164 144 144 ASP ASP A . n 
A 1 165 LEU 165 145 145 LEU LEU A . n 
A 1 166 ILE 166 146 146 ILE ILE A . n 
A 1 167 MET 167 147 147 MET MET A . n 
A 1 168 ALA 168 148 148 ALA ALA A . n 
A 1 169 THR 169 149 149 THR THR A . n 
A 1 170 ASN 170 150 150 ASN ASN A . n 
A 1 171 LEU 171 151 151 LEU LEU A . n 
A 1 172 ILE 172 152 152 ILE ILE A . n 
A 1 173 ASP 173 153 153 ASP ASP A . n 
A 1 174 ARG 174 154 154 ARG ARG A . n 
A 1 175 LEU 175 155 155 LEU LEU A . n 
A 1 176 TYR 176 156 156 TYR TYR A . n 
A 1 177 GLU 177 157 157 GLU GLU A . n 
A 1 178 PRO 178 158 158 PRO PRO A . n 
A 1 179 ARG 179 159 159 ARG ARG A . n 
A 1 180 LEU 180 160 160 LEU LEU A . n 
A 1 181 PHE 181 161 161 PHE PHE A . n 
A 1 182 LEU 182 162 162 LEU LEU A . n 
A 1 183 GLU 183 163 163 GLU GLU A . n 
A 1 184 ASN 184 164 164 ASN ASN A . n 
A 1 185 ILE 185 165 165 ILE ILE A . n 
A 1 186 HIS 186 166 166 HIS HIS A . n 
A 1 187 LYS 187 167 167 LYS LYS A . n 
A 1 188 ARG 188 168 168 ARG ARG A . n 
A 1 189 ILE 189 169 169 ILE ILE A . n 
A 1 190 ASN 190 170 170 ASN ASN A . n 
A 1 191 GLU 191 171 171 GLU GLU A . n 
A 1 192 LYS 192 172 172 LYS LYS A . n 
A 1 193 GLY 193 173 173 GLY GLY A . n 
A 1 194 TYR 194 174 174 TYR TYR A . n 
A 1 195 LEU 195 175 175 LEU LEU A . n 
A 1 196 ILE 196 176 176 ILE ILE A . n 
A 1 197 LEU 197 177 177 LEU LEU A . n 
A 1 198 THR 198 178 178 THR THR A . n 
A 1 199 SER 199 179 179 SER SER A . n 
A 1 200 PRO 200 180 180 PRO PRO A . n 
A 1 201 TYR 201 181 181 TYR TYR A . n 
A 1 202 THR 202 182 182 THR THR A . n 
A 1 203 TRP 203 183 183 TRP TRP A . n 
A 1 204 ARG 204 184 184 ARG ARG A . n 
A 1 205 GLU 205 185 185 GLU GLU A . n 
A 1 206 GLU 206 186 186 GLU GLU A . n 
A 1 207 TYR 207 187 187 TYR TYR A . n 
A 1 208 THR 208 188 188 THR THR A . n 
A 1 209 ALA 209 189 189 ALA ALA A . n 
A 1 210 LYS 210 190 190 LYS LYS A . n 
A 1 211 LYS 211 191 191 LYS LYS A . n 
A 1 212 PHE 212 192 192 PHE PHE A . n 
A 1 213 TRP 213 193 193 TRP TRP A . n 
A 1 214 ILE 214 194 194 ILE ILE A . n 
A 1 215 GLY 215 195 195 GLY GLY A . n 
A 1 216 GLY 216 196 196 GLY GLY A . n 
A 1 217 TYR 217 197 197 TYR TYR A . n 
A 1 218 VAL 218 198 198 VAL VAL A . n 
A 1 219 ASP 219 199 199 ASP ASP A . n 
A 1 220 GLU 220 200 200 GLU GLU A . n 
A 1 221 ASN 221 201 201 ASN ASN A . n 
A 1 222 GLY 222 202 202 GLY GLY A . n 
A 1 223 LYS 223 203 203 LYS LYS A . n 
A 1 224 GLU 224 204 204 GLU GLU A . n 
A 1 225 VAL 225 205 205 VAL VAL A . n 
A 1 226 SER 226 206 206 SER SER A . n 
A 1 227 THR 227 207 207 THR THR A . n 
A 1 228 LEU 228 208 208 LEU LEU A . n 
A 1 229 GLU 229 209 209 GLU GLU A . n 
A 1 230 GLY 230 210 210 GLY GLY A . n 
A 1 231 LEU 231 211 211 LEU LEU A . n 
A 1 232 LYS 232 212 212 LYS LYS A . n 
A 1 233 GLU 233 213 213 GLU GLU A . n 
A 1 234 ILE 234 214 214 ILE ILE A . n 
A 1 235 LEU 235 215 215 LEU LEU A . n 
A 1 236 GLU 236 216 216 GLU GLU A . n 
A 1 237 ILE 237 217 217 ILE ILE A . n 
A 1 238 HIS 238 218 218 HIS HIS A . n 
A 1 239 PHE 239 219 219 PHE PHE A . n 
A 1 240 GLU 240 220 220 GLU GLU A . n 
A 1 241 LEU 241 221 221 LEU LEU A . n 
A 1 242 VAL 242 222 222 VAL VAL A . n 
A 1 243 ALA 243 223 223 ALA ALA A . n 
A 1 244 THR 244 224 224 THR THR A . n 
A 1 245 GLU 245 225 225 GLU GLU A . n 
A 1 246 ASP 246 226 226 ASP ASP A . n 
A 1 247 ILE 247 227 227 ILE ILE A . n 
A 1 248 PRO 248 228 228 PRO PRO A . n 
A 1 249 PHE 249 229 229 PHE PHE A . n 
A 1 250 VAL 250 230 230 VAL VAL A . n 
A 1 251 ILE 251 231 231 ILE ILE A . n 
A 1 252 ARG 252 232 232 ARG ARG A . n 
A 1 253 GLU 253 233 233 GLU GLU A . n 
A 1 254 THR 254 234 234 THR THR A . n 
A 1 255 SER 255 235 235 SER SER A . n 
A 1 256 ARG 256 236 236 ARG ARG A . n 
A 1 257 LYS 257 237 237 LYS LYS A . n 
A 1 258 PHE 258 238 238 PHE PHE A . n 
A 1 259 GLN 259 239 239 GLN GLN A . n 
A 1 260 HIS 260 240 240 HIS HIS A . n 
A 1 261 THR 261 241 241 THR THR A . n 
A 1 262 ILE 262 242 242 ILE ILE A . n 
A 1 263 SER 263 243 243 SER SER A . n 
A 1 264 GLN 264 244 244 GLN GLN A . n 
A 1 265 MET 265 245 245 MET MET A . n 
A 1 266 SER 266 246 246 SER SER A . n 
A 1 267 VAL 267 247 247 VAL VAL A . n 
A 1 268 TRP 268 248 248 TRP TRP A . n 
A 1 269 LYS 269 249 249 LYS LYS A . n 
A 1 270 VAL 270 250 250 VAL VAL A . n 
A 1 271 ILE 271 251 251 ILE ILE A . n 
A 1 272 SER 272 252 ?   ?   ?   A . n 
A 1 273 THR 273 253 ?   ?   ?   A . n 
B 1 1   MET 1   -19 ?   ?   ?   B . n 
B 1 2   GLY 2   -18 ?   ?   ?   B . n 
B 1 3   SER 3   -17 ?   ?   ?   B . n 
B 1 4   SER 4   -16 ?   ?   ?   B . n 
B 1 5   HIS 5   -15 ?   ?   ?   B . n 
B 1 6   HIS 6   -14 ?   ?   ?   B . n 
B 1 7   HIS 7   -13 ?   ?   ?   B . n 
B 1 8   HIS 8   -12 ?   ?   ?   B . n 
B 1 9   HIS 9   -11 ?   ?   ?   B . n 
B 1 10  HIS 10  -10 ?   ?   ?   B . n 
B 1 11  SER 11  -9  ?   ?   ?   B . n 
B 1 12  SER 12  -8  ?   ?   ?   B . n 
B 1 13  GLY 13  -7  ?   ?   ?   B . n 
B 1 14  LEU 14  -6  ?   ?   ?   B . n 
B 1 15  VAL 15  -5  ?   ?   ?   B . n 
B 1 16  PRO 16  -4  ?   ?   ?   B . n 
B 1 17  ARG 17  -3  ?   ?   ?   B . n 
B 1 18  GLY 18  -2  ?   ?   ?   B . n 
B 1 19  SER 19  -1  ?   ?   ?   B . n 
B 1 20  HIS 20  0   ?   ?   ?   B . n 
B 1 21  MET 21  1   ?   ?   ?   B . n 
B 1 22  ILE 22  2   ?   ?   ?   B . n 
B 1 23  PHE 23  3   ?   ?   ?   B . n 
B 1 24  LYS 24  4   ?   ?   ?   B . n 
B 1 25  GLU 25  5   ?   ?   ?   B . n 
B 1 26  LYS 26  6   ?   ?   ?   B . n 
B 1 27  ASN 27  7   ?   ?   ?   B . n 
B 1 28  ILE 28  8   8   ILE ILE B . n 
B 1 29  TYR 29  9   9   TYR TYR B . n 
B 1 30  GLU 30  10  10  GLU GLU B . n 
B 1 31  THR 31  11  11  THR THR B . n 
B 1 32  ASP 32  12  12  ASP ASP B . n 
B 1 33  GLU 33  13  13  GLU GLU B . n 
B 1 34  SER 34  14  14  SER SER B . n 
B 1 35  VAL 35  15  15  VAL VAL B . n 
B 1 36  SER 36  16  16  SER SER B . n 
B 1 37  GLN 37  17  17  GLN GLN B . n 
B 1 38  TYR 38  18  18  TYR TYR B . n 
B 1 39  CYS 39  19  19  CYS CYS B . n 
B 1 40  ASP 40  20  20  ASP ASP B . n 
B 1 41  PHE 41  21  21  PHE PHE B . n 
B 1 42  GLN 42  22  22  GLN GLN B . n 
B 1 43  TYR 43  23  23  TYR TYR B . n 
B 1 44  GLY 44  24  24  GLY GLY B . n 
B 1 45  GLU 45  25  25  GLU GLU B . n 
B 1 46  ASP 46  26  26  ASP ASP B . n 
B 1 47  CYS 47  27  27  CYS CYS B . n 
B 1 48  PHE 48  28  28  PHE PHE B . n 
B 1 49  GLY 49  29  29  GLY GLY B . n 
B 1 50  VAL 50  30  30  VAL VAL B . n 
B 1 51  LEU 51  31  31  LEU LEU B . n 
B 1 52  ASN 52  32  32  ASN ASN B . n 
B 1 53  PHE 53  33  33  PHE PHE B . n 
B 1 54  ALA 54  34  34  ALA ALA B . n 
B 1 55  LEU 55  35  35  LEU LEU B . n 
B 1 56  ALA 56  36  36  ALA ALA B . n 
B 1 57  CYS 57  37  37  CYS CYS B . n 
B 1 58  ALA 58  38  38  ALA ALA B . n 
B 1 59  THR 59  39  39  THR THR B . n 
B 1 60  LYS 60  40  40  LYS LYS B . n 
B 1 61  ALA 61  41  41  ALA ALA B . n 
B 1 62  ILE 62  42  42  ILE ILE B . n 
B 1 63  GLY 63  43  43  GLY GLY B . n 
B 1 64  TYR 64  44  44  TYR TYR B . n 
B 1 65  THR 65  45  45  THR THR B . n 
B 1 66  LYS 66  46  46  LYS LYS B . n 
B 1 67  GLU 67  47  47  GLU GLU B . n 
B 1 68  THR 68  48  48  THR THR B . n 
B 1 69  PRO 69  49  49  PRO PRO B . n 
B 1 70  LYS 70  50  50  LYS LYS B . n 
B 1 71  ASN 71  51  51  ASN ASN B . n 
B 1 72  ARG 72  52  52  ARG ARG B . n 
B 1 73  ALA 73  53  53  ALA ALA B . n 
B 1 74  LEU 74  54  54  LEU LEU B . n 
B 1 75  ASP 75  55  55  ASP ASP B . n 
B 1 76  LEU 76  56  56  LEU LEU B . n 
B 1 77  GLY 77  57  57  GLY GLY B . n 
B 1 78  CYS 78  58  58  CYS CYS B . n 
B 1 79  ALA 79  59  59  ALA ALA B . n 
B 1 80  THR 80  60  60  THR THR B . n 
B 1 81  GLY 81  61  61  GLY GLY B . n 
B 1 82  ARG 82  62  62  ARG ARG B . n 
B 1 83  ALA 83  63  63  ALA ALA B . n 
B 1 84  SER 84  64  64  SER SER B . n 
B 1 85  PHE 85  65  65  PHE PHE B . n 
B 1 86  GLU 86  66  66  GLU GLU B . n 
B 1 87  LEU 87  67  67  LEU LEU B . n 
B 1 88  ALA 88  68  68  ALA ALA B . n 
B 1 89  ARG 89  69  69  ARG ARG B . n 
B 1 90  SER 90  70  70  SER SER B . n 
B 1 91  TYR 91  71  71  TYR TYR B . n 
B 1 92  LYS 92  72  72  LYS LYS B . n 
B 1 93  HIS 93  73  73  HIS HIS B . n 
B 1 94  VAL 94  74  74  VAL VAL B . n 
B 1 95  ASP 95  75  75  ASP ASP B . n 
B 1 96  GLY 96  76  76  GLY GLY B . n 
B 1 97  VAL 97  77  77  VAL VAL B . n 
B 1 98  ASP 98  78  78  ASP ASP B . n 
B 1 99  TYR 99  79  79  TYR TYR B . n 
B 1 100 SER 100 80  80  SER SER B . n 
B 1 101 GLN 101 81  81  GLN GLN B . n 
B 1 102 ALA 102 82  82  ALA ALA B . n 
B 1 103 PHE 103 83  83  PHE PHE B . n 
B 1 104 VAL 104 84  84  VAL VAL B . n 
B 1 105 ASP 105 85  85  ASP ASP B . n 
B 1 106 ALA 106 86  86  ALA ALA B . n 
B 1 107 ALA 107 87  87  ALA ALA B . n 
B 1 108 THR 108 88  88  THR THR B . n 
B 1 109 GLU 109 89  89  GLU GLU B . n 
B 1 110 LEU 110 90  90  LEU LEU B . n 
B 1 111 GLN 111 91  91  GLN GLN B . n 
B 1 112 LYS 112 92  92  LYS LYS B . n 
B 1 113 ASN 113 93  93  ASN ASN B . n 
B 1 114 GLY 114 94  94  GLY GLY B . n 
B 1 115 CYS 115 95  95  CYS CYS B . n 
B 1 116 ILE 116 96  96  ILE ILE B . n 
B 1 117 GLY 117 97  97  GLY GLY B . n 
B 1 118 TYR 118 98  98  TYR TYR B . n 
B 1 119 SER 119 99  99  SER SER B . n 
B 1 120 GLN 120 100 100 GLN GLN B . n 
B 1 121 ASN 121 101 101 ASN ASN B . n 
B 1 122 GLY 122 102 102 GLY GLY B . n 
B 1 123 GLU 123 103 103 GLU GLU B . n 
B 1 124 GLY 124 104 104 GLY GLY B . n 
B 1 125 GLU 125 105 105 GLU GLU B . n 
B 1 126 LEU 126 106 106 LEU LEU B . n 
B 1 127 LYS 127 107 107 LYS LYS B . n 
B 1 128 ASN 128 108 108 ASN ASN B . n 
B 1 129 TYR 129 109 109 TYR TYR B . n 
B 1 130 LYS 130 110 110 LYS LYS B . n 
B 1 131 VAL 131 111 111 VAL VAL B . n 
B 1 132 ILE 132 112 112 ILE ILE B . n 
B 1 133 ASP 133 113 113 ASP ASP B . n 
B 1 134 ARG 134 114 114 ARG ARG B . n 
B 1 135 GLU 135 115 115 GLU GLU B . n 
B 1 136 GLY 136 116 116 GLY GLY B . n 
B 1 137 TYR 137 117 117 TYR TYR B . n 
B 1 138 ALA 138 118 118 ALA ALA B . n 
B 1 139 PHE 139 119 119 PHE PHE B . n 
B 1 140 ARG 140 120 120 ARG ARG B . n 
B 1 141 ASP 141 121 121 ASP ASP B . n 
B 1 142 SER 142 122 122 SER SER B . n 
B 1 143 PHE 143 123 123 PHE PHE B . n 
B 1 144 THR 144 124 124 THR THR B . n 
B 1 145 LYS 145 125 125 LYS LYS B . n 
B 1 146 VAL 146 126 126 VAL VAL B . n 
B 1 147 GLU 147 127 127 GLU GLU B . n 
B 1 148 PHE 148 128 128 PHE PHE B . n 
B 1 149 PHE 149 129 129 PHE PHE B . n 
B 1 150 GLN 150 130 130 GLN GLN B . n 
B 1 151 GLY 151 131 131 GLY GLY B . n 
B 1 152 ASP 152 132 132 ASP ASP B . n 
B 1 153 ALA 153 133 133 ALA ALA B . n 
B 1 154 CYS 154 134 134 CYS CYS B . n 
B 1 155 ASN 155 135 135 ASN ASN B . n 
B 1 156 LEU 156 136 136 LEU LEU B . n 
B 1 157 THR 157 137 137 THR THR B . n 
B 1 158 PRO 158 138 138 PRO PRO B . n 
B 1 159 GLN 159 139 139 GLN GLN B . n 
B 1 160 PHE 160 140 140 PHE PHE B . n 
B 1 161 LYS 161 141 141 LYS LYS B . n 
B 1 162 GLU 162 142 142 GLU GLU B . n 
B 1 163 TYR 163 143 143 TYR TYR B . n 
B 1 164 ASP 164 144 144 ASP ASP B . n 
B 1 165 LEU 165 145 145 LEU LEU B . n 
B 1 166 ILE 166 146 146 ILE ILE B . n 
B 1 167 MET 167 147 147 MET MET B . n 
B 1 168 ALA 168 148 148 ALA ALA B . n 
B 1 169 THR 169 149 149 THR THR B . n 
B 1 170 ASN 170 150 150 ASN ASN B . n 
B 1 171 LEU 171 151 151 LEU LEU B . n 
B 1 172 ILE 172 152 152 ILE ILE B . n 
B 1 173 ASP 173 153 153 ASP ASP B . n 
B 1 174 ARG 174 154 154 ARG ARG B . n 
B 1 175 LEU 175 155 155 LEU LEU B . n 
B 1 176 TYR 176 156 156 TYR TYR B . n 
B 1 177 GLU 177 157 157 GLU GLU B . n 
B 1 178 PRO 178 158 158 PRO PRO B . n 
B 1 179 ARG 179 159 159 ARG ARG B . n 
B 1 180 LEU 180 160 160 LEU LEU B . n 
B 1 181 PHE 181 161 161 PHE PHE B . n 
B 1 182 LEU 182 162 162 LEU LEU B . n 
B 1 183 GLU 183 163 163 GLU GLU B . n 
B 1 184 ASN 184 164 164 ASN ASN B . n 
B 1 185 ILE 185 165 165 ILE ILE B . n 
B 1 186 HIS 186 166 166 HIS HIS B . n 
B 1 187 LYS 187 167 167 LYS LYS B . n 
B 1 188 ARG 188 168 168 ARG ARG B . n 
B 1 189 ILE 189 169 169 ILE ILE B . n 
B 1 190 ASN 190 170 170 ASN ASN B . n 
B 1 191 GLU 191 171 171 GLU GLU B . n 
B 1 192 LYS 192 172 172 LYS LYS B . n 
B 1 193 GLY 193 173 173 GLY GLY B . n 
B 1 194 TYR 194 174 174 TYR TYR B . n 
B 1 195 LEU 195 175 175 LEU LEU B . n 
B 1 196 ILE 196 176 176 ILE ILE B . n 
B 1 197 LEU 197 177 177 LEU LEU B . n 
B 1 198 THR 198 178 178 THR THR B . n 
B 1 199 SER 199 179 179 SER SER B . n 
B 1 200 PRO 200 180 180 PRO PRO B . n 
B 1 201 TYR 201 181 181 TYR TYR B . n 
B 1 202 THR 202 182 182 THR THR B . n 
B 1 203 TRP 203 183 183 TRP TRP B . n 
B 1 204 ARG 204 184 184 ARG ARG B . n 
B 1 205 GLU 205 185 185 GLU GLU B . n 
B 1 206 GLU 206 186 186 GLU GLU B . n 
B 1 207 TYR 207 187 187 TYR TYR B . n 
B 1 208 THR 208 188 188 THR THR B . n 
B 1 209 ALA 209 189 189 ALA ALA B . n 
B 1 210 LYS 210 190 190 LYS LYS B . n 
B 1 211 LYS 211 191 191 LYS LYS B . n 
B 1 212 PHE 212 192 192 PHE PHE B . n 
B 1 213 TRP 213 193 193 TRP TRP B . n 
B 1 214 ILE 214 194 194 ILE ILE B . n 
B 1 215 GLY 215 195 195 GLY GLY B . n 
B 1 216 GLY 216 196 196 GLY GLY B . n 
B 1 217 TYR 217 197 197 TYR TYR B . n 
B 1 218 VAL 218 198 198 VAL VAL B . n 
B 1 219 ASP 219 199 199 ASP ASP B . n 
B 1 220 GLU 220 200 200 GLU GLU B . n 
B 1 221 ASN 221 201 201 ASN ASN B . n 
B 1 222 GLY 222 202 202 GLY GLY B . n 
B 1 223 LYS 223 203 203 LYS LYS B . n 
B 1 224 GLU 224 204 204 GLU GLU B . n 
B 1 225 VAL 225 205 205 VAL VAL B . n 
B 1 226 SER 226 206 206 SER SER B . n 
B 1 227 THR 227 207 207 THR THR B . n 
B 1 228 LEU 228 208 208 LEU LEU B . n 
B 1 229 GLU 229 209 209 GLU GLU B . n 
B 1 230 GLY 230 210 210 GLY GLY B . n 
B 1 231 LEU 231 211 211 LEU LEU B . n 
B 1 232 LYS 232 212 212 LYS LYS B . n 
B 1 233 GLU 233 213 213 GLU GLU B . n 
B 1 234 ILE 234 214 214 ILE ILE B . n 
B 1 235 LEU 235 215 215 LEU LEU B . n 
B 1 236 GLU 236 216 216 GLU GLU B . n 
B 1 237 ILE 237 217 217 ILE ILE B . n 
B 1 238 HIS 238 218 218 HIS HIS B . n 
B 1 239 PHE 239 219 219 PHE PHE B . n 
B 1 240 GLU 240 220 220 GLU GLU B . n 
B 1 241 LEU 241 221 221 LEU LEU B . n 
B 1 242 VAL 242 222 222 VAL VAL B . n 
B 1 243 ALA 243 223 223 ALA ALA B . n 
B 1 244 THR 244 224 224 THR THR B . n 
B 1 245 GLU 245 225 225 GLU GLU B . n 
B 1 246 ASP 246 226 226 ASP ASP B . n 
B 1 247 ILE 247 227 227 ILE ILE B . n 
B 1 248 PRO 248 228 228 PRO PRO B . n 
B 1 249 PHE 249 229 229 PHE PHE B . n 
B 1 250 VAL 250 230 230 VAL VAL B . n 
B 1 251 ILE 251 231 231 ILE ILE B . n 
B 1 252 ARG 252 232 232 ARG ARG B . n 
B 1 253 GLU 253 233 233 GLU GLU B . n 
B 1 254 THR 254 234 234 THR THR B . n 
B 1 255 SER 255 235 235 SER SER B . n 
B 1 256 ARG 256 236 236 ARG ARG B . n 
B 1 257 LYS 257 237 237 LYS LYS B . n 
B 1 258 PHE 258 238 238 PHE PHE B . n 
B 1 259 GLN 259 239 239 GLN GLN B . n 
B 1 260 HIS 260 240 240 HIS HIS B . n 
B 1 261 THR 261 241 241 THR THR B . n 
B 1 262 ILE 262 242 242 ILE ILE B . n 
B 1 263 SER 263 243 243 SER SER B . n 
B 1 264 GLN 264 244 244 GLN GLN B . n 
B 1 265 MET 265 245 245 MET MET B . n 
B 1 266 SER 266 246 246 SER SER B . n 
B 1 267 VAL 267 247 247 VAL VAL B . n 
B 1 268 TRP 268 248 248 TRP TRP B . n 
B 1 269 LYS 269 249 249 LYS LYS B . n 
B 1 270 VAL 270 250 250 VAL VAL B . n 
B 1 271 ILE 271 251 251 ILE ILE B . n 
B 1 272 SER 272 252 ?   ?   ?   B . n 
B 1 273 THR 273 253 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        SAM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   SAM 
_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 
C 2 SAM 1   301 281 SAM SAM A . 
D 3 TRS 1   302 282 TRS TRS A . 
E 4 EDO 1   303 283 EDO EDO A . 
F 4 EDO 1   304 284 EDO EDO A . 
G 4 EDO 1   305 285 EDO EDO A . 
H 2 SAM 1   301 261 SAM SAM B . 
I 3 TRS 1   302 262 TRS TRS B . 
J 5 HOH 1   401 148 HOH HOH A . 
J 5 HOH 2   402 5   HOH HOH A . 
J 5 HOH 3   403 83  HOH HOH A . 
J 5 HOH 4   404 81  HOH HOH A . 
J 5 HOH 5   405 22  HOH HOH A . 
J 5 HOH 6   406 98  HOH HOH A . 
J 5 HOH 7   407 76  HOH HOH A . 
J 5 HOH 8   408 231 HOH HOH A . 
J 5 HOH 9   409 198 HOH HOH A . 
J 5 HOH 10  410 193 HOH HOH A . 
J 5 HOH 11  411 251 HOH HOH A . 
J 5 HOH 12  412 108 HOH HOH A . 
J 5 HOH 13  413 16  HOH HOH A . 
J 5 HOH 14  414 119 HOH HOH A . 
J 5 HOH 15  415 52  HOH HOH A . 
J 5 HOH 16  416 2   HOH HOH A . 
J 5 HOH 17  417 258 HOH HOH A . 
J 5 HOH 18  418 57  HOH HOH A . 
J 5 HOH 19  419 15  HOH HOH A . 
J 5 HOH 20  420 29  HOH HOH A . 
J 5 HOH 21  421 11  HOH HOH A . 
J 5 HOH 22  422 47  HOH HOH A . 
J 5 HOH 23  423 9   HOH HOH A . 
J 5 HOH 24  424 290 HOH HOH A . 
J 5 HOH 25  425 260 HOH HOH A . 
J 5 HOH 26  426 18  HOH HOH A . 
J 5 HOH 27  427 21  HOH HOH A . 
J 5 HOH 28  428 181 HOH HOH A . 
J 5 HOH 29  429 25  HOH HOH A . 
J 5 HOH 30  430 36  HOH HOH A . 
J 5 HOH 31  431 49  HOH HOH A . 
J 5 HOH 32  432 113 HOH HOH A . 
J 5 HOH 33  433 7   HOH HOH A . 
J 5 HOH 34  434 8   HOH HOH A . 
J 5 HOH 35  435 255 HOH HOH A . 
J 5 HOH 36  436 96  HOH HOH A . 
J 5 HOH 37  437 278 HOH HOH A . 
J 5 HOH 38  438 185 HOH HOH A . 
J 5 HOH 39  439 69  HOH HOH A . 
J 5 HOH 40  440 342 HOH HOH A . 
J 5 HOH 41  441 347 HOH HOH A . 
J 5 HOH 42  442 196 HOH HOH A . 
J 5 HOH 43  443 190 HOH HOH A . 
J 5 HOH 44  444 138 HOH HOH A . 
J 5 HOH 45  445 46  HOH HOH A . 
J 5 HOH 46  446 50  HOH HOH A . 
J 5 HOH 47  447 59  HOH HOH A . 
J 5 HOH 48  448 14  HOH HOH A . 
J 5 HOH 49  449 147 HOH HOH A . 
J 5 HOH 50  450 86  HOH HOH A . 
J 5 HOH 51  451 126 HOH HOH A . 
J 5 HOH 52  452 150 HOH HOH A . 
J 5 HOH 53  453 171 HOH HOH A . 
J 5 HOH 54  454 24  HOH HOH A . 
J 5 HOH 55  455 45  HOH HOH A . 
J 5 HOH 56  456 12  HOH HOH A . 
J 5 HOH 57  457 145 HOH HOH A . 
J 5 HOH 58  458 177 HOH HOH A . 
J 5 HOH 59  459 84  HOH HOH A . 
J 5 HOH 60  460 206 HOH HOH A . 
J 5 HOH 61  461 136 HOH HOH A . 
J 5 HOH 62  462 156 HOH HOH A . 
J 5 HOH 63  463 121 HOH HOH A . 
J 5 HOH 64  464 97  HOH HOH A . 
J 5 HOH 65  465 227 HOH HOH A . 
J 5 HOH 66  466 214 HOH HOH A . 
J 5 HOH 67  467 259 HOH HOH A . 
J 5 HOH 68  468 102 HOH HOH A . 
J 5 HOH 69  469 56  HOH HOH A . 
J 5 HOH 70  470 32  HOH HOH A . 
J 5 HOH 71  471 201 HOH HOH A . 
J 5 HOH 72  472 60  HOH HOH A . 
J 5 HOH 73  473 63  HOH HOH A . 
J 5 HOH 74  474 120 HOH HOH A . 
J 5 HOH 75  475 336 HOH HOH A . 
J 5 HOH 76  476 318 HOH HOH A . 
J 5 HOH 77  477 27  HOH HOH A . 
J 5 HOH 78  478 64  HOH HOH A . 
J 5 HOH 79  479 51  HOH HOH A . 
J 5 HOH 80  480 354 HOH HOH A . 
J 5 HOH 81  481 170 HOH HOH A . 
J 5 HOH 82  482 162 HOH HOH A . 
J 5 HOH 83  483 99  HOH HOH A . 
J 5 HOH 84  484 182 HOH HOH A . 
J 5 HOH 85  485 204 HOH HOH A . 
J 5 HOH 86  486 207 HOH HOH A . 
J 5 HOH 87  487 30  HOH HOH A . 
J 5 HOH 88  488 155 HOH HOH A . 
J 5 HOH 89  489 186 HOH HOH A . 
J 5 HOH 90  490 266 HOH HOH A . 
J 5 HOH 91  491 137 HOH HOH A . 
J 5 HOH 92  492 176 HOH HOH A . 
J 5 HOH 93  493 213 HOH HOH A . 
J 5 HOH 94  494 245 HOH HOH A . 
J 5 HOH 95  495 275 HOH HOH A . 
J 5 HOH 96  496 263 HOH HOH A . 
J 5 HOH 97  497 133 HOH HOH A . 
J 5 HOH 98  498 247 HOH HOH A . 
J 5 HOH 99  499 111 HOH HOH A . 
J 5 HOH 100 500 141 HOH HOH A . 
J 5 HOH 101 501 361 HOH HOH A . 
J 5 HOH 102 502 337 HOH HOH A . 
J 5 HOH 103 503 280 HOH HOH A . 
J 5 HOH 104 504 200 HOH HOH A . 
J 5 HOH 105 505 122 HOH HOH A . 
J 5 HOH 106 506 257 HOH HOH A . 
J 5 HOH 107 507 298 HOH HOH A . 
J 5 HOH 108 508 344 HOH HOH A . 
J 5 HOH 109 509 224 HOH HOH A . 
J 5 HOH 110 510 284 HOH HOH A . 
J 5 HOH 111 511 248 HOH HOH A . 
J 5 HOH 112 512 68  HOH HOH A . 
J 5 HOH 113 513 345 HOH HOH A . 
J 5 HOH 114 514 349 HOH HOH A . 
J 5 HOH 115 515 238 HOH HOH A . 
J 5 HOH 116 516 335 HOH HOH A . 
J 5 HOH 117 517 297 HOH HOH A . 
J 5 HOH 118 518 355 HOH HOH A . 
J 5 HOH 119 519 211 HOH HOH A . 
J 5 HOH 120 520 301 HOH HOH A . 
J 5 HOH 121 521 179 HOH HOH A . 
J 5 HOH 122 522 292 HOH HOH A . 
J 5 HOH 123 523 80  HOH HOH A . 
J 5 HOH 124 524 334 HOH HOH A . 
J 5 HOH 125 525 363 HOH HOH A . 
J 5 HOH 126 526 233 HOH HOH A . 
J 5 HOH 127 527 262 HOH HOH A . 
J 5 HOH 128 528 174 HOH HOH A . 
J 5 HOH 129 529 350 HOH HOH A . 
J 5 HOH 130 530 333 HOH HOH A . 
J 5 HOH 131 531 346 HOH HOH A . 
J 5 HOH 132 532 77  HOH HOH A . 
J 5 HOH 133 533 302 HOH HOH A . 
J 5 HOH 134 534 220 HOH HOH A . 
J 5 HOH 135 535 246 HOH HOH A . 
K 5 HOH 1   401 115 HOH HOH B . 
K 5 HOH 2   402 208 HOH HOH B . 
K 5 HOH 3   403 158 HOH HOH B . 
K 5 HOH 4   404 103 HOH HOH B . 
K 5 HOH 5   405 4   HOH HOH B . 
K 5 HOH 6   406 116 HOH HOH B . 
K 5 HOH 7   407 142 HOH HOH B . 
K 5 HOH 8   408 73  HOH HOH B . 
K 5 HOH 9   409 239 HOH HOH B . 
K 5 HOH 10  410 183 HOH HOH B . 
K 5 HOH 11  411 44  HOH HOH B . 
K 5 HOH 12  412 35  HOH HOH B . 
K 5 HOH 13  413 67  HOH HOH B . 
K 5 HOH 14  414 92  HOH HOH B . 
K 5 HOH 15  415 3   HOH HOH B . 
K 5 HOH 16  416 134 HOH HOH B . 
K 5 HOH 17  417 40  HOH HOH B . 
K 5 HOH 18  418 13  HOH HOH B . 
K 5 HOH 19  419 104 HOH HOH B . 
K 5 HOH 20  420 124 HOH HOH B . 
K 5 HOH 21  421 1   HOH HOH B . 
K 5 HOH 22  422 112 HOH HOH B . 
K 5 HOH 23  423 125 HOH HOH B . 
K 5 HOH 24  424 28  HOH HOH B . 
K 5 HOH 25  425 55  HOH HOH B . 
K 5 HOH 26  426 161 HOH HOH B . 
K 5 HOH 27  427 210 HOH HOH B . 
K 5 HOH 28  428 75  HOH HOH B . 
K 5 HOH 29  429 90  HOH HOH B . 
K 5 HOH 30  430 209 HOH HOH B . 
K 5 HOH 31  431 267 HOH HOH B . 
K 5 HOH 32  432 20  HOH HOH B . 
K 5 HOH 33  433 95  HOH HOH B . 
K 5 HOH 34  434 127 HOH HOH B . 
K 5 HOH 35  435 222 HOH HOH B . 
K 5 HOH 36  436 65  HOH HOH B . 
K 5 HOH 37  437 271 HOH HOH B . 
K 5 HOH 38  438 6   HOH HOH B . 
K 5 HOH 39  439 128 HOH HOH B . 
K 5 HOH 40  440 140 HOH HOH B . 
K 5 HOH 41  441 195 HOH HOH B . 
K 5 HOH 42  442 33  HOH HOH B . 
K 5 HOH 43  443 129 HOH HOH B . 
K 5 HOH 44  444 243 HOH HOH B . 
K 5 HOH 45  445 10  HOH HOH B . 
K 5 HOH 46  446 107 HOH HOH B . 
K 5 HOH 47  447 241 HOH HOH B . 
K 5 HOH 48  448 38  HOH HOH B . 
K 5 HOH 49  449 41  HOH HOH B . 
K 5 HOH 50  450 135 HOH HOH B . 
K 5 HOH 51  451 139 HOH HOH B . 
K 5 HOH 52  452 314 HOH HOH B . 
K 5 HOH 53  453 17  HOH HOH B . 
K 5 HOH 54  454 202 HOH HOH B . 
K 5 HOH 55  455 23  HOH HOH B . 
K 5 HOH 56  456 228 HOH HOH B . 
K 5 HOH 57  457 42  HOH HOH B . 
K 5 HOH 58  458 53  HOH HOH B . 
K 5 HOH 59  459 194 HOH HOH B . 
K 5 HOH 60  460 87  HOH HOH B . 
K 5 HOH 61  461 169 HOH HOH B . 
K 5 HOH 62  462 48  HOH HOH B . 
K 5 HOH 63  463 105 HOH HOH B . 
K 5 HOH 64  464 131 HOH HOH B . 
K 5 HOH 65  465 157 HOH HOH B . 
K 5 HOH 66  466 66  HOH HOH B . 
K 5 HOH 67  467 39  HOH HOH B . 
K 5 HOH 68  468 160 HOH HOH B . 
K 5 HOH 69  469 54  HOH HOH B . 
K 5 HOH 70  470 217 HOH HOH B . 
K 5 HOH 71  471 43  HOH HOH B . 
K 5 HOH 72  472 117 HOH HOH B . 
K 5 HOH 73  473 26  HOH HOH B . 
K 5 HOH 74  474 268 HOH HOH B . 
K 5 HOH 75  475 197 HOH HOH B . 
K 5 HOH 76  476 31  HOH HOH B . 
K 5 HOH 77  477 153 HOH HOH B . 
K 5 HOH 78  478 163 HOH HOH B . 
K 5 HOH 79  479 143 HOH HOH B . 
K 5 HOH 80  480 272 HOH HOH B . 
K 5 HOH 81  481 62  HOH HOH B . 
K 5 HOH 82  482 173 HOH HOH B . 
K 5 HOH 83  483 166 HOH HOH B . 
K 5 HOH 84  484 265 HOH HOH B . 
K 5 HOH 85  485 339 HOH HOH B . 
K 5 HOH 86  486 71  HOH HOH B . 
K 5 HOH 87  487 168 HOH HOH B . 
K 5 HOH 88  488 178 HOH HOH B . 
K 5 HOH 89  489 151 HOH HOH B . 
K 5 HOH 90  490 88  HOH HOH B . 
K 5 HOH 91  491 261 HOH HOH B . 
K 5 HOH 92  492 180 HOH HOH B . 
K 5 HOH 93  493 93  HOH HOH B . 
K 5 HOH 94  494 167 HOH HOH B . 
K 5 HOH 95  495 270 HOH HOH B . 
K 5 HOH 96  496 91  HOH HOH B . 
K 5 HOH 97  497 212 HOH HOH B . 
K 5 HOH 98  498 244 HOH HOH B . 
K 5 HOH 99  499 226 HOH HOH B . 
K 5 HOH 100 500 72  HOH HOH B . 
K 5 HOH 101 501 144 HOH HOH B . 
K 5 HOH 102 502 37  HOH HOH B . 
K 5 HOH 103 503 191 HOH HOH B . 
K 5 HOH 104 504 118 HOH HOH B . 
K 5 HOH 105 505 152 HOH HOH B . 
K 5 HOH 106 506 101 HOH HOH B . 
K 5 HOH 107 507 94  HOH HOH B . 
K 5 HOH 108 508 192 HOH HOH B . 
K 5 HOH 109 509 288 HOH HOH B . 
K 5 HOH 110 510 189 HOH HOH B . 
K 5 HOH 111 511 184 HOH HOH B . 
K 5 HOH 112 512 250 HOH HOH B . 
K 5 HOH 113 513 274 HOH HOH B . 
K 5 HOH 114 514 58  HOH HOH B . 
K 5 HOH 115 515 359 HOH HOH B . 
K 5 HOH 116 516 109 HOH HOH B . 
K 5 HOH 117 517 187 HOH HOH B . 
K 5 HOH 118 518 205 HOH HOH B . 
K 5 HOH 119 519 312 HOH HOH B . 
K 5 HOH 120 520 351 HOH HOH B . 
K 5 HOH 121 521 89  HOH HOH B . 
K 5 HOH 122 522 338 HOH HOH B . 
K 5 HOH 123 523 223 HOH HOH B . 
K 5 HOH 124 524 123 HOH HOH B . 
K 5 HOH 125 525 100 HOH HOH B . 
K 5 HOH 126 526 353 HOH HOH B . 
K 5 HOH 127 527 277 HOH HOH B . 
K 5 HOH 128 528 175 HOH HOH B . 
K 5 HOH 129 529 242 HOH HOH B . 
K 5 HOH 130 530 188 HOH HOH B . 
K 5 HOH 131 531 85  HOH HOH B . 
K 5 HOH 132 532 254 HOH HOH B . 
K 5 HOH 133 533 253 HOH HOH B . 
K 5 HOH 134 534 132 HOH HOH B . 
K 5 HOH 135 535 285 HOH HOH B . 
K 5 HOH 136 536 78  HOH HOH B . 
K 5 HOH 137 537 343 HOH HOH B . 
K 5 HOH 138 538 216 HOH HOH B . 
K 5 HOH 139 539 110 HOH HOH B . 
K 5 HOH 140 540 289 HOH HOH B . 
K 5 HOH 141 541 70  HOH HOH B . 
K 5 HOH 142 542 340 HOH HOH B . 
K 5 HOH 143 543 348 HOH HOH B . 
K 5 HOH 144 544 356 HOH HOH B . 
K 5 HOH 145 545 146 HOH HOH B . 
K 5 HOH 146 546 306 HOH HOH B . 
K 5 HOH 147 547 360 HOH HOH B . 
K 5 HOH 148 548 165 HOH HOH B . 
K 5 HOH 149 549 296 HOH HOH B . 
K 5 HOH 150 550 264 HOH HOH B . 
K 5 HOH 151 551 362 HOH HOH B . 
K 5 HOH 152 552 352 HOH HOH B . 
K 5 HOH 153 553 164 HOH HOH B . 
K 5 HOH 154 554 82  HOH HOH B . 
K 5 HOH 155 555 307 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ASP 12  ? CG  ? A ASP 32  CG  
2   1 Y 1 A ASP 12  ? OD1 ? A ASP 32  OD1 
3   1 Y 1 A ASP 12  ? OD2 ? A ASP 32  OD2 
4   1 Y 1 A GLU 13  ? CG  ? A GLU 33  CG  
5   1 Y 1 A GLU 13  ? CD  ? A GLU 33  CD  
6   1 Y 1 A GLU 13  ? OE1 ? A GLU 33  OE1 
7   1 Y 1 A GLU 13  ? OE2 ? A GLU 33  OE2 
8   1 Y 1 A GLU 25  ? CG  ? A GLU 45  CG  
9   1 Y 1 A GLU 25  ? CD  ? A GLU 45  CD  
10  1 Y 1 A GLU 25  ? OE1 ? A GLU 45  OE1 
11  1 Y 1 A GLU 25  ? OE2 ? A GLU 45  OE2 
12  1 Y 1 A ASP 26  ? OD1 ? A ASP 46  OD1 
13  1 Y 1 A ASP 26  ? OD2 ? A ASP 46  OD2 
14  1 Y 1 A LYS 46  ? CG  ? A LYS 66  CG  
15  1 Y 1 A LYS 46  ? CD  ? A LYS 66  CD  
16  1 Y 1 A LYS 46  ? CE  ? A LYS 66  CE  
17  1 Y 1 A LYS 46  ? NZ  ? A LYS 66  NZ  
18  1 Y 1 A GLU 47  ? CG  ? A GLU 67  CG  
19  1 Y 1 A GLU 47  ? CD  ? A GLU 67  CD  
20  1 Y 1 A GLU 47  ? OE1 ? A GLU 67  OE1 
21  1 Y 1 A GLU 47  ? OE2 ? A GLU 67  OE2 
22  1 Y 1 A LYS 50  ? NZ  ? A LYS 70  NZ  
23  1 Y 1 A LYS 72  ? CD  ? A LYS 92  CD  
24  1 Y 1 A LYS 72  ? CE  ? A LYS 92  CE  
25  1 Y 1 A LYS 72  ? NZ  ? A LYS 92  NZ  
26  1 Y 1 A GLU 89  ? CG  ? A GLU 109 CG  
27  1 Y 1 A GLU 89  ? CD  ? A GLU 109 CD  
28  1 Y 1 A GLU 89  ? OE1 ? A GLU 109 OE1 
29  1 Y 1 A GLU 89  ? OE2 ? A GLU 109 OE2 
30  1 Y 1 A LYS 92  ? CD  ? A LYS 112 CD  
31  1 Y 1 A LYS 92  ? CE  ? A LYS 112 CE  
32  1 Y 1 A LYS 92  ? NZ  ? A LYS 112 NZ  
33  1 Y 1 A ILE 96  ? CD1 ? A ILE 116 CD1 
34  1 Y 1 A GLN 139 ? OE1 ? A GLN 159 OE1 
35  1 Y 1 A GLN 139 ? NE2 ? A GLN 159 NE2 
36  1 Y 1 A LYS 141 ? CE  ? A LYS 161 CE  
37  1 Y 1 A LYS 141 ? NZ  ? A LYS 161 NZ  
38  1 Y 1 A LYS 167 ? CE  ? A LYS 187 CE  
39  1 Y 1 A LYS 167 ? NZ  ? A LYS 187 NZ  
40  1 Y 1 A GLU 171 ? CG  ? A GLU 191 CG  
41  1 Y 1 A GLU 171 ? CD  ? A GLU 191 CD  
42  1 Y 1 A GLU 171 ? OE1 ? A GLU 191 OE1 
43  1 Y 1 A GLU 171 ? OE2 ? A GLU 191 OE2 
44  1 Y 1 A LYS 172 ? CG  ? A LYS 192 CG  
45  1 Y 1 A LYS 172 ? CD  ? A LYS 192 CD  
46  1 Y 1 A LYS 172 ? CE  ? A LYS 192 CE  
47  1 Y 1 A LYS 172 ? NZ  ? A LYS 192 NZ  
48  1 Y 1 A ARG 184 ? CZ  ? A ARG 204 CZ  
49  1 Y 1 A ARG 184 ? NH1 ? A ARG 204 NH1 
50  1 Y 1 A ARG 184 ? NH2 ? A ARG 204 NH2 
51  1 Y 1 A GLU 200 ? OE1 ? A GLU 220 OE1 
52  1 Y 1 A GLU 200 ? OE2 ? A GLU 220 OE2 
53  1 Y 1 A LYS 203 ? CE  ? A LYS 223 CE  
54  1 Y 1 A LYS 203 ? NZ  ? A LYS 223 NZ  
55  1 Y 1 A GLU 209 ? CG  ? A GLU 229 CG  
56  1 Y 1 A GLU 209 ? CD  ? A GLU 229 CD  
57  1 Y 1 A GLU 209 ? OE1 ? A GLU 229 OE1 
58  1 Y 1 A GLU 209 ? OE2 ? A GLU 229 OE2 
59  1 Y 1 A GLU 213 ? OE1 ? A GLU 233 OE1 
60  1 Y 1 A GLU 213 ? OE2 ? A GLU 233 OE2 
61  1 Y 1 A LYS 237 ? NZ  ? A LYS 257 NZ  
62  1 Y 1 A LYS 249 ? NZ  ? A LYS 269 NZ  
63  1 Y 1 A ILE 251 ? CG1 ? A ILE 271 CG1 
64  1 Y 1 A ILE 251 ? CG2 ? A ILE 271 CG2 
65  1 Y 1 A ILE 251 ? CD1 ? A ILE 271 CD1 
66  1 Y 1 B ILE 8   ? CB  ? B ILE 28  CB  
67  1 Y 1 B ILE 8   ? CG1 ? B ILE 28  CG1 
68  1 Y 1 B ILE 8   ? CG2 ? B ILE 28  CG2 
69  1 Y 1 B ILE 8   ? CD1 ? B ILE 28  CD1 
70  1 Y 1 B GLU 10  ? CG  ? B GLU 30  CG  
71  1 Y 1 B GLU 10  ? CD  ? B GLU 30  CD  
72  1 Y 1 B GLU 10  ? OE1 ? B GLU 30  OE1 
73  1 Y 1 B GLU 10  ? OE2 ? B GLU 30  OE2 
74  1 Y 1 B GLU 13  ? OE2 ? B GLU 33  OE2 
75  1 Y 1 B GLU 25  ? CG  ? B GLU 45  CG  
76  1 Y 1 B GLU 25  ? CD  ? B GLU 45  CD  
77  1 Y 1 B GLU 25  ? OE1 ? B GLU 45  OE1 
78  1 Y 1 B GLU 25  ? OE2 ? B GLU 45  OE2 
79  1 Y 1 B LYS 46  ? NZ  ? B LYS 66  NZ  
80  1 Y 1 B LYS 72  ? CD  ? B LYS 92  CD  
81  1 Y 1 B LYS 72  ? CE  ? B LYS 92  CE  
82  1 Y 1 B LYS 72  ? NZ  ? B LYS 92  NZ  
83  1 Y 1 B LYS 92  ? CG  ? B LYS 112 CG  
84  1 Y 1 B LYS 92  ? CD  ? B LYS 112 CD  
85  1 Y 1 B LYS 92  ? CE  ? B LYS 112 CE  
86  1 Y 1 B LYS 92  ? NZ  ? B LYS 112 NZ  
87  1 Y 1 B ASN 93  ? ND2 ? B ASN 113 ND2 
88  1 Y 1 B SER 99  ? OG  ? B SER 119 OG  
89  1 Y 1 B LYS 110 ? NZ  ? B LYS 130 NZ  
90  1 Y 1 B ARG 120 ? NH1 ? B ARG 140 NH1 
91  1 Y 1 B ARG 120 ? NH2 ? B ARG 140 NH2 
92  1 Y 1 B GLN 139 ? CG  ? B GLN 159 CG  
93  1 Y 1 B GLN 139 ? CD  ? B GLN 159 CD  
94  1 Y 1 B GLN 139 ? OE1 ? B GLN 159 OE1 
95  1 Y 1 B GLN 139 ? NE2 ? B GLN 159 NE2 
96  1 Y 1 B LYS 141 ? CE  ? B LYS 161 CE  
97  1 Y 1 B LYS 141 ? NZ  ? B LYS 161 NZ  
98  1 Y 1 B LYS 167 ? CD  ? B LYS 187 CD  
99  1 Y 1 B LYS 167 ? CE  ? B LYS 187 CE  
100 1 Y 1 B LYS 167 ? NZ  ? B LYS 187 NZ  
101 1 Y 1 B GLU 171 ? CG  ? B GLU 191 CG  
102 1 Y 1 B GLU 171 ? CD  ? B GLU 191 CD  
103 1 Y 1 B GLU 171 ? OE1 ? B GLU 191 OE1 
104 1 Y 1 B GLU 171 ? OE2 ? B GLU 191 OE2 
105 1 Y 1 B LYS 172 ? CB  ? B LYS 192 CB  
106 1 Y 1 B LYS 172 ? CG  ? B LYS 192 CG  
107 1 Y 1 B LYS 172 ? CD  ? B LYS 192 CD  
108 1 Y 1 B LYS 172 ? CE  ? B LYS 192 CE  
109 1 Y 1 B LYS 172 ? NZ  ? B LYS 192 NZ  
110 1 Y 1 B LYS 190 ? NZ  ? B LYS 210 NZ  
111 1 Y 1 B GLU 200 ? CD  ? B GLU 220 CD  
112 1 Y 1 B GLU 200 ? OE1 ? B GLU 220 OE1 
113 1 Y 1 B GLU 200 ? OE2 ? B GLU 220 OE2 
114 1 Y 1 B GLU 209 ? CG  ? B GLU 229 CG  
115 1 Y 1 B GLU 209 ? CD  ? B GLU 229 CD  
116 1 Y 1 B GLU 209 ? OE1 ? B GLU 229 OE1 
117 1 Y 1 B GLU 209 ? OE2 ? B GLU 229 OE2 
118 1 Y 1 B GLU 213 ? OE1 ? B GLU 233 OE1 
119 1 Y 1 B GLU 213 ? OE2 ? B GLU 233 OE2 
120 1 Y 1 B LYS 237 ? NZ  ? B LYS 257 NZ  
121 1 Y 1 B LYS 249 ? CE  ? B LYS 269 CE  
122 1 Y 1 B LYS 249 ? NZ  ? B LYS 269 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? XDS-Apple_M1 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? XDS-Apple_M1 2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? 1.20.1_4487  3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? 0.9.8.7      4 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487  5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BXL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     70.160 
_cell.length_a_esd                 ? 
_cell.length_b                     92.215 
_cell.length_b_esd                 ? 
_cell.length_c                     95.999 
_cell.length_c_esd                 ? 
_cell.volume                       621094.753 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BXL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BXL 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.53 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.4 
_exptl_crystal.description                  'Small plates' 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M citric acid, pH 5, 20% PEG6000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-29 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97949 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 8.2.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97949 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          34.15 
_reflns.entry_id                                       9BXL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.09 
_reflns.d_resolution_low                               48.27 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     37433 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.56 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.49 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.07673 
_reflns.pdbx_Rpim_I_all                                0.05425 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.05425 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.09 
_reflns_shell.d_res_low                                     2.165 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.11 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3567 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               2.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.7791 
_reflns_shell.pdbx_Rpim_I_all                               0.5509 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.644 
_reflns_shell.pdbx_CC_star                                  0.885 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.36 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.5509 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               33.08 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BXL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.09 
_refine.ls_d_res_low                             48.27 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     37405 
_refine.ls_number_reflns_R_free                  1863 
_refine.ls_number_reflns_R_work                  35542 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.45 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1928 
_refine.ls_R_factor_R_free                       0.2222 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1913 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.2135 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2707 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.09 
_refine_hist.d_res_low                        48.27 
_refine_hist.number_atoms_solvent             290 
_refine_hist.number_atoms_total               4218 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3846 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         82 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0076  ? 4028 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0490  ? 5457 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0556  ? 591  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0215  ? 693  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.2549 ? 1436 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.09 2.15  . . 129 2554 93.91  . . . . 0.2829 . . . . . . . . . . . 0.3456 
'X-RAY DIFFRACTION' 2.15 2.21  . . 144 2674 99.61  . . . . 0.2606 . . . . . . . . . . . 0.3163 
'X-RAY DIFFRACTION' 2.21 2.28  . . 133 2729 100.00 . . . . 0.2620 . . . . . . . . . . . 0.3380 
'X-RAY DIFFRACTION' 2.28 2.36  . . 148 2697 99.89  . . . . 0.2411 . . . . . . . . . . . 0.2793 
'X-RAY DIFFRACTION' 2.36 2.46  . . 144 2704 100.00 . . . . 0.2420 . . . . . . . . . . . 0.2955 
'X-RAY DIFFRACTION' 2.46 2.57  . . 144 2735 100.00 . . . . 0.2238 . . . . . . . . . . . 0.2960 
'X-RAY DIFFRACTION' 2.57 2.70  . . 146 2733 99.97  . . . . 0.2045 . . . . . . . . . . . 0.2431 
'X-RAY DIFFRACTION' 2.70 2.87  . . 139 2709 99.93  . . . . 0.2062 . . . . . . . . . . . 0.2708 
'X-RAY DIFFRACTION' 2.87 3.09  . . 143 2751 99.97  . . . . 0.2141 . . . . . . . . . . . 0.2397 
'X-RAY DIFFRACTION' 3.09 3.41  . . 146 2767 100.00 . . . . 0.1927 . . . . . . . . . . . 0.2164 
'X-RAY DIFFRACTION' 3.41 3.90  . . 144 2754 99.90  . . . . 0.1656 . . . . . . . . . . . 0.1823 
'X-RAY DIFFRACTION' 3.90 4.91  . . 148 2801 99.90  . . . . 0.1379 . . . . . . . . . . . 0.1653 
'X-RAY DIFFRACTION' 4.91 48.27 . . 155 2934 99.81  . . . . 0.1751 . . . . . . . . . . . 0.1816 
# 
_struct.entry_id                     9BXL 
_struct.title                        
'OvoM from Sulfuricurvum sp. isolate STB_99, an ovothiol-biosynthetic N-methyltransferase in complex with SAM' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BXL 
_struct_keywords.text            'ovothiol, S-adenosyl-L-methionine, 5-thiohistidine, 5-selenohistidine, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 2 ? 
I N N 3 ? 
J N N 5 ? 
K N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9BXL 
_struct_ref.pdbx_db_accession          9BXL 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9BXL A 1 ? 273 ? 9BXL -19 ? 253 ? -19 253 
2 1 9BXL B 1 ? 273 ? 9BXL -19 ? 253 ? -19 253 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3570  ? 
1 MORE         7     ? 
1 'SSA (A^2)'  20040 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 B,H,I,K       
1 2 A,C,D,E,F,G,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z           1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 
1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000  
2 'crystal symmetry operation' 2_455 -x-1/2,-y,z+1/2 -1.0000000000 0.0000000000 0.0000000000 -35.0800000000 0.0000000000 
-1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 47.9995000000 
# 
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 ASN A 27  ? GLU A 30  ? ASN A 7   GLU A 10  5 ? 4  
HELX_P HELX_P2  AA2 THR A 31  ? GLY A 44  ? THR A 11  GLY A 24  1 ? 14 
HELX_P HELX_P3  AA3 ASN A 52  ? THR A 65  ? ASN A 32  THR A 45  1 ? 14 
HELX_P HELX_P4  AA4 GLY A 81  ? ALA A 88  ? GLY A 61  ALA A 68  1 ? 8  
HELX_P HELX_P5  AA5 SER A 100 ? GLY A 114 ? SER A 80  GLY A 94  1 ? 15 
HELX_P HELX_P6  AA6 GLU A 135 ? THR A 144 ? GLU A 115 THR A 124 5 ? 10 
HELX_P HELX_P7  AA7 LEU A 171 ? LEU A 175 ? LEU A 151 LEU A 155 5 ? 5  
HELX_P HELX_P8  AA8 GLU A 177 ? GLU A 183 ? GLU A 157 GLU A 163 1 ? 7  
HELX_P HELX_P9  AA9 ASN A 184 ? LYS A 187 ? ASN A 164 LYS A 167 5 ? 4  
HELX_P HELX_P10 AB1 ALA A 209 ? TRP A 213 ? ALA A 189 TRP A 193 5 ? 5  
HELX_P HELX_P11 AB2 SER A 226 ? GLU A 236 ? SER A 206 GLU A 216 1 ? 11 
HELX_P HELX_P12 AB3 ASP B 32  ? GLY B 44  ? ASP B 12  GLY B 24  1 ? 13 
HELX_P HELX_P13 AB4 ASN B 52  ? THR B 65  ? ASN B 32  THR B 45  1 ? 14 
HELX_P HELX_P14 AB5 GLY B 81  ? ARG B 89  ? GLY B 61  ARG B 69  1 ? 9  
HELX_P HELX_P15 AB6 SER B 100 ? GLY B 114 ? SER B 80  GLY B 94  1 ? 15 
HELX_P HELX_P16 AB7 GLU B 135 ? THR B 144 ? GLU B 115 THR B 124 5 ? 10 
HELX_P HELX_P17 AB8 LEU B 171 ? LEU B 175 ? LEU B 151 LEU B 155 5 ? 5  
HELX_P HELX_P18 AB9 GLU B 177 ? GLU B 183 ? GLU B 157 GLU B 163 1 ? 7  
HELX_P HELX_P19 AC1 ASN B 184 ? LYS B 187 ? ASN B 164 LYS B 167 5 ? 4  
HELX_P HELX_P20 AC2 ALA B 209 ? TRP B 213 ? ALA B 189 TRP B 193 5 ? 5  
HELX_P HELX_P21 AC3 SER B 226 ? GLU B 236 ? SER B 206 GLU B 216 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-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 146 ? GLN A 150 ? VAL A 126 GLN A 130 
AA1 2 HIS A 93  ? ASP A 98  ? HIS A 73  ASP A 78  
AA1 3 ARG A 72  ? LEU A 76  ? ARG A 52  LEU A 56  
AA1 4 TYR A 163 ? THR A 169 ? TYR A 143 THR A 149 
AA1 5 ILE A 189 ? SER A 199 ? ILE A 169 SER A 179 
AA1 6 PHE A 258 ? VAL A 270 ? PHE A 238 VAL A 250 
AA1 7 PHE A 239 ? ARG A 252 ? PHE A 219 ARG A 232 
AA2 1 CYS A 115 ? ASN A 121 ? CYS A 95  ASN A 101 
AA2 2 LYS A 127 ? ASP A 133 ? LYS A 107 ASP A 113 
AA3 1 TYR A 217 ? VAL A 218 ? TYR A 197 VAL A 198 
AA3 2 GLU A 224 ? VAL A 225 ? GLU A 204 VAL A 205 
AA4 1 VAL B 146 ? GLN B 150 ? VAL B 126 GLN B 130 
AA4 2 HIS B 93  ? ASP B 98  ? HIS B 73  ASP B 78  
AA4 3 ARG B 72  ? LEU B 76  ? ARG B 52  LEU B 56  
AA4 4 TYR B 163 ? THR B 169 ? TYR B 143 THR B 149 
AA4 5 ILE B 189 ? SER B 199 ? ILE B 169 SER B 179 
AA4 6 PHE B 258 ? VAL B 270 ? PHE B 238 VAL B 250 
AA4 7 PHE B 239 ? ARG B 252 ? PHE B 219 ARG B 232 
AA5 1 CYS B 115 ? ASN B 121 ? CYS B 95  ASN B 101 
AA5 2 LYS B 127 ? ASP B 133 ? LYS B 107 ASP B 113 
AA6 1 TYR B 217 ? VAL B 218 ? TYR B 197 VAL B 198 
AA6 2 GLU B 224 ? VAL B 225 ? GLU B 204 VAL B 205 
# 
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 O PHE A 149 ? O PHE A 129 N GLY A 96  ? N GLY A 76  
AA1 2 3 O ASP A 95  ? O ASP A 75  N ASP A 75  ? N ASP A 55  
AA1 3 4 N LEU A 74  ? N LEU A 54  O MET A 167 ? O MET A 147 
AA1 4 5 N TYR A 163 ? N TYR A 143 O ASN A 190 ? O ASN A 170 
AA1 5 6 N LEU A 195 ? N LEU A 175 O TRP A 268 ? O TRP A 248 
AA1 6 7 O VAL A 267 ? O VAL A 247 N VAL A 242 ? N VAL A 222 
AA2 1 2 N GLN A 120 ? N GLN A 100 O ASN A 128 ? O ASN A 108 
AA3 1 2 N TYR A 217 ? N TYR A 197 O VAL A 225 ? O VAL A 205 
AA4 1 2 O GLU B 147 ? O GLU B 127 N GLY B 96  ? N GLY B 76  
AA4 2 3 O ASP B 95  ? O ASP B 75  N ASP B 75  ? N ASP B 55  
AA4 3 4 N LEU B 74  ? N LEU B 54  O MET B 167 ? O MET B 147 
AA4 4 5 N TYR B 163 ? N TYR B 143 O ASN B 190 ? O ASN B 170 
AA4 5 6 N LEU B 195 ? N LEU B 175 O TRP B 268 ? O TRP B 248 
AA4 6 7 O MET B 265 ? O MET B 245 N GLU B 245 ? N GLU B 225 
AA5 1 2 N ILE B 116 ? N ILE B 96  O ILE B 132 ? O ILE B 112 
AA6 1 2 N TYR B 217 ? N TYR B 197 O VAL B 225 ? O VAL B 205 
# 
_pdbx_entry_details.entry_id                   9BXL 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 C A CYS 27  ? ? O A CYS 27  ? ? 1.364 1.229 0.135 0.019 N 
2 1 C A ARG 159 ? ? O A ARG 159 ? ? 1.351 1.229 0.122 0.019 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 59  ? ? 48.16   -127.33 
2 1 SER A 122 ? ? -141.98 13.25   
3 1 ASN A 135 ? ? -164.50 67.18   
4 1 ALA B 59  ? ? 48.02   -124.71 
5 1 PHE B 119 ? ? -67.94  0.02    
6 1 ASN B 135 ? ? -156.06 56.37   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 120 ? ? 0.221 'SIDE CHAIN' 
2 1 ARG A 159 ? ? 0.222 'SIDE CHAIN' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 -19 ? A MET 1   
2  1 Y 1 A GLY -18 ? A GLY 2   
3  1 Y 1 A SER -17 ? A SER 3   
4  1 Y 1 A SER -16 ? A SER 4   
5  1 Y 1 A HIS -15 ? A HIS 5   
6  1 Y 1 A HIS -14 ? A HIS 6   
7  1 Y 1 A HIS -13 ? A HIS 7   
8  1 Y 1 A HIS -12 ? A HIS 8   
9  1 Y 1 A HIS -11 ? A HIS 9   
10 1 Y 1 A HIS -10 ? A HIS 10  
11 1 Y 1 A SER -9  ? A SER 11  
12 1 Y 1 A SER -8  ? A SER 12  
13 1 Y 1 A GLY -7  ? A GLY 13  
14 1 Y 1 A LEU -6  ? A LEU 14  
15 1 Y 1 A VAL -5  ? A VAL 15  
16 1 Y 1 A PRO -4  ? A PRO 16  
17 1 Y 1 A ARG -3  ? A ARG 17  
18 1 Y 1 A GLY -2  ? A GLY 18  
19 1 Y 1 A SER -1  ? A SER 19  
20 1 Y 1 A HIS 0   ? A HIS 20  
21 1 Y 1 A MET 1   ? A MET 21  
22 1 Y 1 A ILE 2   ? A ILE 22  
23 1 Y 1 A PHE 3   ? A PHE 23  
24 1 Y 1 A LYS 4   ? A LYS 24  
25 1 Y 1 A GLU 5   ? A GLU 25  
26 1 Y 1 A LYS 6   ? A LYS 26  
27 1 Y 1 A SER 252 ? A SER 272 
28 1 Y 1 A THR 253 ? A THR 273 
29 1 Y 1 B MET -19 ? B MET 1   
30 1 Y 1 B GLY -18 ? B GLY 2   
31 1 Y 1 B SER -17 ? B SER 3   
32 1 Y 1 B SER -16 ? B SER 4   
33 1 Y 1 B HIS -15 ? B HIS 5   
34 1 Y 1 B HIS -14 ? B HIS 6   
35 1 Y 1 B HIS -13 ? B HIS 7   
36 1 Y 1 B HIS -12 ? B HIS 8   
37 1 Y 1 B HIS -11 ? B HIS 9   
38 1 Y 1 B HIS -10 ? B HIS 10  
39 1 Y 1 B SER -9  ? B SER 11  
40 1 Y 1 B SER -8  ? B SER 12  
41 1 Y 1 B GLY -7  ? B GLY 13  
42 1 Y 1 B LEU -6  ? B LEU 14  
43 1 Y 1 B VAL -5  ? B VAL 15  
44 1 Y 1 B PRO -4  ? B PRO 16  
45 1 Y 1 B ARG -3  ? B ARG 17  
46 1 Y 1 B GLY -2  ? B GLY 18  
47 1 Y 1 B SER -1  ? B SER 19  
48 1 Y 1 B HIS 0   ? B HIS 20  
49 1 Y 1 B MET 1   ? B MET 21  
50 1 Y 1 B ILE 2   ? B ILE 22  
51 1 Y 1 B PHE 3   ? B PHE 23  
52 1 Y 1 B LYS 4   ? B LYS 24  
53 1 Y 1 B GLU 5   ? B GLU 25  
54 1 Y 1 B LYS 6   ? B LYS 26  
55 1 Y 1 B ASN 7   ? B ASN 27  
56 1 Y 1 B SER 252 ? B SER 272 
57 1 Y 1 B THR 253 ? B THR 273 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
EDO C1     C N N 88  
EDO O1     O N N 89  
EDO C2     C N N 90  
EDO O2     O N N 91  
EDO H11    H N N 92  
EDO H12    H N N 93  
EDO HO1    H N N 94  
EDO H21    H N N 95  
EDO H22    H N N 96  
EDO HO2    H N N 97  
GLN N      N N N 98  
GLN CA     C N S 99  
GLN C      C N N 100 
GLN O      O N N 101 
GLN CB     C N N 102 
GLN CG     C N N 103 
GLN CD     C N N 104 
GLN OE1    O N N 105 
GLN NE2    N N N 106 
GLN OXT    O N N 107 
GLN H      H N N 108 
GLN H2     H N N 109 
GLN HA     H N N 110 
GLN HB2    H N N 111 
GLN HB3    H N N 112 
GLN HG2    H N N 113 
GLN HG3    H N N 114 
GLN HE21   H N N 115 
GLN HE22   H N N 116 
GLN HXT    H N N 117 
GLU N      N N N 118 
GLU CA     C N S 119 
GLU C      C N N 120 
GLU O      O N N 121 
GLU CB     C N N 122 
GLU CG     C N N 123 
GLU CD     C N N 124 
GLU OE1    O N N 125 
GLU OE2    O N N 126 
GLU OXT    O N N 127 
GLU H      H N N 128 
GLU H2     H N N 129 
GLU HA     H N N 130 
GLU HB2    H N N 131 
GLU HB3    H N N 132 
GLU HG2    H N N 133 
GLU HG3    H N N 134 
GLU HE2    H N N 135 
GLU HXT    H N N 136 
GLY N      N N N 137 
GLY CA     C N N 138 
GLY C      C N N 139 
GLY O      O N N 140 
GLY OXT    O N N 141 
GLY H      H N N 142 
GLY H2     H N N 143 
GLY HA2    H N N 144 
GLY HA3    H N N 145 
GLY HXT    H N N 146 
HIS N      N N N 147 
HIS CA     C N S 148 
HIS C      C N N 149 
HIS O      O N N 150 
HIS CB     C N N 151 
HIS CG     C Y N 152 
HIS ND1    N Y N 153 
HIS CD2    C Y N 154 
HIS CE1    C Y N 155 
HIS NE2    N Y N 156 
HIS OXT    O N N 157 
HIS H      H N N 158 
HIS H2     H N N 159 
HIS HA     H N N 160 
HIS HB2    H N N 161 
HIS HB3    H N N 162 
HIS HD1    H N N 163 
HIS HD2    H N N 164 
HIS HE1    H N N 165 
HIS HE2    H N N 166 
HIS HXT    H N N 167 
HOH O      O N N 168 
HOH H1     H N N 169 
HOH H2     H N N 170 
ILE N      N N N 171 
ILE CA     C N S 172 
ILE C      C N N 173 
ILE O      O N N 174 
ILE CB     C N S 175 
ILE CG1    C N N 176 
ILE CG2    C N N 177 
ILE CD1    C N N 178 
ILE OXT    O N N 179 
ILE H      H N N 180 
ILE H2     H N N 181 
ILE HA     H N N 182 
ILE HB     H N N 183 
ILE HG12   H N N 184 
ILE HG13   H N N 185 
ILE HG21   H N N 186 
ILE HG22   H N N 187 
ILE HG23   H N N 188 
ILE HD11   H N N 189 
ILE HD12   H N N 190 
ILE HD13   H N N 191 
ILE HXT    H N N 192 
LEU N      N N N 193 
LEU CA     C N S 194 
LEU C      C N N 195 
LEU O      O N N 196 
LEU CB     C N N 197 
LEU CG     C N N 198 
LEU CD1    C N N 199 
LEU CD2    C N N 200 
LEU OXT    O N N 201 
LEU H      H N N 202 
LEU H2     H N N 203 
LEU HA     H N N 204 
LEU HB2    H N N 205 
LEU HB3    H N N 206 
LEU HG     H N N 207 
LEU HD11   H N N 208 
LEU HD12   H N N 209 
LEU HD13   H N N 210 
LEU HD21   H N N 211 
LEU HD22   H N N 212 
LEU HD23   H N N 213 
LEU HXT    H N N 214 
LYS N      N N N 215 
LYS CA     C N S 216 
LYS C      C N N 217 
LYS O      O N N 218 
LYS CB     C N N 219 
LYS CG     C N N 220 
LYS CD     C N N 221 
LYS CE     C N N 222 
LYS NZ     N N N 223 
LYS OXT    O N N 224 
LYS H      H N N 225 
LYS H2     H N N 226 
LYS HA     H N N 227 
LYS HB2    H N N 228 
LYS HB3    H N N 229 
LYS HG2    H N N 230 
LYS HG3    H N N 231 
LYS HD2    H N N 232 
LYS HD3    H N N 233 
LYS HE2    H N N 234 
LYS HE3    H N N 235 
LYS HZ1    H N N 236 
LYS HZ2    H N N 237 
LYS HZ3    H N N 238 
LYS HXT    H N N 239 
MET N      N N N 240 
MET CA     C N S 241 
MET C      C N N 242 
MET O      O N N 243 
MET CB     C N N 244 
MET CG     C N N 245 
MET SD     S N N 246 
MET CE     C N N 247 
MET OXT    O N N 248 
MET H      H N N 249 
MET H2     H N N 250 
MET HA     H N N 251 
MET HB2    H N N 252 
MET HB3    H N N 253 
MET HG2    H N N 254 
MET HG3    H N N 255 
MET HE1    H N N 256 
MET HE2    H N N 257 
MET HE3    H N N 258 
MET HXT    H N N 259 
PHE N      N N N 260 
PHE CA     C N S 261 
PHE C      C N N 262 
PHE O      O N N 263 
PHE CB     C N N 264 
PHE CG     C Y N 265 
PHE CD1    C Y N 266 
PHE CD2    C Y N 267 
PHE CE1    C Y N 268 
PHE CE2    C Y N 269 
PHE CZ     C Y N 270 
PHE OXT    O N N 271 
PHE H      H N N 272 
PHE H2     H N N 273 
PHE HA     H N N 274 
PHE HB2    H N N 275 
PHE HB3    H N N 276 
PHE HD1    H N N 277 
PHE HD2    H N N 278 
PHE HE1    H N N 279 
PHE HE2    H N N 280 
PHE HZ     H N N 281 
PHE HXT    H N N 282 
PRO N      N N N 283 
PRO CA     C N S 284 
PRO C      C N N 285 
PRO O      O N N 286 
PRO CB     C N N 287 
PRO CG     C N N 288 
PRO CD     C N N 289 
PRO OXT    O N N 290 
PRO H      H N N 291 
PRO HA     H N N 292 
PRO HB2    H N N 293 
PRO HB3    H N N 294 
PRO HG2    H N N 295 
PRO HG3    H N N 296 
PRO HD2    H N N 297 
PRO HD3    H N N 298 
PRO HXT    H N N 299 
SAM N      N N N 300 
SAM CA     C N S 301 
SAM C      C N N 302 
SAM O      O N N 303 
SAM OXT    O N N 304 
SAM CB     C N N 305 
SAM CG     C N N 306 
SAM SD     S N S 307 
SAM CE     C N N 308 
SAM "C5'"  C N N 309 
SAM "C4'"  C N S 310 
SAM "O4'"  O N N 311 
SAM "C3'"  C N S 312 
SAM "O3'"  O N N 313 
SAM "C2'"  C N R 314 
SAM "O2'"  O N N 315 
SAM "C1'"  C N R 316 
SAM N9     N Y N 317 
SAM C8     C Y N 318 
SAM N7     N Y N 319 
SAM C5     C Y N 320 
SAM C6     C Y N 321 
SAM N6     N N N 322 
SAM N1     N Y N 323 
SAM C2     C Y N 324 
SAM N3     N Y N 325 
SAM C4     C Y N 326 
SAM HN1    H N N 327 
SAM HN2    H N N 328 
SAM HA     H N N 329 
SAM HB1    H N N 330 
SAM HB2    H N N 331 
SAM HG1    H N N 332 
SAM HG2    H N N 333 
SAM HE1    H N N 334 
SAM HE2    H N N 335 
SAM HE3    H N N 336 
SAM "H5'1" H N N 337 
SAM "H5'2" H N N 338 
SAM "H4'"  H N N 339 
SAM "H3'"  H N N 340 
SAM "HO3'" H N N 341 
SAM "H2'"  H N N 342 
SAM "HO2'" H N N 343 
SAM "H1'"  H N N 344 
SAM H8     H N N 345 
SAM HN61   H N N 346 
SAM HN62   H N N 347 
SAM H2     H N N 348 
SER N      N N N 349 
SER CA     C N S 350 
SER C      C N N 351 
SER O      O N N 352 
SER CB     C N N 353 
SER OG     O N N 354 
SER OXT    O N N 355 
SER H      H N N 356 
SER H2     H N N 357 
SER HA     H N N 358 
SER HB2    H N N 359 
SER HB3    H N N 360 
SER HG     H N N 361 
SER HXT    H N N 362 
THR N      N N N 363 
THR CA     C N S 364 
THR C      C N N 365 
THR O      O N N 366 
THR CB     C N R 367 
THR OG1    O N N 368 
THR CG2    C N N 369 
THR OXT    O N N 370 
THR H      H N N 371 
THR H2     H N N 372 
THR HA     H N N 373 
THR HB     H N N 374 
THR HG1    H N N 375 
THR HG21   H N N 376 
THR HG22   H N N 377 
THR HG23   H N N 378 
THR HXT    H N N 379 
TRP N      N N N 380 
TRP CA     C N S 381 
TRP C      C N N 382 
TRP O      O N N 383 
TRP CB     C N N 384 
TRP CG     C Y N 385 
TRP CD1    C Y N 386 
TRP CD2    C Y N 387 
TRP NE1    N Y N 388 
TRP CE2    C Y N 389 
TRP CE3    C Y N 390 
TRP CZ2    C Y N 391 
TRP CZ3    C Y N 392 
TRP CH2    C Y N 393 
TRP OXT    O N N 394 
TRP H      H N N 395 
TRP H2     H N N 396 
TRP HA     H N N 397 
TRP HB2    H N N 398 
TRP HB3    H N N 399 
TRP HD1    H N N 400 
TRP HE1    H N N 401 
TRP HE3    H N N 402 
TRP HZ2    H N N 403 
TRP HZ3    H N N 404 
TRP HH2    H N N 405 
TRP HXT    H N N 406 
TRS C      C N N 407 
TRS C1     C N N 408 
TRS C2     C N N 409 
TRS C3     C N N 410 
TRS N      N N N 411 
TRS O1     O N N 412 
TRS O2     O N N 413 
TRS O3     O N N 414 
TRS H11    H N N 415 
TRS H12    H N N 416 
TRS H21    H N N 417 
TRS H22    H N N 418 
TRS H31    H N N 419 
TRS H32    H N N 420 
TRS HN1    H N N 421 
TRS HN2    H N N 422 
TRS HN3    H N N 423 
TRS HO1    H N N 424 
TRS HO2    H N N 425 
TRS HO3    H N N 426 
TYR N      N N N 427 
TYR CA     C N S 428 
TYR C      C N N 429 
TYR O      O N N 430 
TYR CB     C N N 431 
TYR CG     C Y N 432 
TYR CD1    C Y N 433 
TYR CD2    C Y N 434 
TYR CE1    C Y N 435 
TYR CE2    C Y N 436 
TYR CZ     C Y N 437 
TYR OH     O N N 438 
TYR OXT    O N N 439 
TYR H      H N N 440 
TYR H2     H N N 441 
TYR HA     H N N 442 
TYR HB2    H N N 443 
TYR HB3    H N N 444 
TYR HD1    H N N 445 
TYR HD2    H N N 446 
TYR HE1    H N N 447 
TYR HE2    H N N 448 
TYR HH     H N N 449 
TYR HXT    H N N 450 
VAL N      N N N 451 
VAL CA     C N S 452 
VAL C      C N N 453 
VAL O      O N N 454 
VAL CB     C N N 455 
VAL CG1    C N N 456 
VAL CG2    C N N 457 
VAL OXT    O N N 458 
VAL H      H N N 459 
VAL H2     H N N 460 
VAL HA     H N N 461 
VAL HB     H N N 462 
VAL HG11   H N N 463 
VAL HG12   H N N 464 
VAL HG13   H N N 465 
VAL HG21   H N N 466 
VAL HG22   H N N 467 
VAL HG23   H N N 468 
VAL HXT    H N N 469 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
EDO C1    O1     sing N N 83  
EDO C1    C2     sing N N 84  
EDO C1    H11    sing N N 85  
EDO C1    H12    sing N N 86  
EDO O1    HO1    sing N N 87  
EDO C2    O2     sing N N 88  
EDO C2    H21    sing N N 89  
EDO C2    H22    sing N N 90  
EDO O2    HO2    sing N N 91  
GLN N     CA     sing N N 92  
GLN N     H      sing N N 93  
GLN N     H2     sing N N 94  
GLN CA    C      sing N N 95  
GLN CA    CB     sing N N 96  
GLN CA    HA     sing N N 97  
GLN C     O      doub N N 98  
GLN C     OXT    sing N N 99  
GLN CB    CG     sing N N 100 
GLN CB    HB2    sing N N 101 
GLN CB    HB3    sing N N 102 
GLN CG    CD     sing N N 103 
GLN CG    HG2    sing N N 104 
GLN CG    HG3    sing N N 105 
GLN CD    OE1    doub N N 106 
GLN CD    NE2    sing N N 107 
GLN NE2   HE21   sing N N 108 
GLN NE2   HE22   sing N N 109 
GLN OXT   HXT    sing N N 110 
GLU N     CA     sing N N 111 
GLU N     H      sing N N 112 
GLU N     H2     sing N N 113 
GLU CA    C      sing N N 114 
GLU CA    CB     sing N N 115 
GLU CA    HA     sing N N 116 
GLU C     O      doub N N 117 
GLU C     OXT    sing N N 118 
GLU CB    CG     sing N N 119 
GLU CB    HB2    sing N N 120 
GLU CB    HB3    sing N N 121 
GLU CG    CD     sing N N 122 
GLU CG    HG2    sing N N 123 
GLU CG    HG3    sing N N 124 
GLU CD    OE1    doub N N 125 
GLU CD    OE2    sing N N 126 
GLU OE2   HE2    sing N N 127 
GLU OXT   HXT    sing N N 128 
GLY N     CA     sing N N 129 
GLY N     H      sing N N 130 
GLY N     H2     sing N N 131 
GLY CA    C      sing N N 132 
GLY CA    HA2    sing N N 133 
GLY CA    HA3    sing N N 134 
GLY C     O      doub N N 135 
GLY C     OXT    sing N N 136 
GLY OXT   HXT    sing N N 137 
HIS N     CA     sing N N 138 
HIS N     H      sing N N 139 
HIS N     H2     sing N N 140 
HIS CA    C      sing N N 141 
HIS CA    CB     sing N N 142 
HIS CA    HA     sing N N 143 
HIS C     O      doub N N 144 
HIS C     OXT    sing N N 145 
HIS CB    CG     sing N N 146 
HIS CB    HB2    sing N N 147 
HIS CB    HB3    sing N N 148 
HIS CG    ND1    sing Y N 149 
HIS CG    CD2    doub Y N 150 
HIS ND1   CE1    doub Y N 151 
HIS ND1   HD1    sing N N 152 
HIS CD2   NE2    sing Y N 153 
HIS CD2   HD2    sing N N 154 
HIS CE1   NE2    sing Y N 155 
HIS CE1   HE1    sing N N 156 
HIS NE2   HE2    sing N N 157 
HIS OXT   HXT    sing N N 158 
HOH O     H1     sing N N 159 
HOH O     H2     sing N N 160 
ILE N     CA     sing N N 161 
ILE N     H      sing N N 162 
ILE N     H2     sing N N 163 
ILE CA    C      sing N N 164 
ILE CA    CB     sing N N 165 
ILE CA    HA     sing N N 166 
ILE C     O      doub N N 167 
ILE C     OXT    sing N N 168 
ILE CB    CG1    sing N N 169 
ILE CB    CG2    sing N N 170 
ILE CB    HB     sing N N 171 
ILE CG1   CD1    sing N N 172 
ILE CG1   HG12   sing N N 173 
ILE CG1   HG13   sing N N 174 
ILE CG2   HG21   sing N N 175 
ILE CG2   HG22   sing N N 176 
ILE CG2   HG23   sing N N 177 
ILE CD1   HD11   sing N N 178 
ILE CD1   HD12   sing N N 179 
ILE CD1   HD13   sing N N 180 
ILE OXT   HXT    sing N N 181 
LEU N     CA     sing N N 182 
LEU N     H      sing N N 183 
LEU N     H2     sing N N 184 
LEU CA    C      sing N N 185 
LEU CA    CB     sing N N 186 
LEU CA    HA     sing N N 187 
LEU C     O      doub N N 188 
LEU C     OXT    sing N N 189 
LEU CB    CG     sing N N 190 
LEU CB    HB2    sing N N 191 
LEU CB    HB3    sing N N 192 
LEU CG    CD1    sing N N 193 
LEU CG    CD2    sing N N 194 
LEU CG    HG     sing N N 195 
LEU CD1   HD11   sing N N 196 
LEU CD1   HD12   sing N N 197 
LEU CD1   HD13   sing N N 198 
LEU CD2   HD21   sing N N 199 
LEU CD2   HD22   sing N N 200 
LEU CD2   HD23   sing N N 201 
LEU OXT   HXT    sing N N 202 
LYS N     CA     sing N N 203 
LYS N     H      sing N N 204 
LYS N     H2     sing N N 205 
LYS CA    C      sing N N 206 
LYS CA    CB     sing N N 207 
LYS CA    HA     sing N N 208 
LYS C     O      doub N N 209 
LYS C     OXT    sing N N 210 
LYS CB    CG     sing N N 211 
LYS CB    HB2    sing N N 212 
LYS CB    HB3    sing N N 213 
LYS CG    CD     sing N N 214 
LYS CG    HG2    sing N N 215 
LYS CG    HG3    sing N N 216 
LYS CD    CE     sing N N 217 
LYS CD    HD2    sing N N 218 
LYS CD    HD3    sing N N 219 
LYS CE    NZ     sing N N 220 
LYS CE    HE2    sing N N 221 
LYS CE    HE3    sing N N 222 
LYS NZ    HZ1    sing N N 223 
LYS NZ    HZ2    sing N N 224 
LYS NZ    HZ3    sing N N 225 
LYS OXT   HXT    sing N N 226 
MET N     CA     sing N N 227 
MET N     H      sing N N 228 
MET N     H2     sing N N 229 
MET CA    C      sing N N 230 
MET CA    CB     sing N N 231 
MET CA    HA     sing N N 232 
MET C     O      doub N N 233 
MET C     OXT    sing N N 234 
MET CB    CG     sing N N 235 
MET CB    HB2    sing N N 236 
MET CB    HB3    sing N N 237 
MET CG    SD     sing N N 238 
MET CG    HG2    sing N N 239 
MET CG    HG3    sing N N 240 
MET SD    CE     sing N N 241 
MET CE    HE1    sing N N 242 
MET CE    HE2    sing N N 243 
MET CE    HE3    sing N N 244 
MET OXT   HXT    sing N N 245 
PHE N     CA     sing N N 246 
PHE N     H      sing N N 247 
PHE N     H2     sing N N 248 
PHE CA    C      sing N N 249 
PHE CA    CB     sing N N 250 
PHE CA    HA     sing N N 251 
PHE C     O      doub N N 252 
PHE C     OXT    sing N N 253 
PHE CB    CG     sing N N 254 
PHE CB    HB2    sing N N 255 
PHE CB    HB3    sing N N 256 
PHE CG    CD1    doub Y N 257 
PHE CG    CD2    sing Y N 258 
PHE CD1   CE1    sing Y N 259 
PHE CD1   HD1    sing N N 260 
PHE CD2   CE2    doub Y N 261 
PHE CD2   HD2    sing N N 262 
PHE CE1   CZ     doub Y N 263 
PHE CE1   HE1    sing N N 264 
PHE CE2   CZ     sing Y N 265 
PHE CE2   HE2    sing N N 266 
PHE CZ    HZ     sing N N 267 
PHE OXT   HXT    sing N N 268 
PRO N     CA     sing N N 269 
PRO N     CD     sing N N 270 
PRO N     H      sing N N 271 
PRO CA    C      sing N N 272 
PRO CA    CB     sing N N 273 
PRO CA    HA     sing N N 274 
PRO C     O      doub N N 275 
PRO C     OXT    sing N N 276 
PRO CB    CG     sing N N 277 
PRO CB    HB2    sing N N 278 
PRO CB    HB3    sing N N 279 
PRO CG    CD     sing N N 280 
PRO CG    HG2    sing N N 281 
PRO CG    HG3    sing N N 282 
PRO CD    HD2    sing N N 283 
PRO CD    HD3    sing N N 284 
PRO OXT   HXT    sing N N 285 
SAM N     CA     sing N N 286 
SAM N     HN1    sing N N 287 
SAM N     HN2    sing N N 288 
SAM CA    C      sing N N 289 
SAM CA    CB     sing N N 290 
SAM CA    HA     sing N N 291 
SAM C     O      doub N N 292 
SAM C     OXT    sing N N 293 
SAM CB    CG     sing N N 294 
SAM CB    HB1    sing N N 295 
SAM CB    HB2    sing N N 296 
SAM CG    SD     sing N N 297 
SAM CG    HG1    sing N N 298 
SAM CG    HG2    sing N N 299 
SAM SD    CE     sing N N 300 
SAM SD    "C5'"  sing N N 301 
SAM CE    HE1    sing N N 302 
SAM CE    HE2    sing N N 303 
SAM CE    HE3    sing N N 304 
SAM "C5'" "C4'"  sing N N 305 
SAM "C5'" "H5'1" sing N N 306 
SAM "C5'" "H5'2" sing N N 307 
SAM "C4'" "O4'"  sing N N 308 
SAM "C4'" "C3'"  sing N N 309 
SAM "C4'" "H4'"  sing N N 310 
SAM "O4'" "C1'"  sing N N 311 
SAM "C3'" "O3'"  sing N N 312 
SAM "C3'" "C2'"  sing N N 313 
SAM "C3'" "H3'"  sing N N 314 
SAM "O3'" "HO3'" sing N N 315 
SAM "C2'" "O2'"  sing N N 316 
SAM "C2'" "C1'"  sing N N 317 
SAM "C2'" "H2'"  sing N N 318 
SAM "O2'" "HO2'" sing N N 319 
SAM "C1'" N9     sing N N 320 
SAM "C1'" "H1'"  sing N N 321 
SAM N9    C8     sing Y N 322 
SAM N9    C4     sing Y N 323 
SAM C8    N7     doub Y N 324 
SAM C8    H8     sing N N 325 
SAM N7    C5     sing Y N 326 
SAM C5    C6     sing Y N 327 
SAM C5    C4     doub Y N 328 
SAM C6    N6     sing N N 329 
SAM C6    N1     doub Y N 330 
SAM N6    HN61   sing N N 331 
SAM N6    HN62   sing N N 332 
SAM N1    C2     sing Y N 333 
SAM C2    N3     doub Y N 334 
SAM C2    H2     sing N N 335 
SAM N3    C4     sing Y N 336 
SER N     CA     sing N N 337 
SER N     H      sing N N 338 
SER N     H2     sing N N 339 
SER CA    C      sing N N 340 
SER CA    CB     sing N N 341 
SER CA    HA     sing N N 342 
SER C     O      doub N N 343 
SER C     OXT    sing N N 344 
SER CB    OG     sing N N 345 
SER CB    HB2    sing N N 346 
SER CB    HB3    sing N N 347 
SER OG    HG     sing N N 348 
SER OXT   HXT    sing N N 349 
THR N     CA     sing N N 350 
THR N     H      sing N N 351 
THR N     H2     sing N N 352 
THR CA    C      sing N N 353 
THR CA    CB     sing N N 354 
THR CA    HA     sing N N 355 
THR C     O      doub N N 356 
THR C     OXT    sing N N 357 
THR CB    OG1    sing N N 358 
THR CB    CG2    sing N N 359 
THR CB    HB     sing N N 360 
THR OG1   HG1    sing N N 361 
THR CG2   HG21   sing N N 362 
THR CG2   HG22   sing N N 363 
THR CG2   HG23   sing N N 364 
THR OXT   HXT    sing N N 365 
TRP N     CA     sing N N 366 
TRP N     H      sing N N 367 
TRP N     H2     sing N N 368 
TRP CA    C      sing N N 369 
TRP CA    CB     sing N N 370 
TRP CA    HA     sing N N 371 
TRP C     O      doub N N 372 
TRP C     OXT    sing N N 373 
TRP CB    CG     sing N N 374 
TRP CB    HB2    sing N N 375 
TRP CB    HB3    sing N N 376 
TRP CG    CD1    doub Y N 377 
TRP CG    CD2    sing Y N 378 
TRP CD1   NE1    sing Y N 379 
TRP CD1   HD1    sing N N 380 
TRP CD2   CE2    doub Y N 381 
TRP CD2   CE3    sing Y N 382 
TRP NE1   CE2    sing Y N 383 
TRP NE1   HE1    sing N N 384 
TRP CE2   CZ2    sing Y N 385 
TRP CE3   CZ3    doub Y N 386 
TRP CE3   HE3    sing N N 387 
TRP CZ2   CH2    doub Y N 388 
TRP CZ2   HZ2    sing N N 389 
TRP CZ3   CH2    sing Y N 390 
TRP CZ3   HZ3    sing N N 391 
TRP CH2   HH2    sing N N 392 
TRP OXT   HXT    sing N N 393 
TRS C     C1     sing N N 394 
TRS C     C2     sing N N 395 
TRS C     C3     sing N N 396 
TRS C     N      sing N N 397 
TRS C1    O1     sing N N 398 
TRS C1    H11    sing N N 399 
TRS C1    H12    sing N N 400 
TRS C2    O2     sing N N 401 
TRS C2    H21    sing N N 402 
TRS C2    H22    sing N N 403 
TRS C3    O3     sing N N 404 
TRS C3    H31    sing N N 405 
TRS C3    H32    sing N N 406 
TRS N     HN1    sing N N 407 
TRS N     HN2    sing N N 408 
TRS N     HN3    sing N N 409 
TRS O1    HO1    sing N N 410 
TRS O2    HO2    sing N N 411 
TRS O3    HO3    sing N N 412 
TYR N     CA     sing N N 413 
TYR N     H      sing N N 414 
TYR N     H2     sing N N 415 
TYR CA    C      sing N N 416 
TYR CA    CB     sing N N 417 
TYR CA    HA     sing N N 418 
TYR C     O      doub N N 419 
TYR C     OXT    sing N N 420 
TYR CB    CG     sing N N 421 
TYR CB    HB2    sing N N 422 
TYR CB    HB3    sing N N 423 
TYR CG    CD1    doub Y N 424 
TYR CG    CD2    sing Y N 425 
TYR CD1   CE1    sing Y N 426 
TYR CD1   HD1    sing N N 427 
TYR CD2   CE2    doub Y N 428 
TYR CD2   HD2    sing N N 429 
TYR CE1   CZ     doub Y N 430 
TYR CE1   HE1    sing N N 431 
TYR CE2   CZ     sing Y N 432 
TYR CE2   HE2    sing N N 433 
TYR CZ    OH     sing N N 434 
TYR OH    HH     sing N N 435 
TYR OXT   HXT    sing N N 436 
VAL N     CA     sing N N 437 
VAL N     H      sing N N 438 
VAL N     H2     sing N N 439 
VAL CA    C      sing N N 440 
VAL CA    CB     sing N N 441 
VAL CA    HA     sing N N 442 
VAL C     O      doub N N 443 
VAL C     OXT    sing N N 444 
VAL CB    CG1    sing N N 445 
VAL CB    CG2    sing N N 446 
VAL CB    HB     sing N N 447 
VAL CG1   HG11   sing N N 448 
VAL CG1   HG12   sing N N 449 
VAL CG1   HG13   sing N N 450 
VAL CG2   HG21   sing N N 451 
VAL CG2   HG22   sing N N 452 
VAL CG2   HG23   sing N N 453 
VAL OXT   HXT    sing N N 454 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)'                                         'United States' 1937971  1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM147557 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BXL 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.014253 
_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]   0.010844 
_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]   0.010417 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
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.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 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     . ASN A 1 27  ? -23.60500 -6.04700  19.70100 1.000 54.08208 ?  7   ASN A N     1 
ATOM   2    C CA    . ASN A 1 27  ? -22.27600 -6.47100  20.21000 1.000 50.65522 ?  7   ASN A CA    1 
ATOM   3    C C     . ASN A 1 27  ? -21.73300 -7.58600  19.32200 1.000 45.11467 ?  7   ASN A C     1 
ATOM   4    O O     . ASN A 1 27  ? -22.34200 -8.66300  19.28800 1.000 47.47572 ?  7   ASN A O     1 
ATOM   5    C CB    . ASN A 1 27  ? -22.30900 -6.89900  21.68000 1.000 47.30588 ?  7   ASN A CB    1 
ATOM   6    C CG    . ASN A 1 27  ? -20.94800 -7.22500  22.25700 1.000 46.43816 ?  7   ASN A CG    1 
ATOM   7    O OD1   . ASN A 1 27  ? -19.92400 -6.79200  21.73700 1.000 46.90426 ?  7   ASN A OD1   1 
ATOM   8    N ND2   . ASN A 1 27  ? -20.92800 -7.98300  23.34200 1.000 47.53862 ?  7   ASN A ND2   1 
ATOM   9    N N     . ILE A 1 28  ? -20.61900 -7.32100  18.65400 1.000 45.63289 ?  8   ILE A N     1 
ATOM   10   C CA    . ILE A 1 28  ? -19.95700 -8.34900  17.80600 1.000 47.00391 ?  8   ILE A CA    1 
ATOM   11   C C     . ILE A 1 28  ? -19.62300 -9.56900  18.67100 1.000 43.11685 ?  8   ILE A C     1 
ATOM   12   O O     . ILE A 1 28  ? -19.75700 -10.68500 18.17100 1.000 44.09390 ?  8   ILE A O     1 
ATOM   13   C CB    . ILE A 1 28  ? -18.70500 -7.74600  17.13500 1.000 45.78881 ?  8   ILE A CB    1 
ATOM   14   C CG1   . ILE A 1 28  ? -18.04100 -8.74300  16.18400 1.000 44.89015 ?  8   ILE A CG1   1 
ATOM   15   C CG2   . ILE A 1 28  ? -17.72700 -7.20400  18.16600 1.000 40.48684 ?  8   ILE A CG2   1 
ATOM   16   C CD1   . ILE A 1 28  ? -18.95800 -9.23700  15.09600 1.000 48.03715 ?  8   ILE A CD1   1 
ATOM   17   N N     . TYR A 1 29  ? -19.27500 -9.36300  19.93600 1.000 38.52492 ?  9   TYR A N     1 
ATOM   18   C CA    . TYR A 1 29  ? -18.83000 -10.47900 20.80600 1.000 39.64219 ?  9   TYR A CA    1 
ATOM   19   C C     . TYR A 1 29  ? -19.99900 -11.41600 21.14900 1.000 39.70040 ?  9   TYR A C     1 
ATOM   20   O O     . TYR A 1 29  ? -19.74300 -12.47200 21.72700 1.000 36.72532 ?  9   TYR A O     1 
ATOM   21   C CB    . TYR A 1 29  ? -18.12800 -9.88300  22.02700 1.000 37.54349 ?  9   TYR A CB    1 
ATOM   22   C CG    . TYR A 1 29  ? -16.78500 -9.25800  21.75800 1.000 36.87968 ?  9   TYR A CG    1 
ATOM   23   C CD1   . TYR A 1 29  ? -15.79600 -9.94900  21.07800 1.000 35.85325 ?  9   TYR A CD1   1 
ATOM   24   C CD2   . TYR A 1 29  ? -16.49400 -7.98000  22.19900 1.000 38.29789 ?  9   TYR A CD2   1 
ATOM   25   C CE1   . TYR A 1 29  ? -14.55600 -9.38500  20.83900 1.000 31.42487 ?  9   TYR A CE1   1 
ATOM   26   C CE2   . TYR A 1 29  ? -15.25700 -7.40200  21.97300 1.000 35.26484 ?  9   TYR A CE2   1 
ATOM   27   C CZ    . TYR A 1 29  ? -14.28500 -8.10800  21.29200 1.000 36.47864 ?  9   TYR A CZ    1 
ATOM   28   O OH    . TYR A 1 29  ? -13.06300 -7.54000  21.06400 1.000 34.84717 ?  9   TYR A OH    1 
ATOM   29   N N     . GLU A 1 30  ? -21.22900 -11.04600 20.77500 1.000 41.00657 ?  10  GLU A N     1 
ATOM   30   C CA    . GLU A 1 30  ? -22.42900 -11.88600 21.03600 1.000 38.57925 ?  10  GLU A CA    1 
ATOM   31   C C     . GLU A 1 30  ? -22.76900 -12.74700 19.80800 1.000 41.79074 ?  10  GLU A C     1 
ATOM   32   O O     . GLU A 1 30  ? -23.63800 -13.61000 19.93200 1.000 40.52708 ?  10  GLU A O     1 
ATOM   33   C CB    . GLU A 1 30  ? -23.59100 -10.99100 21.46700 1.000 36.35905 ?  10  GLU A CB    1 
ATOM   34   C CG    . GLU A 1 30  ? -23.41100 -10.40200 22.85300 1.000 37.12113 ?  10  GLU A CG    1 
ATOM   35   C CD    . GLU A 1 30  ? -23.77200 -11.31200 24.01300 1.000 36.11358 ?  10  GLU A CD    1 
ATOM   36   O OE1   . GLU A 1 30  ? -24.02500 -12.50300 23.78000 1.000 35.78736 ?  10  GLU A OE1   1 
ATOM   37   O OE2   . GLU A 1 30  ? -23.80700 -10.82100 25.14900 1.000 39.21090 -1 10  GLU A OE2   1 
ATOM   38   N N     . THR A 1 31  ? -22.06900 -12.56000 18.68900 1.000 39.30248 ?  11  THR A N     1 
ATOM   39   C CA    . THR A 1 31  ? -22.38300 -13.29000 17.43200 1.000 40.37217 ?  11  THR A CA    1 
ATOM   40   C C     . THR A 1 31  ? -21.74500 -14.68700 17.40000 1.000 40.54600 ?  11  THR A C     1 
ATOM   41   O O     . THR A 1 31  ? -20.70700 -14.88900 18.03200 1.000 38.77049 ?  11  THR A O     1 
ATOM   42   C CB    . THR A 1 31  ? -21.95600 -12.47400 16.20500 1.000 42.15966 ?  11  THR A CB    1 
ATOM   43   O OG1   . THR A 1 31  ? -20.53600 -12.54200 16.07600 1.000 40.64649 ?  11  THR A OG1   1 
ATOM   44   C CG2   . THR A 1 31  ? -22.40700 -11.03200 16.27700 1.000 43.18613 ?  11  THR A CG2   1 
ATOM   45   N N     . ASP A 1 32  ? -22.35900 -15.60200 16.66000 1.000 36.16602 ?  12  ASP A N     1 
ATOM   46   C CA    . ASP A 1 32  ? -21.82700 -16.95600 16.61000 1.000 35.94206 ?  12  ASP A CA    1 
ATOM   47   C C     . ASP A 1 32  ? -20.49800 -17.00500 15.86800 1.000 36.45591 ?  12  ASP A C     1 
ATOM   48   O O     . ASP A 1 32  ? -19.62000 -17.80200 16.22700 1.000 36.18145 ?  12  ASP A O     1 
ATOM   49   C CB    . ASP A 1 32  ? -22.83300 -17.90000 15.94800 1.000 34.45627 ?  12  ASP A CB    1 
ATOM   50   N N     . GLU A 1 33  ? -20.32600 -16.16600 14.84100 1.000 36.42855 ?  13  GLU A N     1 
ATOM   51   C CA    . GLU A 1 33  ? -19.04200 -16.10300 14.14600 1.000 36.77193 ?  13  GLU A CA    1 
ATOM   52   C C     . GLU A 1 33  ? -17.92900 -15.69500 15.10300 1.000 35.65500 ?  13  GLU A C     1 
ATOM   53   O O     . GLU A 1 33  ? -16.81900 -16.24500 15.05900 1.000 33.16913 ?  13  GLU A O     1 
ATOM   54   C CB    . GLU A 1 33  ? -19.12800 -15.12900 12.96800 1.000 36.08952 ?  13  GLU A CB    1 
ATOM   55   N N     . SER A 1 34  ? -18.22700 -14.75600 16.00000 1.000 30.45214 ?  14  SER A N     1 
ATOM   56   C CA    . SER A 1 34  ? -17.25900 -14.34500 17.00500 1.000 34.89126 ?  14  SER A CA    1 
ATOM   57   C C     . SER A 1 34  ? -17.00000 -15.46400 18.00400 1.000 31.94355 ?  14  SER A C     1 
ATOM   58   O O     . SER A 1 34  ? -15.85100 -15.70000 18.39300 1.000 30.35540 ?  14  SER A O     1 
ATOM   59   C CB    . SER A 1 34  ? -17.74900 -13.08100 17.71300 1.000 32.55322 ?  14  SER A CB    1 
ATOM   60   O OG    . SER A 1 34  ? -16.74500 -12.56300 18.56500 1.000 40.14033 ?  14  SER A OG    1 
ATOM   61   N N     . VAL A 1 35  ? -18.05500 -16.16800 18.42400 1.000 31.33929 ?  15  VAL A N     1 
ATOM   62   C CA    . VAL A 1 35  ? -17.87600 -17.33100 19.29000 1.000 31.11086 ?  15  VAL A CA    1 
ATOM   63   C C     . VAL A 1 35  ? -16.98300 -18.36000 18.60700 1.000 28.18147 ?  15  VAL A C     1 
ATOM   64   O O     . VAL A 1 35  ? -16.04200 -18.89100 19.20900 1.000 27.05315 ?  15  VAL A O     1 
ATOM   65   C CB    . VAL A 1 35  ? -19.24100 -17.93100 19.67800 1.000 31.98371 ?  15  VAL A CB    1 
ATOM   66   C CG1   . VAL A 1 35  ? -19.06300 -19.27600 20.36900 1.000 31.34558 ?  15  VAL A CG1   1 
ATOM   67   C CG2   . VAL A 1 35  ? -19.99500 -16.96100 20.58100 1.000 33.38585 ?  15  VAL A CG2   1 
ATOM   68   N N     . SER A 1 36  ? -17.25800 -18.64500 17.33200 1.000 29.82539 ?  16  SER A N     1 
ATOM   69   C CA    . SER A 1 36  ? -16.45000 -19.61500 16.60000 1.000 30.98041 ?  16  SER A CA    1 
ATOM   70   C C     . SER A 1 36  ? -15.01100 -19.14500 16.46300 1.000 28.61661 ?  16  SER A C     1 
ATOM   71   O O     . SER A 1 36  ? -14.07800 -19.94100 16.60800 1.000 30.43806 ?  16  SER A O     1 
ATOM   72   C CB    . SER A 1 36  ? -17.05900 -19.88200 15.22200 1.000 31.52481 ?  16  SER A CB    1 
ATOM   73   O OG    . SER A 1 36  ? -18.02200 -20.91900 15.29000 1.000 36.32509 ?  16  SER A OG    1 
ATOM   74   N N     . GLN A 1 37  ? -14.81200 -17.85400 16.19000 1.000 26.31727 ?  17  GLN A N     1 
ATOM   75   C CA    . GLN A 1 37  ? -13.45600 -17.33000 16.04500 1.000 28.32707 ?  17  GLN A CA    1 
ATOM   76   C C     . GLN A 1 37  ? -12.64900 -17.50400 17.32500 1.000 26.43567 ?  17  GLN A C     1 
ATOM   77   O O     . GLN A 1 37  ? -11.47400 -17.88200 17.27500 1.000 28.08091 ?  17  GLN A O     1 
ATOM   78   C CB    . GLN A 1 37  ? -13.48700 -15.85400 15.63900 1.000 27.62074 ?  17  GLN A CB    1 
ATOM   79   C CG    . GLN A 1 37  ? -12.09200 -15.30900 15.35100 1.000 29.57074 ?  17  GLN A CG    1 
ATOM   80   C CD    . GLN A 1 37  ? -12.08800 -13.87600 14.84900 1.000 33.49411 ?  17  GLN A CD    1 
ATOM   81   O OE1   . GLN A 1 37  ? -12.74400 -13.00000 15.41600 1.000 31.14279 ?  17  GLN A OE1   1 
ATOM   82   N NE2   . GLN A 1 37  ? -11.34400 -13.63200 13.77400 1.000 33.50440 ?  17  GLN A NE2   1 
ATOM   83   N N     . TYR A 1 38  ? -13.26300 -17.24500 18.48400 1.000 26.12383 ?  18  TYR A N     1 
ATOM   84   C CA    . TYR A 1 38  ? -12.53600 -17.36900 19.74200 1.000 26.24520 ?  18  TYR A CA    1 
ATOM   85   C C     . TYR A 1 38  ? -12.39900 -18.82000 20.20100 1.000 27.52607 ?  18  TYR A C     1 
ATOM   86   O O     . TYR A 1 38  ? -11.41600 -19.16100 20.88000 1.000 24.02210 ?  18  TYR A O     1 
ATOM   87   C CB    . TYR A 1 38  ? -13.19300 -16.49400 20.81600 1.000 22.95907 ?  18  TYR A CB    1 
ATOM   88   C CG    . TYR A 1 38  ? -12.58500 -15.11300 20.77700 1.000 27.17525 ?  18  TYR A CG    1 
ATOM   89   C CD1   . TYR A 1 38  ? -11.40100 -14.84100 21.45600 1.000 28.03440 ?  18  TYR A CD1   1 
ATOM   90   C CD2   . TYR A 1 38  ? -13.14300 -14.10100 19.99900 1.000 27.17401 ?  18  TYR A CD2   1 
ATOM   91   C CE1   . TYR A 1 38  ? -10.80800 -13.59900 21.39000 1.000 25.90103 ?  18  TYR A CE1   1 
ATOM   92   C CE2   . TYR A 1 38  ? -12.55300 -12.84500 19.92800 1.000 30.68503 ?  18  TYR A CE2   1 
ATOM   93   C CZ    . TYR A 1 38  ? -11.38300 -12.60500 20.63000 1.000 30.97716 ?  18  TYR A CZ    1 
ATOM   94   O OH    . TYR A 1 38  ? -10.77500 -11.37200 20.56900 1.000 30.16651 ?  18  TYR A OH    1 
ATOM   95   N N     . CYS A 1 39  ? -13.35000 -19.69000 19.85200 1.000 23.72250 ?  19  CYS A N     1 
ATOM   96   C CA    . CYS A 1 39  ? -13.13800 -21.11900 20.08100 1.000 24.22084 ?  19  CYS A CA    1 
ATOM   97   C C     . CYS A 1 39  ? -11.87800 -21.59100 19.36300 1.000 26.13136 ?  19  CYS A C     1 
ATOM   98   O O     . CYS A 1 39  ? -11.04700 -22.30300 19.93500 1.000 25.23972 ?  19  CYS A O     1 
ATOM   99   C CB    . CYS A 1 39  ? -14.34800 -21.92100 19.59300 1.000 24.94980 ?  19  CYS A CB    1 
ATOM   100  S SG    . CYS A 1 39  ? -15.78900 -21.83100 20.65400 1.000 26.87064 ?  19  CYS A SG    1 
ATOM   101  N N     . ASP A 1 40  ? -11.72300 -21.18400 18.10100 1.000 24.26166 ?  20  ASP A N     1 
ATOM   102  C CA    . ASP A 1 40  ? -10.57200 -21.59000 17.30200 1.000 28.83095 ?  20  ASP A CA    1 
ATOM   103  C C     . ASP A 1 40  ? -9.27500  -21.02200 17.86800 1.000 27.19518 ?  20  ASP A C     1 
ATOM   104  O O     . ASP A 1 40  ? -8.29500  -21.75000 18.07100 1.000 25.78291 ?  20  ASP A O     1 
ATOM   105  C CB    . ASP A 1 40  ? -10.79000 -21.13400 15.85900 1.000 26.99851 ?  20  ASP A CB    1 
ATOM   106  C CG    . ASP A 1 40  ? -9.79000  -21.73200 14.90800 1.000 31.80494 ?  20  ASP A CG    1 
ATOM   107  O OD1   . ASP A 1 40  ? -9.72100  -22.96700 14.82900 1.000 33.28323 ?  20  ASP A OD1   1 
ATOM   108  O OD2   . ASP A 1 40  ? -9.06700  -20.97100 14.23600 1.000 37.43810 -1 20  ASP A OD2   1 
ATOM   109  N N     . PHE A 1 41  ? -9.26300  -19.71300 18.13400 1.000 25.53592 ?  21  PHE A N     1 
ATOM   110  C CA    . PHE A 1 41  ? -8.10800  -19.04700 18.73300 1.000 26.60281 ?  21  PHE A CA    1 
ATOM   111  C C     . PHE A 1 41  ? -7.70100  -19.68800 20.05400 1.000 26.30667 ?  21  PHE A C     1 
ATOM   112  O O     . PHE A 1 41  ? -6.50800  -19.87700 20.32400 1.000 24.06151 ?  21  PHE A O     1 
ATOM   113  C CB    . PHE A 1 41  ? -8.45200  -17.56700 18.93400 1.000 25.68135 ?  21  PHE A CB    1 
ATOM   114  C CG    . PHE A 1 41  ? -7.36600  -16.74500 19.58100 1.000 26.27208 ?  21  PHE A CG    1 
ATOM   115  C CD1   . PHE A 1 41  ? -6.08400  -16.72300 19.06000 1.000 25.13918 ?  21  PHE A CD1   1 
ATOM   116  C CD2   . PHE A 1 41  ? -7.65400  -15.93600 20.67900 1.000 25.31775 ?  21  PHE A CD2   1 
ATOM   117  C CE1   . PHE A 1 41  ? -5.09000  -15.93900 19.64900 1.000 26.87631 ?  21  PHE A CE1   1 
ATOM   118  C CE2   . PHE A 1 41  ? -6.67100  -15.16200 21.27600 1.000 24.91400 ?  21  PHE A CE2   1 
ATOM   119  C CZ    . PHE A 1 41  ? -5.38900  -15.15400 20.75800 1.000 22.97176 ?  21  PHE A CZ    1 
ATOM   120  N N     . GLN A 1 42  ? -8.67400  -20.02500 20.89300 1.000 24.03755 ?  22  GLN A N     1 
ATOM   121  C CA    . GLN A 1 42  ? -8.36000  -20.46700 22.24500 1.000 25.09017 ?  22  GLN A CA    1 
ATOM   122  C C     . GLN A 1 42  ? -8.12300  -21.96600 22.34800 1.000 28.89013 ?  22  GLN A C     1 
ATOM   123  O O     . GLN A 1 42  ? -7.33900  -22.39900 23.20100 1.000 24.49903 ?  22  GLN A O     1 
ATOM   124  C CB    . GLN A 1 42  ? -9.48600  -20.07200 23.20200 1.000 25.34561 ?  22  GLN A CB    1 
ATOM   125  C CG    . GLN A 1 42  ? -9.47300  -18.59100 23.57200 1.000 22.89014 ?  22  GLN A CG    1 
ATOM   126  C CD    . GLN A 1 42  ? -10.08400 -18.33700 24.93500 1.000 25.33847 ?  22  GLN A CD    1 
ATOM   127  O OE1   . GLN A 1 42  ? -11.06300 -18.98600 25.32700 1.000 23.13450 ?  22  GLN A OE1   1 
ATOM   128  N NE2   . GLN A 1 42  ? -9.50200  -17.40100 25.67500 1.000 25.95690 ?  22  GLN A NE2   1 
ATOM   129  N N     . TYR A 1 43  ? -8.78400  -22.76400 21.50200 1.000 25.97177 ?  23  TYR A N     1 
ATOM   130  C CA    . TYR A 1 43  ? -8.75800  -24.21600 21.61500 1.000 30.19457 ?  23  TYR A CA    1 
ATOM   131  C C     . TYR A 1 43  ? -8.25600  -24.92000 20.36000 1.000 30.63409 ?  23  TYR A C     1 
ATOM   132  O O     . TYR A 1 43  ? -8.06900  -26.14400 20.39500 1.000 28.95210 ?  23  TYR A O     1 
ATOM   133  C CB    . TYR A 1 43  ? -10.16300 -24.75200 21.97000 1.000 24.05380 ?  23  TYR A CB    1 
ATOM   134  C CG    . TYR A 1 43  ? -10.71000 -24.22700 23.29300 1.000 25.45441 ?  23  TYR A CG    1 
ATOM   135  C CD1   . TYR A 1 43  ? -10.36300 -24.83100 24.49800 1.000 26.77712 ?  23  TYR A CD1   1 
ATOM   136  C CD2   . TYR A 1 43  ? -11.55900 -23.12400 23.33400 1.000 26.97637 ?  23  TYR A CD2   1 
ATOM   137  C CE1   . TYR A 1 43  ? -10.84700 -24.35500 25.70800 1.000 24.66513 ?  23  TYR A CE1   1 
ATOM   138  C CE2   . TYR A 1 43  ? -12.05000 -22.63900 24.54200 1.000 24.02082 ?  23  TYR A CE2   1 
ATOM   139  C CZ    . TYR A 1 43  ? -11.68600 -23.26200 25.72300 1.000 25.63965 ?  23  TYR A CZ    1 
ATOM   140  O OH    . TYR A 1 43  ? -12.15800 -22.79800 26.92600 1.000 24.95354 ?  23  TYR A OH    1 
ATOM   141  N N     . GLY A 1 44  ? -8.02700  -24.19100 19.26600 1.000 31.42788 ?  24  GLY A N     1 
ATOM   142  C CA    . GLY A 1 44  ? -7.59600  -24.77800 18.01300 1.000 34.14092 ?  24  GLY A CA    1 
ATOM   143  C C     . GLY A 1 44  ? -6.08700  -24.92300 17.91000 1.000 38.10197 ?  24  GLY A C     1 
ATOM   144  O O     . GLY A 1 44  ? -5.34700  -24.82300 18.89000 1.000 41.90874 ?  24  GLY A O     1 
ATOM   145  N N     . GLU A 1 45  ? -5.64800  -25.19300 16.67900 1.000 41.24268 ?  25  GLU A N     1 
ATOM   146  C CA    . GLU A 1 45  ? -4.21500  -25.48800 16.43500 1.000 47.07676 ?  25  GLU A CA    1 
ATOM   147  C C     . GLU A 1 45  ? -3.37500  -24.22400 16.27200 1.000 44.90339 ?  25  GLU A C     1 
ATOM   148  O O     . GLU A 1 45  ? -3.88900  -23.21900 15.77000 1.000 45.25000 ?  25  GLU A O     1 
ATOM   149  C CB    . GLU A 1 45  ? -4.06000  -26.35500 15.18100 1.000 40.47587 ?  25  GLU A CB    1 
ATOM   150  N N     . ASP A 1 46  ? -2.11400  -24.32900 16.65700 1.000 43.39943 ?  26  ASP A N     1 
ATOM   151  C CA    . ASP A 1 46  ? -1.18100  -23.19000 16.56000 1.000 48.72827 ?  26  ASP A CA    1 
ATOM   152  C C     . ASP A 1 46  ? -0.81200  -22.91600 15.10300 1.000 48.96133 ?  26  ASP A C     1 
ATOM   153  O O     . ASP A 1 46  ? -0.79500  -23.86300 14.30900 1.000 47.14510 ?  26  ASP A O     1 
ATOM   154  C CB    . ASP A 1 46  ? 0.05700   -23.46200 17.41200 1.000 46.29913 ?  26  ASP A CB    1 
ATOM   155  C CG    . ASP A 1 46  ? 1.19900   -24.11500 16.65400 1.000 49.34637 ?  26  ASP A CG    1 
ATOM   156  N N     . CYS A 1 47  ? -0.61300  -21.64800 14.76300 1.000 47.88576 ?  27  CYS A N     1 
ATOM   157  C CA    A CYS A 1 47  ? -0.16200  -21.27300 13.38900 0.459 46.64642 ?  27  CYS A CA    1 
ATOM   158  C CA    B CYS A 1 47  ? -0.16200  -21.27200 13.38900 0.541 46.70347 ?  27  CYS A CA    1 
ATOM   159  C C     . CYS A 1 47  ? 1.11000   -20.37300 13.31000 1.000 40.31463 ?  27  CYS A C     1 
ATOM   160  O O     . CYS A 1 47  ? 1.64500   -19.52900 14.23900 1.000 40.04780 ?  27  CYS A O     1 
ATOM   161  C CB    A CYS A 1 47  ? -1.28500  -20.57100 12.62800 0.459 47.95265 ?  27  CYS A CB    1 
ATOM   162  C CB    B CYS A 1 47  ? -1.28500  -20.56800 12.62900 0.541 47.96514 ?  27  CYS A CB    1 
ATOM   163  S SG    A CYS A 1 47  ? -2.92400  -20.74400 13.38000 0.459 81.25000 ?  27  CYS A SG    1 
ATOM   164  S SG    B CYS A 1 47  ? -2.73100  -21.60600 12.29300 0.541 81.25000 ?  27  CYS A SG    1 
ATOM   165  N N     . PHE A 1 48  ? 1.82000   -20.53500 12.19400 1.000 37.29547 ?  28  PHE A N     1 
ATOM   166  C CA    . PHE A 1 48  ? 3.05400   -19.72500 11.97600 1.000 37.19277 ?  28  PHE A CA    1 
ATOM   167  C C     . PHE A 1 48  ? 4.06800   -19.87900 13.12000 1.000 36.83580 ?  28  PHE A C     1 
ATOM   168  O O     . PHE A 1 48  ? 4.86200   -18.96300 13.33500 1.000 43.92916 ?  28  PHE A O     1 
ATOM   169  C CB    . PHE A 1 48  ? 2.69100   -18.26600 11.69200 1.000 35.72405 ?  28  PHE A CB    1 
ATOM   170  C CG    . PHE A 1 48  ? 1.67700   -18.03600 10.60600 1.000 34.67568 ?  28  PHE A CG    1 
ATOM   171  C CD1   . PHE A 1 48  ? 1.96800   -18.33300 9.28600  1.000 33.20867 ?  28  PHE A CD1   1 
ATOM   172  C CD2   . PHE A 1 48  ? 0.44000   -17.49500 10.90200 1.000 33.68129 ?  28  PHE A CD2   1 
ATOM   173  C CE1   . PHE A 1 48  ? 1.03500   -18.10500 8.28900  1.000 33.16517 ?  28  PHE A CE1   1 
ATOM   174  C CE2   . PHE A 1 48  ? -0.49200  -17.27100 9.90400  1.000 33.44056 ?  28  PHE A CE2   1 
ATOM   175  C CZ    . PHE A 1 48  ? -0.19200  -17.57400 8.60000  1.000 30.04093 ?  28  PHE A CZ    1 
ATOM   176  N N     . GLY A 1 49  ? 4.05700   -21.01200 13.81000 1.000 40.00755 ?  29  GLY A N     1 
ATOM   177  C CA    . GLY A 1 49  ? 4.99900   -21.26200 14.91600 1.000 41.34784 ?  29  GLY A CA    1 
ATOM   178  C C     . GLY A 1 49  ? 4.60500   -20.56000 16.20100 1.000 40.39593 ?  29  GLY A C     1 
ATOM   179  O O     . GLY A 1 49  ? 5.39400   -20.59000 17.15100 1.000 42.14799 ?  29  GLY A O     1 
ATOM   180  N N     . VAL A 1 50  ? 3.43500   -19.93200 16.22200 1.000 35.88767 ?  30  VAL A N     1 
ATOM   181  C CA    . VAL A 1 50  ? 3.05500   -19.13800 17.42000 1.000 34.93651 ?  30  VAL A CA    1 
ATOM   182  C C     . VAL A 1 50  ? 2.25500   -20.02200 18.37500 1.000 28.96603 ?  30  VAL A C     1 
ATOM   183  O O     . VAL A 1 50  ? 1.28000   -20.62700 17.94900 1.000 34.47241 ?  30  VAL A O     1 
ATOM   184  C CB    . VAL A 1 50  ? 2.33800   -17.82600 17.03800 1.000 30.61407 ?  30  VAL A CB    1 
ATOM   185  C CG1   . VAL A 1 50  ? 1.97700   -16.99600 18.25700 1.000 28.63901 ?  30  VAL A CG1   1 
ATOM   186  C CG2   . VAL A 1 50  ? 3.17000   -17.01000 16.06400 1.000 32.96703 ?  30  VAL A CG2   1 
ATOM   187  N N     . LEU A 1 51  ? 2.66900   -20.04300 19.62800 1.000 30.90557 ?  31  LEU A N     1 
ATOM   188  C CA    . LEU A 1 51  ? 2.01100   -20.86600 20.62800 1.000 34.42205 ?  31  LEU A CA    1 
ATOM   189  C C     . LEU A 1 51  ? 0.66500   -20.28000 21.04200 1.000 33.14373 ?  31  LEU A C     1 
ATOM   190  O O     . LEU A 1 51  ? 0.41900   -19.07400 20.92300 1.000 32.06164 ?  31  LEU A O     1 
ATOM   191  C CB    . LEU A 1 51  ? 2.91200   -21.01500 21.84900 1.000 35.46525 ?  31  LEU A CB    1 
ATOM   192  C CG    . LEU A 1 51  ? 4.27100   -21.64700 21.51800 1.000 42.10395 ?  31  LEU A CG    1 
ATOM   193  C CD1   . LEU A 1 51  ? 4.99700   -22.05800 22.78600 1.000 39.57805 ?  31  LEU A CD1   1 
ATOM   194  C CD2   . LEU A 1 51  ? 4.09400   -22.85300 20.59600 1.000 40.37479 ?  31  LEU A CD2   1 
ATOM   195  N N     . ASN A 1 52  ? -0.20600  -21.16200 21.53500 1.000 33.07237 ?  32  ASN A N     1 
ATOM   196  C CA    . ASN A 1 52  ? -1.52200  -20.77800 22.03000 1.000 30.39247 ?  32  ASN A CA    1 
ATOM   197  C C     . ASN A 1 52  ? -1.41400  -19.64200 23.04000 1.000 26.82831 ?  32  ASN A C     1 
ATOM   198  O O     . ASN A 1 52  ? -0.68800  -19.74000 24.03100 1.000 27.57958 ?  32  ASN A O     1 
ATOM   199  C CB    . ASN A 1 52  ? -2.20300  -21.99100 22.66500 1.000 25.25038 ?  32  ASN A CB    1 
ATOM   200  C CG    . ASN A 1 52  ? -3.52600  -21.63700 23.31500 1.000 28.78774 ?  32  ASN A CG    1 
ATOM   201  O OD1   . ASN A 1 52  ? -3.56800  -21.20600 24.47500 1.000 24.72418 ?  32  ASN A OD1   1 
ATOM   202  N ND2   . ASN A 1 52  ? -4.61600  -21.82400 22.57500 1.000 23.71934 ?  32  ASN A ND2   1 
ATOM   203  N N     . PHE A 1 53  ? -2.15900  -18.56500 22.77900 1.000 24.57709 ?  33  PHE A N     1 
ATOM   204  C CA    . PHE A 1 53  ? -2.01900  -17.32500 23.54400 1.000 23.30846 ?  33  PHE A CA    1 
ATOM   205  C C     . PHE A 1 53  ? -2.53800  -17.47100 24.97100 1.000 22.67297 ?  33  PHE A C     1 
ATOM   206  O O     . PHE A 1 53  ? -1.89000  -17.02400 25.92800 1.000 22.81190 ?  33  PHE A O     1 
ATOM   207  C CB    . PHE A 1 53  ? -2.76500  -16.19900 22.82200 1.000 23.43835 ?  33  PHE A CB    1 
ATOM   208  C CG    . PHE A 1 53  ? -2.61900  -14.84100 23.47300 1.000 25.06878 ?  33  PHE A CG    1 
ATOM   209  C CD1   . PHE A 1 53  ? -1.39300  -14.19500 23.50100 1.000 23.36623 ?  33  PHE A CD1   1 
ATOM   210  C CD2   . PHE A 1 53  ? -3.71600  -14.21200 24.04400 1.000 22.02435 ?  33  PHE A CD2   1 
ATOM   211  C CE1   . PHE A 1 53  ? -1.26400  -12.93100 24.08000 1.000 22.80201 ?  33  PHE A CE1   1 
ATOM   212  C CE2   . PHE A 1 53  ? -3.60300  -12.96500 24.63300 1.000 24.19895 ?  33  PHE A CE2   1 
ATOM   213  C CZ    . PHE A 1 53  ? -2.37400  -12.31400 24.64800 1.000 24.10935 ?  33  PHE A CZ    1 
ATOM   214  N N     . ALA A 1 54  ? -3.72100  -18.06600 25.13200 1.000 21.36414 ?  34  ALA A N     1 
ATOM   215  C CA    . ALA A 1 54  ? -4.30800  -18.20400 26.46100 1.000 24.57478 ?  34  ALA A CA    1 
ATOM   216  C C     . ALA A 1 54  ? -3.41400  -19.01800 27.39000 1.000 25.21470 ?  34  ALA A C     1 
ATOM   217  O O     . ALA A 1 54  ? -3.25500  -18.67400 28.57200 1.000 22.27741 ?  34  ALA A O     1 
ATOM   218  C CB    . ALA A 1 54  ? -5.69600  -18.83800 26.35300 1.000 22.76076 ?  34  ALA A CB    1 
ATOM   219  N N     . LEU A 1 55  ? -2.80700  -20.09200 26.87400 1.000 24.30308 ?  35  LEU A N     1 
ATOM   220  C CA    . LEU A 1 55  ? -1.91800  -20.89700 27.70800 1.000 27.37121 ?  35  LEU A CA    1 
ATOM   221  C C     . LEU A 1 55  ? -0.63000  -20.14500 28.03200 1.000 23.79354 ?  35  LEU A C     1 
ATOM   222  O O     . LEU A 1 55  ? -0.14100  -20.19500 29.16600 1.000 25.02735 ?  35  LEU A O     1 
ATOM   223  C CB    . LEU A 1 55  ? -1.61300  -22.22800 27.01400 1.000 24.89336 ?  35  LEU A CB    1 
ATOM   224  C CG    . LEU A 1 55  ? -0.59600  -23.10900 27.74600 1.000 28.95076 ?  35  LEU A CG    1 
ATOM   225  C CD1   . LEU A 1 55  ? -1.05400  -23.41900 29.17100 1.000 28.44357 ?  35  LEU A CD1   1 
ATOM   226  C CD2   . LEU A 1 55  ? -0.30400  -24.37700 26.95800 1.000 27.81262 ?  35  LEU A CD2   1 
ATOM   227  N N     . ALA A 1 56  ? -0.07000  -19.43700 27.04900 1.000 24.78438 ?  36  ALA A N     1 
ATOM   228  C CA    . ALA A 1 56  ? 1.13400   -18.64800 27.29700 1.000 24.22416 ?  36  ALA A CA    1 
ATOM   229  C C     . ALA A 1 56  ? 0.89200   -17.61000 28.38600 1.000 24.09141 ?  36  ALA A C     1 
ATOM   230  O O     . ALA A 1 56  ? 1.69600   -17.47100 29.31600 1.000 28.09761 ?  36  ALA A O     1 
ATOM   231  C CB    . ALA A 1 56  ? 1.59700   -17.97800 26.00200 1.000 25.62841 ?  36  ALA A CB    1 
ATOM   232  N N     . CYS A 1 57  ? -0.22500  -16.88100 28.29900 1.000 25.89421 ?  37  CYS A N     1 
ATOM   233  C CA    . CYS A 1 57  ? -0.50100  -15.83700 29.28600 1.000 28.22137 ?  37  CYS A CA    1 
ATOM   234  C C     . CYS A 1 57  ? -0.72100  -16.43900 30.66900 1.000 26.48700 ?  37  CYS A C     1 
ATOM   235  O O     . CYS A 1 57  ? -0.16300  -15.95600 31.66500 1.000 24.46378 ?  37  CYS A O     1 
ATOM   236  C CB    . CYS A 1 57  ? -1.72100  -15.01400 28.86700 1.000 22.56413 ?  37  CYS A CB    1 
ATOM   237  S SG    . CYS A 1 57  ? -1.49800  -13.94800 27.41500 1.000 27.57045 ?  37  CYS A SG    1 
ATOM   238  N N     . ALA A 1 58  ? -1.55300  -17.48400 30.75300 1.000 25.60363 ?  38  ALA A N     1 
ATOM   239  C CA    . ALA A 1 58  ? -1.83300  -18.08900 32.05500 1.000 27.50282 ?  38  ALA A CA    1 
ATOM   240  C C     . ALA A 1 58  ? -0.56300  -18.67500 32.65800 1.000 26.83417 ?  38  ALA A C     1 
ATOM   241  O O     . ALA A 1 58  ? -0.32100  -18.55400 33.86600 1.000 25.79608 ?  38  ALA A O     1 
ATOM   242  C CB    . ALA A 1 58  ? -2.92200  -19.16100 31.92400 1.000 23.62433 ?  38  ALA A CB    1 
ATOM   243  N N     . THR A 1 59  ? 0.27300   -19.29000 31.82100 1.000 28.97343 ?  39  THR A N     1 
ATOM   244  C CA    . THR A 1 59  ? 1.53600   -19.83900 32.29900 1.000 32.21935 ?  39  THR A CA    1 
ATOM   245  C C     . THR A 1 59  ? 2.45200   -18.73300 32.80200 1.000 31.09849 ?  39  THR A C     1 
ATOM   246  O O     . THR A 1 59  ? 3.00800   -18.82500 33.90200 1.000 33.22471 ?  39  THR A O     1 
ATOM   247  C CB    . THR A 1 59  ? 2.21100   -20.64300 31.18600 1.000 32.28302 ?  39  THR A CB    1 
ATOM   248  O OG1   . THR A 1 59  ? 1.33900   -21.70400 30.78500 1.000 31.39543 ?  39  THR A OG1   1 
ATOM   249  C CG2   . THR A 1 59  ? 3.53100   -21.23500 31.67700 1.000 34.89655 ?  39  THR A CG2   1 
ATOM   250  N N     . LYS A 1 60  ? 2.60600   -17.66300 32.01800 1.000 28.59199 ?  40  LYS A N     1 
ATOM   251  C CA    . LYS A 1 60  ? 3.42700   -16.54800 32.48200 1.000 31.59388 ?  40  LYS A CA    1 
ATOM   252  C C     . LYS A 1 60  ? 2.84000   -15.92200 33.74200 1.000 31.83077 ?  40  LYS A C     1 
ATOM   253  O O     . LYS A 1 60  ? 3.57900   -15.53500 34.65500 1.000 30.22979 ?  40  LYS A O     1 
ATOM   254  C CB    . LYS A 1 60  ? 3.58000   -15.50100 31.37600 1.000 31.68008 ?  40  LYS A CB    1 
ATOM   255  C CG    . LYS A 1 60  ? 4.58600   -15.88300 30.29700 1.000 34.35924 ?  40  LYS A CG    1 
ATOM   256  C CD    . LYS A 1 60  ? 4.29500   -15.15300 28.99400 1.000 29.86679 ?  40  LYS A CD    1 
ATOM   257  C CE    . LYS A 1 60  ? 5.06300   -15.74600 27.82400 1.000 32.17103 ?  40  LYS A CE    1 
ATOM   258  N NZ    . LYS A 1 60  ? 6.54300   -15.70400 28.01100 1.000 35.46257 ?  40  LYS A NZ    1 
ATOM   259  N N     . ALA A 1 61  ? 1.50900   -15.84500 33.82600 1.000 29.26311 ?  41  ALA A N     1 
ATOM   260  C CA    . ALA A 1 61  ? 0.88100   -15.23400 34.99100 1.000 28.79504 ?  41  ALA A CA    1 
ATOM   261  C C     . ALA A 1 61  ? 1.12700   -16.05700 36.24700 1.000 33.95848 ?  41  ALA A C     1 
ATOM   262  O O     . ALA A 1 61  ? 1.40100   -15.50000 37.31600 1.000 33.52874 ?  41  ALA A O     1 
ATOM   263  C CB    . ALA A 1 61  ? -0.61900  -15.05200 34.75000 1.000 31.99202 ?  41  ALA A CB    1 
ATOM   264  N N     . ILE A 1 62  ? 1.02200   -17.38300 36.14300 1.000 32.75214 ?  42  ILE A N     1 
ATOM   265  C CA    . ILE A 1 62  ? 1.28600   -18.23400 37.29700 1.000 34.03812 ?  42  ILE A CA    1 
ATOM   266  C C     . ILE A 1 62  ? 2.71300   -18.02000 37.79300 1.000 33.80043 ?  42  ILE A C     1 
ATOM   267  O O     . ILE A 1 62  ? 2.95700   -17.87300 38.99600 1.000 40.85097 ?  42  ILE A O     1 
ATOM   268  C CB    . ILE A 1 62  ? 1.01000   -19.70900 36.94800 1.000 35.04903 ?  42  ILE A CB    1 
ATOM   269  C CG1   . ILE A 1 62  ? -0.49900  -19.96400 36.87500 1.000 30.80511 ?  42  ILE A CG1   1 
ATOM   270  C CG2   . ILE A 1 62  ? 1.66400   -20.63700 37.95700 1.000 31.98733 ?  42  ILE A CG2   1 
ATOM   271  C CD1   . ILE A 1 62  ? -0.89300  -21.11800 35.97200 1.000 31.79934 ?  42  ILE A CD1   1 
ATOM   272  N N     . GLY A 1 63  ? 3.67000   -17.97500 36.86800 1.000 31.87464 ?  43  GLY A N     1 
ATOM   273  C CA    . GLY A 1 63  ? 5.05000   -17.72000 37.25100 1.000 33.59078 ?  43  GLY A CA    1 
ATOM   274  C C     . GLY A 1 63  ? 5.22800   -16.40400 37.98800 1.000 38.53243 ?  43  GLY A C     1 
ATOM   275  O O     . GLY A 1 63  ? 5.83400   -16.36000 39.06200 1.000 40.95733 ?  43  GLY A O     1 
ATOM   276  N N     . TYR A 1 64  ? 4.69400   -15.31300 37.42800 1.000 34.42224 ?  44  TYR A N     1 
ATOM   277  C CA    . TYR A 1 64  ? 4.83800   -14.01100 38.08100 1.000 36.85251 ?  44  TYR A CA    1 
ATOM   278  C C     . TYR A 1 64  ? 4.24200   -14.00200 39.48700 1.000 35.27392 ?  44  TYR A C     1 
ATOM   279  O O     . TYR A 1 64  ? 4.67300   -13.21600 40.33300 1.000 41.08961 ?  44  TYR A O     1 
ATOM   280  C CB    . TYR A 1 64  ? 4.19400   -12.90800 37.23100 1.000 30.72129 ?  44  TYR A CB    1 
ATOM   281  C CG    . TYR A 1 64  ? 4.99300   -12.51300 36.01100 1.000 29.92583 ?  44  TYR A CG    1 
ATOM   282  C CD1   . TYR A 1 64  ? 6.24900   -11.94400 36.13200 1.000 33.48748 ?  44  TYR A CD1   1 
ATOM   283  C CD2   . TYR A 1 64  ? 4.48900   -12.71000 34.73600 1.000 31.64776 ?  44  TYR A CD2   1 
ATOM   284  C CE1   . TYR A 1 64  ? 6.98600   -11.58800 35.01300 1.000 32.69153 ?  44  TYR A CE1   1 
ATOM   285  C CE2   . TYR A 1 64  ? 5.21400   -12.35700 33.60700 1.000 31.23240 ?  44  TYR A CE2   1 
ATOM   286  C CZ    . TYR A 1 64  ? 6.46300   -11.79800 33.75200 1.000 31.88235 ?  44  TYR A CZ    1 
ATOM   287  O OH    . TYR A 1 64  ? 7.18400   -11.44500 32.63000 1.000 31.17876 ?  44  TYR A OH    1 
ATOM   288  N N     . THR A 1 65  ? 3.26400   -14.86100 39.76300 1.000 39.24990 ?  45  THR A N     1 
ATOM   289  C CA    . THR A 1 65  ? 2.58300   -14.87700 41.05300 1.000 39.23662 ?  45  THR A CA    1 
ATOM   290  C C     . THR A 1 65  ? 2.96900   -16.09100 41.89400 1.000 46.33768 ?  45  THR A C     1 
ATOM   291  O O     . THR A 1 65  ? 2.17600   -16.55300 42.72000 1.000 48.87523 ?  45  THR A O     1 
ATOM   292  C CB    . THR A 1 65  ? 1.06700   -14.84800 40.86500 1.000 39.93726 ?  45  THR A CB    1 
ATOM   293  O OG1   . THR A 1 65  ? 0.63000   -16.09900 40.31600 1.000 40.59831 ?  45  THR A OG1   1 
ATOM   294  C CG2   . THR A 1 65  ? 0.65600   -13.70700 39.93000 1.000 31.31948 ?  45  THR A CG2   1 
ATOM   295  N N     . LYS A 1 66  ? 4.18400   -16.61600 41.70100 1.000 48.46793 ?  46  LYS A N     1 
ATOM   296  C CA    . LYS A 1 66  ? 4.56900   -17.86200 42.35900 1.000 48.28382 ?  46  LYS A CA    1 
ATOM   297  C C     . LYS A 1 66  ? 4.75900   -17.69700 43.86000 1.000 51.43640 ?  46  LYS A C     1 
ATOM   298  O O     . LYS A 1 66  ? 4.66100   -18.68600 44.59400 1.000 62.27841 ?  46  LYS A O     1 
ATOM   299  C CB    . LYS A 1 66  ? 5.85100   -18.42300 41.73400 1.000 46.96182 ?  46  LYS A CB    1 
ATOM   300  N N     . GLU A 1 67  ? 5.02600   -16.48500 44.33400 1.000 48.93228 ?  47  GLU A N     1 
ATOM   301  C CA    . GLU A 1 67  ? 5.14900   -16.24900 45.76300 1.000 49.32379 ?  47  GLU A CA    1 
ATOM   302  C C     . GLU A 1 67  ? 3.81100   -15.97800 46.44600 1.000 52.41267 ?  47  GLU A C     1 
ATOM   303  O O     . GLU A 1 67  ? 3.79200   -15.76700 47.66300 1.000 55.38592 ?  47  GLU A O     1 
ATOM   304  C CB    . GLU A 1 67  ? 6.10500   -15.07700 46.01400 1.000 48.51652 ?  47  GLU A CB    1 
ATOM   305  N N     . THR A 1 68  ? 2.69500   -15.97700 45.71000 1.000 50.77792 ?  48  THR A N     1 
ATOM   306  C CA    . THR A 1 68  ? 1.40400   -15.63800 46.29300 1.000 47.57036 ?  48  THR A CA    1 
ATOM   307  C C     . THR A 1 68  ? 0.64000   -16.89000 46.70000 1.000 45.18267 ?  48  THR A C     1 
ATOM   308  O O     . THR A 1 68  ? 0.93700   -17.99300 46.23600 1.000 43.09756 ?  48  THR A O     1 
ATOM   309  C CB    . THR A 1 68  ? 0.56900   -14.82900 45.29800 1.000 49.74884 ?  48  THR A CB    1 
ATOM   310  O OG1   . THR A 1 68  ? -0.19900  -15.72300 44.47700 1.000 50.97366 ?  48  THR A OG1   1 
ATOM   311  C CG2   . THR A 1 68  ? 1.46400   -13.96300 44.42300 1.000 44.81373 ?  48  THR A CG2   1 
ATOM   312  N N     . PRO A 1 69  ? -0.35100  -16.74300 47.58600 1.000 45.37584 ?  49  PRO A N     1 
ATOM   313  C CA    . PRO A 1 69  ? -1.12800  -17.91300 48.03900 1.000 46.14520 ?  49  PRO A CA    1 
ATOM   314  C C     . PRO A 1 69  ? -1.86100  -18.67400 46.93500 1.000 47.00869 ?  49  PRO A C     1 
ATOM   315  O O     . PRO A 1 69  ? -2.11500  -19.87600 47.09700 1.000 49.76949 ?  49  PRO A O     1 
ATOM   316  C CB    . PRO A 1 69  ? -2.12300  -17.30700 49.04400 1.000 45.15248 ?  49  PRO A CB    1 
ATOM   317  C CG    . PRO A 1 69  ? -1.88400  -15.81600 49.03300 1.000 45.58556 ?  49  PRO A CG    1 
ATOM   318  C CD    . PRO A 1 69  ? -0.51600  -15.59800 48.49100 1.000 44.48966 ?  49  PRO A CD    1 
ATOM   319  N N     . LYS A 1 70  ? -2.23600  -18.02100 45.83900 1.000 43.03991 ?  50  LYS A N     1 
ATOM   320  C CA    . LYS A 1 70  ? -2.88100  -18.70300 44.71200 1.000 41.63761 ?  50  LYS A CA    1 
ATOM   321  C C     . LYS A 1 70  ? -4.18900  -19.38400 45.13200 1.000 37.85003 ?  50  LYS A C     1 
ATOM   322  O O     . LYS A 1 70  ? -4.45600  -20.54400 44.81000 1.000 37.99075 ?  50  LYS A O     1 
ATOM   323  C CB    . LYS A 1 70  ? -1.91900  -19.69800 44.05300 1.000 41.45191 ?  50  LYS A CB    1 
ATOM   324  C CG    . LYS A 1 70  ? -0.69000  -19.01700 43.45800 1.000 41.52854 ?  50  LYS A CG    1 
ATOM   325  C CD    . LYS A 1 70  ? 0.21900   -19.96300 42.70800 1.000 41.94928 ?  50  LYS A CD    1 
ATOM   326  C CE    . LYS A 1 70  ? 1.20600   -19.16800 41.88300 1.000 44.52492 ?  50  LYS A CE    1 
ATOM   327  N N     . ASN A 1 71  ? -5.02000  -18.63400 45.85400 1.000 37.27679 ?  51  ASN A N     1 
ATOM   328  C CA    . ASN A 1 71  ? -6.35500  -19.08600 46.22900 1.000 36.01350 ?  51  ASN A CA    1 
ATOM   329  C C     . ASN A 1 71  ? -7.41800  -18.67900 45.21500 1.000 35.81418 ?  51  ASN A C     1 
ATOM   330  O O     . ASN A 1 71  ? -8.29600  -19.48100 44.88000 1.000 36.05465 ?  51  ASN A O     1 
ATOM   331  C CB    . ASN A 1 71  ? -6.73000  -18.52000 47.60200 1.000 38.28798 ?  51  ASN A CB    1 
ATOM   332  C CG    . ASN A 1 71  ? -5.82400  -19.03000 48.71700 1.000 49.80782 ?  51  ASN A CG    1 
ATOM   333  O OD1   . ASN A 1 71  ? -5.26500  -20.13100 48.63900 1.000 46.53339 ?  51  ASN A OD1   1 
ATOM   334  N ND2   . ASN A 1 71  ? -5.64200  -18.20400 49.74700 1.000 44.03282 ?  51  ASN A ND2   1 
ATOM   335  N N     . ARG A 1 72  ? -7.36100  -17.44300 44.72500 1.000 30.07199 ?  52  ARG A N     1 
ATOM   336  C CA    . ARG A 1 72  ? -8.44100  -16.87400 43.93400 1.000 31.79161 ?  52  ARG A CA    1 
ATOM   337  C C     . ARG A 1 72  ? -7.85300  -16.06400 42.79100 1.000 32.03788 ?  52  ARG A C     1 
ATOM   338  O O     . ARG A 1 72  ? -7.02800  -15.17300 43.01900 1.000 31.20437 ?  52  ARG A O     1 
ATOM   339  C CB    . ARG A 1 72  ? -9.34500  -15.98000 44.79500 1.000 32.39973 ?  52  ARG A CB    1 
ATOM   340  C CG    . ARG A 1 72  ? -10.29600 -16.74400 45.71500 1.000 33.17084 ?  52  ARG A CG    1 
ATOM   341  C CD    . ARG A 1 72  ? -11.10000 -15.79400 46.59600 1.000 32.50138 ?  52  ARG A CD    1 
ATOM   342  N NE    . ARG A 1 72  ? -11.87100 -14.83600 45.81100 1.000 33.21399 ?  52  ARG A NE    1 
ATOM   343  C CZ    . ARG A 1 72  ? -13.07100 -15.09100 45.30400 1.000 31.83904 ?  52  ARG A CZ    1 
ATOM   344  N NH1   . ARG A 1 72  ? -13.63700 -16.27900 45.43900 1.000 29.33206 ?  52  ARG A NH1   1 
ATOM   345  N NH2   . ARG A 1 72  ? -13.71400 -14.13400 44.63800 1.000 33.01151 ?  52  ARG A NH2   1 
ATOM   346  N N     . ALA A 1 73  ? -8.28500  -16.37200 41.57200 1.000 30.00398 ?  53  ALA A N     1 
ATOM   347  C CA    . ALA A 1 73  ? -7.89200  -15.62100 40.38900 1.000 31.54472 ?  53  ALA A CA    1 
ATOM   348  C C     . ALA A 1 73  ? -9.13000  -15.21700 39.59500 1.000 27.27879 ?  53  ALA A C     1 
ATOM   349  O O     . ALA A 1 73  ? -10.17200 -15.88100 39.64500 1.000 29.48241 ?  53  ALA A O     1 
ATOM   350  C CB    . ALA A 1 73  ? -6.93100  -16.44000 39.50600 1.000 25.88864 ?  53  ALA A CB    1 
ATOM   351  N N     . LEU A 1 74  ? -9.00700  -14.11800 38.86300 1.000 25.68348 ?  54  LEU A N     1 
ATOM   352  C CA    . LEU A 1 74  ? -10.06700 -13.63300 37.99500 1.000 25.54577 ?  54  LEU A CA    1 
ATOM   353  C C     . LEU A 1 74  ? -9.51400  -13.48200 36.58400 1.000 25.71304 ?  54  LEU A C     1 
ATOM   354  O O     . LEU A 1 74  ? -8.47500  -12.84500 36.38400 1.000 27.38073 ?  54  LEU A O     1 
ATOM   355  C CB    . LEU A 1 74  ? -10.63700 -12.30200 38.51400 1.000 27.71355 ?  54  LEU A CB    1 
ATOM   356  C CG    . LEU A 1 74  ? -11.56500 -11.49100 37.60000 1.000 26.91182 ?  54  LEU A CG    1 
ATOM   357  C CD1   . LEU A 1 74  ? -12.85400 -12.24100 37.33700 1.000 26.33328 ?  54  LEU A CD1   1 
ATOM   358  C CD2   . LEU A 1 74  ? -11.86500 -10.10600 38.20900 1.000 23.50377 ?  54  LEU A CD2   1 
ATOM   359  N N     . ASP A 1 75  ? -10.19100 -14.10500 35.62000 1.000 26.64132 ?  55  ASP A N     1 
ATOM   360  C CA    . ASP A 1 75  ? -9.88700  -13.98000 34.19300 1.000 26.11865 ?  55  ASP A CA    1 
ATOM   361  C C     . ASP A 1 75  ? -10.96400 -13.07400 33.61100 1.000 23.55195 ?  55  ASP A C     1 
ATOM   362  O O     . ASP A 1 75  ? -12.08800 -13.52200 33.36000 1.000 24.92424 ?  55  ASP A O     1 
ATOM   363  C CB    . ASP A 1 75  ? -9.86700  -15.35800 33.52800 1.000 23.77430 ?  55  ASP A CB    1 
ATOM   364  C CG    . ASP A 1 75  ? -9.59900  -15.30700 32.01300 1.000 22.92764 ?  55  ASP A CG    1 
ATOM   365  O OD1   . ASP A 1 75  ? -9.08000  -14.29500 31.49000 1.000 24.77216 ?  55  ASP A OD1   1 
ATOM   366  O OD2   . ASP A 1 75  ? -9.90900  -16.31000 31.33400 1.000 24.88741 -1 55  ASP A OD2   1 
ATOM   367  N N     . LEU A 1 76  ? -10.61500 -11.80000 33.40900 1.000 23.25105 ?  56  LEU A N     1 
ATOM   368  C CA    . LEU A 1 76  ? -11.56100 -10.73100 33.10200 1.000 21.59114 ?  56  LEU A CA    1 
ATOM   369  C C     . LEU A 1 76  ? -11.53000 -10.45900 31.60500 1.000 24.59475 ?  56  LEU A C     1 
ATOM   370  O O     . LEU A 1 76  ? -10.46600 -10.16600 31.04900 1.000 25.78095 ?  56  LEU A O     1 
ATOM   371  C CB    . LEU A 1 76  ? -11.21000 -9.46600  33.88400 1.000 22.11129 ?  56  LEU A CB    1 
ATOM   372  C CG    . LEU A 1 76  ? -12.25300 -8.34700  33.98700 1.000 26.68555 ?  56  LEU A CG    1 
ATOM   373  C CD1   . LEU A 1 76  ? -13.65400 -8.87100  34.28900 1.000 21.89664 ?  56  LEU A CD1   1 
ATOM   374  C CD2   . LEU A 1 76  ? -11.81900 -7.26200  34.98100 1.000 25.52201 ?  56  LEU A CD2   1 
ATOM   375  N N     . GLY A 1 77  ? -12.69300 -10.52300 30.96600 1.000 24.49938 ?  57  GLY A N     1 
ATOM   376  C CA    . GLY A 1 77  ? -12.74000 -10.61600 29.51700 1.000 26.15832 ?  57  GLY A CA    1 
ATOM   377  C C     . GLY A 1 77  ? -12.34900 -11.99300 29.02100 1.000 25.94464 ?  57  GLY A C     1 
ATOM   378  O O     . GLY A 1 77  ? -11.57900 -12.11300 28.05800 1.000 24.35020 ?  57  GLY A O     1 
ATOM   379  N N     . CYS A 1 78  ? -12.86700 -13.04300 29.65500 1.000 20.52253 ?  58  CYS A N     1 
ATOM   380  C CA    . CYS A 1 78  ? -12.36300 -14.39200 29.44100 1.000 24.95022 ?  58  CYS A CA    1 
ATOM   381  C C     . CYS A 1 78  ? -12.75300 -14.98300 28.09000 1.000 24.85113 ?  58  CYS A C     1 
ATOM   382  O O     . CYS A 1 78  ? -12.18900 -16.01500 27.71200 1.000 26.43847 ?  58  CYS A O     1 
ATOM   383  C CB    . CYS A 1 78  ? -12.84600 -15.30700 30.57000 1.000 22.47923 ?  58  CYS A CB    1 
ATOM   384  S SG    . CYS A 1 78  ? -14.63700 -15.50100 30.61200 1.000 22.96579 ?  58  CYS A SG    1 
ATOM   385  N N     . ALA A 1 79  ? -13.66900 -14.35500 27.35100 1.000 24.15795 ?  59  ALA A N     1 
ATOM   386  C CA    . ALA A 1 79  ? -14.16300 -14.92100 26.09600 1.000 23.96888 ?  59  ALA A CA    1 
ATOM   387  C C     . ALA A 1 79  ? -14.54400 -16.39000 26.29900 1.000 26.51566 ?  59  ALA A C     1 
ATOM   388  O O     . ALA A 1 79  ? -15.29200 -16.70600 27.22800 1.000 25.60427 ?  59  ALA A O     1 
ATOM   389  C CB    . ALA A 1 79  ? -13.12600 -14.75800 24.97900 1.000 23.26408 ?  59  ALA A CB    1 
ATOM   390  N N     . THR A 1 80  ? -14.02700 -17.30900 25.47400 1.000 24.01730 ?  60  THR A N     1 
ATOM   391  C CA    . THR A 1 80  ? -14.50600 -18.68500 25.56800 1.000 23.69522 ?  60  THR A CA    1 
ATOM   392  C C     . THR A 1 80  ? -13.79700 -19.49300 26.66800 1.000 25.88972 ?  60  THR A C     1 
ATOM   393  O O     . THR A 1 80  ? -13.90900 -20.72900 26.69600 1.000 24.90872 ?  60  THR A O     1 
ATOM   394  C CB    . THR A 1 80  ? -14.39900 -19.38500 24.20700 1.000 24.21223 ?  60  THR A CB    1 
ATOM   395  O OG1   . THR A 1 80  ? -13.16300 -19.04600 23.56900 1.000 25.77168 ?  60  THR A OG1   1 
ATOM   396  C CG2   . THR A 1 80  ? -15.54600 -18.92100 23.29800 1.000 23.75085 ?  60  THR A CG2   1 
ATOM   397  N N     . GLY A 1 81  ? -13.08400 -18.82100 27.57600 1.000 25.01016 ?  61  GLY A N     1 
ATOM   398  C CA    . GLY A 1 81  ? -12.72100 -19.38300 28.86600 1.000 24.42156 ?  61  GLY A CA    1 
ATOM   399  C C     . GLY A 1 81  ? -11.42400 -20.16500 28.95700 1.000 22.27625 ?  61  GLY A C     1 
ATOM   400  O O     . GLY A 1 81  ? -11.11600 -20.67500 30.03800 1.000 26.98472 ?  61  GLY A O     1 
ATOM   401  N N     . ARG A 1 82  ? -10.63400 -20.25700 27.88200 1.000 24.85072 ?  62  ARG A N     1 
ATOM   402  C CA    . ARG A 1 82  ? -9.45600  -21.12600 27.91300 1.000 26.60193 ?  62  ARG A CA    1 
ATOM   403  C C     . ARG A 1 82  ? -8.48300  -20.74000 29.02200 1.000 26.35818 ?  62  ARG A C     1 
ATOM   404  O O     . ARG A 1 82  ? -7.90900  -21.61900 29.68300 1.000 26.34551 ?  62  ARG A O     1 
ATOM   405  C CB    . ARG A 1 82  ? -8.73400  -21.11500 26.56800 1.000 27.87249 ?  62  ARG A CB    1 
ATOM   406  C CG    . ARG A 1 82  ? -7.39500  -21.88500 26.58900 1.000 24.56660 ?  62  ARG A CG    1 
ATOM   407  C CD    . ARG A 1 82  ? -7.60600  -23.37700 26.80000 1.000 27.25361 ?  62  ARG A CD    1 
ATOM   408  N NE    . ARG A 1 82  ? -6.35100  -24.09800 26.96900 1.000 24.82437 ?  62  ARG A NE    1 
ATOM   409  C CZ    . ARG A 1 82  ? -5.61700  -24.56100 25.96500 1.000 28.08124 ?  62  ARG A CZ    1 
ATOM   410  N NH1   . ARG A 1 82  ? -5.98100  -24.38700 24.70400 1.000 25.42550 ?  62  ARG A NH1   1 
ATOM   411  N NH2   . ARG A 1 82  ? -4.47500  -25.19100 26.23100 1.000 28.61260 ?  62  ARG A NH2   1 
ATOM   412  N N     . ALA A 1 83  ? -8.28300  -19.43800 29.24500 1.000 21.77226 ?  63  ALA A N     1 
ATOM   413  C CA    . ALA A 1 83  ? -7.30700  -19.02100 30.25000 1.000 23.32400 ?  63  ALA A CA    1 
ATOM   414  C C     . ALA A 1 83  ? -7.81900  -19.26300 31.66500 1.000 24.62115 ?  63  ALA A C     1 
ATOM   415  O O     . ALA A 1 83  ? -7.01500  -19.44500 32.58800 1.000 22.70837 ?  63  ALA A O     1 
ATOM   416  C CB    . ALA A 1 83  ? -6.93800  -17.54700 30.05800 1.000 20.19473 ?  63  ALA A CB    1 
ATOM   417  N N     . SER A 1 84  ? -9.14300  -19.27400 31.85500 1.000 21.35845 ?  64  SER A N     1 
ATOM   418  C CA    . SER A 1 84  ? -9.69900  -19.62700 33.15700 1.000 22.97025 ?  64  SER A CA    1 
ATOM   419  C C     . SER A 1 84  ? -9.37300  -21.06900 33.52200 1.000 26.03117 ?  64  SER A C     1 
ATOM   420  O O     . SER A 1 84  ? -8.89500  -21.34600 34.62900 1.000 23.59202 ?  64  SER A O     1 
ATOM   421  C CB    . SER A 1 84  ? -11.20900 -19.39000 33.16700 1.000 23.50902 ?  64  SER A CB    1 
ATOM   422  O OG    . SER A 1 84  ? -11.49600 -18.07900 32.72800 1.000 25.45707 ?  64  SER A OG    1 
ATOM   423  N N     . PHE A 1 85  ? -9.63200  -22.00500 32.59900 1.000 24.40181 ?  65  PHE A N     1 
ATOM   424  C CA    . PHE A 1 85  ? -9.27300  -23.40400 32.82400 1.000 24.43989 ?  65  PHE A CA    1 
ATOM   425  C C     . PHE A 1 85  ? -7.79000  -23.55700 33.14500 1.000 26.01339 ?  65  PHE A C     1 
ATOM   426  O O     . PHE A 1 85  ? -7.41800  -24.30100 34.05700 1.000 27.67392 ?  65  PHE A O     1 
ATOM   427  C CB    . PHE A 1 85  ? -9.62900  -24.24300 31.59700 1.000 21.39389 ?  65  PHE A CB    1 
ATOM   428  C CG    . PHE A 1 85  ? -11.11000 -24.32300 31.31200 1.000 22.28765 ?  65  PHE A CG    1 
ATOM   429  C CD1   . PHE A 1 85  ? -12.00500 -24.65800 32.30600 1.000 23.19691 ?  65  PHE A CD1   1 
ATOM   430  C CD2   . PHE A 1 85  ? -11.59500 -24.08600 30.03800 1.000 24.97626 ?  65  PHE A CD2   1 
ATOM   431  C CE1   . PHE A 1 85  ? -13.35800 -24.74900 32.04700 1.000 25.15857 ?  65  PHE A CE1   1 
ATOM   432  C CE2   . PHE A 1 85  ? -12.95400 -24.17200 29.76200 1.000 26.86218 ?  65  PHE A CE2   1 
ATOM   433  C CZ    . PHE A 1 85  ? -13.83700 -24.51200 30.77100 1.000 27.83456 ?  65  PHE A CZ    1 
ATOM   434  N N     . GLU A 1 86  ? -6.92400  -22.85700 32.40600 1.000 27.96399 ?  66  GLU A N     1 
ATOM   435  C CA    . GLU A 1 86  ? -5.48900  -22.99900 32.64000 1.000 30.25146 ?  66  GLU A CA    1 
ATOM   436  C C     . GLU A 1 86  ? -5.08300  -22.42400 33.99100 1.000 28.60046 ?  66  GLU A C     1 
ATOM   437  O O     . GLU A 1 86  ? -4.25100  -23.01300 34.68700 1.000 26.81330 ?  66  GLU A O     1 
ATOM   438  C CB    . GLU A 1 86  ? -4.69400  -22.33400 31.51700 1.000 24.17104 ?  66  GLU A CB    1 
ATOM   439  C CG    . GLU A 1 86  ? -4.90900  -22.96900 30.14600 1.000 27.58921 ?  66  GLU A CG    1 
ATOM   440  C CD    . GLU A 1 86  ? -4.36500  -24.39300 30.05400 1.000 30.09799 ?  66  GLU A CD    1 
ATOM   441  O OE1   . GLU A 1 86  ? -3.66500  -24.84600 30.99200 1.000 25.19882 ?  66  GLU A OE1   1 
ATOM   442  O OE2   . GLU A 1 86  ? -4.64700  -25.06300 29.03600 1.000 29.63376 -1 66  GLU A OE2   1 
ATOM   443  N N     . LEU A 1 87  ? -5.64600  -21.27000 34.37800 1.000 27.44892 ?  67  LEU A N     1 
ATOM   444  C CA    . LEU A 1 87  ? -5.32300  -20.70600 35.68900 1.000 25.70657 ?  67  LEU A CA    1 
ATOM   445  C C     . LEU A 1 87  ? -5.76600  -21.63400 36.81600 1.000 30.82010 ?  67  LEU A C     1 
ATOM   446  O O     . LEU A 1 87  ? -5.11600  -21.69600 37.86800 1.000 27.87875 ?  67  LEU A O     1 
ATOM   447  C CB    . LEU A 1 87  ? -5.97400  -19.33600 35.86200 1.000 24.77833 ?  67  LEU A CB    1 
ATOM   448  C CG    . LEU A 1 87  ? -5.30400  -18.13000 35.20700 1.000 28.98197 ?  67  LEU A CG    1 
ATOM   449  C CD1   . LEU A 1 87  ? -6.20300  -16.90300 35.36100 1.000 27.67386 ?  67  LEU A CD1   1 
ATOM   450  C CD2   . LEU A 1 87  ? -3.92000  -17.88100 35.79500 1.000 24.12564 ?  67  LEU A CD2   1 
ATOM   451  N N     . ALA A 1 88  ? -6.86400  -22.36300 36.61200 1.000 27.60272 ?  68  ALA A N     1 
ATOM   452  C CA    . ALA A 1 88  ? -7.37400  -23.28300 37.61600 1.000 26.05327 ?  68  ALA A CA    1 
ATOM   453  C C     . ALA A 1 88  ? -6.45200  -24.47400 37.86400 1.000 32.04195 ?  68  ALA A C     1 
ATOM   454  O O     . ALA A 1 88  ? -6.63200  -25.17000 38.86700 1.000 31.82448 ?  68  ALA A O     1 
ATOM   455  C CB    . ALA A 1 88  ? -8.76200  -23.78000 37.20100 1.000 27.59743 ?  68  ALA A CB    1 
ATOM   456  N N     . ARG A 1 89  ? -5.48000  -24.73400 36.99100 1.000 29.28566 ?  69  ARG A N     1 
ATOM   457  C CA    . ARG A 1 89  ? -4.51800  -25.79300 37.27800 1.000 32.32901 ?  69  ARG A CA    1 
ATOM   458  C C     . ARG A 1 89  ? -3.60000  -25.42300 38.43200 1.000 33.35664 ?  69  ARG A C     1 
ATOM   459  O O     . ARG A 1 89  ? -2.98900  -26.31000 39.03300 1.000 32.91887 ?  69  ARG A O     1 
ATOM   460  C CB    . ARG A 1 89  ? -3.68300  -26.11400 36.03700 1.000 30.27811 ?  69  ARG A CB    1 
ATOM   461  C CG    . ARG A 1 89  ? -4.50300  -26.49500 34.81600 1.000 27.02896 ?  69  ARG A CG    1 
ATOM   462  C CD    . ARG A 1 89  ? -3.65200  -27.24700 33.80100 1.000 29.29568 ?  69  ARG A CD    1 
ATOM   463  N NE    . ARG A 1 89  ? -3.38300  -28.61700 34.22600 1.000 33.14761 ?  69  ARG A NE    1 
ATOM   464  C CZ    . ARG A 1 89  ? -2.33500  -29.33600 33.83800 1.000 34.75842 ?  69  ARG A CZ    1 
ATOM   465  N NH1   . ARG A 1 89  ? -1.42800  -28.84900 33.00300 1.000 29.32553 ?  69  ARG A NH1   1 
ATOM   466  N NH2   . ARG A 1 89  ? -2.20300  -30.58200 34.28700 1.000 31.24386 ?  69  ARG A NH2   1 
ATOM   467  N N     . SER A 1 90  ? -3.50100  -24.14000 38.75800 1.000 32.62794 ?  70  SER A N     1 
ATOM   468  C CA    . SER A 1 90  ? -2.67000  -23.66400 39.84900 1.000 32.04813 ?  70  SER A CA    1 
ATOM   469  C C     . SER A 1 90  ? -3.44500  -22.98700 40.96200 1.000 31.47982 ?  70  SER A C     1 
ATOM   470  O O     . SER A 1 90  ? -2.97200  -22.97400 42.09600 1.000 37.64544 ?  70  SER A O     1 
ATOM   471  C CB    . SER A 1 90  ? -1.62200  -22.67600 39.32600 1.000 33.96288 ?  70  SER A CB    1 
ATOM   472  O OG    . SER A 1 90  ? -0.64700  -23.36100 38.56500 1.000 46.11342 ?  70  SER A OG    1 
ATOM   473  N N     . TYR A 1 91  ? -4.61100  -22.42600 40.67700 1.000 31.28046 ?  71  TYR A N     1 
ATOM   474  C CA    . TYR A 1 91  ? -5.37100  -21.68500 41.67200 1.000 32.88500 ?  71  TYR A CA    1 
ATOM   475  C C     . TYR A 1 91  ? -6.49800  -22.54800 42.21500 1.000 33.80802 ?  71  TYR A C     1 
ATOM   476  O O     . TYR A 1 91  ? -6.98900  -23.45400 41.53600 1.000 33.64939 ?  71  TYR A O     1 
ATOM   477  C CB    . TYR A 1 91  ? -5.92900  -20.38700 41.07700 1.000 30.41239 ?  71  TYR A CB    1 
ATOM   478  C CG    . TYR A 1 91  ? -4.88500  -19.30000 41.01300 1.000 32.58254 ?  71  TYR A CG    1 
ATOM   479  C CD1   . TYR A 1 91  ? -3.88000  -19.33200 40.04900 1.000 33.55260 ?  71  TYR A CD1   1 
ATOM   480  C CD2   . TYR A 1 91  ? -4.87800  -18.26400 41.93200 1.000 31.63912 ?  71  TYR A CD2   1 
ATOM   481  C CE1   . TYR A 1 91  ? -2.90700  -18.34300 39.99200 1.000 30.61525 ?  71  TYR A CE1   1 
ATOM   482  C CE2   . TYR A 1 91  ? -3.90500  -17.26400 41.87900 1.000 32.84263 ?  71  TYR A CE2   1 
ATOM   483  C CZ    . TYR A 1 91  ? -2.92400  -17.31400 40.91200 1.000 30.74196 ?  71  TYR A CZ    1 
ATOM   484  O OH    . TYR A 1 91  ? -1.95600  -16.33300 40.86900 1.000 33.87512 ?  71  TYR A OH    1 
ATOM   485  N N     . LYS A 1 92  ? -6.89300  -22.27200 43.46000 1.000 32.58423 ?  72  LYS A N     1 
ATOM   486  C CA    . LYS A 1 92  ? -7.95700  -23.06100 44.06900 1.000 31.62957 ?  72  LYS A CA    1 
ATOM   487  C C     . LYS A 1 92  ? -9.32500  -22.70700 43.49500 1.000 34.91540 ?  72  LYS A C     1 
ATOM   488  O O     . LYS A 1 92  ? -10.20100 -23.57800 43.41500 1.000 33.48412 ?  72  LYS A O     1 
ATOM   489  C CB    . LYS A 1 92  ? -7.94700  -22.88300 45.58900 1.000 35.10040 ?  72  LYS A CB    1 
ATOM   490  C CG    . LYS A 1 92  ? -6.64600  -23.29800 46.26200 1.000 35.90553 ?  72  LYS A CG    1 
ATOM   491  N N     . HIS A 1 93  ? -9.53200  -21.44800 43.09800 1.000 31.14430 ?  73  HIS A N     1 
ATOM   492  C CA    . HIS A 1 93  ? -10.77400 -21.02100 42.46800 1.000 30.24881 ?  73  HIS A CA    1 
ATOM   493  C C     . HIS A 1 93  ? -10.47200 -19.96900 41.41300 1.000 30.40148 ?  73  HIS A C     1 
ATOM   494  O O     . HIS A 1 93  ? -9.65700  -19.07000 41.64300 1.000 31.57796 ?  73  HIS A O     1 
ATOM   495  C CB    . HIS A 1 93  ? -11.77300 -20.43000 43.47000 1.000 30.84857 ?  73  HIS A CB    1 
ATOM   496  C CG    . HIS A 1 93  ? -13.05000 -19.97400 42.82800 1.000 33.56721 ?  73  HIS A CG    1 
ATOM   497  N ND1   . HIS A 1 93  ? -13.98300 -20.85300 42.31700 1.000 31.23371 ?  73  HIS A ND1   1 
ATOM   498  C CD2   . HIS A 1 93  ? -13.52700 -18.73100 42.57100 1.000 31.64813 ?  73  HIS A CD2   1 
ATOM   499  C CE1   . HIS A 1 93  ? -14.98700 -20.17200 41.79200 1.000 33.61093 ?  73  HIS A CE1   1 
ATOM   500  N NE2   . HIS A 1 93  ? -14.73700 -18.88200 41.93500 1.000 30.47429 ?  73  HIS A NE2   1 
ATOM   501  N N     . VAL A 1 94  ? -11.14200 -20.07200 40.26600 1.000 26.20927 ?  74  VAL A N     1 
ATOM   502  C CA    . VAL A 1 94  ? -11.01200 -19.10000 39.18900 1.000 27.73585 ?  74  VAL A CA    1 
ATOM   503  C C     . VAL A 1 94  ? -12.40100 -18.65600 38.76400 1.000 28.20478 ?  74  VAL A C     1 
ATOM   504  O O     . VAL A 1 94  ? -13.26400 -19.49100 38.47000 1.000 25.68729 ?  74  VAL A O     1 
ATOM   505  C CB    . VAL A 1 94  ? -10.24700 -19.65700 37.97400 1.000 27.71987 ?  74  VAL A CB    1 
ATOM   506  C CG1   . VAL A 1 94  ? -10.10800 -18.56200 36.90400 1.000 25.58059 ?  74  VAL A CG1   1 
ATOM   507  C CG2   . VAL A 1 94  ? -8.88700  -20.17300 38.38600 1.000 23.11081 ?  74  VAL A CG2   1 
ATOM   508  N N     . ASP A 1 95  ? -12.61100 -17.34700 38.72100 1.000 28.63655 ?  75  ASP A N     1 
ATOM   509  C CA    . ASP A 1 95  ? -13.79900 -16.77000 38.11800 1.000 24.50795 ?  75  ASP A CA    1 
ATOM   510  C C     . ASP A 1 95  ? -13.43700 -16.31900 36.71100 1.000 27.94104 ?  75  ASP A C     1 
ATOM   511  O O     . ASP A 1 95  ? -12.42100 -15.64100 36.51100 1.000 30.85152 ?  75  ASP A O     1 
ATOM   512  C CB    . ASP A 1 95  ? -14.32800 -15.59800 38.94400 1.000 25.55968 ?  75  ASP A CB    1 
ATOM   513  C CG    . ASP A 1 95  ? -14.80900 -16.02800 40.32300 1.000 31.80449 ?  75  ASP A CG    1 
ATOM   514  O OD1   . ASP A 1 95  ? -15.59500 -16.99700 40.40100 1.000 27.64727 ?  75  ASP A OD1   1 
ATOM   515  O OD2   . ASP A 1 95  ? -14.42200 -15.38600 41.32400 1.000 30.31407 -1 75  ASP A OD2   1 
ATOM   516  N N     . GLY A 1 96  ? -14.24400 -16.73100 35.73900 1.000 25.89364 ?  76  GLY A N     1 
ATOM   517  C CA    . GLY A 1 96  ? -14.11500 -16.24600 34.38300 1.000 22.17090 ?  76  GLY A CA    1 
ATOM   518  C C     . GLY A 1 96  ? -15.28400 -15.33300 34.10300 1.000 25.61643 ?  76  GLY A C     1 
ATOM   519  O O     . GLY A 1 96  ? -16.43700 -15.75300 34.23000 1.000 26.21763 ?  76  GLY A O     1 
ATOM   520  N N     . VAL A 1 97  ? -15.01200 -14.07900 33.76100 1.000 22.95858 ?  77  VAL A N     1 
ATOM   521  C CA    . VAL A 1 97  ? -16.05400 -13.08000 33.55400 1.000 23.39119 ?  77  VAL A CA    1 
ATOM   522  C C     . VAL A 1 97  ? -15.88600 -12.48500 32.16400 1.000 24.26204 ?  77  VAL A C     1 
ATOM   523  O O     . VAL A 1 97  ? -14.76100 -12.21400 31.72600 1.000 24.41430 ?  77  VAL A O     1 
ATOM   524  C CB    . VAL A 1 97  ? -16.00300 -11.98100 34.64000 1.000 25.80315 ?  77  VAL A CB    1 
ATOM   525  C CG1   . VAL A 1 97  ? -16.95700 -10.83400 34.30700 1.000 23.71929 ?  77  VAL A CG1   1 
ATOM   526  C CG2   . VAL A 1 97  ? -16.33300 -12.57800 36.01500 1.000 23.20800 ?  77  VAL A CG2   1 
ATOM   527  N N     . ASP A 1 98  ? -17.00300 -12.30000 31.46500 1.000 24.18503 ?  78  ASP A N     1 
ATOM   528  C CA    . ASP A 1 98  ? -16.99400 -11.62300 30.17800 1.000 26.12681 ?  78  ASP A CA    1 
ATOM   529  C C     . ASP A 1 98  ? -18.32300 -10.92200 29.98300 1.000 26.82867 ?  78  ASP A C     1 
ATOM   530  O O     . ASP A 1 98  ? -19.36200 -11.38900 30.45200 1.000 26.76893 ?  78  ASP A O     1 
ATOM   531  C CB    . ASP A 1 98  ? -16.74900 -12.58000 29.00400 1.000 24.79773 ?  78  ASP A CB    1 
ATOM   532  C CG    . ASP A 1 98  ? -16.23300 -11.85700 27.76200 1.000 27.97406 ?  78  ASP A CG    1 
ATOM   533  O OD1   . ASP A 1 98  ? -17.04800 -11.22900 27.03400 1.000 25.31268 ?  78  ASP A OD1   1 
ATOM   534  O OD2   . ASP A 1 98  ? -15.00300 -11.91300 27.52100 1.000 27.22605 -1 78  ASP A OD2   1 
ATOM   535  N N     . TYR A 1 99  ? -18.27900 -9.79500  29.27100 1.000 27.46068 ?  79  TYR A N     1 
ATOM   536  C CA    . TYR A 1 99  ? -19.49600 -9.04800  28.98600 1.000 29.19520 ?  79  TYR A CA    1 
ATOM   537  C C     . TYR A 1 99  ? -20.41100 -9.77700  28.00600 1.000 30.92461 ?  79  TYR A C     1 
ATOM   538  O O     . TYR A 1 99  ? -21.61900 -9.52300  28.00300 1.000 30.85988 ?  79  TYR A O     1 
ATOM   539  C CB    . TYR A 1 99  ? -19.13000 -7.66200  28.45700 1.000 29.15092 ?  79  TYR A CB    1 
ATOM   540  C CG    . TYR A 1 99  ? -20.30800 -6.72400  28.33000 1.000 36.13872 ?  79  TYR A CG    1 
ATOM   541  C CD1   . TYR A 1 99  ? -20.73500 -5.96500  29.41200 1.000 37.32386 ?  79  TYR A CD1   1 
ATOM   542  C CD2   . TYR A 1 99  ? -21.01400 -6.62200  27.13800 1.000 40.83472 ?  79  TYR A CD2   1 
ATOM   543  C CE1   . TYR A 1 99  ? -21.81400 -5.11300  29.30500 1.000 42.76009 ?  79  TYR A CE1   1 
ATOM   544  C CE2   . TYR A 1 99  ? -22.09700 -5.77300  27.02100 1.000 42.62808 ?  79  TYR A CE2   1 
ATOM   545  C CZ    . TYR A 1 99  ? -22.49400 -5.02100  28.10600 1.000 46.23696 ?  79  TYR A CZ    1 
ATOM   546  O OH    . TYR A 1 99  ? -23.57800 -4.17400  27.98700 1.000 57.28038 ?  79  TYR A OH    1 
ATOM   547  N N     . SER A 1 100 ? -19.87700 -10.69100 27.19800 1.000 28.82558 ?  80  SER A N     1 
ATOM   548  C CA    . SER A 1 100 ? -20.66500 -11.40400 26.20000 1.000 29.29858 ?  80  SER A CA    1 
ATOM   549  C C     . SER A 1 100 ? -21.28900 -12.65300 26.82100 1.000 29.92207 ?  80  SER A C     1 
ATOM   550  O O     . SER A 1 100 ? -20.57300 -13.55000 27.29200 1.000 24.86185 ?  80  SER A O     1 
ATOM   551  C CB    . SER A 1 100 ? -19.79600 -11.77000 24.99700 1.000 30.62634 ?  80  SER A CB    1 
ATOM   552  O OG    . SER A 1 100 ? -20.40300 -12.78500 24.21600 1.000 29.75898 ?  80  SER A OG    1 
ATOM   553  N N     . GLN A 1 101 ? -22.62500 -12.71000 26.82300 1.000 30.22861 ?  81  GLN A N     1 
ATOM   554  C CA    . GLN A 1 101 ? -23.31100 -13.91900 27.27600 1.000 30.13471 ?  81  GLN A CA    1 
ATOM   555  C C     . GLN A 1 101 ? -23.00900 -15.08800 26.35200 1.000 28.85853 ?  81  GLN A C     1 
ATOM   556  O O     . GLN A 1 101 ? -22.86700 -16.22900 26.80600 1.000 29.04740 ?  81  GLN A O     1 
ATOM   557  C CB    . GLN A 1 101 ? -24.81900 -13.68000 27.34500 1.000 33.02200 ?  81  GLN A CB    1 
ATOM   558  C CG    . GLN A 1 101 ? -25.59100 -14.83000 27.99400 1.000 27.46871 ?  81  GLN A CG    1 
ATOM   559  C CD    . GLN A 1 101 ? -25.25100 -14.98400 29.46300 1.000 32.61138 ?  81  GLN A CD    1 
ATOM   560  O OE1   . GLN A 1 101 ? -25.46000 -14.06100 30.25300 1.000 33.50969 ?  81  GLN A OE1   1 
ATOM   561  N NE2   . GLN A 1 101 ? -24.72700 -16.14500 29.83800 1.000 33.39691 ?  81  GLN A NE2   1 
ATOM   562  N N     . ALA A 1 102 ? -22.91300 -14.81700 25.04600 1.000 28.54429 ?  82  ALA A N     1 
ATOM   563  C CA    . ALA A 1 102 ? -22.54500 -15.85700 24.09400 1.000 29.95320 ?  82  ALA A CA    1 
ATOM   564  C C     . ALA A 1 102 ? -21.21500 -16.49800 24.46500 1.000 29.79575 ?  82  ALA A C     1 
ATOM   565  O O     . ALA A 1 102 ? -21.07600 -17.72600 24.42100 1.000 27.46479 ?  82  ALA A O     1 
ATOM   566  C CB    . ALA A 1 102 ? -22.48400 -15.27900 22.68200 1.000 28.19322 ?  82  ALA A CB    1 
ATOM   567  N N     . PHE A 1 103 ? -20.21600 -15.68300 24.81600 1.000 28.63435 ?  83  PHE A N     1 
ATOM   568  C CA    . PHE A 1 103 ? -18.93500 -16.24100 25.24700 1.000 25.44554 ?  83  PHE A CA    1 
ATOM   569  C C     . PHE A 1 103 ? -19.09900 -17.05200 26.52800 1.000 25.67724 ?  83  PHE A C     1 
ATOM   570  O O     . PHE A 1 103 ? -18.51900 -18.13700 26.67000 1.000 26.63272 ?  83  PHE A O     1 
ATOM   571  C CB    . PHE A 1 103 ? -17.91700 -15.11600 25.46000 1.000 25.87984 ?  83  PHE A CB    1 
ATOM   572  C CG    . PHE A 1 103 ? -17.33100 -14.57000 24.19200 1.000 26.43320 ?  83  PHE A CG    1 
ATOM   573  C CD1   . PHE A 1 103 ? -17.39500 -15.29500 23.01000 1.000 27.59483 ?  83  PHE A CD1   1 
ATOM   574  C CD2   . PHE A 1 103 ? -16.69700 -13.33100 24.18200 1.000 27.83463 ?  83  PHE A CD2   1 
ATOM   575  C CE1   . PHE A 1 103 ? -16.85200 -14.79300 21.83400 1.000 27.64210 ?  83  PHE A CE1   1 
ATOM   576  C CE2   . PHE A 1 103 ? -16.14700 -12.81900 23.00600 1.000 29.91431 ?  83  PHE A CE2   1 
ATOM   577  C CZ    . PHE A 1 103 ? -16.22300 -13.55800 21.82800 1.000 29.49101 ?  83  PHE A CZ    1 
ATOM   578  N N     . VAL A 1 104 ? -19.88500 -16.53700 27.47600 1.000 25.37253 ?  84  VAL A N     1 
ATOM   579  C CA    . VAL A 1 104 ? -20.06600 -17.21900 28.75500 1.000 27.32284 ?  84  VAL A CA    1 
ATOM   580  C C     . VAL A 1 104 ? -20.77500 -18.55400 28.55700 1.000 26.41608 ?  84  VAL A C     1 
ATOM   581  O O     . VAL A 1 104 ? -20.39800 -19.57000 29.15900 1.000 31.57505 ?  84  VAL A O     1 
ATOM   582  C CB    . VAL A 1 104 ? -20.83300 -16.30900 29.73300 1.000 26.75184 ?  84  VAL A CB    1 
ATOM   583  C CG1   . VAL A 1 104 ? -21.29600 -17.10500 30.96300 1.000 26.92256 ?  84  VAL A CG1   1 
ATOM   584  C CG2   . VAL A 1 104 ? -19.97600 -15.10400 30.13600 1.000 27.75479 ?  84  VAL A CG2   1 
ATOM   585  N N     . ASP A 1 105 ? -21.82100 -18.57100 27.72500 1.000 26.76099 ?  85  ASP A N     1 
ATOM   586  C CA    . ASP A 1 105 ? -22.52700 -19.82200 27.44700 1.000 29.05570 ?  85  ASP A CA    1 
ATOM   587  C C     . ASP A 1 105 ? -21.58600 -20.86600 26.85700 1.000 27.52101 ?  85  ASP A C     1 
ATOM   588  O O     . ASP A 1 105 ? -21.59800 -22.02800 27.27600 1.000 25.76312 ?  85  ASP A O     1 
ATOM   589  C CB    . ASP A 1 105 ? -23.69800 -19.57700 26.49300 1.000 30.34237 ?  85  ASP A CB    1 
ATOM   590  C CG    . ASP A 1 105 ? -24.75800 -18.65300 27.07500 1.000 33.57530 ?  85  ASP A CG    1 
ATOM   591  O OD1   . ASP A 1 105 ? -24.80200 -18.46100 28.31300 1.000 31.78698 ?  85  ASP A OD1   1 
ATOM   592  O OD2   . ASP A 1 105 ? -25.55100 -18.10900 26.27300 1.000 36.66234 -1 85  ASP A OD2   1 
ATOM   593  N N     . ALA A 1 106 ? -20.75200 -20.46100 25.89100 1.000 29.55648 ?  86  ALA A N     1 
ATOM   594  C CA    . ALA A 1 106 ? -19.84300 -21.40400 25.24500 1.000 28.54682 ?  86  ALA A CA    1 
ATOM   595  C C     . ALA A 1 106 ? -18.87100 -21.99900 26.25000 1.000 29.41183 ?  86  ALA A C     1 
ATOM   596  O O     . ALA A 1 106 ? -18.65400 -23.21800 26.27400 1.000 24.06867 ?  86  ALA A O     1 
ATOM   597  C CB    . ALA A 1 106 ? -19.08000 -20.72100 24.11000 1.000 25.39993 ?  86  ALA A CB    1 
ATOM   598  N N     . ALA A 1 107 ? -18.27000 -21.14800 27.08600 1.000 24.46645 ?  87  ALA A N     1 
ATOM   599  C CA    . ALA A 1 107 ? -17.34300 -21.63200 28.10100 1.000 28.06734 ?  87  ALA A CA    1 
ATOM   600  C C     . ALA A 1 107 ? -18.04400 -22.57700 29.06800 1.000 27.66261 ?  87  ALA A C     1 
ATOM   601  O O     . ALA A 1 107 ? -17.52000 -23.64600 29.40700 1.000 27.29948 ?  87  ALA A O     1 
ATOM   602  C CB    . ALA A 1 107 ? -16.72900 -20.44900 28.85600 1.000 25.37160 ?  87  ALA A CB    1 
ATOM   603  N N     . THR A 1 108 ? -19.24100 -22.19400 29.51700 1.000 26.68627 ?  88  THR A N     1 
ATOM   604  C CA    . THR A 1 108 ? -19.99600 -23.03600 30.43800 1.000 28.72668 ?  88  THR A CA    1 
ATOM   605  C C     . THR A 1 108 ? -20.38400 -24.36200 29.78700 1.000 28.42392 ?  88  THR A C     1 
ATOM   606  O O     . THR A 1 108 ? -20.33500 -25.41700 30.43500 1.000 27.42912 ?  88  THR A O     1 
ATOM   607  C CB    . THR A 1 108 ? -21.23500 -22.28900 30.93000 1.000 26.34441 ?  88  THR A CB    1 
ATOM   608  O OG1   . THR A 1 108 ? -20.85200 -20.99600 31.41800 1.000 30.78534 ?  88  THR A OG1   1 
ATOM   609  C CG2   . THR A 1 108 ? -21.90300 -23.05300 32.05400 1.000 33.17125 ?  88  THR A CG2   1 
ATOM   610  N N     . GLU A 1 109 ? -20.77600 -24.32600 28.51100 1.000 28.60649 ?  89  GLU A N     1 
ATOM   611  C CA    . GLU A 1 109 ? -21.16100 -25.54900 27.81200 1.000 29.15985 ?  89  GLU A CA    1 
ATOM   612  C C     . GLU A 1 109 ? -19.99300 -26.51700 27.72400 1.000 30.14669 ?  89  GLU A C     1 
ATOM   613  O O     . GLU A 1 109 ? -20.15500 -27.72200 27.94400 1.000 32.96605 ?  89  GLU A O     1 
ATOM   614  C CB    . GLU A 1 109 ? -21.68200 -25.22100 26.41100 1.000 28.97088 ?  89  GLU A CB    1 
ATOM   615  N N     . LEU A 1 110 ? -18.80600 -26.00700 27.40000 1.000 26.85719 ?  90  LEU A N     1 
ATOM   616  C CA    . LEU A 1 110 ? -17.62700 -26.86300 27.35700 1.000 28.91198 ?  90  LEU A CA    1 
ATOM   617  C C     . LEU A 1 110 ? -17.30700 -27.41400 28.73700 1.000 31.52762 ?  90  LEU A C     1 
ATOM   618  O O     . LEU A 1 110 ? -16.95500 -28.59200 28.88300 1.000 33.02582 ?  90  LEU A O     1 
ATOM   619  C CB    . LEU A 1 110 ? -16.43600 -26.08400 26.80500 1.000 26.02245 ?  90  LEU A CB    1 
ATOM   620  C CG    . LEU A 1 110 ? -15.09800 -26.81700 26.80100 1.000 27.65976 ?  90  LEU A CG    1 
ATOM   621  C CD1   . LEU A 1 110 ? -15.15000 -28.04400 25.88900 1.000 25.33099 ?  90  LEU A CD1   1 
ATOM   622  C CD2   . LEU A 1 110 ? -13.97700 -25.86200 26.39400 1.000 25.37363 ?  90  LEU A CD2   1 
ATOM   623  N N     . GLN A 1 111 ? -17.42900 -26.57300 29.76500 1.000 26.97435 ?  91  GLN A N     1 
ATOM   624  C CA    . GLN A 1 111 ? -17.12500 -27.00800 31.12100 1.000 27.90115 ?  91  GLN A CA    1 
ATOM   625  C C     . GLN A 1 111 ? -18.07100 -28.11800 31.56800 1.000 32.13483 ?  91  GLN A C     1 
ATOM   626  O O     . GLN A 1 111 ? -17.63100 -29.15300 32.07900 1.000 29.10647 ?  91  GLN A O     1 
ATOM   627  C CB    . GLN A 1 111 ? -17.19600 -25.80800 32.06600 1.000 30.09790 ?  91  GLN A CB    1 
ATOM   628  C CG    . GLN A 1 111 ? -17.04100 -26.14200 33.52800 1.000 29.24127 ?  91  GLN A CG    1 
ATOM   629  C CD    . GLN A 1 111 ? -17.30200 -24.93800 34.41700 1.000 31.91957 ?  91  GLN A CD    1 
ATOM   630  O OE1   . GLN A 1 111 ? -18.24100 -24.17400 34.18700 1.000 29.89222 ?  91  GLN A OE1   1 
ATOM   631  N NE2   . GLN A 1 111 ? -16.47500 -24.76700 35.44100 1.000 31.60496 ?  91  GLN A NE2   1 
ATOM   632  N N     . LYS A 1 112 ? -19.37600 -27.93400 31.34600 1.000 28.81405 ?  92  LYS A N     1 
ATOM   633  C CA    . LYS A 1 112 ? -20.38300 -28.84200 31.87900 1.000 31.86426 ?  92  LYS A CA    1 
ATOM   634  C C     . LYS A 1 112 ? -20.69900 -30.01300 30.95300 1.000 33.01678 ?  92  LYS A C     1 
ATOM   635  O O     . LYS A 1 112 ? -20.82700 -31.14000 31.43300 1.000 35.74401 ?  92  LYS A O     1 
ATOM   636  C CB    . LYS A 1 112 ? -21.66500 -28.07600 32.20300 1.000 28.83323 ?  92  LYS A CB    1 
ATOM   637  C CG    . LYS A 1 112 ? -21.47000 -27.03700 33.30600 1.000 36.00662 ?  92  LYS A CG    1 
ATOM   638  N N     . ASN A 1 113 ? -20.83800 -29.78600 29.64200 1.000 32.22690 ?  93  ASN A N     1 
ATOM   639  C CA    . ASN A 1 113 ? -21.07100 -30.90400 28.72500 1.000 36.85500 ?  93  ASN A CA    1 
ATOM   640  C C     . ASN A 1 113 ? -19.80200 -31.66900 28.35900 1.000 35.67803 ?  93  ASN A C     1 
ATOM   641  O O     . ASN A 1 113 ? -19.89700 -32.83200 27.95600 1.000 36.83091 ?  93  ASN A O     1 
ATOM   642  C CB    . ASN A 1 113 ? -21.73300 -30.43600 27.42400 1.000 36.43623 ?  93  ASN A CB    1 
ATOM   643  C CG    . ASN A 1 113 ? -22.98500 -29.60300 27.65500 1.000 41.75984 ?  93  ASN A CG    1 
ATOM   644  O OD1   . ASN A 1 113 ? -23.68100 -29.76100 28.66500 1.000 42.38255 ?  93  ASN A OD1   1 
ATOM   645  N ND2   . ASN A 1 113 ? -23.28300 -28.71000 26.70300 1.000 35.68814 ?  93  ASN A ND2   1 
ATOM   646  N N     . GLY A 1 114 ? -18.62600 -31.05600 28.46100 1.000 29.04116 ?  94  GLY A N     1 
ATOM   647  C CA    . GLY A 1 114 ? -17.39000 -31.72300 28.09300 1.000 30.03293 ?  94  GLY A CA    1 
ATOM   648  C C     . GLY A 1 114 ? -16.99700 -31.57600 26.63600 1.000 34.04106 ?  94  GLY A C     1 
ATOM   649  O O     . GLY A 1 114 ? -15.90300 -32.01600 26.24900 1.000 31.29262 ?  94  GLY A O     1 
ATOM   650  N N     . CYS A 1 115 ? -17.84600 -30.96600 25.81700 1.000 34.09308 ?  95  CYS A N     1 
ATOM   651  C CA    . CYS A 1 115 ? -17.50800 -30.72600 24.42600 1.000 32.79802 ?  95  CYS A CA    1 
ATOM   652  C C     . CYS A 1 115 ? -18.33200 -29.55900 23.91400 1.000 32.54913 ?  95  CYS A C     1 
ATOM   653  O O     . CYS A 1 115 ? -19.38800 -29.22600 24.45400 1.000 33.27098 ?  95  CYS A O     1 
ATOM   654  C CB    . CYS A 1 115 ? -17.74400 -31.97000 23.56100 1.000 33.63794 ?  95  CYS A CB    1 
ATOM   655  S SG    . CYS A 1 115 ? -19.48900 -32.33300 23.34500 1.000 44.78884 ?  95  CYS A SG    1 
ATOM   656  N N     . ILE A 1 116 ? -17.81500 -28.92700 22.87000 1.000 29.83542 ?  96  ILE A N     1 
ATOM   657  C CA    . ILE A 1 116 ? -18.54500 -27.90700 22.14400 1.000 31.21729 ?  96  ILE A CA    1 
ATOM   658  C C     . ILE A 1 116 ? -18.04900 -27.95800 20.70900 1.000 31.56319 ?  96  ILE A C     1 
ATOM   659  O O     . ILE A 1 116 ? -16.90500 -28.35000 20.44000 1.000 29.01279 ?  96  ILE A O     1 
ATOM   660  C CB    . ILE A 1 116 ? -18.36300 -26.51100 22.79600 1.000 32.98425 ?  96  ILE A CB    1 
ATOM   661  C CG1   . ILE A 1 116 ? -19.33500 -25.50100 22.19500 1.000 39.29800 ?  96  ILE A CG1   1 
ATOM   662  C CG2   . ILE A 1 116 ? -16.91500 -26.03400 22.68500 1.000 27.37574 ?  96  ILE A CG2   1 
ATOM   663  N N     . GLY A 1 117 ? -18.92700 -27.62200 19.78300 1.000 27.70104 ?  97  GLY A N     1 
ATOM   664  C CA    . GLY A 1 117 ? -18.56600 -27.55900 18.38900 1.000 31.91060 ?  97  GLY A CA    1 
ATOM   665  C C     . GLY A 1 117 ? -18.41100 -26.12200 17.93800 1.000 34.59576 ?  97  GLY A C     1 
ATOM   666  O O     . GLY A 1 117 ? -18.91000 -25.19700 18.57500 1.000 27.92073 ?  97  GLY A O     1 
ATOM   667  N N     . TYR A 1 118 ? -17.70900 -25.93900 16.82300 1.000 31.40395 ?  98  TYR A N     1 
ATOM   668  C CA    . TYR A 1 118 ? -17.59500 -24.60200 16.25400 1.000 35.18290 ?  98  TYR A CA    1 
ATOM   669  C C     . TYR A 1 118 ? -17.29300 -24.71200 14.76600 1.000 34.59412 ?  98  TYR A C     1 
ATOM   670  O O     . TYR A 1 118 ? -16.87600 -25.76300 14.27200 1.000 35.31441 ?  98  TYR A O     1 
ATOM   671  C CB    . TYR A 1 118 ? -16.53500 -23.76700 16.99200 1.000 29.28375 ?  98  TYR A CB    1 
ATOM   672  C CG    . TYR A 1 118 ? -15.09200 -24.12200 16.70400 1.000 29.58827 ?  98  TYR A CG    1 
ATOM   673  C CD1   . TYR A 1 118 ? -14.43100 -25.10100 17.44100 1.000 31.96540 ?  98  TYR A CD1   1 
ATOM   674  C CD2   . TYR A 1 118 ? -14.37900 -23.46100 15.70800 1.000 31.84851 ?  98  TYR A CD2   1 
ATOM   675  C CE1   . TYR A 1 118 ? -13.09000 -25.42100 17.18200 1.000 31.74037 ?  98  TYR A CE1   1 
ATOM   676  C CE2   . TYR A 1 118 ? -13.05800 -23.76600 15.44500 1.000 31.88941 ?  98  TYR A CE2   1 
ATOM   677  C CZ    . TYR A 1 118 ? -12.41400 -24.74100 16.18100 1.000 34.78071 ?  98  TYR A CZ    1 
ATOM   678  O OH    . TYR A 1 118 ? -11.09300 -25.02900 15.90000 1.000 33.61960 ?  98  TYR A OH    1 
ATOM   679  N N     . SER A 1 119 ? -17.53400 -23.61100 14.06100 1.000 34.85699 ?  99  SER A N     1 
ATOM   680  C CA    . SER A 1 119 ? -17.32500 -23.52300 12.62300 1.000 35.83338 ?  99  SER A CA    1 
ATOM   681  C C     . SER A 1 119 ? -16.02900 -22.77600 12.35300 1.000 38.08573 ?  99  SER A C     1 
ATOM   682  O O     . SER A 1 119 ? -15.89600 -21.60600 12.71700 1.000 40.11931 ?  99  SER A O     1 
ATOM   683  C CB    . SER A 1 119 ? -18.48800 -22.80800 11.94300 1.000 34.66441 ?  99  SER A CB    1 
ATOM   684  O OG    . SER A 1 119 ? -19.58400 -23.68200 11.79400 1.000 44.31946 ?  99  SER A OG    1 
ATOM   685  N N     . GLN A 1 120 ? -15.08100 -23.45800 11.73200 1.000 34.82899 ?  100 GLN A N     1 
ATOM   686  C CA    . GLN A 1 120 ? -13.84500 -22.84700 11.28600 1.000 40.22264 ?  100 GLN A CA    1 
ATOM   687  C C     . GLN A 1 120 ? -14.02900 -22.28400 9.88000  1.000 43.21346 ?  100 GLN A C     1 
ATOM   688  O O     . GLN A 1 120 ? -14.64500 -22.91900 9.02000  1.000 39.26198 ?  100 GLN A O     1 
ATOM   689  C CB    . GLN A 1 120 ? -12.72800 -23.88200 11.30700 1.000 38.45113 ?  100 GLN A CB    1 
ATOM   690  C CG    . GLN A 1 120 ? -11.35400 -23.32400 11.49400 1.000 40.98360 ?  100 GLN A CG    1 
ATOM   691  C CD    . GLN A 1 120 ? -10.30500 -24.39800 11.35400 1.000 41.82291 ?  100 GLN A CD    1 
ATOM   692  O OE1   . GLN A 1 120 ? -10.43000 -25.30600 10.52500 1.000 46.79013 ?  100 GLN A OE1   1 
ATOM   693  N NE2   . GLN A 1 120 ? -9.27400  -24.32000 12.18100 1.000 43.14970 ?  100 GLN A NE2   1 
ATOM   694  N N     . ASN A 1 121 ? -13.50300 -21.08600 9.65100  1.000 39.61729 ?  101 ASN A N     1 
ATOM   695  C CA    . ASN A 1 121 ? -13.68800 -20.43100 8.36500  1.000 37.67593 ?  101 ASN A CA    1 
ATOM   696  C C     . ASN A 1 121 ? -12.68800 -20.94300 7.33100  1.000 39.63950 ?  101 ASN A C     1 
ATOM   697  O O     . ASN A 1 121 ? -11.55000 -21.29300 7.65500  1.000 40.49158 ?  101 ASN A O     1 
ATOM   698  C CB    . ASN A 1 121 ? -13.56400 -18.91900 8.52600  1.000 36.99084 ?  101 ASN A CB    1 
ATOM   699  C CG    . ASN A 1 121 ? -14.60700 -18.36200 9.45800  1.000 43.46788 ?  101 ASN A CG    1 
ATOM   700  O OD1   . ASN A 1 121 ? -15.55800 -19.05500 9.82700  1.000 49.21639 ?  101 ASN A OD1   1 
ATOM   701  N ND2   . ASN A 1 121 ? -14.43900 -17.11000 9.85300  1.000 45.35605 ?  101 ASN A ND2   1 
ATOM   702  N N     . GLY A 1 122 ? -13.14200 -21.01300 6.07800  1.000 38.09769 ?  102 GLY A N     1 
ATOM   703  C CA    . GLY A 1 122 ? -12.32600 -21.41500 4.94700  1.000 35.32349 ?  102 GLY A CA    1 
ATOM   704  C C     . GLY A 1 122 ? -12.36600 -20.34500 3.87600  1.000 38.50103 ?  102 GLY A C     1 
ATOM   705  O O     . GLY A 1 122 ? -12.39000 -19.14600 4.16000  1.000 38.09210 ?  102 GLY A O     1 
ATOM   706  N N     . GLU A 1 123 ? -12.38900 -20.79200 2.62000  1.000 36.00392 ?  103 GLU A N     1 
ATOM   707  C CA    . GLU A 1 123 ? -12.51400 -19.86400 1.50100  1.000 32.57133 ?  103 GLU A CA    1 
ATOM   708  C C     . GLU A 1 123 ? -13.89000 -19.22400 1.48500  1.000 37.30992 ?  103 GLU A C     1 
ATOM   709  O O     . GLU A 1 123 ? -14.91000 -19.92500 1.47800  1.000 32.66752 ?  103 GLU A O     1 
ATOM   710  C CB    . GLU A 1 123 ? -12.30600 -20.58500 0.16900  1.000 34.86020 ?  103 GLU A CB    1 
ATOM   711  C CG    . GLU A 1 123 ? -10.91500 -20.54400 -0.37400 1.000 30.62039 ?  103 GLU A CG    1 
ATOM   712  C CD    . GLU A 1 123 ? -10.82400 -21.22400 -1.71400 1.000 31.01589 ?  103 GLU A CD    1 
ATOM   713  O OE1   . GLU A 1 123 ? -11.67900 -20.94000 -2.58200 1.000 28.71504 ?  103 GLU A OE1   1 
ATOM   714  O OE2   . GLU A 1 123 ? -9.91400  -22.05400 -1.89400 1.000 32.41790 -1 103 GLU A OE2   1 
ATOM   715  N N     . GLY A 1 124 ? -13.91700 -17.89600 1.42200  1.000 34.21562 ?  104 GLY A N     1 
ATOM   716  C CA    . GLY A 1 124 ? -15.18600 -17.20800 1.25900  1.000 34.29495 ?  104 GLY A CA    1 
ATOM   717  C C     . GLY A 1 124 ? -16.09500 -17.46700 2.43900  1.000 36.50591 ?  104 GLY A C     1 
ATOM   718  O O     . GLY A 1 124 ? -15.72700 -17.23900 3.59700  1.000 40.21688 ?  104 GLY A O     1 
ATOM   719  N N     . GLU A 1 125 ? -17.29600 -17.96000 2.14800  1.000 37.44081 ?  105 GLU A N     1 
ATOM   720  C CA    . GLU A 1 125 ? -18.27900 -18.28600 3.17100  1.000 40.63212 ?  105 GLU A CA    1 
ATOM   721  C C     . GLU A 1 125 ? -18.17400 -19.72700 3.67300  1.000 38.43289 ?  105 GLU A C     1 
ATOM   722  O O     . GLU A 1 125 ? -18.99800 -20.14000 4.49800  1.000 39.15497 ?  105 GLU A O     1 
ATOM   723  C CB    . GLU A 1 125 ? -19.69600 -18.04400 2.63300  1.000 38.17302 ?  105 GLU A CB    1 
ATOM   724  C CG    . GLU A 1 125 ? -20.00500 -18.85600 1.38300  1.000 44.17159 ?  105 GLU A CG    1 
ATOM   725  C CD    . GLU A 1 125 ? -21.48800 -18.92300 1.05800  1.000 47.69270 ?  105 GLU A CD    1 
ATOM   726  O OE1   . GLU A 1 125 ? -22.18700 -17.91800 1.30800  1.000 47.88384 ?  105 GLU A OE1   1 
ATOM   727  O OE2   . GLU A 1 125 ? -21.94100 -19.97400 0.53100  1.000 46.86011 -1 105 GLU A OE2   1 
ATOM   728  N N     . LEU A 1 126 ? -17.19800 -20.49800 3.20400  1.000 35.72731 ?  106 LEU A N     1 
ATOM   729  C CA    . LEU A 1 126 ? -17.14200 -21.91600 3.53900  1.000 36.64437 ?  106 LEU A CA    1 
ATOM   730  C C     . LEU A 1 126 ? -16.68700 -22.12900 4.98000  1.000 36.95271 ?  106 LEU A C     1 
ATOM   731  O O     . LEU A 1 126 ? -15.80900 -21.42000 5.48300  1.000 37.12343 ?  106 LEU A O     1 
ATOM   732  C CB    . LEU A 1 126 ? -16.19500 -22.64200 2.58600  1.000 33.62602 ?  106 LEU A CB    1 
ATOM   733  C CG    . LEU A 1 126 ? -16.58500 -22.63500 1.10600  1.000 37.65298 ?  106 LEU A CG    1 
ATOM   734  C CD1   . LEU A 1 126 ? -15.51600 -23.35300 0.28200  1.000 35.78617 ?  106 LEU A CD1   1 
ATOM   735  C CD2   . LEU A 1 126 ? -17.97100 -23.25400 0.89900  1.000 35.11599 ?  106 LEU A CD2   1 
ATOM   736  N N     . LYS A 1 127 ? -17.27400 -23.13000 5.64000  1.000 34.41929 ?  107 LYS A N     1 
ATOM   737  C CA    . LYS A 1 127 ? -16.96800 -23.44000 7.03200  1.000 37.79711 ?  107 LYS A CA    1 
ATOM   738  C C     . LYS A 1 127 ? -16.61700 -24.91200 7.19500  1.000 43.35618 ?  107 LYS A C     1 
ATOM   739  O O     . LYS A 1 127 ? -17.10000 -25.77300 6.45200  1.000 46.31085 ?  107 LYS A O     1 
ATOM   740  C CB    . LYS A 1 127 ? -18.12700 -23.09700 7.96600  1.000 34.83637 ?  107 LYS A CB    1 
ATOM   741  C CG    . LYS A 1 127 ? -18.86300 -21.83300 7.60000  1.000 38.47328 ?  107 LYS A CG    1 
ATOM   742  C CD    . LYS A 1 127 ? -18.13400 -20.61500 8.12300  1.000 41.28965 ?  107 LYS A CD    1 
ATOM   743  C CE    . LYS A 1 127 ? -19.11700 -19.53900 8.57200  1.000 47.08423 ?  107 LYS A CE    1 
ATOM   744  N NZ    . LYS A 1 127 ? -18.41800 -18.30200 9.01600  1.000 47.96400 ?  107 LYS A NZ    1 
ATOM   745  N N     . ASN A 1 128 ? -15.75900 -25.18400 8.18000  1.000 39.81449 ?  108 ASN A N     1 
ATOM   746  C CA    . ASN A 1 128 ? -15.33600 -26.53000 8.54900  1.000 41.96613 ?  108 ASN A CA    1 
ATOM   747  C C     . ASN A 1 128 ? -15.73000 -26.76700 9.99900  1.000 42.89103 ?  108 ASN A C     1 
ATOM   748  O O     . ASN A 1 128 ? -15.27700 -26.04500 10.89500 1.000 38.54159 ?  108 ASN A O     1 
ATOM   749  C CB    . ASN A 1 128 ? -13.82300 -26.71100 8.38600  1.000 43.36800 ?  108 ASN A CB    1 
ATOM   750  C CG    . ASN A 1 128 ? -13.26600 -25.99900 7.16000  1.000 51.52792 ?  108 ASN A CG    1 
ATOM   751  O OD1   . ASN A 1 128 ? -13.96700 -25.79500 6.16600  1.000 56.35138 ?  108 ASN A OD1   1 
ATOM   752  N ND2   . ASN A 1 128 ? -12.00200 -25.58900 7.23900  1.000 49.13041 ?  108 ASN A ND2   1 
ATOM   753  N N     . TYR A 1 129 ? -16.56500 -27.77200 10.23000 1.000 36.47035 ?  109 TYR A N     1 
ATOM   754  C CA    . TYR A 1 129 ? -16.99300 -28.08700 11.58500 1.000 37.85081 ?  109 TYR A CA    1 
ATOM   755  C C     . TYR A 1 129 ? -15.84300 -28.72200 12.36200 1.000 36.70215 ?  109 TYR A C     1 
ATOM   756  O O     . TYR A 1 129 ? -15.16500 -29.62500 11.85800 1.000 40.23814 ?  109 TYR A O     1 
ATOM   757  C CB    . TYR A 1 129 ? -18.19600 -29.02800 11.54800 1.000 35.08539 ?  109 TYR A CB    1 
ATOM   758  C CG    . TYR A 1 129 ? -18.69400 -29.43000 12.91200 1.000 34.10837 ?  109 TYR A CG    1 
ATOM   759  C CD1   . TYR A 1 129 ? -19.48000 -28.56900 13.67000 1.000 37.29203 ?  109 TYR A CD1   1 
ATOM   760  C CD2   . TYR A 1 129 ? -18.35700 -30.66500 13.45400 1.000 33.18311 ?  109 TYR A CD2   1 
ATOM   761  C CE1   . TYR A 1 129 ? -19.93500 -28.93400 14.93700 1.000 36.48867 ?  109 TYR A CE1   1 
ATOM   762  C CE2   . TYR A 1 129 ? -18.79800 -31.04000 14.71100 1.000 37.00909 ?  109 TYR A CE2   1 
ATOM   763  C CZ    . TYR A 1 129 ? -19.58300 -30.17300 15.45300 1.000 38.72281 ?  109 TYR A CZ    1 
ATOM   764  O OH    . TYR A 1 129 ? -20.02200 -30.55800 16.70400 1.000 44.18198 ?  109 TYR A OH    1 
ATOM   765  N N     . LYS A 1 130 ? -15.62000 -28.24600 13.58800 1.000 33.91251 ?  110 LYS A N     1 
ATOM   766  C CA    . LYS A 1 130 ? -14.61900 -28.81300 14.48400 1.000 34.24151 ?  110 LYS A CA    1 
ATOM   767  C C     . LYS A 1 130 ? -15.24300 -29.04000 15.85400 1.000 33.47555 ?  110 LYS A C     1 
ATOM   768  O O     . LYS A 1 130 ? -16.21900 -28.38400 16.22600 1.000 34.66038 ?  110 LYS A O     1 
ATOM   769  C CB    . LYS A 1 130 ? -13.38800 -27.90400 14.63000 1.000 35.67766 ?  110 LYS A CB    1 
ATOM   770  C CG    . LYS A 1 130 ? -12.69500 -27.53200 13.31800 1.000 39.43138 ?  110 LYS A CG    1 
ATOM   771  C CD    . LYS A 1 130 ? -12.08300 -28.75600 12.65200 1.000 40.00746 ?  110 LYS A CD    1 
ATOM   772  C CE    . LYS A 1 130 ? -10.98500 -28.37000 11.66800 1.000 42.30903 ?  110 LYS A CE    1 
ATOM   773  N NZ    . LYS A 1 130 ? -9.71600  -29.11700 11.93100 1.000 46.63568 ?  110 LYS A NZ    1 
ATOM   774  N N     . VAL A 1 131 ? -14.65300 -29.96300 16.61200 1.000 26.91969 ?  111 VAL A N     1 
ATOM   775  C CA    . VAL A 1 131 ? -15.07900 -30.27500 17.97000 1.000 28.50926 ?  111 VAL A CA    1 
ATOM   776  C C     . VAL A 1 131 ? -13.95900 -29.93800 18.94700 1.000 33.81052 ?  111 VAL A C     1 
ATOM   777  O O     . VAL A 1 131 ? -12.78800 -30.25300 18.70100 1.000 32.00403 ?  111 VAL A O     1 
ATOM   778  C CB    . VAL A 1 131 ? -15.48100 -31.75600 18.11300 1.000 32.36844 ?  111 VAL A CB    1 
ATOM   779  C CG1   . VAL A 1 131 ? -15.87400 -32.06300 19.55900 1.000 31.24824 ?  111 VAL A CG1   1 
ATOM   780  C CG2   . VAL A 1 131 ? -16.62300 -32.08600 17.16200 1.000 31.55363 ?  111 VAL A CG2   1 
ATOM   781  N N     . ILE A 1 132 ? -14.32100 -29.29100 20.05400 1.000 30.25086 ?  112 ILE A N     1 
ATOM   782  C CA    . ILE A 1 132 ? -13.42600 -29.11000 21.19100 1.000 28.57866 ?  112 ILE A CA    1 
ATOM   783  C C     . ILE A 1 132 ? -13.83000 -30.11000 22.26200 1.000 30.00244 ?  112 ILE A C     1 
ATOM   784  O O     . ILE A 1 132 ? -14.97200 -30.09700 22.73700 1.000 29.65326 ?  112 ILE A O     1 
ATOM   785  C CB    . ILE A 1 132 ? -13.47500 -27.67100 21.72900 1.000 29.71477 ?  112 ILE A CB    1 
ATOM   786  C CG1   . ILE A 1 132 ? -13.04900 -26.69100 20.63300 1.000 26.56323 ?  112 ILE A CG1   1 
ATOM   787  C CG2   . ILE A 1 132 ? -12.57000 -27.51400 22.95900 1.000 25.14939 ?  112 ILE A CG2   1 
ATOM   788  C CD1   . ILE A 1 132 ? -13.60700 -25.29000 20.82900 1.000 26.43942 ?  112 ILE A CD1   1 
ATOM   789  N N     . ASP A 1 133 ? -12.90500 -30.97700 22.65100 1.000 27.25431 ?  113 ASP A N     1 
ATOM   790  C CA    . ASP A 1 133 ? -13.17500 -31.99300 23.66100 1.000 28.93382 ?  113 ASP A CA    1 
ATOM   791  C C     . ASP A 1 133 ? -12.41600 -31.63900 24.93700 1.000 30.14415 ?  113 ASP A C     1 
ATOM   792  O O     . ASP A 1 133 ? -11.18000 -31.68000 24.96900 1.000 26.60382 ?  113 ASP A O     1 
ATOM   793  C CB    . ASP A 1 133 ? -12.80200 -33.38000 23.14200 1.000 33.20529 ?  113 ASP A CB    1 
ATOM   794  C CG    . ASP A 1 133 ? -12.92000 -34.44700 24.20500 1.000 33.53800 ?  113 ASP A CG    1 
ATOM   795  O OD1   . ASP A 1 133 ? -13.70400 -34.26500 25.15700 1.000 35.71761 ?  113 ASP A OD1   1 
ATOM   796  O OD2   . ASP A 1 133 ? -12.25300 -35.49100 24.07000 1.000 43.64742 -1 113 ASP A OD2   1 
ATOM   797  N N     . ARG A 1 134 ? -13.17100 -31.30600 25.98900 1.000 30.97503 ?  114 ARG A N     1 
ATOM   798  C CA    . ARG A 1 134 ? -12.57300 -30.92000 27.26400 1.000 28.78724 ?  114 ARG A CA    1 
ATOM   799  C C     . ARG A 1 134 ? -11.56100 -31.95200 27.74300 1.000 32.30713 ?  114 ARG A C     1 
ATOM   800  O O     . ARG A 1 134 ? -10.53900 -31.60300 28.34500 1.000 30.94212 ?  114 ARG A O     1 
ATOM   801  C CB    . ARG A 1 134 ? -13.67300 -30.72700 28.31100 1.000 27.42000 ?  114 ARG A CB    1 
ATOM   802  C CG    . ARG A 1 134 ? -13.17300 -30.48100 29.72600 1.000 30.81993 ?  114 ARG A CG    1 
ATOM   803  C CD    . ARG A 1 134 ? -14.31200 -30.60500 30.73300 1.000 29.50112 ?  114 ARG A CD    1 
ATOM   804  N NE    . ARG A 1 134 ? -14.62200 -32.00500 30.99400 1.000 35.73531 ?  114 ARG A NE    1 
ATOM   805  C CZ    . ARG A 1 134 ? -15.82100 -32.46200 31.33000 1.000 34.01386 ?  114 ARG A CZ    1 
ATOM   806  N NH1   . ARG A 1 134 ? -16.85900 -31.65100 31.46500 1.000 29.19888 ?  114 ARG A NH1   1 
ATOM   807  N NH2   . ARG A 1 134 ? -15.98100 -33.76600 31.53800 1.000 27.45800 ?  114 ARG A NH2   1 
ATOM   808  N N     . GLU A 1 135 ? -11.82600 -33.22700 27.47300 1.000 29.32625 ?  115 GLU A N     1 
ATOM   809  C CA    . GLU A 1 135 ? -10.98100 -34.30800 27.95300 1.000 33.85686 ?  115 GLU A CA    1 
ATOM   810  C C     . GLU A 1 135 ? -9.71300  -34.48700 27.13100 1.000 30.73963 ?  115 GLU A C     1 
ATOM   811  O O     . GLU A 1 135 ? -8.85400  -35.28900 27.51500 1.000 32.63691 ?  115 GLU A O     1 
ATOM   812  C CB    . GLU A 1 135 ? -11.79000 -35.60900 27.98400 1.000 34.29222 ?  115 GLU A CB    1 
ATOM   813  C CG    . GLU A 1 135 ? -12.88800 -35.58000 29.04400 1.000 31.31306 ?  115 GLU A CG    1 
ATOM   814  C CD    . GLU A 1 135 ? -12.33100 -35.29200 30.43500 1.000 33.22593 ?  115 GLU A CD    1 
ATOM   815  O OE1   . GLU A 1 135 ? -11.27500 -35.87700 30.77500 1.000 39.76718 ?  115 GLU A OE1   1 
ATOM   816  O OE2   . GLU A 1 135 ? -12.93800 -34.48700 31.18500 1.000 34.81446 -1 115 GLU A OE2   1 
ATOM   817  N N     . GLY A 1 136 ? -9.56700  -33.76500 26.02400 1.000 29.37455 ?  116 GLY A N     1 
ATOM   818  C CA    . GLY A 1 136 ? -8.32100  -33.78000 25.29100 1.000 24.28688 ?  116 GLY A CA    1 
ATOM   819  C C     . GLY A 1 136 ? -7.25800  -32.82100 25.77900 1.000 29.15956 ?  116 GLY A C     1 
ATOM   820  O O     . GLY A 1 136 ? -6.16900  -32.79600 25.20100 1.000 29.16631 ?  116 GLY A O     1 
ATOM   821  N N     . TYR A 1 137 ? -7.54800  -32.06000 26.83600 1.000 25.53823 ?  117 TYR A N     1 
ATOM   822  C CA    . TYR A 1 137 ? -6.60200  -31.02300 27.31800 1.000 26.89379 ?  117 TYR A CA    1 
ATOM   823  C C     . TYR A 1 137 ? -6.18300  -31.29700 28.76300 1.000 28.59652 ?  117 TYR A C     1 
ATOM   824  O O     . TYR A 1 137 ? -6.99000  -31.80200 29.53400 1.000 29.65557 ?  117 TYR A O     1 
ATOM   825  C CB    . TYR A 1 137 ? -7.22000  -29.62500 27.22000 1.000 23.71380 ?  117 TYR A CB    1 
ATOM   826  C CG    . TYR A 1 137 ? -7.61500  -29.15000 25.84900 1.000 24.75285 ?  117 TYR A CG    1 
ATOM   827  C CD1   . TYR A 1 137 ? -8.82100  -29.52600 25.29100 1.000 25.90083 ?  117 TYR A CD1   1 
ATOM   828  C CD2   . TYR A 1 137 ? -6.80500  -28.29100 25.12600 1.000 24.60986 ?  117 TYR A CD2   1 
ATOM   829  C CE1   . TYR A 1 137 ? -9.20200  -29.08900 24.03700 1.000 28.15807 ?  117 TYR A CE1   1 
ATOM   830  C CE2   . TYR A 1 137 ? -7.17200  -27.84000 23.87000 1.000 21.88327 ?  117 TYR A CE2   1 
ATOM   831  C CZ    . TYR A 1 137 ? -8.37600  -28.24400 23.32400 1.000 27.20146 ?  117 TYR A CZ    1 
ATOM   832  O OH    . TYR A 1 137 ? -8.77300  -27.82500 22.08400 1.000 31.88900 ?  117 TYR A OH    1 
ATOM   833  N N     . ALA A 1 138 ? -4.96300  -30.92400 29.11400 1.000 27.18181 ?  118 ALA A N     1 
ATOM   834  C CA    . ALA A 1 138 ? -4.45200  -31.09600 30.49100 1.000 30.96307 ?  118 ALA A CA    1 
ATOM   835  C C     . ALA A 1 138 ? -5.35000  -30.40300 31.52900 1.000 31.26398 ?  118 ALA A C     1 
ATOM   836  O O     . ALA A 1 138 ? -5.44900  -30.92700 32.63100 1.000 29.38741 ?  118 ALA A O     1 
ATOM   837  C CB    . ALA A 1 138 ? -3.04300  -30.57500 30.53800 1.000 30.39898 ?  118 ALA A CB    1 
ATOM   838  N N     . PHE A 1 139 ? -6.01200  -29.30000 31.16700 1.000 27.46543 ?  119 PHE A N     1 
ATOM   839  C CA    . PHE A 1 139 ? -6.84400  -28.53000 32.12900 1.000 27.87058 ?  119 PHE A CA    1 
ATOM   840  C C     . PHE A 1 139 ? -8.05600  -29.35500 32.58300 1.000 29.85334 ?  119 PHE A C     1 
ATOM   841  O O     . PHE A 1 139 ? -8.77100  -28.87700 33.45900 1.000 30.16486 ?  119 PHE A O     1 
ATOM   842  C CB    . PHE A 1 139 ? -7.22000  -27.16400 31.54200 1.000 28.55488 ?  119 PHE A CB    1 
ATOM   843  C CG    . PHE A 1 139 ? -8.11200  -27.15100 30.32700 1.000 26.89640 ?  119 PHE A CG    1 
ATOM   844  C CD1   . PHE A 1 139 ? -9.41600  -27.61000 30.38500 1.000 24.96885 ?  119 PHE A CD1   1 
ATOM   845  C CD2   . PHE A 1 139 ? -7.66400  -26.60900 29.13600 1.000 25.90442 ?  119 PHE A CD2   1 
ATOM   846  C CE1   . PHE A 1 139 ? -10.23500 -27.57100 29.27000 1.000 28.78385 ?  119 PHE A CE1   1 
ATOM   847  C CE2   . PHE A 1 139 ? -8.48500  -26.56600 28.02200 1.000 24.94782 ?  119 PHE A CE2   1 
ATOM   848  C CZ    . PHE A 1 139 ? -9.76700  -27.05100 28.09000 1.000 25.33996 ?  119 PHE A CZ    1 
ATOM   849  N N     . ARG A 1 140 ? -8.25800  -30.54000 32.00500 1.000 27.82471 ?  120 ARG A N     1 
ATOM   850  C CA    . ARG A 1 140 ? -9.37600  -31.44700 32.38400 1.000 29.90889 ?  120 ARG A CA    1 
ATOM   851  C C     . ARG A 1 140 ? -9.28100  -31.81900 33.86200 1.000 28.61453 ?  120 ARG A C     1 
ATOM   852  O O     . ARG A 1 140 ? -10.27700 -32.26500 34.40000 1.000 33.12182 ?  120 ARG A O     1 
ATOM   853  C CB    . ARG A 1 140 ? -9.35100  -32.72000 31.53600 1.000 31.02905 ?  120 ARG A CB    1 
ATOM   854  C CG    . ARG A 1 140 ? -8.26600  -33.71400 31.91500 1.000 34.17513 ?  120 ARG A CG    1 
ATOM   855  C CD    . ARG A 1 140 ? -7.86600  -34.54900 30.71900 1.000 35.43208 ?  120 ARG A CD    1 
ATOM   856  N NE    . ARG A 1 140 ? -8.31600  -35.92200 30.82800 1.000 42.43511 ?  120 ARG A NE    1 
ATOM   857  C CZ    . ARG A 1 140 ? -7.66400  -36.86800 31.48900 1.000 43.66498 ?  120 ARG A CZ    1 
ATOM   858  N NH1   . ARG A 1 140 ? -6.37300  -37.05000 31.28100 1.000 42.85373 ?  120 ARG A NH1   1 
ATOM   859  N NH2   . ARG A 1 140 ? -8.30400  -37.62500 32.35800 1.000 47.50678 ?  120 ARG A NH2   1 
ATOM   860  N N     . ASP A 1 141 ? -8.11300  -31.64000 34.46900 1.000 30.17376 ?  121 ASP A N     1 
ATOM   861  C CA    . ASP A 1 141 ? -7.88900  -31.99900 35.89200 1.000 32.66488 ?  121 ASP A CA    1 
ATOM   862  C C     . ASP A 1 141 ? -8.36700  -30.89400 36.83600 1.000 34.65067 ?  121 ASP A C     1 
ATOM   863  O O     . ASP A 1 141 ? -8.30900  -31.11300 38.04500 1.000 36.22901 ?  121 ASP A O     1 
ATOM   864  C CB    . ASP A 1 141 ? -6.40600  -32.26300 36.12400 1.000 32.23558 ?  121 ASP A CB    1 
ATOM   865  C CG    . ASP A 1 141 ? -5.47600  -31.09300 35.84500 1.000 38.26559 ?  121 ASP A CG    1 
ATOM   866  O OD1   . ASP A 1 141 ? -5.96400  -30.01900 35.44800 1.000 35.06375 ?  121 ASP A OD1   1 
ATOM   867  O OD2   . ASP A 1 141 ? -4.26300  -31.27300 36.01700 1.000 33.96557 -1 121 ASP A OD2   1 
ATOM   868  N N     . SER A 1 142 ? -8.83100  -29.76300 36.30600 1.000 29.66784 ?  122 SER A N     1 
ATOM   869  C CA    . SER A 1 142 ? -9.14600  -28.61100 37.18900 1.000 33.03358 ?  122 SER A CA    1 
ATOM   870  C C     . SER A 1 142 ? -10.39700 -27.83300 36.76100 1.000 30.58964 ?  122 SER A C     1 
ATOM   871  O O     . SER A 1 142 ? -10.62400 -26.78100 37.34700 1.000 31.10796 ?  122 SER A O     1 
ATOM   872  C CB    . SER A 1 142 ? -7.94200  -27.70600 37.21900 1.000 27.43634 ?  122 SER A CB    1 
ATOM   873  O OG    . SER A 1 142 ? -6.74600  -28.41700 37.46500 1.000 34.71381 ?  122 SER A OG    1 
ATOM   874  N N     . PHE A 1 143 ? -11.22800 -28.36300 35.85700 1.000 29.51598 ?  123 PHE A N     1 
ATOM   875  C CA    . PHE A 1 143 ? -12.29800 -27.53000 35.31600 1.000 30.25848 ?  123 PHE A CA    1 
ATOM   876  C C     . PHE A 1 143 ? -13.43800 -27.28700 36.30100 1.000 31.67224 ?  123 PHE A C     1 
ATOM   877  O O     . PHE A 1 143 ? -14.22700 -26.35900 36.09200 1.000 32.93656 ?  123 PHE A O     1 
ATOM   878  C CB    . PHE A 1 143 ? -12.82700 -28.13600 34.01500 1.000 30.24221 ?  123 PHE A CB    1 
ATOM   879  C CG    . PHE A 1 143 ? -13.56200 -29.43800 34.18700 1.000 30.09923 ?  123 PHE A CG    1 
ATOM   880  C CD1   . PHE A 1 143 ? -14.92100 -29.45900 34.48400 1.000 31.34721 ?  123 PHE A CD1   1 
ATOM   881  C CD2   . PHE A 1 143 ? -12.90200 -30.64800 33.99200 1.000 33.10364 ?  123 PHE A CD2   1 
ATOM   882  C CE1   . PHE A 1 143 ? -15.59700 -30.66500 34.62500 1.000 31.49008 ?  123 PHE A CE1   1 
ATOM   883  C CE2   . PHE A 1 143 ? -13.57200 -31.85200 34.12400 1.000 31.89805 ?  123 PHE A CE2   1 
ATOM   884  C CZ    . PHE A 1 143 ? -14.92400 -31.85700 34.44500 1.000 30.08174 ?  123 PHE A CZ    1 
ATOM   885  N N     . THR A 1 144 ? -13.54300 -28.08200 37.36700 1.000 28.38400 ?  124 THR A N     1 
ATOM   886  C CA    . THR A 1 144 ? -14.55300 -27.82600 38.38600 1.000 30.87671 ?  124 THR A CA    1 
ATOM   887  C C     . THR A 1 144 ? -14.18800 -26.67300 39.31400 1.000 31.80368 ?  124 THR A C     1 
ATOM   888  O O     . THR A 1 144 ? -15.04600 -26.22200 40.08100 1.000 31.06658 ?  124 THR A O     1 
ATOM   889  C CB    . THR A 1 144 ? -14.78800 -29.08200 39.22300 1.000 34.65767 ?  124 THR A CB    1 
ATOM   890  O OG1   . THR A 1 144 ? -13.56900 -29.43400 39.88900 1.000 34.55916 ?  124 THR A OG1   1 
ATOM   891  C CG2   . THR A 1 144 ? -15.22600 -30.24300 38.32900 1.000 32.90725 ?  124 THR A CG2   1 
ATOM   892  N N     . LYS A 1 145 ? -12.94800 -26.18700 39.27200 1.000 31.19987 ?  125 LYS A N     1 
ATOM   893  C CA    . LYS A 1 145 ? -12.54300 -25.03700 40.06700 1.000 29.18010 ?  125 LYS A CA    1 
ATOM   894  C C     . LYS A 1 145 ? -12.82400 -23.70700 39.37100 1.000 32.04477 ?  125 LYS A C     1 
ATOM   895  O O     . LYS A 1 145 ? -12.38200 -22.66300 39.85900 1.000 29.08479 ?  125 LYS A O     1 
ATOM   896  C CB    . LYS A 1 145 ? -11.06100 -25.15000 40.43200 1.000 28.28574 ?  125 LYS A CB    1 
ATOM   897  C CG    . LYS A 1 145 ? -10.77500 -26.33700 41.33800 1.000 34.32804 ?  125 LYS A CG    1 
ATOM   898  C CD    . LYS A 1 145 ? -9.37500  -26.32100 41.93400 1.000 34.25815 ?  125 LYS A CD    1 
ATOM   899  C CE    . LYS A 1 145 ? -8.32000  -26.59100 40.87900 1.000 35.79284 ?  125 LYS A CE    1 
ATOM   900  N NZ    . LYS A 1 145 ? -6.93800  -26.19500 41.32700 1.000 33.82766 ?  125 LYS A NZ    1 
ATOM   901  N N     . VAL A 1 146 ? -13.56100 -23.72000 38.26200 1.000 28.51410 ?  126 VAL A N     1 
ATOM   902  C CA    . VAL A 1 146 ? -13.86800 -22.51200 37.50400 1.000 29.18010 ?  126 VAL A CA    1 
ATOM   903  C C     . VAL A 1 146 ? -15.36200 -22.24700 37.58800 1.000 28.44228 ?  126 VAL A C     1 
ATOM   904  O O     . VAL A 1 146 ? -16.17900 -23.17200 37.60300 1.000 28.29306 ?  126 VAL A O     1 
ATOM   905  C CB    . VAL A 1 146 ? -13.43700 -22.61100 36.01900 1.000 28.51843 ?  126 VAL A CB    1 
ATOM   906  C CG1   . VAL A 1 146 ? -13.69600 -21.28800 35.29200 1.000 25.62339 ?  126 VAL A CG1   1 
ATOM   907  C CG2   . VAL A 1 146 ? -11.97400 -23.00200 35.89400 1.000 26.76890 ?  126 VAL A CG2   1 
ATOM   908  N N     . GLU A 1 147 ? -15.71300 -20.96600 37.62000 1.000 29.91432 ?  127 GLU A N     1 
ATOM   909  C CA    . GLU A 1 147 ? -17.08600 -20.51800 37.45900 1.000 31.91697 ?  127 GLU A CA    1 
ATOM   910  C C     . GLU A 1 147 ? -17.10900 -19.35400 36.47800 1.000 28.56266 ?  127 GLU A C     1 
ATOM   911  O O     . GLU A 1 147 ? -16.35500 -18.38600 36.64100 1.000 27.70948 ?  127 GLU A O     1 
ATOM   912  C CB    . GLU A 1 147 ? -17.68300 -20.09100 38.79400 1.000 33.71212 ?  127 GLU A CB    1 
ATOM   913  C CG    . GLU A 1 147 ? -19.11400 -20.52800 38.97700 1.000 41.50701 ?  127 GLU A CG    1 
ATOM   914  C CD    . GLU A 1 147 ? -19.62100 -20.23600 40.37700 1.000 51.36530 ?  127 GLU A CD    1 
ATOM   915  O OE1   . GLU A 1 147 ? -18.82500 -20.35600 41.34500 1.000 46.21708 ?  127 GLU A OE1   1 
ATOM   916  O OE2   . GLU A 1 147 ? -20.81700 -19.89500 40.50200 1.000 52.69335 -1 127 GLU A OE2   1 
ATOM   917  N N     . PHE A 1 148 ? -17.97300 -19.44500 35.47100 1.000 27.08313 ?  128 PHE A N     1 
ATOM   918  C CA    . PHE A 1 148 ? -18.09700 -18.41300 34.45000 1.000 27.97013 ?  128 PHE A CA    1 
ATOM   919  C C     . PHE A 1 148 ? -19.30400 -17.52200 34.71600 1.000 29.57463 ?  128 PHE A C     1 
ATOM   920  O O     . PHE A 1 148 ? -20.37600 -18.00500 35.08800 1.000 29.72108 ?  128 PHE A O     1 
ATOM   921  C CB    . PHE A 1 148 ? -18.21300 -19.04300 33.06700 1.000 27.37949 ?  128 PHE A CB    1 
ATOM   922  C CG    . PHE A 1 148 ? -16.97600 -19.77400 32.64100 1.000 25.66953 ?  128 PHE A CG    1 
ATOM   923  C CD1   . PHE A 1 148 ? -15.80300 -19.08000 32.38300 1.000 24.69691 ?  128 PHE A CD1   1 
ATOM   924  C CD2   . PHE A 1 148 ? -16.97700 -21.15100 32.51800 1.000 25.01542 ?  128 PHE A CD2   1 
ATOM   925  C CE1   . PHE A 1 148 ? -14.65500 -19.75100 31.99100 1.000 24.29596 ?  128 PHE A CE1   1 
ATOM   926  C CE2   . PHE A 1 148 ? -15.82900 -21.82900 32.12600 1.000 27.35747 ?  128 PHE A CE2   1 
ATOM   927  C CZ    . PHE A 1 148 ? -14.66900 -21.12600 31.86700 1.000 25.37681 ?  128 PHE A CZ    1 
ATOM   928  N N     . PHE A 1 149 ? -19.12700 -16.22000 34.51200 1.000 24.48447 ?  129 PHE A N     1 
ATOM   929  C CA    . PHE A 1 149 ? -20.19600 -15.25200 34.73000 1.000 29.74180 ?  129 PHE A CA    1 
ATOM   930  C C     . PHE A 1 149 ? -20.19600 -14.21600 33.62100 1.000 27.57536 ?  129 PHE A C     1 
ATOM   931  O O     . PHE A 1 149 ? -19.14000 -13.82800 33.11400 1.000 23.92768 ?  129 PHE A O     1 
ATOM   932  C CB    . PHE A 1 149 ? -20.05800 -14.48100 36.04900 1.000 27.82748 ?  129 PHE A CB    1 
ATOM   933  C CG    . PHE A 1 149 ? -19.95700 -15.34200 37.27700 1.000 30.62639 ?  129 PHE A CG    1 
ATOM   934  C CD1   . PHE A 1 149 ? -18.73800 -15.87400 37.67300 1.000 28.01744 ?  129 PHE A CD1   1 
ATOM   935  C CD2   . PHE A 1 149 ? -21.06800 -15.55500 38.07700 1.000 31.24755 ?  129 PHE A CD2   1 
ATOM   936  C CE1   . PHE A 1 149 ? -18.64000 -16.63800 38.81700 1.000 31.64519 ?  129 PHE A CE1   1 
ATOM   937  C CE2   . PHE A 1 149 ? -20.96800 -16.31800 39.23100 1.000 33.45039 ?  129 PHE A CE2   1 
ATOM   938  C CZ    . PHE A 1 149 ? -19.75700 -16.86200 39.59400 1.000 32.97810 ?  129 PHE A CZ    1 
ATOM   939  N N     . GLN A 1 150 ? -21.38800 -13.73800 33.27900 1.000 25.32367 ?  130 GLN A N     1 
ATOM   940  C CA    . GLN A 1 150 ? -21.49200 -12.49700 32.53000 1.000 28.80323 ?  130 GLN A CA    1 
ATOM   941  C C     . GLN A 1 150 ? -21.32200 -11.31000 33.47600 1.000 31.03383 ?  130 GLN A C     1 
ATOM   942  O O     . GLN A 1 150 ? -21.85100 -11.31000 34.59200 1.000 29.46596 ?  130 GLN A O     1 
ATOM   943  C CB    . GLN A 1 150 ? -22.83200 -12.40800 31.80700 1.000 30.41697 ?  130 GLN A CB    1 
ATOM   944  C CG    . GLN A 1 150 ? -22.83900 -11.38600 30.67900 1.000 28.91782 ?  130 GLN A CG    1 
ATOM   945  C CD    . GLN A 1 150 ? -23.28700 -10.01100 31.15300 1.000 37.06360 ?  130 GLN A CD    1 
ATOM   946  O OE1   . GLN A 1 150 ? -23.78300 -9.86300  32.27400 1.000 38.44426 ?  130 GLN A OE1   1 
ATOM   947  N NE2   . GLN A 1 150 ? -23.09900 -8.99800  30.31000 1.000 36.33830 ?  130 GLN A NE2   1 
ATOM   948  N N     . GLY A 1 151 ? -20.57000 -10.30600 33.03200 1.000 28.60461 ?  131 GLY A N     1 
ATOM   949  C CA    . GLY A 1 151 ? -20.34500 -9.12700  33.85400 1.000 27.43142 ?  131 GLY A CA    1 
ATOM   950  C C     . GLY A 1 151 ? -19.55600 -8.07800  33.09800 1.000 27.54992 ?  131 GLY A C     1 
ATOM   951  O O     . GLY A 1 151 ? -18.95700 -8.34200  32.04800 1.000 24.65149 ?  131 GLY A O     1 
ATOM   952  N N     . ASP A 1 152 ? -19.55500 -6.87400  33.66100 1.000 28.03964 ?  132 ASP A N     1 
ATOM   953  C CA    . ASP A 1 152 ? -18.90900 -5.70700  33.06000 1.000 25.40011 ?  132 ASP A CA    1 
ATOM   954  C C     . ASP A 1 152 ? -17.65500 -5.35900  33.84600 1.000 26.12552 ?  132 ASP A C     1 
ATOM   955  O O     . ASP A 1 152 ? -17.73700 -5.01800  35.03500 1.000 26.21639 ?  132 ASP A O     1 
ATOM   956  C CB    . ASP A 1 152 ? -19.87100 -4.52000  33.03400 1.000 30.04637 ?  132 ASP A CB    1 
ATOM   957  C CG    . ASP A 1 152 ? -19.26600 -3.27000  32.40600 1.000 30.83870 ?  132 ASP A CG    1 
ATOM   958  O OD1   . ASP A 1 152 ? -18.05400 -3.25600  32.06000 1.000 24.36709 ?  132 ASP A OD1   1 
ATOM   959  O OD2   . ASP A 1 152 ? -20.03700 -2.29700  32.24400 1.000 30.86944 -1 132 ASP A OD2   1 
ATOM   960  N N     . ALA A 1 153 ? -16.50600 -5.42100  33.16900 1.000 24.34659 ?  133 ALA A N     1 
ATOM   961  C CA    . ALA A 1 153 ? -15.22200 -5.09100  33.78800 1.000 25.16592 ?  133 ALA A CA    1 
ATOM   962  C C     . ALA A 1 153 ? -15.17000 -3.64900  34.27200 1.000 30.93421 ?  133 ALA A C     1 
ATOM   963  O O     . ALA A 1 153 ? -14.41900 -3.33300  35.20400 1.000 27.35951 ?  133 ALA A O     1 
ATOM   964  C CB    . ALA A 1 153 ? -14.08400 -5.33000  32.79500 1.000 24.20342 ?  133 ALA A CB    1 
ATOM   965  N N     . CYS A 1 154 ? -15.92000 -2.75800  33.63500 1.000 26.30137 ?  134 CYS A N     1 
ATOM   966  C CA    . CYS A 1 154 ? -15.91500 -1.36000  34.03900 1.000 27.95969 ?  134 CYS A CA    1 
ATOM   967  C C     . CYS A 1 154 ? -16.79800 -1.09000  35.25400 1.000 27.49846 ?  134 CYS A C     1 
ATOM   968  O O     . CYS A 1 154 ? -16.81300 0.04000   35.75100 1.000 31.32788 ?  134 CYS A O     1 
ATOM   969  C CB    . CYS A 1 154 ? -16.35500 -0.49200  32.85500 1.000 29.48270 ?  134 CYS A CB    1 
ATOM   970  S SG    . CYS A 1 154 ? -15.17100 -0.53700  31.48900 1.000 29.65962 ?  134 CYS A SG    1 
ATOM   971  N N     . ASN A 1 155 ? -17.51900 -2.09200  35.74500 1.000 27.66742 ?  135 ASN A N     1 
ATOM   972  C CA    . ASN A 1 155 ? -18.44600 -1.91800  36.85800 1.000 29.04269 ?  135 ASN A CA    1 
ATOM   973  C C     . ASN A 1 155 ? -18.81100 -3.29000  37.42000 1.000 29.42241 ?  135 ASN A C     1 
ATOM   974  O O     . ASN A 1 155 ? -19.95600 -3.74000  37.30200 1.000 32.61656 ?  135 ASN A O     1 
ATOM   975  C CB    . ASN A 1 155 ? -19.69600 -1.15900  36.39900 1.000 28.71879 ?  135 ASN A CB    1 
ATOM   976  C CG    . ASN A 1 155 ? -20.44700 -0.50800  37.55400 1.000 29.78134 ?  135 ASN A CG    1 
ATOM   977  O OD1   . ASN A 1 155 ? -20.06300 -0.63900  38.71300 1.000 28.72703 ?  135 ASN A OD1   1 
ATOM   978  N ND2   . ASN A 1 155 ? -21.52700 0.19400   37.23400 1.000 27.50083 ?  135 ASN A ND2   1 
ATOM   979  N N     . LEU A 1 156 ? -17.84200 -3.96700  38.01900 1.000 26.80136 ?  136 LEU A N     1 
ATOM   980  C CA    . LEU A 1 156 ? -18.04700 -5.33200  38.47800 1.000 30.00132 ?  136 LEU A CA    1 
ATOM   981  C C     . LEU A 1 156 ? -18.91800 -5.34300  39.72700 1.000 30.49417 ?  136 LEU A C     1 
ATOM   982  O O     . LEU A 1 156 ? -18.81700 -4.45600  40.57700 1.000 27.31305 ?  136 LEU A O     1 
ATOM   983  C CB    . LEU A 1 156 ? -16.70100 -5.99500  38.78800 1.000 25.93788 ?  136 LEU A CB    1 
ATOM   984  C CG    . LEU A 1 156 ? -15.80300 -6.42100  37.62200 1.000 25.98477 ?  136 LEU A CG    1 
ATOM   985  C CD1   . LEU A 1 156 ? -14.40300 -6.78000  38.13200 1.000 26.98363 ?  136 LEU A CD1   1 
ATOM   986  C CD2   . LEU A 1 156 ? -16.41500 -7.59700  36.84400 1.000 28.04193 ?  136 LEU A CD2   1 
ATOM   987  N N     . THR A 1 157 ? -19.76000 -6.37400  39.85200 1.000 29.58904 ?  137 THR A N     1 
ATOM   988  C CA    . THR A 1 157 ? -20.54800 -6.52900  41.06900 1.000 32.98011 ?  137 THR A CA    1 
ATOM   989  C C     . THR A 1 157 ? -19.63000 -6.86100  42.24700 1.000 32.29699 ?  137 THR A C     1 
ATOM   990  O O     . THR A 1 157 ? -18.48100 -7.26900  42.05400 1.000 31.59046 ?  137 THR A O     1 
ATOM   991  C CB    . THR A 1 157 ? -21.61700 -7.60900  40.89300 1.000 33.56687 ?  137 THR A CB    1 
ATOM   992  O OG1   . THR A 1 157 ? -21.00000 -8.87300  40.62100 1.000 36.78498 ?  137 THR A OG1   1 
ATOM   993  C CG2   . THR A 1 157 ? -22.56100 -7.23800  39.76100 1.000 32.24814 ?  137 THR A CG2   1 
ATOM   994  N N     . PRO A 1 158 ? -20.10900 -6.67500  43.48600 1.000 37.44283 ?  138 PRO A N     1 
ATOM   995  C CA    . PRO A 1 158 ? -19.20000 -6.77200  44.64400 1.000 36.19880 ?  138 PRO A CA    1 
ATOM   996  C C     . PRO A 1 158 ? -18.64100 -8.16200  44.91200 1.000 36.00743 ?  138 PRO A C     1 
ATOM   997  O O     . PRO A 1 158 ? -17.57900 -8.26300  45.54300 1.000 36.36470 ?  138 PRO A O     1 
ATOM   998  C CB    . PRO A 1 158 ? -20.07300 -6.29600  45.81400 1.000 37.91678 ?  138 PRO A CB    1 
ATOM   999  C CG    . PRO A 1 158 ? -21.09300 -5.39400  45.16100 1.000 38.19717 ?  138 PRO A CG    1 
ATOM   1000 C CD    . PRO A 1 158 ? -21.41200 -6.10100  43.87900 1.000 37.62017 ?  138 PRO A CD    1 
ATOM   1001 N N     . GLN A 1 159 ? -19.30500 -9.23200  44.47400 1.000 35.90802 ?  139 GLN A N     1 
ATOM   1002 C CA    . GLN A 1 159 ? -18.82400 -10.56500 44.82200 1.000 38.29150 ?  139 GLN A CA    1 
ATOM   1003 C C     . GLN A 1 159 ? -17.44800 -10.85300 44.22800 1.000 37.74084 ?  139 GLN A C     1 
ATOM   1004 O O     . GLN A 1 159 ? -16.75100 -11.74800 44.71400 1.000 39.77445 ?  139 GLN A O     1 
ATOM   1005 C CB    . GLN A 1 159 ? -19.83900 -11.63100 44.38400 1.000 36.67436 ?  139 GLN A CB    1 
ATOM   1006 C CG    . GLN A 1 159 ? -20.03200 -11.77000 42.87100 1.000 40.14246 ?  139 GLN A CG    1 
ATOM   1007 C CD    . GLN A 1 159 ? -21.17500 -12.71400 42.50000 1.000 40.08328 ?  139 GLN A CD    1 
ATOM   1008 N N     . PHE A 1 160 ? -17.02600 -10.09800 43.21100 1.000 35.64921 ?  140 PHE A N     1 
ATOM   1009 C CA    . PHE A 1 160 ? -15.76900 -10.38100 42.52000 1.000 35.12949 ?  140 PHE A CA    1 
ATOM   1010 C C     . PHE A 1 160 ? -14.66500 -9.59700  43.21700 1.000 31.18167 ?  140 PHE A C     1 
ATOM   1011 O O     . PHE A 1 160 ? -14.27900 -8.49800  42.81300 1.000 30.65916 ?  140 PHE A O     1 
ATOM   1012 C CB    . PHE A 1 160 ? -15.88600 -10.03500 41.04100 1.000 33.15142 ?  140 PHE A CB    1 
ATOM   1013 C CG    . PHE A 1 160 ? -16.93000 -10.83700 40.31500 1.000 32.44209 ?  140 PHE A CG    1 
ATOM   1014 C CD1   . PHE A 1 160 ? -16.70900 -12.16600 39.99900 1.000 27.10028 ?  140 PHE A CD1   1 
ATOM   1015 C CD2   . PHE A 1 160 ? -18.14700 -10.26800 39.97100 1.000 34.88763 ?  140 PHE A CD2   1 
ATOM   1016 C CE1   . PHE A 1 160 ? -17.67400 -12.91000 39.33600 1.000 31.52079 ?  140 PHE A CE1   1 
ATOM   1017 C CE2   . PHE A 1 160 ? -19.11700 -11.01100 39.30500 1.000 33.93507 ?  140 PHE A CE2   1 
ATOM   1018 C CZ    . PHE A 1 160 ? -18.88300 -12.32800 38.99000 1.000 30.17053 ?  140 PHE A CZ    1 
ATOM   1019 N N     . LYS A 1 161 ? -14.14500 -10.18800 44.28900 1.000 31.97999 ?  141 LYS A N     1 
ATOM   1020 C CA    . LYS A 1 161 ? -13.20300 -9.49400  45.15200 1.000 30.93059 ?  141 LYS A CA    1 
ATOM   1021 C C     . LYS A 1 161 ? -12.21300 -10.49400 45.72200 1.000 33.19923 ?  141 LYS A C     1 
ATOM   1022 O O     . LYS A 1 161 ? -12.32300 -11.70400 45.51400 1.000 33.11782 ?  141 LYS A O     1 
ATOM   1023 C CB    . LYS A 1 161 ? -13.92100 -8.77200  46.29400 1.000 36.99931 ?  141 LYS A CB    1 
ATOM   1024 C CG    . LYS A 1 161 ? -14.84200 -9.69000  47.10100 1.000 36.20949 ?  141 LYS A CG    1 
ATOM   1025 C CD    . LYS A 1 161 ? -15.20300 -9.08800  48.45000 1.000 44.99224 ?  141 LYS A CD    1 
ATOM   1026 N N     . GLU A 1 162 ? -11.23700 -9.95700  46.45400 1.000 34.35993 ?  142 GLU A N     1 
ATOM   1027 C CA    . GLU A 1 162 ? -10.29800 -10.75500 47.23500 1.000 35.34693 ?  142 GLU A CA    1 
ATOM   1028 C C     . GLU A 1 162 ? -9.54700  -11.75400 46.35400 1.000 34.10037 ?  142 GLU A C     1 
ATOM   1029 O O     . GLU A 1 162 ? -9.49100  -12.95400 46.63500 1.000 35.01907 ?  142 GLU A O     1 
ATOM   1030 C CB    . GLU A 1 162 ? -11.02000 -11.44700 48.39100 1.000 38.96872 ?  142 GLU A CB    1 
ATOM   1031 C CG    . GLU A 1 162 ? -11.50700 -10.44600 49.44800 1.000 40.61724 ?  142 GLU A CG    1 
ATOM   1032 C CD    . GLU A 1 162 ? -12.48000 -11.05800 50.44100 1.000 47.86266 ?  142 GLU A CD    1 
ATOM   1033 O OE1   . GLU A 1 162 ? -13.02200 -12.14700 50.16200 1.000 50.79939 ?  142 GLU A OE1   1 
ATOM   1034 O OE2   . GLU A 1 162 ? -12.70000 -10.45100 51.50700 1.000 54.83427 -1 142 GLU A OE2   1 
ATOM   1035 N N     . TYR A 1 163 ? -8.95800  -11.23900 45.28100 1.000 30.00870 ?  143 TYR A N     1 
ATOM   1036 C CA    . TYR A 1 163 ? -8.21100  -12.04400 44.32900 1.000 31.85454 ?  143 TYR A CA    1 
ATOM   1037 C C     . TYR A 1 163 ? -6.71700  -11.91800 44.59300 1.000 31.89382 ?  143 TYR A C     1 
ATOM   1038 O O     . TYR A 1 163 ? -6.21000  -10.83000 44.89300 1.000 29.49023 ?  143 TYR A O     1 
ATOM   1039 C CB    . TYR A 1 163 ? -8.52100  -11.62500 42.88600 1.000 31.10767 ?  143 TYR A CB    1 
ATOM   1040 C CG    . TYR A 1 163 ? -9.91800  -11.99600 42.45000 1.000 29.52625 ?  143 TYR A CG    1 
ATOM   1041 C CD1   . TYR A 1 163 ? -10.28700 -13.33000 42.31800 1.000 29.14789 ?  143 TYR A CD1   1 
ATOM   1042 C CD2   . TYR A 1 163 ? -10.87300 -11.01900 42.19300 1.000 27.64316 ?  143 TYR A CD2   1 
ATOM   1043 C CE1   . TYR A 1 163 ? -11.57500 -13.68600 41.93200 1.000 29.89309 ?  143 TYR A CE1   1 
ATOM   1044 C CE2   . TYR A 1 163 ? -12.16500 -11.36000 41.80600 1.000 28.71239 ?  143 TYR A CE2   1 
ATOM   1045 C CZ    . TYR A 1 163 ? -12.50900 -12.70000 41.67600 1.000 28.89989 ?  143 TYR A CZ    1 
ATOM   1046 O OH    . TYR A 1 163 ? -13.77800 -13.06500 41.29100 1.000 29.85229 ?  143 TYR A OH    1 
ATOM   1047 N N     . ASP A 1 164 ? -6.02000  -13.04500 44.49200 1.000 30.41988 ?  144 ASP A N     1 
ATOM   1048 C CA    . ASP A 1 164 ? -4.56900  -12.99700 44.46000 1.000 32.19750 ?  144 ASP A CA    1 
ATOM   1049 C C     . ASP A 1 164 ? -4.07100  -12.54500 43.10000 1.000 32.87205 ?  144 ASP A C     1 
ATOM   1050 O O     . ASP A 1 164 ? -3.05200  -11.84900 43.01500 1.000 31.04037 ?  144 ASP A O     1 
ATOM   1051 C CB    . ASP A 1 164 ? -4.00300  -14.36300 44.83900 1.000 30.52830 ?  144 ASP A CB    1 
ATOM   1052 C CG    . ASP A 1 164 ? -4.54000  -14.83800 46.16800 1.000 37.17766 ?  144 ASP A CG    1 
ATOM   1053 O OD1   . ASP A 1 164 ? -4.31700  -14.13100 47.17500 1.000 39.39052 ?  144 ASP A OD1   1 
ATOM   1054 O OD2   . ASP A 1 164 ? -5.22500  -15.87800 46.20500 1.000 37.52727 -1 144 ASP A OD2   1 
ATOM   1055 N N     . LEU A 1 165 ? -4.80500  -12.88300 42.04200 1.000 29.04580 ?  145 LEU A N     1 
ATOM   1056 C CA    . LEU A 1 165 ? -4.44300  -12.52100 40.67900 1.000 29.87863 ?  145 LEU A CA    1 
ATOM   1057 C C     . LEU A 1 165 ? -5.68300  -12.05500 39.93200 1.000 28.28444 ?  145 LEU A C     1 
ATOM   1058 O O     . LEU A 1 165 ? -6.73500  -12.69500 39.99900 1.000 27.79833 ?  145 LEU A O     1 
ATOM   1059 C CB    . LEU A 1 165 ? -3.78700  -13.70700 39.94800 1.000 26.58384 ?  145 LEU A CB    1 
ATOM   1060 C CG    . LEU A 1 165 ? -3.70200  -13.65200 38.42100 1.000 29.03076 ?  145 LEU A CG    1 
ATOM   1061 C CD1   . LEU A 1 165 ? -2.85600  -12.47000 37.97500 1.000 24.67372 ?  145 LEU A CD1   1 
ATOM   1062 C CD2   . LEU A 1 165 ? -3.10500  -14.95700 37.89500 1.000 26.16873 ?  145 LEU A CD2   1 
ATOM   1063 N N     . ILE A 1 166 ? -5.56500  -10.93700 39.23100 1.000 26.25773 ?  146 ILE A N     1 
ATOM   1064 C CA    . ILE A 1 166 ? -6.55900  -10.53500 38.25200 1.000 27.34178 ?  146 ILE A CA    1 
ATOM   1065 C C     . ILE A 1 166 ? -5.83900  -10.38300 36.92400 1.000 28.37802 ?  146 ILE A C     1 
ATOM   1066 O O     . ILE A 1 166 ? -4.95400  -9.52700  36.78100 1.000 28.72083 ?  146 ILE A O     1 
ATOM   1067 C CB    . ILE A 1 166 ? -7.28200  -9.23900  38.64800 1.000 26.78863 ?  146 ILE A CB    1 
ATOM   1068 C CG1   . ILE A 1 166 ? -8.09500  -9.45900  39.92900 1.000 24.70720 ?  146 ILE A CG1   1 
ATOM   1069 C CG2   . ILE A 1 166 ? -8.17900  -8.77500  37.51200 1.000 26.25234 ?  146 ILE A CG2   1 
ATOM   1070 C CD1   . ILE A 1 166 ? -9.03000  -8.30900  40.25000 1.000 24.53685 ?  146 ILE A CD1   1 
ATOM   1071 N N     . MET A 1 167 ? -6.20800  -11.21800 35.96000 1.000 24.72390 ?  147 MET A N     1 
ATOM   1072 C CA    . MET A 1 167 ? -5.58700  -11.21600 34.64600 1.000 26.15691 ?  147 MET A CA    1 
ATOM   1073 C C     . MET A 1 167 ? -6.61300  -10.76600 33.62000 1.000 24.32076 ?  147 MET A C     1 
ATOM   1074 O O     . MET A 1 167 ? -7.71300  -11.32100 33.55200 1.000 24.85466 ?  147 MET A O     1 
ATOM   1075 C CB    . MET A 1 167 ? -5.03000  -12.60200 34.29600 1.000 22.95980 ?  147 MET A CB    1 
ATOM   1076 C CG    . MET A 1 167 ? -4.18300  -12.61900 33.04500 1.000 22.89265 ?  147 MET A CG    1 
ATOM   1077 S SD    . MET A 1 167 ? -3.51300  -14.24200 32.62100 1.000 33.67030 ?  147 MET A SD    1 
ATOM   1078 C CE    . MET A 1 167 ? -4.96600  -15.10300 32.02900 1.000 28.44829 ?  147 MET A CE    1 
ATOM   1079 N N     . ALA A 1 168 ? -6.25500  -9.75800  32.82900 1.000 25.90155 ?  148 ALA A N     1 
ATOM   1080 C CA    . ALA A 1 168 ? -7.14500  -9.21200  31.80300 1.000 25.85262 ?  148 ALA A CA    1 
ATOM   1081 C C     . ALA A 1 168 ? -6.34700  -9.09600  30.51100 1.000 25.53514 ?  148 ALA A C     1 
ATOM   1082 O O     . ALA A 1 168 ? -5.64700  -8.09900  30.29800 1.000 24.96006 ?  148 ALA A O     1 
ATOM   1083 C CB    . ALA A 1 168 ? -7.71800  -7.86100  32.22800 1.000 24.52339 ?  148 ALA A CB    1 
ATOM   1084 N N     . THR A 1 169 ? -6.44200  -10.11300 29.65700 1.000 23.23108 ?  149 THR A N     1 
ATOM   1085 C CA    . THR A 1 169 ? -5.63700  -10.16000 28.44200 1.000 25.70588 ?  149 THR A CA    1 
ATOM   1086 C C     . THR A 1 169 ? -6.43600  -9.53900  27.30100 1.000 23.64155 ?  149 THR A C     1 
ATOM   1087 O O     . THR A 1 169 ? -7.56500  -9.96200  27.01800 1.000 22.13814 ?  149 THR A O     1 
ATOM   1088 C CB    . THR A 1 169 ? -5.21400  -11.59300 28.08800 1.000 23.81799 ?  149 THR A CB    1 
ATOM   1089 O OG1   . THR A 1 169 ? -6.37100  -12.40200 27.84500 1.000 26.76251 ?  149 THR A OG1   1 
ATOM   1090 C CG2   . THR A 1 169 ? -4.38500  -12.21900 29.21900 1.000 24.74467 ?  149 THR A CG2   1 
ATOM   1091 N N     . ASN A 1 170 ? -5.84500  -8.53800  26.65900 1.000 22.97551 ?  150 ASN A N     1 
ATOM   1092 C CA    . ASN A 1 170 ? -6.43300  -7.86200  25.49900 1.000 26.44737 ?  150 ASN A CA    1 
ATOM   1093 C C     . ASN A 1 170 ? -7.82200  -7.30200  25.80700 1.000 25.36457 ?  150 ASN A C     1 
ATOM   1094 O O     . ASN A 1 170 ? -8.73600  -7.36100  24.98000 1.000 24.94283 ?  150 ASN A O     1 
ATOM   1095 C CB    . ASN A 1 170 ? -6.45300  -8.80000  24.29000 1.000 23.50243 ?  150 ASN A CB    1 
ATOM   1096 C CG    . ASN A 1 170 ? -5.03500  -9.24300  23.87300 1.000 27.43977 ?  150 ASN A CG    1 
ATOM   1097 O OD1   . ASN A 1 170 ? -4.02600  -8.66100  24.30600 1.000 26.42836 ?  150 ASN A OD1   1 
ATOM   1098 N ND2   . ASN A 1 170 ? -4.95900  -10.26200 23.03300 1.000 24.99419 ?  150 ASN A ND2   1 
ATOM   1099 N N     . LEU A 1 171 ? -7.97600  -6.73400  27.00400 1.000 24.97624 ?  151 LEU A N     1 
ATOM   1100 C CA    . LEU A 1 171 ? -9.25000  -6.18400  27.45300 1.000 21.90294 ?  151 LEU A CA    1 
ATOM   1101 C C     . LEU A 1 171 ? -9.34300  -4.66900  27.30500 1.000 26.29990 ?  151 LEU A C     1 
ATOM   1102 O O     . LEU A 1 171 ? -10.35700 -4.16800  26.80500 1.000 24.71311 ?  151 LEU A O     1 
ATOM   1103 C CB    . LEU A 1 171 ? -9.50400  -6.55700  28.92000 1.000 20.73966 ?  151 LEU A CB    1 
ATOM   1104 C CG    . LEU A 1 171 ? -10.84300 -6.04400  29.46200 1.000 24.27493 ?  151 LEU A CG    1 
ATOM   1105 C CD1   . LEU A 1 171 ? -12.01100 -6.58600  28.65200 1.000 21.51798 ?  151 LEU A CD1   1 
ATOM   1106 C CD2   . LEU A 1 171 ? -11.01500 -6.38600  30.94900 1.000 23.47952 ?  151 LEU A CD2   1 
ATOM   1107 N N     . ILE A 1 172 ? -8.30800  -3.92800  27.73000 1.000 20.66824 ?  152 ILE A N     1 
ATOM   1108 C CA    . ILE A 1 172 ? -8.47900  -2.49500  27.97300 1.000 23.08822 ?  152 ILE A CA    1 
ATOM   1109 C C     . ILE A 1 172 ? -8.82000  -1.75000  26.68700 1.000 24.61315 ?  152 ILE A C     1 
ATOM   1110 O O     . ILE A 1 172 ? -9.63100  -0.81400  26.70200 1.000 26.13567 ?  152 ILE A O     1 
ATOM   1111 C CB    . ILE A 1 172 ? -7.23300  -1.90400  28.65700 1.000 23.10512 ?  152 ILE A CB    1 
ATOM   1112 C CG1   . ILE A 1 172 ? -5.96900  -2.15800  27.82300 1.000 24.64436 ?  152 ILE A CG1   1 
ATOM   1113 C CG2   . ILE A 1 172 ? -7.07900  -2.47200  30.05300 1.000 21.47091 ?  152 ILE A CG2   1 
ATOM   1114 C CD1   . ILE A 1 172 ? -4.74900  -1.37700  28.30300 1.000 23.60369 ?  152 ILE A CD1   1 
ATOM   1115 N N     . ASP A 1 173 ? -8.22800  -2.14700  25.55500 1.000 21.92532 ?  153 ASP A N     1 
ATOM   1116 C CA    . ASP A 1 173 ? -8.56000  -1.47500  24.30000 1.000 24.20396 ?  153 ASP A CA    1 
ATOM   1117 C C     . ASP A 1 173 ? -9.86800  -1.97400  23.68400 1.000 24.32623 ?  153 ASP A C     1 
ATOM   1118 O O     . ASP A 1 173 ? -10.17100 -1.63000  22.53600 1.000 24.68617 ?  153 ASP A O     1 
ATOM   1119 C CB    . ASP A 1 173 ? -7.40300  -1.56800  23.28200 1.000 28.07933 ?  153 ASP A CB    1 
ATOM   1120 C CG    . ASP A 1 173 ? -6.80800  -2.98200  23.13700 1.000 29.27689 ?  153 ASP A CG    1 
ATOM   1121 O OD1   . ASP A 1 173 ? -6.84600  -3.79300  24.08700 1.000 26.42358 ?  153 ASP A OD1   1 
ATOM   1122 O OD2   . ASP A 1 173 ? -6.27200  -3.26800  22.04200 1.000 31.94016 -1 153 ASP A OD2   1 
ATOM   1123 N N     . ARG A 1 174 ? -10.66000 -2.74500  24.42600 1.000 23.60210 ?  154 ARG A N     1 
ATOM   1124 C CA    . ARG A 1 174 ? -12.03900 -3.02700  24.05500 1.000 24.20060 ?  154 ARG A CA    1 
ATOM   1125 C C     . ARG A 1 174 ? -13.04600 -2.43600  25.04200 1.000 25.41465 ?  154 ARG A C     1 
ATOM   1126 O O     . ARG A 1 174 ? -14.24400 -2.68800  24.90500 1.000 27.17163 ?  154 ARG A O     1 
ATOM   1127 C CB    . ARG A 1 174 ? -12.25100 -4.53900  23.91600 1.000 25.99864 ?  154 ARG A CB    1 
ATOM   1128 C CG    . ARG A 1 174 ? -11.41000 -5.17200  22.82500 1.000 24.45334 ?  154 ARG A CG    1 
ATOM   1129 C CD    . ARG A 1 174 ? -11.76900 -4.58500  21.46800 1.000 29.55011 ?  154 ARG A CD    1 
ATOM   1130 N NE    . ARG A 1 174 ? -11.16200 -5.31000  20.35500 1.000 33.26050 ?  154 ARG A NE    1 
ATOM   1131 C CZ    . ARG A 1 174 ? -10.23500 -4.80300  19.55100 1.000 37.10163 ?  154 ARG A CZ    1 
ATOM   1132 N NH1   . ARG A 1 174 ? -9.72800  -3.59400  19.75200 1.000 36.61028 ?  154 ARG A NH1   1 
ATOM   1133 N NH2   . ARG A 1 174 ? -9.81900  -5.51800  18.51000 1.000 40.59229 ?  154 ARG A NH2   1 
ATOM   1134 N N     . LEU A 1 175 ? -12.56800 -1.63700  25.99100 1.000 26.23996 ?  155 LEU A N     1 
ATOM   1135 C CA    . LEU A 1 175 ? -13.45300 -1.09400  27.05300 1.000 24.30707 ?  155 LEU A CA    1 
ATOM   1136 C C     . LEU A 1 175 ? -14.02600 0.28100   26.67900 1.000 26.43834 ?  155 LEU A C     1 
ATOM   1137 O O     . LEU A 1 175 ? -13.26600 1.12100   26.21100 1.000 23.50719 ?  155 LEU A O     1 
ATOM   1138 C CB    . LEU A 1 175 ? -12.66000 -1.03500  28.36500 1.000 23.05219 ?  155 LEU A CB    1 
ATOM   1139 C CG    . LEU A 1 175 ? -12.31600 -2.37100  29.01800 1.000 24.78332 ?  155 LEU A CG    1 
ATOM   1140 C CD1   . LEU A 1 175 ? -11.74700 -2.15300  30.40800 1.000 23.54188 ?  155 LEU A CD1   1 
ATOM   1141 C CD2   . LEU A 1 175 ? -13.52700 -3.28300  29.08000 1.000 18.92090 ?  155 LEU A CD2   1 
ATOM   1142 N N     . TYR A 1 176 ? -15.31700 0.49600   26.94300 1.000 27.23000 ?  156 TYR A N     1 
ATOM   1143 C CA    . TYR A 1 176 ? -15.98500 1.80000   26.67300 1.000 26.05657 ?  156 TYR A CA    1 
ATOM   1144 C C     . TYR A 1 176 ? -15.30300 2.91700   27.47200 1.000 28.37204 ?  156 TYR A C     1 
ATOM   1145 O O     . TYR A 1 176 ? -15.11200 3.99100   26.91600 1.000 27.13860 ?  156 TYR A O     1 
ATOM   1146 C CB    . TYR A 1 176 ? -17.49400 1.69900   26.91300 1.000 27.23039 ?  156 TYR A CB    1 
ATOM   1147 C CG    . TYR A 1 176 ? -17.97800 1.33200   28.29200 1.000 29.11587 ?  156 TYR A CG    1 
ATOM   1148 C CD1   . TYR A 1 176 ? -18.24500 2.30300   29.23900 1.000 25.05920 ?  156 TYR A CD1   1 
ATOM   1149 C CD2   . TYR A 1 176 ? -18.24100 0.01500   28.62700 1.000 30.80767 ?  156 TYR A CD2   1 
ATOM   1150 C CE1   . TYR A 1 176 ? -18.71900 1.97500   30.49600 1.000 27.05055 ?  156 TYR A CE1   1 
ATOM   1151 C CE2   . TYR A 1 176 ? -18.71600 -0.33200  29.88000 1.000 29.53949 ?  156 TYR A CE2   1 
ATOM   1152 C CZ    . TYR A 1 176 ? -18.95800 0.65300   30.81900 1.000 29.35952 ?  156 TYR A CZ    1 
ATOM   1153 O OH    . TYR A 1 176 ? -19.42700 0.32100   32.06200 1.000 24.98071 ?  156 TYR A OH    1 
ATOM   1154 N N     . GLU A 1 177 ? -14.95600 2.66200   28.72700 1.000 26.13305 ?  157 GLU A N     1 
ATOM   1155 C CA    . GLU A 1 177 ? -14.18000 3.64800   29.51900 1.000 27.90396 ?  157 GLU A CA    1 
ATOM   1156 C C     . GLU A 1 177 ? -13.19900 2.87400   30.40400 1.000 28.41419 ?  157 GLU A C     1 
ATOM   1157 O O     . GLU A 1 177 ? -13.56300 2.51600   31.52700 1.000 25.50321 ?  157 GLU A O     1 
ATOM   1158 C CB    . GLU A 1 177 ? -15.05700 4.61700   30.31300 1.000 31.93517 ?  157 GLU A CB    1 
ATOM   1159 C CG    . GLU A 1 177 ? -14.51200 6.03200   30.37800 1.000 28.52694 ?  157 GLU A CG    1 
ATOM   1160 C CD    . GLU A 1 177 ? -13.16900 6.24800   31.05800 1.000 31.65085 ?  157 GLU A CD    1 
ATOM   1161 O OE1   . GLU A 1 177 ? -12.17100 5.66600   30.61800 1.000 27.02875 ?  157 GLU A OE1   1 
ATOM   1162 O OE2   . GLU A 1 177 ? -13.11800 7.03100   32.00300 1.000 30.17893 -1 157 GLU A OE2   1 
ATOM   1163 N N     . PRO A 1 178 ? -11.97900 2.60400   29.89600 1.000 26.51679 ?  158 PRO A N     1 
ATOM   1164 C CA    . PRO A 1 178 ? -10.97700 1.82400   30.63400 1.000 26.99824 ?  158 PRO A CA    1 
ATOM   1165 C C     . PRO A 1 178 ? -10.64900 2.30000   32.06400 1.000 28.78502 ?  158 PRO A C     1 
ATOM   1166 O O     . PRO A 1 178 ? -10.38800 1.47300   32.88700 1.000 28.22689 ?  158 PRO A O     1 
ATOM   1167 C CB    . PRO A 1 178 ? -9.74900  1.90500   29.70800 1.000 25.07975 ?  158 PRO A CB    1 
ATOM   1168 C CG    . PRO A 1 178 ? -10.04000 2.99600   28.72300 1.000 28.11497 ?  158 PRO A CG    1 
ATOM   1169 C CD    . PRO A 1 178 ? -11.53800 2.99000   28.56600 1.000 24.60595 ?  158 PRO A CD    1 
ATOM   1170 N N     . ARG A 1 179 ? -10.68000 3.60300   32.32400 1.000 27.82472 ?  159 ARG A N     1 
ATOM   1171 C CA    A ARG A 1 179 ? -10.45300 4.11200   33.71300 0.466 28.37130 ?  159 ARG A CA    1 
ATOM   1172 C CA    B ARG A 1 179 ? -10.45500 4.11700   33.71200 0.534 28.23116 ?  159 ARG A CA    1 
ATOM   1173 C C     . ARG A 1 179 ? -11.39000 3.57500   34.83400 1.000 25.69978 ?  159 ARG A C     1 
ATOM   1174 O O     . ARG A 1 179 ? -11.14800 3.22100   36.11500 1.000 29.57358 ?  159 ARG A O     1 
ATOM   1175 C CB    A ARG A 1 179 ? -10.50000 5.64300   33.71100 0.466 28.58474 ?  159 ARG A CB    1 
ATOM   1176 C CB    B ARG A 1 179 ? -10.50900 5.64900   33.70500 0.534 28.43942 ?  159 ARG A CB    1 
ATOM   1177 C CG    A ARG A 1 179 ? -9.22800  6.31100   33.21600 0.466 30.67447 ?  159 ARG A CG    1 
ATOM   1178 C CG    B ARG A 1 179 ? -9.22900  6.32900   33.24200 0.534 29.80977 ?  159 ARG A CG    1 
ATOM   1179 C CD    A ARG A 1 179 ? -9.47000  7.78400   32.96000 0.466 30.69899 ?  159 ARG A CD    1 
ATOM   1180 C CD    B ARG A 1 179 ? -9.37600  7.83900   33.19700 0.534 30.59472 ?  159 ARG A CD    1 
ATOM   1181 N NE    A ARG A 1 179 ? -8.62500  8.63300   33.78400 0.466 32.49936 ?  159 ARG A NE    1 
ATOM   1182 N NE    B ARG A 1 179 ? -10.72300 8.25000   32.82700 0.534 30.76800 ?  159 ARG A NE    1 
ATOM   1183 C CZ    A ARG A 1 179 ? -7.29800  8.59900   33.78700 0.466 32.33635 ?  159 ARG A CZ    1 
ATOM   1184 C CZ    B ARG A 1 179 ? -11.10800 9.50800   32.64400 0.534 30.46628 ?  159 ARG A CZ    1 
ATOM   1185 N NH1   A ARG A 1 179 ? -6.63200  8.65700   32.64800 0.466 31.68273 ?  159 ARG A NH1   1 
ATOM   1186 N NH1   B ARG A 1 179 ? -10.35600 10.50300  33.07800 0.534 29.79193 ?  159 ARG A NH1   1 
ATOM   1187 N NH2   A ARG A 1 179 ? -6.64200  8.51300   34.93000 0.466 31.69440 ?  159 ARG A NH2   1 
ATOM   1188 N NH2   B ARG A 1 179 ? -12.25100 9.76700   32.03300 0.534 28.19841 ?  159 ARG A NH2   1 
ATOM   1189 N N     . LEU A 1 180 ? -12.63200 3.35300   34.41000 1.000 26.73230 ?  160 LEU A N     1 
ATOM   1190 C CA    . LEU A 1 180 ? -13.61700 2.78500   35.36800 1.000 26.80410 ?  160 LEU A CA    1 
ATOM   1191 C C     . LEU A 1 180 ? -13.08500 1.46100   35.91500 1.000 30.65782 ?  160 LEU A C     1 
ATOM   1192 O O     . LEU A 1 180 ? -13.28800 1.18700   37.09600 1.000 31.44260 ?  160 LEU A O     1 
ATOM   1193 C CB    . LEU A 1 180 ? -14.92300 2.54900   34.61300 1.000 26.41404 ?  160 LEU A CB    1 
ATOM   1194 C CG    . LEU A 1 180 ? -16.04600 3.55100   34.86000 1.000 31.27054 ?  160 LEU A CG    1 
ATOM   1195 C CD1   . LEU A 1 180 ? -15.52600 4.97200   34.79000 1.000 29.95215 ?  160 LEU A CD1   1 
ATOM   1196 C CD2   . LEU A 1 180 ? -17.16600 3.35000   33.85400 1.000 29.27039 ?  160 LEU A CD2   1 
ATOM   1197 N N     . PHE A 1 181 ? -12.44300 0.67600   35.05700 1.000 28.14293 ?  161 PHE A N     1 
ATOM   1198 C CA    . PHE A 1 181 ? -11.83400 -0.59700  35.49700 1.000 30.15868 ?  161 PHE A CA    1 
ATOM   1199 C C     . PHE A 1 181 ? -10.49300 -0.32100  36.17400 1.000 26.37290 ?  161 PHE A C     1 
ATOM   1200 O O     . PHE A 1 181 ? -10.34700 -0.66400  37.34100 1.000 27.48716 ?  161 PHE A O     1 
ATOM   1201 C CB    . PHE A 1 181 ? -11.68500 -1.52600  34.28600 1.000 27.11416 ?  161 PHE A CB    1 
ATOM   1202 C CG    . PHE A 1 181 ? -10.60500 -2.57400  34.35200 1.000 25.67246 ?  161 PHE A CG    1 
ATOM   1203 C CD1   . PHE A 1 181 ? -10.64600 -3.58700  35.29500 1.000 26.04288 ?  161 PHE A CD1   1 
ATOM   1204 C CD2   . PHE A 1 181 ? -9.56700  -2.57100  33.43800 1.000 24.83141 ?  161 PHE A CD2   1 
ATOM   1205 C CE1   . PHE A 1 181 ? -9.65500  -4.55300  35.33900 1.000 27.01365 ?  161 PHE A CE1   1 
ATOM   1206 C CE2   . PHE A 1 181 ? -8.58100  -3.54300  33.47800 1.000 26.56407 ?  161 PHE A CE2   1 
ATOM   1207 C CZ    . PHE A 1 181 ? -8.62700  -4.53200  34.42800 1.000 25.18515 ?  161 PHE A CZ    1 
ATOM   1208 N N     . LEU A 1 182 ? -9.57800  0.32200   35.46500 1.000 27.14948 ?  162 LEU A N     1 
ATOM   1209 C CA    . LEU A 1 182 ? -8.19100  0.48900   35.96700 1.000 27.13655 ?  162 LEU A CA    1 
ATOM   1210 C C     . LEU A 1 182 ? -8.10500  1.25500   37.28900 1.000 30.54234 ?  162 LEU A C     1 
ATOM   1211 O O     . LEU A 1 182 ? -7.33200  0.83300   38.15200 1.000 27.61927 ?  162 LEU A O     1 
ATOM   1212 C CB    . LEU A 1 182 ? -7.40600  1.19500   34.86400 1.000 27.98476 ?  162 LEU A CB    1 
ATOM   1213 C CG    . LEU A 1 182 ? -7.22700  0.40300   33.57100 1.000 30.60958 ?  162 LEU A CG    1 
ATOM   1214 C CD1   . LEU A 1 182 ? -6.81400  1.32100   32.43500 1.000 28.62928 ?  162 LEU A CD1   1 
ATOM   1215 C CD2   . LEU A 1 182 ? -6.21100  -0.71100  33.75200 1.000 25.92546 ?  162 LEU A CD2   1 
ATOM   1216 N N     . GLU A 1 183 ? -8.85100  2.34500   37.42400 1.000 29.77043 ?  163 GLU A N     1 
ATOM   1217 C CA    . GLU A 1 183 ? -8.69700  3.16200   38.62800 1.000 31.27876 ?  163 GLU A CA    1 
ATOM   1218 C C     . GLU A 1 183 ? -9.25200  2.47900   39.86800 1.000 32.16202 ?  163 GLU A C     1 
ATOM   1219 O O     . GLU A 1 183 ? -8.87700  2.85500   40.98200 1.000 30.32350 ?  163 GLU A O     1 
ATOM   1220 C CB    . GLU A 1 183 ? -9.37300  4.52500   38.45400 1.000 28.78006 ?  163 GLU A CB    1 
ATOM   1221 C CG    . GLU A 1 183 ? -8.81000  5.35800   37.30900 1.000 30.32428 ?  163 GLU A CG    1 
ATOM   1222 C CD    . GLU A 1 183 ? -9.37800  6.78100   37.27900 1.000 32.69996 ?  163 GLU A CD    1 
ATOM   1223 O OE1   . GLU A 1 183 ? -10.40900 7.04600   37.94100 1.000 28.85624 ?  163 GLU A OE1   1 
ATOM   1224 O OE2   . GLU A 1 183 ? -8.79300  7.63300   36.57800 1.000 29.61780 -1 163 GLU A OE2   1 
ATOM   1225 N N     . ASN A 1 184 ? -10.11300 1.47400   39.69900 1.000 31.96180 ?  164 ASN A N     1 
ATOM   1226 C CA    . ASN A 1 184 ? -10.79000 0.82300   40.80900 1.000 31.69163 ?  164 ASN A CA    1 
ATOM   1227 C C     . ASN A 1 184 ? -10.36000 -0.61500  41.05800 1.000 30.15991 ?  164 ASN A C     1 
ATOM   1228 O O     . ASN A 1 184 ? -10.68500 -1.15500  42.11800 1.000 29.35820 ?  164 ASN A O     1 
ATOM   1229 C CB    . ASN A 1 184 ? -12.30300 0.84700   40.57800 1.000 28.28375 ?  164 ASN A CB    1 
ATOM   1230 C CG    . ASN A 1 184 ? -12.85700 2.24300   40.60800 1.000 31.48841 ?  164 ASN A CG    1 
ATOM   1231 O OD1   . ASN A 1 184 ? -12.87000 2.88700   41.65900 1.000 32.94193 ?  164 ASN A OD1   1 
ATOM   1232 N ND2   . ASN A 1 184 ? -13.30600 2.73200   39.45600 1.000 28.86948 ?  164 ASN A ND2   1 
ATOM   1233 N N     . ILE A 1 185 ? -9.63400  -1.24900  40.13200 1.000 30.89293 ?  165 ILE A N     1 
ATOM   1234 C CA    . ILE A 1 185 ? -9.41600  -2.69100  40.23000 1.000 25.35628 ?  165 ILE A CA    1 
ATOM   1235 C C     . ILE A 1 185 ? -8.59700  -3.07700  41.46300 1.000 30.58756 ?  165 ILE A C     1 
ATOM   1236 O O     . ILE A 1 185 ? -8.73100  -4.20200  41.96300 1.000 30.34442 ?  165 ILE A O     1 
ATOM   1237 C CB    . ILE A 1 185 ? -8.76700  -3.21100  38.92700 1.000 28.33898 ?  165 ILE A CB    1 
ATOM   1238 C CG1   . ILE A 1 185 ? -8.92300  -4.73300  38.81600 1.000 27.96727 ?  165 ILE A CG1   1 
ATOM   1239 C CG2   . ILE A 1 185 ? -7.29900  -2.80200  38.84600 1.000 29.62516 ?  165 ILE A CG2   1 
ATOM   1240 C CD1   . ILE A 1 185 ? -10.35600 -5.20900  38.93900 1.000 24.52964 ?  165 ILE A CD1   1 
ATOM   1241 N N     . HIS A 1 186 ? -7.78200  -2.15600  42.00200 1.000 32.80418 ?  166 HIS A N     1 
ATOM   1242 C CA    . HIS A 1 186 ? -6.97200  -2.48800  43.17400 1.000 31.32085 ?  166 HIS A CA    1 
ATOM   1243 C C     . HIS A 1 186 ? -7.83500  -2.87000  44.37500 1.000 33.28620 ?  166 HIS A C     1 
ATOM   1244 O O     . HIS A 1 186 ? -7.38500  -3.62200  45.24600 1.000 30.48535 ?  166 HIS A O     1 
ATOM   1245 C CB    . HIS A 1 186 ? -6.05200  -1.31700  43.53400 1.000 33.69818 ?  166 HIS A CB    1 
ATOM   1246 C CG    . HIS A 1 186 ? -6.78300  -0.08900  43.96900 1.000 33.84090 ?  166 HIS A CG    1 
ATOM   1247 N ND1   . HIS A 1 186 ? -7.46800  0.72200   43.08900 1.000 33.45528 ?  166 HIS A ND1   1 
ATOM   1248 C CD2   . HIS A 1 186 ? -6.96000  0.45200   45.19600 1.000 33.58983 ?  166 HIS A CD2   1 
ATOM   1249 C CE1   . HIS A 1 186 ? -8.02900  1.71400   43.75500 1.000 34.60338 ?  166 HIS A CE1   1 
ATOM   1250 N NE2   . HIS A 1 186 ? -7.73700  1.57300   45.03600 1.000 32.23289 ?  166 HIS A NE2   1 
ATOM   1251 N N     . LYS A 1 187 ? -9.07900  -2.39100  44.43100 1.000 33.66862 ?  167 LYS A N     1 
ATOM   1252 C CA    . LYS A 1 187 ? -9.96400  -2.75700  45.53100 1.000 33.17443 ?  167 LYS A CA    1 
ATOM   1253 C C     . LYS A 1 187 ? -10.42100 -4.20500  45.47400 1.000 33.97937 ?  167 LYS A C     1 
ATOM   1254 O O     . LYS A 1 187 ? -11.04300 -4.66900  46.43300 1.000 33.88331 ?  167 LYS A O     1 
ATOM   1255 C CB    . LYS A 1 187 ? -11.19500 -1.84600  45.56400 1.000 31.11211 ?  167 LYS A CB    1 
ATOM   1256 C CG    . LYS A 1 187 ? -10.88200 -0.35000  45.64500 1.000 31.17589 ?  167 LYS A CG    1 
ATOM   1257 C CD    . LYS A 1 187 ? -12.11200 0.50300   45.31900 1.000 30.48857 ?  167 LYS A CD    1 
ATOM   1258 N N     . ARG A 1 188 ? -10.14200 -4.92300  44.38500 1.000 33.30608 ?  168 ARG A N     1 
ATOM   1259 C CA    . ARG A 1 188 ? -10.55400 -6.31500  44.24000 1.000 29.68737 ?  168 ARG A CA    1 
ATOM   1260 C C     . ARG A 1 188 ? -9.40400  -7.29800  44.39100 1.000 31.00703 ?  168 ARG A C     1 
ATOM   1261 O O     . ARG A 1 188 ? -9.62600  -8.50900  44.28800 1.000 31.24730 ?  168 ARG A O     1 
ATOM   1262 C CB    . ARG A 1 188 ? -11.23400 -6.52500  42.87900 1.000 34.45074 ?  168 ARG A CB    1 
ATOM   1263 C CG    . ARG A 1 188 ? -12.27100 -5.45600  42.52500 1.000 31.83593 ?  168 ARG A CG    1 
ATOM   1264 C CD    . ARG A 1 188 ? -13.47300 -5.53200  43.46100 1.000 33.59410 ?  168 ARG A CD    1 
ATOM   1265 N NE    . ARG A 1 188 ? -14.53500 -4.60900  43.07700 1.000 34.04836 ?  168 ARG A NE    1 
ATOM   1266 C CZ    . ARG A 1 188 ? -15.73400 -4.98900  42.66000 1.000 34.28758 ?  168 ARG A CZ    1 
ATOM   1267 N NH1   . ARG A 1 188 ? -16.03300 -6.26900  42.48500 1.000 27.77468 ?  168 ARG A NH1   1 
ATOM   1268 N NH2   . ARG A 1 188 ? -16.65200 -4.06400  42.39800 1.000 26.28494 ?  168 ARG A NH2   1 
ATOM   1269 N N     . ILE A 1 189 ? -8.19100  -6.81300  44.64100 1.000 30.40934 ?  169 ILE A N     1 
ATOM   1270 C CA    . ILE A 1 189 ? -6.99300  -7.64000  44.73700 1.000 33.22511 ?  169 ILE A CA    1 
ATOM   1271 C C     . ILE A 1 189 ? -6.48800  -7.61000  46.17100 1.000 36.33953 ?  169 ILE A C     1 
ATOM   1272 O O     . ILE A 1 189 ? -6.49300  -6.55600  46.81700 1.000 35.71982 ?  169 ILE A O     1 
ATOM   1273 C CB    . ILE A 1 189 ? -5.90200  -7.14500  43.76700 1.000 33.89366 ?  169 ILE A CB    1 
ATOM   1274 C CG1   . ILE A 1 189 ? -6.45400  -7.08400  42.33600 1.000 31.08934 ?  169 ILE A CG1   1 
ATOM   1275 C CG2   . ILE A 1 189 ? -4.64800  -8.00300  43.87600 1.000 32.65075 ?  169 ILE A CG2   1 
ATOM   1276 C CD1   . ILE A 1 189 ? -5.62100  -6.23100  41.37500 1.000 26.51472 ?  169 ILE A CD1   1 
ATOM   1277 N N     . ASN A 1 190 ? -6.05300  -8.76300  46.67000 1.000 35.76326 ?  170 ASN A N     1 
ATOM   1278 C CA    . ASN A 1 190 ? -5.47600  -8.81700  48.00400 1.000 38.33853 ?  170 ASN A CA    1 
ATOM   1279 C C     . ASN A 1 190 ? -4.12900  -8.09900  48.04800 1.000 42.07766 ?  170 ASN A C     1 
ATOM   1280 O O     . ASN A 1 190 ? -3.47200  -7.87800  47.02400 1.000 41.35252 ?  170 ASN A O     1 
ATOM   1281 C CB    . ASN A 1 190 ? -5.29200  -10.26000 48.46300 1.000 35.11176 ?  170 ASN A CB    1 
ATOM   1282 C CG    . ASN A 1 190 ? -6.57700  -11.04100 48.44100 1.000 38.05325 ?  170 ASN A CG    1 
ATOM   1283 O OD1   . ASN A 1 190 ? -7.59400  -10.59000 48.96700 1.000 38.73390 ?  170 ASN A OD1   1 
ATOM   1284 N ND2   . ASN A 1 190 ? -6.53700  -12.23900 47.85800 1.000 38.25052 ?  170 ASN A ND2   1 
ATOM   1285 N N     . GLU A 1 191 ? -3.72900  -7.72000  49.26400 1.000 49.18137 ?  171 GLU A N     1 
ATOM   1286 C CA    . GLU A 1 191 ? -2.40700  -7.14700  49.48000 1.000 45.81501 ?  171 GLU A CA    1 
ATOM   1287 C C     . GLU A 1 191 ? -1.34200  -8.09600  48.95000 1.000 39.65953 ?  171 GLU A C     1 
ATOM   1288 O O     . GLU A 1 191 ? -1.45300  -9.31800  49.08500 1.000 44.83026 ?  171 GLU A O     1 
ATOM   1289 C CB    . GLU A 1 191 ? -2.18800  -6.87800  50.97000 1.000 48.53747 ?  171 GLU A CB    1 
ATOM   1290 N N     . LYS A 1 192 ? -0.32200  -7.52900  48.31100 1.000 44.01571 ?  172 LYS A N     1 
ATOM   1291 C CA    . LYS A 1 192 ? 0.74100   -8.26100  47.62100 1.000 47.74912 ?  172 LYS A CA    1 
ATOM   1292 C C     . LYS A 1 192 ? 0.22600   -9.08200  46.44400 1.000 42.96064 ?  172 LYS A C     1 
ATOM   1293 O O     . LYS A 1 192 ? 0.98600   -9.86800  45.86900 1.000 42.53105 ?  172 LYS A O     1 
ATOM   1294 C CB    . LYS A 1 192 ? 1.52700   -9.17400  48.57300 1.000 41.83274 ?  172 LYS A CB    1 
ATOM   1295 N N     . GLY A 1 193 ? -1.04000  -8.92100  46.06200 1.000 40.96199 ?  173 GLY A N     1 
ATOM   1296 C CA    . GLY A 1 193 ? -1.55800  -9.55500  44.87100 1.000 35.56485 ?  173 GLY A CA    1 
ATOM   1297 C C     . GLY A 1 193 ? -1.10700  -8.85300  43.60400 1.000 35.91292 ?  173 GLY A C     1 
ATOM   1298 O O     . GLY A 1 193 ? -0.35800  -7.87100  43.62000 1.000 33.56647 ?  173 GLY A O     1 
ATOM   1299 N N     . TYR A 1 194 ? -1.59600  -9.37200  42.47700 1.000 33.77019 ?  174 TYR A N     1 
ATOM   1300 C CA    . TYR A 1 194 ? -1.12800  -8.96800  41.15900 1.000 30.52556 ?  174 TYR A CA    1 
ATOM   1301 C C     . TYR A 1 194 ? -2.28700  -8.66100  40.21600 1.000 30.16728 ?  174 TYR A C     1 
ATOM   1302 O O     . TYR A 1 194 ? -3.31200  -9.35400  40.20900 1.000 27.93715 ?  174 TYR A O     1 
ATOM   1303 C CB    . TYR A 1 194 ? -0.25000  -10.06100 40.53400 1.000 32.42272 ?  174 TYR A CB    1 
ATOM   1304 C CG    . TYR A 1 194 ? 1.15200   -10.15000 41.11000 1.000 36.58449 ?  174 TYR A CG    1 
ATOM   1305 C CD1   . TYR A 1 194 ? 1.42400   -10.94900 42.21300 1.000 38.39074 ?  174 TYR A CD1   1 
ATOM   1306 C CD2   . TYR A 1 194 ? 2.20500   -9.44100  40.54400 1.000 35.49732 ?  174 TYR A CD2   1 
ATOM   1307 C CE1   . TYR A 1 194 ? 2.71100   -11.03800 42.73600 1.000 37.05573 ?  174 TYR A CE1   1 
ATOM   1308 C CE2   . TYR A 1 194 ? 3.49400   -9.52200  41.06400 1.000 37.10467 ?  174 TYR A CE2   1 
ATOM   1309 C CZ    . TYR A 1 194 ? 3.73600   -10.32500 42.15600 1.000 38.81442 ?  174 TYR A CZ    1 
ATOM   1310 O OH    . TYR A 1 194 ? 5.00900   -10.40800 42.66900 1.000 41.99721 ?  174 TYR A OH    1 
ATOM   1311 N N     . LEU A 1 195 ? -2.10300  -7.62500  39.40800 1.000 25.62924 ?  175 LEU A N     1 
ATOM   1312 C CA    . LEU A 1 195 ? -2.91800  -7.37100  38.23200 1.000 24.84913 ?  175 LEU A CA    1 
ATOM   1313 C C     . LEU A 1 195 ? -2.01400  -7.56500  37.02600 1.000 29.82835 ?  175 LEU A C     1 
ATOM   1314 O O     . LEU A 1 195 ? -0.96400  -6.91800  36.92800 1.000 25.79490 ?  175 LEU A O     1 
ATOM   1315 C CB    . LEU A 1 195 ? -3.50400  -5.95400  38.25400 1.000 27.32909 ?  175 LEU A CB    1 
ATOM   1316 C CG    . LEU A 1 195 ? -4.09300  -5.40600  36.94300 1.000 27.89201 ?  175 LEU A CG    1 
ATOM   1317 C CD1   . LEU A 1 195 ? -5.51500  -5.95500  36.73100 1.000 25.71494 ?  175 LEU A CD1   1 
ATOM   1318 C CD2   . LEU A 1 195 ? -4.09900  -3.85800  36.89200 1.000 24.53573 ?  175 LEU A CD2   1 
ATOM   1319 N N     . ILE A 1 196 ? -2.40300  -8.46200  36.12200 1.000 28.02045 ?  176 ILE A N     1 
ATOM   1320 C CA    . ILE A 1 196 ? -1.63000  -8.73200  34.91500 1.000 25.74913 ?  176 ILE A CA    1 
ATOM   1321 C C     . ILE A 1 196 ? -2.48500  -8.37200  33.71200 1.000 27.47887 ?  176 ILE A C     1 
ATOM   1322 O O     . ILE A 1 196 ? -3.57700  -8.93100  33.52100 1.000 24.84370 ?  176 ILE A O     1 
ATOM   1323 C CB    . ILE A 1 196 ? -1.15800  -10.19100 34.84000 1.000 25.26820 ?  176 ILE A CB    1 
ATOM   1324 C CG1   . ILE A 1 196 ? -0.37100  -10.53500 36.10600 1.000 25.83282 ?  176 ILE A CG1   1 
ATOM   1325 C CG2   . ILE A 1 196 ? -0.33500  -10.41300 33.57400 1.000 22.54582 ?  176 ILE A CG2   1 
ATOM   1326 C CD1   . ILE A 1 196 ? 0.51200   -11.74300 35.99500 1.000 27.83258 ?  176 ILE A CD1   1 
ATOM   1327 N N     . LEU A 1 197 ? -1.98600  -7.43900  32.90800 1.000 22.27808 ?  177 LEU A N     1 
ATOM   1328 C CA    . LEU A 1 197 ? -2.66200  -6.97600  31.71300 1.000 25.21930 ?  177 LEU A CA    1 
ATOM   1329 C C     . LEU A 1 197 ? -1.85300  -7.39500  30.49900 1.000 24.94419 ?  177 LEU A C     1 
ATOM   1330 O O     . LEU A 1 197 ? -0.63000  -7.53900  30.56600 1.000 26.52475 ?  177 LEU A O     1 
ATOM   1331 C CB    . LEU A 1 197 ? -2.80300  -5.44700  31.70000 1.000 24.13620 ?  177 LEU A CB    1 
ATOM   1332 C CG    . LEU A 1 197 ? -3.44600  -4.72400  32.88700 1.000 25.78092 ?  177 LEU A CG    1 
ATOM   1333 C CD1   . LEU A 1 197 ? -3.44100  -3.22400  32.63900 1.000 22.50816 ?  177 LEU A CD1   1 
ATOM   1334 C CD2   . LEU A 1 197 ? -4.85500  -5.22400  33.15300 1.000 27.32448 ?  177 LEU A CD2   1 
ATOM   1335 N N     . THR A 1 198 ? -2.53900  -7.57400  29.38500 1.000 18.33175 ?  178 THR A N     1 
ATOM   1336 C CA    . THR A 1 198 ? -1.88600  -7.54400  28.09300 1.000 21.76376 ?  178 THR A CA    1 
ATOM   1337 C C     . THR A 1 198 ? -2.73900  -6.71800  27.15200 1.000 23.00905 ?  178 THR A C     1 
ATOM   1338 O O     . THR A 1 198 ? -3.96800  -6.66000  27.28300 1.000 23.55877 ?  178 THR A O     1 
ATOM   1339 C CB    . THR A 1 198 ? -1.66600  -8.95100  27.47100 1.000 23.24350 ?  178 THR A CB    1 
ATOM   1340 O OG1   . THR A 1 198 ? -2.88200  -9.38700  26.84300 1.000 27.54058 ?  178 THR A OG1   1 
ATOM   1341 C CG2   . THR A 1 198 ? -1.23200  -9.96000  28.50800 1.000 22.20212 ?  178 THR A CG2   1 
ATOM   1342 N N     . SER A 1 199 ? -2.08400  -6.11100  26.18400 1.000 24.46935 ?  179 SER A N     1 
ATOM   1343 C CA    . SER A 1 199 ? -2.82600  -5.41500  25.15400 1.000 23.95772 ?  179 SER A CA    1 
ATOM   1344 C C     . SER A 1 199 ? -1.91000  -5.10900  23.97900 1.000 25.66125 ?  179 SER A C     1 
ATOM   1345 O O     . SER A 1 199 ? -0.73600  -4.76900  24.17800 1.000 25.78625 ?  179 SER A O     1 
ATOM   1346 C CB    . SER A 1 199 ? -3.43600  -4.12100  25.71500 1.000 22.30673 ?  179 SER A CB    1 
ATOM   1347 O OG    . SER A 1 199 ? -4.05400  -3.37300  24.68700 1.000 22.65497 ?  179 SER A OG    1 
ATOM   1348 N N     . PRO A 1 200 ? -2.40800  -5.21700  22.74400 1.000 23.47784 ?  180 PRO A N     1 
ATOM   1349 C CA    . PRO A 1 200 ? -1.69900  -4.64800  21.59900 1.000 23.38426 ?  180 PRO A CA    1 
ATOM   1350 C C     . PRO A 1 200 ? -1.94400  -3.15700  21.40900 1.000 27.26378 ?  180 PRO A C     1 
ATOM   1351 O O     . PRO A 1 200 ? -1.42600  -2.58200  20.44200 1.000 22.88998 ?  180 PRO A O     1 
ATOM   1352 C CB    . PRO A 1 200 ? -2.29000  -5.43700  20.43500 1.000 24.40989 ?  180 PRO A CB    1 
ATOM   1353 C CG    . PRO A 1 200 ? -3.71200  -5.57900  20.83000 1.000 23.64168 ?  180 PRO A CG    1 
ATOM   1354 C CD    . PRO A 1 200 ? -3.66800  -5.85000  22.32500 1.000 24.07053 ?  180 PRO A CD    1 
ATOM   1355 N N     . TYR A 1 201 ? -2.75900  -2.52900  22.26400 1.000 22.86481 ?  181 TYR A N     1 
ATOM   1356 C CA    . TYR A 1 201 ? -2.95300  -1.07600  22.23400 1.000 27.82563 ?  181 TYR A CA    1 
ATOM   1357 C C     . TYR A 1 201 ? -3.59700  -0.61400  20.92700 1.000 27.28428 ?  181 TYR A C     1 
ATOM   1358 O O     . TYR A 1 201 ? -3.26500  0.44300   20.38800 1.000 28.18177 ?  181 TYR A O     1 
ATOM   1359 C CB    . TYR A 1 201 ? -1.63300  -0.34000  22.46700 1.000 23.44219 ?  181 TYR A CB    1 
ATOM   1360 C CG    . TYR A 1 201 ? -0.87600  -0.78200  23.69600 1.000 24.17359 ?  181 TYR A CG    1 
ATOM   1361 C CD1   . TYR A 1 201 ? -1.53500  -1.04800  24.88600 1.000 20.39318 ?  181 TYR A CD1   1 
ATOM   1362 C CD2   . TYR A 1 201 ? 0.50800   -0.92900  23.66400 1.000 25.84886 ?  181 TYR A CD2   1 
ATOM   1363 C CE1   . TYR A 1 201 ? -0.83500  -1.43900  26.02500 1.000 21.26070 ?  181 TYR A CE1   1 
ATOM   1364 C CE2   . TYR A 1 201 ? 1.21900   -1.32300  24.79800 1.000 23.50118 ?  181 TYR A CE2   1 
ATOM   1365 C CZ    . TYR A 1 201 ? 0.53800   -1.57000  25.97300 1.000 24.72243 ?  181 TYR A CZ    1 
ATOM   1366 O OH    . TYR A 1 201 ? 1.23200   -1.95800  27.09600 1.000 26.15916 ?  181 TYR A OH    1 
ATOM   1367 N N     . THR A 1 202 ? -4.52800  -1.41400  20.41400 1.000 29.69906 ?  182 THR A N     1 
ATOM   1368 C CA    . THR A 1 202 ? -5.24900  -1.08700  19.18600 1.000 28.51248 ?  182 THR A CA    1 
ATOM   1369 C C     . THR A 1 202 ? -6.51700  -0.30400  19.53900 1.000 30.09929 ?  182 THR A C     1 
ATOM   1370 O O     . THR A 1 202 ? -7.64300  -0.79400  19.44900 1.000 30.60933 ?  182 THR A O     1 
ATOM   1371 C CB    . THR A 1 202 ? -5.56600  -2.36500  18.41400 1.000 34.64240 ?  182 THR A CB    1 
ATOM   1372 O OG1   . THR A 1 202 ? -6.49300  -3.16300  19.16500 1.000 40.19189 ?  182 THR A OG1   1 
ATOM   1373 C CG2   . THR A 1 202 ? -4.31000  -3.19300  18.24300 1.000 29.67329 ?  182 THR A CG2   1 
ATOM   1374 N N     . TRP A 1 203 ? -6.31300  0.94000   19.97500 1.000 29.21644 ?  183 TRP A N     1 
ATOM   1375 C CA    . TRP A 1 203 ? -7.43900  1.80000   20.31800 1.000 31.73895 ?  183 TRP A CA    1 
ATOM   1376 C C     . TRP A 1 203 ? -8.21500  2.15200   19.05600 1.000 32.58856 ?  183 TRP A C     1 
ATOM   1377 O O     . TRP A 1 203 ? -7.62600  2.51800   18.03700 1.000 33.68832 ?  183 TRP A O     1 
ATOM   1378 C CB    . TRP A 1 203 ? -6.95500  3.06700   21.02500 1.000 26.68265 ?  183 TRP A CB    1 
ATOM   1379 C CG    . TRP A 1 203 ? -6.24700  2.77500   22.29900 1.000 27.03030 ?  183 TRP A CG    1 
ATOM   1380 C CD1   . TRP A 1 203 ? -4.90000  2.78000   22.50200 1.000 23.49024 ?  183 TRP A CD1   1 
ATOM   1381 C CD2   . TRP A 1 203 ? -6.84200  2.38400   23.54600 1.000 26.62368 ?  183 TRP A CD2   1 
ATOM   1382 N NE1   . TRP A 1 203 ? -4.61600  2.42900   23.79800 1.000 25.32125 ?  183 TRP A NE1   1 
ATOM   1383 C CE2   . TRP A 1 203 ? -5.79200  2.18200   24.46200 1.000 27.98492 ?  183 TRP A CE2   1 
ATOM   1384 C CE3   . TRP A 1 203 ? -8.16000  2.20000   23.97900 1.000 25.88466 ?  183 TRP A CE3   1 
ATOM   1385 C CZ2   . TRP A 1 203 ? -6.01900  1.79300   25.78700 1.000 25.30609 ?  183 TRP A CZ2   1 
ATOM   1386 C CZ3   . TRP A 1 203 ? -8.38300  1.81800   25.29600 1.000 24.78826 ?  183 TRP A CZ3   1 
ATOM   1387 C CH2   . TRP A 1 203 ? -7.31800  1.62100   26.18200 1.000 25.74949 ?  183 TRP A CH2   1 
ATOM   1388 N N     . ARG A 1 204 ? -9.53600  2.00400   19.11500 1.000 33.99733 ?  184 ARG A N     1 
ATOM   1389 C CA    . ARG A 1 204 ? -10.40700 2.33900   17.99600 1.000 36.31648 ?  184 ARG A CA    1 
ATOM   1390 C C     . ARG A 1 204 ? -11.69600 2.93600   18.54200 1.000 35.95273 ?  184 ARG A C     1 
ATOM   1391 O O     . ARG A 1 204 ? -12.19000 2.51600   19.59500 1.000 31.50836 ?  184 ARG A O     1 
ATOM   1392 C CB    . ARG A 1 204 ? -10.72700 1.11400   17.13200 1.000 38.71152 ?  184 ARG A CB    1 
ATOM   1393 C CG    . ARG A 1 204 ? -9.54400  0.56500   16.34500 1.000 39.92470 ?  184 ARG A CG    1 
ATOM   1394 C CD    . ARG A 1 204 ? -9.87200  -0.78400  15.72300 1.000 44.40421 ?  184 ARG A CD    1 
ATOM   1395 N NE    . ARG A 1 204 ? -10.54900 -0.64700  14.43800 1.000 45.33270 ?  184 ARG A NE    1 
ATOM   1396 N N     . GLU A 1 205 ? -12.24900 3.89800   17.80400 1.000 33.91636 ?  185 GLU A N     1 
ATOM   1397 C CA    . GLU A 1 205 ? -13.43800 4.58800   18.28200 1.000 35.04517 ?  185 GLU A CA    1 
ATOM   1398 C C     . GLU A 1 205 ? -14.66400 3.68700   18.29700 1.000 32.45300 ?  185 GLU A C     1 
ATOM   1399 O O     . GLU A 1 205 ? -15.59400 3.95200   19.06200 1.000 36.45944 ?  185 GLU A O     1 
ATOM   1400 C CB    . GLU A 1 205 ? -13.69300 5.84700   17.44400 1.000 37.16123 ?  185 GLU A CB    1 
ATOM   1401 C CG    . GLU A 1 205 ? -12.94300 7.06600   17.98200 1.000 40.50701 ?  185 GLU A CG    1 
ATOM   1402 C CD    . GLU A 1 205 ? -12.80600 8.19000   16.97000 1.000 51.72498 ?  185 GLU A CD    1 
ATOM   1403 O OE1   . GLU A 1 205 ? -13.55600 8.19000   15.96900 1.000 59.58519 ?  185 GLU A OE1   1 
ATOM   1404 O OE2   . GLU A 1 205 ? -11.95000 9.07700   17.17100 1.000 54.65513 -1 185 GLU A OE2   1 
ATOM   1405 N N     . GLU A 1 206 ? -14.68000 2.61300   17.50600 1.000 35.28568 ?  186 GLU A N     1 
ATOM   1406 C CA    . GLU A 1 206 ? -15.79700 1.67500   17.58500 1.000 34.52487 ?  186 GLU A CA    1 
ATOM   1407 C C     . GLU A 1 206 ? -15.89300 1.00800   18.95100 1.000 33.48885 ?  186 GLU A C     1 
ATOM   1408 O O     . GLU A 1 206 ? -16.97200 0.53600   19.32300 1.000 32.81408 ?  186 GLU A O     1 
ATOM   1409 C CB    . GLU A 1 206 ? -15.68400 0.60300   16.49900 1.000 39.25080 ?  186 GLU A CB    1 
ATOM   1410 C CG    . GLU A 1 206 ? -14.43000 -0.24000  16.58400 1.000 43.57268 ?  186 GLU A CG    1 
ATOM   1411 C CD    . GLU A 1 206 ? -14.19900 -1.09200  15.34400 1.000 50.41269 ?  186 GLU A CD    1 
ATOM   1412 O OE1   . GLU A 1 206 ? -14.76200 -2.20600  15.26200 1.000 52.71922 ?  186 GLU A OE1   1 
ATOM   1413 O OE2   . GLU A 1 206 ? -13.45400 -0.63500  14.44500 1.000 61.99966 -1 186 GLU A OE2   1 
ATOM   1414 N N     . TYR A 1 207 ? -14.80200 0.96700   19.71000 1.000 31.47733 ?  187 TYR A N     1 
ATOM   1415 C CA    . TYR A 1 207 ? -14.79800 0.38700   21.04900 1.000 30.27785 ?  187 TYR A CA    1 
ATOM   1416 C C     . TYR A 1 207 ? -14.67400 1.41800   22.15700 1.000 32.15012 ?  187 TYR A C     1 
ATOM   1417 O O     . TYR A 1 207 ? -15.28000 1.25000   23.21400 1.000 29.05169 ?  187 TYR A O     1 
ATOM   1418 C CB    . TYR A 1 207 ? -13.64600 -0.61400  21.19000 1.000 31.43707 ?  187 TYR A CB    1 
ATOM   1419 C CG    . TYR A 1 207 ? -13.73300 -1.80800  20.27300 1.000 31.95000 ?  187 TYR A CG    1 
ATOM   1420 C CD1   . TYR A 1 207 ? -14.66900 -2.80900  20.49400 1.000 35.89487 ?  187 TYR A CD1   1 
ATOM   1421 C CD2   . TYR A 1 207 ? -12.86900 -1.94300  19.19300 1.000 34.78952 ?  187 TYR A CD2   1 
ATOM   1422 C CE1   . TYR A 1 207 ? -14.74500 -3.92200  19.66200 1.000 40.43366 ?  187 TYR A CE1   1 
ATOM   1423 C CE2   . TYR A 1 207 ? -12.93700 -3.05100  18.35000 1.000 38.72112 ?  187 TYR A CE2   1 
ATOM   1424 C CZ    . TYR A 1 207 ? -13.88100 -4.03600  18.58900 1.000 42.66293 ?  187 TYR A CZ    1 
ATOM   1425 O OH    . TYR A 1 207 ? -13.96600 -5.14500  17.76700 1.000 48.22733 ?  187 TYR A OH    1 
ATOM   1426 N N     . THR A 1 208 ? -13.83600 2.41700   21.94000 1.000 29.25604 ?  188 THR A N     1 
ATOM   1427 C CA    . THR A 1 208 ? -13.56000 3.41300   22.99300 1.000 28.10419 ?  188 THR A CA    1 
ATOM   1428 C C     . THR A 1 208 ? -13.50500 4.80500   22.36900 1.000 30.12289 ?  188 THR A C     1 
ATOM   1429 O O     . THR A 1 208 ? -12.75500 4.99100   21.42000 1.000 30.03041 ?  188 THR A O     1 
ATOM   1430 C CB    . THR A 1 208 ? -12.23100 3.09500   23.69300 1.000 28.15743 ?  188 THR A CB    1 
ATOM   1431 O OG1   . THR A 1 208 ? -12.12200 1.70100   23.98100 1.000 24.43052 ?  188 THR A OG1   1 
ATOM   1432 C CG2   . THR A 1 208 ? -12.03600 3.91000   24.95300 1.000 26.83172 ?  188 THR A CG2   1 
ATOM   1433 N N     . ALA A 1 209 ? -14.28800 5.73800   22.88800 1.000 27.02817 ?  189 ALA A N     1 
ATOM   1434 C CA    . ALA A 1 209 ? -14.16700 7.12800   22.41200 1.000 31.59708 ?  189 ALA A CA    1 
ATOM   1435 C C     . ALA A 1 209 ? -12.72300 7.59700   22.62100 1.000 31.90352 ?  189 ALA A C     1 
ATOM   1436 O O     . ALA A 1 209 ? -12.15000 7.27500   23.65700 1.000 32.24184 ?  189 ALA A O     1 
ATOM   1437 C CB    . ALA A 1 209 ? -15.15700 8.01200   23.11800 1.000 32.32165 ?  189 ALA A CB    1 
ATOM   1438 N N     . LYS A 1 210 ? -12.18300 8.35500   21.67100 1.000 32.93366 ?  190 LYS A N     1 
ATOM   1439 C CA    . LYS A 1 210 ? -10.76400 8.79700   21.72300 1.000 35.16294 ?  190 LYS A CA    1 
ATOM   1440 C C     . LYS A 1 210 ? -10.41300 9.44900   23.06200 1.000 33.45653 ?  190 LYS A C     1 
ATOM   1441 O O     . LYS A 1 210 ? -9.33200  9.17400   23.56600 1.000 30.39119 ?  190 LYS A O     1 
ATOM   1442 C CB    . LYS A 1 210 ? -10.48500 9.77200   20.57700 1.000 40.79125 ?  190 LYS A CB    1 
ATOM   1443 C CG    . LYS A 1 210 ? -9.02500  10.13100  20.35400 1.000 39.13236 ?  190 LYS A CG    1 
ATOM   1444 C CD    . LYS A 1 210 ? -8.58800  9.82900   18.94500 1.000 45.07047 ?  190 LYS A CD    1 
ATOM   1445 C CE    . LYS A 1 210 ? -7.94600  11.00600  18.24600 1.000 43.27301 ?  190 LYS A CE    1 
ATOM   1446 N NZ    . LYS A 1 210 ? -7.51000  10.64600  16.87700 1.000 45.40513 ?  190 LYS A NZ    1 
ATOM   1447 N N     . LYS A 1 211 ? -11.29900 10.28800  23.59300 1.000 28.94456 ?  191 LYS A N     1 
ATOM   1448 C CA    . LYS A 1 211 ? -11.04500 10.98000  24.88400 1.000 34.06485 ?  191 LYS A CA    1 
ATOM   1449 C C     . LYS A 1 211 ? -10.69700 9.96700   25.98000 1.000 30.10650 ?  191 LYS A C     1 
ATOM   1450 O O     . LYS A 1 211 ? -10.05800 10.37100  26.94500 1.000 28.85469 ?  191 LYS A O     1 
ATOM   1451 C CB    . LYS A 1 211 ? -12.25800 11.81600  25.30300 1.000 34.09933 ?  191 LYS A CB    1 
ATOM   1452 C CG    . LYS A 1 211 ? -13.52500 11.04000  25.62100 1.000 38.46560 ?  191 LYS A CG    1 
ATOM   1453 C CD    . LYS A 1 211 ? -14.72400 11.93700  25.82900 1.000 41.83143 ?  191 LYS A CD    1 
ATOM   1454 C CE    . LYS A 1 211 ? -14.54700 12.89800  26.98300 1.000 42.83810 ?  191 LYS A CE    1 
ATOM   1455 N NZ    . LYS A 1 211 ? -15.70900 13.80400  27.12900 1.000 46.38964 ?  191 LYS A NZ    1 
ATOM   1456 N N     . PHE A 1 212 ? -11.09600 8.71000   25.80900 1.000 27.05779 ?  192 PHE A N     1 
ATOM   1457 C CA    . PHE A 1 212 ? -10.86700 7.67800   26.84900 1.000 30.43164 ?  192 PHE A CA    1 
ATOM   1458 C C     . PHE A 1 212 ? -9.70700  6.73600   26.49000 1.000 32.14810 ?  192 PHE A C     1 
ATOM   1459 O O     . PHE A 1 212 ? -9.40800  5.86400   27.31000 1.000 30.33499 ?  192 PHE A O     1 
ATOM   1460 C CB    . PHE A 1 212 ? -12.16500 6.91800   27.09700 1.000 28.87532 ?  192 PHE A CB    1 
ATOM   1461 C CG    . PHE A 1 212 ? -13.30000 7.78800   27.56700 1.000 33.23915 ?  192 PHE A CG    1 
ATOM   1462 C CD1   . PHE A 1 212 ? -13.11600 8.68800   28.60300 1.000 28.98313 ?  192 PHE A CD1   1 
ATOM   1463 C CD2   . PHE A 1 212 ? -14.54400 7.71800   26.96600 1.000 32.72625 ?  192 PHE A CD2   1 
ATOM   1464 C CE1   . PHE A 1 212 ? -14.15800 9.48900   29.03800 1.000 31.21753 ?  192 PHE A CE1   1 
ATOM   1465 C CE2   . PHE A 1 212 ? -15.58300 8.52300   27.40000 1.000 33.14020 ?  192 PHE A CE2   1 
ATOM   1466 C CZ    . PHE A 1 212 ? -15.38900 9.40500   28.43500 1.000 30.78392 ?  192 PHE A CZ    1 
ATOM   1467 N N     . TRP A 1 213 ? -9.07500  6.89700   25.32600 1.000 26.78906 ?  193 TRP A N     1 
ATOM   1468 C CA    . TRP A 1 213 ? -7.90800  6.06500   25.03700 1.000 27.62530 ?  193 TRP A CA    1 
ATOM   1469 C C     . TRP A 1 213 ? -6.84500  6.29600   26.10800 1.000 28.89076 ?  193 TRP A C     1 
ATOM   1470 O O     . TRP A 1 213 ? -6.55700  7.44000   26.47500 1.000 28.97327 ?  193 TRP A O     1 
ATOM   1471 C CB    . TRP A 1 213 ? -7.32700  6.38700   23.65500 1.000 27.34836 ?  193 TRP A CB    1 
ATOM   1472 C CG    . TRP A 1 213 ? -8.22200  6.09900   22.48100 1.000 31.42292 ?  193 TRP A CG    1 
ATOM   1473 C CD1   . TRP A 1 213 ? -9.50100  5.60900   22.51700 1.000 28.99232 ?  193 TRP A CD1   1 
ATOM   1474 C CD2   . TRP A 1 213 ? -7.90100  6.28000   21.08900 1.000 32.22369 ?  193 TRP A CD2   1 
ATOM   1475 N NE1   . TRP A 1 213 ? -9.99000  5.47900   21.23800 1.000 31.41746 ?  193 TRP A NE1   1 
ATOM   1476 C CE2   . TRP A 1 213 ? -9.02800  5.88000   20.34400 1.000 32.48636 ?  193 TRP A CE2   1 
ATOM   1477 C CE3   . TRP A 1 213 ? -6.76700  6.73100   20.40300 1.000 32.32619 ?  193 TRP A CE3   1 
ATOM   1478 C CZ2   . TRP A 1 213 ? -9.05700  5.92600   18.94500 1.000 31.98774 ?  193 TRP A CZ2   1 
ATOM   1479 C CZ3   . TRP A 1 213 ? -6.79800  6.77800   19.01100 1.000 34.98584 ?  193 TRP A CZ3   1 
ATOM   1480 C CH2   . TRP A 1 213 ? -7.93700  6.37600   18.30000 1.000 33.61147 ?  193 TRP A CH2   1 
ATOM   1481 N N     . ILE A 1 214 ? -6.27500  5.20500   26.62900 1.000 25.57101 ?  194 ILE A N     1 
ATOM   1482 C CA    . ILE A 1 214 ? -5.21800  5.33300   27.62900 1.000 26.26707 ?  194 ILE A CA    1 
ATOM   1483 C C     . ILE A 1 214 ? -3.91500  5.81300   26.98800 1.000 26.39867 ?  194 ILE A C     1 
ATOM   1484 O O     . ILE A 1 214 ? -3.08300  6.45000   27.64500 1.000 27.47774 ?  194 ILE A O     1 
ATOM   1485 C CB    . ILE A 1 214 ? -5.03900  3.99200   28.37400 1.000 25.99484 ?  194 ILE A CB    1 
ATOM   1486 C CG1   . ILE A 1 214 ? -6.33800  3.59000   29.07500 1.000 25.52835 ?  194 ILE A CG1   1 
ATOM   1487 C CG2   . ILE A 1 214 ? -3.90400  4.06000   29.37700 1.000 23.90985 ?  194 ILE A CG2   1 
ATOM   1488 C CD1   . ILE A 1 214 ? -6.85100  4.61300   30.05400 1.000 30.90249 ?  194 ILE A CD1   1 
ATOM   1489 N N     . GLY A 1 215 ? -3.71300  5.51500   25.71400 1.000 25.72220 ?  195 GLY A N     1 
ATOM   1490 C CA    . GLY A 1 215 ? -2.52200  5.92700   25.01000 1.000 27.93156 ?  195 GLY A CA    1 
ATOM   1491 C C     . GLY A 1 215 ? -2.78500  5.96300   23.52200 1.000 27.60460 ?  195 GLY A C     1 
ATOM   1492 O O     . GLY A 1 215 ? -3.92800  5.85900   23.07300 1.000 25.96581 ?  195 GLY A O     1 
ATOM   1493 N N     . GLY A 1 216 ? -1.70600  6.10200   22.76100 1.000 27.12859 ?  196 GLY A N     1 
ATOM   1494 C CA    . GLY A 1 216 ? -1.83400  6.23100   21.32100 1.000 25.95449 ?  196 GLY A CA    1 
ATOM   1495 C C     . GLY A 1 216 ? -2.49700  7.51500   20.87000 1.000 30.25613 ?  196 GLY A C     1 
ATOM   1496 O O     . GLY A 1 216 ? -3.27000  7.50200   19.90300 1.000 31.38329 ?  196 GLY A O     1 
ATOM   1497 N N     . TYR A 1 217 ? -2.21100  8.63300   21.53800 1.000 26.14780 ?  197 TYR A N     1 
ATOM   1498 C CA    . TYR A 1 217 ? -2.76500  9.91200   21.12100 1.000 30.00012 ?  197 TYR A CA    1 
ATOM   1499 C C     . TYR A 1 217 ? -1.76700  11.02700  21.41400 1.000 29.75540 ?  197 TYR A C     1 
ATOM   1500 O O     . TYR A 1 217 ? -0.86300  10.89100  22.24400 1.000 28.30110 ?  197 TYR A O     1 
ATOM   1501 C CB    . TYR A 1 217 ? -4.11000  10.19700  21.80500 1.000 29.78210 ?  197 TYR A CB    1 
ATOM   1502 C CG    . TYR A 1 217 ? -4.00100  10.33700  23.30500 1.000 30.24498 ?  197 TYR A CG    1 
ATOM   1503 C CD1   . TYR A 1 217 ? -4.09600  9.22300   24.13500 1.000 27.66593 ?  197 TYR A CD1   1 
ATOM   1504 C CD2   . TYR A 1 217 ? -3.79400  11.58400  23.89700 1.000 30.10207 ?  197 TYR A CD2   1 
ATOM   1505 C CE1   . TYR A 1 217 ? -3.98600  9.34800   25.51600 1.000 29.50674 ?  197 TYR A CE1   1 
ATOM   1506 C CE2   . TYR A 1 217 ? -3.67700  11.71100  25.27000 1.000 30.65804 ?  197 TYR A CE2   1 
ATOM   1507 C CZ    . TYR A 1 217 ? -3.77800  10.59100  26.07200 1.000 28.51508 ?  197 TYR A CZ    1 
ATOM   1508 O OH    . TYR A 1 217 ? -3.66700  10.70900  27.43900 1.000 30.79141 ?  197 TYR A OH    1 
ATOM   1509 N N     . VAL A 1 218 ? -1.94400  12.13400  20.70600 1.000 30.99718 ?  198 VAL A N     1 
ATOM   1510 C CA    . VAL A 1 218 ? -1.23100  13.37200  20.99600 1.000 29.27115 ?  198 VAL A CA    1 
ATOM   1511 C C     . VAL A 1 218 ? -2.09300  14.18400  21.95300 1.000 28.38909 ?  198 VAL A C     1 
ATOM   1512 O O     . VAL A 1 218 ? -3.25200  14.48800  21.64800 1.000 28.98694 ?  198 VAL A O     1 
ATOM   1513 C CB    . VAL A 1 218 ? -0.93700  14.15700  19.70900 1.000 28.61230 ?  198 VAL A CB    1 
ATOM   1514 C CG1   . VAL A 1 218 ? -0.10200  15.39400  20.01800 1.000 28.18572 ?  198 VAL A CG1   1 
ATOM   1515 C CG2   . VAL A 1 218 ? -0.24000  13.25900  18.69300 1.000 26.38803 ?  198 VAL A CG2   1 
ATOM   1516 N N     . ASP A 1 219 ? -1.54000  14.52600  23.11200 1.000 27.00584 ?  199 ASP A N     1 
ATOM   1517 C CA    . ASP A 1 219 ? -2.30600  15.25200  24.11200 1.000 30.60087 ?  199 ASP A CA    1 
ATOM   1518 C C     . ASP A 1 219 ? -2.44100  16.73000  23.71700 1.000 33.86498 ?  199 ASP A C     1 
ATOM   1519 O O     . ASP A 1 219 ? -1.98800  17.16300  22.64900 1.000 28.81846 ?  199 ASP A O     1 
ATOM   1520 C CB    . ASP A 1 219 ? -1.68600  15.05100  25.50100 1.000 31.41848 ?  199 ASP A CB    1 
ATOM   1521 C CG    . ASP A 1 219 ? -0.33800  15.75500  25.69000 1.000 36.03506 ?  199 ASP A CG    1 
ATOM   1522 O OD1   . ASP A 1 219 ? -0.02700  16.75400  25.00200 1.000 32.49990 ?  199 ASP A OD1   1 
ATOM   1523 O OD2   . ASP A 1 219 ? 0.42200   15.29400  26.57400 1.000 35.50349 -1 199 ASP A OD2   1 
ATOM   1524 N N     . GLU A 1 220 ? -3.07400  17.51900  24.59400 1.000 31.68880 ?  200 GLU A N     1 
ATOM   1525 C CA    . GLU A 1 220 ? -3.38800  18.90800  24.27400 1.000 35.61041 ?  200 GLU A CA    1 
ATOM   1526 C C     . GLU A 1 220 ? -2.15000  19.79100  24.22400 1.000 35.86897 ?  200 GLU A C     1 
ATOM   1527 O O     . GLU A 1 220 ? -2.25200  20.95300  23.81600 1.000 37.23079 ?  200 GLU A O     1 
ATOM   1528 C CB    . GLU A 1 220 ? -4.38700  19.49100  25.28600 1.000 33.10633 ?  200 GLU A CB    1 
ATOM   1529 C CG    . GLU A 1 220 ? -3.89200  19.55500  26.73400 1.000 37.67364 ?  200 GLU A CG    1 
ATOM   1530 C CD    . GLU A 1 220 ? -5.01800  19.85100  27.72800 1.000 36.88119 ?  200 GLU A CD    1 
ATOM   1531 N N     . ASN A 1 221 ? -0.99200  19.27000  24.62500 1.000 35.43334 ?  201 ASN A N     1 
ATOM   1532 C CA    . ASN A 1 221 ? 0.25700   20.01400  24.59800 1.000 33.96976 ?  201 ASN A CA    1 
ATOM   1533 C C     . ASN A 1 221 ? 1.24600   19.45100  23.58100 1.000 30.45336 ?  201 ASN A C     1 
ATOM   1534 O O     . ASN A 1 221 ? 2.44700   19.71300  23.67600 1.000 31.12755 ?  201 ASN A O     1 
ATOM   1535 C CB    . ASN A 1 221 ? 0.84700   20.03900  26.00300 1.000 35.78176 ?  201 ASN A CB    1 
ATOM   1536 C CG    . ASN A 1 221 ? -0.00600  20.86500  26.96200 1.000 45.27958 ?  201 ASN A CG    1 
ATOM   1537 O OD1   . ASN A 1 221 ? -0.54900  21.91600  26.59100 1.000 41.03302 ?  201 ASN A OD1   1 
ATOM   1538 N ND2   . ASN A 1 221 ? -0.18500  20.35300  28.18400 1.000 43.53178 ?  201 ASN A ND2   1 
ATOM   1539 N N     . GLY A 1 222 ? 0.75600   18.69700  22.59700 1.000 32.68792 ?  202 GLY A N     1 
ATOM   1540 C CA    . GLY A 1 222 ? 1.60300   18.21000  21.52200 1.000 28.66410 ?  202 GLY A CA    1 
ATOM   1541 C C     . GLY A 1 222 ? 2.55100   17.09200  21.88400 1.000 28.20462 ?  202 GLY A C     1 
ATOM   1542 O O     . GLY A 1 222 ? 3.47400   16.81700  21.11400 1.000 27.98378 ?  202 GLY A O     1 
ATOM   1543 N N     . LYS A 1 223 ? 2.36100   16.44000  23.02600 1.000 28.14722 ?  203 LYS A N     1 
ATOM   1544 C CA    . LYS A 1 223 ? 3.18200   15.30800  23.43600 1.000 28.21288 ?  203 LYS A CA    1 
ATOM   1545 C C     . LYS A 1 223 ? 2.50000   14.00200  23.02600 1.000 31.13420 ?  203 LYS A C     1 
ATOM   1546 O O     . LYS A 1 223 ? 1.27000   13.88700  23.07200 1.000 30.56825 ?  203 LYS A O     1 
ATOM   1547 C CB    . LYS A 1 223 ? 3.40800   15.33200  24.95100 1.000 30.26538 ?  203 LYS A CB    1 
ATOM   1548 C CG    . LYS A 1 223 ? 4.44700   16.33500  25.40500 1.000 33.37736 ?  203 LYS A CG    1 
ATOM   1549 C CD    . LYS A 1 223 ? 4.62100   16.32600  26.91600 1.000 33.74067 ?  203 LYS A CD    1 
ATOM   1550 N N     . GLU A 1 224 ? 3.29200   13.02000  22.61100 1.000 29.74952 ?  204 GLU A N     1 
ATOM   1551 C CA    . GLU A 1 224 ? 2.73900   11.72700  22.22400 1.000 33.06975 ?  204 GLU A CA    1 
ATOM   1552 C C     . GLU A 1 224 ? 2.63900   10.85100  23.46700 1.000 33.05374 ?  204 GLU A C     1 
ATOM   1553 O O     . GLU A 1 224 ? 3.63500   10.64900  24.17500 1.000 35.43194 ?  204 GLU A O     1 
ATOM   1554 C CB    . GLU A 1 224 ? 3.59300   11.07500  21.13800 1.000 32.61115 ?  204 GLU A CB    1 
ATOM   1555 C CG    . GLU A 1 224 ? 3.53000   11.84800  19.81800 1.000 32.84984 ?  204 GLU A CG    1 
ATOM   1556 C CD    . GLU A 1 224 ? 4.18400   11.11700  18.66800 1.000 36.13456 ?  204 GLU A CD    1 
ATOM   1557 O OE1   . GLU A 1 224 ? 4.93300   10.15100  18.93200 1.000 42.70628 ?  204 GLU A OE1   1 
ATOM   1558 O OE2   . GLU A 1 224 ? 3.94800   11.50800  17.49800 1.000 40.66121 -1 204 GLU A OE2   1 
ATOM   1559 N N     . VAL A 1 225 ? 1.43300   10.36300  23.75000 1.000 27.29116 ?  205 VAL A N     1 
ATOM   1560 C CA    . VAL A 1 225 ? 1.16900   9.55500   24.93600 1.000 31.90656 ?  205 VAL A CA    1 
ATOM   1561 C C     . VAL A 1 225 ? 1.16400   8.08700   24.52900 1.000 32.89419 ?  205 VAL A C     1 
ATOM   1562 O O     . VAL A 1 225 ? 0.36600   7.66700   23.68200 1.000 30.77444 ?  205 VAL A O     1 
ATOM   1563 C CB    . VAL A 1 225 ? -0.16100  9.94400   25.60000 1.000 30.95151 ?  205 VAL A CB    1 
ATOM   1564 C CG1   . VAL A 1 225 ? -0.36700  9.13700   26.88300 1.000 33.64127 ?  205 VAL A CG1   1 
ATOM   1565 C CG2   . VAL A 1 225 ? -0.19000  11.43500  25.88900 1.000 35.54664 ?  205 VAL A CG2   1 
ATOM   1566 N N     . SER A 1 226 ? 2.06200   7.30900   25.11500 1.000 29.60977 ?  206 SER A N     1 
ATOM   1567 C CA    . SER A 1 226 ? 2.05000   5.87000   24.92300 1.000 27.42776 ?  206 SER A CA    1 
ATOM   1568 C C     . SER A 1 226 ? 1.12200   5.23100   25.94100 1.000 27.55397 ?  206 SER A C     1 
ATOM   1569 O O     . SER A 1 226 ? 0.93300   5.75200   27.04300 1.000 28.97652 ?  206 SER A O     1 
ATOM   1570 C CB    . SER A 1 226 ? 3.46000   5.30100   25.05300 1.000 26.89329 ?  206 SER A CB    1 
ATOM   1571 O OG    . SER A 1 226 ? 3.73300   4.90100   26.37800 1.000 32.74651 ?  206 SER A OG    1 
ATOM   1572 N N     . THR A 1 227 ? 0.52200   4.10100   25.55900 1.000 28.23977 ?  207 THR A N     1 
ATOM   1573 C CA    . THR A 1 227 ? -0.44000  3.47000   26.45700 1.000 28.26239 ?  207 THR A CA    1 
ATOM   1574 C C     . THR A 1 227 ? 0.22600   3.01100   27.74900 1.000 26.26883 ?  207 THR A C     1 
ATOM   1575 O O     . THR A 1 227 ? -0.35900  3.13600   28.83000 1.000 29.45798 ?  207 THR A O     1 
ATOM   1576 C CB    . THR A 1 227 ? -1.14900  2.30200   25.76900 1.000 26.47804 ?  207 THR A CB    1 
ATOM   1577 O OG1   . THR A 1 227 ? -1.73400  2.73800   24.53200 1.000 23.27218 ?  207 THR A OG1   1 
ATOM   1578 C CG2   . THR A 1 227 ? -2.25100  1.75200   26.68200 1.000 25.64520 ?  207 THR A CG2   1 
ATOM   1579 N N     . LEU A 1 228 ? 1.45500   2.49000   27.66700 1.000 26.71046 ?  208 LEU A N     1 
ATOM   1580 C CA    . LEU A 1 228 ? 2.12500   2.04400   28.88800 1.000 26.91813 ?  208 LEU A CA    1 
ATOM   1581 C C     . LEU A 1 228 ? 2.37900   3.21600   29.83200 1.000 26.20753 ?  208 LEU A C     1 
ATOM   1582 O O     . LEU A 1 228 ? 2.21200   3.08700   31.05100 1.000 28.33585 ?  208 LEU A O     1 
ATOM   1583 C CB    . LEU A 1 228 ? 3.43300   1.31900   28.55200 1.000 28.70526 ?  208 LEU A CB    1 
ATOM   1584 C CG    . LEU A 1 228 ? 4.21200   0.72100   29.73100 1.000 32.12962 ?  208 LEU A CG    1 
ATOM   1585 C CD1   . LEU A 1 228 ? 3.40700   -0.38300  30.40200 1.000 27.05817 ?  208 LEU A CD1   1 
ATOM   1586 C CD2   . LEU A 1 228 ? 5.57200   0.18400   29.28600 1.000 32.06181 ?  208 LEU A CD2   1 
ATOM   1587 N N     . GLU A 1 229 ? 2.77100   4.37000   29.28500 1.000 29.05581 ?  209 GLU A N     1 
ATOM   1588 C CA    . GLU A 1 229 ? 2.88700   5.58100   30.09400 1.000 29.84353 ?  209 GLU A CA    1 
ATOM   1589 C C     . GLU A 1 229 ? 1.55500   5.92200   30.75500 1.000 28.65417 ?  209 GLU A C     1 
ATOM   1590 O O     . GLU A 1 229 ? 1.49000   6.15400   31.96800 1.000 29.40185 ?  209 GLU A O     1 
ATOM   1591 C CB    . GLU A 1 229 ? 3.37900   6.74800   29.23200 1.000 27.70301 ?  209 GLU A CB    1 
ATOM   1592 N N     . GLY A 1 230 ? 0.47300   5.94200   29.96900 1.000 27.68998 ?  210 GLY A N     1 
ATOM   1593 C CA    . GLY A 1 230 ? -0.84300  6.18100   30.54000 1.000 26.20816 ?  210 GLY A CA    1 
ATOM   1594 C C     . GLY A 1 230 ? -1.22400  5.15500   31.58900 1.000 30.38750 ?  210 GLY A C     1 
ATOM   1595 O O     . GLY A 1 230 ? -1.91100  5.47700   32.56100 1.000 30.48315 ?  210 GLY A O     1 
ATOM   1596 N N     . LEU A 1 231 ? -0.76100  3.91600   31.42400 1.000 27.49043 ?  211 LEU A N     1 
ATOM   1597 C CA    . LEU A 1 231 ? -1.04300  2.88700   32.42000 1.000 29.89145 ?  211 LEU A CA    1 
ATOM   1598 C C     . LEU A 1 231 ? -0.25200  3.13500   33.69600 1.000 28.41465 ?  211 LEU A C     1 
ATOM   1599 O O     . LEU A 1 231 ? -0.77800  2.96600   34.80300 1.000 30.12998 ?  211 LEU A O     1 
ATOM   1600 C CB    . LEU A 1 231 ? -0.72200  1.50400   31.85100 1.000 20.97706 ?  211 LEU A CB    1 
ATOM   1601 C CG    . LEU A 1 231 ? -1.67300  0.92800   30.78900 1.000 26.68642 ?  211 LEU A CG    1 
ATOM   1602 C CD1   . LEU A 1 231 ? -1.09700  -0.37400  30.22200 1.000 21.91268 ?  211 LEU A CD1   1 
ATOM   1603 C CD2   . LEU A 1 231 ? -3.07900  0.67200   31.34400 1.000 22.59158 ?  211 LEU A CD2   1 
ATOM   1604 N N     . LYS A 1 232 ? 1.02300   3.50200   33.56300 1.000 27.06538 ?  212 LYS A N     1 
ATOM   1605 C CA    . LYS A 1 232 ? 1.80400   3.85300   34.74300 1.000 32.07249 ?  212 LYS A CA    1 
ATOM   1606 C C     . LYS A 1 232 ? 1.12500   4.97000   35.52400 1.000 30.92703 ?  212 LYS A C     1 
ATOM   1607 O O     . LYS A 1 232 ? 0.98500   4.88600   36.75000 1.000 34.06490 ?  212 LYS A O     1 
ATOM   1608 C CB    . LYS A 1 232 ? 3.21800   4.27100   34.33700 1.000 33.99081 ?  212 LYS A CB    1 
ATOM   1609 C CG    . LYS A 1 232 ? 4.13900   3.12400   33.98600 1.000 32.39320 ?  212 LYS A CG    1 
ATOM   1610 C CD    . LYS A 1 232 ? 5.49500   3.63600   33.51700 1.000 33.95341 ?  212 LYS A CD    1 
ATOM   1611 C CE    . LYS A 1 232 ? 6.34900   2.49800   32.99000 1.000 41.98885 ?  212 LYS A CE    1 
ATOM   1612 N NZ    . LYS A 1 232 ? 7.51700   2.97400   32.19600 1.000 46.33935 ?  212 LYS A NZ    1 
ATOM   1613 N N     . GLU A 1 233 ? 0.66300   6.00700   34.82000 1.000 30.71929 ?  213 GLU A N     1 
ATOM   1614 C CA    . GLU A 1 233 ? 0.03500   7.14200   35.48800 1.000 33.01897 ?  213 GLU A CA    1 
ATOM   1615 C C     . GLU A 1 233 ? -1.17600  6.69700   36.30300 1.000 33.65825 ?  213 GLU A C     1 
ATOM   1616 O O     . GLU A 1 233 ? -1.33800  7.11200   37.45500 1.000 34.38390 ?  213 GLU A O     1 
ATOM   1617 C CB    . GLU A 1 233 ? -0.33800  8.20800   34.45200 1.000 27.59000 ?  213 GLU A CB    1 
ATOM   1618 C CG    . GLU A 1 233 ? -1.43300  9.17800   34.87800 1.000 39.27229 ?  213 GLU A CG    1 
ATOM   1619 C CD    . GLU A 1 233 ? -1.63400  10.31400  33.87900 1.000 41.41725 ?  213 GLU A CD    1 
ATOM   1620 N N     . ILE A 1 234 ? -2.00900  5.81200   35.74700 1.000 30.25638 ?  214 ILE A N     1 
ATOM   1621 C CA    . ILE A 1 234 ? -3.17800  5.33600   36.48700 1.000 30.74403 ?  214 ILE A CA    1 
ATOM   1622 C C     . ILE A 1 234 ? -2.77800  4.35600   37.58300 1.000 32.16053 ?  214 ILE A C     1 
ATOM   1623 O O     . ILE A 1 234 ? -3.26300  4.44200   38.71600 1.000 30.57508 ?  214 ILE A O     1 
ATOM   1624 C CB    . ILE A 1 234 ? -4.20400  4.69800   35.53300 1.000 32.21888 ?  214 ILE A CB    1 
ATOM   1625 C CG1   . ILE A 1 234 ? -4.79500  5.73800   34.59000 1.000 31.90371 ?  214 ILE A CG1   1 
ATOM   1626 C CG2   . ILE A 1 234 ? -5.30600  3.98500   36.32600 1.000 29.37737 ?  214 ILE A CG2   1 
ATOM   1627 C CD1   . ILE A 1 234 ? -5.56200  5.13100   33.44700 1.000 33.08428 ?  214 ILE A CD1   1 
ATOM   1628 N N     . LEU A 1 235 ? -1.90600  3.40300   37.27200 1.000 31.32001 ?  215 LEU A N     1 
ATOM   1629 C CA    . LEU A 1 235 ? -1.72500  2.25900   38.15500 1.000 32.57835 ?  215 LEU A CA    1 
ATOM   1630 C C     . LEU A 1 235 ? -0.66200  2.47000   39.22600 1.000 34.83941 ?  215 LEU A C     1 
ATOM   1631 O O     . LEU A 1 235 ? -0.68200  1.76400   40.24300 1.000 32.58727 ?  215 LEU A O     1 
ATOM   1632 C CB    . LEU A 1 235 ? -1.38500  1.00700   37.33100 1.000 31.40792 ?  215 LEU A CB    1 
ATOM   1633 C CG    . LEU A 1 235 ? -2.52600  0.55200   36.41200 1.000 32.44187 ?  215 LEU A CG    1 
ATOM   1634 C CD1   . LEU A 1 235 ? -2.08800  -0.57400  35.46400 1.000 25.07422 ?  215 LEU A CD1   1 
ATOM   1635 C CD2   . LEU A 1 235 ? -3.73200  0.13400   37.24000 1.000 30.92710 ?  215 LEU A CD2   1 
ATOM   1636 N N     . GLU A 1 236 ? 0.25900   3.41500   39.04600 1.000 32.94688 ?  216 GLU A N     1 
ATOM   1637 C CA    . GLU A 1 236 ? 1.31800   3.53200   40.04300 1.000 36.95474 ?  216 GLU A CA    1 
ATOM   1638 C C     . GLU A 1 236 ? 0.84100   4.18500   41.33600 1.000 33.66166 ?  216 GLU A C     1 
ATOM   1639 O O     . GLU A 1 236 ? 1.61400   4.26400   42.29300 1.000 35.88545 ?  216 GLU A O     1 
ATOM   1640 C CB    . GLU A 1 236 ? 2.52500   4.25800   39.43300 1.000 31.30987 ?  216 GLU A CB    1 
ATOM   1641 C CG    . GLU A 1 236 ? 3.26100   3.29900   38.48000 1.000 36.95707 ?  216 GLU A CG    1 
ATOM   1642 C CD    . GLU A 1 236 ? 4.50800   3.86000   37.82900 1.000 39.66135 ?  216 GLU A CD    1 
ATOM   1643 O OE1   . GLU A 1 236 ? 4.69300   5.09900   37.81700 1.000 40.14532 ?  216 GLU A OE1   1 
ATOM   1644 O OE2   . GLU A 1 236 ? 5.30800   3.04000   37.31900 1.000 39.64303 -1 216 GLU A OE2   1 
ATOM   1645 N N     . ILE A 1 237 ? -0.42600  4.59900   41.40200 1.000 33.72080 ?  217 ILE A N     1 
ATOM   1646 C CA    . ILE A 1 237 ? -1.00600  5.03800   42.66500 1.000 33.13993 ?  217 ILE A CA    1 
ATOM   1647 C C     . ILE A 1 237 ? -1.12600  3.87400   43.64200 1.000 36.93356 ?  217 ILE A C     1 
ATOM   1648 O O     . ILE A 1 237 ? -0.92200  4.04000   44.85000 1.000 39.35255 ?  217 ILE A O     1 
ATOM   1649 C CB    . ILE A 1 237 ? -2.37200  5.69900   42.41600 1.000 38.16403 ?  217 ILE A CB    1 
ATOM   1650 C CG1   . ILE A 1 237 ? -2.25200  6.75400   41.31400 1.000 35.83897 ?  217 ILE A CG1   1 
ATOM   1651 C CG2   . ILE A 1 237 ? -2.93000  6.28000   43.70600 1.000 40.05254 ?  217 ILE A CG2   1 
ATOM   1652 C CD1   . ILE A 1 237 ? -1.91900  8.11700   41.82100 1.000 39.63450 ?  217 ILE A CD1   1 
ATOM   1653 N N     . HIS A 1 238 ? -1.48600  2.68400   43.15200 1.000 34.48689 ?  218 HIS A N     1 
ATOM   1654 C CA    . HIS A 1 238 ? -1.66700  1.53100   44.03000 1.000 33.22425 ?  218 HIS A CA    1 
ATOM   1655 C C     . HIS A 1 238 ? -0.84100  0.31800   43.63900 1.000 36.64147 ?  218 HIS A C     1 
ATOM   1656 O O     . HIS A 1 238 ? -0.85300  -0.67800  44.37200 1.000 39.94179 ?  218 HIS A O     1 
ATOM   1657 C CB    . HIS A 1 238 ? -3.14700  1.12700   44.08600 1.000 32.16012 ?  218 HIS A CB    1 
ATOM   1658 C CG    . HIS A 1 238 ? -4.04500  2.20100   44.61100 1.000 38.20542 ?  218 HIS A CG    1 
ATOM   1659 N ND1   . HIS A 1 238 ? -4.09100  2.54600   45.94600 1.000 37.01547 ?  218 HIS A ND1   1 
ATOM   1660 C CD2   . HIS A 1 238 ? -4.92400  3.01600   43.97900 1.000 36.81810 ?  218 HIS A CD2   1 
ATOM   1661 C CE1   . HIS A 1 238 ? -4.96800  3.52000   46.11500 1.000 35.56807 ?  218 HIS A CE1   1 
ATOM   1662 N NE2   . HIS A 1 238 ? -5.48700  3.82500   44.93800 1.000 37.57206 ?  218 HIS A NE2   1 
ATOM   1663 N N     . PHE A 1 239 ? -0.12800  0.36000   42.51700 1.000 36.26540 ?  219 PHE A N     1 
ATOM   1664 C CA    . PHE A 1 239 ? 0.63900   -0.78000  42.04200 1.000 35.76190 ?  219 PHE A CA    1 
ATOM   1665 C C     . PHE A 1 239 ? 2.08100   -0.36700  41.81300 1.000 37.10909 ?  219 PHE A C     1 
ATOM   1666 O O     . PHE A 1 239 ? 2.39000   0.80700   41.59600 1.000 35.80674 ?  219 PHE A O     1 
ATOM   1667 C CB    . PHE A 1 239 ? 0.09500   -1.35100  40.72600 1.000 32.59668 ?  219 PHE A CB    1 
ATOM   1668 C CG    . PHE A 1 239 ? -1.31600  -1.84000  40.80800 1.000 33.14399 ?  219 PHE A CG    1 
ATOM   1669 C CD1   . PHE A 1 239 ? -2.37600  -0.98000  40.54800 1.000 30.72578 ?  219 PHE A CD1   1 
ATOM   1670 C CD2   . PHE A 1 239 ? -1.58400  -3.15700  41.12800 1.000 26.82348 ?  219 PHE A CD2   1 
ATOM   1671 C CE1   . PHE A 1 239 ? -3.68000  -1.43000  40.61000 1.000 31.89818 ?  219 PHE A CE1   1 
ATOM   1672 C CE2   . PHE A 1 239 ? -2.88800  -3.61700  41.19700 1.000 29.68586 ?  219 PHE A CE2   1 
ATOM   1673 C CZ    . PHE A 1 239 ? -3.93700  -2.76000  40.93800 1.000 29.51251 ?  219 PHE A CZ    1 
ATOM   1674 N N     . GLU A 1 240 ? 2.95800   -1.35900  41.84400 1.000 32.48653 ?  220 GLU A N     1 
ATOM   1675 C CA    . GLU A 1 240 ? 4.31200   -1.23100  41.34100 1.000 36.68442 ?  220 GLU A CA    1 
ATOM   1676 C C     . GLU A 1 240 ? 4.41700   -2.06300  40.07100 1.000 33.32183 ?  220 GLU A C     1 
ATOM   1677 O O     . GLU A 1 240 ? 3.90300   -3.18100  40.01700 1.000 35.78175 ?  220 GLU A O     1 
ATOM   1678 C CB    . GLU A 1 240 ? 5.32800   -1.70300  42.38300 1.000 36.95727 ?  220 GLU A CB    1 
ATOM   1679 C CG    . GLU A 1 240 ? 6.77300   -1.61400  41.93000 1.000 48.41863 ?  220 GLU A CG    1 
ATOM   1680 C CD    . GLU A 1 240 ? 7.69100   -2.55500  42.70300 1.000 54.63859 ?  220 GLU A CD    1 
ATOM   1681 O OE1   . GLU A 1 240 ? 7.17700   -3.39900  43.47300 1.000 54.92085 ?  220 GLU A OE1   1 
ATOM   1682 O OE2   . GLU A 1 240 ? 8.92800   -2.43800  42.55100 1.000 60.71274 -1 220 GLU A OE2   1 
ATOM   1683 N N     . LEU A 1 241 ? 5.04900   -1.50900  39.03900 1.000 33.65057 ?  221 LEU A N     1 
ATOM   1684 C CA    . LEU A 1 241 ? 5.23300   -2.23500  37.78700 1.000 32.58176 ?  221 LEU A CA    1 
ATOM   1685 C C     . LEU A 1 241 ? 6.42100   -3.18100  37.91600 1.000 34.68534 ?  221 LEU A C     1 
ATOM   1686 O O     . LEU A 1 241 ? 7.55200   -2.74000  38.14900 1.000 34.08445 ?  221 LEU A O     1 
ATOM   1687 C CB    . LEU A 1 241 ? 5.43900   -1.26700  36.62300 1.000 30.40412 ?  221 LEU A CB    1 
ATOM   1688 C CG    . LEU A 1 241 ? 5.77600   -1.96100  35.29800 1.000 32.13969 ?  221 LEU A CG    1 
ATOM   1689 C CD1   . LEU A 1 241 ? 4.67000   -2.94300  34.86500 1.000 28.88201 ?  221 LEU A CD1   1 
ATOM   1690 C CD2   . LEU A 1 241 ? 6.05400   -0.94800  34.21000 1.000 28.33206 ?  221 LEU A CD2   1 
ATOM   1691 N N     . VAL A 1 242 ? 6.17500   -4.47400  37.74200 1.000 32.73377 ?  222 VAL A N     1 
ATOM   1692 C CA    . VAL A 1 242 ? 7.18900   -5.49000  37.98200 1.000 33.06734 ?  222 VAL A CA    1 
ATOM   1693 C C     . VAL A 1 242 ? 7.88700   -5.91900  36.69900 1.000 35.74027 ?  222 VAL A C     1 
ATOM   1694 O O     . VAL A 1 242 ? 9.09200   -6.17700  36.70800 1.000 33.76045 ?  222 VAL A O     1 
ATOM   1695 C CB    . VAL A 1 242 ? 6.55900   -6.70100  38.70000 1.000 40.15025 ?  222 VAL A CB    1 
ATOM   1696 C CG1   . VAL A 1 242 ? 7.61700   -7.75000  38.98600 1.000 42.69552 ?  222 VAL A CG1   1 
ATOM   1697 C CG2   . VAL A 1 242 ? 5.89100   -6.23600  39.98300 1.000 42.23511 ?  222 VAL A CG2   1 
ATOM   1698 N N     . ALA A 1 243 ? 7.15700   -6.00000  35.58800 1.000 31.46314 ?  223 ALA A N     1 
ATOM   1699 C CA    . ALA A 1 243 ? 7.73800   -6.56300  34.37500 1.000 29.68642 ?  223 ALA A CA    1 
ATOM   1700 C C     . ALA A 1 243 ? 6.85000   -6.23300  33.19100 1.000 31.79037 ?  223 ALA A C     1 
ATOM   1701 O O     . ALA A 1 243 ? 5.64200   -6.02100  33.34300 1.000 30.35216 ?  223 ALA A O     1 
ATOM   1702 C CB    . ALA A 1 243 ? 7.91600   -8.08500  34.47900 1.000 31.13224 ?  223 ALA A CB    1 
ATOM   1703 N N     . THR A 1 244 ? 7.47000   -6.17800  32.01800 1.000 30.34434 ?  224 THR A N     1 
ATOM   1704 C CA    . THR A 1 244 ? 6.76500   -6.16900  30.74900 1.000 30.82136 ?  224 THR A CA    1 
ATOM   1705 C C     . THR A 1 244 ? 7.38800   -7.22600  29.85600 1.000 32.53455 ?  224 THR A C     1 
ATOM   1706 O O     . THR A 1 244 ? 8.57000   -7.55700  29.99000 1.000 31.39732 ?  224 THR A O     1 
ATOM   1707 C CB    . THR A 1 244 ? 6.82500   -4.81700  30.02000 1.000 29.92522 ?  224 THR A CB    1 
ATOM   1708 O OG1   . THR A 1 244 ? 8.19300   -4.41400  29.86400 1.000 28.02174 ?  224 THR A OG1   1 
ATOM   1709 C CG2   . THR A 1 244 ? 6.05600   -3.75000  30.78400 1.000 30.52591 ?  224 THR A CG2   1 
ATOM   1710 N N     . GLU A 1 245 ? 6.58100   -7.75300  28.94400 1.000 29.51469 ?  225 GLU A N     1 
ATOM   1711 C CA    . GLU A 1 245 ? 7.11700   -8.64300  27.93500 1.000 29.29936 ?  225 GLU A CA    1 
ATOM   1712 C C     . GLU A 1 245 ? 6.15600   -8.68400  26.75600 1.000 30.16126 ?  225 GLU A C     1 
ATOM   1713 O O     . GLU A 1 245 ? 4.94800   -8.48700  26.91300 1.000 31.49858 ?  225 GLU A O     1 
ATOM   1714 C CB    . GLU A 1 245 ? 7.39100   -10.03000 28.54300 1.000 30.44752 ?  225 GLU A CB    1 
ATOM   1715 C CG    . GLU A 1 245 ? 6.24000   -10.99700 28.56000 1.000 32.18173 ?  225 GLU A CG    1 
ATOM   1716 C CD    . GLU A 1 245 ? 6.65300   -12.35300 29.14200 1.000 36.04547 ?  225 GLU A CD    1 
ATOM   1717 O OE1   . GLU A 1 245 ? 6.66900   -12.51600 30.38500 1.000 32.63494 ?  225 GLU A OE1   1 
ATOM   1718 O OE2   . GLU A 1 245 ? 6.95600   -13.25900 28.34100 1.000 36.42476 -1 225 GLU A OE2   1 
ATOM   1719 N N     . ASP A 1 246 ? 6.71400   -8.90500  25.56900 1.000 29.91342 ?  226 ASP A N     1 
ATOM   1720 C CA    . ASP A 1 246 ? 5.93000   -9.01300  24.34700 1.000 32.30522 ?  226 ASP A CA    1 
ATOM   1721 C C     . ASP A 1 246 ? 5.51600   -10.46400 24.13400 1.000 31.52955 ?  226 ASP A C     1 
ATOM   1722 O O     . ASP A 1 246 ? 6.33700   -11.37500 24.27800 1.000 33.21929 ?  226 ASP A O     1 
ATOM   1723 C CB    . ASP A 1 246 ? 6.73100   -8.51000  23.15000 1.000 30.68718 ?  226 ASP A CB    1 
ATOM   1724 C CG    . ASP A 1 246 ? 6.80500   -6.98600  23.09000 1.000 38.28273 ?  226 ASP A CG    1 
ATOM   1725 O OD1   . ASP A 1 246 ? 5.86200   -6.29600  23.54500 1.000 32.51985 ?  226 ASP A OD1   1 
ATOM   1726 O OD2   . ASP A 1 246 ? 7.81700   -6.47400  22.57200 1.000 43.85291 -1 226 ASP A OD2   1 
ATOM   1727 N N     . ILE A 1 247 ? 4.24200   -10.67600 23.81600 1.000 29.86575 ?  227 ILE A N     1 
ATOM   1728 C CA    . ILE A 1 247 ? 3.69600   -12.01600 23.60200 1.000 27.53671 ?  227 ILE A CA    1 
ATOM   1729 C C     . ILE A 1 247 ? 2.94200   -12.05500 22.27800 1.000 27.17168 ?  227 ILE A C     1 
ATOM   1730 O O     . ILE A 1 247 ? 1.86600   -11.45600 22.16800 1.000 27.49611 ?  227 ILE A O     1 
ATOM   1731 C CB    . ILE A 1 247 ? 2.76700   -12.43700 24.75000 1.000 26.60798 ?  227 ILE A CB    1 
ATOM   1732 C CG1   . ILE A 1 247 ? 3.49400   -12.38600 26.09200 1.000 26.27798 ?  227 ILE A CG1   1 
ATOM   1733 C CG2   . ILE A 1 247 ? 2.20200   -13.83000 24.48000 1.000 24.05514 ?  227 ILE A CG2   1 
ATOM   1734 C CD1   . ILE A 1 247 ? 2.58800   -12.60100 27.28100 1.000 23.08860 ?  227 ILE A CD1   1 
ATOM   1735 N N     . PRO A 1 248 ? 3.45100   -12.74100 21.26000 1.000 26.15656 ?  228 PRO A N     1 
ATOM   1736 C CA    . PRO A 1 248 ? 2.73800   -12.80100 19.97800 1.000 25.82952 ?  228 PRO A CA    1 
ATOM   1737 C C     . PRO A 1 248 ? 1.50000   -13.68700 20.04800 1.000 27.39172 ?  228 PRO A C     1 
ATOM   1738 O O     . PRO A 1 248 ? 1.37900   -14.58400 20.88700 1.000 28.61014 ?  228 PRO A O     1 
ATOM   1739 C CB    . PRO A 1 248 ? 3.78200   -13.39800 19.02900 1.000 28.70753 ?  228 PRO A CB    1 
ATOM   1740 C CG    . PRO A 1 248 ? 4.61100   -14.27700 19.93000 1.000 30.28318 ?  228 PRO A CG    1 
ATOM   1741 C CD    . PRO A 1 248 ? 4.71900   -13.49200 21.22400 1.000 28.74500 ?  228 PRO A CD    1 
ATOM   1742 N N     . PHE A 1 249 ? 0.56500   -13.42300 19.14000 1.000 23.63250 ?  229 PHE A N     1 
ATOM   1743 C CA    . PHE A 1 249 ? -0.57200  -14.30600 18.96100 1.000 23.54123 ?  229 PHE A CA    1 
ATOM   1744 C C     . PHE A 1 249 ? -1.04300  -14.20400 17.52300 1.000 25.43586 ?  229 PHE A C     1 
ATOM   1745 O O     . PHE A 1 249 ? -0.84100  -13.18600 16.85000 1.000 23.24511 ?  229 PHE A O     1 
ATOM   1746 C CB    . PHE A 1 249 ? -1.71700  -14.01200 19.95000 1.000 24.07829 ?  229 PHE A CB    1 
ATOM   1747 C CG    . PHE A 1 249 ? -2.46000  -12.72300 19.69000 1.000 25.54567 ?  229 PHE A CG    1 
ATOM   1748 C CD1   . PHE A 1 249 ? -3.49700  -12.66300 18.77000 1.000 27.66991 ?  229 PHE A CD1   1 
ATOM   1749 C CD2   . PHE A 1 249 ? -2.14400  -11.57400 20.40300 1.000 25.57374 ?  229 PHE A CD2   1 
ATOM   1750 C CE1   . PHE A 1 249 ? -4.18900  -11.45200 18.54700 1.000 28.68317 ?  229 PHE A CE1   1 
ATOM   1751 C CE2   . PHE A 1 249 ? -2.83800  -10.38200 20.19000 1.000 27.25099 ?  229 PHE A CE2   1 
ATOM   1752 C CZ    . PHE A 1 249 ? -3.85900  -10.32800 19.26400 1.000 26.18455 ?  229 PHE A CZ    1 
ATOM   1753 N N     . VAL A 1 250 ? -1.65800  -15.28600 17.05800 1.000 25.17475 ?  230 VAL A N     1 
ATOM   1754 C CA    . VAL A 1 250 ? -2.23200  -15.37800 15.72600 1.000 24.74662 ?  230 VAL A CA    1 
ATOM   1755 C C     . VAL A 1 250 ? -3.68000  -15.79700 15.88700 1.000 27.95637 ?  230 VAL A C     1 
ATOM   1756 O O     . VAL A 1 250 ? -3.97100  -16.76700 16.59800 1.000 30.75592 ?  230 VAL A O     1 
ATOM   1757 C CB    . VAL A 1 250 ? -1.47800  -16.39300 14.84700 1.000 27.96215 ?  230 VAL A CB    1 
ATOM   1758 C CG1   . VAL A 1 250 ? -2.21900  -16.59300 13.51300 1.000 27.16053 ?  230 VAL A CG1   1 
ATOM   1759 C CG2   . VAL A 1 250 ? -0.02300  -15.94800 14.63300 1.000 26.84367 ?  230 VAL A CG2   1 
ATOM   1760 N N     . ILE A 1 251 ? -4.58600  -15.08300 15.23300 1.000 24.54141 ?  231 ILE A N     1 
ATOM   1761 C CA    . ILE A 1 251 ? -6.00200  -15.41900 15.27500 1.000 26.50003 ?  231 ILE A CA    1 
ATOM   1762 C C     . ILE A 1 251 ? -6.49400  -15.56100 13.84400 1.000 31.52007 ?  231 ILE A C     1 
ATOM   1763 O O     . ILE A 1 251 ? -6.26800  -14.67100 13.01100 1.000 27.99629 ?  231 ILE A O     1 
ATOM   1764 C CB    . ILE A 1 251 ? -6.82800  -14.37900 16.06000 1.000 26.97823 ?  231 ILE A CB    1 
ATOM   1765 C CG1   . ILE A 1 251 ? -8.30300  -14.77600 16.10300 1.000 31.43303 ?  231 ILE A CG1   1 
ATOM   1766 C CG2   . ILE A 1 251 ? -6.65200  -12.97200 15.51300 1.000 25.64606 ?  231 ILE A CG2   1 
ATOM   1767 C CD1   . ILE A 1 251 ? -8.98300  -14.38700 17.41400 1.000 27.81085 ?  231 ILE A CD1   1 
ATOM   1768 N N     . ARG A 1 252 ? -7.13500  -16.69400 13.55400 1.000 26.05831 ?  232 ARG A N     1 
ATOM   1769 C CA    . ARG A 1 252 ? -7.53900  -16.99800 12.18900 1.000 27.91708 ?  232 ARG A CA    1 
ATOM   1770 C C     . ARG A 1 252 ? -8.74800  -16.16800 11.79000 1.000 29.77603 ?  232 ARG A C     1 
ATOM   1771 O O     . ARG A 1 252 ? -9.66500  -15.95500 12.58600 1.000 30.00670 ?  232 ARG A O     1 
ATOM   1772 C CB    . ARG A 1 252 ? -7.86500  -18.48800 12.04400 1.000 31.81886 ?  232 ARG A CB    1 
ATOM   1773 C CG    . ARG A 1 252 ? -8.91900  -18.78400 10.97900 1.000 32.32234 ?  232 ARG A CG    1 
ATOM   1774 C CD    . ARG A 1 252 ? -9.29800  -20.25000 10.94200 1.000 40.35477 ?  232 ARG A CD    1 
ATOM   1775 N NE    . ARG A 1 252 ? -8.10900  -21.07700 11.04900 1.000 39.61567 ?  232 ARG A NE    1 
ATOM   1776 C CZ    . ARG A 1 252 ? -7.80900  -22.05900 10.21400 1.000 47.29276 ?  232 ARG A CZ    1 
ATOM   1777 N NH1   . ARG A 1 252 ? -8.61700  -22.38700 9.21600  1.000 44.90877 ?  232 ARG A NH1   1 
ATOM   1778 N NH2   . ARG A 1 252 ? -6.66900  -22.72600 10.38100 1.000 48.80413 ?  232 ARG A NH2   1 
ATOM   1779 N N     . GLU A 1 253 ? -8.74500  -15.69700 10.54500 1.000 28.03426 ?  233 GLU A N     1 
ATOM   1780 C CA    . GLU A 1 253 ? -9.92000  -15.08700 9.94400  1.000 28.47219 ?  233 GLU A CA    1 
ATOM   1781 C C     . GLU A 1 253 ? -10.50200 -15.96300 8.84500  1.000 35.10819 ?  233 GLU A C     1 
ATOM   1782 O O     . GLU A 1 253 ? -11.71500 -16.19300 8.81300  1.000 35.89800 ?  233 GLU A O     1 
ATOM   1783 C CB    . GLU A 1 253 ? -9.57000  -13.68800 9.41400  1.000 28.80119 ?  233 GLU A CB    1 
ATOM   1784 C CG    . GLU A 1 253 ? -9.05200  -12.78000 10.52600 1.000 30.87012 ?  233 GLU A CG    1 
ATOM   1785 C CD    . GLU A 1 253 ? -8.65900  -11.38000 10.06800 1.000 36.30954 ?  233 GLU A CD    1 
ATOM   1786 O OE1   . GLU A 1 253 ? -8.54500  -11.14300 8.85100  1.000 36.71757 ?  233 GLU A OE1   1 
ATOM   1787 O OE2   . GLU A 1 253 ? -8.44700  -10.51400 10.94400 1.000 36.60363 -1 233 GLU A OE2   1 
ATOM   1788 N N     . THR A 1 254 ? -9.65900  -16.48100 7.95500  1.000 28.17781 ?  234 THR A N     1 
ATOM   1789 C CA    . THR A 1 254 ? -10.01200 -17.54600 7.03100  1.000 27.02257 ?  234 THR A CA    1 
ATOM   1790 C C     . THR A 1 254 ? -8.89200  -18.57900 7.04700  1.000 30.66227 ?  234 THR A C     1 
ATOM   1791 O O     . THR A 1 254 ? -7.91700  -18.45900 7.79900  1.000 28.47277 ?  234 THR A O     1 
ATOM   1792 C CB    . THR A 1 254 ? -10.23900 -17.03000 5.60200  1.000 29.76146 ?  234 THR A CB    1 
ATOM   1793 O OG1   . THR A 1 254 ? -8.97300  -16.77300 4.98500  1.000 29.83122 ?  234 THR A OG1   1 
ATOM   1794 C CG2   . THR A 1 254 ? -11.09400 -15.75300 5.58600  1.000 27.63479 ?  234 THR A CG2   1 
ATOM   1795 N N     . SER A 1 255 ? -9.03500  -19.60600 6.20300  1.000 27.62781 ?  235 SER A N     1 
ATOM   1796 C CA    . SER A 1 255 ? -7.99700  -20.62300 6.09600  1.000 31.76503 ?  235 SER A CA    1 
ATOM   1797 C C     . SER A 1 255 ? -6.69900  -20.05300 5.56000  1.000 30.83429 ?  235 SER A C     1 
ATOM   1798 O O     . SER A 1 255 ? -5.65200  -20.68600 5.71900  1.000 29.41225 ?  235 SER A O     1 
ATOM   1799 C CB    . SER A 1 255 ? -8.45300  -21.76400 5.18600  1.000 32.66065 ?  235 SER A CB    1 
ATOM   1800 O OG    . SER A 1 255 ? -8.85600  -21.24900 3.92700  1.000 35.59146 ?  235 SER A OG    1 
ATOM   1801 N N     . ARG A 1 256 ? -6.74200  -18.88000 4.92200  1.000 27.27433 ?  236 ARG A N     1 
ATOM   1802 C CA    . ARG A 1 256 ? -5.54700  -18.25200 4.38200  1.000 28.49811 ?  236 ARG A CA    1 
ATOM   1803 C C     . ARG A 1 256 ? -5.23000  -16.88800 4.98700  1.000 26.94804 ?  236 ARG A C     1 
ATOM   1804 O O     . ARG A 1 256 ? -4.10200  -16.41400 4.81800  1.000 29.79835 ?  236 ARG A O     1 
ATOM   1805 C CB    . ARG A 1 256 ? -5.66600  -18.10400 2.85600  1.000 29.39899 ?  236 ARG A CB    1 
ATOM   1806 C CG    . ARG A 1 256 ? -5.72600  -19.43600 2.11000  1.000 27.37240 ?  236 ARG A CG    1 
ATOM   1807 C CD    . ARG A 1 256 ? -5.81400  -19.25900 0.58300  1.000 25.57583 ?  236 ARG A CD    1 
ATOM   1808 N NE    . ARG A 1 256 ? -5.52000  -20.50800 -0.11700 1.000 25.27369 ?  236 ARG A NE    1 
ATOM   1809 C CZ    . ARG A 1 256 ? -4.28900  -20.93000 -0.37800 1.000 31.10571 ?  236 ARG A CZ    1 
ATOM   1810 N NH1   . ARG A 1 256 ? -3.22800  -20.20700 -0.05300 1.000 27.44650 ?  236 ARG A NH1   1 
ATOM   1811 N NH2   . ARG A 1 256 ? -4.11700  -22.09900 -0.99300 1.000 28.34150 ?  236 ARG A NH2   1 
ATOM   1812 N N     . LYS A 1 257 ? -6.16800  -16.24700 5.68300  1.000 24.22401 ?  237 LYS A N     1 
ATOM   1813 C CA    . LYS A 1 257 ? -5.97700  -14.89300 6.19200  1.000 25.88577 ?  237 LYS A CA    1 
ATOM   1814 C C     . LYS A 1 257 ? -5.97000  -14.90500 7.71100  1.000 26.19413 ?  237 LYS A C     1 
ATOM   1815 O O     . LYS A 1 257 ? -6.91100  -15.41000 8.33500  1.000 29.36833 ?  237 LYS A O     1 
ATOM   1816 C CB    . LYS A 1 257 ? -7.07300  -13.95100 5.69700  1.000 27.24180 ?  237 LYS A CB    1 
ATOM   1817 C CG    . LYS A 1 257 ? -6.85400  -12.47800 6.09100  1.000 27.45265 ?  237 LYS A CG    1 
ATOM   1818 C CD    . LYS A 1 257 ? -7.53000  -11.53000 5.10100  1.000 35.41305 ?  237 LYS A CD    1 
ATOM   1819 C CE    . LYS A 1 257 ? -8.38800  -10.48700 5.81500  1.000 39.84366 ?  237 LYS A CE    1 
ATOM   1820 N N     . PHE A 1 258 ? -4.92200  -14.33800 8.30500  1.000 23.46544 ?  238 PHE A N     1 
ATOM   1821 C CA    . PHE A 1 258 ? -4.78400  -14.30800 9.75500  1.000 24.27378 ?  238 PHE A CA    1 
ATOM   1822 C C     . PHE A 1 258 ? -4.38400  -12.91800 10.22600 1.000 27.09429 ?  238 PHE A C     1 
ATOM   1823 O O     . PHE A 1 258 ? -3.82800  -12.10900 9.47500  1.000 28.98771 ?  238 PHE A O     1 
ATOM   1824 C CB    . PHE A 1 258 ? -3.74100  -15.32100 10.25300 1.000 26.67189 ?  238 PHE A CB    1 
ATOM   1825 C CG    . PHE A 1 258 ? -4.00100  -16.73700 9.80000  1.000 26.87329 ?  238 PHE A CG    1 
ATOM   1826 C CD1   . PHE A 1 258 ? -3.75400  -17.11500 8.49100  1.000 25.09545 ?  238 PHE A CD1   1 
ATOM   1827 C CD2   . PHE A 1 258 ? -4.47300  -17.68400 10.68900 1.000 29.56094 ?  238 PHE A CD2   1 
ATOM   1828 C CE1   . PHE A 1 258 ? -3.99100  -18.41700 8.06300  1.000 28.11723 ?  238 PHE A CE1   1 
ATOM   1829 C CE2   . PHE A 1 258 ? -4.70700  -18.98800 10.27300 1.000 35.41448 ?  238 PHE A CE2   1 
ATOM   1830 C CZ    . PHE A 1 258 ? -4.46600  -19.35300 8.95400  1.000 30.92679 ?  238 PHE A CZ    1 
ATOM   1831 N N     . GLN A 1 259 ? -4.66200  -12.65600 11.49700 1.000 23.48869 ?  239 GLN A N     1 
ATOM   1832 C CA    . GLN A 1 259 ? -4.08700  -11.52000 12.19600 1.000 27.40552 ?  239 GLN A CA    1 
ATOM   1833 C C     . GLN A 1 259 ? -2.94400  -12.02400 13.06500 1.000 25.62532 ?  239 GLN A C     1 
ATOM   1834 O O     . GLN A 1 259 ? -3.10700  -12.99500 13.81000 1.000 27.93477 ?  239 GLN A O     1 
ATOM   1835 C CB    . GLN A 1 259 ? -5.13500  -10.80000 13.04100 1.000 27.73765 ?  239 GLN A CB    1 
ATOM   1836 C CG    . GLN A 1 259 ? -4.61200  -9.53700  13.70600 1.000 33.41020 ?  239 GLN A CG    1 
ATOM   1837 C CD    . GLN A 1 259 ? -5.49700  -9.06100  14.83800 1.000 36.09735 ?  239 GLN A CD    1 
ATOM   1838 O OE1   . GLN A 1 259 ? -5.07700  -9.01800  15.99000 1.000 34.07909 ?  239 GLN A OE1   1 
ATOM   1839 N NE2   . GLN A 1 259 ? -6.73900  -8.70700  14.51100 1.000 37.71097 ?  239 GLN A NE2   1 
ATOM   1840 N N     . HIS A 1 260 ? -1.78600  -11.38300 12.93900 1.000 26.40286 ?  240 HIS A N     1 
ATOM   1841 C CA    . HIS A 1 260 ? -0.57100  -11.73900 13.66700 1.000 24.85222 ?  240 HIS A CA    1 
ATOM   1842 C C     . HIS A 1 260 ? -0.14000  -10.49400 14.43400 1.000 28.68490 ?  240 HIS A C     1 
ATOM   1843 O O     . HIS A 1 260 ? 0.24000   -9.48500  13.82700 1.000 25.69367 ?  240 HIS A O     1 
ATOM   1844 C CB    . HIS A 1 260 ? 0.50300   -12.22300 12.69500 1.000 26.11323 ?  240 HIS A CB    1 
ATOM   1845 C CG    . HIS A 1 260 ? 1.70700   -12.82400 13.34800 1.000 27.13941 ?  240 HIS A CG    1 
ATOM   1846 N ND1   . HIS A 1 260 ? 2.61500   -13.59800 12.65600 1.000 29.37160 ?  240 HIS A ND1   1 
ATOM   1847 C CD2   . HIS A 1 260 ? 2.16700   -12.75300 14.61900 1.000 31.12951 ?  240 HIS A CD2   1 
ATOM   1848 C CE1   . HIS A 1 260 ? 3.57900   -13.98300 13.47400 1.000 27.88422 ?  240 HIS A CE1   1 
ATOM   1849 N NE2   . HIS A 1 260 ? 3.33200   -13.48300 14.67100 1.000 30.94111 ?  240 HIS A NE2   1 
ATOM   1850 N N     . THR A 1 261 ? -0.20200  -10.56400 15.76400 1.000 25.98119 ?  241 THR A N     1 
ATOM   1851 C CA    . THR A 1 261 ? -0.14500  -9.39100  16.62000 1.000 25.67990 ?  241 THR A CA    1 
ATOM   1852 C C     . THR A 1 261 ? 0.80600   -9.63100  17.78700 1.000 26.66109 ?  241 THR A C     1 
ATOM   1853 O O     . THR A 1 261 ? 0.95700   -10.75800 18.26700 1.000 25.20815 ?  241 THR A O     1 
ATOM   1854 C CB    . THR A 1 261 ? -1.55400  -9.04500  17.13100 1.000 26.21558 ?  241 THR A CB    1 
ATOM   1855 O OG1   . THR A 1 261 ? -2.41100  -8.78900  16.01300 1.000 29.21220 ?  241 THR A OG1   1 
ATOM   1856 C CG2   . THR A 1 261 ? -1.55800  -7.83900  18.06700 1.000 24.13233 ?  241 THR A CG2   1 
ATOM   1857 N N     . ILE A 1 262 ? 1.45000   -8.55900  18.23700 1.000 23.16922 ?  242 ILE A N     1 
ATOM   1858 C CA    . ILE A 1 262 ? 2.36500   -8.60500  19.37200 1.000 24.16301 ?  242 ILE A CA    1 
ATOM   1859 C C     . ILE A 1 262 ? 1.70300   -7.81800  20.49400 1.000 24.46274 ?  242 ILE A C     1 
ATOM   1860 O O     . ILE A 1 262 ? 1.69300   -6.58300  20.47600 1.000 24.57080 ?  242 ILE A O     1 
ATOM   1861 C CB    . ILE A 1 262 ? 3.74700   -8.03600  19.03400 1.000 23.60236 ?  242 ILE A CB    1 
ATOM   1862 C CG1   . ILE A 1 262 ? 4.33700   -8.73500  17.81700 1.000 26.88615 ?  242 ILE A CG1   1 
ATOM   1863 C CG2   . ILE A 1 262 ? 4.69000   -8.23600  20.20400 1.000 26.11463 ?  242 ILE A CG2   1 
ATOM   1864 C CD1   . ILE A 1 262 ? 5.42600   -7.93700  17.15200 1.000 30.43680 ?  242 ILE A CD1   1 
ATOM   1865 N N     . SER A 1 263 ? 1.13500   -8.52900  21.45900 1.000 25.09121 ?  243 SER A N     1 
ATOM   1866 C CA    . SER A 1 263 ? 0.51400   -7.90300  22.61200 1.000 26.55581 ?  243 SER A CA    1 
ATOM   1867 C C     . SER A 1 263 ? 1.56900   -7.68300  23.69300 1.000 26.49027 ?  243 SER A C     1 
ATOM   1868 O O     . SER A 1 263 ? 2.52500   -8.45400  23.82500 1.000 26.44631 ?  243 SER A O     1 
ATOM   1869 C CB    . SER A 1 263 ? -0.63200  -8.77800  23.12600 1.000 27.97898 ?  243 SER A CB    1 
ATOM   1870 O OG    . SER A 1 263 ? -1.32500  -8.17600  24.19900 1.000 29.26116 ?  243 SER A OG    1 
ATOM   1871 N N     . GLN A 1 264 ? 1.41900   -6.60400  24.44900 1.000 26.87719 ?  244 GLN A N     1 
ATOM   1872 C CA    . GLN A 1 264 ? 2.35900   -6.31800  25.52500 1.000 27.21338 ?  244 GLN A CA    1 
ATOM   1873 C C     . GLN A 1 264 ? 1.72400   -6.68300  26.85700 1.000 26.34659 ?  244 GLN A C     1 
ATOM   1874 O O     . GLN A 1 264 ? 0.68700   -6.12100  27.22900 1.000 24.20055 ?  244 GLN A O     1 
ATOM   1875 C CB    . GLN A 1 264 ? 2.79700   -4.85400  25.54500 1.000 27.63513 ?  244 GLN A CB    1 
ATOM   1876 C CG    . GLN A 1 264 ? 3.67100   -4.55200  26.76700 1.000 26.07265 ?  244 GLN A CG    1 
ATOM   1877 C CD    . GLN A 1 264 ? 4.35200   -3.19800  26.69900 1.000 29.42129 ?  244 GLN A CD    1 
ATOM   1878 O OE1   . GLN A 1 264 ? 3.69200   -2.16100  26.76700 1.000 27.79111 ?  244 GLN A OE1   1 
ATOM   1879 N NE2   . GLN A 1 264 ? 5.67700   -3.20100  26.57400 1.000 23.62485 ?  244 GLN A NE2   1 
ATOM   1880 N N     . MET A 1 265 ? 2.36900   -7.59700  27.57600 1.000 24.33406 ?  245 MET A N     1 
ATOM   1881 C CA    . MET A 1 265 ? 1.98200   -7.94700  28.93300 1.000 26.05939 ?  245 MET A CA    1 
ATOM   1882 C C     . MET A 1 265 ? 2.66400   -6.99300  29.90000 1.000 27.19191 ?  245 MET A C     1 
ATOM   1883 O O     . MET A 1 265 ? 3.85400   -6.70400  29.74600 1.000 27.91039 ?  245 MET A O     1 
ATOM   1884 C CB    . MET A 1 265 ? 2.37300   -9.39400  29.25600 1.000 26.16716 ?  245 MET A CB    1 
ATOM   1885 C CG    . MET A 1 265 ? 2.09600   -9.79100  30.70300 1.000 27.51410 ?  245 MET A CG    1 
ATOM   1886 S SD    . MET A 1 265 ? 2.40700   -11.54200 31.05000 1.000 27.36656 ?  245 MET A SD    1 
ATOM   1887 C CE    . MET A 1 265 ? 0.84500   -12.26000 30.56700 1.000 24.23724 ?  245 MET A CE    1 
ATOM   1888 N N     . SER A 1 266 ? 1.90900   -6.48700  30.87700 1.000 24.81886 ?  246 SER A N     1 
ATOM   1889 C CA    . SER A 1 266 ? 2.46700   -5.69800  31.96200 1.000 24.45129 ?  246 SER A CA    1 
ATOM   1890 C C     . SER A 1 266 ? 1.96900   -6.25600  33.28800 1.000 27.00325 ?  246 SER A C     1 
ATOM   1891 O O     . SER A 1 266 ? 0.78000   -6.57400  33.43600 1.000 24.56978 ?  246 SER A O     1 
ATOM   1892 C CB    . SER A 1 266 ? 2.11200   -4.20200  31.83600 1.000 26.30302 ?  246 SER A CB    1 
ATOM   1893 O OG    . SER A 1 266 ? 0.73200   -4.00600  31.60300 1.000 26.64656 ?  246 SER A OG    1 
ATOM   1894 N N     . VAL A 1 267 ? 2.89100   -6.37000  34.24700 1.000 26.80842 ?  247 VAL A N     1 
ATOM   1895 C CA    . VAL A 1 267 ? 2.67300   -7.07500  35.51100 1.000 27.44334 ?  247 VAL A CA    1 
ATOM   1896 C C     . VAL A 1 267 ? 2.74900   -6.06000  36.64500 1.000 31.51655 ?  247 VAL A C     1 
ATOM   1897 O O     . VAL A 1 267 ? 3.78000   -5.39800  36.82700 1.000 31.40530 ?  247 VAL A O     1 
ATOM   1898 C CB    . VAL A 1 267 ? 3.70000   -8.20100  35.71100 1.000 27.37086 ?  247 VAL A CB    1 
ATOM   1899 C CG1   . VAL A 1 267 ? 3.46800   -8.90700  37.02000 1.000 27.25823 ?  247 VAL A CG1   1 
ATOM   1900 C CG2   . VAL A 1 267 ? 3.62800   -9.18900  34.55100 1.000 27.76121 ?  247 VAL A CG2   1 
ATOM   1901 N N     . TRP A 1 268 ? 1.67100   -5.95000  37.41900 1.000 27.48746 ?  248 TRP A N     1 
ATOM   1902 C CA    . TRP A 1 268 ? 1.54200   -4.92300  38.44200 1.000 30.05285 ?  248 TRP A CA    1 
ATOM   1903 C C     . TRP A 1 268 ? 1.28400   -5.57000  39.79500 1.000 32.56052 ?  248 TRP A C     1 
ATOM   1904 O O     . TRP A 1 268 ? 0.34200   -6.35600  39.94200 1.000 30.50882 ?  248 TRP A O     1 
ATOM   1905 C CB    . TRP A 1 268 ? 0.41800   -3.93900  38.08000 1.000 27.01828 ?  248 TRP A CB    1 
ATOM   1906 C CG    . TRP A 1 268 ? 0.46700   -3.45600  36.63000 1.000 29.02909 ?  248 TRP A CG    1 
ATOM   1907 C CD1   . TRP A 1 268 ? 0.00700   -4.12300  35.52400 1.000 27.87554 ?  248 TRP A CD1   1 
ATOM   1908 C CD2   . TRP A 1 268 ? 0.99900   -2.20900  36.15000 1.000 27.95121 ?  248 TRP A CD2   1 
ATOM   1909 N NE1   . TRP A 1 268 ? 0.22300   -3.37000  34.38900 1.000 26.30953 ?  248 TRP A NE1   1 
ATOM   1910 C CE2   . TRP A 1 268 ? 0.83100   -2.19200  34.74700 1.000 26.39361 ?  248 TRP A CE2   1 
ATOM   1911 C CE3   . TRP A 1 268 ? 1.60700   -1.10700  36.77000 1.000 30.00059 ?  248 TRP A CE3   1 
ATOM   1912 C CZ2   . TRP A 1 268 ? 1.24400   -1.11500  33.95700 1.000 27.64016 ?  248 TRP A CZ2   1 
ATOM   1913 C CZ3   . TRP A 1 268 ? 2.01800   -0.03700  35.98300 1.000 31.91187 ?  248 TRP A CZ3   1 
ATOM   1914 C CH2   . TRP A 1 268 ? 1.83200   -0.04800  34.59000 1.000 28.95894 ?  248 TRP A CH2   1 
ATOM   1915 N N     . LYS A 1 269 ? 2.12400   -5.24000  40.77600 1.000 33.51957 ?  249 LYS A N     1 
ATOM   1916 C CA    . LYS A 1 269 ? 1.99100   -5.74800  42.13700 1.000 35.36015 ?  249 LYS A CA    1 
ATOM   1917 C C     . LYS A 1 269 ? 1.34700   -4.68900  43.02300 1.000 33.95829 ?  249 LYS A C     1 
ATOM   1918 O O     . LYS A 1 269 ? 1.80500   -3.54000  43.06300 1.000 35.91922 ?  249 LYS A O     1 
ATOM   1919 C CB    . LYS A 1 269 ? 3.35000   -6.15400  42.71500 1.000 38.66563 ?  249 LYS A CB    1 
ATOM   1920 C CG    . LYS A 1 269 ? 3.25900   -6.77700  44.11400 1.000 38.59586 ?  249 LYS A CG    1 
ATOM   1921 C CD    . LYS A 1 269 ? 4.61400   -7.28800  44.60800 1.000 41.30895 ?  249 LYS A CD    1 
ATOM   1922 C CE    . LYS A 1 269 ? 4.43800   -8.45900  45.59600 1.000 41.72281 ?  249 LYS A CE    1 
ATOM   1923 N N     . VAL A 1 270 ? 0.28800   -5.08200  43.73300 1.000 33.90585 ?  250 VAL A N     1 
ATOM   1924 C CA    . VAL A 1 270 ? -0.38200  -4.17200  44.65500 1.000 40.24911 ?  250 VAL A CA    1 
ATOM   1925 C C     . VAL A 1 270 ? 0.61800   -3.63100  45.66600 1.000 40.41131 ?  250 VAL A C     1 
ATOM   1926 O O     . VAL A 1 270 ? 1.42000   -4.38300  46.23300 1.000 41.93040 ?  250 VAL A O     1 
ATOM   1927 C CB    . VAL A 1 270 ? -1.55000  -4.88800  45.34600 1.000 39.35732 ?  250 VAL A CB    1 
ATOM   1928 C CG1   . VAL A 1 270 ? -2.01500  -4.09400  46.55800 1.000 43.51596 ?  250 VAL A CG1   1 
ATOM   1929 C CG2   . VAL A 1 270 ? -2.68900  -5.05600  44.37200 1.000 36.65057 ?  250 VAL A CG2   1 
ATOM   1930 N N     . ILE A 1 271 ? 0.58400   -2.31800  45.88300 1.000 39.66235 ?  251 ILE A N     1 
ATOM   1931 C CA    . ILE A 1 271 ? 1.52500   -1.65000  46.78200 1.000 46.50191 ?  251 ILE A CA    1 
ATOM   1932 C C     . ILE A 1 271 ? 0.98100   -1.61100  48.20700 1.000 48.25773 ?  251 ILE A C     1 
ATOM   1933 O O     . ILE A 1 271 ? 1.60900   -2.12800  49.13500 1.000 52.84359 ?  251 ILE A O     1 
ATOM   1934 C CB    . ILE A 1 271 ? 1.85200   -0.22600  46.28100 1.000 41.06634 ?  251 ILE A CB    1 
ATOM   1935 N N     . ILE B 1 28  ? -44.82200 -16.71800 46.84600 1.000 53.61253 ?  8   ILE B N     1 
ATOM   1936 C CA    . ILE B 1 28  ? -44.50200 -15.44300 47.55400 1.000 57.84013 ?  8   ILE B CA    1 
ATOM   1937 C C     . ILE B 1 28  ? -43.05100 -15.04400 47.27400 1.000 55.46095 ?  8   ILE B C     1 
ATOM   1938 O O     . ILE B 1 28  ? -42.17000 -15.48100 48.02000 1.000 60.57234 ?  8   ILE B O     1 
ATOM   1939 N N     . TYR B 1 29  ? -42.82600 -14.25100 46.23100 1.000 52.61580 ?  9   TYR B N     1 
ATOM   1940 C CA    . TYR B 1 29  ? -41.45400 -13.77200 45.93300 1.000 55.22595 ?  9   TYR B CA    1 
ATOM   1941 C C     . TYR B 1 29  ? -40.92100 -13.00000 47.13600 1.000 56.16370 ?  9   TYR B C     1 
ATOM   1942 O O     . TYR B 1 29  ? -41.58900 -12.05600 47.57800 1.000 50.60707 ?  9   TYR B O     1 
ATOM   1943 C CB    . TYR B 1 29  ? -41.39600 -12.88900 44.68800 1.000 52.08917 ?  9   TYR B CB    1 
ATOM   1944 C CG    . TYR B 1 29  ? -39.98800 -12.51600 44.30500 1.000 55.85415 ?  9   TYR B CG    1 
ATOM   1945 C CD1   . TYR B 1 29  ? -39.10800 -13.47000 43.82500 1.000 56.30325 ?  9   TYR B CD1   1 
ATOM   1946 C CD2   . TYR B 1 29  ? -39.52400 -11.21900 44.44300 1.000 54.63011 ?  9   TYR B CD2   1 
ATOM   1947 C CE1   . TYR B 1 29  ? -37.80900 -13.14400 43.47400 1.000 57.23492 ?  9   TYR B CE1   1 
ATOM   1948 C CE2   . TYR B 1 29  ? -38.22600 -10.87700 44.09900 1.000 49.48338 ?  9   TYR B CE2   1 
ATOM   1949 C CZ    . TYR B 1 29  ? -37.36600 -11.84200 43.61400 1.000 49.24801 ?  9   TYR B CZ    1 
ATOM   1950 O OH    . TYR B 1 29  ? -36.08200 -11.51600 43.27500 1.000 53.61245 ?  9   TYR B OH    1 
ATOM   1951 N N     . GLU B 1 30  ? -39.73400 -13.37800 47.60800 1.000 57.84801 ?  10  GLU B N     1 
ATOM   1952 C CA    . GLU B 1 30  ? -39.14600 -12.74400 48.81300 1.000 58.01679 ?  10  GLU B CA    1 
ATOM   1953 C C     . GLU B 1 30  ? -37.89900 -11.93300 48.45300 1.000 57.06525 ?  10  GLU B C     1 
ATOM   1954 O O     . GLU B 1 30  ? -36.97000 -12.51600 47.88900 1.000 59.76124 ?  10  GLU B O     1 
ATOM   1955 C CB    . GLU B 1 30  ? -38.79200 -13.83200 49.82300 1.000 57.48517 ?  10  GLU B CB    1 
ATOM   1956 N N     . THR B 1 31  ? -37.88600 -10.64500 48.79700 1.000 55.68452 ?  11  THR B N     1 
ATOM   1957 C CA    . THR B 1 31  ? -36.72200 -9.75800  48.52400 1.000 54.28835 ?  11  THR B CA    1 
ATOM   1958 C C     . THR B 1 31  ? -35.73600 -9.71800  49.70400 1.000 52.77923 ?  11  THR B C     1 
ATOM   1959 O O     . THR B 1 31  ? -36.14800 -10.05500 50.81900 1.000 52.40536 ?  11  THR B O     1 
ATOM   1960 C CB    . THR B 1 31  ? -37.20800 -8.34600  48.18000 1.000 52.56296 ?  11  THR B CB    1 
ATOM   1961 O OG1   . THR B 1 31  ? -37.41300 -7.63400  49.40000 1.000 50.02471 ?  11  THR B OG1   1 
ATOM   1962 C CG2   . THR B 1 31  ? -38.47100 -8.34600  47.34700 1.000 51.35259 ?  11  THR B CG2   1 
ATOM   1963 N N     . ASP B 1 32  ? -34.49100 -9.28600  49.46100 1.000 56.99273 ?  12  ASP B N     1 
ATOM   1964 C CA    . ASP B 1 32  ? -33.43000 -9.21300  50.50800 1.000 52.22589 ?  12  ASP B CA    1 
ATOM   1965 C C     . ASP B 1 32  ? -33.38700 -7.82600  51.16000 1.000 51.22351 ?  12  ASP B C     1 
ATOM   1966 O O     . ASP B 1 32  ? -34.19800 -7.00100  50.77900 1.000 47.41194 ?  12  ASP B O     1 
ATOM   1967 C CB    . ASP B 1 32  ? -32.05600 -9.58700  49.94900 1.000 48.64046 ?  12  ASP B CB    1 
ATOM   1968 C CG    . ASP B 1 32  ? -31.47700 -8.60500  48.94300 1.000 53.95137 ?  12  ASP B CG    1 
ATOM   1969 O OD1   . ASP B 1 32  ? -31.19500 -7.45300  49.32600 1.000 52.91011 ?  12  ASP B OD1   1 
ATOM   1970 O OD2   . ASP B 1 32  ? -31.27600 -9.01300  47.78800 1.000 55.80966 ?  12  ASP B OD2   1 
ATOM   1971 N N     . GLU B 1 33  ? -32.38900 -7.55700  52.00600 1.000 48.04427 ?  13  GLU B N     1 
ATOM   1972 C CA    . GLU B 1 33  ? -32.36100 -6.30300  52.81200 1.000 47.72544 ?  13  GLU B CA    1 
ATOM   1973 C C     . GLU B 1 33  ? -32.24100 -5.03700  51.95400 1.000 43.65990 ?  13  GLU B C     1 
ATOM   1974 O O     . GLU B 1 33  ? -33.01300 -4.10600  52.18400 1.000 41.06394 ?  13  GLU B O     1 
ATOM   1975 C CB    . GLU B 1 33  ? -31.25800 -6.39700  53.86800 1.000 48.61989 ?  13  GLU B CB    1 
ATOM   1976 C CG    . GLU B 1 33  ? -31.51900 -7.47200  54.90400 1.000 48.51030 ?  13  GLU B CG    1 
ATOM   1977 C CD    . GLU B 1 33  ? -30.46700 -7.55900  55.99600 1.000 56.43391 ?  13  GLU B CD    1 
ATOM   1978 O OE1   . GLU B 1 33  ? -30.41700 -6.64300  56.83800 1.000 56.93047 ?  13  GLU B OE1   1 
ATOM   1979 N N     . SER B 1 34  ? -31.28600 -5.00900  51.03400 1.000 46.07414 ?  14  SER B N     1 
ATOM   1980 C CA    . SER B 1 34  ? -31.12100 -3.83300  50.14900 1.000 43.99875 ?  14  SER B CA    1 
ATOM   1981 C C     . SER B 1 34  ? -32.40200 -3.62200  49.33500 1.000 42.47955 ?  14  SER B C     1 
ATOM   1982 O O     . SER B 1 34  ? -32.91100 -2.49600  49.31100 1.000 36.45954 ?  14  SER B O     1 
ATOM   1983 C CB    . SER B 1 34  ? -29.91800 -3.98300  49.27200 1.000 46.77785 ?  14  SER B CB    1 
ATOM   1984 O OG    . SER B 1 34  ? -28.88400 -4.68000  49.94800 1.000 56.28241 ?  14  SER B OG    1 
ATOM   1985 N N     . VAL B 1 35  ? -32.90000 -4.68300  48.71100 1.000 40.41060 ?  15  VAL B N     1 
ATOM   1986 C CA    . VAL B 1 35  ? -34.14100 -4.59000  47.90000 1.000 37.12001 ?  15  VAL B CA    1 
ATOM   1987 C C     . VAL B 1 35  ? -35.31200 -4.26800  48.83300 1.000 35.50683 ?  15  VAL B C     1 
ATOM   1988 O O     . VAL B 1 35  ? -36.14100 -3.44300  48.45700 1.000 36.34832 ?  15  VAL B O     1 
ATOM   1989 C CB    . VAL B 1 35  ? -34.36200 -5.88500  47.10100 1.000 38.29340 ?  15  VAL B CB    1 
ATOM   1990 C CG1   . VAL B 1 35  ? -35.55400 -5.77500  46.17100 1.000 35.33814 ?  15  VAL B CG1   1 
ATOM   1991 C CG2   . VAL B 1 35  ? -33.11900 -6.28100  46.32500 1.000 39.46795 ?  15  VAL B CG2   1 
ATOM   1992 N N     . SER B 1 36  ? -35.34200 -4.88000  50.01500 1.000 34.13295 ?  16  SER B N     1 
ATOM   1993 C CA    . SER B 1 36  ? -36.44600 -4.65300  50.98400 1.000 38.09280 ?  16  SER B CA    1 
ATOM   1994 C C     . SER B 1 36  ? -36.52200 -3.17300  51.35900 1.000 33.30632 ?  16  SER B C     1 
ATOM   1995 O O     . SER B 1 36  ? -37.63200 -2.66100  51.45500 1.000 35.29084 ?  16  SER B O     1 
ATOM   1996 C CB    . SER B 1 36  ? -36.30100 -5.51800  52.21000 1.000 39.48309 ?  16  SER B CB    1 
ATOM   1997 O OG    . SER B 1 36  ? -36.63000 -6.86700  51.92500 1.000 41.09940 ?  16  SER B OG    1 
ATOM   1998 N N     . GLN B 1 37  ? -35.37000 -2.53500  51.53900 1.000 32.86710 ?  17  GLN B N     1 
ATOM   1999 C CA    . GLN B 1 37  ? -35.33300 -1.10400  51.92400 1.000 32.65383 ?  17  GLN B CA    1 
ATOM   2000 C C     . GLN B 1 37  ? -36.00500 -0.27800  50.82800 1.000 29.38573 ?  17  GLN B C     1 
ATOM   2001 O O     . GLN B 1 37  ? -36.78500 0.60700   51.16300 1.000 31.39268 ?  17  GLN B O     1 
ATOM   2002 C CB    . GLN B 1 37  ? -33.90000 -0.62500  52.15600 1.000 30.26220 ?  17  GLN B CB    1 
ATOM   2003 C CG    . GLN B 1 37  ? -33.82500 0.79900   52.68200 1.000 33.78838 ?  17  GLN B CG    1 
ATOM   2004 C CD    . GLN B 1 37  ? -32.42100 1.22100   53.03100 1.000 34.49401 ?  17  GLN B CD    1 
ATOM   2005 O OE1   . GLN B 1 37  ? -31.50100 1.10400   52.22800 1.000 34.32146 ?  17  GLN B OE1   1 
ATOM   2006 N NE2   . GLN B 1 37  ? -32.25000 1.72900   54.23900 1.000 34.02961 ?  17  GLN B NE2   1 
ATOM   2007 N N     . TYR B 1 38  ? -35.69300 -0.58900  49.57700 1.000 26.54423 ?  18  TYR B N     1 
ATOM   2008 C CA    . TYR B 1 38  ? -36.33400 0.13600   48.45000 1.000 29.68495 ?  18  TYR B CA    1 
ATOM   2009 C C     . TYR B 1 38  ? -37.79300 -0.30500  48.29600 1.000 31.91836 ?  18  TYR B C     1 
ATOM   2010 O O     . TYR B 1 38  ? -38.60400 0.54200   47.95700 1.000 31.42195 ?  18  TYR B O     1 
ATOM   2011 C CB    . TYR B 1 38  ? -35.46100 0.08400   47.19800 1.000 27.68659 ?  18  TYR B CB    1 
ATOM   2012 C CG    . TYR B 1 38  ? -34.46600 1.21200   47.19600 1.000 30.85380 ?  18  TYR B CG    1 
ATOM   2013 C CD1   . TYR B 1 38  ? -34.80800 2.46100   46.71200 1.000 30.31903 ?  18  TYR B CD1   1 
ATOM   2014 C CD2   . TYR B 1 38  ? -33.21700 1.05500   47.76600 1.000 31.88047 ?  18  TYR B CD2   1 
ATOM   2015 C CE1   . TYR B 1 38  ? -33.91300 3.51500   46.74100 1.000 29.12756 ?  18  TYR B CE1   1 
ATOM   2016 C CE2   . TYR B 1 38  ? -32.31100 2.09700   47.80600 1.000 31.64816 ?  18  TYR B CE2   1 
ATOM   2017 C CZ    . TYR B 1 38  ? -32.66200 3.33000   47.29400 1.000 31.30080 ?  18  TYR B CZ    1 
ATOM   2018 O OH    . TYR B 1 38  ? -31.76900 4.36000   47.33800 1.000 38.83663 ?  18  TYR B OH    1 
ATOM   2019 N N     . CYS B 1 39  ? -38.10500 -1.57300  48.56000 1.000 29.46122 ?  19  CYS B N     1 
ATOM   2020 C CA    . CYS B 1 39  ? -39.50800 -1.97700  48.56600 1.000 29.03137 ?  19  CYS B CA    1 
ATOM   2021 C C     . CYS B 1 39  ? -40.29500 -1.14500  49.56500 1.000 30.61161 ?  19  CYS B C     1 
ATOM   2022 O O     . CYS B 1 39  ? -41.37100 -0.62300  49.25500 1.000 31.14292 ?  19  CYS B O     1 
ATOM   2023 C CB    . CYS B 1 39  ? -39.62700 -3.46200  48.91600 1.000 32.46049 ?  19  CYS B CB    1 
ATOM   2024 S SG    . CYS B 1 39  ? -39.13600 -4.55700  47.60500 1.000 32.39434 ?  19  CYS B SG    1 
ATOM   2025 N N     . ASP B 1 40  ? -39.76300 -1.01400  50.77800 1.000 32.79748 ?  20  ASP B N     1 
ATOM   2026 C CA    . ASP B 1 40  ? -40.42500 -0.23300  51.80800 1.000 30.31663 ?  20  ASP B CA    1 
ATOM   2027 C C     . ASP B 1 40  ? -40.47500 1.23700   51.42400 1.000 29.83131 ?  20  ASP B C     1 
ATOM   2028 O O     . ASP B 1 40  ? -41.51500 1.88900   51.54200 1.000 29.63083 ?  20  ASP B O     1 
ATOM   2029 C CB    . ASP B 1 40  ? -39.69200 -0.41900  53.13100 1.000 31.04599 ?  20  ASP B CB    1 
ATOM   2030 C CG    . ASP B 1 40  ? -40.54200 -0.05400  54.32500 1.000 37.23616 ?  20  ASP B CG    1 
ATOM   2031 O OD1   . ASP B 1 40  ? -41.78000 -0.22400  54.25700 1.000 40.15158 ?  20  ASP B OD1   1 
ATOM   2032 O OD2   . ASP B 1 40  ? -39.97100 0.40500   55.33400 1.000 40.61704 -1 20  ASP B OD2   1 
ATOM   2033 N N     . PHE B 1 41  ? -39.35100 1.76900   50.95200 1.000 30.83563 ?  21  PHE B N     1 
ATOM   2034 C CA    . PHE B 1 41  ? -39.28000 3.17400   50.56200 1.000 30.02272 ?  21  PHE B CA    1 
ATOM   2035 C C     . PHE B 1 41  ? -40.25000 3.48300   49.42500 1.000 29.37625 ?  21  PHE B C     1 
ATOM   2036 O O     . PHE B 1 41  ? -40.96200 4.49600   49.45000 1.000 30.36193 ?  21  PHE B O     1 
ATOM   2037 C CB    . PHE B 1 41  ? -37.83800 3.50300   50.16600 1.000 28.94262 ?  21  PHE B CB    1 
ATOM   2038 C CG    . PHE B 1 41  ? -37.62600 4.91200   49.65000 1.000 32.03783 ?  21  PHE B CG    1 
ATOM   2039 C CD1   . PHE B 1 41  ? -37.98700 6.01400   50.41500 1.000 26.86815 ?  21  PHE B CD1   1 
ATOM   2040 C CD2   . PHE B 1 41  ? -37.00900 5.12600   48.41400 1.000 27.63579 ?  21  PHE B CD2   1 
ATOM   2041 C CE1   . PHE B 1 41  ? -37.75500 7.31000   49.94100 1.000 28.90162 ?  21  PHE B CE1   1 
ATOM   2042 C CE2   . PHE B 1 41  ? -36.78300 6.40300   47.93500 1.000 27.96807 ?  21  PHE B CE2   1 
ATOM   2043 C CZ    . PHE B 1 41  ? -37.15400 7.50100   48.69900 1.000 28.34300 ?  21  PHE B CZ    1 
ATOM   2044 N N     . GLN B 1 42  ? -40.30000 2.61600   48.42600 1.000 26.93314 ?  22  GLN B N     1 
ATOM   2045 C CA    . GLN B 1 42  ? -41.06000 2.93500   47.22600 1.000 30.44240 ?  22  GLN B CA    1 
ATOM   2046 C C     . GLN B 1 42  ? -42.53100 2.55300   47.32000 1.000 28.59076 ?  22  GLN B C     1 
ATOM   2047 O O     . GLN B 1 42  ? -43.36500 3.18300   46.66400 1.000 32.21539 ?  22  GLN B O     1 
ATOM   2048 C CB    . GLN B 1 42  ? -40.42900 2.25400   46.01200 1.000 28.77440 ?  22  GLN B CB    1 
ATOM   2049 C CG    . GLN B 1 42  ? -39.19100 2.97000   45.49800 1.000 28.73361 ?  22  GLN B CG    1 
ATOM   2050 C CD    . GLN B 1 42  ? -38.96300 2.72600   44.02100 1.000 29.69373 ?  22  GLN B CD    1 
ATOM   2051 O OE1   . GLN B 1 42  ? -39.18800 1.61700   43.51700 1.000 26.99263 ?  22  GLN B OE1   1 
ATOM   2052 N NE2   . GLN B 1 42  ? -38.53900 3.76800   43.30900 1.000 28.72032 ?  22  GLN B NE2   1 
ATOM   2053 N N     . TYR B 1 43  ? -42.87400 1.55500   48.12800 1.000 27.88692 ?  23  TYR B N     1 
ATOM   2054 C CA    . TYR B 1 43  ? -44.23100 1.04600   48.16100 1.000 30.91909 ?  23  TYR B CA    1 
ATOM   2055 C C     . TYR B 1 43  ? -44.86700 1.07300   49.54100 1.000 31.80234 ?  23  TYR B C     1 
ATOM   2056 O O     . TYR B 1 43  ? -46.07600 0.82500   49.64500 1.000 32.71388 ?  23  TYR B O     1 
ATOM   2057 C CB    . TYR B 1 43  ? -44.27100 -0.39200  47.61500 1.000 28.36963 ?  23  TYR B CB    1 
ATOM   2058 C CG    . TYR B 1 43  ? -43.84800 -0.51400  46.16600 1.000 28.77827 ?  23  TYR B CG    1 
ATOM   2059 C CD1   . TYR B 1 43  ? -44.73700 -0.22800  45.13600 1.000 28.92808 ?  23  TYR B CD1   1 
ATOM   2060 C CD2   . TYR B 1 43  ? -42.55700 -0.91100  45.82300 1.000 29.59842 ?  23  TYR B CD2   1 
ATOM   2061 C CE1   . TYR B 1 43  ? -44.35600 -0.34300  43.80200 1.000 28.03675 ?  23  TYR B CE1   1 
ATOM   2062 C CE2   . TYR B 1 43  ? -42.16500 -1.02300  44.49200 1.000 26.24801 ?  23  TYR B CE2   1 
ATOM   2063 C CZ    . TYR B 1 43  ? -43.07200 -0.73600  43.48700 1.000 27.63678 ?  23  TYR B CZ    1 
ATOM   2064 O OH    . TYR B 1 43  ? -42.70300 -0.84600  42.16800 1.000 22.87462 ?  23  TYR B OH    1 
ATOM   2065 N N     . GLY B 1 44  ? -44.09800 1.36700   50.59600 1.000 27.72970 ?  24  GLY B N     1 
ATOM   2066 C CA    . GLY B 1 44  ? -44.59800 1.35800   51.95500 1.000 29.75042 ?  24  GLY B CA    1 
ATOM   2067 C C     . GLY B 1 44  ? -45.30400 2.64500   52.32800 1.000 30.84429 ?  24  GLY B C     1 
ATOM   2068 O O     . GLY B 1 44  ? -45.65200 3.47300   51.48000 1.000 32.71630 ?  24  GLY B O     1 
ATOM   2069 N N     . GLU B 1 45  ? -45.50100 2.81700   53.62900 1.000 28.67314 ?  25  GLU B N     1 
ATOM   2070 C CA    . GLU B 1 45  ? -46.28900 3.92700   54.13700 1.000 36.63902 ?  25  GLU B CA    1 
ATOM   2071 C C     . GLU B 1 45  ? -45.45700 5.20700   54.19700 1.000 31.35832 ?  25  GLU B C     1 
ATOM   2072 O O     . GLU B 1 45  ? -44.23500 5.17500   54.34800 1.000 35.73622 ?  25  GLU B O     1 
ATOM   2073 C CB    . GLU B 1 45  ? -46.85000 3.57900   55.51900 1.000 33.14259 ?  25  GLU B CB    1 
ATOM   2074 N N     . ASP B 1 46  ? -46.13400 6.33900   54.05000 1.000 34.28588 ?  26  ASP B N     1 
ATOM   2075 C CA    . ASP B 1 46  ? -45.46500 7.63500   54.10600 1.000 34.42409 ?  26  ASP B CA    1 
ATOM   2076 C C     . ASP B 1 46  ? -44.98300 7.90900   55.52100 1.000 33.87307 ?  26  ASP B C     1 
ATOM   2077 O O     . ASP B 1 46  ? -45.75500 7.81300   56.47500 1.000 40.34027 ?  26  ASP B O     1 
ATOM   2078 C CB    . ASP B 1 46  ? -46.41700 8.74500   53.66800 1.000 36.34291 ?  26  ASP B CB    1 
ATOM   2079 C CG    . ASP B 1 46  ? -46.73300 8.70600   52.17900 1.000 38.11380 ?  26  ASP B CG    1 
ATOM   2080 O OD1   . ASP B 1 46  ? -46.21800 7.81900   51.44800 1.000 36.14738 ?  26  ASP B OD1   1 
ATOM   2081 O OD2   . ASP B 1 46  ? -47.51400 9.58000   51.74300 1.000 39.62406 -1 26  ASP B OD2   1 
ATOM   2082 N N     . CYS B 1 47  ? -43.71000 8.24100   55.66800 1.000 35.83523 ?  27  CYS B N     1 
ATOM   2083 C CA    . CYS B 1 47  ? -43.14400 8.50500   56.98300 1.000 35.59759 ?  27  CYS B CA    1 
ATOM   2084 C C     . CYS B 1 47  ? -43.10400 10.00800  57.23900 1.000 38.09298 ?  27  CYS B C     1 
ATOM   2085 O O     . CYS B 1 47  ? -42.85000 10.79500  56.32200 1.000 33.08134 ?  27  CYS B O     1 
ATOM   2086 C CB    . CYS B 1 47  ? -41.73900 7.90600   57.11200 1.000 33.50092 ?  27  CYS B CB    1 
ATOM   2087 S SG    . CYS B 1 47  ? -41.59000 6.12400   56.70900 1.000 38.41207 ?  27  CYS B SG    1 
ATOM   2088 N N     . PHE B 1 48  ? -43.38700 10.39800  58.48900 1.000 35.87657 ?  28  PHE B N     1 
ATOM   2089 C CA    . PHE B 1 48  ? -43.30100 11.79300  58.94200 1.000 32.80013 ?  28  PHE B CA    1 
ATOM   2090 C C     . PHE B 1 48  ? -44.11800 12.73900  58.07100 1.000 34.48680 ?  28  PHE B C     1 
ATOM   2091 O O     . PHE B 1 48  ? -43.79100 13.92200  57.94400 1.000 36.85152 ?  28  PHE B O     1 
ATOM   2092 C CB    . PHE B 1 48  ? -41.85200 12.27900  59.00500 1.000 28.94893 ?  28  PHE B CB    1 
ATOM   2093 C CG    . PHE B 1 48  ? -40.99400 11.51300  59.96300 1.000 31.14495 ?  28  PHE B CG    1 
ATOM   2094 C CD1   . PHE B 1 48  ? -41.27000 11.51900  61.31700 1.000 32.79846 ?  28  PHE B CD1   1 
ATOM   2095 C CD2   . PHE B 1 48  ? -39.89600 10.80500  59.51300 1.000 28.53480 ?  28  PHE B CD2   1 
ATOM   2096 C CE1   . PHE B 1 48  ? -40.47400 10.82500  62.20200 1.000 30.78130 ?  28  PHE B CE1   1 
ATOM   2097 C CE2   . PHE B 1 48  ? -39.10300 10.10400  60.38900 1.000 28.52235 ?  28  PHE B CE2   1 
ATOM   2098 C CZ    . PHE B 1 48  ? -39.38700 10.11800  61.73600 1.000 31.35195 ?  28  PHE B CZ    1 
ATOM   2099 N N     . GLY B 1 49  ? -45.17100 12.22400  57.44600 1.000 37.45920 ?  29  GLY B N     1 
ATOM   2100 C CA    . GLY B 1 49  ? -46.01300 13.04900  56.60800 1.000 32.59333 ?  29  GLY B CA    1 
ATOM   2101 C C     . GLY B 1 49  ? -45.44400 13.38100  55.25000 1.000 37.05846 ?  29  GLY B C     1 
ATOM   2102 O O     . GLY B 1 49  ? -46.00200 14.23900  54.55700 1.000 36.37582 ?  29  GLY B O     1 
ATOM   2103 N N     . VAL B 1 50  ? -44.36100 12.73700  54.83800 1.000 34.42793 ?  30  VAL B N     1 
ATOM   2104 C CA    . VAL B 1 50  ? -43.71300 13.07100  53.57700 1.000 31.55701 ?  30  VAL B CA    1 
ATOM   2105 C C     . VAL B 1 50  ? -44.30500 12.21000  52.47000 1.000 31.20909 ?  30  VAL B C     1 
ATOM   2106 O O     . VAL B 1 50  ? -44.39300 10.98200  52.60100 1.000 32.61744 ?  30  VAL B O     1 
ATOM   2107 C CB    . VAL B 1 50  ? -42.18900 12.90000  53.67800 1.000 28.98373 ?  30  VAL B CB    1 
ATOM   2108 C CG1   . VAL B 1 50  ? -41.52000 13.24600  52.35500 1.000 27.55640 ?  30  VAL B CG1   1 
ATOM   2109 C CG2   . VAL B 1 50  ? -41.65000 13.80000  54.79000 1.000 30.47818 ?  30  VAL B CG2   1 
ATOM   2110 N N     . LEU B 1 51  ? -44.73600 12.86700  51.39300 1.000 32.65320 ?  31  LEU B N     1 
ATOM   2111 C CA    . LEU B 1 51  ? -45.28800 12.18100  50.23200 1.000 32.88500 ?  31  LEU B CA    1 
ATOM   2112 C C     . LEU B 1 51  ? -44.29200 11.16800  49.67600 1.000 31.33913 ?  31  LEU B C     1 
ATOM   2113 O O     . LEU B 1 51  ? -43.08100 11.39700  49.69400 1.000 30.35076 ?  31  LEU B O     1 
ATOM   2114 C CB    . LEU B 1 51  ? -45.62800 13.19600  49.14300 1.000 28.43755 ?  31  LEU B CB    1 
ATOM   2115 C CG    . LEU B 1 51  ? -46.40000 12.60900  47.95900 1.000 37.57469 ?  31  LEU B CG    1 
ATOM   2116 C CD1   . LEU B 1 51  ? -47.70800 11.96900  48.44900 1.000 41.20904 ?  31  LEU B CD1   1 
ATOM   2117 C CD2   . LEU B 1 51  ? -46.63300 13.63000  46.84300 1.000 39.84802 ?  31  LEU B CD2   1 
ATOM   2118 N N     . ASN B 1 52  ? -44.81200 10.05300  49.17200 1.000 26.28274 ?  32  ASN B N     1 
ATOM   2119 C CA    . ASN B 1 52  ? -43.98200 9.04300   48.53200 1.000 29.52232 ?  32  ASN B CA    1 
ATOM   2120 C C     . ASN B 1 52  ? -43.09800 9.67600   47.46400 1.000 28.47537 ?  32  ASN B C     1 
ATOM   2121 O O     . ASN B 1 52  ? -43.58500 10.37500  46.57000 1.000 28.69019 ?  32  ASN B O     1 
ATOM   2122 C CB    . ASN B 1 52  ? -44.86200 7.95800   47.91000 1.000 26.56227 ?  32  ASN B CB    1 
ATOM   2123 C CG    . ASN B 1 52  ? -44.05300 6.91300   47.18900 1.000 28.68425 ?  32  ASN B CG    1 
ATOM   2124 O OD1   . ASN B 1 52  ? -43.84600 6.98900   45.97500 1.000 27.80270 ?  32  ASN B OD1   1 
ATOM   2125 N ND2   . ASN B 1 52  ? -43.56300 5.93600   47.93900 1.000 31.79983 ?  32  ASN B ND2   1 
ATOM   2126 N N     . PHE B 1 53  ? -41.79100 9.41400   47.56000 1.000 25.36383 ?  33  PHE B N     1 
ATOM   2127 C CA    . PHE B 1 53  ? -40.81900 10.09200  46.70200 1.000 23.40126 ?  33  PHE B CA    1 
ATOM   2128 C C     . PHE B 1 53  ? -41.01500 9.72700   45.23700 1.000 24.92167 ?  33  PHE B C     1 
ATOM   2129 O O     . PHE B 1 53  ? -40.98900 10.59800  44.36500 1.000 23.21363 ?  33  PHE B O     1 
ATOM   2130 C CB    . PHE B 1 53  ? -39.39600 9.74900   47.15000 1.000 25.56803 ?  33  PHE B CB    1 
ATOM   2131 C CG    . PHE B 1 53  ? -38.31100 10.51000  46.41400 1.000 27.86018 ?  33  PHE B CG    1 
ATOM   2132 C CD1   . PHE B 1 53  ? -38.22500 11.89700  46.50100 1.000 25.42972 ?  33  PHE B CD1   1 
ATOM   2133 C CD2   . PHE B 1 53  ? -37.36700 9.83000   45.64600 1.000 26.30408 ?  33  PHE B CD2   1 
ATOM   2134 C CE1   . PHE B 1 53  ? -37.22500 12.58500  45.83700 1.000 21.92341 ?  33  PHE B CE1   1 
ATOM   2135 C CE2   . PHE B 1 53  ? -36.36400 10.51500  44.97700 1.000 24.40945 ?  33  PHE B CE2   1 
ATOM   2136 C CZ    . PHE B 1 53  ? -36.29600 11.89800  45.07600 1.000 26.15886 ?  33  PHE B CZ    1 
ATOM   2137 N N     . ALA B 1 54  ? -41.18600 8.43700   44.94000 1.000 25.16068 ?  34  ALA B N     1 
ATOM   2138 C CA    . ALA B 1 54  ? -41.32900 8.02500   43.54500 1.000 25.52297 ?  34  ALA B CA    1 
ATOM   2139 C C     . ALA B 1 54  ? -42.57700 8.63600   42.91400 1.000 27.76418 ?  34  ALA B C     1 
ATOM   2140 O O     . ALA B 1 54  ? -42.53400 9.13400   41.78200 1.000 28.17644 ?  34  ALA B O     1 
ATOM   2141 C CB    . ALA B 1 54  ? -41.36300 6.49900   43.44600 1.000 25.08782 ?  34  ALA B CB    1 
ATOM   2142 N N     . LEU B 1 55  ? -43.70300 8.60400   43.63200 1.000 28.02471 ?  35  LEU B N     1 
ATOM   2143 C CA    . LEU B 1 55  ? -44.91700 9.24400   43.13100 1.000 27.29548 ?  35  LEU B CA    1 
ATOM   2144 C C     . LEU B 1 55  ? -44.70000 10.73800  42.91800 1.000 26.36072 ?  35  LEU B C     1 
ATOM   2145 O O     . LEU B 1 55  ? -45.07900 11.28500  41.87700 1.000 28.97211 ?  35  LEU B O     1 
ATOM   2146 C CB    . LEU B 1 55  ? -46.07900 8.99800   44.09300 1.000 27.71757 ?  35  LEU B CB    1 
ATOM   2147 C CG    . LEU B 1 55  ? -47.35700 9.79100   43.80900 1.000 31.79548 ?  35  LEU B CG    1 
ATOM   2148 C CD1   . LEU B 1 55  ? -48.06200 9.29600   42.53900 1.000 31.04291 ?  35  LEU B CD1   1 
ATOM   2149 C CD2   . LEU B 1 55  ? -48.28500 9.75700   45.00900 1.000 28.39643 ?  35  LEU B CD2   1 
ATOM   2150 N N     . ALA B 1 56  ? -44.05800 11.40900  43.88200 1.000 26.41788 ?  36  ALA B N     1 
ATOM   2151 C CA    . ALA B 1 56  ? -43.83900 12.85000  43.76500 1.000 27.40367 ?  36  ALA B CA    1 
ATOM   2152 C C     . ALA B 1 56  ? -42.97500 13.19000  42.55700 1.000 30.88495 ?  36  ALA B C     1 
ATOM   2153 O O     . ALA B 1 56  ? -43.27200 14.13800  41.81500 1.000 24.60108 ?  36  ALA B O     1 
ATOM   2154 C CB    . ALA B 1 56  ? -43.20300 13.39100  45.04600 1.000 25.01955 ?  36  ALA B CB    1 
ATOM   2155 N N     . CYS B 1 57  ? -41.89500 12.42800  42.34500 1.000 28.38859 ?  37  CYS B N     1 
ATOM   2156 C CA    . CYS B 1 57  ? -41.02200 12.67200  41.20300 1.000 27.61131 ?  37  CYS B CA    1 
ATOM   2157 C C     . CYS B 1 57  ? -41.74600 12.41800  39.88200 1.000 29.17312 ?  37  CYS B C     1 
ATOM   2158 O O     . CYS B 1 57  ? -41.60100 13.19300  38.92800 1.000 27.58539 ?  37  CYS B O     1 
ATOM   2159 C CB    . CYS B 1 57  ? -39.77700 11.79200  41.30400 1.000 27.37285 ?  37  CYS B CB    1 
ATOM   2160 S SG    . CYS B 1 57  ? -38.58300 12.30200  42.57000 1.000 25.60210 ?  37  CYS B SG    1 
ATOM   2161 N N     . ALA B 1 58  ? -42.50500 11.32500  39.79400 1.000 29.41854 ?  38  ALA B N     1 
ATOM   2162 C CA    . ALA B 1 58  ? -43.21100 11.04000  38.55000 1.000 28.12643 ?  38  ALA B CA    1 
ATOM   2163 C C     . ALA B 1 58  ? -44.26600 12.10200  38.27900 1.000 29.09020 ?  38  ALA B C     1 
ATOM   2164 O O     . ALA B 1 58  ? -44.40500 12.58200  37.14500 1.000 30.01692 ?  38  ALA B O     1 
ATOM   2165 C CB    . ALA B 1 58  ? -43.83800 9.64900   38.61000 1.000 26.29014 ?  38  ALA B CB    1 
ATOM   2166 N N     . THR B 1 59  ? -45.00100 12.49300  39.32000 1.000 29.88590 ?  39  THR B N     1 
ATOM   2167 C CA    . THR B 1 59  ? -46.03200 13.50900  39.16900 1.000 31.48447 ?  39  THR B CA    1 
ATOM   2168 C C     . THR B 1 59  ? -45.42900 14.82400  38.71000 1.000 33.48765 ?  39  THR B C     1 
ATOM   2169 O O     . THR B 1 59  ? -45.98100 15.50000  37.83100 1.000 35.09704 ?  39  THR B O     1 
ATOM   2170 C CB    . THR B 1 59  ? -46.77500 13.68700  40.49300 1.000 28.16434 ?  39  THR B CB    1 
ATOM   2171 O OG1   . THR B 1 59  ? -47.43300 12.46100  40.82700 1.000 28.63482 ?  39  THR B OG1   1 
ATOM   2172 C CG2   . THR B 1 59  ? -47.80900 14.80900  40.39400 1.000 29.16731 ?  39  THR B CG2   1 
ATOM   2173 N N     . LYS B 1 60  ? -44.28300 15.19500  39.28000 1.000 31.71226 ?  40  LYS B N     1 
ATOM   2174 C CA    . LYS B 1 60  ? -43.65100 16.44200  38.87800 1.000 28.52797 ?  40  LYS B CA    1 
ATOM   2175 C C     . LYS B 1 60  ? -43.14500 16.35700  37.44600 1.000 31.92760 ?  40  LYS B C     1 
ATOM   2176 O O     . LYS B 1 60  ? -43.27100 17.31900  36.68200 1.000 30.96141 ?  40  LYS B O     1 
ATOM   2177 C CB    . LYS B 1 60  ? -42.52300 16.79500  39.84800 1.000 31.23925 ?  40  LYS B CB    1 
ATOM   2178 C CG    . LYS B 1 60  ? -42.99100 17.64700  41.03800 1.000 35.78799 ?  40  LYS B CG    1 
ATOM   2179 C CD    . LYS B 1 60  ? -42.19600 17.33800  42.29700 1.000 34.57605 ?  40  LYS B CD    1 
ATOM   2180 C CE    . LYS B 1 60  ? -42.97100 17.66100  43.56900 1.000 33.59954 ?  40  LYS B CE    1 
ATOM   2181 N NZ    . LYS B 1 60  ? -43.61700 18.99600  43.49200 1.000 31.71763 ?  40  LYS B NZ    1 
ATOM   2182 N N     . ALA B 1 61  ? -42.58600 15.20400  37.06600 1.000 27.58061 ?  41  ALA B N     1 
ATOM   2183 C CA    . ALA B 1 61  ? -42.11100 15.01200  35.69800 1.000 30.81287 ?  41  ALA B CA    1 
ATOM   2184 C C     . ALA B 1 61  ? -43.25400 15.15600  34.70600 1.000 32.24716 ?  41  ALA B C     1 
ATOM   2185 O O     . ALA B 1 61  ? -43.11900 15.83100  33.67800 1.000 32.68303 ?  41  ALA B O     1 
ATOM   2186 C CB    . ALA B 1 61  ? -41.45100 13.63700  35.55300 1.000 26.07378 ?  41  ALA B CB    1 
ATOM   2187 N N     . ILE B 1 62  ? -44.39100 14.52500  35.00300 1.000 31.31947 ?  42  ILE B N     1 
ATOM   2188 C CA    . ILE B 1 62  ? -45.55400 14.65400  34.13600 1.000 31.19892 ?  42  ILE B CA    1 
ATOM   2189 C C     . ILE B 1 62  ? -45.94600 16.11700  34.00500 1.000 32.87588 ?  42  ILE B C     1 
ATOM   2190 O O     . ILE B 1 62  ? -46.24500 16.59800  32.90600 1.000 38.24245 ?  42  ILE B O     1 
ATOM   2191 C CB    . ILE B 1 62  ? -46.71000 13.78500  34.66600 1.000 32.89551 ?  42  ILE B CB    1 
ATOM   2192 C CG1   . ILE B 1 62  ? -46.39600 12.30000  34.43300 1.000 31.48037 ?  42  ILE B CG1   1 
ATOM   2193 C CG2   . ILE B 1 62  ? -48.04400 14.17800  34.01300 1.000 32.42279 ?  42  ILE B CG2   1 
ATOM   2194 C CD1   . ILE B 1 62  ? -47.13700 11.36100  35.36100 1.000 33.02246 ?  42  ILE B CD1   1 
ATOM   2195 N N     . GLY B 1 63  ? -45.90800 16.85600  35.11500 1.000 34.73483 ?  43  GLY B N     1 
ATOM   2196 C CA    . GLY B 1 63  ? -46.27000 18.26300  35.07100 1.000 32.16370 ?  43  GLY B CA    1 
ATOM   2197 C C     . GLY B 1 63  ? -45.32000 19.09300  34.22900 1.000 34.96617 ?  43  GLY B C     1 
ATOM   2198 O O     . GLY B 1 63  ? -45.74500 20.00100  33.51200 1.000 37.41440 ?  43  GLY B O     1 
ATOM   2199 N N     . TYR B 1 64  ? -44.02100 18.79200  34.29700 1.000 30.63325 ?  44  TYR B N     1 
ATOM   2200 C CA    . TYR B 1 64  ? -43.04400 19.56900  33.54000 1.000 33.80702 ?  44  TYR B CA    1 
ATOM   2201 C C     . TYR B 1 64  ? -43.05500 19.23800  32.05100 1.000 36.15515 ?  44  TYR B C     1 
ATOM   2202 O O     . TYR B 1 64  ? -42.52300 20.01500  31.24800 1.000 35.97303 ?  44  TYR B O     1 
ATOM   2203 C CB    . TYR B 1 64  ? -41.63700 19.35800  34.11700 1.000 30.31259 ?  44  TYR B CB    1 
ATOM   2204 C CG    . TYR B 1 64  ? -41.37200 20.14100  35.38400 1.000 31.20087 ?  44  TYR B CG    1 
ATOM   2205 C CD1   . TYR B 1 64  ? -41.46800 21.53100  35.40100 1.000 29.38184 ?  44  TYR B CD1   1 
ATOM   2206 C CD2   . TYR B 1 64  ? -41.03800 19.49700  36.56500 1.000 31.08812 ?  44  TYR B CD2   1 
ATOM   2207 C CE1   . TYR B 1 64  ? -41.23700 22.25400  36.56000 1.000 32.68280 ?  44  TYR B CE1   1 
ATOM   2208 C CE2   . TYR B 1 64  ? -40.80200 20.21000  37.73400 1.000 30.55394 ?  44  TYR B CE2   1 
ATOM   2209 C CZ    . TYR B 1 64  ? -40.90200 21.59200  37.72500 1.000 35.31214 ?  44  TYR B CZ    1 
ATOM   2210 O OH    . TYR B 1 64  ? -40.67600 22.31200  38.88600 1.000 34.16082 ?  44  TYR B OH    1 
ATOM   2211 N N     . THR B 1 65  ? -43.65900 18.11900  31.65900 1.000 35.57325 ?  45  THR B N     1 
ATOM   2212 C CA    . THR B 1 65  ? -43.63200 17.65000  30.27900 1.000 34.72425 ?  45  THR B CA    1 
ATOM   2213 C C     . THR B 1 65  ? -45.00900 17.71300  29.62700 1.000 35.86667 ?  45  THR B C     1 
ATOM   2214 O O     . THR B 1 65  ? -45.30500 16.93800  28.71300 1.000 36.80488 ?  45  THR B O     1 
ATOM   2215 C CB    . THR B 1 65  ? -43.09400 16.21900  30.21400 1.000 36.22813 ?  45  THR B CB    1 
ATOM   2216 O OG1   . THR B 1 65  ? -43.88800 15.37200  31.05600 1.000 33.71591 ?  45  THR B OG1   1 
ATOM   2217 C CG2   . THR B 1 65  ? -41.63700 16.16000  30.66500 1.000 32.99936 ?  45  THR B CG2   1 
ATOM   2218 N N     . LYS B 1 66  ? -45.86300 18.63000  30.08500 1.000 35.78049 ?  46  LYS B N     1 
ATOM   2219 C CA    . LYS B 1 66  ? -47.26200 18.56600  29.69100 1.000 37.30709 ?  46  LYS B CA    1 
ATOM   2220 C C     . LYS B 1 66  ? -47.47400 18.98200  28.24100 1.000 34.84230 ?  46  LYS B C     1 
ATOM   2221 O O     . LYS B 1 66  ? -48.53600 18.69900  27.67900 1.000 32.54761 ?  46  LYS B O     1 
ATOM   2222 C CB    . LYS B 1 66  ? -48.12300 19.42100  30.63000 1.000 36.41160 ?  46  LYS B CB    1 
ATOM   2223 C CG    . LYS B 1 66  ? -47.58300 20.80100  30.92100 1.000 36.58037 ?  46  LYS B CG    1 
ATOM   2224 C CD    . LYS B 1 66  ? -48.43900 21.51700  31.96700 1.000 41.10258 ?  46  LYS B CD    1 
ATOM   2225 C CE    . LYS B 1 66  ? -47.85900 22.89200  32.30900 1.000 37.07092 ?  46  LYS B CE    1 
ATOM   2226 N N     . GLU B 1 67  ? -46.49500 19.63200  27.61600 1.000 33.57918 ?  47  GLU B N     1 
ATOM   2227 C CA    . GLU B 1 67  ? -46.60000 19.99200  26.20900 1.000 39.91741 ?  47  GLU B CA    1 
ATOM   2228 C C     . GLU B 1 67  ? -45.69600 19.13200  25.32900 1.000 41.11975 ?  47  GLU B C     1 
ATOM   2229 O O     . GLU B 1 67  ? -45.43900 19.48700  24.17200 1.000 36.51475 ?  47  GLU B O     1 
ATOM   2230 C CB    . GLU B 1 67  ? -46.28700 21.47600  26.01700 1.000 38.87917 ?  47  GLU B CB    1 
ATOM   2231 C CG    . GLU B 1 67  ? -47.17600 22.38000  26.85100 1.000 44.72063 ?  47  GLU B CG    1 
ATOM   2232 C CD    . GLU B 1 67  ? -47.68400 23.59200  26.08600 1.000 46.76666 ?  47  GLU B CD    1 
ATOM   2233 O OE1   . GLU B 1 67  ? -46.94600 24.11500  25.22300 1.000 43.55302 ?  47  GLU B OE1   1 
ATOM   2234 O OE2   . GLU B 1 67  ? -48.82100 24.02900  26.36200 1.000 50.62975 -1 47  GLU B OE2   1 
ATOM   2235 N N     . THR B 1 68  ? -45.20200 18.01300  25.85800 1.000 34.91618 ?  48  THR B N     1 
ATOM   2236 C CA    . THR B 1 68  ? -44.39400 17.08200  25.09400 1.000 38.95257 ?  48  THR B CA    1 
ATOM   2237 C C     . THR B 1 68  ? -45.24000 15.91600  24.62900 1.000 37.70901 ?  48  THR B C     1 
ATOM   2238 O O     . THR B 1 68  ? -46.30600 15.64400  25.19200 1.000 36.40715 ?  48  THR B O     1 
ATOM   2239 C CB    . THR B 1 68  ? -43.22700 16.54300  25.93300 1.000 37.37036 ?  48  THR B CB    1 
ATOM   2240 O OG1   . THR B 1 68  ? -43.71100 15.54400  26.85200 1.000 43.36741 ?  48  THR B OG1   1 
ATOM   2241 C CG2   . THR B 1 68  ? -42.55100 17.66700  26.69200 1.000 38.33510 ?  48  THR B CG2   1 
ATOM   2242 N N     . PRO B 1 69  ? -44.80000 15.20600  23.59100 1.000 40.54823 ?  49  PRO B N     1 
ATOM   2243 C CA    . PRO B 1 69  ? -45.42300 13.92000  23.28600 1.000 40.63195 ?  49  PRO B CA    1 
ATOM   2244 C C     . PRO B 1 69  ? -45.25600 12.99600  24.47900 1.000 41.88475 ?  49  PRO B C     1 
ATOM   2245 O O     . PRO B 1 69  ? -44.32200 13.12900  25.27400 1.000 43.12316 ?  49  PRO B O     1 
ATOM   2246 C CB    . PRO B 1 69  ? -44.64300 13.42300  22.06500 1.000 38.25795 ?  49  PRO B CB    1 
ATOM   2247 C CG    . PRO B 1 69  ? -44.08500 14.65100  21.45100 1.000 38.72866 ?  49  PRO B CG    1 
ATOM   2248 C CD    . PRO B 1 69  ? -43.75900 15.55400  22.60800 1.000 40.41117 ?  49  PRO B CD    1 
ATOM   2249 N N     . LYS B 1 70  ? -46.19600 12.07300  24.61500 1.000 40.41315 ?  50  LYS B N     1 
ATOM   2250 C CA    . LYS B 1 70  ? -46.22900 11.22000  25.79000 1.000 39.88100 ?  50  LYS B CA    1 
ATOM   2251 C C     . LYS B 1 70  ? -46.03800 9.76700   25.38000 1.000 37.48524 ?  50  LYS B C     1 
ATOM   2252 O O     . LYS B 1 70  ? -46.79800 8.89700   25.81000 1.000 40.59440 ?  50  LYS B O     1 
ATOM   2253 C CB    . LYS B 1 70  ? -47.55800 11.41300  26.53200 1.000 44.86134 ?  50  LYS B CB    1 
ATOM   2254 C CG    . LYS B 1 70  ? -47.58200 12.60600  27.48800 1.000 40.67795 ?  50  LYS B CG    1 
ATOM   2255 C CD    . LYS B 1 70  ? -46.39300 12.56000  28.43700 1.000 41.31775 ?  50  LYS B CD    1 
ATOM   2256 C CE    . LYS B 1 70  ? -45.96900 13.95800  28.89600 1.000 44.67582 ?  50  LYS B CE    1 
ATOM   2257 N NZ    . LYS B 1 70  ? -46.71700 14.46800  30.08500 1.000 48.27221 ?  50  LYS B NZ    1 
ATOM   2258 N N     . ASN B 1 71  ? -45.04000 9.49000   24.54000 1.000 36.86311 ?  51  ASN B N     1 
ATOM   2259 C CA    . ASN B 1 71  ? -44.88200 8.14900   23.98600 1.000 36.79461 ?  51  ASN B CA    1 
ATOM   2260 C C     . ASN B 1 71  ? -43.87400 7.28300   24.73200 1.000 36.30629 ?  51  ASN B C     1 
ATOM   2261 O O     . ASN B 1 71  ? -44.14400 6.10100   24.94800 1.000 35.71623 ?  51  ASN B O     1 
ATOM   2262 C CB    . ASN B 1 71  ? -44.48900 8.22100   22.50600 1.000 36.81786 ?  51  ASN B CB    1 
ATOM   2263 C CG    . ASN B 1 71  ? -45.48800 9.01100   21.67800 1.000 45.21875 ?  51  ASN B CG    1 
ATOM   2264 O OD1   . ASN B 1 71  ? -46.69800 8.88200   21.86400 1.000 47.16053 ?  51  ASN B OD1   1 
ATOM   2265 N ND2   . ASN B 1 71  ? -44.98600 9.83000   20.75500 1.000 43.66729 ?  51  ASN B ND2   1 
ATOM   2266 N N     . ARG B 1 72  ? -42.72300 7.82600   25.13400 1.000 35.29085 ?  52  ARG B N     1 
ATOM   2267 C CA    . ARG B 1 72  ? -41.64700 6.99800   25.67200 1.000 35.27395 ?  52  ARG B CA    1 
ATOM   2268 C C     . ARG B 1 72  ? -40.93900 7.70500   26.81700 1.000 33.32827 ?  52  ARG B C     1 
ATOM   2269 O O     . ARG B 1 72  ? -40.49200 8.84600   26.66700 1.000 30.17276 ?  52  ARG B O     1 
ATOM   2270 C CB    . ARG B 1 72  ? -40.63600 6.64000   24.57500 1.000 34.03856 ?  52  ARG B CB    1 
ATOM   2271 C CG    . ARG B 1 72  ? -41.16500 5.62500   23.56400 1.000 32.75187 ?  52  ARG B CG    1 
ATOM   2272 C CD    . ARG B 1 72  ? -40.19700 5.44000   22.40800 1.000 34.32061 ?  52  ARG B CD    1 
ATOM   2273 N NE    . ARG B 1 72  ? -38.86600 5.03500   22.85100 1.000 37.50330 ?  52  ARG B NE    1 
ATOM   2274 C CZ    . ARG B 1 72  ? -38.55800 3.80100   23.22900 1.000 35.33880 ?  52  ARG B CZ    1 
ATOM   2275 N NH1   . ARG B 1 72  ? -39.47500 2.84900   23.29100 1.000 33.87228 ?  52  ARG B NH1   1 
ATOM   2276 N NH2   . ARG B 1 72  ? -37.30100 3.51300   23.55400 1.000 36.27108 ?  52  ARG B NH2   1 
ATOM   2277 N N     . ALA B 1 73  ? -40.81300 7.00800   27.94900 1.000 33.59888 ?  53  ALA B N     1 
ATOM   2278 C CA    . ALA B 1 73  ? -40.11100 7.52100   29.11800 1.000 31.48178 ?  53  ALA B CA    1 
ATOM   2279 C C     . ALA B 1 73  ? -39.14600 6.47000   29.65100 1.000 30.07431 ?  53  ALA B C     1 
ATOM   2280 O O     . ALA B 1 73  ? -39.46300 5.27800   29.68800 1.000 31.39837 ?  53  ALA B O     1 
ATOM   2281 C CB    . ALA B 1 73  ? -41.09000 7.93300   30.22300 1.000 27.38650 ?  53  ALA B CB    1 
ATOM   2282 N N     . LEU B 1 74  ? -37.96700 6.91900   30.06500 1.000 24.75693 ?  54  LEU B N     1 
ATOM   2283 C CA    . LEU B 1 74  ? -36.96600 6.06700   30.68800 1.000 29.63930 ?  54  LEU B CA    1 
ATOM   2284 C C     . LEU B 1 74  ? -36.78400 6.47500   32.14700 1.000 28.95061 ?  54  LEU B C     1 
ATOM   2285 O O     . LEU B 1 74  ? -36.54100 7.65100   32.44500 1.000 27.90987 ?  54  LEU B O     1 
ATOM   2286 C CB    . LEU B 1 74  ? -35.64200 6.15200   29.92700 1.000 26.67719 ?  54  LEU B CB    1 
ATOM   2287 C CG    . LEU B 1 74  ? -34.41800 5.47100   30.53900 1.000 28.76403 ?  54  LEU B CG    1 
ATOM   2288 C CD1   . LEU B 1 74  ? -34.64200 3.97800   30.72500 1.000 28.17997 ?  54  LEU B CD1   1 
ATOM   2289 C CD2   . LEU B 1 74  ? -33.20700 5.73300   29.65500 1.000 24.99993 ?  54  LEU B CD2   1 
ATOM   2290 N N     . ASP B 1 75  ? -36.92700 5.50400   33.05100 1.000 28.61685 ?  55  ASP B N     1 
ATOM   2291 C CA    . ASP B 1 75  ? -36.70200 5.69300   34.48600 1.000 28.01602 ?  55  ASP B CA    1 
ATOM   2292 C C     . ASP B 1 75  ? -35.37400 4.99600   34.79100 1.000 28.73943 ?  55  ASP B C     1 
ATOM   2293 O O     . ASP B 1 75  ? -35.32300 3.77400   34.96700 1.000 26.29383 ?  55  ASP B O     1 
ATOM   2294 C CB    . ASP B 1 75  ? -37.88800 5.14900   35.29000 1.000 24.65559 ?  55  ASP B CB    1 
ATOM   2295 C CG    . ASP B 1 75  ? -37.68400 5.20900   36.81000 1.000 28.17250 ?  55  ASP B CG    1 
ATOM   2296 O OD1   . ASP B 1 75  ? -36.78000 5.91700   37.31000 1.000 24.94802 ?  55  ASP B OD1   1 
ATOM   2297 O OD2   . ASP B 1 75  ? -38.45700 4.52600   37.52100 1.000 29.29427 -1 55  ASP B OD2   1 
ATOM   2298 N N     . LEU B 1 76  ? -34.30100 5.78900   34.81900 1.000 26.67294 ?  56  LEU B N     1 
ATOM   2299 C CA    . LEU B 1 76  ? -32.92800 5.30000   34.85100 1.000 27.51139 ?  56  LEU B CA    1 
ATOM   2300 C C     . LEU B 1 76  ? -32.45800 5.22200   36.29700 1.000 28.21227 ?  56  LEU B C     1 
ATOM   2301 O O     . LEU B 1 76  ? -32.46500 6.23300   37.00700 1.000 25.29768 ?  56  LEU B O     1 
ATOM   2302 C CB    . LEU B 1 76  ? -32.01900 6.22200   34.03600 1.000 26.44426 ?  56  LEU B CB    1 
ATOM   2303 C CG    . LEU B 1 76  ? -30.63300 5.72300   33.63700 1.000 25.58319 ?  56  LEU B CG    1 
ATOM   2304 C CD1   . LEU B 1 76  ? -30.61200 4.22100   33.32600 1.000 22.54087 ?  56  LEU B CD1   1 
ATOM   2305 C CD2   . LEU B 1 76  ? -30.06800 6.55300   32.49700 1.000 28.01483 ?  56  LEU B CD2   1 
ATOM   2306 N N     . GLY B 1 77  ? -32.03800 4.03100   36.72700 1.000 24.72655 ?  57  GLY B N     1 
ATOM   2307 C CA    . GLY B 1 77  ? -31.82700 3.80600   38.13900 1.000 25.41591 ?  57  GLY B CA    1 
ATOM   2308 C C     . GLY B 1 77  ? -33.14600 3.62900   38.86600 1.000 26.77835 ?  57  GLY B C     1 
ATOM   2309 O O     . GLY B 1 77  ? -33.36000 4.21100   39.93500 1.000 25.28188 ?  57  GLY B O     1 
ATOM   2310 N N     . CYS B 1 78  ? -34.02300 2.78300   38.30800 1.000 26.87554 ?  58  CYS B N     1 
ATOM   2311 C CA    . CYS B 1 78  ? -35.41100 2.68200   38.75300 1.000 26.26063 ?  58  CYS B CA    1 
ATOM   2312 C C     . CYS B 1 78  ? -35.58200 1.90000   40.04600 1.000 27.48566 ?  58  CYS B C     1 
ATOM   2313 O O     . CYS B 1 78  ? -36.69100 1.89200   40.59400 1.000 27.75861 ?  58  CYS B O     1 
ATOM   2314 C CB    . CYS B 1 78  ? -36.27500 2.02900   37.66100 1.000 27.18580 ?  58  CYS B CB    1 
ATOM   2315 S SG    . CYS B 1 78  ? -35.80800 0.29300   37.26600 1.000 24.76382 ?  58  CYS B SG    1 
ATOM   2316 N N     . ALA B 1 79  ? -34.52300 1.25200   40.54200 1.000 27.63882 ?  59  ALA B N     1 
ATOM   2317 C CA    . ALA B 1 79  ? -34.60800 0.41400   41.73200 1.000 28.10990 ?  59  ALA B CA    1 
ATOM   2318 C C     . ALA B 1 79  ? -35.80400 -0.51800  41.60600 1.000 27.59116 ?  59  ALA B C     1 
ATOM   2319 O O     . ALA B 1 79  ? -35.93500 -1.22400  40.60300 1.000 28.62972 ?  59  ALA B O     1 
ATOM   2320 C CB    . ALA B 1 79  ? -34.70300 1.26200   43.00400 1.000 24.81109 ?  59  ALA B CB    1 
ATOM   2321 N N     . THR B 1 80  ? -36.70400 -0.49700  42.57800 1.000 25.05158 ?  60  THR B N     1 
ATOM   2322 C CA    . THR B 1 80  ? -37.80900 -1.44200  42.58100 1.000 27.58491 ?  60  THR B CA    1 
ATOM   2323 C C     . THR B 1 80  ? -39.00600 -0.96800  41.75300 1.000 29.11116 ?  60  THR B C     1 
ATOM   2324 O O     . THR B 1 80  ? -40.07800 -1.58200  41.82500 1.000 29.06127 ?  60  THR B O     1 
ATOM   2325 C CB    . THR B 1 80  ? -38.22800 -1.74400  44.01800 1.000 27.56504 ?  60  THR B CB    1 
ATOM   2326 O OG1   . THR B 1 80  ? -38.30000 -0.51500  44.76300 1.000 27.89029 ?  60  THR B OG1   1 
ATOM   2327 C CG2   . THR B 1 80  ? -37.19300 -2.68000  44.68100 1.000 23.44643 ?  60  THR B CG2   1 
ATOM   2328 N N     . GLY B 1 81  ? -38.85500 0.11300   40.98300 1.000 26.13578 ?  61  GLY B N     1 
ATOM   2329 C CA    . GLY B 1 81  ? -39.71600 0.38000   39.84400 1.000 26.91177 ?  61  GLY B CA    1 
ATOM   2330 C C     . GLY B 1 81  ? -40.94600 1.24600   40.06500 1.000 29.77246 ?  61  GLY B C     1 
ATOM   2331 O O     . GLY B 1 81  ? -41.69800 1.46000   39.10300 1.000 26.95711 ?  61  GLY B O     1 
ATOM   2332 N N     . ARG B 1 82  ? -41.17200 1.76500   41.27700 1.000 27.76596 ?  62  ARG B N     1 
ATOM   2333 C CA    . ARG B 1 82  ? -42.40400 2.51300   41.53800 1.000 28.56644 ?  62  ARG B CA    1 
ATOM   2334 C C     . ARG B 1 82  ? -42.56700 3.69800   40.58800 1.000 28.91927 ?  62  ARG B C     1 
ATOM   2335 O O     . ARG B 1 82  ? -43.67500 3.97200   40.11400 1.000 29.64420 ?  62  ARG B O     1 
ATOM   2336 C CB    . ARG B 1 82  ? -42.44200 2.99100   42.99200 1.000 28.46420 ?  62  ARG B CB    1 
ATOM   2337 C CG    . ARG B 1 82  ? -43.59700 3.96500   43.30000 1.000 29.55066 ?  62  ARG B CG    1 
ATOM   2338 C CD    . ARG B 1 82  ? -44.92400 3.25400   43.49200 1.000 30.24492 ?  62  ARG B CD    1 
ATOM   2339 N NE    . ARG B 1 82  ? -46.03700 4.17600   43.69800 1.000 34.27817 ?  62  ARG B NE    1 
ATOM   2340 C CZ    . ARG B 1 82  ? -46.53900 4.50900   44.88100 1.000 34.42161 ?  62  ARG B CZ    1 
ATOM   2341 N NH1   . ARG B 1 82  ? -45.98500 4.09600   46.01100 1.000 29.39719 ?  62  ARG B NH1   1 
ATOM   2342 N NH2   . ARG B 1 82  ? -47.63300 5.26600   44.93000 1.000 30.67491 ?  62  ARG B NH2   1 
ATOM   2343 N N     . ALA B 1 83  ? -41.48500 4.42200   40.29700 1.000 26.96957 ?  63  ALA B N     1 
ATOM   2344 C CA    . ALA B 1 83  ? -41.63500 5.59100   39.43300 1.000 28.53292 ?  63  ALA B CA    1 
ATOM   2345 C C     . ALA B 1 83  ? -41.90900 5.18600   37.98700 1.000 29.98409 ?  63  ALA B C     1 
ATOM   2346 O O     . ALA B 1 83  ? -42.55100 5.94200   37.24500 1.000 28.07858 ?  63  ALA B O     1 
ATOM   2347 C CB    . ALA B 1 83  ? -40.39900 6.48300   39.51400 1.000 24.57661 ?  63  ALA B CB    1 
ATOM   2348 N N     . SER B 1 84  ? -41.43800 4.00600   37.56800 1.000 27.07074 ?  64  SER B N     1 
ATOM   2349 C CA    . SER B 1 84  ? -41.78700 3.49900   36.24200 1.000 28.27187 ?  64  SER B CA    1 
ATOM   2350 C C     . SER B 1 84  ? -43.28100 3.26000   36.13600 1.000 27.89966 ?  64  SER B C     1 
ATOM   2351 O O     . SER B 1 84  ? -43.93000 3.69700   35.17600 1.000 32.17938 ?  64  SER B O     1 
ATOM   2352 C CB    . SER B 1 84  ? -41.03300 2.20500   35.94600 1.000 27.51806 ?  64  SER B CB    1 
ATOM   2353 O OG    . SER B 1 84  ? -39.64000 2.39100   36.02900 1.000 31.52555 ?  64  SER B OG    1 
ATOM   2354 N N     . PHE B 1 85  ? -43.84200 2.56000   37.11900 1.000 27.47192 ?  65  PHE B N     1 
ATOM   2355 C CA    . PHE B 1 85  ? -45.28100 2.33100   37.14800 1.000 29.74768 ?  65  PHE B CA    1 
ATOM   2356 C C     . PHE B 1 85  ? -46.03700 3.65100   37.14000 1.000 32.41772 ?  65  PHE B C     1 
ATOM   2357 O O     . PHE B 1 85  ? -46.99400 3.82500   36.38100 1.000 33.63932 ?  65  PHE B O     1 
ATOM   2358 C CB    . PHE B 1 85  ? -45.65600 1.50400   38.37800 1.000 26.22759 ?  65  PHE B CB    1 
ATOM   2359 C CG    . PHE B 1 85  ? -45.20000 0.06600   38.31000 1.000 30.02977 ?  65  PHE B CG    1 
ATOM   2360 C CD1   . PHE B 1 85  ? -45.52100 -0.72600  37.22000 1.000 30.00996 ?  65  PHE B CD1   1 
ATOM   2361 C CD2   . PHE B 1 85  ? -44.45600 -0.48800  39.34000 1.000 28.13259 ?  65  PHE B CD2   1 
ATOM   2362 C CE1   . PHE B 1 85  ? -45.10900 -2.04600  37.15700 1.000 30.31843 ?  65  PHE B CE1   1 
ATOM   2363 C CE2   . PHE B 1 85  ? -44.04000 -1.80600  39.28900 1.000 32.30127 ?  65  PHE B CE2   1 
ATOM   2364 C CZ    . PHE B 1 85  ? -44.36500 -2.58900  38.18900 1.000 30.74333 ?  65  PHE B CZ    1 
ATOM   2365 N N     . GLU B 1 86  ? -45.60200 4.60600   37.96900 1.000 32.87304 ?  66  GLU B N     1 
ATOM   2366 C CA    . GLU B 1 86  ? -46.28600 5.89100   38.02600 1.000 30.94182 ?  66  GLU B CA    1 
ATOM   2367 C C     . GLU B 1 86  ? -46.15900 6.64800   36.70900 1.000 33.64886 ?  66  GLU B C     1 
ATOM   2368 O O     . GLU B 1 86  ? -47.10700 7.31900   36.27900 1.000 32.75723 ?  66  GLU B O     1 
ATOM   2369 C CB    . GLU B 1 86  ? -45.74900 6.73100   39.18800 1.000 31.16728 ?  66  GLU B CB    1 
ATOM   2370 C CG    . GLU B 1 86  ? -45.95200 6.12200   40.57600 1.000 30.84662 ?  66  GLU B CG    1 
ATOM   2371 C CD    . GLU B 1 86  ? -47.41200 6.09900   41.00800 1.000 35.43495 ?  66  GLU B CD    1 
ATOM   2372 O OE1   . GLU B 1 86  ? -48.29200 6.50300   40.21200 1.000 31.76466 ?  66  GLU B OE1   1 
ATOM   2373 O OE2   . GLU B 1 86  ? -47.68100 5.66900   42.14900 1.000 36.81201 -1 66  GLU B OE2   1 
ATOM   2374 N N     . LEU B 1 87  ? -44.99900 6.55600   36.05000 1.000 31.76647 ?  67  LEU B N     1 
ATOM   2375 C CA    . LEU B 1 87  ? -44.85400 7.21200   34.75200 1.000 33.34133 ?  67  LEU B CA    1 
ATOM   2376 C C     . LEU B 1 87  ? -45.68700 6.53200   33.67200 1.000 35.49344 ?  67  LEU B C     1 
ATOM   2377 O O     . LEU B 1 87  ? -46.05000 7.18300   32.68300 1.000 37.45759 ?  67  LEU B O     1 
ATOM   2378 C CB    . LEU B 1 87  ? -43.38800 7.24800   34.32300 1.000 29.42435 ?  67  LEU B CB    1 
ATOM   2379 C CG    . LEU B 1 87  ? -42.51400 8.28600   35.04100 1.000 30.65489 ?  67  LEU B CG    1 
ATOM   2380 C CD1   . LEU B 1 87  ? -41.04900 8.04100   34.73600 1.000 25.62495 ?  67  LEU B CD1   1 
ATOM   2381 C CD2   . LEU B 1 87  ? -42.91000 9.71500   34.68300 1.000 28.95511 ?  67  LEU B CD2   1 
ATOM   2382 N N     . ALA B 1 88  ? -46.01100 5.25000   33.84400 1.000 31.95960 ?  68  ALA B N     1 
ATOM   2383 C CA    . ALA B 1 88  ? -46.81100 4.54400   32.85000 1.000 35.96127 ?  68  ALA B CA    1 
ATOM   2384 C C     . ALA B 1 88  ? -48.26600 4.99100   32.84700 1.000 35.75707 ?  68  ALA B C     1 
ATOM   2385 O O     . ALA B 1 88  ? -48.98600 4.72300   31.87800 1.000 39.01209 ?  68  ALA B O     1 
ATOM   2386 C CB    . ALA B 1 88  ? -46.74000 3.03700   33.08700 1.000 35.69165 ?  68  ALA B CB    1 
ATOM   2387 N N     . ARG B 1 89  ? -48.72300 5.65500   33.90600 1.000 35.20051 ?  69  ARG B N     1 
ATOM   2388 C CA    . ARG B 1 89  ? -50.07000 6.20000   33.88200 1.000 37.61385 ?  69  ARG B CA    1 
ATOM   2389 C C     . ARG B 1 89  ? -50.21700 7.33200   32.87200 1.000 38.88515 ?  69  ARG B C     1 
ATOM   2390 O O     . ARG B 1 89  ? -51.34800 7.70200   32.54400 1.000 39.00078 ?  69  ARG B O     1 
ATOM   2391 C CB    . ARG B 1 89  ? -50.46300 6.68000   35.27900 1.000 33.74555 ?  69  ARG B CB    1 
ATOM   2392 C CG    . ARG B 1 89  ? -50.32500 5.61000   36.34500 1.000 36.65266 ?  69  ARG B CG    1 
ATOM   2393 C CD    . ARG B 1 89  ? -51.08700 5.97400   37.61300 1.000 39.80200 ?  69  ARG B CD    1 
ATOM   2394 N NE    . ARG B 1 89  ? -52.52100 5.74100   37.48100 1.000 45.09665 ?  69  ARG B NE    1 
ATOM   2395 C CZ    . ARG B 1 89  ? -53.45100 6.38200   38.17700 1.000 44.08146 ?  69  ARG B CZ    1 
ATOM   2396 N NH1   . ARG B 1 89  ? -53.13100 7.28000   39.09500 1.000 40.77787 ?  69  ARG B NH1   1 
ATOM   2397 N NH2   . ARG B 1 89  ? -54.73400 6.10800   37.95400 1.000 43.20642 ?  69  ARG B NH2   1 
ATOM   2398 N N     . SER B 1 90  ? -49.11300 7.87000   32.35300 1.000 37.88470 ?  70  SER B N     1 
ATOM   2399 C CA    . SER B 1 90  ? -49.16900 8.99800   31.43200 1.000 36.06998 ?  70  SER B CA    1 
ATOM   2400 C C     . SER B 1 90  ? -48.48900 8.74000   30.09500 1.000 39.53889 ?  70  SER B C     1 
ATOM   2401 O O     . SER B 1 90  ? -48.91700 9.30800   29.08800 1.000 40.23334 ?  70  SER B O     1 
ATOM   2402 C CB    . SER B 1 90  ? -48.54400 10.24300  32.08400 1.000 36.58280 ?  70  SER B CB    1 
ATOM   2403 O OG    . SER B 1 90  ? -48.16500 11.21100  31.11700 1.000 44.66328 ?  70  SER B OG    1 
ATOM   2404 N N     . TYR B 1 91  ? -47.45200 7.90400   30.05100 1.000 36.82439 ?  71  TYR B N     1 
ATOM   2405 C CA    . TYR B 1 91  ? -46.73000 7.61400   28.81900 1.000 35.50781 ?  71  TYR B CA    1 
ATOM   2406 C C     . TYR B 1 91  ? -47.22100 6.30200   28.21600 1.000 38.96498 ?  71  TYR B C     1 
ATOM   2407 O O     . TYR B 1 91  ? -47.70900 5.41400   28.92300 1.000 37.72496 ?  71  TYR B O     1 
ATOM   2408 C CB    . TYR B 1 91  ? -45.21500 7.54900   29.06900 1.000 36.08181 ?  71  TYR B CB    1 
ATOM   2409 C CG    . TYR B 1 91  ? -44.60600 8.90700   29.34900 1.000 34.60445 ?  71  TYR B CG    1 
ATOM   2410 C CD1   . TYR B 1 91  ? -44.74600 9.50800   30.59900 1.000 36.28806 ?  71  TYR B CD1   1 
ATOM   2411 C CD2   . TYR B 1 91  ? -43.91900 9.60400   28.36100 1.000 34.21816 ?  71  TYR B CD2   1 
ATOM   2412 C CE1   . TYR B 1 91  ? -44.21400 10.76100  30.85800 1.000 32.26392 ?  71  TYR B CE1   1 
ATOM   2413 C CE2   . TYR B 1 91  ? -43.38100 10.86200  28.61400 1.000 34.64504 ?  71  TYR B CE2   1 
ATOM   2414 C CZ    . TYR B 1 91  ? -43.53400 11.43100  29.86200 1.000 31.37323 ?  71  TYR B CZ    1 
ATOM   2415 O OH    . TYR B 1 91  ? -43.00700 12.67300  30.11900 1.000 34.82728 ?  71  TYR B OH    1 
ATOM   2416 N N     . LYS B 1 92  ? -47.10000 6.19200   26.89000 1.000 36.35621 ?  72  LYS B N     1 
ATOM   2417 C CA    . LYS B 1 92  ? -47.52400 4.96200   26.22200 1.000 39.17175 ?  72  LYS B CA    1 
ATOM   2418 C C     . LYS B 1 92  ? -46.60100 3.80300   26.57200 1.000 40.36282 ?  72  LYS B C     1 
ATOM   2419 O O     . LYS B 1 92  ? -47.05600 2.66200   26.73000 1.000 35.99343 ?  72  LYS B O     1 
ATOM   2420 C CB    . LYS B 1 92  ? -47.57700 5.16100   24.70500 1.000 36.62417 ?  72  LYS B CB    1 
ATOM   2421 C CG    . LYS B 1 92  ? -48.57200 6.21200   24.23700 1.000 40.14192 ?  72  LYS B CG    1 
ATOM   2422 N N     . HIS B 1 93  ? -45.30500 4.07500   26.70400 1.000 36.61131 ?  73  HIS B N     1 
ATOM   2423 C CA    . HIS B 1 93  ? -44.34200 3.05700   27.08700 1.000 36.29952 ?  73  HIS B CA    1 
ATOM   2424 C C     . HIS B 1 93  ? -43.32600 3.66400   28.04400 1.000 37.56394 ?  73  HIS B C     1 
ATOM   2425 O O     . HIS B 1 93  ? -42.91900 4.81800   27.88300 1.000 34.76176 ?  73  HIS B O     1 
ATOM   2426 C CB    . HIS B 1 93  ? -43.61600 2.46900   25.87600 1.000 36.43110 ?  73  HIS B CB    1 
ATOM   2427 C CG    . HIS B 1 93  ? -42.63900 1.39700   26.23600 1.000 35.59187 ?  73  HIS B CG    1 
ATOM   2428 N ND1   . HIS B 1 93  ? -43.03000 0.11800   26.57100 1.000 38.50073 ?  73  HIS B ND1   1 
ATOM   2429 C CD2   . HIS B 1 93  ? -41.29200 1.42600   26.36800 1.000 36.27962 ?  73  HIS B CD2   1 
ATOM   2430 C CE1   . HIS B 1 93  ? -41.96200 -0.60300  26.86800 1.000 36.79578 ?  73  HIS B CE1   1 
ATOM   2431 N NE2   . HIS B 1 93  ? -40.89500 0.16800   26.75500 1.000 39.27384 ?  73  HIS B NE2   1 
ATOM   2432 N N     . VAL B 1 94  ? -42.93200 2.88600   29.04600 1.000 35.33865 ?  74  VAL B N     1 
ATOM   2433 C CA    . VAL B 1 94  ? -41.92400 3.29500   30.01200 1.000 30.79656 ?  74  VAL B CA    1 
ATOM   2434 C C     . VAL B 1 94  ? -40.92600 2.16000   30.15300 1.000 33.67778 ?  74  VAL B C     1 
ATOM   2435 O O     . VAL B 1 94  ? -41.31600 1.01600   30.41300 1.000 33.18581 ?  74  VAL B O     1 
ATOM   2436 C CB    . VAL B 1 94  ? -42.52800 3.64400   31.38400 1.000 30.69247 ?  74  VAL B CB    1 
ATOM   2437 C CG1   . VAL B 1 94  ? -41.42100 3.83500   32.39900 1.000 31.21355 ?  74  VAL B CG1   1 
ATOM   2438 C CG2   . VAL B 1 94  ? -43.38200 4.89600   31.28900 1.000 29.27918 ?  74  VAL B CG2   1 
ATOM   2439 N N     . ASP B 1 95  ? -39.65000 2.47600   29.95200 1.000 32.85992 ?  75  ASP B N     1 
ATOM   2440 C CA    . ASP B 1 95  ? -38.54300 1.58700   30.27100 1.000 30.66274 ?  75  ASP B CA    1 
ATOM   2441 C C     . ASP B 1 95  ? -38.01000 1.93300   31.65500 1.000 29.48815 ?  75  ASP B C     1 
ATOM   2442 O O     . ASP B 1 95  ? -37.70200 3.09900   31.93700 1.000 27.66474 ?  75  ASP B O     1 
ATOM   2443 C CB    . ASP B 1 95  ? -37.42900 1.72200   29.23500 1.000 30.29658 ?  75  ASP B CB    1 
ATOM   2444 C CG    . ASP B 1 95  ? -37.84300 1.20700   27.88000 1.000 34.70265 ?  75  ASP B CG    1 
ATOM   2445 O OD1   . ASP B 1 95  ? -38.51300 0.14700   27.83100 1.000 33.52086 ?  75  ASP B OD1   1 
ATOM   2446 O OD2   . ASP B 1 95  ? -37.49300 1.85900   26.87400 1.000 32.88778 -1 75  ASP B OD2   1 
ATOM   2447 N N     . GLY B 1 96  ? -37.91700 0.93000   32.51800 1.000 27.89760 ?  76  GLY B N     1 
ATOM   2448 C CA    . GLY B 1 96  ? -37.22500 1.10700   33.78100 1.000 28.50117 ?  76  GLY B CA    1 
ATOM   2449 C C     . GLY B 1 96  ? -35.93200 0.31700   33.78800 1.000 31.91382 ?  76  GLY B C     1 
ATOM   2450 O O     . GLY B 1 96  ? -35.96200 -0.90600  33.62000 1.000 30.81902 ?  76  GLY B O     1 
ATOM   2451 N N     . VAL B 1 97  ? -34.79500 0.99000   33.96700 1.000 26.41282 ?  77  VAL B N     1 
ATOM   2452 C CA    . VAL B 1 97  ? -33.48600 0.34900   33.89400 1.000 28.57800 ?  77  VAL B CA    1 
ATOM   2453 C C     . VAL B 1 97  ? -32.75200 0.54900   35.21500 1.000 30.83018 ?  77  VAL B C     1 
ATOM   2454 O O     . VAL B 1 97  ? -32.78100 1.64400   35.79200 1.000 29.02682 ?  77  VAL B O     1 
ATOM   2455 C CB    . VAL B 1 97  ? -32.65800 0.90800   32.71900 1.000 28.02315 ?  77  VAL B CB    1 
ATOM   2456 C CG1   . VAL B 1 97  ? -31.20700 0.48100   32.82900 1.000 26.50733 ?  77  VAL B CG1   1 
ATOM   2457 C CG2   . VAL B 1 97  ? -33.25700 0.47500   31.38400 1.000 27.32899 ?  77  VAL B CG2   1 
ATOM   2458 N N     . ASP B 1 98  ? -32.09700 -0.51300  35.70100 1.000 29.55420 ?  78  ASP B N     1 
ATOM   2459 C CA    . ASP B 1 98  ? -31.26200 -0.39900  36.88700 1.000 29.12598 ?  78  ASP B CA    1 
ATOM   2460 C C     . ASP B 1 98  ? -30.03700 -1.29600  36.75800 1.000 31.03443 ?  78  ASP B C     1 
ATOM   2461 O O     . ASP B 1 98  ? -30.06900 -2.34600  36.10700 1.000 29.68752 ?  78  ASP B O     1 
ATOM   2462 C CB    . ASP B 1 98  ? -32.03500 -0.74800  38.17000 1.000 28.40635 ?  78  ASP B CB    1 
ATOM   2463 C CG    . ASP B 1 98  ? -31.40400 -0.13700  39.42300 1.000 30.78152 ?  78  ASP B CG    1 
ATOM   2464 O OD1   . ASP B 1 98  ? -30.50200 -0.77500  40.01300 1.000 30.24990 ?  78  ASP B OD1   1 
ATOM   2465 O OD2   . ASP B 1 98  ? -31.79800 0.98800   39.81200 1.000 29.13179 -1 78  ASP B OD2   1 
ATOM   2466 N N     . TYR B 1 99  ? -28.95300 -0.87400  37.40800 1.000 29.41919 ?  79  TYR B N     1 
ATOM   2467 C CA    . TYR B 1 99  ? -27.73400 -1.67100  37.40000 1.000 28.80467 ?  79  TYR B CA    1 
ATOM   2468 C C     . TYR B 1 99  ? -27.91400 -2.97200  38.17000 1.000 33.24856 ?  79  TYR B C     1 
ATOM   2469 O O     . TYR B 1 99  ? -27.25800 -3.97500  37.85800 1.000 32.62747 ?  79  TYR B O     1 
ATOM   2470 C CB    . TYR B 1 99  ? -26.58900 -0.84800  37.98300 1.000 27.59963 ?  79  TYR B CB    1 
ATOM   2471 C CG    . TYR B 1 99  ? -25.34800 -1.63800  38.33900 1.000 32.19500 ?  79  TYR B CG    1 
ATOM   2472 C CD1   . TYR B 1 99  ? -24.45100 -2.05200  37.35400 1.000 33.00401 ?  79  TYR B CD1   1 
ATOM   2473 C CD2   . TYR B 1 99  ? -25.05700 -1.95300  39.66100 1.000 33.60593 ?  79  TYR B CD2   1 
ATOM   2474 C CE1   . TYR B 1 99  ? -23.30100 -2.76500  37.68100 1.000 29.03634 ?  79  TYR B CE1   1 
ATOM   2475 C CE2   . TYR B 1 99  ? -23.90700 -2.66600  39.99600 1.000 35.75818 ?  79  TYR B CE2   1 
ATOM   2476 C CZ    . TYR B 1 99  ? -23.03800 -3.06800  39.00200 1.000 31.21508 ?  79  TYR B CZ    1 
ATOM   2477 O OH    . TYR B 1 99  ? -21.90500 -3.77100  39.33300 1.000 33.96324 ?  79  TYR B OH    1 
ATOM   2478 N N     . SER B 1 100 ? -28.80500 -2.98300  39.15600 1.000 30.01238 ?  80  SER B N     1 
ATOM   2479 C CA    . SER B 1 100 ? -28.96200 -4.12300  40.04500 1.000 31.16290 ?  80  SER B CA    1 
ATOM   2480 C C     . SER B 1 100 ? -29.97800 -5.10100  39.46100 1.000 31.70394 ?  80  SER B C     1 
ATOM   2481 O O     . SER B 1 100 ? -31.15900 -4.76100  39.30200 1.000 26.83650 ?  80  SER B O     1 
ATOM   2482 C CB    . SER B 1 100 ? -29.39700 -3.65200  41.43400 1.000 30.90158 ?  80  SER B CB    1 
ATOM   2483 O OG    . SER B 1 100 ? -30.00900 -4.70000  42.16400 1.000 31.39854 ?  80  SER B OG    1 
ATOM   2484 N N     . GLN B 1 101 ? -29.51600 -6.31900  39.15600 1.000 31.93195 ?  81  GLN B N     1 
ATOM   2485 C CA    . GLN B 1 101 ? -30.42900 -7.37700  38.73600 1.000 27.41875 ?  81  GLN B CA    1 
ATOM   2486 C C     . GLN B 1 101 ? -31.45500 -7.68000  39.81900 1.000 28.82714 ?  81  GLN B C     1 
ATOM   2487 O O     . GLN B 1 101 ? -32.61400 -7.98900  39.51700 1.000 30.61451 ?  81  GLN B O     1 
ATOM   2488 C CB    . GLN B 1 101 ? -29.64300 -8.64300  38.38000 1.000 33.94304 ?  81  GLN B CB    1 
ATOM   2489 C CG    . GLN B 1 101 ? -30.50200 -9.76100  37.78900 1.000 30.53259 ?  81  GLN B CG    1 
ATOM   2490 C CD    . GLN B 1 101 ? -31.06800 -9.40100  36.43700 1.000 34.84409 ?  81  GLN B CD    1 
ATOM   2491 O OE1   . GLN B 1 101 ? -30.32100 -9.14400  35.48800 1.000 35.41425 ?  81  GLN B OE1   1 
ATOM   2492 N NE2   . GLN B 1 101 ? -32.39500 -9.36600  36.33900 1.000 34.35085 ?  81  GLN B NE2   1 
ATOM   2493 N N     . ALA B 1 102 ? -31.04500 -7.61100  41.08900 1.000 27.62768 ?  82  ALA B N     1 
ATOM   2494 C CA    . ALA B 1 102 ? -31.97500 -7.90300  42.17500 1.000 31.29739 ?  82  ALA B CA    1 
ATOM   2495 C C     . ALA B 1 102 ? -33.11800 -6.89500  42.21200 1.000 31.81785 ?  82  ALA B C     1 
ATOM   2496 O O     . ALA B 1 102 ? -34.28300 -7.28200  42.37900 1.000 28.14169 ?  82  ALA B O     1 
ATOM   2497 C CB    . ALA B 1 102 ? -31.23600 -7.93800  43.51200 1.000 33.29527 ?  82  ALA B CB    1 
ATOM   2498 N N     . PHE B 1 103 ? -32.81300 -5.60500  42.03000 1.000 27.92193 ?  83  PHE B N     1 
ATOM   2499 C CA    . PHE B 1 103 ? -33.87300 -4.60600  41.94200 1.000 28.46630 ?  83  PHE B CA    1 
ATOM   2500 C C     . PHE B 1 103 ? -34.79800 -4.90000  40.76700 1.000 29.33857 ?  83  PHE B C     1 
ATOM   2501 O O     . PHE B 1 103 ? -36.02800 -4.83300  40.89200 1.000 31.36559 ?  83  PHE B O     1 
ATOM   2502 C CB    . PHE B 1 103 ? -33.27500 -3.20300  41.80000 1.000 28.54382 ?  83  PHE B CB    1 
ATOM   2503 C CG    . PHE B 1 103 ? -32.81800 -2.59500  43.09300 1.000 31.16131 ?  83  PHE B CG    1 
ATOM   2504 C CD1   . PHE B 1 103 ? -33.40200 -2.95600  44.29300 1.000 31.85576 ?  83  PHE B CD1   1 
ATOM   2505 C CD2   . PHE B 1 103 ? -31.82000 -1.62600  43.09900 1.000 31.71034 ?  83  PHE B CD2   1 
ATOM   2506 C CE1   . PHE B 1 103 ? -32.99000 -2.38100  45.47700 1.000 35.66455 ?  83  PHE B CE1   1 
ATOM   2507 C CE2   . PHE B 1 103 ? -31.40100 -1.05000  44.27300 1.000 31.72194 ?  83  PHE B CE2   1 
ATOM   2508 C CZ    . PHE B 1 103 ? -31.98400 -1.42700  45.46800 1.000 37.20333 ?  83  PHE B CZ    1 
ATOM   2509 N N     . VAL B 1 104 ? -34.21600 -5.22200  39.61200 1.000 27.78955 ?  84  VAL B N     1 
ATOM   2510 C CA    . VAL B 1 104 ? -35.00300 -5.46400  38.40600 1.000 29.07351 ?  84  VAL B CA    1 
ATOM   2511 C C     . VAL B 1 104 ? -35.94800 -6.64600  38.60500 1.000 33.77041 ?  84  VAL B C     1 
ATOM   2512 O O     . VAL B 1 104 ? -37.12200 -6.60100  38.20200 1.000 31.88458 ?  84  VAL B O     1 
ATOM   2513 C CB    . VAL B 1 104 ? -34.05700 -5.67500  37.21100 1.000 32.97765 ?  84  VAL B CB    1 
ATOM   2514 C CG1   . VAL B 1 104 ? -34.80900 -6.22000  36.00300 1.000 35.89676 ?  84  VAL B CG1   1 
ATOM   2515 C CG2   . VAL B 1 104 ? -33.33000 -4.36100  36.87900 1.000 31.42381 ?  84  VAL B CG2   1 
ATOM   2516 N N     . ASP B 1 105 ? -35.46000 -7.71500  39.24800 1.000 33.02211 ?  85  ASP B N     1 
ATOM   2517 C CA    . ASP B 1 105 ? -36.29400 -8.89300  39.47600 1.000 32.22595 ?  85  ASP B CA    1 
ATOM   2518 C C     . ASP B 1 105 ? -37.43200 -8.60400  40.44500 1.000 33.89434 ?  85  ASP B C     1 
ATOM   2519 O O     . ASP B 1 105 ? -38.52300 -9.17000  40.30500 1.000 31.47918 ?  85  ASP B O     1 
ATOM   2520 C CB    . ASP B 1 105 ? -35.44800 -10.05300 40.00000 1.000 32.68556 ?  85  ASP B CB    1 
ATOM   2521 C CG    . ASP B 1 105 ? -34.43500 -10.53600 38.98800 1.000 32.09995 ?  85  ASP B CG    1 
ATOM   2522 O OD1   . ASP B 1 105 ? -34.62600 -10.27700 37.78000 1.000 35.82867 ?  85  ASP B OD1   1 
ATOM   2523 O OD2   . ASP B 1 105 ? -33.44500 -11.16900 39.40300 1.000 36.48325 -1 85  ASP B OD2   1 
ATOM   2524 N N     . ALA B 1 106 ? -37.19800 -7.74700  41.44200 1.000 31.66822 ?  86  ALA B N     1 
ATOM   2525 C CA    . ALA B 1 106 ? -38.27700 -7.38000  42.34900 1.000 32.18906 ?  86  ALA B CA    1 
ATOM   2526 C C     . ALA B 1 106 ? -39.39100 -6.67200  41.59200 1.000 31.80169 ?  86  ALA B C     1 
ATOM   2527 O O     . ALA B 1 106 ? -40.56500 -7.04400  41.70400 1.000 31.57924 ?  86  ALA B O     1 
ATOM   2528 C CB    . ALA B 1 106 ? -37.74300 -6.50100  43.48300 1.000 33.50072 ?  86  ALA B CB    1 
ATOM   2529 N N     . ALA B 1 107 ? -39.02900 -5.65600  40.79700 1.000 32.53409 ?  87  ALA B N     1 
ATOM   2530 C CA    . ALA B 1 107 ? -40.01200 -4.92900  39.99600 1.000 33.67649 ?  87  ALA B CA    1 
ATOM   2531 C C     . ALA B 1 107 ? -40.73600 -5.86400  39.03200 1.000 34.59143 ?  87  ALA B C     1 
ATOM   2532 O O     . ALA B 1 107 ? -41.96800 -5.84700  38.94100 1.000 35.57385 ?  87  ALA B O     1 
ATOM   2533 C CB    . ALA B 1 107 ? -39.33100 -3.78400  39.23300 1.000 30.03125 ?  87  ALA B CB    1 
ATOM   2534 N N     . THR B 1 108 ? -39.97800 -6.68900  38.30900 1.000 32.20115 ?  88  THR B N     1 
ATOM   2535 C CA    . THR B 1 108 ? -40.57400 -7.63100  37.36900 1.000 34.64802 ?  88  THR B CA    1 
ATOM   2536 C C     . THR B 1 108 ? -41.52800 -8.59300  38.06600 1.000 36.31747 ?  88  THR B C     1 
ATOM   2537 O O     . THR B 1 108 ? -42.58800 -8.92900  37.52100 1.000 37.68758 ?  88  THR B O     1 
ATOM   2538 C CB    . THR B 1 108 ? -39.46900 -8.40400  36.65500 1.000 34.05890 ?  88  THR B CB    1 
ATOM   2539 O OG1   . THR B 1 108 ? -38.60200 -7.48100  35.98500 1.000 35.02017 ?  88  THR B OG1   1 
ATOM   2540 C CG2   . THR B 1 108 ? -40.05900 -9.37200  35.65300 1.000 35.69408 ?  88  THR B CG2   1 
ATOM   2541 N N     . GLU B 1 109 ? -41.16300 -9.05000  39.27100 1.000 34.96896 ?  89  GLU B N     1 
ATOM   2542 C CA    . GLU B 1 109 ? -42.01500 -9.97600  40.01200 1.000 34.97043 ?  89  GLU B CA    1 
ATOM   2543 C C     . GLU B 1 109 ? -43.32900 -9.32400  40.41800 1.000 40.62882 ?  89  GLU B C     1 
ATOM   2544 O O     . GLU B 1 109 ? -44.39800 -9.93800  40.29500 1.000 37.48152 ?  89  GLU B O     1 
ATOM   2545 C CB    . GLU B 1 109 ? -41.28000 -10.49500 41.24600 1.000 41.35252 ?  89  GLU B CB    1 
ATOM   2546 C CG    . GLU B 1 109 ? -40.65000 -11.86700 41.06700 1.000 47.56880 ?  89  GLU B CG    1 
ATOM   2547 C CD    . GLU B 1 109 ? -41.60600 -12.87800 40.43100 1.000 54.22731 ?  89  GLU B CD    1 
ATOM   2548 O OE1   . GLU B 1 109 ? -42.61400 -13.24400 41.08200 1.000 49.88217 ?  89  GLU B OE1   1 
ATOM   2549 O OE2   . GLU B 1 109 ? -41.34600 -13.30600 39.28100 1.000 55.30119 -1 89  GLU B OE2   1 
ATOM   2550 N N     . LEU B 1 110 ? -43.26700 -8.09100  40.93000 1.000 35.88348 ?  90  LEU B N     1 
ATOM   2551 C CA    . LEU B 1 110 ? -44.48800 -7.37700  41.28500 1.000 37.23419 ?  90  LEU B CA    1 
ATOM   2552 C C     . LEU B 1 110 ? -45.34400 -7.12000  40.05300 1.000 36.53948 ?  90  LEU B C     1 
ATOM   2553 O O     . LEU B 1 110 ? -46.57800 -7.16400  40.11800 1.000 40.09775 ?  90  LEU B O     1 
ATOM   2554 C CB    . LEU B 1 110 ? -44.14500 -6.05900  41.98100 1.000 33.98734 ?  90  LEU B CB    1 
ATOM   2555 C CG    . LEU B 1 110 ? -45.35000 -5.23300  42.43900 1.000 35.96944 ?  90  LEU B CG    1 
ATOM   2556 C CD1   . LEU B 1 110 ? -46.17800 -5.99500  43.46700 1.000 37.02432 ?  90  LEU B CD1   1 
ATOM   2557 C CD2   . LEU B 1 110 ? -44.89400 -3.88000  42.98400 1.000 37.67499 ?  90  LEU B CD2   1 
ATOM   2558 N N     . GLN B 1 111 ? -44.70000 -6.84800  38.92300 1.000 35.59782 ?  91  GLN B N     1 
ATOM   2559 C CA    . GLN B 1 111 ? -45.42000 -6.68300  37.66700 1.000 37.96489 ?  91  GLN B CA    1 
ATOM   2560 C C     . GLN B 1 111 ? -46.07300 -7.98900  37.23100 1.000 38.69138 ?  91  GLN B C     1 
ATOM   2561 O O     . GLN B 1 111 ? -47.26000 -8.01500  36.88600 1.000 38.43761 ?  91  GLN B O     1 
ATOM   2562 C CB    . GLN B 1 111 ? -44.45800 -6.18200  36.59200 1.000 35.28851 ?  91  GLN B CB    1 
ATOM   2563 C CG    . GLN B 1 111 ? -45.12800 -5.59600  35.36400 1.000 36.50550 ?  91  GLN B CG    1 
ATOM   2564 C CD    . GLN B 1 111 ? -44.12900 -5.33000  34.26700 1.000 35.79733 ?  91  GLN B CD    1 
ATOM   2565 O OE1   . GLN B 1 111 ? -43.05400 -5.93800  34.23600 1.000 30.12592 ?  91  GLN B OE1   1 
ATOM   2566 N NE2   . GLN B 1 111 ? -44.46100 -4.40800  33.36600 1.000 35.13088 ?  91  GLN B NE2   1 
ATOM   2567 N N     . LYS B 1 112 ? -45.31400 -9.08900  37.26500 1.000 38.67158 ?  92  LYS B N     1 
ATOM   2568 C CA    . LYS B 1 112 ? -45.80000 -10.36600 36.73900 1.000 40.77130 ?  92  LYS B CA    1 
ATOM   2569 C C     . LYS B 1 112 ? -46.80400 -11.02100 37.68200 1.000 42.22067 ?  92  LYS B C     1 
ATOM   2570 O O     . LYS B 1 112 ? -47.96800 -11.23300 37.32000 1.000 46.73365 ?  92  LYS B O     1 
ATOM   2571 C CB    . LYS B 1 112 ? -44.62400 -11.30400 36.47600 1.000 38.68770 ?  92  LYS B CB    1 
ATOM   2572 N N     . ASN B 1 113 ? -46.37100 -11.35700 38.89600 1.000 41.49280 ?  93  ASN B N     1 
ATOM   2573 C CA    . ASN B 1 113 ? -47.23200 -12.08300 39.82600 1.000 41.83575 ?  93  ASN B CA    1 
ATOM   2574 C C     . ASN B 1 113 ? -48.15500 -11.18400 40.64000 1.000 41.44087 ?  93  ASN B C     1 
ATOM   2575 O O     . ASN B 1 113 ? -49.09600 -11.69200 41.25500 1.000 39.96147 ?  93  ASN B O     1 
ATOM   2576 C CB    . ASN B 1 113 ? -46.38200 -12.93600 40.76600 1.000 42.77940 ?  93  ASN B CB    1 
ATOM   2577 C CG    . ASN B 1 113 ? -46.00200 -14.26500 40.15100 1.000 48.22165 ?  93  ASN B CG    1 
ATOM   2578 O OD1   . ASN B 1 113 ? -45.11000 -14.33600 39.30700 1.000 51.98872 ?  93  ASN B OD1   1 
ATOM   2579 N N     . GLY B 1 114 ? -47.92300 -9.87600  40.66900 1.000 38.20524 ?  94  GLY B N     1 
ATOM   2580 C CA    . GLY B 1 114 ? -48.83700 -8.99300  41.36600 1.000 39.09421 ?  94  GLY B CA    1 
ATOM   2581 C C     . GLY B 1 114 ? -48.60200 -8.85200  42.85400 1.000 42.04709 ?  94  GLY B C     1 
ATOM   2582 O O     . GLY B 1 114 ? -49.37800 -8.16100  43.52700 1.000 40.77058 ?  94  GLY B O     1 
ATOM   2583 N N     . CYS B 1 115 ? -47.55700 -9.47300  43.39100 1.000 41.37968 ?  95  CYS B N     1 
ATOM   2584 C CA    . CYS B 1 115 ? -47.26900 -9.35600  44.81100 1.000 41.07135 ?  95  CYS B CA    1 
ATOM   2585 C C     . CYS B 1 115 ? -45.81000 -9.71700  45.05900 1.000 42.00586 ?  95  CYS B C     1 
ATOM   2586 O O     . CYS B 1 115 ? -45.25800 -10.58700 44.37900 1.000 45.32946 ?  95  CYS B O     1 
ATOM   2587 C CB    . CYS B 1 115 ? -48.19800 -10.25400 45.63500 1.000 45.36369 ?  95  CYS B CB    1 
ATOM   2588 S SG    . CYS B 1 115 ? -47.75600 -11.99400 45.52900 1.000 57.14312 ?  95  CYS B SG    1 
ATOM   2589 N N     . ILE B 1 116 ? -45.19100 -9.03400  46.02800 1.000 37.15138 ?  96  ILE B N     1 
ATOM   2590 C CA    . ILE B 1 116 ? -43.86300 -9.37700  46.52400 1.000 36.62081 ?  96  ILE B CA    1 
ATOM   2591 C C     . ILE B 1 116 ? -43.84200 -9.16900  48.02700 1.000 32.29630 ?  96  ILE B C     1 
ATOM   2592 O O     . ILE B 1 116 ? -44.61300 -8.37900  48.58400 1.000 33.96261 ?  96  ILE B O     1 
ATOM   2593 C CB    . ILE B 1 116 ? -42.73200 -8.54800  45.88000 1.000 35.96407 ?  96  ILE B CB    1 
ATOM   2594 C CG1   . ILE B 1 116 ? -42.99700 -7.05700  46.09200 1.000 34.75184 ?  96  ILE B CG1   1 
ATOM   2595 C CG2   . ILE B 1 116 ? -42.59200 -8.87200  44.41300 1.000 40.39352 ?  96  ILE B CG2   1 
ATOM   2596 C CD1   . ILE B 1 116 ? -41.91200 -6.17500  45.54700 1.000 38.33327 ?  96  ILE B CD1   1 
ATOM   2597 N N     . GLY B 1 117 ? -42.94100 -9.88400  48.68500 1.000 33.58118 ?  97  GLY B N     1 
ATOM   2598 C CA    . GLY B 1 117 ? -42.76400 -9.78500  50.11900 1.000 37.94219 ?  97  GLY B CA    1 
ATOM   2599 C C     . GLY B 1 117 ? -41.39300 -9.23400  50.42100 1.000 41.44125 ?  97  GLY B C     1 
ATOM   2600 O O     . GLY B 1 117 ? -40.44700 -9.42300  49.64900 1.000 39.52253 ?  97  GLY B O     1 
ATOM   2601 N N     . TYR B 1 118 ? -41.27800 -8.52400  51.55000 1.000 35.97121 ?  98  TYR B N     1 
ATOM   2602 C CA    . TYR B 1 118 ? -40.02100 -7.88700  51.91200 1.000 38.59054 ?  98  TYR B CA    1 
ATOM   2603 C C     . TYR B 1 118 ? -39.90300 -7.79900  53.42700 1.000 39.96102 ?  98  TYR B C     1 
ATOM   2604 O O     . TYR B 1 118 ? -40.89700 -7.88700  54.15600 1.000 37.15956 ?  98  TYR B O     1 
ATOM   2605 C CB    . TYR B 1 118 ? -39.88200 -6.50000  51.25900 1.000 35.72251 ?  98  TYR B CB    1 
ATOM   2606 C CG    . TYR B 1 118 ? -40.73300 -5.38700  51.84100 1.000 32.78768 ?  98  TYR B CG    1 
ATOM   2607 C CD1   . TYR B 1 118 ? -40.30800 -4.65800  52.94900 1.000 36.31015 ?  98  TYR B CD1   1 
ATOM   2608 C CD2   . TYR B 1 118 ? -41.93900 -5.02800  51.25200 1.000 34.16209 ?  98  TYR B CD2   1 
ATOM   2609 C CE1   . TYR B 1 118 ? -41.07600 -3.62300  53.46800 1.000 36.82471 ?  98  TYR B CE1   1 
ATOM   2610 C CE2   . TYR B 1 118 ? -42.71100 -3.99300  51.76300 1.000 34.48423 ?  98  TYR B CE2   1 
ATOM   2611 C CZ    . TYR B 1 118 ? -42.27100 -3.29500  52.86800 1.000 33.06489 ?  98  TYR B CZ    1 
ATOM   2612 O OH    . TYR B 1 118 ? -43.03400 -2.27600  53.38100 1.000 37.70825 ?  98  TYR B OH    1 
ATOM   2613 N N     . SER B 1 119 ? -38.66200 -7.61500  53.88600 1.000 38.58730 ?  99  SER B N     1 
ATOM   2614 C CA    . SER B 1 119 ? -38.31400 -7.64400  55.30500 1.000 41.17742 ?  99  SER B CA    1 
ATOM   2615 C C     . SER B 1 119 ? -38.00300 -6.22500  55.77100 1.000 38.21383 ?  99  SER B C     1 
ATOM   2616 O O     . SER B 1 119 ? -36.91000 -5.70500  55.53200 1.000 47.38604 ?  99  SER B O     1 
ATOM   2617 C CB    . SER B 1 119 ? -37.13100 -8.58100  55.55400 1.000 38.44476 ?  99  SER B CB    1 
ATOM   2618 N N     . GLN B 1 120 ? -38.97300 -5.61200  56.43900 1.000 34.82125 ?  100 GLN B N     1 
ATOM   2619 C CA    . GLN B 1 120 ? -38.78400 -4.32700  57.09400 1.000 37.36643 ?  100 GLN B CA    1 
ATOM   2620 C C     . GLN B 1 120 ? -37.90900 -4.46400  58.34000 1.000 39.94170 ?  100 GLN B C     1 
ATOM   2621 O O     . GLN B 1 120 ? -38.08800 -5.38100  59.14400 1.000 36.60131 ?  100 GLN B O     1 
ATOM   2622 C CB    . GLN B 1 120 ? -40.14300 -3.76800  57.48800 1.000 39.65448 ?  100 GLN B CB    1 
ATOM   2623 C CG    . GLN B 1 120 ? -40.26000 -2.28300  57.49600 1.000 39.03964 ?  100 GLN B CG    1 
ATOM   2624 C CD    . GLN B 1 120 ? -41.61300 -1.86400  58.00500 1.000 43.47595 ?  100 GLN B CD    1 
ATOM   2625 O OE1   . GLN B 1 120 ? -42.07400 -2.37200  59.03200 1.000 38.85443 ?  100 GLN B OE1   1 
ATOM   2626 N NE2   . GLN B 1 120 ? -42.26800 -0.95000  57.29200 1.000 38.22621 ?  100 GLN B NE2   1 
ATOM   2627 N N     . ASN B 1 121 ? -36.97400 -3.53000  58.52100 1.000 35.70148 ?  101 ASN B N     1 
ATOM   2628 C CA    . ASN B 1 121 ? -36.09400 -3.56700  59.68600 1.000 32.79504 ?  101 ASN B CA    1 
ATOM   2629 C C     . ASN B 1 121 ? -36.76600 -2.98900  60.93000 1.000 35.14025 ?  101 ASN B C     1 
ATOM   2630 O O     . ASN B 1 121 ? -37.44800 -1.96000  60.87000 1.000 32.41021 ?  101 ASN B O     1 
ATOM   2631 C CB    . ASN B 1 121 ? -34.80400 -2.80300  59.39700 1.000 39.90322 ?  101 ASN B CB    1 
ATOM   2632 C CG    . ASN B 1 121 ? -33.86000 -3.57300  58.50000 1.000 42.63174 ?  101 ASN B CG    1 
ATOM   2633 O OD1   . ASN B 1 121 ? -34.16000 -4.68500  58.07800 1.000 46.01487 ?  101 ASN B OD1   1 
ATOM   2634 N ND2   . ASN B 1 121 ? -32.72100 -2.97500  58.18900 1.000 43.11232 ?  101 ASN B ND2   1 
ATOM   2635 N N     . GLY B 1 122 ? -36.57500 -3.66500  62.06300 1.000 31.48446 ?  102 GLY B N     1 
ATOM   2636 C CA    . GLY B 1 122 ? -36.98700 -3.13000  63.35000 1.000 32.01357 ?  102 GLY B CA    1 
ATOM   2637 C C     . GLY B 1 122 ? -35.80700 -2.86100  64.26900 1.000 36.61172 ?  102 GLY B C     1 
ATOM   2638 O O     . GLY B 1 122 ? -34.77000 -2.33200  63.83700 1.000 35.17198 ?  102 GLY B O     1 
ATOM   2639 N N     . GLU B 1 123 ? -35.95900 -3.22200  65.54300 1.000 34.72152 ?  103 GLU B N     1 
ATOM   2640 C CA    . GLU B 1 123 ? -34.88200 -3.10200  66.51900 1.000 30.97760 ?  103 GLU B CA    1 
ATOM   2641 C C     . GLU B 1 123 ? -33.79000 -4.13600  66.27400 1.000 33.38203 ?  103 GLU B C     1 
ATOM   2642 O O     . GLU B 1 123 ? -34.06700 -5.33700  66.22200 1.000 29.38941 ?  103 GLU B O     1 
ATOM   2643 C CB    . GLU B 1 123 ? -35.43100 -3.30300  67.92600 1.000 33.03879 ?  103 GLU B CB    1 
ATOM   2644 C CG    . GLU B 1 123 ? -35.57100 -2.08400  68.74500 1.000 29.27109 ?  103 GLU B CG    1 
ATOM   2645 C CD    . GLU B 1 123 ? -36.12400 -2.39900  70.10900 1.000 29.21664 ?  103 GLU B CD    1 
ATOM   2646 O OE1   . GLU B 1 123 ? -35.41200 -3.05600  70.89500 1.000 28.46156 ?  103 GLU B OE1   1 
ATOM   2647 O OE2   . GLU B 1 123 ? -37.27000 -1.99700  70.39700 1.000 31.82087 -1 103 GLU B OE2   1 
ATOM   2648 N N     . GLY B 1 124 ? -32.54300 -3.67200  66.17500 1.000 33.74038 ?  104 GLY B N     1 
ATOM   2649 C CA    . GLY B 1 124 ? -31.40700 -4.58200  66.08000 1.000 30.29727 ?  104 GLY B CA    1 
ATOM   2650 C C     . GLY B 1 124 ? -31.48600 -5.47200  64.85400 1.000 34.99125 ?  104 GLY B C     1 
ATOM   2651 O O     . GLY B 1 124 ? -31.49300 -4.99500  63.71500 1.000 30.84096 ?  104 GLY B O     1 
ATOM   2652 N N     . GLU B 1 125 ? -31.53700 -6.79000  65.07400 1.000 32.14210 ?  105 GLU B N     1 
ATOM   2653 C CA    . GLU B 1 125 ? -31.69200 -7.74900  63.98800 1.000 34.99671 ?  105 GLU B CA    1 
ATOM   2654 C C     . GLU B 1 125 ? -33.15100 -8.11900  63.72800 1.000 33.30891 ?  105 GLU B C     1 
ATOM   2655 O O     . GLU B 1 125 ? -33.42500 -8.86900  62.78900 1.000 35.99317 ?  105 GLU B O     1 
ATOM   2656 C CB    . GLU B 1 125 ? -30.88300 -9.03000  64.28200 1.000 32.66435 ?  105 GLU B CB    1 
ATOM   2657 C CG    . GLU B 1 125 ? -31.45900 -9.83400  65.45100 1.000 35.52335 ?  105 GLU B CG    1 
ATOM   2658 C CD    . GLU B 1 125 ? -30.78200 -11.18400 65.66300 1.000 39.16809 ?  105 GLU B CD    1 
ATOM   2659 O OE1   . GLU B 1 125 ? -29.73300 -11.44000 65.03700 1.000 43.86847 ?  105 GLU B OE1   1 
ATOM   2660 O OE2   . GLU B 1 125 ? -31.29900 -11.98900 66.47000 1.000 36.16522 -1 105 GLU B OE2   1 
ATOM   2661 N N     . LEU B 1 126 ? -34.09300 -7.61900  64.52200 1.000 31.54769 ?  106 LEU B N     1 
ATOM   2662 C CA    . LEU B 1 126 ? -35.48500 -8.01700  64.35800 1.000 33.29161 ?  106 LEU B CA    1 
ATOM   2663 C C     . LEU B 1 126 ? -36.05400 -7.45800  63.05800 1.000 35.28064 ?  106 LEU B C     1 
ATOM   2664 O O     . LEU B 1 126 ? -35.69800 -6.35300  62.63100 1.000 34.10223 ?  106 LEU B O     1 
ATOM   2665 C CB    . LEU B 1 126 ? -36.31500 -7.54100  65.54700 1.000 25.72113 ?  106 LEU B CB    1 
ATOM   2666 C CG    . LEU B 1 126 ? -35.80800 -8.09000  66.88000 1.000 31.72522 ?  106 LEU B CG    1 
ATOM   2667 C CD1   . LEU B 1 126 ? -36.63900 -7.54000  68.02300 1.000 30.19178 ?  106 LEU B CD1   1 
ATOM   2668 C CD2   . LEU B 1 126 ? -35.82800 -9.63600  66.86300 1.000 28.41144 ?  106 LEU B CD2   1 
ATOM   2669 N N     . LYS B 1 127 ? -36.92900 -8.25400  62.46000 1.000 33.23364 ?  107 LYS B N     1 
ATOM   2670 C CA    . LYS B 1 127 ? -37.50500 -7.87500  61.15500 1.000 36.31335 ?  107 LYS B CA    1 
ATOM   2671 C C     . LYS B 1 127 ? -39.02400 -8.03800  61.16200 1.000 40.85374 ?  107 LYS B C     1 
ATOM   2672 O O     . LYS B 1 127 ? -39.52100 -8.88100  61.91200 1.000 39.67989 ?  107 LYS B O     1 
ATOM   2673 C CB    . LYS B 1 127 ? -36.89200 -8.72300  60.04100 1.000 37.12550 ?  107 LYS B CB    1 
ATOM   2674 C CG    . LYS B 1 127 ? -35.37500 -8.79200  60.00300 1.000 39.89677 ?  107 LYS B CG    1 
ATOM   2675 C CD    . LYS B 1 127 ? -34.75700 -7.64600  59.25700 1.000 38.63005 ?  107 LYS B CD    1 
ATOM   2676 C CE    . LYS B 1 127 ? -33.26600 -7.54200  59.48700 1.000 44.27957 ?  107 LYS B CE    1 
ATOM   2677 N NZ    . LYS B 1 127 ? -32.58700 -6.88800  58.34900 1.000 43.05400 ?  107 LYS B NZ    1 
ATOM   2678 N N     . ASN B 1 128 ? -39.71200 -7.23200  60.36100 1.000 39.50392 ?  108 ASN B N     1 
ATOM   2679 C CA    . ASN B 1 128 ? -41.17900 -7.31200  60.20400 1.000 40.06413 ?  108 ASN B CA    1 
ATOM   2680 C C     . ASN B 1 128 ? -41.44200 -7.64200  58.73200 1.000 39.01444 ?  108 ASN B C     1 
ATOM   2681 O O     . ASN B 1 128 ? -40.95100 -6.92000  57.86800 1.000 40.32838 ?  108 ASN B O     1 
ATOM   2682 C CB    . ASN B 1 128 ? -41.84900 -6.00300  60.60900 1.000 36.18914 ?  108 ASN B CB    1 
ATOM   2683 C CG    . ASN B 1 128 ? -41.57900 -5.59200  62.03900 1.000 44.62844 ?  108 ASN B CG    1 
ATOM   2684 O OD1   . ASN B 1 128 ? -41.81800 -6.35700  62.96700 1.000 46.73665 ?  108 ASN B OD1   1 
ATOM   2685 N ND2   . ASN B 1 128 ? -41.09900 -4.37500  62.22700 1.000 47.55453 ?  108 ASN B ND2   1 
ATOM   2686 N N     . TYR B 1 129 ? -42.16700 -8.71500  58.46800 1.000 39.30005 ?  109 TYR B N     1 
ATOM   2687 C CA    . TYR B 1 129 ? -42.38700 -9.14000  57.06800 1.000 38.57252 ?  109 TYR B CA    1 
ATOM   2688 C C     . TYR B 1 129 ? -43.60100 -8.39700  56.51700 1.000 39.56859 ?  109 TYR B C     1 
ATOM   2689 O O     . TYR B 1 129 ? -44.57000 -8.20700  57.25400 1.000 40.45402 ?  109 TYR B O     1 
ATOM   2690 C CB    . TYR B 1 129 ? -42.50900 -10.66000 56.98300 1.000 45.94262 ?  109 TYR B CB    1 
ATOM   2691 C CG    . TYR B 1 129 ? -42.92000 -11.19700 55.63700 1.000 50.20905 ?  109 TYR B CG    1 
ATOM   2692 C CD1   . TYR B 1 129 ? -41.99400 -11.36300 54.62200 1.000 51.12596 ?  109 TYR B CD1   1 
ATOM   2693 C CD2   . TYR B 1 129 ? -44.23500 -11.54400 55.37600 1.000 56.24097 ?  109 TYR B CD2   1 
ATOM   2694 C CE1   . TYR B 1 129 ? -42.36300 -11.85600 53.38200 1.000 54.43246 ?  109 TYR B CE1   1 
ATOM   2695 C CE2   . TYR B 1 129 ? -44.62200 -12.03900 54.14300 1.000 56.51535 ?  109 TYR B CE2   1 
ATOM   2696 C CZ    . TYR B 1 129 ? -43.68100 -12.19600 53.14300 1.000 59.26858 ?  109 TYR B CZ    1 
ATOM   2697 O OH    . TYR B 1 129 ? -44.05100 -12.69000 51.91800 1.000 67.89348 ?  109 TYR B OH    1 
ATOM   2698 N N     . LYS B 1 130 ? -43.51500 -7.97300  55.26400 1.000 37.48499 ?  110 LYS B N     1 
ATOM   2699 C CA    . LYS B 1 130 ? -44.61400 -7.19300  54.64600 1.000 36.56598 ?  110 LYS B CA    1 
ATOM   2700 C C     . LYS B 1 130 ? -44.83600 -7.65700  53.20700 1.000 36.74317 ?  110 LYS B C     1 
ATOM   2701 O O     . LYS B 1 130 ? -43.89900 -8.17000  52.60900 1.000 37.18981 ?  110 LYS B O     1 
ATOM   2702 C CB    . LYS B 1 130 ? -44.31800 -5.68900  54.69500 1.000 38.02494 ?  110 LYS B CB    1 
ATOM   2703 C CG    . LYS B 1 130 ? -44.19300 -5.07500  56.08100 1.000 36.48450 ?  110 LYS B CG    1 
ATOM   2704 C CD    . LYS B 1 130 ? -45.50800 -4.57900  56.62100 1.000 39.65912 ?  110 LYS B CD    1 
ATOM   2705 C CE    . LYS B 1 130 ? -45.36600 -3.32900  57.46100 1.000 40.65004 ?  110 LYS B CE    1 
ATOM   2706 N N     . VAL B 1 131 ? -46.04300 -7.44400  52.69400 1.000 37.80521 ?  111 VAL B N     1 
ATOM   2707 C CA    . VAL B 1 131 ? -46.39700 -7.87800  51.31800 1.000 37.21216 ?  111 VAL B CA    1 
ATOM   2708 C C     . VAL B 1 131 ? -46.85700 -6.67000  50.50200 1.000 38.55811 ?  111 VAL B C     1 
ATOM   2709 O O     . VAL B 1 131 ? -47.69900 -5.91400  51.00100 1.000 38.11869 ?  111 VAL B O     1 
ATOM   2710 C CB    . VAL B 1 131 ? -47.48000 -8.97200  51.34100 1.000 39.75227 ?  111 VAL B CB    1 
ATOM   2711 C CG1   . VAL B 1 131 ? -47.95600 -9.32400  49.94100 1.000 40.27747 ?  111 VAL B CG1   1 
ATOM   2712 C CG2   . VAL B 1 131 ? -47.01200 -10.21900 52.07300 1.000 38.04550 ?  111 VAL B CG2   1 
ATOM   2713 N N     . ILE B 1 132 ? -46.30600 -6.49900  49.30400 1.000 35.78804 ?  112 ILE B N     1 
ATOM   2714 C CA    . ILE B 1 132 ? -46.78800 -5.42700  48.39200 1.000 35.78133 ?  112 ILE B CA    1 
ATOM   2715 C C     . ILE B 1 132 ? -47.76400 -6.05100  47.39900 1.000 37.82921 ?  112 ILE B C     1 
ATOM   2716 O O     . ILE B 1 132 ? -47.38000 -7.00100  46.73300 1.000 37.42492 ?  112 ILE B O     1 
ATOM   2717 C CB    . ILE B 1 132 ? -45.63600 -4.70900  47.66500 1.000 37.36677 ?  112 ILE B CB    1 
ATOM   2718 C CG1   . ILE B 1 132 ? -44.65100 -4.08500  48.65600 1.000 39.90737 ?  112 ILE B CG1   1 
ATOM   2719 C CG2   . ILE B 1 132 ? -46.16600 -3.68300  46.67900 1.000 33.95869 ?  112 ILE B CG2   1 
ATOM   2720 C CD1   . ILE B 1 132 ? -43.26900 -3.87800  48.09600 1.000 39.41744 ?  112 ILE B CD1   1 
ATOM   2721 N N     . ASP B 1 133 ? -48.96600 -5.50300  47.31300 1.000 38.55463 ?  113 ASP B N     1 
ATOM   2722 C CA    . ASP B 1 133 ? -49.98500 -5.97000  46.37900 1.000 37.99021 ?  113 ASP B CA    1 
ATOM   2723 C C     . ASP B 1 133 ? -50.15700 -4.94700  45.26100 1.000 38.17397 ?  113 ASP B C     1 
ATOM   2724 O O     . ASP B 1 133 ? -50.61400 -3.82900  45.50800 1.000 36.47402 ?  113 ASP B O     1 
ATOM   2725 C CB    . ASP B 1 133 ? -51.30900 -6.21100  47.10300 1.000 39.83257 ?  113 ASP B CB    1 
ATOM   2726 C CG    . ASP B 1 133 ? -52.39000 -6.79400  46.19300 1.000 46.37547 ?  113 ASP B CG    1 
ATOM   2727 O OD1   . ASP B 1 133 ? -52.12200 -7.07900  45.00400 1.000 47.13040 ?  113 ASP B OD1   1 
ATOM   2728 O OD2   . ASP B 1 133 ? -53.52200 -6.98400  46.68500 1.000 51.51992 -1 113 ASP B OD2   1 
ATOM   2729 N N     . ARG B 1 134 ? -49.79900 -5.35000  44.03800 1.000 40.15171 ?  114 ARG B N     1 
ATOM   2730 C CA    . ARG B 1 134 ? -49.91500 -4.48700  42.86500 1.000 39.45373 ?  114 ARG B CA    1 
ATOM   2731 C C     . ARG B 1 134 ? -51.28700 -3.83900  42.76900 1.000 41.80591 ?  114 ARG B C     1 
ATOM   2732 O O     . ARG B 1 134 ? -51.40100 -2.64400  42.47100 1.000 42.68510 ?  114 ARG B O     1 
ATOM   2733 C CB    . ARG B 1 134 ? -49.63200 -5.30700  41.60500 1.000 40.81228 ?  114 ARG B CB    1 
ATOM   2734 C CG    . ARG B 1 134 ? -49.42400 -4.50100  40.34100 1.000 40.21436 ?  114 ARG B CG    1 
ATOM   2735 C CD    . ARG B 1 134 ? -49.47400 -5.41300  39.12600 1.000 38.23852 ?  114 ARG B CD    1 
ATOM   2736 N NE    . ARG B 1 134 ? -50.66500 -6.25600  39.15000 1.000 41.85874 ?  114 ARG B NE    1 
ATOM   2737 C CZ    . ARG B 1 134 ? -50.74700 -7.47100  38.62100 1.000 45.43320 ?  114 ARG B CZ    1 
ATOM   2738 N NH1   . ARG B 1 134 ? -49.71000 -8.04300  38.02400 1.000 40.56184 ?  114 ARG B NH1   1 
ATOM   2739 N NH2   . ARG B 1 134 ? -51.89900 -8.13200  38.69100 1.000 42.34194 ?  114 ARG B NH2   1 
ATOM   2740 N N     . GLU B 1 135 ? -52.34100 -4.61100  43.03000 1.000 43.77744 ?  115 GLU B N     1 
ATOM   2741 C CA    . GLU B 1 135 ? -53.70200 -4.10000  42.92500 1.000 46.01623 ?  115 GLU B CA    1 
ATOM   2742 C C     . GLU B 1 135 ? -54.07000 -3.15100  44.05400 1.000 46.28610 ?  115 GLU B C     1 
ATOM   2743 O O     . GLU B 1 135 ? -55.19100 -2.62800  44.05600 1.000 46.94815 ?  115 GLU B O     1 
ATOM   2744 C CB    . GLU B 1 135 ? -54.69100 -5.26600  42.86800 1.000 49.82649 ?  115 GLU B CB    1 
ATOM   2745 C CG    . GLU B 1 135 ? -54.37400 -6.25200  41.75100 1.000 45.73411 ?  115 GLU B CG    1 
ATOM   2746 C CD    . GLU B 1 135 ? -54.48000 -5.60200  40.38000 1.000 51.61769 ?  115 GLU B CD    1 
ATOM   2747 O OE1   . GLU B 1 135 ? -55.50100 -4.93000  40.12600 1.000 50.31312 ?  115 GLU B OE1   1 
ATOM   2748 O OE2   . GLU B 1 135 ? -53.53800 -5.74500  39.56500 1.000 53.71759 -1 115 GLU B OE2   1 
ATOM   2749 N N     . GLY B 1 136 ? -53.16300 -2.90100  44.99400 1.000 42.61582 ?  116 GLY B N     1 
ATOM   2750 C CA    . GLY B 1 136 ? -53.40500 -1.91100  46.01500 1.000 38.94589 ?  116 GLY B CA    1 
ATOM   2751 C C     . GLY B 1 136 ? -53.08300 -0.48400  45.63500 1.000 41.28452 ?  116 GLY B C     1 
ATOM   2752 O O     . GLY B 1 136 ? -53.28500 0.41100   46.45900 1.000 39.75721 ?  116 GLY B O     1 
ATOM   2753 N N     . TYR B 1 137 ? -52.60300 -0.23100  44.41700 1.000 38.49611 ?  117 TYR B N     1 
ATOM   2754 C CA    . TYR B 1 137 ? -52.14300 1.09400   44.02100 1.000 36.64804 ?  117 TYR B CA    1 
ATOM   2755 C C     . TYR B 1 137 ? -52.80800 1.52600   42.72000 1.000 38.26371 ?  117 TYR B C     1 
ATOM   2756 O O     . TYR B 1 137 ? -53.14500 0.70000   41.86600 1.000 41.59481 ?  117 TYR B O     1 
ATOM   2757 C CB    . TYR B 1 137 ? -50.62300 1.13000   43.83600 1.000 34.50938 ?  117 TYR B CB    1 
ATOM   2758 C CG    . TYR B 1 137 ? -49.81700 0.63900   45.01400 1.000 33.95858 ?  117 TYR B CG    1 
ATOM   2759 C CD1   . TYR B 1 137 ? -49.62600 -0.72200  45.23500 1.000 36.73902 ?  117 TYR B CD1   1 
ATOM   2760 C CD2   . TYR B 1 137 ? -49.21900 1.53200   45.88700 1.000 35.68255 ?  117 TYR B CD2   1 
ATOM   2761 C CE1   . TYR B 1 137 ? -48.88000 -1.17700  46.30900 1.000 35.42873 ?  117 TYR B CE1   1 
ATOM   2762 C CE2   . TYR B 1 137 ? -48.46900 1.08900   46.97000 1.000 32.88758 ?  117 TYR B CE2   1 
ATOM   2763 C CZ    . TYR B 1 137 ? -48.30200 -0.26800  47.17300 1.000 35.53148 ?  117 TYR B CZ    1 
ATOM   2764 O OH    . TYR B 1 137 ? -47.55700 -0.71200  48.24800 1.000 34.76342 ?  117 TYR B OH    1 
ATOM   2765 N N     . ALA B 1 138 ? -52.96300 2.84100   42.56300 1.000 36.38016 ?  118 ALA B N     1 
ATOM   2766 C CA    . ALA B 1 138 ? -53.65200 3.37100   41.39200 1.000 38.63522 ?  118 ALA B CA    1 
ATOM   2767 C C     . ALA B 1 138 ? -52.93400 3.02200   40.09400 1.000 41.92751 ?  118 ALA B C     1 
ATOM   2768 O O     . ALA B 1 138 ? -53.58100 2.90900   39.04600 1.000 43.47814 ?  118 ALA B O     1 
ATOM   2769 C CB    . ALA B 1 138 ? -53.80700 4.88700   41.51500 1.000 40.24518 ?  118 ALA B CB    1 
ATOM   2770 N N     . PHE B 1 139 ? -51.60500 2.84500   40.13300 1.000 37.38081 ?  119 PHE B N     1 
ATOM   2771 C CA    . PHE B 1 139 ? -50.87700 2.50000   38.91500 1.000 36.38373 ?  119 PHE B CA    1 
ATOM   2772 C C     . PHE B 1 139 ? -51.21800 1.10300   38.41300 1.000 37.78870 ?  119 PHE B C     1 
ATOM   2773 O O     . PHE B 1 139 ? -50.65200 0.67400   37.40200 1.000 37.15442 ?  119 PHE B O     1 
ATOM   2774 C CB    . PHE B 1 139 ? -49.35100 2.64400   39.12500 1.000 35.68276 ?  119 PHE B CB    1 
ATOM   2775 C CG    . PHE B 1 139 ? -48.75400 1.66500   40.12600 1.000 37.85702 ?  119 PHE B CG    1 
ATOM   2776 C CD1   . PHE B 1 139 ? -48.69600 0.29600   39.85800 1.000 36.70372 ?  119 PHE B CD1   1 
ATOM   2777 C CD2   . PHE B 1 139 ? -48.24500 2.12000   41.33600 1.000 35.86282 ?  119 PHE B CD2   1 
ATOM   2778 C CE1   . PHE B 1 139 ? -48.15800 -0.58800  40.77100 1.000 35.34150 ?  119 PHE B CE1   1 
ATOM   2779 C CE2   . PHE B 1 139 ? -47.69500 1.23500   42.25500 1.000 31.21064 ?  119 PHE B CE2   1 
ATOM   2780 C CZ    . PHE B 1 139 ? -47.65500 -0.11700  41.97800 1.000 32.42767 ?  119 PHE B CZ    1 
ATOM   2781 N N     . ARG B 1 140 ? -52.10100 0.37400   39.10000 1.000 37.21504 ?  120 ARG B N     1 
ATOM   2782 C CA    . ARG B 1 140 ? -52.53400 -0.92300  38.59800 1.000 41.69933 ?  120 ARG B CA    1 
ATOM   2783 C C     . ARG B 1 140 ? -53.17700 -0.81900  37.21800 1.000 40.56572 ?  120 ARG B C     1 
ATOM   2784 O O     . ARG B 1 140 ? -53.20000 -1.81000  36.48200 1.000 40.82082 ?  120 ARG B O     1 
ATOM   2785 C CB    . ARG B 1 140 ? -53.49900 -1.57600  39.59000 1.000 39.15129 ?  120 ARG B CB    1 
ATOM   2786 C CG    . ARG B 1 140 ? -54.88200 -0.94300  39.64700 1.000 45.83425 ?  120 ARG B CG    1 
ATOM   2787 C CD    . ARG B 1 140 ? -55.55300 -1.26000  40.97600 1.000 49.54174 ?  120 ARG B CD    1 
ATOM   2788 N NE    . ARG B 1 140 ? -56.92900 -0.78700  41.04500 1.000 54.56696 ?  120 ARG B NE    1 
ATOM   2789 C CZ    . ARG B 1 140 ? -57.90500 -1.42500  41.67700 1.000 47.87506 ?  120 ARG B CZ    1 
ATOM   2790 N N     . ASP B 1 141 ? -53.66800 0.36200   36.83800 1.000 39.22274 ?  121 ASP B N     1 
ATOM   2791 C CA    . ASP B 1 141 ? -54.29900 0.54900   35.53700 1.000 43.14204 ?  121 ASP B CA    1 
ATOM   2792 C C     . ASP B 1 141 ? -53.30200 0.67000   34.38800 1.000 42.71234 ?  121 ASP B C     1 
ATOM   2793 O O     . ASP B 1 141 ? -53.73000 0.76600   33.23100 1.000 40.17439 ?  121 ASP B O     1 
ATOM   2794 C CB    . ASP B 1 141 ? -55.20100 1.79200   35.55500 1.000 39.92977 ?  121 ASP B CB    1 
ATOM   2795 C CG    . ASP B 1 141 ? -54.42200 3.08700   35.77400 1.000 46.62802 ?  121 ASP B CG    1 
ATOM   2796 O OD1   . ASP B 1 141 ? -53.17800 3.03800   35.92400 1.000 46.36483 ?  121 ASP B OD1   1 
ATOM   2797 O OD2   . ASP B 1 141 ? -55.05800 4.16400   35.79600 1.000 45.96014 -1 121 ASP B OD2   1 
ATOM   2798 N N     . SER B 1 142 ? -51.99100 0.67800   34.66300 1.000 39.56174 ?  122 SER B N     1 
ATOM   2799 C CA    . SER B 1 142 ? -51.03500 0.97200   33.60200 1.000 39.41290 ?  122 SER B CA    1 
ATOM   2800 C C     . SER B 1 142 ? -49.80200 0.08300   33.61400 1.000 35.77513 ?  122 SER B C     1 
ATOM   2801 O O     . SER B 1 142 ? -48.88300 0.32800   32.81900 1.000 37.21598 ?  122 SER B O     1 
ATOM   2802 C CB    . SER B 1 142 ? -50.59400 2.43800   33.67700 1.000 36.46853 ?  122 SER B CB    1 
ATOM   2803 O OG    . SER B 1 142 ? -51.69300 3.27600   33.97900 1.000 40.75613 ?  122 SER B OG    1 
ATOM   2804 N N     . PHE B 1 143 ? -49.75600 -0.95100  34.46100 1.000 37.54744 ?  123 PHE B N     1 
ATOM   2805 C CA    . PHE B 1 143 ? -48.49800 -1.65500  34.70100 1.000 33.21916 ?  123 PHE B CA    1 
ATOM   2806 C C     . PHE B 1 143 ? -48.04300 -2.48400  33.51200 1.000 37.57891 ?  123 PHE B C     1 
ATOM   2807 O O     . PHE B 1 143 ? -46.86100 -2.83100  33.43800 1.000 36.50296 ?  123 PHE B O     1 
ATOM   2808 C CB    . PHE B 1 143 ? -48.60200 -2.53800  35.95100 1.000 36.93229 ?  123 PHE B CB    1 
ATOM   2809 C CG    . PHE B 1 143 ? -49.51100 -3.73400  35.79600 1.000 37.41159 ?  123 PHE B CG    1 
ATOM   2810 C CD1   . PHE B 1 143 ? -49.05800 -4.90400  35.20100 1.000 37.34695 ?  123 PHE B CD1   1 
ATOM   2811 C CD2   . PHE B 1 143 ? -50.80700 -3.70000  36.28700 1.000 37.39745 ?  123 PHE B CD2   1 
ATOM   2812 C CE1   . PHE B 1 143 ? -49.90100 -6.00000  35.05900 1.000 39.62411 ?  123 PHE B CE1   1 
ATOM   2813 C CE2   . PHE B 1 143 ? -51.64500 -4.79400  36.16100 1.000 37.50343 ?  123 PHE B CE2   1 
ATOM   2814 C CZ    . PHE B 1 143 ? -51.19100 -5.94200  35.54500 1.000 40.68930 ?  123 PHE B CZ    1 
ATOM   2815 N N     . THR B 1 144 ? -48.93900 -2.81800  32.58400 1.000 35.56560 ?  124 THR B N     1 
ATOM   2816 C CA    . THR B 1 144 ? -48.50600 -3.56300  31.40700 1.000 34.43970 ?  124 THR B CA    1 
ATOM   2817 C C     . THR B 1 144 ? -47.70100 -2.71500  30.43400 1.000 36.71109 ?  124 THR B C     1 
ATOM   2818 O O     . THR B 1 144 ? -47.12700 -3.26700  29.49100 1.000 35.55836 ?  124 THR B O     1 
ATOM   2819 C CB    . THR B 1 144 ? -49.71400 -4.15500  30.68400 1.000 36.47420 ?  124 THR B CB    1 
ATOM   2820 O OG1   . THR B 1 144 ? -50.60800 -3.09900  30.31100 1.000 41.25475 ?  124 THR B OG1   1 
ATOM   2821 C CG2   . THR B 1 144 ? -50.44100 -5.12800  31.59700 1.000 39.05976 ?  124 THR B CG2   1 
ATOM   2822 N N     . LYS B 1 145 ? -47.64100 -1.40100  30.63600 1.000 36.29166 ?  125 LYS B N     1 
ATOM   2823 C CA    . LYS B 1 145 ? -46.96100 -0.50200  29.71900 1.000 34.31257 ?  125 LYS B CA    1 
ATOM   2824 C C     . LYS B 1 145 ? -45.50700 -0.26200  30.10100 1.000 36.14863 ?  125 LYS B C     1 
ATOM   2825 O O     . LYS B 1 145 ? -44.85500 0.60100   29.50300 1.000 33.90603 ?  125 LYS B O     1 
ATOM   2826 C CB    . LYS B 1 145 ? -47.72500 0.81800   29.64900 1.000 37.85242 ?  125 LYS B CB    1 
ATOM   2827 C CG    . LYS B 1 145 ? -49.22500 0.60300   29.44900 1.000 38.61207 ?  125 LYS B CG    1 
ATOM   2828 C CD    . LYS B 1 145 ? -50.02100 1.82800   29.84800 1.000 38.88162 ?  125 LYS B CD    1 
ATOM   2829 C CE    . LYS B 1 145 ? -49.78300 2.95400   28.87900 1.000 36.07063 ?  125 LYS B CE    1 
ATOM   2830 N NZ    . LYS B 1 145 ? -50.13500 4.25300   29.50900 1.000 39.72272 ?  125 LYS B NZ    1 
ATOM   2831 N N     . VAL B 1 146 ? -44.98900 -1.02700  31.06200 1.000 35.79714 ?  126 VAL B N     1 
ATOM   2832 C CA    . VAL B 1 146 ? -43.62300 -0.90600  31.55900 1.000 35.54951 ?  126 VAL B CA    1 
ATOM   2833 C C     . VAL B 1 146 ? -42.84500 -2.16000  31.19400 1.000 33.55958 ?  126 VAL B C     1 
ATOM   2834 O O     . VAL B 1 146 ? -43.36600 -3.27800  31.28900 1.000 35.44939 ?  126 VAL B O     1 
ATOM   2835 C CB    . VAL B 1 146 ? -43.58200 -0.69800  33.09200 1.000 35.06184 ?  126 VAL B CB    1 
ATOM   2836 C CG1   . VAL B 1 146 ? -42.13800 -0.61100  33.58400 1.000 33.40608 ?  126 VAL B CG1   1 
ATOM   2837 C CG2   . VAL B 1 146 ? -44.34200 0.55200   33.49600 1.000 32.96891 ?  126 VAL B CG2   1 
ATOM   2838 N N     . GLU B 1 147 ? -41.58500 -1.97000  30.81600 1.000 34.23022 ?  127 GLU B N     1 
ATOM   2839 C CA    . GLU B 1 147 ? -40.61100 -3.04600  30.71000 1.000 35.36496 ?  127 GLU B CA    1 
ATOM   2840 C C     . GLU B 1 147 ? -39.41000 -2.70800  31.58400 1.000 34.39743 ?  127 GLU B C     1 
ATOM   2841 O O     . GLU B 1 147 ? -38.86900 -1.60000  31.49000 1.000 32.59498 ?  127 GLU B O     1 
ATOM   2842 C CB    . GLU B 1 147 ? -40.16200 -3.22800  29.26600 1.000 38.65290 ?  127 GLU B CB    1 
ATOM   2843 C CG    . GLU B 1 147 ? -41.10400 -4.03200  28.40500 1.000 46.92074 ?  127 GLU B CG    1 
ATOM   2844 C CD    . GLU B 1 147 ? -40.48700 -4.34500  27.06400 1.000 49.14076 ?  127 GLU B CD    1 
ATOM   2845 O OE1   . GLU B 1 147 ? -40.63500 -3.51400  26.14200 1.000 52.29230 ?  127 GLU B OE1   1 
ATOM   2846 O OE2   . GLU B 1 147 ? -39.83800 -5.40800  26.94100 1.000 56.06603 -1 127 GLU B OE2   1 
ATOM   2847 N N     . PHE B 1 148 ? -39.00000 -3.65300  32.42600 1.000 31.41631 ?  128 PHE B N     1 
ATOM   2848 C CA    . PHE B 1 148 ? -37.84400 -3.49200  33.30200 1.000 32.49150 ?  128 PHE B CA    1 
ATOM   2849 C C     . PHE B 1 148 ? -36.63700 -4.23700  32.74500 1.000 38.00891 ?  128 PHE B C     1 
ATOM   2850 O O     . PHE B 1 148 ? -36.75500 -5.38500  32.30400 1.000 38.59594 ?  128 PHE B O     1 
ATOM   2851 C CB    . PHE B 1 148 ? -38.15600 -4.00500  34.70600 1.000 29.90989 ?  128 PHE B CB    1 
ATOM   2852 C CG    . PHE B 1 148 ? -39.17400 -3.17700  35.43700 1.000 34.41597 ?  128 PHE B CG    1 
ATOM   2853 C CD1   . PHE B 1 148 ? -38.87400 -1.87800  35.83800 1.000 28.53373 ?  128 PHE B CD1   1 
ATOM   2854 C CD2   . PHE B 1 148 ? -40.43200 -3.69200  35.72300 1.000 31.69567 ?  128 PHE B CD2   1 
ATOM   2855 C CE1   . PHE B 1 148 ? -39.80700 -1.11600  36.51100 1.000 27.07716 ?  128 PHE B CE1   1 
ATOM   2856 C CE2   . PHE B 1 148 ? -41.36600 -2.92700  36.40100 1.000 31.13100 ?  128 PHE B CE2   1 
ATOM   2857 C CZ    . PHE B 1 148 ? -41.05200 -1.64000  36.79200 1.000 31.19794 ?  128 PHE B CZ    1 
ATOM   2858 N N     . PHE B 1 149 ? -35.47200 -3.58500  32.77600 1.000 33.15430 ?  129 PHE B N     1 
ATOM   2859 C CA    . PHE B 1 149 ? -34.24900 -4.17400  32.24500 1.000 31.05288 ?  129 PHE B CA    1 
ATOM   2860 C C     . PHE B 1 149 ? -33.08700 -3.90400  33.19000 1.000 32.99326 ?  129 PHE B C     1 
ATOM   2861 O O     . PHE B 1 149 ? -33.02800 -2.85800  33.84200 1.000 30.02878 ?  129 PHE B O     1 
ATOM   2862 C CB    . PHE B 1 149 ? -33.86200 -3.60000  30.87400 1.000 32.10900 ?  129 PHE B CB    1 
ATOM   2863 C CG    . PHE B 1 149 ? -34.94000 -3.69300  29.82900 1.000 36.21567 ?  129 PHE B CG    1 
ATOM   2864 C CD1   . PHE B 1 149 ? -35.87900 -2.68400  29.69800 1.000 36.03998 ?  129 PHE B CD1   1 
ATOM   2865 C CD2   . PHE B 1 149 ? -34.99800 -4.77300  28.96300 1.000 39.76632 ?  129 PHE B CD2   1 
ATOM   2866 C CE1   . PHE B 1 149 ? -36.85900 -2.75100  28.72700 1.000 39.83623 ?  129 PHE B CE1   1 
ATOM   2867 C CE2   . PHE B 1 149 ? -35.98300 -4.84800  27.99600 1.000 40.15345 ?  129 PHE B CE2   1 
ATOM   2868 C CZ    . PHE B 1 149 ? -36.91300 -3.83300  27.87700 1.000 38.28943 ?  129 PHE B CZ    1 
ATOM   2869 N N     . GLN B 1 150 ? -32.15100 -4.84900  33.24400 1.000 30.02189 ?  130 GLN B N     1 
ATOM   2870 C CA    . GLN B 1 150 ? -30.84900 -4.56500  33.82200 1.000 31.62636 ?  130 GLN B CA    1 
ATOM   2871 C C     . GLN B 1 150 ? -30.02400 -3.80400  32.79700 1.000 30.90028 ?  130 GLN B C     1 
ATOM   2872 O O     . GLN B 1 150 ? -30.07000 -4.10800  31.60200 1.000 30.11406 ?  130 GLN B O     1 
ATOM   2873 C CB    . GLN B 1 150 ? -30.13200 -5.85100  34.22600 1.000 30.30519 ?  130 GLN B CB    1 
ATOM   2874 C CG    . GLN B 1 150 ? -28.91000 -5.63200  35.10800 1.000 32.76092 ?  130 GLN B CG    1 
ATOM   2875 C CD    . GLN B 1 150 ? -27.66200 -5.25700  34.32000 1.000 33.99347 ?  130 GLN B CD    1 
ATOM   2876 O OE1   . GLN B 1 150 ? -27.54000 -5.55700  33.12600 1.000 32.66149 ?  130 GLN B OE1   1 
ATOM   2877 N NE2   . GLN B 1 150 ? -26.72500 -4.59500  34.98700 1.000 31.90222 ?  130 GLN B NE2   1 
ATOM   2878 N N     . GLY B 1 151 ? -29.29000 -2.80200  33.26200 1.000 26.88369 ?  131 GLY B N     1 
ATOM   2879 C CA    . GLY B 1 151 ? -28.47600 -2.00000  32.36300 1.000 30.18675 ?  131 GLY B CA    1 
ATOM   2880 C C     . GLY B 1 151 ? -27.74100 -0.93100  33.14300 1.000 33.14692 ?  131 GLY B C     1 
ATOM   2881 O O     . GLY B 1 151 ? -27.99000 -0.71500  34.33400 1.000 29.16626 ?  131 GLY B O     1 
ATOM   2882 N N     . ASP B 1 152 ? -26.81800 -0.26600  32.44800 1.000 26.51462 ?  132 ASP B N     1 
ATOM   2883 C CA    . ASP B 1 152 ? -25.90900 0.69900   33.05300 1.000 26.28785 ?  132 ASP B CA    1 
ATOM   2884 C C     . ASP B 1 152 ? -26.12500 2.05900   32.41100 1.000 27.84010 ?  132 ASP B C     1 
ATOM   2885 O O     . ASP B 1 152 ? -26.07200 2.18400   31.18200 1.000 30.58806 ?  132 ASP B O     1 
ATOM   2886 C CB    . ASP B 1 152 ? -24.44800 0.25800   32.89600 1.000 27.34753 ?  132 ASP B CB    1 
ATOM   2887 C CG    . ASP B 1 152 ? -23.51300 0.96100   33.88500 1.000 30.20235 ?  132 ASP B CG    1 
ATOM   2888 O OD1   . ASP B 1 152 ? -23.59000 2.20400   34.00100 1.000 26.98192 ?  132 ASP B OD1   1 
ATOM   2889 O OD2   . ASP B 1 152 ? -22.70400 0.27300   34.55600 1.000 27.51728 -1 132 ASP B OD2   1 
ATOM   2890 N N     . ALA B 1 153 ? -26.35500 3.07200   33.24700 1.000 28.01150 ?  133 ALA B N     1 
ATOM   2891 C CA    . ALA B 1 153 ? -26.59200 4.42600   32.76000 1.000 26.44497 ?  133 ALA B CA    1 
ATOM   2892 C C     . ALA B 1 153 ? -25.38300 4.99100   32.03000 1.000 29.86066 ?  133 ALA B C     1 
ATOM   2893 O O     . ALA B 1 153 ? -25.52700 5.89900   31.20500 1.000 28.21583 ?  133 ALA B O     1 
ATOM   2894 C CB    . ALA B 1 153 ? -26.96700 5.34500   33.92500 1.000 24.69574 ?  133 ALA B CB    1 
ATOM   2895 N N     . CYS B 1 154 ? -24.18700 4.49400   32.33100 1.000 26.26702 ?  134 CYS B N     1 
ATOM   2896 C CA    . CYS B 1 154 ? -22.98400 4.95900   31.65200 1.000 29.10856 ?  134 CYS B CA    1 
ATOM   2897 C C     . CYS B 1 154 ? -22.65600 4.15500   30.40100 1.000 28.27374 ?  134 CYS B C     1 
ATOM   2898 O O     . CYS B 1 154 ? -21.64500 4.43800   29.75600 1.000 28.80058 ?  134 CYS B O     1 
ATOM   2899 C CB    . CYS B 1 154 ? -21.78400 4.91900   32.59700 1.000 28.44512 ?  134 CYS B CB    1 
ATOM   2900 S SG    . CYS B 1 154 ? -21.98700 5.90500   34.09100 1.000 29.22177 ?  134 CYS B SG    1 
ATOM   2901 N N     . ASN B 1 155 ? -23.47900 3.17000   30.04000 1.000 29.92599 ?  135 ASN B N     1 
ATOM   2902 C CA    . ASN B 1 155 ? -23.23800 2.34700   28.85800 1.000 32.32116 ?  135 ASN B CA    1 
ATOM   2903 C C     . ASN B 1 155 ? -24.55400 1.75300   28.36900 1.000 33.25190 ?  135 ASN B C     1 
ATOM   2904 O O     . ASN B 1 155 ? -24.69200 0.52900   28.26600 1.000 33.61115 ?  135 ASN B O     1 
ATOM   2905 C CB    . ASN B 1 155 ? -22.21900 1.24400   29.17600 1.000 32.99329 ?  135 ASN B CB    1 
ATOM   2906 C CG    . ASN B 1 155 ? -21.65000 0.58300   27.92900 1.000 33.69826 ?  135 ASN B CG    1 
ATOM   2907 O OD1   . ASN B 1 155 ? -21.34100 1.24700   26.93600 1.000 34.72880 ?  135 ASN B OD1   1 
ATOM   2908 N ND2   . ASN B 1 155 ? -21.49400 -0.73800  27.98700 1.000 31.98668 ?  135 ASN B ND2   1 
ATOM   2909 N N     . LEU B 1 156 ? -25.53000 2.61600   28.08900 1.000 34.79251 ?  136 LEU B N     1 
ATOM   2910 C CA    . LEU B 1 156 ? -26.86000 2.15400   27.72000 1.000 34.63758 ?  136 LEU B CA    1 
ATOM   2911 C C     . LEU B 1 156 ? -26.84100 1.51100   26.34100 1.000 40.68546 ?  136 LEU B C     1 
ATOM   2912 O O     . LEU B 1 156 ? -26.22900 2.02800   25.40000 1.000 34.15064 ?  136 LEU B O     1 
ATOM   2913 C CB    . LEU B 1 156 ? -27.86000 3.30700   27.72600 1.000 33.01922 ?  136 LEU B CB    1 
ATOM   2914 C CG    . LEU B 1 156 ? -28.39500 3.72200   29.10100 1.000 36.28616 ?  136 LEU B CG    1 
ATOM   2915 C CD1   . LEU B 1 156 ? -29.33700 4.90900   28.98400 1.000 29.12485 ?  136 LEU B CD1   1 
ATOM   2916 C CD2   . LEU B 1 156 ? -29.06500 2.55700   29.80800 1.000 31.78218 ?  136 LEU B CD2   1 
ATOM   2917 N N     . THR B 1 157 ? -27.52400 0.37400   26.23800 1.000 38.02196 ?  137 THR B N     1 
ATOM   2918 C CA    . THR B 1 157 ? -27.71000 -0.31700  24.97700 1.000 40.03091 ?  137 THR B CA    1 
ATOM   2919 C C     . THR B 1 157 ? -28.37800 0.60800   23.95600 1.000 41.47370 ?  137 THR B C     1 
ATOM   2920 O O     . THR B 1 157 ? -29.11500 1.52700   24.32700 1.000 39.47478 ?  137 THR B O     1 
ATOM   2921 C CB    . THR B 1 157 ? -28.55000 -1.57100  25.22400 1.000 37.10841 ?  137 THR B CB    1 
ATOM   2922 O OG1   . THR B 1 157 ? -27.85100 -2.42000  26.12900 1.000 47.35533 ?  137 THR B OG1   1 
ATOM   2923 C CG2   . THR B 1 157 ? -28.84600 -2.32000  23.94300 1.000 45.54917 ?  137 THR B CG2   1 
ATOM   2924 N N     . PRO B 1 158 ? -28.11300 0.41000   22.65900 1.000 42.73615 ?  138 PRO B N     1 
ATOM   2925 C CA    . PRO B 1 158 ? -28.63100 1.35700   21.65500 1.000 38.50728 ?  138 PRO B CA    1 
ATOM   2926 C C     . PRO B 1 158 ? -30.14900 1.38400   21.53900 1.000 41.27400 ?  138 PRO B C     1 
ATOM   2927 O O     . PRO B 1 158 ? -30.69000 2.39200   21.06800 1.000 44.01640 ?  138 PRO B O     1 
ATOM   2928 C CB    . PRO B 1 158 ? -27.98300 0.87300   20.35100 1.000 42.16730 ?  138 PRO B CB    1 
ATOM   2929 C CG    . PRO B 1 158 ? -26.75700 0.13900   20.80100 1.000 41.01580 ?  138 PRO B CG    1 
ATOM   2930 C CD    . PRO B 1 158 ? -27.18800 -0.56400  22.05800 1.000 39.89722 ?  138 PRO B CD    1 
ATOM   2931 N N     . GLN B 1 159 ? -30.85900 0.32800   21.94900 1.000 39.52645 ?  139 GLN B N     1 
ATOM   2932 C CA    . GLN B 1 159 ? -32.31600 0.34100   21.84100 1.000 37.40241 ?  139 GLN B CA    1 
ATOM   2933 C C     . GLN B 1 159 ? -32.96400 1.34800   22.78900 1.000 42.98421 ?  139 GLN B C     1 
ATOM   2934 O O     . GLN B 1 159 ? -34.12800 1.72200   22.58300 1.000 38.28701 ?  139 GLN B O     1 
ATOM   2935 C CB    . GLN B 1 159 ? -32.88000 -1.05700  22.10400 1.000 32.77795 ?  139 GLN B CB    1 
ATOM   2936 N N     . PHE B 1 160 ? -32.24400 1.78900   23.82400 1.000 39.46185 ?  140 PHE B N     1 
ATOM   2937 C CA    . PHE B 1 160 ? -32.78600 2.72200   24.80900 1.000 36.59198 ?  140 PHE B CA    1 
ATOM   2938 C C     . PHE B 1 160 ? -32.58100 4.12700   24.26200 1.000 35.00820 ?  140 PHE B C     1 
ATOM   2939 O O     . PHE B 1 160 ? -31.65100 4.85300   24.62200 1.000 33.77604 ?  140 PHE B O     1 
ATOM   2940 C CB    . PHE B 1 160 ? -32.12700 2.51900   26.16500 1.000 35.16237 ?  140 PHE B CB    1 
ATOM   2941 C CG    . PHE B 1 160 ? -32.47900 1.21000   26.80800 1.000 38.66143 ?  140 PHE B CG    1 
ATOM   2942 C CD1   . PHE B 1 160 ? -33.73300 1.00500   27.34900 1.000 37.21387 ?  140 PHE B CD1   1 
ATOM   2943 C CD2   . PHE B 1 160 ? -31.56600 0.17600   26.84800 1.000 42.26205 ?  140 PHE B CD2   1 
ATOM   2944 C CE1   . PHE B 1 160 ? -34.06800 -0.20200  27.93200 1.000 38.31170 ?  140 PHE B CE1   1 
ATOM   2945 C CE2   . PHE B 1 160 ? -31.89300 -1.03600  27.42700 1.000 42.96237 ?  140 PHE B CE2   1 
ATOM   2946 C CZ    . PHE B 1 160 ? -33.14600 -1.22400  27.96900 1.000 41.55267 ?  140 PHE B CZ    1 
ATOM   2947 N N     . LYS B 1 161 ? -33.48300 4.50600   23.36700 1.000 32.89271 ?  141 LYS B N     1 
ATOM   2948 C CA    . LYS B 1 161 ? -33.35800 5.73900   22.61400 1.000 34.16741 ?  141 LYS B CA    1 
ATOM   2949 C C     . LYS B 1 161 ? -34.74900 6.31100   22.39200 1.000 34.57594 ?  141 LYS B C     1 
ATOM   2950 O O     . LYS B 1 161 ? -35.75600 5.71300   22.78100 1.000 34.43376 ?  141 LYS B O     1 
ATOM   2951 C CB    . LYS B 1 161 ? -32.63400 5.48900   21.28400 1.000 37.25519 ?  141 LYS B CB    1 
ATOM   2952 C CG    . LYS B 1 161 ? -33.34300 4.49500   20.38100 1.000 37.46768 ?  141 LYS B CG    1 
ATOM   2953 C CD    . LYS B 1 161 ? -32.68700 4.40500   19.01000 1.000 39.87159 ?  141 LYS B CD    1 
ATOM   2954 N N     . GLU B 1 162 ? -34.78600 7.48600   21.76400 1.000 34.16240 ?  142 GLU B N     1 
ATOM   2955 C CA    . GLU B 1 162 ? -36.02400 8.14100   21.34000 1.000 38.54529 ?  142 GLU B CA    1 
ATOM   2956 C C     . GLU B 1 162 ? -37.00000 8.31200   22.50100 1.000 35.13359 ?  142 GLU B C     1 
ATOM   2957 O O     . GLU B 1 162 ? -38.18200 7.98100   22.41100 1.000 36.56388 ?  142 GLU B O     1 
ATOM   2958 C CB    . GLU B 1 162 ? -36.67200 7.38200   20.17800 1.000 37.45940 ?  142 GLU B CB    1 
ATOM   2959 C CG    . GLU B 1 162 ? -35.83000 7.42000   18.91000 1.000 41.16960 ?  142 GLU B CG    1 
ATOM   2960 C CD    . GLU B 1 162 ? -36.44900 6.64600   17.75900 1.000 49.67300 ?  142 GLU B CD    1 
ATOM   2961 O OE1   . GLU B 1 162 ? -37.14200 5.64000   18.01800 1.000 51.03690 ?  142 GLU B OE1   1 
ATOM   2962 O OE2   . GLU B 1 162 ? -36.23300 7.04100   16.59500 1.000 54.86902 -1 142 GLU B OE2   1 
ATOM   2963 N N     . TYR B 1 163 ? -36.50000 8.85700   23.60100 1.000 35.68041 ?  143 TYR B N     1 
ATOM   2964 C CA    . TYR B 1 163 ? -37.35000 9.13500   24.74500 1.000 30.43709 ?  143 TYR B CA    1 
ATOM   2965 C C     . TYR B 1 163 ? -37.84700 10.56800  24.70000 1.000 36.26002 ?  143 TYR B C     1 
ATOM   2966 O O     . TYR B 1 163 ? -37.10100 11.49700  24.37200 1.000 34.57972 ?  143 TYR B O     1 
ATOM   2967 C CB    . TYR B 1 163 ? -36.60100 8.88200   26.05100 1.000 30.56924 ?  143 TYR B CB    1 
ATOM   2968 C CG    . TYR B 1 163 ? -36.33400 7.41500   26.26200 1.000 31.05928 ?  143 TYR B CG    1 
ATOM   2969 C CD1   . TYR B 1 163 ? -37.35200 6.55500   26.63800 1.000 31.50848 ?  143 TYR B CD1   1 
ATOM   2970 C CD2   . TYR B 1 163 ? -35.06600 6.88200   26.04200 1.000 31.39394 ?  143 TYR B CD2   1 
ATOM   2971 C CE1   . TYR B 1 163 ? -37.11200 5.19700   26.82200 1.000 28.39415 ?  143 TYR B CE1   1 
ATOM   2972 C CE2   . TYR B 1 163 ? -34.81600 5.53700   26.22100 1.000 29.85296 ?  143 TYR B CE2   1 
ATOM   2973 C CZ    . TYR B 1 163 ? -35.83900 4.69500   26.60700 1.000 30.88586 ?  143 TYR B CZ    1 
ATOM   2974 O OH    . TYR B 1 163 ? -35.58100 3.34500   26.77500 1.000 31.50190 ?  143 TYR B OH    1 
ATOM   2975 N N     . ASP B 1 164 ? -39.12600 10.73600  25.00900 1.000 34.11584 ?  144 ASP B N     1 
ATOM   2976 C CA    . ASP B 1 164 ? -39.63600 12.05900  25.30800 1.000 33.39296 ?  144 ASP B CA    1 
ATOM   2977 C C     . ASP B 1 164 ? -39.21900 12.51200  26.69400 1.000 34.17157 ?  144 ASP B C     1 
ATOM   2978 O O     . ASP B 1 164 ? -39.12000 13.71900  26.93600 1.000 31.77995 ?  144 ASP B O     1 
ATOM   2979 C CB    . ASP B 1 164 ? -41.15500 12.06100  25.17300 1.000 35.20342 ?  144 ASP B CB    1 
ATOM   2980 C CG    . ASP B 1 164 ? -41.61300 11.40400  23.88600 1.000 40.70497 ?  144 ASP B CG    1 
ATOM   2981 O OD1   . ASP B 1 164 ? -41.15000 11.84700  22.80900 1.000 38.70319 ?  144 ASP B OD1   1 
ATOM   2982 O OD2   . ASP B 1 164 ? -42.41300 10.43900  23.95200 1.000 38.93810 -1 144 ASP B OD2   1 
ATOM   2983 N N     . LEU B 1 165 ? -38.94700 11.57000  27.59900 1.000 30.94212 ?  145 LEU B N     1 
ATOM   2984 C CA    . LEU B 1 165 ? -38.49600 11.91300  28.93900 1.000 27.60772 ?  145 LEU B CA    1 
ATOM   2985 C C     . LEU B 1 165 ? -37.51200 10.86400  29.43900 1.000 31.08137 ?  145 LEU B C     1 
ATOM   2986 O O     . LEU B 1 165 ? -37.76200 9.65900   29.31300 1.000 27.27470 ?  145 LEU B O     1 
ATOM   2987 C CB    . LEU B 1 165 ? -39.68600 12.03400  29.89400 1.000 26.16807 ?  145 LEU B CB    1 
ATOM   2988 C CG    . LEU B 1 165 ? -39.31600 11.97700  31.37300 1.000 29.90048 ?  145 LEU B CG    1 
ATOM   2989 C CD1   . LEU B 1 165 ? -38.71100 13.30600  31.83100 1.000 27.16055 ?  145 LEU B CD1   1 
ATOM   2990 C CD2   . LEU B 1 165 ? -40.52000 11.60900  32.21600 1.000 25.50381 ?  145 LEU B CD2   1 
ATOM   2991 N N     . ILE B 1 166 ? -36.38600 11.32400  29.98000 1.000 24.90192 ?  146 ILE B N     1 
ATOM   2992 C CA    . ILE B 1 166 ? -35.48000 10.47800  30.74300 1.000 27.84085 ?  146 ILE B CA    1 
ATOM   2993 C C     . ILE B 1 166 ? -35.41000 11.04900  32.15300 1.000 30.38008 ?  146 ILE B C     1 
ATOM   2994 O O     . ILE B 1 166 ? -34.97000 12.18800  32.34500 1.000 28.44450 ?  146 ILE B O     1 
ATOM   2995 C CB    . ILE B 1 166 ? -34.08300 10.39800  30.11000 1.000 31.54319 ?  146 ILE B CB    1 
ATOM   2996 C CG1   . ILE B 1 166 ? -34.17400 9.82500   28.69200 1.000 28.90963 ?  146 ILE B CG1   1 
ATOM   2997 C CG2   . ILE B 1 166 ? -33.15500 9.54600   30.98000 1.000 25.40773 ?  146 ILE B CG2   1 
ATOM   2998 C CD1   . ILE B 1 166 ? -32.84200 9.38700   28.12300 1.000 27.54289 ?  146 ILE B CD1   1 
ATOM   2999 N N     . MET B 1 167 ? -35.87000 10.27400  33.12700 1.000 30.56869 ?  147 MET B N     1 
ATOM   3000 C CA    . MET B 1 167 ? -35.86300 10.67200  34.52600 1.000 28.77348 ?  147 MET B CA    1 
ATOM   3001 C C     . MET B 1 167 ? -34.88200 9.79200   35.28100 1.000 28.60043 ?  147 MET B C     1 
ATOM   3002 O O     . MET B 1 167 ? -34.98700 8.56400   35.23600 1.000 25.24788 ?  147 MET B O     1 
ATOM   3003 C CB    . MET B 1 167 ? -37.26000 10.56000  35.14000 1.000 26.37259 ?  147 MET B CB    1 
ATOM   3004 C CG    . MET B 1 167 ? -37.37100 11.26400  36.49500 1.000 29.24940 ?  147 MET B CG    1 
ATOM   3005 S SD    . MET B 1 167 ? -39.00100 11.10100  37.25200 1.000 35.17648 ?  147 MET B SD    1 
ATOM   3006 C CE    . MET B 1 167 ? -39.09600 9.34300   37.59600 1.000 26.99303 ?  147 MET B CE    1 
ATOM   3007 N N     . ALA B 1 168 ? -33.91900 10.41800  35.95500 1.000 27.00024 ?  148 ALA B N     1 
ATOM   3008 C CA    . ALA B 1 168 ? -32.89800 9.69800   36.71300 1.000 30.41381 ?  148 ALA B CA    1 
ATOM   3009 C C     . ALA B 1 168 ? -32.84400 10.34700  38.09300 1.000 30.62719 ?  148 ALA B C     1 
ATOM   3010 O O     . ALA B 1 168 ? -32.16000 11.35900  38.28700 1.000 27.67671 ?  148 ALA B O     1 
ATOM   3011 C CB    . ALA B 1 168 ? -31.55200 9.73700   36.00000 1.000 26.49461 ?  148 ALA B CB    1 
ATOM   3012 N N     . THR B 1 169 ? -33.58200 9.77400   39.04700 1.000 27.41154 ?  149 THR B N     1 
ATOM   3013 C CA    . THR B 1 169 ? -33.68600 10.34900  40.38000 1.000 27.69384 ?  149 THR B CA    1 
ATOM   3014 C C     . THR B 1 169 ? -32.64900 9.71300   41.30000 1.000 25.65048 ?  149 THR B C     1 
ATOM   3015 O O     . THR B 1 169 ? -32.55600 8.48400   41.38900 1.000 22.58700 ?  149 THR B O     1 
ATOM   3016 C CB    . THR B 1 169 ? -35.10100 10.17200  40.95000 1.000 26.54585 ?  149 THR B CB    1 
ATOM   3017 O OG1   . THR B 1 169 ? -35.38800 8.77900   41.14400 1.000 25.57767 ?  149 THR B OG1   1 
ATOM   3018 C CG2   . THR B 1 169 ? -36.13500 10.77100  40.00800 1.000 25.16676 ?  149 THR B CG2   1 
ATOM   3019 N N     . ASN B 1 170 ? -31.86500 10.56200  41.96700 1.000 22.68568 ?  150 ASN B N     1 
ATOM   3020 C CA    . ASN B 1 170 ? -30.87200 10.13700  42.95000 1.000 22.46988 ?  150 ASN B CA    1 
ATOM   3021 C C     . ASN B 1 170 ? -29.92900 9.09100   42.36300 1.000 26.10249 ?  150 ASN B C     1 
ATOM   3022 O O     . ASN B 1 170 ? -29.67900 8.03700   42.95000 1.000 25.58536 ?  150 ASN B O     1 
ATOM   3023 C CB    . ASN B 1 170 ? -31.55000 9.62700   44.22100 1.000 23.76533 ?  150 ASN B CB    1 
ATOM   3024 C CG    . ASN B 1 170 ? -32.34900 10.71000  44.92700 1.000 26.57242 ?  150 ASN B CG    1 
ATOM   3025 O OD1   . ASN B 1 170 ? -32.26700 11.90200  44.58000 1.000 24.55292 ?  150 ASN B OD1   1 
ATOM   3026 N ND2   . ASN B 1 170 ? -33.12100 10.30700  45.92300 1.000 22.18457 ?  150 ASN B ND2   1 
ATOM   3027 N N     . LEU B 1 171 ? -29.40700 9.39400   41.17500 1.000 26.56254 ?  151 LEU B N     1 
ATOM   3028 C CA    . LEU B 1 171 ? -28.47400 8.51700   40.47700 1.000 23.56563 ?  151 LEU B CA    1 
ATOM   3029 C C     . LEU B 1 171 ? -27.07600 9.09800   40.32900 1.000 25.73107 ?  151 LEU B C     1 
ATOM   3030 O O     . LEU B 1 171 ? -26.09800 8.37000   40.51100 1.000 26.50137 ?  151 LEU B O     1 
ATOM   3031 C CB    . LEU B 1 171 ? -29.01300 8.16700   39.08700 1.000 24.01220 ?  151 LEU B CB    1 
ATOM   3032 C CG    . LEU B 1 171 ? -28.08500 7.27600   38.25900 1.000 24.79323 ?  151 LEU B CG    1 
ATOM   3033 C CD1   . LEU B 1 171 ? -27.93000 5.90300   38.91700 1.000 22.88083 ?  151 LEU B CD1   1 
ATOM   3034 C CD2   . LEU B 1 171 ? -28.58400 7.15700   36.82900 1.000 22.93803 ?  151 LEU B CD2   1 
ATOM   3035 N N     . ILE B 1 172 ? -26.94700 10.39400  40.02500 1.000 23.24686 ?  152 ILE B N     1 
ATOM   3036 C CA    . ILE B 1 172 ? -25.66000 10.92900  39.57900 1.000 24.17992 ?  152 ILE B CA    1 
ATOM   3037 C C     . ILE B 1 172 ? -24.60900 10.83600  40.67600 1.000 25.42545 ?  152 ILE B C     1 
ATOM   3038 O O     . ILE B 1 172 ? -23.42600 10.61200  40.39100 1.000 25.90329 ?  152 ILE B O     1 
ATOM   3039 C CB    . ILE B 1 172 ? -25.81800 12.37500  39.07500 1.000 27.67153 ?  152 ILE B CB    1 
ATOM   3040 C CG1   . ILE B 1 172 ? -26.43500 13.26700  40.15700 1.000 23.08852 ?  152 ILE B CG1   1 
ATOM   3041 C CG2   . ILE B 1 172 ? -26.65900 12.41600  37.79200 1.000 25.37974 ?  152 ILE B CG2   1 
ATOM   3042 C CD1   . ILE B 1 172 ? -26.28800 14.75900  39.85800 1.000 24.59404 ?  152 ILE B CD1   1 
ATOM   3043 N N     . ASP B 1 173 ? -24.99800 11.02700  41.93800 1.000 25.21654 ?  153 ASP B N     1 
ATOM   3044 C CA    . ASP B 1 173 ? -24.03000 10.94100  43.02200 1.000 25.49316 ?  153 ASP B CA    1 
ATOM   3045 C C     . ASP B 1 173 ? -23.84400 9.51500   43.50800 1.000 27.18858 ?  153 ASP B C     1 
ATOM   3046 O O     . ASP B 1 173 ? -23.27300 9.29600   44.58200 1.000 25.81005 ?  153 ASP B O     1 
ATOM   3047 C CB    . ASP B 1 173 ? -24.40800 11.87200  44.18800 1.000 26.59926 ?  153 ASP B CB    1 
ATOM   3048 C CG    . ASP B 1 173 ? -25.86000 11.73200  44.63400 1.000 32.68220 ?  153 ASP B CG    1 
ATOM   3049 O OD1   . ASP B 1 173 ? -26.76200 11.45800  43.79900 1.000 29.35077 ?  153 ASP B OD1   1 
ATOM   3050 O OD2   . ASP B 1 173 ? -26.09700 11.93400  45.84600 1.000 33.54830 -1 153 ASP B OD2   1 
ATOM   3051 N N     . ARG B 1 174 ? -24.31100 8.54200   42.73300 1.000 27.37719 ?  154 ARG B N     1 
ATOM   3052 C CA    . ARG B 1 174 ? -23.98200 7.14400   42.94900 1.000 29.48098 ?  154 ARG B CA    1 
ATOM   3053 C C     . ARG B 1 174 ? -23.18500 6.57400   41.78200 1.000 28.05100 ?  154 ARG B C     1 
ATOM   3054 O O     . ARG B 1 174 ? -22.96000 5.35700   41.73400 1.000 32.02219 ?  154 ARG B O     1 
ATOM   3055 C CB    . ARG B 1 174 ? -25.25800 6.32700   43.17700 1.000 32.59916 ?  154 ARG B CB    1 
ATOM   3056 C CG    . ARG B 1 174 ? -25.97600 6.64600   44.48000 1.000 33.87819 ?  154 ARG B CG    1 
ATOM   3057 C CD    . ARG B 1 174 ? -25.01000 6.70800   45.64900 1.000 38.25353 ?  154 ARG B CD    1 
ATOM   3058 N NE    . ARG B 1 174 ? -25.69200 6.96100   46.91500 1.000 42.38799 ?  154 ARG B NE    1 
ATOM   3059 C CZ    . ARG B 1 174 ? -26.29300 6.02700   47.64300 1.000 45.58965 ?  154 ARG B CZ    1 
ATOM   3060 N NH1   . ARG B 1 174 ? -26.30500 4.75600   47.26700 1.000 38.99890 ?  154 ARG B NH1   1 
ATOM   3061 N NH2   . ARG B 1 174 ? -26.88100 6.37500   48.78500 1.000 47.14394 ?  154 ARG B NH2   1 
ATOM   3062 N N     . LEU B 1 175 ? -22.76500 7.42100   40.83800 1.000 27.11274 ?  155 LEU B N     1 
ATOM   3063 C CA    . LEU B 1 175 ? -22.00900 7.01300   39.65800 1.000 28.89257 ?  155 LEU B CA    1 
ATOM   3064 C C     . LEU B 1 175 ? -20.53200 7.33100   39.84800 1.000 29.82527 ?  155 LEU B C     1 
ATOM   3065 O O     . LEU B 1 175 ? -20.18200 8.38700   40.38500 1.000 26.19580 ?  155 LEU B O     1 
ATOM   3066 C CB    . LEU B 1 175 ? -22.51700 7.73700   38.41200 1.000 24.95736 ?  155 LEU B CB    1 
ATOM   3067 C CG    . LEU B 1 175 ? -23.96000 7.46200   38.00000 1.000 27.94837 ?  155 LEU B CG    1 
ATOM   3068 C CD1   . LEU B 1 175 ? -24.25700 8.14400   36.66900 1.000 24.70788 ?  155 LEU B CD1   1 
ATOM   3069 C CD2   . LEU B 1 175 ? -24.22700 5.95600   37.89800 1.000 24.56303 ?  155 LEU B CD2   1 
ATOM   3070 N N     . TYR B 1 176 ? -19.66400 6.41800   39.40300 1.000 29.16708 ?  156 TYR B N     1 
ATOM   3071 C CA    . TYR B 1 176 ? -18.23300 6.67000   39.54900 1.000 28.09761 ?  156 TYR B CA    1 
ATOM   3072 C C     . TYR B 1 176 ? -17.79600 7.85000   38.69200 1.000 27.46649 ?  156 TYR B C     1 
ATOM   3073 O O     . TYR B 1 176 ? -16.99700 8.68400   39.13300 1.000 29.56786 ?  156 TYR B O     1 
ATOM   3074 C CB    . TYR B 1 176 ? -17.41500 5.42300   39.19100 1.000 31.06690 ?  156 TYR B CB    1 
ATOM   3075 C CG    . TYR B 1 176 ? -15.92100 5.67000   39.33200 1.000 29.64398 ?  156 TYR B CG    1 
ATOM   3076 C CD1   . TYR B 1 176 ? -15.31900 5.73700   40.58500 1.000 26.93599 ?  156 TYR B CD1   1 
ATOM   3077 C CD2   . TYR B 1 176 ? -15.12500 5.87100   38.21200 1.000 29.50166 ?  156 TYR B CD2   1 
ATOM   3078 C CE1   . TYR B 1 176 ? -13.96400 5.97100   40.71600 1.000 28.13496 ?  156 TYR B CE1   1 
ATOM   3079 C CE2   . TYR B 1 176 ? -13.77600 6.10900   38.33100 1.000 27.91510 ?  156 TYR B CE2   1 
ATOM   3080 C CZ    . TYR B 1 176 ? -13.19600 6.16200   39.58000 1.000 31.04674 ?  156 TYR B CZ    1 
ATOM   3081 O OH    . TYR B 1 176 ? -11.84100 6.41800   39.67800 1.000 27.69112 ?  156 TYR B OH    1 
ATOM   3082 N N     . GLU B 1 177 ? -18.32300 7.94700   37.47100 1.000 26.39413 ?  157 GLU B N     1 
ATOM   3083 C CA    . GLU B 1 177 ? -17.96700 9.01300   36.53500 1.000 28.15458 ?  157 GLU B CA    1 
ATOM   3084 C C     . GLU B 1 177 ? -19.25200 9.53700   35.91500 1.000 29.21161 ?  157 GLU B C     1 
ATOM   3085 O O     . GLU B 1 177 ? -19.57400 9.23400   34.76000 1.000 28.02702 ?  157 GLU B O     1 
ATOM   3086 C CB    . GLU B 1 177 ? -16.99200 8.50200   35.47000 1.000 27.26781 ?  157 GLU B CB    1 
ATOM   3087 C CG    . GLU B 1 177 ? -16.42700 9.58300   34.55700 1.000 29.63071 ?  157 GLU B CG    1 
ATOM   3088 C CD    . GLU B 1 177 ? -15.44900 9.01900   33.54200 1.000 29.36322 ?  157 GLU B CD    1 
ATOM   3089 O OE1   . GLU B 1 177 ? -15.07900 7.83400   33.67200 1.000 26.71463 ?  157 GLU B OE1   1 
ATOM   3090 O OE2   . GLU B 1 177 ? -15.05500 9.75400   32.61400 1.000 31.82731 -1 157 GLU B OE2   1 
ATOM   3091 N N     . PRO B 1 178 ? -20.01700 10.34200  36.66300 1.000 30.57576 ?  158 PRO B N     1 
ATOM   3092 C CA    . PRO B 1 178 ? -21.36000 10.72300  36.18900 1.000 26.26766 ?  158 PRO B CA    1 
ATOM   3093 C C     . PRO B 1 178 ? -21.33900 11.45000  34.86400 1.000 28.01736 ?  158 PRO B C     1 
ATOM   3094 O O     . PRO B 1 178 ? -22.30900 11.37400  34.09800 1.000 26.44026 ?  158 PRO B O     1 
ATOM   3095 C CB    . PRO B 1 178 ? -21.90200 11.61300  37.32200 1.000 27.55754 ?  158 PRO B CB    1 
ATOM   3096 C CG    . PRO B 1 178 ? -20.68100 12.07800  38.08500 1.000 27.72887 ?  158 PRO B CG    1 
ATOM   3097 C CD    . PRO B 1 178 ? -19.69000 10.94100  37.97300 1.000 28.77592 ?  158 PRO B CD    1 
ATOM   3098 N N     . ARG B 1 179 ? -20.24300 12.14300  34.56000 1.000 29.88618 ?  159 ARG B N     1 
ATOM   3099 C CA    . ARG B 1 179 ? -20.15600 12.84800  33.29200 1.000 29.73907 ?  159 ARG B CA    1 
ATOM   3100 C C     . ARG B 1 179 ? -20.28000 11.88900  32.11700 1.000 33.30966 ?  159 ARG B C     1 
ATOM   3101 O O     . ARG B 1 179 ? -20.85300 12.25100  31.08600 1.000 35.50802 ?  159 ARG B O     1 
ATOM   3102 C CB    . ARG B 1 179 ? -18.84900 13.64100  33.23200 1.000 39.98017 ?  159 ARG B CB    1 
ATOM   3103 C CG    . ARG B 1 179 ? -18.74600 14.56600  32.04000 1.000 40.50607 ?  159 ARG B CG    1 
ATOM   3104 C CD    . ARG B 1 179 ? -17.36300 15.17800  31.94100 1.000 42.69878 ?  159 ARG B CD    1 
ATOM   3105 N NE    . ARG B 1 179 ? -17.28000 16.42200  32.69600 1.000 52.79657 ?  159 ARG B NE    1 
ATOM   3106 C CZ    . ARG B 1 179 ? -17.50900 17.62300  32.17900 1.000 50.76118 ?  159 ARG B CZ    1 
ATOM   3107 N NH1   . ARG B 1 179 ? -17.88700 17.77000  30.91800 1.000 44.81256 ?  159 ARG B NH1   1 
ATOM   3108 N NH2   . ARG B 1 179 ? -17.37400 18.70000  32.95100 1.000 46.89286 ?  159 ARG B NH2   1 
ATOM   3109 N N     . LEU B 1 180 ? -19.79900 10.65000  32.26600 1.000 33.27589 ?  160 LEU B N     1 
ATOM   3110 C CA    . LEU B 1 180 ? -19.93800 9.66800   31.19100 1.000 32.73465 ?  160 LEU B CA    1 
ATOM   3111 C C     . LEU B 1 180 ? -21.40400 9.45300   30.82800 1.000 34.76352 ?  160 LEU B C     1 
ATOM   3112 O O     . LEU B 1 180 ? -21.74400 9.28300   29.65100 1.000 35.58925 ?  160 LEU B O     1 
ATOM   3113 C CB    . LEU B 1 180 ? -19.27700 8.35000   31.60900 1.000 32.27996 ?  160 LEU B CB    1 
ATOM   3114 C CG    . LEU B 1 180 ? -19.15600 7.16000   30.65500 1.000 33.51309 ?  160 LEU B CG    1 
ATOM   3115 C CD1   . LEU B 1 180 ? -18.49900 7.55400   29.34200 1.000 37.30527 ?  160 LEU B CD1   1 
ATOM   3116 C CD2   . LEU B 1 180 ? -18.34600 6.06000   31.33800 1.000 31.94346 ?  160 LEU B CD2   1 
ATOM   3117 N N     . PHE B 1 181 ? -22.28700 9.48300   31.82400 1.000 29.64827 ?  161 PHE B N     1 
ATOM   3118 C CA    . PHE B 1 181 ? -23.71800 9.36000   31.57600 1.000 28.48810 ?  161 PHE B CA    1 
ATOM   3119 C C     . PHE B 1 181 ? -24.29200 10.65600  31.01300 1.000 28.71181 ?  161 PHE B C     1 
ATOM   3120 O O     . PHE B 1 181 ? -25.02700 10.63900  30.02100 1.000 32.04300 ?  161 PHE B O     1 
ATOM   3121 C CB    . PHE B 1 181 ? -24.41800 8.94400   32.87900 1.000 27.81616 ?  161 PHE B CB    1 
ATOM   3122 C CG    . PHE B 1 181 ? -25.84700 9.43100   33.01800 1.000 28.44899 ?  161 PHE B CG    1 
ATOM   3123 C CD1   . PHE B 1 181 ? -26.83400 9.02900   32.13200 1.000 29.52951 ?  161 PHE B CD1   1 
ATOM   3124 C CD2   . PHE B 1 181 ? -26.21000 10.23800  34.08400 1.000 29.69859 ?  161 PHE B CD2   1 
ATOM   3125 C CE1   . PHE B 1 181 ? -28.14400 9.46400   32.28200 1.000 27.60689 ?  161 PHE B CE1   1 
ATOM   3126 C CE2   . PHE B 1 181 ? -27.51500 10.66400  34.24300 1.000 26.61887 ?  161 PHE B CE2   1 
ATOM   3127 C CZ    . PHE B 1 181 ? -28.48100 10.28000  33.34100 1.000 29.78515 ?  161 PHE B CZ    1 
ATOM   3128 N N     . LEU B 1 182 ? -23.92300 11.79300  31.61000 1.000 31.23187 ?  162 LEU B N     1 
ATOM   3129 C CA    . LEU B 1 182 ? -24.59800 13.05800  31.31600 1.000 31.73289 ?  162 LEU B CA    1 
ATOM   3130 C C     . LEU B 1 182 ? -24.20500 13.65900  29.96800 1.000 33.00494 ?  162 LEU B C     1 
ATOM   3131 O O     . LEU B 1 182 ? -25.04600 14.29600  29.32500 1.000 32.90968 ?  162 LEU B O     1 
ATOM   3132 C CB    . LEU B 1 182 ? -24.31600 14.06800  32.43000 1.000 28.82615 ?  162 LEU B CB    1 
ATOM   3133 C CG    . LEU B 1 182 ? -24.96100 13.71900  33.77000 1.000 32.27061 ?  162 LEU B CG    1 
ATOM   3134 C CD1   . LEU B 1 182 ? -24.37100 14.58500  34.85800 1.000 27.97887 ?  162 LEU B CD1   1 
ATOM   3135 C CD2   . LEU B 1 182 ? -26.47700 13.89700  33.69600 1.000 29.73087 ?  162 LEU B CD2   1 
ATOM   3136 N N     . GLU B 1 183 ? -22.94500 13.52000  29.53100 1.000 33.14884 ?  163 GLU B N     1 
ATOM   3137 C CA    . GLU B 1 183 ? -22.54300 14.23400  28.31700 1.000 36.53620 ?  163 GLU B CA    1 
ATOM   3138 C C     . GLU B 1 183 ? -23.09800 13.59800  27.04800 1.000 37.66122 ?  163 GLU B C     1 
ATOM   3139 O O     . GLU B 1 183 ? -23.12200 14.25400  26.00200 1.000 38.43591 ?  163 GLU B O     1 
ATOM   3140 C CB    . GLU B 1 183 ? -21.01300 14.33900  28.20100 1.000 35.07296 ?  163 GLU B CB    1 
ATOM   3141 C CG    . GLU B 1 183 ? -20.23200 13.04100  28.37500 1.000 40.11794 ?  163 GLU B CG    1 
ATOM   3142 C CD    . GLU B 1 183 ? -18.71800 13.26300  28.44900 1.000 48.40380 ?  163 GLU B CD    1 
ATOM   3143 O OE1   . GLU B 1 183 ? -18.28700 14.43300  28.60400 1.000 44.86901 ?  163 GLU B OE1   1 
ATOM   3144 O OE2   . GLU B 1 183 ? -17.96100 12.26200  28.38900 1.000 46.81359 -1 163 GLU B OE2   1 
ATOM   3145 N N     . ASN B 1 184 ? -23.55800 12.35200  27.11800 1.000 37.79739 ?  164 ASN B N     1 
ATOM   3146 C CA    . ASN B 1 184 ? -24.09700 11.66900  25.95400 1.000 38.63087 ?  164 ASN B CA    1 
ATOM   3147 C C     . ASN B 1 184 ? -25.61100 11.52100  25.97200 1.000 38.85917 ?  164 ASN B C     1 
ATOM   3148 O O     . ASN B 1 184 ? -26.18600 11.14600  24.94500 1.000 39.93048 ?  164 ASN B O     1 
ATOM   3149 C CB    . ASN B 1 184 ? -23.45900 10.27800  25.82200 1.000 39.76103 ?  164 ASN B CB    1 
ATOM   3150 C CG    . ASN B 1 184 ? -21.94400 10.34000  25.75400 1.000 44.98660 ?  164 ASN B CG    1 
ATOM   3151 O OD1   . ASN B 1 184 ? -21.37900 11.00700  24.88500 1.000 46.19676 ?  164 ASN B OD1   1 
ATOM   3152 N ND2   . ASN B 1 184 ? -21.27800 9.65500   26.67800 1.000 41.43366 ?  164 ASN B ND2   1 
ATOM   3153 N N     . ILE B 1 185 ? -26.27600 11.82300  27.09000 1.000 35.97460 ?  165 ILE B N     1 
ATOM   3154 C CA    . ILE B 1 185 ? -27.67200 11.42700  27.24900 1.000 35.94404 ?  165 ILE B CA    1 
ATOM   3155 C C     . ILE B 1 185 ? -28.61600 12.17500  26.31000 1.000 33.95655 ?  165 ILE B C     1 
ATOM   3156 O O     . ILE B 1 185 ? -29.71700 11.68400  26.02900 1.000 33.29296 ?  165 ILE B O     1 
ATOM   3157 C CB    . ILE B 1 185 ? -28.09100 11.59700  28.72100 1.000 31.91192 ?  165 ILE B CB    1 
ATOM   3158 C CG1   . ILE B 1 185 ? -29.30800 10.71500  29.04300 1.000 29.67930 ?  165 ILE B CG1   1 
ATOM   3159 C CG2   . ILE B 1 185 ? -28.29000 13.08300  29.07200 1.000 31.66274 ?  165 ILE B CG2   1 
ATOM   3160 C CD1   . ILE B 1 185 ? -29.13100 9.22800   28.68400 1.000 29.11219 ?  165 ILE B CD1   1 
ATOM   3161 N N     . HIS B 1 186 ? -28.21600 13.33900  25.79400 1.000 36.21556 ?  166 HIS B N     1 
ATOM   3162 C CA    . HIS B 1 186 ? -29.05700 14.04700  24.83000 1.000 37.64297 ?  166 HIS B CA    1 
ATOM   3163 C C     . HIS B 1 186 ? -29.27800 13.22900  23.56200 1.000 38.14311 ?  166 HIS B C     1 
ATOM   3164 O O     . HIS B 1 186 ? -30.26400 13.45600  22.84800 1.000 37.76832 ?  166 HIS B O     1 
ATOM   3165 C CB    . HIS B 1 186 ? -28.42900 15.39500  24.47900 1.000 34.97568 ?  166 HIS B CB    1 
ATOM   3166 C CG    . HIS B 1 186 ? -27.11700 15.27100  23.77400 1.000 38.26872 ?  166 HIS B CG    1 
ATOM   3167 N ND1   . HIS B 1 186 ? -25.97100 14.83800  24.40800 1.000 39.64408 ?  166 HIS B ND1   1 
ATOM   3168 C CD2   . HIS B 1 186 ? -26.77000 15.50300  22.48500 1.000 36.68063 ?  166 HIS B CD2   1 
ATOM   3169 C CE1   . HIS B 1 186 ? -24.97200 14.81700  23.54100 1.000 40.38968 ?  166 HIS B CE1   1 
ATOM   3170 N NE2   . HIS B 1 186 ? -25.43100 15.21200  22.36700 1.000 38.83235 ?  166 HIS B NE2   1 
ATOM   3171 N N     . LYS B 1 187 ? -28.38700 12.27400  23.27800 1.000 39.32049 ?  167 LYS B N     1 
ATOM   3172 C CA    . LYS B 1 187 ? -28.53300 11.40100  22.12000 1.000 38.90730 ?  167 LYS B CA    1 
ATOM   3173 C C     . LYS B 1 187 ? -29.72600 10.45800  22.23300 1.000 39.37811 ?  167 LYS B C     1 
ATOM   3174 O O     . LYS B 1 187 ? -30.18900 9.94800   21.21000 1.000 39.73642 ?  167 LYS B O     1 
ATOM   3175 C CB    . LYS B 1 187 ? -27.25300 10.58300  21.91000 1.000 38.49991 ?  167 LYS B CB    1 
ATOM   3176 C CG    . LYS B 1 187 ? -26.00700 11.41200  21.62100 1.000 37.27732 ?  167 LYS B CG    1 
ATOM   3177 N N     . ARG B 1 188 ? -30.22400 10.20200  23.43800 1.000 35.46398 ?  168 ARG B N     1 
ATOM   3178 C CA    . ARG B 1 188 ? -31.34600 9.29700   23.63400 1.000 33.72573 ?  168 ARG B CA    1 
ATOM   3179 C C     . ARG B 1 188 ? -32.67800 10.02100  23.79100 1.000 37.47530 ?  168 ARG B C     1 
ATOM   3180 O O     . ARG B 1 188 ? -33.70100 9.36400   24.00100 1.000 37.15154 ?  168 ARG B O     1 
ATOM   3181 C CB    . ARG B 1 188 ? -31.09700 8.41100   24.85700 1.000 34.46457 ?  168 ARG B CB    1 
ATOM   3182 C CG    . ARG B 1 188 ? -29.65500 7.91300   24.98000 1.000 36.04231 ?  168 ARG B CG    1 
ATOM   3183 C CD    . ARG B 1 188 ? -29.29300 7.00700   23.82500 1.000 37.82492 ?  168 ARG B CD    1 
ATOM   3184 N NE    . ARG B 1 188 ? -28.04900 6.28800   24.06800 1.000 43.05764 ?  168 ARG B NE    1 
ATOM   3185 C CZ    . ARG B 1 188 ? -27.96400 4.97800   24.25700 1.000 40.22573 ?  168 ARG B CZ    1 
ATOM   3186 N NH1   . ARG B 1 188 ? -29.04100 4.21100   24.27800 1.000 34.31103 ?  168 ARG B NH1   1 
ATOM   3187 N NH2   . ARG B 1 188 ? -26.76600 4.42300   24.42800 1.000 41.71655 ?  168 ARG B NH2   1 
ATOM   3188 N N     . ILE B 1 189 ? -32.69500 11.34900  23.69300 1.000 33.09846 ?  169 ILE B N     1 
ATOM   3189 C CA    . ILE B 1 189 ? -33.89100 12.14800  23.94900 1.000 38.49266 ?  169 ILE B CA    1 
ATOM   3190 C C     . ILE B 1 189 ? -34.31400 12.83000  22.65800 1.000 37.85606 ?  169 ILE B C     1 
ATOM   3191 O O     . ILE B 1 189 ? -33.48100 13.41500  21.95700 1.000 37.13339 ?  169 ILE B O     1 
ATOM   3192 C CB    . ILE B 1 189 ? -33.65500 13.18900  25.05500 1.000 36.91734 ?  169 ILE B CB    1 
ATOM   3193 C CG1   . ILE B 1 189 ? -32.98400 12.53900  26.26600 1.000 36.45047 ?  169 ILE B CG1   1 
ATOM   3194 C CG2   . ILE B 1 189 ? -34.96700 13.87100  25.42700 1.000 37.15677 ?  169 ILE B CG2   1 
ATOM   3195 C CD1   . ILE B 1 189 ? -32.82500 13.47100  27.45700 1.000 33.21503 ?  169 ILE B CD1   1 
ATOM   3196 N N     . ASN B 1 190 ? -35.61000 12.76200  22.35500 1.000 38.92621 ?  170 ASN B N     1 
ATOM   3197 C CA    . ASN B 1 190 ? -36.15700 13.38500  21.16200 1.000 39.95329 ?  170 ASN B CA    1 
ATOM   3198 C C     . ASN B 1 190 ? -36.07200 14.90400  21.26200 1.000 42.49347 ?  170 ASN B C     1 
ATOM   3199 O O     . ASN B 1 190 ? -35.86100 15.47600  22.33800 1.000 42.27829 ?  170 ASN B O     1 
ATOM   3200 C CB    . ASN B 1 190 ? -37.61200 12.97700  20.95900 1.000 39.62131 ?  170 ASN B CB    1 
ATOM   3201 C CG    . ASN B 1 190 ? -37.77200 11.50100  20.73800 1.000 39.21591 ?  170 ASN B CG    1 
ATOM   3202 O OD1   . ASN B 1 190 ? -36.96800 10.87500  20.04500 1.000 44.45041 ?  170 ASN B OD1   1 
ATOM   3203 N ND2   . ASN B 1 190 ? -38.81200 10.92800  21.32500 1.000 37.93849 ?  170 ASN B ND2   1 
ATOM   3204 N N     . GLU B 1 191 ? -36.24400 15.55800  20.11300 1.000 45.73224 ?  171 GLU B N     1 
ATOM   3205 C CA    . GLU B 1 191 ? -36.30400 17.01200  20.07800 1.000 44.31578 ?  171 GLU B CA    1 
ATOM   3206 C C     . GLU B 1 191 ? -37.47600 17.49600  20.92400 1.000 42.41967 ?  171 GLU B C     1 
ATOM   3207 O O     . GLU B 1 191 ? -38.57100 16.92700  20.88100 1.000 45.65704 ?  171 GLU B O     1 
ATOM   3208 C CB    . GLU B 1 191 ? -36.44600 17.50400  18.63300 1.000 46.92772 ?  171 GLU B CB    1 
ATOM   3209 N N     . LYS B 1 192 ? -37.23200 18.53600  21.71900 1.000 44.00918 ?  172 LYS B N     1 
ATOM   3210 C CA    . LYS B 1 192 ? -38.17100 19.06200  22.70500 1.000 46.47447 ?  172 LYS B CA    1 
ATOM   3211 C C     . LYS B 1 192 ? -38.39000 18.14200  23.90200 1.000 41.19691 ?  172 LYS B C     1 
ATOM   3212 O O     . LYS B 1 192 ? -39.19200 18.48300  24.78600 1.000 39.24092 ?  172 LYS B O     1 
ATOM   3213 N N     . GLY B 1 193 ? -37.72100 16.98400  23.96300 1.000 39.36690 ?  173 GLY B N     1 
ATOM   3214 C CA    . GLY B 1 193 ? -37.83200 16.09100  25.09900 1.000 34.54325 ?  173 GLY B CA    1 
ATOM   3215 C C     . GLY B 1 193 ? -37.07400 16.61800  26.30100 1.000 34.69528 ?  173 GLY B C     1 
ATOM   3216 O O     . GLY B 1 193 ? -36.41000 17.65200  26.25500 1.000 33.62788 ?  173 GLY B O     1 
ATOM   3217 N N     . TYR B 1 194 ? -37.16100 15.87200  27.40100 1.000 33.48950 ?  174 TYR B N     1 
ATOM   3218 C CA    . TYR B 1 194 ? -36.72000 16.36500  28.70000 1.000 33.58782 ?  174 TYR B CA    1 
ATOM   3219 C C     . TYR B 1 194 ? -35.78000 15.38500  29.38800 1.000 31.95020 ?  174 TYR B C     1 
ATOM   3220 O O     . TYR B 1 194 ? -35.91500 14.16400  29.26700 1.000 28.08284 ?  174 TYR B O     1 
ATOM   3221 C CB    . TYR B 1 194 ? -37.91100 16.62900  29.62800 1.000 32.75595 ?  174 TYR B CB    1 
ATOM   3222 C CG    . TYR B 1 194 ? -38.60300 17.96100  29.41800 1.000 32.35446 ?  174 TYR B CG    1 
ATOM   3223 C CD1   . TYR B 1 194 ? -39.45900 18.16400  28.34400 1.000 36.74949 ?  174 TYR B CD1   1 
ATOM   3224 C CD2   . TYR B 1 194 ? -38.40700 19.00700  30.30200 1.000 33.51823 ?  174 TYR B CD2   1 
ATOM   3225 C CE1   . TYR B 1 194 ? -40.09600 19.38800  28.15700 1.000 37.91667 ?  174 TYR B CE1   1 
ATOM   3226 C CE2   . TYR B 1 194 ? -39.04000 20.22700  30.12500 1.000 36.91454 ?  174 TYR B CE2   1 
ATOM   3227 C CZ    . TYR B 1 194 ? -39.88300 20.41100  29.05300 1.000 34.91450 ?  174 TYR B CZ    1 
ATOM   3228 O OH    . TYR B 1 194 ? -40.51300 21.62100  28.87800 1.000 37.55864 ?  174 TYR B OH    1 
ATOM   3229 N N     . LEU B 1 195 ? -34.82600 15.94300  30.12400 1.000 31.70687 ?  175 LEU B N     1 
ATOM   3230 C CA    . LEU B 1 195 ? -34.01600 15.19600  31.07500 1.000 30.80369 ?  175 LEU B CA    1 
ATOM   3231 C C     . LEU B 1 195 ? -34.31600 15.76600  32.45100 1.000 29.95272 ?  175 LEU B C     1 
ATOM   3232 O O     . LEU B 1 195 ? -34.12600 16.96700  32.68300 1.000 26.99224 ?  175 LEU B O     1 
ATOM   3233 C CB    . LEU B 1 195 ? -32.51900 15.28900  30.74600 1.000 31.70947 ?  175 LEU B CB    1 
ATOM   3234 C CG    . LEU B 1 195 ? -31.58200 14.79200  31.85600 1.000 27.93817 ?  175 LEU B CG    1 
ATOM   3235 C CD1   . LEU B 1 195 ? -31.52300 13.27400  31.88900 1.000 23.82790 ?  175 LEU B CD1   1 
ATOM   3236 C CD2   . LEU B 1 195 ? -30.17100 15.37600  31.69600 1.000 29.61032 ?  175 LEU B CD2   1 
ATOM   3237 N N     . ILE B 1 196 ? -34.81200 14.92100  33.35200 1.000 28.66851 ?  176 ILE B N     1 
ATOM   3238 C CA    . ILE B 1 196 ? -35.16400 15.35000  34.70200 1.000 27.49983 ?  176 ILE B CA    1 
ATOM   3239 C C     . ILE B 1 196 ? -34.29600 14.58200  35.68400 1.000 28.73630 ?  176 ILE B C     1 
ATOM   3240 O O     . ILE B 1 196 ? -34.31800 13.34500  35.71000 1.000 28.32646 ?  176 ILE B O     1 
ATOM   3241 C CB    . ILE B 1 196 ? -36.65700 15.15100  34.99800 1.000 26.54666 ?  176 ILE B CB    1 
ATOM   3242 C CG1   . ILE B 1 196 ? -37.48700 15.98800  34.01400 1.000 29.00498 ?  176 ILE B CG1   1 
ATOM   3243 C CG2   . ILE B 1 196 ? -36.97300 15.54600  36.43800 1.000 23.62799 ?  176 ILE B CG2   1 
ATOM   3244 C CD1   . ILE B 1 196 ? -38.87400 16.38000  34.52500 1.000 31.86556 ?  176 ILE B CD1   1 
ATOM   3245 N N     . LEU B 1 197 ? -33.52900 15.32000  36.47900 1.000 26.92294 ?  177 LEU B N     1 
ATOM   3246 C CA    . LEU B 1 197 ? -32.61200 14.77400  37.46300 1.000 26.87821 ?  177 LEU B CA    1 
ATOM   3247 C C     . LEU B 1 197 ? -33.07200 15.17200  38.85600 1.000 25.97055 ?  177 LEU B C     1 
ATOM   3248 O O     . LEU B 1 197 ? -33.65000 16.24400  39.04700 1.000 28.80149 ?  177 LEU B O     1 
ATOM   3249 C CB    . LEU B 1 197 ? -31.19100 15.31000  37.24500 1.000 23.41078 ?  177 LEU B CB    1 
ATOM   3250 C CG    . LEU B 1 197 ? -30.47700 15.01900  35.92500 1.000 26.68224 ?  177 LEU B CG    1 
ATOM   3251 C CD1   . LEU B 1 197 ? -29.05500 15.60300  35.96000 1.000 22.56836 ?  177 LEU B CD1   1 
ATOM   3252 C CD2   . LEU B 1 197 ? -30.44900 13.51500  35.61800 1.000 24.97170 ?  177 LEU B CD2   1 
ATOM   3253 N N     . THR B 1 198 ? -32.82500 14.30000  39.83300 1.000 26.88587 ?  178 THR B N     1 
ATOM   3254 C CA    . THR B 1 198 ? -32.84500 14.70200  41.23200 1.000 28.48655 ?  178 THR B CA    1 
ATOM   3255 C C     . THR B 1 198 ? -31.60400 14.16500  41.91200 1.000 27.49504 ?  178 THR B C     1 
ATOM   3256 O O     . THR B 1 198 ? -31.09000 13.10400  41.55400 1.000 27.06958 ?  178 THR B O     1 
ATOM   3257 C CB    . THR B 1 198 ? -34.06600 14.21000  42.02600 1.000 27.54603 ?  178 THR B CB    1 
ATOM   3258 O OG1   . THR B 1 198 ? -33.85000 12.84800  42.43300 1.000 25.80828 ?  178 THR B OG1   1 
ATOM   3259 C CG2   . THR B 1 198 ? -35.35700 14.34700  41.21800 1.000 29.40372 ?  178 THR B CG2   1 
ATOM   3260 N N     . SER B 1 199 ? -31.14200 14.90100  42.90900 1.000 25.29459 ?  179 SER B N     1 
ATOM   3261 C CA    . SER B 1 199 ? -29.98800 14.46100  43.67200 1.000 24.94310 ?  179 SER B CA    1 
ATOM   3262 C C     . SER B 1 199 ? -29.85000 15.33100  44.90600 1.000 26.22841 ?  179 SER B C     1 
ATOM   3263 O O     . SER B 1 199 ? -30.08600 16.54700  44.83800 1.000 26.52500 ?  179 SER B O     1 
ATOM   3264 C CB    . SER B 1 199 ? -28.70200 14.52800  42.84500 1.000 24.13701 ?  179 SER B CB    1 
ATOM   3265 O OG    . SER B 1 199 ? -27.58200 14.34100  43.68200 1.000 24.45367 ?  179 SER B OG    1 
ATOM   3266 N N     . PRO B 1 200 ? -29.50600 14.74700  46.04700 1.000 24.29581 ?  180 PRO B N     1 
ATOM   3267 C CA    . PRO B 1 200 ? -29.09900 15.54400  47.20500 1.000 23.95009 ?  180 PRO B CA    1 
ATOM   3268 C C     . PRO B 1 200 ? -27.62300 15.89100  47.21200 1.000 24.13080 ?  180 PRO B C     1 
ATOM   3269 O O     . PRO B 1 200 ? -27.15800 16.47800  48.19100 1.000 23.97771 ?  180 PRO B O     1 
ATOM   3270 C CB    . PRO B 1 200 ? -29.44100 14.61600  48.37000 1.000 24.37669 ?  180 PRO B CB    1 
ATOM   3271 C CG    . PRO B 1 200 ? -29.13400 13.26300  47.81700 1.000 26.45182 ?  180 PRO B CG    1 
ATOM   3272 C CD    . PRO B 1 200 ? -29.60400 13.31400  46.38100 1.000 26.97497 ?  180 PRO B CD    1 
ATOM   3273 N N     . TYR B 1 201 ? -26.87900 15.51300  46.17300 1.000 25.35749 ?  181 TYR B N     1 
ATOM   3274 C CA    . TYR B 1 201 ? -25.50700 15.97900  45.98100 1.000 26.29792 ?  181 TYR B CA    1 
ATOM   3275 C C     . TYR B 1 201 ? -24.58100 15.50300  47.08600 1.000 27.52179 ?  181 TYR B C     1 
ATOM   3276 O O     . TYR B 1 201 ? -23.66100 16.22300  47.48900 1.000 27.72493 ?  181 TYR B O     1 
ATOM   3277 C CB    . TYR B 1 201 ? -25.43600 17.50500  45.88400 1.000 25.49368 ?  181 TYR B CB    1 
ATOM   3278 C CG    . TYR B 1 201 ? -26.36000 18.12400  44.87300 1.000 27.11215 ?  181 TYR B CG    1 
ATOM   3279 C CD1   . TYR B 1 201 ? -26.59500 17.51200  43.65000 1.000 23.22868 ?  181 TYR B CD1   1 
ATOM   3280 C CD2   . TYR B 1 201 ? -26.98000 19.34400  45.13000 1.000 25.76678 ?  181 TYR B CD2   1 
ATOM   3281 C CE1   . TYR B 1 201 ? -27.42700 18.09300  42.70800 1.000 23.15149 ?  181 TYR B CE1   1 
ATOM   3282 C CE2   . TYR B 1 201 ? -27.81800 19.92800  44.19900 1.000 21.14771 ?  181 TYR B CE2   1 
ATOM   3283 C CZ    . TYR B 1 201 ? -28.03600 19.30100  42.99100 1.000 23.58697 ?  181 TYR B CZ    1 
ATOM   3284 O OH    . TYR B 1 201 ? -28.85700 19.88300  42.05500 1.000 25.41472 ?  181 TYR B OH    1 
ATOM   3285 N N     . THR B 1 202 ? -24.82300 14.30300  47.59800 1.000 27.33242 ?  182 THR B N     1 
ATOM   3286 C CA    . THR B 1 202 ? -23.99900 13.75500  48.66700 1.000 27.95587 ?  182 THR B CA    1 
ATOM   3287 C C     . THR B 1 202 ? -22.79000 13.03100  48.06800 1.000 27.69610 ?  182 THR B C     1 
ATOM   3288 O O     . THR B 1 202 ? -22.60300 11.82400  48.20000 1.000 28.22767 ?  182 THR B O     1 
ATOM   3289 C CB    . THR B 1 202 ? -24.84100 12.84900  49.56000 1.000 30.88941 ?  182 THR B CB    1 
ATOM   3290 O OG1   . THR B 1 202 ? -25.51400 11.88100  48.75600 1.000 35.03351 ?  182 THR B OG1   1 
ATOM   3291 C CG2   . THR B 1 202 ? -25.89200 13.67000  50.30400 1.000 33.64070 ?  182 THR B CG2   1 
ATOM   3292 N N     . TRP B 1 203 ? -21.96500 13.81500  47.37600 1.000 28.74318 ?  183 TRP B N     1 
ATOM   3293 C CA    . TRP B 1 203 ? -20.77200 13.27300  46.73600 1.000 26.99392 ?  183 TRP B CA    1 
ATOM   3294 C C     . TRP B 1 203 ? -19.84600 12.64100  47.76900 1.000 33.65243 ?  183 TRP B C     1 
ATOM   3295 O O     . TRP B 1 203 ? -19.49600 13.27000  48.77700 1.000 30.09856 ?  183 TRP B O     1 
ATOM   3296 C CB    . TRP B 1 203 ? -20.03700 14.37400  45.97100 1.000 23.91980 ?  183 TRP B CB    1 
ATOM   3297 C CG    . TRP B 1 203 ? -20.86900 14.99500  44.89800 1.000 27.61863 ?  183 TRP B CG    1 
ATOM   3298 C CD1   . TRP B 1 203 ? -21.44400 16.22600  44.91900 1.000 24.87476 ?  183 TRP B CD1   1 
ATOM   3299 C CD2   . TRP B 1 203 ? -21.23400 14.39900  43.64700 1.000 25.81008 ?  183 TRP B CD2   1 
ATOM   3300 N NE1   . TRP B 1 203 ? -22.14100 16.44200  43.75100 1.000 26.37838 ?  183 TRP B NE1   1 
ATOM   3301 C CE2   . TRP B 1 203 ? -22.02600 15.33500  42.95400 1.000 24.58385 ?  183 TRP B CE2   1 
ATOM   3302 C CE3   . TRP B 1 203 ? -20.96200 13.16400  43.04400 1.000 25.74047 ?  183 TRP B CE3   1 
ATOM   3303 C CZ2   . TRP B 1 203 ? -22.55000 15.07900  41.69000 1.000 24.00977 ?  183 TRP B CZ2   1 
ATOM   3304 C CZ3   . TRP B 1 203 ? -21.47800 12.91100  41.79300 1.000 27.46923 ?  183 TRP B CZ3   1 
ATOM   3305 C CH2   . TRP B 1 203 ? -22.26500 13.86000  41.12600 1.000 25.03290 ?  183 TRP B CH2   1 
ATOM   3306 N N     . ARG B 1 204 ? -19.44700 11.39400  47.50500 1.000 32.42735 ?  184 ARG B N     1 
ATOM   3307 C CA    . ARG B 1 204 ? -18.59100 10.61500  48.39000 1.000 32.89388 ?  184 ARG B CA    1 
ATOM   3308 C C     . ARG B 1 204 ? -17.59000 9.82500   47.55600 1.000 36.23037 ?  184 ARG B C     1 
ATOM   3309 O O     . ARG B 1 204 ? -17.93000 9.31500   46.48100 1.000 32.02854 ?  184 ARG B O     1 
ATOM   3310 C CB    . ARG B 1 204 ? -19.41400 9.65600   49.25200 1.000 36.06374 ?  184 ARG B CB    1 
ATOM   3311 C CG    . ARG B 1 204 ? -20.29400 10.34900  50.29200 1.000 40.47712 ?  184 ARG B CG    1 
ATOM   3312 C CD    . ARG B 1 204 ? -21.12400 9.33100   51.07100 1.000 47.21887 ?  184 ARG B CD    1 
ATOM   3313 N NE    . ARG B 1 204 ? -20.29900 8.55300   51.99500 1.000 51.85152 ?  184 ARG B NE    1 
ATOM   3314 C CZ    . ARG B 1 204 ? -19.60100 9.05800   53.00700 1.000 52.35029 ?  184 ARG B CZ    1 
ATOM   3315 N NH1   . ARG B 1 204 ? -19.66600 10.34200  53.32400 1.000 48.82571 ?  184 ARG B NH1   1 
ATOM   3316 N NH2   . ARG B 1 204 ? -18.82100 8.25300   53.72200 1.000 58.31916 ?  184 ARG B NH2   1 
ATOM   3317 N N     . GLU B 1 205 ? -16.35500 9.72200   48.05400 1.000 32.73213 ?  185 GLU B N     1 
ATOM   3318 C CA    . GLU B 1 205 ? -15.32800 9.00500   47.31000 1.000 35.20251 ?  185 GLU B CA    1 
ATOM   3319 C C     . GLU B 1 205 ? -15.60100 7.50900   47.23900 1.000 36.93708 ?  185 GLU B C     1 
ATOM   3320 O O     . GLU B 1 205 ? -15.03200 6.82900   46.37900 1.000 35.99327 ?  185 GLU B O     1 
ATOM   3321 C CB    . GLU B 1 205 ? -13.95200 9.27700   47.91800 1.000 34.87411 ?  185 GLU B CB    1 
ATOM   3322 C CG    . GLU B 1 205 ? -13.24800 10.44700  47.24300 1.000 43.57189 ?  185 GLU B CG    1 
ATOM   3323 C CD    . GLU B 1 205 ? -12.06500 10.96900  48.03800 1.000 53.94057 ?  185 GLU B CD    1 
ATOM   3324 O OE1   . GLU B 1 205 ? -11.04600 10.25600  48.11700 1.000 54.73659 ?  185 GLU B OE1   1 
ATOM   3325 O OE2   . GLU B 1 205 ? -12.15200 12.10100  48.57500 1.000 55.14507 -1 185 GLU B OE2   1 
ATOM   3326 N N     . GLU B 1 206 ? -16.46800 6.98200   48.10300 1.000 33.35510 ?  186 GLU B N     1 
ATOM   3327 C CA    . GLU B 1 206 ? -16.82100 5.57400   48.00600 1.000 37.47266 ?  186 GLU B CA    1 
ATOM   3328 C C     . GLU B 1 206 ? -17.65000 5.27600   46.75900 1.000 36.07932 ?  186 GLU B C     1 
ATOM   3329 O O     . GLU B 1 206 ? -17.65300 4.13700   46.28700 1.000 36.04516 ?  186 GLU B O     1 
ATOM   3330 C CB    . GLU B 1 206 ? -17.55200 5.13700   49.28000 1.000 40.38868 ?  186 GLU B CB    1 
ATOM   3331 C CG    . GLU B 1 206 ? -19.06900 5.26500   49.24200 1.000 47.17660 ?  186 GLU B CG    1 
ATOM   3332 C CD    . GLU B 1 206 ? -19.74100 4.78600   50.53700 1.000 51.92052 ?  186 GLU B CD    1 
ATOM   3333 O OE1   . GLU B 1 206 ? -19.75900 5.55600   51.52400 1.000 52.37350 ?  186 GLU B OE1   1 
ATOM   3334 O OE2   . GLU B 1 206 ? -20.24500 3.63800   50.56800 1.000 57.29318 -1 186 GLU B OE2   1 
ATOM   3335 N N     . TYR B 1 207 ? -18.32400 6.27500   46.19400 1.000 35.25733 ?  187 TYR B N     1 
ATOM   3336 C CA    . TYR B 1 207 ? -19.07300 6.11100   44.95500 1.000 31.39818 ?  187 TYR B CA    1 
ATOM   3337 C C     . TYR B 1 207 ? -18.42100 6.79700   43.76600 1.000 31.31764 ?  187 TYR B C     1 
ATOM   3338 O O     . TYR B 1 207 ? -18.44900 6.25300   42.66100 1.000 29.25590 ?  187 TYR B O     1 
ATOM   3339 C CB    . TYR B 1 207 ? -20.50300 6.64500   45.11800 1.000 30.27426 ?  187 TYR B CB    1 
ATOM   3340 C CG    . TYR B 1 207 ? -21.32500 5.92300   46.17200 1.000 38.62515 ?  187 TYR B CG    1 
ATOM   3341 C CD1   . TYR B 1 207 ? -21.63200 4.57300   46.04300 1.000 37.77955 ?  187 TYR B CD1   1 
ATOM   3342 C CD2   . TYR B 1 207 ? -21.78500 6.59300   47.30200 1.000 38.78584 ?  187 TYR B CD2   1 
ATOM   3343 C CE1   . TYR B 1 207 ? -22.38900 3.91400   47.00400 1.000 41.26936 ?  187 TYR B CE1   1 
ATOM   3344 C CE2   . TYR B 1 207 ? -22.53400 5.94000   48.27000 1.000 39.67315 ?  187 TYR B CE2   1 
ATOM   3345 C CZ    . TYR B 1 207 ? -22.83300 4.60400   48.11500 1.000 44.59723 ?  187 TYR B CZ    1 
ATOM   3346 O OH    . TYR B 1 207 ? -23.58200 3.95300   49.07200 1.000 50.33264 ?  187 TYR B OH    1 
ATOM   3347 N N     . THR B 1 208 ? -17.81500 7.96900   43.97000 1.000 29.86477 ?  188 THR B N     1 
ATOM   3348 C CA    . THR B 1 208 ? -17.36300 8.83200   42.88100 1.000 29.40611 ?  188 THR B CA    1 
ATOM   3349 C C     . THR B 1 208 ? -15.94900 9.32300   43.14900 1.000 28.70293 ?  188 THR B C     1 
ATOM   3350 O O     . THR B 1 208 ? -15.66100 9.83300   44.23400 1.000 32.67418 ?  188 THR B O     1 
ATOM   3351 C CB    . THR B 1 208 ? -18.30700 10.03400  42.72000 1.000 28.33948 ?  188 THR B CB    1 
ATOM   3352 O OG1   . THR B 1 208 ? -19.65900 9.56500   42.66200 1.000 29.24543 ?  188 THR B OG1   1 
ATOM   3353 C CG2   . THR B 1 208 ? -17.97700 10.84900  41.46100 1.000 27.14806 ?  188 THR B CG2   1 
ATOM   3354 N N     . ALA B 1 209 ? -15.07200 9.17200   42.16100 1.000 28.83084 ?  189 ALA B N     1 
ATOM   3355 C CA    . ALA B 1 209 ? -13.74500 9.75900   42.26100 1.000 31.97957 ?  189 ALA B CA    1 
ATOM   3356 C C     . ALA B 1 209 ? -13.85800 11.27200  42.39800 1.000 31.26169 ?  189 ALA B C     1 
ATOM   3357 O O     . ALA B 1 209 ? -14.62100 11.92100  41.67600 1.000 27.02771 ?  189 ALA B O     1 
ATOM   3358 C CB    . ALA B 1 209 ? -12.90300 9.39900   41.03900 1.000 28.45815 ?  189 ALA B CB    1 
ATOM   3359 N N     . LYS B 1 210 ? -13.10800 11.82400  43.35100 1.000 31.79541 ?  190 LYS B N     1 
ATOM   3360 C CA    . LYS B 1 210 ? -13.12700 13.25900  43.60500 1.000 28.32617 ?  190 LYS B CA    1 
ATOM   3361 C C     . LYS B 1 210 ? -13.04200 14.07500  42.32100 1.000 28.93627 ?  190 LYS B C     1 
ATOM   3362 O O     . LYS B 1 210 ? -13.82700 15.00200  42.11000 1.000 28.83850 ?  190 LYS B O     1 
ATOM   3363 C CB    . LYS B 1 210 ? -11.98400 13.62400  44.55100 1.000 34.80808 ?  190 LYS B CB    1 
ATOM   3364 C CG    . LYS B 1 210 ? -11.89500 15.12100  44.84100 1.000 34.20119 ?  190 LYS B CG    1 
ATOM   3365 C CD    . LYS B 1 210 ? -12.60200 15.49900  46.13800 1.000 41.68687 ?  190 LYS B CD    1 
ATOM   3366 C CE    . LYS B 1 210 ? -11.91900 16.70900  46.78400 1.000 39.33163 ?  190 LYS B CE    1 
ATOM   3367 N N     . LYS B 1 211 ? -12.12500 13.71900  41.42400 1.000 29.64483 ?  191 LYS B N     1 
ATOM   3368 C CA    . LYS B 1 211 ? -12.00900 14.43900  40.16100 1.000 31.11865 ?  191 LYS B CA    1 
ATOM   3369 C C     . LYS B 1 211 ? -13.26900 14.34500  39.30500 1.000 29.80005 ?  191 LYS B C     1 
ATOM   3370 O O     . LYS B 1 211 ? -13.39400 15.10200  38.33800 1.000 28.80484 ?  191 LYS B O     1 
ATOM   3371 C CB    . LYS B 1 211 ? -10.80900 13.91200  39.37200 1.000 29.00543 ?  191 LYS B CB    1 
ATOM   3372 C CG    . LYS B 1 211 ? -10.94800 12.45100  38.95400 1.000 35.17440 ?  191 LYS B CG    1 
ATOM   3373 C CD    . LYS B 1 211 ? -9.73400  11.98900  38.15000 1.000 36.33417 ?  191 LYS B CD    1 
ATOM   3374 C CE    . LYS B 1 211 ? -9.85500  10.52800  37.72200 1.000 36.60664 ?  191 LYS B CE    1 
ATOM   3375 N NZ    . LYS B 1 211 ? -8.66700  10.08600  36.93900 1.000 36.75525 ?  191 LYS B NZ    1 
ATOM   3376 N N     . PHE B 1 212 ? -14.20300 13.45400  39.63300 1.000 28.27069 ?  192 PHE B N     1 
ATOM   3377 C CA    . PHE B 1 212 ? -15.43100 13.30500  38.86700 1.000 27.90934 ?  192 PHE B CA    1 
ATOM   3378 C C     . PHE B 1 212 ? -16.64700 13.89900  39.57100 1.000 26.90190 ?  192 PHE B C     1 
ATOM   3379 O O     . PHE B 1 212 ? -17.74500 13.88700  39.00500 1.000 28.75050 ?  192 PHE B O     1 
ATOM   3380 C CB    . PHE B 1 212 ? -15.65100 11.82400  38.55500 1.000 30.12029 ?  192 PHE B CB    1 
ATOM   3381 C CG    . PHE B 1 212 ? -14.66700 11.27700  37.54600 1.000 34.16940 ?  192 PHE B CG    1 
ATOM   3382 C CD1   . PHE B 1 212 ? -14.13200 12.11400  36.56000 1.000 31.32849 ?  192 PHE B CD1   1 
ATOM   3383 C CD2   . PHE B 1 212 ? -14.27800 9.93800   37.57400 1.000 29.29341 ?  192 PHE B CD2   1 
ATOM   3384 C CE1   . PHE B 1 212 ? -13.22500 11.62500  35.62300 1.000 33.93704 ?  192 PHE B CE1   1 
ATOM   3385 C CE2   . PHE B 1 212 ? -13.37300 9.44300   36.63800 1.000 29.47378 ?  192 PHE B CE2   1 
ATOM   3386 C CZ    . PHE B 1 212 ? -12.84500 10.28600  35.66400 1.000 30.47107 ?  192 PHE B CZ    1 
ATOM   3387 N N     . TRP B 1 213 ? -16.47600 14.41900  40.78400 1.000 27.27609 ?  193 TRP B N     1 
ATOM   3388 C CA    . TRP B 1 213 ? -17.56000 15.12000  41.45900 1.000 26.55470 ?  193 TRP B CA    1 
ATOM   3389 C C     . TRP B 1 213 ? -18.02300 16.29200  40.60300 1.000 27.18452 ?  193 TRP B C     1 
ATOM   3390 O O     . TRP B 1 213 ? -17.21200 17.10400  40.14900 1.000 27.48423 ?  193 TRP B O     1 
ATOM   3391 C CB    . TRP B 1 213 ? -17.09700 15.63800  42.81800 1.000 25.94162 ?  193 TRP B CB    1 
ATOM   3392 C CG    . TRP B 1 213 ? -16.82100 14.59000  43.84100 1.000 27.91931 ?  193 TRP B CG    1 
ATOM   3393 C CD1   . TRP B 1 213 ? -16.71300 13.24200  43.64100 1.000 29.89587 ?  193 TRP B CD1   1 
ATOM   3394 C CD2   . TRP B 1 213 ? -16.58700 14.81200  45.23200 1.000 29.91899 ?  193 TRP B CD2   1 
ATOM   3395 N NE1   . TRP B 1 213 ? -16.43600 12.60700  44.83000 1.000 31.59114 ?  193 TRP B NE1   1 
ATOM   3396 C CE2   . TRP B 1 213 ? -16.35300 13.55200  45.82300 1.000 31.24291 ?  193 TRP B CE2   1 
ATOM   3397 C CE3   . TRP B 1 213 ? -16.55300 15.95700  46.03900 1.000 28.64713 ?  193 TRP B CE3   1 
ATOM   3398 C CZ2   . TRP B 1 213 ? -16.09200 13.40500  47.18100 1.000 29.57877 ?  193 TRP B CZ2   1 
ATOM   3399 C CZ3   . TRP B 1 213 ? -16.29300 15.80800  47.39100 1.000 31.74504 ?  193 TRP B CZ3   1 
ATOM   3400 C CH2   . TRP B 1 213 ? -16.06400 14.54200  47.94800 1.000 33.97792 ?  193 TRP B CH2   1 
ATOM   3401 N N     . ILE B 1 214 ? -19.33300 16.38000  40.38000 1.000 23.78471 ?  194 ILE B N     1 
ATOM   3402 C CA    . ILE B 1 214 ? -19.85300 17.48700  39.59400 1.000 24.47375 ?  194 ILE B CA    1 
ATOM   3403 C C     . ILE B 1 214 ? -19.92100 18.76500  40.41600 1.000 28.35582 ?  194 ILE B C     1 
ATOM   3404 O O     . ILE B 1 214 ? -19.86900 19.86600  39.84900 1.000 25.99559 ?  194 ILE B O     1 
ATOM   3405 C CB    . ILE B 1 214 ? -21.21100 17.08400  39.00000 1.000 27.08404 ?  194 ILE B CB    1 
ATOM   3406 C CG1   . ILE B 1 214 ? -20.99400 15.95900  37.97900 1.000 26.54113 ?  194 ILE B CG1   1 
ATOM   3407 C CG2   . ILE B 1 214 ? -21.90600 18.26900  38.34500 1.000 26.41823 ?  194 ILE B CG2   1 
ATOM   3408 C CD1   . ILE B 1 214 ? -22.26700 15.30100  37.54900 1.000 30.68720 ?  194 ILE B CD1   1 
ATOM   3409 N N     . GLY B 1 215 ? -20.00000 18.65500  41.73600 1.000 26.99829 ?  195 GLY B N     1 
ATOM   3410 C CA    . GLY B 1 215 ? -19.92600 19.82000  42.58700 1.000 28.10189 ?  195 GLY B CA    1 
ATOM   3411 C C     . GLY B 1 215 ? -19.57600 19.40200  43.99300 1.000 29.89077 ?  195 GLY B C     1 
ATOM   3412 O O     . GLY B 1 215 ? -19.18600 18.26100  44.24100 1.000 28.14987 ?  195 GLY B O     1 
ATOM   3413 N N     . GLY B 1 216 ? -19.73800 20.33900  44.92300 1.000 29.28712 ?  196 GLY B N     1 
ATOM   3414 C CA    . GLY B 1 216 ? -19.44300 20.02700  46.30900 1.000 28.83099 ?  196 GLY B CA    1 
ATOM   3415 C C     . GLY B 1 216 ? -17.97000 19.91500  46.63000 1.000 31.93374 ?  196 GLY B C     1 
ATOM   3416 O O     . GLY B 1 216 ? -17.59800 19.16800  47.53700 1.000 34.19985 ?  196 GLY B O     1 
ATOM   3417 N N     . TYR B 1 217 ? -17.12000 20.63900  45.90400 1.000 32.30878 ?  197 TYR B N     1 
ATOM   3418 C CA    . TYR B 1 217 ? -15.68500 20.64700  46.13400 1.000 33.32250 ?  197 TYR B CA    1 
ATOM   3419 C C     . TYR B 1 217 ? -15.15500 22.05800  45.90700 1.000 34.58751 ?  197 TYR B C     1 
ATOM   3420 O O     . TYR B 1 217 ? -15.80600 22.89800  45.28000 1.000 29.16554 ?  197 TYR B O     1 
ATOM   3421 C CB    . TYR B 1 217 ? -14.95800 19.66300  45.20900 1.000 32.60372 ?  197 TYR B CB    1 
ATOM   3422 C CG    . TYR B 1 217 ? -15.07100 20.02800  43.74900 1.000 34.00807 ?  197 TYR B CG    1 
ATOM   3423 C CD1   . TYR B 1 217 ? -16.13900 19.57600  42.99100 1.000 30.18679 ?  197 TYR B CD1   1 
ATOM   3424 C CD2   . TYR B 1 217 ? -14.11400 20.83000  43.12600 1.000 35.30148 ?  197 TYR B CD2   1 
ATOM   3425 C CE1   . TYR B 1 217 ? -16.25400 19.90300  41.64900 1.000 31.25178 ?  197 TYR B CE1   1 
ATOM   3426 C CE2   . TYR B 1 217 ? -14.22400 21.16600  41.78200 1.000 32.93103 ?  197 TYR B CE2   1 
ATOM   3427 C CZ    . TYR B 1 217 ? -15.29600 20.69700  41.05000 1.000 31.38910 ?  197 TYR B CZ    1 
ATOM   3428 O OH    . TYR B 1 217 ? -15.43200 21.02100  39.71700 1.000 32.45185 ?  197 TYR B OH    1 
ATOM   3429 N N     . VAL B 1 218 ? -13.95400 22.30800  46.41600 1.000 38.08471 ?  198 VAL B N     1 
ATOM   3430 C CA    . VAL B 1 218 ? -13.25500 23.56700  46.19100 1.000 34.33842 ?  198 VAL B CA    1 
ATOM   3431 C C     . VAL B 1 218 ? -12.28300 23.35800  45.04400 1.000 31.80956 ?  198 VAL B C     1 
ATOM   3432 O O     . VAL B 1 218 ? -11.45500 22.44000  45.08600 1.000 33.23705 ?  198 VAL B O     1 
ATOM   3433 C CB    . VAL B 1 218 ? -12.52600 24.03500  47.46000 1.000 35.20500 ?  198 VAL B CB    1 
ATOM   3434 C CG1   . VAL B 1 218 ? -11.80500 25.36700  47.20500 1.000 37.55647 ?  198 VAL B CG1   1 
ATOM   3435 C CG2   . VAL B 1 218 ? -13.50800 24.15700  48.62100 1.000 37.19098 ?  198 VAL B CG2   1 
ATOM   3436 N N     . ASP B 1 219 ? -12.39000 24.18600  44.00700 1.000 29.70349 ?  199 ASP B N     1 
ATOM   3437 C CA    . ASP B 1 219 ? -11.50700 24.02100  42.86500 1.000 31.95452 ?  199 ASP B CA    1 
ATOM   3438 C C     . ASP B 1 219 ? -10.09400 24.48200  43.23200 1.000 36.46328 ?  199 ASP B C     1 
ATOM   3439 O O     . ASP B 1 219 ? -9.81700  24.89900  44.36400 1.000 31.46509 ?  199 ASP B O     1 
ATOM   3440 C CB    . ASP B 1 219 ? -12.06100 24.75000  41.63300 1.000 32.36133 ?  199 ASP B CB    1 
ATOM   3441 C CG    . ASP B 1 219 ? -12.17000 26.27500  41.81100 1.000 41.51202 ?  199 ASP B CG    1 
ATOM   3442 O OD1   . ASP B 1 219 ? -11.30800 26.90900  42.46400 1.000 35.33788 ?  199 ASP B OD1   1 
ATOM   3443 O OD2   . ASP B 1 219 ? -13.13000 26.84900  41.25200 1.000 44.55603 -1 199 ASP B OD2   1 
ATOM   3444 N N     . GLU B 1 220 ? -9.18500  24.40400  42.25300 1.000 31.35933 ?  200 GLU B N     1 
ATOM   3445 C CA    . GLU B 1 220 ? -7.78700  24.74000  42.50900 1.000 37.27962 ?  200 GLU B CA    1 
ATOM   3446 C C     . GLU B 1 220 ? -7.57900  26.22600  42.79300 1.000 36.02700 ?  200 GLU B C     1 
ATOM   3447 O O     . GLU B 1 220 ? -6.51300  26.60500  43.28700 1.000 39.76166 ?  200 GLU B O     1 
ATOM   3448 C CB    . GLU B 1 220 ? -6.90600  24.30600  41.33100 1.000 36.30803 ?  200 GLU B CB    1 
ATOM   3449 C CG    . GLU B 1 220 ? -7.26600  24.95100  40.00300 1.000 42.16240 ?  200 GLU B CG    1 
ATOM   3450 N N     . ASN B 1 221 ? -8.56300  27.07000  42.49900 1.000 31.21725 ?  201 ASN B N     1 
ATOM   3451 C CA    . ASN B 1 221 ? -8.46200  28.49700  42.75400 1.000 33.00080 ?  201 ASN B CA    1 
ATOM   3452 C C     . ASN B 1 221 ? -9.09100  28.90600  44.07700 1.000 34.04820 ?  201 ASN B C     1 
ATOM   3453 O O     . ASN B 1 221 ? -9.21300  30.10400  44.34900 1.000 34.56536 ?  201 ASN B O     1 
ATOM   3454 C CB    . ASN B 1 221 ? -9.10900  29.27800  41.61400 1.000 33.21530 ?  201 ASN B CB    1 
ATOM   3455 C CG    . ASN B 1 221 ? -8.53600  28.91200  40.26600 1.000 35.02253 ?  201 ASN B CG    1 
ATOM   3456 O OD1   . ASN B 1 221 ? -7.32600  28.72400  40.12100 1.000 35.07705 ?  201 ASN B OD1   1 
ATOM   3457 N ND2   . ASN B 1 221 ? -9.40000  28.81600  39.26700 1.000 32.85509 ?  201 ASN B ND2   1 
ATOM   3458 N N     . GLY B 1 222 ? -9.50400  27.94600  44.89700 1.000 34.04247 ?  202 GLY B N     1 
ATOM   3459 C CA    . GLY B 1 222 ? -10.11000 28.27300  46.16800 1.000 32.79875 ?  202 GLY B CA    1 
ATOM   3460 C C     . GLY B 1 222 ? -11.58000 28.62500  46.12200 1.000 34.43087 ?  202 GLY B C     1 
ATOM   3461 O O     . GLY B 1 222 ? -12.11800 29.07800  47.13800 1.000 36.72948 ?  202 GLY B O     1 
ATOM   3462 N N     . LYS B 1 223 ? -12.25400 28.42600  44.99100 1.000 31.37759 ?  203 LYS B N     1 
ATOM   3463 C CA    . LYS B 1 223 ? -13.67100 28.74000  44.86700 1.000 33.98105 ?  203 LYS B CA    1 
ATOM   3464 C C     . LYS B 1 223 ? -14.50500 27.47500  45.01800 1.000 36.85899 ?  203 LYS B C     1 
ATOM   3465 O O     . LYS B 1 223 ? -14.13000 26.40100  44.53500 1.000 34.28961 ?  203 LYS B O     1 
ATOM   3466 C CB    . LYS B 1 223 ? -13.97700 29.40700  43.52500 1.000 39.34367 ?  203 LYS B CB    1 
ATOM   3467 C CG    . LYS B 1 223 ? -13.28300 30.75700  43.34500 1.000 41.55678 ?  203 LYS B CG    1 
ATOM   3468 C CD    . LYS B 1 223 ? -14.18000 31.94300  43.68200 1.000 40.07547 ?  203 LYS B CD    1 
ATOM   3469 C CE    . LYS B 1 223 ? -13.37300 33.24200  43.66500 1.000 38.64617 ?  203 LYS B CE    1 
ATOM   3470 N NZ    . LYS B 1 223 ? -13.91800 34.26200  42.70900 1.000 42.91949 ?  203 LYS B NZ    1 
ATOM   3471 N N     . GLU B 1 224 ? -15.63100 27.60700  45.70500 1.000 36.17052 ?  204 GLU B N     1 
ATOM   3472 C CA    . GLU B 1 224 ? -16.52300 26.47900  45.91400 1.000 34.95821 ?  204 GLU B CA    1 
ATOM   3473 C C     . GLU B 1 224 ? -17.36800 26.25400  44.66900 1.000 34.09082 ?  204 GLU B C     1 
ATOM   3474 O O     . GLU B 1 224 ? -17.93900 27.20200  44.11600 1.000 35.09268 ?  204 GLU B O     1 
ATOM   3475 C CB    . GLU B 1 224 ? -17.40400 26.73600  47.13400 1.000 40.06311 ?  204 GLU B CB    1 
ATOM   3476 C CG    . GLU B 1 224 ? -16.59900 26.81900  48.43000 1.000 38.22936 ?  204 GLU B CG    1 
ATOM   3477 C CD    . GLU B 1 224 ? -17.47300 26.92100  49.66200 1.000 44.72937 ?  204 GLU B CD    1 
ATOM   3478 O OE1   . GLU B 1 224 ? -18.70200 27.10200  49.51400 1.000 45.00199 ?  204 GLU B OE1   1 
ATOM   3479 O OE2   . GLU B 1 224 ? -16.92600 26.80200  50.78000 1.000 51.71313 -1 204 GLU B OE2   1 
ATOM   3480 N N     . VAL B 1 225 ? -17.43500 25.00300  44.22000 1.000 32.74112 ?  205 VAL B N     1 
ATOM   3481 C CA    . VAL B 1 225 ? -18.21500 24.62600  43.04400 1.000 31.58629 ?  205 VAL B CA    1 
ATOM   3482 C C     . VAL B 1 225 ? -19.52200 23.98500  43.50200 1.000 33.65969 ?  205 VAL B C     1 
ATOM   3483 O O     . VAL B 1 225 ? -19.52200 22.97100  44.21200 1.000 33.09963 ?  205 VAL B O     1 
ATOM   3484 C CB    . VAL B 1 225 ? -17.42700 23.67900  42.12800 1.000 34.46570 ?  205 VAL B CB    1 
ATOM   3485 C CG1   . VAL B 1 225 ? -18.28900 23.24700  40.94600 1.000 31.47455 ?  205 VAL B CG1   1 
ATOM   3486 C CG2   . VAL B 1 225 ? -16.15200 24.36500  41.64300 1.000 33.08524 ?  205 VAL B CG2   1 
ATOM   3487 N N     . SER B 1 226 ? -20.63700 24.58200  43.09800 1.000 28.47216 ?  206 SER B N     1 
ATOM   3488 C CA    . SER B 1 226 ? -21.94600 24.01500  43.36800 1.000 30.43513 ?  206 SER B CA    1 
ATOM   3489 C C     . SER B 1 226 ? -22.27900 22.96100  42.31900 1.000 31.76773 ?  206 SER B C     1 
ATOM   3490 O O     . SER B 1 226 ? -21.85500 23.06900  41.16300 1.000 29.59023 ?  206 SER B O     1 
ATOM   3491 C CB    . SER B 1 226 ? -22.99500 25.13000  43.39200 1.000 33.48063 ?  206 SER B CB    1 
ATOM   3492 O OG    . SER B 1 226 ? -23.48700 25.42700  42.10300 1.000 30.80805 ?  206 SER B OG    1 
ATOM   3493 N N     . THR B 1 227 ? -23.02000 21.92400  42.73200 1.000 26.24962 ?  207 THR B N     1 
ATOM   3494 C CA    . THR B 1 227 ? -23.33200 20.84400  41.79700 1.000 29.61353 ?  207 THR B CA    1 
ATOM   3495 C C     . THR B 1 227 ? -24.26200 21.32400  40.68700 1.000 28.35073 ?  207 THR B C     1 
ATOM   3496 O O     . THR B 1 227 ? -24.09800 20.93000  39.52500 1.000 27.05070 ?  207 THR B O     1 
ATOM   3497 C CB    . THR B 1 227 ? -23.93700 19.64100  42.52500 1.000 26.56086 ?  207 THR B CB    1 
ATOM   3498 O OG1   . THR B 1 227 ? -23.08900 19.24500  43.61500 1.000 26.05520 ?  207 THR B OG1   1 
ATOM   3499 C CG2   . THR B 1 227 ? -24.09100 18.45600  41.55100 1.000 26.75096 ?  207 THR B CG2   1 
ATOM   3500 N N     . LEU B 1 228 ? -25.23100 22.18500  41.01700 1.000 28.00471 ?  208 LEU B N     1 
ATOM   3501 C CA    . LEU B 1 228 ? -26.10200 22.73300  39.97900 1.000 30.10506 ?  208 LEU B CA    1 
ATOM   3502 C C     . LEU B 1 228 ? -25.29600 23.47100  38.91400 1.000 30.68167 ?  208 LEU B C     1 
ATOM   3503 O O     . LEU B 1 228 ? -25.56400 23.33800  37.71100 1.000 27.10824 ?  208 LEU B O     1 
ATOM   3504 C CB    . LEU B 1 228 ? -27.15200 23.65800  40.59800 1.000 30.56730 ?  208 LEU B CB    1 
ATOM   3505 C CG    . LEU B 1 228 ? -28.15000 24.26200  39.59800 1.000 32.04581 ?  208 LEU B CG    1 
ATOM   3506 C CD1   . LEU B 1 228 ? -28.96700 23.18200  38.89500 1.000 31.35252 ?  208 LEU B CD1   1 
ATOM   3507 C CD2   . LEU B 1 228 ? -29.06700 25.24800  40.29900 1.000 27.95177 ?  208 LEU B CD2   1 
ATOM   3508 N N     . GLU B 1 229 ? -24.27900 24.22400  39.33100 1.000 28.19104 ?  209 GLU B N     1 
ATOM   3509 C CA    . GLU B 1 229 ? -23.45000 24.91300  38.34800 1.000 30.93466 ?  209 GLU B CA    1 
ATOM   3510 C C     . GLU B 1 229 ? -22.64600 23.91300  37.52600 1.000 32.69540 ?  209 GLU B C     1 
ATOM   3511 O O     . GLU B 1 229 ? -22.53600 24.05200  36.30200 1.000 33.74799 ?  209 GLU B O     1 
ATOM   3512 C CB    . GLU B 1 229 ? -22.53400 25.93100  39.03900 1.000 29.63127 ?  209 GLU B CB    1 
ATOM   3513 N N     . GLY B 1 230 ? -22.09400 22.88300  38.17400 1.000 31.32726 ?  210 GLY B N     1 
ATOM   3514 C CA    . GLY B 1 230 ? -21.41400 21.84600  37.41700 1.000 28.47187 ?  210 GLY B CA    1 
ATOM   3515 C C     . GLY B 1 230 ? -22.33600 21.19300  36.40500 1.000 30.03557 ?  210 GLY B C     1 
ATOM   3516 O O     . GLY B 1 230 ? -21.92500 20.88200  35.28500 1.000 27.03025 ?  210 GLY B O     1 
ATOM   3517 N N     . LEU B 1 231 ? -23.60500 21.00400  36.78200 1.000 30.47868 ?  211 LEU B N     1 
ATOM   3518 C CA    . LEU B 1 231 ? -24.58600 20.41500  35.87400 1.000 28.50851 ?  211 LEU B CA    1 
ATOM   3519 C C     . LEU B 1 231 ? -24.85200 21.32800  34.68800 1.000 29.71448 ?  211 LEU B C     1 
ATOM   3520 O O     . LEU B 1 231 ? -24.95500 20.85900  33.54800 1.000 30.38832 ?  211 LEU B O     1 
ATOM   3521 C CB    . LEU B 1 231 ? -25.88600 20.12600  36.63100 1.000 24.68432 ?  211 LEU B CB    1 
ATOM   3522 C CG    . LEU B 1 231 ? -25.81600 18.97200  37.63600 1.000 24.48147 ?  211 LEU B CG    1 
ATOM   3523 C CD1   . LEU B 1 231 ? -27.07500 18.91700  38.50100 1.000 25.84509 ?  211 LEU B CD1   1 
ATOM   3524 C CD2   . LEU B 1 231 ? -25.58500 17.62300  36.93400 1.000 23.10764 ?  211 LEU B CD2   1 
ATOM   3525 N N     . LYS B 1 232 ? -24.97500 22.63600  34.93300 1.000 29.19778 ?  212 LYS B N     1 
ATOM   3526 C CA    . LYS B 1 232 ? -25.17000 23.56800  33.82800 1.000 30.02870 ?  212 LYS B CA    1 
ATOM   3527 C C     . LYS B 1 232 ? -24.01000 23.49200  32.84500 1.000 33.38848 ?  212 LYS B C     1 
ATOM   3528 O O     . LYS B 1 232 ? -24.21400 23.42700  31.62700 1.000 32.02973 ?  212 LYS B O     1 
ATOM   3529 C CB    . LYS B 1 232 ? -25.33700 24.98600  34.36500 1.000 33.11674 ?  212 LYS B CB    1 
ATOM   3530 C CG    . LYS B 1 232 ? -26.61800 25.18600  35.15300 1.000 32.48293 ?  212 LYS B CG    1 
ATOM   3531 C CD    . LYS B 1 232 ? -27.02500 26.64900  35.17400 1.000 39.80479 ?  212 LYS B CD    1 
ATOM   3532 C CE    . LYS B 1 232 ? -27.07300 27.18400  36.58700 1.000 39.47111 ?  212 LYS B CE    1 
ATOM   3533 N NZ    . LYS B 1 232 ? -27.05900 28.68300  36.61700 1.000 46.32818 ?  212 LYS B NZ    1 
ATOM   3534 N N     . GLU B 1 233 ? -22.78000 23.46900  33.36600 1.000 31.05098 ?  213 GLU B N     1 
ATOM   3535 C CA    . GLU B 1 233 ? -21.59800 23.42300  32.50900 1.000 34.49377 ?  213 GLU B CA    1 
ATOM   3536 C C     . GLU B 1 233 ? -21.61500 22.19400  31.60000 1.000 32.11848 ?  213 GLU B C     1 
ATOM   3537 O O     . GLU B 1 233 ? -21.30000 22.28900  30.40900 1.000 30.50543 ?  213 GLU B O     1 
ATOM   3538 C CB    . GLU B 1 233 ? -20.33100 23.45900  33.37200 1.000 30.93971 ?  213 GLU B CB    1 
ATOM   3539 C CG    . GLU B 1 233 ? -19.06500 22.98400  32.66600 1.000 40.10160 ?  213 GLU B CG    1 
ATOM   3540 C CD    . GLU B 1 233 ? -17.79300 23.53100  33.29600 1.000 40.38670 ?  213 GLU B CD    1 
ATOM   3541 N N     . ILE B 1 234 ? -22.00300 21.03700  32.13400 1.000 33.50535 ?  214 ILE B N     1 
ATOM   3542 C CA    . ILE B 1 234 ? -22.08800 19.84100  31.30500 1.000 33.07401 ?  214 ILE B CA    1 
ATOM   3543 C C     . ILE B 1 234 ? -23.28200 19.92400  30.36100 1.000 33.74422 ?  214 ILE B C     1 
ATOM   3544 O O     . ILE B 1 234 ? -23.15100 19.71800  29.14900 1.000 32.15904 ?  214 ILE B O     1 
ATOM   3545 C CB    . ILE B 1 234 ? -22.14800 18.57400  32.18000 1.000 31.68153 ?  214 ILE B CB    1 
ATOM   3546 C CG1   . ILE B 1 234 ? -20.82400 18.37800  32.92700 1.000 32.90478 ?  214 ILE B CG1   1 
ATOM   3547 C CG2   . ILE B 1 234 ? -22.47300 17.35700  31.32400 1.000 27.91489 ?  214 ILE B CG2   1 
ATOM   3548 C CD1   . ILE B 1 234 ? -20.91400 17.41700  34.09000 1.000 32.39397 ?  214 ILE B CD1   1 
ATOM   3549 N N     . LEU B 1 235 ? -24.46100 20.23300  30.89300 1.000 31.45131 ?  215 LEU B N     1 
ATOM   3550 C CA    . LEU B 1 235 ? -25.68200 20.01200  30.13300 1.000 31.56023 ?  215 LEU B CA    1 
ATOM   3551 C C     . LEU B 1 235 ? -26.08700 21.18000  29.25000 1.000 31.99887 ?  215 LEU B C     1 
ATOM   3552 O O     . LEU B 1 235 ? -26.89000 20.98500  28.33000 1.000 32.25714 ?  215 LEU B O     1 
ATOM   3553 C CB    . LEU B 1 235 ? -26.84400 19.68000  31.07100 1.000 29.18161 ?  215 LEU B CB    1 
ATOM   3554 C CG    . LEU B 1 235 ? -26.67400 18.37700  31.84100 1.000 29.19359 ?  215 LEU B CG    1 
ATOM   3555 C CD1   . LEU B 1 235 ? -27.62100 18.34300  33.02600 1.000 26.78588 ?  215 LEU B CD1   1 
ATOM   3556 C CD2   . LEU B 1 235 ? -26.90900 17.18900  30.90300 1.000 29.50780 ?  215 LEU B CD2   1 
ATOM   3557 N N     . GLU B 1 236 ? -25.57400 22.38200  29.49100 1.000 31.87519 ?  216 GLU B N     1 
ATOM   3558 C CA    . GLU B 1 236 ? -26.07800 23.50200  28.70300 1.000 36.24909 ?  216 GLU B CA    1 
ATOM   3559 C C     . GLU B 1 236 ? -25.55700 23.50500  27.27000 1.000 36.13390 ?  216 GLU B C     1 
ATOM   3560 O O     . GLU B 1 236 ? -26.03400 24.30700  26.46300 1.000 34.12309 ?  216 GLU B O     1 
ATOM   3561 C CB    . GLU B 1 236 ? -25.76300 24.82800  29.39700 1.000 35.63427 ?  216 GLU B CB    1 
ATOM   3562 C CG    . GLU B 1 236 ? -26.77400 25.12800  30.49800 1.000 37.44683 ?  216 GLU B CG    1 
ATOM   3563 C CD    . GLU B 1 236 ? -26.54700 26.46700  31.17000 1.000 40.78514 ?  216 GLU B CD    1 
ATOM   3564 O OE1   . GLU B 1 236 ? -25.41300 26.99100  31.10700 1.000 40.07830 ?  216 GLU B OE1   1 
ATOM   3565 O OE2   . GLU B 1 236 ? -27.51300 26.99500  31.75900 1.000 38.55992 -1 216 GLU B OE2   1 
ATOM   3566 N N     . ILE B 1 237 ? -24.61200 22.61900  26.93400 1.000 36.50764 ?  217 ILE B N     1 
ATOM   3567 C CA    . ILE B 1 237 ? -24.27100 22.38400  25.53500 1.000 35.74865 ?  217 ILE B CA    1 
ATOM   3568 C C     . ILE B 1 237 ? -25.49700 21.93500  24.74500 1.000 39.68656 ?  217 ILE B C     1 
ATOM   3569 O O     . ILE B 1 237 ? -25.69500 22.35300  23.59800 1.000 37.34245 ?  217 ILE B O     1 
ATOM   3570 C CB    . ILE B 1 237 ? -23.13200 21.35800  25.43100 1.000 39.30114 ?  217 ILE B CB    1 
ATOM   3571 C CG1   . ILE B 1 237 ? -21.90400 21.85700  26.18900 1.000 42.09329 ?  217 ILE B CG1   1 
ATOM   3572 C CG2   . ILE B 1 237 ? -22.81000 21.05000  23.98100 1.000 39.63396 ?  217 ILE B CG2   1 
ATOM   3573 C CD1   . ILE B 1 237 ? -21.01300 20.74300  26.68800 1.000 41.11049 ?  217 ILE B CD1   1 
ATOM   3574 N N     . HIS B 1 238 ? -26.34200 21.08500  25.33700 1.000 35.13999 ?  218 HIS B N     1 
ATOM   3575 C CA    . HIS B 1 238 ? -27.46600 20.50900  24.60900 1.000 34.23435 ?  218 HIS B CA    1 
ATOM   3576 C C     . HIS B 1 238 ? -28.81700 20.68200  25.28300 1.000 34.19488 ?  218 HIS B C     1 
ATOM   3577 O O     . HIS B 1 238 ? -29.82200 20.22200  24.72800 1.000 36.55195 ?  218 HIS B O     1 
ATOM   3578 C CB    . HIS B 1 238 ? -27.22900 19.01100  24.35600 1.000 36.12446 ?  218 HIS B CB    1 
ATOM   3579 C CG    . HIS B 1 238 ? -26.08600 18.73300  23.43100 1.000 39.32331 ?  218 HIS B CG    1 
ATOM   3580 N ND1   . HIS B 1 238 ? -24.92000 18.13000  23.84900 1.000 39.48781 ?  218 HIS B ND1   1 
ATOM   3581 C CD2   . HIS B 1 238 ? -25.93100 18.98100  22.10900 1.000 37.12937 ?  218 HIS B CD2   1 
ATOM   3582 C CE1   . HIS B 1 238 ? -24.09200 18.02200  22.82400 1.000 43.59182 ?  218 HIS B CE1   1 
ATOM   3583 N NE2   . HIS B 1 238 ? -24.68400 18.52500  21.75500 1.000 39.40844 ?  218 HIS B NE2   1 
ATOM   3584 N N     . PHE B 1 239 ? -28.88200 21.32700  26.44600 1.000 35.53567 ?  219 PHE B N     1 
ATOM   3585 C CA    . PHE B 1 239 ? -30.13200 21.47300  27.17700 1.000 32.52604 ?  219 PHE B CA    1 
ATOM   3586 C C     . PHE B 1 239 ? -30.27600 22.91400  27.64000 1.000 34.78221 ?  219 PHE B C     1 
ATOM   3587 O O     . PHE B 1 239 ? -29.30200 23.66400  27.72500 1.000 35.49272 ?  219 PHE B O     1 
ATOM   3588 C CB    . PHE B 1 239 ? -30.21300 20.55800  28.41000 1.000 33.01437 ?  219 PHE B CB    1 
ATOM   3589 C CG    . PHE B 1 239 ? -30.25900 19.07700  28.09400 1.000 31.11035 ?  219 PHE B CG    1 
ATOM   3590 C CD1   . PHE B 1 239 ? -29.09000 18.36900  27.87400 1.000 30.87534 ?  219 PHE B CD1   1 
ATOM   3591 C CD2   . PHE B 1 239 ? -31.46400 18.40100  28.05300 1.000 28.47924 ?  219 PHE B CD2   1 
ATOM   3592 C CE1   . PHE B 1 239 ? -29.12100 17.01400  27.59900 1.000 31.83851 ?  219 PHE B CE1   1 
ATOM   3593 C CE2   . PHE B 1 239 ? -31.50700 17.03900  27.78100 1.000 33.40547 ?  219 PHE B CE2   1 
ATOM   3594 C CZ    . PHE B 1 239 ? -30.33700 16.34600  27.54900 1.000 31.83562 ?  219 PHE B CZ    1 
ATOM   3595 N N     . GLU B 1 240 ? -31.51300 23.28100  27.95400 1.000 32.32546 ?  220 GLU B N     1 
ATOM   3596 C CA    . GLU B 1 240 ? -31.82500 24.52000  28.64900 1.000 36.51152 ?  220 GLU B CA    1 
ATOM   3597 C C     . GLU B 1 240 ? -32.39800 24.17500  30.01900 1.000 34.80402 ?  220 GLU B C     1 
ATOM   3598 O O     . GLU B 1 240 ? -33.30000 23.33200  30.12600 1.000 30.91487 ?  220 GLU B O     1 
ATOM   3599 C CB    . GLU B 1 240 ? -32.81300 25.36000  27.84200 1.000 37.93379 ?  220 GLU B CB    1 
ATOM   3600 C CG    . GLU B 1 240 ? -33.79700 26.15500  28.68000 1.000 45.33461 ?  220 GLU B CG    1 
ATOM   3601 C CD    . GLU B 1 240 ? -34.82700 26.88600  27.82400 1.000 56.69079 ?  220 GLU B CD    1 
ATOM   3602 O OE1   . GLU B 1 240 ? -34.85200 26.66700  26.58800 1.000 55.84222 ?  220 GLU B OE1   1 
ATOM   3603 O OE2   . GLU B 1 240 ? -35.62000 27.66900  28.39300 1.000 59.67038 -1 220 GLU B OE2   1 
ATOM   3604 N N     . LEU B 1 241 ? -31.85500 24.80300  31.06400 1.000 31.65660 ?  221 LEU B N     1 
ATOM   3605 C CA    . LEU B 1 241 ? -32.35600 24.59300  32.41700 1.000 32.15361 ?  221 LEU B CA    1 
ATOM   3606 C C     . LEU B 1 241 ? -33.67900 25.33100  32.58100 1.000 34.14439 ?  221 LEU B C     1 
ATOM   3607 O O     . LEU B 1 241 ? -33.73400 26.55600  32.44100 1.000 37.09773 ?  221 LEU B O     1 
ATOM   3608 C CB    . LEU B 1 241 ? -31.33900 25.06300  33.45000 1.000 30.53639 ?  221 LEU B CB    1 
ATOM   3609 C CG    . LEU B 1 241 ? -31.82500 24.94100  34.89500 1.000 29.81820 ?  221 LEU B CG    1 
ATOM   3610 C CD1   . LEU B 1 241 ? -32.23600 23.50500  35.24300 1.000 28.73212 ?  221 LEU B CD1   1 
ATOM   3611 C CD2   . LEU B 1 241 ? -30.77000 25.45700  35.85100 1.000 29.40752 ?  221 LEU B CD2   1 
ATOM   3612 N N     . VAL B 1 242 ? -34.73500 24.58200  32.89100 1.000 32.60665 ?  222 VAL B N     1 
ATOM   3613 C CA    . VAL B 1 242 ? -36.10500 25.08400  32.86700 1.000 35.69422 ?  222 VAL B CA    1 
ATOM   3614 C C     . VAL B 1 242 ? -36.62800 25.35600  34.27400 1.000 34.22398 ?  222 VAL B C     1 
ATOM   3615 O O     . VAL B 1 242 ? -37.38400 26.30700  34.49200 1.000 33.47183 ?  222 VAL B O     1 
ATOM   3616 C CB    . VAL B 1 242 ? -37.00400 24.08300  32.11800 1.000 34.90630 ?  222 VAL B CB    1 
ATOM   3617 C CG1   . VAL B 1 242 ? -38.45700 24.28400  32.46400 1.000 36.18855 ?  222 VAL B CG1   1 
ATOM   3618 C CG2   . VAL B 1 242 ? -36.78200 24.21400  30.62200 1.000 40.38576 ?  222 VAL B CG2   1 
ATOM   3619 N N     . ALA B 1 243 ? -36.22700 24.53800  35.24000 1.000 32.22519 ?  223 ALA B N     1 
ATOM   3620 C CA    . ALA B 1 243 ? -36.79400 24.66500  36.57600 1.000 32.64557 ?  223 ALA B CA    1 
ATOM   3621 C C     . ALA B 1 243 ? -35.94900 23.86700  37.55300 1.000 31.46339 ?  223 ALA B C     1 
ATOM   3622 O O     . ALA B 1 243 ? -35.32600 22.87100  37.17600 1.000 30.14276 ?  223 ALA B O     1 
ATOM   3623 C CB    . ALA B 1 243 ? -38.25000 24.17400  36.63000 1.000 31.18104 ?  223 ALA B CB    1 
ATOM   3624 N N     . THR B 1 244 ? -35.93800 24.32400  38.80500 1.000 28.17987 ?  224 THR B N     1 
ATOM   3625 C CA    . THR B 1 244 ? -35.38100 23.58700  39.92500 1.000 28.05641 ?  224 THR B CA    1 
ATOM   3626 C C     . THR B 1 244 ? -36.38600 23.62600  41.06000 1.000 30.39433 ?  224 THR B C     1 
ATOM   3627 O O     . THR B 1 244 ? -37.17200 24.57000  41.18400 1.000 30.66882 ?  224 THR B O     1 
ATOM   3628 C CB    . THR B 1 244 ? -34.05200 24.16100  40.43700 1.000 29.09996 ?  224 THR B CB    1 
ATOM   3629 O OG1   . THR B 1 244 ? -34.23600 25.52700  40.81800 1.000 33.31195 ?  224 THR B OG1   1 
ATOM   3630 C CG2   . THR B 1 244 ? -32.98200 24.07900  39.35900 1.000 28.31515 ?  224 THR B CG2   1 
ATOM   3631 N N     . GLU B 1 245 ? -36.32800 22.60100  41.90600 1.000 25.34662 ?  225 GLU B N     1 
ATOM   3632 C CA    . GLU B 1 245 ? -37.31300 22.43200  42.95700 1.000 28.82168 ?  225 GLU B CA    1 
ATOM   3633 C C     . GLU B 1 245 ? -36.76900 21.42300  43.96300 1.000 30.88768 ?  225 GLU B C     1 
ATOM   3634 O O     . GLU B 1 245 ? -36.14700 20.43000  43.57500 1.000 28.87016 ?  225 GLU B O     1 
ATOM   3635 C CB    . GLU B 1 245 ? -38.63900 21.97900  42.33800 1.000 30.50352 ?  225 GLU B CB    1 
ATOM   3636 C CG    . GLU B 1 245 ? -39.65500 21.43800  43.27500 1.000 35.65013 ?  225 GLU B CG    1 
ATOM   3637 C CD    . GLU B 1 245 ? -40.89900 20.96100  42.54200 1.000 36.88908 ?  225 GLU B CD    1 
ATOM   3638 O OE1   . GLU B 1 245 ? -40.96000 21.05900  41.28900 1.000 37.03434 ?  225 GLU B OE1   1 
ATOM   3639 O OE2   . GLU B 1 245 ? -41.82600 20.49900  43.22700 1.000 42.02456 -1 225 GLU B OE2   1 
ATOM   3640 N N     . ASP B 1 246 ? -36.98600 21.69600  45.24700 1.000 29.29696 ?  226 ASP B N     1 
ATOM   3641 C CA    . ASP B 1 246 ? -36.54700 20.81800  46.32400 1.000 28.72217 ?  226 ASP B CA    1 
ATOM   3642 C C     . ASP B 1 246 ? -37.64900 19.82200  46.65800 1.000 31.91893 ?  226 ASP B C     1 
ATOM   3643 O O     . ASP B 1 246 ? -38.81200 20.20600  46.83700 1.000 31.06092 ?  226 ASP B O     1 
ATOM   3644 C CB    . ASP B 1 246 ? -36.17600 21.62800  47.56400 1.000 28.30037 ?  226 ASP B CB    1 
ATOM   3645 C CG    . ASP B 1 246 ? -34.77800 22.23800  47.47600 1.000 33.92001 ?  226 ASP B CG    1 
ATOM   3646 O OD1   . ASP B 1 246 ? -33.92600 21.73700  46.70700 1.000 30.01222 ?  226 ASP B OD1   1 
ATOM   3647 O OD2   . ASP B 1 246 ? -34.52500 23.22000  48.19900 1.000 38.14372 -1 226 ASP B OD2   1 
ATOM   3648 N N     . ILE B 1 247 ? -37.29600 18.53000  46.73900 1.000 25.61664 ?  227 ILE B N     1 
ATOM   3649 C CA    . ILE B 1 247 ? -38.23200 17.47300  47.00700 1.000 27.03386 ?  227 ILE B CA    1 
ATOM   3650 C C     . ILE B 1 247 ? -37.74100 16.63800  48.18200 1.000 28.14063 ?  227 ILE B C     1 
ATOM   3651 O O     . ILE B 1 247 ? -36.68600 15.99300  48.07300 1.000 26.74932 ?  227 ILE B O     1 
ATOM   3652 C CB    . ILE B 1 247 ? -38.47500 16.55900  45.77700 1.000 26.94843 ?  227 ILE B CB    1 
ATOM   3653 C CG1   . ILE B 1 247 ? -38.90300 17.39700  44.56400 1.000 25.05219 ?  227 ILE B CG1   1 
ATOM   3654 C CG2   . ILE B 1 247 ? -39.52400 15.49900  46.09500 1.000 23.42413 ?  227 ILE B CG2   1 
ATOM   3655 C CD1   . ILE B 1 247 ? -38.91700 16.61300  43.27400 1.000 28.39046 ?  227 ILE B CD1   1 
ATOM   3656 N N     . PRO B 1 248 ? -38.43900 16.61400  49.31300 1.000 26.09312 ?  228 PRO B N     1 
ATOM   3657 C CA    . PRO B 1 248 ? -38.00500 15.79700  50.45000 1.000 24.81796 ?  228 PRO B CA    1 
ATOM   3658 C C     . PRO B 1 248 ? -38.36300 14.32900  50.27900 1.000 27.93051 ?  228 PRO B C     1 
ATOM   3659 O O     . PRO B 1 248 ? -39.32100 13.96800  49.59000 1.000 26.79525 ?  228 PRO B O     1 
ATOM   3660 C CB    . PRO B 1 248 ? -38.78300 16.39700  51.62300 1.000 26.76811 ?  228 PRO B CB    1 
ATOM   3661 C CG    . PRO B 1 248 ? -40.08600 16.83300  50.97800 1.000 29.30023 ?  228 PRO B CG    1 
ATOM   3662 C CD    . PRO B 1 248 ? -39.70700 17.31900  49.59000 1.000 25.45783 ?  228 PRO B CD    1 
ATOM   3663 N N     . PHE B 1 249 ? -37.58100 13.47800  50.94100 1.000 27.42669 ?  229 PHE B N     1 
ATOM   3664 C CA    . PHE B 1 249 ? -37.92000 12.06900  51.05100 1.000 26.54883 ?  229 PHE B CA    1 
ATOM   3665 C C     . PHE B 1 249 ? -37.39200 11.51900  52.36900 1.000 26.72037 ?  229 PHE B C     1 
ATOM   3666 O O     . PHE B 1 249 ? -36.42800 12.03900  52.94700 1.000 26.31901 ?  229 PHE B O     1 
ATOM   3667 C CB    . PHE B 1 249 ? -37.40400 11.25200  49.84700 1.000 26.93026 ?  229 PHE B CB    1 
ATOM   3668 C CG    . PHE B 1 249 ? -35.90600 11.10800  49.78500 1.000 26.31448 ?  229 PHE B CG    1 
ATOM   3669 C CD1   . PHE B 1 249 ? -35.24800 10.12900  50.51200 1.000 25.56206 ?  229 PHE B CD1   1 
ATOM   3670 C CD2   . PHE B 1 249 ? -35.15900 11.94100  48.96500 1.000 27.95248 ?  229 PHE B CD2   1 
ATOM   3671 C CE1   . PHE B 1 249 ? -33.86600 9.99100   50.42700 1.000 27.09368 ?  229 PHE B CE1   1 
ATOM   3672 C CE2   . PHE B 1 249 ? -33.78100 11.81300  48.88500 1.000 27.72163 ?  229 PHE B CE2   1 
ATOM   3673 C CZ    . PHE B 1 249 ? -33.13700 10.83800  49.62000 1.000 28.63519 ?  229 PHE B CZ    1 
ATOM   3674 N N     . VAL B 1 250 ? -38.06000 10.46700  52.84300 1.000 29.60711 ?  230 VAL B N     1 
ATOM   3675 C CA    . VAL B 1 250 ? -37.71200 9.77500   54.07700 1.000 22.82288 ?  230 VAL B CA    1 
ATOM   3676 C C     . VAL B 1 250 ? -37.55900 8.30400   53.73400 1.000 29.14303 ?  230 VAL B C     1 
ATOM   3677 O O     . VAL B 1 250 ? -38.50000 7.68400   53.22100 1.000 31.61487 ?  230 VAL B O     1 
ATOM   3678 C CB    . VAL B 1 250 ? -38.78200 9.95000   55.17000 1.000 27.15007 ?  230 VAL B CB    1 
ATOM   3679 C CG1   . VAL B 1 250 ? -38.41100 9.14700   56.41200 1.000 24.56875 ?  230 VAL B CG1   1 
ATOM   3680 C CG2   . VAL B 1 250 ? -38.99500 11.41800  55.50700 1.000 28.35520 ?  230 VAL B CG2   1 
ATOM   3681 N N     . ILE B 1 251 ? -36.39000 7.73900   54.01300 1.000 26.83639 ?  231 ILE B N     1 
ATOM   3682 C CA    . ILE B 1 251 ? -36.16600 6.31800   53.81000 1.000 26.30750 ?  231 ILE B CA    1 
ATOM   3683 C C     . ILE B 1 251 ? -35.88700 5.68900   55.17100 1.000 29.05294 ?  231 ILE B C     1 
ATOM   3684 O O     . ILE B 1 251 ? -35.04400 6.18000   55.93300 1.000 27.24658 ?  231 ILE B O     1 
ATOM   3685 C CB    . ILE B 1 251 ? -35.03800 6.05100   52.79400 1.000 27.65428 ?  231 ILE B CB    1 
ATOM   3686 C CG1   . ILE B 1 251 ? -34.74300 4.54400   52.69800 1.000 31.01278 ?  231 ILE B CG1   1 
ATOM   3687 C CG2   . ILE B 1 251 ? -33.79300 6.84600   53.11600 1.000 32.12680 ?  231 ILE B CG2   1 
ATOM   3688 C CD1   . ILE B 1 251 ? -34.30100 4.12900   51.30500 1.000 29.51396 ?  231 ILE B CD1   1 
ATOM   3689 N N     . ARG B 1 252 ? -36.63200 4.63200   55.48900 1.000 27.53347 ?  232 ARG B N     1 
ATOM   3690 C CA    . ARG B 1 252 ? -36.51000 3.97700   56.78400 1.000 27.41997 ?  232 ARG B CA    1 
ATOM   3691 C C     . ARG B 1 252 ? -35.23300 3.15000   56.84500 1.000 29.66375 ?  232 ARG B C     1 
ATOM   3692 O O     . ARG B 1 252 ? -34.88700 2.45100   55.89200 1.000 31.69415 ?  232 ARG B O     1 
ATOM   3693 C CB    . ARG B 1 252 ? -37.72500 3.07800   57.03300 1.000 31.05316 ?  232 ARG B CB    1 
ATOM   3694 C CG    . ARG B 1 252 ? -37.66100 2.26400   58.31300 1.000 33.62294 ?  232 ARG B CG    1 
ATOM   3695 C CD    . ARG B 1 252 ? -38.76800 1.21000   58.38200 1.000 39.00153 ?  232 ARG B CD    1 
ATOM   3696 N NE    . ARG B 1 252 ? -39.98400 1.73000   58.99500 1.000 42.84665 ?  232 ARG B NE    1 
ATOM   3697 C CZ    . ARG B 1 252 ? -41.01700 2.23200   58.32500 1.000 47.94797 ?  232 ARG B CZ    1 
ATOM   3698 N NH1   . ARG B 1 252 ? -41.03200 2.27900   56.99700 1.000 40.80206 ?  232 ARG B NH1   1 
ATOM   3699 N NH2   . ARG B 1 252 ? -42.06200 2.70500   59.00200 1.000 46.74010 ?  232 ARG B NH2   1 
ATOM   3700 N N     . GLU B 1 253 ? -34.52500 3.23800   57.97200 1.000 25.69887 ?  233 GLU B N     1 
ATOM   3701 C CA    . GLU B 1 253 ? -33.37700 2.38000   58.25100 1.000 29.83488 ?  233 GLU B CA    1 
ATOM   3702 C C     . GLU B 1 253 ? -33.65100 1.39100   59.37600 1.000 34.56064 ?  233 GLU B C     1 
ATOM   3703 O O     . GLU B 1 253 ? -33.33700 0.20600   59.24100 1.000 34.80478 ?  233 GLU B O     1 
ATOM   3704 C CB    . GLU B 1 253 ? -32.14500 3.23400   58.57900 1.000 26.10532 ?  233 GLU B CB    1 
ATOM   3705 C CG    . GLU B 1 253 ? -31.82500 4.21200   57.45800 1.000 31.37338 ?  233 GLU B CG    1 
ATOM   3706 C CD    . GLU B 1 253 ? -30.74300 5.21700   57.81400 1.000 34.22513 ?  233 GLU B CD    1 
ATOM   3707 O OE1   . GLU B 1 253 ? -30.54900 5.47900   59.02000 1.000 35.32697 ?  233 GLU B OE1   1 
ATOM   3708 O OE2   . GLU B 1 253 ? -30.11200 5.76900   56.88000 1.000 35.60382 -1 233 GLU B OE2   1 
ATOM   3709 N N     . THR B 1 254 ? -34.23000 1.83700   60.49200 1.000 31.04503 ?  234 THR B N     1 
ATOM   3710 C CA    . THR B 1 254 ? -34.81400 0.92400   61.47200 1.000 32.36773 ?  234 THR B CA    1 
ATOM   3711 C C     . THR B 1 254 ? -36.21600 1.40300   61.81400 1.000 32.05165 ?  234 THR B C     1 
ATOM   3712 O O     . THR B 1 254 ? -36.70000 2.40300   61.28500 1.000 31.30541 ?  234 THR B O     1 
ATOM   3713 C CB    . THR B 1 254 ? -33.97700 0.81400   62.75400 1.000 32.61844 ?  234 THR B CB    1 
ATOM   3714 O OG1   . THR B 1 254 ? -34.12000 2.01900   63.52300 1.000 33.35453 ?  234 THR B OG1   1 
ATOM   3715 C CG2   . THR B 1 254 ? -32.50500 0.58800   62.43100 1.000 36.24070 ?  234 THR B CG2   1 
ATOM   3716 N N     . SER B 1 255 ? -36.85600 0.68200   62.73600 1.000 34.60073 ?  235 SER B N     1 
ATOM   3717 C CA    . SER B 1 255 ? -38.15100 1.10200   63.26200 1.000 33.29752 ?  235 SER B CA    1 
ATOM   3718 C C     . SER B 1 255 ? -38.10700 2.50900   63.85600 1.000 28.82692 ?  235 SER B C     1 
ATOM   3719 O O     . SER B 1 255 ? -39.13300 3.19700   63.89100 1.000 30.87385 ?  235 SER B O     1 
ATOM   3720 C CB    . SER B 1 255 ? -38.62600 0.10600   64.32300 1.000 31.50222 ?  235 SER B CB    1 
ATOM   3721 O OG    . SER B 1 255 ? -37.62700 -0.08600  65.32500 1.000 35.50675 ?  235 SER B OG    1 
ATOM   3722 N N     . ARG B 1 256 ? -36.94500 2.94300   64.33700 1.000 26.95251 ?  236 ARG B N     1 
ATOM   3723 C CA    . ARG B 1 256 ? -36.85400 4.26700   65.01100 1.000 26.66969 ?  236 ARG B CA    1 
ATOM   3724 C C     . ARG B 1 256 ? -35.88000 5.21600   64.29300 1.000 26.88308 ?  236 ARG B C     1 
ATOM   3725 O O     . ARG B 1 256 ? -35.91500 6.40000   64.59300 1.000 30.78464 ?  236 ARG B O     1 
ATOM   3726 C CB    . ARG B 1 256 ? -36.48800 4.07900   66.48500 1.000 26.41806 ?  236 ARG B CB    1 
ATOM   3727 C CG    . ARG B 1 256 ? -37.56400 3.41000   67.32400 1.000 26.83638 ?  236 ARG B CG    1 
ATOM   3728 C CD    . ARG B 1 256 ? -37.13100 3.31600   68.77100 1.000 27.13330 ?  236 ARG B CD    1 
ATOM   3729 N NE    . ARG B 1 256 ? -38.23300 2.98400   69.65700 1.000 24.93655 ?  236 ARG B NE    1 
ATOM   3730 C CZ    . ARG B 1 256 ? -39.03100 3.87500   70.22800 1.000 31.25411 ?  236 ARG B CZ    1 
ATOM   3731 N NH1   . ARG B 1 256 ? -38.81300 5.16600   70.05800 1.000 24.19503 ?  236 ARG B NH1   1 
ATOM   3732 N NH2   . ARG B 1 256 ? -40.04500 3.47300   70.97300 1.000 30.72966 ?  236 ARG B NH2   1 
ATOM   3733 N N     . LYS B 1 257 ? -35.05200 4.70800   63.39000 1.000 27.52042 ?  237 LYS B N     1 
ATOM   3734 C CA    . LYS B 1 257 ? -34.05000 5.55800   62.70100 1.000 27.56934 ?  237 LYS B CA    1 
ATOM   3735 C C     . LYS B 1 257 ? -34.40900 5.69400   61.22100 1.000 27.48145 ?  237 LYS B C     1 
ATOM   3736 O O     . LYS B 1 257 ? -34.61700 4.66800   60.57900 1.000 28.93420 ?  237 LYS B O     1 
ATOM   3737 C CB    . LYS B 1 257 ? -32.62000 5.03900   62.87600 1.000 27.84964 ?  237 LYS B CB    1 
ATOM   3738 C CG    . LYS B 1 257 ? -31.54900 5.87000   62.18800 1.000 34.64484 ?  237 LYS B CG    1 
ATOM   3739 C CD    . LYS B 1 257 ? -30.15800 5.60700   62.70400 1.000 37.62004 ?  237 LYS B CD    1 
ATOM   3740 C CE    . LYS B 1 257 ? -29.50600 4.41000   62.04900 1.000 42.11957 ?  237 LYS B CE    1 
ATOM   3741 N N     . PHE B 1 258 ? -34.42100 6.92800   60.72300 1.000 24.12857 ?  238 PHE B N     1 
ATOM   3742 C CA    . PHE B 1 258 ? -34.75900 7.20300   59.31000 1.000 25.78753 ?  238 PHE B CA    1 
ATOM   3743 C C     . PHE B 1 258 ? -33.83000 8.26000   58.70100 1.000 26.57264 ?  238 PHE B C     1 
ATOM   3744 O O     . PHE B 1 258 ? -33.32000 9.10600   59.43900 1.000 27.57656 ?  238 PHE B O     1 
ATOM   3745 C CB    . PHE B 1 258 ? -36.19000 7.73800   59.21900 1.000 26.64077 ?  238 PHE B CB    1 
ATOM   3746 C CG    . PHE B 1 258 ? -37.28300 6.88700   59.81200 1.000 27.05498 ?  238 PHE B CG    1 
ATOM   3747 C CD1   . PHE B 1 258 ? -37.48800 6.83400   61.18000 1.000 23.87243 ?  238 PHE B CD1   1 
ATOM   3748 C CD2   . PHE B 1 258 ? -38.14100 6.17400   58.99300 1.000 29.51441 ?  238 PHE B CD2   1 
ATOM   3749 C CE1   . PHE B 1 258 ? -38.49700 6.05300   61.71700 1.000 30.51851 ?  238 PHE B CE1   1 
ATOM   3750 C CE2   . PHE B 1 258 ? -39.15300 5.39700   59.53200 1.000 28.98580 ?  238 PHE B CE2   1 
ATOM   3751 C CZ    . PHE B 1 258 ? -39.32900 5.33700   60.89200 1.000 26.34803 ?  238 PHE B CZ    1 
ATOM   3752 N N     . GLN B 1 259 ? -33.58400 8.18500   57.39700 1.000 26.95366 ?  239 GLN B N     1 
ATOM   3753 C CA    . GLN B 1 259 ? -32.84800 9.27500   56.70700 1.000 27.35175 ?  239 GLN B CA    1 
ATOM   3754 C C     . GLN B 1 259 ? -33.89000 10.24000  56.13700 1.000 29.66832 ?  239 GLN B C     1 
ATOM   3755 O O     . GLN B 1 259 ? -34.81800 9.77800   55.46600 1.000 25.83697 ?  239 GLN B O     1 
ATOM   3756 C CB    . GLN B 1 259 ? -31.91400 8.77900   55.60800 1.000 27.76558 ?  239 GLN B CB    1 
ATOM   3757 C CG    . GLN B 1 259 ? -31.42700 9.87500   54.67500 1.000 25.35911 ?  239 GLN B CG    1 
ATOM   3758 C CD    . GLN B 1 259 ? -30.80900 9.33600   53.41000 1.000 31.14225 ?  239 GLN B CD    1 
ATOM   3759 O OE1   . GLN B 1 259 ? -30.82700 9.98000   52.36500 1.000 32.53000 ?  239 GLN B OE1   1 
ATOM   3760 N NE2   . GLN B 1 259 ? -30.24700 8.14400   53.49700 1.000 38.50676 ?  239 GLN B NE2   1 
ATOM   3761 N N     . HIS B 1 260 ? -33.75800 11.51300  56.47200 1.000 25.05000 ?  240 HIS B N     1 
ATOM   3762 C CA    . HIS B 1 260 ? -34.68300 12.55700  55.98300 1.000 24.66815 ?  240 HIS B CA    1 
ATOM   3763 C C     . HIS B 1 260 ? -33.83200 13.48600  55.12500 1.000 27.24471 ?  240 HIS B C     1 
ATOM   3764 O O     . HIS B 1 260 ? -32.96400 14.19000  55.66200 1.000 24.03087 ?  240 HIS B O     1 
ATOM   3765 C CB    . HIS B 1 260 ? -35.38900 13.20900  57.16800 1.000 24.79671 ?  240 HIS B CB    1 
ATOM   3766 C CG    . HIS B 1 260 ? -36.59800 13.98600  56.83100 1.000 26.74241 ?  240 HIS B CG    1 
ATOM   3767 N ND1   . HIS B 1 260 ? -37.51000 14.35500  57.79200 1.000 29.57689 ?  240 HIS B ND1   1 
ATOM   3768 C CD2   . HIS B 1 260 ? -37.04500 14.46400  55.67800 1.000 25.34017 ?  240 HIS B CD2   1 
ATOM   3769 C CE1   . HIS B 1 260 ? -38.48000 15.03700  57.21700 1.000 32.77688 ?  240 HIS B CE1   1 
ATOM   3770 N NE2   . HIS B 1 260 ? -38.21700 15.10600  55.93600 1.000 31.55637 ?  240 HIS B NE2   1 
ATOM   3771 N N     . THR B 1 261 ? -34.10700 13.49800  53.83000 1.000 24.41310 ?  241 THR B N     1 
ATOM   3772 C CA    . THR B 1 261 ? -33.21300 14.23300  52.90500 1.000 25.69473 ?  241 THR B CA    1 
ATOM   3773 C C     . THR B 1 261 ? -33.99000 15.12500  51.93100 1.000 28.61775 ?  241 THR B C     1 
ATOM   3774 O O     . THR B 1 261 ? -35.09700 14.74800  51.52900 1.000 25.27527 ?  241 THR B O     1 
ATOM   3775 C CB    . THR B 1 261 ? -32.30000 13.21400  52.19800 1.000 28.22175 ?  241 THR B CB    1 
ATOM   3776 O OG1   . THR B 1 261 ? -31.35700 12.71300  53.14400 1.000 28.39386 ?  241 THR B OG1   1 
ATOM   3777 C CG2   . THR B 1 261 ? -31.56600 13.78500  51.00600 1.000 27.35064 ?  241 THR B CG2   1 
ATOM   3778 N N     . ILE B 1 262 ? -33.40000 16.26000  51.57000 1.000 23.82869 ?  242 ILE B N     1 
ATOM   3779 C CA    . ILE B 1 262 ? -34.01400 17.16000  50.56100 1.000 24.30168 ?  242 ILE B CA    1 
ATOM   3780 C C     . ILE B 1 262 ? -33.21200 17.02600  49.26800 1.000 25.20545 ?  242 ILE B C     1 
ATOM   3781 O O     . ILE B 1 262 ? -32.06500 17.46000  49.22500 1.000 22.68152 ?  242 ILE B O     1 
ATOM   3782 C CB    . ILE B 1 262 ? -34.09400 18.61400  51.05900 1.000 27.83100 ?  242 ILE B CB    1 
ATOM   3783 C CG1   . ILE B 1 262 ? -34.93100 18.71700  52.33500 1.000 25.06785 ?  242 ILE B CG1   1 
ATOM   3784 C CG2   . ILE B 1 262 ? -34.62100 19.52500  49.96600 1.000 26.52753 ?  242 ILE B CG2   1 
ATOM   3785 C CD1   . ILE B 1 262 ? -34.32600 19.60800  53.38200 1.000 34.75420 ?  242 ILE B CD1   1 
ATOM   3786 N N     . SER B 1 263 ? -33.81300 16.38900  48.27900 1.000 25.12689 ?  243 SER B N     1 
ATOM   3787 C CA    . SER B 1 263 ? -33.16200 16.25500  46.98900 1.000 26.29146 ?  243 SER B CA    1 
ATOM   3788 C C     . SER B 1 263 ? -33.57500 17.43100  46.11700 1.000 28.22312 ?  243 SER B C     1 
ATOM   3789 O O     . SER B 1 263 ? -34.67700 17.96700  46.25800 1.000 32.82818 ?  243 SER B O     1 
ATOM   3790 C CB    . SER B 1 263 ? -33.54600 14.92400  46.33300 1.000 26.17874 ?  243 SER B CB    1 
ATOM   3791 O OG    . SER B 1 263 ? -32.92600 14.75900  45.07400 1.000 33.23909 ?  243 SER B OG    1 
ATOM   3792 N N     . GLN B 1 264 ? -32.67600 17.86000  45.23900 1.000 25.16626 ?  244 GLN B N     1 
ATOM   3793 C CA    . GLN B 1 264 ? -32.99300 18.92900  44.30500 1.000 28.38731 ?  244 GLN B CA    1 
ATOM   3794 C C     . GLN B 1 264 ? -33.30700 18.32400  42.94800 1.000 28.27776 ?  244 GLN B C     1 
ATOM   3795 O O     . GLN B 1 264 ? -32.49200 17.58100  42.39200 1.000 27.36275 ?  244 GLN B O     1 
ATOM   3796 C CB    . GLN B 1 264 ? -31.85200 19.93900  44.16300 1.000 27.08859 ?  244 GLN B CB    1 
ATOM   3797 C CG    . GLN B 1 264 ? -32.11800 20.94700  43.03600 1.000 27.36747 ?  244 GLN B CG    1 
ATOM   3798 C CD    . GLN B 1 264 ? -31.23300 22.17000  43.11500 1.000 28.64570 ?  244 GLN B CD    1 
ATOM   3799 O OE1   . GLN B 1 264 ? -30.04200 22.11000  42.80300 1.000 26.52889 ?  244 GLN B OE1   1 
ATOM   3800 N NE2   . GLN B 1 264 ? -31.80800 23.28600  43.54800 1.000 25.63838 ?  244 GLN B NE2   1 
ATOM   3801 N N     . MET B 1 265 ? -34.48400 18.64900  42.41800 1.000 25.57736 ?  245 MET B N     1 
ATOM   3802 C CA    . MET B 1 265 ? -34.84900 18.24000  41.07300 1.000 24.65541 ?  245 MET B CA    1 
ATOM   3803 C C     . MET B 1 265 ? -34.43400 19.35200  40.12100 1.000 25.99729 ?  245 MET B C     1 
ATOM   3804 O O     . MET B 1 265 ? -34.69600 20.53100  40.39000 1.000 24.98664 ?  245 MET B O     1 
ATOM   3805 C CB    . MET B 1 265 ? -36.35300 17.98300  40.95700 1.000 24.05699 ?  245 MET B CB    1 
ATOM   3806 C CG    . MET B 1 265 ? -36.84900 17.80000  39.51300 1.000 23.63145 ?  245 MET B CG    1 
ATOM   3807 S SD    . MET B 1 265 ? -38.61600 17.35800  39.43700 1.000 26.15168 ?  245 MET B SD    1 
ATOM   3808 C CE    . MET B 1 265 ? -38.56000 15.59000  39.82600 1.000 25.54921 ?  245 MET B CE    1 
ATOM   3809 N N     . SER B 1 266 ? -33.78100 18.98400  39.01900 1.000 27.59455 ?  246 SER B N     1 
ATOM   3810 C CA    . SER B 1 266 ? -33.48000 19.91900  37.94200 1.000 26.34686 ?  246 SER B CA    1 
ATOM   3811 C C     . SER B 1 266 ? -34.08600 19.40900  36.63800 1.000 28.19978 ?  246 SER B C     1 
ATOM   3812 O O     . SER B 1 266 ? -34.03200 18.21100  36.33900 1.000 24.08980 ?  246 SER B O     1 
ATOM   3813 C CB    . SER B 1 266 ? -31.97100 20.13100  37.77900 1.000 25.11750 ?  246 SER B CB    1 
ATOM   3814 O OG    . SER B 1 266 ? -31.28600 18.90100  37.73200 1.000 24.58445 ?  246 SER B OG    1 
ATOM   3815 N N     . VAL B 1 267 ? -34.64100 20.33400  35.85900 1.000 26.13593 ?  247 VAL B N     1 
ATOM   3816 C CA    . VAL B 1 267 ? -35.44800 20.02800  34.68500 1.000 29.70525 ?  247 VAL B CA    1 
ATOM   3817 C C     . VAL B 1 267 ? -34.76300 20.63800  33.46800 1.000 30.09659 ?  247 VAL B C     1 
ATOM   3818 O O     . VAL B 1 267 ? -34.49700 21.84700  33.44000 1.000 28.38870 ?  247 VAL B O     1 
ATOM   3819 C CB    . VAL B 1 267 ? -36.88100 20.55700  34.84900 1.000 29.08124 ?  247 VAL B CB    1 
ATOM   3820 C CG1   . VAL B 1 267 ? -37.74500 20.18400  33.64900 1.000 26.78339 ?  247 VAL B CG1   1 
ATOM   3821 C CG2   . VAL B 1 267 ? -37.47200 20.01000  36.14000 1.000 25.96080 ?  247 VAL B CG2   1 
ATOM   3822 N N     . TRP B 1 268 ? -34.46900 19.80100  32.47200 1.000 26.90840 ?  248 TRP B N     1 
ATOM   3823 C CA    . TRP B 1 268 ? -33.66900 20.19900  31.32000 1.000 29.88803 ?  248 TRP B CA    1 
ATOM   3824 C C     . TRP B 1 268 ? -34.39900 19.82200  30.03700 1.000 34.85142 ?  248 TRP B C     1 
ATOM   3825 O O     . TRP B 1 268 ? -34.77600 18.65800  29.85100 1.000 31.80347 ?  248 TRP B O     1 
ATOM   3826 C CB    . TRP B 1 268 ? -32.28000 19.54000  31.35900 1.000 28.36726 ?  248 TRP B CB    1 
ATOM   3827 C CG    . TRP B 1 268 ? -31.58000 19.63600  32.70400 1.000 27.06867 ?  248 TRP B CG    1 
ATOM   3828 C CD1   . TRP B 1 268 ? -31.79200 18.84500  33.80300 1.000 27.85385 ?  248 TRP B CD1   1 
ATOM   3829 C CD2   . TRP B 1 268 ? -30.56000 20.57700  33.07800 1.000 31.35834 ?  248 TRP B CD2   1 
ATOM   3830 N NE1   . TRP B 1 268 ? -30.96700 19.23500  34.83400 1.000 29.99731 ?  248 TRP B NE1   1 
ATOM   3831 C CE2   . TRP B 1 268 ? -30.20200 20.29800  34.41700 1.000 29.85904 ?  248 TRP B CE2   1 
ATOM   3832 C CE3   . TRP B 1 268 ? -29.91900 21.63200  32.41200 1.000 27.73475 ?  248 TRP B CE3   1 
ATOM   3833 C CZ2   . TRP B 1 268 ? -29.22800 21.03800  35.10500 1.000 26.02338 ?  248 TRP B CZ2   1 
ATOM   3834 C CZ3   . TRP B 1 268 ? -28.94700 22.36500  33.09900 1.000 28.12878 ?  248 TRP B CZ3   1 
ATOM   3835 C CH2   . TRP B 1 268 ? -28.61300 22.06200  34.42700 1.000 27.54008 ?  248 TRP B CH2   1 
ATOM   3836 N N     . LYS B 1 269 ? -34.57900 20.80400  29.15300 1.000 32.50553 ?  249 LYS B N     1 
ATOM   3837 C CA    . LYS B 1 269 ? -35.20200 20.61000  27.84800 1.000 34.35489 ?  249 LYS B CA    1 
ATOM   3838 C C     . LYS B 1 269 ? -34.12200 20.57900  26.76700 1.000 35.03798 ?  249 LYS B C     1 
ATOM   3839 O O     . LYS B 1 269 ? -33.23600 21.43800  26.74500 1.000 30.81360 ?  249 LYS B O     1 
ATOM   3840 C CB    . LYS B 1 269 ? -36.21000 21.73300  27.57100 1.000 37.95141 ?  249 LYS B CB    1 
ATOM   3841 C CG    . LYS B 1 269 ? -37.14800 21.48800  26.39700 1.000 37.58213 ?  249 LYS B CG    1 
ATOM   3842 C CD    . LYS B 1 269 ? -38.15600 22.61900  26.25200 1.000 41.02347 ?  249 LYS B CD    1 
ATOM   3843 N N     . VAL B 1 270 ? -34.19400 19.59000  25.87300 1.000 37.78214 ?  250 VAL B N     1 
ATOM   3844 C CA    . VAL B 1 270 ? -33.20100 19.48300  24.80700 1.000 35.37805 ?  250 VAL B CA    1 
ATOM   3845 C C     . VAL B 1 270 ? -33.35400 20.64100  23.83600 1.000 40.20738 ?  250 VAL B C     1 
ATOM   3846 O O     . VAL B 1 270 ? -34.47500 21.06800  23.51900 1.000 42.71107 ?  250 VAL B O     1 
ATOM   3847 C CB    . VAL B 1 270 ? -33.32600 18.14600  24.06100 1.000 37.85277 ?  250 VAL B CB    1 
ATOM   3848 C CG1   . VAL B 1 270 ? -32.10700 17.92000  23.18900 1.000 40.89334 ?  250 VAL B CG1   1 
ATOM   3849 C CG2   . VAL B 1 270 ? -33.46200 17.02100  25.03200 1.000 39.60998 ?  250 VAL B CG2   1 
ATOM   3850 N N     . ILE B 1 271 ? -32.22100 21.15400  23.36200 1.000 41.79671 ?  251 ILE B N     1 
ATOM   3851 C CA    . ILE B 1 271 ? -32.20000 22.13700  22.29000 1.000 43.21465 ?  251 ILE B CA    1 
ATOM   3852 C C     . ILE B 1 271 ? -32.20100 21.41800  20.94900 1.000 43.79451 ?  251 ILE B C     1 
ATOM   3853 O O     . ILE B 1 271 ? -33.12100 21.58200  20.15100 1.000 53.25290 ?  251 ILE B O     1 
ATOM   3854 C CB    . ILE B 1 271 ? -30.98600 23.06100  22.39200 1.000 39.97646 ?  251 ILE B CB    1 
ATOM   3855 C CG1   . ILE B 1 271 ? -31.00500 23.86600  23.69700 1.000 39.75806 ?  251 ILE B CG1   1 
ATOM   3856 C CG2   . ILE B 1 271 ? -30.97900 24.00100  21.21700 1.000 47.83547 ?  251 ILE B CG2   1 
ATOM   3857 C CD1   . ILE B 1 271 ? -32.40100 24.19100  24.20900 1.000 44.92866 ?  251 ILE B CD1   1 
HETATM 3858 N N     . SAM C 2 .   ? -9.04800  -12.35800 26.97400 1.000 21.74445 ?  301 SAM A N     1 
HETATM 3859 C CA    . SAM C 2 .   ? -9.39900  -12.97600 25.67700 1.000 24.35592 ?  301 SAM A CA    1 
HETATM 3860 C C     . SAM C 2 .   ? -8.13400  -13.19100 24.84000 1.000 26.99617 ?  301 SAM A C     1 
HETATM 3861 O O     . SAM C 2 .   ? -8.24600  -13.85200 23.81600 1.000 29.60174 ?  301 SAM A O     1 
HETATM 3862 O OXT   . SAM C 2 .   ? -7.11200  -12.67800 25.24300 1.000 27.12935 ?  301 SAM A OXT   1 
HETATM 3863 C CB    . SAM C 2 .   ? -10.37000 -12.08700 24.90000 1.000 26.30110 ?  301 SAM A CB    1 
HETATM 3864 C CG    . SAM C 2 .   ? -9.81200  -10.74600 24.46400 1.000 24.99557 ?  301 SAM A CG    1 
HETATM 3865 S SD    . SAM C 2 .   ? -10.96000 -9.97800  23.29800 1.000 25.33759 ?  301 SAM A SD    1 
HETATM 3866 C CE    . SAM C 2 .   ? -9.88100  -8.92000  22.34600 1.000 24.42643 ?  301 SAM A CE    1 
HETATM 3867 C "C5'" . SAM C 2 .   ? -11.75200 -8.80800  24.41700 1.000 25.32415 ?  301 SAM A "C5'" 1 
HETATM 3868 C "C4'" . SAM C 2 .   ? -12.70400 -9.53000  25.34500 1.000 27.03962 ?  301 SAM A "C4'" 1 
HETATM 3869 O "O4'" . SAM C 2 .   ? -13.19100 -8.60900  26.34300 1.000 26.16133 ?  301 SAM A "O4'" 1 
HETATM 3870 C "C3'" . SAM C 2 .   ? -13.93600 -10.13600 24.67500 1.000 26.38472 ?  301 SAM A "C3'" 1 
HETATM 3871 O "O3'" . SAM C 2 .   ? -14.14500 -11.45600 25.15200 1.000 24.63205 ?  301 SAM A "O3'" 1 
HETATM 3872 C "C2'" . SAM C 2 .   ? -15.06200 -9.18700  25.09300 1.000 29.05973 ?  301 SAM A "C2'" 1 
HETATM 3873 O "O2'" . SAM C 2 .   ? -16.32100 -9.82100  25.11100 1.000 25.64770 ?  301 SAM A "O2'" 1 
HETATM 3874 C "C1'" . SAM C 2 .   ? -14.58000 -8.76600  26.47400 1.000 25.49090 ?  301 SAM A "C1'" 1 
HETATM 3875 N N9    . SAM C 2 .   ? -15.12100 -7.50100  26.94400 1.000 28.06003 ?  301 SAM A N9    1 
HETATM 3876 C C8    . SAM C 2 .   ? -15.25800 -6.34400  26.22700 1.000 24.33482 ?  301 SAM A C8    1 
HETATM 3877 N N7    . SAM C 2 .   ? -15.75300 -5.35900  26.92800 1.000 25.62655 ?  301 SAM A N7    1 
HETATM 3878 C C5    . SAM C 2 .   ? -15.94700 -5.89700  28.18900 1.000 26.78375 ?  301 SAM A C5    1 
HETATM 3879 C C6    . SAM C 2 .   ? -16.45400 -5.35400  29.38400 1.000 26.65596 ?  301 SAM A C6    1 
HETATM 3880 N N6    . SAM C 2 .   ? -16.87300 -4.10000  29.50900 1.000 26.98829 ?  301 SAM A N6    1 
HETATM 3881 N N1    . SAM C 2 .   ? -16.51300 -6.16800  30.46100 1.000 27.39628 ?  301 SAM A N1    1 
HETATM 3882 C C2    . SAM C 2 .   ? -16.09000 -7.43000  30.33200 1.000 27.36836 ?  301 SAM A C2    1 
HETATM 3883 N N3    . SAM C 2 .   ? -15.59900 -8.04700  29.26400 1.000 27.86547 ?  301 SAM A N3    1 
HETATM 3884 C C4    . SAM C 2 .   ? -15.55200 -7.21800  28.21300 1.000 25.69255 ?  301 SAM A C4    1 
HETATM 3885 C C     . TRS D 3 .   ? -10.60700 -9.28900  16.02100 1.000 35.88106 ?  302 TRS A C     1 
HETATM 3886 C C1    . TRS D 3 .   ? -9.78500  -10.37500 15.29000 1.000 37.53500 ?  302 TRS A C1    1 
HETATM 3887 C C2    . TRS D 3 .   ? -10.02500 -7.89200  15.83100 1.000 34.18231 ?  302 TRS A C2    1 
HETATM 3888 C C3    . TRS D 3 .   ? -10.68400 -9.63600  17.51700 1.000 38.25368 ?  302 TRS A C3    1 
HETATM 3889 N N     . TRS D 3 .   ? -11.96700 -9.25700  15.48500 1.000 38.52740 ?  302 TRS A N     1 
HETATM 3890 O O1    . TRS D 3 .   ? -9.74100  -10.30800 13.86500 1.000 32.61107 ?  302 TRS A O1    1 
HETATM 3891 O O2    . TRS D 3 .   ? -8.74300  -7.83500  16.42600 1.000 40.38088 ?  302 TRS A O2    1 
HETATM 3892 O O3    . TRS D 3 .   ? -11.43100 -8.72500  18.30700 1.000 40.43908 ?  302 TRS A O3    1 
HETATM 3893 C C1    . EDO E 4 .   ? -14.18900 -2.21700  39.81400 1.000 34.03546 ?  303 EDO A C1    1 
HETATM 3894 O O1    . EDO E 4 .   ? -12.88600 -2.61100  39.38400 1.000 38.40865 ?  303 EDO A O1    1 
HETATM 3895 C C2    . EDO E 4 .   ? -14.93100 -1.74900  38.57700 1.000 35.49281 ?  303 EDO A C2    1 
HETATM 3896 O O2    . EDO E 4 .   ? -15.14200 -2.89800  37.76300 1.000 27.56728 ?  303 EDO A O2    1 
HETATM 3897 C C1    . EDO F 4 .   ? -16.52400 1.95100   38.46100 1.000 32.97484 ?  304 EDO A C1    1 
HETATM 3898 O O1    . EDO F 4 .   ? -17.59600 1.74600   37.53100 1.000 31.72964 ?  304 EDO A O1    1 
HETATM 3899 C C2    . EDO F 4 .   ? -17.06900 1.79900   39.87600 1.000 34.13398 ?  304 EDO A C2    1 
HETATM 3900 O O2    . EDO F 4 .   ? -17.57000 0.46600   40.02600 1.000 46.37255 ?  304 EDO A O2    1 
HETATM 3901 C C1    . EDO G 4 .   ? -6.57400  -29.49500 40.82200 1.000 43.36051 ?  305 EDO A C1    1 
HETATM 3902 O O1    . EDO G 4 .   ? -5.64500  -28.59300 40.18900 1.000 45.04660 ?  305 EDO A O1    1 
HETATM 3903 C C2    . EDO G 4 .   ? -5.90300  -30.81200 41.18300 1.000 49.06065 ?  305 EDO A C2    1 
HETATM 3904 O O2    . EDO G 4 .   ? -5.40000  -31.40700 39.98300 1.000 50.39514 ?  305 EDO A O2    1 
HETATM 3905 N N     . SAM H 2 .   ? -34.34400 6.30400   41.49800 1.000 22.57139 ?  301 SAM B N     1 
HETATM 3906 C CA    . SAM H 2 .   ? -34.51100 5.66600   42.82200 1.000 25.26016 ?  301 SAM B CA    1 
HETATM 3907 C C     . SAM H 2 .   ? -34.94300 6.71000   43.85100 1.000 26.14724 ?  301 SAM B C     1 
HETATM 3908 O O     . SAM H 2 .   ? -34.97000 7.88500   43.50600 1.000 27.74938 ?  301 SAM B O     1 
HETATM 3909 O OXT   . SAM H 2 .   ? -35.21400 6.28600   44.93100 1.000 24.28141 ?  301 SAM B OXT   1 
HETATM 3910 C CB    . SAM H 2 .   ? -33.21800 4.99700   43.29800 1.000 27.29044 ?  301 SAM B CB    1 
HETATM 3911 C CG    . SAM H 2 .   ? -32.08100 5.90800   43.69900 1.000 24.72177 ?  301 SAM B CG    1 
HETATM 3912 S SD    . SAM H 2 .   ? -30.80700 4.89300   44.48800 1.000 29.43432 ?  301 SAM B SD    1 
HETATM 3913 C CE    . SAM H 2 .   ? -29.96700 6.08900   45.51200 1.000 29.34016 ?  301 SAM B CE    1 
HETATM 3914 C "C5'" . SAM H 2 .   ? -29.68200 4.72500   43.08900 1.000 29.82629 ?  301 SAM B "C5'" 1 
HETATM 3915 C "C4'" . SAM H 2 .   ? -30.19000 3.66500   42.13400 1.000 28.16923 ?  301 SAM B "C4'" 1 
HETATM 3916 O "O4'" . SAM H 2 .   ? -29.40700 3.68300   40.92100 1.000 28.92527 ?  301 SAM B "O4'" 1 
HETATM 3917 C "C3'" . SAM H 2 .   ? -30.13200 2.23400   42.66200 1.000 27.57509 ?  301 SAM B "C3'" 1 
HETATM 3918 O "O3'" . SAM H 2 .   ? -31.32800 1.55800   42.30900 1.000 25.38764 ?  301 SAM B "O3'" 1 
HETATM 3919 C "C2'" . SAM H 2 .   ? -28.90800 1.65300   41.95100 1.000 28.90266 ?  301 SAM B "C2'" 1 
HETATM 3920 O "O2'" . SAM H 2 .   ? -28.98400 0.25500   41.78900 1.000 28.47600 ?  301 SAM B "O2'" 1 
HETATM 3921 C "C1'" . SAM H 2 .   ? -28.98800 2.37800   40.61500 1.000 29.09291 ?  301 SAM B "C1'" 1 
HETATM 3922 N N9    . SAM H 2 .   ? -27.72200 2.46600   39.90400 1.000 27.43643 ?  301 SAM B N9    1 
HETATM 3923 C C8    . SAM H 2 .   ? -26.47900 2.63700   40.45400 1.000 27.55861 ?  301 SAM B C8    1 
HETATM 3924 N N7    . SAM H 2 .   ? -25.52500 2.69600   39.56300 1.000 29.11196 ?  301 SAM B N7    1 
HETATM 3925 C C5    . SAM H 2 .   ? -26.17800 2.56000   38.34900 1.000 25.34505 ?  301 SAM B C5    1 
HETATM 3926 C C6    . SAM H 2 .   ? -25.71300 2.53800   37.02300 1.000 25.82296 ?  301 SAM B C6    1 
HETATM 3927 N N6    . SAM H 2 .   ? -24.43300 2.65900   36.68700 1.000 24.52884 ?  301 SAM B N6    1 
HETATM 3928 N N1    . SAM H 2 .   ? -26.63300 2.38700   36.04300 1.000 30.65560 ?  301 SAM B N1    1 
HETATM 3929 C C2    . SAM H 2 .   ? -27.92000 2.26400   36.38800 1.000 27.79479 ?  301 SAM B C2    1 
HETATM 3930 N N3    . SAM H 2 .   ? -28.47000 2.26800   37.59600 1.000 26.81530 ?  301 SAM B N3    1 
HETATM 3931 C C4    . SAM H 2 .   ? -27.53600 2.42100   38.54600 1.000 26.34479 ?  301 SAM B C4    1 
HETATM 3932 C C     . TRS I 3 .   ? -29.46600 4.06200   51.61800 1.000 42.99875 ?  302 TRS B C     1 
HETATM 3933 C C1    . TRS I 3 .   ? -30.54400 4.59400   52.56600 1.000 39.38411 ?  302 TRS B C1    1 
HETATM 3934 C C2    . TRS I 3 .   ? -28.16100 4.82200   51.82300 1.000 40.81918 ?  302 TRS B C2    1 
HETATM 3935 C C3    . TRS I 3 .   ? -29.91700 4.16600   50.15500 1.000 41.43591 ?  302 TRS B C3    1 
HETATM 3936 N N     . TRS I 3 .   ? -29.22700 2.65500   51.93500 1.000 39.08352 ?  302 TRS B N     1 
HETATM 3937 O O1    . TRS I 3 .   ? -30.08000 4.67300   53.90200 1.000 40.80647 ?  302 TRS B O1    1 
HETATM 3938 O O2    . TRS I 3 .   ? -28.39400 6.14800   51.40500 1.000 41.65930 ?  302 TRS B O2    1 
HETATM 3939 O O3    . TRS I 3 .   ? -28.89800 3.73700   49.26500 1.000 42.36362 ?  302 TRS B O3    1 
HETATM 3940 O O     . HOH J 5 .   ? -2.68500  -12.36100 47.26800 1.000 43.45607 ?  401 HOH A O     1 
HETATM 3941 O O     . HOH J 5 .   ? -10.01600 6.50200   29.81000 1.000 29.40588 ?  402 HOH A O     1 
HETATM 3942 O O     . HOH J 5 .   ? -13.89000 -8.47600  16.80500 1.000 44.99497 ?  403 HOH A O     1 
HETATM 3943 O O     . HOH J 5 .   ? -11.86900 -30.41400 38.32400 1.000 35.26680 ?  404 HOH A O     1 
HETATM 3944 O O     . HOH J 5 .   ? -9.19600  -22.93600 -4.13300 1.000 26.29160 ?  405 HOH A O     1 
HETATM 3945 O O     . HOH J 5 .   ? -19.830   -23.027   19.555   1.000 39.70416 ?  406 HOH A O     1 
HETATM 3946 O O     . HOH J 5 .   ? -7.38200  -9.38200  17.94600 1.000 39.10764 ?  407 HOH A O     1 
HETATM 3947 O O     . HOH J 5 .   ? -21.88800 -28.74000 24.10800 1.000 39.58693 ?  408 HOH A O     1 
HETATM 3948 O O     . HOH J 5 .   ? -5.12500  -15.37800 49.29700 1.000 43.43247 ?  409 HOH A O     1 
HETATM 3949 O O     . HOH J 5 .   ? -5.16800  -22.84800 7.06700  1.000 41.41512 ?  410 HOH A O     1 
HETATM 3950 O O     . HOH J 5 .   ? -14.61300 -11.72500 17.31700 1.000 40.70963 ?  411 HOH A O     1 
HETATM 3951 O O     . HOH J 5 .   ? -19.40500 3.21500   36.32300 1.000 32.03187 ?  412 HOH A O     1 
HETATM 3952 O O     . HOH J 5 .   ? -8.73900  -11.87400 30.05200 1.000 25.53090 ?  413 HOH A O     1 
HETATM 3953 O O     . HOH J 5 .   ? -25.07700 -18.13300 23.65800 1.000 43.63749 ?  414 HOH A O     1 
HETATM 3954 O O     . HOH J 5 .   ? -15.67600 -17.23400 12.85400 1.000 36.31782 ?  415 HOH A O     1 
HETATM 3955 O O     . HOH J 5 .   ? -9.96800  -17.15200 28.79600 1.000 22.95673 ?  416 HOH A O     1 
HETATM 3956 O O     . HOH J 5 .   ? -5.64200  1.25700   16.75000 1.000 37.41404 ?  417 HOH A O     1 
HETATM 3957 O O     . HOH J 5 .   ? -23.32900 -8.23300  25.66700 1.000 40.60948 ?  418 HOH A O     1 
HETATM 3958 O O     . HOH J 5 .   ? -4.50000  -27.74100 28.99000 1.000 29.59873 ?  419 HOH A O     1 
HETATM 3959 O O     . HOH J 5 .   ? 1.45800   -17.01700 22.30000 1.000 26.81411 ?  420 HOH A O     1 
HETATM 3960 O O     . HOH J 5 .   ? -10.31200 0.90300   21.63500 1.000 28.99931 ?  421 HOH A O     1 
HETATM 3961 O O     . HOH J 5 .   ? -16.69700 -0.86700  24.09900 1.000 30.24171 ?  422 HOH A O     1 
HETATM 3962 O O     . HOH J 5 .   ? 0.28600   -3.95500  28.94300 1.000 24.55112 ?  423 HOH A O     1 
HETATM 3963 O O     . HOH J 5 .   ? -20.03600 -20.78200 17.08600 1.000 41.65458 ?  424 HOH A O     1 
HETATM 3964 O O     . HOH J 5 .   ? -14.44800 -25.88600 3.50800  1.000 46.40722 ?  425 HOH A O     1 
HETATM 3965 O O     . HOH J 5 .   ? -2.23100  -24.13000 33.28000 1.000 31.46102 ?  426 HOH A O     1 
HETATM 3966 O O     . HOH J 5 .   ? -5.50300  -18.14400 23.09100 1.000 25.49222 ?  427 HOH A O     1 
HETATM 3967 O O     . HOH J 5 .   ? 7.69400   -15.86400 25.56000 1.000 51.08405 ?  428 HOH A O     1 
HETATM 3968 O O     . HOH J 5 .   ? -19.27000 -21.96600 35.38200 1.000 29.21203 ?  429 HOH A O     1 
HETATM 3969 O O     . HOH J 5 .   ? -1.77800  -26.79700 30.94200 1.000 29.69600 ?  430 HOH A O     1 
HETATM 3970 O O     . HOH J 5 .   ? -3.89900  8.68400   29.23800 1.000 31.00267 ?  431 HOH A O     1 
HETATM 3971 O O     . HOH J 5 .   ? -10.50900 -31.10200 21.37000 1.000 36.01098 ?  432 HOH A O     1 
HETATM 3972 O O     . HOH J 5 .   ? -5.96700  -5.74400  28.89000 1.000 23.07182 ?  433 HOH A O     1 
HETATM 3973 O O     . HOH J 5 .   ? -9.45400  -26.37100 34.29900 1.000 25.36964 ?  434 HOH A O     1 
HETATM 3974 O O     . HOH J 5 .   ? 0.37100   -23.24800 32.82000 1.000 40.02931 ?  435 HOH A O     1 
HETATM 3975 O O     . HOH J 5 .   ? -16.44500 5.08900   24.79900 1.000 30.84774 ?  436 HOH A O     1 
HETATM 3976 O O     . HOH J 5 .   ? -6.85200  4.55400   41.69100 1.000 38.80904 ?  437 HOH A O     1 
HETATM 3977 O O     . HOH J 5 .   ? -1.07600  -1.14200  18.14000 1.000 36.20908 ?  438 HOH A O     1 
HETATM 3978 O O     . HOH J 5 .   ? 5.96500   1.12800   39.18600 1.000 33.99144 ?  439 HOH A O     1 
HETATM 3979 O O     . HOH J 5 .   ? -13.09500 2.05500   14.94900 1.000 42.77024 ?  440 HOH A O     1 
HETATM 3980 O O     . HOH J 5 .   ? -7.95000  -21.83700 0.03400  1.000 34.35432 ?  441 HOH A O     1 
HETATM 3981 O O     . HOH J 5 .   ? -12.96200 -23.61100 43.45100 1.000 37.50916 ?  442 HOH A O     1 
HETATM 3982 O O     . HOH J 5 .   ? 6.24600   3.88600   26.91200 1.000 41.01365 ?  443 HOH A O     1 
HETATM 3983 O O     . HOH J 5 .   ? -10.71000 4.89200   15.73600 1.000 38.53531 ?  444 HOH A O     1 
HETATM 3984 O O     . HOH J 5 .   ? -7.22700  -11.50400 22.04500 1.000 28.01803 ?  445 HOH A O     1 
HETATM 3985 O O     . HOH J 5 .   ? -21.04700 -6.08500  36.30400 1.000 31.04773 ?  446 HOH A O     1 
HETATM 3986 O O     . HOH J 5 .   ? -16.25100 -15.08400 43.39200 1.000 35.83505 ?  447 HOH A O     1 
HETATM 3987 O O     . HOH J 5 .   ? 5.42400   -14.07500 16.40700 1.000 30.17023 ?  448 HOH A O     1 
HETATM 3988 O O     . HOH J 5 .   ? 2.14900   13.88000  28.23700 1.000 38.27834 ?  449 HOH A O     1 
HETATM 3989 O O     . HOH J 5 .   ? -10.70900 -7.46000  47.57700 1.000 35.57464 ?  450 HOH A O     1 
HETATM 3990 O O     . HOH J 5 .   ? -6.30600  -23.80100 -1.29000 1.000 34.19116 ?  451 HOH A O     1 
HETATM 3991 O O     . HOH J 5 .   ? -23.76400 -14.92400 34.17500 1.000 35.23888 ?  452 HOH A O     1 
HETATM 3992 O O     . HOH J 5 .   ? -4.572    -33.538   33.152   1.000 35.92481 ?  453 HOH A O     1 
HETATM 3993 O O     . HOH J 5 .   ? -3.87600  -18.89300 20.49800 1.000 25.41599 ?  454 HOH A O     1 
HETATM 3994 O O     . HOH J 5 .   ? -6.04300  0.91600   40.66000 1.000 32.29542 ?  455 HOH A O     1 
HETATM 3995 O O     . HOH J 5 .   ? -6.82600  -16.17500 24.59400 1.000 23.69130 ?  456 HOH A O     1 
HETATM 3996 O O     . HOH J 5 .   ? 3.83600   -21.09800 35.37700 1.000 39.61385 ?  457 HOH A O     1 
HETATM 3997 O O     . HOH J 5 .   ? 4.542     20.387    25.461   1.000 35.76654 ?  458 HOH A O     1 
HETATM 3998 O O     . HOH J 5 .   ? 4.88500   -0.02600  25.31000 1.000 32.65145 ?  459 HOH A O     1 
HETATM 3999 O O     . HOH J 5 .   ? -3.20500  -23.25900 44.94300 1.000 47.13198 ?  460 HOH A O     1 
HETATM 4000 O O     . HOH J 5 .   ? 4.06500   8.60400   26.72300 1.000 40.73513 ?  461 HOH A O     1 
HETATM 4001 O O     . HOH J 5 .   ? -6.89200  -5.72100  17.04800 1.000 43.50229 ?  462 HOH A O     1 
HETATM 4002 O O     . HOH J 5 .   ? 0.74800   -30.67700 32.50600 1.000 35.99375 ?  463 HOH A O     1 
HETATM 4003 O O     . HOH J 5 .   ? -19.96700 -8.12300  37.56200 1.000 30.32576 ?  464 HOH A O     1 
HETATM 4004 O O     . HOH J 5 .   ? -9.99800  -25.82400 45.22600 1.000 36.88970 ?  465 HOH A O     1 
HETATM 4005 O O     . HOH J 5 .   ? -11.45500 -32.26000 37.04600 1.000 36.62351 ?  466 HOH A O     1 
HETATM 4006 O O     . HOH J 5 .   ? -16.03200 -35.35600 26.50300 1.000 44.75153 ?  467 HOH A O     1 
HETATM 4007 O O     . HOH J 5 .   ? -3.87400  2.62400   40.89400 1.000 35.42137 ?  468 HOH A O     1 
HETATM 4008 O O     . HOH J 5 .   ? 4.81400   -18.29400 20.53400 1.000 34.21925 ?  469 HOH A O     1 
HETATM 4009 O O     . HOH J 5 .   ? -8.44100  -14.84800 28.70300 1.000 23.33403 ?  470 HOH A O     1 
HETATM 4010 O O     . HOH J 5 .   ? -15.93400 -18.50700 6.21200  1.000 40.40681 ?  471 HOH A O     1 
HETATM 4011 O O     . HOH J 5 .   ? -6.10200  -15.22700 27.17700 1.000 26.65492 ?  472 HOH A O     1 
HETATM 4012 O O     . HOH J 5 .   ? 9.61400   -9.20100  25.48800 1.000 31.73904 ?  473 HOH A O     1 
HETATM 4013 O O     . HOH J 5 .   ? -21.91900 -9.76200  37.06900 1.000 37.21045 ?  474 HOH A O     1 
HETATM 4014 O O     . HOH J 5 .   ? -22.18500 -9.54700  44.00100 1.000 43.30647 ?  475 HOH A O     1 
HETATM 4015 O O     . HOH J 5 .   ? -24.50000 -20.21000 30.65300 1.000 39.55101 ?  476 HOH A O     1 
HETATM 4016 O O     . HOH J 5 .   ? 1.94200   11.10600  15.38600 1.000 36.96760 ?  477 HOH A O     1 
HETATM 4017 O O     . HOH J 5 .   ? -7.03300  -18.86600 15.53600 1.000 32.63725 ?  478 HOH A O     1 
HETATM 4018 O O     . HOH J 5 .   ? 7.35800   -5.61800  26.40500 1.000 28.70381 ?  479 HOH A O     1 
HETATM 4019 O O     . HOH J 5 .   ? -27.13200 -11.66600 29.84200 1.000 44.08970 ?  480 HOH A O     1 
HETATM 4020 O O     . HOH J 5 .   ? -25.91700 -5.65200  17.87500 1.000 56.92892 ?  481 HOH A O     1 
HETATM 4021 O O     . HOH J 5 .   ? -22.42600 -14.87600 13.17900 1.000 43.34959 ?  482 HOH A O     1 
HETATM 4022 O O     . HOH J 5 .   ? -18.46200 -7.76000  25.22500 1.000 31.49172 ?  483 HOH A O     1 
HETATM 4023 O O     . HOH J 5 .   ? -6.70300  9.20400   28.86600 1.000 43.51266 ?  484 HOH A O     1 
HETATM 4024 O O     . HOH J 5 .   ? -1.49300  -19.86400 17.16400 1.000 39.15654 ?  485 HOH A O     1 
HETATM 4025 O O     . HOH J 5 .   ? 1.31800   -21.83800 24.72800 1.000 33.65194 ?  486 HOH A O     1 
HETATM 4026 O O     . HOH J 5 .   ? -16.72000 -2.54100  26.69500 1.000 26.38171 ?  487 HOH A O     1 
HETATM 4027 O O     . HOH J 5 .   ? -13.75300 11.37700  22.26000 1.000 38.12329 ?  488 HOH A O     1 
HETATM 4028 O O     . HOH J 5 .   ? -25.00500 -14.72200 15.49500 1.000 47.76034 ?  489 HOH A O     1 
HETATM 4029 O O     . HOH J 5 .   ? -11.16800 -24.69000 -1.08900 1.000 43.66907 ?  490 HOH A O     1 
HETATM 4030 O O     . HOH J 5 .   ? 6.58700   -15.65100 34.26200 1.000 31.43301 ?  491 HOH A O     1 
HETATM 4031 O O     . HOH J 5 .   ? -12.36300 -23.82800 2.62200  1.000 43.16192 ?  492 HOH A O     1 
HETATM 4032 O O     . HOH J 5 .   ? -9.61000  -30.31600 40.67200 1.000 43.83589 ?  493 HOH A O     1 
HETATM 4033 O O     . HOH J 5 .   ? -7.85000  -11.51800 19.74600 1.000 37.45089 ?  494 HOH A O     1 
HETATM 4034 O O     . HOH J 5 .   ? -12.68800 -18.93600 46.66700 1.000 40.10453 ?  495 HOH A O     1 
HETATM 4035 O O     . HOH J 5 .   ? -7.71900  12.31300  26.25800 1.000 40.92449 ?  496 HOH A O     1 
HETATM 4036 O O     . HOH J 5 .   ? -12.68700 -31.88600 15.12100 1.000 36.74092 ?  497 HOH A O     1 
HETATM 4037 O O     . HOH J 5 .   ? -1.146    -33.528   34.235   1.000 42.81133 ?  498 HOH A O     1 
HETATM 4038 O O     . HOH J 5 .   ? -1.85800  -17.72500 19.01500 1.000 32.14439 ?  499 HOH A O     1 
HETATM 4039 O O     . HOH J 5 .   ? 7.71800   -0.82000  26.45100 1.000 42.06934 ?  500 HOH A O     1 
HETATM 4040 O O     . HOH J 5 .   ? -24.44200 -17.56500 32.62300 1.000 43.35051 ?  501 HOH A O     1 
HETATM 4041 O O     . HOH J 5 .   ? -20.85400 -2.76500  42.26600 1.000 39.18399 ?  502 HOH A O     1 
HETATM 4042 O O     . HOH J 5 .   ? 10.56700  -6.49800  32.45900 1.000 38.56786 ?  503 HOH A O     1 
HETATM 4043 O O     . HOH J 5 .   ? 6.97500   -11.13800 39.79700 1.000 46.05007 ?  504 HOH A O     1 
HETATM 4044 O O     . HOH J 5 .   ? -7.26300  -6.25200  21.86200 1.000 27.94208 ?  505 HOH A O     1 
HETATM 4045 O O     . HOH J 5 .   ? -13.41000 -19.67100 12.69400 1.000 39.19297 ?  506 HOH A O     1 
HETATM 4046 O O     . HOH J 5 .   ? -10.57300 -20.00800 47.02100 1.000 37.02836 ?  507 HOH A O     1 
HETATM 4047 O O     . HOH J 5 .   ? -2.61100  -29.39000 38.14400 1.000 39.79301 ?  508 HOH A O     1 
HETATM 4048 O O     . HOH J 5 .   ? -21.22900 -21.09800 34.65500 1.000 42.65572 ?  509 HOH A O     1 
HETATM 4049 O O     . HOH J 5 .   ? -5.00700  -19.85000 16.14700 1.000 43.45347 ?  510 HOH A O     1 
HETATM 4050 O O     . HOH J 5 .   ? -24.37100 -3.23200  31.03100 1.000 40.75972 ?  511 HOH A O     1 
HETATM 4051 O O     . HOH J 5 .   ? -18.17700 -5.51800  24.69600 1.000 34.56228 ?  512 HOH A O     1 
HETATM 4052 O O     . HOH J 5 .   ? -3.65500  -27.53200 42.66100 1.000 50.18431 ?  513 HOH A O     1 
HETATM 4053 O O     . HOH J 5 .   ? -19.30200 -34.11500 31.78300 1.000 46.90522 ?  514 HOH A O     1 
HETATM 4054 O O     . HOH J 5 .   ? -17.79900 3.42000   22.72100 1.000 38.65013 ?  515 HOH A O     1 
HETATM 4055 O O     . HOH J 5 .   ? -16.00300 -23.55200 42.10600 1.000 43.02988 ?  516 HOH A O     1 
HETATM 4056 O O     . HOH J 5 .   ? -22.60800 -11.42100 38.95800 1.000 46.10465 ?  517 HOH A O     1 
HETATM 4057 O O     . HOH J 5 .   ? -24.60700 -12.31200 36.40700 1.000 46.35845 ?  518 HOH A O     1 
HETATM 4058 O O     . HOH J 5 .   ? -10.41900 -24.87900 4.21300  1.000 44.64873 ?  519 HOH A O     1 
HETATM 4059 O O     . HOH J 5 .   ? 8.58700   -8.43900  19.72000 1.000 39.73394 ?  520 HOH A O     1 
HETATM 4060 O O     . HOH J 5 .   ? -18.22400 -16.06700 42.73400 1.000 43.94230 ?  521 HOH A O     1 
HETATM 4061 O O     . HOH J 5 .   ? 6.34000   -18.94000 29.76700 1.000 43.32300 ?  522 HOH A O     1 
HETATM 4062 O O     . HOH J 5 .   ? 0.47000   -27.27600 30.18700 1.000 36.44831 ?  523 HOH A O     1 
HETATM 4063 O O     . HOH J 5 .   ? -18.61300 -27.57100 36.70400 1.000 37.70390 ?  524 HOH A O     1 
HETATM 4064 O O     . HOH J 5 .   ? -25.90500 -8.27400  17.69300 1.000 61.65288 ?  525 HOH A O     1 
HETATM 4065 O O     . HOH J 5 .   ? 3.73400   11.58800  27.88700 1.000 43.66131 ?  526 HOH A O     1 
HETATM 4066 O O     . HOH J 5 .   ? 3.21900   -21.28200 26.31400 1.000 38.61990 ?  527 HOH A O     1 
HETATM 4067 O O     . HOH J 5 .   ? 8.27800   -15.37800 35.89600 1.000 40.56721 ?  528 HOH A O     1 
HETATM 4068 O O     . HOH J 5 .   ? -19.47700 1.72300   43.22200 1.000 46.86760 ?  529 HOH A O     1 
HETATM 4069 O O     . HOH J 5 .   ? -20.42400 -23.41700 38.37900 1.000 46.80173 ?  530 HOH A O     1 
HETATM 4070 O O     . HOH J 5 .   ? 0.41600   -26.71400 36.06800 1.000 48.82866 ?  531 HOH A O     1 
HETATM 4071 O O     . HOH J 5 .   ? -6.62100  -7.70000  20.19000 1.000 32.54144 ?  532 HOH A O     1 
HETATM 4072 O O     . HOH J 5 .   ? 4.95800   -19.78200 28.11700 1.000 42.92270 ?  533 HOH A O     1 
HETATM 4073 O O     . HOH J 5 .   ? 2.18700   -23.11200 34.62200 1.000 36.36667 ?  534 HOH A O     1 
HETATM 4074 O O     . HOH J 5 .   ? 4.05000   -17.29100 22.64400 1.000 36.68113 ?  535 HOH A O     1 
HETATM 4075 O O     . HOH K 5 .   ? -35.46600 -9.41200  43.97000 1.000 37.80851 ?  401 HOH B O     1 
HETATM 4076 O O     . HOH K 5 .   ? -27.99300 -9.27800  35.21100 1.000 40.32487 ?  402 HOH B O     1 
HETATM 4077 O O     . HOH K 5 .   ? -30.83900 -9.22700  33.18300 1.000 38.51427 ?  403 HOH B O     1 
HETATM 4078 O O     . HOH K 5 .   ? -25.42500 -5.32000  38.69400 1.000 35.04237 ?  404 HOH B O     1 
HETATM 4079 O O     . HOH K 5 .   ? -22.23200 -2.12900  33.91200 1.000 25.44008 ?  405 HOH B O     1 
HETATM 4080 O O     . HOH K 5 .   ? -50.98500 7.48500   40.43100 1.000 39.48354 ?  406 HOH B O     1 
HETATM 4081 O O     . HOH K 5 .   ? -48.10000 8.91200   49.33300 1.000 40.75790 ?  407 HOH B O     1 
HETATM 4082 O O     . HOH K 5 .   ? -41.64100 13.99500  48.46300 1.000 33.86693 ?  408 HOH B O     1 
HETATM 4083 O O     . HOH K 5 .   ? -41.33500 -10.73300 61.82800 1.000 41.94348 ?  409 HOH B O     1 
HETATM 4084 O O     . HOH K 5 .   ? -43.59600 8.32500   60.05800 1.000 38.79511 ?  410 HOH B O     1 
HETATM 4085 O O     . HOH K 5 .   ? -29.90900 26.77200  30.73500 1.000 34.33519 ?  411 HOH B O     1 
HETATM 4086 O O     . HOH K 5 .   ? -44.42800 6.01300   50.78200 1.000 35.63104 ?  412 HOH B O     1 
HETATM 4087 O O     . HOH K 5 .   ? -28.51700 -0.80100  28.39500 1.000 34.74040 ?  413 HOH B O     1 
HETATM 4088 O O     . HOH K 5 .   ? -38.16700 0.01500   68.91800 1.000 32.60594 ?  414 HOH B O     1 
HETATM 4089 O O     . HOH K 5 .   ? -38.66600 3.79000   40.07900 1.000 25.77590 ?  415 HOH B O     1 
HETATM 4090 O O     . HOH K 5 .   ? -51.85400 -1.83500  32.30800 1.000 39.79835 ?  416 HOH B O     1 
HETATM 4091 O O     . HOH K 5 .   ? -48.64400 8.57900   38.09800 1.000 36.22083 ?  417 HOH B O     1 
HETATM 4092 O O     . HOH K 5 .   ? -29.76300 11.76600  39.45100 1.000 21.05945 ?  418 HOH B O     1 
HETATM 4093 O O     . HOH K 5 .   ? -17.74300 13.03000  36.44600 1.000 36.52814 ?  419 HOH B O     1 
HETATM 4094 O O     . HOH K 5 .   ? -50.348   12.776    30.846   1.000 43.42659 ?  420 HOH B O     1 
HETATM 4095 O O     . HOH K 5 .   ? -34.57800 7.07500   38.46400 1.000 24.05636 ?  421 HOH B O     1 
HETATM 4096 O O     . HOH K 5 .   ? -22.44600 16.85300  25.68800 1.000 43.56665 ?  422 HOH B O     1 
HETATM 4097 O O     . HOH K 5 .   ? -13.36300 25.86300  38.74200 1.000 42.85619 ?  423 HOH B O     1 
HETATM 4098 O O     . HOH K 5 .   ? -36.92300 0.62900   24.52200 1.000 34.60442 ?  424 HOH B O     1 
HETATM 4099 O O     . HOH K 5 .   ? -40.86000 -5.97000  32.61800 1.000 30.14280 ?  425 HOH B O     1 
HETATM 4100 O O     . HOH K 5 .   ? -17.73600 13.13600  50.85900 1.000 38.78208 ?  426 HOH B O     1 
HETATM 4101 O O     . HOH K 5 .   ? -28.61700 26.29300  27.42400 1.000 45.08413 ?  427 HOH B O     1 
HETATM 4102 O O     . HOH K 5 .   ? -38.59500 3.77600   53.78400 1.000 32.16654 ?  428 HOH B O     1 
HETATM 4103 O O     . HOH K 5 .   ? -34.41700 23.71000  44.26500 1.000 33.16269 ?  429 HOH B O     1 
HETATM 4104 O O     . HOH K 5 .   ? -31.08000 14.88400  20.65800 1.000 48.94295 ?  430 HOH B O     1 
HETATM 4105 O O     . HOH K 5 .   ? -37.36300 -0.37000  55.66800 1.000 41.36477 ?  431 HOH B O     1 
HETATM 4106 O O     . HOH K 5 .   ? -39.62200 17.21400  54.87600 1.000 27.50270 ?  432 HOH B O     1 
HETATM 4107 O O     . HOH K 5 .   ? -47.391   26.825    25.303   1.000 31.55465 ?  433 HOH B O     1 
HETATM 4108 O O     . HOH K 5 .   ? -40.85100 24.98100  39.52700 1.000 36.87383 ?  434 HOH B O     1 
HETATM 4109 O O     . HOH K 5 .   ? -15.62900 12.45200  32.57600 1.000 43.72116 ?  435 HOH B O     1 
HETATM 4110 O O     . HOH K 5 .   ? -42.42100 10.83700  20.56200 1.000 38.24484 ?  436 HOH B O     1 
HETATM 4111 O O     . HOH K 5 .   ? -29.63100 8.08600   58.99000 1.000 39.52915 ?  437 HOH B O     1 
HETATM 4112 O O     . HOH K 5 .   ? -30.56500 18.32200  40.33700 1.000 24.79790 ?  438 HOH B O     1 
HETATM 4113 O O     . HOH K 5 .   ? -32.12900 22.60800  17.77600 1.000 51.18222 ?  439 HOH B O     1 
HETATM 4114 O O     . HOH K 5 .   ? -30.06000 7.60300   49.73300 1.000 40.56847 ?  440 HOH B O     1 
HETATM 4115 O O     . HOH K 5 .   ? -43.94300 20.50400  28.26300 1.000 40.93273 ?  441 HOH B O     1 
HETATM 4116 O O     . HOH K 5 .   ? -38.06100 6.19800   44.57500 1.000 27.89819 ?  442 HOH B O     1 
HETATM 4117 O O     . HOH K 5 .   ? -12.07900 29.18200  39.93200 1.000 40.10976 ?  443 HOH B O     1 
HETATM 4118 O O     . HOH K 5 .   ? -15.62000 11.20100  50.29600 1.000 37.61136 ?  444 HOH B O     1 
HETATM 4119 O O     . HOH K 5 .   ? -40.19700 6.41700   46.58200 1.000 28.35602 ?  445 HOH B O     1 
HETATM 4120 O O     . HOH K 5 .   ? -43.66000 20.97500  40.59800 1.000 39.91931 ?  446 HOH B O     1 
HETATM 4121 O O     . HOH K 5 .   ? -32.24000 -1.00100  65.42500 1.000 34.03485 ?  447 HOH B O     1 
HETATM 4122 O O     . HOH K 5 .   ? -19.52000 5.98200   35.88200 1.000 28.98159 ?  448 HOH B O     1 
HETATM 4123 O O     . HOH K 5 .   ? -26.28600 -1.22400  29.76400 1.000 35.16919 ?  449 HOH B O     1 
HETATM 4124 O O     . HOH K 5 .   ? -29.22200 -3.07100  29.13900 1.000 40.64979 ?  450 HOH B O     1 
HETATM 4125 O O     . HOH K 5 .   ? -38.73400 -4.09800  69.24000 1.000 41.77162 ?  451 HOH B O     1 
HETATM 4126 O O     . HOH K 5 .   ? -25.65500 27.21900  42.12100 1.000 44.08904 ?  452 HOH B O     1 
HETATM 4127 O O     . HOH K 5 .   ? -20.65200 10.36100  45.17500 1.000 25.83601 ?  453 HOH B O     1 
HETATM 4128 O O     . HOH K 5 .   ? -35.88200 1.51100   20.38500 1.000 44.15969 ?  454 HOH B O     1 
HETATM 4129 O O     . HOH K 5 .   ? -26.00300 15.77500  27.06900 1.000 33.52967 ?  455 HOH B O     1 
HETATM 4130 O O     . HOH K 5 .   ? -11.31300 10.15800  44.75400 1.000 43.05393 ?  456 HOH B O     1 
HETATM 4131 O O     . HOH K 5 .   ? -26.76300 -6.92900  39.42100 1.000 32.87537 ?  457 HOH B O     1 
HETATM 4132 O O     . HOH K 5 .   ? -38.00000 -1.85200  73.13200 1.000 30.18318 ?  458 HOH B O     1 
HETATM 4133 O O     . HOH K 5 .   ? -46.10000 0.00100   26.36700 1.000 41.40455 ?  459 HOH B O     1 
HETATM 4134 O O     . HOH K 5 .   ? -3.89700  26.66500  42.15400 1.000 35.58567 ?  460 HOH B O     1 
HETATM 4135 O O     . HOH K 5 .   ? -24.17200 9.24600   47.70100 1.000 40.58954 ?  461 HOH B O     1 
HETATM 4136 O O     . HOH K 5 .   ? -17.83500 20.68500  38.01900 1.000 30.58991 ?  462 HOH B O     1 
HETATM 4137 O O     . HOH K 5 .   ? -40.39100 0.64100   70.78900 1.000 37.00846 ?  463 HOH B O     1 
HETATM 4138 O O     . HOH K 5 .   ? -26.71300 1.94900   50.76300 1.000 42.40219 ?  464 HOH B O     1 
HETATM 4139 O O     . HOH K 5 .   ? -10.01500 11.86300  41.97800 1.000 33.31138 ?  465 HOH B O     1 
HETATM 4140 O O     . HOH K 5 .   ? -38.55700 24.04700  45.71700 1.000 34.14216 ?  466 HOH B O     1 
HETATM 4141 O O     . HOH K 5 .   ? -28.15400 23.89800  44.01600 1.000 29.64305 ?  467 HOH B O     1 
HETATM 4142 O O     . HOH K 5 .   ? -44.71700 19.35300  46.12200 1.000 41.57634 ?  468 HOH B O     1 
HETATM 4143 O O     . HOH K 5 .   ? -36.98000 6.09000   40.37100 1.000 24.19298 ?  469 HOH B O     1 
HETATM 4144 O O     . HOH K 5 .   ? -31.72000 -13.02800 38.04100 1.000 46.14760 ?  470 HOH B O     1 
HETATM 4145 O O     . HOH K 5 .   ? -42.26600 2.56700   22.64200 1.000 34.68398 ?  471 HOH B O     1 
HETATM 4146 O O     . HOH K 5 .   ? -21.38500 14.14400  50.79700 1.000 35.11092 ?  472 HOH B O     1 
HETATM 4147 O O     . HOH K 5 .   ? -20.39000 2.01100   34.32000 1.000 29.54257 ?  473 HOH B O     1 
HETATM 4148 O O     . HOH K 5 .   ? -52.62100 4.24600   31.39900 1.000 41.26498 ?  474 HOH B O     1 
HETATM 4149 O O     . HOH K 5 .   ? -56.49100 2.87700   39.14500 1.000 44.79066 ?  475 HOH B O     1 
HETATM 4150 O O     . HOH K 5 .   ? -50.28700 4.36800   42.38000 1.000 33.56806 ?  476 HOH B O     1 
HETATM 4151 O O     . HOH K 5 .   ? -18.48900 10.33800  26.11800 1.000 44.65935 ?  477 HOH B O     1 
HETATM 4152 O O     . HOH K 5 .   ? -44.56600 0.58800   58.25000 1.000 44.74629 ?  478 HOH B O     1 
HETATM 4153 O O     . HOH K 5 .   ? -45.71900 -6.87300  59.59500 1.000 44.51581 ?  479 HOH B O     1 
HETATM 4154 O O     . HOH K 5 .   ? -18.73800 29.95500  44.75800 1.000 48.36590 ?  480 HOH B O     1 
HETATM 4155 O O     . HOH K 5 .   ? -40.26400 14.64300  22.99300 1.000 35.86008 ?  481 HOH B O     1 
HETATM 4156 O O     . HOH K 5 .   ? -6.33000  30.29000  37.83500 1.000 35.21549 ?  482 HOH B O     1 
HETATM 4157 O O     . HOH K 5 .   ? -38.53900 -4.39500  66.35300 1.000 39.35892 ?  483 HOH B O     1 
HETATM 4158 O O     . HOH K 5 .   ? -36.35900 13.83100  17.72600 1.000 48.67872 ?  484 HOH B O     1 
HETATM 4159 O O     . HOH K 5 .   ? -51.81300 4.60100   44.63200 1.000 39.25762 ?  485 HOH B O     1 
HETATM 4160 O O     . HOH K 5 .   ? -32.49300 -7.36500  31.73700 1.000 37.84423 ?  486 HOH B O     1 
HETATM 4161 O O     . HOH K 5 .   ? -22.60000 2.28000   39.51800 1.000 33.15197 ?  487 HOH B O     1 
HETATM 4162 O O     . HOH K 5 .   ? -23.90600 -4.13800  34.21000 1.000 35.55209 ?  488 HOH B O     1 
HETATM 4163 O O     . HOH K 5 .   ? -28.31000 -7.52600  42.21800 1.000 36.92417 ?  489 HOH B O     1 
HETATM 4164 O O     . HOH K 5 .   ? -40.80300 7.50000   49.59500 1.000 34.36623 ?  490 HOH B O     1 
HETATM 4165 O O     . HOH K 5 .   ? -46.20000 18.71200  42.04700 1.000 37.85732 ?  491 HOH B O     1 
HETATM 4166 O O     . HOH K 5 .   ? -15.641   24.406    51.989   1.000 41.60258 ?  492 HOH B O     1 
HETATM 4167 O O     . HOH K 5 .   ? -25.14400 28.20300  38.84900 1.000 43.76339 ?  493 HOH B O     1 
HETATM 4168 O O     . HOH K 5 .   ? -21.60300 12.51500  52.66600 1.000 40.29701 ?  494 HOH B O     1 
HETATM 4169 O O     . HOH K 5 .   ? -27.30300 10.02100  50.26300 1.000 45.91043 ?  495 HOH B O     1 
HETATM 4170 O O     . HOH K 5 .   ? -43.32600 -10.52100 60.54800 1.000 38.63750 ?  496 HOH B O     1 
HETATM 4171 O O     . HOH K 5 .   ? -37.34300 26.97200  38.79600 1.000 40.66598 ?  497 HOH B O     1 
HETATM 4172 O O     . HOH K 5 .   ? -23.62300 2.81600   43.18200 1.000 36.16245 ?  498 HOH B O     1 
HETATM 4173 O O     . HOH K 5 .   ? -37.19800 27.58000  41.11700 1.000 48.20278 ?  499 HOH B O     1 
HETATM 4174 O O     . HOH K 5 .   ? -49.01400 6.48000   53.17900 1.000 40.34288 ?  500 HOH B O     1 
HETATM 4175 O O     . HOH K 5 .   ? -34.24000 -3.46200  54.86300 1.000 36.14959 ?  501 HOH B O     1 
HETATM 4176 O O     . HOH K 5 .   ? -20.90300 3.80200   38.55200 1.000 28.72747 ?  502 HOH B O     1 
HETATM 4177 O O     . HOH K 5 .   ? -47.07900 4.14100   48.90700 1.000 37.24764 ?  503 HOH B O     1 
HETATM 4178 O O     . HOH K 5 .   ? -44.33900 19.88000  37.86900 1.000 37.08786 ?  504 HOH B O     1 
HETATM 4179 O O     . HOH K 5 .   ? -44.76500 0.44400   55.34800 1.000 38.58200 ?  505 HOH B O     1 
HETATM 4180 O O     . HOH K 5 .   ? -42.51500 22.21100  26.67700 1.000 48.94263 ?  506 HOH B O     1 
HETATM 4181 O O     . HOH K 5 .   ? -40.63600 9.79000   51.31900 1.000 33.45637 ?  507 HOH B O     1 
HETATM 4182 O O     . HOH K 5 .   ? -44.48400 4.21100   22.54400 1.000 43.23202 ?  508 HOH B O     1 
HETATM 4183 O O     . HOH K 5 .   ? -47.34100 11.22200  19.33700 1.000 44.90556 ?  509 HOH B O     1 
HETATM 4184 O O     . HOH K 5 .   ? -32.76100 6.60900   49.20100 1.000 39.01911 ?  510 HOH B O     1 
HETATM 4185 O O     . HOH K 5 .   ? -25.04300 18.36500  27.12100 1.000 37.53715 ?  511 HOH B O     1 
HETATM 4186 O O     . HOH K 5 .   ? -29.04100 -4.67900  45.11800 1.000 41.08795 ?  512 HOH B O     1 
HETATM 4187 O O     . HOH K 5 .   ? -53.95100 6.56900   31.24900 1.000 56.63844 ?  513 HOH B O     1 
HETATM 4188 O O     . HOH K 5 .   ? -38.14200 7.92700   42.34500 1.000 28.09212 ?  514 HOH B O     1 
HETATM 4189 O O     . HOH K 5 .   ? -25.21400 5.72800   27.96900 1.000 36.44332 ?  515 HOH B O     1 
HETATM 4190 O O     . HOH K 5 .   ? -20.22000 27.15700  41.34300 1.000 35.59976 ?  516 HOH B O     1 
HETATM 4191 O O     . HOH K 5 .   ? -27.29600 6.99900   56.21500 1.000 45.23943 ?  517 HOH B O     1 
HETATM 4192 O O     . HOH K 5 .   ? -22.33900 27.08700  31.76200 1.000 42.43600 ?  518 HOH B O     1 
HETATM 4193 O O     . HOH K 5 .   ? -28.22500 3.23100   56.92700 1.000 46.90256 ?  519 HOH B O     1 
HETATM 4194 O O     . HOH K 5 .   ? -12.42300 7.14800   44.60900 1.000 46.68920 ?  520 HOH B O     1 
HETATM 4195 O O     . HOH K 5 .   ? -26.48600 3.27500   44.46600 1.000 35.57002 ?  521 HOH B O     1 
HETATM 4196 O O     . HOH K 5 .   ? -58.07300 4.66000   36.72200 1.000 47.89002 ?  522 HOH B O     1 
HETATM 4197 O O     . HOH K 5 .   ? -30.61900 26.26000  43.53300 1.000 40.83752 ?  523 HOH B O     1 
HETATM 4198 O O     . HOH K 5 .   ? -48.52700 5.90400   47.94400 1.000 44.66394 ?  524 HOH B O     1 
HETATM 4199 O O     . HOH K 5 .   ? -16.81800 8.08300   51.10900 1.000 42.62435 ?  525 HOH B O     1 
HETATM 4200 O O     . HOH K 5 .   ? -34.29500 -8.98400  33.76100 1.000 39.75065 ?  526 HOH B O     1 
HETATM 4201 O O     . HOH K 5 .   ? -10.005   28.971    49.607   1.000 40.43580 ?  527 HOH B O     1 
HETATM 4202 O O     . HOH K 5 .   ? -38.84900 25.92700  43.63800 1.000 43.16845 ?  528 HOH B O     1 
HETATM 4203 O O     . HOH K 5 .   ? -24.66500 8.49800   50.03200 1.000 43.39691 ?  529 HOH B O     1 
HETATM 4204 O O     . HOH K 5 .   ? -36.52200 -2.46700  54.93200 1.000 38.52863 ?  530 HOH B O     1 
HETATM 4205 O O     . HOH K 5 .   ? -28.56800 9.65500   46.24500 1.000 34.31374 ?  531 HOH B O     1 
HETATM 4206 O O     . HOH K 5 .   ? -23.69200 28.17800  37.11800 1.000 43.07629 ?  532 HOH B O     1 
HETATM 4207 O O     . HOH K 5 .   ? -16.05800 3.31200   43.27900 1.000 44.28763 ?  533 HOH B O     1 
HETATM 4208 O O     . HOH K 5 .   ? -46.24500 18.72600  39.25700 1.000 35.35510 ?  534 HOH B O     1 
HETATM 4209 O O     . HOH K 5 .   ? -19.33700 -3.06800  26.32200 1.000 37.89685 ?  535 HOH B O     1 
HETATM 4210 O O     . HOH K 5 .   ? -28.72100 2.48800   45.70900 1.000 36.33937 ?  536 HOH B O     1 
HETATM 4211 O O     . HOH K 5 .   ? -41.293   3.535     66.889   1.000 38.08345 ?  537 HOH B O     1 
HETATM 4212 O O     . HOH K 5 .   ? -14.14300 14.79700  33.88900 1.000 42.02157 ?  538 HOH B O     1 
HETATM 4213 O O     . HOH K 5 .   ? -37.49900 -1.57900  24.67800 1.000 40.77272 ?  539 HOH B O     1 
HETATM 4214 O O     . HOH K 5 .   ? -23.50600 10.46400  53.75800 1.000 52.83151 ?  540 HOH B O     1 
HETATM 4215 O O     . HOH K 5 .   ? -23.41000 -6.14200  36.29800 1.000 33.81981 ?  541 HOH B O     1 
HETATM 4216 O O     . HOH K 5 .   ? -56.42900 1.88800   44.11300 1.000 50.95478 ?  542 HOH B O     1 
HETATM 4217 O O     . HOH K 5 .   ? -31.838   23.077    51.132   1.000 43.41146 ?  543 HOH B O     1 
HETATM 4218 O O     . HOH K 5 .   ? -39.07400 -11.20300 57.68800 1.000 43.40509 ?  544 HOH B O     1 
HETATM 4219 O O     . HOH K 5 .   ? -29.47900 9.49500   48.50900 1.000 41.22658 ?  545 HOH B O     1 
HETATM 4220 O O     . HOH K 5 .   ? -18.44600 7.04300   25.36700 1.000 42.72526 ?  546 HOH B O     1 
HETATM 4221 O O     . HOH K 5 .   ? -34.04500 28.07800  36.33200 1.000 47.60046 ?  547 HOH B O     1 
HETATM 4222 O O     . HOH K 5 .   ? -27.76200 0.60500   46.53000 1.000 50.26819 ?  548 HOH B O     1 
HETATM 4223 O O     . HOH K 5 .   ? -49.89600 13.13700  37.34400 1.000 38.16787 ?  549 HOH B O     1 
HETATM 4224 O O     . HOH K 5 .   ? -3.97500  24.65100  40.14100 1.000 41.55209 ?  550 HOH B O     1 
HETATM 4225 O O     . HOH K 5 .   ? -25.35000 -5.49000  41.80700 1.000 42.27709 ?  551 HOH B O     1 
HETATM 4226 O O     . HOH K 5 .   ? -9.32800  17.33700  40.72500 1.000 49.36394 ?  552 HOH B O     1 
HETATM 4227 O O     . HOH K 5 .   ? -42.67100 7.25000   61.83300 1.000 41.04434 ?  553 HOH B O     1 
HETATM 4228 O O     . HOH K 5 .   ? -28.21200 26.36600  43.39000 1.000 33.94983 ?  554 HOH B O     1 
HETATM 4229 O O     . HOH K 5 .   ? -54.26200 -5.25100  33.14000 1.000 49.16577 ?  555 HOH B O     1 
# 
