data_9BXM
# 
_entry.id   9BXM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9BXM         pdb_00009bxm 10.2210/pdb9bxm/pdb 
WWPDB D_1000281148 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-08 ? 
2 'Structure model' 1 1 2025-02-05 ? 
3 'Structure model' 1 2 2025-03-19 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' '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 
3 3 'Structure model' citation        
# 
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' 
6 3 'Structure model' '_citation.journal_volume'          
7 3 'Structure model' '_citation.page_first'              
8 3 'Structure model' '_citation.page_last'               
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BXM 
_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            33 
_citation.language                  ? 
_citation.page_first                528 
_citation.page_last                 538.e5 
_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 1,2-ETHANEDIOL                             62.068    2   ? ? ? ? 
3 water       nat water                                      18.015    228 ? ? ? ? 
# 
_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 1,2-ETHANEDIOL EDO 
3 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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 
SER 'L-peptide linking' y SERINE          ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -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   ?   ?   ?   A . n 
A 1 28  ILE 28  8   ?   ?   ?   A . n 
A 1 29  TYR 29  9   ?   ?   ?   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   7   ASN ASN 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 
# 
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 EDO 1   301 301 EDO EDO B . 
D 2 EDO 1   302 302 EDO EDO B . 
E 3 HOH 1   301 29  HOH HOH A . 
E 3 HOH 2   302 2   HOH HOH A . 
E 3 HOH 3   303 24  HOH HOH A . 
E 3 HOH 4   304 84  HOH HOH A . 
E 3 HOH 5   305 18  HOH HOH A . 
E 3 HOH 6   306 116 HOH HOH A . 
E 3 HOH 7   307 61  HOH HOH A . 
E 3 HOH 8   308 157 HOH HOH A . 
E 3 HOH 9   309 88  HOH HOH A . 
E 3 HOH 10  310 164 HOH HOH A . 
E 3 HOH 11  311 17  HOH HOH A . 
E 3 HOH 12  312 1   HOH HOH A . 
E 3 HOH 13  313 9   HOH HOH A . 
E 3 HOH 14  314 7   HOH HOH A . 
E 3 HOH 15  315 91  HOH HOH A . 
E 3 HOH 16  316 26  HOH HOH A . 
E 3 HOH 17  317 4   HOH HOH A . 
E 3 HOH 18  318 85  HOH HOH A . 
E 3 HOH 19  319 16  HOH HOH A . 
E 3 HOH 20  320 100 HOH HOH A . 
E 3 HOH 21  321 134 HOH HOH A . 
E 3 HOH 22  322 103 HOH HOH A . 
E 3 HOH 23  323 87  HOH HOH A . 
E 3 HOH 24  324 50  HOH HOH A . 
E 3 HOH 25  325 31  HOH HOH A . 
E 3 HOH 26  326 28  HOH HOH A . 
E 3 HOH 27  327 41  HOH HOH A . 
E 3 HOH 28  328 72  HOH HOH A . 
E 3 HOH 29  329 68  HOH HOH A . 
E 3 HOH 30  330 57  HOH HOH A . 
E 3 HOH 31  331 225 HOH HOH A . 
E 3 HOH 32  332 20  HOH HOH A . 
E 3 HOH 33  333 35  HOH HOH A . 
E 3 HOH 34  334 45  HOH HOH A . 
E 3 HOH 35  335 95  HOH HOH A . 
E 3 HOH 36  336 220 HOH HOH A . 
E 3 HOH 37  337 27  HOH HOH A . 
E 3 HOH 38  338 184 HOH HOH A . 
E 3 HOH 39  339 146 HOH HOH A . 
E 3 HOH 40  340 190 HOH HOH A . 
E 3 HOH 41  341 120 HOH HOH A . 
E 3 HOH 42  342 49  HOH HOH A . 
E 3 HOH 43  343 71  HOH HOH A . 
E 3 HOH 44  344 114 HOH HOH A . 
E 3 HOH 45  345 105 HOH HOH A . 
E 3 HOH 46  346 70  HOH HOH A . 
E 3 HOH 47  347 64  HOH HOH A . 
E 3 HOH 48  348 33  HOH HOH A . 
E 3 HOH 49  349 93  HOH HOH A . 
E 3 HOH 50  350 102 HOH HOH A . 
E 3 HOH 51  351 138 HOH HOH A . 
E 3 HOH 52  352 99  HOH HOH A . 
E 3 HOH 53  353 127 HOH HOH A . 
E 3 HOH 54  354 22  HOH HOH A . 
E 3 HOH 55  355 119 HOH HOH A . 
E 3 HOH 56  356 254 HOH HOH A . 
E 3 HOH 57  357 161 HOH HOH A . 
E 3 HOH 58  358 51  HOH HOH A . 
E 3 HOH 59  359 253 HOH HOH A . 
E 3 HOH 60  360 125 HOH HOH A . 
E 3 HOH 61  361 46  HOH HOH A . 
E 3 HOH 62  362 211 HOH HOH A . 
E 3 HOH 63  363 53  HOH HOH A . 
E 3 HOH 64  364 209 HOH HOH A . 
E 3 HOH 65  365 175 HOH HOH A . 
E 3 HOH 66  366 47  HOH HOH A . 
E 3 HOH 67  367 206 HOH HOH A . 
E 3 HOH 68  368 205 HOH HOH A . 
E 3 HOH 69  369 208 HOH HOH A . 
E 3 HOH 70  370 128 HOH HOH A . 
E 3 HOH 71  371 98  HOH HOH A . 
E 3 HOH 72  372 148 HOH HOH A . 
E 3 HOH 73  373 129 HOH HOH A . 
E 3 HOH 74  374 217 HOH HOH A . 
E 3 HOH 75  375 5   HOH HOH A . 
E 3 HOH 76  376 246 HOH HOH A . 
E 3 HOH 77  377 152 HOH HOH A . 
E 3 HOH 78  378 222 HOH HOH A . 
E 3 HOH 79  379 83  HOH HOH A . 
E 3 HOH 80  380 178 HOH HOH A . 
E 3 HOH 81  381 216 HOH HOH A . 
E 3 HOH 82  382 247 HOH HOH A . 
E 3 HOH 83  383 223 HOH HOH A . 
E 3 HOH 84  384 13  HOH HOH A . 
E 3 HOH 85  385 218 HOH HOH A . 
E 3 HOH 86  386 215 HOH HOH A . 
E 3 HOH 87  387 249 HOH HOH A . 
E 3 HOH 88  388 165 HOH HOH A . 
E 3 HOH 89  389 207 HOH HOH A . 
E 3 HOH 90  390 251 HOH HOH A . 
E 3 HOH 91  391 224 HOH HOH A . 
E 3 HOH 92  392 252 HOH HOH A . 
E 3 HOH 93  393 212 HOH HOH A . 
E 3 HOH 94  394 160 HOH HOH A . 
E 3 HOH 95  395 96  HOH HOH A . 
E 3 HOH 96  396 94  HOH HOH A . 
E 3 HOH 97  397 250 HOH HOH A . 
E 3 HOH 98  398 54  HOH HOH A . 
E 3 HOH 99  399 221 HOH HOH A . 
E 3 HOH 100 400 141 HOH HOH A . 
E 3 HOH 101 401 219 HOH HOH A . 
E 3 HOH 102 402 159 HOH HOH A . 
E 3 HOH 103 403 143 HOH HOH A . 
E 3 HOH 104 404 115 HOH HOH A . 
E 3 HOH 105 405 214 HOH HOH A . 
E 3 HOH 106 406 177 HOH HOH A . 
F 3 HOH 1   401 32  HOH HOH B . 
F 3 HOH 2   402 52  HOH HOH B . 
F 3 HOH 3   403 42  HOH HOH B . 
F 3 HOH 4   404 19  HOH HOH B . 
F 3 HOH 5   405 233 HOH HOH B . 
F 3 HOH 6   406 58  HOH HOH B . 
F 3 HOH 7   407 59  HOH HOH B . 
F 3 HOH 8   408 14  HOH HOH B . 
F 3 HOH 9   409 112 HOH HOH B . 
F 3 HOH 10  410 80  HOH HOH B . 
F 3 HOH 11  411 25  HOH HOH B . 
F 3 HOH 12  412 30  HOH HOH B . 
F 3 HOH 13  413 69  HOH HOH B . 
F 3 HOH 14  414 12  HOH HOH B . 
F 3 HOH 15  415 90  HOH HOH B . 
F 3 HOH 16  416 118 HOH HOH B . 
F 3 HOH 17  417 56  HOH HOH B . 
F 3 HOH 18  418 55  HOH HOH B . 
F 3 HOH 19  419 65  HOH HOH B . 
F 3 HOH 20  420 21  HOH HOH B . 
F 3 HOH 21  421 15  HOH HOH B . 
F 3 HOH 22  422 11  HOH HOH B . 
F 3 HOH 23  423 62  HOH HOH B . 
F 3 HOH 24  424 67  HOH HOH B . 
F 3 HOH 25  425 188 HOH HOH B . 
F 3 HOH 26  426 37  HOH HOH B . 
F 3 HOH 27  427 202 HOH HOH B . 
F 3 HOH 28  428 236 HOH HOH B . 
F 3 HOH 29  429 204 HOH HOH B . 
F 3 HOH 30  430 48  HOH HOH B . 
F 3 HOH 31  431 231 HOH HOH B . 
F 3 HOH 32  432 153 HOH HOH B . 
F 3 HOH 33  433 36  HOH HOH B . 
F 3 HOH 34  434 38  HOH HOH B . 
F 3 HOH 35  435 3   HOH HOH B . 
F 3 HOH 36  436 243 HOH HOH B . 
F 3 HOH 37  437 111 HOH HOH B . 
F 3 HOH 38  438 135 HOH HOH B . 
F 3 HOH 39  439 101 HOH HOH B . 
F 3 HOH 40  440 155 HOH HOH B . 
F 3 HOH 41  441 182 HOH HOH B . 
F 3 HOH 42  442 86  HOH HOH B . 
F 3 HOH 43  443 40  HOH HOH B . 
F 3 HOH 44  444 147 HOH HOH B . 
F 3 HOH 45  445 156 HOH HOH B . 
F 3 HOH 46  446 145 HOH HOH B . 
F 3 HOH 47  447 104 HOH HOH B . 
F 3 HOH 48  448 123 HOH HOH B . 
F 3 HOH 49  449 97  HOH HOH B . 
F 3 HOH 50  450 137 HOH HOH B . 
F 3 HOH 51  451 74  HOH HOH B . 
F 3 HOH 52  452 185 HOH HOH B . 
F 3 HOH 53  453 75  HOH HOH B . 
F 3 HOH 54  454 154 HOH HOH B . 
F 3 HOH 55  455 23  HOH HOH B . 
F 3 HOH 56  456 44  HOH HOH B . 
F 3 HOH 57  457 180 HOH HOH B . 
F 3 HOH 58  458 34  HOH HOH B . 
F 3 HOH 59  459 10  HOH HOH B . 
F 3 HOH 60  460 79  HOH HOH B . 
F 3 HOH 61  461 117 HOH HOH B . 
F 3 HOH 62  462 82  HOH HOH B . 
F 3 HOH 63  463 106 HOH HOH B . 
F 3 HOH 64  464 169 HOH HOH B . 
F 3 HOH 65  465 174 HOH HOH B . 
F 3 HOH 66  466 149 HOH HOH B . 
F 3 HOH 67  467 39  HOH HOH B . 
F 3 HOH 68  468 122 HOH HOH B . 
F 3 HOH 69  469 150 HOH HOH B . 
F 3 HOH 70  470 142 HOH HOH B . 
F 3 HOH 71  471 76  HOH HOH B . 
F 3 HOH 72  472 227 HOH HOH B . 
F 3 HOH 73  473 60  HOH HOH B . 
F 3 HOH 74  474 151 HOH HOH B . 
F 3 HOH 75  475 139 HOH HOH B . 
F 3 HOH 76  476 173 HOH HOH B . 
F 3 HOH 77  477 196 HOH HOH B . 
F 3 HOH 78  478 167 HOH HOH B . 
F 3 HOH 79  479 130 HOH HOH B . 
F 3 HOH 80  480 63  HOH HOH B . 
F 3 HOH 81  481 108 HOH HOH B . 
F 3 HOH 82  482 186 HOH HOH B . 
F 3 HOH 83  483 124 HOH HOH B . 
F 3 HOH 84  484 229 HOH HOH B . 
F 3 HOH 85  485 81  HOH HOH B . 
F 3 HOH 86  486 66  HOH HOH B . 
F 3 HOH 87  487 89  HOH HOH B . 
F 3 HOH 88  488 107 HOH HOH B . 
F 3 HOH 89  489 92  HOH HOH B . 
F 3 HOH 90  490 255 HOH HOH B . 
F 3 HOH 91  491 132 HOH HOH B . 
F 3 HOH 92  492 109 HOH HOH B . 
F 3 HOH 93  493 113 HOH HOH B . 
F 3 HOH 94  494 234 HOH HOH B . 
F 3 HOH 95  495 73  HOH HOH B . 
F 3 HOH 96  496 199 HOH HOH B . 
F 3 HOH 97  497 191 HOH HOH B . 
F 3 HOH 98  498 230 HOH HOH B . 
F 3 HOH 99  499 203 HOH HOH B . 
F 3 HOH 100 500 163 HOH HOH B . 
F 3 HOH 101 501 244 HOH HOH B . 
F 3 HOH 102 502 258 HOH HOH B . 
F 3 HOH 103 503 193 HOH HOH B . 
F 3 HOH 104 504 239 HOH HOH B . 
F 3 HOH 105 505 171 HOH HOH B . 
F 3 HOH 106 506 200 HOH HOH B . 
F 3 HOH 107 507 197 HOH HOH B . 
F 3 HOH 108 508 192 HOH HOH B . 
F 3 HOH 109 509 235 HOH HOH B . 
F 3 HOH 110 510 210 HOH HOH B . 
F 3 HOH 111 511 195 HOH HOH B . 
F 3 HOH 112 512 241 HOH HOH B . 
F 3 HOH 113 513 162 HOH HOH B . 
F 3 HOH 114 514 183 HOH HOH B . 
F 3 HOH 115 515 198 HOH HOH B . 
F 3 HOH 116 516 240 HOH HOH B . 
F 3 HOH 117 517 194 HOH HOH B . 
F 3 HOH 118 518 232 HOH HOH B . 
F 3 HOH 119 519 256 HOH HOH B . 
F 3 HOH 120 520 201 HOH HOH B . 
F 3 HOH 121 521 238 HOH HOH B . 
F 3 HOH 122 522 226 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 GLU 10  ? CB  ? A GLU 30  CB  
2   1 Y 1 A GLU 10  ? CG  ? A GLU 30  CG  
3   1 Y 1 A GLU 10  ? CD  ? A GLU 30  CD  
4   1 Y 1 A GLU 10  ? OE1 ? A GLU 30  OE1 
5   1 Y 1 A GLU 10  ? OE2 ? A GLU 30  OE2 
6   1 Y 1 A THR 11  ? CB  ? A THR 31  CB  
7   1 Y 1 A THR 11  ? OG1 ? A THR 31  OG1 
8   1 Y 1 A THR 11  ? CG2 ? A THR 31  CG2 
9   1 Y 1 A ASP 12  ? CG  ? A ASP 32  CG  
10  1 Y 1 A ASP 12  ? OD1 ? A ASP 32  OD1 
11  1 Y 1 A ASP 12  ? OD2 ? A ASP 32  OD2 
12  1 Y 1 A GLU 13  ? CG  ? A GLU 33  CG  
13  1 Y 1 A GLU 13  ? CD  ? A GLU 33  CD  
14  1 Y 1 A GLU 13  ? OE1 ? A GLU 33  OE1 
15  1 Y 1 A GLU 13  ? OE2 ? A GLU 33  OE2 
16  1 Y 1 A SER 14  ? OG  ? A SER 34  OG  
17  1 Y 1 A GLU 25  ? CB  ? A GLU 45  CB  
18  1 Y 1 A GLU 25  ? CG  ? A GLU 45  CG  
19  1 Y 1 A GLU 25  ? CD  ? A GLU 45  CD  
20  1 Y 1 A GLU 25  ? OE1 ? A GLU 45  OE1 
21  1 Y 1 A GLU 25  ? OE2 ? A GLU 45  OE2 
22  1 Y 1 A ASP 26  ? OD2 ? A ASP 46  OD2 
23  1 Y 1 A LYS 46  ? CG  ? A LYS 66  CG  
24  1 Y 1 A LYS 46  ? CD  ? A LYS 66  CD  
25  1 Y 1 A LYS 46  ? CE  ? A LYS 66  CE  
26  1 Y 1 A LYS 46  ? NZ  ? A LYS 66  NZ  
27  1 Y 1 A GLU 47  ? CG  ? A GLU 67  CG  
28  1 Y 1 A GLU 47  ? CD  ? A GLU 67  CD  
29  1 Y 1 A GLU 47  ? OE1 ? A GLU 67  OE1 
30  1 Y 1 A GLU 47  ? OE2 ? A GLU 67  OE2 
31  1 Y 1 A LYS 50  ? CE  ? A LYS 70  CE  
32  1 Y 1 A LYS 50  ? NZ  ? A LYS 70  NZ  
33  1 Y 1 A LYS 72  ? CE  ? A LYS 92  CE  
34  1 Y 1 A LYS 72  ? NZ  ? A LYS 92  NZ  
35  1 Y 1 A GLU 89  ? OE1 ? A GLU 109 OE1 
36  1 Y 1 A GLU 89  ? OE2 ? A GLU 109 OE2 
37  1 Y 1 A LYS 92  ? CG  ? A LYS 112 CG  
38  1 Y 1 A LYS 92  ? CD  ? A LYS 112 CD  
39  1 Y 1 A LYS 92  ? CE  ? A LYS 112 CE  
40  1 Y 1 A LYS 92  ? NZ  ? A LYS 112 NZ  
41  1 Y 1 A ILE 96  ? CD1 ? A ILE 116 CD1 
42  1 Y 1 A LYS 107 ? NZ  ? A LYS 127 NZ  
43  1 Y 1 A ASN 108 ? ND2 ? A ASN 128 ND2 
44  1 Y 1 A LYS 110 ? NZ  ? A LYS 130 NZ  
45  1 Y 1 A GLN 139 ? OE1 ? A GLN 159 OE1 
46  1 Y 1 A GLN 139 ? NE2 ? A GLN 159 NE2 
47  1 Y 1 A LYS 167 ? CE  ? A LYS 187 CE  
48  1 Y 1 A LYS 167 ? NZ  ? A LYS 187 NZ  
49  1 Y 1 A GLU 171 ? CG  ? A GLU 191 CG  
50  1 Y 1 A GLU 171 ? CD  ? A GLU 191 CD  
51  1 Y 1 A GLU 171 ? OE1 ? A GLU 191 OE1 
52  1 Y 1 A GLU 171 ? OE2 ? A GLU 191 OE2 
53  1 Y 1 A LYS 172 ? CG  ? A LYS 192 CG  
54  1 Y 1 A LYS 172 ? CD  ? A LYS 192 CD  
55  1 Y 1 A LYS 172 ? CE  ? A LYS 192 CE  
56  1 Y 1 A LYS 172 ? NZ  ? A LYS 192 NZ  
57  1 Y 1 A ARG 184 ? CZ  ? A ARG 204 CZ  
58  1 Y 1 A ARG 184 ? NH1 ? A ARG 204 NH1 
59  1 Y 1 A ARG 184 ? NH2 ? A ARG 204 NH2 
60  1 Y 1 A GLU 186 ? CD  ? A GLU 206 CD  
61  1 Y 1 A GLU 186 ? OE1 ? A GLU 206 OE1 
62  1 Y 1 A GLU 186 ? OE2 ? A GLU 206 OE2 
63  1 Y 1 A LYS 190 ? NZ  ? A LYS 210 NZ  
64  1 Y 1 A LYS 191 ? NZ  ? A LYS 211 NZ  
65  1 Y 1 A GLU 200 ? CG  ? A GLU 220 CG  
66  1 Y 1 A GLU 200 ? CD  ? A GLU 220 CD  
67  1 Y 1 A GLU 200 ? OE1 ? A GLU 220 OE1 
68  1 Y 1 A GLU 200 ? OE2 ? A GLU 220 OE2 
69  1 Y 1 A ASN 201 ? CG  ? A ASN 221 CG  
70  1 Y 1 A ASN 201 ? OD1 ? A ASN 221 OD1 
71  1 Y 1 A ASN 201 ? ND2 ? A ASN 221 ND2 
72  1 Y 1 A LYS 203 ? NZ  ? A LYS 223 NZ  
73  1 Y 1 A GLU 209 ? CG  ? A GLU 229 CG  
74  1 Y 1 A GLU 209 ? CD  ? A GLU 229 CD  
75  1 Y 1 A GLU 209 ? OE1 ? A GLU 229 OE1 
76  1 Y 1 A GLU 209 ? OE2 ? A GLU 229 OE2 
77  1 Y 1 A LYS 212 ? NZ  ? A LYS 232 NZ  
78  1 Y 1 A GLU 213 ? CG  ? A GLU 233 CG  
79  1 Y 1 A GLU 213 ? CD  ? A GLU 233 CD  
80  1 Y 1 A GLU 213 ? OE1 ? A GLU 233 OE1 
81  1 Y 1 A GLU 213 ? OE2 ? A GLU 233 OE2 
82  1 Y 1 A ILE 217 ? CD1 ? A ILE 237 CD1 
83  1 Y 1 A GLU 220 ? CG  ? A GLU 240 CG  
84  1 Y 1 A GLU 220 ? CD  ? A GLU 240 CD  
85  1 Y 1 A GLU 220 ? OE1 ? A GLU 240 OE1 
86  1 Y 1 A GLU 220 ? OE2 ? A GLU 240 OE2 
87  1 Y 1 A VAL 222 ? CG1 ? A VAL 242 CG1 
88  1 Y 1 A VAL 222 ? CG2 ? A VAL 242 CG2 
89  1 Y 1 A ILE 231 ? CD1 ? A ILE 251 CD1 
90  1 Y 1 A GLU 233 ? OE1 ? A GLU 253 OE1 
91  1 Y 1 A LYS 237 ? CE  ? A LYS 257 CE  
92  1 Y 1 A LYS 237 ? NZ  ? A LYS 257 NZ  
93  1 Y 1 A LYS 249 ? NZ  ? A LYS 269 NZ  
94  1 Y 1 A ILE 251 ? CG1 ? A ILE 271 CG1 
95  1 Y 1 A ILE 251 ? CG2 ? A ILE 271 CG2 
96  1 Y 1 A ILE 251 ? CD1 ? A ILE 271 CD1 
97  1 Y 1 B ASN 7   ? CG  ? B ASN 27  CG  
98  1 Y 1 B ASN 7   ? OD1 ? B ASN 27  OD1 
99  1 Y 1 B ASN 7   ? ND2 ? B ASN 27  ND2 
100 1 Y 1 B ILE 8   ? CG1 ? B ILE 28  CG1 
101 1 Y 1 B ILE 8   ? CG2 ? B ILE 28  CG2 
102 1 Y 1 B ILE 8   ? CD1 ? B ILE 28  CD1 
103 1 Y 1 B GLU 10  ? CD  ? B GLU 30  CD  
104 1 Y 1 B GLU 10  ? OE1 ? B GLU 30  OE1 
105 1 Y 1 B GLU 10  ? OE2 ? B GLU 30  OE2 
106 1 Y 1 B GLU 13  ? CG  ? B GLU 33  CG  
107 1 Y 1 B GLU 13  ? CD  ? B GLU 33  CD  
108 1 Y 1 B GLU 13  ? OE1 ? B GLU 33  OE1 
109 1 Y 1 B GLU 13  ? OE2 ? B GLU 33  OE2 
110 1 Y 1 B GLU 25  ? CD  ? B GLU 45  CD  
111 1 Y 1 B GLU 25  ? OE1 ? B GLU 45  OE1 
112 1 Y 1 B GLU 25  ? OE2 ? B GLU 45  OE2 
113 1 Y 1 B LYS 46  ? CE  ? B LYS 66  CE  
114 1 Y 1 B LYS 46  ? NZ  ? B LYS 66  NZ  
115 1 Y 1 B GLU 47  ? CG  ? B GLU 67  CG  
116 1 Y 1 B GLU 47  ? CD  ? B GLU 67  CD  
117 1 Y 1 B GLU 47  ? OE1 ? B GLU 67  OE1 
118 1 Y 1 B GLU 47  ? OE2 ? B GLU 67  OE2 
119 1 Y 1 B LYS 50  ? NZ  ? B LYS 70  NZ  
120 1 Y 1 B SER 70  ? OG  ? B SER 90  OG  
121 1 Y 1 B LYS 72  ? CD  ? B LYS 92  CD  
122 1 Y 1 B LYS 72  ? CE  ? B LYS 92  CE  
123 1 Y 1 B LYS 72  ? NZ  ? B LYS 92  NZ  
124 1 Y 1 B SER 80  ? OG  ? B SER 100 OG  
125 1 Y 1 B LYS 92  ? CG  ? B LYS 112 CG  
126 1 Y 1 B LYS 92  ? CD  ? B LYS 112 CD  
127 1 Y 1 B LYS 92  ? CE  ? B LYS 112 CE  
128 1 Y 1 B LYS 92  ? NZ  ? B LYS 112 NZ  
129 1 Y 1 B ASN 93  ? ND2 ? B ASN 113 ND2 
130 1 Y 1 B SER 99  ? OG  ? B SER 119 OG  
131 1 Y 1 B LYS 107 ? CE  ? B LYS 127 CE  
132 1 Y 1 B LYS 107 ? NZ  ? B LYS 127 NZ  
133 1 Y 1 B LYS 110 ? NZ  ? B LYS 130 NZ  
134 1 Y 1 B ARG 120 ? NH1 ? B ARG 140 NH1 
135 1 Y 1 B ARG 120 ? NH2 ? B ARG 140 NH2 
136 1 Y 1 B SER 122 ? OG  ? B SER 142 OG  
137 1 Y 1 B GLN 139 ? CG  ? B GLN 159 CG  
138 1 Y 1 B GLN 139 ? CD  ? B GLN 159 CD  
139 1 Y 1 B GLN 139 ? OE1 ? B GLN 159 OE1 
140 1 Y 1 B GLN 139 ? NE2 ? B GLN 159 NE2 
141 1 Y 1 B LYS 141 ? NZ  ? B LYS 161 NZ  
142 1 Y 1 B ARG 154 ? CD  ? B ARG 174 CD  
143 1 Y 1 B ARG 154 ? NE  ? B ARG 174 NE  
144 1 Y 1 B ARG 154 ? CZ  ? B ARG 174 CZ  
145 1 Y 1 B ARG 154 ? NH1 ? B ARG 174 NH1 
146 1 Y 1 B ARG 154 ? NH2 ? B ARG 174 NH2 
147 1 Y 1 B GLU 171 ? CG  ? B GLU 191 CG  
148 1 Y 1 B GLU 171 ? CD  ? B GLU 191 CD  
149 1 Y 1 B GLU 171 ? OE1 ? B GLU 191 OE1 
150 1 Y 1 B GLU 171 ? OE2 ? B GLU 191 OE2 
151 1 Y 1 B LYS 172 ? CG  ? B LYS 192 CG  
152 1 Y 1 B LYS 172 ? CD  ? B LYS 192 CD  
153 1 Y 1 B LYS 172 ? CE  ? B LYS 192 CE  
154 1 Y 1 B LYS 172 ? NZ  ? B LYS 192 NZ  
155 1 Y 1 B ARG 184 ? NE  ? B ARG 204 NE  
156 1 Y 1 B ARG 184 ? CZ  ? B ARG 204 CZ  
157 1 Y 1 B ARG 184 ? NH1 ? B ARG 204 NH1 
158 1 Y 1 B ARG 184 ? NH2 ? B ARG 204 NH2 
159 1 Y 1 B GLU 185 ? OE2 ? B GLU 205 OE2 
160 1 Y 1 B GLU 186 ? CG  ? B GLU 206 CG  
161 1 Y 1 B GLU 186 ? CD  ? B GLU 206 CD  
162 1 Y 1 B GLU 186 ? OE1 ? B GLU 206 OE1 
163 1 Y 1 B GLU 186 ? OE2 ? B GLU 206 OE2 
164 1 Y 1 B LYS 190 ? NZ  ? B LYS 210 NZ  
165 1 Y 1 B GLU 200 ? CG  ? B GLU 220 CG  
166 1 Y 1 B GLU 200 ? CD  ? B GLU 220 CD  
167 1 Y 1 B GLU 200 ? OE1 ? B GLU 220 OE1 
168 1 Y 1 B GLU 200 ? OE2 ? B GLU 220 OE2 
169 1 Y 1 B GLU 209 ? CG  ? B GLU 229 CG  
170 1 Y 1 B GLU 209 ? CD  ? B GLU 229 CD  
171 1 Y 1 B GLU 209 ? OE1 ? B GLU 229 OE1 
172 1 Y 1 B GLU 209 ? OE2 ? B GLU 229 OE2 
173 1 Y 1 B GLU 213 ? CG  ? B GLU 233 CG  
174 1 Y 1 B GLU 213 ? CD  ? B GLU 233 CD  
175 1 Y 1 B GLU 213 ? OE1 ? B GLU 233 OE1 
176 1 Y 1 B GLU 213 ? OE2 ? B GLU 233 OE2 
177 1 Y 1 B GLU 220 ? CG  ? B GLU 240 CG  
178 1 Y 1 B GLU 220 ? CD  ? B GLU 240 CD  
179 1 Y 1 B GLU 220 ? OE1 ? B GLU 240 OE1 
180 1 Y 1 B GLU 220 ? OE2 ? B GLU 240 OE2 
181 1 Y 1 B GLU 233 ? CG  ? B GLU 253 CG  
182 1 Y 1 B GLU 233 ? CD  ? B GLU 253 CD  
183 1 Y 1 B GLU 233 ? OE1 ? B GLU 253 OE1 
184 1 Y 1 B GLU 233 ? OE2 ? B GLU 253 OE2 
185 1 Y 1 B LYS 237 ? NZ  ? B LYS 257 NZ  
186 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                     9BXM 
_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                         9BXM 
_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                   9BXM 
_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             2.48 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.5 
_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 citrate pH 5, 24% 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 EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-14 
_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   1.0 
_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 8.2.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          37.71 
_reflns.entry_id                                       9BXM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.27 
_reflns.d_resolution_low                               39.62 
_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                                     28478 
_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                           96.68 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.63 
_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                                0.04593 
_reflns.pdbx_Rpim_I_all                                0.03248 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.03248 
_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                                    2.27 
_reflns_shell.d_res_low                                     2.351 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.93 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2306 
_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                               1.7 
_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                               0.4406 
_reflns_shell.pdbx_Rpim_I_all                               0.3115 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.764 
_reflns_shell.pdbx_CC_star                                  0.931 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          79.83 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.3115 
_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                               37.32 
_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                                 9BXM 
_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                            2.27 
_refine.ls_d_res_low                             39.62 
_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                     28475 
_refine.ls_number_reflns_R_free                  1430 
_refine.ls_number_reflns_R_work                  27145 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.45 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1893 
_refine.ls_R_factor_R_free                       0.2358 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1869 
_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          SIR 
_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                 23.3296 
_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                            0.2342 
_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                       2.27 
_refine_hist.d_res_low                        39.62 
_refine_hist.number_atoms_solvent             228 
_refine_hist.number_atoms_total               3998 
_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        3762 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         8 
_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' ? 0.0043  ? 3855 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6783  ? 5223 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0469  ? 573  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0066  ? 669  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.8237 ? 1334 ? 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' 2.27 2.35  . . 116 2140 77.63  . . . . 0.2290 . . . . . . . . . . . 0.2811 
'X-RAY DIFFRACTION' 2.35 2.44  . . 132 2493 90.24  . . . . 0.2395 . . . . . . . . . . . 0.2901 
'X-RAY DIFFRACTION' 2.44 2.55  . . 141 2697 97.09  . . . . 0.2213 . . . . . . . . . . . 0.3305 
'X-RAY DIFFRACTION' 2.55 2.69  . . 143 2781 99.76  . . . . 0.2051 . . . . . . . . . . . 0.2451 
'X-RAY DIFFRACTION' 2.69 2.85  . . 144 2774 99.97  . . . . 0.2009 . . . . . . . . . . . 0.2407 
'X-RAY DIFFRACTION' 2.85 3.07  . . 157 2800 100.00 . . . . 0.2197 . . . . . . . . . . . 0.2648 
'X-RAY DIFFRACTION' 3.07 3.38  . . 139 2800 99.97  . . . . 0.2044 . . . . . . . . . . . 0.2784 
'X-RAY DIFFRACTION' 3.38 3.87  . . 148 2834 99.50  . . . . 0.1793 . . . . . . . . . . . 0.2332 
'X-RAY DIFFRACTION' 3.87 4.88  . . 152 2836 99.83  . . . . 0.1408 . . . . . . . . . . . 0.1845 
'X-RAY DIFFRACTION' 4.88 39.62 . . 158 2990 99.87  . . . . 0.1843 . . . . . . . . . . . 0.2114 
# 
_struct.entry_id                     9BXM 
_struct.title                        
'OvoM from Sulfuricurvum sp. isolate STB_99, a SAM-dependent N-methyltransferase involved in ovothiol biosynthesis' 
_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        9BXM 
_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 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9BXM 
_struct_ref.pdbx_db_accession          9BXM 
_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 9BXM A 1 ? 273 ? 9BXM -19 ? 253 ? -19 253 
2 1 9BXM B 1 ? 273 ? 9BXM -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)' 3000  ? 
1 MORE         -3    ? 
1 'SSA (A^2)'  20210 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 B,C,D,F 
1 2 A,E     
# 
_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 GLU A 30  ? GLY A 44  ? GLU A 10  GLY A 24  1 ? 15 
HELX_P HELX_P2  AA2 ASN A 52  ? THR A 65  ? ASN A 32  THR A 45  1 ? 14 
HELX_P HELX_P3  AA3 GLY A 81  ? ALA A 88  ? GLY A 61  ALA A 68  1 ? 8  
HELX_P HELX_P4  AA4 SER A 100 ? GLY A 114 ? SER A 80  GLY A 94  1 ? 15 
HELX_P HELX_P5  AA5 GLU A 135 ? THR A 144 ? GLU A 115 THR A 124 5 ? 10 
HELX_P HELX_P6  AA6 LEU A 171 ? LEU A 175 ? LEU A 151 LEU A 155 5 ? 5  
HELX_P HELX_P7  AA7 GLU A 177 ? GLU A 183 ? GLU A 157 GLU A 163 1 ? 7  
HELX_P HELX_P8  AA8 ASN A 184 ? LYS A 187 ? ASN A 164 LYS A 167 5 ? 4  
HELX_P HELX_P9  AA9 ALA A 209 ? TRP A 213 ? ALA A 189 TRP A 193 5 ? 5  
HELX_P HELX_P10 AB1 SER A 226 ? GLU A 236 ? SER A 206 GLU A 216 1 ? 11 
HELX_P HELX_P11 AB2 ASP B 32  ? GLY B 44  ? ASP B 12  GLY B 24  1 ? 13 
HELX_P HELX_P12 AB3 ASN B 52  ? THR B 65  ? ASN B 32  THR B 45  1 ? 14 
HELX_P HELX_P13 AB4 GLY B 81  ? ALA B 88  ? GLY B 61  ALA B 68  1 ? 8  
HELX_P HELX_P14 AB5 SER B 100 ? GLY B 114 ? SER B 80  GLY B 94  1 ? 15 
HELX_P HELX_P15 AB6 GLU B 135 ? THR B 144 ? GLU B 115 THR B 124 5 ? 10 
HELX_P HELX_P16 AB7 ASP B 152 ? LEU B 156 ? ASP B 132 LEU B 136 5 ? 5  
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 ? 3 ? 
AA5 ? 7 ? 
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 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? anti-parallel 
AA5 6 7 ? 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 TYR B 29  ? GLU B 30  ? TYR B 9   GLU B 10  
AA4 2 CYS B 115 ? ASN B 121 ? CYS B 95  ASN B 101 
AA4 3 LYS B 127 ? ASP B 133 ? LYS B 107 ASP B 113 
AA5 1 VAL B 146 ? GLN B 150 ? VAL B 126 GLN B 130 
AA5 2 HIS B 93  ? ASP B 98  ? HIS B 73  ASP B 78  
AA5 3 ARG B 72  ? LEU B 76  ? ARG B 52  LEU B 56  
AA5 4 TYR B 163 ? THR B 169 ? TYR B 143 THR B 149 
AA5 5 ILE B 189 ? SER B 199 ? ILE B 169 SER B 179 
AA5 6 PHE B 258 ? VAL B 270 ? PHE B 238 VAL B 250 
AA5 7 PHE B 239 ? ARG B 252 ? PHE B 219 ARG B 232 
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 197 ? N LEU A 177 O SER A 266 ? O SER A 246 
AA1 6 7 O MET A 265 ? O MET A 245 N GLU A 245 ? N GLU A 225 
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 N TYR B 29  ? N TYR B 9   O GLY B 117 ? O GLY B 97  
AA4 2 3 N GLN B 120 ? N GLN B 100 O ASN B 128 ? O ASN B 108 
AA5 1 2 O PHE B 149 ? O PHE B 129 N GLY B 96  ? N GLY B 76  
AA5 2 3 O ASP B 95  ? O ASP B 75  N ASP B 75  ? N ASP B 55  
AA5 3 4 N LEU B 76  ? N LEU B 56  O MET B 167 ? O MET B 147 
AA5 4 5 N TYR B 163 ? N TYR B 143 O ASN B 190 ? O ASN B 170 
AA5 5 6 N LEU B 195 ? N LEU B 175 O TRP B 268 ? O TRP B 248 
AA5 6 7 O MET B 265 ? O MET B 245 N GLU B 245 ? N GLU B 225 
AA6 1 2 N TYR B 217 ? N TYR B 197 O VAL B 225 ? O VAL B 205 
# 
_pdbx_entry_details.entry_id                   9BXM 
_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     N 
_pdbx_entry_details.has_protein_modification   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  ? ? 52.01   -116.78 
2 1 ASN A 135 ? ? -158.75 70.17   
3 1 LYS B 50  ? ? -97.17  56.59   
4 1 ALA B 59  ? ? 52.02   -120.98 
5 1 ASN B 135 ? ? -157.54 66.65   
# 
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 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       522 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.82 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -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 ASN 7   ? A ASN 27  
28 1 Y 1 A ILE 8   ? A ILE 28  
29 1 Y 1 A TYR 9   ? A TYR 29  
30 1 Y 1 A SER 252 ? A SER 272 
31 1 Y 1 A THR 253 ? A THR 273 
32 1 Y 1 B MET -19 ? B MET 1   
33 1 Y 1 B GLY -18 ? B GLY 2   
34 1 Y 1 B SER -17 ? B SER 3   
35 1 Y 1 B SER -16 ? B SER 4   
36 1 Y 1 B HIS -15 ? B HIS 5   
37 1 Y 1 B HIS -14 ? B HIS 6   
38 1 Y 1 B HIS -13 ? B HIS 7   
39 1 Y 1 B HIS -12 ? B HIS 8   
40 1 Y 1 B HIS -11 ? B HIS 9   
41 1 Y 1 B HIS -10 ? B HIS 10  
42 1 Y 1 B SER -9  ? B SER 11  
43 1 Y 1 B SER -8  ? B SER 12  
44 1 Y 1 B GLY -7  ? B GLY 13  
45 1 Y 1 B LEU -6  ? B LEU 14  
46 1 Y 1 B VAL -5  ? B VAL 15  
47 1 Y 1 B PRO -4  ? B PRO 16  
48 1 Y 1 B ARG -3  ? B ARG 17  
49 1 Y 1 B GLY -2  ? B GLY 18  
50 1 Y 1 B SER -1  ? B SER 19  
51 1 Y 1 B HIS 0   ? B HIS 20  
52 1 Y 1 B MET 1   ? B MET 21  
53 1 Y 1 B ILE 2   ? B ILE 22  
54 1 Y 1 B PHE 3   ? B PHE 23  
55 1 Y 1 B LYS 4   ? B LYS 24  
56 1 Y 1 B GLU 5   ? B GLU 25  
57 1 Y 1 B LYS 6   ? B LYS 26  
58 1 Y 1 B SER 252 ? B SER 272 
59 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 
SER N    N N N 300 
SER CA   C N S 301 
SER C    C N N 302 
SER O    O N N 303 
SER CB   C N N 304 
SER OG   O N N 305 
SER OXT  O N N 306 
SER H    H N N 307 
SER H2   H N N 308 
SER HA   H N N 309 
SER HB2  H N N 310 
SER HB3  H N N 311 
SER HG   H N N 312 
SER HXT  H N N 313 
THR N    N N N 314 
THR CA   C N S 315 
THR C    C N N 316 
THR O    O N N 317 
THR CB   C N R 318 
THR OG1  O N N 319 
THR CG2  C N N 320 
THR OXT  O N N 321 
THR H    H N N 322 
THR H2   H N N 323 
THR HA   H N N 324 
THR HB   H N N 325 
THR HG1  H N N 326 
THR HG21 H N N 327 
THR HG22 H N N 328 
THR HG23 H N N 329 
THR HXT  H N N 330 
TRP N    N N N 331 
TRP CA   C N S 332 
TRP C    C N N 333 
TRP O    O N N 334 
TRP CB   C N N 335 
TRP CG   C Y N 336 
TRP CD1  C Y N 337 
TRP CD2  C Y N 338 
TRP NE1  N Y N 339 
TRP CE2  C Y N 340 
TRP CE3  C Y N 341 
TRP CZ2  C Y N 342 
TRP CZ3  C Y N 343 
TRP CH2  C Y N 344 
TRP OXT  O N N 345 
TRP H    H N N 346 
TRP H2   H N N 347 
TRP HA   H N N 348 
TRP HB2  H N N 349 
TRP HB3  H N N 350 
TRP HD1  H N N 351 
TRP HE1  H N N 352 
TRP HE3  H N N 353 
TRP HZ2  H N N 354 
TRP HZ3  H N N 355 
TRP HH2  H N N 356 
TRP HXT  H N N 357 
TYR N    N N N 358 
TYR CA   C N S 359 
TYR C    C N N 360 
TYR O    O N N 361 
TYR CB   C N N 362 
TYR CG   C Y N 363 
TYR CD1  C Y N 364 
TYR CD2  C Y N 365 
TYR CE1  C Y N 366 
TYR CE2  C Y N 367 
TYR CZ   C Y N 368 
TYR OH   O N N 369 
TYR OXT  O N N 370 
TYR H    H N N 371 
TYR H2   H N N 372 
TYR HA   H N N 373 
TYR HB2  H N N 374 
TYR HB3  H N N 375 
TYR HD1  H N N 376 
TYR HD2  H N N 377 
TYR HE1  H N N 378 
TYR HE2  H N N 379 
TYR HH   H N N 380 
TYR HXT  H N N 381 
VAL N    N N N 382 
VAL CA   C N S 383 
VAL C    C N N 384 
VAL O    O N N 385 
VAL CB   C N N 386 
VAL CG1  C N N 387 
VAL CG2  C N N 388 
VAL OXT  O N N 389 
VAL H    H N N 390 
VAL H2   H N N 391 
VAL HA   H N N 392 
VAL HB   H N N 393 
VAL HG11 H N N 394 
VAL HG12 H N N 395 
VAL HG13 H N N 396 
VAL HG21 H N N 397 
VAL HG22 H N N 398 
VAL HG23 H N N 399 
VAL HXT  H N N 400 
# 
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 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
# 
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 
# 
_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                    9BXM 
_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   . GLU A 1 30  ? -23.93400 -14.16100 13.17800 1.000 57.20318 ?  10  GLU A N   1 
ATOM   2    C CA  . GLU A 1 30  ? -23.34300 -12.92400 13.67800 1.000 61.57737 ?  10  GLU A CA  1 
ATOM   3    C C   . GLU A 1 30  ? -22.58900 -13.19600 14.97400 1.000 65.01610 ?  10  GLU A C   1 
ATOM   4    O O   . GLU A 1 30  ? -21.35900 -13.29900 14.97800 1.000 63.90711 ?  10  GLU A O   1 
ATOM   5    N N   . THR A 1 31  ? -23.33500 -13.30700 16.07600 1.000 54.65439 ?  11  THR A N   1 
ATOM   6    C CA  . THR A 1 31  ? -22.72100 -13.69800 17.33800 1.000 56.27687 ?  11  THR A CA  1 
ATOM   7    C C   . THR A 1 31  ? -22.08200 -15.07600 17.22900 1.000 50.97484 ?  11  THR A C   1 
ATOM   8    O O   . THR A 1 31  ? -21.01000 -15.31800 17.79600 1.000 52.79914 ?  11  THR A O   1 
ATOM   9    N N   . ASP A 1 32  ? -22.71800 -15.98800 16.48600 1.000 53.57108 ?  12  ASP A N   1 
ATOM   10   C CA  . ASP A 1 32  ? -22.17700 -17.33500 16.34300 1.000 42.15204 ?  12  ASP A CA  1 
ATOM   11   C C   . ASP A 1 32  ? -20.85100 -17.32100 15.59700 1.000 47.15575 ?  12  ASP A C   1 
ATOM   12   O O   . ASP A 1 32  ? -19.96500 -18.13600 15.87900 1.000 46.06130 ?  12  ASP A O   1 
ATOM   13   C CB  . ASP A 1 32  ? -23.18600 -18.23400 15.62900 1.000 48.02814 ?  12  ASP A CB  1 
ATOM   14   N N   . GLU A 1 33  ? -20.69700 -16.40700 14.63500 1.000 47.27093 ?  13  GLU A N   1 
ATOM   15   C CA  . GLU A 1 33  ? -19.42300 -16.28100 13.93500 1.000 47.82023 ?  13  GLU A CA  1 
ATOM   16   C C   . GLU A 1 33  ? -18.31000 -15.88100 14.89800 1.000 41.32658 ?  13  GLU A C   1 
ATOM   17   O O   . GLU A 1 33  ? -17.24300 -16.50600 14.92500 1.000 37.07052 ?  13  GLU A O   1 
ATOM   18   C CB  . GLU A 1 33  ? -19.54900 -15.26700 12.79700 1.000 47.87719 ?  13  GLU A CB  1 
ATOM   19   N N   . SER A 1 34  ? -18.55000 -14.84700 15.71000 1.000 35.60418 ?  14  SER A N   1 
ATOM   20   C CA  . SER A 1 34  ? -17.53800 -14.40800 16.66400 1.000 38.82785 ?  14  SER A CA  1 
ATOM   21   C C   . SER A 1 34  ? -17.22100 -15.50400 17.67100 1.000 35.15754 ?  14  SER A C   1 
ATOM   22   O O   . SER A 1 34  ? -16.05200 -15.73000 18.00300 1.000 39.55500 ?  14  SER A O   1 
ATOM   23   C CB  . SER A 1 34  ? -18.00000 -13.13600 17.37600 1.000 36.82492 ?  14  SER A CB  1 
ATOM   24   N N   . VAL A 1 35  ? -18.24700 -16.20700 18.15800 1.000 37.67887 ?  15  VAL A N   1 
ATOM   25   C CA  . VAL A 1 35  ? -18.01700 -17.28500 19.11600 1.000 37.97423 ?  15  VAL A CA  1 
ATOM   26   C C   . VAL A 1 35  ? -17.19500 -18.39500 18.47400 1.000 35.23417 ?  15  VAL A C   1 
ATOM   27   O O   . VAL A 1 35  ? -16.24500 -18.91200 19.07600 1.000 35.64551 ?  15  VAL A O   1 
ATOM   28   C CB  . VAL A 1 35  ? -19.35800 -17.81400 19.66200 1.000 42.66908 ?  15  VAL A CB  1 
ATOM   29   C CG1 . VAL A 1 35  ? -19.18000 -19.20000 20.26700 1.000 36.68160 ?  15  VAL A CG1 1 
ATOM   30   C CG2 . VAL A 1 35  ? -19.93500 -16.85000 20.68400 1.000 43.50616 ?  15  VAL A CG2 1 
ATOM   31   N N   . SER A 1 36  ? -17.53800 -18.77200 17.24000 1.000 32.43765 ?  16  SER A N   1 
ATOM   32   C CA  . SER A 1 36  ? -16.76300 -19.78600 16.53100 1.000 35.03037 ?  16  SER A CA  1 
ATOM   33   C C   . SER A 1 36  ? -15.32800 -19.33100 16.31500 1.000 35.27308 ?  16  SER A C   1 
ATOM   34   O O   . SER A 1 36  ? -14.39600 -20.14400 16.36600 1.000 36.31389 ?  16  SER A O   1 
ATOM   35   C CB  . SER A 1 36  ? -17.42200 -20.11300 15.19100 1.000 35.86494 ?  16  SER A CB  1 
ATOM   36   O OG  . SER A 1 36  ? -18.44500 -21.08200 15.34900 1.000 44.27215 ?  16  SER A OG  1 
ATOM   37   N N   . GLN A 1 37  ? -15.12900 -18.03600 16.06800 1.000 30.94406 ?  17  GLN A N   1 
ATOM   38   C CA  . GLN A 1 37  ? -13.78100 -17.53800 15.83200 1.000 33.80733 ?  17  GLN A CA  1 
ATOM   39   C C   . GLN A 1 37  ? -12.93200 -17.63900 17.09300 1.000 34.64701 ?  17  GLN A C   1 
ATOM   40   O O   . GLN A 1 37  ? -11.75500 -18.01200 17.02700 1.000 31.04157 ?  17  GLN A O   1 
ATOM   41   C CB  . GLN A 1 37  ? -13.83600 -16.09800 15.32800 1.000 34.00664 ?  17  GLN A CB  1 
ATOM   42   C CG  . GLN A 1 37  ? -12.48400 -15.56100 14.93200 1.000 37.38039 ?  17  GLN A CG  1 
ATOM   43   C CD  . GLN A 1 37  ? -12.54000 -14.11900 14.49600 1.000 43.66282 ?  17  GLN A CD  1 
ATOM   44   O OE1 . GLN A 1 37  ? -13.01300 -13.25300 15.23500 1.000 51.03635 ?  17  GLN A OE1 1 
ATOM   45   N NE2 . GLN A 1 37  ? -12.04300 -13.84400 13.29500 1.000 46.11721 ?  17  GLN A NE2 1 
ATOM   46   N N   . TYR A 1 38  ? -13.51900 -17.33500 18.25400 1.000 30.96273 ?  18  TYR A N   1 
ATOM   47   C CA  . TYR A 1 38  ? -12.78400 -17.41500 19.51000 1.000 34.43769 ?  18  TYR A CA  1 
ATOM   48   C C   . TYR A 1 38  ? -12.62000 -18.85200 19.98500 1.000 34.62757 ?  18  TYR A C   1 
ATOM   49   O O   . TYR A 1 38  ? -11.65200 -19.15800 20.69400 1.000 38.01741 ?  18  TYR A O   1 
ATOM   50   C CB  . TYR A 1 38  ? -13.48200 -16.57300 20.57800 1.000 31.26523 ?  18  TYR A CB  1 
ATOM   51   C CG  . TYR A 1 38  ? -13.03700 -15.12800 20.58200 1.000 40.80260 ?  18  TYR A CG  1 
ATOM   52   C CD1 . TYR A 1 38  ? -13.64900 -14.18800 19.75500 1.000 40.01838 ?  18  TYR A CD1 1 
ATOM   53   C CD2 . TYR A 1 38  ? -11.98300 -14.70700 21.38400 1.000 36.98014 ?  18  TYR A CD2 1 
ATOM   54   C CE1 . TYR A 1 38  ? -13.24100 -12.86700 19.74500 1.000 42.33546 ?  18  TYR A CE1 1 
ATOM   55   C CE2 . TYR A 1 38  ? -11.56600 -13.38700 21.38400 1.000 43.74732 ?  18  TYR A CE2 1 
ATOM   56   C CZ  . TYR A 1 38  ? -12.19900 -12.47000 20.56200 1.000 57.07321 ?  18  TYR A CZ  1 
ATOM   57   O OH  . TYR A 1 38  ? -11.78900 -11.15300 20.55100 1.000 57.64675 ?  18  TYR A OH  1 
ATOM   58   N N   . CYS A 1 39  ? -13.55000 -19.73700 19.61900 1.000 31.12619 ?  19  CYS A N   1 
ATOM   59   C CA  . CYS A 1 39  ? -13.36200 -21.16400 19.86500 1.000 31.64839 ?  19  CYS A CA  1 
ATOM   60   C C   . CYS A 1 39  ? -12.12000 -21.67100 19.14800 1.000 30.53974 ?  19  CYS A C   1 
ATOM   61   O O   . CYS A 1 39  ? -11.31300 -22.41700 19.71600 1.000 34.72587 ?  19  CYS A O   1 
ATOM   62   C CB  . CYS A 1 39  ? -14.59100 -21.94300 19.39400 1.000 32.21540 ?  19  CYS A CB  1 
ATOM   63   S SG  . CYS A 1 39  ? -16.01500 -21.85600 20.47400 1.000 32.76142 ?  19  CYS A SG  1 
ATOM   64   N N   . ASP A 1 40  ? -11.96400 -21.28100 17.88300 1.000 29.75795 ?  20  ASP A N   1 
ATOM   65   C CA  . ASP A 1 40  ? -10.78300 -21.65800 17.11800 1.000 33.20591 ?  20  ASP A CA  1 
ATOM   66   C C   . ASP A 1 40  ? -9.52700  -21.02200 17.69400 1.000 31.04457 ?  20  ASP A C   1 
ATOM   67   O O   . ASP A 1 40  ? -8.49200  -21.68400 17.82300 1.000 34.25299 ?  20  ASP A O   1 
ATOM   68   C CB  . ASP A 1 40  ? -10.96200 -21.24700 15.65900 1.000 34.38589 ?  20  ASP A CB  1 
ATOM   69   C CG  . ASP A 1 40  ? -10.02000 -21.97300 14.74000 1.000 35.79007 ?  20  ASP A CG  1 
ATOM   70   O OD1 . ASP A 1 40  ? -10.10800 -23.21700 14.66300 1.000 39.00572 ?  20  ASP A OD1 1 
ATOM   71   O OD2 . ASP A 1 40  ? -9.18100  -21.30000 14.10800 1.000 40.88727 -1 20  ASP A OD2 1 
ATOM   72   N N   . PHE A 1 41  ? -9.60700  -19.73600 18.03800 1.000 35.41167 ?  21  PHE A N   1 
ATOM   73   C CA  . PHE A 1 41  ? -8.47600  -19.03100 18.62900 1.000 34.17170 ?  21  PHE A CA  1 
ATOM   74   C C   . PHE A 1 41  ? -8.02500  -19.70500 19.91700 1.000 32.24637 ?  21  PHE A C   1 
ATOM   75   O O   . PHE A 1 41  ? -6.83700  -19.99500 20.09900 1.000 32.38823 ?  21  PHE A O   1 
ATOM   76   C CB  . PHE A 1 41  ? -8.87500  -17.57300 18.87100 1.000 33.26368 ?  21  PHE A CB  1 
ATOM   77   C CG  . PHE A 1 41  ? -7.81500  -16.73100 19.52900 1.000 30.63225 ?  21  PHE A CG  1 
ATOM   78   C CD1 . PHE A 1 41  ? -6.51600  -16.71100 19.04200 1.000 33.48488 ?  21  PHE A CD1 1 
ATOM   79   C CD2 . PHE A 1 41  ? -8.13800  -15.90100 20.59400 1.000 33.62090 ?  21  PHE A CD2 1 
ATOM   80   C CE1 . PHE A 1 41  ? -5.54900  -15.90900 19.63100 1.000 28.34170 ?  21  PHE A CE1 1 
ATOM   81   C CE2 . PHE A 1 41  ? -7.17800  -15.09600 21.18600 1.000 36.10323 ?  21  PHE A CE2 1 
ATOM   82   C CZ  . PHE A 1 41  ? -5.88000  -15.10100 20.70300 1.000 30.39213 ?  21  PHE A CZ  1 
ATOM   83   N N   . GLN A 1 42  ? -8.97200  -20.00800 20.80400 1.000 28.59754 ?  22  GLN A N   1 
ATOM   84   C CA  . GLN A 1 42  ? -8.63500  -20.44700 22.15100 1.000 30.56376 ?  22  GLN A CA  1 
ATOM   85   C C   . GLN A 1 42  ? -8.38900  -21.94400 22.26400 1.000 30.06554 ?  22  GLN A C   1 
ATOM   86   O O   . GLN A 1 42  ? -7.66300  -22.37400 23.16800 1.000 29.20616 ?  22  GLN A O   1 
ATOM   87   C CB  . GLN A 1 42  ? -9.74300  -20.04300 23.12600 1.000 28.03124 ?  22  GLN A CB  1 
ATOM   88   C CG  . GLN A 1 42  ? -9.76000  -18.56100 23.43000 1.000 34.35068 ?  22  GLN A CG  1 
ATOM   89   C CD  . GLN A 1 42  ? -10.35600 -18.26400 24.78600 1.000 38.69173 ?  22  GLN A CD  1 
ATOM   90   O OE1 . GLN A 1 42  ? -11.19400 -19.01600 25.29200 1.000 34.73025 ?  22  GLN A OE1 1 
ATOM   91   N NE2 . GLN A 1 42  ? -9.90200  -17.17800 25.40100 1.000 37.25753 ?  22  GLN A NE2 1 
ATOM   92   N N   . TYR A 1 43  ? -8.97200  -22.75200 21.38200 1.000 28.96283 ?  23  TYR A N   1 
ATOM   93   C CA  . TYR A 1 43  ? -8.86500  -24.19800 21.49400 1.000 31.48882 ?  23  TYR A CA  1 
ATOM   94   C C   . TYR A 1 43  ? -8.29600  -24.85800 20.24600 1.000 36.13058 ?  23  TYR A C   1 
ATOM   95   O O   . TYR A 1 43  ? -8.12800  -26.08200 20.23900 1.000 36.58537 ?  23  TYR A O   1 
ATOM   96   C CB  . TYR A 1 43  ? -10.24000 -24.80500 21.81500 1.000 30.33419 ?  23  TYR A CB  1 
ATOM   97   C CG  . TYR A 1 43  ? -10.84700 -24.29500 23.10900 1.000 35.24172 ?  23  TYR A CG  1 
ATOM   98   C CD1 . TYR A 1 43  ? -10.51200 -24.86300 24.33600 1.000 30.19991 ?  23  TYR A CD1 1 
ATOM   99   C CD2 . TYR A 1 43  ? -11.74400 -23.23000 23.10400 1.000 30.40531 ?  23  TYR A CD2 1 
ATOM   100  C CE1 . TYR A 1 43  ? -11.06400 -24.39000 25.51600 1.000 29.21509 ?  23  TYR A CE1 1 
ATOM   101  C CE2 . TYR A 1 43  ? -12.29700 -22.75000 24.27500 1.000 25.49819 ?  23  TYR A CE2 1 
ATOM   102  C CZ  . TYR A 1 43  ? -11.95300 -23.33000 25.47600 1.000 29.86093 ?  23  TYR A CZ  1 
ATOM   103  O OH  . TYR A 1 43  ? -12.50300 -22.85500 26.64000 1.000 29.50120 ?  23  TYR A OH  1 
ATOM   104  N N   . GLY A 1 44  ? -7.98800  -24.09000 19.20000 1.000 37.13444 ?  24  GLY A N   1 
ATOM   105  C CA  . GLY A 1 44  ? -7.48700  -24.63900 17.95700 1.000 43.92564 ?  24  GLY A CA  1 
ATOM   106  C C   . GLY A 1 44  ? -5.98700  -24.88000 17.97800 1.000 54.48996 ?  24  GLY A C   1 
ATOM   107  O O   . GLY A 1 44  ? -5.32100  -24.80700 19.01300 1.000 50.89254 ?  24  GLY A O   1 
ATOM   108  N N   . GLU A 1 45  ? -5.45300  -25.17500 16.79600 1.000 57.98183 ?  25  GLU A N   1 
ATOM   109  C CA  . GLU A 1 45  ? -4.04400  -25.50000 16.63900 1.000 59.32844 ?  25  GLU A CA  1 
ATOM   110  C C   . GLU A 1 45  ? -3.23300  -24.24200 16.33700 1.000 59.36676 ?  25  GLU A C   1 
ATOM   111  O O   . GLU A 1 45  ? -3.74700  -23.24600 15.81900 1.000 52.51482 ?  25  GLU A O   1 
ATOM   112  N N   . ASP A 1 46  ? -1.94300  -24.31000 16.66200 1.000 51.08932 ?  26  ASP A N   1 
ATOM   113  C CA  . ASP A 1 46  ? -1.04500  -23.18100 16.46200 1.000 47.74863 ?  26  ASP A CA  1 
ATOM   114  C C   . ASP A 1 46  ? -0.88100  -22.85900 14.97700 1.000 44.95207 ?  26  ASP A C   1 
ATOM   115  O O   . ASP A 1 46  ? -1.01100  -23.72500 14.10800 1.000 47.48057 ?  26  ASP A O   1 
ATOM   116  C CB  . ASP A 1 46  ? 0.31700   -23.46900 17.10200 1.000 49.10447 ?  26  ASP A CB  1 
ATOM   117  C CG  . ASP A 1 46  ? 0.95500   -24.74800 16.57800 1.000 66.07353 ?  26  ASP A CG  1 
ATOM   118  O OD1 . ASP A 1 46  ? 2.01300   -24.66100 15.91300 1.000 61.07420 ?  26  ASP A OD1 1 
ATOM   119  N N   . CYS A 1 47  ? -0.60400  -21.58400 14.69500 1.000 44.43685 ?  27  CYS A N   1 
ATOM   120  C CA  . CYS A 1 47  ? -0.42400  -21.07600 13.34100 1.000 39.41144 ?  27  CYS A CA  1 
ATOM   121  C C   . CYS A 1 47  ? 0.87200   -20.28400 13.27000 1.000 37.23072 ?  27  CYS A C   1 
ATOM   122  O O   . CYS A 1 47  ? 1.21500   -19.56300 14.20900 1.000 39.03559 ?  27  CYS A O   1 
ATOM   123  C CB  . CYS A 1 47  ? -1.59000  -20.17000 12.91000 1.000 33.95669 ?  27  CYS A CB  1 
ATOM   124  S SG  . CYS A 1 47  ? -3.21700  -20.92900 12.98000 1.000 60.57248 ?  27  CYS A SG  1 
ATOM   125  N N   . PHE A 1 48  ? 1.58500   -20.42300 12.15200 1.000 34.96610 ?  28  PHE A N   1 
ATOM   126  C CA  . PHE A 1 48  ? 2.82600   -19.68800 11.89700 1.000 33.27461 ?  28  PHE A CA  1 
ATOM   127  C C   . PHE A 1 48  ? 3.83700   -19.84500 13.02600 1.000 32.70538 ?  28  PHE A C   1 
ATOM   128  O O   . PHE A 1 48  ? 4.65200   -18.95100 13.26600 1.000 46.25568 ?  28  PHE A O   1 
ATOM   129  C CB  . PHE A 1 48  ? 2.55900   -18.20100 11.65200 1.000 33.48298 ?  28  PHE A CB  1 
ATOM   130  C CG  . PHE A 1 48  ? 1.52400   -17.93800 10.61100 1.000 34.74999 ?  28  PHE A CG  1 
ATOM   131  C CD1 . PHE A 1 48  ? 1.73800   -18.31900 9.30000  1.000 34.37591 ?  28  PHE A CD1 1 
ATOM   132  C CD2 . PHE A 1 48  ? 0.34100   -17.29700 10.93800 1.000 37.97167 ?  28  PHE A CD2 1 
ATOM   133  C CE1 . PHE A 1 48  ? 0.78800   -18.07200 8.33300  1.000 38.36066 ?  28  PHE A CE1 1 
ATOM   134  C CE2 . PHE A 1 48  ? -0.61300  -17.04900 9.97700  1.000 36.85712 ?  28  PHE A CE2 1 
ATOM   135  C CZ  . PHE A 1 48  ? -0.39200  -17.43600 8.67200  1.000 33.11494 ?  28  PHE A CZ  1 
ATOM   136  N N   . GLY A 1 49  ? 3.79400   -20.96600 13.73500 1.000 36.62860 ?  29  GLY A N   1 
ATOM   137  C CA  . GLY A 1 49  ? 4.70600   -21.15200 14.84300 1.000 36.82326 ?  29  GLY A CA  1 
ATOM   138  C C   . GLY A 1 49  ? 4.32100   -20.43800 16.11700 1.000 38.48515 ?  29  GLY A C   1 
ATOM   139  O O   . GLY A 1 49  ? 5.06200   -20.51800 17.10000 1.000 42.01513 ?  29  GLY A O   1 
ATOM   140  N N   . VAL A 1 50  ? 3.18600   -19.74500 16.13600 1.000 38.56516 ?  30  VAL A N   1 
ATOM   141  C CA  . VAL A 1 50  ? 2.75700   -18.98400 17.30300 1.000 35.37919 ?  30  VAL A CA  1 
ATOM   142  C C   . VAL A 1 50  ? 1.92800   -19.89000 18.20300 1.000 37.06808 ?  30  VAL A C   1 
ATOM   143  O O   . VAL A 1 50  ? 0.92300   -20.46900 17.77300 1.000 34.38832 ?  30  VAL A O   1 
ATOM   144  C CB  . VAL A 1 50  ? 1.96600   -17.73500 16.88400 1.000 33.55158 ?  30  VAL A CB  1 
ATOM   145  C CG1 . VAL A 1 50  ? 1.36800   -17.05400 18.10300 1.000 29.64807 ?  30  VAL A CG1 1 
ATOM   146  C CG2 . VAL A 1 50  ? 2.87300   -16.78200 16.12900 1.000 34.10675 ?  30  VAL A CG2 1 
ATOM   147  N N   . LEU A 1 51  ? 2.35000   -20.01000 19.45500 1.000 29.72013 ?  31  LEU A N   1 
ATOM   148  C CA  . LEU A 1 51  ? 1.67800   -20.88200 20.39900 1.000 35.18321 ?  31  LEU A CA  1 
ATOM   149  C C   . LEU A 1 51  ? 0.34000   -20.28900 20.83300 1.000 35.17791 ?  31  LEU A C   1 
ATOM   150  O O   . LEU A 1 51  ? 0.06400   -19.09900 20.65600 1.000 34.48554 ?  31  LEU A O   1 
ATOM   151  C CB  . LEU A 1 51  ? 2.56500   -21.12800 21.61800 1.000 39.17675 ?  31  LEU A CB  1 
ATOM   152  C CG  . LEU A 1 51  ? 3.83500   -21.92400 21.30900 1.000 51.57410 ?  31  LEU A CG  1 
ATOM   153  C CD1 . LEU A 1 51  ? 4.55400   -22.33200 22.58400 1.000 45.39333 ?  31  LEU A CD1 1 
ATOM   154  C CD2 . LEU A 1 51  ? 3.51100   -23.14500 20.45600 1.000 40.91671 ?  31  LEU A CD2 1 
ATOM   155  N N   . ASN A 1 52  ? -0.49000  -21.15000 21.41200 1.000 35.40193 ?  32  ASN A N   1 
ATOM   156  C CA  . ASN A 1 52  ? -1.79900  -20.76100 21.91900 1.000 31.98175 ?  32  ASN A CA  1 
ATOM   157  C C   . ASN A 1 52  ? -1.68900  -19.59100 22.89100 1.000 27.02861 ?  32  ASN A C   1 
ATOM   158  O O   . ASN A 1 52  ? -0.97000  -19.66600 23.88900 1.000 30.84837 ?  32  ASN A O   1 
ATOM   159  C CB  . ASN A 1 52  ? -2.44900  -21.96400 22.60200 1.000 29.82408 ?  32  ASN A CB  1 
ATOM   160  C CG  . ASN A 1 52  ? -3.82800  -21.65500 23.13100 1.000 32.02310 ?  32  ASN A CG  1 
ATOM   161  O OD1 . ASN A 1 52  ? -3.97100  -21.08900 24.21500 1.000 31.77588 ?  32  ASN A OD1 1 
ATOM   162  N ND2 . ASN A 1 52  ? -4.85400  -22.03900 22.37900 1.000 31.78974 ?  32  ASN A ND2 1 
ATOM   163  N N   . PHE A 1 53  ? -2.42200  -18.51400 22.59600 1.000 29.50469 ?  33  PHE A N   1 
ATOM   164  C CA  . PHE A 1 53  ? -2.29600  -17.27900 23.36200 1.000 28.35510 ?  33  PHE A CA  1 
ATOM   165  C C   . PHE A 1 53  ? -2.82200  -17.44100 24.78300 1.000 32.18273 ?  33  PHE A C   1 
ATOM   166  O O   . PHE A 1 53  ? -2.16600  -17.02000 25.74400 1.000 30.62856 ?  33  PHE A O   1 
ATOM   167  C CB  . PHE A 1 53  ? -3.03200  -16.15200 22.63900 1.000 31.54834 ?  33  PHE A CB  1 
ATOM   168  C CG  . PHE A 1 53  ? -2.85200  -14.80500 23.26600 1.000 31.40197 ?  33  PHE A CG  1 
ATOM   169  C CD1 . PHE A 1 53  ? -1.60800  -14.19800 23.28400 1.000 26.92900 ?  33  PHE A CD1 1 
ATOM   170  C CD2 . PHE A 1 53  ? -3.93300  -14.13500 23.82300 1.000 27.61298 ?  33  PHE A CD2 1 
ATOM   171  C CE1 . PHE A 1 53  ? -1.44100  -12.94700 23.85500 1.000 31.97218 ?  33  PHE A CE1 1 
ATOM   172  C CE2 . PHE A 1 53  ? -3.77200  -12.88500 24.39300 1.000 32.17302 ?  33  PHE A CE2 1 
ATOM   173  C CZ  . PHE A 1 53  ? -2.52400  -12.28800 24.40800 1.000 30.73896 ?  33  PHE A CZ  1 
ATOM   174  N N   . ALA A 1 54  ? -3.99800  -18.05200 24.93700 1.000 27.35651 ?  34  ALA A N   1 
ATOM   175  C CA  . ALA A 1 54  ? -4.57600  -18.21100 26.26800 1.000 32.23963 ?  34  ALA A CA  1 
ATOM   176  C C   . ALA A 1 54  ? -3.69900  -19.08400 27.15500 1.000 31.52864 ?  34  ALA A C   1 
ATOM   177  O O   . ALA A 1 54  ? -3.54100  -18.80100 28.35000 1.000 29.78579 ?  34  ALA A O   1 
ATOM   178  C CB  . ALA A 1 54  ? -5.98600  -18.78800 26.16300 1.000 26.98122 ?  34  ALA A CB  1 
ATOM   179  N N   . LEU A 1 55  ? -3.11100  -20.14200 26.59200 1.000 28.77137 ?  35  LEU A N   1 
ATOM   180  C CA  . LEU A 1 55  ? -2.19900  -20.96900 27.37500 1.000 31.96322 ?  35  LEU A CA  1 
ATOM   181  C C   . LEU A 1 55  ? -0.94000  -20.19900 27.75000 1.000 28.12407 ?  35  LEU A C   1 
ATOM   182  O O   . LEU A 1 55  ? -0.46900  -20.29000 28.88800 1.000 32.88874 ?  35  LEU A O   1 
ATOM   183  C CB  . LEU A 1 55  ? -1.83700  -22.23900 26.60400 1.000 33.88870 ?  35  LEU A CB  1 
ATOM   184  C CG  . LEU A 1 55  ? -0.91400  -23.20500 27.35600 1.000 31.86368 ?  35  LEU A CG  1 
ATOM   185  C CD1 . LEU A 1 55  ? -1.40900  -23.49200 28.77800 1.000 31.47125 ?  35  LEU A CD1 1 
ATOM   186  C CD2 . LEU A 1 55  ? -0.75100  -24.48800 26.57000 1.000 33.06555 ?  35  LEU A CD2 1 
ATOM   187  N N   . ALA A 1 56  ? -0.38500  -19.43600 26.80600 1.000 29.57850 ?  36  ALA A N   1 
ATOM   188  C CA  . ALA A 1 56  ? 0.83200   -18.67600 27.07700 1.000 29.82803 ?  36  ALA A CA  1 
ATOM   189  C C   . ALA A 1 56  ? 0.60400   -17.64200 28.17400 1.000 27.90401 ?  36  ALA A C   1 
ATOM   190  O O   . ALA A 1 56  ? 1.41400   -17.51000 29.09800 1.000 32.14377 ?  36  ALA A O   1 
ATOM   191  C CB  . ALA A 1 56  ? 1.32200   -18.00400 25.79300 1.000 27.87624 ?  36  ALA A CB  1 
ATOM   192  N N   . CYS A 1 57  ? -0.50300  -16.90100 28.08900 1.000 31.13146 ?  37  CYS A N   1 
ATOM   193  C CA  . CYS A 1 57  ? -0.79300  -15.87300 29.08600 1.000 27.83824 ?  37  CYS A CA  1 
ATOM   194  C C   . CYS A 1 57  ? -1.01800  -16.48800 30.46000 1.000 33.07301 ?  37  CYS A C   1 
ATOM   195  O O   . CYS A 1 57  ? -0.51900  -15.98100 31.47400 1.000 28.99904 ?  37  CYS A O   1 
ATOM   196  C CB  . CYS A 1 57  ? -2.02100  -15.07100 28.66200 1.000 31.12885 ?  37  CYS A CB  1 
ATOM   197  S SG  . CYS A 1 57  ? -1.77300  -13.99000 27.25300 1.000 36.35670 ?  37  CYS A SG  1 
ATOM   198  N N   . ALA A 1 58  ? -1.78700  -17.57700 30.51300 1.000 27.63847 ?  38  ALA A N   1 
ATOM   199  C CA  . ALA A 1 58  ? -2.07700  -18.21700 31.79100 1.000 31.99523 ?  38  ALA A CA  1 
ATOM   200  C C   . ALA A 1 58  ? -0.82000  -18.82500 32.39200 1.000 28.25551 ?  38  ALA A C   1 
ATOM   201  O O   . ALA A 1 58  ? -0.58200  -18.71600 33.60100 1.000 28.38885 ?  38  ALA A O   1 
ATOM   202  C CB  . ALA A 1 58  ? -3.15400  -19.28400 31.60900 1.000 27.77763 ?  38  ALA A CB  1 
ATOM   203  N N   . THR A 1 59  ? 0.00300   -19.45200 31.55200 1.000 29.57895 ?  39  THR A N   1 
ATOM   204  C CA  . THR A 1 59  ? 1.25700   -20.02500 32.02300 1.000 34.86773 ?  39  THR A CA  1 
ATOM   205  C C   . THR A 1 59  ? 2.18900   -18.93600 32.53800 1.000 28.39967 ?  39  THR A C   1 
ATOM   206  O O   . THR A 1 59  ? 2.79200   -19.07100 33.60800 1.000 32.20181 ?  39  THR A O   1 
ATOM   207  C CB  . THR A 1 59  ? 1.91300   -20.82300 30.89500 1.000 32.02685 ?  39  THR A CB  1 
ATOM   208  O OG1 . THR A 1 59  ? 1.06100   -21.91700 30.54700 1.000 31.02619 ?  39  THR A OG1 1 
ATOM   209  C CG2 . THR A 1 59  ? 3.26200   -21.36700 31.33500 1.000 33.74321 ?  39  THR A CG2 1 
ATOM   210  N N   . LYS A 1 60  ? 2.30000   -17.83300 31.79600 1.000 25.15085 ?  40  LYS A N   1 
ATOM   211  C CA  . LYS A 1 60  ? 3.14600   -16.73300 32.25200 1.000 35.96169 ?  40  LYS A CA  1 
ATOM   212  C C   . LYS A 1 60  ? 2.58400   -16.09000 33.51400 1.000 37.17618 ?  40  LYS A C   1 
ATOM   213  O O   . LYS A 1 60  ? 3.34300   -15.67500 34.40000 1.000 38.80611 ?  40  LYS A O   1 
ATOM   214  C CB  . LYS A 1 60  ? 3.30600   -15.69800 31.14300 1.000 29.99219 ?  40  LYS A CB  1 
ATOM   215  C CG  . LYS A 1 60  ? 4.20700   -16.15600 30.01700 1.000 35.70157 ?  40  LYS A CG  1 
ATOM   216  C CD  . LYS A 1 60  ? 3.97300   -15.31000 28.78100 1.000 40.05775 ?  40  LYS A CD  1 
ATOM   217  C CE  . LYS A 1 60  ? 4.65900   -15.90700 27.56700 1.000 37.07317 ?  40  LYS A CE  1 
ATOM   218  N NZ  . LYS A 1 60  ? 6.13900   -15.86200 27.71000 1.000 44.11446 ?  40  LYS A NZ  1 
ATOM   219  N N   . ALA A 1 61  ? 1.25600   -16.01600 33.62200 1.000 33.48933 ?  41  ALA A N   1 
ATOM   220  C CA  . ALA A 1 61  ? 0.63400   -15.45000 34.81500 1.000 30.92389 ?  41  ALA A CA  1 
ATOM   221  C C   . ALA A 1 61  ? 0.90600   -16.30600 36.04600 1.000 33.50488 ?  41  ALA A C   1 
ATOM   222  O O   . ALA A 1 61  ? 1.13300   -15.77600 37.14000 1.000 36.06214 ?  41  ALA A O   1 
ATOM   223  C CB  . ALA A 1 61  ? -0.87300  -15.29000 34.60000 1.000 30.03462 ?  41  ALA A CB  1 
ATOM   224  N N   . ILE A 1 62  ? 0.88600   -17.63100 35.89200 1.000 35.43489 ?  42  ILE A N   1 
ATOM   225  C CA  . ILE A 1 62  ? 1.14900   -18.50000 37.03600 1.000 40.38253 ?  42  ILE A CA  1 
ATOM   226  C C   . ILE A 1 62  ? 2.59100   -18.33200 37.50400 1.000 36.89842 ?  42  ILE A C   1 
ATOM   227  O O   . ILE A 1 62  ? 2.87300   -18.33900 38.70900 1.000 44.44732 ?  42  ILE A O   1 
ATOM   228  C CB  . ILE A 1 62  ? 0.81600   -19.96600 36.69000 1.000 35.88087 ?  42  ILE A CB  1 
ATOM   229  C CG1 . ILE A 1 62  ? -0.69500  -20.14600 36.54700 1.000 33.79217 ?  42  ILE A CG1 1 
ATOM   230  C CG2 . ILE A 1 62  ? 1.34800   -20.91200 37.75500 1.000 32.20979 ?  42  ILE A CG2 1 
ATOM   231  C CD1 . ILE A 1 62  ? -1.09900  -21.26500 35.61300 1.000 32.53311 ?  42  ILE A CD1 1 
ATOM   232  N N   . GLY A 1 63  ? 3.52000   -18.15000 36.56500 1.000 37.89565 ?  43  GLY A N   1 
ATOM   233  C CA  . GLY A 1 63  ? 4.90500   -17.92500 36.95000 1.000 40.61390 ?  43  GLY A CA  1 
ATOM   234  C C   . GLY A 1 63  ? 5.09200   -16.64100 37.73800 1.000 38.35132 ?  43  GLY A C   1 
ATOM   235  O O   . GLY A 1 63  ? 5.74200   -16.63200 38.78600 1.000 43.95857 ?  43  GLY A O   1 
ATOM   236  N N   . TYR A 1 64  ? 4.51700   -15.53800 37.24600 1.000 41.41775 ?  44  TYR A N   1 
ATOM   237  C CA  . TYR A 1 64  ? 4.64900   -14.25000 37.92100 1.000 38.27354 ?  44  TYR A CA  1 
ATOM   238  C C   . TYR A 1 64  ? 3.98400   -14.23300 39.29100 1.000 42.88637 ?  44  TYR A C   1 
ATOM   239  O O   . TYR A 1 64  ? 4.30100   -13.35900 40.10400 1.000 48.86902 ?  44  TYR A O   1 
ATOM   240  C CB  . TYR A 1 64  ? 4.05400   -13.13200 37.05700 1.000 31.30202 ?  44  TYR A CB  1 
ATOM   241  C CG  . TYR A 1 64  ? 4.88600   -12.77400 35.85000 1.000 32.03003 ?  44  TYR A CG  1 
ATOM   242  C CD1 . TYR A 1 64  ? 6.20700   -12.37300 35.98700 1.000 34.11854 ?  44  TYR A CD1 1 
ATOM   243  C CD2 . TYR A 1 64  ? 4.34800   -12.83300 34.56700 1.000 33.63969 ?  44  TYR A CD2 1 
ATOM   244  C CE1 . TYR A 1 64  ? 6.97000   -12.04600 34.88300 1.000 33.58176 ?  44  TYR A CE1 1 
ATOM   245  C CE2 . TYR A 1 64  ? 5.10700   -12.50900 33.45600 1.000 31.18488 ?  44  TYR A CE2 1 
ATOM   246  C CZ  . TYR A 1 64  ? 6.41700   -12.11600 33.62300 1.000 32.01862 ?  44  TYR A CZ  1 
ATOM   247  O OH  . TYR A 1 64  ? 7.18100   -11.78300 32.52900 1.000 35.37995 ?  44  TYR A OH  1 
ATOM   248  N N   . THR A 1 65  ? 3.06700   -15.16200 39.56000 1.000 40.58235 ?  45  THR A N   1 
ATOM   249  C CA  . THR A 1 65  ? 2.33000   -15.19200 40.81700 1.000 41.22014 ?  45  THR A CA  1 
ATOM   250  C C   . THR A 1 65  ? 2.67200   -16.41500 41.66100 1.000 46.76990 ?  45  THR A C   1 
ATOM   251  O O   . THR A 1 65  ? 1.87900   -16.80700 42.52400 1.000 50.99556 ?  45  THR A O   1 
ATOM   252  C CB  . THR A 1 65  ? 0.82600   -15.14600 40.54700 1.000 39.02647 ?  45  THR A CB  1 
ATOM   253  O OG1 . THR A 1 65  ? 0.43400   -16.30500 39.80000 1.000 38.18699 ?  45  THR A OG1 1 
ATOM   254  C CG2 . THR A 1 65  ? 0.45800   -13.90000 39.75300 1.000 35.00291 ?  45  THR A CG2 1 
ATOM   255  N N   . LYS A 1 66  ? 3.84300   -17.02000 41.43200 1.000 50.05287 ?  46  LYS A N   1 
ATOM   256  C CA  . LYS A 1 66  ? 4.19000   -18.26500 42.11400 1.000 51.16495 ?  46  LYS A CA  1 
ATOM   257  C C   . LYS A 1 66  ? 4.31200   -18.06400 43.62100 1.000 54.25862 ?  46  LYS A C   1 
ATOM   258  O O   . LYS A 1 66  ? 3.94600   -18.94900 44.40400 1.000 64.11419 ?  46  LYS A O   1 
ATOM   259  C CB  . LYS A 1 66  ? 5.49200   -18.82800 41.54500 1.000 48.69497 ?  46  LYS A CB  1 
ATOM   260  N N   . GLU A 1 67  ? 4.81600   -16.90900 44.04600 1.000 44.49184 ?  47  GLU A N   1 
ATOM   261  C CA  . GLU A 1 67  ? 4.99400   -16.61000 45.46200 1.000 49.87830 ?  47  GLU A CA  1 
ATOM   262  C C   . GLU A 1 67  ? 3.68900   -16.28900 46.18500 1.000 53.31017 ?  47  GLU A C   1 
ATOM   263  O O   . GLU A 1 67  ? 3.71000   -16.10500 47.40600 1.000 56.96205 ?  47  GLU A O   1 
ATOM   264  C CB  . GLU A 1 67  ? 5.97200   -15.44000 45.63100 1.000 51.93534 ?  47  GLU A CB  1 
ATOM   265  N N   . THR A 1 68  ? 2.56100   -16.22200 45.47900 1.000 51.18838 ?  48  THR A N   1 
ATOM   266  C CA  . THR A 1 68  ? 1.29600   -15.82400 46.07900 1.000 45.86913 ?  48  THR A CA  1 
ATOM   267  C C   . THR A 1 68  ? 0.46600   -17.04100 46.46500 1.000 41.20734 ?  48  THR A C   1 
ATOM   268  O O   . THR A 1 68  ? 0.71300   -18.15200 45.98900 1.000 45.08857 ?  48  THR A O   1 
ATOM   269  C CB  . THR A 1 68  ? 0.49900   -14.93400 45.11300 1.000 48.85594 ?  48  THR A CB  1 
ATOM   270  O OG1 . THR A 1 68  ? -0.30200  -15.75100 44.24800 1.000 53.50635 ?  48  THR A OG1 1 
ATOM   271  C CG2 . THR A 1 68  ? 1.43600   -14.07800 44.27700 1.000 49.70788 ?  48  THR A CG2 1 
ATOM   272  N N   . PRO A 1 69  ? -0.51100  -16.87000 47.36200 1.000 40.65327 ?  49  PRO A N   1 
ATOM   273  C CA  . PRO A 1 69  ? -1.33900  -18.01600 47.77900 1.000 44.46742 ?  49  PRO A CA  1 
ATOM   274  C C   . PRO A 1 69  ? -2.00300  -18.76900 46.63900 1.000 44.58285 ?  49  PRO A C   1 
ATOM   275  O O   . PRO A 1 69  ? -2.20300  -19.98600 46.75700 1.000 48.81342 ?  49  PRO A O   1 
ATOM   276  C CB  . PRO A 1 69  ? -2.39100  -17.37600 48.69700 1.000 46.43865 ?  49  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 69  ? -1.83700  -16.05500 49.10500 1.000 50.03090 ?  49  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 69  ? -0.58300  -15.76400 48.32900 1.000 44.63230 ?  49  PRO A CD  1 
ATOM   279  N N   . LYS A 1 70  ? -2.36200  -18.09200 45.54900 1.000 38.88924 ?  50  LYS A N   1 
ATOM   280  C CA  . LYS A 1 70  ? -3.00800  -18.73800 44.40300 1.000 43.02864 ?  50  LYS A CA  1 
ATOM   281  C C   . LYS A 1 70  ? -4.31600  -19.42200 44.81300 1.000 40.51842 ?  50  LYS A C   1 
ATOM   282  O O   . LYS A 1 70  ? -4.55800  -20.59200 44.51000 1.000 37.56632 ?  50  LYS A O   1 
ATOM   283  C CB  . LYS A 1 70  ? -2.05700  -19.72800 43.71700 1.000 40.47679 ?  50  LYS A CB  1 
ATOM   284  C CG  . LYS A 1 70  ? -0.95300  -19.07200 42.88900 1.000 40.08585 ?  50  LYS A CG  1 
ATOM   285  C CD  . LYS A 1 70  ? 0.01200   -20.10100 42.31500 1.000 42.91630 ?  50  LYS A CD  1 
ATOM   286  N N   . ASN A 1 71  ? -5.17100  -18.67700 45.51400 1.000 33.60076 ?  51  ASN A N   1 
ATOM   287  C CA  . ASN A 1 71  ? -6.49100  -19.16700 45.89300 1.000 38.96780 ?  51  ASN A CA  1 
ATOM   288  C C   . ASN A 1 71  ? -7.57300  -18.73700 44.91100 1.000 36.60713 ?  51  ASN A C   1 
ATOM   289  O O   . ASN A 1 71  ? -8.28100  -19.58200 44.36000 1.000 41.21633 ?  51  ASN A O   1 
ATOM   290  C CB  . ASN A 1 71  ? -6.85500  -18.69400 47.30700 1.000 37.44084 ?  51  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 71  ? -5.94500  -19.28100 48.37100 1.000 53.04581 ?  51  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 71  ? -5.59800  -20.46400 48.32600 1.000 56.93055 ?  51  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 71  ? -5.54900  -18.45300 49.33300 1.000 53.65267 ?  51  ASN A ND2 1 
ATOM   294  N N   . ARG A 1 72  ? -7.70500  -17.43600 44.67100 1.000 32.20236 ?  52  ARG A N   1 
ATOM   295  C CA  . ARG A 1 72  ? -8.74800  -16.88200 43.82000 1.000 36.87861 ?  52  ARG A CA  1 
ATOM   296  C C   . ARG A 1 72  ? -8.10700  -16.10900 42.67700 1.000 37.83909 ?  52  ARG A C   1 
ATOM   297  O O   . ARG A 1 72  ? -7.21300  -15.28600 42.90300 1.000 33.30292 ?  52  ARG A O   1 
ATOM   298  C CB  . ARG A 1 72  ? -9.67900  -15.96800 44.62800 1.000 34.38544 ?  52  ARG A CB  1 
ATOM   299  C CG  . ARG A 1 72  ? -10.48500 -16.71700 45.68000 1.000 33.87063 ?  52  ARG A CG  1 
ATOM   300  C CD  . ARG A 1 72  ? -11.38200 -15.80100 46.49400 1.000 38.66097 ?  52  ARG A CD  1 
ATOM   301  N NE  . ARG A 1 72  ? -12.03200 -14.77500 45.69000 1.000 38.04984 ?  52  ARG A NE  1 
ATOM   302  C CZ  . ARG A 1 72  ? -13.21300 -14.93000 45.10800 1.000 35.48492 ?  52  ARG A CZ  1 
ATOM   303  N NH1 . ARG A 1 72  ? -13.85100 -16.08700 45.14300 1.000 28.58529 ?  52  ARG A NH1 1 
ATOM   304  N NH2 . ARG A 1 72  ? -13.76400 -13.89900 44.47400 1.000 35.57159 ?  52  ARG A NH2 1 
ATOM   305  N N   . ALA A 1 73  ? -8.56000  -16.38200 41.45300 1.000 36.15256 ?  53  ALA A N   1 
ATOM   306  C CA  . ALA A 1 73  ? -8.13400  -15.64400 40.27500 1.000 35.74147 ?  53  ALA A CA  1 
ATOM   307  C C   . ALA A 1 73  ? -9.35500  -15.21500 39.47500 1.000 27.18100 ?  53  ALA A C   1 
ATOM   308  O O   . ALA A 1 73  ? -10.37400 -15.90600 39.45000 1.000 30.05845 ?  53  ALA A O   1 
ATOM   309  C CB  . ALA A 1 73  ? -7.19400  -16.47400 39.38600 1.000 30.98915 ?  53  ALA A CB  1 
ATOM   310  N N   . LEU A 1 74  ? -9.23300  -14.07200 38.81100 1.000 31.69381 ?  54  LEU A N   1 
ATOM   311  C CA  . LEU A 1 74  ? -10.28800 -13.50300 37.98500 1.000 31.39414 ?  54  LEU A CA  1 
ATOM   312  C C   . LEU A 1 74  ? -9.75500  -13.27800 36.57500 1.000 31.76231 ?  54  LEU A C   1 
ATOM   313  O O   . LEU A 1 74  ? -8.74400  -12.59000 36.38900 1.000 30.75475 ?  54  LEU A O   1 
ATOM   314  C CB  . LEU A 1 74  ? -10.79500 -12.18700 38.57800 1.000 26.77943 ?  54  LEU A CB  1 
ATOM   315  C CG  . LEU A 1 74  ? -11.84300 -11.46500 37.72900 1.000 35.50256 ?  54  LEU A CG  1 
ATOM   316  C CD1 . LEU A 1 74  ? -13.13000 -12.26100 37.72100 1.000 30.78357 ?  54  LEU A CD1 1 
ATOM   317  C CD2 . LEU A 1 74  ? -12.08300 -10.05900 38.25300 1.000 26.97038 ?  54  LEU A CD2 1 
ATOM   318  N N   . ASP A 1 75  ? -10.42800 -13.86500 35.58700 1.000 31.82280 ?  55  ASP A N   1 
ATOM   319  C CA  . ASP A 1 75  ? -10.04800 -13.76000 34.17700 1.000 29.44418 ?  55  ASP A CA  1 
ATOM   320  C C   . ASP A 1 75  ? -11.11700 -12.92900 33.47400 1.000 28.44048 ?  55  ASP A C   1 
ATOM   321  O O   . ASP A 1 75  ? -12.19800 -13.43200 33.15500 1.000 30.08260 ?  55  ASP A O   1 
ATOM   322  C CB  . ASP A 1 75  ? -9.88900  -15.15000 33.55600 1.000 26.95797 ?  55  ASP A CB  1 
ATOM   323  C CG  . ASP A 1 75  ? -9.65700  -15.11400 32.05000 1.000 39.42724 ?  55  ASP A CG  1 
ATOM   324  O OD1 . ASP A 1 75  ? -9.01500  -14.16000 31.54200 1.000 42.08883 ?  55  ASP A OD1 1 
ATOM   325  O OD2 . ASP A 1 75  ? -10.11300 -16.07000 31.37400 1.000 44.49437 -1 55  ASP A OD2 1 
ATOM   326  N N   . LEU A 1 76  ? -10.81200 -11.65200 33.25200 1.000 27.80512 ?  56  LEU A N   1 
ATOM   327  C CA  . LEU A 1 76  ? -11.72700 -10.72500 32.60500 1.000 29.18025 ?  56  LEU A CA  1 
ATOM   328  C C   . LEU A 1 76  ? -11.48900 -10.72100 31.10300 1.000 33.51717 ?  56  LEU A C   1 
ATOM   329  O O   . LEU A 1 76  ? -10.34400 -10.66800 30.64200 1.000 32.89761 ?  56  LEU A O   1 
ATOM   330  C CB  . LEU A 1 76  ? -11.55000 -9.31400  33.15800 1.000 32.74126 ?  56  LEU A CB  1 
ATOM   331  C CG  . LEU A 1 76  ? -11.96800 -9.12200  34.60400 1.000 34.27335 ?  56  LEU A CG  1 
ATOM   332  C CD1 . LEU A 1 76  ? -11.38800 -7.81900  35.12600 1.000 37.11868 ?  56  LEU A CD1 1 
ATOM   333  C CD2 . LEU A 1 76  ? -13.47800 -9.12200  34.69900 1.000 35.66064 ?  56  LEU A CD2 1 
ATOM   334  N N   . GLY A 1 77  ? -12.57700 -10.74600 30.34400 1.000 29.34212 ?  57  GLY A N   1 
ATOM   335  C CA  . GLY A 1 77  ? -12.46200 -10.99900 28.92100 1.000 33.00306 ?  57  GLY A CA  1 
ATOM   336  C C   . GLY A 1 77  ? -12.12300 -12.44700 28.65100 1.000 30.98661 ?  57  GLY A C   1 
ATOM   337  O O   . GLY A 1 77  ? -11.27900 -12.73500 27.79200 1.000 36.25473 ?  57  GLY A O   1 
ATOM   338  N N   . CYS A 1 78  ? -12.75500 -13.36900 29.38200 1.000 30.61138 ?  58  CYS A N   1 
ATOM   339  C CA  . CYS A 1 78  ? -12.43700 -14.78500 29.25500 1.000 33.90219 ?  58  CYS A CA  1 
ATOM   340  C C   . CYS A 1 78  ? -12.90100 -15.37300 27.93000 1.000 28.97252 ?  58  CYS A C   1 
ATOM   341  O O   . CYS A 1 78  ? -12.40800 -16.43600 27.53700 1.000 36.12774 ?  58  CYS A O   1 
ATOM   342  C CB  . CYS A 1 78  ? -13.05800 -15.56700 30.41300 1.000 32.58351 ?  58  CYS A CB  1 
ATOM   343  S SG  . CYS A 1 78  ? -14.86700 -15.57400 30.42600 1.000 30.84872 ?  58  CYS A SG  1 
ATOM   344  N N   . ALA A 1 79  ? -13.82700 -14.71000 27.24100 1.000 31.29194 ?  59  ALA A N   1 
ATOM   345  C CA  . ALA A 1 79  ? -14.36100 -15.19500 25.97600 1.000 32.13413 ?  59  ALA A CA  1 
ATOM   346  C C   . ALA A 1 79  ? -14.84400 -16.63300 26.12200 1.000 34.75486 ?  59  ALA A C   1 
ATOM   347  O O   . ALA A 1 79  ? -15.75700 -16.90400 26.90900 1.000 34.57196 ?  59  ALA A O   1 
ATOM   348  C CB  . ALA A 1 79  ? -13.31200 -15.07600 24.86800 1.000 37.38612 ?  59  ALA A CB  1 
ATOM   349  N N   . THR A 1 80  ? -14.22500 -17.56500 25.39700 1.000 27.16745 ?  60  THR A N   1 
ATOM   350  C CA  . THR A 1 80  ? -14.66700 -18.95400 25.39900 1.000 27.77341 ?  60  THR A CA  1 
ATOM   351  C C   . THR A 1 80  ? -14.02000 -19.78500 26.50500 1.000 33.58884 ?  60  THR A C   1 
ATOM   352  O O   . THR A 1 80  ? -14.20700 -21.00700 26.53000 1.000 30.77483 ?  60  THR A O   1 
ATOM   353  C CB  . THR A 1 80  ? -14.39900 -19.60400 24.03300 1.000 29.68377 ?  60  THR A CB  1 
ATOM   354  O OG1 . THR A 1 80  ? -13.14400 -19.14900 23.51900 1.000 36.47319 ?  60  THR A OG1 1 
ATOM   355  C CG2 . THR A 1 80  ? -15.49100 -19.21100 23.04700 1.000 32.95693 ?  60  THR A CG2 1 
ATOM   356  N N   . GLY A 1 81  ? -13.24900 -19.16000 27.40000 1.000 33.15829 ?  61  GLY A N   1 
ATOM   357  C CA  . GLY A 1 81  ? -12.91500 -19.74700 28.68300 1.000 29.33003 ?  61  GLY A CA  1 
ATOM   358  C C   . GLY A 1 81  ? -11.55400 -20.39900 28.82400 1.000 28.43063 ?  61  GLY A C   1 
ATOM   359  O O   . GLY A 1 81  ? -11.25200 -20.90500 29.91100 1.000 30.03630 ?  61  GLY A O   1 
ATOM   360  N N   . ARG A 1 82  ? -10.71600 -20.39500 27.78300 1.000 29.94040 ?  62  ARG A N   1 
ATOM   361  C CA  . ARG A 1 82  ? -9.48500  -21.18200 27.83100 1.000 32.42166 ?  62  ARG A CA  1 
ATOM   362  C C   . ARG A 1 82  ? -8.56800  -20.72800 28.96300 1.000 28.39531 ?  62  ARG A C   1 
ATOM   363  O O   . ARG A 1 82  ? -8.05800  -21.55400 29.72900 1.000 30.35625 ?  62  ARG A O   1 
ATOM   364  C CB  . ARG A 1 82  ? -8.75700  -21.11400 26.49200 1.000 28.46896 ?  62  ARG A CB  1 
ATOM   365  C CG  . ARG A 1 82  ? -7.49200  -21.95800 26.45700 1.000 29.10354 ?  62  ARG A CG  1 
ATOM   366  C CD  . ARG A 1 82  ? -7.78500  -23.43200 26.67400 1.000 31.84806 ?  62  ARG A CD  1 
ATOM   367  N NE  . ARG A 1 82  ? -6.56100  -24.21100 26.82800 1.000 29.17695 ?  62  ARG A NE  1 
ATOM   368  C CZ  . ARG A 1 82  ? -5.86800  -24.71900 25.81800 1.000 32.42140 ?  62  ARG A CZ  1 
ATOM   369  N NH1 . ARG A 1 82  ? -6.23900  -24.52600 24.56100 1.000 31.95686 ?  62  ARG A NH1 1 
ATOM   370  N NH2 . ARG A 1 82  ? -4.78000  -25.44300 26.07500 1.000 33.42009 ?  62  ARG A NH2 1 
ATOM   371  N N   . ALA A 1 83  ? -8.35300  -19.41600 29.09000 1.000 25.41759 ?  63  ALA A N   1 
ATOM   372  C CA  . ALA A 1 83  ? -7.44500  -18.91400 30.11800 1.000 28.99059 ?  63  ALA A CA  1 
ATOM   373  C C   . ALA A 1 83  ? -7.94200  -19.25000 31.51900 1.000 30.90097 ?  63  ALA A C   1 
ATOM   374  O O   . ALA A 1 83  ? -7.13500  -19.53200 32.41300 1.000 30.80955 ?  63  ALA A O   1 
ATOM   375  C CB  . ALA A 1 83  ? -7.25100  -17.40200 29.96500 1.000 26.49603 ?  63  ALA A CB  1 
ATOM   376  N N   . SER A 1 84  ? -9.26400  -19.23200 31.73100 1.000 28.21893 ?  64  SER A N   1 
ATOM   377  C CA  . SER A 1 84  ? -9.80700  -19.59500 33.03800 1.000 29.09886 ?  64  SER A CA  1 
ATOM   378  C C   . SER A 1 84  ? -9.53100  -21.05700 33.36500 1.000 30.67773 ?  64  SER A C   1 
ATOM   379  O O   . SER A 1 84  ? -9.12500  -21.38000 34.48700 1.000 29.49850 ?  64  SER A O   1 
ATOM   380  C CB  . SER A 1 84  ? -11.31200 -19.31700 33.09400 1.000 27.07697 ?  64  SER A CB  1 
ATOM   381  O OG  . SER A 1 84  ? -11.62500 -18.02100 32.61600 1.000 33.19618 ?  64  SER A OG  1 
ATOM   382  N N   . PHE A 1 85  ? -9.75800  -21.95300 32.39800 1.000 28.93983 ?  65  PHE A N   1 
ATOM   383  C CA  . PHE A 1 85  ? -9.47700  -23.37100 32.60700 1.000 25.47140 ?  65  PHE A CA  1 
ATOM   384  C C   . PHE A 1 85  ? -8.00800  -23.59900 32.93000 1.000 27.03314 ?  65  PHE A C   1 
ATOM   385  O O   . PHE A 1 85  ? -7.67300  -24.42100 33.78800 1.000 31.69464 ?  65  PHE A O   1 
ATOM   386  C CB  . PHE A 1 85  ? -9.86000  -24.17700 31.36500 1.000 25.54543 ?  65  PHE A CB  1 
ATOM   387  C CG  . PHE A 1 85  ? -11.33900 -24.27100 31.12000 1.000 27.82445 ?  65  PHE A CG  1 
ATOM   388  C CD1 . PHE A 1 85  ? -12.20700 -24.61300 32.14200 1.000 24.74920 ?  65  PHE A CD1 1 
ATOM   389  C CD2 . PHE A 1 85  ? -11.85700 -24.03100 29.85900 1.000 27.60394 ?  65  PHE A CD2 1 
ATOM   390  C CE1 . PHE A 1 85  ? -13.55900 -24.70800 31.91600 1.000 23.74003 ?  65  PHE A CE1 1 
ATOM   391  C CE2 . PHE A 1 85  ? -13.21400 -24.12400 29.62200 1.000 28.33925 ?  65  PHE A CE2 1 
ATOM   392  C CZ  . PHE A 1 85  ? -14.06700 -24.46300 30.65600 1.000 27.98108 ?  65  PHE A CZ  1 
ATOM   393  N N   . GLU A 1 86  ? -7.11500  -22.87700 32.25100 1.000 30.41562 ?  66  GLU A N   1 
ATOM   394  C CA  . GLU A 1 86  ? -5.68700  -23.07400 32.47400 1.000 31.77050 ?  66  GLU A CA  1 
ATOM   395  C C   . GLU A 1 86  ? -5.25200  -22.50400 33.81500 1.000 31.36819 ?  66  GLU A C   1 
ATOM   396  O O   . GLU A 1 86  ? -4.39300  -23.08100 34.48900 1.000 32.70184 ?  66  GLU A O   1 
ATOM   397  C CB  . GLU A 1 86  ? -4.88500  -22.43600 31.34100 1.000 31.95182 ?  66  GLU A CB  1 
ATOM   398  C CG  . GLU A 1 86  ? -5.13600  -23.04500 29.97300 1.000 34.78665 ?  66  GLU A CG  1 
ATOM   399  C CD  . GLU A 1 86  ? -4.62100  -24.46900 29.86300 1.000 38.85967 ?  66  GLU A CD  1 
ATOM   400  O OE1 . GLU A 1 86  ? -3.80100  -24.88500 30.71400 1.000 37.08058 ?  66  GLU A OE1 1 
ATOM   401  O OE2 . GLU A 1 86  ? -5.03100  -25.16900 28.91200 1.000 35.97189 -1 66  GLU A OE2 1 
ATOM   402  N N   . LEU A 1 87  ? -5.81800  -21.36100 34.20800 1.000 33.51444 ?  67  LEU A N   1 
ATOM   403  C CA  . LEU A 1 87  ? -5.50200  -20.80000 35.51600 1.000 29.72168 ?  67  LEU A CA  1 
ATOM   404  C C   . LEU A 1 87  ? -5.95900  -21.73000 36.62700 1.000 31.22601 ?  67  LEU A C   1 
ATOM   405  O O   . LEU A 1 87  ? -5.33700  -21.78800 37.69500 1.000 31.15925 ?  67  LEU A O   1 
ATOM   406  C CB  . LEU A 1 87  ? -6.15400  -19.42700 35.67000 1.000 28.47532 ?  67  LEU A CB  1 
ATOM   407  C CG  . LEU A 1 87  ? -5.47900  -18.23700 34.99300 1.000 35.05097 ?  67  LEU A CG  1 
ATOM   408  C CD1 . LEU A 1 87  ? -6.33300  -16.99400 35.20000 1.000 29.96948 ?  67  LEU A CD1 1 
ATOM   409  C CD2 . LEU A 1 87  ? -4.08000  -18.01800 35.54000 1.000 32.47586 ?  67  LEU A CD2 1 
ATOM   410  N N   . ALA A 1 88  ? -7.04500  -22.47000 36.38600 1.000 30.92978 ?  68  ALA A N   1 
ATOM   411  C CA  . ALA A 1 88  ? -7.60300  -23.35000 37.40400 1.000 30.67193 ?  68  ALA A CA  1 
ATOM   412  C C   . ALA A 1 88  ? -6.68200  -24.51600 37.72800 1.000 31.24935 ?  68  ALA A C   1 
ATOM   413  O O   . ALA A 1 88  ? -6.83700  -25.13700 38.78100 1.000 35.15429 ?  68  ALA A O   1 
ATOM   414  C CB  . ALA A 1 88  ? -8.96200  -23.87400 36.95300 1.000 28.90436 ?  68  ALA A CB  1 
ATOM   415  N N   . ARG A 1 89  ? -5.73700  -24.84000 36.84700 1.000 33.21748 ?  69  ARG A N   1 
ATOM   416  C CA  . ARG A 1 89  ? -4.79000  -25.90000 37.15700 1.000 33.06162 ?  69  ARG A CA  1 
ATOM   417  C C   . ARG A 1 89  ? -3.87300  -25.51000 38.30500 1.000 36.93067 ?  69  ARG A C   1 
ATOM   418  O O   . ARG A 1 89  ? -3.35400  -26.38800 38.99900 1.000 39.75318 ?  69  ARG A O   1 
ATOM   419  C CB  . ARG A 1 89  ? -3.96900  -26.25100 35.91600 1.000 35.78629 ?  69  ARG A CB  1 
ATOM   420  C CG  . ARG A 1 89  ? -4.81800  -26.55000 34.68600 1.000 32.44573 ?  69  ARG A CG  1 
ATOM   421  C CD  . ARG A 1 89  ? -4.02100  -27.31400 33.64200 1.000 34.22285 ?  69  ARG A CD  1 
ATOM   422  N NE  . ARG A 1 89  ? -3.72000  -28.67200 34.07500 1.000 39.79033 ?  69  ARG A NE  1 
ATOM   423  C CZ  . ARG A 1 89  ? -2.65500  -29.36300 33.69300 1.000 37.61404 ?  69  ARG A CZ  1 
ATOM   424  N NH1 . ARG A 1 89  ? -1.74900  -28.84500 32.87800 1.000 31.53872 ?  69  ARG A NH1 1 
ATOM   425  N NH2 . ARG A 1 89  ? -2.49800  -30.60800 34.13400 1.000 33.94784 ?  69  ARG A NH2 1 
ATOM   426  N N   . SER A 1 90  ? -3.68200  -24.21300 38.53200 1.000 37.32272 ?  70  SER A N   1 
ATOM   427  C CA  . SER A 1 90  ? -2.82700  -23.73800 39.60500 1.000 36.89835 ?  70  SER A CA  1 
ATOM   428  C C   . SER A 1 90  ? -3.57200  -23.02000 40.72000 1.000 32.44957 ?  70  SER A C   1 
ATOM   429  O O   . SER A 1 90  ? -3.06000  -22.97500 41.84100 1.000 38.88364 ?  70  SER A O   1 
ATOM   430  C CB  . SER A 1 90  ? -1.74000  -22.80800 39.04300 1.000 36.44047 ?  70  SER A CB  1 
ATOM   431  O OG  . SER A 1 90  ? -0.86000  -23.53900 38.20000 1.000 48.23533 ?  70  SER A OG  1 
ATOM   432  N N   . TYR A 1 91  ? -4.76000  -22.48100 40.46300 1.000 31.33355 ?  71  TYR A N   1 
ATOM   433  C CA  . TYR A 1 91  ? -5.52500  -21.76300 41.47300 1.000 27.59408 ?  71  TYR A CA  1 
ATOM   434  C C   . TYR A 1 91  ? -6.65600  -22.63600 42.00600 1.000 36.83489 ?  71  TYR A C   1 
ATOM   435  O O   . TYR A 1 91  ? -7.10300  -23.58300 41.35300 1.000 37.30818 ?  71  TYR A O   1 
ATOM   436  C CB  . TYR A 1 91  ? -6.09600  -20.45900 40.90400 1.000 35.80813 ?  71  TYR A CB  1 
ATOM   437  C CG  . TYR A 1 91  ? -5.07700  -19.34800 40.82600 1.000 33.97497 ?  71  TYR A CG  1 
ATOM   438  C CD1 . TYR A 1 91  ? -4.04100  -19.39900 39.90300 1.000 32.91790 ?  71  TYR A CD1 1 
ATOM   439  C CD2 . TYR A 1 91  ? -5.13200  -18.26400 41.69000 1.000 32.27094 ?  71  TYR A CD2 1 
ATOM   440  C CE1 . TYR A 1 91  ? -3.09800  -18.39700 39.83100 1.000 33.78039 ?  71  TYR A CE1 1 
ATOM   441  C CE2 . TYR A 1 91  ? -4.19100  -17.25100 41.62600 1.000 33.46134 ?  71  TYR A CE2 1 
ATOM   442  C CZ  . TYR A 1 91  ? -3.17400  -17.32600 40.69800 1.000 37.42451 ?  71  TYR A CZ  1 
ATOM   443  O OH  . TYR A 1 91  ? -2.22900  -16.32800 40.62700 1.000 38.06532 ?  71  TYR A OH  1 
ATOM   444  N N   . LYS A 1 92  ? -7.11600  -22.30400 43.21700 1.000 32.93536 ?  72  LYS A N   1 
ATOM   445  C CA  . LYS A 1 92  ? -8.20800  -23.06200 43.81800 1.000 33.66662 ?  72  LYS A CA  1 
ATOM   446  C C   . LYS A 1 92  ? -9.56400  -22.65800 43.25700 1.000 35.06048 ?  72  LYS A C   1 
ATOM   447  O O   . LYS A 1 92  ? -10.47600 -23.49000 43.18800 1.000 38.25850 ?  72  LYS A O   1 
ATOM   448  C CB  . LYS A 1 92  ? -8.20500  -22.89400 45.33700 1.000 34.74464 ?  72  LYS A CB  1 
ATOM   449  C CG  . LYS A 1 92  ? -6.83700  -23.04400 45.97500 1.000 35.21184 ?  72  LYS A CG  1 
ATOM   450  C CD  . LYS A 1 92  ? -6.95800  -23.27500 47.47200 1.000 36.89259 ?  72  LYS A CD  1 
ATOM   451  N N   . HIS A 1 93  ? -9.71800  -21.39900 42.86100 1.000 31.71178 ?  73  HIS A N   1 
ATOM   452  C CA  . HIS A 1 93  ? -10.94900 -20.92600 42.25100 1.000 36.45878 ?  73  HIS A CA  1 
ATOM   453  C C   . HIS A 1 93  ? -10.62100 -19.88900 41.19400 1.000 37.64504 ?  73  HIS A C   1 
ATOM   454  O O   . HIS A 1 93  ? -9.77700  -19.01500 41.41200 1.000 34.53163 ?  73  HIS A O   1 
ATOM   455  C CB  . HIS A 1 93  ? -11.90300 -20.30500 43.27100 1.000 36.88227 ?  73  HIS A CB  1 
ATOM   456  C CG  . HIS A 1 93  ? -13.19800 -19.85800 42.67100 1.000 41.69459 ?  73  HIS A CG  1 
ATOM   457  N ND1 . HIS A 1 93  ? -14.09400 -20.73600 42.09700 1.000 37.63506 ?  73  HIS A ND1 1 
ATOM   458  C CD2 . HIS A 1 93  ? -13.72800 -18.62200 42.51200 1.000 35.86310 ?  73  HIS A CD2 1 
ATOM   459  C CE1 . HIS A 1 93  ? -15.13300 -20.06200 41.63700 1.000 30.85977 ?  73  HIS A CE1 1 
ATOM   460  N NE2 . HIS A 1 93  ? -14.93500 -18.77700 41.87300 1.000 40.43368 ?  73  HIS A NE2 1 
ATOM   461  N N   . VAL A 1 94  ? -11.29400 -19.98800 40.05300 1.000 33.34718 ?  74  VAL A N   1 
ATOM   462  C CA  . VAL A 1 94  ? -11.14000 -19.02900 38.97000 1.000 31.77848 ?  74  VAL A CA  1 
ATOM   463  C C   . VAL A 1 94  ? -12.52200 -18.55100 38.55500 1.000 31.81838 ?  74  VAL A C   1 
ATOM   464  O O   . VAL A 1 94  ? -13.40600 -19.36600 38.27100 1.000 32.89666 ?  74  VAL A O   1 
ATOM   465  C CB  . VAL A 1 94  ? -10.38800 -19.63100 37.76800 1.000 29.43833 ?  74  VAL A CB  1 
ATOM   466  C CG1 . VAL A 1 94  ? -10.22600 -18.58900 36.67400 1.000 30.22172 ?  74  VAL A CG1 1 
ATOM   467  C CG2 . VAL A 1 94  ? -9.03200  -20.15000 38.20600 1.000 31.03639 ?  74  VAL A CG2 1 
ATOM   468  N N   . ASP A 1 95  ? -12.71200 -17.23500 38.53600 1.000 30.16742 ?  75  ASP A N   1 
ATOM   469  C CA  . ASP A 1 95  ? -13.90900 -16.62800 37.97500 1.000 29.26230 ?  75  ASP A CA  1 
ATOM   470  C C   . ASP A 1 95  ? -13.58100 -16.14700 36.57100 1.000 31.71211 ?  75  ASP A C   1 
ATOM   471  O O   . ASP A 1 95  ? -12.64900 -15.36200 36.37800 1.000 29.85322 ?  75  ASP A O   1 
ATOM   472  C CB  . ASP A 1 95  ? -14.39700 -15.46400 38.83600 1.000 29.65909 ?  75  ASP A CB  1 
ATOM   473  C CG  . ASP A 1 95  ? -14.94500 -15.91600 40.17500 1.000 36.01294 ?  75  ASP A CG  1 
ATOM   474  O OD1 . ASP A 1 95  ? -15.71800 -16.89600 40.21100 1.000 38.08511 ?  75  ASP A OD1 1 
ATOM   475  O OD2 . ASP A 1 95  ? -14.61700 -15.27500 41.19500 1.000 40.36777 -1 75  ASP A OD2 1 
ATOM   476  N N   . GLY A 1 96  ? -14.33700 -16.63800 35.58100 1.000 28.47680 ?  76  GLY A N   1 
ATOM   477  C CA  . GLY A 1 96  ? -14.23000 -16.15100 34.22100 1.000 27.82208 ?  76  GLY A CA  1 
ATOM   478  C C   . GLY A 1 96  ? -15.39000 -15.22000 33.92200 1.000 29.99435 ?  76  GLY A C   1 
ATOM   479  O O   . GLY A 1 96  ? -16.55300 -15.57400 34.12500 1.000 31.75696 ?  76  GLY A O   1 
ATOM   480  N N   . VAL A 1 97  ? -15.06000 -14.02100 33.45100 1.000 28.67424 ?  77  VAL A N   1 
ATOM   481  C CA  . VAL A 1 97  ? -16.04900 -12.98000 33.20300 1.000 27.06295 ?  77  VAL A CA  1 
ATOM   482  C C   . VAL A 1 97  ? -15.88800 -12.47800 31.77600 1.000 28.74974 ?  77  VAL A C   1 
ATOM   483  O O   . VAL A 1 97  ? -14.77000 -12.20400 31.32600 1.000 30.02960 ?  77  VAL A O   1 
ATOM   484  C CB  . VAL A 1 97  ? -15.91100 -11.81900 34.21400 1.000 34.66840 ?  77  VAL A CB  1 
ATOM   485  C CG1 . VAL A 1 97  ? -16.92500 -10.73100 33.92200 1.000 32.16919 ?  77  VAL A CG1 1 
ATOM   486  C CG2 . VAL A 1 97  ? -16.07300 -12.32800 35.64200 1.000 26.18883 ?  77  VAL A CG2 1 
ATOM   487  N N   . ASP A 1 98  ? -17.00500 -12.36200 31.06100 1.000 32.37775 ?  78  ASP A N   1 
ATOM   488  C CA  . ASP A 1 98  ? -17.00400 -11.73900 29.74600 1.000 34.77533 ?  78  ASP A CA  1 
ATOM   489  C C   . ASP A 1 98  ? -18.25900 -10.89500 29.58900 1.000 34.28938 ?  78  ASP A C   1 
ATOM   490  O O   . ASP A 1 98  ? -19.28800 -11.16400 30.21100 1.000 36.83712 ?  78  ASP A O   1 
ATOM   491  C CB  . ASP A 1 98  ? -16.92600 -12.76800 28.61300 1.000 31.71552 ?  78  ASP A CB  1 
ATOM   492  C CG  . ASP A 1 98  ? -16.42300 -12.16000 27.31900 1.000 43.33753 ?  78  ASP A CG  1 
ATOM   493  O OD1 . ASP A 1 98  ? -17.25700 -11.64200 26.53700 1.000 41.66062 ?  78  ASP A OD1 1 
ATOM   494  O OD2 . ASP A 1 98  ? -15.19000 -12.18100 27.09400 1.000 37.61046 -1 78  ASP A OD2 1 
ATOM   495  N N   . TYR A 1 99  ? -18.16900 -9.86800  28.74300 1.000 38.70471 ?  79  TYR A N   1 
ATOM   496  C CA  . TYR A 1 99  ? -19.32200 -8.99700  28.54400 1.000 36.84501 ?  79  TYR A CA  1 
ATOM   497  C C   . TYR A 1 99  ? -20.41500 -9.68500  27.73600 1.000 38.75202 ?  79  TYR A C   1 
ATOM   498  O O   . TYR A 1 99  ? -21.60300 -9.44600  27.97500 1.000 39.37746 ?  79  TYR A O   1 
ATOM   499  C CB  . TYR A 1 99  ? -18.89100 -7.69800  27.86700 1.000 37.87699 ?  79  TYR A CB  1 
ATOM   500  C CG  . TYR A 1 99  ? -20.01700 -6.70100  27.70600 1.000 42.93716 ?  79  TYR A CG  1 
ATOM   501  C CD1 . TYR A 1 99  ? -20.51800 -6.00500  28.80200 1.000 45.50422 ?  79  TYR A CD1 1 
ATOM   502  C CD2 . TYR A 1 99  ? -20.57100 -6.44500  26.45700 1.000 46.41196 ?  79  TYR A CD2 1 
ATOM   503  C CE1 . TYR A 1 99  ? -21.55100 -5.08800  28.65900 1.000 51.08667 ?  79  TYR A CE1 1 
ATOM   504  C CE2 . TYR A 1 99  ? -21.60200 -5.53400  26.30300 1.000 53.32378 ?  79  TYR A CE2 1 
ATOM   505  C CZ  . TYR A 1 99  ? -22.08900 -4.85700  27.40500 1.000 54.54496 ?  79  TYR A CZ  1 
ATOM   506  O OH  . TYR A 1 99  ? -23.11400 -3.94900  27.24500 1.000 66.60631 ?  79  TYR A OH  1 
ATOM   507  N N   . SER A 1 100 ? -20.04100 -10.54300 26.79200 1.000 36.52625 ?  80  SER A N   1 
ATOM   508  C CA  . SER A 1 100 ? -21.00000 -11.19100 25.90700 1.000 34.82989 ?  80  SER A CA  1 
ATOM   509  C C   . SER A 1 100 ? -21.53300 -12.46400 26.55800 1.000 37.53530 ?  80  SER A C   1 
ATOM   510  O O   . SER A 1 100 ? -20.75900 -13.37100 26.89100 1.000 39.49199 ?  80  SER A O   1 
ATOM   511  C CB  . SER A 1 100 ? -20.35000 -11.50000 24.56000 1.000 39.32321 ?  80  SER A CB  1 
ATOM   512  O OG  . SER A 1 100 ? -20.97500 -12.60400 23.92900 1.000 45.88407 ?  80  SER A OG  1 
ATOM   513  N N   . GLN A 1 101 ? -22.85400 -12.52800 26.74200 1.000 28.57479 ?  81  GLN A N   1 
ATOM   514  C CA  . GLN A 1 101 ? -23.46800 -13.74100 27.26300 1.000 36.77598 ?  81  GLN A CA  1 
ATOM   515  C C   . GLN A 1 101 ? -23.20600 -14.92900 26.34800 1.000 36.68372 ?  81  GLN A C   1 
ATOM   516  O O   . GLN A 1 101 ? -23.07400 -16.06300 26.82400 1.000 35.87267 ?  81  GLN A O   1 
ATOM   517  C CB  . GLN A 1 101 ? -24.97100 -13.52500 27.45000 1.000 37.48208 ?  81  GLN A CB  1 
ATOM   518  C CG  . GLN A 1 101 ? -25.68700 -14.68000 28.12500 1.000 35.51420 ?  81  GLN A CG  1 
ATOM   519  C CD  . GLN A 1 101 ? -25.21700 -14.89100 29.54600 1.000 37.52202 ?  81  GLN A CD  1 
ATOM   520  O OE1 . GLN A 1 101 ? -25.27600 -13.98000 30.37100 1.000 42.04566 ?  81  GLN A OE1 1 
ATOM   521  N NE2 . GLN A 1 101 ? -24.75000 -16.09800 29.84100 1.000 39.63145 ?  81  GLN A NE2 1 
ATOM   522  N N   . ALA A 1 102 ? -23.10600 -14.68200 25.03900 1.000 35.95530 ?  82  ALA A N   1 
ATOM   523  C CA  . ALA A 1 102 ? -22.88900 -15.76700 24.08800 1.000 36.43916 ?  82  ALA A CA  1 
ATOM   524  C C   . ALA A 1 102 ? -21.54800 -16.45300 24.31800 1.000 37.52483 ?  82  ALA A C   1 
ATOM   525  O O   . ALA A 1 102 ? -21.43300 -17.67400 24.16400 1.000 38.92170 ?  82  ALA A O   1 
ATOM   526  C CB  . ALA A 1 102 ? -22.98500 -15.23300 22.66200 1.000 28.04961 ?  82  ALA A CB  1 
ATOM   527  N N   . PHE A 1 103 ? -20.51600 -15.68400 24.67400 1.000 34.99029 ?  83  PHE A N   1 
ATOM   528  C CA  . PHE A 1 103 ? -19.22500 -16.28900 24.98300 1.000 36.30898 ?  83  PHE A CA  1 
ATOM   529  C C   . PHE A 1 103 ? -19.27800 -17.04300 26.30300 1.000 31.91182 ?  83  PHE A C   1 
ATOM   530  O O   . PHE A 1 103 ? -18.66000 -18.10500 26.44400 1.000 33.66966 ?  83  PHE A O   1 
ATOM   531  C CB  . PHE A 1 103 ? -18.13700 -15.21800 25.02200 1.000 34.00488 ?  83  PHE A CB  1 
ATOM   532  C CG  . PHE A 1 103 ? -17.70300 -14.75800 23.67100 1.000 36.15116 ?  83  PHE A CG  1 
ATOM   533  C CD1 . PHE A 1 103 ? -18.42400 -13.79900 22.99200 1.000 48.55352 ?  83  PHE A CD1 1 
ATOM   534  C CD2 . PHE A 1 103 ? -16.58700 -15.29500 23.06900 1.000 39.61071 ?  83  PHE A CD2 1 
ATOM   535  C CE1 . PHE A 1 103 ? -18.03700 -13.37200 21.74200 1.000 47.42774 ?  83  PHE A CE1 1 
ATOM   536  C CE2 . PHE A 1 103 ? -16.19500 -14.86800 21.81800 1.000 43.26761 ?  83  PHE A CE2 1 
ATOM   537  C CZ  . PHE A 1 103 ? -16.91800 -13.90800 21.15500 1.000 36.66966 ?  83  PHE A CZ  1 
ATOM   538  N N   . VAL A 1 104 ? -20.01300 -16.50800 27.28100 1.000 34.32143 ?  84  VAL A N   1 
ATOM   539  C CA  . VAL A 1 104 ? -20.17200 -17.19400 28.56000 1.000 33.54960 ?  84  VAL A CA  1 
ATOM   540  C C   . VAL A 1 104 ? -20.87800 -18.52700 28.36500 1.000 35.45528 ?  84  VAL A C   1 
ATOM   541  O O   . VAL A 1 104 ? -20.50200 -19.54000 28.97100 1.000 34.20824 ?  84  VAL A O   1 
ATOM   542  C CB  . VAL A 1 104 ? -20.93100 -16.29700 29.55500 1.000 33.26693 ?  84  VAL A CB  1 
ATOM   543  C CG1 . VAL A 1 104 ? -21.26300 -17.07400 30.82700 1.000 32.39717 ?  84  VAL A CG1 1 
ATOM   544  C CG2 . VAL A 1 104 ? -20.12000 -15.04900 29.88200 1.000 32.75302 ?  84  VAL A CG2 1 
ATOM   545  N N   . ASP A 1 105 ? -21.91700 -18.54900 27.52400 1.000 31.03790 ?  85  ASP A N   1 
ATOM   546  C CA  . ASP A 1 105 ? -22.65800 -19.78600 27.29500 1.000 33.19668 ?  85  ASP A CA  1 
ATOM   547  C C   . ASP A 1 105 ? -21.76800 -20.85300 26.67900 1.000 27.40372 ?  85  ASP A C   1 
ATOM   548  O O   . ASP A 1 105 ? -21.81900 -22.01900 27.08200 1.000 28.75397 ?  85  ASP A O   1 
ATOM   549  C CB  . ASP A 1 105 ? -23.86700 -19.52200 26.39700 1.000 32.36484 ?  85  ASP A CB  1 
ATOM   550  C CG  . ASP A 1 105 ? -24.84800 -18.55300 27.01900 1.000 42.47670 ?  85  ASP A CG  1 
ATOM   551  O OD1 . ASP A 1 105 ? -24.82800 -18.40900 28.26100 1.000 46.33682 ?  85  ASP A OD1 1 
ATOM   552  O OD2 . ASP A 1 105 ? -25.63400 -17.93100 26.27300 1.000 47.63053 -1 85  ASP A OD2 1 
ATOM   553  N N   . ALA A 1 106 ? -20.94400 -20.46800 25.70000 1.000 27.79632 ?  86  ALA A N   1 
ATOM   554  C CA  . ALA A 1 106 ? -20.03500 -21.42200 25.07200 1.000 29.12860 ?  86  ALA A CA  1 
ATOM   555  C C   . ALA A 1 106 ? -19.05600 -21.99500 26.08700 1.000 29.84146 ?  86  ALA A C   1 
ATOM   556  O O   . ALA A 1 106 ? -18.82500 -23.20900 26.12000 1.000 32.51363 ?  86  ALA A O   1 
ATOM   557  C CB  . ALA A 1 106 ? -19.28700 -20.75400 23.91900 1.000 28.50241 ?  86  ALA A CB  1 
ATOM   558  N N   . ALA A 1 107 ? -18.48000 -21.13700 26.93200 1.000 29.23447 ?  87  ALA A N   1 
ATOM   559  C CA  . ALA A 1 107 ? -17.58200 -21.62000 27.97500 1.000 33.65993 ?  87  ALA A CA  1 
ATOM   560  C C   . ALA A 1 107 ? -18.31000 -22.55900 28.92700 1.000 31.25188 ?  87  ALA A C   1 
ATOM   561  O O   . ALA A 1 107 ? -17.80800 -23.63800 29.26100 1.000 30.22974 ?  87  ALA A O   1 
ATOM   562  C CB  . ALA A 1 107 ? -16.98200 -20.43700 28.73800 1.000 31.65169 ?  87  ALA A CB  1 
ATOM   563  N N   . THR A 1 108 ? -19.50400 -22.16000 29.37400 1.000 29.71083 ?  88  THR A N   1 
ATOM   564  C CA  . THR A 1 108 ? -20.27200 -22.99800 30.28800 1.000 27.50628 ?  88  THR A CA  1 
ATOM   565  C C   . THR A 1 108 ? -20.67800 -24.30700 29.62600 1.000 31.57730 ?  88  THR A C   1 
ATOM   566  O O   . THR A 1 108 ? -20.65300 -25.36700 30.26500 1.000 33.80894 ?  88  THR A O   1 
ATOM   567  C CB  . THR A 1 108 ? -21.49600 -22.23300 30.78800 1.000 29.09506 ?  88  THR A CB  1 
ATOM   568  O OG1 . THR A 1 108 ? -21.09500 -20.91400 31.17100 1.000 28.29448 ?  88  THR A OG1 1 
ATOM   569  C CG2 . THR A 1 108 ? -22.11700 -22.92800 31.98600 1.000 28.73008 ?  88  THR A CG2 1 
ATOM   570  N N   . GLU A 1 109 ? -21.03300 -24.25600 28.33900 1.000 27.59399 ?  89  GLU A N   1 
ATOM   571  C CA  . GLU A 1 109 ? -21.37000 -25.47400 27.60700 1.000 31.57243 ?  89  GLU A CA  1 
ATOM   572  C C   . GLU A 1 109 ? -20.20400 -26.45500 27.60600 1.000 32.21177 ?  89  GLU A C   1 
ATOM   573  O O   . GLU A 1 109 ? -20.38000 -27.64200 27.90100 1.000 34.58157 ?  89  GLU A O   1 
ATOM   574  C CB  . GLU A 1 109 ? -21.78700 -25.12800 26.17500 1.000 31.61161 ?  89  GLU A CB  1 
ATOM   575  C CG  . GLU A 1 109 ? -23.24600 -24.70900 26.04300 1.000 38.51588 ?  89  GLU A CG  1 
ATOM   576  C CD  . GLU A 1 109 ? -23.44300 -23.60300 25.01900 1.000 35.08981 ?  89  GLU A CD  1 
ATOM   577  N N   . LEU A 1 110 ? -18.99800 -25.97700 27.28100 1.000 27.71428 ?  90  LEU A N   1 
ATOM   578  C CA  . LEU A 1 110 ? -17.84000 -26.86600 27.27900 1.000 32.79779 ?  90  LEU A CA  1 
ATOM   579  C C   . LEU A 1 110 ? -17.54100 -27.37700 28.68100 1.000 32.35607 ?  90  LEU A C   1 
ATOM   580  O O   . LEU A 1 110 ? -17.18700 -28.54900 28.86000 1.000 36.34220 ?  90  LEU A O   1 
ATOM   581  C CB  . LEU A 1 110 ? -16.61800 -26.15300 26.69100 1.000 23.26493 ?  90  LEU A CB  1 
ATOM   582  C CG  . LEU A 1 110 ? -15.30900 -26.95200 26.67700 1.000 36.05127 ?  90  LEU A CG  1 
ATOM   583  C CD1 . LEU A 1 110 ? -15.41700 -28.21600 25.82700 1.000 30.36848 ?  90  LEU A CD1 1 
ATOM   584  C CD2 . LEU A 1 110 ? -14.15500 -26.08100 26.19800 1.000 32.45370 ?  90  LEU A CD2 1 
ATOM   585  N N   . GLN A 1 111 ? -17.68400 -26.51500 29.68600 1.000 32.99848 ?  91  GLN A N   1 
ATOM   586  C CA  . GLN A 1 111 ? -17.47500 -26.93800 31.06500 1.000 33.31361 ?  91  GLN A CA  1 
ATOM   587  C C   . GLN A 1 111 ? -18.46900 -28.02200 31.46000 1.000 34.37143 ?  91  GLN A C   1 
ATOM   588  O O   . GLN A 1 111 ? -18.08300 -29.08200 31.96600 1.000 36.43880 ?  91  GLN A O   1 
ATOM   589  C CB  . GLN A 1 111 ? -17.59100 -25.72800 31.98800 1.000 28.84880 ?  91  GLN A CB  1 
ATOM   590  C CG  . GLN A 1 111 ? -17.40200 -26.02000 33.45700 1.000 28.38051 ?  91  GLN A CG  1 
ATOM   591  C CD  . GLN A 1 111 ? -17.53200 -24.76200 34.28500 1.000 32.55074 ?  91  GLN A CD  1 
ATOM   592  O OE1 . GLN A 1 111 ? -18.49000 -24.00100 34.13300 1.000 32.97780 ?  91  GLN A OE1 1 
ATOM   593  N NE2 . GLN A 1 111 ? -16.56300 -24.52500 35.15600 1.000 31.93128 ?  91  GLN A NE2 1 
ATOM   594  N N   . LYS A 1 112 ? -19.75700 -27.78500 31.20800 1.000 32.70447 ?  92  LYS A N   1 
ATOM   595  C CA  . LYS A 1 112 ? -20.79300 -28.68200 31.70900 1.000 31.34350 ?  92  LYS A CA  1 
ATOM   596  C C   . LYS A 1 112 ? -20.99800 -29.88800 30.79600 1.000 32.60968 ?  92  LYS A C   1 
ATOM   597  O O   . LYS A 1 112 ? -21.03000 -31.03000 31.27100 1.000 38.78553 ?  92  LYS A O   1 
ATOM   598  C CB  . LYS A 1 112 ? -22.10500 -27.91200 31.89100 1.000 36.37148 ?  92  LYS A CB  1 
ATOM   599  N N   . ASN A 1 113 ? -21.14700 -29.66200 29.48700 1.000 32.75166 ?  93  ASN A N   1 
ATOM   600  C CA  . ASN A 1 113 ? -21.39100 -30.76900 28.56600 1.000 36.84747 ?  93  ASN A CA  1 
ATOM   601  C C   . ASN A 1 113 ? -20.13100 -31.54200 28.19900 1.000 37.60883 ?  93  ASN A C   1 
ATOM   602  O O   . ASN A 1 113 ? -20.24300 -32.64200 27.64800 1.000 37.58447 ?  93  ASN A O   1 
ATOM   603  C CB  . ASN A 1 113 ? -22.04000 -30.27400 27.27400 1.000 36.91274 ?  93  ASN A CB  1 
ATOM   604  C CG  . ASN A 1 113 ? -23.30900 -29.50200 27.51900 1.000 39.70817 ?  93  ASN A CG  1 
ATOM   605  O OD1 . ASN A 1 113 ? -23.99300 -29.71000 28.52100 1.000 43.09516 ?  93  ASN A OD1 1 
ATOM   606  N ND2 . ASN A 1 113 ? -23.64000 -28.60700 26.59600 1.000 43.56591 ?  93  ASN A ND2 1 
ATOM   607  N N   . GLY A 1 114 ? -18.94700 -30.99900 28.47100 1.000 32.74058 ?  94  GLY A N   1 
ATOM   608  C CA  . GLY A 1 114 ? -17.71500 -31.66400 28.10200 1.000 36.11098 ?  94  GLY A CA  1 
ATOM   609  C C   . GLY A 1 114 ? -17.34300 -31.56600 26.64000 1.000 40.85244 ?  94  GLY A C   1 
ATOM   610  O O   . GLY A 1 114 ? -16.29500 -32.10100 26.24600 1.000 36.87548 ?  94  GLY A O   1 
ATOM   611  N N   . CYS A 1 115 ? -18.15700 -30.90300 25.82300 1.000 36.04476 ?  95  CYS A N   1 
ATOM   612  C CA  . CYS A 1 115 ? -17.83700 -30.73700 24.41500 1.000 37.87221 ?  95  CYS A CA  1 
ATOM   613  C C   . CYS A 1 115 ? -18.64500 -29.57500 23.86600 1.000 33.36727 ?  95  CYS A C   1 
ATOM   614  O O   . CYS A 1 115 ? -19.71100 -29.23000 24.38200 1.000 36.00052 ?  95  CYS A O   1 
ATOM   615  C CB  . CYS A 1 115 ? -18.12600 -32.00900 23.60900 1.000 38.96163 ?  95  CYS A CB  1 
ATOM   616  S SG  . CYS A 1 115 ? -19.87300 -32.48000 23.60700 1.000 49.36236 ?  95  CYS A SG  1 
ATOM   617  N N   . ILE A 1 116 ? -18.12000 -28.97800 22.80500 1.000 34.29018 ?  96  ILE A N   1 
ATOM   618  C CA  . ILE A 1 116 ? -18.82300 -27.92600 22.08700 1.000 31.06466 ?  96  ILE A CA  1 
ATOM   619  C C   . ILE A 1 116 ? -18.37400 -27.99200 20.63600 1.000 33.63949 ?  96  ILE A C   1 
ATOM   620  O O   . ILE A 1 116 ? -17.24200 -28.38800 20.34000 1.000 30.80223 ?  96  ILE A O   1 
ATOM   621  C CB  . ILE A 1 116 ? -18.57000 -26.54200 22.73100 1.000 29.61412 ?  96  ILE A CB  1 
ATOM   622  C CG1 . ILE A 1 116 ? -19.59500 -25.51600 22.24500 1.000 33.64976 ?  96  ILE A CG1 1 
ATOM   623  C CG2 . ILE A 1 116 ? -17.14300 -26.07100 22.48800 1.000 28.30748 ?  96  ILE A CG2 1 
ATOM   624  N N   . GLY A 1 117 ? -19.28100 -27.65600 19.73100 1.000 35.88127 ?  97  GLY A N   1 
ATOM   625  C CA  . GLY A 1 117 ? -18.97400 -27.60200 18.31800 1.000 38.75730 ?  97  GLY A CA  1 
ATOM   626  C C   . GLY A 1 117 ? -18.80700 -26.16500 17.86300 1.000 35.56633 ?  97  GLY A C   1 
ATOM   627  O O   . GLY A 1 117 ? -19.35500 -25.24100 18.46000 1.000 35.72564 ?  97  GLY A O   1 
ATOM   628  N N   . TYR A 1 118 ? -18.02800 -25.98100 16.80100 1.000 35.35987 ?  98  TYR A N   1 
ATOM   629  C CA  . TYR A 1 118 ? -17.86300 -24.65900 16.22000 1.000 37.62891 ?  98  TYR A CA  1 
ATOM   630  C C   . TYR A 1 118 ? -17.56200 -24.80600 14.73500 1.000 35.31077 ?  98  TYR A C   1 
ATOM   631  O O   . TYR A 1 118 ? -17.11200 -25.85700 14.27100 1.000 37.22904 ?  98  TYR A O   1 
ATOM   632  C CB  . TYR A 1 118 ? -16.77900 -23.85000 16.95600 1.000 36.40461 ?  98  TYR A CB  1 
ATOM   633  C CG  . TYR A 1 118 ? -15.34000 -24.22900 16.65000 1.000 35.04221 ?  98  TYR A CG  1 
ATOM   634  C CD1 . TYR A 1 118 ? -14.65700 -23.63900 15.59500 1.000 33.86873 ?  98  TYR A CD1 1 
ATOM   635  C CD2 . TYR A 1 118 ? -14.65500 -25.14100 17.44400 1.000 32.94914 ?  98  TYR A CD2 1 
ATOM   636  C CE1 . TYR A 1 118 ? -13.34500 -23.96500 15.31900 1.000 33.31858 ?  98  TYR A CE1 1 
ATOM   637  C CE2 . TYR A 1 118 ? -13.33800 -25.47600 17.17800 1.000 37.11046 ?  98  TYR A CE2 1 
ATOM   638  C CZ  . TYR A 1 118 ? -12.68800 -24.88100 16.10900 1.000 34.47719 ?  98  TYR A CZ  1 
ATOM   639  O OH  . TYR A 1 118 ? -11.37900 -25.19800 15.82800 1.000 41.01543 ?  98  TYR A OH  1 
ATOM   640  N N   . SER A 1 119 ? -17.83500 -23.73800 13.99200 1.000 40.35638 ?  99  SER A N   1 
ATOM   641  C CA  . SER A 1 119 ? -17.65900 -23.71100 12.54500 1.000 39.89415 ?  99  SER A CA  1 
ATOM   642  C C   . SER A 1 119 ? -16.38100 -22.94500 12.22400 1.000 39.88123 ?  99  SER A C   1 
ATOM   643  O O   . SER A 1 119 ? -16.33000 -21.72000 12.36400 1.000 44.40472 ?  99  SER A O   1 
ATOM   644  C CB  . SER A 1 119 ? -18.86500 -23.06900 11.86400 1.000 34.98207 ?  99  SER A CB  1 
ATOM   645  O OG  . SER A 1 119 ? -19.99700 -23.91700 11.93400 1.000 54.12205 ?  99  SER A OG  1 
ATOM   646  N N   . GLN A 1 120 ? -15.35300 -23.66700 11.79700 1.000 37.73824 ?  100 GLN A N   1 
ATOM   647  C CA  . GLN A 1 120 ? -14.11000 -23.04100 11.37700 1.000 42.51001 ?  100 GLN A CA  1 
ATOM   648  C C   . GLN A 1 120 ? -14.27900 -22.41600 9.99800  1.000 44.12019 ?  100 GLN A C   1 
ATOM   649  O O   . GLN A 1 120 ? -14.83200 -23.03300 9.08400  1.000 46.14387 ?  100 GLN A O   1 
ATOM   650  C CB  . GLN A 1 120 ? -12.97800 -24.06600 11.35400 1.000 37.37967 ?  100 GLN A CB  1 
ATOM   651  C CG  . GLN A 1 120 ? -11.59700 -23.45000 11.40000 1.000 44.68730 ?  100 GLN A CG  1 
ATOM   652  C CD  . GLN A 1 120 ? -10.50400 -24.48000 11.23200 1.000 43.63669 ?  100 GLN A CD  1 
ATOM   653  O OE1 . GLN A 1 120 ? -10.50400 -25.25500 10.27600 1.000 46.49029 ?  100 GLN A OE1 1 
ATOM   654  N NE2 . GLN A 1 120 ? -9.56600  -24.49900 12.16800 1.000 45.53176 ?  100 GLN A NE2 1 
ATOM   655  N N   . ASN A 1 121 ? -13.80200 -21.18500 9.85300  1.000 44.96951 ?  101 ASN A N   1 
ATOM   656  C CA  . ASN A 1 121 ? -13.94000 -20.46100 8.59700  1.000 42.60591 ?  101 ASN A CA  1 
ATOM   657  C C   . ASN A 1 121 ? -12.98800 -21.01800 7.54700  1.000 40.14921 ?  101 ASN A C   1 
ATOM   658  O O   . ASN A 1 121 ? -11.81100 -21.27300 7.82700  1.000 40.53576 ?  101 ASN A O   1 
ATOM   659  C CB  . ASN A 1 121 ? -13.68400 -18.97400 8.81600  1.000 45.70328 ?  101 ASN A CB  1 
ATOM   660  C CG  . ASN A 1 121 ? -14.81900 -18.29800 9.54400  1.000 45.25495 ?  101 ASN A CG  1 
ATOM   661  O OD1 . ASN A 1 121 ? -15.93700 -18.81000 9.58200  1.000 57.00319 ?  101 ASN A OD1 1 
ATOM   662  N ND2 . ASN A 1 121 ? -14.53700 -17.14700 10.14000 1.000 59.44535 ?  101 ASN A ND2 1 
ATOM   663  N N   . GLY A 1 122 ? -13.49600 -21.19800 6.33300  1.000 40.94016 ?  102 GLY A N   1 
ATOM   664  C CA  . GLY A 1 122 ? -12.64300 -21.67000 5.23300  1.000 35.86628 ?  102 GLY A CA  1 
ATOM   665  C C   . GLY A 1 122 ? -12.54300 -20.63200 4.14000  1.000 42.63277 ?  102 GLY A C   1 
ATOM   666  O O   . GLY A 1 122 ? -12.35300 -19.46100 4.46500  1.000 42.36550 ?  102 GLY A O   1 
ATOM   667  N N   . GLU A 1 123 ? -12.67400 -21.05600 2.89000  1.000 40.26264 ?  103 GLU A N   1 
ATOM   668  C CA  . GLU A 1 123 ? -12.62800 -20.12900 1.73900  1.000 34.09274 ?  103 GLU A CA  1 
ATOM   669  C C   . GLU A 1 123 ? -13.97900 -19.43600 1.59600  1.000 41.77254 ?  103 GLU A C   1 
ATOM   670  O O   . GLU A 1 123 ? -14.98900 -20.12900 1.51700  1.000 37.19338 ?  103 GLU A O   1 
ATOM   671  C CB  . GLU A 1 123 ? -12.31300 -20.92500 0.48100  1.000 41.31932 ?  103 GLU A CB  1 
ATOM   672  C CG  . GLU A 1 123 ? -11.51900 -20.18200 -0.56600 1.000 35.38918 ?  103 GLU A CG  1 
ATOM   673  C CD  . GLU A 1 123 ? -11.26400 -21.06000 -1.77600 1.000 38.59874 ?  103 GLU A CD  1 
ATOM   674  O OE1 . GLU A 1 123 ? -10.31400 -21.85200 -1.73200 1.000 35.31219 ?  103 GLU A OE1 1 
ATOM   675  O OE2 . GLU A 1 123 ? -12.03700 -20.96800 -2.74000 1.000 33.80257 -1 103 GLU A OE2 1 
ATOM   676  N N   . GLY A 1 124 ? -13.97400 -18.11100 1.57000  1.000 39.76495 ?  104 GLY A N   1 
ATOM   677  C CA  . GLY A 1 124 ? -15.21800 -17.34900 1.38200  1.000 35.19465 ?  104 GLY A CA  1 
ATOM   678  C C   . GLY A 1 124 ? -16.20800 -17.56400 2.50100  1.000 37.39373 ?  104 GLY A C   1 
ATOM   679  O O   . GLY A 1 124 ? -15.88600 -17.21400 3.63800  1.000 50.50484 ?  104 GLY A O   1 
ATOM   680  N N   . GLU A 1 125 ? -17.36500 -18.12600 2.18100  1.000 42.63739 ?  105 GLU A N   1 
ATOM   681  C CA  . GLU A 1 125 ? -18.42700 -18.36700 3.18400  1.000 46.72661 ?  105 GLU A CA  1 
ATOM   682  C C   . GLU A 1 125 ? -18.34900 -19.81100 3.68600  1.000 41.94119 ?  105 GLU A C   1 
ATOM   683  O O   . GLU A 1 125 ? -19.07200 -20.14100 4.62600  1.000 47.77127 ?  105 GLU A O   1 
ATOM   684  C CB  . GLU A 1 125 ? -19.78500 -18.06400 2.54800  1.000 39.22749 ?  105 GLU A CB  1 
ATOM   685  C CG  . GLU A 1 125 ? -20.29800 -19.15300 1.62700  1.000 41.52216 ?  105 GLU A CG  1 
ATOM   686  C CD  . GLU A 1 125 ? -21.73600 -18.96000 1.17700  1.000 52.97938 ?  105 GLU A CD  1 
ATOM   687  O OE1 . GLU A 1 125 ? -22.25700 -17.84600 1.35300  1.000 45.23560 ?  105 GLU A OE1 1 
ATOM   688  O OE2 . GLU A 1 125 ? -22.32900 -19.92200 0.65400  1.000 42.71062 -1 105 GLU A OE2 1 
ATOM   689  N N   . LEU A 1 126 ? -17.50300 -20.63100 3.07800  1.000 40.92994 ?  106 LEU A N   1 
ATOM   690  C CA  . LEU A 1 126 ? -17.45100 -22.06800 3.44400  1.000 41.73311 ?  106 LEU A CA  1 
ATOM   691  C C   . LEU A 1 126 ? -16.97300 -22.23600 4.88700  1.000 40.50594 ?  106 LEU A C   1 
ATOM   692  O O   . LEU A 1 126 ? -16.10000 -21.48100 5.32400  1.000 37.40502 ?  106 LEU A O   1 
ATOM   693  C CB  . LEU A 1 126 ? -16.55700 -22.80600 2.44900  1.000 33.78837 ?  106 LEU A CB  1 
ATOM   694  C CG  . LEU A 1 126 ? -16.94200 -22.62200 0.98400  1.000 41.39366 ?  106 LEU A CG  1 
ATOM   695  C CD1 . LEU A 1 126 ? -15.88200 -23.20800 0.06800  1.000 40.04895 ?  106 LEU A CD1 1 
ATOM   696  C CD2 . LEU A 1 126 ? -18.30300 -23.23200 0.69700  1.000 34.81058 ?  106 LEU A CD2 1 
ATOM   697  N N   . LYS A 1 127 ? -17.56300 -23.19400 5.58500  1.000 42.42540 ?  107 LYS A N   1 
ATOM   698  C CA  . LYS A 1 127 ? -17.21400 -23.43000 7.00500  1.000 44.29681 ?  107 LYS A CA  1 
ATOM   699  C C   . LYS A 1 127 ? -16.89800 -24.91000 7.20200  1.000 44.06553 ?  107 LYS A C   1 
ATOM   700  O O   . LYS A 1 127 ? -17.45000 -25.73200 6.47000  1.000 49.43450 ?  107 LYS A O   1 
ATOM   701  C CB  . LYS A 1 127 ? -18.33600 -22.93100 7.91800  1.000 38.42138 ?  107 LYS A CB  1 
ATOM   702  C CG  . LYS A 1 127 ? -18.14200 -21.52300 8.45800  1.000 40.81587 ?  107 LYS A CG  1 
ATOM   703  C CD  . LYS A 1 127 ? -19.22900 -20.57900 8.01400  1.000 47.66858 ?  107 LYS A CD  1 
ATOM   704  C CE  . LYS A 1 127 ? -18.85800 -19.12100 8.17600  1.000 36.65031 ?  107 LYS A CE  1 
ATOM   705  N N   . ASN A 1 128 ? -16.00300 -25.20700 8.13700  1.000 47.74138 ?  108 ASN A N   1 
ATOM   706  C CA  . ASN A 1 128 ? -15.60200 -26.60100 8.42900  1.000 42.66227 ?  108 ASN A CA  1 
ATOM   707  C C   . ASN A 1 128 ? -15.94000 -26.89500 9.89300  1.000 43.57934 ?  108 ASN A C   1 
ATOM   708  O O   . ASN A 1 128 ? -15.37300 -26.24700 10.76800 1.000 41.34905 ?  108 ASN A O   1 
ATOM   709  C CB  . ASN A 1 128 ? -14.12600 -26.81000 8.10700  1.000 44.33292 ?  108 ASN A CB  1 
ATOM   710  C CG  . ASN A 1 128 ? -13.81300 -26.68200 6.63200  1.000 59.22104 ?  108 ASN A CG  1 
ATOM   711  O OD1 . ASN A 1 128 ? -13.70900 -27.68400 5.92900  1.000 59.84944 ?  108 ASN A OD1 1 
ATOM   712  N N   . TYR A 1 129 ? -16.83800 -27.84100 10.13200 1.000 39.84750 ?  109 TYR A N   1 
ATOM   713  C CA  . TYR A 1 129 ? -17.28100 -28.13300 11.51500 1.000 42.70404 ?  109 TYR A CA  1 
ATOM   714  C C   . TYR A 1 129 ? -16.14500 -28.76200 12.32000 1.000 36.07835 ?  109 TYR A C   1 
ATOM   715  O O   . TYR A 1 129 ? -15.44300 -29.63900 11.81400 1.000 35.52993 ?  109 TYR A O   1 
ATOM   716  C CB  . TYR A 1 129 ? -18.53800 -29.00100 11.52300 1.000 39.83104 ?  109 TYR A CB  1 
ATOM   717  C CG  . TYR A 1 129 ? -18.99300 -29.44500 12.88700 1.000 37.85351 ?  109 TYR A CG  1 
ATOM   718  C CD1 . TYR A 1 129 ? -19.63400 -28.57100 13.74600 1.000 41.57910 ?  109 TYR A CD1 1 
ATOM   719  C CD2 . TYR A 1 129 ? -18.78000 -30.74100 13.31600 1.000 40.37706 ?  109 TYR A CD2 1 
ATOM   720  C CE1 . TYR A 1 129 ? -20.05700 -28.97600 14.99900 1.000 43.49860 ?  109 TYR A CE1 1 
ATOM   721  C CE2 . TYR A 1 129 ? -19.19600 -31.16200 14.56500 1.000 39.82860 ?  109 TYR A CE2 1 
ATOM   722  C CZ  . TYR A 1 129 ? -19.83400 -30.27700 15.41000 1.000 43.50996 ?  109 TYR A CZ  1 
ATOM   723  O OH  . TYR A 1 129 ? -20.24500 -30.69800 16.64700 1.000 50.54941 ?  109 TYR A OH  1 
ATOM   724  N N   . LYS A 1 130 ? -15.98400 -28.28400 13.54400 1.000 31.51089 ?  110 LYS A N   1 
ATOM   725  C CA  . LYS A 1 130 ? -14.93400 -28.82600 14.43100 1.000 35.72823 ?  110 LYS A CA  1 
ATOM   726  C C   . LYS A 1 130 ? -15.54000 -29.06900 15.81100 1.000 34.60223 ?  110 LYS A C   1 
ATOM   727  O O   . LYS A 1 130 ? -16.51700 -28.39800 16.14400 1.000 35.34095 ?  110 LYS A O   1 
ATOM   728  C CB  . LYS A 1 130 ? -13.73700 -27.87400 14.49700 1.000 34.09972 ?  110 LYS A CB  1 
ATOM   729  C CG  . LYS A 1 130 ? -13.03200 -27.58100 13.18200 1.000 39.73634 ?  110 LYS A CG  1 
ATOM   730  C CD  . LYS A 1 130 ? -12.21600 -28.74500 12.67800 1.000 41.36524 ?  110 LYS A CD  1 
ATOM   731  C CE  . LYS A 1 130 ? -11.13700 -28.33500 11.70000 1.000 41.62883 ?  110 LYS A CE  1 
ATOM   732  N N   . VAL A 1 131 ? -14.97500 -30.00700 16.55400 1.000 28.07145 ?  111 VAL A N   1 
ATOM   733  C CA  . VAL A 1 131 ? -15.42000 -30.33900 17.90100 1.000 29.62843 ?  111 VAL A CA  1 
ATOM   734  C C   . VAL A 1 131 ? -14.29000 -30.04800 18.88000 1.000 37.49869 ?  111 VAL A C   1 
ATOM   735  O O   . VAL A 1 131 ? -13.12900 -30.38000 18.62100 1.000 37.43764 ?  111 VAL A O   1 
ATOM   736  C CB  . VAL A 1 131 ? -15.85900 -31.81500 18.01600 1.000 42.55922 ?  111 VAL A CB  1 
ATOM   737  C CG1 . VAL A 1 131 ? -16.30600 -32.13400 19.44200 1.000 34.64441 ?  111 VAL A CG1 1 
ATOM   738  C CG2 . VAL A 1 131 ? -16.97200 -32.12300 17.03400 1.000 42.68337 ?  111 VAL A CG2 1 
ATOM   739  N N   . ILE A 1 132 ? -14.63400 -29.42200 20.00300 1.000 32.55413 ?  112 ILE A N   1 
ATOM   740  C CA  . ILE A 1 132 ? -13.72100 -29.23100 21.12400 1.000 31.90221 ?  112 ILE A CA  1 
ATOM   741  C C   . ILE A 1 132 ? -14.13400 -30.20200 22.21700 1.000 30.36211 ?  112 ILE A C   1 
ATOM   742  O O   . ILE A 1 132 ? -15.24600 -30.10400 22.74800 1.000 34.53919 ?  112 ILE A O   1 
ATOM   743  C CB  . ILE A 1 132 ? -13.75000 -27.78800 21.64500 1.000 32.35440 ?  112 ILE A CB  1 
ATOM   744  C CG1 . ILE A 1 132 ? -13.33200 -26.80800 20.54900 1.000 33.11425 ?  112 ILE A CG1 1 
ATOM   745  C CG2 . ILE A 1 132 ? -12.86800 -27.65000 22.88200 1.000 29.06595 ?  112 ILE A CG2 1 
ATOM   746  C CD1 . ILE A 1 132 ? -13.74000 -25.38000 20.83600 1.000 26.14265 ?  112 ILE A CD1 1 
ATOM   747  N N   . ASP A 1 133 ? -13.25600 -31.14100 22.55100 1.000 31.69646 ?  113 ASP A N   1 
ATOM   748  C CA  . ASP A 1 133 ? -13.52900 -32.11600 23.60000 1.000 34.22092 ?  113 ASP A CA  1 
ATOM   749  C C   . ASP A 1 133 ? -12.76200 -31.72000 24.85600 1.000 35.06267 ?  113 ASP A C   1 
ATOM   750  O O   . ASP A 1 133 ? -11.52600 -31.70100 24.85700 1.000 31.38548 ?  113 ASP A O   1 
ATOM   751  C CB  . ASP A 1 133 ? -13.16100 -33.52900 23.14300 1.000 33.87270 ?  113 ASP A CB  1 
ATOM   752  C CG  . ASP A 1 133 ? -13.32100 -34.56200 24.24700 1.000 43.94503 ?  113 ASP A CG  1 
ATOM   753  O OD1 . ASP A 1 133 ? -14.15500 -34.35000 25.15400 1.000 46.78538 ?  113 ASP A OD1 1 
ATOM   754  O OD2 . ASP A 1 133 ? -12.63500 -35.60500 24.19500 1.000 53.67747 -1 113 ASP A OD2 1 
ATOM   755  N N   . ARG A 1 134 ? -13.50100 -31.39600 25.91800 1.000 33.12034 ?  114 ARG A N   1 
ATOM   756  C CA  . ARG A 1 134 ? -12.87200 -31.00600 27.17400 1.000 36.65041 ?  114 ARG A CA  1 
ATOM   757  C C   . ARG A 1 134 ? -11.89400 -32.06500 27.66200 1.000 33.67746 ?  114 ARG A C   1 
ATOM   758  O O   . ARG A 1 134 ? -10.85300 -31.73200 28.23500 1.000 34.45607 ?  114 ARG A O   1 
ATOM   759  C CB  . ARG A 1 134 ? -13.94900 -30.74100 28.22500 1.000 35.20183 ?  114 ARG A CB  1 
ATOM   760  C CG  . ARG A 1 134 ? -13.42200 -30.32800 29.58800 1.000 33.86836 ?  114 ARG A CG  1 
ATOM   761  C CD  . ARG A 1 134 ? -14.50400 -30.48600 30.64200 1.000 33.82692 ?  114 ARG A CD  1 
ATOM   762  N NE  . ARG A 1 134 ? -14.78700 -31.89600 30.87800 1.000 39.62241 ?  114 ARG A NE  1 
ATOM   763  C CZ  . ARG A 1 134 ? -15.97500 -32.38300 31.20200 1.000 34.76479 ?  114 ARG A CZ  1 
ATOM   764  N NH1 . ARG A 1 134 ? -17.02400 -31.59300 31.38300 1.000 29.92796 ?  114 ARG A NH1 1 
ATOM   765  N NH2 . ARG A 1 134 ? -16.11300 -33.69700 31.35200 1.000 33.40057 ?  114 ARG A NH2 1 
ATOM   766  N N   . GLU A 1 135 ? -12.19900 -33.33700 27.42700 1.000 34.38801 ?  115 GLU A N   1 
ATOM   767  C CA  . GLU A 1 135 ? -11.37400 -34.43500 27.91000 1.000 36.89059 ?  115 GLU A CA  1 
ATOM   768  C C   . GLU A 1 135 ? -10.10500 -34.63700 27.08900 1.000 36.15652 ?  115 GLU A C   1 
ATOM   769  O O   . GLU A 1 135 ? -9.30700  -35.51700 27.42200 1.000 36.36549 ?  115 GLU A O   1 
ATOM   770  C CB  . GLU A 1 135 ? -12.20200 -35.72400 27.94400 1.000 37.53228 ?  115 GLU A CB  1 
ATOM   771  C CG  . GLU A 1 135 ? -13.30600 -35.72900 29.01000 1.000 35.34797 ?  115 GLU A CG  1 
ATOM   772  C CD  . GLU A 1 135 ? -12.79100 -35.35900 30.39400 1.000 36.06538 ?  115 GLU A CD  1 
ATOM   773  O OE1 . GLU A 1 135 ? -11.82100 -35.99500 30.85500 1.000 43.64179 ?  115 GLU A OE1 1 
ATOM   774  O OE2 . GLU A 1 135 ? -13.36600 -34.45200 31.03200 1.000 38.60851 -1 115 GLU A OE2 1 
ATOM   775  N N   . GLY A 1 136 ? -9.89100  -33.84600 26.03800 1.000 37.39094 ?  116 GLY A N   1 
ATOM   776  C CA  . GLY A 1 136 ? -8.65000  -33.89100 25.29200 1.000 30.31811 ?  116 GLY A CA  1 
ATOM   777  C C   . GLY A 1 136 ? -7.57500  -32.93500 25.75300 1.000 32.15817 ?  116 GLY A C   1 
ATOM   778  O O   . GLY A 1 136 ? -6.46000  -32.97300 25.22800 1.000 39.00554 ?  116 GLY A O   1 
ATOM   779  N N   . TYR A 1 137 ? -7.86300  -32.07800 26.72800 1.000 33.47424 ?  117 TYR A N   1 
ATOM   780  C CA  . TYR A 1 137 ? -6.91200  -31.07800 27.18900 1.000 30.96136 ?  117 TYR A CA  1 
ATOM   781  C C   . TYR A 1 137 ? -6.45300  -31.38900 28.60500 1.000 32.24760 ?  117 TYR A C   1 
ATOM   782  O O   . TYR A 1 137 ? -7.19700  -31.95900 29.40800 1.000 30.35955 ?  117 TYR A O   1 
ATOM   783  C CB  . TYR A 1 137 ? -7.51800  -29.67400 27.15200 1.000 24.01793 ?  117 TYR A CB  1 
ATOM   784  C CG  . TYR A 1 137 ? -7.86900  -29.20100 25.76500 1.000 28.46041 ?  117 TYR A CG  1 
ATOM   785  C CD1 . TYR A 1 137 ? -9.08200  -29.54500 25.18400 1.000 28.65582 ?  117 TYR A CD1 1 
ATOM   786  C CD2 . TYR A 1 137 ? -6.99300  -28.40800 25.03700 1.000 26.29102 ?  117 TYR A CD2 1 
ATOM   787  C CE1 . TYR A 1 137 ? -9.41200  -29.11900 23.91500 1.000 29.16292 ?  117 TYR A CE1 1 
ATOM   788  C CE2 . TYR A 1 137 ? -7.31500  -27.97200 23.76500 1.000 27.89969 ?  117 TYR A CE2 1 
ATOM   789  C CZ  . TYR A 1 137 ? -8.52500  -28.33300 23.20700 1.000 33.77038 ?  117 TYR A CZ  1 
ATOM   790  O OH  . TYR A 1 137 ? -8.85500  -27.90900 21.93800 1.000 36.71673 ?  117 TYR A OH  1 
ATOM   791  N N   . ALA A 1 138 ? -5.21800  -30.98700 28.90900 1.000 28.56720 ?  118 ALA A N   1 
ATOM   792  C CA  . ALA A 1 138 ? -4.69100  -31.18500 30.25400 1.000 31.35108 ?  118 ALA A CA  1 
ATOM   793  C C   . ALA A 1 138 ? -5.52000  -30.45200 31.30200 1.000 35.28262 ?  118 ALA A C   1 
ATOM   794  O O   . ALA A 1 138 ? -5.51400  -30.84200 32.47500 1.000 29.64008 ?  118 ALA A O   1 
ATOM   795  C CB  . ALA A 1 138 ? -3.23300  -30.73200 30.31900 1.000 29.67824 ?  118 ALA A CB  1 
ATOM   796  N N   . PHE A 1 139 ? -6.24200  -29.39600 30.90900 1.000 31.11295 ?  119 PHE A N   1 
ATOM   797  C CA  . PHE A 1 139 ? -7.00500  -28.64900 31.90500 1.000 32.00930 ?  119 PHE A CA  1 
ATOM   798  C C   . PHE A 1 139 ? -8.24700  -29.38600 32.37900 1.000 31.83190 ?  119 PHE A C   1 
ATOM   799  O O   . PHE A 1 139 ? -8.96500  -28.85100 33.23000 1.000 37.64952 ?  119 PHE A O   1 
ATOM   800  C CB  . PHE A 1 139 ? -7.38000  -27.24900 31.38300 1.000 29.94917 ?  119 PHE A CB  1 
ATOM   801  C CG  . PHE A 1 139 ? -8.34800  -27.22900 30.21200 1.000 26.57626 ?  119 PHE A CG  1 
ATOM   802  C CD1 . PHE A 1 139 ? -9.67100  -27.62500 30.35000 1.000 32.02701 ?  119 PHE A CD1 1 
ATOM   803  C CD2 . PHE A 1 139 ? -7.93800  -26.74000 28.98500 1.000 28.28156 ?  119 PHE A CD2 1 
ATOM   804  C CE1 . PHE A 1 139 ? -10.55100 -27.57400 29.27700 1.000 31.49109 ?  119 PHE A CE1 1 
ATOM   805  C CE2 . PHE A 1 139 ? -8.81300  -26.68200 27.90800 1.000 26.47010 ?  119 PHE A CE2 1 
ATOM   806  C CZ  . PHE A 1 139 ? -10.11600 -27.10400 28.05500 1.000 25.18615 ?  119 PHE A CZ  1 
ATOM   807  N N   . ARG A 1 140 ? -8.51700  -30.58700 31.86700 1.000 31.53278 ?  120 ARG A N   1 
ATOM   808  C CA  . ARG A 1 140 ? -9.68700  -31.34300 32.29700 1.000 31.79414 ?  120 ARG A CA  1 
ATOM   809  C C   . ARG A 1 140 ? -9.59300  -31.79600 33.74400 1.000 30.08804 ?  120 ARG A C   1 
ATOM   810  O O   . ARG A 1 140 ? -10.59300 -32.27300 34.28900 1.000 33.79789 ?  120 ARG A O   1 
ATOM   811  C CB  . ARG A 1 140 ? -9.88200  -32.56200 31.40000 1.000 31.92950 ?  120 ARG A CB  1 
ATOM   812  C CG  . ARG A 1 140 ? -8.81600  -33.63400 31.59000 1.000 35.40605 ?  120 ARG A CG  1 
ATOM   813  C CD  . ARG A 1 140 ? -8.85800  -34.61300 30.44200 1.000 35.06381 ?  120 ARG A CD  1 
ATOM   814  N NE  . ARG A 1 140 ? -7.97600  -35.75400 30.63700 1.000 40.75717 ?  120 ARG A NE  1 
ATOM   815  C CZ  . ARG A 1 140 ? -8.26000  -36.80300 31.39600 1.000 46.13594 ?  120 ARG A CZ  1 
ATOM   816  N NH1 . ARG A 1 140 ? -9.39100  -36.87800 32.08000 1.000 48.27556 ?  120 ARG A NH1 1 
ATOM   817  N NH2 . ARG A 1 140 ? -7.38800  -37.80100 31.46900 1.000 43.78885 ?  120 ARG A NH2 1 
ATOM   818  N N   . ASP A 1 141 ? -8.42700  -31.66600 34.37400 1.000 33.33854 ?  121 ASP A N   1 
ATOM   819  C CA  . ASP A 1 141 ? -8.26500  -32.04000 35.77200 1.000 36.94588 ?  121 ASP A CA  1 
ATOM   820  C C   . ASP A 1 141 ? -8.72100  -30.95000 36.73300 1.000 38.22755 ?  121 ASP A C   1 
ATOM   821  O O   . ASP A 1 141 ? -8.69600  -31.17400 37.94700 1.000 42.67121 ?  121 ASP A O   1 
ATOM   822  C CB  . ASP A 1 141 ? -6.80000  -32.41000 36.06000 1.000 32.53847 ?  121 ASP A CB  1 
ATOM   823  C CG  . ASP A 1 141 ? -5.81200  -31.29800 35.69600 1.000 44.73627 ?  121 ASP A CG  1 
ATOM   824  O OD1 . ASP A 1 141 ? -6.24000  -30.16300 35.36700 1.000 36.02429 ?  121 ASP A OD1 1 
ATOM   825  O OD2 . ASP A 1 141 ? -4.58800  -31.56600 35.73900 1.000 40.33919 -1 121 ASP A OD2 1 
ATOM   826  N N   . SER A 1 142 ? -9.15400  -29.78800 36.22400 1.000 31.36305 ?  122 SER A N   1 
ATOM   827  C CA  . SER A 1 142 ? -9.43000  -28.64600 37.08600 1.000 35.77187 ?  122 SER A CA  1 
ATOM   828  C C   . SER A 1 142 ? -10.66000 -27.84700 36.67300 1.000 31.20638 ?  122 SER A C   1 
ATOM   829  O O   . SER A 1 142 ? -10.90400 -26.78600 37.25900 1.000 34.56254 ?  122 SER A O   1 
ATOM   830  C CB  . SER A 1 142 ? -8.22400  -27.70000 37.11300 1.000 27.70383 ?  122 SER A CB  1 
ATOM   831  O OG  . SER A 1 142 ? -7.00500  -28.41600 37.16700 1.000 37.65437 ?  122 SER A OG  1 
ATOM   832  N N   . PHE A 1 143 ? -11.44300 -28.31000 35.69500 1.000 27.55219 ?  123 PHE A N   1 
ATOM   833  C CA  . PHE A 1 143 ? -12.47600 -27.45500 35.11500 1.000 27.08945 ?  123 PHE A CA  1 
ATOM   834  C C   . PHE A 1 143 ? -13.61800 -27.16100 36.07900 1.000 33.48097 ?  123 PHE A C   1 
ATOM   835  O O   . PHE A 1 143 ? -14.34400 -26.18500 35.86800 1.000 34.90366 ?  123 PHE A O   1 
ATOM   836  C CB  . PHE A 1 143 ? -13.02000 -28.07900 33.82700 1.000 30.40533 ?  123 PHE A CB  1 
ATOM   837  C CG  . PHE A 1 143 ? -13.86100 -29.30400 34.04800 1.000 32.69061 ?  123 PHE A CG  1 
ATOM   838  C CD1 . PHE A 1 143 ? -15.23500 -29.20600 34.20100 1.000 32.75405 ?  123 PHE A CD1 1 
ATOM   839  C CD2 . PHE A 1 143 ? -13.27800 -30.55900 34.06800 1.000 33.66271 ?  123 PHE A CD2 1 
ATOM   840  C CE1 . PHE A 1 143 ? -16.01000 -30.33500 34.39800 1.000 33.31044 ?  123 PHE A CE1 1 
ATOM   841  C CE2 . PHE A 1 143 ? -14.04200 -31.69200 34.26100 1.000 31.17423 ?  123 PHE A CE2 1 
ATOM   842  C CZ  . PHE A 1 143 ? -15.41000 -31.57900 34.42900 1.000 36.40433 ?  123 PHE A CZ  1 
ATOM   843  N N   . THR A 1 144 ? -13.80400 -27.97100 37.12200 1.000 27.11820 ?  124 THR A N   1 
ATOM   844  C CA  . THR A 1 144 ? -14.85600 -27.70400 38.09400 1.000 34.16815 ?  124 THR A CA  1 
ATOM   845  C C   . THR A 1 144 ? -14.50800 -26.56400 39.03900 1.000 39.62792 ?  124 THR A C   1 
ATOM   846  O O   . THR A 1 144 ? -15.38200 -26.12200 39.79200 1.000 34.44517 ?  124 THR A O   1 
ATOM   847  C CB  . THR A 1 144 ? -15.16000 -28.95500 38.92300 1.000 39.59741 ?  124 THR A CB  1 
ATOM   848  O OG1 . THR A 1 144 ? -13.97900 -29.35400 39.63200 1.000 37.68467 ?  124 THR A OG1 1 
ATOM   849  C CG2 . THR A 1 144 ? -15.62200 -30.08900 38.03000 1.000 38.82607 ?  124 THR A CG2 1 
ATOM   850  N N   . LYS A 1 145 ? -13.26200 -26.09500 39.02900 1.000 33.70722 ?  125 LYS A N   1 
ATOM   851  C CA  . LYS A 1 145 ? -12.84200 -24.98300 39.86400 1.000 32.25612 ?  125 LYS A CA  1 
ATOM   852  C C   . LYS A 1 145 ? -13.10500 -23.63400 39.21000 1.000 33.65552 ?  125 LYS A C   1 
ATOM   853  O O   . LYS A 1 145 ? -12.65900 -22.60700 39.73100 1.000 30.17329 ?  125 LYS A O   1 
ATOM   854  C CB  . LYS A 1 145 ? -11.35800 -25.12500 40.21200 1.000 32.18898 ?  125 LYS A CB  1 
ATOM   855  C CG  . LYS A 1 145 ? -11.03900 -26.37800 41.00900 1.000 35.77702 ?  125 LYS A CG  1 
ATOM   856  C CD  . LYS A 1 145 ? -9.66000  -26.31000 41.65000 1.000 39.37404 ?  125 LYS A CD  1 
ATOM   857  C CE  . LYS A 1 145 ? -8.59100  -26.80400 40.70000 1.000 36.17944 ?  125 LYS A CE  1 
ATOM   858  N NZ  . LYS A 1 145 ? -7.22900  -26.31300 41.07600 1.000 38.73649 ?  125 LYS A NZ  1 
ATOM   859  N N   . VAL A 1 146 ? -13.82900 -23.61500 38.09200 1.000 33.25969 ?  126 VAL A N   1 
ATOM   860  C CA  . VAL A 1 146 ? -14.10800 -22.39900 37.33900 1.000 31.19771 ?  126 VAL A CA  1 
ATOM   861  C C   . VAL A 1 146 ? -15.59700 -22.10300 37.39800 1.000 28.33074 ?  126 VAL A C   1 
ATOM   862  O O   . VAL A 1 146 ? -16.42600 -23.01800 37.36700 1.000 33.52903 ?  126 VAL A O   1 
ATOM   863  C CB  . VAL A 1 146 ? -13.65100 -22.51500 35.86800 1.000 33.48181 ?  126 VAL A CB  1 
ATOM   864  C CG1 . VAL A 1 146 ? -13.75400 -21.16100 35.17100 1.000 33.07847 ?  126 VAL A CG1 1 
ATOM   865  C CG2 . VAL A 1 146 ? -12.23500 -23.04700 35.79000 1.000 30.84017 ?  126 VAL A CG2 1 
ATOM   866  N N   . GLU A 1 147 ? -15.93200 -20.81800 37.45700 1.000 29.03551 ?  127 GLU A N   1 
ATOM   867  C CA  . GLU A 1 147 ? -17.29600 -20.34700 37.28700 1.000 37.50723 ?  127 GLU A CA  1 
ATOM   868  C C   . GLU A 1 147 ? -17.28800 -19.21500 36.27500 1.000 28.70494 ?  127 GLU A C   1 
ATOM   869  O O   . GLU A 1 147 ? -16.48400 -18.28500 36.39100 1.000 29.93557 ?  127 GLU A O   1 
ATOM   870  C CB  . GLU A 1 147 ? -17.88000 -19.87000 38.61300 1.000 37.77726 ?  127 GLU A CB  1 
ATOM   871  C CG  . GLU A 1 147 ? -19.07900 -20.65600 39.05500 1.000 45.28421 ?  127 GLU A CG  1 
ATOM   872  C CD  . GLU A 1 147 ? -19.92000 -19.89900 40.05200 1.000 56.32022 ?  127 GLU A CD  1 
ATOM   873  O OE1 . GLU A 1 147 ? -19.53400 -19.85600 41.24200 1.000 50.51448 ?  127 GLU A OE1 1 
ATOM   874  O OE2 . GLU A 1 147 ? -20.96500 -19.34600 39.64300 1.000 56.59767 -1 127 GLU A OE2 1 
ATOM   875  N N   . PHE A 1 148 ? -18.17400 -19.29100 35.28400 1.000 29.03180 ?  128 PHE A N   1 
ATOM   876  C CA  . PHE A 1 148 ? -18.24800 -18.28500 34.23100 1.000 29.37139 ?  128 PHE A CA  1 
ATOM   877  C C   . PHE A 1 148 ? -19.44300 -17.36700 34.45900 1.000 28.21197 ?  128 PHE A C   1 
ATOM   878  O O   . PHE A 1 148 ? -20.53700 -17.83300 34.78800 1.000 34.97198 ?  128 PHE A O   1 
ATOM   879  C CB  . PHE A 1 148 ? -18.33300 -18.94500 32.85600 1.000 29.58302 ?  128 PHE A CB  1 
ATOM   880  C CG  . PHE A 1 148 ? -17.08600 -19.68400 32.46900 1.000 28.84829 ?  128 PHE A CG  1 
ATOM   881  C CD1 . PHE A 1 148 ? -15.91400 -18.99700 32.20800 1.000 27.53173 ?  128 PHE A CD1 1 
ATOM   882  C CD2 . PHE A 1 148 ? -17.08600 -21.06400 32.36300 1.000 28.23874 ?  128 PHE A CD2 1 
ATOM   883  C CE1 . PHE A 1 148 ? -14.76500 -19.67300 31.84700 1.000 30.90615 ?  128 PHE A CE1 1 
ATOM   884  C CE2 . PHE A 1 148 ? -15.94100 -21.74600 32.00300 1.000 29.40515 ?  128 PHE A CE2 1 
ATOM   885  C CZ  . PHE A 1 148 ? -14.77600 -21.04800 31.74700 1.000 27.74617 ?  128 PHE A CZ  1 
ATOM   886  N N   . PHE A 1 149 ? -19.22800 -16.06500 34.28800 1.000 30.69605 ?  129 PHE A N   1 
ATOM   887  C CA  . PHE A 1 149 ? -20.26100 -15.05800 34.47900 1.000 26.90204 ?  129 PHE A CA  1 
ATOM   888  C C   . PHE A 1 149 ? -20.20900 -14.03700 33.35300 1.000 33.44696 ?  129 PHE A C   1 
ATOM   889  O O   . PHE A 1 149 ? -19.15000 -13.75500 32.78400 1.000 30.65847 ?  129 PHE A O   1 
ATOM   890  C CB  . PHE A 1 149 ? -20.10400 -14.28300 35.79400 1.000 28.64931 ?  129 PHE A CB  1 
ATOM   891  C CG  . PHE A 1 149 ? -19.95100 -15.13700 37.01300 1.000 34.80852 ?  129 PHE A CG  1 
ATOM   892  C CD1 . PHE A 1 149 ? -18.71700 -15.65600 37.36300 1.000 27.97024 ?  129 PHE A CD1 1 
ATOM   893  C CD2 . PHE A 1 149 ? -21.03500 -15.37400 37.84000 1.000 32.75661 ?  129 PHE A CD2 1 
ATOM   894  C CE1 . PHE A 1 149 ? -18.57100 -16.41400 38.49600 1.000 34.21569 ?  129 PHE A CE1 1 
ATOM   895  C CE2 . PHE A 1 149 ? -20.89400 -16.13900 38.97600 1.000 42.87797 ?  129 PHE A CE2 1 
ATOM   896  C CZ  . PHE A 1 149 ? -19.66000 -16.66100 39.30600 1.000 38.76894 ?  129 PHE A CZ  1 
ATOM   897  N N   . GLN A 1 150 ? -21.36900 -13.45100 33.07000 1.000 33.15403 ?  130 GLN A N   1 
ATOM   898  C CA  . GLN A 1 150 ? -21.44200 -12.25600 32.24200 1.000 39.50851 ?  130 GLN A CA  1 
ATOM   899  C C   . GLN A 1 150 ? -21.28600 -11.03300 33.13700 1.000 39.09256 ?  130 GLN A C   1 
ATOM   900  O O   . GLN A 1 150 ? -21.90200 -10.95800 34.20700 1.000 39.82513 ?  130 GLN A O   1 
ATOM   901  C CB  . GLN A 1 150 ? -22.76800 -12.20200 31.48200 1.000 35.06289 ?  130 GLN A CB  1 
ATOM   902  C CG  . GLN A 1 150 ? -22.82200 -11.14700 30.38900 1.000 31.73963 ?  130 GLN A CG  1 
ATOM   903  C CD  . GLN A 1 150 ? -23.11700 -9.75700  30.92700 1.000 46.30239 ?  130 GLN A CD  1 
ATOM   904  O OE1 . GLN A 1 150 ? -23.71800 -9.61000  31.99200 1.000 35.98820 ?  130 GLN A OE1 1 
ATOM   905  N NE2 . GLN A 1 150 ? -22.69700 -8.73000  30.19000 1.000 37.71318 ?  130 GLN A NE2 1 
ATOM   906  N N   . GLY A 1 151 ? -20.46000 -10.08400 32.70500 1.000 39.68825 ?  131 GLY A N   1 
ATOM   907  C CA  . GLY A 1 151 ? -20.24500 -8.88100  33.48800 1.000 35.63886 ?  131 GLY A CA  1 
ATOM   908  C C   . GLY A 1 151 ? -19.42100 -7.88100  32.71300 1.000 33.97466 ?  131 GLY A C   1 
ATOM   909  O O   . GLY A 1 151 ? -18.82100 -8.20000  31.68400 1.000 34.93919 ?  131 GLY A O   1 
ATOM   910  N N   . ASP A 1 152 ? -19.40000 -6.65400  33.22900 1.000 40.46453 ?  132 ASP A N   1 
ATOM   911  C CA  . ASP A 1 152 ? -18.66400 -5.55500  32.61900 1.000 31.04130 ?  132 ASP A CA  1 
ATOM   912  C C   . ASP A 1 152 ? -17.50400 -5.18200  33.53000 1.000 34.76958 ?  132 ASP A C   1 
ATOM   913  O O   . ASP A 1 152 ? -17.71500 -4.76800  34.67600 1.000 35.36578 ?  132 ASP A O   1 
ATOM   914  C CB  . ASP A 1 152 ? -19.58600 -4.36100  32.35800 1.000 39.37798 ?  132 ASP A CB  1 
ATOM   915  C CG  . ASP A 1 152 ? -18.83200 -3.05600  32.12400 1.000 41.43681 ?  132 ASP A CG  1 
ATOM   916  O OD1 . ASP A 1 152 ? -17.73000 -3.07700  31.53000 1.000 43.33570 ?  132 ASP A OD1 1 
ATOM   917  O OD2 . ASP A 1 152 ? -19.37700 -1.99400  32.50100 1.000 49.09539 -1 132 ASP A OD2 1 
ATOM   918  N N   . ALA A 1 153 ? -16.28200 -5.32800  33.00700 1.000 29.91425 ?  133 ALA A N   1 
ATOM   919  C CA  . ALA A 1 153 ? -15.07600 -5.02000  33.76600 1.000 31.05354 ?  133 ALA A CA  1 
ATOM   920  C C   . ALA A 1 153 ? -15.01400 -3.56700  34.21500 1.000 30.88342 ?  133 ALA A C   1 
ATOM   921  O O   . ALA A 1 153 ? -14.26900 -3.25500  35.14900 1.000 36.21887 ?  133 ALA A O   1 
ATOM   922  C CB  . ALA A 1 153 ? -13.83600 -5.35100  32.93200 1.000 28.11451 ?  133 ALA A CB  1 
ATOM   923  N N   . CYS A 1 154 ? -15.75800 -2.66900  33.56600 1.000 35.83918 ?  134 CYS A N   1 
ATOM   924  C CA  . CYS A 1 154 ? -15.76000 -1.27600  33.99600 1.000 34.85291 ?  134 CYS A CA  1 
ATOM   925  C C   . CYS A 1 154 ? -16.64400 -1.04600  35.21300 1.000 36.22259 ?  134 CYS A C   1 
ATOM   926  O O   . CYS A 1 154 ? -16.59300 0.03600   35.80500 1.000 40.13062 ?  134 CYS A O   1 
ATOM   927  C CB  . CYS A 1 154 ? -16.21100 -0.37200  32.85000 1.000 35.72666 ?  134 CYS A CB  1 
ATOM   928  S SG  . CYS A 1 154 ? -15.03700 -0.28100  31.48300 1.000 42.70002 ?  134 CYS A SG  1 
ATOM   929  N N   . ASN A 1 155 ? -17.44400 -2.03700  35.60000 1.000 34.78927 ?  135 ASN A N   1 
ATOM   930  C CA  . ASN A 1 155 ? -18.35800 -1.89700  36.72500 1.000 34.21283 ?  135 ASN A CA  1 
ATOM   931  C C   . ASN A 1 155 ? -18.73400 -3.27200  37.25700 1.000 31.97015 ?  135 ASN A C   1 
ATOM   932  O O   . ASN A 1 155 ? -19.87100 -3.72600  37.09300 1.000 39.36542 ?  135 ASN A O   1 
ATOM   933  C CB  . ASN A 1 155 ? -19.60800 -1.12100  36.30800 1.000 36.64673 ?  135 ASN A CB  1 
ATOM   934  C CG  . ASN A 1 155 ? -20.31900 -0.48900  37.48400 1.000 38.47735 ?  135 ASN A CG  1 
ATOM   935  O OD1 . ASN A 1 155 ? -19.94800 -0.70400  38.63700 1.000 36.13612 ?  135 ASN A OD1 1 
ATOM   936  N ND2 . ASN A 1 155 ? -21.36300 0.28100   37.19900 1.000 37.79969 ?  135 ASN A ND2 1 
ATOM   937  N N   . LEU A 1 156 ? -17.78000 -3.94500  37.88500 1.000 32.64013 ?  136 LEU A N   1 
ATOM   938  C CA  . LEU A 1 156 ? -17.99200 -5.30200  38.36200 1.000 37.77541 ?  136 LEU A CA  1 
ATOM   939  C C   . LEU A 1 156 ? -18.83900 -5.29100  39.62600 1.000 31.65274 ?  136 LEU A C   1 
ATOM   940  O O   . LEU A 1 156 ? -18.66700 -4.43300  40.49800 1.000 30.29350 ?  136 LEU A O   1 
ATOM   941  C CB  . LEU A 1 156 ? -16.65000 -5.97800  38.64500 1.000 29.16920 ?  136 LEU A CB  1 
ATOM   942  C CG  . LEU A 1 156 ? -15.83900 -6.37900  37.41400 1.000 26.01589 ?  136 LEU A CG  1 
ATOM   943  C CD1 . LEU A 1 156 ? -14.40400 -6.64500  37.82100 1.000 29.68243 ?  136 LEU A CD1 1 
ATOM   944  C CD2 . LEU A 1 156 ? -16.44600 -7.59300  36.75300 1.000 33.46156 ?  136 LEU A CD2 1 
ATOM   945  N N   . THR A 1 157 ? -19.74400 -6.25900  39.73000 1.000 34.50974 ?  137 THR A N   1 
ATOM   946  C CA  . THR A 1 157 ? -20.56000 -6.37600  40.93000 1.000 36.49577 ?  137 THR A CA  1 
ATOM   947  C C   . THR A 1 157 ? -19.67200 -6.64700  42.14500 1.000 37.89491 ?  137 THR A C   1 
ATOM   948  O O   . THR A 1 157 ? -18.55200 -7.15100  42.00800 1.000 40.28214 ?  137 THR A O   1 
ATOM   949  C CB  . THR A 1 157 ? -21.59600 -7.48900  40.78100 1.000 34.83626 ?  137 THR A CB  1 
ATOM   950  O OG1 . THR A 1 157 ? -20.93500 -8.75700  40.73400 1.000 42.96258 ?  137 THR A OG1 1 
ATOM   951  C CG2 . THR A 1 157 ? -22.41600 -7.29000  39.51500 1.000 35.55421 ?  137 THR A CG2 1 
ATOM   952  N N   . PRO A 1 158 ? -20.15000 -6.32600  43.35200 1.000 41.88532 ?  138 PRO A N   1 
ATOM   953  C CA  . PRO A 1 158 ? -19.26300 -6.36300  44.52800 1.000 40.07696 ?  138 PRO A CA  1 
ATOM   954  C C   . PRO A 1 158 ? -18.74300 -7.74800  44.89700 1.000 43.64389 ?  138 PRO A C   1 
ATOM   955  O O   . PRO A 1 158 ? -17.74900 -7.83500  45.63000 1.000 44.24740 ?  138 PRO A O   1 
ATOM   956  C CB  . PRO A 1 158 ? -20.14700 -5.78600  45.64500 1.000 41.90995 ?  138 PRO A CB  1 
ATOM   957  C CG  . PRO A 1 158 ? -21.18000 -4.96900  44.92100 1.000 38.84165 ?  138 PRO A CG  1 
ATOM   958  C CD  . PRO A 1 158 ? -21.47000 -5.76700  43.69100 1.000 42.92960 ?  138 PRO A CD  1 
ATOM   959  N N   . GLN A 1 159 ? -19.36800 -8.83100  44.42400 1.000 39.39404 ?  139 GLN A N   1 
ATOM   960  C CA  . GLN A 1 159 ? -18.92400 -10.16200 44.82800 1.000 37.60660 ?  139 GLN A CA  1 
ATOM   961  C C   . GLN A 1 159 ? -17.56700 -10.53200 44.23900 1.000 43.52758 ?  139 GLN A C   1 
ATOM   962  O O   . GLN A 1 159 ? -16.88800 -11.41300 44.78000 1.000 46.26571 ?  139 GLN A O   1 
ATOM   963  C CB  . GLN A 1 159 ? -19.96800 -11.21500 44.43900 1.000 43.35564 ?  139 GLN A CB  1 
ATOM   964  C CG  . GLN A 1 159 ? -20.82900 -10.85500 43.23400 1.000 49.18220 ?  139 GLN A CG  1 
ATOM   965  C CD  . GLN A 1 159 ? -21.28500 -12.08000 42.45500 1.000 50.57154 ?  139 GLN A CD  1 
ATOM   966  N N   . PHE A 1 160 ? -17.15400 -9.88700  43.15600 1.000 37.57591 ?  140 PHE A N   1 
ATOM   967  C CA  . PHE A 1 160 ? -15.89600 -10.23200 42.50300 1.000 40.33974 ?  140 PHE A CA  1 
ATOM   968  C C   . PHE A 1 160 ? -14.78500 -9.44800  43.19100 1.000 33.23106 ?  140 PHE A C   1 
ATOM   969  O O   . PHE A 1 160 ? -14.43100 -8.33400  42.79900 1.000 37.05189 ?  140 PHE A O   1 
ATOM   970  C CB  . PHE A 1 160 ? -15.97800 -9.94700  41.00900 1.000 36.74336 ?  140 PHE A CB  1 
ATOM   971  C CG  . PHE A 1 160 ? -16.99700 -10.79200 40.29200 1.000 38.04047 ?  140 PHE A CG  1 
ATOM   972  C CD1 . PHE A 1 160 ? -16.65300 -12.03500 39.79100 1.000 37.97527 ?  140 PHE A CD1 1 
ATOM   973  C CD2 . PHE A 1 160 ? -18.30200 -10.35800 40.13700 1.000 40.31683 ?  140 PHE A CD2 1 
ATOM   974  C CE1 . PHE A 1 160 ? -17.58300 -12.82200 39.13600 1.000 36.74090 ?  140 PHE A CE1 1 
ATOM   975  C CE2 . PHE A 1 160 ? -19.23800 -11.14800 39.48500 1.000 44.69064 ?  140 PHE A CE2 1 
ATOM   976  C CZ  . PHE A 1 160 ? -18.87300 -12.38000 38.98400 1.000 30.12081 ?  140 PHE A CZ  1 
ATOM   977  N N   . LYS A 1 161 ? -14.22300 -10.05100 44.23600 1.000 32.66290 ?  141 LYS A N   1 
ATOM   978  C CA  . LYS A 1 161 ? -13.23500 -9.39600  45.07700 1.000 33.24249 ?  141 LYS A CA  1 
ATOM   979  C C   . LYS A 1 161 ? -12.30200 -10.44900 45.65600 1.000 38.00502 ?  141 LYS A C   1 
ATOM   980  O O   . LYS A 1 161 ? -12.47700 -11.65400 45.44000 1.000 38.01022 ?  141 LYS A O   1 
ATOM   981  C CB  . LYS A 1 161 ? -13.91000 -8.61200  46.20500 1.000 44.24073 ?  141 LYS A CB  1 
ATOM   982  C CG  . LYS A 1 161 ? -14.60300 -9.51800  47.21500 1.000 41.16224 ?  141 LYS A CG  1 
ATOM   983  C CD  . LYS A 1 161 ? -15.52100 -8.73700  48.13300 1.000 44.52947 ?  141 LYS A CD  1 
ATOM   984  C CE  . LYS A 1 161 ? -16.29300 -9.67200  49.04600 1.000 47.46648 ?  141 LYS A CE  1 
ATOM   985  N NZ  . LYS A 1 161 ? -16.38100 -9.14900  50.43500 1.000 55.54069 ?  141 LYS A NZ  1 
ATOM   986  N N   . GLU A 1 162 ? -11.30800 -9.97600  46.40900 1.000 32.82111 ?  142 GLU A N   1 
ATOM   987  C CA  . GLU A 1 162 ? -10.41000 -10.83900 47.17200 1.000 38.19101 ?  142 GLU A CA  1 
ATOM   988  C C   . GLU A 1 162 ? -9.69200  -11.83400 46.26000 1.000 39.80953 ?  142 GLU A C   1 
ATOM   989  O O   . GLU A 1 162 ? -9.63300  -13.03600 46.52800 1.000 40.06649 ?  142 GLU A O   1 
ATOM   990  C CB  . GLU A 1 162 ? -11.16700 -11.55300 48.29400 1.000 38.19539 ?  142 GLU A CB  1 
ATOM   991  C CG  . GLU A 1 162 ? -11.53000 -10.62400 49.45100 1.000 39.77477 ?  142 GLU A CG  1 
ATOM   992  C CD  . GLU A 1 162 ? -12.56700 -11.21200 50.38600 1.000 45.91002 ?  142 GLU A CD  1 
ATOM   993  O OE1 . GLU A 1 162 ? -12.86500 -12.42000 50.27000 1.000 61.30016 ?  142 GLU A OE1 1 
ATOM   994  O OE2 . GLU A 1 162 ? -13.07700 -10.46700 51.25000 1.000 56.52404 -1 142 GLU A OE2 1 
ATOM   995  N N   . TYR A 1 163 ? -9.14300  -11.31600 45.16900 1.000 33.56385 ?  143 TYR A N   1 
ATOM   996  C CA  . TYR A 1 163 ? -8.40000  -12.11700 44.21200 1.000 33.19651 ?  143 TYR A CA  1 
ATOM   997  C C   . TYR A 1 163 ? -6.90900  -11.96400 44.46600 1.000 35.66443 ?  143 TYR A C   1 
ATOM   998  O O   . TYR A 1 163 ? -6.43100  -10.87400 44.80100 1.000 32.05798 ?  143 TYR A O   1 
ATOM   999  C CB  . TYR A 1 163 ? -8.72700  -11.70000 42.77400 1.000 30.90718 ?  143 TYR A CB  1 
ATOM   1000 C CG  . TYR A 1 163 ? -10.15300 -11.98900 42.37700 1.000 33.48615 ?  143 TYR A CG  1 
ATOM   1001 C CD1 . TYR A 1 163 ? -10.59000 -13.29200 42.18200 1.000 32.15906 ?  143 TYR A CD1 1 
ATOM   1002 C CD2 . TYR A 1 163 ? -11.06900 -10.96200 42.22100 1.000 28.97181 ?  143 TYR A CD2 1 
ATOM   1003 C CE1 . TYR A 1 163 ? -11.89800 -13.55800 41.82800 1.000 31.77044 ?  143 TYR A CE1 1 
ATOM   1004 C CE2 . TYR A 1 163 ? -12.37000 -11.22100 41.86500 1.000 32.21618 ?  143 TYR A CE2 1 
ATOM   1005 C CZ  . TYR A 1 163 ? -12.78400 -12.51800 41.67500 1.000 33.15348 ?  143 TYR A CZ  1 
ATOM   1006 O OH  . TYR A 1 163 ? -14.09000 -12.77000 41.32300 1.000 39.15646 ?  143 TYR A OH  1 
ATOM   1007 N N   . ASP A 1 164 ? -6.18000  -13.07000 44.32500 1.000 31.34692 ?  144 ASP A N   1 
ATOM   1008 C CA  . ASP A 1 164 ? -4.72800  -12.99700 44.30700 1.000 36.88945 ?  144 ASP A CA  1 
ATOM   1009 C C   . ASP A 1 164 ? -4.19900  -12.61300 42.93600 1.000 37.87179 ?  144 ASP A C   1 
ATOM   1010 O O   . ASP A 1 164 ? -3.08900  -12.08000 42.83500 1.000 33.77590 ?  144 ASP A O   1 
ATOM   1011 C CB  . ASP A 1 164 ? -4.13000  -14.33000 44.74800 1.000 34.01236 ?  144 ASP A CB  1 
ATOM   1012 C CG  . ASP A 1 164 ? -4.64300  -14.76700 46.10000 1.000 40.92641 ?  144 ASP A CG  1 
ATOM   1013 O OD1 . ASP A 1 164 ? -4.28000  -14.12400 47.10500 1.000 45.37714 ?  144 ASP A OD1 1 
ATOM   1014 O OD2 . ASP A 1 164 ? -5.41800  -15.74400 46.16200 1.000 44.23537 -1 144 ASP A OD2 1 
ATOM   1015 N N   . LEU A 1 165 ? -4.97600  -12.85700 41.88500 1.000 34.06726 ?  145 LEU A N   1 
ATOM   1016 C CA  . LEU A 1 165 ? -4.58400  -12.49300 40.53500 1.000 29.78676 ?  145 LEU A CA  1 
ATOM   1017 C C   . LEU A 1 165 ? -5.81000  -12.03100 39.77100 1.000 28.58892 ?  145 LEU A C   1 
ATOM   1018 O O   . LEU A 1 165 ? -6.84600  -12.70000 39.78700 1.000 26.35467 ?  145 LEU A O   1 
ATOM   1019 C CB  . LEU A 1 165 ? -3.92300  -13.67200 39.81200 1.000 32.80406 ?  145 LEU A CB  1 
ATOM   1020 C CG  . LEU A 1 165 ? -3.85100  -13.54300 38.29100 1.000 30.93905 ?  145 LEU A CG  1 
ATOM   1021 C CD1 . LEU A 1 165 ? -2.82700  -12.49800 37.90700 1.000 29.29987 ?  145 LEU A CD1 1 
ATOM   1022 C CD2 . LEU A 1 165 ? -3.50800  -14.88300 37.67300 1.000 36.15309 ?  145 LEU A CD2 1 
ATOM   1023 N N   . ILE A 1 166 ? -5.69600  -10.88000 39.12000 1.000 28.59114 ?  146 ILE A N   1 
ATOM   1024 C CA  . ILE A 1 166 ? -6.68900  -10.41100 38.16700 1.000 29.61400 ?  146 ILE A CA  1 
ATOM   1025 C C   . ILE A 1 166 ? -5.97800  -10.22900 36.83400 1.000 32.03059 ?  146 ILE A C   1 
ATOM   1026 O O   . ILE A 1 166 ? -5.01000  -9.46100  36.73300 1.000 29.98550 ?  146 ILE A O   1 
ATOM   1027 C CB  . ILE A 1 166 ? -7.36200  -9.11100  38.62800 1.000 31.33200 ?  146 ILE A CB  1 
ATOM   1028 C CG1 . ILE A 1 166 ? -8.10800  -9.34600  39.94100 1.000 28.34056 ?  146 ILE A CG1 1 
ATOM   1029 C CG2 . ILE A 1 166 ? -8.30700  -8.60200  37.54700 1.000 30.64781 ?  146 ILE A CG2 1 
ATOM   1030 C CD1 . ILE A 1 166 ? -9.16500  -8.30100  40.25400 1.000 30.94880 ?  146 ILE A CD1 1 
ATOM   1031 N N   . MET A 1 167 ? -6.43400  -10.95900 35.82500 1.000 27.25218 ?  147 MET A N   1 
ATOM   1032 C CA  . MET A 1 167 ? -5.87200  -10.89500 34.48500 1.000 27.58686 ?  147 MET A CA  1 
ATOM   1033 C C   . MET A 1 167 ? -6.94200  -10.36900 33.54000 1.000 30.52727 ?  147 MET A C   1 
ATOM   1034 O O   . MET A 1 167 ? -8.10400  -10.78000 33.61700 1.000 33.47255 ?  147 MET A O   1 
ATOM   1035 C CB  . MET A 1 167 ? -5.36500  -12.26900 34.04100 1.000 33.53463 ?  147 MET A CB  1 
ATOM   1036 C CG  . MET A 1 167 ? -4.70100  -12.30100 32.67500 1.000 47.01457 ?  147 MET A CG  1 
ATOM   1037 S SD  . MET A 1 167 ? -3.61800  -13.73600 32.50600 1.000 49.38397 ?  147 MET A SD  1 
ATOM   1038 C CE  . MET A 1 167 ? -4.78800  -14.98300 31.98000 1.000 39.11231 ?  147 MET A CE  1 
ATOM   1039 N N   . ALA A 1 168 ? -6.55800  -9.43600  32.68200 1.000 28.76930 ?  148 ALA A N   1 
ATOM   1040 C CA  . ALA A 1 168 ? -7.46900  -8.79900  31.73700 1.000 31.77471 ?  148 ALA A CA  1 
ATOM   1041 C C   . ALA A 1 168 ? -6.81300  -8.90500  30.36600 1.000 30.61041 ?  148 ALA A C   1 
ATOM   1042 O O   . ALA A 1 168 ? -5.93100  -8.10900  30.02600 1.000 33.68756 ?  148 ALA A O   1 
ATOM   1043 C CB  . ALA A 1 168 ? -7.75300  -7.35000  32.13000 1.000 29.37089 ?  148 ALA A CB  1 
ATOM   1044 N N   . THR A 1 169 ? -7.24300  -9.89100  29.58700 1.000 35.23869 ?  149 THR A N   1 
ATOM   1045 C CA  . THR A 1 169 ? -6.55400  -10.27300 28.36400 1.000 36.99396 ?  149 THR A CA  1 
ATOM   1046 C C   . THR A 1 169 ? -7.15500  -9.53000  27.17900 1.000 33.68389 ?  149 THR A C   1 
ATOM   1047 O O   . THR A 1 169 ? -8.33800  -9.71400  26.86400 1.000 37.70442 ?  149 THR A O   1 
ATOM   1048 C CB  . THR A 1 169 ? -6.64400  -11.78500 28.16300 1.000 40.78821 ?  149 THR A CB  1 
ATOM   1049 O OG1 . THR A 1 169 ? -5.67900  -12.42800 29.00300 1.000 52.30136 ?  149 THR A OG1 1 
ATOM   1050 C CG2 . THR A 1 169 ? -6.37600  -12.16100 26.71500 1.000 40.36939 ?  149 THR A CG2 1 
ATOM   1051 N N   . ASN A 1 170 ? -6.33400  -8.70000  26.52500 1.000 31.19442 ?  150 ASN A N   1 
ATOM   1052 C CA  . ASN A 1 170 ? -6.75000  -7.91500  25.36300 1.000 33.05292 ?  150 ASN A CA  1 
ATOM   1053 C C   . ASN A 1 170 ? -8.07000  -7.19500  25.62700 1.000 37.78021 ?  150 ASN A C   1 
ATOM   1054 O O   . ASN A 1 170 ? -9.00700  -7.24700  24.82800 1.000 38.48389 ?  150 ASN A O   1 
ATOM   1055 C CB  . ASN A 1 170 ? -6.85200  -8.79800  24.11700 1.000 33.53236 ?  150 ASN A CB  1 
ATOM   1056 C CG  . ASN A 1 170 ? -5.51000  -9.37600  23.69200 1.000 36.40177 ?  150 ASN A CG  1 
ATOM   1057 O OD1 . ASN A 1 170 ? -4.45300  -8.83200  24.01200 1.000 33.89705 ?  150 ASN A OD1 1 
ATOM   1058 N ND2 . ASN A 1 170 ? -5.55100  -10.48400 22.96400 1.000 34.35655 ?  150 ASN A ND2 1 
ATOM   1059 N N   . LEU A 1 171 ? -8.14400  -6.51700  26.76800 1.000 39.27552 ?  151 LEU A N   1 
ATOM   1060 C CA  . LEU A 1 171 ? -9.41200  -5.94400  27.20500 1.000 34.38035 ?  151 LEU A CA  1 
ATOM   1061 C C   . LEU A 1 171 ? -9.43500  -4.42500  27.23400 1.000 30.62237 ?  151 LEU A C   1 
ATOM   1062 O O   . LEU A 1 171 ? -10.46700 -3.83500  26.90300 1.000 32.11400 ?  151 LEU A O   1 
ATOM   1063 C CB  . LEU A 1 171 ? -9.78100  -6.47500  28.59700 1.000 29.86253 ?  151 LEU A CB  1 
ATOM   1064 C CG  . LEU A 1 171 ? -11.20200 -6.14800  29.05200 1.000 34.84393 ?  151 LEU A CG  1 
ATOM   1065 C CD1 . LEU A 1 171 ? -12.22300 -6.64900  28.04000 1.000 35.79966 ?  151 LEU A CD1 1 
ATOM   1066 C CD2 . LEU A 1 171 ? -11.47100 -6.73200  30.42500 1.000 32.56755 ?  151 LEU A CD2 1 
ATOM   1067 N N   . ILE A 1 172 ? -8.33500  -3.76900  27.62400 1.000 28.01427 ?  152 ILE A N   1 
ATOM   1068 C CA  . ILE A 1 172 ? -8.40600  -2.33700  27.92200 1.000 29.83399 ?  152 ILE A CA  1 
ATOM   1069 C C   . ILE A 1 172 ? -8.74900  -1.53600  26.67400 1.000 34.22313 ?  152 ILE A C   1 
ATOM   1070 O O   . ILE A 1 172 ? -9.48300  -0.54200  26.74500 1.000 31.20306 ?  152 ILE A O   1 
ATOM   1071 C CB  . ILE A 1 172 ? -7.09900  -1.83500  28.56900 1.000 28.82499 ?  152 ILE A CB  1 
ATOM   1072 C CG1 . ILE A 1 172 ? -5.88700  -2.12700  27.68500 1.000 29.63676 ?  152 ILE A CG1 1 
ATOM   1073 C CG2 . ILE A 1 172 ? -6.92800  -2.41300  29.96800 1.000 28.99776 ?  152 ILE A CG2 1 
ATOM   1074 C CD1 . ILE A 1 172 ? -4.63200  -1.40900  28.15000 1.000 32.10482 ?  152 ILE A CD1 1 
ATOM   1075 N N   . ASP A 1 173 ? -8.23100  -1.94700  25.51500 1.000 31.04897 ?  153 ASP A N   1 
ATOM   1076 C CA  . ASP A 1 173 ? -8.52200  -1.25200  24.26700 1.000 30.48544 ?  153 ASP A CA  1 
ATOM   1077 C C   . ASP A 1 173 ? -9.86500  -1.65100  23.68200 1.000 34.25899 ?  153 ASP A C   1 
ATOM   1078 O O   . ASP A 1 173 ? -10.12000 -1.41800  22.49500 1.000 30.42689 ?  153 ASP A O   1 
ATOM   1079 C CB  . ASP A 1 173 ? -7.40700  -1.48600  23.24200 1.000 32.16797 ?  153 ASP A CB  1 
ATOM   1080 C CG  . ASP A 1 173 ? -7.05400  -2.95100  23.07600 1.000 38.31580 ?  153 ASP A CG  1 
ATOM   1081 O OD1 . ASP A 1 173 ? -7.22500  -3.74200  24.03000 1.000 42.74546 ?  153 ASP A OD1 1 
ATOM   1082 O OD2 . ASP A 1 173 ? -6.59700  -3.31300  21.97600 1.000 46.19805 -1 153 ASP A OD2 1 
ATOM   1083 N N   . ARG A 1 174 ? -10.72600 -2.25900  24.49500 1.000 34.51384 ?  154 ARG A N   1 
ATOM   1084 C CA  . ARG A 1 174 ? -12.08700 -2.56900  24.08600 1.000 41.96756 ?  154 ARG A CA  1 
ATOM   1085 C C   . ARG A 1 174 ? -13.11000 -2.05200  25.09000 1.000 34.81063 ?  154 ARG A C   1 
ATOM   1086 O O   . ARG A 1 174 ? -14.30900 -2.30400  24.92100 1.000 36.65587 ?  154 ARG A O   1 
ATOM   1087 C CB  . ARG A 1 174 ? -12.25500 -4.07800  23.88300 1.000 36.57667 ?  154 ARG A CB  1 
ATOM   1088 C CG  . ARG A 1 174 ? -11.72300 -4.57600  22.54800 1.000 43.55360 ?  154 ARG A CG  1 
ATOM   1089 C CD  . ARG A 1 174 ? -11.36100 -6.05700  22.61200 1.000 50.70534 ?  154 ARG A CD  1 
ATOM   1090 N NE  . ARG A 1 174 ? -12.53500 -6.90700  22.44000 1.000 62.06711 ?  154 ARG A NE  1 
ATOM   1091 C CZ  . ARG A 1 174 ? -13.23800 -7.00800  21.31900 1.000 62.26502 ?  154 ARG A CZ  1 
ATOM   1092 N NH1 . ARG A 1 174 ? -12.87000 -6.38600  20.21000 1.000 56.64682 ?  154 ARG A NH1 1 
ATOM   1093 N NH2 . ARG A 1 174 ? -14.33800 -7.75900  21.30800 1.000 65.01560 ?  154 ARG A NH2 1 
ATOM   1094 N N   . LEU A 1 175 ? -12.66700 -1.32900  26.11800 1.000 28.72934 ?  155 LEU A N   1 
ATOM   1095 C CA  . LEU A 1 175 ? -13.54300 -0.80700  27.15400 1.000 31.88880 ?  155 LEU A CA  1 
ATOM   1096 C C   . LEU A 1 175 ? -13.99400 0.60300   26.79200 1.000 29.87045 ?  155 LEU A C   1 
ATOM   1097 O O   . LEU A 1 175 ? -13.20100 1.41100   26.29500 1.000 27.32414 ?  155 LEU A O   1 
ATOM   1098 C CB  . LEU A 1 175 ? -12.81800 -0.79600  28.50000 1.000 22.86705 ?  155 LEU A CB  1 
ATOM   1099 C CG  . LEU A 1 175 ? -12.42400 -2.15300  29.07900 1.000 29.82750 ?  155 LEU A CG  1 
ATOM   1100 C CD1 . LEU A 1 175 ? -11.74700 -1.96400  30.42300 1.000 20.89603 ?  155 LEU A CD1 1 
ATOM   1101 C CD2 . LEU A 1 175 ? -13.62700 -3.08600  29.20800 1.000 25.93239 ?  155 LEU A CD2 1 
ATOM   1102 N N   . TYR A 1 176 ? -15.27300 0.89800   27.05300 1.000 28.32044 ?  156 TYR A N   1 
ATOM   1103 C CA  . TYR A 1 176 ? -15.80200 2.21800   26.72000 1.000 30.42706 ?  156 TYR A CA  1 
ATOM   1104 C C   . TYR A 1 176 ? -15.13000 3.31400   27.54000 1.000 32.21732 ?  156 TYR A C   1 
ATOM   1105 O O   . TYR A 1 176 ? -14.99600 4.44300   27.05700 1.000 33.55545 ?  156 TYR A O   1 
ATOM   1106 C CB  . TYR A 1 176 ? -17.32300 2.25600   26.90600 1.000 27.30959 ?  156 TYR A CB  1 
ATOM   1107 C CG  . TYR A 1 176 ? -17.82700 1.84200   28.27400 1.000 29.65501 ?  156 TYR A CG  1 
ATOM   1108 C CD1 . TYR A 1 176 ? -18.11300 0.51300   28.55400 1.000 34.86182 ?  156 TYR A CD1 1 
ATOM   1109 C CD2 . TYR A 1 176 ? -18.04600 2.78100   29.27200 1.000 34.64420 ?  156 TYR A CD2 1 
ATOM   1110 C CE1 . TYR A 1 176 ? -18.58600 0.12500   29.79800 1.000 38.36350 ?  156 TYR A CE1 1 
ATOM   1111 C CE2 . TYR A 1 176 ? -18.52000 2.40300   30.52300 1.000 37.52087 ?  156 TYR A CE2 1 
ATOM   1112 C CZ  . TYR A 1 176 ? -18.78900 1.07300   30.77800 1.000 37.88974 ?  156 TYR A CZ  1 
ATOM   1113 O OH  . TYR A 1 176 ? -19.25900 0.67900   32.01100 1.000 43.48997 ?  156 TYR A OH  1 
ATOM   1114 N N   . GLU A 1 177 ? -14.69800 3.00300   28.76000 1.000 30.49647 ?  157 GLU A N   1 
ATOM   1115 C CA  . GLU A 1 177 ? -13.90700 3.93200   29.57200 1.000 31.59699 ?  157 GLU A CA  1 
ATOM   1116 C C   . GLU A 1 177 ? -12.98500 3.10900   30.45400 1.000 33.16661 ?  157 GLU A C   1 
ATOM   1117 O O   . GLU A 1 177 ? -13.35000 2.72500   31.57300 1.000 37.33907 ?  157 GLU A O   1 
ATOM   1118 C CB  . GLU A 1 177 ? -14.78400 4.85300   30.42100 1.000 34.82155 ?  157 GLU A CB  1 
ATOM   1119 C CG  . GLU A 1 177 ? -14.28300 6.31000   30.53100 1.000 35.69794 ?  157 GLU A CG  1 
ATOM   1120 C CD  . GLU A 1 177 ? -12.96400 6.45600   31.29600 1.000 34.92928 ?  157 GLU A CD  1 
ATOM   1121 O OE1 . GLU A 1 177 ? -11.93700 5.90800   30.85400 1.000 38.87266 ?  157 GLU A OE1 1 
ATOM   1122 O OE2 . GLU A 1 177 ? -12.94100 7.15600   32.32900 1.000 40.41845 -1 157 GLU A OE2 1 
ATOM   1123 N N   . PRO A 1 178 ? -11.76700 2.81700   29.99000 1.000 32.97071 ?  158 PRO A N   1 
ATOM   1124 C CA  . PRO A 1 178 ? -10.87900 1.93000   30.75800 1.000 31.83212 ?  158 PRO A CA  1 
ATOM   1125 C C   . PRO A 1 178 ? -10.48900 2.44600   32.13900 1.000 32.14549 ?  158 PRO A C   1 
ATOM   1126 O O   . PRO A 1 178 ? -10.10500 1.63400   32.98900 1.000 31.88002 ?  158 PRO A O   1 
ATOM   1127 C CB  . PRO A 1 178 ? -9.65200  1.79100   29.84300 1.000 29.25157 ?  158 PRO A CB  1 
ATOM   1128 C CG  . PRO A 1 178 ? -9.72800  2.94700   28.92100 1.000 29.63120 ?  158 PRO A CG  1 
ATOM   1129 C CD  . PRO A 1 178 ? -11.18700 3.15000   28.68000 1.000 29.13165 ?  158 PRO A CD  1 
ATOM   1130 N N   . ARG A 1 179 ? -10.56800 3.75500   32.40000 1.000 32.61673 ?  159 ARG A N   1 
ATOM   1131 C CA  . ARG A 1 179 ? -10.24000 4.23600   33.74100 1.000 32.75829 ?  159 ARG A CA  1 
ATOM   1132 C C   . ARG A 1 179 ? -11.23200 3.73200   34.78100 1.000 34.42423 ?  159 ARG A C   1 
ATOM   1133 O O   . ARG A 1 179 ? -10.85700 3.53100   35.94200 1.000 34.77113 ?  159 ARG A O   1 
ATOM   1134 C CB  . ARG A 1 179 ? -10.17200 5.76700   33.77600 1.000 34.29946 ?  159 ARG A CB  1 
ATOM   1135 C CG  . ARG A 1 179 ? -8.93200  6.36500   33.11900 1.000 35.77031 ?  159 ARG A CG  1 
ATOM   1136 C CD  . ARG A 1 179 ? -8.88700  7.87900   33.30100 1.000 37.34905 ?  159 ARG A CD  1 
ATOM   1137 N NE  . ARG A 1 179 ? -10.14000 8.48300   32.86700 1.000 50.45342 ?  159 ARG A NE  1 
ATOM   1138 C CZ  . ARG A 1 179 ? -10.40200 9.78300   32.87600 1.000 55.44444 ?  159 ARG A CZ  1 
ATOM   1139 N NH1 . ARG A 1 179 ? -9.51000  10.66700  33.30000 1.000 54.82878 ?  159 ARG A NH1 1 
ATOM   1140 N NH2 . ARG A 1 179 ? -11.58900 10.20700  32.44300 1.000 42.31405 ?  159 ARG A NH2 1 
ATOM   1141 N N   . LEU A 1 180 ? -12.49100 3.52300   34.39000 1.000 27.59941 ?  160 LEU A N   1 
ATOM   1142 C CA  . LEU A 1 180 ? -13.46000 2.93600   35.31100 1.000 33.58707 ?  160 LEU A CA  1 
ATOM   1143 C C   . LEU A 1 180 ? -12.96600 1.60500   35.84700 1.000 34.69635 ?  160 LEU A C   1 
ATOM   1144 O O   . LEU A 1 180 ? -13.21300 1.26900   37.01100 1.000 37.77713 ?  160 LEU A O   1 
ATOM   1145 C CB  . LEU A 1 180 ? -14.80700 2.74700   34.61400 1.000 28.56700 ?  160 LEU A CB  1 
ATOM   1146 C CG  . LEU A 1 180 ? -15.84200 3.85800   34.81900 1.000 34.91620 ?  160 LEU A CG  1 
ATOM   1147 C CD1 . LEU A 1 180 ? -15.28800 5.19500   34.34500 1.000 37.49599 ?  160 LEU A CD1 1 
ATOM   1148 C CD2 . LEU A 1 180 ? -17.11800 3.51100   34.08000 1.000 35.97195 ?  160 LEU A CD2 1 
ATOM   1149 N N   . PHE A 1 181 ? -12.25500 0.84700   35.01600 1.000 36.13594 ?  161 PHE A N   1 
ATOM   1150 C CA  . PHE A 1 181 ? -11.69400 -0.43000  35.41900 1.000 35.31998 ?  161 PHE A CA  1 
ATOM   1151 C C   . PHE A 1 181 ? -10.33900 -0.25500  36.10100 1.000 29.14340 ?  161 PHE A C   1 
ATOM   1152 O O   . PHE A 1 181 ? -10.13600 -0.73500  37.21900 1.000 32.96507 ?  161 PHE A O   1 
ATOM   1153 C CB  . PHE A 1 181 ? -11.58900 -1.34700  34.19200 1.000 28.27073 ?  161 PHE A CB  1 
ATOM   1154 C CG  . PHE A 1 181 ? -10.59700 -2.46500  34.34600 1.000 33.45721 ?  161 PHE A CG  1 
ATOM   1155 C CD1 . PHE A 1 181 ? -10.84200 -3.51300  35.22100 1.000 32.52534 ?  161 PHE A CD1 1 
ATOM   1156 C CD2 . PHE A 1 181 ? -9.43900  -2.48900  33.58900 1.000 32.61451 ?  161 PHE A CD2 1 
ATOM   1157 C CE1 . PHE A 1 181 ? -9.93700  -4.54900  35.35900 1.000 28.44373 ?  161 PHE A CE1 1 
ATOM   1158 C CE2 . PHE A 1 181 ? -8.53000  -3.52600  33.71500 1.000 37.07644 ?  161 PHE A CE2 1 
ATOM   1159 C CZ  . PHE A 1 181 ? -8.77900  -4.55600  34.60300 1.000 35.49162 ?  161 PHE A CZ  1 
ATOM   1160 N N   . LEU A 1 182 ? -9.41800  0.46800   35.45900 1.000 30.72637 ?  162 LEU A N   1 
ATOM   1161 C CA  . LEU A 1 182 ? -8.03900  0.51900   35.93600 1.000 32.78495 ?  162 LEU A CA  1 
ATOM   1162 C C   . LEU A 1 182 ? -7.91300  1.26600   37.25900 1.000 33.94873 ?  162 LEU A C   1 
ATOM   1163 O O   . LEU A 1 182 ? -7.11100  0.87700   38.11600 1.000 31.44779 ?  162 LEU A O   1 
ATOM   1164 C CB  . LEU A 1 182 ? -7.14800  1.16600   34.87700 1.000 38.30529 ?  162 LEU A CB  1 
ATOM   1165 C CG  . LEU A 1 182 ? -7.02100  0.43500   33.53800 1.000 37.89950 ?  162 LEU A CG  1 
ATOM   1166 C CD1 . LEU A 1 182 ? -6.52500  1.39900   32.47100 1.000 35.57963 ?  162 LEU A CD1 1 
ATOM   1167 C CD2 . LEU A 1 182 ? -6.09800  -0.76900  33.65300 1.000 31.92809 ?  162 LEU A CD2 1 
ATOM   1168 N N   . GLU A 1 183 ? -8.67600  2.35100   37.44300 1.000 32.56056 ?  163 GLU A N   1 
ATOM   1169 C CA  . GLU A 1 183 ? -8.52400  3.16800   38.64400 1.000 35.84631 ?  163 GLU A CA  1 
ATOM   1170 C C   . GLU A 1 183 ? -9.08900  2.49500   39.88800 1.000 34.56819 ?  163 GLU A C   1 
ATOM   1171 O O   . GLU A 1 183 ? -8.72700  2.88300   41.00400 1.000 33.01966 ?  163 GLU A O   1 
ATOM   1172 C CB  . GLU A 1 183 ? -9.18900  4.53900   38.45000 1.000 30.10294 ?  163 GLU A CB  1 
ATOM   1173 C CG  . GLU A 1 183 ? -8.55900  5.38000   37.33300 1.000 33.74934 ?  163 GLU A CG  1 
ATOM   1174 C CD  . GLU A 1 183 ? -9.04300  6.83300   37.30100 1.000 39.60571 ?  163 GLU A CD  1 
ATOM   1175 O OE1 . GLU A 1 183 ? -10.02900 7.17000   37.99400 1.000 35.84489 ?  163 GLU A OE1 1 
ATOM   1176 O OE2 . GLU A 1 183 ? -8.43700  7.64200   36.56100 1.000 42.77575 -1 163 GLU A OE2 1 
ATOM   1177 N N   . ASN A 1 184 ? -9.94500  1.48500   39.72600 1.000 31.77306 ?  164 ASN A N   1 
ATOM   1178 C CA  . ASN A 1 184 ? -10.62000 0.85100   40.84900 1.000 34.84145 ?  164 ASN A CA  1 
ATOM   1179 C C   . ASN A 1 184 ? -10.24000 -0.60500  41.06800 1.000 31.64549 ?  164 ASN A C   1 
ATOM   1180 O O   . ASN A 1 184 ? -10.54600 -1.14400  42.13700 1.000 36.33614 ?  164 ASN A O   1 
ATOM   1181 C CB  . ASN A 1 184 ? -12.14500 0.94300   40.67100 1.000 29.54572 ?  164 ASN A CB  1 
ATOM   1182 C CG  . ASN A 1 184 ? -12.63900 2.37700   40.65700 1.000 38.40241 ?  164 ASN A CG  1 
ATOM   1183 O OD1 . ASN A 1 184 ? -12.55700 3.07900   41.66500 1.000 36.92439 ?  164 ASN A OD1 1 
ATOM   1184 N ND2 . ASN A 1 184 ? -13.13700 2.82800   39.50800 1.000 35.57721 ?  164 ASN A ND2 1 
ATOM   1185 N N   . ILE A 1 185 ? -9.56200  -1.24700  40.11100 1.000 33.13480 ?  165 ILE A N   1 
ATOM   1186 C CA  . ILE A 1 185 ? -9.35000  -2.68900  40.17900 1.000 30.58801 ?  165 ILE A CA  1 
ATOM   1187 C C   . ILE A 1 185 ? -8.52000  -3.10800  41.38600 1.000 29.97480 ?  165 ILE A C   1 
ATOM   1188 O O   . ILE A 1 185 ? -8.65200  -4.24700  41.85200 1.000 30.16229 ?  165 ILE A O   1 
ATOM   1189 C CB  . ILE A 1 185 ? -8.70600  -3.19800  38.87400 1.000 28.64530 ?  165 ILE A CB  1 
ATOM   1190 C CG1 . ILE A 1 185 ? -8.91600  -4.70800  38.75000 1.000 27.75161 ?  165 ILE A CG1 1 
ATOM   1191 C CG2 . ILE A 1 185 ? -7.22900  -2.81200  38.79900 1.000 32.74813 ?  165 ILE A CG2 1 
ATOM   1192 C CD1 . ILE A 1 185 ? -10.37500 -5.12100  38.92600 1.000 26.33680 ?  165 ILE A CD1 1 
ATOM   1193 N N   . HIS A 1 186 ? -7.68000  -2.21800  41.92200 1.000 31.49305 ?  166 HIS A N   1 
ATOM   1194 C CA  . HIS A 1 186 ? -6.88800  -2.56300  43.09800 1.000 34.11216 ?  166 HIS A CA  1 
ATOM   1195 C C   . HIS A 1 186 ? -7.75800  -2.92300  44.29800 1.000 33.46845 ?  166 HIS A C   1 
ATOM   1196 O O   . HIS A 1 186 ? -7.29500  -3.63900  45.19200 1.000 32.91002 ?  166 HIS A O   1 
ATOM   1197 C CB  . HIS A 1 186 ? -5.96000  -1.40500  43.46200 1.000 32.78507 ?  166 HIS A CB  1 
ATOM   1198 C CG  . HIS A 1 186 ? -6.68600  -0.18900  43.94500 1.000 35.47907 ?  166 HIS A CG  1 
ATOM   1199 N ND1 . HIS A 1 186 ? -7.40800  0.62800   43.10200 1.000 32.97342 ?  166 HIS A ND1 1 
ATOM   1200 C CD2 . HIS A 1 186 ? -6.80600  0.34700   45.18200 1.000 35.85231 ?  166 HIS A CD2 1 
ATOM   1201 C CE1 . HIS A 1 186 ? -7.94500  1.61300   43.79900 1.000 34.39361 ?  166 HIS A CE1 1 
ATOM   1202 N NE2 . HIS A 1 186 ? -7.59300  1.46700   45.06400 1.000 37.00147 ?  166 HIS A NE2 1 
ATOM   1203 N N   . LYS A 1 187 ? -9.00300  -2.44500  44.34600 1.000 31.40809 ?  167 LYS A N   1 
ATOM   1204 C CA  . LYS A 1 187 ? -9.87600  -2.78000  45.46400 1.000 35.25537 ?  167 LYS A CA  1 
ATOM   1205 C C   . LYS A 1 187 ? -10.35600 -4.22500  45.42500 1.000 37.73521 ?  167 LYS A C   1 
ATOM   1206 O O   . LYS A 1 187 ? -10.86700 -4.71400  46.43800 1.000 34.99471 ?  167 LYS A O   1 
ATOM   1207 C CB  . LYS A 1 187 ? -11.07700 -1.82900  45.50200 1.000 35.99854 ?  167 LYS A CB  1 
ATOM   1208 C CG  . LYS A 1 187 ? -10.70800 -0.35800  45.70300 1.000 39.31714 ?  167 LYS A CG  1 
ATOM   1209 C CD  . LYS A 1 187 ? -11.86600 0.57100   45.33800 1.000 36.51635 ?  167 LYS A CD  1 
ATOM   1210 N N   . ARG A 1 188 ? -10.19200 -4.91700  44.29800 1.000 33.74889 ?  168 ARG A N   1 
ATOM   1211 C CA  . ARG A 1 188 ? -10.60500 -6.30600  44.15400 1.000 31.71366 ?  168 ARG A CA  1 
ATOM   1212 C C   . ARG A 1 188 ? -9.45000  -7.28700  44.29700 1.000 32.54894 ?  168 ARG A C   1 
ATOM   1213 O O   . ARG A 1 188 ? -9.66800  -8.50000  44.19700 1.000 31.37653 ?  168 ARG A O   1 
ATOM   1214 C CB  . ARG A 1 188 ? -11.28600 -6.50500  42.79600 1.000 35.22812 ?  168 ARG A CB  1 
ATOM   1215 C CG  . ARG A 1 188 ? -12.23800 -5.38100  42.43400 1.000 33.27780 ?  168 ARG A CG  1 
ATOM   1216 C CD  . ARG A 1 188 ? -13.44100 -5.39000  43.35000 1.000 38.37303 ?  168 ARG A CD  1 
ATOM   1217 N NE  . ARG A 1 188 ? -14.48500 -4.47900  42.90200 1.000 42.40186 ?  168 ARG A NE  1 
ATOM   1218 C CZ  . ARG A 1 188 ? -15.68300 -4.86300  42.48700 1.000 38.53651 ?  168 ARG A CZ  1 
ATOM   1219 N NH1 . ARG A 1 188 ? -16.00200 -6.14500  42.38800 1.000 34.57047 ?  168 ARG A NH1 1 
ATOM   1220 N NH2 . ARG A 1 188 ? -16.58200 -3.93800  42.16700 1.000 35.88244 ?  168 ARG A NH2 1 
ATOM   1221 N N   . ILE A 1 189 ? -8.23100  -6.79400  44.51900 1.000 31.73230 ?  169 ILE A N   1 
ATOM   1222 C CA  . ILE A 1 189 ? -7.03000  -7.61900  44.60700 1.000 33.20780 ?  169 ILE A CA  1 
ATOM   1223 C C   . ILE A 1 189 ? -6.52500  -7.61800  46.04100 1.000 36.32082 ?  169 ILE A C   1 
ATOM   1224 O O   . ILE A 1 189 ? -6.52000  -6.57600  46.70500 1.000 40.96619 ?  169 ILE A O   1 
ATOM   1225 C CB  . ILE A 1 189 ? -5.92200  -7.11500  43.66100 1.000 38.64428 ?  169 ILE A CB  1 
ATOM   1226 C CG1 . ILE A 1 189 ? -6.46200  -6.90200  42.24100 1.000 33.26991 ?  169 ILE A CG1 1 
ATOM   1227 C CG2 . ILE A 1 189 ? -4.73100  -8.06800  43.68000 1.000 31.07058 ?  169 ILE A CG2 1 
ATOM   1228 C CD1 . ILE A 1 189 ? -5.38200  -6.51300  41.24900 1.000 33.75556 ?  169 ILE A CD1 1 
ATOM   1229 N N   . ASN A 1 190 ? -6.07600  -8.78300  46.50500 1.000 39.99455 ?  170 ASN A N   1 
ATOM   1230 C CA  . ASN A 1 190 ? -5.47100  -8.89900  47.82100 1.000 37.26517 ?  170 ASN A CA  1 
ATOM   1231 C C   . ASN A 1 190 ? -4.11400  -8.20300  47.85900 1.000 41.83616 ?  170 ASN A C   1 
ATOM   1232 O O   . ASN A 1 190 ? -3.48400  -7.94600  46.82900 1.000 39.98268 ?  170 ASN A O   1 
ATOM   1233 C CB  . ASN A 1 190 ? -5.30100  -10.36500 48.20900 1.000 33.61063 ?  170 ASN A CB  1 
ATOM   1234 C CG  . ASN A 1 190 ? -6.61500  -11.10100 48.28200 1.000 40.95669 ?  170 ASN A CG  1 
ATOM   1235 O OD1 . ASN A 1 190 ? -7.61000  -10.55700 48.75600 1.000 41.22781 ?  170 ASN A OD1 1 
ATOM   1236 N ND2 . ASN A 1 190 ? -6.62700  -12.35200 47.82600 1.000 38.00305 ?  170 ASN A ND2 1 
ATOM   1237 N N   . GLU A 1 191 ? -3.67000  -7.89200  49.07700 1.000 46.45088 ?  171 GLU A N   1 
ATOM   1238 C CA  . GLU A 1 191 ? -2.33200  -7.34900  49.26700 1.000 42.45966 ?  171 GLU A CA  1 
ATOM   1239 C C   . GLU A 1 191 ? -1.30000  -8.33900  48.74600 1.000 39.39795 ?  171 GLU A C   1 
ATOM   1240 O O   . GLU A 1 191 ? -1.47100  -9.55700  48.85800 1.000 47.41123 ?  171 GLU A O   1 
ATOM   1241 C CB  . GLU A 1 191 ? -2.08300  -7.04800  50.74700 1.000 48.30357 ?  171 GLU A CB  1 
ATOM   1242 N N   . LYS A 1 192 ? -0.23800  -7.81000  48.14400 1.000 46.09221 ?  172 LYS A N   1 
ATOM   1243 C CA  . LYS A 1 192 ? 0.77300   -8.59200  47.43900 1.000 47.56902 ?  172 LYS A CA  1 
ATOM   1244 C C   . LYS A 1 192 ? 0.19400   -9.36200  46.25400 1.000 45.94232 ?  172 LYS A C   1 
ATOM   1245 O O   . LYS A 1 192 ? 0.87900   -10.22100 45.68500 1.000 45.73177 ?  172 LYS A O   1 
ATOM   1246 C CB  . LYS A 1 192 ? 1.50400   -9.55400  48.38800 1.000 44.80691 ?  172 LYS A CB  1 
ATOM   1247 N N   . GLY A 1 193 ? -1.05400  -9.08400  45.87100 1.000 39.90390 ?  173 GLY A N   1 
ATOM   1248 C CA  . GLY A 1 193 ? -1.64700  -9.68600  44.69700 1.000 35.33460 ?  173 GLY A CA  1 
ATOM   1249 C C   . GLY A 1 193 ? -1.14100  -9.04400  43.41800 1.000 37.52442 ?  173 GLY A C   1 
ATOM   1250 O O   . GLY A 1 193 ? -0.34100  -8.10700  43.42200 1.000 34.77881 ?  173 GLY A O   1 
ATOM   1251 N N   . TYR A 1 194 ? -1.63100  -9.56000  42.29100 1.000 36.65100 ?  174 TYR A N   1 
ATOM   1252 C CA  . TYR A 1 194 ? -1.12900  -9.14200  40.99100 1.000 33.25418 ?  174 TYR A CA  1 
ATOM   1253 C C   . TYR A 1 194 ? -2.27300  -8.76900  40.06200 1.000 37.49115 ?  174 TYR A C   1 
ATOM   1254 O O   . TYR A 1 194 ? -3.33800  -9.39200  40.07800 1.000 33.87692 ?  174 TYR A O   1 
ATOM   1255 C CB  . TYR A 1 194 ? -0.28000  -10.24100 40.34200 1.000 31.74067 ?  174 TYR A CB  1 
ATOM   1256 C CG  . TYR A 1 194 ? 1.11500   -10.37600 40.92100 1.000 34.66662 ?  174 TYR A CG  1 
ATOM   1257 C CD1 . TYR A 1 194 ? 1.34200   -11.11700 42.07300 1.000 39.45366 ?  174 TYR A CD1 1 
ATOM   1258 C CD2 . TYR A 1 194 ? 2.20400   -9.77400  40.30800 1.000 36.51136 ?  174 TYR A CD2 1 
ATOM   1259 C CE1 . TYR A 1 194 ? 2.61400   -11.24800 42.60500 1.000 35.50863 ?  174 TYR A CE1 1 
ATOM   1260 C CE2 . TYR A 1 194 ? 3.48200   -9.89800  40.83100 1.000 39.93052 ?  174 TYR A CE2 1 
ATOM   1261 C CZ  . TYR A 1 194 ? 3.67900   -10.63700 41.98300 1.000 40.89619 ?  174 TYR A CZ  1 
ATOM   1262 O OH  . TYR A 1 194 ? 4.94400   -10.76900 42.51100 1.000 45.19521 ?  174 TYR A OH  1 
ATOM   1263 N N   . LEU A 1 195 ? -2.04300  -7.73700  39.26300 1.000 30.53381 ?  175 LEU A N   1 
ATOM   1264 C CA  . LEU A 1 195 ? -2.86700  -7.41300  38.11100 1.000 30.45573 ?  175 LEU A CA  1 
ATOM   1265 C C   . LEU A 1 195 ? -2.00200  -7.63200  36.88100 1.000 31.80659 ?  175 LEU A C   1 
ATOM   1266 O O   . LEU A 1 195 ? -0.89800  -7.08400  36.79200 1.000 29.99705 ?  175 LEU A O   1 
ATOM   1267 C CB  . LEU A 1 195 ? -3.37100  -5.97000  38.16800 1.000 27.60809 ?  175 LEU A CB  1 
ATOM   1268 C CG  . LEU A 1 195 ? -4.01600  -5.42800  36.88500 1.000 30.78414 ?  175 LEU A CG  1 
ATOM   1269 C CD1 . LEU A 1 195 ? -5.45800  -5.90600  36.77200 1.000 31.16924 ?  175 LEU A CD1 1 
ATOM   1270 C CD2 . LEU A 1 195 ? -3.95800  -3.90900  36.84000 1.000 28.07674 ?  175 LEU A CD2 1 
ATOM   1271 N N   . ILE A 1 196 ? -2.47700  -8.45400  35.95400 1.000 30.78906 ?  176 ILE A N   1 
ATOM   1272 C CA  . ILE A 1 196 ? -1.74200  -8.73400  34.73000 1.000 29.76882 ?  176 ILE A CA  1 
ATOM   1273 C C   . ILE A 1 196 ? -2.60500  -8.29900  33.56100 1.000 31.68619 ?  176 ILE A C   1 
ATOM   1274 O O   . ILE A 1 196 ? -3.75400  -8.73800  33.42700 1.000 31.03064 ?  176 ILE A O   1 
ATOM   1275 C CB  . ILE A 1 196 ? -1.34500  -10.21200 34.62000 1.000 28.03107 ?  176 ILE A CB  1 
ATOM   1276 C CG1 . ILE A 1 196 ? -0.33000  -10.54000 35.71800 1.000 28.34445 ?  176 ILE A CG1 1 
ATOM   1277 C CG2 . ILE A 1 196 ? -0.75600  -10.49500 33.24300 1.000 29.61443 ?  176 ILE A CG2 1 
ATOM   1278 C CD1 . ILE A 1 196 ? 0.10600   -11.98400 35.76100 1.000 29.44909 ?  176 ILE A CD1 1 
ATOM   1279 N N   . LEU A 1 197 ? -2.06000  -7.41600  32.73500 1.000 27.20926 ?  177 LEU A N   1 
ATOM   1280 C CA  . LEU A 1 197 ? -2.74800  -6.89300  31.57000 1.000 27.34535 ?  177 LEU A CA  1 
ATOM   1281 C C   . LEU A 1 197 ? -1.98600  -7.29100  30.32100 1.000 29.02221 ?  177 LEU A C   1 
ATOM   1282 O O   . LEU A 1 197 ? -0.75300  -7.28800  30.30400 1.000 31.36484 ?  177 LEU A O   1 
ATOM   1283 C CB  . LEU A 1 197 ? -2.85700  -5.37100  31.61500 1.000 25.16572 ?  177 LEU A CB  1 
ATOM   1284 C CG  . LEU A 1 197 ? -3.52900  -4.72300  32.81600 1.000 32.41923 ?  177 LEU A CG  1 
ATOM   1285 C CD1 . LEU A 1 197 ? -3.32400  -3.22800  32.71600 1.000 27.00129 ?  177 LEU A CD1 1 
ATOM   1286 C CD2 . LEU A 1 197 ? -5.00200  -5.07100  32.87300 1.000 25.38106 ?  177 LEU A CD2 1 
ATOM   1287 N N   . THR A 1 198 ? -2.72700  -7.63100  29.28200 1.000 25.21486 ?  178 THR A N   1 
ATOM   1288 C CA  . THR A 1 198 ? -2.18400  -7.79500  27.94700 1.000 32.20306 ?  178 THR A CA  1 
ATOM   1289 C C   . THR A 1 198 ? -3.02300  -6.95900  26.99900 1.000 30.82432 ?  178 THR A C   1 
ATOM   1290 O O   . THR A 1 198 ? -4.24600  -6.87700  27.15300 1.000 34.01374 ?  178 THR A O   1 
ATOM   1291 C CB  . THR A 1 198 ? -2.20500  -9.25500  27.49800 1.000 32.41373 ?  178 THR A CB  1 
ATOM   1292 O OG1 . THR A 1 198 ? -3.56400  -9.64800  27.25900 1.000 39.50192 ?  178 THR A OG1 1 
ATOM   1293 C CG2 . THR A 1 198 ? -1.60200  -10.14500 28.56500 1.000 33.38831 ?  178 THR A CG2 1 
ATOM   1294 N N   . SER A 1 199 ? -2.36500  -6.33900  26.02000 1.000 28.59342 ?  179 SER A N   1 
ATOM   1295 C CA  . SER A 1 199 ? -3.10900  -5.53000  25.07100 1.000 30.04757 ?  179 SER A CA  1 
ATOM   1296 C C   . SER A 1 199 ? -2.22500  -5.23900  23.87600 1.000 29.42535 ?  179 SER A C   1 
ATOM   1297 O O   . SER A 1 199 ? -1.03100  -4.97400  24.06100 1.000 31.57301 ?  179 SER A O   1 
ATOM   1298 C CB  . SER A 1 199 ? -3.57700  -4.21500  25.70800 1.000 28.69465 ?  179 SER A CB  1 
ATOM   1299 O OG  . SER A 1 199 ? -4.22100  -3.39500  24.75500 1.000 35.14942 ?  179 SER A OG  1 
ATOM   1300 N N   . PRO A 1 200 ? -2.75600  -5.29300  22.65200 1.000 29.43555 ?  180 PRO A N   1 
ATOM   1301 C CA  . PRO A 1 200 ? -2.03000  -4.75700  21.49800 1.000 28.96370 ?  180 PRO A CA  1 
ATOM   1302 C C   . PRO A 1 200 ? -2.13800  -3.24900  21.35700 1.000 30.46662 ?  180 PRO A C   1 
ATOM   1303 O O   . PRO A 1 200 ? -1.56200  -2.69400  20.41500 1.000 29.88548 ?  180 PRO A O   1 
ATOM   1304 C CB  . PRO A 1 200 ? -2.71500  -5.45500  20.32300 1.000 30.69343 ?  180 PRO A CB  1 
ATOM   1305 C CG  . PRO A 1 200 ? -4.12300  -5.59700  20.77700 1.000 30.37733 ?  180 PRO A CG  1 
ATOM   1306 C CD  . PRO A 1 200 ? -4.03100  -5.91400  22.25400 1.000 34.10997 ?  180 PRO A CD  1 
ATOM   1307 N N   . TYR A 1 201 ? -2.88000  -2.58300  22.24400 1.000 30.60022 ?  181 TYR A N   1 
ATOM   1308 C CA  . TYR A 1 201 ? -3.03100  -1.12600  22.20700 1.000 34.81614 ?  181 TYR A CA  1 
ATOM   1309 C C   . TYR A 1 201 ? -3.66800  -0.66800  20.89600 1.000 29.76097 ?  181 TYR A C   1 
ATOM   1310 O O   . TYR A 1 201 ? -3.25700  0.32600   20.29000 1.000 30.81091 ?  181 TYR A O   1 
ATOM   1311 C CB  . TYR A 1 201 ? -1.69200  -0.42300  22.43800 1.000 24.83328 ?  181 TYR A CB  1 
ATOM   1312 C CG  . TYR A 1 201 ? -0.93600  -0.91100  23.65700 1.000 27.18784 ?  181 TYR A CG  1 
ATOM   1313 C CD1 . TYR A 1 201 ? -1.60100  -1.22100  24.83800 1.000 26.34365 ?  181 TYR A CD1 1 
ATOM   1314 C CD2 . TYR A 1 201 ? 0.44600   -1.05100  23.62800 1.000 24.14947 ?  181 TYR A CD2 1 
ATOM   1315 C CE1 . TYR A 1 201 ? -0.91000  -1.65900  25.95500 1.000 19.53733 ?  181 TYR A CE1 1 
ATOM   1316 C CE2 . TYR A 1 201 ? 1.14600   -1.48400  24.73800 1.000 29.19903 ?  181 TYR A CE2 1 
ATOM   1317 C CZ  . TYR A 1 201 ? 0.46300   -1.78900  25.89800 1.000 30.06890 ?  181 TYR A CZ  1 
ATOM   1318 O OH  . TYR A 1 201 ? 1.16400   -2.22200  27.00100 1.000 29.89614 ?  181 TYR A OH  1 
ATOM   1319 N N   . THR A 1 202 ? -4.68900  -1.39700  20.45500 1.000 33.69083 ?  182 THR A N   1 
ATOM   1320 C CA  . THR A 1 202 ? -5.41600  -1.05800  19.23000 1.000 37.21551 ?  182 THR A CA  1 
ATOM   1321 C C   . THR A 1 202 ? -6.63300  -0.20400  19.59000 1.000 33.37573 ?  182 THR A C   1 
ATOM   1322 O O   . THR A 1 202 ? -7.78800  -0.62100  19.50100 1.000 41.67695 ?  182 THR A O   1 
ATOM   1323 C CB  . THR A 1 202 ? -5.81600  -2.32300  18.48000 1.000 37.30080 ?  182 THR A CB  1 
ATOM   1324 O OG1 . THR A 1 202 ? -6.61200  -3.14800  19.33400 1.000 44.31615 ?  182 THR A OG1 1 
ATOM   1325 C CG2 . THR A 1 202 ? -4.58000  -3.10500  18.06800 1.000 39.80368 ?  182 THR A CG2 1 
ATOM   1326 N N   . TRP A 1 203 ? -6.34500  1.02400   20.01300 1.000 35.88246 ?  183 TRP A N   1 
ATOM   1327 C CA  . TRP A 1 203 ? -7.40100  1.95800   20.37800 1.000 34.32268 ?  183 TRP A CA  1 
ATOM   1328 C C   . TRP A 1 203 ? -8.19700  2.34800   19.13900 1.000 32.70640 ?  183 TRP A C   1 
ATOM   1329 O O   . TRP A 1 203 ? -7.62300  2.63800   18.08500 1.000 34.03609 ?  183 TRP A O   1 
ATOM   1330 C CB  . TRP A 1 203 ? -6.80400  3.19000   21.05700 1.000 26.40660 ?  183 TRP A CB  1 
ATOM   1331 C CG  . TRP A 1 203 ? -6.07600  2.84100   22.31800 1.000 26.56478 ?  183 TRP A CG  1 
ATOM   1332 C CD1 . TRP A 1 203 ? -4.72600  2.73600   22.48400 1.000 27.01754 ?  183 TRP A CD1 1 
ATOM   1333 C CD2 . TRP A 1 203 ? -6.66300  2.50700   23.58400 1.000 29.56904 ?  183 TRP A CD2 1 
ATOM   1334 N NE1 . TRP A 1 203 ? -4.43500  2.37600   23.77500 1.000 32.13659 ?  183 TRP A NE1 1 
ATOM   1335 C CE2 . TRP A 1 203 ? -5.60600  2.22900   24.47200 1.000 26.95164 ?  183 TRP A CE2 1 
ATOM   1336 C CE3 . TRP A 1 203 ? -7.98000  2.42700   24.05300 1.000 26.55865 ?  183 TRP A CE3 1 
ATOM   1337 C CZ2 . TRP A 1 203 ? -5.82200  1.87100   25.80000 1.000 24.49927 ?  183 TRP A CZ2 1 
ATOM   1338 C CZ3 . TRP A 1 203 ? -8.19300  2.07800   25.37400 1.000 28.68751 ?  183 TRP A CZ3 1 
ATOM   1339 C CH2 . TRP A 1 203 ? -7.11800  1.79900   26.23300 1.000 28.67388 ?  183 TRP A CH2 1 
ATOM   1340 N N   . ARG A 1 204 ? -9.52300  2.33300   19.26600 1.000 35.86390 ?  184 ARG A N   1 
ATOM   1341 C CA  . ARG A 1 204 ? -10.42700 2.57100   18.14800 1.000 37.89278 ?  184 ARG A CA  1 
ATOM   1342 C C   . ARG A 1 204 ? -11.68600 3.24700   18.66800 1.000 38.32778 ?  184 ARG A C   1 
ATOM   1343 O O   . ARG A 1 204 ? -12.21800 2.86100   19.71200 1.000 33.67433 ?  184 ARG A O   1 
ATOM   1344 C CB  . ARG A 1 204 ? -10.79700 1.26600   17.42800 1.000 39.86330 ?  184 ARG A CB  1 
ATOM   1345 C CG  . ARG A 1 204 ? -9.83400  0.85000   16.32700 1.000 43.70748 ?  184 ARG A CG  1 
ATOM   1346 C CD  . ARG A 1 204 ? -10.08600 -0.58800  15.86700 1.000 52.06342 ?  184 ARG A CD  1 
ATOM   1347 N NE  . ARG A 1 204 ? -10.98300 -0.66700  14.71700 1.000 54.76335 ?  184 ARG A NE  1 
ATOM   1348 N N   . GLU A 1 205 ? -12.16800 4.24300   17.92300 1.000 37.08020 ?  185 GLU A N   1 
ATOM   1349 C CA  . GLU A 1 205 ? -13.33700 5.00100   18.35600 1.000 38.82280 ?  185 GLU A CA  1 
ATOM   1350 C C   . GLU A 1 205 ? -14.61300 4.16700   18.36100 1.000 36.29104 ?  185 GLU A C   1 
ATOM   1351 O O   . GLU A 1 205 ? -15.55800 4.51500   19.07200 1.000 37.15617 ?  185 GLU A O   1 
ATOM   1352 C CB  . GLU A 1 205 ? -13.50800 6.24800   17.48100 1.000 42.57902 ?  185 GLU A CB  1 
ATOM   1353 C CG  . GLU A 1 205 ? -12.36800 7.25300   17.64700 1.000 44.32608 ?  185 GLU A CG  1 
ATOM   1354 C CD  . GLU A 1 205 ? -12.50500 8.48000   16.76100 1.000 63.55452 ?  185 GLU A CD  1 
ATOM   1355 O OE1 . GLU A 1 205 ? -13.61400 8.71700   16.23100 1.000 64.78593 ?  185 GLU A OE1 1 
ATOM   1356 O OE2 . GLU A 1 205 ? -11.49900 9.20700   16.58900 1.000 60.22148 -1 185 GLU A OE2 1 
ATOM   1357 N N   . GLU A 1 206 ? -14.66400 3.06800   17.60900 1.000 37.83878 ?  186 GLU A N   1 
ATOM   1358 C CA  . GLU A 1 206 ? -15.82200 2.18400   17.69300 1.000 37.44198 ?  186 GLU A CA  1 
ATOM   1359 C C   . GLU A 1 206 ? -15.94200 1.52400   19.06000 1.000 40.93309 ?  186 GLU A C   1 
ATOM   1360 O O   . GLU A 1 206 ? -17.03200 1.06700   19.42200 1.000 38.84867 ?  186 GLU A O   1 
ATOM   1361 C CB  . GLU A 1 206 ? -15.76100 1.10700   16.60300 1.000 32.39702 ?  186 GLU A CB  1 
ATOM   1362 C CG  . GLU A 1 206 ? -14.51500 0.24000   16.64200 1.000 46.48604 ?  186 GLU A CG  1 
ATOM   1363 N N   . TYR A 1 207 ? -14.85300 1.45600   19.82100 1.000 37.11464 ?  187 TYR A N   1 
ATOM   1364 C CA  . TYR A 1 207 ? -14.86700 0.88900   21.16300 1.000 36.81556 ?  187 TYR A CA  1 
ATOM   1365 C C   . TYR A 1 207 ? -14.71100 1.93500   22.25300 1.000 40.28465 ?  187 TYR A C   1 
ATOM   1366 O O   . TYR A 1 207 ? -15.42200 1.88400   23.26000 1.000 40.21814 ?  187 TYR A O   1 
ATOM   1367 C CB  . TYR A 1 207 ? -13.75100 -0.15200  21.31000 1.000 37.22298 ?  187 TYR A CB  1 
ATOM   1368 C CG  . TYR A 1 207 ? -14.05300 -1.48700  20.66000 1.000 40.81784 ?  187 TYR A CG  1 
ATOM   1369 C CD1 . TYR A 1 207 ? -14.90400 -2.40100  21.27100 1.000 46.18758 ?  187 TYR A CD1 1 
ATOM   1370 C CD2 . TYR A 1 207 ? -13.48000 -1.83500  19.44500 1.000 41.27634 ?  187 TYR A CD2 1 
ATOM   1371 C CE1 . TYR A 1 207 ? -15.18000 -3.62500  20.68400 1.000 53.29146 ?  187 TYR A CE1 1 
ATOM   1372 C CE2 . TYR A 1 207 ? -13.74900 -3.05400  18.85000 1.000 44.84776 ?  187 TYR A CE2 1 
ATOM   1373 C CZ  . TYR A 1 207 ? -14.59800 -3.94400  19.47500 1.000 49.16549 ?  187 TYR A CZ  1 
ATOM   1374 O OH  . TYR A 1 207 ? -14.87100 -5.15700  18.89300 1.000 59.21499 ?  187 TYR A OH  1 
ATOM   1375 N N   . THR A 1 208 ? -13.80100 2.88700   22.06400 1.000 36.28369 ?  188 THR A N   1 
ATOM   1376 C CA  . THR A 1 208 ? -13.44100 3.86300   23.07900 1.000 33.37446 ?  188 THR A CA  1 
ATOM   1377 C C   . THR A 1 208 ? -13.37000 5.23800   22.43900 1.000 33.76933 ?  188 THR A C   1 
ATOM   1378 O O   . THR A 1 208 ? -12.64500 5.42600   21.45900 1.000 31.57922 ?  188 THR A O   1 
ATOM   1379 C CB  . THR A 1 208 ? -12.08500 3.52400   23.71200 1.000 34.55970 ?  188 THR A CB  1 
ATOM   1380 O OG1 . THR A 1 208 ? -12.02400 2.12300   24.01200 1.000 30.38692 ?  188 THR A OG1 1 
ATOM   1381 C CG2 . THR A 1 208 ? -11.88100 4.32500   24.99400 1.000 29.80006 ?  188 THR A CG2 1 
ATOM   1382 N N   . ALA A 1 209 ? -14.11100 6.19600   22.99000 1.000 37.15673 ?  189 ALA A N   1 
ATOM   1383 C CA  . ALA A 1 209 ? -13.93500 7.58200   22.57400 1.000 36.76703 ?  189 ALA A CA  1 
ATOM   1384 C C   . ALA A 1 209 ? -12.48100 8.00500   22.77400 1.000 34.60572 ?  189 ALA A C   1 
ATOM   1385 O O   . ALA A 1 209 ? -11.81500 7.58400   23.72300 1.000 34.71216 ?  189 ALA A O   1 
ATOM   1386 C CB  . ALA A 1 209 ? -14.87300 8.50400   23.35700 1.000 29.44012 ?  189 ALA A CB  1 
ATOM   1387 N N   . LYS A 1 210 ? -11.99000 8.84400   21.85700 1.000 36.42574 ?  190 LYS A N   1 
ATOM   1388 C CA  . LYS A 1 210 ? -10.57300 9.20200   21.85500 1.000 33.83176 ?  190 LYS A CA  1 
ATOM   1389 C C   . LYS A 1 210 ? -10.14000 9.82200   23.17600 1.000 36.32955 ?  190 LYS A C   1 
ATOM   1390 O O   . LYS A 1 210 ? -9.02600  9.56800   23.64900 1.000 36.79786 ?  190 LYS A O   1 
ATOM   1391 C CB  . LYS A 1 210 ? -10.27600 10.15400  20.69800 1.000 39.60457 ?  190 LYS A CB  1 
ATOM   1392 C CG  . LYS A 1 210 ? -8.79600  10.38000  20.45400 1.000 43.48519 ?  190 LYS A CG  1 
ATOM   1393 C CD  . LYS A 1 210 ? -8.49600  10.38200  18.96900 1.000 55.02296 ?  190 LYS A CD  1 
ATOM   1394 C CE  . LYS A 1 210 ? -7.23400  11.15900  18.66400 1.000 51.24528 ?  190 LYS A CE  1 
ATOM   1395 N N   . LYS A 1 211 ? -11.00300 10.63800  23.78900 1.000 34.05096 ?  191 LYS A N   1 
ATOM   1396 C CA  . LYS A 1 211 ? -10.64000 11.28500  25.04500 1.000 35.02756 ?  191 LYS A CA  1 
ATOM   1397 C C   . LYS A 1 211 ? -10.33100 10.27600  26.14500 1.000 31.28030 ?  191 LYS A C   1 
ATOM   1398 O O   . LYS A 1 211 ? -9.69900  10.64000  27.14300 1.000 32.20747 ?  191 LYS A O   1 
ATOM   1399 C CB  . LYS A 1 211 ? -11.75800 12.23600  25.49300 1.000 32.35691 ?  191 LYS A CB  1 
ATOM   1400 C CG  . LYS A 1 211 ? -13.05100 11.53600  25.88700 1.000 40.22806 ?  191 LYS A CG  1 
ATOM   1401 C CD  . LYS A 1 211 ? -14.27100 12.45900  25.78800 1.000 47.15110 ?  191 LYS A CD  1 
ATOM   1402 C CE  . LYS A 1 211 ? -14.42100 13.37200  27.00000 1.000 46.94958 ?  191 LYS A CE  1 
ATOM   1403 N N   . PHE A 1 212 ? -10.72900 9.01400   25.97200 1.000 29.90241 ?  192 PHE A N   1 
ATOM   1404 C CA  . PHE A 1 212 ? -10.53200 7.98700   26.98400 1.000 32.45908 ?  192 PHE A CA  1 
ATOM   1405 C C   . PHE A 1 212 ? -9.42800  6.99500   26.63600 1.000 39.35707 ?  192 PHE A C   1 
ATOM   1406 O O   . PHE A 1 212 ? -9.18800  6.06300   27.41700 1.000 32.58942 ?  192 PHE A O   1 
ATOM   1407 C CB  . PHE A 1 212 ? -11.84800 7.23400   27.23300 1.000 29.37192 ?  192 PHE A CB  1 
ATOM   1408 C CG  . PHE A 1 212 ? -12.97500 8.11600   27.70700 1.000 34.65724 ?  192 PHE A CG  1 
ATOM   1409 C CD1 . PHE A 1 212 ? -12.79300 8.99500   28.76700 1.000 32.25118 ?  192 PHE A CD1 1 
ATOM   1410 C CD2 . PHE A 1 212 ? -14.22300 8.05200   27.09900 1.000 33.56619 ?  192 PHE A CD2 1 
ATOM   1411 C CE1 . PHE A 1 212 ? -13.83000 9.80300   29.20700 1.000 33.22745 ?  192 PHE A CE1 1 
ATOM   1412 C CE2 . PHE A 1 212 ? -15.26500 8.85600   27.53200 1.000 36.64830 ?  192 PHE A CE2 1 
ATOM   1413 C CZ  . PHE A 1 212 ? -15.06800 9.73300   28.58700 1.000 39.17463 ?  192 PHE A CZ  1 
ATOM   1414 N N   . TRP A 1 213 ? -8.75900  7.15500   25.49100 1.000 33.00254 ?  193 TRP A N   1 
ATOM   1415 C CA  . TRP A 1 213 ? -7.63000  6.29000   25.16500 1.000 28.33080 ?  193 TRP A CA  1 
ATOM   1416 C C   . TRP A 1 213 ? -6.53200  6.46100   26.21100 1.000 24.04587 ?  193 TRP A C   1 
ATOM   1417 O O   . TRP A 1 213 ? -6.18200  7.58400   26.58300 1.000 30.79892 ?  193 TRP A O   1 
ATOM   1418 C CB  . TRP A 1 213 ? -7.08500  6.61900   23.77200 1.000 27.30143 ?  193 TRP A CB  1 
ATOM   1419 C CG  . TRP A 1 213 ? -8.03400  6.34900   22.64000 1.000 30.59315 ?  193 TRP A CG  1 
ATOM   1420 C CD1 . TRP A 1 213 ? -9.32800  5.92800   22.73600 1.000 31.23007 ?  193 TRP A CD1 1 
ATOM   1421 C CD2 . TRP A 1 213 ? -7.76500  6.49700   21.23700 1.000 29.50918 ?  193 TRP A CD2 1 
ATOM   1422 N NE1 . TRP A 1 213 ? -9.87800  5.80100   21.48600 1.000 31.65029 ?  193 TRP A NE1 1 
ATOM   1423 C CE2 . TRP A 1 213 ? -8.93900  6.14300   20.54800 1.000 31.16792 ?  193 TRP A CE2 1 
ATOM   1424 C CE3 . TRP A 1 213 ? -6.64500  6.89700   20.50000 1.000 31.93321 ?  193 TRP A CE3 1 
ATOM   1425 C CZ2 . TRP A 1 213 ? -9.02700  6.16900   19.15500 1.000 34.19366 ?  193 TRP A CZ2 1 
ATOM   1426 C CZ3 . TRP A 1 213 ? -6.73400  6.92700   19.12000 1.000 35.60684 ?  193 TRP A CZ3 1 
ATOM   1427 C CH2 . TRP A 1 213 ? -7.91800  6.56300   18.46100 1.000 35.27760 ?  193 TRP A CH2 1 
ATOM   1428 N N   . ILE A 1 214 ? -5.99700  5.34000   26.70000 1.000 27.74180 ?  194 ILE A N   1 
ATOM   1429 C CA  . ILE A 1 214 ? -4.91300  5.40700   27.67700 1.000 31.45031 ?  194 ILE A CA  1 
ATOM   1430 C C   . ILE A 1 214 ? -3.60500  5.79500   26.99700 1.000 29.37035 ?  194 ILE A C   1 
ATOM   1431 O O   . ILE A 1 214 ? -2.70300  6.35600   27.62900 1.000 30.90502 ?  194 ILE A O   1 
ATOM   1432 C CB  . ILE A 1 214 ? -4.79000  4.06900   28.42800 1.000 28.71411 ?  194 ILE A CB  1 
ATOM   1433 C CG1 . ILE A 1 214 ? -6.10100  3.74500   29.13000 1.000 30.86850 ?  194 ILE A CG1 1 
ATOM   1434 C CG2 . ILE A 1 214 ? -3.64900  4.10900   29.43400 1.000 29.32067 ?  194 ILE A CG2 1 
ATOM   1435 C CD1 . ILE A 1 214 ? -6.60100  4.88000   30.00200 1.000 33.66758 ?  194 ILE A CD1 1 
ATOM   1436 N N   . GLY A 1 215 ? -3.48300  5.52100   25.71300 1.000 28.57401 ?  195 GLY A N   1 
ATOM   1437 C CA  . GLY A 1 215 ? -2.29900  5.88900   24.97400 1.000 30.14600 ?  195 GLY A CA  1 
ATOM   1438 C C   . GLY A 1 215 ? -2.60600  5.94100   23.50200 1.000 31.13961 ?  195 GLY A C   1 
ATOM   1439 O O   . GLY A 1 215 ? -3.76200  5.83400   23.09000 1.000 24.28108 ?  195 GLY A O   1 
ATOM   1440 N N   . GLY A 1 216 ? -1.55100  6.10000   22.70600 1.000 31.46162 ?  196 GLY A N   1 
ATOM   1441 C CA  . GLY A 1 216 ? -1.72300  6.18200   21.26600 1.000 30.22612 ?  196 GLY A CA  1 
ATOM   1442 C C   . GLY A 1 216 ? -2.29100  7.50000   20.79200 1.000 34.17400 ?  196 GLY A C   1 
ATOM   1443 O O   . GLY A 1 216 ? -2.97400  7.54300   19.76300 1.000 34.59201 ?  196 GLY A O   1 
ATOM   1444 N N   . TYR A 1 217 ? -2.03200  8.58300   21.52100 1.000 29.41526 ?  197 TYR A N   1 
ATOM   1445 C CA  . TYR A 1 217 ? -2.58100  9.88500   21.17500 1.000 31.28999 ?  197 TYR A CA  1 
ATOM   1446 C C   . TYR A 1 217 ? -1.56900  10.97700  21.48800 1.000 30.61553 ?  197 TYR A C   1 
ATOM   1447 O O   . TYR A 1 217 ? -0.66200  10.80800  22.30700 1.000 35.45758 ?  197 TYR A O   1 
ATOM   1448 C CB  . TYR A 1 217 ? -3.90000  10.15400  21.91700 1.000 30.88487 ?  197 TYR A CB  1 
ATOM   1449 C CG  . TYR A 1 217 ? -3.74700  10.32800  23.41000 1.000 30.85266 ?  197 TYR A CG  1 
ATOM   1450 C CD1 . TYR A 1 217 ? -3.75300  9.22800   24.25600 1.000 31.31583 ?  197 TYR A CD1 1 
ATOM   1451 C CD2 . TYR A 1 217 ? -3.61400  11.59300  23.97900 1.000 32.19188 ?  197 TYR A CD2 1 
ATOM   1452 C CE1 . TYR A 1 217 ? -3.61400  9.37400   25.62200 1.000 32.96359 ?  197 TYR A CE1 1 
ATOM   1453 C CE2 . TYR A 1 217 ? -3.47700  11.74800  25.34600 1.000 36.40569 ?  197 TYR A CE2 1 
ATOM   1454 C CZ  . TYR A 1 217 ? -3.47800  10.63200  26.16200 1.000 35.90392 ?  197 TYR A CZ  1 
ATOM   1455 O OH  . TYR A 1 217 ? -3.34100  10.76900  27.52400 1.000 38.87530 ?  197 TYR A OH  1 
ATOM   1456 N N   . VAL A 1 218 ? -1.73400  12.10200  20.80500 1.000 31.35497 ?  198 VAL A N   1 
ATOM   1457 C CA  . VAL A 1 218 ? -0.99300  13.32100  21.09800 1.000 36.06974 ?  198 VAL A CA  1 
ATOM   1458 C C   . VAL A 1 218 ? -1.80400  14.12900  22.10500 1.000 33.01463 ?  198 VAL A C   1 
ATOM   1459 O O   . VAL A 1 218 ? -2.96500  14.46400  21.84800 1.000 38.29858 ?  198 VAL A O   1 
ATOM   1460 C CB  . VAL A 1 218 ? -0.73800  14.13200  19.82000 1.000 33.92215 ?  198 VAL A CB  1 
ATOM   1461 C CG1 . VAL A 1 218 ? 0.00800   15.42600  20.14800 1.000 30.19268 ?  198 VAL A CG1 1 
ATOM   1462 C CG2 . VAL A 1 218 ? 0.01900   13.29700  18.79600 1.000 29.40272 ?  198 VAL A CG2 1 
ATOM   1463 N N   . ASP A 1 219 ? -1.20100  14.44400  23.24900 1.000 35.85823 ?  199 ASP A N   1 
ATOM   1464 C CA  . ASP A 1 219 ? -1.92800  15.15700  24.29100 1.000 38.49659 ?  199 ASP A CA  1 
ATOM   1465 C C   . ASP A 1 219 ? -2.01500  16.65000  23.96800 1.000 39.94775 ?  199 ASP A C   1 
ATOM   1466 O O   . ASP A 1 219 ? -1.50600  17.12900  22.95000 1.000 37.71615 ?  199 ASP A O   1 
ATOM   1467 C CB  . ASP A 1 219 ? -1.29300  14.90700  25.66100 1.000 36.96961 ?  199 ASP A CB  1 
ATOM   1468 C CG  . ASP A 1 219 ? 0.11500   15.49200  25.79800 1.000 42.17812 ?  199 ASP A CG  1 
ATOM   1469 O OD1 . ASP A 1 219 ? 0.51200   16.38400  25.02000 1.000 45.57831 ?  199 ASP A OD1 1 
ATOM   1470 O OD2 . ASP A 1 219 ? 0.83200   15.05600  26.72200 1.000 49.02604 -1 199 ASP A OD2 1 
ATOM   1471 N N   . GLU A 1 220 ? -2.66000  17.39800  24.86500 1.000 41.82168 ?  200 GLU A N   1 
ATOM   1472 C CA  . GLU A 1 220 ? -2.86400  18.82900  24.67700 1.000 42.14179 ?  200 GLU A CA  1 
ATOM   1473 C C   . GLU A 1 220 ? -1.56300  19.62200  24.68800 1.000 41.60841 ?  200 GLU A C   1 
ATOM   1474 O O   . GLU A 1 220 ? -1.56400  20.78000  24.26000 1.000 49.13783 ?  200 GLU A O   1 
ATOM   1475 C CB  . GLU A 1 220 ? -3.80500  19.36500  25.75900 1.000 38.23055 ?  200 GLU A CB  1 
ATOM   1476 N N   . ASN A 1 221 ? -0.46700  19.03500  25.16600 1.000 37.92149 ?  201 ASN A N   1 
ATOM   1477 C CA  . ASN A 1 221 ? 0.83700   19.68300  25.18100 1.000 38.21434 ?  201 ASN A CA  1 
ATOM   1478 C C   . ASN A 1 221 ? 1.72600   19.24700  24.02200 1.000 36.35361 ?  201 ASN A C   1 
ATOM   1479 O O   . ASN A 1 221 ? 2.92900   19.52300  24.04100 1.000 36.27859 ?  201 ASN A O   1 
ATOM   1480 C CB  . ASN A 1 221 ? 1.54500   19.40900  26.51100 1.000 41.27255 ?  201 ASN A CB  1 
ATOM   1481 N N   . GLY A 1 222 ? 1.16800   18.57400  23.01800 1.000 37.69846 ?  202 GLY A N   1 
ATOM   1482 C CA  . GLY A 1 222 ? 1.94200   18.15300  21.86600 1.000 29.81688 ?  202 GLY A CA  1 
ATOM   1483 C C   . GLY A 1 222 ? 2.84500   16.96200  22.09600 1.000 35.17291 ?  202 GLY A C   1 
ATOM   1484 O O   . GLY A 1 222 ? 3.68400   16.66600  21.23900 1.000 34.57306 ?  202 GLY A O   1 
ATOM   1485 N N   . LYS A 1 223 ? 2.70700   16.27500  23.22600 1.000 31.52534 ?  203 LYS A N   1 
ATOM   1486 C CA  . LYS A 1 223 ? 3.50100   15.09400  23.52400 1.000 32.26191 ?  203 LYS A CA  1 
ATOM   1487 C C   . LYS A 1 223 ? 2.74900   13.84300  23.08700 1.000 41.57910 ?  203 LYS A C   1 
ATOM   1488 O O   . LYS A 1 223 ? 1.52200   13.76400  23.21400 1.000 36.71658 ?  203 LYS A O   1 
ATOM   1489 C CB  . LYS A 1 223 ? 3.82300   15.02600  25.02000 1.000 33.94004 ?  203 LYS A CB  1 
ATOM   1490 C CG  . LYS A 1 223 ? 4.76300   16.13300  25.50300 1.000 37.58329 ?  203 LYS A CG  1 
ATOM   1491 C CD  . LYS A 1 223 ? 4.68000   16.36000  27.01300 1.000 40.14515 ?  203 LYS A CD  1 
ATOM   1492 C CE  . LYS A 1 223 ? 6.06600   16.35800  27.65400 1.000 37.21675 ?  203 LYS A CE  1 
ATOM   1493 N N   . GLU A 1 224 ? 3.48700   12.87500  22.55100 1.000 31.90120 ?  204 GLU A N   1 
ATOM   1494 C CA  . GLU A 1 224 ? 2.90700   11.59100  22.18300 1.000 39.40338 ?  204 GLU A CA  1 
ATOM   1495 C C   . GLU A 1 224 ? 2.87500   10.69600  23.41200 1.000 33.84232 ?  204 GLU A C   1 
ATOM   1496 O O   . GLU A 1 224 ? 3.87600   10.56700  24.12300 1.000 35.88152 ?  204 GLU A O   1 
ATOM   1497 C CB  . GLU A 1 224 ? 3.70000   10.94000  21.05000 1.000 37.37388 ?  204 GLU A CB  1 
ATOM   1498 C CG  . GLU A 1 224 ? 3.98300   11.90100  19.90500 1.000 36.03959 ?  204 GLU A CG  1 
ATOM   1499 C CD  . GLU A 1 224 ? 4.35400   11.19600  18.62000 1.000 39.02177 ?  204 GLU A CD  1 
ATOM   1500 O OE1 . GLU A 1 224 ? 5.11500   10.21000  18.68400 1.000 46.32406 ?  204 GLU A OE1 1 
ATOM   1501 O OE2 . GLU A 1 224 ? 3.88300   11.62400  17.54500 1.000 45.74254 -1 204 GLU A OE2 1 
ATOM   1502 N N   . VAL A 1 225 ? 1.71700   10.10700  23.67700 1.000 29.60416 ?  205 VAL A N   1 
ATOM   1503 C CA  . VAL A 1 225 ? 1.50100   9.31100   24.87800 1.000 33.66325 ?  205 VAL A CA  1 
ATOM   1504 C C   . VAL A 1 225 ? 1.45600   7.84300   24.47800 1.000 30.54529 ?  205 VAL A C   1 
ATOM   1505 O O   . VAL A 1 225 ? 0.63100   7.44000   23.64900 1.000 28.06081 ?  205 VAL A O   1 
ATOM   1506 C CB  . VAL A 1 225 ? 0.22000   9.73500   25.61000 1.000 33.16672 ?  205 VAL A CB  1 
ATOM   1507 C CG1 . VAL A 1 225 ? 0.01700   8.89500   26.85300 1.000 33.05781 ?  205 VAL A CG1 1 
ATOM   1508 C CG2 . VAL A 1 225 ? 0.29900   11.21300  25.97700 1.000 36.36884 ?  205 VAL A CG2 1 
ATOM   1509 N N   . SER A 1 226 ? 2.35800   7.05300   25.04700 1.000 30.56511 ?  206 SER A N   1 
ATOM   1510 C CA  . SER A 1 226 ? 2.31300   5.61200   24.87800 1.000 33.29164 ?  206 SER A CA  1 
ATOM   1511 C C   . SER A 1 226 ? 1.38100   5.00800   25.91600 1.000 32.59845 ?  206 SER A C   1 
ATOM   1512 O O   . SER A 1 226 ? 1.25600   5.51200   27.03800 1.000 31.16179 ?  206 SER A O   1 
ATOM   1513 C CB  . SER A 1 226 ? 3.70400   5.00200   25.02100 1.000 23.96552 ?  206 SER A CB  1 
ATOM   1514 O OG  . SER A 1 226 ? 3.90100   4.51000   26.33300 1.000 38.77149 ?  206 SER A OG  1 
ATOM   1515 N N   . THR A 1 227 ? 0.72100   3.91500   25.53500 1.000 32.59317 ?  207 THR A N   1 
ATOM   1516 C CA  . THR A 1 227 ? -0.24400  3.30700   26.44500 1.000 30.56784 ?  207 THR A CA  1 
ATOM   1517 C C   . THR A 1 227 ? 0.42700   2.81100   27.72400 1.000 26.91627 ?  207 THR A C   1 
ATOM   1518 O O   . THR A 1 227 ? -0.12000  2.98400   28.81800 1.000 31.09546 ?  207 THR A O   1 
ATOM   1519 C CB  . THR A 1 227 ? -0.99600  2.17600   25.74800 1.000 25.01529 ?  207 THR A CB  1 
ATOM   1520 O OG1 . THR A 1 227 ? -1.52400  2.65300   24.50600 1.000 26.55692 ?  207 THR A OG1 1 
ATOM   1521 C CG2 . THR A 1 227 ? -2.13500  1.68400   26.62400 1.000 25.28909 ?  207 THR A CG2 1 
ATOM   1522 N N   . LEU A 1 228 ? 1.61600   2.21300   27.61600 1.000 25.41132 ?  208 LEU A N   1 
ATOM   1523 C CA  . LEU A 1 228 ? 2.31500   1.76800   28.81900 1.000 29.82349 ?  208 LEU A CA  1 
ATOM   1524 C C   . LEU A 1 228 ? 2.55900   2.93100   29.77400 1.000 28.51177 ?  208 LEU A C   1 
ATOM   1525 O O   . LEU A 1 228 ? 2.28700   2.82000   30.97500 1.000 31.50917 ?  208 LEU A O   1 
ATOM   1526 C CB  . LEU A 1 228 ? 3.63700   1.08200   28.45700 1.000 26.53167 ?  208 LEU A CB  1 
ATOM   1527 C CG  . LEU A 1 228 ? 4.33800   0.33900   29.60900 1.000 33.62325 ?  208 LEU A CG  1 
ATOM   1528 C CD1 . LEU A 1 228 ? 3.38600   -0.61100  30.32400 1.000 26.02317 ?  208 LEU A CD1 1 
ATOM   1529 C CD2 . LEU A 1 228 ? 5.57600   -0.41100  29.12400 1.000 33.04434 ?  208 LEU A CD2 1 
ATOM   1530 N N   . GLU A 1 229 ? 3.04800   4.06100   29.25200 1.000 28.89900 ?  209 GLU A N   1 
ATOM   1531 C CA  . GLU A 1 229 ? 3.23000   5.24600   30.08600 1.000 32.78657 ?  209 GLU A CA  1 
ATOM   1532 C C   . GLU A 1 229 ? 1.92000   5.66400   30.74000 1.000 31.49637 ?  209 GLU A C   1 
ATOM   1533 O O   . GLU A 1 229 ? 1.88100   5.95200   31.94300 1.000 37.17494 ?  209 GLU A O   1 
ATOM   1534 C CB  . GLU A 1 229 ? 3.80200   6.39500   29.25300 1.000 27.75061 ?  209 GLU A CB  1 
ATOM   1535 N N   . GLY A 1 230 ? 0.83300   5.69800   29.96300 1.000 29.27822 ?  210 GLY A N   1 
ATOM   1536 C CA  . GLY A 1 230 ? -0.45900  6.05500   30.52800 1.000 28.45242 ?  210 GLY A CA  1 
ATOM   1537 C C   . GLY A 1 230 ? -0.92400  5.07100   31.58400 1.000 33.22468 ?  210 GLY A C   1 
ATOM   1538 O O   . GLY A 1 230 ? -1.54400  5.45500   32.57800 1.000 36.98578 ?  210 GLY A O   1 
ATOM   1539 N N   . LEU A 1 231 ? -0.63600  3.78600   31.38000 1.000 27.96073 ?  211 LEU A N   1 
ATOM   1540 C CA  . LEU A 1 231 ? -0.96200  2.79400   32.39600 1.000 30.88064 ?  211 LEU A CA  1 
ATOM   1541 C C   . LEU A 1 231 ? -0.13200  3.01500   33.65200 1.000 33.08493 ?  211 LEU A C   1 
ATOM   1542 O O   . LEU A 1 231 ? -0.63400  2.87100   34.77400 1.000 29.52190 ?  211 LEU A O   1 
ATOM   1543 C CB  . LEU A 1 231 ? -0.73800  1.38700   31.84400 1.000 26.71319 ?  211 LEU A CB  1 
ATOM   1544 C CG  . LEU A 1 231 ? -1.67400  0.92300   30.72800 1.000 30.43113 ?  211 LEU A CG  1 
ATOM   1545 C CD1 . LEU A 1 231 ? -1.10000  -0.30400  30.02700 1.000 27.98930 ?  211 LEU A CD1 1 
ATOM   1546 C CD2 . LEU A 1 231 ? -3.07000  0.63000   31.27400 1.000 28.81944 ?  211 LEU A CD2 1 
ATOM   1547 N N   . LYS A 1 232 ? 1.14700   3.36000   33.48000 1.000 30.91613 ?  212 LYS A N   1 
ATOM   1548 C CA  . LYS A 1 232 ? 1.99100   3.67300   34.62700 1.000 35.45966 ?  212 LYS A CA  1 
ATOM   1549 C C   . LYS A 1 232 ? 1.41000   4.82500   35.43900 1.000 35.60293 ?  212 LYS A C   1 
ATOM   1550 O O   . LYS A 1 232 ? 1.39200   4.77300   36.67300 1.000 35.07130 ?  212 LYS A O   1 
ATOM   1551 C CB  . LYS A 1 232 ? 3.41100   4.00300   34.16200 1.000 33.10535 ?  212 LYS A CB  1 
ATOM   1552 C CG  . LYS A 1 232 ? 4.21900   2.78400   33.73700 1.000 33.65122 ?  212 LYS A CG  1 
ATOM   1553 C CD  . LYS A 1 232 ? 5.71300   3.05400   33.78900 1.000 35.05244 ?  212 LYS A CD  1 
ATOM   1554 C CE  . LYS A 1 232 ? 6.39000   2.69100   32.47800 1.000 40.82255 ?  212 LYS A CE  1 
ATOM   1555 N N   . GLU A 1 233 ? 0.91200   5.86500   34.76300 1.000 35.38615 ?  213 GLU A N   1 
ATOM   1556 C CA  . GLU A 1 233 ? 0.33800   7.00100   35.47600 1.000 35.14336 ?  213 GLU A CA  1 
ATOM   1557 C C   . GLU A 1 233 ? -0.86800  6.58200   36.30700 1.000 37.58378 ?  213 GLU A C   1 
ATOM   1558 O O   . GLU A 1 233 ? -1.02200  7.01800   37.45400 1.000 36.39606 ?  213 GLU A O   1 
ATOM   1559 C CB  . GLU A 1 233 ? -0.04500  8.10400   34.48800 1.000 34.41988 ?  213 GLU A CB  1 
ATOM   1560 N N   . ILE A 1 234 ? -1.72600  5.72400   35.75600 1.000 35.52928 ?  214 ILE A N   1 
ATOM   1561 C CA  . ILE A 1 234 ? -2.92100  5.31300   36.48700 1.000 34.84826 ?  214 ILE A CA  1 
ATOM   1562 C C   . ILE A 1 234 ? -2.58200  4.28800   37.56100 1.000 33.98265 ?  214 ILE A C   1 
ATOM   1563 O O   . ILE A 1 234 ? -3.08800  4.36400   38.68600 1.000 37.23280 ?  214 ILE A O   1 
ATOM   1564 C CB  . ILE A 1 234 ? -3.98800  4.77100   35.51700 1.000 38.22667 ?  214 ILE A CB  1 
ATOM   1565 C CG1 . ILE A 1 234 ? -4.53500  5.88700   34.62800 1.000 35.49671 ?  214 ILE A CG1 1 
ATOM   1566 C CG2 . ILE A 1 234 ? -5.13000  4.11800   36.28800 1.000 29.60997 ?  214 ILE A CG2 1 
ATOM   1567 C CD1 . ILE A 1 234 ? -5.20900  5.37000   33.37200 1.000 35.37251 ?  214 ILE A CD1 1 
ATOM   1568 N N   . LEU A 1 235 ? -1.72500  3.32100   37.24500 1.000 34.15602 ?  215 LEU A N   1 
ATOM   1569 C CA  . LEU A 1 235 ? -1.57500  2.15500   38.10800 1.000 35.26077 ?  215 LEU A CA  1 
ATOM   1570 C C   . LEU A 1 235 ? -0.48900  2.30000   39.16700 1.000 36.84655 ?  215 LEU A C   1 
ATOM   1571 O O   . LEU A 1 235 ? -0.55000  1.59900   40.18600 1.000 34.14000 ?  215 LEU A O   1 
ATOM   1572 C CB  . LEU A 1 235 ? -1.30800  0.90400   37.26000 1.000 29.42093 ?  215 LEU A CB  1 
ATOM   1573 C CG  . LEU A 1 235 ? -2.47300  0.47300   36.36500 1.000 32.89485 ?  215 LEU A CG  1 
ATOM   1574 C CD1 . LEU A 1 235 ? -2.07300  -0.66300  35.43200 1.000 24.72354 ?  215 LEU A CD1 1 
ATOM   1575 C CD2 . LEU A 1 235 ? -3.67300  0.06800   37.22000 1.000 30.75464 ?  215 LEU A CD2 1 
ATOM   1576 N N   . GLU A 1 236 ? 0.49200   3.18400   38.97400 1.000 36.81853 ?  216 GLU A N   1 
ATOM   1577 C CA  . GLU A 1 236 ? 1.55500   3.28200   39.97200 1.000 39.13972 ?  216 GLU A CA  1 
ATOM   1578 C C   . GLU A 1 236 ? 1.11400   3.98500   41.25000 1.000 40.28833 ?  216 GLU A C   1 
ATOM   1579 O O   . GLU A 1 236 ? 1.90100   4.06100   42.19900 1.000 42.24260 ?  216 GLU A O   1 
ATOM   1580 C CB  . GLU A 1 236 ? 2.77800   3.97400   39.37100 1.000 36.32593 ?  216 GLU A CB  1 
ATOM   1581 C CG  . GLU A 1 236 ? 3.60300   3.01200   38.52100 1.000 42.14873 ?  216 GLU A CG  1 
ATOM   1582 C CD  . GLU A 1 236 ? 4.72800   3.67800   37.77100 1.000 48.39961 ?  216 GLU A CD  1 
ATOM   1583 O OE1 . GLU A 1 236 ? 4.71700   4.92400   37.65600 1.000 55.01289 ?  216 GLU A OE1 1 
ATOM   1584 O OE2 . GLU A 1 236 ? 5.62300   2.94800   37.28500 1.000 46.23123 -1 216 GLU A OE2 1 
ATOM   1585 N N   . ILE A 1 237 ? -0.12100  4.48300   41.31000 1.000 37.85428 ?  217 ILE A N   1 
ATOM   1586 C CA  . ILE A 1 237 ? -0.65700  4.93200   42.58700 1.000 38.46185 ?  217 ILE A CA  1 
ATOM   1587 C C   . ILE A 1 237 ? -0.86100  3.74700   43.52400 1.000 41.36650 ?  217 ILE A C   1 
ATOM   1588 O O   . ILE A 1 237 ? -0.68500  3.87200   44.74200 1.000 47.33789 ?  217 ILE A O   1 
ATOM   1589 C CB  . ILE A 1 237 ? -1.96400  5.71900   42.37500 1.000 35.72565 ?  217 ILE A CB  1 
ATOM   1590 C CG1 . ILE A 1 237 ? -1.77600  6.78200   41.29600 1.000 46.97181 ?  217 ILE A CG1 1 
ATOM   1591 C CG2 . ILE A 1 237 ? -2.41500  6.36800   43.67500 1.000 48.22688 ?  217 ILE A CG2 1 
ATOM   1592 N N   . HIS A 1 238 ? -1.21800  2.57700   42.98800 1.000 38.29139 ?  218 HIS A N   1 
ATOM   1593 C CA  . HIS A 1 238 ? -1.51400  1.42100   43.82200 1.000 39.06031 ?  218 HIS A CA  1 
ATOM   1594 C C   . HIS A 1 238 ? -0.73900  0.16700   43.44700 1.000 36.69998 ?  218 HIS A C   1 
ATOM   1595 O O   . HIS A 1 238 ? -0.85000  -0.83700  44.15800 1.000 40.13802 ?  218 HIS A O   1 
ATOM   1596 C CB  . HIS A 1 238 ? -3.01900  1.11300   43.78900 1.000 37.53410 ?  218 HIS A CB  1 
ATOM   1597 C CG  . HIS A 1 238 ? -3.86400  2.17900   44.41200 1.000 41.40159 ?  218 HIS A CG  1 
ATOM   1598 N ND1 . HIS A 1 238 ? -3.94500  2.36100   45.77700 1.000 42.19609 ?  218 HIS A ND1 1 
ATOM   1599 C CD2 . HIS A 1 238 ? -4.65200  3.13200   43.85900 1.000 41.06081 ?  218 HIS A CD2 1 
ATOM   1600 C CE1 . HIS A 1 238 ? -4.75600  3.37200   46.03700 1.000 39.43614 ?  218 HIS A CE1 1 
ATOM   1601 N NE2 . HIS A 1 238 ? -5.19700  3.85800   44.89000 1.000 47.26274 ?  218 HIS A NE2 1 
ATOM   1602 N N   . PHE A 1 239 ? 0.04800   0.19400   42.37400 1.000 31.97112 ?  219 PHE A N   1 
ATOM   1603 C CA  . PHE A 1 239 ? 0.78500   -0.97200  41.90600 1.000 34.50262 ?  219 PHE A CA  1 
ATOM   1604 C C   . PHE A 1 239 ? 2.23200   -0.59500  41.62800 1.000 33.71174 ?  219 PHE A C   1 
ATOM   1605 O O   . PHE A 1 239 ? 2.58400   0.58100   41.50400 1.000 38.09802 ?  219 PHE A O   1 
ATOM   1606 C CB  . PHE A 1 239 ? 0.18600   -1.56300  40.62000 1.000 29.73793 ?  219 PHE A CB  1 
ATOM   1607 C CG  . PHE A 1 239 ? -1.23800  -2.02100  40.74700 1.000 36.19435 ?  219 PHE A CG  1 
ATOM   1608 C CD1 . PHE A 1 239 ? -2.28700  -1.13900  40.52900 1.000 31.37390 ?  219 PHE A CD1 1 
ATOM   1609 C CD2 . PHE A 1 239 ? -1.53000  -3.34300  41.04000 1.000 32.87264 ?  219 PHE A CD2 1 
ATOM   1610 C CE1 . PHE A 1 239 ? -3.59800  -1.56300  40.62300 1.000 32.22627 ?  219 PHE A CE1 1 
ATOM   1611 C CE2 . PHE A 1 239 ? -2.84000  -3.77000  41.14200 1.000 32.37271 ?  219 PHE A CE2 1 
ATOM   1612 C CZ  . PHE A 1 239 ? -3.87400  -2.88000  40.93300 1.000 34.72217 ?  219 PHE A CZ  1 
ATOM   1613 N N   . GLU A 1 240 ? 3.06900   -1.62000  41.50400 1.000 34.44618 ?  220 GLU A N   1 
ATOM   1614 C CA  . GLU A 1 240 ? 4.41800   -1.48300  40.97400 1.000 36.40499 ?  220 GLU A CA  1 
ATOM   1615 C C   . GLU A 1 240 ? 4.51900   -2.32400  39.71100 1.000 30.93519 ?  220 GLU A C   1 
ATOM   1616 O O   . GLU A 1 240 ? 4.03400   -3.45800  39.68200 1.000 38.17426 ?  220 GLU A O   1 
ATOM   1617 C CB  . GLU A 1 240 ? 5.47000   -1.92700  41.99500 1.000 29.24569 ?  220 GLU A CB  1 
ATOM   1618 N N   . LEU A 1 241 ? 5.12600   -1.76800  38.66800 1.000 34.88282 ?  221 LEU A N   1 
ATOM   1619 C CA  . LEU A 1 241 ? 5.31300   -2.50600  37.42500 1.000 31.93135 ?  221 LEU A CA  1 
ATOM   1620 C C   . LEU A 1 241 ? 6.47200   -3.47800  37.59700 1.000 34.25624 ?  221 LEU A C   1 
ATOM   1621 O O   . LEU A 1 241 ? 7.61800   -3.05800  37.79400 1.000 35.88260 ?  221 LEU A O   1 
ATOM   1622 C CB  . LEU A 1 241 ? 5.56700   -1.54600  36.26400 1.000 30.52379 ?  221 LEU A CB  1 
ATOM   1623 C CG  . LEU A 1 241 ? 5.79000   -2.21500  34.90500 1.000 36.91858 ?  221 LEU A CG  1 
ATOM   1624 C CD1 . LEU A 1 241 ? 4.60600   -3.09100  34.53600 1.000 30.90006 ?  221 LEU A CD1 1 
ATOM   1625 C CD2 . LEU A 1 241 ? 6.04800   -1.17600  33.82200 1.000 31.67608 ?  221 LEU A CD2 1 
ATOM   1626 N N   . VAL A 1 242 ? 6.17900   -4.77600  37.52400 1.000 31.93624 ?  222 VAL A N   1 
ATOM   1627 C CA  . VAL A 1 242 ? 7.17600   -5.80100  37.81400 1.000 31.88855 ?  222 VAL A CA  1 
ATOM   1628 C C   . VAL A 1 242 ? 7.85500   -6.29300  36.53900 1.000 34.89598 ?  222 VAL A C   1 
ATOM   1629 O O   . VAL A 1 242 ? 9.05100   -6.60000  36.54900 1.000 38.53493 ?  222 VAL A O   1 
ATOM   1630 C CB  . VAL A 1 242 ? 6.54800   -6.97600  38.58800 1.000 35.71034 ?  222 VAL A CB  1 
ATOM   1631 N N   . ALA A 1 243 ? 7.11500   -6.37700  35.43300 1.000 33.94494 ?  223 ALA A N   1 
ATOM   1632 C CA  . ALA A 1 243 ? 7.68600   -6.94400  34.21600 1.000 30.10026 ?  223 ALA A CA  1 
ATOM   1633 C C   . ALA A 1 243 ? 6.82700   -6.57700  33.01600 1.000 34.60119 ?  223 ALA A C   1 
ATOM   1634 O O   . ALA A 1 243 ? 5.64500   -6.24500  33.15000 1.000 32.47173 ?  223 ALA A O   1 
ATOM   1635 C CB  . ALA A 1 243 ? 7.81900   -8.47000  34.31400 1.000 29.52796 ?  223 ALA A CB  1 
ATOM   1636 N N   . THR A 1 244 ? 7.44700   -6.64500  31.83500 1.000 29.23481 ?  224 THR A N   1 
ATOM   1637 C CA  . THR A 1 244 ? 6.73500   -6.55400  30.56800 1.000 35.61885 ?  224 THR A CA  1 
ATOM   1638 C C   . THR A 1 244 ? 7.29700   -7.60900  29.62900 1.000 36.05808 ?  224 THR A C   1 
ATOM   1639 O O   . THR A 1 244 ? 8.47400   -7.96800  29.71600 1.000 34.71140 ?  224 THR A O   1 
ATOM   1640 C CB  . THR A 1 244 ? 6.86400   -5.17900  29.88800 1.000 34.39720 ?  224 THR A CB  1 
ATOM   1641 O OG1 . THR A 1 244 ? 8.23100   -4.75900  29.90000 1.000 34.00061 ?  224 THR A OG1 1 
ATOM   1642 C CG2 . THR A 1 244 ? 6.03000   -4.13900  30.61300 1.000 32.11515 ?  224 THR A CG2 1 
ATOM   1643 N N   . GLU A 1 245 ? 6.44900   -8.10800  28.73200 1.000 29.97030 ?  225 GLU A N   1 
ATOM   1644 C CA  . GLU A 1 245 ? 6.93400   -8.94400  27.64500 1.000 36.30671 ?  225 GLU A CA  1 
ATOM   1645 C C   . GLU A 1 245 ? 5.91800   -8.92800  26.51900 1.000 38.91109 ?  225 GLU A C   1 
ATOM   1646 O O   . GLU A 1 245 ? 4.71900   -8.72800  26.74000 1.000 33.33887 ?  225 GLU A O   1 
ATOM   1647 C CB  . GLU A 1 245 ? 7.21900   -10.38000 28.09500 1.000 35.74086 ?  225 GLU A CB  1 
ATOM   1648 C CG  . GLU A 1 245 ? 6.07000   -11.07900 28.77300 1.000 41.32571 ?  225 GLU A CG  1 
ATOM   1649 C CD  . GLU A 1 245 ? 6.46200   -12.44900 29.29700 1.000 41.80853 ?  225 GLU A CD  1 
ATOM   1650 O OE1 . GLU A 1 245 ? 6.98300   -13.26400 28.50800 1.000 47.50233 ?  225 GLU A OE1 1 
ATOM   1651 O OE2 . GLU A 1 245 ? 6.23800   -12.71300 30.49800 1.000 50.59170 -1 225 GLU A OE2 1 
ATOM   1652 N N   . ASP A 1 246 ? 6.42000   -9.12200  25.30800 1.000 37.82293 ?  226 ASP A N   1 
ATOM   1653 C CA  . ASP A 1 246 ? 5.57500   -9.17000  24.12900 1.000 35.72938 ?  226 ASP A CA  1 
ATOM   1654 C C   . ASP A 1 246 ? 5.17200   -10.61800 23.87700 1.000 36.74304 ?  226 ASP A C   1 
ATOM   1655 O O   . ASP A 1 246 ? 6.01700   -11.51800 23.91500 1.000 37.23000 ?  226 ASP A O   1 
ATOM   1656 C CB  . ASP A 1 246 ? 6.31000   -8.57100  22.93200 1.000 30.30099 ?  226 ASP A CB  1 
ATOM   1657 C CG  . ASP A 1 246 ? 6.22700   -7.04500  22.90300 1.000 40.36084 ?  226 ASP A CG  1 
ATOM   1658 O OD1 . ASP A 1 246 ? 5.37900   -6.48200  23.62900 1.000 36.51927 ?  226 ASP A OD1 1 
ATOM   1659 O OD2 . ASP A 1 246 ? 7.01000   -6.40600  22.16700 1.000 47.02748 -1 226 ASP A OD2 1 
ATOM   1660 N N   . ILE A 1 247 ? 3.87700   -10.84500 23.68000 1.000 32.53096 ?  227 ILE A N   1 
ATOM   1661 C CA  . ILE A 1 247 ? 3.33000   -12.16900 23.41500 1.000 31.99006 ?  227 ILE A CA  1 
ATOM   1662 C C   . ILE A 1 247 ? 2.55600   -12.10500 22.10800 1.000 31.38231 ?  227 ILE A C   1 
ATOM   1663 O O   . ILE A 1 247 ? 1.55300   -11.39100 22.01800 1.000 29.50270 ?  227 ILE A O   1 
ATOM   1664 C CB  . ILE A 1 247 ? 2.42300   -12.67800 24.55100 1.000 31.49208 ?  227 ILE A CB  1 
ATOM   1665 C CG1 . ILE A 1 247 ? 3.12900   -12.58700 25.90500 1.000 28.54307 ?  227 ILE A CG1 1 
ATOM   1666 C CG2 . ILE A 1 247 ? 1.97400   -14.10100 24.27000 1.000 24.36963 ?  227 ILE A CG2 1 
ATOM   1667 C CD1 . ILE A 1 247 ? 2.18600   -12.76000 27.07700 1.000 27.83650 ?  227 ILE A CD1 1 
ATOM   1668 N N   . PRO A 1 248 ? 2.97100   -12.82200 21.06900 1.000 32.03291 ?  228 PRO A N   1 
ATOM   1669 C CA  . PRO A 1 248 ? 2.23200   -12.79800 19.80700 1.000 31.12434 ?  228 PRO A CA  1 
ATOM   1670 C C   . PRO A 1 248 ? 0.99600   -13.68000 19.87800 1.000 32.19953 ?  228 PRO A C   1 
ATOM   1671 O O   . PRO A 1 248 ? 0.92600   -14.63500 20.65600 1.000 25.37302 ?  228 PRO A O   1 
ATOM   1672 C CB  . PRO A 1 248 ? 3.24400   -13.36500 18.80700 1.000 32.12614 ?  228 PRO A CB  1 
ATOM   1673 C CG  . PRO A 1 248 ? 4.01600   -14.34700 19.63200 1.000 32.60236 ?  228 PRO A CG  1 
ATOM   1674 C CD  . PRO A 1 248 ? 4.14700   -13.70900 21.00000 1.000 35.58630 ?  228 PRO A CD  1 
ATOM   1675 N N   . PHE A 1 249 ? 0.01200   -13.35100 19.04400 1.000 23.32923 ?  229 PHE A N   1 
ATOM   1676 C CA  . PHE A 1 249 ? -1.14300  -14.22400 18.89300 1.000 29.37294 ?  229 PHE A CA  1 
ATOM   1677 C C   . PHE A 1 249 ? -1.65600  -14.13900 17.46500 1.000 28.73697 ?  229 PHE A C   1 
ATOM   1678 O O   . PHE A 1 249 ? -1.47000  -13.13400 16.77300 1.000 31.29608 ?  229 PHE A O   1 
ATOM   1679 C CB  . PHE A 1 249 ? -2.25700  -13.91000 19.91500 1.000 29.84158 ?  229 PHE A CB  1 
ATOM   1680 C CG  . PHE A 1 249 ? -2.94200  -12.57400 19.73300 1.000 31.66211 ?  229 PHE A CG  1 
ATOM   1681 C CD1 . PHE A 1 249 ? -3.99000  -12.41900 18.83600 1.000 37.25322 ?  229 PHE A CD1 1 
ATOM   1682 C CD2 . PHE A 1 249 ? -2.57600  -11.48700 20.51200 1.000 38.03591 ?  229 PHE A CD2 1 
ATOM   1683 C CE1 . PHE A 1 249 ? -4.63300  -11.19100 18.69400 1.000 36.27524 ?  229 PHE A CE1 1 
ATOM   1684 C CE2 . PHE A 1 249 ? -3.21300  -10.26000 20.37600 1.000 34.18984 ?  229 PHE A CE2 1 
ATOM   1685 C CZ  . PHE A 1 249 ? -4.24100  -10.11400 19.46900 1.000 36.38655 ?  229 PHE A CZ  1 
ATOM   1686 N N   . VAL A 1 250 ? -2.28000  -15.22500 17.02500 1.000 29.06585 ?  230 VAL A N   1 
ATOM   1687 C CA  . VAL A 1 250 ? -2.83500  -15.34400 15.68500 1.000 31.60222 ?  230 VAL A CA  1 
ATOM   1688 C C   . VAL A 1 250 ? -4.28600  -15.77900 15.81600 1.000 31.93995 ?  230 VAL A C   1 
ATOM   1689 O O   . VAL A 1 250 ? -4.58900  -16.72700 16.54800 1.000 31.28736 ?  230 VAL A O   1 
ATOM   1690 C CB  . VAL A 1 250 ? -2.04400  -16.35200 14.82800 1.000 35.25661 ?  230 VAL A CB  1 
ATOM   1691 C CG1 . VAL A 1 250 ? -2.72900  -16.56500 13.48500 1.000 29.28414 ?  230 VAL A CG1 1 
ATOM   1692 C CG2 . VAL A 1 250 ? -0.61000  -15.87600 14.63500 1.000 29.58692 ?  230 VAL A CG2 1 
ATOM   1693 N N   . ILE A 1 251 ? -5.18300  -15.08500 15.12400 1.000 34.08027 ?  231 ILE A N   1 
ATOM   1694 C CA  . ILE A 1 251 ? -6.59000  -15.45800 15.07700 1.000 33.57444 ?  231 ILE A CA  1 
ATOM   1695 C C   . ILE A 1 251 ? -6.96900  -15.66800 13.61800 1.000 35.35110 ?  231 ILE A C   1 
ATOM   1696 O O   . ILE A 1 251 ? -6.65400  -14.83200 12.76200 1.000 29.98885 ?  231 ILE A O   1 
ATOM   1697 C CB  . ILE A 1 251 ? -7.49300  -14.40600 15.75100 1.000 37.64478 ?  231 ILE A CB  1 
ATOM   1698 C CG1 . ILE A 1 251 ? -8.54600  -13.88000 14.77000 1.000 43.55792 ?  231 ILE A CG1 1 
ATOM   1699 C CG2 . ILE A 1 251 ? -6.66900  -13.26000 16.31400 1.000 42.24701 ?  231 ILE A CG2 1 
ATOM   1700 N N   . ARG A 1 252 ? -7.61500  -16.79600 13.33500 1.000 30.37212 ?  232 ARG A N   1 
ATOM   1701 C CA  . ARG A 1 252 ? -8.00700  -17.11600 11.97200 1.000 30.66830 ?  232 ARG A CA  1 
ATOM   1702 C C   . ARG A 1 252 ? -9.23000  -16.30100 11.57700 1.000 35.08911 ?  232 ARG A C   1 
ATOM   1703 O O   . ARG A 1 252 ? -10.19900 -16.21200 12.33500 1.000 36.45981 ?  232 ARG A O   1 
ATOM   1704 C CB  . ARG A 1 252 ? -8.29900  -18.61000 11.83100 1.000 36.50092 ?  232 ARG A CB  1 
ATOM   1705 C CG  . ARG A 1 252 ? -8.93500  -18.96900 10.50000 1.000 39.04135 ?  232 ARG A CG  1 
ATOM   1706 C CD  . ARG A 1 252 ? -9.54700  -20.36000 10.48200 1.000 36.70070 ?  232 ARG A CD  1 
ATOM   1707 N NE  . ARG A 1 252 ? -8.65700  -21.36100 11.05400 1.000 43.76233 ?  232 ARG A NE  1 
ATOM   1708 C CZ  . ARG A 1 252 ? -7.58900  -21.85900 10.44300 1.000 52.51608 ?  232 ARG A CZ  1 
ATOM   1709 N NH1 . ARG A 1 252 ? -7.25500  -21.48400 9.21800  1.000 52.18397 ?  232 ARG A NH1 1 
ATOM   1710 N NH2 . ARG A 1 252 ? -6.83500  -22.75200 11.08000 1.000 52.11040 ?  232 ARG A NH2 1 
ATOM   1711 N N   . GLU A 1 253 ? -9.17300  -15.68600 10.39700 1.000 32.62515 ?  233 GLU A N   1 
ATOM   1712 C CA  . GLU A 1 253 ? -10.34000 -15.04400 9.80800  1.000 35.63705 ?  233 GLU A CA  1 
ATOM   1713 C C   . GLU A 1 253 ? -10.92300 -15.84000 8.64800  1.000 38.00268 ?  233 GLU A C   1 
ATOM   1714 O O   . GLU A 1 253 ? -12.14200 -16.00200 8.56300  1.000 42.83453 ?  233 GLU A O   1 
ATOM   1715 C CB  . GLU A 1 253 ? -9.99200  -13.62600 9.35000  1.000 42.64801 ?  233 GLU A CB  1 
ATOM   1716 C CG  . GLU A 1 253 ? -8.94000  -12.94800 10.21700 1.000 49.45798 ?  233 GLU A CG  1 
ATOM   1717 C CD  . GLU A 1 253 ? -9.23500  -11.47900 10.44800 1.000 53.16178 ?  233 GLU A CD  1 
ATOM   1718 O OE2 . GLU A 1 253 ? -9.34600  -10.72500 9.45700  1.000 64.08761 -1 233 GLU A OE2 1 
ATOM   1719 N N   . THR A 1 254 ? -10.08000 -16.33400 7.74900  1.000 38.81623 ?  234 THR A N   1 
ATOM   1720 C CA  . THR A 1 254 ? -10.43500 -17.35000 6.77000  1.000 31.66885 ?  234 THR A CA  1 
ATOM   1721 C C   . THR A 1 254 ? -9.35200  -18.41700 6.79300  1.000 35.84405 ?  234 THR A C   1 
ATOM   1722 O O   . THR A 1 254 ? -8.39800  -18.34300 7.56800  1.000 37.57718 ?  234 THR A O   1 
ATOM   1723 C CB  . THR A 1 254 ? -10.57700 -16.77600 5.35200  1.000 33.47507 ?  234 THR A CB  1 
ATOM   1724 O OG1 . THR A 1 254 ? -9.28000  -16.66100 4.75000  1.000 35.26563 ?  234 THR A OG1 1 
ATOM   1725 C CG2 . THR A 1 254 ? -11.24800 -15.40800 5.36700  1.000 34.23687 ?  234 THR A CG2 1 
ATOM   1726 N N   . SER A 1 255 ? -9.49100  -19.41100 5.91700  1.000 39.38319 ?  235 SER A N   1 
ATOM   1727 C CA  . SER A 1 255 ? -8.46100  -20.43400 5.79400  1.000 40.05843 ?  235 SER A CA  1 
ATOM   1728 C C   . SER A 1 255 ? -7.11800  -19.85700 5.36600  1.000 33.65768 ?  235 SER A C   1 
ATOM   1729 O O   . SER A 1 255 ? -6.08100  -20.47200 5.63000  1.000 34.68331 ?  235 SER A O   1 
ATOM   1730 C CB  . SER A 1 255 ? -8.90500  -21.50500 4.79600  1.000 32.07363 ?  235 SER A CB  1 
ATOM   1731 O OG  . SER A 1 255 ? -9.14100  -20.92600 3.52000  1.000 48.48601 ?  235 SER A OG  1 
ATOM   1732 N N   . ARG A 1 256 ? -7.11700  -18.68600 4.73800  1.000 29.94202 ?  236 ARG A N   1 
ATOM   1733 C CA  . ARG A 1 256 ? -5.85200  -18.10500 4.21300  1.000 34.83763 ?  236 ARG A CA  1 
ATOM   1734 C C   . ARG A 1 256 ? -5.54000  -16.75800 4.87400  1.000 31.98950 ?  236 ARG A C   1 
ATOM   1735 O O   . ARG A 1 256 ? -4.38900  -16.32700 4.80700  1.000 34.13171 ?  236 ARG A O   1 
ATOM   1736 C CB  . ARG A 1 256 ? -5.93600  -17.99000 2.69000  1.000 29.06388 ?  236 ARG A CB  1 
ATOM   1737 C CG  . ARG A 1 256 ? -6.07800  -19.32400 1.97600  1.000 29.30910 ?  236 ARG A CG  1 
ATOM   1738 C CD  . ARG A 1 256 ? -5.99300  -19.17400 0.47300  1.000 28.11570 ?  236 ARG A CD  1 
ATOM   1739 N NE  . ARG A 1 256 ? -5.74000  -20.44900 -0.17200 1.000 29.72830 ?  236 ARG A NE  1 
ATOM   1740 C CZ  . ARG A 1 256 ? -4.53500  -20.95900 -0.37600 1.000 34.28627 ?  236 ARG A CZ  1 
ATOM   1741 N NH1 . ARG A 1 256 ? -3.45900  -20.28000 -0.02400 1.000 32.83791 ?  236 ARG A NH1 1 
ATOM   1742 N NH2 . ARG A 1 256 ? -4.40800  -22.14500 -0.94200 1.000 33.31326 ?  236 ARG A NH2 1 
ATOM   1743 N N   . LYS A 1 257 ? -6.53500  -16.12700 5.48200  1.000 31.08494 ?  237 LYS A N   1 
ATOM   1744 C CA  . LYS A 1 257 ? -6.31700  -14.78400 6.06600  1.000 29.27580 ?  237 LYS A CA  1 
ATOM   1745 C C   . LYS A 1 257 ? -6.34200  -14.87300 7.58700  1.000 31.02210 ?  237 LYS A C   1 
ATOM   1746 O O   . LYS A 1 257 ? -7.28400  -15.43400 8.13500  1.000 32.81767 ?  237 LYS A O   1 
ATOM   1747 C CB  . LYS A 1 257 ? -7.33900  -13.76800 5.55900  1.000 38.51555 ?  237 LYS A CB  1 
ATOM   1748 C CG  . LYS A 1 257 ? -7.13500  -12.33700 6.03300  1.000 37.62532 ?  237 LYS A CG  1 
ATOM   1749 C CD  . LYS A 1 257 ? -8.37400  -11.48300 5.88800  1.000 43.31330 ?  237 LYS A CD  1 
ATOM   1750 N N   . PHE A 1 258 ? -5.31600  -14.32500 8.20900  1.000 29.97383 ?  238 PHE A N   1 
ATOM   1751 C CA  . PHE A 1 258 ? -5.21300  -14.37400 9.68000  1.000 30.13533 ?  238 PHE A CA  1 
ATOM   1752 C C   . PHE A 1 258 ? -4.77400  -13.02500 10.24300 1.000 32.89492 ?  238 PHE A C   1 
ATOM   1753 O O   . PHE A 1 258 ? -4.17300  -12.22600 9.52400  1.000 29.22870 ?  238 PHE A O   1 
ATOM   1754 C CB  . PHE A 1 258 ? -4.18600  -15.41700 10.12300 1.000 27.64242 ?  238 PHE A CB  1 
ATOM   1755 C CG  . PHE A 1 258 ? -4.38800  -16.82600 9.63200  1.000 34.99314 ?  238 PHE A CG  1 
ATOM   1756 C CD1 . PHE A 1 258 ? -4.05200  -17.18800 8.33900  1.000 32.86130 ?  238 PHE A CD1 1 
ATOM   1757 C CD2 . PHE A 1 258 ? -4.87100  -17.80300 10.48200 1.000 32.87171 ?  238 PHE A CD2 1 
ATOM   1758 C CE1 . PHE A 1 258 ? -4.22800  -18.48700 7.89700  1.000 35.02928 ?  238 PHE A CE1 1 
ATOM   1759 C CE2 . PHE A 1 258 ? -5.04000  -19.10300 10.04100 1.000 43.29537 ?  238 PHE A CE2 1 
ATOM   1760 C CZ  . PHE A 1 258 ? -4.71800  -19.44300 8.75000  1.000 37.84774 ?  238 PHE A CZ  1 
ATOM   1761 N N   . GLN A 1 259 ? -5.11200  -12.77900 11.50200 1.000 32.26627 ?  239 GLN A N   1 
ATOM   1762 C CA  . GLN A 1 259 ? -4.59200  -11.58100 12.18500 1.000 31.46844 ?  239 GLN A CA  1 
ATOM   1763 C C   . GLN A 1 259 ? -3.39500  -12.04700 13.00700 1.000 25.21000 ?  239 GLN A C   1 
ATOM   1764 O O   . GLN A 1 259 ? -3.55200  -12.99200 13.76600 1.000 33.55372 ?  239 GLN A O   1 
ATOM   1765 C CB  . GLN A 1 259 ? -5.64900  -10.93000 13.07000 1.000 31.65060 ?  239 GLN A CB  1 
ATOM   1766 C CG  . GLN A 1 259 ? -5.16100  -9.66200  13.75400 1.000 37.02080 ?  239 GLN A CG  1 
ATOM   1767 C CD  . GLN A 1 259 ? -6.00400  -9.24900  14.93500 1.000 42.99908 ?  239 GLN A CD  1 
ATOM   1768 O OE1 . GLN A 1 259 ? -5.50300  -8.73300  15.93000 1.000 36.93263 ?  239 GLN A OE1 1 
ATOM   1769 N NE2 . GLN A 1 259 ? -7.30400  -9.46100  14.82600 1.000 37.00495 ?  239 GLN A NE2 1 
ATOM   1770 N N   . HIS A 1 260 ? -2.24000  -11.43900 12.79000 1.000 29.27951 ?  240 HIS A N   1 
ATOM   1771 C CA  . HIS A 1 260 ? -1.02700  -11.76100 13.58100 1.000 31.63417 ?  240 HIS A CA  1 
ATOM   1772 C C   . HIS A 1 260 ? -0.69700  -10.49800 14.37600 1.000 30.50418 ?  240 HIS A C   1 
ATOM   1773 O O   . HIS A 1 260 ? -0.35000  -9.47900  13.77800 1.000 30.98840 ?  240 HIS A O   1 
ATOM   1774 C CB  . HIS A 1 260 ? 0.06900   -12.32900 12.67300 1.000 29.43086 ?  240 HIS A CB  1 
ATOM   1775 C CG  . HIS A 1 260 ? 1.25500   -12.84900 13.39400 1.000 28.86228 ?  240 HIS A CG  1 
ATOM   1776 N ND1 . HIS A 1 260 ? 2.23800   -13.56900 12.75600 1.000 29.38063 ?  240 HIS A ND1 1 
ATOM   1777 C CD2 . HIS A 1 260 ? 1.62000   -12.76500 14.66900 1.000 30.41137 ?  240 HIS A CD2 1 
ATOM   1778 C CE1 . HIS A 1 260 ? 3.16400   -13.90100 13.63500 1.000 32.20378 ?  240 HIS A CE1 1 
ATOM   1779 N NE2 . HIS A 1 260 ? 2.80500   -13.42200 14.80000 1.000 35.80980 ?  240 HIS A NE2 1 
ATOM   1780 N N   . THR A 1 261 ? -0.82200  -10.58400 15.69400 1.000 31.81981 ?  241 THR A N   1 
ATOM   1781 C CA  . THR A 1 261 ? -0.66400  -9.38300  16.54100 1.000 28.32527 ?  241 THR A CA  1 
ATOM   1782 C C   . THR A 1 261 ? 0.26400   -9.66800  17.72300 1.000 32.36532 ?  241 THR A C   1 
ATOM   1783 O O   . THR A 1 261 ? 0.24500   -10.78300 18.23400 1.000 27.24529 ?  241 THR A O   1 
ATOM   1784 C CB  . THR A 1 261 ? -2.04700  -8.86500  16.96400 1.000 33.22964 ?  241 THR A CB  1 
ATOM   1785 O OG1 . THR A 1 261 ? -2.77900  -8.53400  15.78500 1.000 34.60714 ?  241 THR A OG1 1 
ATOM   1786 C CG2 . THR A 1 261 ? -1.98100  -7.66700  17.87900 1.000 28.08521 ?  241 THR A CG2 1 
ATOM   1787 N N   . ILE A 1 262 ? 1.05200   -8.66700  18.10700 1.000 28.69561 ?  242 ILE A N   1 
ATOM   1788 C CA  . ILE A 1 262 ? 1.97900   -8.79700  19.25800 1.000 27.36626 ?  242 ILE A CA  1 
ATOM   1789 C C   . ILE A 1 262 ? 1.40500   -7.97500  20.41200 1.000 29.29040 ?  242 ILE A C   1 
ATOM   1790 O O   . ILE A 1 262 ? 1.46100   -6.74900  20.35200 1.000 27.53512 ?  242 ILE A O   1 
ATOM   1791 C CB  . ILE A 1 262 ? 3.40300   -8.36000  18.87700 1.000 27.66392 ?  242 ILE A CB  1 
ATOM   1792 C CG1 . ILE A 1 262 ? 3.89300   -9.05600  17.60800 1.000 35.17636 ?  242 ILE A CG1 1 
ATOM   1793 C CG2 . ILE A 1 262 ? 4.35100   -8.58600  20.03900 1.000 33.28503 ?  242 ILE A CG2 1 
ATOM   1794 C CD1 . ILE A 1 262 ? 4.66300   -8.15100  16.68300 1.000 35.77327 ?  242 ILE A CD1 1 
ATOM   1795 N N   . SER A 1 263 ? 0.84500   -8.65800  21.39900 1.000 27.83823 ?  243 SER A N   1 
ATOM   1796 C CA  . SER A 1 263 ? 0.27400   -7.97100  22.57600 1.000 31.27541 ?  243 SER A CA  1 
ATOM   1797 C C   . SER A 1 263 ? 1.36900   -7.77200  23.62100 1.000 27.27019 ?  243 SER A C   1 
ATOM   1798 O O   . SER A 1 263 ? 2.28700   -8.58700  23.68800 1.000 33.67596 ?  243 SER A O   1 
ATOM   1799 C CB  . SER A 1 263 ? -0.91900  -8.71400  23.12900 1.000 33.09318 ?  243 SER A CB  1 
ATOM   1800 O OG  . SER A 1 263 ? -1.04200  -8.51400  24.52300 1.000 46.73826 ?  243 SER A OG  1 
ATOM   1801 N N   . GLN A 1 264 ? 1.27100   -6.69000  24.37200 1.000 30.25581 ?  244 GLN A N   1 
ATOM   1802 C CA  . GLN A 1 264 ? 2.23700   -6.44400  25.43500 1.000 31.79542 ?  244 GLN A CA  1 
ATOM   1803 C C   . GLN A 1 264 ? 1.61900   -6.83900  26.76700 1.000 30.21092 ?  244 GLN A C   1 
ATOM   1804 O O   . GLN A 1 264 ? 0.59600   -6.27400  27.17600 1.000 31.78379 ?  244 GLN A O   1 
ATOM   1805 C CB  . GLN A 1 264 ? 2.68400   -4.98400  25.47400 1.000 31.21030 ?  244 GLN A CB  1 
ATOM   1806 C CG  . GLN A 1 264 ? 3.54700   -4.67600  26.68600 1.000 29.01080 ?  244 GLN A CG  1 
ATOM   1807 C CD  . GLN A 1 264 ? 4.29000   -3.37000  26.55000 1.000 32.31632 ?  244 GLN A CD  1 
ATOM   1808 O OE1 . GLN A 1 264 ? 3.68400   -2.30000  26.51700 1.000 28.38927 ?  244 GLN A OE1 1 
ATOM   1809 N NE2 . GLN A 1 264 ? 5.61500   -3.44700  26.47800 1.000 30.91446 ?  244 GLN A NE2 1 
ATOM   1810 N N   . MET A 1 265 ? 2.23200   -7.81100  27.43200 1.000 26.97502 ?  245 MET A N   1 
ATOM   1811 C CA  . MET A 1 265 ? 1.83000   -8.16100  28.78200 1.000 31.20006 ?  245 MET A CA  1 
ATOM   1812 C C   . MET A 1 265 ? 2.52300   -7.22200  29.75600 1.000 31.27656 ?  245 MET A C   1 
ATOM   1813 O O   . MET A 1 265 ? 3.71300   -6.93200  29.61300 1.000 32.17749 ?  245 MET A O   1 
ATOM   1814 C CB  . MET A 1 265 ? 2.18800   -9.61400  29.10400 1.000 32.36947 ?  245 MET A CB  1 
ATOM   1815 C CG  . MET A 1 265 ? 1.95900   -9.99400  30.56800 1.000 30.50337 ?  245 MET A CG  1 
ATOM   1816 S SD  . MET A 1 265 ? 2.18200   -11.75400 30.91900 1.000 36.00441 ?  245 MET A SD  1 
ATOM   1817 C CE  . MET A 1 265 ? 0.60600   -12.44200 30.39300 1.000 31.85519 ?  245 MET A CE  1 
ATOM   1818 N N   . SER A 1 266 ? 1.76700   -6.71900  30.72600 1.000 24.55730 ?  246 SER A N   1 
ATOM   1819 C CA  . SER A 1 266 ? 2.32400   -5.91300  31.80200 1.000 26.08387 ?  246 SER A CA  1 
ATOM   1820 C C   . SER A 1 266 ? 1.86500   -6.50300  33.12500 1.000 30.60894 ?  246 SER A C   1 
ATOM   1821 O O   . SER A 1 266 ? 0.68600   -6.83900  33.28200 1.000 28.76655 ?  246 SER A O   1 
ATOM   1822 C CB  . SER A 1 266 ? 1.91200   -4.43700  31.68500 1.000 29.50221 ?  246 SER A CB  1 
ATOM   1823 O OG  . SER A 1 266 ? 0.53900   -4.29700  31.36800 1.000 28.77348 ?  246 SER A OG  1 
ATOM   1824 N N   . VAL A 1 267 ? 2.79800   -6.63200  34.06400 1.000 30.61482 ?  247 VAL A N   1 
ATOM   1825 C CA  . VAL A 1 267 ? 2.56900   -7.30100  35.33900 1.000 28.42109 ?  247 VAL A CA  1 
ATOM   1826 C C   . VAL A 1 267 ? 2.70500   -6.26600  36.44700 1.000 35.36447 ?  247 VAL A C   1 
ATOM   1827 O O   . VAL A 1 267 ? 3.74000   -5.59900  36.56300 1.000 32.19624 ?  247 VAL A O   1 
ATOM   1828 C CB  . VAL A 1 267 ? 3.55000   -8.46500  35.54400 1.000 28.24612 ?  247 VAL A CB  1 
ATOM   1829 C CG1 . VAL A 1 267 ? 3.26600   -9.18200  36.85000 1.000 25.62367 ?  247 VAL A CG1 1 
ATOM   1830 C CG2 . VAL A 1 267 ? 3.46900   -9.42900  34.36800 1.000 28.26895 ?  247 VAL A CG2 1 
ATOM   1831 N N   . TRP A 1 268 ? 1.66700   -6.14600  37.26900 1.000 30.73083 ?  248 TRP A N   1 
ATOM   1832 C CA  . TRP A 1 268 ? 1.58200   -5.11200  38.28800 1.000 30.27818 ?  248 TRP A CA  1 
ATOM   1833 C C   . TRP A 1 268 ? 1.30700   -5.75800  39.63900 1.000 31.91419 ?  248 TRP A C   1 
ATOM   1834 O O   . TRP A 1 268 ? 0.34800   -6.52400  39.77800 1.000 32.29239 ?  248 TRP A O   1 
ATOM   1835 C CB  . TRP A 1 268 ? 0.48200   -4.10000  37.94300 1.000 26.87051 ?  248 TRP A CB  1 
ATOM   1836 C CG  . TRP A 1 268 ? 0.49700   -3.65000  36.50900 1.000 28.00454 ?  248 TRP A CG  1 
ATOM   1837 C CD1 . TRP A 1 268 ? -0.04300  -4.29900  35.43600 1.000 25.76537 ?  248 TRP A CD1 1 
ATOM   1838 C CD2 . TRP A 1 268 ? 1.07600   -2.44300  35.99700 1.000 30.96908 ?  248 TRP A CD2 1 
ATOM   1839 N NE1 . TRP A 1 268 ? 0.16200   -3.56800  34.28600 1.000 27.26955 ?  248 TRP A NE1 1 
ATOM   1840 C CE2 . TRP A 1 268 ? 0.85400   -2.42900  34.60300 1.000 27.76290 ?  248 TRP A CE2 1 
ATOM   1841 C CE3 . TRP A 1 268 ? 1.76400   -1.37300  36.58100 1.000 34.72380 ?  248 TRP A CE3 1 
ATOM   1842 C CZ2 . TRP A 1 268 ? 1.29400   -1.38800  33.78600 1.000 31.51040 ?  248 TRP A CZ2 1 
ATOM   1843 C CZ3 . TRP A 1 268 ? 2.20400   -0.33800  35.76600 1.000 32.53799 ?  248 TRP A CZ3 1 
ATOM   1844 C CH2 . TRP A 1 268 ? 1.96500   -0.35500  34.38300 1.000 28.43268 ?  248 TRP A CH2 1 
ATOM   1845 N N   . LYS A 1 269 ? 2.15000   -5.45500  40.62500 1.000 30.94427 ?  249 LYS A N   1 
ATOM   1846 C CA  . LYS A 1 269 ? 2.00300   -5.97200  41.98000 1.000 30.40051 ?  249 LYS A CA  1 
ATOM   1847 C C   . LYS A 1 269 ? 1.42800   -4.89300  42.88600 1.000 36.53003 ?  249 LYS A C   1 
ATOM   1848 O O   . LYS A 1 269 ? 1.92600   -3.76100  42.90400 1.000 32.87947 ?  249 LYS A O   1 
ATOM   1849 C CB  . LYS A 1 269 ? 3.34700   -6.45400  42.53100 1.000 38.18306 ?  249 LYS A CB  1 
ATOM   1850 C CG  . LYS A 1 269 ? 3.23800   -7.21200  43.84900 1.000 40.39353 ?  249 LYS A CG  1 
ATOM   1851 C CD  . LYS A 1 269 ? 4.59900   -7.67700  44.35300 1.000 46.19301 ?  249 LYS A CD  1 
ATOM   1852 C CE  . LYS A 1 269 ? 4.45200   -8.82700  45.34300 1.000 48.04120 ?  249 LYS A CE  1 
ATOM   1853 N N   . VAL A 1 270 ? 0.38800   -5.25000  43.64300 1.000 36.71185 ?  250 VAL A N   1 
ATOM   1854 C CA  . VAL A 1 270 ? -0.23000  -4.29700  44.55800 1.000 42.62477 ?  250 VAL A CA  1 
ATOM   1855 C C   . VAL A 1 270 ? 0.78600   -3.85500  45.59900 1.000 40.99464 ?  250 VAL A C   1 
ATOM   1856 O O   . VAL A 1 270 ? 1.49700   -4.67800  46.18700 1.000 42.61778 ?  250 VAL A O   1 
ATOM   1857 C CB  . VAL A 1 270 ? -1.47000  -4.91900  45.21800 1.000 48.98300 ?  250 VAL A CB  1 
ATOM   1858 C CG1 . VAL A 1 270 ? -2.20100  -3.88600  46.05900 1.000 43.73498 ?  250 VAL A CG1 1 
ATOM   1859 C CG2 . VAL A 1 270 ? -2.39000  -5.48500  44.16200 1.000 40.89572 ?  250 VAL A CG2 1 
ATOM   1860 N N   . ILE A 1 271 ? 0.86900   -2.54700  45.82100 1.000 44.21099 ?  251 ILE A N   1 
ATOM   1861 C CA  . ILE A 1 271 ? 1.76400   -1.99200  46.83100 1.000 52.21155 ?  251 ILE A CA  1 
ATOM   1862 C C   . ILE A 1 271 ? 0.98200   -1.68600  48.10300 1.000 52.96046 ?  251 ILE A C   1 
ATOM   1863 O O   . ILE A 1 271 ? 0.50500   -2.59600  48.78300 1.000 57.69097 ?  251 ILE A O   1 
ATOM   1864 C CB  . ILE A 1 271 ? 2.48100   -0.73100  46.31500 1.000 43.75925 ?  251 ILE A CB  1 
ATOM   1865 N N   . ASN B 1 27  ? -45.58400 -18.79000 48.48000 1.000 67.13940 ?  7   ASN B N   1 
ATOM   1866 C CA  . ASN B 1 27  ? -45.97800 -18.64100 47.08500 1.000 63.32767 ?  7   ASN B CA  1 
ATOM   1867 C C   . ASN B 1 27  ? -45.55000 -17.28500 46.52800 1.000 65.32716 ?  7   ASN B C   1 
ATOM   1868 O O   . ASN B 1 27  ? -45.54700 -17.08100 45.31200 1.000 67.52432 ?  7   ASN B O   1 
ATOM   1869 C CB  . ASN B 1 27  ? -47.49100 -18.81400 46.93600 1.000 56.40746 ?  7   ASN B CB  1 
ATOM   1870 N N   . ILE B 1 28  ? -45.18500 -16.36100 47.42000 1.000 54.11069 ?  8   ILE B N   1 
ATOM   1871 C CA  . ILE B 1 28  ? -44.86200 -14.98500 47.04900 1.000 58.85016 ?  8   ILE B CA  1 
ATOM   1872 C C   . ILE B 1 28  ? -43.35200 -14.82300 46.95100 1.000 47.67569 ?  8   ILE B C   1 
ATOM   1873 O O   . ILE B 1 28  ? -42.59300 -15.42000 47.72400 1.000 46.83059 ?  8   ILE B O   1 
ATOM   1874 C CB  . ILE B 1 28  ? -45.45800 -13.97900 48.05400 1.000 57.59532 ?  8   ILE B CB  1 
ATOM   1875 N N   . TYR B 1 29  ? -42.91800 -14.00700 45.99500 1.000 49.79073 ?  9   TYR B N   1 
ATOM   1876 C CA  . TYR B 1 29  ? -41.50300 -13.70600 45.83400 1.000 51.68349 ?  9   TYR B CA  1 
ATOM   1877 C C   . TYR B 1 29  ? -41.02900 -12.83300 46.98900 1.000 48.76880 ?  9   TYR B C   1 
ATOM   1878 O O   . TYR B 1 29  ? -41.69800 -11.86600 47.36400 1.000 47.89819 ?  9   TYR B O   1 
ATOM   1879 C CB  . TYR B 1 29  ? -41.27600 -13.00900 44.49100 1.000 48.46756 ?  9   TYR B CB  1 
ATOM   1880 C CG  . TYR B 1 29  ? -39.85700 -12.56900 44.21300 1.000 53.11576 ?  9   TYR B CG  1 
ATOM   1881 C CD1 . TYR B 1 29  ? -38.92700 -13.45100 43.67700 1.000 52.25615 ?  9   TYR B CD1 1 
ATOM   1882 C CD2 . TYR B 1 29  ? -39.45500 -11.26200 44.45700 1.000 49.31752 ?  9   TYR B CD2 1 
ATOM   1883 C CE1 . TYR B 1 29  ? -37.63000 -13.04800 43.41000 1.000 53.22795 ?  9   TYR B CE1 1 
ATOM   1884 C CE2 . TYR B 1 29  ? -38.16200 -10.85100 44.19500 1.000 47.71096 ?  9   TYR B CE2 1 
ATOM   1885 C CZ  . TYR B 1 29  ? -37.25400 -11.74800 43.67200 1.000 49.66819 ?  9   TYR B CZ  1 
ATOM   1886 O OH  . TYR B 1 29  ? -35.96700 -11.34000 43.41000 1.000 59.15432 ?  9   TYR B OH  1 
ATOM   1887 N N   . GLU B 1 30  ? -39.88000 -13.18200 47.56300 1.000 48.61206 ?  10  GLU B N   1 
ATOM   1888 C CA  . GLU B 1 30  ? -39.32700 -12.48400 48.71700 1.000 50.88040 ?  10  GLU B CA  1 
ATOM   1889 C C   . GLU B 1 30  ? -38.01900 -11.80700 48.33200 1.000 55.39763 ?  10  GLU B C   1 
ATOM   1890 O O   . GLU B 1 30  ? -37.12700 -12.44100 47.75600 1.000 50.13286 ?  10  GLU B O   1 
ATOM   1891 C CB  . GLU B 1 30  ? -39.09500 -13.44700 49.88600 1.000 50.15016 ?  10  GLU B CB  1 
ATOM   1892 C CG  . GLU B 1 30  ? -40.33900 -13.73200 50.71600 1.000 50.23958 ?  10  GLU B CG  1 
ATOM   1893 N N   . THR B 1 31  ? -37.90900 -10.52500 48.66000 1.000 46.87774 ?  11  THR B N   1 
ATOM   1894 C CA  . THR B 1 31  ? -36.72600 -9.73200  48.37800 1.000 45.68164 ?  11  THR B CA  1 
ATOM   1895 C C   . THR B 1 31  ? -35.76200 -9.75600  49.56500 1.000 48.14836 ?  11  THR B C   1 
ATOM   1896 O O   . THR B 1 31  ? -36.15700 -9.97100  50.71300 1.000 46.85841 ?  11  THR B O   1 
ATOM   1897 C CB  . THR B 1 31  ? -37.12900 -8.29600  48.05100 1.000 46.09928 ?  11  THR B CB  1 
ATOM   1898 O OG1 . THR B 1 31  ? -37.67100 -7.67700  49.22600 1.000 45.61267 ?  11  THR B OG1 1 
ATOM   1899 C CG2 . THR B 1 31  ? -38.18300 -8.28400  46.95200 1.000 44.36433 ?  11  THR B CG2 1 
ATOM   1900 N N   . ASP B 1 32  ? -34.48200 -9.52900  49.27000 1.000 50.84907 ?  12  ASP B N   1 
ATOM   1901 C CA  . ASP B 1 32  ? -33.43900 -9.50500  50.28700 1.000 48.32118 ?  12  ASP B CA  1 
ATOM   1902 C C   . ASP B 1 32  ? -33.42400 -8.15200  51.00100 1.000 45.58642 ?  12  ASP B C   1 
ATOM   1903 O O   . ASP B 1 32  ? -34.21500 -7.25400  50.70400 1.000 43.91709 ?  12  ASP B O   1 
ATOM   1904 C CB  . ASP B 1 32  ? -32.08000 -9.83400  49.66200 1.000 45.06230 ?  12  ASP B CB  1 
ATOM   1905 C CG  . ASP B 1 32  ? -31.61100 -8.78200  48.65600 1.000 57.12660 ?  12  ASP B CG  1 
ATOM   1906 O OD1 . ASP B 1 32  ? -31.88600 -7.58400  48.89600 1.000 55.78812 ?  12  ASP B OD1 1 
ATOM   1907 O OD2 . ASP B 1 32  ? -31.00300 -9.13500  47.61800 1.000 62.46366 -1 12  ASP B OD2 1 
ATOM   1908 N N   . GLU B 1 33  ? -32.48300 -7.99900  51.93900 1.000 43.79269 ?  13  GLU B N   1 
ATOM   1909 C CA  . GLU B 1 33  ? -32.45600 -6.81600  52.79800 1.000 48.16675 ?  13  GLU B CA  1 
ATOM   1910 C C   . GLU B 1 33  ? -32.22100 -5.54100  51.99400 1.000 44.27712 ?  13  GLU B C   1 
ATOM   1911 O O   . GLU B 1 33  ? -32.92900 -4.54300  52.17800 1.000 43.14128 ?  13  GLU B O   1 
ATOM   1912 C CB  . GLU B 1 33  ? -31.38500 -6.98100  53.87700 1.000 41.03180 ?  13  GLU B CB  1 
ATOM   1913 N N   . SER B 1 34  ? -31.22700 -5.55000  51.10000 1.000 39.67367 ?  14  SER B N   1 
ATOM   1914 C CA  . SER B 1 34  ? -30.93100 -4.35400  50.31300 1.000 46.04890 ?  14  SER B CA  1 
ATOM   1915 C C   . SER B 1 34  ? -32.10500 -3.98200  49.42200 1.000 44.79764 ?  14  SER B C   1 
ATOM   1916 O O   . SER B 1 34  ? -32.49000 -2.81100  49.33600 1.000 42.99873 ?  14  SER B O   1 
ATOM   1917 C CB  . SER B 1 34  ? -29.67400 -4.56000  49.46700 1.000 44.30398 ?  14  SER B CB  1 
ATOM   1918 O OG  . SER B 1 34  ? -28.67100 -5.26000  50.18200 1.000 56.70151 ?  14  SER B OG  1 
ATOM   1919 N N   . VAL B 1 35  ? -32.68200 -4.97100  48.74000 1.000 41.88095 ?  15  VAL B N   1 
ATOM   1920 C CA  . VAL B 1 35  ? -33.84400 -4.69600  47.90900 1.000 36.71501 ?  15  VAL B CA  1 
ATOM   1921 C C   . VAL B 1 35  ? -35.03500 -4.31100  48.77800 1.000 38.15018 ?  15  VAL B C   1 
ATOM   1922 O O   . VAL B 1 35  ? -35.79600 -3.39900  48.43400 1.000 36.99314 ?  15  VAL B O   1 
ATOM   1923 C CB  . VAL B 1 35  ? -34.14300 -5.90700  47.01000 1.000 42.24675 ?  15  VAL B CB  1 
ATOM   1924 C CG1 . VAL B 1 35  ? -35.39600 -5.66600  46.18900 1.000 43.28576 ?  15  VAL B CG1 1 
ATOM   1925 C CG2 . VAL B 1 35  ? -32.95500 -6.18200  46.09900 1.000 41.33836 ?  15  VAL B CG2 1 
ATOM   1926 N N   . SER B 1 36  ? -35.19200 -4.96300  49.93600 1.000 37.72250 ?  16  SER B N   1 
ATOM   1927 C CA  . SER B 1 36  ? -36.32700 -4.66200  50.80800 1.000 40.96338 ?  16  SER B CA  1 
ATOM   1928 C C   . SER B 1 36  ? -36.33800 -3.20000  51.23600 1.000 35.58148 ?  16  SER B C   1 
ATOM   1929 O O   . SER B 1 36  ? -37.40900 -2.59300  51.34600 1.000 33.41139 ?  16  SER B O   1 
ATOM   1930 C CB  . SER B 1 36  ? -36.32100 -5.57000  52.03900 1.000 42.23704 ?  16  SER B CB  1 
ATOM   1931 O OG  . SER B 1 36  ? -36.63900 -6.91000  51.69200 1.000 43.27194 ?  16  SER B OG  1 
ATOM   1932 N N   . GLN B 1 37  ? -35.16100 -2.61600  51.48100 1.000 36.42883 ?  17  GLN B N   1 
ATOM   1933 C CA  . GLN B 1 37  ? -35.11600 -1.21400  51.88400 1.000 39.49939 ?  17  GLN B CA  1 
ATOM   1934 C C   . GLN B 1 37  ? -35.72000 -0.31400  50.81500 1.000 34.93054 ?  17  GLN B C   1 
ATOM   1935 O O   . GLN B 1 37  ? -36.42300 0.65400   51.13000 1.000 35.50902 ?  17  GLN B O   1 
ATOM   1936 C CB  . GLN B 1 37  ? -33.68300 -0.78300  52.17900 1.000 37.73869 ?  17  GLN B CB  1 
ATOM   1937 C CG  . GLN B 1 37  ? -33.60200 0.65300   52.68000 1.000 43.36092 ?  17  GLN B CG  1 
ATOM   1938 C CD  . GLN B 1 37  ? -32.22000 1.02200   53.15600 1.000 45.59879 ?  17  GLN B CD  1 
ATOM   1939 O OE1 . GLN B 1 37  ? -31.25600 0.94700   52.39600 1.000 47.17070 ?  17  GLN B OE1 1 
ATOM   1940 N NE2 . GLN B 1 37  ? -32.11200 1.43200   54.41500 1.000 44.10594 ?  17  GLN B NE2 1 
ATOM   1941 N N   . TYR B 1 38  ? -35.45700 -0.61400  49.54700 1.000 30.11948 ?  18  TYR B N   1 
ATOM   1942 C CA  . TYR B 1 38  ? -36.06100 0.17000   48.48000 1.000 33.19910 ?  18  TYR B CA  1 
ATOM   1943 C C   . TYR B 1 38  ? -37.52600 -0.18800  48.26700 1.000 40.32893 ?  18  TYR B C   1 
ATOM   1944 O O   . TYR B 1 38  ? -38.31200 0.68500   47.87800 1.000 40.19370 ?  18  TYR B O   1 
ATOM   1945 C CB  . TYR B 1 38  ? -35.26000 -0.00100  47.19200 1.000 34.57435 ?  18  TYR B CB  1 
ATOM   1946 C CG  . TYR B 1 38  ? -34.07600 0.93600   47.12800 1.000 41.24197 ?  18  TYR B CG  1 
ATOM   1947 C CD1 . TYR B 1 38  ? -32.90000 0.64300   47.80600 1.000 44.29252 ?  18  TYR B CD1 1 
ATOM   1948 C CD2 . TYR B 1 38  ? -34.13900 2.12400   46.40800 1.000 49.01963 ?  18  TYR B CD2 1 
ATOM   1949 C CE1 . TYR B 1 38  ? -31.82200 1.49800   47.76400 1.000 49.42766 ?  18  TYR B CE1 1 
ATOM   1950 C CE2 . TYR B 1 38  ? -33.06100 2.98600   46.35700 1.000 46.39042 ?  18  TYR B CE2 1 
ATOM   1951 C CZ  . TYR B 1 38  ? -31.90600 2.66700   47.03600 1.000 55.35120 ?  18  TYR B CZ  1 
ATOM   1952 O OH  . TYR B 1 38  ? -30.83000 3.52200   46.99000 1.000 70.29127 ?  18  TYR B OH  1 
ATOM   1953 N N   . CYS B 1 39  ? -37.91400 -1.44500  48.52000 1.000 30.25685 ?  19  CYS B N   1 
ATOM   1954 C CA  . CYS B 1 39  ? -39.32900 -1.79600  48.47100 1.000 36.12143 ?  19  CYS B CA  1 
ATOM   1955 C C   . CYS B 1 39  ? -40.11900 -0.96600  49.47100 1.000 32.12360 ?  19  CYS B C   1 
ATOM   1956 O O   . CYS B 1 39  ? -41.16900 -0.40500  49.14300 1.000 37.09095 ?  19  CYS B O   1 
ATOM   1957 C CB  . CYS B 1 39  ? -39.52400 -3.28700  48.75300 1.000 36.17766 ?  19  CYS B CB  1 
ATOM   1958 S SG  . CYS B 1 39  ? -38.98300 -4.41600  47.45100 1.000 39.35492 ?  19  CYS B SG  1 
ATOM   1959 N N   . ASP B 1 40  ? -39.62100 -0.88400  50.70500 1.000 33.16969 ?  20  ASP B N   1 
ATOM   1960 C CA  . ASP B 1 40  ? -40.27000 -0.06600  51.72100 1.000 38.17791 ?  20  ASP B CA  1 
ATOM   1961 C C   . ASP B 1 40  ? -40.26000 1.40400   51.32800 1.000 36.06719 ?  20  ASP B C   1 
ATOM   1962 O O   . ASP B 1 40  ? -41.25400 2.11300   51.51600 1.000 36.14694 ?  20  ASP B O   1 
ATOM   1963 C CB  . ASP B 1 40  ? -39.56700 -0.26800  53.06000 1.000 38.56686 ?  20  ASP B CB  1 
ATOM   1964 C CG  . ASP B 1 40  ? -40.46300 0.02800   54.23300 1.000 45.33037 ?  20  ASP B CG  1 
ATOM   1965 O OD1 . ASP B 1 40  ? -41.68200 -0.21600  54.11900 1.000 49.96930 ?  20  ASP B OD1 1 
ATOM   1966 O OD2 . ASP B 1 40  ? -39.94600 0.49200   55.27000 1.000 50.51229 -1 20  ASP B OD2 1 
ATOM   1967 N N   . PHE B 1 41  ? -39.14700 1.86900   50.76000 1.000 32.21594 ?  21  PHE B N   1 
ATOM   1968 C CA  . PHE B 1 41  ? -39.02200 3.26700   50.35900 1.000 33.43155 ?  21  PHE B CA  1 
ATOM   1969 C C   . PHE B 1 41  ? -40.00200 3.61400   49.24400 1.000 34.67418 ?  21  PHE B C   1 
ATOM   1970 O O   . PHE B 1 41  ? -40.61500 4.68800   49.26000 1.000 35.62947 ?  21  PHE B O   1 
ATOM   1971 C CB  . PHE B 1 41  ? -37.57500 3.53100   49.92700 1.000 32.27362 ?  21  PHE B CB  1 
ATOM   1972 C CG  . PHE B 1 41  ? -37.30100 4.93900   49.46100 1.000 39.33692 ?  21  PHE B CG  1 
ATOM   1973 C CD1 . PHE B 1 41  ? -37.68300 6.03300   50.22500 1.000 37.81080 ?  21  PHE B CD1 1 
ATOM   1974 C CD2 . PHE B 1 41  ? -36.61100 5.16300   48.27700 1.000 32.93675 ?  21  PHE B CD2 1 
ATOM   1975 C CE1 . PHE B 1 41  ? -37.40700 7.32300   49.80200 1.000 33.61972 ?  21  PHE B CE1 1 
ATOM   1976 C CE2 . PHE B 1 41  ? -36.32900 6.44700   47.85100 1.000 36.85755 ?  21  PHE B CE2 1 
ATOM   1977 C CZ  . PHE B 1 41  ? -36.72800 7.53000   48.61200 1.000 36.42285 ?  21  PHE B CZ  1 
ATOM   1978 N N   . GLN B 1 42  ? -40.18500 2.71100   48.28400 1.000 31.23917 ?  22  GLN B N   1 
ATOM   1979 C CA  . GLN B 1 42  ? -40.95000 3.03800   47.08600 1.000 35.61993 ?  22  GLN B CA  1 
ATOM   1980 C C   . GLN B 1 42  ? -42.42700 2.67600   47.19000 1.000 31.90938 ?  22  GLN B C   1 
ATOM   1981 O O   . GLN B 1 42  ? -43.26600 3.35300   46.58900 1.000 34.67687 ?  22  GLN B O   1 
ATOM   1982 C CB  . GLN B 1 42  ? -40.33500 2.34100   45.87200 1.000 34.21427 ?  22  GLN B CB  1 
ATOM   1983 C CG  . GLN B 1 42  ? -39.05300 2.99500   45.37700 1.000 35.03329 ?  22  GLN B CG  1 
ATOM   1984 C CD  . GLN B 1 42  ? -38.71800 2.60000   43.95300 1.000 36.70373 ?  22  GLN B CD  1 
ATOM   1985 O OE1 . GLN B 1 42  ? -39.23100 1.60900   43.43500 1.000 40.68248 ?  22  GLN B OE1 1 
ATOM   1986 N NE2 . GLN B 1 42  ? -37.87200 3.38900   43.30400 1.000 46.83478 ?  22  GLN B NE2 1 
ATOM   1987 N N   . TYR B 1 43  ? -42.77000 1.63900   47.94700 1.000 33.51416 ?  23  TYR B N   1 
ATOM   1988 C CA  . TYR B 1 43  ? -44.14700 1.17500   48.04400 1.000 34.91198 ?  23  TYR B CA  1 
ATOM   1989 C C   . TYR B 1 43  ? -44.71500 1.24200   49.45400 1.000 38.10325 ?  23  TYR B C   1 
ATOM   1990 O O   . TYR B 1 43  ? -45.92000 1.01700   49.62600 1.000 37.47445 ?  23  TYR B O   1 
ATOM   1991 C CB  . TYR B 1 43  ? -44.25800 -0.26800  47.52200 1.000 30.12145 ?  23  TYR B CB  1 
ATOM   1992 C CG  . TYR B 1 43  ? -43.82600 -0.41300  46.07400 1.000 26.03661 ?  23  TYR B CG  1 
ATOM   1993 C CD1 . TYR B 1 43  ? -44.69300 -0.10000  45.04000 1.000 30.10325 ?  23  TYR B CD1 1 
ATOM   1994 C CD2 . TYR B 1 43  ? -42.54900 -0.85200  45.74600 1.000 27.13023 ?  23  TYR B CD2 1 
ATOM   1995 C CE1 . TYR B 1 43  ? -44.31100 -0.22300  43.71500 1.000 29.71642 ?  23  TYR B CE1 1 
ATOM   1996 C CE2 . TYR B 1 43  ? -42.15100 -0.98300  44.42100 1.000 30.47073 ?  23  TYR B CE2 1 
ATOM   1997 C CZ  . TYR B 1 43  ? -43.04400 -0.66300  43.41000 1.000 30.08710 ?  23  TYR B CZ  1 
ATOM   1998 O OH  . TYR B 1 43  ? -42.67500 -0.78300  42.09400 1.000 33.19598 ?  23  TYR B OH  1 
ATOM   1999 N N   . GLY B 1 44  ? -43.89800 1.55600   50.45600 1.000 37.32759 ?  24  GLY B N   1 
ATOM   2000 C CA  . GLY B 1 44  ? -44.32800 1.54000   51.83700 1.000 34.84364 ?  24  GLY B CA  1 
ATOM   2001 C C   . GLY B 1 44  ? -45.06800 2.80000   52.24300 1.000 36.43041 ?  24  GLY B C   1 
ATOM   2002 O O   . GLY B 1 44  ? -45.41900 3.65700   51.42900 1.000 39.61226 ?  24  GLY B O   1 
ATOM   2003 N N   . GLU B 1 45  ? -45.30500 2.89900   53.54700 1.000 31.68661 ?  25  GLU B N   1 
ATOM   2004 C CA  . GLU B 1 45  ? -46.07700 3.99200   54.11500 1.000 43.10039 ?  25  GLU B CA  1 
ATOM   2005 C C   . GLU B 1 45  ? -45.23500 5.25800   54.21100 1.000 37.55828 ?  25  GLU B C   1 
ATOM   2006 O O   . GLU B 1 45  ? -44.01700 5.20900   54.39100 1.000 41.36754 ?  25  GLU B O   1 
ATOM   2007 C CB  . GLU B 1 45  ? -46.59700 3.60800   55.50200 1.000 39.91764 ?  25  GLU B CB  1 
ATOM   2008 C CG  . GLU B 1 45  ? -47.99300 3.00500   55.50000 1.000 43.04289 ?  25  GLU B CG  1 
ATOM   2009 N N   . ASP B 1 46  ? -45.89900 6.40300   54.09600 1.000 37.82706 ?  26  ASP B N   1 
ATOM   2010 C CA  . ASP B 1 46  ? -45.20400 7.68000   54.17900 1.000 40.04017 ?  26  ASP B CA  1 
ATOM   2011 C C   . ASP B 1 46  ? -44.68900 7.90500   55.59600 1.000 42.33643 ?  26  ASP B C   1 
ATOM   2012 O O   . ASP B 1 46  ? -45.37400 7.60800   56.57700 1.000 43.82784 ?  26  ASP B O   1 
ATOM   2013 C CB  . ASP B 1 46  ? -46.13900 8.82000   53.76700 1.000 43.20153 ?  26  ASP B CB  1 
ATOM   2014 C CG  . ASP B 1 46  ? -46.49900 8.78500   52.28600 1.000 43.87146 ?  26  ASP B CG  1 
ATOM   2015 O OD1 . ASP B 1 46  ? -46.02100 7.87900   51.56300 1.000 43.15885 ?  26  ASP B OD1 1 
ATOM   2016 O OD2 . ASP B 1 46  ? -47.27200 9.66500   51.84700 1.000 47.04028 -1 26  ASP B OD2 1 
ATOM   2017 N N   . CYS B 1 47  ? -43.47000 8.42500   55.70000 1.000 39.56379 ?  27  CYS B N   1 
ATOM   2018 C CA  . CYS B 1 47  ? -42.82700 8.69100   56.97800 1.000 38.03705 ?  27  CYS B CA  1 
ATOM   2019 C C   . CYS B 1 47  ? -42.76500 10.19100  57.22500 1.000 37.27808 ?  27  CYS B C   1 
ATOM   2020 O O   . CYS B 1 47  ? -42.44900 10.96300  56.31500 1.000 35.28973 ?  27  CYS B O   1 
ATOM   2021 C CB  . CYS B 1 47  ? -41.40800 8.11700   57.01700 1.000 36.67100 ?  27  CYS B CB  1 
ATOM   2022 S SG  . CYS B 1 47  ? -41.28300 6.33000   56.79700 1.000 47.31851 ?  27  CYS B SG  1 
ATOM   2023 N N   . PHE B 1 48  ? -43.06200 10.59700  58.46200 1.000 35.72980 ?  28  PHE B N   1 
ATOM   2024 C CA  . PHE B 1 48  ? -42.96500 11.99500  58.88300 1.000 30.77432 ?  28  PHE B CA  1 
ATOM   2025 C C   . PHE B 1 48  ? -43.79700 12.91700  57.99900 1.000 36.26165 ?  28  PHE B C   1 
ATOM   2026 O O   . PHE B 1 48  ? -43.44000 14.08100  57.79100 1.000 38.05240 ?  28  PHE B O   1 
ATOM   2027 C CB  . PHE B 1 48  ? -41.50800 12.46800  58.91200 1.000 32.60804 ?  28  PHE B CB  1 
ATOM   2028 C CG  . PHE B 1 48  ? -40.62200 11.65700  59.81300 1.000 36.16959 ?  28  PHE B CG  1 
ATOM   2029 C CD1 . PHE B 1 48  ? -40.86800 11.59200  61.17200 1.000 33.63565 ?  28  PHE B CD1 1 
ATOM   2030 C CD2 . PHE B 1 48  ? -39.53200 10.97400  59.30200 1.000 36.62125 ?  28  PHE B CD2 1 
ATOM   2031 C CE1 . PHE B 1 48  ? -40.04600 10.85100  62.00400 1.000 35.57201 ?  28  PHE B CE1 1 
ATOM   2032 C CE2 . PHE B 1 48  ? -38.70700 10.23600  60.12700 1.000 33.16360 ?  28  PHE B CE2 1 
ATOM   2033 C CZ  . PHE B 1 48  ? -38.96600 10.17600  61.48000 1.000 32.92420 ?  28  PHE B CZ  1 
ATOM   2034 N N   . GLY B 1 49  ? -44.90200 12.40100  57.46500 1.000 40.69430 ?  29  GLY B N   1 
ATOM   2035 C CA  . GLY B 1 49  ? -45.75400 13.18200  56.59400 1.000 40.65617 ?  29  GLY B CA  1 
ATOM   2036 C C   . GLY B 1 49  ? -45.17000 13.49600  55.23700 1.000 41.72606 ?  29  GLY B C   1 
ATOM   2037 O O   . GLY B 1 49  ? -45.69500 14.36900  54.54100 1.000 40.76713 ?  29  GLY B O   1 
ATOM   2038 N N   . VAL B 1 50  ? -44.10800 12.81400  54.83100 1.000 38.10289 ?  30  VAL B N   1 
ATOM   2039 C CA  . VAL B 1 50  ? -43.43300 13.11300  53.57500 1.000 35.82419 ?  30  VAL B CA  1 
ATOM   2040 C C   . VAL B 1 50  ? -44.03300 12.25000  52.47500 1.000 34.26776 ?  30  VAL B C   1 
ATOM   2041 O O   . VAL B 1 50  ? -44.13200 11.02500  52.61800 1.000 34.36910 ?  30  VAL B O   1 
ATOM   2042 C CB  . VAL B 1 50  ? -41.91600 12.89100  53.69800 1.000 31.97152 ?  30  VAL B CB  1 
ATOM   2043 C CG1 . VAL B 1 50  ? -41.22500 13.16300  52.36600 1.000 26.87894 ?  30  VAL B CG1 1 
ATOM   2044 C CG2 . VAL B 1 50  ? -41.35000 13.78500  54.78300 1.000 30.61958 ?  30  VAL B CG2 1 
ATOM   2045 N N   . LEU B 1 51  ? -44.44100 12.89400  51.38000 1.000 37.93190 ?  31  LEU B N   1 
ATOM   2046 C CA  . LEU B 1 51  ? -45.00700 12.18100  50.24200 1.000 34.97931 ?  31  LEU B CA  1 
ATOM   2047 C C   . LEU B 1 51  ? -43.99200 11.21200  49.64800 1.000 37.57114 ?  31  LEU B C   1 
ATOM   2048 O O   . LEU B 1 51  ? -42.78400 11.46400  49.65200 1.000 33.48371 ?  31  LEU B O   1 
ATOM   2049 C CB  . LEU B 1 51  ? -45.46700 13.17100  49.17400 1.000 33.70763 ?  31  LEU B CB  1 
ATOM   2050 C CG  . LEU B 1 51  ? -46.52400 12.66100  48.19700 1.000 41.51531 ?  31  LEU B CG  1 
ATOM   2051 C CD1 . LEU B 1 51  ? -47.90700 12.75100  48.81400 1.000 50.55824 ?  31  LEU B CD1 1 
ATOM   2052 C CD2 . LEU B 1 51  ? -46.45900 13.44600  46.88600 1.000 44.14314 ?  31  LEU B CD2 1 
ATOM   2053 N N   . ASN B 1 52  ? -44.50300 10.09000  49.13800 1.000 25.67243 ?  32  ASN B N   1 
ATOM   2054 C CA  . ASN B 1 52  ? -43.66400 9.08400   48.50500 1.000 33.63144 ?  32  ASN B CA  1 
ATOM   2055 C C   . ASN B 1 52  ? -42.76000 9.72800   47.46500 1.000 30.95091 ?  32  ASN B C   1 
ATOM   2056 O O   . ASN B 1 52  ? -43.22900 10.44100  46.57400 1.000 35.60065 ?  32  ASN B O   1 
ATOM   2057 C CB  . ASN B 1 52  ? -44.53500 8.01100   47.84800 1.000 35.20939 ?  32  ASN B CB  1 
ATOM   2058 C CG  . ASN B 1 52  ? -43.71600 6.93900   47.16800 1.000 39.27768 ?  32  ASN B CG  1 
ATOM   2059 O OD1 . ASN B 1 52  ? -43.47000 6.99900   45.96100 1.000 38.99210 ?  32  ASN B OD1 1 
ATOM   2060 N ND2 . ASN B 1 52  ? -43.29200 5.94300   47.93800 1.000 37.21042 ?  32  ASN B ND2 1 
ATOM   2061 N N   . PHE B 1 53  ? -41.45400 9.48500   47.59500 1.000 27.86778 ?  33  PHE B N   1 
ATOM   2062 C CA  . PHE B 1 53  ? -40.48400 10.15700  46.73600 1.000 29.05656 ?  33  PHE B CA  1 
ATOM   2063 C C   . PHE B 1 53  ? -40.69400 9.80600   45.27100 1.000 27.52661 ?  33  PHE B C   1 
ATOM   2064 O O   . PHE B 1 53  ? -40.66600 10.68700  44.40600 1.000 30.49118 ?  33  PHE B O   1 
ATOM   2065 C CB  . PHE B 1 53  ? -39.06300 9.79700   47.17200 1.000 30.35509 ?  33  PHE B CB  1 
ATOM   2066 C CG  . PHE B 1 53  ? -37.98600 10.55000  46.43000 1.000 30.84865 ?  33  PHE B CG  1 
ATOM   2067 C CD1 . PHE B 1 53  ? -37.92300 11.93200  46.48200 1.000 27.22632 ?  33  PHE B CD1 1 
ATOM   2068 C CD2 . PHE B 1 53  ? -37.03400 9.87200   45.68700 1.000 30.35908 ?  33  PHE B CD2 1 
ATOM   2069 C CE1 . PHE B 1 53  ? -36.93400 12.62200  45.80400 1.000 29.71716 ?  33  PHE B CE1 1 
ATOM   2070 C CE2 . PHE B 1 53  ? -36.04100 10.55800  45.00800 1.000 31.52916 ?  33  PHE B CE2 1 
ATOM   2071 C CZ  . PHE B 1 53  ? -35.99000 11.93400  45.07000 1.000 28.00597 ?  33  PHE B CZ  1 
ATOM   2072 N N   . ALA B 1 54  ? -40.89400 8.52200   44.96900 1.000 29.84759 ?  34  ALA B N   1 
ATOM   2073 C CA  . ALA B 1 54  ? -41.04200 8.11000   43.57700 1.000 29.10961 ?  34  ALA B CA  1 
ATOM   2074 C C   . ALA B 1 54  ? -42.30000 8.70500   42.95800 1.000 35.03624 ?  34  ALA B C   1 
ATOM   2075 O O   . ALA B 1 54  ? -42.28900 9.13700   41.79800 1.000 33.18961 ?  34  ALA B O   1 
ATOM   2076 C CB  . ALA B 1 54  ? -41.05800 6.58600   43.48000 1.000 26.93958 ?  34  ALA B CB  1 
ATOM   2077 N N   . LEU B 1 55  ? -43.39500 8.73900   43.72300 1.000 32.94955 ?  35  LEU B N   1 
ATOM   2078 C CA  . LEU B 1 55  ? -44.61700 9.38300   43.25200 1.000 36.06384 ?  35  LEU B CA  1 
ATOM   2079 C C   . LEU B 1 55  ? -44.40000 10.86900  43.00200 1.000 32.04443 ?  35  LEU B C   1 
ATOM   2080 O O   . LEU B 1 55  ? -44.83500 11.40200  41.97400 1.000 32.93893 ?  35  LEU B O   1 
ATOM   2081 C CB  . LEU B 1 55  ? -45.73900 9.17300   44.26700 1.000 35.47764 ?  35  LEU B CB  1 
ATOM   2082 C CG  . LEU B 1 55  ? -47.05500 9.86700   43.93800 1.000 38.75390 ?  35  LEU B CG  1 
ATOM   2083 C CD1 . LEU B 1 55  ? -47.64000 9.30200   42.65200 1.000 37.37542 ?  35  LEU B CD1 1 
ATOM   2084 C CD2 . LEU B 1 55  ? -48.03100 9.72400   45.09000 1.000 34.12628 ?  35  LEU B CD2 1 
ATOM   2085 N N   . ALA B 1 56  ? -43.72300 11.55000  43.93100 1.000 34.45002 ?  36  ALA B N   1 
ATOM   2086 C CA  . ALA B 1 56  ? -43.49500 12.98500  43.79000 1.000 32.13627 ?  36  ALA B CA  1 
ATOM   2087 C C   . ALA B 1 56  ? -42.62100 13.28900  42.58200 1.000 33.67127 ?  36  ALA B C   1 
ATOM   2088 O O   . ALA B 1 56  ? -42.89700 14.22600  41.82500 1.000 32.71217 ?  36  ALA B O   1 
ATOM   2089 C CB  . ALA B 1 56  ? -42.85800 13.53900  45.06600 1.000 30.93419 ?  36  ALA B CB  1 
ATOM   2090 N N   . CYS B 1 57  ? -41.55700 12.50700  42.38700 1.000 30.50692 ?  37  CYS B N   1 
ATOM   2091 C CA  . CYS B 1 57  ? -40.68800 12.71600  41.23200 1.000 31.14031 ?  37  CYS B CA  1 
ATOM   2092 C C   . CYS B 1 57  ? -41.44100 12.48500  39.92800 1.000 35.98365 ?  37  CYS B C   1 
ATOM   2093 O O   . CYS B 1 57  ? -41.33600 13.28200  38.98600 1.000 30.98904 ?  37  CYS B O   1 
ATOM   2094 C CB  . CYS B 1 57  ? -39.46500 11.80000  41.31600 1.000 34.52180 ?  37  CYS B CB  1 
ATOM   2095 S SG  . CYS B 1 57  ? -38.26700 12.28300  42.59000 1.000 37.13116 ?  37  CYS B SG  1 
ATOM   2096 N N   . ALA B 1 58  ? -42.21200 11.39800  39.85500 1.000 33.81755 ?  38  ALA B N   1 
ATOM   2097 C CA  . ALA B 1 58  ? -42.92300 11.08300  38.61900 1.000 29.25895 ?  38  ALA B CA  1 
ATOM   2098 C C   . ALA B 1 58  ? -44.00800 12.11300  38.32900 1.000 35.72766 ?  38  ALA B C   1 
ATOM   2099 O O   . ALA B 1 58  ? -44.19800 12.52300  37.17600 1.000 37.15089 ?  38  ALA B O   1 
ATOM   2100 C CB  . ALA B 1 58  ? -43.51800 9.67900   38.70100 1.000 23.63968 ?  38  ALA B CB  1 
ATOM   2101 N N   . THR B 1 59  ? -44.72600 12.54400  39.36800 1.000 35.80810 ?  39  THR B N   1 
ATOM   2102 C CA  . THR B 1 59  ? -45.74600 13.57700  39.20800 1.000 30.18958 ?  39  THR B CA  1 
ATOM   2103 C C   . THR B 1 59  ? -45.13800 14.87100  38.68200 1.000 40.77312 ?  39  THR B C   1 
ATOM   2104 O O   . THR B 1 59  ? -45.65300 15.48000  37.73600 1.000 41.43987 ?  39  THR B O   1 
ATOM   2105 C CB  . THR B 1 59  ? -46.44200 13.82300  40.54800 1.000 30.93736 ?  39  THR B CB  1 
ATOM   2106 O OG1 . THR B 1 59  ? -46.93700 12.58300  41.06200 1.000 36.30080 ?  39  THR B OG1 1 
ATOM   2107 C CG2 . THR B 1 59  ? -47.59200 14.80800  40.40100 1.000 31.66340 ?  39  THR B CG2 1 
ATOM   2108 N N   . LYS B 1 60  ? -44.03900 15.31100  39.29900 1.000 34.95050 ?  40  LYS B N   1 
ATOM   2109 C CA  . LYS B 1 60  ? -43.37700 16.53200  38.85200 1.000 31.66131 ?  40  LYS B CA  1 
ATOM   2110 C C   . LYS B 1 60  ? -42.85700 16.38800  37.42900 1.000 33.56417 ?  40  LYS B C   1 
ATOM   2111 O O   . LYS B 1 60  ? -42.97300 17.31700  36.62000 1.000 36.08235 ?  40  LYS B O   1 
ATOM   2112 C CB  . LYS B 1 60  ? -42.23600 16.88800  39.80500 1.000 33.23882 ?  40  LYS B CB  1 
ATOM   2113 C CG  . LYS B 1 60  ? -42.65000 17.76400  40.97900 1.000 41.52756 ?  40  LYS B CG  1 
ATOM   2114 C CD  . LYS B 1 60  ? -41.85700 17.40400  42.22300 1.000 38.26205 ?  40  LYS B CD  1 
ATOM   2115 C CE  . LYS B 1 60  ? -42.70100 17.50700  43.47900 1.000 39.43816 ?  40  LYS B CE  1 
ATOM   2116 N NZ  . LYS B 1 60  ? -43.30000 18.86900  43.60200 1.000 39.20726 ?  40  LYS B NZ  1 
ATOM   2117 N N   . ALA B 1 61  ? -42.28400 15.22500  37.10400 1.000 30.30332 ?  41  ALA B N   1 
ATOM   2118 C CA  . ALA B 1 61  ? -41.78200 14.99300  35.75400 1.000 29.46086 ?  41  ALA B CA  1 
ATOM   2119 C C   . ALA B 1 61  ? -42.90800 15.04400  34.73600 1.000 32.88777 ?  41  ALA B C   1 
ATOM   2120 O O   . ALA B 1 61  ? -42.73800 15.58400  33.63600 1.000 31.73402 ?  41  ALA B O   1 
ATOM   2121 C CB  . ALA B 1 61  ? -41.05900 13.64600  35.68600 1.000 28.02703 ?  41  ALA B CB  1 
ATOM   2122 N N   . ILE B 1 62  ? -44.06800 14.48400  35.08500 1.000 36.93908 ?  42  ILE B N   1 
ATOM   2123 C CA  . ILE B 1 62  ? -45.23300 14.58500  34.21500 1.000 34.44009 ?  42  ILE B CA  1 
ATOM   2124 C C   . ILE B 1 62  ? -45.63100 16.04300  34.04000 1.000 36.59389 ?  42  ILE B C   1 
ATOM   2125 O O   . ILE B 1 62  ? -45.93100 16.48900  32.92700 1.000 40.29123 ?  42  ILE B O   1 
ATOM   2126 C CB  . ILE B 1 62  ? -46.38700 13.73300  34.77400 1.000 37.17964 ?  42  ILE B CB  1 
ATOM   2127 C CG1 . ILE B 1 62  ? -46.07400 12.24300  34.59900 1.000 39.58293 ?  42  ILE B CG1 1 
ATOM   2128 C CG2 . ILE B 1 62  ? -47.69900 14.07900  34.09300 1.000 38.57980 ?  42  ILE B CG2 1 
ATOM   2129 C CD1 . ILE B 1 62  ? -46.93800 11.32900  35.44600 1.000 38.09719 ?  42  ILE B CD1 1 
ATOM   2130 N N   . GLY B 1 63  ? -45.59900 16.81600  35.12800 1.000 39.89501 ?  43  GLY B N   1 
ATOM   2131 C CA  . GLY B 1 63  ? -45.93500 18.22700  35.03600 1.000 37.86007 ?  43  GLY B CA  1 
ATOM   2132 C C   . GLY B 1 63  ? -44.96900 19.01600  34.17000 1.000 39.89267 ?  43  GLY B C   1 
ATOM   2133 O O   . GLY B 1 63  ? -45.39100 19.82800  33.34400 1.000 47.36132 ?  43  GLY B O   1 
ATOM   2134 N N   . TYR B 1 64  ? -43.66400 18.78300  34.33400 1.000 32.84901 ?  44  TYR B N   1 
ATOM   2135 C CA  . TYR B 1 64  ? -42.67800 19.54000  33.56600 1.000 37.99517 ?  44  TYR B CA  1 
ATOM   2136 C C   . TYR B 1 64  ? -42.67300 19.16500  32.08900 1.000 36.46903 ?  44  TYR B C   1 
ATOM   2137 O O   . TYR B 1 64  ? -42.17700 19.94400  31.26700 1.000 38.29261 ?  44  TYR B O   1 
ATOM   2138 C CB  . TYR B 1 64  ? -41.27900 19.34000  34.15500 1.000 33.44454 ?  44  TYR B CB  1 
ATOM   2139 C CG  . TYR B 1 64  ? -41.05600 20.11600  35.42900 1.000 32.09953 ?  44  TYR B CG  1 
ATOM   2140 C CD1 . TYR B 1 64  ? -41.08500 21.50500  35.43500 1.000 31.53995 ?  44  TYR B CD1 1 
ATOM   2141 C CD2 . TYR B 1 64  ? -40.83300 19.46000  36.62900 1.000 32.38392 ?  44  TYR B CD2 1 
ATOM   2142 C CE1 . TYR B 1 64  ? -40.89100 22.21800  36.60500 1.000 37.68379 ?  44  TYR B CE1 1 
ATOM   2143 C CE2 . TYR B 1 64  ? -40.63800 20.16000  37.79700 1.000 36.22672 ?  44  TYR B CE2 1 
ATOM   2144 C CZ  . TYR B 1 64  ? -40.66600 21.53600  37.78300 1.000 33.77530 ?  44  TYR B CZ  1 
ATOM   2145 O OH  . TYR B 1 64  ? -40.47100 22.23100  38.95500 1.000 42.27079 ?  44  TYR B OH  1 
ATOM   2146 N N   . THR B 1 65  ? -43.20600 17.99800  31.73500 1.000 36.47402 ?  45  THR B N   1 
ATOM   2147 C CA  . THR B 1 65  ? -43.26100 17.54300  30.35200 1.000 39.93347 ?  45  THR B CA  1 
ATOM   2148 C C   . THR B 1 65  ? -44.67700 17.63800  29.78400 1.000 39.04651 ?  45  THR B C   1 
ATOM   2149 O O   . THR B 1 65  ? -45.04200 16.88200  28.88000 1.000 42.34544 ?  45  THR B O   1 
ATOM   2150 C CB  . THR B 1 65  ? -42.72400 16.11600  30.24200 1.000 39.41300 ?  45  THR B CB  1 
ATOM   2151 O OG1 . THR B 1 65  ? -43.52700 15.22600  31.03100 1.000 35.87878 ?  45  THR B OG1 1 
ATOM   2152 C CG2 . THR B 1 65  ? -41.28300 16.05100  30.73200 1.000 38.22888 ?  45  THR B CG2 1 
ATOM   2153 N N   . LYS B 1 66  ? -45.46700 18.58100  30.30800 1.000 38.61801 ?  46  LYS B N   1 
ATOM   2154 C CA  . LYS B 1 66  ? -46.87200 18.72900  29.92800 1.000 46.74021 ?  46  LYS B CA  1 
ATOM   2155 C C   . LYS B 1 66  ? -47.04700 18.90100  28.42500 1.000 41.88661 ?  46  LYS B C   1 
ATOM   2156 O O   . LYS B 1 66  ? -48.03400 18.42800  27.84700 1.000 33.54200 ?  46  LYS B O   1 
ATOM   2157 C CB  . LYS B 1 66  ? -47.47700 19.93500  30.64800 1.000 41.95438 ?  46  LYS B CB  1 
ATOM   2158 C CG  . LYS B 1 66  ? -48.16400 19.62300  31.95000 1.000 46.98527 ?  46  LYS B CG  1 
ATOM   2159 C CD  . LYS B 1 66  ? -48.58100 20.90600  32.65500 1.000 46.09584 ?  46  LYS B CD  1 
ATOM   2160 N N   . GLU B 1 67  ? -46.12000 19.60600  27.78200 1.000 35.38568 ?  47  GLU B N   1 
ATOM   2161 C CA  . GLU B 1 67  ? -46.24900 19.97500  26.38300 1.000 39.89866 ?  47  GLU B CA  1 
ATOM   2162 C C   . GLU B 1 67  ? -45.43400 19.07100  25.46500 1.000 42.65456 ?  47  GLU B C   1 
ATOM   2163 O O   . GLU B 1 67  ? -45.23000 19.41200  24.29500 1.000 39.96827 ?  47  GLU B O   1 
ATOM   2164 C CB  . GLU B 1 67  ? -45.84500 21.43900  26.19300 1.000 37.57288 ?  47  GLU B CB  1 
ATOM   2165 N N   . THR B 1 68  ? -44.96600 17.93000  25.96600 1.000 39.72474 ?  48  THR B N   1 
ATOM   2166 C CA  . THR B 1 68  ? -44.22500 16.98800  25.14600 1.000 38.24296 ?  48  THR B CA  1 
ATOM   2167 C C   . THR B 1 68  ? -45.14600 15.88700  24.65600 1.000 43.42028 ?  48  THR B C   1 
ATOM   2168 O O   . THR B 1 68  ? -46.20900 15.64900  25.23500 1.000 39.07838 ?  48  THR B O   1 
ATOM   2169 C CB  . THR B 1 68  ? -43.07500 16.35300  25.94000 1.000 45.86681 ?  48  THR B CB  1 
ATOM   2170 O OG1 . THR B 1 68  ? -43.59400 15.31400  26.78500 1.000 47.53916 ?  48  THR B OG1 1 
ATOM   2171 C CG2 . THR B 1 68  ? -42.36800 17.38900  26.79100 1.000 40.45129 ?  48  THR B CG2 1 
ATOM   2172 N N   . PRO B 1 69  ? -44.77400 15.19000  23.58300 1.000 46.28641 ?  49  PRO B N   1 
ATOM   2173 C CA  . PRO B 1 69  ? -45.43100 13.91300  23.29700 1.000 42.63048 ?  49  PRO B CA  1 
ATOM   2174 C C   . PRO B 1 69  ? -45.10500 12.96000  24.43300 1.000 51.90755 ?  49  PRO B C   1 
ATOM   2175 O O   . PRO B 1 69  ? -43.94600 12.81600  24.82400 1.000 56.67669 ?  49  PRO B O   1 
ATOM   2176 C CB  . PRO B 1 69  ? -44.79000 13.45900  21.97800 1.000 42.40989 ?  49  PRO B CB  1 
ATOM   2177 C CG  . PRO B 1 69  ? -44.05100 14.64800  21.45100 1.000 46.33856 ?  49  PRO B CG  1 
ATOM   2178 C CD  . PRO B 1 69  ? -43.67200 15.46400  22.64300 1.000 43.80913 ?  49  PRO B CD  1 
ATOM   2179 N N   . LYS B 1 70  ? -46.12600 12.33400  24.99300 1.000 50.62569 ?  50  LYS B N   1 
ATOM   2180 C CA  . LYS B 1 70  ? -45.89800 11.44400  26.12600 1.000 47.53575 ?  50  LYS B CA  1 
ATOM   2181 C C   . LYS B 1 70  ? -45.81200 9.99700   25.64800 1.000 41.11855 ?  50  LYS B C   1 
ATOM   2182 O O   . LYS B 1 70  ? -46.54300 9.11600   26.09400 1.000 46.78000 ?  50  LYS B O   1 
ATOM   2183 C CB  . LYS B 1 70  ? -46.98500 11.64500  27.17600 1.000 48.92274 ?  50  LYS B CB  1 
ATOM   2184 C CG  . LYS B 1 70  ? -47.09500 13.09200  27.62300 1.000 47.08492 ?  50  LYS B CG  1 
ATOM   2185 C CD  . LYS B 1 70  ? -46.01500 13.45800  28.63200 1.000 48.44855 ?  50  LYS B CD  1 
ATOM   2186 C CE  . LYS B 1 70  ? -46.60400 14.10600  29.87700 1.000 45.83805 ?  50  LYS B CE  1 
ATOM   2187 N N   . ASN B 1 71  ? -44.88000 9.76100   24.72100 1.000 38.80067 ?  51  ASN B N   1 
ATOM   2188 C CA  . ASN B 1 71  ? -44.74400 8.44600   24.10500 1.000 42.08290 ?  51  ASN B CA  1 
ATOM   2189 C C   . ASN B 1 71  ? -43.78500 7.53000   24.86400 1.000 41.04260 ?  51  ASN B C   1 
ATOM   2190 O O   . ASN B 1 71  ? -44.14600 6.39700   25.19400 1.000 41.37790 ?  51  ASN B O   1 
ATOM   2191 C CB  . ASN B 1 71  ? -44.28700 8.59100   22.65100 1.000 43.15102 ?  51  ASN B CB  1 
ATOM   2192 C CG  . ASN B 1 71  ? -45.32800 9.26300   21.77900 1.000 45.65109 ?  51  ASN B CG  1 
ATOM   2193 O OD1 . ASN B 1 71  ? -46.52900 9.06100   21.95700 1.000 48.02605 ?  51  ASN B OD1 1 
ATOM   2194 N ND2 . ASN B 1 71  ? -44.87100 10.07500  20.83200 1.000 41.14675 ?  51  ASN B ND2 1 
ATOM   2195 N N   . ARG B 1 72  ? -42.56600 7.99300   25.14100 1.000 38.12542 ?  52  ARG B N   1 
ATOM   2196 C CA  . ARG B 1 72  ? -41.52600 7.14200   25.70600 1.000 32.57819 ?  52  ARG B CA  1 
ATOM   2197 C C   . ARG B 1 72  ? -40.79800 7.86600   26.82700 1.000 30.98221 ?  52  ARG B C   1 
ATOM   2198 O O   . ARG B 1 72  ? -40.34400 8.99900   26.64900 1.000 33.13181 ?  52  ARG B O   1 
ATOM   2199 C CB  . ARG B 1 72  ? -40.51800 6.71200   24.63400 1.000 33.82304 ?  52  ARG B CB  1 
ATOM   2200 C CG  . ARG B 1 72  ? -41.11100 5.83200   23.55500 1.000 31.21729 ?  52  ARG B CG  1 
ATOM   2201 C CD  . ARG B 1 72  ? -40.13100 5.58200   22.42300 1.000 40.32335 ?  52  ARG B CD  1 
ATOM   2202 N NE  . ARG B 1 72  ? -38.78600 5.25400   22.88400 1.000 39.34315 ?  52  ARG B NE  1 
ATOM   2203 C CZ  . ARG B 1 72  ? -38.39400 4.03500   23.22900 1.000 35.26667 ?  52  ARG B CZ  1 
ATOM   2204 N NH1 . ARG B 1 72  ? -39.24500 3.02200   23.27100 1.000 30.96868 ?  52  ARG B NH1 1 
ATOM   2205 N NH2 . ARG B 1 72  ? -37.11800 3.82800   23.54200 1.000 39.81420 ?  52  ARG B NH2 1 
ATOM   2206 N N   . ALA B 1 73  ? -40.66500 7.19700   27.96800 1.000 35.02176 ?  53  ALA B N   1 
ATOM   2207 C CA  . ALA B 1 73  ? -39.91900 7.71300   29.10400 1.000 34.17830 ?  53  ALA B CA  1 
ATOM   2208 C C   . ALA B 1 73  ? -38.89400 6.68300   29.55600 1.000 33.30096 ?  53  ALA B C   1 
ATOM   2209 O O   . ALA B 1 73  ? -39.15200 5.47700   29.52300 1.000 30.40651 ?  53  ALA B O   1 
ATOM   2210 C CB  . ALA B 1 73  ? -40.84700 8.06600   30.26900 1.000 31.11384 ?  53  ALA B CB  1 
ATOM   2211 N N   . LEU B 1 74  ? -37.73100 7.16300   29.97600 1.000 33.13614 ?  54  LEU B N   1 
ATOM   2212 C CA  . LEU B 1 74  ? -36.68500 6.32300   30.53900 1.000 30.48273 ?  54  LEU B CA  1 
ATOM   2213 C C   . LEU B 1 74  ? -36.49700 6.68200   32.00700 1.000 31.25723 ?  54  LEU B C   1 
ATOM   2214 O O   . LEU B 1 74  ? -36.30300 7.85500   32.34500 1.000 31.06222 ?  54  LEU B O   1 
ATOM   2215 C CB  . LEU B 1 74  ? -35.37100 6.49300   29.77200 1.000 32.23831 ?  54  LEU B CB  1 
ATOM   2216 C CG  . LEU B 1 74  ? -34.17400 5.69900   30.30600 1.000 34.74991 ?  54  LEU B CG  1 
ATOM   2217 C CD1 . LEU B 1 74  ? -34.47100 4.20900   30.30400 1.000 32.19018 ?  54  LEU B CD1 1 
ATOM   2218 C CD2 . LEU B 1 74  ? -32.92800 6.00400   29.48900 1.000 25.82620 ?  54  LEU B CD2 1 
ATOM   2219 N N   . ASP B 1 75  ? -36.56700 5.67300   32.86900 1.000 34.47906 ?  55  ASP B N   1 
ATOM   2220 C CA  . ASP B 1 75  ? -36.40600 5.82400   34.31400 1.000 35.79278 ?  55  ASP B CA  1 
ATOM   2221 C C   . ASP B 1 75  ? -35.09000 5.15300   34.69000 1.000 34.39917 ?  55  ASP B C   1 
ATOM   2222 O O   . ASP B 1 75  ? -35.03300 3.93100   34.84900 1.000 37.90262 ?  55  ASP B O   1 
ATOM   2223 C CB  . ASP B 1 75  ? -37.59700 5.21000   35.05300 1.000 33.79255 ?  55  ASP B CB  1 
ATOM   2224 C CG  . ASP B 1 75  ? -37.49300 5.34500   36.56400 1.000 38.82639 ?  55  ASP B CG  1 
ATOM   2225 O OD1 . ASP B 1 75  ? -36.76800 6.24200   37.05000 1.000 43.01383 ?  55  ASP B OD1 1 
ATOM   2226 O OD2 . ASP B 1 75  ? -38.14900 4.54600   37.27100 1.000 43.48922 -1 55  ASP B OD2 1 
ATOM   2227 N N   . LEU B 1 76  ? -34.03000 5.95200   34.81300 1.000 34.47489 ?  56  LEU B N   1 
ATOM   2228 C CA  . LEU B 1 76  ? -32.70400 5.42400   35.10600 1.000 36.97816 ?  56  LEU B CA  1 
ATOM   2229 C C   . LEU B 1 76  ? -32.51100 5.28800   36.60900 1.000 33.46795 ?  56  LEU B C   1 
ATOM   2230 O O   . LEU B 1 76  ? -32.71300 6.24800   37.35900 1.000 36.34263 ?  56  LEU B O   1 
ATOM   2231 C CB  . LEU B 1 76  ? -31.62400 6.32900   34.51700 1.000 34.75897 ?  56  LEU B CB  1 
ATOM   2232 C CG  . LEU B 1 76  ? -31.32700 6.11500   33.04200 1.000 36.18107 ?  56  LEU B CG  1 
ATOM   2233 C CD1 . LEU B 1 76  ? -30.38700 7.18900   32.54700 1.000 37.07059 ?  56  LEU B CD1 1 
ATOM   2234 C CD2 . LEU B 1 76  ? -30.73000 4.73500   32.82600 1.000 35.01476 ?  56  LEU B CD2 1 
ATOM   2235 N N   . GLY B 1 77  ? -32.09500 4.10000   37.04200 1.000 35.28959 ?  57  GLY B N   1 
ATOM   2236 C CA  . GLY B 1 77  ? -32.04100 3.80200   38.45800 1.000 36.31340 ?  57  GLY B CA  1 
ATOM   2237 C C   . GLY B 1 77  ? -33.44100 3.64200   39.01300 1.000 36.06888 ?  57  GLY B C   1 
ATOM   2238 O O   . GLY B 1 77  ? -33.80100 4.26300   40.01900 1.000 32.38132 ?  57  GLY B O   1 
ATOM   2239 N N   . CYS B 1 78  ? -34.24700 2.81400   38.34000 1.000 35.60097 ?  58  CYS B N   1 
ATOM   2240 C CA  . CYS B 1 78  ? -35.64200 2.60700   38.70900 1.000 30.63245 ?  58  CYS B CA  1 
ATOM   2241 C C   . CYS B 1 78  ? -35.80400 1.82500   40.00000 1.000 31.45589 ?  58  CYS B C   1 
ATOM   2242 O O   . CYS B 1 78  ? -36.90700 1.82300   40.56100 1.000 34.44966 ?  58  CYS B O   1 
ATOM   2243 C CB  . CYS B 1 78  ? -36.36800 1.87300   37.58200 1.000 35.60445 ?  58  CYS B CB  1 
ATOM   2244 S SG  . CYS B 1 78  ? -35.67900 0.22400   37.25400 1.000 37.52767 ?  58  CYS B SG  1 
ATOM   2245 N N   . ALA B 1 79  ? -34.74700 1.15600   40.47100 1.000 31.23136 ?  59  ALA B N   1 
ATOM   2246 C CA  . ALA B 1 79  ? -34.80400 0.34500   41.68100 1.000 31.15129 ?  59  ALA B CA  1 
ATOM   2247 C C   . ALA B 1 79  ? -35.96600 -0.63900  41.60900 1.000 29.53863 ?  59  ALA B C   1 
ATOM   2248 O O   . ALA B 1 79  ? -36.03300 -1.45000  40.68000 1.000 32.47616 ?  59  ALA B O   1 
ATOM   2249 C CB  . ALA B 1 79  ? -34.90800 1.23300   42.92600 1.000 31.99706 ?  59  ALA B CB  1 
ATOM   2250 N N   . THR B 1 80  ? -36.89600 -0.56700  42.55900 1.000 27.69671 ?  60  THR B N   1 
ATOM   2251 C CA  . THR B 1 80  ? -38.01200 -1.50600  42.60000 1.000 30.65057 ?  60  THR B CA  1 
ATOM   2252 C C   . THR B 1 80  ? -39.22800 -1.03800  41.79800 1.000 35.51095 ?  60  THR B C   1 
ATOM   2253 O O   . THR B 1 80  ? -40.31000 -1.61900  41.94600 1.000 34.19326 ?  60  THR B O   1 
ATOM   2254 C CB  . THR B 1 80  ? -38.41100 -1.78900  44.04900 1.000 31.99775 ?  60  THR B CB  1 
ATOM   2255 O OG1 . THR B 1 80  ? -38.47600 -0.56000  44.78500 1.000 31.23095 ?  60  THR B OG1 1 
ATOM   2256 C CG2 . THR B 1 80  ? -37.39400 -2.72400  44.70000 1.000 30.30432 ?  60  THR B CG2 1 
ATOM   2257 N N   . GLY B 1 81  ? -39.08400 0.00700   40.97900 1.000 35.23952 ?  61  GLY B N   1 
ATOM   2258 C CA  . GLY B 1 81  ? -39.99300 0.25300   39.87600 1.000 32.97598 ?  61  GLY B CA  1 
ATOM   2259 C C   . GLY B 1 81  ? -41.11400 1.24700   40.09900 1.000 34.94372 ?  61  GLY B C   1 
ATOM   2260 O O   . GLY B 1 81  ? -41.87800 1.49800   39.15800 1.000 37.16597 ?  61  GLY B O   1 
ATOM   2261 N N   . ARG B 1 82  ? -41.23500 1.83300   41.29400 1.000 34.87690 ?  62  ARG B N   1 
ATOM   2262 C CA  . ARG B 1 82  ? -42.39400 2.67600   41.58600 1.000 34.88498 ?  62  ARG B CA  1 
ATOM   2263 C C   . ARG B 1 82  ? -42.48400 3.86100   40.62700 1.000 35.50688 ?  62  ARG B C   1 
ATOM   2264 O O   . ARG B 1 82  ? -43.55600 4.14700   40.08400 1.000 36.27026 ?  62  ARG B O   1 
ATOM   2265 C CB  . ARG B 1 82  ? -42.35600 3.15700   43.03800 1.000 34.23370 ?  62  ARG B CB  1 
ATOM   2266 C CG  . ARG B 1 82  ? -43.52500 4.07600   43.41100 1.000 36.70085 ?  62  ARG B CG  1 
ATOM   2267 C CD  . ARG B 1 82  ? -44.85000 3.32900   43.50700 1.000 34.91805 ?  62  ARG B CD  1 
ATOM   2268 N NE  . ARG B 1 82  ? -45.98200 4.22200   43.74300 1.000 38.59980 ?  62  ARG B NE  1 
ATOM   2269 C CZ  . ARG B 1 82  ? -46.40300 4.61000   44.94000 1.000 39.57518 ?  62  ARG B CZ  1 
ATOM   2270 N NH1 . ARG B 1 82  ? -45.76600 4.25900   46.04600 1.000 34.44276 ?  62  ARG B NH1 1 
ATOM   2271 N NH2 . ARG B 1 82  ? -47.49500 5.36800   45.03000 1.000 35.84719 ?  62  ARG B NH2 1 
ATOM   2272 N N   . ALA B 1 83  ? -41.36900 4.56300   40.40100 1.000 27.63453 ?  63  ALA B N   1 
ATOM   2273 C CA  . ALA B 1 83  ? -41.42600 5.73800   39.53600 1.000 37.52575 ?  63  ALA B CA  1 
ATOM   2274 C C   . ALA B 1 83  ? -41.75100 5.36500   38.09300 1.000 39.61816 ?  63  ALA B C   1 
ATOM   2275 O O   . ALA B 1 83  ? -42.41600 6.13700   37.39100 1.000 32.37969 ?  63  ALA B O   1 
ATOM   2276 C CB  . ALA B 1 83  ? -40.11300 6.51700   39.60500 1.000 31.56677 ?  63  ALA B CB  1 
ATOM   2277 N N   . SER B 1 84  ? -41.29800 4.19200   37.63200 1.000 33.17598 ?  64  SER B N   1 
ATOM   2278 C CA  . SER B 1 84  ? -41.65000 3.73400   36.29100 1.000 33.80586 ?  64  SER B CA  1 
ATOM   2279 C C   . SER B 1 84  ? -43.14600 3.47600   36.17800 1.000 33.52543 ?  64  SER B C   1 
ATOM   2280 O O   . SER B 1 84  ? -43.78700 3.89100   35.20500 1.000 33.13732 ?  64  SER B O   1 
ATOM   2281 C CB  . SER B 1 84  ? -40.86900 2.46600   35.93600 1.000 33.36734 ?  64  SER B CB  1 
ATOM   2282 O OG  . SER B 1 84  ? -39.47300 2.68100   35.97000 1.000 35.35779 ?  64  SER B OG  1 
ATOM   2283 N N   . PHE B 1 85  ? -43.71400 2.76700   37.15800 1.000 29.95254 ?  65  PHE B N   1 
ATOM   2284 C CA  . PHE B 1 85  ? -45.15200 2.51800   37.15600 1.000 32.59918 ?  65  PHE B CA  1 
ATOM   2285 C C   . PHE B 1 85  ? -45.93200 3.82400   37.16800 1.000 36.08433 ?  65  PHE B C   1 
ATOM   2286 O O   . PHE B 1 85  ? -46.93200 3.96800   36.45200 1.000 37.90704 ?  65  PHE B O   1 
ATOM   2287 C CB  . PHE B 1 85  ? -45.54000 1.65900   38.36100 1.000 26.18995 ?  65  PHE B CB  1 
ATOM   2288 C CG  . PHE B 1 85  ? -45.10300 0.22500   38.25300 1.000 31.90102 ?  65  PHE B CG  1 
ATOM   2289 C CD1 . PHE B 1 85  ? -45.32000 -0.49500  37.09000 1.000 34.20476 ?  65  PHE B CD1 1 
ATOM   2290 C CD2 . PHE B 1 85  ? -44.48700 -0.40800  39.32000 1.000 32.86706 ?  65  PHE B CD2 1 
ATOM   2291 C CE1 . PHE B 1 85  ? -44.92400 -1.81500  36.99300 1.000 36.47250 ?  65  PHE B CE1 1 
ATOM   2292 C CE2 . PHE B 1 85  ? -44.08700 -1.72700  39.22900 1.000 36.68136 ?  65  PHE B CE2 1 
ATOM   2293 C CZ  . PHE B 1 85  ? -44.30700 -2.43200  38.06500 1.000 34.31297 ?  65  PHE B CZ  1 
ATOM   2294 N N   . GLU B 1 86  ? -45.48200 4.79400   37.96700 1.000 33.45240 ?  66  GLU B N   1 
ATOM   2295 C CA  . GLU B 1 86  ? -46.20100 6.06000   38.06000 1.000 37.51008 ?  66  GLU B CA  1 
ATOM   2296 C C   . GLU B 1 86  ? -46.08200 6.86000   36.77200 1.000 36.59454 ?  66  GLU B C   1 
ATOM   2297 O O   . GLU B 1 86  ? -47.04200 7.52300   36.35800 1.000 36.64865 ?  66  GLU B O   1 
ATOM   2298 C CB  . GLU B 1 86  ? -45.69000 6.87600   39.24800 1.000 35.25741 ?  66  GLU B CB  1 
ATOM   2299 C CG  . GLU B 1 86  ? -45.92700 6.21300   40.59800 1.000 36.78349 ?  66  GLU B CG  1 
ATOM   2300 C CD  . GLU B 1 86  ? -47.38900 6.21400   41.01900 1.000 41.14940 ?  66  GLU B CD  1 
ATOM   2301 O OE1 . GLU B 1 86  ? -48.22900 6.79600   40.29700 1.000 38.53809 ?  66  GLU B OE1 1 
ATOM   2302 O OE2 . GLU B 1 86  ? -47.69800 5.62400   42.07600 1.000 41.98398 -1 66  GLU B OE2 1 
ATOM   2303 N N   . LEU B 1 87  ? -44.91200 6.81900   36.12600 1.000 32.59610 ?  67  LEU B N   1 
ATOM   2304 C CA  . LEU B 1 87  ? -44.75700 7.51900   34.85500 1.000 40.74853 ?  67  LEU B CA  1 
ATOM   2305 C C   . LEU B 1 87  ? -45.62200 6.89100   33.77000 1.000 38.51733 ?  67  LEU B C   1 
ATOM   2306 O O   . LEU B 1 87  ? -46.07700 7.58900   32.85700 1.000 43.65222 ?  67  LEU B O   1 
ATOM   2307 C CB  . LEU B 1 87  ? -43.29000 7.52200   34.43000 1.000 31.31256 ?  67  LEU B CB  1 
ATOM   2308 C CG  . LEU B 1 87  ? -42.36000 8.53100   35.10800 1.000 37.14508 ?  67  LEU B CG  1 
ATOM   2309 C CD1 . LEU B 1 87  ? -40.92800 8.32700   34.63500 1.000 36.14617 ?  67  LEU B CD1 1 
ATOM   2310 C CD2 . LEU B 1 87  ? -42.80900 9.96100   34.85500 1.000 30.09943 ?  67  LEU B CD2 1 
ATOM   2311 N N   . ALA B 1 88  ? -45.86500 5.58300   33.86500 1.000 36.93222 ?  68  ALA B N   1 
ATOM   2312 C CA  . ALA B 1 88  ? -46.67300 4.85900   32.89400 1.000 40.29169 ?  68  ALA B CA  1 
ATOM   2313 C C   . ALA B 1 88  ? -48.13700 5.27100   32.91800 1.000 43.04108 ?  68  ALA B C   1 
ATOM   2314 O O   . ALA B 1 88  ? -48.87800 4.90800   32.00000 1.000 45.49934 ?  68  ALA B O   1 
ATOM   2315 C CB  . ALA B 1 88  ? -46.55800 3.35700   33.14300 1.000 38.61988 ?  68  ALA B CB  1 
ATOM   2316 N N   . ARG B 1 89  ? -48.57000 6.00900   33.94100 1.000 44.65962 ?  69  ARG B N   1 
ATOM   2317 C CA  . ARG B 1 89  ? -49.92500 6.54100   33.95400 1.000 42.62114 ?  69  ARG B CA  1 
ATOM   2318 C C   . ARG B 1 89  ? -50.09800 7.68900   32.97200 1.000 45.41115 ?  69  ARG B C   1 
ATOM   2319 O O   . ARG B 1 89  ? -51.23200 7.99500   32.59300 1.000 45.90366 ?  69  ARG B O   1 
ATOM   2320 C CB  . ARG B 1 89  ? -50.29900 7.00500   35.36200 1.000 37.16607 ?  69  ARG B CB  1 
ATOM   2321 C CG  . ARG B 1 89  ? -50.07000 5.96000   36.43600 1.000 41.43307 ?  69  ARG B CG  1 
ATOM   2322 C CD  . ARG B 1 89  ? -50.86000 6.28900   37.69500 1.000 42.73494 ?  69  ARG B CD  1 
ATOM   2323 N NE  . ARG B 1 89  ? -52.28700 6.04900   37.51300 1.000 46.10685 ?  69  ARG B NE  1 
ATOM   2324 C CZ  . ARG B 1 89  ? -53.24300 6.61900   38.23200 1.000 42.08144 ?  69  ARG B CZ  1 
ATOM   2325 N NH1 . ARG B 1 89  ? -52.96300 7.47900   39.19600 1.000 42.27520 ?  69  ARG B NH1 1 
ATOM   2326 N NH2 . ARG B 1 89  ? -54.51200 6.31100   37.98300 1.000 47.68258 ?  69  ARG B NH2 1 
ATOM   2327 N N   . SER B 1 90  ? -49.00500 8.33500   32.56000 1.000 41.15138 ?  70  SER B N   1 
ATOM   2328 C CA  . SER B 1 90  ? -49.06200 9.41100   31.57900 1.000 39.88249 ?  70  SER B CA  1 
ATOM   2329 C C   . SER B 1 90  ? -48.36100 9.07800   30.27500 1.000 46.47313 ?  70  SER B C   1 
ATOM   2330 O O   . SER B 1 90  ? -48.80200 9.54000   29.22100 1.000 49.68229 ?  70  SER B O   1 
ATOM   2331 C CB  . SER B 1 90  ? -48.45200 10.70100  32.14600 1.000 31.21261 ?  70  SER B CB  1 
ATOM   2332 N N   . TYR B 1 91  ? -47.29900 8.28200   30.31500 1.000 39.84071 ?  71  TYR B N   1 
ATOM   2333 C CA  . TYR B 1 91  ? -46.54800 7.95200   29.11600 1.000 33.44643 ?  71  TYR B CA  1 
ATOM   2334 C C   . TYR B 1 91  ? -47.06800 6.65800   28.50400 1.000 38.86214 ?  71  TYR B C   1 
ATOM   2335 O O   . TYR B 1 91  ? -47.61500 5.79500   29.19700 1.000 40.55372 ?  71  TYR B O   1 
ATOM   2336 C CB  . TYR B 1 91  ? -45.05500 7.83600   29.43500 1.000 40.03607 ?  71  TYR B CB  1 
ATOM   2337 C CG  . TYR B 1 91  ? -44.38200 9.18600   29.57400 1.000 36.89043 ?  71  TYR B CG  1 
ATOM   2338 C CD1 . TYR B 1 91  ? -44.57400 9.96600   30.70700 1.000 35.30729 ?  71  TYR B CD1 1 
ATOM   2339 C CD2 . TYR B 1 91  ? -43.57300 9.68800   28.56200 1.000 37.76389 ?  71  TYR B CD2 1 
ATOM   2340 C CE1 . TYR B 1 91  ? -43.97600 11.20600  30.83200 1.000 36.42968 ?  71  TYR B CE1 1 
ATOM   2341 C CE2 . TYR B 1 91  ? -42.97200 10.92400  28.67700 1.000 39.26193 ?  71  TYR B CE2 1 
ATOM   2342 C CZ  . TYR B 1 91  ? -43.17500 11.67900  29.81400 1.000 34.92094 ?  71  TYR B CZ  1 
ATOM   2343 O OH  . TYR B 1 91  ? -42.57600 12.91100  29.93300 1.000 41.93335 ?  71  TYR B OH  1 
ATOM   2344 N N   . LYS B 1 92  ? -46.91000 6.54200   27.18200 1.000 37.64687 ?  72  LYS B N   1 
ATOM   2345 C CA  . LYS B 1 92  ? -47.34500 5.33600   26.48700 1.000 42.94096 ?  72  LYS B CA  1 
ATOM   2346 C C   . LYS B 1 92  ? -46.41200 4.16100   26.74500 1.000 40.81885 ?  72  LYS B C   1 
ATOM   2347 O O   . LYS B 1 92  ? -46.87300 3.01800   26.82500 1.000 42.62367 ?  72  LYS B O   1 
ATOM   2348 C CB  . LYS B 1 92  ? -47.45800 5.60000   24.98200 1.000 38.54683 ?  72  LYS B CB  1 
ATOM   2349 C CG  . LYS B 1 92  ? -48.39000 6.74500   24.61600 1.000 40.60655 ?  72  LYS B CG  1 
ATOM   2350 N N   . HIS B 1 93  ? -45.11200 4.41600   26.87400 1.000 39.81418 ?  73  HIS B N   1 
ATOM   2351 C CA  . HIS B 1 93  ? -44.14800 3.37200   27.17900 1.000 36.94500 ?  73  HIS B CA  1 
ATOM   2352 C C   . HIS B 1 93  ? -43.09800 3.91800   28.13200 1.000 37.27730 ?  73  HIS B C   1 
ATOM   2353 O O   . HIS B 1 93  ? -42.59300 5.02700   27.93700 1.000 37.34566 ?  73  HIS B O   1 
ATOM   2354 C CB  . HIS B 1 93  ? -43.47600 2.84100   25.91300 1.000 33.53018 ?  73  HIS B CB  1 
ATOM   2355 C CG  . HIS B 1 93  ? -42.50800 1.73100   26.17800 1.000 39.72579 ?  73  HIS B CG  1 
ATOM   2356 N ND1 . HIS B 1 93  ? -42.87100 0.56500   26.81600 1.000 39.94549 ?  73  HIS B ND1 1 
ATOM   2357 C CD2 . HIS B 1 93  ? -41.18600 1.61500   25.90900 1.000 42.04857 ?  73  HIS B CD2 1 
ATOM   2358 C CE1 . HIS B 1 93  ? -41.81800 -0.22500  26.92300 1.000 45.23159 ?  73  HIS B CE1 1 
ATOM   2359 N NE2 . HIS B 1 93  ? -40.78200 0.38900   26.38100 1.000 46.83083 ?  73  HIS B NE2 1 
ATOM   2360 N N   . VAL B 1 94  ? -42.76300 3.13700   29.15400 1.000 37.82564 ?  74  VAL B N   1 
ATOM   2361 C CA  . VAL B 1 94  ? -41.73600 3.50700   30.11800 1.000 38.01593 ?  74  VAL B CA  1 
ATOM   2362 C C   . VAL B 1 94  ? -40.72700 2.37300   30.20600 1.000 34.39891 ?  74  VAL B C   1 
ATOM   2363 O O   . VAL B 1 94  ? -41.10400 1.21100   30.39200 1.000 35.68480 ?  74  VAL B O   1 
ATOM   2364 C CB  . VAL B 1 94  ? -42.32500 3.81600   31.50700 1.000 31.92219 ?  74  VAL B CB  1 
ATOM   2365 C CG1 . VAL B 1 94  ? -41.20500 4.06500   32.49500 1.000 31.93829 ?  74  VAL B CG1 1 
ATOM   2366 C CG2 . VAL B 1 94  ? -43.23500 5.02700   31.42900 1.000 31.28453 ?  74  VAL B CG2 1 
ATOM   2367 N N   . ASP B 1 95  ? -39.45000 2.71100   30.06800 1.000 33.94491 ?  75  ASP B N   1 
ATOM   2368 C CA  . ASP B 1 95  ? -38.36200 1.76700   30.27200 1.000 37.07757 ?  75  ASP B CA  1 
ATOM   2369 C C   . ASP B 1 95  ? -37.72500 2.02300   31.63200 1.000 34.14879 ?  75  ASP B C   1 
ATOM   2370 O O   . ASP B 1 95  ? -37.34400 3.15600   31.94000 1.000 34.49036 ?  75  ASP B O   1 
ATOM   2371 C CB  . ASP B 1 95  ? -37.31300 1.89000   29.16900 1.000 32.99799 ?  75  ASP B CB  1 
ATOM   2372 C CG  . ASP B 1 95  ? -37.77100 1.28400   27.85900 1.000 38.17508 ?  75  ASP B CG  1 
ATOM   2373 O OD1 . ASP B 1 95  ? -38.42500 0.21700   27.88500 1.000 40.94546 ?  75  ASP B OD1 1 
ATOM   2374 O OD2 . ASP B 1 95  ? -37.45300 1.86500   26.80100 1.000 38.78744 -1 75  ASP B OD2 1 
ATOM   2375 N N   . GLY B 1 96  ? -37.62200 0.97400   32.44300 1.000 32.97845 ?  76  GLY B N   1 
ATOM   2376 C CA  . GLY B 1 96  ? -36.96700 1.08200   33.73200 1.000 33.65677 ?  76  GLY B CA  1 
ATOM   2377 C C   . GLY B 1 96  ? -35.65100 0.33400   33.74100 1.000 38.97494 ?  76  GLY B C   1 
ATOM   2378 O O   . GLY B 1 96  ? -35.62800 -0.87300  33.49600 1.000 36.04762 ?  76  GLY B O   1 
ATOM   2379 N N   . VAL B 1 97  ? -34.54900 1.02800   34.01600 1.000 36.36792 ?  77  VAL B N   1 
ATOM   2380 C CA  . VAL B 1 97  ? -33.21600 0.44300   33.94500 1.000 39.10080 ?  77  VAL B CA  1 
ATOM   2381 C C   . VAL B 1 97  ? -32.53600 0.60200   35.29800 1.000 37.77769 ?  77  VAL B C   1 
ATOM   2382 O O   . VAL B 1 97  ? -32.56800 1.68700   35.89300 1.000 34.81199 ?  77  VAL B O   1 
ATOM   2383 C CB  . VAL B 1 97  ? -32.37600 1.09300   32.83000 1.000 33.31637 ?  77  VAL B CB  1 
ATOM   2384 C CG1 . VAL B 1 97  ? -30.97200 0.53400   32.83500 1.000 35.07049 ?  77  VAL B CG1 1 
ATOM   2385 C CG2 . VAL B 1 97  ? -33.03500 0.88400   31.47600 1.000 34.90739 ?  77  VAL B CG2 1 
ATOM   2386 N N   . ASP B 1 98  ? -31.92200 -0.47700  35.78100 1.000 32.82491 ?  78  ASP B N   1 
ATOM   2387 C CA  . ASP B 1 98  ? -31.14500 -0.43500  37.01000 1.000 38.08124 ?  78  ASP B CA  1 
ATOM   2388 C C   . ASP B 1 98  ? -29.90300 -1.30400  36.86800 1.000 35.96612 ?  78  ASP B C   1 
ATOM   2389 O O   . ASP B 1 98  ? -29.90700 -2.31600  36.16300 1.000 35.92000 ?  78  ASP B O   1 
ATOM   2390 C CB  . ASP B 1 98  ? -31.95600 -0.89900  38.22700 1.000 34.32716 ?  78  ASP B CB  1 
ATOM   2391 C CG  . ASP B 1 98  ? -31.37200 -0.39300  39.53800 1.000 41.59607 ?  78  ASP B CG  1 
ATOM   2392 O OD1 . ASP B 1 98  ? -30.50600 -1.08400  40.11400 1.000 34.66574 ?  78  ASP B OD1 1 
ATOM   2393 O OD2 . ASP B 1 98  ? -31.77200 0.70300   39.98900 1.000 45.17237 -1 78  ASP B OD2 1 
ATOM   2394 N N   . TYR B 1 99  ? -28.83800 -0.89900  37.56400 1.000 35.73498 ?  79  TYR B N   1 
ATOM   2395 C CA  . TYR B 1 99  ? -27.59800 -1.66100  37.53000 1.000 33.11493 ?  79  TYR B CA  1 
ATOM   2396 C C   . TYR B 1 99  ? -27.74500 -3.00400  38.23000 1.000 37.84281 ?  79  TYR B C   1 
ATOM   2397 O O   . TYR B 1 99  ? -27.11500 -3.98500  37.82100 1.000 35.61180 ?  79  TYR B O   1 
ATOM   2398 C CB  . TYR B 1 99  ? -26.47000 -0.84900  38.16700 1.000 32.46129 ?  79  TYR B CB  1 
ATOM   2399 C CG  . TYR B 1 99  ? -25.18700 -1.62500  38.36300 1.000 37.92818 ?  79  TYR B CG  1 
ATOM   2400 C CD1 . TYR B 1 99  ? -24.33400 -1.88000  37.29000 1.000 39.68969 ?  79  TYR B CD1 1 
ATOM   2401 C CD2 . TYR B 1 99  ? -24.82600 -2.10900  39.61700 1.000 40.99866 ?  79  TYR B CD2 1 
ATOM   2402 C CE1 . TYR B 1 99  ? -23.15900 -2.58900  37.46300 1.000 34.78140 ?  79  TYR B CE1 1 
ATOM   2403 C CE2 . TYR B 1 99  ? -23.64900 -2.82000  39.79700 1.000 41.84722 ?  79  TYR B CE2 1 
ATOM   2404 C CZ  . TYR B 1 99  ? -22.82100 -3.05600  38.71800 1.000 38.77458 ?  79  TYR B CZ  1 
ATOM   2405 O OH  . TYR B 1 99  ? -21.65400 -3.76600  38.89700 1.000 43.75441 ?  79  TYR B OH  1 
ATOM   2406 N N   . SER B 1 100 ? -28.56500 -3.07700  39.27400 1.000 35.81994 ?  80  SER B N   1 
ATOM   2407 C CA  . SER B 1 100 ? -28.68300 -4.29100  40.07100 1.000 39.02793 ?  80  SER B CA  1 
ATOM   2408 C C   . SER B 1 100 ? -29.78500 -5.17500  39.50100 1.000 38.81333 ?  80  SER B C   1 
ATOM   2409 O O   . SER B 1 100 ? -30.94700 -4.75800  39.42100 1.000 41.97275 ?  80  SER B O   1 
ATOM   2410 C CB  . SER B 1 100 ? -28.96300 -3.95400  41.53400 1.000 33.44023 ?  80  SER B CB  1 
ATOM   2411 N N   . GLN B 1 101 ? -29.41500 -6.39900  39.11000 1.000 42.69955 ?  81  GLN B N   1 
ATOM   2412 C CA  . GLN B 1 101 ? -30.40000 -7.36100  38.62900 1.000 37.62681 ?  81  GLN B CA  1 
ATOM   2413 C C   . GLN B 1 101 ? -31.44900 -7.66700  39.68900 1.000 32.97441 ?  81  GLN B C   1 
ATOM   2414 O O   . GLN B 1 101 ? -32.60800 -7.93000  39.35400 1.000 38.33899 ?  81  GLN B O   1 
ATOM   2415 C CB  . GLN B 1 101 ? -29.69800 -8.64700  38.19100 1.000 41.04486 ?  81  GLN B CB  1 
ATOM   2416 C CG  . GLN B 1 101 ? -30.61400 -9.67400  37.54500 1.000 38.97925 ?  81  GLN B CG  1 
ATOM   2417 C CD  . GLN B 1 101 ? -31.09600 -9.23700  36.17900 1.000 47.85260 ?  81  GLN B CD  1 
ATOM   2418 O OE1 . GLN B 1 101 ? -30.29300 -9.01300  35.26900 1.000 50.52924 ?  81  GLN B OE1 1 
ATOM   2419 N NE2 . GLN B 1 101 ? -32.41200 -9.11600  36.02300 1.000 44.93985 ?  81  GLN B NE2 1 
ATOM   2420 N N   . ALA B 1 102 ? -31.06200 -7.63300  40.96700 1.000 35.30427 ?  82  ALA B N   1 
ATOM   2421 C CA  . ALA B 1 102 ? -31.99200 -7.97800  42.03800 1.000 37.82188 ?  82  ALA B CA  1 
ATOM   2422 C C   . ALA B 1 102 ? -33.14700 -6.98800  42.10800 1.000 37.17586 ?  82  ALA B C   1 
ATOM   2423 O O   . ALA B 1 102 ? -34.29900 -7.37900  42.33500 1.000 36.71344 ?  82  ALA B O   1 
ATOM   2424 C CB  . ALA B 1 102 ? -31.24900 -8.03100  43.37000 1.000 37.47636 ?  82  ALA B CB  1 
ATOM   2425 N N   . PHE B 1 103 ? -32.85800 -5.69900  41.91600 1.000 38.28493 ?  83  PHE B N   1 
ATOM   2426 C CA  . PHE B 1 103 ? -33.92100 -4.70200  41.87500 1.000 37.55620 ?  83  PHE B CA  1 
ATOM   2427 C C   . PHE B 1 103 ? -34.79600 -4.88200  40.64200 1.000 33.42245 ?  83  PHE B C   1 
ATOM   2428 O O   . PHE B 1 103 ? -36.02100 -4.74100  40.71900 1.000 35.04945 ?  83  PHE B O   1 
ATOM   2429 C CB  . PHE B 1 103 ? -33.31900 -3.30000  41.91700 1.000 35.49089 ?  83  PHE B CB  1 
ATOM   2430 C CG  . PHE B 1 103 ? -32.77700 -2.92800  43.25900 1.000 40.21751 ?  83  PHE B CG  1 
ATOM   2431 C CD1 . PHE B 1 103 ? -31.46900 -3.22400  43.59800 1.000 49.85681 ?  83  PHE B CD1 1 
ATOM   2432 C CD2 . PHE B 1 103 ? -33.57900 -2.30800  44.19200 1.000 39.86174 ?  83  PHE B CD2 1 
ATOM   2433 C CE1 . PHE B 1 103 ? -30.96700 -2.89500  44.83700 1.000 50.79917 ?  83  PHE B CE1 1 
ATOM   2434 C CE2 . PHE B 1 103 ? -33.08600 -1.97900  45.43400 1.000 46.09116 ?  83  PHE B CE2 1 
ATOM   2435 C CZ  . PHE B 1 103 ? -31.77800 -2.27100  45.75700 1.000 48.33764 ?  83  PHE B CZ  1 
ATOM   2436 N N   . VAL B 1 104 ? -34.18400 -5.19700  39.49900 1.000 34.21494 ?  84  VAL B N   1 
ATOM   2437 C CA  . VAL B 1 104 ? -34.94900 -5.44600  38.27900 1.000 34.64566 ?  84  VAL B CA  1 
ATOM   2438 C C   . VAL B 1 104 ? -35.92400 -6.59800  38.48900 1.000 40.58039 ?  84  VAL B C   1 
ATOM   2439 O O   . VAL B 1 104 ? -37.09700 -6.52300  38.10200 1.000 38.08201 ?  84  VAL B O   1 
ATOM   2440 C CB  . VAL B 1 104 ? -33.99800 -5.72800  37.10300 1.000 40.51396 ?  84  VAL B CB  1 
ATOM   2441 C CG1 . VAL B 1 104 ? -34.78100 -6.20600  35.89000 1.000 40.01752 ?  84  VAL B CG1 1 
ATOM   2442 C CG2 . VAL B 1 104 ? -33.18200 -4.49100  36.76800 1.000 43.67561 ?  84  VAL B CG2 1 
ATOM   2443 N N   . ASP B 1 105 ? -35.44900 -7.68100  39.11000 1.000 42.50855 ?  85  ASP B N   1 
ATOM   2444 C CA  . ASP B 1 105 ? -36.27600 -8.87000  39.28700 1.000 38.16818 ?  85  ASP B CA  1 
ATOM   2445 C C   . ASP B 1 105 ? -37.43500 -8.60400  40.23400 1.000 38.00261 ?  85  ASP B C   1 
ATOM   2446 O O   . ASP B 1 105 ? -38.52500 -9.15800  40.05700 1.000 40.04553 ?  85  ASP B O   1 
ATOM   2447 C CB  . ASP B 1 105 ? -35.42100 -10.02400 39.80100 1.000 36.83498 ?  85  ASP B CB  1 
ATOM   2448 C CG  . ASP B 1 105 ? -34.44900 -10.52600 38.76200 1.000 43.71159 ?  85  ASP B CG  1 
ATOM   2449 O OD1 . ASP B 1 105 ? -34.66000 -10.23600 37.56400 1.000 53.59074 ?  85  ASP B OD1 1 
ATOM   2450 O OD2 . ASP B 1 105 ? -33.47300 -11.21000 39.13700 1.000 46.60024 -1 85  ASP B OD2 1 
ATOM   2451 N N   . ALA B 1 106 ? -37.22100 -7.76600  41.25000 1.000 36.73071 ?  86  ALA B N   1 
ATOM   2452 C CA  . ALA B 1 106 ? -38.31000 -7.43200  42.16300 1.000 36.23022 ?  86  ALA B CA  1 
ATOM   2453 C C   . ALA B 1 106 ? -39.38800 -6.61900  41.45600 1.000 33.42921 ?  86  ALA B C   1 
ATOM   2454 O O   . ALA B 1 106 ? -40.58500 -6.86300  41.64400 1.000 38.43872 ?  86  ALA B O   1 
ATOM   2455 C CB  . ALA B 1 106 ? -37.77300 -6.67600  43.38000 1.000 34.90617 ?  86  ALA B CB  1 
ATOM   2456 N N   . ALA B 1 107 ? -38.98500 -5.65100  40.62800 1.000 37.52004 ?  87  ALA B N   1 
ATOM   2457 C CA  . ALA B 1 107 ? -39.97100 -4.87000  39.88700 1.000 37.96037 ?  87  ALA B CA  1 
ATOM   2458 C C   . ALA B 1 107 ? -40.72000 -5.74100  38.88500 1.000 39.75810 ?  87  ALA B C   1 
ATOM   2459 O O   . ALA B 1 107 ? -41.94200 -5.61800  38.73800 1.000 33.97246 ?  87  ALA B O   1 
ATOM   2460 C CB  . ALA B 1 107 ? -39.29600 -3.69400  39.18300 1.000 31.03306 ?  87  ALA B CB  1 
ATOM   2461 N N   . THR B 1 108 ? -40.00400 -6.63500  38.19400 1.000 37.10511 ?  88  THR B N   1 
ATOM   2462 C CA  . THR B 1 108 ? -40.64600 -7.50800  37.21700 1.000 38.95831 ?  88  THR B CA  1 
ATOM   2463 C C   . THR B 1 108 ? -41.60200 -8.48600  37.88600 1.000 45.05103 ?  88  THR B C   1 
ATOM   2464 O O   . THR B 1 108 ? -42.66300 -8.79500  37.33300 1.000 45.03622 ?  88  THR B O   1 
ATOM   2465 C CB  . THR B 1 108 ? -39.58900 -8.26600  36.41200 1.000 42.14857 ?  88  THR B CB  1 
ATOM   2466 O OG1 . THR B 1 108 ? -38.46700 -7.40800  36.17000 1.000 44.00605 ?  88  THR B OG1 1 
ATOM   2467 C CG2 . THR B 1 108 ? -40.16500 -8.72300  35.08300 1.000 49.98414 ?  88  THR B CG2 1 
ATOM   2468 N N   . GLU B 1 109 ? -41.24000 -8.98500  39.07300 1.000 40.61270 ?  89  GLU B N   1 
ATOM   2469 C CA  . GLU B 1 109 ? -42.12900 -9.88500  39.80100 1.000 42.99612 ?  89  GLU B CA  1 
ATOM   2470 C C   . GLU B 1 109 ? -43.41000 -9.17500  40.21300 1.000 42.59266 ?  89  GLU B C   1 
ATOM   2471 O O   . GLU B 1 109 ? -44.50300 -9.74200  40.10500 1.000 40.95230 ?  89  GLU B O   1 
ATOM   2472 C CB  . GLU B 1 109 ? -41.41600 -10.45000 41.02900 1.000 44.30513 ?  89  GLU B CB  1 
ATOM   2473 C CG  . GLU B 1 109 ? -41.04800 -11.91900 40.91800 1.000 57.53091 ?  89  GLU B CG  1 
ATOM   2474 C CD  . GLU B 1 109 ? -42.25900 -12.83800 40.91800 1.000 61.48859 ?  89  GLU B CD  1 
ATOM   2475 O OE1 . GLU B 1 109 ? -43.21300 -12.58700 41.68700 1.000 61.65228 ?  89  GLU B OE1 1 
ATOM   2476 O OE2 . GLU B 1 109 ? -42.25700 -13.81300 40.13800 1.000 68.98708 -1 89  GLU B OE2 1 
ATOM   2477 N N   . LEU B 1 110 ? -43.29800 -7.93700  40.69800 1.000 41.33995 ?  90  LEU B N   1 
ATOM   2478 C CA  . LEU B 1 110 ? -44.49800 -7.17800  41.02900 1.000 41.92166 ?  90  LEU B CA  1 
ATOM   2479 C C   . LEU B 1 110 ? -45.34600 -6.93000  39.79200 1.000 43.45932 ?  90  LEU B C   1 
ATOM   2480 O O   . LEU B 1 110 ? -46.57800 -6.88700  39.87400 1.000 45.24490 ?  90  LEU B O   1 
ATOM   2481 C CB  . LEU B 1 110 ? -44.11900 -5.85500  41.69300 1.000 35.88009 ?  90  LEU B CB  1 
ATOM   2482 C CG  . LEU B 1 110 ? -45.26800 -5.06100  42.32600 1.000 40.16425 ?  90  LEU B CG  1 
ATOM   2483 C CD1 . LEU B 1 110 ? -45.97800 -5.88200  43.39300 1.000 38.80708 ?  90  LEU B CD1 1 
ATOM   2484 C CD2 . LEU B 1 110 ? -44.75700 -3.75400  42.90500 1.000 38.18975 ?  90  LEU B CD2 1 
ATOM   2485 N N   . GLN B 1 111 ? -44.70400 -6.78500  38.63800 1.000 41.66579 ?  91  GLN B N   1 
ATOM   2486 C CA  . GLN B 1 111 ? -45.42700 -6.56900  37.39500 1.000 47.02287 ?  91  GLN B CA  1 
ATOM   2487 C C   . GLN B 1 111 ? -46.12100 -7.84300  36.91900 1.000 39.89756 ?  91  GLN B C   1 
ATOM   2488 O O   . GLN B 1 111 ? -47.26900 -7.79300  36.46800 1.000 46.70692 ?  91  GLN B O   1 
ATOM   2489 C CB  . GLN B 1 111 ? -44.45500 -6.04400  36.34100 1.000 40.25291 ?  91  GLN B CB  1 
ATOM   2490 C CG  . GLN B 1 111 ? -45.08200 -5.48200  35.09600 1.000 34.80401 ?  91  GLN B CG  1 
ATOM   2491 C CD  . GLN B 1 111 ? -44.02200 -5.09000  34.09500 1.000 42.06730 ?  91  GLN B CD  1 
ATOM   2492 O OE1 . GLN B 1 111 ? -42.92600 -5.65400  34.08900 1.000 42.87581 ?  91  GLN B OE1 1 
ATOM   2493 N NE2 . GLN B 1 111 ? -44.33200 -4.12100  33.24700 1.000 36.90448 ?  91  GLN B NE2 1 
ATOM   2494 N N   . LYS B 1 112 ? -45.45500 -8.99500  37.02400 1.000 44.01768 ?  92  LYS B N   1 
ATOM   2495 C CA  . LYS B 1 112 ? -46.02300 -10.23500 36.49900 1.000 46.21168 ?  92  LYS B CA  1 
ATOM   2496 C C   . LYS B 1 112 ? -47.01400 -10.86500 37.47500 1.000 47.92520 ?  92  LYS B C   1 
ATOM   2497 O O   . LYS B 1 112 ? -48.18000 -11.09200 37.13000 1.000 54.52355 ?  92  LYS B O   1 
ATOM   2498 C CB  . LYS B 1 112 ? -44.90500 -11.22500 36.15900 1.000 44.22353 ?  92  LYS B CB  1 
ATOM   2499 N N   . ASN B 1 113 ? -46.56600 -11.15700 38.69800 1.000 46.33968 ?  93  ASN B N   1 
ATOM   2500 C CA  . ASN B 1 113 ? -47.38400 -11.86600 39.67700 1.000 51.78831 ?  93  ASN B CA  1 
ATOM   2501 C C   . ASN B 1 113 ? -48.25200 -10.95000 40.52900 1.000 41.43407 ?  93  ASN B C   1 
ATOM   2502 O O   . ASN B 1 113 ? -49.14700 -11.44500 41.22200 1.000 45.41159 ?  93  ASN B O   1 
ATOM   2503 C CB  . ASN B 1 113 ? -46.49700 -12.71000 40.59900 1.000 48.33714 ?  93  ASN B CB  1 
ATOM   2504 C CG  . ASN B 1 113 ? -45.58900 -13.64600 39.83200 1.000 54.48472 ?  93  ASN B CG  1 
ATOM   2505 O OD1 . ASN B 1 113 ? -45.99100 -14.19900 38.80900 1.000 56.65027 ?  93  ASN B OD1 1 
ATOM   2506 N N   . GLY B 1 114 ? -48.00500 -9.64400  40.51400 1.000 43.03414 ?  94  GLY B N   1 
ATOM   2507 C CA  . GLY B 1 114 ? -48.82700 -8.70900  41.24900 1.000 40.98281 ?  94  GLY B CA  1 
ATOM   2508 C C   . GLY B 1 114 ? -48.50400 -8.56500  42.72100 1.000 42.18125 ?  94  GLY B C   1 
ATOM   2509 O O   . GLY B 1 114 ? -49.18100 -7.79200  43.41100 1.000 44.94539 ?  94  GLY B O   1 
ATOM   2510 N N   . CYS B 1 115 ? -47.49900 -9.27100  43.23200 1.000 40.33591 ?  95  CYS B N   1 
ATOM   2511 C CA  . CYS B 1 115 ? -47.17000 -9.15600  44.64300 1.000 42.37802 ?  95  CYS B CA  1 
ATOM   2512 C C   . CYS B 1 115 ? -45.71800 -9.54700  44.87500 1.000 41.92448 ?  95  CYS B C   1 
ATOM   2513 O O   . CYS B 1 115 ? -45.17700 -10.42700 44.20000 1.000 46.02260 ?  95  CYS B O   1 
ATOM   2514 C CB  . CYS B 1 115 ? -48.09600 -10.02300 45.50500 1.000 44.33464 ?  95  CYS B CB  1 
ATOM   2515 S SG  . CYS B 1 115 ? -47.81600 -11.79500 45.33600 1.000 62.97539 ?  95  CYS B SG  1 
ATOM   2516 N N   . ILE B 1 116 ? -45.09300 -8.86900  45.83600 1.000 41.17289 ?  96  ILE B N   1 
ATOM   2517 C CA  . ILE B 1 116 ? -43.78100 -9.24400  46.34100 1.000 36.09211 ?  96  ILE B CA  1 
ATOM   2518 C C   . ILE B 1 116 ? -43.78200 -9.01700  47.84300 1.000 33.58889 ?  96  ILE B C   1 
ATOM   2519 O O   . ILE B 1 116 ? -44.57000 -8.22700  48.37000 1.000 38.21825 ?  96  ILE B O   1 
ATOM   2520 C CB  . ILE B 1 116 ? -42.63400 -8.45500  45.68000 1.000 39.20211 ?  96  ILE B CB  1 
ATOM   2521 C CG1 . ILE B 1 116 ? -42.89800 -6.95900  45.75100 1.000 40.73354 ?  96  ILE B CG1 1 
ATOM   2522 C CG2 . ILE B 1 116 ? -42.43300 -8.88300  44.23300 1.000 40.84477 ?  96  ILE B CG2 1 
ATOM   2523 C CD1 . ILE B 1 116 ? -41.75000 -6.13400  45.22000 1.000 37.41036 ?  96  ILE B CD1 1 
ATOM   2524 N N   . GLY B 1 117 ? -42.90000 -9.72900  48.53300 1.000 32.04227 ?  97  GLY B N   1 
ATOM   2525 C CA  . GLY B 1 117 ? -42.71700 -9.57400  49.96300 1.000 39.84211 ?  97  GLY B CA  1 
ATOM   2526 C C   . GLY B 1 117 ? -41.35700 -8.96800  50.25200 1.000 43.29841 ?  97  GLY B C   1 
ATOM   2527 O O   . GLY B 1 117 ? -40.40600 -9.16000  49.48700 1.000 41.40153 ?  97  GLY B O   1 
ATOM   2528 N N   . TYR B 1 118 ? -41.26800 -8.22600  51.35900 1.000 39.57990 ?  98  TYR B N   1 
ATOM   2529 C CA  . TYR B 1 118 ? -40.02000 -7.57700  51.74200 1.000 41.44109 ?  98  TYR B CA  1 
ATOM   2530 C C   . TYR B 1 118 ? -39.89500 -7.53600  53.25800 1.000 39.44927 ?  98  TYR B C   1 
ATOM   2531 O O   . TYR B 1 118 ? -40.88500 -7.60900  53.99100 1.000 34.80815 ?  98  TYR B O   1 
ATOM   2532 C CB  . TYR B 1 118 ? -39.90300 -6.16200  51.14100 1.000 35.21817 ?  98  TYR B CB  1 
ATOM   2533 C CG  . TYR B 1 118 ? -40.84400 -5.10500  51.68800 1.000 37.24338 ?  98  TYR B CG  1 
ATOM   2534 C CD1 . TYR B 1 118 ? -42.09700 -4.90000  51.12200 1.000 35.86645 ?  98  TYR B CD1 1 
ATOM   2535 C CD2 . TYR B 1 118 ? -40.46000 -4.27200  52.73600 1.000 42.47800 ?  98  TYR B CD2 1 
ATOM   2536 C CE1 . TYR B 1 118 ? -42.95100 -3.91800  51.60300 1.000 38.07499 ?  98  TYR B CE1 1 
ATOM   2537 C CE2 . TYR B 1 118 ? -41.31300 -3.28600  53.22100 1.000 36.66064 ?  98  TYR B CE2 1 
ATOM   2538 C CZ  . TYR B 1 118 ? -42.55400 -3.11500  52.65200 1.000 40.67019 ?  98  TYR B CZ  1 
ATOM   2539 O OH  . TYR B 1 118 ? -43.40600 -2.13900  53.12800 1.000 47.86625 ?  98  TYR B OH  1 
ATOM   2540 N N   . SER B 1 119 ? -38.64800 -7.42100  53.71700 1.000 36.30032 ?  99  SER B N   1 
ATOM   2541 C CA  . SER B 1 119 ? -38.32000 -7.41800  55.13800 1.000 39.75124 ?  99  SER B CA  1 
ATOM   2542 C C   . SER B 1 119 ? -38.09900 -5.98100  55.59700 1.000 39.14308 ?  99  SER B C   1 
ATOM   2543 O O   . SER B 1 119 ? -37.14200 -5.32600  55.17300 1.000 53.50256 ?  99  SER B O   1 
ATOM   2544 C CB  . SER B 1 119 ? -37.08100 -8.26900  55.41000 1.000 36.65312 ?  99  SER B CB  1 
ATOM   2545 N N   . GLN B 1 120 ? -38.98000 -5.49800  56.46300 1.000 33.45155 ?  100 GLN B N   1 
ATOM   2546 C CA  . GLN B 1 120 ? -38.76800 -4.22800  57.14100 1.000 38.95696 ?  100 GLN B CA  1 
ATOM   2547 C C   . GLN B 1 120 ? -37.88600 -4.43800  58.36400 1.000 42.09971 ?  100 GLN B C   1 
ATOM   2548 O O   . GLN B 1 120 ? -38.01500 -5.44100  59.07000 1.000 41.67742 ?  100 GLN B O   1 
ATOM   2549 C CB  . GLN B 1 120 ? -40.10400 -3.62800  57.56600 1.000 37.40797 ?  100 GLN B CB  1 
ATOM   2550 C CG  . GLN B 1 120 ? -40.30200 -2.19500  57.17000 1.000 45.07399 ?  100 GLN B CG  1 
ATOM   2551 C CD  . GLN B 1 120 ? -41.62300 -1.66400  57.66300 1.000 47.31463 ?  100 GLN B CD  1 
ATOM   2552 O OE1 . GLN B 1 120 ? -42.18100 -2.17100  58.63800 1.000 49.86898 ?  100 GLN B OE1 1 
ATOM   2553 N NE2 . GLN B 1 120 ? -42.14500 -0.65100  56.98400 1.000 41.82655 ?  100 GLN B NE2 1 
ATOM   2554 N N   . ASN B 1 121 ? -36.99100 -3.49000  58.61800 1.000 38.72040 ?  101 ASN B N   1 
ATOM   2555 C CA  . ASN B 1 121 ? -36.07300 -3.60000  59.74300 1.000 36.08451 ?  101 ASN B CA  1 
ATOM   2556 C C   . ASN B 1 121 ? -36.66900 -2.96200  60.99100 1.000 38.03268 ?  101 ASN B C   1 
ATOM   2557 O O   . ASN B 1 121 ? -37.32000 -1.91700  60.92100 1.000 36.18382 ?  101 ASN B O   1 
ATOM   2558 C CB  . ASN B 1 121 ? -34.73400 -2.93900  59.41800 1.000 49.00858 ?  101 ASN B CB  1 
ATOM   2559 C CG  . ASN B 1 121 ? -33.81500 -3.84400  58.62600 1.000 47.06546 ?  101 ASN B CG  1 
ATOM   2560 O OD1 . ASN B 1 121 ? -33.91300 -5.07100  58.69400 1.000 51.10901 ?  101 ASN B OD1 1 
ATOM   2561 N ND2 . ASN B 1 121 ? -32.91100 -3.23900  57.86700 1.000 45.09982 ?  101 ASN B ND2 1 
ATOM   2562 N N   . GLY B 1 122 ? -36.44100 -3.60000  62.13200 1.000 37.35630 ?  102 GLY B N   1 
ATOM   2563 C CA  . GLY B 1 122 ? -36.84400 -3.03800  63.40500 1.000 34.76740 ?  102 GLY B CA  1 
ATOM   2564 C C   . GLY B 1 122 ? -35.67500 -2.82800  64.34600 1.000 36.87955 ?  102 GLY B C   1 
ATOM   2565 O O   . GLY B 1 122 ? -34.58800 -2.41900  63.92700 1.000 36.00406 ?  102 GLY B O   1 
ATOM   2566 N N   . GLU B 1 123 ? -35.89800 -3.10500  65.62800 1.000 40.14903 ?  103 GLU B N   1 
ATOM   2567 C CA  . GLU B 1 123 ? -34.83700 -3.02300  66.62000 1.000 38.37473 ?  103 GLU B CA  1 
ATOM   2568 C C   . GLU B 1 123 ? -33.77600 -4.07500  66.34000 1.000 34.67460 ?  103 GLU B C   1 
ATOM   2569 O O   . GLU B 1 123 ? -34.09200 -5.26100  66.20800 1.000 35.25393 ?  103 GLU B O   1 
ATOM   2570 C CB  . GLU B 1 123 ? -35.41300 -3.23800  68.01200 1.000 39.40613 ?  103 GLU B CB  1 
ATOM   2571 C CG  . GLU B 1 123 ? -35.73600 -1.98300  68.75800 1.000 34.30808 ?  103 GLU B CG  1 
ATOM   2572 C CD  . GLU B 1 123 ? -36.29700 -2.28500  70.12100 1.000 37.90381 ?  103 GLU B CD  1 
ATOM   2573 O OE1 . GLU B 1 123 ? -35.66900 -3.07800  70.85400 1.000 36.59971 ?  103 GLU B OE1 1 
ATOM   2574 O OE2 . GLU B 1 123 ? -37.36700 -1.73900  70.45200 1.000 39.18385 -1 103 GLU B OE2 1 
ATOM   2575 N N   . GLY B 1 124 ? -32.51700 -3.64300  66.26300 1.000 32.91916 ?  104 GLY B N   1 
ATOM   2576 C CA  . GLY B 1 124 ? -31.40300 -4.55800  66.08400 1.000 29.64552 ?  104 GLY B CA  1 
ATOM   2577 C C   . GLY B 1 124 ? -31.52800 -5.45500  64.86900 1.000 38.18217 ?  104 GLY B C   1 
ATOM   2578 O O   . GLY B 1 124 ? -31.52300 -4.97500  63.73300 1.000 38.14624 ?  104 GLY B O   1 
ATOM   2579 N N   . GLU B 1 125 ? -31.64500 -6.76400  65.10000 1.000 40.03048 ?  105 GLU B N   1 
ATOM   2580 C CA  . GLU B 1 125 ? -31.81100 -7.74500  64.03500 1.000 40.18790 ?  105 GLU B CA  1 
ATOM   2581 C C   . GLU B 1 125 ? -33.26700 -8.12900  63.79700 1.000 39.19284 ?  105 GLU B C   1 
ATOM   2582 O O   . GLU B 1 125 ? -33.54500 -8.90800  62.87800 1.000 41.69488 ?  105 GLU B O   1 
ATOM   2583 C CB  . GLU B 1 125 ? -31.00200 -9.01100  64.35100 1.000 38.27728 ?  105 GLU B CB  1 
ATOM   2584 C CG  . GLU B 1 125 ? -31.54200 -9.79900  65.54400 1.000 39.57643 ?  105 GLU B CG  1 
ATOM   2585 C CD  . GLU B 1 125 ? -31.02800 -11.22800 65.60100 1.000 45.54103 ?  105 GLU B CD  1 
ATOM   2586 O OE1 . GLU B 1 125 ? -30.24200 -11.61600 64.71200 1.000 57.89300 ?  105 GLU B OE1 1 
ATOM   2587 O OE2 . GLU B 1 125 ? -31.40300 -11.96300 66.54100 1.000 39.57024 -1 105 GLU B OE2 1 
ATOM   2588 N N   . LEU B 1 126 ? -34.19500 -7.61700  64.60000 1.000 32.95119 ?  106 LEU B N   1 
ATOM   2589 C CA  . LEU B 1 126 ? -35.59700 -7.96600  64.42800 1.000 35.59152 ?  106 LEU B CA  1 
ATOM   2590 C C   . LEU B 1 126 ? -36.12800 -7.40800  63.11600 1.000 40.66318 ?  106 LEU B C   1 
ATOM   2591 O O   . LEU B 1 126 ? -35.75800 -6.31100  62.68900 1.000 37.18049 ?  106 LEU B O   1 
ATOM   2592 C CB  . LEU B 1 126 ? -36.42600 -7.44500  65.59500 1.000 29.76520 ?  106 LEU B CB  1 
ATOM   2593 C CG  . LEU B 1 126 ? -36.02500 -8.05200  66.93600 1.000 35.80078 ?  106 LEU B CG  1 
ATOM   2594 C CD1 . LEU B 1 126 ? -36.93000 -7.54500  68.04100 1.000 28.81209 ?  106 LEU B CD1 1 
ATOM   2595 C CD2 . LEU B 1 126 ? -36.03700 -9.57600  66.86100 1.000 33.33419 ?  106 LEU B CD2 1 
ATOM   2596 N N   . LYS B 1 127 ? -37.00300 -8.17500  62.47800 1.000 40.29142 ?  107 LYS B N   1 
ATOM   2597 C CA  . LYS B 1 127 ? -37.49600 -7.84800  61.15200 1.000 43.60658 ?  107 LYS B CA  1 
ATOM   2598 C C   . LYS B 1 127 ? -39.00700 -8.02300  61.10300 1.000 43.66925 ?  107 LYS B C   1 
ATOM   2599 O O   . LYS B 1 127 ? -39.55700 -8.95500  61.69800 1.000 45.76635 ?  107 LYS B O   1 
ATOM   2600 C CB  . LYS B 1 127 ? -36.81300 -8.72200  60.08200 1.000 37.84114 ?  107 LYS B CB  1 
ATOM   2601 C CG  . LYS B 1 127 ? -35.82400 -7.95800  59.20200 1.000 44.80930 ?  107 LYS B CG  1 
ATOM   2602 C CD  . LYS B 1 127 ? -34.39000 -8.39800  59.44100 1.000 52.88263 ?  107 LYS B CD  1 
ATOM   2603 N N   . ASN B 1 128 ? -39.66800 -7.09300  60.42100 1.000 43.25725 ?  108 ASN B N   1 
ATOM   2604 C CA  . ASN B 1 128 ? -41.06700 -7.19800  60.03800 1.000 41.90421 ?  108 ASN B CA  1 
ATOM   2605 C C   . ASN B 1 128 ? -41.13300 -7.55900  58.55800 1.000 41.51319 ?  108 ASN B C   1 
ATOM   2606 O O   . ASN B 1 128 ? -40.28200 -7.14500  57.76800 1.000 43.29417 ?  108 ASN B O   1 
ATOM   2607 C CB  . ASN B 1 128 ? -41.81000 -5.87700  60.27700 1.000 36.81295 ?  108 ASN B CB  1 
ATOM   2608 C CG  . ASN B 1 128 ? -41.85600 -5.47500  61.74300 1.000 47.70598 ?  108 ASN B CG  1 
ATOM   2609 O OD1 . ASN B 1 128 ? -41.44700 -4.37200  62.11000 1.000 57.35221 ?  108 ASN B OD1 1 
ATOM   2610 N ND2 . ASN B 1 128 ? -42.38100 -6.35300  62.58000 1.000 57.00225 ?  108 ASN B ND2 1 
ATOM   2611 N N   . TYR B 1 129 ? -42.15000 -8.32700  58.17900 1.000 39.01146 ?  109 TYR B N   1 
ATOM   2612 C CA  . TYR B 1 129 ? -42.32000 -8.74200  56.79200 1.000 39.04314 ?  109 TYR B CA  1 
ATOM   2613 C C   . TYR B 1 129 ? -43.64100 -8.20600  56.26400 1.000 40.11265 ?  109 TYR B C   1 
ATOM   2614 O O   . TYR B 1 129 ? -44.66900 -8.30300  56.94300 1.000 43.20493 ?  109 TYR B O   1 
ATOM   2615 C CB  . TYR B 1 129 ? -42.24000 -10.26700 56.65100 1.000 46.71942 ?  109 TYR B CB  1 
ATOM   2616 C CG  . TYR B 1 129 ? -40.87200 -10.80600 57.02100 1.000 52.49092 ?  109 TYR B CG  1 
ATOM   2617 C CD1 . TYR B 1 129 ? -40.44900 -10.84100 58.34900 1.000 54.57861 ?  109 TYR B CD1 1 
ATOM   2618 C CD2 . TYR B 1 129 ? -39.98100 -11.22900 56.04100 1.000 55.75552 ?  109 TYR B CD2 1 
ATOM   2619 C CE1 . TYR B 1 129 ? -39.19100 -11.31300 58.69600 1.000 51.36136 ?  109 TYR B CE1 1 
ATOM   2620 C CE2 . TYR B 1 129 ? -38.71800 -11.70400 56.37900 1.000 60.47127 ?  109 TYR B CE2 1 
ATOM   2621 C CZ  . TYR B 1 129 ? -38.33100 -11.74300 57.70700 1.000 54.34118 ?  109 TYR B CZ  1 
ATOM   2622 O OH  . TYR B 1 129 ? -37.08200 -12.21200 58.04500 1.000 59.08559 ?  109 TYR B OH  1 
ATOM   2623 N N   . LYS B 1 130 ? -43.60300 -7.61700  55.06600 1.000 37.49025 ?  110 LYS B N   1 
ATOM   2624 C CA  . LYS B 1 130 ? -44.76800 -6.98000  54.47000 1.000 33.40876 ?  110 LYS B CA  1 
ATOM   2625 C C   . LYS B 1 130 ? -44.93000 -7.45400  53.03500 1.000 36.10401 ?  110 LYS B C   1 
ATOM   2626 O O   . LYS B 1 130 ? -44.00200 -7.98500  52.42400 1.000 34.67248 ?  110 LYS B O   1 
ATOM   2627 C CB  . LYS B 1 130 ? -44.66200 -5.44900  54.49300 1.000 42.10014 ?  110 LYS B CB  1 
ATOM   2628 C CG  . LYS B 1 130 ? -43.76000 -4.89600  55.58100 1.000 42.84116 ?  110 LYS B CG  1 
ATOM   2629 C CD  . LYS B 1 130 ? -44.54500 -4.49000  56.81700 1.000 45.14047 ?  110 LYS B CD  1 
ATOM   2630 C CE  . LYS B 1 130 ? -45.54900 -3.39400  56.50800 1.000 39.68320 ?  110 LYS B CE  1 
ATOM   2631 N N   . VAL B 1 131 ? -46.12500 -7.23800  52.49600 1.000 40.70195 ?  111 VAL B N   1 
ATOM   2632 C CA  . VAL B 1 131 ? -46.47000 -7.66000  51.14600 1.000 40.52725 ?  111 VAL B CA  1 
ATOM   2633 C C   . VAL B 1 131 ? -46.93400 -6.44000  50.36500 1.000 42.51970 ?  111 VAL B C   1 
ATOM   2634 O O   . VAL B 1 131 ? -47.78000 -5.67300  50.84000 1.000 42.04381 ?  111 VAL B O   1 
ATOM   2635 C CB  . VAL B 1 131 ? -47.55100 -8.75600  51.15300 1.000 43.04036 ?  111 VAL B CB  1 
ATOM   2636 C CG1 . VAL B 1 131 ? -47.91600 -9.15500  49.73400 1.000 39.07642 ?  111 VAL B CG1 1 
ATOM   2637 C CG2 . VAL B 1 131 ? -47.06600 -9.96300  51.94000 1.000 34.54958 ?  111 VAL B CG2 1 
ATOM   2638 N N   . ILE B 1 132 ? -46.36200 -6.25200  49.18200 1.000 40.11273 ?  112 ILE B N   1 
ATOM   2639 C CA  . ILE B 1 132 ? -46.77700 -5.21100  48.25400 1.000 40.60214 ?  112 ILE B CA  1 
ATOM   2640 C C   . ILE B 1 132 ? -47.73000 -5.84900  47.25900 1.000 40.56749 ?  112 ILE B C   1 
ATOM   2641 O O   . ILE B 1 132 ? -47.37700 -6.83500  46.60400 1.000 36.71224 ?  112 ILE B O   1 
ATOM   2642 C CB  . ILE B 1 132 ? -45.57300 -4.58300  47.53400 1.000 36.65726 ?  112 ILE B CB  1 
ATOM   2643 C CG1 . ILE B 1 132 ? -44.60100 -3.97600  48.54600 1.000 40.60513 ?  112 ILE B CG1 1 
ATOM   2644 C CG2 . ILE B 1 132 ? -46.02900 -3.54100  46.52600 1.000 34.40000 ?  112 ILE B CG2 1 
ATOM   2645 C CD1 . ILE B 1 132 ? -43.22500 -3.71400  47.97000 1.000 37.93953 ?  112 ILE B CD1 1 
ATOM   2646 N N   . ASP B 1 133 ? -48.94000 -5.31000  47.15300 1.000 40.78321 ?  113 ASP B N   1 
ATOM   2647 C CA  . ASP B 1 133 ? -49.91700 -5.79300  46.18600 1.000 40.44507 ?  113 ASP B CA  1 
ATOM   2648 C C   . ASP B 1 133 ? -50.12300 -4.72700  45.11900 1.000 40.36184 ?  113 ASP B C   1 
ATOM   2649 O O   . ASP B 1 133 ? -50.54000 -3.60600  45.42800 1.000 39.80280 ?  113 ASP B O   1 
ATOM   2650 C CB  . ASP B 1 133 ? -51.23900 -6.15600  46.86200 1.000 46.15992 ?  113 ASP B CB  1 
ATOM   2651 C CG  . ASP B 1 133 ? -52.28600 -6.63500  45.87100 1.000 46.23989 ?  113 ASP B CG  1 
ATOM   2652 O OD1 . ASP B 1 133 ? -51.92200 -7.36100  44.92100 1.000 48.75862 ?  113 ASP B OD1 1 
ATOM   2653 O OD2 . ASP B 1 133 ? -53.47600 -6.30200  46.05200 1.000 59.19450 -1 113 ASP B OD2 1 
ATOM   2654 N N   . ARG B 1 134 ? -49.81400 -5.08500  43.87100 1.000 41.53327 ?  114 ARG B N   1 
ATOM   2655 C CA  . ARG B 1 134 ? -49.97700 -4.17200  42.74400 1.000 42.24814 ?  114 ARG B CA  1 
ATOM   2656 C C   . ARG B 1 134 ? -51.36400 -3.54500  42.71600 1.000 49.44542 ?  114 ARG B C   1 
ATOM   2657 O O   . ARG B 1 134 ? -51.50700 -2.34000  42.47600 1.000 45.42311 ?  114 ARG B O   1 
ATOM   2658 C CB  . ARG B 1 134 ? -49.72000 -4.93300  41.44700 1.000 46.70265 ?  114 ARG B CB  1 
ATOM   2659 C CG  . ARG B 1 134 ? -49.34800 -4.08600  40.25900 1.000 49.99830 ?  114 ARG B CG  1 
ATOM   2660 C CD  . ARG B 1 134 ? -49.33800 -4.96700  39.03200 1.000 46.99022 ?  114 ARG B CD  1 
ATOM   2661 N NE  . ARG B 1 134 ? -50.53100 -5.80400  38.99400 1.000 44.50251 ?  114 ARG B NE  1 
ATOM   2662 C CZ  . ARG B 1 134 ? -50.57000 -7.03600  38.50700 1.000 47.99776 ?  114 ARG B CZ  1 
ATOM   2663 N NH1 . ARG B 1 134 ? -49.48700 -7.62600  38.02800 1.000 43.20151 ?  114 ARG B NH1 1 
ATOM   2664 N NH2 . ARG B 1 134 ? -51.72700 -7.69100  38.49500 1.000 46.67918 ?  114 ARG B NH2 1 
ATOM   2665 N N   . GLU B 1 135 ? -52.40000 -4.35300  42.95600 1.000 51.28129 ?  115 GLU B N   1 
ATOM   2666 C CA  . GLU B 1 135 ? -53.77600 -3.87800  42.87800 1.000 49.04459 ?  115 GLU B CA  1 
ATOM   2667 C C   . GLU B 1 135 ? -54.13500 -2.90800  43.99400 1.000 50.05055 ?  115 GLU B C   1 
ATOM   2668 O O   . GLU B 1 135 ? -55.20300 -2.29000  43.92800 1.000 53.11761 ?  115 GLU B O   1 
ATOM   2669 C CB  . GLU B 1 135 ? -54.74400 -5.06400  42.89000 1.000 53.23558 ?  115 GLU B CB  1 
ATOM   2670 C CG  . GLU B 1 135 ? -54.48500 -6.09100  41.79400 1.000 48.75748 ?  115 GLU B CG  1 
ATOM   2671 C CD  . GLU B 1 135 ? -54.42500 -5.46700  40.41000 1.000 53.57434 ?  115 GLU B CD  1 
ATOM   2672 O OE1 . GLU B 1 135 ? -55.48700 -5.07700  39.87800 1.000 56.59371 ?  115 GLU B OE1 1 
ATOM   2673 O OE2 . GLU B 1 135 ? -53.31200 -5.36700  39.85100 1.000 57.84973 -1 115 GLU B OE2 1 
ATOM   2674 N N   . GLY B 1 136 ? -53.28300 -2.76400  45.00900 1.000 44.73516 ?  116 GLY B N   1 
ATOM   2675 C CA  . GLY B 1 136 ? -53.48900 -1.77400  46.04400 1.000 43.59058 ?  116 GLY B CA  1 
ATOM   2676 C C   . GLY B 1 136 ? -53.04800 -0.37100  45.69600 1.000 45.39313 ?  116 GLY B C   1 
ATOM   2677 O O   . GLY B 1 136 ? -53.16600 0.53200   46.52900 1.000 48.51396 ?  116 GLY B O   1 
ATOM   2678 N N   . TYR B 1 137 ? -52.54900 -0.15300  44.48300 1.000 38.94837 ?  117 TYR B N   1 
ATOM   2679 C CA  . TYR B 1 137 ? -52.05100 1.14600   44.06000 1.000 40.96205 ?  117 TYR B CA  1 
ATOM   2680 C C   . TYR B 1 137 ? -52.74500 1.58000   42.77800 1.000 39.81086 ?  117 TYR B C   1 
ATOM   2681 O O   . TYR B 1 137 ? -53.16300 0.75200   41.96500 1.000 44.20555 ?  117 TYR B O   1 
ATOM   2682 C CB  . TYR B 1 137 ? -50.53300 1.12700   43.83200 1.000 39.89018 ?  117 TYR B CB  1 
ATOM   2683 C CG  . TYR B 1 137 ? -49.71600 0.70500   45.03300 1.000 37.26181 ?  117 TYR B CG  1 
ATOM   2684 C CD1 . TYR B 1 137 ? -49.53400 -0.63700  45.33900 1.000 38.76635 ?  117 TYR B CD1 1 
ATOM   2685 C CD2 . TYR B 1 137 ? -49.11000 1.65100   45.84700 1.000 37.82492 ?  117 TYR B CD2 1 
ATOM   2686 C CE1 . TYR B 1 137 ? -48.78300 -1.02500  46.43400 1.000 40.23971 ?  117 TYR B CE1 1 
ATOM   2687 C CE2 . TYR B 1 137 ? -48.35900 1.27400   46.94500 1.000 38.52233 ?  117 TYR B CE2 1 
ATOM   2688 C CZ  . TYR B 1 137 ? -48.19800 -0.06500  47.23400 1.000 37.53066 ?  117 TYR B CZ  1 
ATOM   2689 O OH  . TYR B 1 137 ? -47.45000 -0.44400  48.32700 1.000 35.95220 ?  117 TYR B OH  1 
ATOM   2690 N N   . ALA B 1 138 ? -52.84000 2.89900   42.59600 1.000 38.90262 ?  118 ALA B N   1 
ATOM   2691 C CA  . ALA B 1 138 ? -53.53400 3.44200   41.43300 1.000 40.11045 ?  118 ALA B CA  1 
ATOM   2692 C C   . ALA B 1 138 ? -52.81200 3.12400   40.12900 1.000 45.39588 ?  118 ALA B C   1 
ATOM   2693 O O   . ALA B 1 138 ? -53.44900 3.09700   39.06900 1.000 43.38616 ?  118 ALA B O   1 
ATOM   2694 C CB  . ALA B 1 138 ? -53.71100 4.95300   41.58500 1.000 43.76816 ?  118 ALA B CB  1 
ATOM   2695 N N   . PHE B 1 139 ? -51.49600 2.88000   40.17200 1.000 40.72043 ?  119 PHE B N   1 
ATOM   2696 C CA  . PHE B 1 139 ? -50.80400 2.54200   38.93100 1.000 38.89136 ?  119 PHE B CA  1 
ATOM   2697 C C   . PHE B 1 139 ? -51.14600 1.15200   38.42800 1.000 36.92905 ?  119 PHE B C   1 
ATOM   2698 O O   . PHE B 1 139 ? -50.53900 0.70500   37.44900 1.000 42.98869 ?  119 PHE B O   1 
ATOM   2699 C CB  . PHE B 1 139 ? -49.28000 2.69100   39.08800 1.000 33.18676 ?  119 PHE B CB  1 
ATOM   2700 C CG  . PHE B 1 139 ? -48.64700 1.73000   40.06900 1.000 37.93951 ?  119 PHE B CG  1 
ATOM   2701 C CD1 . PHE B 1 139 ? -48.49300 0.38000   39.76800 1.000 40.06853 ?  119 PHE B CD1 1 
ATOM   2702 C CD2 . PHE B 1 139 ? -48.17800 2.19000   41.28700 1.000 38.81813 ?  119 PHE B CD2 1 
ATOM   2703 C CE1 . PHE B 1 139 ? -47.90900 -0.48600  40.66900 1.000 38.06608 ?  119 PHE B CE1 1 
ATOM   2704 C CE2 . PHE B 1 139 ? -47.58600 1.32800   42.18800 1.000 36.88055 ?  119 PHE B CE2 1 
ATOM   2705 C CZ  . PHE B 1 139 ? -47.45400 -0.01100  41.88100 1.000 36.19027 ?  119 PHE B CZ  1 
ATOM   2706 N N   . ARG B 1 140 ? -52.07900 0.45000   39.07500 1.000 39.22468 ?  120 ARG B N   1 
ATOM   2707 C CA  . ARG B 1 140 ? -52.52600 -0.84000  38.56300 1.000 43.48565 ?  120 ARG B CA  1 
ATOM   2708 C C   . ARG B 1 140 ? -53.15300 -0.71600  37.17900 1.000 37.44730 ?  120 ARG B C   1 
ATOM   2709 O O   . ARG B 1 140 ? -53.28900 -1.72400  36.47900 1.000 47.70041 ?  120 ARG B O   1 
ATOM   2710 C CB  . ARG B 1 140 ? -53.51600 -1.47800  39.54300 1.000 41.95589 ?  120 ARG B CB  1 
ATOM   2711 C CG  . ARG B 1 140 ? -54.85700 -0.76400  39.61800 1.000 47.63734 ?  120 ARG B CG  1 
ATOM   2712 C CD  . ARG B 1 140 ? -55.84400 -1.49100  40.52400 1.000 49.88645 ?  120 ARG B CD  1 
ATOM   2713 N NE  . ARG B 1 140 ? -56.62900 -0.56200  41.32900 1.000 58.35613 ?  120 ARG B NE  1 
ATOM   2714 C CZ  . ARG B 1 140 ? -57.92700 -0.68800  41.56800 1.000 56.31226 ?  120 ARG B CZ  1 
ATOM   2715 N N   . ASP B 1 141 ? -53.52000 0.49700   36.76500 1.000 44.71589 ?  121 ASP B N   1 
ATOM   2716 C CA  . ASP B 1 141 ? -54.13800 0.73800   35.46800 1.000 43.24657 ?  121 ASP B CA  1 
ATOM   2717 C C   . ASP B 1 141 ? -53.12800 0.89000   34.33600 1.000 49.16255 ?  121 ASP B C   1 
ATOM   2718 O O   . ASP B 1 141 ? -53.54100 1.08500   33.18800 1.000 43.94008 ?  121 ASP B O   1 
ATOM   2719 C CB  . ASP B 1 141 ? -55.01500 1.99300   35.53100 1.000 42.80163 ?  121 ASP B CB  1 
ATOM   2720 C CG  . ASP B 1 141 ? -54.21600 3.25900   35.81300 1.000 54.51538 ?  121 ASP B CG  1 
ATOM   2721 O OD1 . ASP B 1 141 ? -53.01200 3.16000   36.14200 1.000 53.02075 ?  121 ASP B OD1 1 
ATOM   2722 O OD2 . ASP B 1 141 ? -54.79800 4.36400   35.71400 1.000 50.61683 -1 121 ASP B OD2 1 
ATOM   2723 N N   . SER B 1 142 ? -51.82200 0.81900   34.61700 1.000 43.45896 ?  122 SER B N   1 
ATOM   2724 C CA  . SER B 1 142 ? -50.84000 1.11600   33.58100 1.000 46.49345 ?  122 SER B CA  1 
ATOM   2725 C C   . SER B 1 142 ? -49.59600 0.24100   33.63900 1.000 40.48699 ?  122 SER B C   1 
ATOM   2726 O O   . SER B 1 142 ? -48.64300 0.50900   32.89500 1.000 46.47419 ?  122 SER B O   1 
ATOM   2727 C CB  . SER B 1 142 ? -50.42600 2.58700   33.66400 1.000 44.21865 ?  122 SER B CB  1 
ATOM   2728 N N   . PHE B 1 143 ? -49.56600 -0.79400  34.48000 1.000 41.21662 ?  123 PHE B N   1 
ATOM   2729 C CA  . PHE B 1 143 ? -48.31800 -1.51300  34.70900 1.000 37.48827 ?  123 PHE B CA  1 
ATOM   2730 C C   . PHE B 1 143 ? -47.87800 -2.34100  33.50900 1.000 47.22057 ?  123 PHE B C   1 
ATOM   2731 O O   . PHE B 1 143 ? -46.71100 -2.74100  33.44900 1.000 48.45467 ?  123 PHE B O   1 
ATOM   2732 C CB  . PHE B 1 143 ? -48.43300 -2.40800  35.94400 1.000 41.63083 ?  123 PHE B CB  1 
ATOM   2733 C CG  . PHE B 1 143 ? -49.37900 -3.56100  35.77800 1.000 43.14453 ?  123 PHE B CG  1 
ATOM   2734 C CD1 . PHE B 1 143 ? -48.93200 -4.77900  35.29400 1.000 37.70712 ?  123 PHE B CD1 1 
ATOM   2735 C CD2 . PHE B 1 143 ? -50.71000 -3.43300  36.13200 1.000 43.90889 ?  123 PHE B CD2 1 
ATOM   2736 C CE1 . PHE B 1 143 ? -49.79800 -5.84000  35.14900 1.000 45.79569 ?  123 PHE B CE1 1 
ATOM   2737 C CE2 . PHE B 1 143 ? -51.58300 -4.49300  35.98900 1.000 42.28621 ?  123 PHE B CE2 1 
ATOM   2738 C CZ  . PHE B 1 143 ? -51.12600 -5.69600  35.49600 1.000 41.19921 ?  123 PHE B CZ  1 
ATOM   2739 N N   . THR B 1 144 ? -48.77100 -2.61800  32.56100 1.000 40.63909 ?  124 THR B N   1 
ATOM   2740 C CA  . THR B 1 144 ? -48.37300 -3.35000  31.36500 1.000 37.72487 ?  124 THR B CA  1 
ATOM   2741 C C   . THR B 1 144 ? -47.63900 -2.47800  30.36000 1.000 40.92950 ?  124 THR B C   1 
ATOM   2742 O O   . THR B 1 144 ? -47.16300 -2.99900  29.34500 1.000 43.08130 ?  124 THR B O   1 
ATOM   2743 C CB  . THR B 1 144 ? -49.59600 -3.98000  30.69200 1.000 47.92219 ?  124 THR B CB  1 
ATOM   2744 O OG1 . THR B 1 144 ? -50.42300 -2.94600  30.14200 1.000 44.34527 ?  124 THR B OG1 1 
ATOM   2745 C CG2 . THR B 1 144 ? -50.40300 -4.79500  31.69600 1.000 39.30616 ?  124 THR B CG2 1 
ATOM   2746 N N   . LYS B 1 145 ? -47.53000 -1.17500  30.61200 1.000 42.08187 ?  125 LYS B N   1 
ATOM   2747 C CA  . LYS B 1 145 ? -46.84000 -0.26500  29.71000 1.000 37.21527 ?  125 LYS B CA  1 
ATOM   2748 C C   . LYS B 1 145 ? -45.37300 -0.06800  30.07700 1.000 40.72587 ?  125 LYS B C   1 
ATOM   2749 O O   . LYS B 1 145 ? -44.70800 0.78600   29.47900 1.000 36.70058 ?  125 LYS B O   1 
ATOM   2750 C CB  . LYS B 1 145 ? -47.55900 1.08300   29.68300 1.000 42.32031 ?  125 LYS B CB  1 
ATOM   2751 C CG  . LYS B 1 145 ? -48.81900 1.06900   28.83700 1.000 43.29399 ?  125 LYS B CG  1 
ATOM   2752 C CD  . LYS B 1 145 ? -49.91700 1.91200   29.45900 1.000 38.58884 ?  125 LYS B CD  1 
ATOM   2753 C CE  . LYS B 1 145 ? -49.63800 3.38200   29.29500 1.000 36.60729 ?  125 LYS B CE  1 
ATOM   2754 N NZ  . LYS B 1 145 ? -50.54300 4.18400   30.16500 1.000 46.65451 ?  125 LYS B NZ  1 
ATOM   2755 N N   . VAL B 1 146 ? -44.85600 -0.85000  31.02600 1.000 39.16435 ?  126 VAL B N   1 
ATOM   2756 C CA  . VAL B 1 146 ? -43.49800 -0.71000  31.54200 1.000 42.82151 ?  126 VAL B CA  1 
ATOM   2757 C C   . VAL B 1 146 ? -42.69000 -1.94500  31.17300 1.000 38.48800 ?  126 VAL B C   1 
ATOM   2758 O O   . VAL B 1 146 ? -43.20600 -3.06700  31.19400 1.000 35.05359 ?  126 VAL B O   1 
ATOM   2759 C CB  . VAL B 1 146 ? -43.48100 -0.51600  33.07400 1.000 36.68526 ?  126 VAL B CB  1 
ATOM   2760 C CG1 . VAL B 1 146 ? -42.06100 -0.26900  33.56500 1.000 33.60900 ?  126 VAL B CG1 1 
ATOM   2761 C CG2 . VAL B 1 146 ? -44.39200 0.62200   33.48000 1.000 34.28585 ?  126 VAL B CG2 1 
ATOM   2762 N N   . GLU B 1 147 ? -41.41400 -1.73500  30.86000 1.000 37.75041 ?  127 GLU B N   1 
ATOM   2763 C CA  . GLU B 1 147 ? -40.45900 -2.81800  30.65900 1.000 43.62626 ?  127 GLU B CA  1 
ATOM   2764 C C   . GLU B 1 147 ? -39.22400 -2.53400  31.50100 1.000 35.27209 ?  127 GLU B C   1 
ATOM   2765 O O   . GLU B 1 147 ? -38.60300 -1.47700  31.35400 1.000 38.41502 ?  127 GLU B O   1 
ATOM   2766 C CB  . GLU B 1 147 ? -40.08600 -2.95000  29.18300 1.000 43.22463 ?  127 GLU B CB  1 
ATOM   2767 C CG  . GLU B 1 147 ? -40.57400 -4.21800  28.52400 1.000 57.49420 ?  127 GLU B CG  1 
ATOM   2768 C CD  . GLU B 1 147 ? -39.79300 -4.53300  27.26700 1.000 61.96961 ?  127 GLU B CD  1 
ATOM   2769 O OE1 . GLU B 1 147 ? -39.87400 -3.73300  26.30800 1.000 63.72323 ?  127 GLU B OE1 1 
ATOM   2770 O OE2 . GLU B 1 147 ? -39.08800 -5.56800  27.24400 1.000 65.94809 -1 127 GLU B OE2 1 
ATOM   2771 N N   . PHE B 1 148 ? -38.86700 -3.47100  32.37400 1.000 40.63908 ?  128 PHE B N   1 
ATOM   2772 C CA  . PHE B 1 148 ? -37.73600 -3.31400  33.28100 1.000 36.71534 ?  128 PHE B CA  1 
ATOM   2773 C C   . PHE B 1 148 ? -36.52000 -4.05400  32.73800 1.000 40.65079 ?  128 PHE B C   1 
ATOM   2774 O O   . PHE B 1 148 ? -36.62800 -5.21000  32.31800 1.000 41.25832 ?  128 PHE B O   1 
ATOM   2775 C CB  . PHE B 1 148 ? -38.08500 -3.83300  34.67600 1.000 32.91057 ?  128 PHE B CB  1 
ATOM   2776 C CG  . PHE B 1 148 ? -39.13700 -3.02300  35.38100 1.000 34.64201 ?  128 PHE B CG  1 
ATOM   2777 C CD1 . PHE B 1 148 ? -38.85900 -1.74200  35.82700 1.000 34.67437 ?  128 PHE B CD1 1 
ATOM   2778 C CD2 . PHE B 1 148 ? -40.39800 -3.54800  35.61300 1.000 30.75830 ?  128 PHE B CD2 1 
ATOM   2779 C CE1 . PHE B 1 148 ? -39.82100 -0.99600  36.48500 1.000 29.56487 ?  128 PHE B CE1 1 
ATOM   2780 C CE2 . PHE B 1 148 ? -41.36700 -2.80800  36.26900 1.000 36.19682 ?  128 PHE B CE2 1 
ATOM   2781 C CZ  . PHE B 1 148 ? -41.07800 -1.52900  36.70600 1.000 31.84336 ?  128 PHE B CZ  1 
ATOM   2782 N N   . PHE B 1 149 ? -35.36300 -3.39300  32.75700 1.000 36.00868 ?  129 PHE B N   1 
ATOM   2783 C CA  . PHE B 1 149 ? -34.12800 -3.96200  32.24000 1.000 35.96288 ?  129 PHE B CA  1 
ATOM   2784 C C   . PHE B 1 149 ? -32.98400 -3.72400  33.21200 1.000 37.16382 ?  129 PHE B C   1 
ATOM   2785 O O   . PHE B 1 149 ? -32.95400 -2.72200  33.93200 1.000 36.69553 ?  129 PHE B O   1 
ATOM   2786 C CB  . PHE B 1 149 ? -33.71800 -3.35600  30.89000 1.000 41.59937 ?  129 PHE B CB  1 
ATOM   2787 C CG  . PHE B 1 149 ? -34.78500 -3.39700  29.83800 1.000 41.85401 ?  129 PHE B CG  1 
ATOM   2788 C CD1 . PHE B 1 149 ? -35.71100 -2.37300  29.73100 1.000 37.45743 ?  129 PHE B CD1 1 
ATOM   2789 C CD2 . PHE B 1 149 ? -34.83300 -4.43600  28.92300 1.000 40.75051 ?  129 PHE B CD2 1 
ATOM   2790 C CE1 . PHE B 1 149 ? -36.68000 -2.39500  28.74500 1.000 41.04864 ?  129 PHE B CE1 1 
ATOM   2791 C CE2 . PHE B 1 149 ? -35.80200 -4.46400  27.93700 1.000 43.90957 ?  129 PHE B CE2 1 
ATOM   2792 C CZ  . PHE B 1 149 ? -36.72500 -3.44100  27.84800 1.000 42.86447 ?  129 PHE B CZ  1 
ATOM   2793 N N   . GLN B 1 150 ? -32.03000 -4.64800  33.21400 1.000 37.87265 ?  130 GLN B N   1 
ATOM   2794 C CA  . GLN B 1 150 ? -30.75000 -4.40500  33.85800 1.000 40.30235 ?  130 GLN B CA  1 
ATOM   2795 C C   . GLN B 1 150 ? -29.87300 -3.62200  32.89400 1.000 34.68152 ?  130 GLN B C   1 
ATOM   2796 O O   . GLN B 1 150 ? -29.83700 -3.91600  31.69600 1.000 38.56617 ?  130 GLN B O   1 
ATOM   2797 C CB  . GLN B 1 150 ? -30.06900 -5.71400  34.25000 1.000 35.23776 ?  130 GLN B CB  1 
ATOM   2798 C CG  . GLN B 1 150 ? -28.85100 -5.53800  35.14900 1.000 38.22304 ?  130 GLN B CG  1 
ATOM   2799 C CD  . GLN B 1 150 ? -27.58600 -5.20900  34.37500 1.000 39.65708 ?  130 GLN B CD  1 
ATOM   2800 O OE1 . GLN B 1 150 ? -27.44600 -5.57500  33.21100 1.000 39.93154 ?  130 GLN B OE1 1 
ATOM   2801 N NE2 . GLN B 1 150 ? -26.65400 -4.52200  35.02500 1.000 40.40719 ?  130 GLN B NE2 1 
ATOM   2802 N N   . GLY B 1 151 ? -29.18200 -2.61500  33.41000 1.000 38.42665 ?  131 GLY B N   1 
ATOM   2803 C CA  . GLY B 1 151 ? -28.33800 -1.81200  32.54500 1.000 38.81638 ?  131 GLY B CA  1 
ATOM   2804 C C   . GLY B 1 151 ? -27.57100 -0.77900  33.33600 1.000 39.14000 ?  131 GLY B C   1 
ATOM   2805 O O   . GLY B 1 151 ? -27.75000 -0.62700  34.54900 1.000 37.36131 ?  131 GLY B O   1 
ATOM   2806 N N   . ASP B 1 152 ? -26.71800 -0.05800  32.61000 1.000 40.16985 ?  132 ASP B N   1 
ATOM   2807 C CA  . ASP B 1 152 ? -25.81600 0.94400   33.16100 1.000 33.60088 ?  132 ASP B CA  1 
ATOM   2808 C C   . ASP B 1 152 ? -26.03200 2.26100   32.43100 1.000 39.25625 ?  132 ASP B C   1 
ATOM   2809 O O   . ASP B 1 152 ? -25.92700 2.31500   31.20100 1.000 37.95447 ?  132 ASP B O   1 
ATOM   2810 C CB  . ASP B 1 152 ? -24.35500 0.50100   33.01500 1.000 43.12415 ?  132 ASP B CB  1 
ATOM   2811 C CG  . ASP B 1 152 ? -23.42000 1.24900   33.94100 1.000 48.15687 ?  132 ASP B CG  1 
ATOM   2812 O OD1 . ASP B 1 152 ? -23.57400 2.48700   34.06700 1.000 46.70303 ?  132 ASP B OD1 1 
ATOM   2813 O OD2 . ASP B 1 152 ? -22.53100 0.60100   34.54200 1.000 48.76547 -1 132 ASP B OD2 1 
ATOM   2814 N N   . ALA B 1 153 ? -26.30400 3.32400   33.19400 1.000 29.99278 ?  133 ALA B N   1 
ATOM   2815 C CA  . ALA B 1 153 ? -26.52600 4.63700   32.59800 1.000 36.90319 ?  133 ALA B CA  1 
ATOM   2816 C C   . ALA B 1 153 ? -25.30000 5.13300   31.84700 1.000 37.21385 ?  133 ALA B C   1 
ATOM   2817 O O   . ALA B 1 153 ? -25.43300 5.88400   30.87400 1.000 36.41185 ?  133 ALA B O   1 
ATOM   2818 C CB  . ALA B 1 153 ? -26.92000 5.64400   33.68000 1.000 37.84827 ?  133 ALA B CB  1 
ATOM   2819 N N   . CYS B 1 154 ? -24.10200 4.73400   32.28000 1.000 35.53517 ?  134 CYS B N   1 
ATOM   2820 C CA  . CYS B 1 154 ? -22.87400 5.16500   31.62600 1.000 38.12245 ?  134 CYS B CA  1 
ATOM   2821 C C   . CYS B 1 154 ? -22.56600 4.37500   30.36500 1.000 37.97066 ?  134 CYS B C   1 
ATOM   2822 O O   . CYS B 1 154 ? -21.58100 4.68300   29.68700 1.000 39.94533 ?  134 CYS B O   1 
ATOM   2823 C CB  . CYS B 1 154 ? -21.69800 5.05200   32.59300 1.000 37.50891 ?  134 CYS B CB  1 
ATOM   2824 S SG  . CYS B 1 154 ? -21.84200 6.13000   34.01700 1.000 43.25044 ?  134 CYS B SG  1 
ATOM   2825 N N   . ASN B 1 155 ? -23.37000 3.36600   30.04200 1.000 36.55206 ?  135 ASN B N   1 
ATOM   2826 C CA  . ASN B 1 155 ? -23.14800 2.57500   28.84000 1.000 42.23640 ?  135 ASN B CA  1 
ATOM   2827 C C   . ASN B 1 155 ? -24.44300 1.89800   28.41400 1.000 36.79080 ?  135 ASN B C   1 
ATOM   2828 O O   . ASN B 1 155 ? -24.56100 0.67100   28.46800 1.000 36.13893 ?  135 ASN B O   1 
ATOM   2829 C CB  . ASN B 1 155 ? -22.05000 1.54100   29.07600 1.000 47.97390 ?  135 ASN B CB  1 
ATOM   2830 C CG  . ASN B 1 155 ? -21.51600 0.96500   27.78600 1.000 43.49014 ?  135 ASN B CG  1 
ATOM   2831 O OD1 . ASN B 1 155 ? -21.19400 1.69900   26.84800 1.000 44.67609 ?  135 ASN B OD1 1 
ATOM   2832 N ND2 . ASN B 1 155 ? -21.43100 -0.35800  27.72400 1.000 39.11386 ?  135 ASN B ND2 1 
ATOM   2833 N N   . LEU B 1 156 ? -25.42100 2.69300   27.99800 1.000 39.35696 ?  136 LEU B N   1 
ATOM   2834 C CA  . LEU B 1 156 ? -26.71400 2.16400   27.59400 1.000 38.67008 ?  136 LEU B CA  1 
ATOM   2835 C C   . LEU B 1 156 ? -26.61700 1.53900   26.20600 1.000 45.39040 ?  136 LEU B C   1 
ATOM   2836 O O   . LEU B 1 156 ? -25.86300 2.00700   25.34500 1.000 41.90223 ?  136 LEU B O   1 
ATOM   2837 C CB  . LEU B 1 156 ? -27.76600 3.27600   27.60300 1.000 40.28305 ?  136 LEU B CB  1 
ATOM   2838 C CG  . LEU B 1 156 ? -28.23300 3.75200   28.99300 1.000 38.75954 ?  136 LEU B CG  1 
ATOM   2839 C CD1 . LEU B 1 156 ? -29.20500 4.92300   28.88100 1.000 31.66858 ?  136 LEU B CD1 1 
ATOM   2840 C CD2 . LEU B 1 156 ? -28.84800 2.60200   29.77900 1.000 36.86066 ?  136 LEU B CD2 1 
ATOM   2841 N N   . THR B 1 157 ? -27.37400 0.46300   25.99500 1.000 43.05252 ?  137 THR B N   1 
ATOM   2842 C CA  . THR B 1 157 ? -27.38800 -0.18800  24.69700 1.000 46.33449 ?  137 THR B CA  1 
ATOM   2843 C C   . THR B 1 157 ? -28.13600 0.68100   23.68100 1.000 50.63205 ?  137 THR B C   1 
ATOM   2844 O O   . THR B 1 157 ? -28.94700 1.53400   24.05600 1.000 43.94894 ?  137 THR B O   1 
ATOM   2845 C CB  . THR B 1 157 ? -28.01800 -1.57300  24.81100 1.000 41.09275 ?  137 THR B CB  1 
ATOM   2846 O OG1 . THR B 1 157 ? -29.38800 -1.45200  25.19000 1.000 44.91032 ?  137 THR B OG1 1 
ATOM   2847 C CG2 . THR B 1 157 ? -27.28400 -2.41100  25.84900 1.000 42.49742 ?  137 THR B CG2 1 
ATOM   2848 N N   . PRO B 1 158 ? -27.87100 0.48100   22.38500 1.000 50.74429 ?  138 PRO B N   1 
ATOM   2849 C CA  . PRO B 1 158 ? -28.40400 1.40600   21.36900 1.000 46.69134 ?  138 PRO B CA  1 
ATOM   2850 C C   . PRO B 1 158 ? -29.91900 1.52200   21.34600 1.000 43.79826 ?  138 PRO B C   1 
ATOM   2851 O O   . PRO B 1 158 ? -30.43500 2.58100   20.97200 1.000 50.49295 ?  138 PRO B O   1 
ATOM   2852 C CB  . PRO B 1 158 ? -27.88400 0.83100   20.04500 1.000 47.62308 ?  138 PRO B CB  1 
ATOM   2853 C CG  . PRO B 1 158 ? -26.89600 -0.19700  20.38900 1.000 48.07518 ?  138 PRO B CG  1 
ATOM   2854 C CD  . PRO B 1 158 ? -26.95300 -0.51800  21.82500 1.000 43.10367 ?  138 PRO B CD  1 
ATOM   2855 N N   . GLN B 1 159 ? -30.65200 0.47800   21.73600 1.000 46.82170 ?  139 GLN B N   1 
ATOM   2856 C CA  . GLN B 1 159 ? -32.10800 0.49500   21.61700 1.000 40.29879 ?  139 GLN B CA  1 
ATOM   2857 C C   . GLN B 1 159 ? -32.76500 1.50900   22.54300 1.000 50.35847 ?  139 GLN B C   1 
ATOM   2858 O O   . GLN B 1 159 ? -33.90300 1.91600   22.28600 1.000 47.58867 ?  139 GLN B O   1 
ATOM   2859 C CB  . GLN B 1 159 ? -32.67400 -0.90200  21.90300 1.000 32.58654 ?  139 GLN B CB  1 
ATOM   2860 N N   . PHE B 1 160 ? -32.08000 1.92500   23.60900 1.000 43.76237 ?  140 PHE B N   1 
ATOM   2861 C CA  . PHE B 1 160 ? -32.65300 2.84600   24.58700 1.000 41.49531 ?  140 PHE B CA  1 
ATOM   2862 C C   . PHE B 1 160 ? -32.43600 4.26400   24.07400 1.000 41.35221 ?  140 PHE B C   1 
ATOM   2863 O O   . PHE B 1 160 ? -31.50500 4.97200   24.46100 1.000 37.39119 ?  140 PHE B O   1 
ATOM   2864 C CB  . PHE B 1 160 ? -32.03100 2.63300   25.96000 1.000 41.48112 ?  140 PHE B CB  1 
ATOM   2865 C CG  . PHE B 1 160 ? -32.42300 1.33500   26.60000 1.000 40.62059 ?  140 PHE B CG  1 
ATOM   2866 C CD1 . PHE B 1 160 ? -31.80000 0.15500   26.23300 1.000 42.65762 ?  140 PHE B CD1 1 
ATOM   2867 C CD2 . PHE B 1 160 ? -33.41800 1.29000   27.55700 1.000 37.97502 ?  140 PHE B CD2 1 
ATOM   2868 C CE1 . PHE B 1 160 ? -32.16400 -1.04800  26.81000 1.000 40.90137 ?  140 PHE B CE1 1 
ATOM   2869 C CE2 . PHE B 1 160 ? -33.78500 0.09100   28.14000 1.000 39.53299 ?  140 PHE B CE2 1 
ATOM   2870 C CZ  . PHE B 1 160 ? -33.15400 -1.07700  27.77000 1.000 39.61134 ?  140 PHE B CZ  1 
ATOM   2871 N N   . LYS B 1 161 ? -33.32800 4.68200   23.18200 1.000 40.18545 ?  141 LYS B N   1 
ATOM   2872 C CA  . LYS B 1 161 ? -33.20400 5.95700   22.49800 1.000 40.28773 ?  141 LYS B CA  1 
ATOM   2873 C C   . LYS B 1 161 ? -34.59000 6.55300   22.30900 1.000 36.87601 ?  141 LYS B C   1 
ATOM   2874 O O   . LYS B 1 161 ? -35.60300 5.95600   22.68500 1.000 39.67623 ?  141 LYS B O   1 
ATOM   2875 C CB  . LYS B 1 161 ? -32.49800 5.78600   21.14800 1.000 44.57759 ?  141 LYS B CB  1 
ATOM   2876 C CG  . LYS B 1 161 ? -33.22100 4.83800   20.20100 1.000 41.55938 ?  141 LYS B CG  1 
ATOM   2877 C CD  . LYS B 1 161 ? -32.52800 4.76000   18.85100 1.000 39.77353 ?  141 LYS B CD  1 
ATOM   2878 C CE  . LYS B 1 161 ? -33.34600 3.94900   17.85900 1.000 48.98048 ?  141 LYS B CE  1 
ATOM   2879 N N   . GLU B 1 162 ? -34.62300 7.74500   21.71900 1.000 39.25322 ?  142 GLU B N   1 
ATOM   2880 C CA  . GLU B 1 162 ? -35.86300 8.39000   21.29400 1.000 49.87948 ?  142 GLU B CA  1 
ATOM   2881 C C   . GLU B 1 162 ? -36.83800 8.54500   22.45800 1.000 42.29528 ?  142 GLU B C   1 
ATOM   2882 O O   . GLU B 1 162 ? -38.02600 8.22500   22.36200 1.000 39.75947 ?  142 GLU B O   1 
ATOM   2883 C CB  . GLU B 1 162 ? -36.50600 7.62300   20.13700 1.000 45.34821 ?  142 GLU B CB  1 
ATOM   2884 C CG  . GLU B 1 162 ? -35.74000 7.74500   18.82700 1.000 47.82984 ?  142 GLU B CG  1 
ATOM   2885 C CD  . GLU B 1 162 ? -36.25000 6.79200   17.76600 1.000 53.42579 ?  142 GLU B CD  1 
ATOM   2886 O OE1 . GLU B 1 162 ? -37.39300 6.30800   17.90100 1.000 67.28851 ?  142 GLU B OE1 1 
ATOM   2887 O OE2 . GLU B 1 162 ? -35.51000 6.53200   16.79300 1.000 63.96973 -1 142 GLU B OE2 1 
ATOM   2888 N N   . TYR B 1 163 ? -36.31800 9.03600   23.57700 1.000 34.52923 ?  143 TYR B N   1 
ATOM   2889 C CA  . TYR B 1 163 ? -37.12800 9.28900   24.75700 1.000 36.95850 ?  143 TYR B CA  1 
ATOM   2890 C C   . TYR B 1 163 ? -37.57300 10.74300  24.76800 1.000 36.24173 ?  143 TYR B C   1 
ATOM   2891 O O   . TYR B 1 163 ? -36.81200 11.64000  24.39700 1.000 35.03237 ?  143 TYR B O   1 
ATOM   2892 C CB  . TYR B 1 163 ? -36.34900 8.96600   26.03300 1.000 34.08570 ?  143 TYR B CB  1 
ATOM   2893 C CG  . TYR B 1 163 ? -36.12100 7.49300   26.21200 1.000 34.43535 ?  143 TYR B CG  1 
ATOM   2894 C CD1 . TYR B 1 163 ? -37.17800 6.63900   26.50100 1.000 34.63857 ?  143 TYR B CD1 1 
ATOM   2895 C CD2 . TYR B 1 163 ? -34.85500 6.94400   26.05900 1.000 32.20838 ?  143 TYR B CD2 1 
ATOM   2896 C CE1 . TYR B 1 163 ? -36.97400 5.28600   26.65400 1.000 32.82096 ?  143 TYR B CE1 1 
ATOM   2897 C CE2 . TYR B 1 163 ? -34.64600 5.59100   26.20800 1.000 33.64495 ?  143 TYR B CE2 1 
ATOM   2898 C CZ  . TYR B 1 163 ? -35.70900 4.76700   26.50400 1.000 31.99146 ?  143 TYR B CZ  1 
ATOM   2899 O OH  . TYR B 1 163 ? -35.50400 3.41500   26.65600 1.000 37.91241 ?  143 TYR B OH  1 
ATOM   2900 N N   . ASP B 1 164 ? -38.82100 10.96900  25.17200 1.000 38.30975 ?  144 ASP B N   1 
ATOM   2901 C CA  . ASP B 1 164 ? -39.26000 12.33000  25.44800 1.000 34.33530 ?  144 ASP B CA  1 
ATOM   2902 C C   . ASP B 1 164 ? -38.82900 12.76700  26.83700 1.000 37.55021 ?  144 ASP B C   1 
ATOM   2903 O O   . ASP B 1 164 ? -38.68500 13.96800  27.09500 1.000 36.70291 ?  144 ASP B O   1 
ATOM   2904 C CB  . ASP B 1 164 ? -40.77800 12.43800  25.31400 1.000 40.89705 ?  144 ASP B CB  1 
ATOM   2905 C CG  . ASP B 1 164 ? -41.28600 11.88600  24.00000 1.000 41.63625 ?  144 ASP B CG  1 
ATOM   2906 O OD1 . ASP B 1 164 ? -40.86900 12.38900  22.93200 1.000 40.30523 ?  144 ASP B OD1 1 
ATOM   2907 O OD2 . ASP B 1 164 ? -42.10700 10.94500  24.03900 1.000 44.39239 -1 144 ASP B OD2 1 
ATOM   2908 N N   . LEU B 1 165 ? -38.61400 11.80700  27.73300 1.000 33.78740 ?  145 LEU B N   1 
ATOM   2909 C CA  . LEU B 1 165 ? -38.21100 12.09000  29.09900 1.000 33.52534 ?  145 LEU B CA  1 
ATOM   2910 C C   . LEU B 1 165 ? -37.19700 11.05200  29.54100 1.000 31.61923 ?  145 LEU B C   1 
ATOM   2911 O O   . LEU B 1 165 ? -37.43300 9.84900   29.39600 1.000 36.78333 ?  145 LEU B O   1 
ATOM   2912 C CB  . LEU B 1 165 ? -39.41600 12.08300  30.04500 1.000 33.04507 ?  145 LEU B CB  1 
ATOM   2913 C CG  . LEU B 1 165 ? -39.06200 11.94300  31.52200 1.000 30.80895 ?  145 LEU B CG  1 
ATOM   2914 C CD1 . LEU B 1 165 ? -38.41600 13.23100  31.99500 1.000 30.71582 ?  145 LEU B CD1 1 
ATOM   2915 C CD2 . LEU B 1 165 ? -40.29400 11.63100  32.34500 1.000 26.47485 ?  145 LEU B CD2 1 
ATOM   2916 N N   . ILE B 1 166 ? -36.06900 11.51500  30.06600 1.000 26.49911 ?  146 ILE B N   1 
ATOM   2917 C CA  . ILE B 1 166 ? -35.12700 10.66000  30.77200 1.000 34.26139 ?  146 ILE B CA  1 
ATOM   2918 C C   . ILE B 1 166 ? -35.02300 11.18500  32.19700 1.000 31.24136 ?  146 ILE B C   1 
ATOM   2919 O O   . ILE B 1 166 ? -34.63400 12.33900  32.41200 1.000 36.30104 ?  146 ILE B O   1 
ATOM   2920 C CB  . ILE B 1 166 ? -33.75400 10.61700  30.08300 1.000 31.15154 ?  146 ILE B CB  1 
ATOM   2921 C CG1 . ILE B 1 166 ? -33.92100 10.09800  28.64700 1.000 33.09634 ?  146 ILE B CG1 1 
ATOM   2922 C CG2 . ILE B 1 166 ? -32.78200 9.75200   30.89300 1.000 25.13626 ?  146 ILE B CG2 1 
ATOM   2923 C CD1 . ILE B 1 166 ? -32.66600 9.56700   28.00300 1.000 30.70609 ?  146 ILE B CD1 1 
ATOM   2924 N N   . MET B 1 167 ? -35.41100 10.35700  33.16000 1.000 32.33388 ?  147 MET B N   1 
ATOM   2925 C CA  . MET B 1 167 ? -35.34400 10.69900  34.57300 1.000 34.15663 ?  147 MET B CA  1 
ATOM   2926 C C   . MET B 1 167 ? -34.26100 9.84800   35.21800 1.000 35.52453 ?  147 MET B C   1 
ATOM   2927 O O   . MET B 1 167 ? -34.28900 8.61900   35.11400 1.000 35.92329 ?  147 MET B O   1 
ATOM   2928 C CB  . MET B 1 167 ? -36.69200 10.48000  35.26000 1.000 36.65124 ?  147 MET B CB  1 
ATOM   2929 C CG  . MET B 1 167 ? -36.84100 11.24300  36.57400 1.000 42.49641 ?  147 MET B CG  1 
ATOM   2930 S SD  . MET B 1 167 ? -38.53100 11.30100  37.22000 1.000 51.34372 ?  147 MET B SD  1 
ATOM   2931 C CE  . MET B 1 167 ? -38.69500 9.65600   37.91700 1.000 44.49894 ?  147 MET B CE  1 
ATOM   2932 N N   . ALA B 1 168 ? -33.30200 10.50200  35.86500 1.000 37.65911 ?  148 ALA B N   1 
ATOM   2933 C CA  . ALA B 1 168 ? -32.24300 9.83200   36.61300 1.000 35.35618 ?  148 ALA B CA  1 
ATOM   2934 C C   . ALA B 1 168 ? -32.33300 10.31400  38.05500 1.000 36.58145 ?  148 ALA B C   1 
ATOM   2935 O O   . ALA B 1 168 ? -31.93100 11.44100  38.36600 1.000 30.78028 ?  148 ALA B O   1 
ATOM   2936 C CB  . ALA B 1 168 ? -30.86900 10.12100  36.01100 1.000 35.08862 ?  148 ALA B CB  1 
ATOM   2937 N N   . THR B 1 169 ? -32.85900 9.46100   38.92800 1.000 39.13698 ?  149 THR B N   1 
ATOM   2938 C CA  . THR B 1 169 ? -33.23200 9.84000   40.28400 1.000 38.47275 ?  149 THR B CA  1 
ATOM   2939 C C   . THR B 1 169 ? -32.15000 9.40800   41.26700 1.000 32.39305 ?  149 THR B C   1 
ATOM   2940 O O   . THR B 1 169 ? -31.83600 8.21500   41.36600 1.000 33.09916 ?  149 THR B O   1 
ATOM   2941 C CB  . THR B 1 169 ? -34.58100 9.21700   40.64800 1.000 39.80048 ?  149 THR B CB  1 
ATOM   2942 O OG1 . THR B 1 169 ? -35.63400 10.02700  40.11200 1.000 51.11055 ?  149 THR B OG1 1 
ATOM   2943 C CG2 . THR B 1 169 ? -34.74200 9.10700   42.14800 1.000 41.00586 ?  149 THR B CG2 1 
ATOM   2944 N N   . ASN B 1 170 ? -31.59300 10.38200  41.99500 1.000 31.95675 ?  150 ASN B N   1 
ATOM   2945 C CA  . ASN B 1 170 ? -30.56500 10.14800  43.01800 1.000 34.00692 ?  150 ASN B CA  1 
ATOM   2946 C C   . ASN B 1 170 ? -29.46100 9.23100   42.49900 1.000 31.78065 ?  150 ASN B C   1 
ATOM   2947 O O   . ASN B 1 170 ? -29.05400 8.26900   43.15300 1.000 37.66830 ?  150 ASN B O   1 
ATOM   2948 C CB  . ASN B 1 170 ? -31.18400 9.58800   44.30100 1.000 33.66458 ?  150 ASN B CB  1 
ATOM   2949 C CG  . ASN B 1 170 ? -32.08800 10.58800  44.99900 1.000 35.61636 ?  150 ASN B CG  1 
ATOM   2950 O OD1 . ASN B 1 170 ? -32.02000 11.79100  44.74400 1.000 34.01324 ?  150 ASN B OD1 1 
ATOM   2951 N ND2 . ASN B 1 170 ? -32.93900 10.09300  45.88600 1.000 34.46200 ?  150 ASN B ND2 1 
ATOM   2952 N N   . LEU B 1 171 ? -28.96600 9.54300   41.31000 1.000 35.49749 ?  151 LEU B N   1 
ATOM   2953 C CA  . LEU B 1 171 ? -28.04800 8.64500   40.62100 1.000 36.10494 ?  151 LEU B CA  1 
ATOM   2954 C C   . LEU B 1 171 ? -26.66700 9.23400   40.37900 1.000 30.67418 ?  151 LEU B C   1 
ATOM   2955 O O   . LEU B 1 171 ? -25.67400 8.51600   40.51700 1.000 35.05026 ?  151 LEU B O   1 
ATOM   2956 C CB  . LEU B 1 171 ? -28.65600 8.20700   39.28100 1.000 33.15174 ?  151 LEU B CB  1 
ATOM   2957 C CG  . LEU B 1 171 ? -27.78800 7.31200   38.39700 1.000 38.75235 ?  151 LEU B CG  1 
ATOM   2958 C CD1 . LEU B 1 171 ? -27.74000 5.90100   38.95500 1.000 34.63465 ?  151 LEU B CD1 1 
ATOM   2959 C CD2 . LEU B 1 171 ? -28.31700 7.31000   36.97600 1.000 37.49286 ?  151 LEU B CD2 1 
ATOM   2960 N N   . ILE B 1 172 ? -26.56700 10.51800  40.02100 1.000 28.27067 ?  152 ILE B N   1 
ATOM   2961 C CA  . ILE B 1 172 ? -25.27700 11.05700  39.58900 1.000 28.93609 ?  152 ILE B CA  1 
ATOM   2962 C C   . ILE B 1 172 ? -24.24700 10.96500  40.70800 1.000 31.70410 ?  152 ILE B C   1 
ATOM   2963 O O   . ILE B 1 172 ? -23.06200 10.70900  40.45500 1.000 29.22216 ?  152 ILE B O   1 
ATOM   2964 C CB  . ILE B 1 172 ? -25.42700 12.50000  39.06500 1.000 31.35791 ?  152 ILE B CB  1 
ATOM   2965 C CG1 . ILE B 1 172 ? -26.06800 13.40500  40.11500 1.000 29.65449 ?  152 ILE B CG1 1 
ATOM   2966 C CG2 . ILE B 1 172 ? -26.19300 12.52200  37.74700 1.000 26.50581 ?  152 ILE B CG2 1 
ATOM   2967 C CD1 . ILE B 1 172 ? -25.60500 14.84200  40.01900 1.000 30.76753 ?  152 ILE B CD1 1 
ATOM   2968 N N   . ASP B 1 173 ? -24.67400 11.14900  41.96300 1.000 29.63266 ?  153 ASP B N   1 
ATOM   2969 C CA  . ASP B 1 173 ? -23.74700 11.06100  43.08400 1.000 32.05400 ?  153 ASP B CA  1 
ATOM   2970 C C   . ASP B 1 173 ? -23.51700 9.62400   43.54100 1.000 33.64922 ?  153 ASP B C   1 
ATOM   2971 O O   . ASP B 1 173 ? -22.98500 9.39800   44.63900 1.000 34.35915 ?  153 ASP B O   1 
ATOM   2972 C CB  . ASP B 1 173 ? -24.21700 11.93300  44.25700 1.000 31.85206 ?  153 ASP B CB  1 
ATOM   2973 C CG  . ASP B 1 173 ? -25.66600 11.68300  44.64400 1.000 38.11944 ?  153 ASP B CG  1 
ATOM   2974 O OD1 . ASP B 1 173 ? -26.48700 11.30900  43.77700 1.000 39.13978 ?  153 ASP B OD1 1 
ATOM   2975 O OD2 . ASP B 1 173 ? -25.98000 11.86100  45.83600 1.000 41.08489 -1 153 ASP B OD2 1 
ATOM   2976 N N   . ARG B 1 174 ? -23.89800 8.65300   42.71200 1.000 34.57073 ?  154 ARG B N   1 
ATOM   2977 C CA  . ARG B 1 174 ? -23.56100 7.25400   42.93000 1.000 35.33451 ?  154 ARG B CA  1 
ATOM   2978 C C   . ARG B 1 174 ? -22.77600 6.67600   41.76100 1.000 32.34488 ?  154 ARG B C   1 
ATOM   2979 O O   . ARG B 1 174 ? -22.50800 5.46900   41.74100 1.000 36.47714 ?  154 ARG B O   1 
ATOM   2980 C CB  . ARG B 1 174 ? -24.83100 6.43700   43.19100 1.000 35.49073 ?  154 ARG B CB  1 
ATOM   2981 C CG  . ARG B 1 174 ? -25.61100 6.89600   44.42700 1.000 32.26450 ?  154 ARG B CG  1 
ATOM   2982 N N   . LEU B 1 175 ? -22.38700 7.50900   40.79900 1.000 28.65023 ?  155 LEU B N   1 
ATOM   2983 C CA  . LEU B 1 175 ? -21.62500 7.08700   39.63000 1.000 30.31230 ?  155 LEU B CA  1 
ATOM   2984 C C   . LEU B 1 175 ? -20.15000 7.42200   39.81000 1.000 30.97070 ?  155 LEU B C   1 
ATOM   2985 O O   . LEU B 1 175 ? -19.80600 8.49100   40.32200 1.000 33.60655 ?  155 LEU B O   1 
ATOM   2986 C CB  . LEU B 1 175 ? -22.14800 7.77000   38.36700 1.000 28.74299 ?  155 LEU B CB  1 
ATOM   2987 C CG  . LEU B 1 175 ? -23.62000 7.52400   38.06400 1.000 33.80247 ?  155 LEU B CG  1 
ATOM   2988 C CD1 . LEU B 1 175 ? -24.00900 8.23100   36.78500 1.000 29.59434 ?  155 LEU B CD1 1 
ATOM   2989 C CD2 . LEU B 1 175 ? -23.88300 6.02900   37.96900 1.000 29.08256 ?  155 LEU B CD2 1 
ATOM   2990 N N   . TYR B 1 176 ? -19.27600 6.51600   39.36500 1.000 27.57721 ?  156 TYR B N   1 
ATOM   2991 C CA  . TYR B 1 176 ? -17.84800 6.77900   39.50300 1.000 32.19667 ?  156 TYR B CA  1 
ATOM   2992 C C   . TYR B 1 176 ? -17.42000 7.97900   38.66500 1.000 30.89407 ?  156 TYR B C   1 
ATOM   2993 O O   . TYR B 1 176 ? -16.60200 8.78900   39.11200 1.000 31.44652 ?  156 TYR B O   1 
ATOM   2994 C CB  . TYR B 1 176 ? -17.02700 5.54400   39.12700 1.000 29.52988 ?  156 TYR B CB  1 
ATOM   2995 C CG  . TYR B 1 176 ? -15.54500 5.78000   39.32000 1.000 33.72653 ?  156 TYR B CG  1 
ATOM   2996 C CD1 . TYR B 1 176 ? -14.98300 5.80100   40.59500 1.000 29.16539 ?  156 TYR B CD1 1 
ATOM   2997 C CD2 . TYR B 1 176 ? -14.71500 6.02900   38.23400 1.000 31.47515 ?  156 TYR B CD2 1 
ATOM   2998 C CE1 . TYR B 1 176 ? -13.63400 6.04100   40.77600 1.000 27.13409 ?  156 TYR B CE1 1 
ATOM   2999 C CE2 . TYR B 1 176 ? -13.36500 6.26300   38.40600 1.000 33.56954 ?  156 TYR B CE2 1 
ATOM   3000 C CZ  . TYR B 1 176 ? -12.83100 6.27000   39.67800 1.000 30.83309 ?  156 TYR B CZ  1 
ATOM   3001 O OH  . TYR B 1 176 ? -11.48400 6.51000   39.84000 1.000 35.67756 ?  156 TYR B OH  1 
ATOM   3002 N N   . GLU B 1 177 ? -17.95700 8.11000   37.45200 1.000 28.34546 ?  157 GLU B N   1 
ATOM   3003 C CA  . GLU B 1 177 ? -17.65800 9.23900   36.56600 1.000 26.39283 ?  157 GLU B CA  1 
ATOM   3004 C C   . GLU B 1 177 ? -18.96900 9.73700   35.97800 1.000 26.56661 ?  157 GLU B C   1 
ATOM   3005 O O   . GLU B 1 177 ? -19.31300 9.42500   34.83100 1.000 32.62356 ?  157 GLU B O   1 
ATOM   3006 C CB  . GLU B 1 177 ? -16.67100 8.82900   35.46500 1.000 31.71169 ?  157 GLU B CB  1 
ATOM   3007 C CG  . GLU B 1 177 ? -16.13700 9.97700   34.60800 1.000 30.29625 ?  157 GLU B CG  1 
ATOM   3008 C CD  . GLU B 1 177 ? -15.12600 9.51200   33.56400 1.000 39.23837 ?  157 GLU B CD  1 
ATOM   3009 O OE1 . GLU B 1 177 ? -14.67000 8.35300   33.64800 1.000 39.08451 ?  157 GLU B OE1 1 
ATOM   3010 O OE2 . GLU B 1 177 ? -14.79200 10.30200  32.65600 1.000 45.85849 -1 157 GLU B OE2 1 
ATOM   3011 N N   . PRO B 1 178 ? -19.73800 10.51900  36.74300 1.000 29.38620 ?  158 PRO B N   1 
ATOM   3012 C CA  . PRO B 1 178 ? -21.08000 10.91600  36.27800 1.000 28.56158 ?  158 PRO B CA  1 
ATOM   3013 C C   . PRO B 1 178 ? -21.07500 11.67800  34.97000 1.000 31.76450 ?  158 PRO B C   1 
ATOM   3014 O O   . PRO B 1 178 ? -22.08800 11.67000  34.25900 1.000 30.63718 ?  158 PRO B O   1 
ATOM   3015 C CB  . PRO B 1 178 ? -21.61300 11.79100  37.42400 1.000 30.41349 ?  158 PRO B CB  1 
ATOM   3016 C CG  . PRO B 1 178 ? -20.40900 12.20800  38.19800 1.000 29.35833 ?  158 PRO B CG  1 
ATOM   3017 C CD  . PRO B 1 178 ? -19.42600 11.07900  38.07000 1.000 29.83676 ?  158 PRO B CD  1 
ATOM   3018 N N   . ARG B 1 179 ? -19.94500 12.22000  34.54900 1.000 34.14508 ?  159 ARG B N   1 
ATOM   3019 C CA  . ARG B 1 179 ? -19.92000 13.02000  33.30000 1.000 35.66669 ?  159 ARG B CA  1 
ATOM   3020 C C   . ARG B 1 179 ? -20.06200 12.08200  32.09200 1.000 35.16036 ?  159 ARG B C   1 
ATOM   3021 O O   . ARG B 1 179 ? -20.62100 12.51500  31.09000 1.000 38.46906 ?  159 ARG B O   1 
ATOM   3022 C CB  . ARG B 1 179 ? -18.66600 13.90100  33.25600 1.000 37.17387 ?  159 ARG B CB  1 
ATOM   3023 C CG  . ARG B 1 179 ? -18.43600 14.63600  31.94700 1.000 42.00854 ?  159 ARG B CG  1 
ATOM   3024 C CD  . ARG B 1 179 ? -17.01700 15.16000  31.90200 1.000 43.58618 ?  159 ARG B CD  1 
ATOM   3025 N NE  . ARG B 1 179 ? -16.79100 16.17300  32.92000 1.000 53.66139 ?  159 ARG B NE  1 
ATOM   3026 C CZ  . ARG B 1 179 ? -17.04400 17.46700  32.76700 1.000 58.47387 ?  159 ARG B CZ  1 
ATOM   3027 N NH1 . ARG B 1 179 ? -17.39600 17.93900  31.58500 1.000 44.85597 ?  159 ARG B NH1 1 
ATOM   3028 N NH2 . ARG B 1 179 ? -16.94300 18.28600  33.79900 1.000 50.51800 ?  159 ARG B NH2 1 
ATOM   3029 N N   . LEU B 1 180 ? -19.62100 10.83100  32.21700 1.000 32.69927 ?  160 LEU B N   1 
ATOM   3030 C CA  . LEU B 1 180 ? -19.71700 9.84500   31.11200 1.000 34.51163 ?  160 LEU B CA  1 
ATOM   3031 C C   . LEU B 1 180 ? -21.17700 9.73500   30.67900 1.000 35.27683 ?  160 LEU B C   1 
ATOM   3032 O O   . LEU B 1 180 ? -21.42700 9.71800   29.47600 1.000 39.63065 ?  160 LEU B O   1 
ATOM   3033 C CB  . LEU B 1 180 ? -19.17000 8.49900   31.59400 1.000 35.51907 ?  160 LEU B CB  1 
ATOM   3034 C CG  . LEU B 1 180 ? -18.96200 7.41900   30.53800 1.000 39.02464 ?  160 LEU B CG  1 
ATOM   3035 C CD1 . LEU B 1 180 ? -18.14800 7.95200   29.37400 1.000 43.01520 ?  160 LEU B CD1 1 
ATOM   3036 C CD2 . LEU B 1 180 ? -18.27500 6.21200   31.14900 1.000 38.99193 ?  160 LEU B CD2 1 
ATOM   3037 N N   . PHE B 1 181 ? -22.08700 9.70000   31.64300 1.000 40.06678 ?  161 PHE B N   1 
ATOM   3038 C CA  . PHE B 1 181 ? -23.53900 9.61000   31.34600 1.000 38.80846 ?  161 PHE B CA  1 
ATOM   3039 C C   . PHE B 1 181 ? -24.08500 10.95800  30.88100 1.000 32.44076 ?  161 PHE B C   1 
ATOM   3040 O O   . PHE B 1 181 ? -24.76600 10.99100  29.86000 1.000 36.99039 ?  161 PHE B O   1 
ATOM   3041 C CB  . PHE B 1 181 ? -24.25800 9.09100   32.59200 1.000 30.75831 ?  161 PHE B CB  1 
ATOM   3042 C CG  . PHE B 1 181 ? -25.64700 9.60800   32.85900 1.000 37.79048 ?  161 PHE B CG  1 
ATOM   3043 C CD1 . PHE B 1 181 ? -26.70800 9.26500   32.03900 1.000 34.45262 ?  161 PHE B CD1 1 
ATOM   3044 C CD2 . PHE B 1 181 ? -25.90000 10.39600  33.96800 1.000 36.04356 ?  161 PHE B CD2 1 
ATOM   3045 C CE1 . PHE B 1 181 ? -27.98300 9.73400   32.30200 1.000 34.68194 ?  161 PHE B CE1 1 
ATOM   3046 C CE2 . PHE B 1 181 ? -27.17800 10.85700  34.23500 1.000 33.79894 ?  161 PHE B CE2 1 
ATOM   3047 C CZ  . PHE B 1 181 ? -28.21600 10.52800  33.39900 1.000 40.87083 ?  161 PHE B CZ  1 
ATOM   3048 N N   . LEU B 1 182 ? -23.73200 12.03200  31.57200 1.000 38.60966 ?  162 LEU B N   1 
ATOM   3049 C CA  . LEU B 1 182 ? -24.33700 13.35900  31.29500 1.000 33.79649 ?  162 LEU B CA  1 
ATOM   3050 C C   . LEU B 1 182 ? -23.92300 13.94700  29.94300 1.000 36.10076 ?  162 LEU B C   1 
ATOM   3051 O O   . LEU B 1 182 ? -24.78400 14.54100  29.30100 1.000 39.62374 ?  162 LEU B O   1 
ATOM   3052 C CB  . LEU B 1 182 ? -23.96200 14.28100  32.45500 1.000 28.10267 ?  162 LEU B CB  1 
ATOM   3053 C CG  . LEU B 1 182 ? -24.68900 13.99400  33.76400 1.000 36.83689 ?  162 LEU B CG  1 
ATOM   3054 C CD1 . LEU B 1 182 ? -24.10500 14.82300  34.88900 1.000 33.68112 ?  162 LEU B CD1 1 
ATOM   3055 C CD2 . LEU B 1 182 ? -26.17700 14.26200  33.62400 1.000 30.16356 ?  162 LEU B CD2 1 
ATOM   3056 N N   . GLU B 1 183 ? -22.68300 13.75900  29.51800 1.000 35.54345 ?  163 GLU B N   1 
ATOM   3057 C CA  . GLU B 1 183 ? -22.18600 14.40900  28.27500 1.000 44.06038 ?  163 GLU B CA  1 
ATOM   3058 C C   . GLU B 1 183 ? -22.74100 13.73200  27.01500 1.000 42.65130 ?  163 GLU B C   1 
ATOM   3059 O O   . GLU B 1 183 ? -22.55700 14.29300  25.94000 1.000 42.36336 ?  163 GLU B O   1 
ATOM   3060 C CB  . GLU B 1 183 ? -20.65400 14.43500  28.27500 1.000 43.95446 ?  163 GLU B CB  1 
ATOM   3061 C CG  . GLU B 1 183 ? -20.00500 13.08900  28.02700 1.000 45.17949 ?  163 GLU B CG  1 
ATOM   3062 C CD  . GLU B 1 183 ? -18.55400 13.02300  28.47100 1.000 54.86342 ?  163 GLU B CD  1 
ATOM   3063 O OE1 . GLU B 1 183 ? -17.91800 14.08900  28.55400 1.000 50.27586 ?  163 GLU B OE1 1 
ATOM   3064 O OE2 . GLU B 1 183 ? -18.06400 11.91000  28.73000 1.000 50.89044 -1 163 GLU B OE2 1 
ATOM   3065 N N   . ASN B 1 184 ? -23.41500 12.59700  27.16000 1.000 40.78392 ?  164 ASN B N   1 
ATOM   3066 C CA  . ASN B 1 184 ? -23.89400 11.83800  25.98200 1.000 41.05334 ?  164 ASN B CA  1 
ATOM   3067 C C   . ASN B 1 184 ? -25.40100 11.57700  26.07000 1.000 37.13191 ?  164 ASN B C   1 
ATOM   3068 O O   . ASN B 1 184 ? -25.94200 11.04300  25.10700 1.000 41.60414 ?  164 ASN B O   1 
ATOM   3069 C CB  . ASN B 1 184 ? -23.12500 10.52600  25.85300 1.000 39.91491 ?  164 ASN B CB  1 
ATOM   3070 C CG  . ASN B 1 184 ? -21.64300 10.71100  25.61600 1.000 52.34971 ?  164 ASN B CG  1 
ATOM   3071 O OD1 . ASN B 1 184 ? -21.24200 11.37700  24.66600 1.000 56.83087 ?  164 ASN B OD1 1 
ATOM   3072 N ND2 . ASN B 1 184 ? -20.82600 10.11800  26.47000 1.000 44.79995 ?  164 ASN B ND2 1 
ATOM   3073 N N   . ILE B 1 185 ? -26.05300 11.96400  27.16200 1.000 34.91483 ?  165 ILE B N   1 
ATOM   3074 C CA  . ILE B 1 185 ? -27.49500 11.61300  27.34400 1.000 35.69210 ?  165 ILE B CA  1 
ATOM   3075 C C   . ILE B 1 185 ? -28.36800 12.35100  26.31600 1.000 31.93329 ?  165 ILE B C   1 
ATOM   3076 O O   . ILE B 1 185 ? -29.40600 11.81300  25.94200 1.000 36.14399 ?  165 ILE B O   1 
ATOM   3077 C CB  . ILE B 1 185 ? -27.95100 11.84800  28.79700 1.000 30.82770 ?  165 ILE B CB  1 
ATOM   3078 C CG1 . ILE B 1 185 ? -29.20600 11.03700  29.12600 1.000 33.17853 ?  165 ILE B CG1 1 
ATOM   3079 C CG2 . ILE B 1 185 ? -28.13300 13.32700  29.09100 1.000 33.96531 ?  165 ILE B CG2 1 
ATOM   3080 C CD1 . ILE B 1 185 ? -29.10100 9.58400   28.73800 1.000 33.02356 ?  165 ILE B CD1 1 
ATOM   3081 N N   . HIS B 1 186 ? -27.93300 13.52300  25.86000 1.000 37.17610 ?  166 HIS B N   1 
ATOM   3082 C CA  . HIS B 1 186 ? -28.74300 14.26100  24.88900 1.000 36.62115 ?  166 HIS B CA  1 
ATOM   3083 C C   . HIS B 1 186 ? -29.01900 13.43300  23.64000 1.000 40.75460 ?  166 HIS B C   1 
ATOM   3084 O O   . HIS B 1 186 ? -30.04300 13.63300  22.97700 1.000 38.56315 ?  166 HIS B O   1 
ATOM   3085 C CB  . HIS B 1 186 ? -28.04200 15.56300  24.50100 1.000 35.94439 ?  166 HIS B CB  1 
ATOM   3086 C CG  . HIS B 1 186 ? -26.72400 15.35100  23.82500 1.000 43.79438 ?  166 HIS B CG  1 
ATOM   3087 N ND1 . HIS B 1 186 ? -25.57800 15.02700  24.51900 1.000 43.15088 ?  166 HIS B ND1 1 
ATOM   3088 C CD2 . HIS B 1 186 ? -26.37400 15.39000  22.51700 1.000 40.66808 ?  166 HIS B CD2 1 
ATOM   3089 C CE1 . HIS B 1 186 ? -24.57600 14.88500  23.66800 1.000 39.22478 ?  166 HIS B CE1 1 
ATOM   3090 N NE2 . HIS B 1 186 ? -25.03300 15.10000  22.44700 1.000 41.30959 ?  166 HIS B NE2 1 
ATOM   3091 N N   . LYS B 1 187 ? -28.11800 12.50500  23.30400 1.000 37.41770 ?  167 LYS B N   1 
ATOM   3092 C CA  . LYS B 1 187 ? -28.29100 11.66100  22.12800 1.000 36.85658 ?  167 LYS B CA  1 
ATOM   3093 C C   . LYS B 1 187 ? -29.49700 10.73800  22.24000 1.000 38.12516 ?  167 LYS B C   1 
ATOM   3094 O O   . LYS B 1 187 ? -30.02900 10.31200  21.20900 1.000 37.07724 ?  167 LYS B O   1 
ATOM   3095 C CB  . LYS B 1 187 ? -27.02000 10.83900  21.89300 1.000 35.12070 ?  167 LYS B CB  1 
ATOM   3096 C CG  . LYS B 1 187 ? -25.75400 11.67300  21.82600 1.000 36.63669 ?  167 LYS B CG  1 
ATOM   3097 C CD  . LYS B 1 187 ? -24.62500 10.92900  21.13300 1.000 53.36243 ?  167 LYS B CD  1 
ATOM   3098 C CE  . LYS B 1 187 ? -23.27400 11.33000  21.70200 1.000 49.17894 ?  167 LYS B CE  1 
ATOM   3099 N NZ  . LYS B 1 187 ? -22.30600 10.20600  21.66800 1.000 57.12015 ?  167 LYS B NZ  1 
ATOM   3100 N N   . ARG B 1 188 ? -29.93700 10.41800  23.45500 1.000 35.59957 ?  168 ARG B N   1 
ATOM   3101 C CA  . ARG B 1 188 ? -31.03800 9.49200   23.65800 1.000 36.88669 ?  168 ARG B CA  1 
ATOM   3102 C C   . ARG B 1 188 ? -32.38700 10.18800  23.80400 1.000 35.76488 ?  168 ARG B C   1 
ATOM   3103 O O   . ARG B 1 188 ? -33.40100 9.51200   23.99700 1.000 38.71426 ?  168 ARG B O   1 
ATOM   3104 C CB  . ARG B 1 188 ? -30.75200 8.64100   24.89200 1.000 39.38809 ?  168 ARG B CB  1 
ATOM   3105 C CG  . ARG B 1 188 ? -29.31100 8.18000   24.97400 1.000 36.03998 ?  168 ARG B CG  1 
ATOM   3106 C CD  . ARG B 1 188 ? -29.14100 6.87600   24.24000 1.000 44.30548 ?  168 ARG B CD  1 
ATOM   3107 N NE  . ARG B 1 188 ? -27.90700 6.18400   24.57900 1.000 49.46226 ?  168 ARG B NE  1 
ATOM   3108 C CZ  . ARG B 1 188 ? -27.67800 4.90500   24.31700 1.000 50.58053 ?  168 ARG B CZ  1 
ATOM   3109 N NH1 . ARG B 1 188 ? -28.63600 4.10800   23.86900 1.000 46.50564 ?  168 ARG B NH1 1 
ATOM   3110 N NH2 . ARG B 1 188 ? -26.45800 4.41400   24.51000 1.000 46.92629 ?  168 ARG B NH2 1 
ATOM   3111 N N   . ILE B 1 189 ? -32.42600 11.51200  23.71600 1.000 36.57137 ?  169 ILE B N   1 
ATOM   3112 C CA  . ILE B 1 189 ? -33.63400 12.29000  23.96500 1.000 38.76552 ?  169 ILE B CA  1 
ATOM   3113 C C   . ILE B 1 189 ? -34.07000 12.96500  22.67400 1.000 43.98825 ?  169 ILE B C   1 
ATOM   3114 O O   . ILE B 1 189 ? -33.24600 13.53500  21.94900 1.000 45.72901 ?  169 ILE B O   1 
ATOM   3115 C CB  . ILE B 1 189 ? -33.42100 13.34500  25.06800 1.000 42.29709 ?  169 ILE B CB  1 
ATOM   3116 C CG1 . ILE B 1 189 ? -32.75400 12.72600  26.29800 1.000 40.32702 ?  169 ILE B CG1 1 
ATOM   3117 C CG2 . ILE B 1 189 ? -34.74000 14.00500  25.42800 1.000 39.30390 ?  169 ILE B CG2 1 
ATOM   3118 C CD1 . ILE B 1 189 ? -32.89600 13.57400  27.53900 1.000 37.06971 ?  169 ILE B CD1 1 
ATOM   3119 N N   . ASN B 1 190 ? -35.37200 12.92400  22.40600 1.000 38.57613 ?  170 ASN B N   1 
ATOM   3120 C CA  . ASN B 1 190 ? -35.91400 13.59600  21.23900 1.000 41.02805 ?  170 ASN B CA  1 
ATOM   3121 C C   . ASN B 1 190 ? -35.76200 15.10700  21.36900 1.000 45.34142 ?  170 ASN B C   1 
ATOM   3122 O O   . ASN B 1 190 ? -35.48300 15.65000  22.44300 1.000 40.46290 ?  170 ASN B O   1 
ATOM   3123 C CB  . ASN B 1 190 ? -37.38800 13.25100  21.05500 1.000 40.79226 ?  170 ASN B CB  1 
ATOM   3124 C CG  . ASN B 1 190 ? -37.60600 11.78900  20.81000 1.000 40.49509 ?  170 ASN B CG  1 
ATOM   3125 O OD1 . ASN B 1 190 ? -36.92200 11.18200  19.98700 1.000 44.55817 ?  170 ASN B OD1 1 
ATOM   3126 N ND2 . ASN B 1 190 ? -38.55700 11.20400  21.52600 1.000 41.12472 ?  170 ASN B ND2 1 
ATOM   3127 N N   . GLU B 1 191 ? -35.94900 15.78600  20.24000 1.000 47.37428 ?  171 GLU B N   1 
ATOM   3128 C CA  . GLU B 1 191 ? -36.00700 17.23900  20.24900 1.000 48.27659 ?  171 GLU B CA  1 
ATOM   3129 C C   . GLU B 1 191 ? -37.17300 17.69300  21.11700 1.000 41.78427 ?  171 GLU B C   1 
ATOM   3130 O O   . GLU B 1 191 ? -38.23300 17.06000  21.14200 1.000 41.16879 ?  171 GLU B O   1 
ATOM   3131 C CB  . GLU B 1 191 ? -36.16000 17.77400  18.82500 1.000 47.07031 ?  171 GLU B CB  1 
ATOM   3132 N N   . LYS B 1 192 ? -36.96100 18.78400  21.84900 1.000 47.35717 ?  172 LYS B N   1 
ATOM   3133 C CA  . LYS B 1 192 ? -37.89100 19.29200  22.85400 1.000 49.90969 ?  172 LYS B CA  1 
ATOM   3134 C C   . LYS B 1 192 ? -38.15300 18.28600  23.97200 1.000 38.73145 ?  172 LYS B C   1 
ATOM   3135 O O   . LYS B 1 192 ? -39.09500 18.46300  24.75200 1.000 44.57766 ?  172 LYS B O   1 
ATOM   3136 C CB  . LYS B 1 192 ? -39.21900 19.73600  22.22100 1.000 43.85045 ?  172 LYS B CB  1 
ATOM   3137 N N   . GLY B 1 193 ? -37.34900 17.22800  24.06900 1.000 37.67566 ?  173 GLY B N   1 
ATOM   3138 C CA  . GLY B 1 193 ? -37.43400 16.30300  25.17600 1.000 33.17648 ?  173 GLY B CA  1 
ATOM   3139 C C   . GLY B 1 193 ? -36.76500 16.86200  26.41600 1.000 32.54969 ?  173 GLY B C   1 
ATOM   3140 O O   . GLY B 1 193 ? -36.18200 17.94500  26.41200 1.000 36.84608 ?  173 GLY B O   1 
ATOM   3141 N N   . TYR B 1 194 ? -36.85100 16.09900  27.50300 1.000 32.08333 ?  174 TYR B N   1 
ATOM   3142 C CA  . TYR B 1 194 ? -36.42600 16.57600  28.81300 1.000 37.62390 ?  174 TYR B CA  1 
ATOM   3143 C C   . TYR B 1 194 ? -35.48500 15.58800  29.48500 1.000 35.94637 ?  174 TYR B C   1 
ATOM   3144 O O   . TYR B 1 194 ? -35.65200 14.37100  29.36300 1.000 32.59802 ?  174 TYR B O   1 
ATOM   3145 C CB  . TYR B 1 194 ? -37.62900 16.81800  29.72900 1.000 28.45110 ?  174 TYR B CB  1 
ATOM   3146 C CG  . TYR B 1 194 ? -38.33400 18.12800  29.47400 1.000 36.28612 ?  174 TYR B CG  1 
ATOM   3147 C CD1 . TYR B 1 194 ? -39.30600 18.23700  28.48600 1.000 36.29761 ?  174 TYR B CD1 1 
ATOM   3148 C CD2 . TYR B 1 194 ? -38.03800 19.25400  30.22800 1.000 34.80354 ?  174 TYR B CD2 1 
ATOM   3149 C CE1 . TYR B 1 194 ? -39.95700 19.43400  28.25400 1.000 35.06516 ?  174 TYR B CE1 1 
ATOM   3150 C CE2 . TYR B 1 194 ? -38.68600 20.45300  30.00400 1.000 39.73953 ?  174 TYR B CE2 1 
ATOM   3151 C CZ  . TYR B 1 194 ? -39.64700 20.53600  29.01700 1.000 36.13217 ?  174 TYR B CZ  1 
ATOM   3152 O OH  . TYR B 1 194 ? -40.29600 21.72600  28.78700 1.000 46.19295 ?  174 TYR B OH  1 
ATOM   3153 N N   . LEU B 1 195 ? -34.49900 16.12800  30.19800 1.000 35.75563 ?  175 LEU B N   1 
ATOM   3154 C CA  . LEU B 1 195 ? -33.66500 15.36800  31.12100 1.000 35.02014 ?  175 LEU B CA  1 
ATOM   3155 C C   . LEU B 1 195 ? -33.94000 15.88200  32.52500 1.000 31.35901 ?  175 LEU B C   1 
ATOM   3156 O O   . LEU B 1 195 ? -33.72200 17.06400  32.80600 1.000 31.62882 ?  175 LEU B O   1 
ATOM   3157 C CB  . LEU B 1 195 ? -32.17800 15.50900  30.78800 1.000 30.55594 ?  175 LEU B CB  1 
ATOM   3158 C CG  . LEU B 1 195 ? -31.25400 14.95200  31.87600 1.000 33.36505 ?  175 LEU B CG  1 
ATOM   3159 C CD1 . LEU B 1 195 ? -31.33000 13.43900  31.89700 1.000 26.09933 ?  175 LEU B CD1 1 
ATOM   3160 C CD2 . LEU B 1 195 ? -29.81200 15.41500  31.67500 1.000 28.80998 ?  175 LEU B CD2 1 
ATOM   3161 N N   . ILE B 1 196 ? -34.41500 15.00300  33.40200 1.000 32.66485 ?  176 ILE B N   1 
ATOM   3162 C CA  . ILE B 1 196 ? -34.76100 15.38200  34.76700 1.000 31.35743 ?  176 ILE B CA  1 
ATOM   3163 C C   . ILE B 1 196 ? -33.85300 14.61900  35.71900 1.000 34.76319 ?  176 ILE B C   1 
ATOM   3164 O O   . ILE B 1 196 ? -33.84900 13.38000  35.73000 1.000 35.55688 ?  176 ILE B O   1 
ATOM   3165 C CB  . ILE B 1 196 ? -36.24400 15.12700  35.07100 1.000 29.20941 ?  176 ILE B CB  1 
ATOM   3166 C CG1 . ILE B 1 196 ? -37.11300 15.91700  34.07700 1.000 30.72868 ?  176 ILE B CG1 1 
ATOM   3167 C CG2 . ILE B 1 196 ? -36.56600 15.52800  36.49900 1.000 28.62769 ?  176 ILE B CG2 1 
ATOM   3168 C CD1 . ILE B 1 196 ? -38.51700 16.23200  34.56400 1.000 28.89966 ?  176 ILE B CD1 1 
ATOM   3169 N N   . LEU B 1 197 ? -33.07000 15.36300  36.49700 1.000 29.28218 ?  177 LEU B N   1 
ATOM   3170 C CA  . LEU B 1 197 ? -32.14900 14.80900  37.47700 1.000 27.17017 ?  177 LEU B CA  1 
ATOM   3171 C C   . LEU B 1 197 ? -32.61100 15.18700  38.87400 1.000 29.48669 ?  177 LEU B C   1 
ATOM   3172 O O   . LEU B 1 197 ? -33.09800 16.29900  39.09300 1.000 32.67520 ?  177 LEU B O   1 
ATOM   3173 C CB  . LEU B 1 197 ? -30.72400 15.33300  37.27600 1.000 25.87305 ?  177 LEU B CB  1 
ATOM   3174 C CG  . LEU B 1 197 ? -30.06800 15.27000  35.89200 1.000 31.67358 ?  177 LEU B CG  1 
ATOM   3175 C CD1 . LEU B 1 197 ? -28.74000 16.03900  35.89000 1.000 27.26609 ?  177 LEU B CD1 1 
ATOM   3176 C CD2 . LEU B 1 197 ? -29.86700 13.82900  35.45300 1.000 27.66133 ?  177 LEU B CD2 1 
ATOM   3177 N N   . THR B 1 198 ? -32.46000 14.26300  39.81700 1.000 30.19645 ?  178 THR B N   1 
ATOM   3178 C CA  . THR B 1 198 ? -32.58500 14.58600  41.22800 1.000 30.69241 ?  178 THR B CA  1 
ATOM   3179 C C   . THR B 1 198 ? -31.34200 14.07700  41.92800 1.000 30.50089 ?  178 THR B C   1 
ATOM   3180 O O   . THR B 1 198 ? -30.84300 12.99900  41.60400 1.000 32.32111 ?  178 THR B O   1 
ATOM   3181 C CB  . THR B 1 198 ? -33.82400 13.97100  41.87400 1.000 32.81121 ?  178 THR B CB  1 
ATOM   3182 O OG1 . THR B 1 198 ? -33.64300 12.55700  41.99400 1.000 40.35039 ?  178 THR B OG1 1 
ATOM   3183 C CG2 . THR B 1 198 ? -35.06000 14.25200  41.04600 1.000 38.64661 ?  178 THR B CG2 1 
ATOM   3184 N N   . SER B 1 199 ? -30.83800 14.86000  42.88000 1.000 31.43803 ?  179 SER B N   1 
ATOM   3185 C CA  . SER B 1 199 ? -29.68700 14.40100  43.63200 1.000 30.80176 ?  179 SER B CA  1 
ATOM   3186 C C   . SER B 1 199 ? -29.55200 15.24500  44.88100 1.000 32.07242 ?  179 SER B C   1 
ATOM   3187 O O   . SER B 1 199 ? -29.77500 16.46100  44.82100 1.000 31.08776 ?  179 SER B O   1 
ATOM   3188 C CB  . SER B 1 199 ? -28.40200 14.48100  42.80400 1.000 30.07436 ?  179 SER B CB  1 
ATOM   3189 O OG  . SER B 1 199 ? -27.27000 14.27700  43.63200 1.000 34.74799 ?  179 SER B OG  1 
ATOM   3190 N N   . PRO B 1 200 ? -29.21300 14.64500  46.02400 1.000 28.76848 ?  180 PRO B N   1 
ATOM   3191 C CA  . PRO B 1 200 ? -28.83400 15.43500  47.19300 1.000 27.48351 ?  180 PRO B CA  1 
ATOM   3192 C C   . PRO B 1 200 ? -27.37400 15.84400  47.19400 1.000 28.90221 ?  180 PRO B C   1 
ATOM   3193 O O   . PRO B 1 200 ? -26.91600 16.43000  48.17700 1.000 32.28642 ?  180 PRO B O   1 
ATOM   3194 C CB  . PRO B 1 200 ? -29.13000 14.47500  48.34700 1.000 28.55849 ?  180 PRO B CB  1 
ATOM   3195 C CG  . PRO B 1 200 ? -28.81200 13.14400  47.77500 1.000 31.46723 ?  180 PRO B CG  1 
ATOM   3196 C CD  . PRO B 1 200 ? -29.26000 13.20300  46.32700 1.000 31.58066 ?  180 PRO B CD  1 
ATOM   3197 N N   . TYR B 1 201 ? -26.63700 15.51500  46.13300 1.000 29.83904 ?  181 TYR B N   1 
ATOM   3198 C CA  . TYR B 1 201 ? -25.24800 15.94200  45.95700 1.000 31.06957 ?  181 TYR B CA  1 
ATOM   3199 C C   . TYR B 1 201 ? -24.35300 15.40500  47.07200 1.000 28.92079 ?  181 TYR B C   1 
ATOM   3200 O O   . TYR B 1 201 ? -23.46300 16.09700  47.56700 1.000 28.25961 ?  181 TYR B O   1 
ATOM   3201 C CB  . TYR B 1 201 ? -25.14100 17.46500  45.85700 1.000 28.37545 ?  181 TYR B CB  1 
ATOM   3202 C CG  . TYR B 1 201 ? -26.07800 18.09200  44.84400 1.000 30.50213 ?  181 TYR B CG  1 
ATOM   3203 C CD1 . TYR B 1 201 ? -26.32200 17.48100  43.62300 1.000 32.69716 ?  181 TYR B CD1 1 
ATOM   3204 C CD2 . TYR B 1 201 ? -26.69400 19.31100  45.10000 1.000 31.65649 ?  181 TYR B CD2 1 
ATOM   3205 C CE1 . TYR B 1 201 ? -27.16700 18.05500  42.69200 1.000 32.52056 ?  181 TYR B CE1 1 
ATOM   3206 C CE2 . TYR B 1 201 ? -27.54100 19.89400  44.17700 1.000 29.58736 ?  181 TYR B CE2 1 
ATOM   3207 C CZ  . TYR B 1 201 ? -27.77100 19.25900  42.97200 1.000 28.54789 ?  181 TYR B CZ  1 
ATOM   3208 O OH  . TYR B 1 201 ? -28.60700 19.82700  42.04300 1.000 30.66822 ?  181 TYR B OH  1 
ATOM   3209 N N   . THR B 1 202 ? -24.58300 14.15000  47.45600 1.000 29.53193 ?  182 THR B N   1 
ATOM   3210 C CA  . THR B 1 202 ? -23.80800 13.49700  48.51000 1.000 28.57991 ?  182 THR B CA  1 
ATOM   3211 C C   . THR B 1 202 ? -22.54900 12.87900  47.90200 1.000 24.92007 ?  182 THR B C   1 
ATOM   3212 O O   . THR B 1 202 ? -22.37900 11.66500  47.83600 1.000 31.68529 ?  182 THR B O   1 
ATOM   3213 C CB  . THR B 1 202 ? -24.64900 12.44100  49.21800 1.000 26.49477 ?  182 THR B CB  1 
ATOM   3214 O OG1 . THR B 1 202 ? -25.93100 12.98200  49.55300 1.000 41.68875 ?  182 THR B OG1 1 
ATOM   3215 C CG2 . THR B 1 202 ? -23.95500 11.98100  50.49900 1.000 34.14411 ?  182 THR B CG2 1 
ATOM   3216 N N   . TRP B 1 203 ? -21.64900 13.74800  47.45200 1.000 28.68267 ?  183 TRP B N   1 
ATOM   3217 C CA  . TRP B 1 203 ? -20.42700 13.26800  46.81800 1.000 31.74271 ?  183 TRP B CA  1 
ATOM   3218 C C   . TRP B 1 203 ? -19.53100 12.59200  47.84800 1.000 34.69102 ?  183 TRP B C   1 
ATOM   3219 O O   . TRP B 1 203 ? -19.22800 13.16600  48.90100 1.000 32.03423 ?  183 TRP B O   1 
ATOM   3220 C CB  . TRP B 1 203 ? -19.69500 14.42000  46.13600 1.000 27.32410 ?  183 TRP B CB  1 
ATOM   3221 C CG  . TRP B 1 203 ? -20.52400 15.05300  45.07100 1.000 33.06097 ?  183 TRP B CG  1 
ATOM   3222 C CD1 . TRP B 1 203 ? -21.13800 16.27000  45.12400 1.000 24.35505 ?  183 TRP B CD1 1 
ATOM   3223 C CD2 . TRP B 1 203 ? -20.86900 14.48100  43.80500 1.000 28.39271 ?  183 TRP B CD2 1 
ATOM   3224 N NE1 . TRP B 1 203 ? -21.82800 16.49900  43.96300 1.000 28.11237 ?  183 TRP B NE1 1 
ATOM   3225 C CE2 . TRP B 1 203 ? -21.68100 15.41500  43.13500 1.000 25.57933 ?  183 TRP B CE2 1 
ATOM   3226 C CE3 . TRP B 1 203 ? -20.56100 13.27200  43.16800 1.000 29.03123 ?  183 TRP B CE3 1 
ATOM   3227 C CZ2 . TRP B 1 203 ? -22.19200 15.18200  41.85700 1.000 25.97320 ?  183 TRP B CZ2 1 
ATOM   3228 C CZ3 . TRP B 1 203 ? -21.06900 13.04000  41.89900 1.000 30.97941 ?  183 TRP B CZ3 1 
ATOM   3229 C CH2 . TRP B 1 203 ? -21.87700 13.99200  41.25700 1.000 29.32095 ?  183 TRP B CH2 1 
ATOM   3230 N N   . ARG B 1 204 ? -19.13500 11.35700  47.55300 1.000 33.28545 ?  184 ARG B N   1 
ATOM   3231 C CA  . ARG B 1 204 ? -18.24700 10.58300  48.41000 1.000 35.58054 ?  184 ARG B CA  1 
ATOM   3232 C C   . ARG B 1 204 ? -17.20400 9.88400   47.55200 1.000 36.05754 ?  184 ARG B C   1 
ATOM   3233 O O   . ARG B 1 204 ? -17.52500 9.36900   46.47800 1.000 35.31431 ?  184 ARG B O   1 
ATOM   3234 C CB  . ARG B 1 204 ? -19.02200 9.54600   49.23200 1.000 28.81663 ?  184 ARG B CB  1 
ATOM   3235 C CG  . ARG B 1 204 ? -20.09100 10.13800  50.13200 1.000 37.22704 ?  184 ARG B CG  1 
ATOM   3236 C CD  . ARG B 1 204 ? -21.28100 9.20200   50.25800 1.000 43.97422 ?  184 ARG B CD  1 
ATOM   3237 N N   . GLU B 1 205 ? -15.95500 9.86700   48.03300 1.000 36.24032 ?  185 GLU B N   1 
ATOM   3238 C CA  . GLU B 1 205 ? -14.88800 9.16900   47.32200 1.000 38.68611 ?  185 GLU B CA  1 
ATOM   3239 C C   . GLU B 1 205 ? -15.14200 7.67100   47.22100 1.000 41.24028 ?  185 GLU B C   1 
ATOM   3240 O O   . GLU B 1 205 ? -14.60400 7.02200   46.31800 1.000 42.80974 ?  185 GLU B O   1 
ATOM   3241 C CB  . GLU B 1 205 ? -13.53900 9.42800   47.99900 1.000 42.51446 ?  185 GLU B CB  1 
ATOM   3242 C CG  . GLU B 1 205 ? -12.74600 10.56600  47.37500 1.000 47.08353 ?  185 GLU B CG  1 
ATOM   3243 C CD  . GLU B 1 205 ? -11.49500 10.91000  48.15500 1.000 52.03511 ?  185 GLU B CD  1 
ATOM   3244 O OE1 . GLU B 1 205 ? -11.17800 12.11900  48.25400 1.000 59.24377 ?  185 GLU B OE1 1 
ATOM   3245 N N   . GLU B 1 206 ? -15.95000 7.10700   48.12200 1.000 40.43643 ?  186 GLU B N   1 
ATOM   3246 C CA  . GLU B 1 206 ? -16.30800 5.69900   48.00300 1.000 38.23518 ?  186 GLU B CA  1 
ATOM   3247 C C   . GLU B 1 206 ? -17.08800 5.42600   46.72400 1.000 45.24975 ?  186 GLU B C   1 
ATOM   3248 O O   . GLU B 1 206 ? -17.02200 4.31900   46.18000 1.000 42.03241 ?  186 GLU B O   1 
ATOM   3249 C CB  . GLU B 1 206 ? -17.12200 5.26100   49.22100 1.000 38.50078 ?  186 GLU B CB  1 
ATOM   3250 N N   . TYR B 1 207 ? -17.83000 6.41400   46.23100 1.000 35.98912 ?  187 TYR B N   1 
ATOM   3251 C CA  . TYR B 1 207 ? -18.64000 6.24700   45.03400 1.000 34.06342 ?  187 TYR B CA  1 
ATOM   3252 C C   . TYR B 1 207 ? -18.03500 6.92400   43.81600 1.000 35.22407 ?  187 TYR B C   1 
ATOM   3253 O O   . TYR B 1 207 ? -18.08100 6.36200   42.71800 1.000 36.76302 ?  187 TYR B O   1 
ATOM   3254 C CB  . TYR B 1 207 ? -20.05400 6.79600   45.26500 1.000 37.82505 ?  187 TYR B CB  1 
ATOM   3255 C CG  . TYR B 1 207 ? -20.92000 5.93800   46.16200 1.000 44.13429 ?  187 TYR B CG  1 
ATOM   3256 C CD1 . TYR B 1 207 ? -21.54500 4.79400   45.67500 1.000 48.43355 ?  187 TYR B CD1 1 
ATOM   3257 C CD2 . TYR B 1 207 ? -21.11500 6.27100   47.49600 1.000 45.97107 ?  187 TYR B CD2 1 
ATOM   3258 C CE1 . TYR B 1 207 ? -22.34200 4.00800   46.49400 1.000 47.01439 ?  187 TYR B CE1 1 
ATOM   3259 C CE2 . TYR B 1 207 ? -21.90800 5.48800   48.32200 1.000 49.62261 ?  187 TYR B CE2 1 
ATOM   3260 C CZ  . TYR B 1 207 ? -22.51800 4.36100   47.81800 1.000 51.66021 ?  187 TYR B CZ  1 
ATOM   3261 O OH  . TYR B 1 207 ? -23.30700 3.58700   48.64100 1.000 62.31440 ?  187 TYR B OH  1 
ATOM   3262 N N   . THR B 1 208 ? -17.45600 8.11000   43.99000 1.000 38.03633 ?  188 THR B N   1 
ATOM   3263 C CA  . THR B 1 208 ? -17.00800 8.94600   42.88600 1.000 34.24838 ?  188 THR B CA  1 
ATOM   3264 C C   . THR B 1 208 ? -15.60100 9.44600   43.16600 1.000 29.36073 ?  188 THR B C   1 
ATOM   3265 O O   . THR B 1 208 ? -15.33000 9.95900   44.25400 1.000 32.80798 ?  188 THR B O   1 
ATOM   3266 C CB  . THR B 1 208 ? -17.96400 10.13200  42.68500 1.000 31.55427 ?  188 THR B CB  1 
ATOM   3267 O OG1 . THR B 1 208 ? -19.31300 9.65300   42.66400 1.000 26.43192 ?  188 THR B OG1 1 
ATOM   3268 C CG2 . THR B 1 208 ? -17.66000 10.86900  41.39200 1.000 25.04364 ?  188 THR B CG2 1 
ATOM   3269 N N   . ALA B 1 209 ? -14.70600 9.28300   42.19400 1.000 29.20371 ?  189 ALA B N   1 
ATOM   3270 C CA  . ALA B 1 209 ? -13.38100 9.87100   42.31600 1.000 35.65442 ?  189 ALA B CA  1 
ATOM   3271 C C   . ALA B 1 209 ? -13.50300 11.38700  42.40500 1.000 35.71068 ?  189 ALA B C   1 
ATOM   3272 O O   . ALA B 1 209 ? -14.27400 12.00500  41.66500 1.000 32.85322 ?  189 ALA B O   1 
ATOM   3273 C CB  . ALA B 1 209 ? -12.50400 9.47600   41.12700 1.000 33.37274 ?  189 ALA B CB  1 
ATOM   3274 N N   . LYS B 1 210 ? -12.74000 11.97900  43.33100 1.000 34.49511 ?  190 LYS B N   1 
ATOM   3275 C CA  . LYS B 1 210 ? -12.82800 13.41600  43.58500 1.000 36.23198 ?  190 LYS B CA  1 
ATOM   3276 C C   . LYS B 1 210 ? -12.71000 14.23200  42.30300 1.000 33.42214 ?  190 LYS B C   1 
ATOM   3277 O O   . LYS B 1 210 ? -13.43700 15.21400  42.11600 1.000 38.36853 ?  190 LYS B O   1 
ATOM   3278 C CB  . LYS B 1 210 ? -11.74700 13.83400  44.58500 1.000 40.57617 ?  190 LYS B CB  1 
ATOM   3279 C CG  . LYS B 1 210 ? -11.71200 15.33000  44.87600 1.000 40.10037 ?  190 LYS B CG  1 
ATOM   3280 C CD  . LYS B 1 210 ? -12.34800 15.68200  46.20900 1.000 45.10804 ?  190 LYS B CD  1 
ATOM   3281 C CE  . LYS B 1 210 ? -11.67300 16.90900  46.80400 1.000 41.71969 ?  190 LYS B CE  1 
ATOM   3282 N N   . LYS B 1 211 ? -11.80900 13.83500  41.40100 1.000 33.58605 ?  191 LYS B N   1 
ATOM   3283 C CA  . LYS B 1 211 ? -11.65600 14.55700  40.14200 1.000 36.51547 ?  191 LYS B CA  1 
ATOM   3284 C C   . LYS B 1 211 ? -12.91200 14.49200  39.28400 1.000 31.99716 ?  191 LYS B C   1 
ATOM   3285 O O   . LYS B 1 211 ? -13.04900 15.27900  38.34300 1.000 33.61365 ?  191 LYS B O   1 
ATOM   3286 C CB  . LYS B 1 211 ? -10.45900 14.00500  39.36300 1.000 36.22555 ?  191 LYS B CB  1 
ATOM   3287 C CG  . LYS B 1 211 ? -10.61500 12.55100  38.93500 1.000 42.76053 ?  191 LYS B CG  1 
ATOM   3288 C CD  . LYS B 1 211 ? -9.30400  11.98600  38.42300 1.000 43.25983 ?  191 LYS B CD  1 
ATOM   3289 C CE  . LYS B 1 211 ? -9.45400  10.54300  37.98000 1.000 39.70640 ?  191 LYS B CE  1 
ATOM   3290 N NZ  . LYS B 1 211 ? -8.44200  10.19400  36.93400 1.000 43.59035 ?  191 LYS B NZ  1 
ATOM   3291 N N   . PHE B 1 212 ? -13.83100 13.57800  39.58700 1.000 33.03715 ?  192 PHE B N   1 
ATOM   3292 C CA  . PHE B 1 212 ? -15.07100 13.43900  38.83800 1.000 30.23101 ?  192 PHE B CA  1 
ATOM   3293 C C   . PHE B 1 212 ? -16.27500 14.02100  39.56500 1.000 30.62004 ?  192 PHE B C   1 
ATOM   3294 O O   . PHE B 1 212 ? -17.38000 13.99200  39.02000 1.000 28.96863 ?  192 PHE B O   1 
ATOM   3295 C CB  . PHE B 1 212 ? -15.32700 11.96600  38.51100 1.000 29.79969 ?  192 PHE B CB  1 
ATOM   3296 C CG  . PHE B 1 212 ? -14.30500 11.36500  37.58200 1.000 37.63204 ?  192 PHE B CG  1 
ATOM   3297 C CD1 . PHE B 1 212 ? -13.71800 12.13100  36.58400 1.000 30.49863 ?  192 PHE B CD1 1 
ATOM   3298 C CD2 . PHE B 1 212 ? -13.93200 10.03500  37.70800 1.000 31.96676 ?  192 PHE B CD2 1 
ATOM   3299 C CE1 . PHE B 1 212 ? -12.78300 11.58100  35.72900 1.000 38.19242 ?  192 PHE B CE1 1 
ATOM   3300 C CE2 . PHE B 1 212 ? -12.99500 9.48200   36.85700 1.000 38.64936 ?  192 PHE B CE2 1 
ATOM   3301 C CZ  . PHE B 1 212 ? -12.41900 10.25200  35.86400 1.000 38.19973 ?  192 PHE B CZ  1 
ATOM   3302 N N   . TRP B 1 213 ? -16.09300 14.53700  40.77900 1.000 30.76941 ?  193 TRP B N   1 
ATOM   3303 C CA  . TRP B 1 213 ? -17.17600 15.23900  41.45400 1.000 30.10167 ?  193 TRP B CA  1 
ATOM   3304 C C   . TRP B 1 213 ? -17.64700 16.40000  40.59000 1.000 32.12294 ?  193 TRP B C   1 
ATOM   3305 O O   . TRP B 1 213 ? -16.83700 17.18500  40.09000 1.000 31.89584 ?  193 TRP B O   1 
ATOM   3306 C CB  . TRP B 1 213 ? -16.71700 15.76400  42.81200 1.000 28.91495 ?  193 TRP B CB  1 
ATOM   3307 C CG  . TRP B 1 213 ? -16.48000 14.71200  43.83800 1.000 30.67163 ?  193 TRP B CG  1 
ATOM   3308 C CD1 . TRP B 1 213 ? -16.30100 13.37600  43.62500 1.000 36.45392 ?  193 TRP B CD1 1 
ATOM   3309 C CD2 . TRP B 1 213 ? -16.37200 14.91300  45.24800 1.000 31.41431 ?  193 TRP B CD2 1 
ATOM   3310 N NE1 . TRP B 1 213 ? -16.09300 12.73000  44.82100 1.000 31.52754 ?  193 TRP B NE1 1 
ATOM   3311 C CE2 . TRP B 1 213 ? -16.13300 13.65200  45.83300 1.000 30.93181 ?  193 TRP B CE2 1 
ATOM   3312 C CE3 . TRP B 1 213 ? -16.45400 16.03800  46.07500 1.000 29.78032 ?  193 TRP B CE3 1 
ATOM   3313 C CZ2 . TRP B 1 213 ? -15.98000 13.48500  47.20500 1.000 32.67581 ?  193 TRP B CZ2 1 
ATOM   3314 C CZ3 . TRP B 1 213 ? -16.30200 15.87100  47.43700 1.000 36.46809 ?  193 TRP B CZ3 1 
ATOM   3315 C CH2 . TRP B 1 213 ? -16.06700 14.60200  47.98900 1.000 36.04983 ?  193 TRP B CH2 1 
ATOM   3316 N N   . ILE B 1 214 ? -18.95900 16.50000  40.39900 1.000 28.23954 ?  194 ILE B N   1 
ATOM   3317 C CA  . ILE B 1 214 ? -19.47800 17.60100  39.60400 1.000 27.93757 ?  194 ILE B CA  1 
ATOM   3318 C C   . ILE B 1 214 ? -19.51900 18.88300  40.42700 1.000 34.24447 ?  194 ILE B C   1 
ATOM   3319 O O   . ILE B 1 214 ? -19.47100 19.98700  39.87200 1.000 30.73703 ?  194 ILE B O   1 
ATOM   3320 C CB  . ILE B 1 214 ? -20.85600 17.22400  39.04000 1.000 26.84159 ?  194 ILE B CB  1 
ATOM   3321 C CG1 . ILE B 1 214 ? -20.69200 16.09400  38.03000 1.000 24.37119 ?  194 ILE B CG1 1 
ATOM   3322 C CG2 . ILE B 1 214 ? -21.53800 18.41800  38.38000 1.000 27.87035 ?  194 ILE B CG2 1 
ATOM   3323 C CD1 . ILE B 1 214 ? -21.98900 15.49700  37.59400 1.000 33.34734 ?  194 ILE B CD1 1 
ATOM   3324 N N   . GLY B 1 215 ? -19.57900 18.76700  41.74200 1.000 31.07533 ?  195 GLY B N   1 
ATOM   3325 C CA  . GLY B 1 215 ? -19.58200 19.92900  42.59300 1.000 31.85699 ?  195 GLY B CA  1 
ATOM   3326 C C   . GLY B 1 215 ? -19.24800 19.52100  43.99800 1.000 34.76457 ?  195 GLY B C   1 
ATOM   3327 O O   . GLY B 1 215 ? -18.82200 18.39400  44.25000 1.000 33.32611 ?  195 GLY B O   1 
ATOM   3328 N N   . GLY B 1 216 ? -19.45200 20.45100  44.92300 1.000 33.22973 ?  196 GLY B N   1 
ATOM   3329 C CA  . GLY B 1 216 ? -19.22200 20.14900  46.32400 1.000 33.28678 ?  196 GLY B CA  1 
ATOM   3330 C C   . GLY B 1 216 ? -17.75700 20.05000  46.68200 1.000 36.03198 ?  196 GLY B C   1 
ATOM   3331 O O   . GLY B 1 216 ? -17.38700 19.26600  47.56600 1.000 35.65997 ?  196 GLY B O   1 
ATOM   3332 N N   . TYR B 1 217 ? -16.91200 20.82900  46.01300 1.000 34.08710 ?  197 TYR B N   1 
ATOM   3333 C CA  . TYR B 1 217 ? -15.48000 20.80400  46.25300 1.000 37.98648 ?  197 TYR B CA  1 
ATOM   3334 C C   . TYR B 1 217 ? -14.91500 22.19100  45.98900 1.000 33.54051 ?  197 TYR B C   1 
ATOM   3335 O O   . TYR B 1 217 ? -15.52800 23.01800  45.30900 1.000 35.97808 ?  197 TYR B O   1 
ATOM   3336 C CB  . TYR B 1 217 ? -14.77600 19.76300  45.37200 1.000 35.08585 ?  197 TYR B CB  1 
ATOM   3337 C CG  . TYR B 1 217 ? -14.83600 20.10200  43.89900 1.000 36.83687 ?  197 TYR B CG  1 
ATOM   3338 C CD1 . TYR B 1 217 ? -15.91100 19.69300  43.12100 1.000 30.96649 ?  197 TYR B CD1 1 
ATOM   3339 C CD2 . TYR B 1 217 ? -13.82800 20.84400  43.28800 1.000 29.95599 ?  197 TYR B CD2 1 
ATOM   3340 C CE1 . TYR B 1 217 ? -15.97800 19.99900  41.77900 1.000 38.34662 ?  197 TYR B CE1 1 
ATOM   3341 C CE2 . TYR B 1 217 ? -13.89100 21.16100  41.94000 1.000 28.74483 ?  197 TYR B CE2 1 
ATOM   3342 C CZ  . TYR B 1 217 ? -14.96400 20.73600  41.19500 1.000 32.84603 ?  197 TYR B CZ  1 
ATOM   3343 O OH  . TYR B 1 217 ? -15.04100 21.04500  39.85900 1.000 38.46722 ?  197 TYR B OH  1 
ATOM   3344 N N   . VAL B 1 218 ? -13.73300 22.42700  46.53600 1.000 36.25306 ?  198 VAL B N   1 
ATOM   3345 C CA  . VAL B 1 218 ? -12.98500 23.65400  46.31000 1.000 35.23035 ?  198 VAL B CA  1 
ATOM   3346 C C   . VAL B 1 218 ? -12.02200 23.40700  45.15700 1.000 28.01305 ?  198 VAL B C   1 
ATOM   3347 O O   . VAL B 1 218 ? -11.24100 22.45100  45.19100 1.000 27.13866 ?  198 VAL B O   1 
ATOM   3348 C CB  . VAL B 1 218 ? -12.22900 24.06700  47.58300 1.000 39.53128 ?  198 VAL B CB  1 
ATOM   3349 C CG1 . VAL B 1 218 ? -11.47800 25.37300  47.37000 1.000 32.69318 ?  198 VAL B CG1 1 
ATOM   3350 C CG2 . VAL B 1 218 ? -13.19000 24.16600  48.76400 1.000 34.65155 ?  198 VAL B CG2 1 
ATOM   3351 N N   . ASP B 1 219 ? -12.07500 24.25500  44.13300 1.000 29.17301 ?  199 ASP B N   1 
ATOM   3352 C CA  . ASP B 1 219 ? -11.18000 24.06900  43.00000 1.000 34.52845 ?  199 ASP B CA  1 
ATOM   3353 C C   . ASP B 1 219 ? -9.75400  24.49700  43.36200 1.000 36.89598 ?  199 ASP B C   1 
ATOM   3354 O O   . ASP B 1 219 ? -9.46300  24.91300  44.48700 1.000 34.16758 ?  199 ASP B O   1 
ATOM   3355 C CB  . ASP B 1 219 ? -11.69600 24.81500  41.76500 1.000 36.94401 ?  199 ASP B CB  1 
ATOM   3356 C CG  . ASP B 1 219 ? -11.82600 26.32300  41.97700 1.000 43.42280 ?  199 ASP B CG  1 
ATOM   3357 O OD1 . ASP B 1 219 ? -10.99900 26.92700  42.69600 1.000 39.19301 ?  199 ASP B OD1 1 
ATOM   3358 O OD2 . ASP B 1 219 ? -12.75900 26.91500  41.38600 1.000 48.34190 -1 199 ASP B OD2 1 
ATOM   3359 N N   . GLU B 1 220 ? -8.85500  24.40500  42.37600 1.000 34.28079 ?  200 GLU B N   1 
ATOM   3360 C CA  . GLU B 1 220 ? -7.44800  24.72100  42.59200 1.000 45.99363 ?  200 GLU B CA  1 
ATOM   3361 C C   . GLU B 1 220 ? -7.21700  26.19300  42.90900 1.000 41.21814 ?  200 GLU B C   1 
ATOM   3362 O O   . GLU B 1 220 ? -6.14200  26.54700  43.40600 1.000 42.94152 ?  200 GLU B O   1 
ATOM   3363 C CB  . GLU B 1 220 ? -6.62900  24.32400  41.35900 1.000 40.52472 ?  200 GLU B CB  1 
ATOM   3364 N N   . ASN B 1 221 ? -8.19200  27.05300  42.62900 1.000 38.20730 ?  201 ASN B N   1 
ATOM   3365 C CA  . ASN B 1 221 ? -8.07000  28.48300  42.86400 1.000 34.23138 ?  201 ASN B CA  1 
ATOM   3366 C C   . ASN B 1 221 ? -8.67100  28.92800  44.18800 1.000 37.50623 ?  201 ASN B C   1 
ATOM   3367 O O   . ASN B 1 221 ? -8.60800  30.11900  44.51100 1.000 38.07063 ?  201 ASN B O   1 
ATOM   3368 C CB  . ASN B 1 221 ? -8.72300  29.25500  41.71900 1.000 36.58659 ?  201 ASN B CB  1 
ATOM   3369 C CG  . ASN B 1 221 ? -8.14800  28.88200  40.37300 1.000 41.82311 ?  201 ASN B CG  1 
ATOM   3370 O OD1 . ASN B 1 221 ? -6.94700  28.65200  40.25000 1.000 37.41663 ?  201 ASN B OD1 1 
ATOM   3371 N ND2 . ASN B 1 221 ? -8.99900  28.82500  39.35400 1.000 40.44124 ?  201 ASN B ND2 1 
ATOM   3372 N N   . GLY B 1 222 ? -9.24800  28.01200  44.95600 1.000 36.67938 ?  202 GLY B N   1 
ATOM   3373 C CA  . GLY B 1 222 ? -9.85300  28.36300  46.22200 1.000 37.56173 ?  202 GLY B CA  1 
ATOM   3374 C C   . GLY B 1 222 ? -11.32100 28.71300  46.16300 1.000 34.63146 ?  202 GLY B C   1 
ATOM   3375 O O   . GLY B 1 222 ? -11.86600 29.18100  47.16800 1.000 41.86183 ?  202 GLY B O   1 
ATOM   3376 N N   . LYS B 1 223 ? -11.97900 28.50800  45.02600 1.000 38.12853 ?  203 LYS B N   1 
ATOM   3377 C CA  . LYS B 1 223 ? -13.39600 28.81100  44.86900 1.000 40.41530 ?  203 LYS B CA  1 
ATOM   3378 C C   . LYS B 1 223 ? -14.22700 27.55500  45.08400 1.000 37.44424 ?  203 LYS B C   1 
ATOM   3379 O O   . LYS B 1 223 ? -13.86600 26.46700  44.62500 1.000 41.12314 ?  203 LYS B O   1 
ATOM   3380 C CB  . LYS B 1 223 ? -13.69700 29.38400  43.48000 1.000 43.14764 ?  203 LYS B CB  1 
ATOM   3381 C CG  . LYS B 1 223 ? -12.95200 30.66300  43.14600 1.000 49.79823 ?  203 LYS B CG  1 
ATOM   3382 C CD  . LYS B 1 223 ? -13.42100 31.84800  43.97800 1.000 50.63760 ?  203 LYS B CD  1 
ATOM   3383 C CE  . LYS B 1 223 ? -12.74200 33.14700  43.52700 1.000 48.93098 ?  203 LYS B CE  1 
ATOM   3384 N NZ  . LYS B 1 223 ? -13.63000 34.07200  42.75200 1.000 49.30227 ?  203 LYS B NZ  1 
ATOM   3385 N N   . GLU B 1 224 ? -15.34600 27.71000  45.77700 1.000 38.13756 ?  204 GLU B N   1 
ATOM   3386 C CA  . GLU B 1 224 ? -16.25700 26.59700  45.97700 1.000 37.45426 ?  204 GLU B CA  1 
ATOM   3387 C C   . GLU B 1 224 ? -17.05800 26.35800  44.70400 1.000 39.68259 ?  204 GLU B C   1 
ATOM   3388 O O   . GLU B 1 224 ? -17.47500 27.30300  44.02700 1.000 41.62233 ?  204 GLU B O   1 
ATOM   3389 C CB  . GLU B 1 224 ? -17.18500 26.87500  47.15700 1.000 39.98829 ?  204 GLU B CB  1 
ATOM   3390 C CG  . GLU B 1 224 ? -16.47200 26.80300  48.49800 1.000 47.78823 ?  204 GLU B CG  1 
ATOM   3391 C CD  . GLU B 1 224 ? -17.40100 27.02900  49.66800 1.000 57.16451 ?  204 GLU B CD  1 
ATOM   3392 O OE1 . GLU B 1 224 ? -18.45500 27.67300  49.47100 1.000 57.44699 ?  204 GLU B OE1 1 
ATOM   3393 O OE2 . GLU B 1 224 ? -17.07700 26.56400  50.78400 1.000 65.36583 -1 204 GLU B OE2 1 
ATOM   3394 N N   . VAL B 1 225 ? -17.24500 25.08500  44.36800 1.000 38.09611 ?  205 VAL B N   1 
ATOM   3395 C CA  . VAL B 1 225 ? -17.96300 24.67800  43.16600 1.000 33.81533 ?  205 VAL B CA  1 
ATOM   3396 C C   . VAL B 1 225 ? -19.27700 24.03900  43.59000 1.000 35.22348 ?  205 VAL B C   1 
ATOM   3397 O O   . VAL B 1 225 ? -19.28400 23.02500  44.30100 1.000 30.49370 ?  205 VAL B O   1 
ATOM   3398 C CB  . VAL B 1 225 ? -17.12900 23.71500  42.31000 1.000 35.21860 ?  205 VAL B CB  1 
ATOM   3399 C CG1 . VAL B 1 225 ? -17.91600 23.28100  41.08100 1.000 32.55668 ?  205 VAL B CG1 1 
ATOM   3400 C CG2 . VAL B 1 225 ? -15.81600 24.37500  41.90200 1.000 34.89306 ?  205 VAL B CG2 1 
ATOM   3401 N N   . SER B 1 226 ? -20.38600 24.63700  43.16700 1.000 32.76265 ?  206 SER B N   1 
ATOM   3402 C CA  . SER B 1 226 ? -21.69700 24.06500  43.42800 1.000 33.91243 ?  206 SER B CA  1 
ATOM   3403 C C   . SER B 1 226 ? -22.02400 23.03500  42.35700 1.000 33.62189 ?  206 SER B C   1 
ATOM   3404 O O   . SER B 1 226 ? -21.63200 23.18200  41.19700 1.000 34.24583 ?  206 SER B O   1 
ATOM   3405 C CB  . SER B 1 226 ? -22.76100 25.16300  43.46700 1.000 33.62885 ?  206 SER B CB  1 
ATOM   3406 O OG  . SER B 1 226 ? -23.43800 25.28000  42.23100 1.000 35.61946 ?  206 SER B OG  1 
ATOM   3407 N N   . THR B 1 227 ? -22.72900 21.97500  42.75400 1.000 28.19623 ?  207 THR B N   1 
ATOM   3408 C CA  . THR B 1 227 ? -23.02200 20.90900  41.80000 1.000 35.94955 ?  207 THR B CA  1 
ATOM   3409 C C   . THR B 1 227 ? -23.93900 21.39500  40.68200 1.000 31.90316 ?  207 THR B C   1 
ATOM   3410 O O   . THR B 1 227 ? -23.75600 21.01400  39.51900 1.000 31.80937 ?  207 THR B O   1 
ATOM   3411 C CB  . THR B 1 227 ? -23.62600 19.70100  42.51800 1.000 31.97341 ?  207 THR B CB  1 
ATOM   3412 O OG1 . THR B 1 227 ? -22.79600 19.33700  43.63100 1.000 31.90785 ?  207 THR B OG1 1 
ATOM   3413 C CG2 . THR B 1 227 ? -23.72400 18.51800  41.56900 1.000 35.51666 ?  207 THR B CG2 1 
ATOM   3414 N N   . LEU B 1 228 ? -24.92000 22.24600  41.00600 1.000 25.58489 ?  208 LEU B N   1 
ATOM   3415 C CA  . LEU B 1 228 ? -25.80100 22.78300  39.97100 1.000 32.40820 ?  208 LEU B CA  1 
ATOM   3416 C C   . LEU B 1 228 ? -25.01800 23.57400  38.93000 1.000 31.44679 ?  208 LEU B C   1 
ATOM   3417 O O   . LEU B 1 228 ? -25.31100 23.49300  37.73200 1.000 33.18150 ?  208 LEU B O   1 
ATOM   3418 C CB  . LEU B 1 228 ? -26.89000 23.65900  40.59500 1.000 33.14666 ?  208 LEU B CB  1 
ATOM   3419 C CG  . LEU B 1 228 ? -28.00800 24.10900  39.64400 1.000 35.32639 ?  208 LEU B CG  1 
ATOM   3420 C CD1 . LEU B 1 228 ? -28.69000 22.92100  38.96700 1.000 28.89600 ?  208 LEU B CD1 1 
ATOM   3421 C CD2 . LEU B 1 228 ? -29.02900 24.98000  40.36500 1.000 35.29176 ?  208 LEU B CD2 1 
ATOM   3422 N N   . GLU B 1 229 ? -24.02300 24.35000  39.37000 1.000 28.69931 ?  209 GLU B N   1 
ATOM   3423 C CA  . GLU B 1 229 ? -23.16100 25.05400  38.42600 1.000 32.25592 ?  209 GLU B CA  1 
ATOM   3424 C C   . GLU B 1 229 ? -22.37700 24.07300  37.56600 1.000 35.30276 ?  209 GLU B C   1 
ATOM   3425 O O   . GLU B 1 229 ? -22.24000 24.27100  36.35100 1.000 37.21396 ?  209 GLU B O   1 
ATOM   3426 C CB  . GLU B 1 229 ? -22.20800 25.99000  39.17600 1.000 30.61206 ?  209 GLU B CB  1 
ATOM   3427 N N   . GLY B 1 230 ? -21.85900 23.00500  38.17900 1.000 30.01969 ?  210 GLY B N   1 
ATOM   3428 C CA  . GLY B 1 230 ? -21.15900 21.99100  37.41000 1.000 28.74737 ?  210 GLY B CA  1 
ATOM   3429 C C   . GLY B 1 230 ? -22.07000 21.27100  36.43500 1.000 28.43539 ?  210 GLY B C   1 
ATOM   3430 O O   . GLY B 1 230 ? -21.64400 20.88900  35.34300 1.000 29.81333 ?  210 GLY B O   1 
ATOM   3431 N N   . LEU B 1 231 ? -23.33200 21.06700  36.81700 1.000 28.05187 ?  211 LEU B N   1 
ATOM   3432 C CA  . LEU B 1 231 ? -24.28800 20.46800  35.89200 1.000 29.25058 ?  211 LEU B CA  1 
ATOM   3433 C C   . LEU B 1 231 ? -24.55400 21.39800  34.71800 1.000 31.19559 ?  211 LEU B C   1 
ATOM   3434 O O   . LEU B 1 231 ? -24.65600 20.95000  33.57100 1.000 33.75949 ?  211 LEU B O   1 
ATOM   3435 C CB  . LEU B 1 231 ? -25.58900 20.13200  36.62100 1.000 25.14242 ?  211 LEU B CB  1 
ATOM   3436 C CG  . LEU B 1 231 ? -25.52400 18.99200  37.63900 1.000 24.91964 ?  211 LEU B CG  1 
ATOM   3437 C CD1 . LEU B 1 231 ? -26.77300 18.97900  38.50800 1.000 28.23493 ?  211 LEU B CD1 1 
ATOM   3438 C CD2 . LEU B 1 231 ? -25.33600 17.65100  36.94800 1.000 24.54029 ?  211 LEU B CD2 1 
ATOM   3439 N N   . LYS B 1 232 ? -24.65600 22.70100  34.98800 1.000 28.45973 ?  212 LYS B N   1 
ATOM   3440 C CA  . LYS B 1 232 ? -24.82100 23.67100  33.90900 1.000 33.68942 ?  212 LYS B CA  1 
ATOM   3441 C C   . LYS B 1 232 ? -23.64900 23.62300  32.93400 1.000 37.00195 ?  212 LYS B C   1 
ATOM   3442 O O   . LYS B 1 232 ? -23.84600 23.63500  31.71500 1.000 39.41706 ?  212 LYS B O   1 
ATOM   3443 C CB  . LYS B 1 232 ? -24.98200 25.07300  34.49000 1.000 35.18906 ?  212 LYS B CB  1 
ATOM   3444 C CG  . LYS B 1 232 ? -26.31400 25.28100  35.18000 1.000 34.24851 ?  212 LYS B CG  1 
ATOM   3445 C CD  . LYS B 1 232 ? -26.72800 26.73900  35.15200 1.000 46.79270 ?  212 LYS B CD  1 
ATOM   3446 C CE  . LYS B 1 232 ? -26.88600 27.29100  36.55200 1.000 41.73699 ?  212 LYS B CE  1 
ATOM   3447 N NZ  . LYS B 1 232 ? -26.95100 28.77800  36.52700 1.000 55.03642 ?  212 LYS B NZ  1 
ATOM   3448 N N   . GLU B 1 233 ? -22.42200 23.54900  33.45100 1.000 36.43484 ?  213 GLU B N   1 
ATOM   3449 C CA  . GLU B 1 233 ? -21.25800 23.53200  32.57000 1.000 37.91087 ?  213 GLU B CA  1 
ATOM   3450 C C   . GLU B 1 233 ? -21.28700 22.32700  31.63500 1.000 33.29014 ?  213 GLU B C   1 
ATOM   3451 O O   . GLU B 1 233 ? -20.93600 22.43600  30.45500 1.000 38.76278 ?  213 GLU B O   1 
ATOM   3452 C CB  . GLU B 1 233 ? -19.97200 23.54200  33.39900 1.000 29.75565 ?  213 GLU B CB  1 
ATOM   3453 N N   . ILE B 1 234 ? -21.71400 21.17200  32.13800 1.000 33.69400 ?  214 ILE B N   1 
ATOM   3454 C CA  . ILE B 1 234 ? -21.76000 19.97700  31.30200 1.000 38.16396 ?  214 ILE B CA  1 
ATOM   3455 C C   . ILE B 1 234 ? -22.93600 20.03100  30.33300 1.000 33.36701 ?  214 ILE B C   1 
ATOM   3456 O O   . ILE B 1 234 ? -22.77900 19.78900  29.13000 1.000 36.49020 ?  214 ILE B O   1 
ATOM   3457 C CB  . ILE B 1 234 ? -21.80800 18.71400  32.18200 1.000 34.19141 ?  214 ILE B CB  1 
ATOM   3458 C CG1 . ILE B 1 234 ? -20.52600 18.60500  33.00800 1.000 40.99246 ?  214 ILE B CG1 1 
ATOM   3459 C CG2 . ILE B 1 234 ? -22.05400 17.46500  31.33600 1.000 30.02668 ?  214 ILE B CG2 1 
ATOM   3460 C CD1 . ILE B 1 234 ? -20.57800 17.54400  34.08300 1.000 36.06914 ?  214 ILE B CD1 1 
ATOM   3461 N N   . LEU B 1 235 ? -24.12400 20.36800  30.83500 1.000 34.54962 ?  215 LEU B N   1 
ATOM   3462 C CA  . LEU B 1 235 ? -25.35800 20.14600  30.09400 1.000 33.27680 ?  215 LEU B CA  1 
ATOM   3463 C C   . LEU B 1 235 ? -25.78700 21.31700  29.22700 1.000 35.16890 ?  215 LEU B C   1 
ATOM   3464 O O   . LEU B 1 235 ? -26.54100 21.10600  28.27200 1.000 38.53679 ?  215 LEU B O   1 
ATOM   3465 C CB  . LEU B 1 235 ? -26.50000 19.81500  31.05600 1.000 34.69116 ?  215 LEU B CB  1 
ATOM   3466 C CG  . LEU B 1 235 ? -26.32100 18.52500  31.84800 1.000 36.09011 ?  215 LEU B CG  1 
ATOM   3467 C CD1 . LEU B 1 235 ? -27.33400 18.45200  32.98100 1.000 31.56936 ?  215 LEU B CD1 1 
ATOM   3468 C CD2 . LEU B 1 235 ? -26.46000 17.34300  30.90600 1.000 33.76413 ?  215 LEU B CD2 1 
ATOM   3469 N N   . GLU B 1 236 ? -25.35000 22.53900  29.52900 1.000 34.78070 ?  216 GLU B N   1 
ATOM   3470 C CA  . GLU B 1 236 ? -25.83600 23.66100  28.73400 1.000 41.70589 ?  216 GLU B CA  1 
ATOM   3471 C C   . GLU B 1 236 ? -25.26900 23.65700  27.31800 1.000 42.44664 ?  216 GLU B C   1 
ATOM   3472 O O   . GLU B 1 236 ? -25.70500 24.46700  26.49200 1.000 37.38368 ?  216 GLU B O   1 
ATOM   3473 C CB  . GLU B 1 236 ? -25.53500 24.97800  29.45900 1.000 37.63599 ?  216 GLU B CB  1 
ATOM   3474 C CG  . GLU B 1 236 ? -26.35700 25.13400  30.75000 1.000 46.89130 ?  216 GLU B CG  1 
ATOM   3475 C CD  . GLU B 1 236 ? -26.33500 26.54100  31.32600 1.000 52.13794 ?  216 GLU B CD  1 
ATOM   3476 O OE1 . GLU B 1 236 ? -25.23100 27.11700  31.44100 1.000 60.30515 ?  216 GLU B OE1 1 
ATOM   3477 O OE2 . GLU B 1 236 ? -27.41400 27.05500  31.70000 1.000 45.31219 -1 216 GLU B OE2 1 
ATOM   3478 N N   . ILE B 1 237 ? -24.33600 22.74900  27.01600 1.000 40.61707 ?  217 ILE B N   1 
ATOM   3479 C CA  . ILE B 1 237 ? -23.93100 22.52200  25.63300 1.000 45.71946 ?  217 ILE B CA  1 
ATOM   3480 C C   . ILE B 1 237 ? -25.11700 22.04300  24.80300 1.000 45.69237 ?  217 ILE B C   1 
ATOM   3481 O O   . ILE B 1 237 ? -25.28500 22.44800  23.64800 1.000 41.74602 ?  217 ILE B O   1 
ATOM   3482 C CB  . ILE B 1 237 ? -22.76100 21.52200  25.57400 1.000 44.04280 ?  217 ILE B CB  1 
ATOM   3483 C CG1 . ILE B 1 237 ? -21.60800 22.00700  26.45100 1.000 50.55491 ?  217 ILE B CG1 1 
ATOM   3484 C CG2 . ILE B 1 237 ? -22.29700 21.31600  24.13700 1.000 49.38339 ?  217 ILE B CG2 1 
ATOM   3485 C CD1 . ILE B 1 237 ? -21.19700 23.43500  26.16600 1.000 45.16337 ?  217 ILE B CD1 1 
ATOM   3486 N N   . HIS B 1 238 ? -25.96700 21.18800  25.38000 1.000 38.12565 ?  218 HIS B N   1 
ATOM   3487 C CA  . HIS B 1 238 ? -27.07800 20.60200  24.64500 1.000 41.34634 ?  218 HIS B CA  1 
ATOM   3488 C C   . HIS B 1 238 ? -28.42600 20.75000  25.33800 1.000 36.66240 ?  218 HIS B C   1 
ATOM   3489 O O   . HIS B 1 238 ? -29.41900 20.20400  24.84300 1.000 36.02479 ?  218 HIS B O   1 
ATOM   3490 C CB  . HIS B 1 238 ? -26.81300 19.11100  24.38000 1.000 37.22127 ?  218 HIS B CB  1 
ATOM   3491 C CG  . HIS B 1 238 ? -25.71000 18.86100  23.39800 1.000 44.66785 ?  218 HIS B CG  1 
ATOM   3492 N ND1 . HIS B 1 238 ? -24.47200 18.38500  23.77500 1.000 48.42604 ?  218 HIS B ND1 1 
ATOM   3493 C CD2 . HIS B 1 238 ? -25.65600 19.02400  22.05500 1.000 39.52557 ?  218 HIS B CD2 1 
ATOM   3494 C CE1 . HIS B 1 238 ? -23.70300 18.26500  22.70600 1.000 44.39227 ?  218 HIS B CE1 1 
ATOM   3495 N NE2 . HIS B 1 238 ? -24.39900 18.64600  21.64900 1.000 48.06753 ?  218 HIS B NE2 1 
ATOM   3496 N N   . PHE B 1 239 ? -28.49900 21.47800  26.45000 1.000 36.81854 ?  219 PHE B N   1 
ATOM   3497 C CA  . PHE B 1 239 ? -29.72300 21.59300  27.23000 1.000 32.67294 ?  219 PHE B CA  1 
ATOM   3498 C C   . PHE B 1 239 ? -29.90400 23.03700  27.67600 1.000 37.10061 ?  219 PHE B C   1 
ATOM   3499 O O   . PHE B 1 239 ? -28.96500 23.83900  27.65800 1.000 44.69530 ?  219 PHE B O   1 
ATOM   3500 C CB  . PHE B 1 239 ? -29.70100 20.68100  28.46700 1.000 32.91619 ?  219 PHE B CB  1 
ATOM   3501 C CG  . PHE B 1 239 ? -29.77600 19.21000  28.15900 1.000 36.26538 ?  219 PHE B CG  1 
ATOM   3502 C CD1 . PHE B 1 239 ? -31.00400 18.57600  28.03800 1.000 31.87009 ?  219 PHE B CD1 1 
ATOM   3503 C CD2 . PHE B 1 239 ? -28.62300 18.45400  28.02500 1.000 34.49268 ?  219 PHE B CD2 1 
ATOM   3504 C CE1 . PHE B 1 239 ? -31.07800 17.22300  27.76800 1.000 33.25845 ?  219 PHE B CE1 1 
ATOM   3505 C CE2 . PHE B 1 239 ? -28.69100 17.09900  27.75500 1.000 33.04551 ?  219 PHE B CE2 1 
ATOM   3506 C CZ  . PHE B 1 239 ? -29.91900 16.48400  27.62600 1.000 36.98665 ?  219 PHE B CZ  1 
ATOM   3507 N N   . GLU B 1 240 ? -31.12700 23.36100  28.09400 1.000 35.26326 ?  220 GLU B N   1 
ATOM   3508 C CA  . GLU B 1 240 ? -31.41900 24.61500  28.77900 1.000 36.78306 ?  220 GLU B CA  1 
ATOM   3509 C C   . GLU B 1 240 ? -32.00000 24.29300  30.14600 1.000 33.95203 ?  220 GLU B C   1 
ATOM   3510 O O   . GLU B 1 240 ? -32.85900 23.41100  30.26000 1.000 34.55909 ?  220 GLU B O   1 
ATOM   3511 C CB  . GLU B 1 240 ? -32.39800 25.48200  27.98000 1.000 32.63896 ?  220 GLU B CB  1 
ATOM   3512 N N   . LEU B 1 241 ? -31.53200 24.99400  31.18000 1.000 29.68974 ?  221 LEU B N   1 
ATOM   3513 C CA  . LEU B 1 241 ? -32.04800 24.76700  32.52500 1.000 33.97047 ?  221 LEU B CA  1 
ATOM   3514 C C   . LEU B 1 241 ? -33.41600 25.41900  32.65600 1.000 34.96484 ?  221 LEU B C   1 
ATOM   3515 O O   . LEU B 1 241 ? -33.54800 26.63500  32.48900 1.000 38.80105 ?  221 LEU B O   1 
ATOM   3516 C CB  . LEU B 1 241 ? -31.09400 25.30200  33.58900 1.000 31.42804 ?  221 LEU B CB  1 
ATOM   3517 C CG  . LEU B 1 241 ? -31.58700 25.06300  35.02100 1.000 34.76754 ?  221 LEU B CG  1 
ATOM   3518 C CD1 . LEU B 1 241 ? -32.00400 23.61100  35.24400 1.000 31.17075 ?  221 LEU B CD1 1 
ATOM   3519 C CD2 . LEU B 1 241 ? -30.54700 25.48400  36.04800 1.000 33.16575 ?  221 LEU B CD2 1 
ATOM   3520 N N   . VAL B 1 242 ? -34.42700 24.61300  32.95900 1.000 33.95783 ?  222 VAL B N   1 
ATOM   3521 C CA  . VAL B 1 242 ? -35.80700 25.07200  32.98300 1.000 37.51877 ?  222 VAL B CA  1 
ATOM   3522 C C   . VAL B 1 242 ? -36.29100 25.32900  34.40400 1.000 40.06769 ?  222 VAL B C   1 
ATOM   3523 O O   . VAL B 1 242 ? -36.96900 26.32500  34.66000 1.000 36.42489 ?  222 VAL B O   1 
ATOM   3524 C CB  . VAL B 1 242 ? -36.71300 24.05000  32.26100 1.000 36.95561 ?  222 VAL B CB  1 
ATOM   3525 C CG1 . VAL B 1 242 ? -38.15600 24.20300  32.70900 1.000 39.38899 ?  222 VAL B CG1 1 
ATOM   3526 C CG2 . VAL B 1 242 ? -36.59200 24.21300  30.76000 1.000 45.14792 ?  222 VAL B CG2 1 
ATOM   3527 N N   . ALA B 1 243 ? -35.94900 24.45000  35.34100 1.000 30.20950 ?  223 ALA B N   1 
ATOM   3528 C CA  . ALA B 1 243 ? -36.46900 24.59700  36.69200 1.000 36.12969 ?  223 ALA B CA  1 
ATOM   3529 C C   . ALA B 1 243 ? -35.59200 23.82700  37.66400 1.000 35.35366 ?  223 ALA B C   1 
ATOM   3530 O O   . ALA B 1 243 ? -34.90600 22.87300  37.29100 1.000 36.85986 ?  223 ALA B O   1 
ATOM   3531 C CB  . ALA B 1 243 ? -37.91900 24.10900  36.79100 1.000 30.76863 ?  223 ALA B CB  1 
ATOM   3532 N N   . THR B 1 244 ? -35.62500 24.26600  38.92000 1.000 35.29448 ?  224 THR B N   1 
ATOM   3533 C CA  . THR B 1 244 ? -35.06900 23.51600  40.03100 1.000 34.60687 ?  224 THR B CA  1 
ATOM   3534 C C   . THR B 1 244 ? -36.10900 23.47700  41.13600 1.000 36.83939 ?  224 THR B C   1 
ATOM   3535 O O   . THR B 1 244 ? -36.90800 24.40400  41.29000 1.000 34.32214 ?  224 THR B O   1 
ATOM   3536 C CB  . THR B 1 244 ? -33.76900 24.12000  40.57200 1.000 34.05804 ?  224 THR B CB  1 
ATOM   3537 O OG1 . THR B 1 244 ? -33.94400 25.52400  40.78700 1.000 39.69796 ?  224 THR B OG1 1 
ATOM   3538 C CG2 . THR B 1 244 ? -32.64000 23.90900  39.57600 1.000 31.71243 ?  224 THR B CG2 1 
ATOM   3539 N N   . GLU B 1 245 ? -36.08900 22.39300  41.90400 1.000 30.34825 ?  225 GLU B N   1 
ATOM   3540 C CA  . GLU B 1 245 ? -37.06900 22.17900  42.95500 1.000 30.89976 ?  225 GLU B CA  1 
ATOM   3541 C C   . GLU B 1 245 ? -36.46100 21.25700  44.00100 1.000 34.36842 ?  225 GLU B C   1 
ATOM   3542 O O   . GLU B 1 245 ? -35.73500 20.32000  43.66200 1.000 33.00138 ?  225 GLU B O   1 
ATOM   3543 C CB  . GLU B 1 245 ? -38.35400 21.58400  42.37300 1.000 35.94722 ?  225 GLU B CB  1 
ATOM   3544 C CG  . GLU B 1 245 ? -39.58900 21.78600  43.21100 1.000 47.15085 ?  225 GLU B CG  1 
ATOM   3545 C CD  . GLU B 1 245 ? -40.78000 21.04500  42.63600 1.000 53.35458 ?  225 GLU B CD  1 
ATOM   3546 O OE1 . GLU B 1 245 ? -40.93300 21.04800  41.39300 1.000 49.95071 ?  225 GLU B OE1 1 
ATOM   3547 O OE2 . GLU B 1 245 ? -41.55900 20.46300  43.42500 1.000 51.94880 -1 225 GLU B OE2 1 
ATOM   3548 N N   . ASP B 1 246 ? -36.74200 21.53700  45.26600 1.000 33.42701 ?  226 ASP B N   1 
ATOM   3549 C CA  . ASP B 1 246 ? -36.29600 20.69500  46.36400 1.000 31.39719 ?  226 ASP B CA  1 
ATOM   3550 C C   . ASP B 1 246 ? -37.38200 19.66800  46.66300 1.000 33.66923 ?  226 ASP B C   1 
ATOM   3551 O O   . ASP B 1 246 ? -38.55700 20.02600  46.79900 1.000 36.16265 ?  226 ASP B O   1 
ATOM   3552 C CB  . ASP B 1 246 ? -35.97800 21.54200  47.59800 1.000 28.12128 ?  226 ASP B CB  1 
ATOM   3553 C CG  . ASP B 1 246 ? -34.58400 22.15800  47.54400 1.000 37.83026 ?  226 ASP B CG  1 
ATOM   3554 O OD1 . ASP B 1 246 ? -33.82000 21.84300  46.60600 1.000 32.71195 ?  226 ASP B OD1 1 
ATOM   3555 O OD2 . ASP B 1 246 ? -34.25500 22.97400  48.43200 1.000 41.01932 -1 226 ASP B OD2 1 
ATOM   3556 N N   . ILE B 1 247 ? -37.00000 18.39500  46.71900 1.000 30.93928 ?  227 ILE B N   1 
ATOM   3557 C CA  . ILE B 1 247 ? -37.92400 17.30200  46.98500 1.000 32.64492 ?  227 ILE B CA  1 
ATOM   3558 C C   . ILE B 1 247 ? -37.39500 16.49200  48.16400 1.000 31.04721 ?  227 ILE B C   1 
ATOM   3559 O O   . ILE B 1 247 ? -36.33700 15.86600  48.05700 1.000 28.33434 ?  227 ILE B O   1 
ATOM   3560 C CB  . ILE B 1 247 ? -38.12300 16.39100  45.76300 1.000 32.51288 ?  227 ILE B CB  1 
ATOM   3561 C CG1 . ILE B 1 247 ? -38.38800 17.22300  44.50400 1.000 32.17972 ?  227 ILE B CG1 1 
ATOM   3562 C CG2 . ILE B 1 247 ? -39.27500 15.41900  46.02200 1.000 26.78770 ?  227 ILE B CG2 1 
ATOM   3563 C CD1 . ILE B 1 247 ? -38.58800 16.38600  43.25800 1.000 36.31254 ?  227 ILE B CD1 1 
ATOM   3564 N N   . PRO B 1 248 ? -38.09000 16.47000  49.29600 1.000 34.66991 ?  228 PRO B N   1 
ATOM   3565 C CA  . PRO B 1 248 ? -37.62700 15.67500  50.43500 1.000 28.17327 ?  228 PRO B CA  1 
ATOM   3566 C C   . PRO B 1 248 ? -38.02400 14.21400  50.30400 1.000 32.75625 ?  228 PRO B C   1 
ATOM   3567 O O   . PRO B 1 248 ? -39.03300 13.86800  49.68700 1.000 27.63496 ?  228 PRO B O   1 
ATOM   3568 C CB  . PRO B 1 248 ? -38.34700 16.32400  51.62200 1.000 31.60307 ?  228 PRO B CB  1 
ATOM   3569 C CG  . PRO B 1 248 ? -39.63700 16.79900  51.02600 1.000 35.80685 ?  228 PRO B CG  1 
ATOM   3570 C CD  . PRO B 1 248 ? -39.30800 17.23800  49.61400 1.000 31.05775 ?  228 PRO B CD  1 
ATOM   3571 N N   . PHE B 1 249 ? -37.20700 13.34900  50.89900 1.000 31.51078 ?  229 PHE B N   1 
ATOM   3572 C CA  . PHE B 1 249 ? -37.53600 11.93700  51.00100 1.000 30.34272 ?  229 PHE B CA  1 
ATOM   3573 C C   . PHE B 1 249 ? -37.01600 11.38700  52.32000 1.000 31.67958 ?  229 PHE B C   1 
ATOM   3574 O O   . PHE B 1 249 ? -36.08900 11.93400  52.92500 1.000 26.89429 ?  229 PHE B O   1 
ATOM   3575 C CB  . PHE B 1 249 ? -36.98900 11.12100  49.81200 1.000 33.39705 ?  229 PHE B CB  1 
ATOM   3576 C CG  . PHE B 1 249 ? -35.48600 11.08600  49.70700 1.000 32.17730 ?  229 PHE B CG  1 
ATOM   3577 C CD1 . PHE B 1 249 ? -34.80800 12.03600  48.96000 1.000 36.60251 ?  229 PHE B CD1 1 
ATOM   3578 C CD2 . PHE B 1 249 ? -34.75500 10.07800  50.31500 1.000 34.65488 ?  229 PHE B CD2 1 
ATOM   3579 C CE1 . PHE B 1 249 ? -33.42900 11.99300  48.84100 1.000 34.59651 ?  229 PHE B CE1 1 
ATOM   3580 C CE2 . PHE B 1 249 ? -33.37600 10.02900  50.19800 1.000 28.75275 ?  229 PHE B CE2 1 
ATOM   3581 C CZ  . PHE B 1 249 ? -32.71600 10.98500  49.45700 1.000 33.22300 ?  229 PHE B CZ  1 
ATOM   3582 N N   . VAL B 1 250 ? -37.65900 10.31600  52.77400 1.000 31.82988 ?  230 VAL B N   1 
ATOM   3583 C CA  . VAL B 1 250 ? -37.29200 9.61300   53.99700 1.000 32.99533 ?  230 VAL B CA  1 
ATOM   3584 C C   . VAL B 1 250 ? -37.06300 8.15000   53.64000 1.000 32.19735 ?  230 VAL B C   1 
ATOM   3585 O O   . VAL B 1 250 ? -37.89700 7.54000   52.96500 1.000 34.39686 ?  230 VAL B O   1 
ATOM   3586 C CB  . VAL B 1 250 ? -38.38500 9.73900   55.07600 1.000 30.83861 ?  230 VAL B CB  1 
ATOM   3587 C CG1 . VAL B 1 250 ? -38.00000 8.95800   56.32900 1.000 28.68816 ?  230 VAL B CG1 1 
ATOM   3588 C CG2 . VAL B 1 250 ? -38.65400 11.20300  55.40400 1.000 31.48591 ?  230 VAL B CG2 1 
ATOM   3589 N N   . ILE B 1 251 ? -35.93200 7.59500   54.06600 1.000 34.45077 ?  231 ILE B N   1 
ATOM   3590 C CA  . ILE B 1 251 ? -35.65700 6.16800   53.91700 1.000 36.96713 ?  231 ILE B CA  1 
ATOM   3591 C C   . ILE B 1 251 ? -35.53700 5.57100   55.31300 1.000 34.42539 ?  231 ILE B C   1 
ATOM   3592 O O   . ILE B 1 251 ? -34.74100 6.04700   56.13100 1.000 33.97550 ?  231 ILE B O   1 
ATOM   3593 C CB  . ILE B 1 251 ? -34.38600 5.88900   53.09900 1.000 38.92228 ?  231 ILE B CB  1 
ATOM   3594 C CG1 . ILE B 1 251 ? -34.38500 6.66000   51.78800 1.000 37.85710 ?  231 ILE B CG1 1 
ATOM   3595 C CG2 . ILE B 1 251 ? -34.28700 4.40500   52.77100 1.000 37.72483 ?  231 ILE B CG2 1 
ATOM   3596 C CD1 . ILE B 1 251 ? -33.06100 6.57000   51.05000 1.000 39.31955 ?  231 ILE B CD1 1 
ATOM   3597 N N   . ARG B 1 252 ? -36.31800 4.52600   55.58000 1.000 33.96620 ?  232 ARG B N   1 
ATOM   3598 C CA  . ARG B 1 252 ? -36.28900 3.85100   56.87100 1.000 34.22443 ?  232 ARG B CA  1 
ATOM   3599 C C   . ARG B 1 252 ? -35.03900 2.98400   56.96600 1.000 38.96719 ?  232 ARG B C   1 
ATOM   3600 O O   . ARG B 1 252 ? -34.78000 2.15800   56.08300 1.000 41.97103 ?  232 ARG B O   1 
ATOM   3601 C CB  . ARG B 1 252 ? -37.55300 3.00900   57.05000 1.000 36.47346 ?  232 ARG B CB  1 
ATOM   3602 C CG  . ARG B 1 252 ? -37.60100 2.21900   58.35000 1.000 36.09111 ?  232 ARG B CG  1 
ATOM   3603 C CD  . ARG B 1 252 ? -38.74000 1.19500   58.37400 1.000 38.52136 ?  232 ARG B CD  1 
ATOM   3604 N NE  . ARG B 1 252 ? -39.91700 1.72100   59.05900 1.000 41.89856 ?  232 ARG B NE  1 
ATOM   3605 C CZ  . ARG B 1 252 ? -40.91000 2.36400   58.45500 1.000 54.91496 ?  232 ARG B CZ  1 
ATOM   3606 N NH1 . ARG B 1 252 ? -40.92200 2.54000   57.14200 1.000 48.08951 ?  232 ARG B NH1 1 
ATOM   3607 N NH2 . ARG B 1 252 ? -41.91200 2.84700   59.18700 1.000 48.21211 ?  232 ARG B NH2 1 
ATOM   3608 N N   . GLU B 1 253 ? -34.25600 3.17800   58.02500 1.000 35.58357 ?  233 GLU B N   1 
ATOM   3609 C CA  . GLU B 1 253 ? -33.14100 2.29000   58.32900 1.000 41.58522 ?  233 GLU B CA  1 
ATOM   3610 C C   . GLU B 1 253 ? -33.46500 1.31600   59.45500 1.000 47.89327 ?  233 GLU B C   1 
ATOM   3611 O O   . GLU B 1 253 ? -33.13200 0.13100   59.35800 1.000 51.91179 ?  233 GLU B O   1 
ATOM   3612 C CB  . GLU B 1 253 ? -31.88900 3.09800   58.68700 1.000 29.63443 ?  233 GLU B CB  1 
ATOM   3613 N N   . THR B 1 254 ? -34.09900 1.78800   60.52800 1.000 38.92275 ?  234 THR B N   1 
ATOM   3614 C CA  . THR B 1 254 ? -34.68700 0.91700   61.53700 1.000 36.89799 ?  234 THR B CA  1 
ATOM   3615 C C   . THR B 1 254 ? -36.09000 1.42000   61.84400 1.000 37.33489 ?  234 THR B C   1 
ATOM   3616 O O   . THR B 1 254 ? -36.58800 2.36100   61.22100 1.000 38.67949 ?  234 THR B O   1 
ATOM   3617 C CB  . THR B 1 254 ? -33.85200 0.84900   62.82700 1.000 34.45243 ?  234 THR B CB  1 
ATOM   3618 O OG1 . THR B 1 254 ? -34.07600 2.02900   63.61000 1.000 37.57251 ?  234 THR B OG1 1 
ATOM   3619 C CG2 . THR B 1 254 ? -32.36400 0.70300   62.53100 1.000 39.34216 ?  234 THR B CG2 1 
ATOM   3620 N N   . SER B 1 255 ? -36.72900 0.78400   62.82300 1.000 38.23967 ?  235 SER B N   1 
ATOM   3621 C CA  . SER B 1 255 ? -38.02900 1.24900   63.28800 1.000 39.21057 ?  235 SER B CA  1 
ATOM   3622 C C   . SER B 1 255 ? -37.95700 2.65700   63.85900 1.000 36.38328 ?  235 SER B C   1 
ATOM   3623 O O   . SER B 1 255 ? -38.97400 3.36000   63.88300 1.000 34.41789 ?  235 SER B O   1 
ATOM   3624 C CB  . SER B 1 255 ? -38.57700 0.28900   64.34700 1.000 41.74231 ?  235 SER B CB  1 
ATOM   3625 O OG  . SER B 1 255 ? -37.59800 0.02000   65.34300 1.000 44.21627 ?  235 SER B OG  1 
ATOM   3626 N N   . ARG B 1 256 ? -36.77900 3.08600   64.31300 1.000 32.86375 ?  236 ARG B N   1 
ATOM   3627 C CA  . ARG B 1 256 ? -36.61300 4.38600   64.93800 1.000 35.52677 ?  236 ARG B CA  1 
ATOM   3628 C C   . ARG B 1 256 ? -35.61700 5.29500   64.23100 1.000 33.33158 ?  236 ARG B C   1 
ATOM   3629 O O   . ARG B 1 256 ? -35.59400 6.49200   64.53000 1.000 36.59478 ?  236 ARG B O   1 
ATOM   3630 C CB  . ARG B 1 256 ? -36.17700 4.21800   66.40600 1.000 29.71500 ?  236 ARG B CB  1 
ATOM   3631 C CG  . ARG B 1 256 ? -37.18500 3.46800   67.26300 1.000 30.04728 ?  236 ARG B CG  1 
ATOM   3632 C CD  . ARG B 1 256 ? -36.83800 3.52600   68.74800 1.000 29.42491 ?  236 ARG B CD  1 
ATOM   3633 N NE  . ARG B 1 256 ? -37.99000 3.19300   69.57900 1.000 30.56497 ?  236 ARG B NE  1 
ATOM   3634 C CZ  . ARG B 1 256 ? -38.84000 4.08600   70.06600 1.000 32.77866 ?  236 ARG B CZ  1 
ATOM   3635 N NH1 . ARG B 1 256 ? -38.68000 5.37900   69.85200 1.000 33.15713 ?  236 ARG B NH1 1 
ATOM   3636 N NH2 . ARG B 1 256 ? -39.87900 3.67000   70.78600 1.000 33.60074 ?  236 ARG B NH2 1 
ATOM   3637 N N   . LYS B 1 257 ? -34.79800 4.74300   63.33900 1.000 32.19775 ?  237 LYS B N   1 
ATOM   3638 C CA  . LYS B 1 257 ? -33.74400 5.54800   62.67000 1.000 32.00856 ?  237 LYS B CA  1 
ATOM   3639 C C   . LYS B 1 257 ? -34.05600 5.68600   61.18200 1.000 28.35683 ?  237 LYS B C   1 
ATOM   3640 O O   . LYS B 1 257 ? -34.30900 4.67300   60.53700 1.000 36.36243 ?  237 LYS B O   1 
ATOM   3641 C CB  . LYS B 1 257 ? -32.35100 4.95100   62.86200 1.000 29.52059 ?  237 LYS B CB  1 
ATOM   3642 C CG  . LYS B 1 257 ? -31.21400 5.69500   62.18000 1.000 32.35522 ?  237 LYS B CG  1 
ATOM   3643 C CD  . LYS B 1 257 ? -29.85600 5.08800   62.45200 1.000 38.27629 ?  237 LYS B CD  1 
ATOM   3644 C CE  . LYS B 1 257 ? -28.73900 5.77100   61.69500 1.000 31.94329 ?  237 LYS B CE  1 
ATOM   3645 N N   . PHE B 1 258 ? -34.03400 6.91200   60.68600 1.000 25.44826 ?  238 PHE B N   1 
ATOM   3646 C CA  . PHE B 1 258 ? -34.37200 7.16100   59.27000 1.000 33.12387 ?  238 PHE B CA  1 
ATOM   3647 C C   . PHE B 1 258 ? -33.41800 8.18500   58.66600 1.000 28.96144 ?  238 PHE B C   1 
ATOM   3648 O O   . PHE B 1 258 ? -32.78700 8.93400   59.40500 1.000 33.02672 ?  238 PHE B O   1 
ATOM   3649 C CB  . PHE B 1 258 ? -35.80400 7.69200   59.12600 1.000 25.65558 ?  238 PHE B CB  1 
ATOM   3650 C CG  . PHE B 1 258 ? -36.91300 6.89200   59.75900 1.000 31.12402 ?  238 PHE B CG  1 
ATOM   3651 C CD1 . PHE B 1 258 ? -37.08500 6.86200   61.13300 1.000 29.22377 ?  238 PHE B CD1 1 
ATOM   3652 C CD2 . PHE B 1 258 ? -37.82600 6.21100   58.97300 1.000 33.10737 ?  238 PHE B CD2 1 
ATOM   3653 C CE1 . PHE B 1 258 ? -38.10900 6.12800   61.70600 1.000 34.59046 ?  238 PHE B CE1 1 
ATOM   3654 C CE2 . PHE B 1 258 ? -38.85700 5.48700   59.54600 1.000 35.47515 ?  238 PHE B CE2 1 
ATOM   3655 C CZ  . PHE B 1 258 ? -38.99700 5.44600   60.91100 1.000 34.18064 ?  238 PHE B CZ  1 
ATOM   3656 N N   . GLN B 1 259 ? -33.29800 8.17500   57.34800 1.000 30.35088 ?  239 GLN B N   1 
ATOM   3657 C CA  . GLN B 1 259 ? -32.52400 9.23300   56.66900 1.000 30.13992 ?  239 GLN B CA  1 
ATOM   3658 C C   . GLN B 1 259 ? -33.54400 10.22000  56.10300 1.000 31.35125 ?  239 GLN B C   1 
ATOM   3659 O O   . GLN B 1 259 ? -34.45200 9.78800   55.39800 1.000 33.88960 ?  239 GLN B O   1 
ATOM   3660 C CB  . GLN B 1 259 ? -31.62000 8.66600   55.58100 1.000 30.23681 ?  239 GLN B CB  1 
ATOM   3661 C CG  . GLN B 1 259 ? -31.09200 9.72400   54.62800 1.000 31.77169 ?  239 GLN B CG  1 
ATOM   3662 C CD  . GLN B 1 259 ? -30.53100 9.15100   53.35100 1.000 39.31730 ?  239 GLN B CD  1 
ATOM   3663 O OE1 . GLN B 1 259 ? -30.56100 9.78300   52.29800 1.000 40.97109 ?  239 GLN B OE1 1 
ATOM   3664 N NE2 . GLN B 1 259 ? -30.00000 7.94400   53.43900 1.000 42.66232 ?  239 GLN B NE2 1 
ATOM   3665 N N   . HIS B 1 260 ? -33.42100 11.48000  56.47900 1.000 26.72863 ?  240 HIS B N   1 
ATOM   3666 C CA  . HIS B 1 260 ? -34.32900 12.52700  55.96300 1.000 29.99670 ?  240 HIS B CA  1 
ATOM   3667 C C   . HIS B 1 260 ? -33.46600 13.41300  55.07300 1.000 32.31330 ?  240 HIS B C   1 
ATOM   3668 O O   . HIS B 1 260 ? -32.59000 14.12800  55.57200 1.000 27.88946 ?  240 HIS B O   1 
ATOM   3669 C CB  . HIS B 1 260 ? -35.03000 13.23800  57.12200 1.000 31.22257 ?  240 HIS B CB  1 
ATOM   3670 C CG  . HIS B 1 260 ? -36.26100 13.97400  56.75600 1.000 31.21465 ?  240 HIS B CG  1 
ATOM   3671 N ND1 . HIS B 1 260 ? -37.21300 14.30600  57.69200 1.000 29.09818 ?  240 HIS B ND1 1 
ATOM   3672 C CD2 . HIS B 1 260 ? -36.69700 14.44000  55.59200 1.000 30.58293 ?  240 HIS B CD2 1 
ATOM   3673 C CE1 . HIS B 1 260 ? -38.19300 14.95200  57.09400 1.000 37.58364 ?  240 HIS B CE1 1 
ATOM   3674 N NE2 . HIS B 1 260 ? -37.89900 15.04000  55.82000 1.000 39.65665 ?  240 HIS B NE2 1 
ATOM   3675 N N   . THR B 1 261 ? -33.71600 13.35400  53.77700 1.000 26.90727 ?  241 THR B N   1 
ATOM   3676 C CA  . THR B 1 261 ? -32.81700 14.07100  52.84700 1.000 34.81861 ?  241 THR B CA  1 
ATOM   3677 C C   . THR B 1 261 ? -33.62500 14.94200  51.88100 1.000 36.56157 ?  241 THR B C   1 
ATOM   3678 O O   . THR B 1 261 ? -34.71900 14.53100  51.48400 1.000 32.18502 ?  241 THR B O   1 
ATOM   3679 C CB  . THR B 1 261 ? -31.86500 13.06200  52.18500 1.000 28.39712 ?  241 THR B CB  1 
ATOM   3680 O OG1 . THR B 1 261 ? -31.00400 12.53800  53.19100 1.000 29.40221 ?  241 THR B OG1 1 
ATOM   3681 C CG2 . THR B 1 261 ? -31.03000 13.66500  51.08100 1.000 34.17011 ?  241 THR B CG2 1 
ATOM   3682 N N   . ILE B 1 262 ? -33.07900 16.10400  51.53300 1.000 32.93256 ?  242 ILE B N   1 
ATOM   3683 C CA  . ILE B 1 262 ? -33.74300 16.99200  50.54300 1.000 32.59280 ?  242 ILE B CA  1 
ATOM   3684 C C   . ILE B 1 262 ? -32.97400 16.93600  49.22600 1.000 35.18973 ?  242 ILE B C   1 
ATOM   3685 O O   . ILE B 1 262 ? -31.88000 17.50300  49.16100 1.000 29.28480 ?  242 ILE B O   1 
ATOM   3686 C CB  . ILE B 1 262 ? -33.89600 18.43100  51.06900 1.000 37.73113 ?  242 ILE B CB  1 
ATOM   3687 C CG1 . ILE B 1 262 ? -34.68500 18.46400  52.37800 1.000 36.22527 ?  242 ILE B CG1 1 
ATOM   3688 C CG2 . ILE B 1 262 ? -34.52900 19.32100  50.01500 1.000 30.34483 ?  242 ILE B CG2 1 
ATOM   3689 C CD1 . ILE B 1 262 ? -33.93100 19.08700  53.51800 1.000 44.89280 ?  242 ILE B CD1 1 
ATOM   3690 N N   . SER B 1 263 ? -33.51800 16.22200  48.24400 1.000 27.85456 ?  243 SER B N   1 
ATOM   3691 C CA  . SER B 1 263 ? -32.93200 16.21300  46.91400 1.000 25.87560 ?  243 SER B CA  1 
ATOM   3692 C C   . SER B 1 263 ? -33.29100 17.48300  46.15900 1.000 31.23966 ?  243 SER B C   1 
ATOM   3693 O O   . SER B 1 263 ? -34.29800 18.13900  46.43200 1.000 33.33833 ?  243 SER B O   1 
ATOM   3694 C CB  . SER B 1 263 ? -33.41200 15.00700  46.10300 1.000 29.83085 ?  243 SER B CB  1 
ATOM   3695 O OG  . SER B 1 263 ? -32.55500 13.89900  46.26600 1.000 38.90405 ?  243 SER B OG  1 
ATOM   3696 N N   . GLN B 1 264 ? -32.46000 17.81800  45.18100 1.000 25.69088 ?  244 GLN B N   1 
ATOM   3697 C CA  . GLN B 1 264 ? -32.75700 18.89100  44.24500 1.000 29.42833 ?  244 GLN B CA  1 
ATOM   3698 C C   . GLN B 1 264 ? -33.05000 18.27900  42.88500 1.000 29.14761 ?  244 GLN B C   1 
ATOM   3699 O O   . GLN B 1 264 ? -32.21600 17.55100  42.33300 1.000 31.65361 ?  244 GLN B O   1 
ATOM   3700 C CB  . GLN B 1 264 ? -31.60800 19.89500  44.14300 1.000 31.64100 ?  244 GLN B CB  1 
ATOM   3701 C CG  . GLN B 1 264 ? -31.82900 20.92300  43.04300 1.000 32.24949 ?  244 GLN B CG  1 
ATOM   3702 C CD  . GLN B 1 264 ? -30.87100 22.08800  43.12000 1.000 30.29692 ?  244 GLN B CD  1 
ATOM   3703 O OE1 . GLN B 1 264 ? -29.71800 21.98600  42.70700 1.000 32.60674 ?  244 GLN B OE1 1 
ATOM   3704 N NE2 . GLN B 1 264 ? -31.34700 23.21200  43.64100 1.000 30.09800 ?  244 GLN B NE2 1 
ATOM   3705 N N   . MET B 1 265 ? -34.23600 18.55900  42.36100 1.000 29.41020 ?  245 MET B N   1 
ATOM   3706 C CA  . MET B 1 265 ? -34.58900 18.16800  41.00900 1.000 27.44696 ?  245 MET B CA  1 
ATOM   3707 C C   . MET B 1 265 ? -34.23600 19.31500  40.07600 1.000 31.73578 ?  245 MET B C   1 
ATOM   3708 O O   . MET B 1 265 ? -34.61000 20.46600  40.33100 1.000 30.42723 ?  245 MET B O   1 
ATOM   3709 C CB  . MET B 1 265 ? -36.07800 17.84600  40.89900 1.000 32.16774 ?  245 MET B CB  1 
ATOM   3710 C CG  . MET B 1 265 ? -36.61200 17.84200  39.47700 1.000 28.00248 ?  245 MET B CG  1 
ATOM   3711 S SD  . MET B 1 265 ? -38.34500 17.32900  39.43900 1.000 34.57801 ?  245 MET B SD  1 
ATOM   3712 C CE  . MET B 1 265 ? -38.22400 15.55400  39.68500 1.000 28.72431 ?  245 MET B CE  1 
ATOM   3713 N N   . SER B 1 266 ? -33.50700 19.00600  39.00900 1.000 27.66806 ?  246 SER B N   1 
ATOM   3714 C CA  . SER B 1 266 ? -33.18300 19.97400  37.97000 1.000 30.03308 ?  246 SER B CA  1 
ATOM   3715 C C   . SER B 1 266 ? -33.76600 19.47700  36.65600 1.000 30.42347 ?  246 SER B C   1 
ATOM   3716 O O   . SER B 1 266 ? -33.66700 18.28600  36.34000 1.000 31.39626 ?  246 SER B O   1 
ATOM   3717 C CB  . SER B 1 266 ? -31.66900 20.17600  37.84600 1.000 27.25001 ?  246 SER B CB  1 
ATOM   3718 O OG  . SER B 1 266 ? -30.99700 18.93000  37.75900 1.000 25.31924 ?  246 SER B OG  1 
ATOM   3719 N N   . VAL B 1 267 ? -34.37000 20.38600  35.89600 1.000 32.98846 ?  247 VAL B N   1 
ATOM   3720 C CA  . VAL B 1 267 ? -35.13400 20.05100  34.69700 1.000 32.76803 ?  247 VAL B CA  1 
ATOM   3721 C C   . VAL B 1 267 ? -34.44700 20.68900  33.49800 1.000 32.77324 ?  247 VAL B C   1 
ATOM   3722 O O   . VAL B 1 267 ? -34.22000 21.90500  33.47600 1.000 33.19558 ?  247 VAL B O   1 
ATOM   3723 C CB  . VAL B 1 267 ? -36.59200 20.51900  34.81800 1.000 33.23682 ?  247 VAL B CB  1 
ATOM   3724 C CG1 . VAL B 1 267 ? -37.38600 20.10900  33.59200 1.000 27.10667 ?  247 VAL B CG1 1 
ATOM   3725 C CG2 . VAL B 1 267 ? -37.21900 19.94500  36.08600 1.000 26.89108 ?  247 VAL B CG2 1 
ATOM   3726 N N   . TRP B 1 268 ? -34.12900 19.87200  32.49600 1.000 31.19936 ?  248 TRP B N   1 
ATOM   3727 C CA  . TRP B 1 268 ? -33.31500 20.28700  31.36200 1.000 29.18822 ?  248 TRP B CA  1 
ATOM   3728 C C   . TRP B 1 268 ? -34.00700 19.90700  30.06200 1.000 33.89482 ?  248 TRP B C   1 
ATOM   3729 O O   . TRP B 1 268 ? -34.34400 18.73700  29.85200 1.000 32.25834 ?  248 TRP B O   1 
ATOM   3730 C CB  . TRP B 1 268 ? -31.93100 19.63800  31.41800 1.000 27.36988 ?  248 TRP B CB  1 
ATOM   3731 C CG  . TRP B 1 268 ? -31.27600 19.72100  32.75400 1.000 27.99673 ?  248 TRP B CG  1 
ATOM   3732 C CD1 . TRP B 1 268 ? -31.49000 18.90300  33.82500 1.000 28.75361 ?  248 TRP B CD1 1 
ATOM   3733 C CD2 . TRP B 1 268 ? -30.27500 20.66200  33.16000 1.000 28.96480 ?  248 TRP B CD2 1 
ATOM   3734 N NE1 . TRP B 1 268 ? -30.69100 19.28400  34.88000 1.000 29.34520 ?  248 TRP B NE1 1 
ATOM   3735 C CE2 . TRP B 1 268 ? -29.93700 20.36300  34.49600 1.000 31.64949 ?  248 TRP B CE2 1 
ATOM   3736 C CE3 . TRP B 1 268 ? -29.64100 21.73700  32.52600 1.000 26.78661 ?  248 TRP B CE3 1 
ATOM   3737 C CZ2 . TRP B 1 268 ? -28.99700 21.10200  35.21100 1.000 22.81266 ?  248 TRP B CZ2 1 
ATOM   3738 C CZ3 . TRP B 1 268 ? -28.70300 22.46300  33.23400 1.000 31.11394 ?  248 TRP B CZ3 1 
ATOM   3739 C CH2 . TRP B 1 268 ? -28.38900 22.14200  34.56200 1.000 30.44805 ?  248 TRP B CH2 1 
ATOM   3740 N N   . LYS B 1 269 ? -34.19200 20.89100  29.18600 1.000 32.48358 ?  249 LYS B N   1 
ATOM   3741 C CA  . LYS B 1 269 ? -34.82500 20.70400  27.88700 1.000 37.36239 ?  249 LYS B CA  1 
ATOM   3742 C C   . LYS B 1 269 ? -33.76500 20.74600  26.79000 1.000 34.35199 ?  249 LYS B C   1 
ATOM   3743 O O   . LYS B 1 269 ? -32.89200 21.62000  26.79100 1.000 35.31957 ?  249 LYS B O   1 
ATOM   3744 C CB  . LYS B 1 269 ? -35.88900 21.78700  27.64900 1.000 43.50619 ?  249 LYS B CB  1 
ATOM   3745 C CG  . LYS B 1 269 ? -36.78500 21.56900  26.44100 1.000 42.58263 ?  249 LYS B CG  1 
ATOM   3746 C CD  . LYS B 1 269 ? -37.72300 22.75500  26.24300 1.000 46.47542 ?  249 LYS B CD  1 
ATOM   3747 C CE  . LYS B 1 269 ? -38.93700 22.36900  25.40900 1.000 42.25175 ?  249 LYS B CE  1 
ATOM   3748 N N   . VAL B 1 270 ? -33.84400 19.79900  25.85200 1.000 37.92583 ?  250 VAL B N   1 
ATOM   3749 C CA  . VAL B 1 270 ? -32.81900 19.67400  24.82000 1.000 40.36932 ?  250 VAL B CA  1 
ATOM   3750 C C   . VAL B 1 270 ? -32.84300 20.88800  23.89900 1.000 38.49587 ?  250 VAL B C   1 
ATOM   3751 O O   . VAL B 1 270 ? -33.87800 21.54700  23.72100 1.000 52.04386 ?  250 VAL B O   1 
ATOM   3752 C CB  . VAL B 1 270 ? -33.01100 18.37100  24.02200 1.000 37.81284 ?  250 VAL B CB  1 
ATOM   3753 C CG1 . VAL B 1 270 ? -31.74300 18.01400  23.26200 1.000 47.00380 ?  250 VAL B CG1 1 
ATOM   3754 C CG2 . VAL B 1 270 ? -33.38700 17.24600  24.95300 1.000 40.15896 ?  250 VAL B CG2 1 
ATOM   3755 N N   . ILE B 1 271 ? -31.68200 21.18900  23.32000 1.000 50.24782 ?  251 ILE B N   1 
ATOM   3756 C CA  . ILE B 1 271 ? -31.49000 22.27400  22.35500 1.000 49.56966 ?  251 ILE B CA  1 
ATOM   3757 C C   . ILE B 1 271 ? -31.72100 23.61500  23.02400 1.000 49.08413 ?  251 ILE B C   1 
ATOM   3758 O O   . ILE B 1 271 ? -30.83200 24.12000  23.71700 1.000 50.22518 ?  251 ILE B O   1 
ATOM   3759 C CB  . ILE B 1 271 ? -32.39000 22.09500  21.11300 1.000 48.20679 ?  251 ILE B CB  1 
ATOM   3760 C CG1 . ILE B 1 271 ? -31.94300 20.87200  20.30700 1.000 46.95734 ?  251 ILE B CG1 1 
ATOM   3761 C CG2 . ILE B 1 271 ? -32.37400 23.34100  20.24900 1.000 66.47787 ?  251 ILE B CG2 1 
ATOM   3762 C CD1 . ILE B 1 271 ? -30.46400 20.53300  20.45100 1.000 49.17660 ?  251 ILE B CD1 1 
HETATM 3763 C C1  . EDO C 2 .   ? -29.48200 -0.93400  29.08100 1.000 42.87909 ?  301 EDO B C1  1 
HETATM 3764 O O1  . EDO C 2 .   ? -28.22900 -0.61600  28.45600 1.000 43.39153 ?  301 EDO B O1  1 
HETATM 3765 C C2  . EDO C 2 .   ? -29.78300 -2.41100  28.86000 1.000 42.98652 ?  301 EDO B C2  1 
HETATM 3766 O O2  . EDO C 2 .   ? -28.60600 -3.17400  29.14300 1.000 45.92352 ?  301 EDO B O2  1 
HETATM 3767 C C1  . EDO D 2 .   ? -41.95300 7.52100   61.98700 1.000 42.75562 ?  302 EDO B C1  1 
HETATM 3768 O O1  . EDO D 2 .   ? -42.66500 6.30300   62.23200 1.000 57.56095 ?  302 EDO B O1  1 
HETATM 3769 C C2  . EDO D 2 .   ? -42.06600 7.89000   60.51500 1.000 44.24577 ?  302 EDO B C2  1 
HETATM 3770 O O2  . EDO D 2 .   ? -43.31700 8.55500   60.28000 1.000 48.34511 ?  302 EDO B O2  1 
HETATM 3771 O O   . HOH E 3 .   ? -12.01800 -30.35400 38.43800 1.000 40.65508 ?  301 HOH A O   1 
HETATM 3772 O O   . HOH E 3 .   ? -9.72900  6.66200   29.88800 1.000 33.05335 ?  302 HOH A O   1 
HETATM 3773 O O   . HOH E 3 .   ? -4.97400  -27.73600 28.64900 1.000 34.44879 ?  303 HOH A O   1 
HETATM 3774 O O   . HOH E 3 .   ? -16.49700 -10.11800 24.57900 1.000 42.37069 ?  304 HOH A O   1 
HETATM 3775 O O   . HOH E 3 .   ? -19.58700 -21.86900 35.12600 1.000 31.25611 ?  305 HOH A O   1 
HETATM 3776 O O   . HOH E 3 .   ? 4.89800   -0.42200  25.19500 1.000 34.06662 ?  306 HOH A O   1 
HETATM 3777 O O   . HOH E 3 .   ? -6.19900  0.82900   40.55300 1.000 36.13207 ?  307 HOH A O   1 
HETATM 3778 O O   . HOH E 3 .   ? -5.81600  1.32000   16.74700 1.000 45.04716 ?  308 HOH A O   1 
HETATM 3779 O O   . HOH E 3 .   ? -2.29700  -12.43200 47.13800 1.000 41.93611 ?  309 HOH A O   1 
HETATM 3780 O O   . HOH E 3 .   ? -19.97900 -22.79800 19.13400 1.000 43.11141 ?  310 HOH A O   1 
HETATM 3781 O O   . HOH E 3 .   ? -6.10900  -5.80700  28.65300 1.000 32.54208 ?  311 HOH A O   1 
HETATM 3782 O O   . HOH E 3 .   ? 0.12900   -4.12800  28.78100 1.000 24.82126 ?  312 HOH A O   1 
HETATM 3783 O O   . HOH E 3 .   ? 2.32600   11.03800  15.45700 1.000 39.07702 ?  313 HOH A O   1 
HETATM 3784 O O   . HOH E 3 .   ? -3.17800  8.60400   29.10000 1.000 32.87639 ?  314 HOH A O   1 
HETATM 3785 O O   . HOH E 3 .   ? -9.41000  -23.02100 -3.98500 1.000 35.69269 ?  315 HOH A O   1 
HETATM 3786 O O   . HOH E 3 .   ? -10.12600 -17.31500 28.68600 1.000 38.14689 ?  316 HOH A O   1 
HETATM 3787 O O   . HOH E 3 .   ? -9.72200  -26.38900 34.05000 1.000 29.18773 ?  317 HOH A O   1 
HETATM 3788 O O   . HOH E 3 .   ? 4.97900   -14.42600 42.50600 1.000 44.18592 ?  318 HOH A O   1 
HETATM 3789 O O   . HOH E 3 .   ? -2.43800  -24.37100 33.01600 1.000 35.88102 ?  319 HOH A O   1 
HETATM 3790 O O   . HOH E 3 .   ? 3.61200   -21.34300 34.86800 1.000 42.50556 ?  320 HOH A O   1 
HETATM 3791 O O   . HOH E 3 .   ? -8.04800  -18.72900 15.21400 1.000 36.59112 ?  321 HOH A O   1 
HETATM 3792 O O   . HOH E 3 .   ? -10.73200 -7.44000  47.24100 1.000 42.69853 ?  322 HOH A O   1 
HETATM 3793 O O   . HOH E 3 .   ? -14.08300 -11.45700 24.69800 1.000 38.18691 ?  323 HOH A O   1 
HETATM 3794 O O   . HOH E 3 .   ? -6.66900  -23.66800 -1.23700 1.000 40.73367 ?  324 HOH A O   1 
HETATM 3795 O O   . HOH E 3 .   ? -5.79900  -18.12700 22.86800 1.000 38.14593 ?  325 HOH A O   1 
HETATM 3796 O O   . HOH E 3 .   ? 6.14900   1.06300   39.21500 1.000 35.86357 ?  326 HOH A O   1 
HETATM 3797 O O   . HOH E 3 .   ? 4.98900   20.40000  25.68700 1.000 36.55434 ?  327 HOH A O   1 
HETATM 3798 O O   . HOH E 3 .   ? -12.21600 -34.80600 33.54600 1.000 40.99066 ?  328 HOH A O   1 
HETATM 3799 O O   . HOH E 3 .   ? -13.27100 -23.45000 43.27600 1.000 41.39086 ?  329 HOH A O   1 
HETATM 3800 O O   . HOH E 3 .   ? -7.59500  -15.75200 24.70500 1.000 40.47378 ?  330 HOH A O   1 
HETATM 3801 O O   . HOH E 3 .   ? 1.33100   -16.99900 22.10200 1.000 36.04106 ?  331 HOH A O   1 
HETATM 3802 O O   . HOH E 3 .   ? -16.19700 5.69000   24.79300 1.000 33.50381 ?  332 HOH A O   1 
HETATM 3803 O O   . HOH E 3 .   ? 5.19500   -14.06000 16.12400 1.000 32.85323 ?  333 HOH A O   1 
HETATM 3804 O O   . HOH E 3 .   ? -16.90800 -4.40200  29.18000 1.000 42.00019 ?  334 HOH A O   1 
HETATM 3805 O O   . HOH E 3 .   ? 4.98200   12.42000  15.07100 1.000 39.36937 ?  335 HOH A O   1 
HETATM 3806 O O   . HOH E 3 .   ? -16.39300 -35.60900 26.32900 1.000 51.81858 ?  336 HOH A O   1 
HETATM 3807 O O   . HOH E 3 .   ? -2.03200  -27.08800 30.52800 1.000 35.34756 ?  337 HOH A O   1 
HETATM 3808 O O   . HOH E 3 .   ? -23.29500 -18.99700 22.48100 1.000 40.37665 ?  338 HOH A O   1 
HETATM 3809 O O   . HOH E 3 .   ? -26.02300 -14.99700 14.92800 1.000 60.22550 ?  339 HOH A O   1 
HETATM 3810 O O   . HOH E 3 .   ? -23.78400 -14.36500 34.28800 1.000 40.08122 ?  340 HOH A O   1 
HETATM 3811 O O   . HOH E 3 .   ? -21.66100 -9.59900  36.71800 1.000 45.36947 ?  341 HOH A O   1 
HETATM 3812 O O   . HOH E 3 .   ? -4.19600  -18.89300 20.24900 1.000 34.97868 ?  342 HOH A O   1 
HETATM 3813 O O   . HOH E 3 .   ? -8.18900  -21.98800 0.19700  1.000 35.45398 ?  343 HOH A O   1 
HETATM 3814 O O   . HOH E 3 .   ? -7.52300  4.01200   15.55800 1.000 43.88238 ?  344 HOH A O   1 
HETATM 3815 O O   . HOH E 3 .   ? -5.43000  -22.76700 7.25000  1.000 45.99627 ?  345 HOH A O   1 
HETATM 3816 O O   . HOH E 3 .   ? 9.19700   -9.89400  25.21500 1.000 35.37173 ?  346 HOH A O   1 
HETATM 3817 O O   . HOH E 3 .   ? -10.46300 5.02400   15.72700 1.000 45.44064 ?  347 HOH A O   1 
HETATM 3818 O O   . HOH E 3 .   ? -16.96400 1.83900   38.04700 1.000 40.20065 ?  348 HOH A O   1 
HETATM 3819 O O   . HOH E 3 .   ? -10.94200 4.84300   43.31000 1.000 45.80172 ?  349 HOH A O   1 
HETATM 3820 O O   . HOH E 3 .   ? -6.51700  4.68100   41.58100 1.000 44.05627 ?  350 HOH A O   1 
HETATM 3821 O O   . HOH E 3 .   ? -9.90200  -2.61700  19.57700 1.000 45.05517 ?  351 HOH A O   1 
HETATM 3822 O O   . HOH E 3 .   ? -7.69900  -6.00800  21.99300 1.000 43.22640 ?  352 HOH A O   1 
HETATM 3823 O O   . HOH E 3 .   ? -13.28500 11.87800  22.46600 1.000 45.97781 ?  353 HOH A O   1 
HETATM 3824 O O   . HOH E 3 .   ? -12.93000 -23.97000 2.68900  1.000 39.26217 ?  354 HOH A O   1 
HETATM 3825 O O   . HOH E 3 .   ? -5.81500  -28.59200 39.85100 1.000 46.61415 ?  355 HOH A O   1 
HETATM 3826 O O   . HOH E 3 .   ? -8.33200  -26.93500 9.20900  1.000 54.14321 ?  356 HOH A O   1 
HETATM 3827 O O   . HOH E 3 .   ? 7.98600   -12.35600 21.88800 1.000 48.13798 ?  357 HOH A O   1 
HETATM 3828 O O   . HOH E 3 .   ? -15.37000 -8.78300  28.41700 1.000 38.08112 ?  358 HOH A O   1 
HETATM 3829 O O   . HOH E 3 .   ? -20.79200 -6.46900  35.91400 1.000 46.13242 ?  359 HOH A O   1 
HETATM 3830 O O   . HOH E 3 .   ? -24.39700 -9.99300  26.10100 1.000 46.01105 ?  360 HOH A O   1 
HETATM 3831 O O   . HOH E 3 .   ? 4.66900   -18.23100 20.27900 1.000 43.03935 ?  361 HOH A O   1 
HETATM 3832 O O   . HOH E 3 .   ? 7.64700   -5.70100  26.22900 1.000 44.33711 ?  362 HOH A O   1 
HETATM 3833 O O   . HOH E 3 .   ? -16.19300 -6.87400  30.37400 1.000 41.50053 ?  363 HOH A O   1 
HETATM 3834 O O   . HOH E 3 .   ? -17.09700 -14.63000 42.88700 1.000 44.98401 ?  364 HOH A O   1 
HETATM 3835 O O   . HOH E 3 .   ? 1.12700   -21.81400 24.57600 1.000 42.79205 ?  365 HOH A O   1 
HETATM 3836 O O   . HOH E 3 .   ? -19.91200 -8.12500  37.28000 1.000 39.27258 ?  366 HOH A O   1 
HETATM 3837 O O   . HOH E 3 .   ? -12.80900 2.69800   15.17100 1.000 44.59211 ?  367 HOH A O   1 
HETATM 3838 O O   . HOH E 3 .   ? -17.64200 3.95500   22.62300 1.000 44.91247 ?  368 HOH A O   1 
HETATM 3839 O O   . HOH E 3 .   ? -24.12600 -12.11100 36.05900 1.000 51.55386 ?  369 HOH A O   1 
HETATM 3840 O O   . HOH E 3 .   ? -9.64700  -30.21700 40.76300 1.000 43.94696 ?  370 HOH A O   1 
HETATM 3841 O O   . HOH E 3 .   ? 6.44000   -16.04200 34.19000 1.000 38.36640 ?  371 HOH A O   1 
HETATM 3842 O O   . HOH E 3 .   ? 5.560     -16.129   12.261   1.000 41.94403 ?  372 HOH A O   1 
HETATM 3843 O O   . HOH E 3 .   ? -11.53600 -24.62000 -0.88100 1.000 46.23658 ?  373 HOH A O   1 
HETATM 3844 O O   . HOH E 3 .   ? -10.56700 -28.76000 17.78500 1.000 48.98073 ?  374 HOH A O   1 
HETATM 3845 O O   . HOH E 3 .   ? -14.82100 -2.59600  38.18700 1.000 37.92503 ?  375 HOH A O   1 
HETATM 3846 O O   . HOH E 3 .   ? 4.54700   7.63600   36.00500 1.000 55.57898 ?  376 HOH A O   1 
HETATM 3847 O O   . HOH E 3 .   ? -1.221    -33.528   33.959   1.000 50.48007 ?  377 HOH A O   1 
HETATM 3848 O O   . HOH E 3 .   ? -3.95700  -27.11900 42.05000 1.000 53.81657 ?  378 HOH A O   1 
HETATM 3849 O O   . HOH E 3 .   ? -5.64600  -19.65700 15.79500 1.000 41.89707 ?  379 HOH A O   1 
HETATM 3850 O O   . HOH E 3 .   ? -3.04300  8.16200   31.65000 1.000 48.23886 ?  380 HOH A O   1 
HETATM 3851 O O   . HOH E 3 .   ? -12.83400 -31.99900 15.05700 1.000 42.25948 ?  381 HOH A O   1 
HETATM 3852 O O   . HOH E 3 .   ? -7.23700  9.02400   29.35500 1.000 50.56336 ?  382 HOH A O   1 
HETATM 3853 O O   . HOH E 3 .   ? -2.72500  -29.49200 38.05000 1.000 48.78612 ?  383 HOH A O   1 
HETATM 3854 O O   . HOH E 3 .   ? -6.81500  -30.67000 40.65200 1.000 44.95533 ?  384 HOH A O   1 
HETATM 3855 O O   . HOH E 3 .   ? -10.16400 -31.54700 21.33000 1.000 44.14389 ?  385 HOH A O   1 
HETATM 3856 O O   . HOH E 3 .   ? 7.64200   -19.17300 11.69300 1.000 46.52025 ?  386 HOH A O   1 
HETATM 3857 O O   . HOH E 3 .   ? -6.97200  12.64700  26.82000 1.000 52.23547 ?  387 HOH A O   1 
HETATM 3858 O O   . HOH E 3 .   ? -8.64500  -14.86100 28.16700 1.000 47.27400 ?  388 HOH A O   1 
HETATM 3859 O O   . HOH E 3 .   ? -11.85500 -10.08500 15.93500 1.000 55.95655 ?  389 HOH A O   1 
HETATM 3860 O O   . HOH E 3 .   ? -2.70700  13.88900  29.17000 1.000 57.94973 ?  390 HOH A O   1 
HETATM 3861 O O   . HOH E 3 .   ? -0.30600  -26.27100 35.84300 1.000 51.17186 ?  391 HOH A O   1 
HETATM 3862 O O   . HOH E 3 .   ? -0.62200  13.31000  29.58000 1.000 56.33565 ?  392 HOH A O   1 
HETATM 3863 O O   . HOH E 3 .   ? 6.32400   -18.92200 29.69900 1.000 44.89181 ?  393 HOH A O   1 
HETATM 3864 O O   . HOH E 3 .   ? 5.45300   -21.26200 37.13400 1.000 50.48304 ?  394 HOH A O   1 
HETATM 3865 O O   . HOH E 3 .   ? 0.14000   -27.30100 29.95700 1.000 44.77697 ?  395 HOH A O   1 
HETATM 3866 O O   . HOH E 3 .   ? 8.10200   -15.40700 35.69000 1.000 41.43818 ?  396 HOH A O   1 
HETATM 3867 O O   . HOH E 3 .   ? -6.84700  12.91200  23.49500 1.000 51.00727 ?  397 HOH A O   1 
HETATM 3868 O O   . HOH E 3 .   ? -8.66900  -13.44900 24.16400 1.000 47.56495 ?  398 HOH A O   1 
HETATM 3869 O O   . HOH E 3 .   ? -18.66800 -27.82600 36.54800 1.000 39.83115 ?  399 HOH A O   1 
HETATM 3870 O O   . HOH E 3 .   ? 6.52000   -15.30100 14.26400 1.000 34.31680 ?  400 HOH A O   1 
HETATM 3871 O O   . HOH E 3 .   ? -15.98500 -35.53900 21.49300 1.000 56.53592 ?  401 HOH A O   1 
HETATM 3872 O O   . HOH E 3 .   ? 6.96800   -11.36300 19.75700 1.000 40.15490 ?  402 HOH A O   1 
HETATM 3873 O O   . HOH E 3 .   ? 1.82600   -23.49300 34.45200 1.000 47.83933 ?  403 HOH A O   1 
HETATM 3874 O O   . HOH E 3 .   ? -19.32800 -15.98500 9.66500  1.000 60.24204 ?  404 HOH A O   1 
HETATM 3875 O O   . HOH E 3 .   ? -1.24100  -21.60600 8.95700  1.000 43.35956 ?  405 HOH A O   1 
HETATM 3876 O O   . HOH E 3 .   ? 6.59600   -12.14300 17.48900 1.000 44.74264 ?  406 HOH A O   1 
HETATM 3877 O O   . HOH F 3 .   ? -29.50800 26.69900  30.51600 1.000 40.15030 ?  401 HOH B O   1 
HETATM 3878 O O   . HOH F 3 .   ? -26.26200 -1.09100  29.88800 1.000 41.84769 ?  402 HOH B O   1 
HETATM 3879 O O   . HOH F 3 .   ? -44.25100 6.26100   50.88300 1.000 40.18283 ?  403 HOH B O   1 
HETATM 3880 O O   . HOH F 3 .   ? -38.24700 0.10800   68.99400 1.000 36.33726 ?  404 HOH B O   1 
HETATM 3881 O O   . HOH F 3 .   ? -52.69300 2.78900   47.64000 1.000 60.01258 ?  405 HOH B O   1 
HETATM 3882 O O   . HOH F 3 .   ? -17.72600 20.62700  38.11100 1.000 37.18601 ?  406 HOH B O   1 
HETATM 3883 O O   . HOH F 3 .   ? -17.48700 13.03000  50.81800 1.000 41.41098 ?  407 HOH B O   1 
HETATM 3884 O O   . HOH F 3 .   ? -38.60800 3.65100   39.78500 1.000 42.94899 ?  408 HOH B O   1 
HETATM 3885 O O   . HOH F 3 .   ? -14.20900 17.36900  40.31100 1.000 42.16761 ?  409 HOH B O   1 
HETATM 3886 O O   . HOH F 3 .   ? -32.28700 -1.10400  65.56000 1.000 41.38718 ?  410 HOH B O   1 
HETATM 3887 O O   . HOH F 3 .   ? -25.42900 16.18400  27.32300 1.000 38.41229 ?  411 HOH B O   1 
HETATM 3888 O O   . HOH F 3 .   ? -29.43100 12.07600  39.54000 1.000 28.53548 ?  412 HOH B O   1 
HETATM 3889 O O   . HOH F 3 .   ? -51.76200 -1.44400  31.89800 1.000 42.06729 ?  413 HOH B O   1 
HETATM 3890 O O   . HOH F 3 .   ? -18.06400 16.68400  29.25500 1.000 54.09086 ?  414 HOH B O   1 
HETATM 3891 O O   . HOH F 3 .   ? -28.07500 23.62300  44.08600 1.000 32.21251 ?  415 HOH B O   1 
HETATM 3892 O O   . HOH F 3 .   ? -47.78600 8.80500   49.34000 1.000 43.75730 ?  416 HOH B O   1 
HETATM 3893 O O   . HOH F 3 .   ? -12.03500 29.22100  40.17200 1.000 42.87742 ?  417 HOH B O   1 
HETATM 3894 O O   . HOH F 3 .   ? -21.99100 -1.93000  33.74300 1.000 41.70831 ?  418 HOH B O   1 
HETATM 3895 O O   . HOH F 3 .   ? -6.366    30.046    37.995   1.000 40.06954 ?  419 HOH B O   1 
HETATM 3896 O O   . HOH F 3 .   ? -17.77800 13.19300  36.45500 1.000 39.42226 ?  420 HOH B O   1 
HETATM 3897 O O   . HOH F 3 .   ? -41.44400 13.70700  48.43700 1.000 34.60874 ?  421 HOH B O   1 
HETATM 3898 O O   . HOH F 3 .   ? -20.27300 10.36800  45.11000 1.000 31.11706 ?  422 HOH B O   1 
HETATM 3899 O O   . HOH F 3 .   ? -44.42900 0.48900   57.93800 1.000 39.73694 ?  423 HOH B O   1 
HETATM 3900 O O   . HOH F 3 .   ? -28.37200 26.50200  27.56600 1.000 45.22917 ?  424 HOH B O   1 
HETATM 3901 O O   . HOH F 3 .   ? -28.44800 0.08100   41.47800 1.000 44.16080 ?  425 HOH B O   1 
HETATM 3902 O O   . HOH F 3 .   ? -40.73500 -5.85600  32.46600 1.000 37.18436 ?  426 HOH B O   1 
HETATM 3903 O O   . HOH F 3 .   ? -33.99800 23.53500  44.26900 1.000 39.36685 ?  427 HOH B O   1 
HETATM 3904 O O   . HOH F 3 .   ? -46.74100 4.33500   49.12200 1.000 45.11761 ?  428 HOH B O   1 
HETATM 3905 O O   . HOH F 3 .   ? -22.48700 27.16800  31.68600 1.000 52.41084 ?  429 HOH B O   1 
HETATM 3906 O O   . HOH F 3 .   ? -38.16700 -1.50400  73.08000 1.000 32.23425 ?  430 HOH B O   1 
HETATM 3907 O O   . HOH F 3 .   ? -49.79600 -3.51800  49.06700 1.000 49.39015 ?  431 HOH B O   1 
HETATM 3908 O O   . HOH F 3 .   ? -48.31600 15.51700  36.99500 1.000 40.71830 ?  432 HOH B O   1 
HETATM 3909 O O   . HOH F 3 .   ? -48.57800 8.75200   38.30300 1.000 38.80202 ?  433 HOH B O   1 
HETATM 3910 O O   . HOH F 3 .   ? -39.32500 17.21300  54.85200 1.000 37.16294 ?  434 HOH B O   1 
HETATM 3911 O O   . HOH F 3 .   ? -30.32100 18.33400  40.43500 1.000 25.96751 ?  435 HOH B O   1 
HETATM 3912 O O   . HOH F 3 .   ? -36.49800 0.65700   24.47700 1.000 41.35343 ?  436 HOH B O   1 
HETATM 3913 O O   . HOH F 3 .   ? -40.17100 0.89600   70.82200 1.000 38.40735 ?  437 HOH B O   1 
HETATM 3914 O O   . HOH F 3 .   ? -27.73000 9.68700   46.03900 1.000 41.17381 ?  438 HOH B O   1 
HETATM 3915 O O   . HOH F 3 .   ? -32.60800 9.44700   20.54900 1.000 41.55023 ?  439 HOH B O   1 
HETATM 3916 O O   . HOH F 3 .   ? -18.09200 10.64400  26.14700 1.000 51.19357 ?  440 HOH B O   1 
HETATM 3917 O O   . HOH F 3 .   ? -56.12600 0.64100   32.15600 1.000 52.35664 ?  441 HOH B O   1 
HETATM 3918 O O   . HOH F 3 .   ? -37.38000 -0.60300  55.67400 1.000 43.04865 ?  442 HOH B O   1 
HETATM 3919 O O   . HOH F 3 .   ? -20.12500 2.08100   34.46700 1.000 40.92883 ?  443 HOH B O   1 
HETATM 3920 O O   . HOH F 3 .   ? -33.97200 -9.80500  46.50300 1.000 48.42271 ?  444 HOH B O   1 
HETATM 3921 O O   . HOH F 3 .   ? -10.77600 10.33700  44.55100 1.000 48.12802 ?  445 HOH B O   1 
HETATM 3922 O O   . HOH F 3 .   ? -50.26300 4.42000   42.24800 1.000 42.32166 ?  446 HOH B O   1 
HETATM 3923 O O   . HOH F 3 .   ? -42.21600 11.08200  20.75800 1.000 36.79627 ?  447 HOH B O   1 
HETATM 3924 O O   . HOH F 3 .   ? -30.26000 -0.86000  50.40500 1.000 44.08221 ?  448 HOH B O   1 
HETATM 3925 O O   . HOH F 3 .   ? -35.88800 1.67400   20.23000 1.000 44.34779 ?  449 HOH B O   1 
HETATM 3926 O O   . HOH F 3 .   ? -40.46200 7.66700   49.58800 1.000 40.62524 ?  450 HOH B O   1 
HETATM 3927 O O   . HOH F 3 .   ? -26.55000 -6.68100  39.05600 1.000 44.80256 ?  451 HOH B O   1 
HETATM 3928 O O   . HOH F 3 .   ? -28.80000 -7.89200  51.35600 1.000 54.85617 ?  452 HOH B O   1 
HETATM 3929 O O   . HOH F 3 .   ? -18.05200 30.02200  44.80800 1.000 50.24900 ?  453 HOH B O   1 
HETATM 3930 O O   . HOH F 3 .   ? -44.33100 19.32700  46.26500 1.000 45.12641 ?  454 HOH B O   1 
HETATM 3931 O O   . HOH F 3 .   ? -15.23300 11.27300  50.46600 1.000 38.24389 ?  455 HOH B O   1 
HETATM 3932 O O   . HOH F 3 .   ? -40.11800 9.60100   51.39700 1.000 33.92867 ?  456 HOH B O   1 
HETATM 3933 O O   . HOH F 3 .   ? -32.11800 24.79800  47.66800 1.000 53.24854 ?  457 HOH B O   1 
HETATM 3934 O O   . HOH F 3 .   ? -39.76000 6.44200   46.67700 1.000 36.98854 ?  458 HOH B O   1 
HETATM 3935 O O   . HOH F 3 .   ? -25.27900 5.88800   27.95600 1.000 41.78158 ?  459 HOH B O   1 
HETATM 3936 O O   . HOH F 3 .   ? -38.43000 -4.18200  66.64900 1.000 46.45061 ?  460 HOH B O   1 
HETATM 3937 O O   . HOH F 3 .   ? -24.47000 18.32400  27.22700 1.000 42.23268 ?  461 HOH B O   1 
HETATM 3938 O O   . HOH F 3 .   ? -9.76400  11.85900  42.21700 1.000 42.41890 ?  462 HOH B O   1 
HETATM 3939 O O   . HOH F 3 .   ? -48.78600 -9.29600  34.41800 1.000 52.64368 ?  463 HOH B O   1 
HETATM 3940 O O   . HOH F 3 .   ? -43.49400 20.74600  28.55800 1.000 49.08452 ?  464 HOH B O   1 
HETATM 3941 O O   . HOH F 3 .   ? -29.82800 15.59800  20.75700 1.000 52.53835 ?  465 HOH B O   1 
HETATM 3942 O O   . HOH F 3 .   ? -10.08100 28.97800  49.54400 1.000 42.30637 ?  466 HOH B O   1 
HETATM 3943 O O   . HOH F 3 .   ? -42.08600 2.80200   22.40200 1.000 44.37632 ?  467 HOH B O   1 
HETATM 3944 O O   . HOH F 3 .   ? -15.91200 30.36600  47.01000 1.000 49.12176 ?  468 HOH B O   1 
HETATM 3945 O O   . HOH F 3 .   ? -32.58600 -7.26200  31.88400 1.000 40.16082 ?  469 HOH B O   1 
HETATM 3946 O O   . HOH F 3 .   ? -3.556    26.924    41.961   1.000 46.73096 ?  470 HOH B O   1 
HETATM 3947 O O   . HOH F 3 .   ? -21.25800 14.34400  50.75200 1.000 35.16535 ?  471 HOH B O   1 
HETATM 3948 O O   . HOH F 3 .   ? -20.01600 3.88700   38.14000 1.000 45.15870 ?  472 HOH B O   1 
HETATM 3949 O O   . HOH F 3 .   ? -23.80500 9.04100   47.59700 1.000 37.83058 ?  473 HOH B O   1 
HETATM 3950 O O   . HOH F 3 .   ? -36.40500 -2.44900  54.76100 1.000 40.66931 ?  474 HOH B O   1 
HETATM 3951 O O   . HOH F 3 .   ? -30.19500 25.97100  43.40400 1.000 44.68917 ?  475 HOH B O   1 
HETATM 3952 O O   . HOH F 3 .   ? -20.082   26.126    51.465   1.000 46.99493 ?  476 HOH B O   1 
HETATM 3953 O O   . HOH F 3 .   ? -29.27400 9.46600   49.59600 1.000 50.29051 ?  477 HOH B O   1 
HETATM 3954 O O   . HOH F 3 .   ? -34.12700 -3.53600  54.75100 1.000 39.80038 ?  478 HOH B O   1 
HETATM 3955 O O   . HOH F 3 .   ? -20.45000 18.24400  27.99300 1.000 46.93147 ?  479 HOH B O   1 
HETATM 3956 O O   . HOH F 3 .   ? -19.44600 5.90600   35.98300 1.000 35.73544 ?  480 HOH B O   1 
HETATM 3957 O O   . HOH F 3 .   ? -48.78200 6.52800   53.13700 1.000 47.68887 ?  481 HOH B O   1 
HETATM 3958 O O   . HOH F 3 .   ? -41.60300 5.89000   52.64700 1.000 46.79104 ?  482 HOH B O   1 
HETATM 3959 O O   . HOH F 3 .   ? -37.12000 2.12400   53.87000 1.000 44.43774 ?  483 HOH B O   1 
HETATM 3960 O O   . HOH F 3 .   ? -45.61600 -6.83000  59.47400 1.000 46.69098 ?  484 HOH B O   1 
HETATM 3961 O O   . HOH F 3 .   ? -37.48400 6.24400   44.41800 1.000 40.99314 ?  485 HOH B O   1 
HETATM 3962 O O   . HOH F 3 .   ? -41.81000 9.02800   53.02500 1.000 40.11545 ?  486 HOH B O   1 
HETATM 3963 O O   . HOH F 3 .   ? -44.70600 4.61100   22.72100 1.000 43.48258 ?  487 HOH B O   1 
HETATM 3964 O O   . HOH F 3 .   ? -56.49700 2.47300   39.19800 1.000 46.01646 ?  488 HOH B O   1 
HETATM 3965 O O   . HOH F 3 .   ? -12.10400 7.19300   44.46800 1.000 46.15793 ?  489 HOH B O   1 
HETATM 3966 O O   . HOH F 3 .   ? -16.16300 16.10800  35.98600 1.000 46.35943 ?  490 HOH B O   1 
HETATM 3967 O O   . HOH F 3 .   ? -16.24400 8.25900   51.02400 1.000 48.42983 ?  491 HOH B O   1 
HETATM 3968 O O   . HOH F 3 .   ? -47.20400 11.51500  19.29300 1.000 52.89458 ?  492 HOH B O   1 
HETATM 3969 O O   . HOH F 3 .   ? -43.36400 -10.05100 60.52500 1.000 47.98143 ?  493 HOH B O   1 
HETATM 3970 O O   . HOH F 3 .   ? -51.85500 4.76100   44.96800 1.000 51.10993 ?  494 HOH B O   1 
HETATM 3971 O O   . HOH F 3 .   ? -19.92200 27.33300  41.52900 1.000 45.85827 ?  495 HOH B O   1 
HETATM 3972 O O   . HOH F 3 .   ? -38.17400 24.35200  45.88500 1.000 42.57726 ?  496 HOH B O   1 
HETATM 3973 O O   . HOH F 3 .   ? -28.64000 2.31700   37.76600 1.000 41.10593 ?  497 HOH B O   1 
HETATM 3974 O O   . HOH F 3 .   ? -48.27700 -6.25200  54.70100 1.000 50.84163 ?  498 HOH B O   1 
HETATM 3975 O O   . HOH F 3 .   ? -24.26800 28.58500  38.34000 1.000 50.50471 ?  499 HOH B O   1 
HETATM 3976 O O   . HOH F 3 .   ? -39.02300 4.53800   53.46600 1.000 44.88681 ?  500 HOH B O   1 
HETATM 3977 O O   . HOH F 3 .   ? -36.50900 13.85100  17.61900 1.000 47.36828 ?  501 HOH B O   1 
HETATM 3978 O O   . HOH F 3 .   ? -24.87700 30.92200  35.08300 1.000 66.55593 ?  502 HOH B O   1 
HETATM 3979 O O   . HOH F 3 .   ? -32.35800 6.98400   47.14200 1.000 49.52403 ?  503 HOH B O   1 
HETATM 3980 O O   . HOH F 3 .   ? -44.17000 20.32100  37.72000 1.000 45.70666 ?  504 HOH B O   1 
HETATM 3981 O O   . HOH F 3 .   ? -38.95200 -4.38900  68.94700 1.000 48.92871 ?  505 HOH B O   1 
HETATM 3982 O O   . HOH F 3 .   ? -37.40500 27.29300  39.25800 1.000 51.24127 ?  506 HOH B O   1 
HETATM 3983 O O   . HOH F 3 .   ? -29.67900 4.43100   53.49900 1.000 54.81413 ?  507 HOH B O   1 
HETATM 3984 O O   . HOH F 3 .   ? -29.77500 3.08900   41.66000 1.000 49.51753 ?  508 HOH B O   1 
HETATM 3985 O O   . HOH F 3 .   ? -48.31500 5.87700   48.45200 1.000 52.43620 ?  509 HOH B O   1 
HETATM 3986 O O   . HOH F 3 .   ? -41.205   3.823     66.647   1.000 44.94353 ?  510 HOH B O   1 
HETATM 3987 O O   . HOH F 3 .   ? -29.24600 6.98100   50.06800 1.000 56.58226 ?  511 HOH B O   1 
HETATM 3988 O O   . HOH F 3 .   ? -37.52700 -15.82600 46.33800 1.000 62.38878 ?  512 HOH B O   1 
HETATM 3989 O O   . HOH F 3 .   ? -18.14700 7.66200   25.54000 1.000 43.28908 ?  513 HOH B O   1 
HETATM 3990 O O   . HOH F 3 .   ? -41.23300 12.90500  19.09700 1.000 52.27042 ?  514 HOH B O   1 
HETATM 3991 O O   . HOH F 3 .   ? -31.47100 22.66000  51.13900 1.000 48.54863 ?  515 HOH B O   1 
HETATM 3992 O O   . HOH F 3 .   ? -43.72500 -11.95100 52.80600 1.000 58.23195 ?  516 HOH B O   1 
HETATM 3993 O O   . HOH F 3 .   ? -34.11900 6.44300   44.49300 1.000 47.64303 ?  517 HOH B O   1 
HETATM 3994 O O   . HOH F 3 .   ? -51.57900 -2.09700  49.55300 1.000 50.67838 ?  518 HOH B O   1 
HETATM 3995 O O   . HOH F 3 .   ? -44.95800 23.25800  29.84100 1.000 52.56184 ?  519 HOH B O   1 
HETATM 3996 O O   . HOH F 3 .   ? -33.93600 28.08200  37.24100 1.000 55.21060 ?  520 HOH B O   1 
HETATM 3997 O O   . HOH F 3 .   ? -49.81900 13.33700  37.37400 1.000 43.89617 ?  521 HOH B O   1 
HETATM 3998 O O   . HOH F 3 .   ? -19.06200 8.94700   52.90500 1.000 56.90350 ?  522 HOH B O   1 
# 
