data_8YVH
# 
_entry.id   8YVH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8YVH         pdb_00008yvh 10.2210/pdb8yvh/pdb 
WWPDB D_1300044675 ?            ?                   
# 
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 2025-04-02 ? 
2 'Structure model' 2 0 2025-04-16 ? 
# 
_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' Advisory               
2 2 'Structure model' 'Atomic model'         
3 2 'Structure model' 'Database references'  
4 2 'Structure model' 'Derived calculations' 
5 2 'Structure model' 'Polymer sequence'     
6 2 'Structure model' 'Source and taxonomy'  
7 2 'Structure model' 'Structure summary'    
# 
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' atom_site                       
2  2 'Structure model' entity                          
3  2 'Structure model' entity_name_com                 
4  2 'Structure model' entity_poly                     
5  2 'Structure model' entity_poly_seq                 
6  2 'Structure model' entity_src_gen                  
7  2 'Structure model' pdbx_poly_seq_scheme            
8  2 'Structure model' pdbx_struct_sheet_hbond         
9  2 'Structure model' pdbx_unobs_or_zero_occ_residues 
10 2 'Structure model' struct_conf                     
11 2 'Structure model' struct_ref_seq                  
12 2 'Structure model' struct_ref_seq_dif              
13 2 'Structure model' struct_sheet_range              
# 
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' '_atom_site.label_seq_id'                       
2  2 'Structure model' '_entity.formula_weight'                        
3  2 'Structure model' '_entity_poly.pdbx_seq_one_letter_code'         
4  2 'Structure model' '_entity_poly.pdbx_seq_one_letter_code_can'     
5  2 'Structure model' '_entity_src_gen.pdbx_end_seq_num'              
6  2 'Structure model' '_pdbx_struct_sheet_hbond.range_1_label_seq_id' 
7  2 'Structure model' '_pdbx_struct_sheet_hbond.range_2_label_seq_id' 
8  2 'Structure model' '_struct_conf.beg_label_seq_id'                 
9  2 'Structure model' '_struct_conf.end_label_seq_id'                 
10 2 'Structure model' '_struct_ref_seq.seq_align_beg'                 
11 2 'Structure model' '_struct_ref_seq.seq_align_end'                 
12 2 'Structure model' '_struct_sheet_range.beg_label_seq_id'          
13 2 'Structure model' '_struct_sheet_range.end_label_seq_id'          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YVH 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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                 2 
_pdbx_contact_author.email              gaoweizheng@ecust.edu.cn 
_pdbx_contact_author.name_first         GaoWei 
_pdbx_contact_author.name_last          Zheng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5918-6047 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Shi, M.'     1 0009-0009-9756-3822 
'zheng, G.W.' 2 ?                   
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'NADPH complex of Imine Reductase Mutant(M6) from Pochonia chlamydosporia 170' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Shi, M.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0009-0009-9756-3822 
# 
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 Oxidoreductase                                     32828.449 2   ? ? ? ? 
2 non-polymer syn 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 743.405   2   ? ? ? ? 
3 non-polymer syn 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL           122.143   1   ? ? ? ? 
4 water       nat water                                              18.015    455 ? ? ? ? 
# 
_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       
;MGSSHHHHHHSSGENLYFQGMSSSNKPHVSLIGLGNMGLAIANCLIKSGCKLTVWNRSAEKAASLVPQGATVAATPAECV
ASSPTIVICLLNQDVVQQTLDEVIDLSGKTIINLTNGTPQQAVKVATLVQQRGAESYIHGAIMTTPEYLGQPSSVTLISG
PKTAYESQKELLSSIGTTRHVSDDIAKASLLDNALLSVMSGVFEGWVQALAIVGAAGEDEVDFAALASPLVASMADQLPV
IAGRVREKQYVGGSPITMGLEALENISETSRELGVGVLLGSMREVMSEAVKKGKGGESIAGLVPMLTELDKKW
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGENLYFQGMSSSNKPHVSLIGLGNMGLAIANCLIKSGCKLTVWNRSAEKAASLVPQGATVAATPAECV
ASSPTIVICLLNQDVVQQTLDEVIDLSGKTIINLTNGTPQQAVKVATLVQQRGAESYIHGAIMTTPEYLGQPSSVTLISG
PKTAYESQKELLSSIGTTRHVSDDIAKASLLDNALLSVMSGVFEGWVQALAIVGAAGEDEVDFAALASPLVASMADQLPV
IAGRVREKQYVGGSPITMGLEALENISETSRELGVGVLLGSMREVMSEAVKKGKGGESIAGLVPMLTELDKKW
;
_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 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' NAP 
3 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL           TRS 
4 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  GLU n 
1 15  ASN n 
1 16  LEU n 
1 17  TYR n 
1 18  PHE n 
1 19  GLN n 
1 20  GLY n 
1 21  MET n 
1 22  SER n 
1 23  SER n 
1 24  SER n 
1 25  ASN n 
1 26  LYS n 
1 27  PRO n 
1 28  HIS n 
1 29  VAL n 
1 30  SER n 
1 31  LEU n 
1 32  ILE n 
1 33  GLY n 
1 34  LEU n 
1 35  GLY n 
1 36  ASN n 
1 37  MET n 
1 38  GLY n 
1 39  LEU n 
1 40  ALA n 
1 41  ILE n 
1 42  ALA n 
1 43  ASN n 
1 44  CYS n 
1 45  LEU n 
1 46  ILE n 
1 47  LYS n 
1 48  SER n 
1 49  GLY n 
1 50  CYS n 
1 51  LYS n 
1 52  LEU n 
1 53  THR n 
1 54  VAL n 
1 55  TRP n 
1 56  ASN n 
1 57  ARG n 
1 58  SER n 
1 59  ALA n 
1 60  GLU n 
1 61  LYS n 
1 62  ALA n 
1 63  ALA n 
1 64  SER n 
1 65  LEU n 
1 66  VAL n 
1 67  PRO n 
1 68  GLN n 
1 69  GLY n 
1 70  ALA n 
1 71  THR n 
1 72  VAL n 
1 73  ALA n 
1 74  ALA n 
1 75  THR n 
1 76  PRO n 
1 77  ALA n 
1 78  GLU n 
1 79  CYS n 
1 80  VAL n 
1 81  ALA n 
1 82  SER n 
1 83  SER n 
1 84  PRO n 
1 85  THR n 
1 86  ILE n 
1 87  VAL n 
1 88  ILE n 
1 89  CYS n 
1 90  LEU n 
1 91  LEU n 
1 92  ASN n 
1 93  GLN n 
1 94  ASP n 
1 95  VAL n 
1 96  VAL n 
1 97  GLN n 
1 98  GLN n 
1 99  THR n 
1 100 LEU n 
1 101 ASP n 
1 102 GLU n 
1 103 VAL n 
1 104 ILE n 
1 105 ASP n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 LYS n 
1 110 THR n 
1 111 ILE n 
1 112 ILE n 
1 113 ASN n 
1 114 LEU n 
1 115 THR n 
1 116 ASN n 
1 117 GLY n 
1 118 THR n 
1 119 PRO n 
1 120 GLN n 
1 121 GLN n 
1 122 ALA n 
1 123 VAL n 
1 124 LYS n 
1 125 VAL n 
1 126 ALA n 
1 127 THR n 
1 128 LEU n 
1 129 VAL n 
1 130 GLN n 
1 131 GLN n 
1 132 ARG n 
1 133 GLY n 
1 134 ALA n 
1 135 GLU n 
1 136 SER n 
1 137 TYR n 
1 138 ILE n 
1 139 HIS n 
1 140 GLY n 
1 141 ALA n 
1 142 ILE n 
1 143 MET n 
1 144 THR n 
1 145 THR n 
1 146 PRO n 
1 147 GLU n 
1 148 TYR n 
1 149 LEU n 
1 150 GLY n 
1 151 GLN n 
1 152 PRO n 
1 153 SER n 
1 154 SER n 
1 155 VAL n 
1 156 THR n 
1 157 LEU n 
1 158 ILE n 
1 159 SER n 
1 160 GLY n 
1 161 PRO n 
1 162 LYS n 
1 163 THR n 
1 164 ALA n 
1 165 TYR n 
1 166 GLU n 
1 167 SER n 
1 168 GLN n 
1 169 LYS n 
1 170 GLU n 
1 171 LEU n 
1 172 LEU n 
1 173 SER n 
1 174 SER n 
1 175 ILE n 
1 176 GLY n 
1 177 THR n 
1 178 THR n 
1 179 ARG n 
1 180 HIS n 
1 181 VAL n 
1 182 SER n 
1 183 ASP n 
1 184 ASP n 
1 185 ILE n 
1 186 ALA n 
1 187 LYS n 
1 188 ALA n 
1 189 SER n 
1 190 LEU n 
1 191 LEU n 
1 192 ASP n 
1 193 ASN n 
1 194 ALA n 
1 195 LEU n 
1 196 LEU n 
1 197 SER n 
1 198 VAL n 
1 199 MET n 
1 200 SER n 
1 201 GLY n 
1 202 VAL n 
1 203 PHE n 
1 204 GLU n 
1 205 GLY n 
1 206 TRP n 
1 207 VAL n 
1 208 GLN n 
1 209 ALA n 
1 210 LEU n 
1 211 ALA n 
1 212 ILE n 
1 213 VAL n 
1 214 GLY n 
1 215 ALA n 
1 216 ALA n 
1 217 GLY n 
1 218 GLU n 
1 219 ASP n 
1 220 GLU n 
1 221 VAL n 
1 222 ASP n 
1 223 PHE n 
1 224 ALA n 
1 225 ALA n 
1 226 LEU n 
1 227 ALA n 
1 228 SER n 
1 229 PRO n 
1 230 LEU n 
1 231 VAL n 
1 232 ALA n 
1 233 SER n 
1 234 MET n 
1 235 ALA n 
1 236 ASP n 
1 237 GLN n 
1 238 LEU n 
1 239 PRO n 
1 240 VAL n 
1 241 ILE n 
1 242 ALA n 
1 243 GLY n 
1 244 ARG n 
1 245 VAL n 
1 246 ARG n 
1 247 GLU n 
1 248 LYS n 
1 249 GLN n 
1 250 TYR n 
1 251 VAL n 
1 252 GLY n 
1 253 GLY n 
1 254 SER n 
1 255 PRO n 
1 256 ILE n 
1 257 THR n 
1 258 MET n 
1 259 GLY n 
1 260 LEU n 
1 261 GLU n 
1 262 ALA n 
1 263 LEU n 
1 264 GLU n 
1 265 ASN n 
1 266 ILE n 
1 267 SER n 
1 268 GLU n 
1 269 THR n 
1 270 SER n 
1 271 ARG n 
1 272 GLU n 
1 273 LEU n 
1 274 GLY n 
1 275 VAL n 
1 276 GLY n 
1 277 VAL n 
1 278 LEU n 
1 279 LEU n 
1 280 GLY n 
1 281 SER n 
1 282 MET n 
1 283 ARG n 
1 284 GLU n 
1 285 VAL n 
1 286 MET n 
1 287 SER n 
1 288 GLU n 
1 289 ALA n 
1 290 VAL n 
1 291 LYS n 
1 292 LYS n 
1 293 GLY n 
1 294 LYS n 
1 295 GLY n 
1 296 GLY n 
1 297 GLU n 
1 298 SER n 
1 299 ILE n 
1 300 ALA n 
1 301 GLY n 
1 302 LEU n 
1 303 VAL n 
1 304 PRO n 
1 305 MET n 
1 306 LEU n 
1 307 THR n 
1 308 GLU n 
1 309 LEU n 
1 310 ASP n 
1 311 LYS n 
1 312 LYS n 
1 313 TRP 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                   313 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 VFPPC_03305 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Pochonia chlamydosporia 170' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1380566 
_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 
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 
NAP non-polymer         . 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 
;2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
;
'C21 H28 N7 O17 P3' 743.405 
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 
TRS non-polymer         . 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL           'TRIS BUFFER'                                
'C4 H12 N O3 1'     122.143 
TYR 'L-peptide linking' y TYROSINE                                           ?                                            
'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                             ?                                            
'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  GLU 14  -6  ?   ?   ?   A . n 
A 1 15  ASN 15  -5  ?   ?   ?   A . n 
A 1 16  LEU 16  -4  ?   ?   ?   A . n 
A 1 17  TYR 17  -3  ?   ?   ?   A . n 
A 1 18  PHE 18  -2  ?   ?   ?   A . n 
A 1 19  GLN 19  -1  ?   ?   ?   A . n 
A 1 20  GLY 20  0   ?   ?   ?   A . n 
A 1 21  MET 21  1   1   MET MET A . n 
A 1 22  SER 22  2   2   SER SER A . n 
A 1 23  SER 23  3   3   SER SER A . n 
A 1 24  SER 24  4   4   SER SER A . n 
A 1 25  ASN 25  5   5   ASN ASN A . n 
A 1 26  LYS 26  6   6   LYS LYS A . n 
A 1 27  PRO 27  7   7   PRO PRO A . n 
A 1 28  HIS 28  8   8   HIS HIS A . n 
A 1 29  VAL 29  9   9   VAL VAL A . n 
A 1 30  SER 30  10  10  SER SER A . n 
A 1 31  LEU 31  11  11  LEU LEU A . n 
A 1 32  ILE 32  12  12  ILE ILE A . n 
A 1 33  GLY 33  13  13  GLY GLY A . n 
A 1 34  LEU 34  14  14  LEU LEU A . n 
A 1 35  GLY 35  15  15  GLY GLY A . n 
A 1 36  ASN 36  16  16  ASN ASN A . n 
A 1 37  MET 37  17  17  MET MET A . n 
A 1 38  GLY 38  18  18  GLY GLY A . n 
A 1 39  LEU 39  19  19  LEU LEU A . n 
A 1 40  ALA 40  20  20  ALA ALA A . n 
A 1 41  ILE 41  21  21  ILE ILE A . n 
A 1 42  ALA 42  22  22  ALA ALA A . n 
A 1 43  ASN 43  23  23  ASN ASN A . n 
A 1 44  CYS 44  24  24  CYS CYS A . n 
A 1 45  LEU 45  25  25  LEU LEU A . n 
A 1 46  ILE 46  26  26  ILE ILE A . n 
A 1 47  LYS 47  27  27  LYS LYS A . n 
A 1 48  SER 48  28  28  SER SER A . n 
A 1 49  GLY 49  29  29  GLY GLY A . n 
A 1 50  CYS 50  30  30  CYS CYS A . n 
A 1 51  LYS 51  31  31  LYS LYS A . n 
A 1 52  LEU 52  32  32  LEU LEU A . n 
A 1 53  THR 53  33  33  THR THR A . n 
A 1 54  VAL 54  34  34  VAL VAL A . n 
A 1 55  TRP 55  35  35  TRP TRP A . n 
A 1 56  ASN 56  36  36  ASN ASN A . n 
A 1 57  ARG 57  37  37  ARG ARG A . n 
A 1 58  SER 58  38  38  SER SER A . n 
A 1 59  ALA 59  39  39  ALA ALA A . n 
A 1 60  GLU 60  40  40  GLU GLU A . n 
A 1 61  LYS 61  41  41  LYS LYS A . n 
A 1 62  ALA 62  42  42  ALA ALA A . n 
A 1 63  ALA 63  43  43  ALA ALA A . n 
A 1 64  SER 64  44  44  SER SER A . n 
A 1 65  LEU 65  45  45  LEU LEU A . n 
A 1 66  VAL 66  46  46  VAL VAL A . n 
A 1 67  PRO 67  47  47  PRO PRO A . n 
A 1 68  GLN 68  48  48  GLN GLN A . n 
A 1 69  GLY 69  49  49  GLY GLY A . n 
A 1 70  ALA 70  50  50  ALA ALA A . n 
A 1 71  THR 71  51  51  THR THR A . n 
A 1 72  VAL 72  52  52  VAL VAL A . n 
A 1 73  ALA 73  53  53  ALA ALA A . n 
A 1 74  ALA 74  54  54  ALA ALA A . n 
A 1 75  THR 75  55  55  THR THR A . n 
A 1 76  PRO 76  56  56  PRO PRO A . n 
A 1 77  ALA 77  57  57  ALA ALA A . n 
A 1 78  GLU 78  58  58  GLU GLU A . n 
A 1 79  CYS 79  59  59  CYS CYS A . n 
A 1 80  VAL 80  60  60  VAL VAL A . n 
A 1 81  ALA 81  61  61  ALA ALA A . n 
A 1 82  SER 82  62  62  SER SER A . n 
A 1 83  SER 83  63  63  SER SER A . n 
A 1 84  PRO 84  64  64  PRO PRO A . n 
A 1 85  THR 85  65  65  THR THR A . n 
A 1 86  ILE 86  66  66  ILE ILE A . n 
A 1 87  VAL 87  67  67  VAL VAL A . n 
A 1 88  ILE 88  68  68  ILE ILE A . n 
A 1 89  CYS 89  69  69  CYS CYS A . n 
A 1 90  LEU 90  70  70  LEU LEU A . n 
A 1 91  LEU 91  71  71  LEU LEU A . n 
A 1 92  ASN 92  72  72  ASN ASN A . n 
A 1 93  GLN 93  73  73  GLN GLN A . n 
A 1 94  ASP 94  74  74  ASP ASP A . n 
A 1 95  VAL 95  75  75  VAL VAL A . n 
A 1 96  VAL 96  76  76  VAL VAL A . n 
A 1 97  GLN 97  77  77  GLN GLN A . n 
A 1 98  GLN 98  78  78  GLN GLN A . n 
A 1 99  THR 99  79  79  THR THR A . n 
A 1 100 LEU 100 80  80  LEU LEU A . n 
A 1 101 ASP 101 81  81  ASP ASP A . n 
A 1 102 GLU 102 82  82  GLU GLU A . n 
A 1 103 VAL 103 83  83  VAL VAL A . n 
A 1 104 ILE 104 84  84  ILE ILE A . n 
A 1 105 ASP 105 85  85  ASP ASP A . n 
A 1 106 LEU 106 86  86  LEU LEU A . n 
A 1 107 SER 107 87  87  SER SER A . n 
A 1 108 GLY 108 88  88  GLY GLY A . n 
A 1 109 LYS 109 89  89  LYS LYS A . n 
A 1 110 THR 110 90  90  THR THR A . n 
A 1 111 ILE 111 91  91  ILE ILE A . n 
A 1 112 ILE 112 92  92  ILE ILE A . n 
A 1 113 ASN 113 93  93  ASN ASN A . n 
A 1 114 LEU 114 94  94  LEU LEU A . n 
A 1 115 THR 115 95  95  THR THR A . n 
A 1 116 ASN 116 96  96  ASN ASN A . n 
A 1 117 GLY 117 97  97  GLY GLY A . n 
A 1 118 THR 118 98  98  THR THR A . n 
A 1 119 PRO 119 99  99  PRO PRO A . n 
A 1 120 GLN 120 100 100 GLN GLN A . n 
A 1 121 GLN 121 101 101 GLN GLN A . n 
A 1 122 ALA 122 102 102 ALA ALA A . n 
A 1 123 VAL 123 103 103 VAL VAL A . n 
A 1 124 LYS 124 104 104 LYS LYS A . n 
A 1 125 VAL 125 105 105 VAL VAL A . n 
A 1 126 ALA 126 106 106 ALA ALA A . n 
A 1 127 THR 127 107 107 THR THR A . n 
A 1 128 LEU 128 108 108 LEU LEU A . n 
A 1 129 VAL 129 109 109 VAL VAL A . n 
A 1 130 GLN 130 110 110 GLN GLN A . n 
A 1 131 GLN 131 111 111 GLN GLN A . n 
A 1 132 ARG 132 112 112 ARG ARG A . n 
A 1 133 GLY 133 113 113 GLY GLY A . n 
A 1 134 ALA 134 114 114 ALA ALA A . n 
A 1 135 GLU 135 115 115 GLU GLU A . n 
A 1 136 SER 136 116 116 SER SER A . n 
A 1 137 TYR 137 117 117 TYR TYR A . n 
A 1 138 ILE 138 118 118 ILE ILE A . n 
A 1 139 HIS 139 119 119 HIS HIS A . n 
A 1 140 GLY 140 120 120 GLY GLY A . n 
A 1 141 ALA 141 121 121 ALA ALA A . n 
A 1 142 ILE 142 122 122 ILE ILE A . n 
A 1 143 MET 143 123 123 MET MET A . n 
A 1 144 THR 144 124 124 THR THR A . n 
A 1 145 THR 145 125 125 THR THR A . n 
A 1 146 PRO 146 126 126 PRO PRO A . n 
A 1 147 GLU 147 127 127 GLU GLU A . n 
A 1 148 TYR 148 128 128 TYR TYR A . n 
A 1 149 LEU 149 129 129 LEU LEU A . n 
A 1 150 GLY 150 130 130 GLY GLY A . n 
A 1 151 GLN 151 131 131 GLN GLN A . n 
A 1 152 PRO 152 132 132 PRO PRO A . n 
A 1 153 SER 153 133 133 SER SER A . n 
A 1 154 SER 154 134 134 SER SER A . n 
A 1 155 VAL 155 135 135 VAL VAL A . n 
A 1 156 THR 156 136 136 THR THR A . n 
A 1 157 LEU 157 137 137 LEU LEU A . n 
A 1 158 ILE 158 138 138 ILE ILE A . n 
A 1 159 SER 159 139 139 SER SER A . n 
A 1 160 GLY 160 140 140 GLY GLY A . n 
A 1 161 PRO 161 141 141 PRO PRO A . n 
A 1 162 LYS 162 142 142 LYS LYS A . n 
A 1 163 THR 163 143 143 THR THR A . n 
A 1 164 ALA 164 144 144 ALA ALA A . n 
A 1 165 TYR 165 145 145 TYR TYR A . n 
A 1 166 GLU 166 146 146 GLU GLU A . n 
A 1 167 SER 167 147 147 SER SER A . n 
A 1 168 GLN 168 148 148 GLN GLN A . n 
A 1 169 LYS 169 149 149 LYS LYS A . n 
A 1 170 GLU 170 150 150 GLU GLU A . n 
A 1 171 LEU 171 151 151 LEU LEU A . n 
A 1 172 LEU 172 152 152 LEU LEU A . n 
A 1 173 SER 173 153 153 SER SER A . n 
A 1 174 SER 174 154 154 SER SER A . n 
A 1 175 ILE 175 155 155 ILE ILE A . n 
A 1 176 GLY 176 156 156 GLY GLY A . n 
A 1 177 THR 177 157 157 THR THR A . n 
A 1 178 THR 178 158 158 THR THR A . n 
A 1 179 ARG 179 159 159 ARG ARG A . n 
A 1 180 HIS 180 160 160 HIS HIS A . n 
A 1 181 VAL 181 161 161 VAL VAL A . n 
A 1 182 SER 182 162 162 SER SER A . n 
A 1 183 ASP 183 163 163 ASP ASP A . n 
A 1 184 ASP 184 164 164 ASP ASP A . n 
A 1 185 ILE 185 165 165 ILE ILE A . n 
A 1 186 ALA 186 166 166 ALA ALA A . n 
A 1 187 LYS 187 167 167 LYS LYS A . n 
A 1 188 ALA 188 168 168 ALA ALA A . n 
A 1 189 SER 189 169 169 SER SER A . n 
A 1 190 LEU 190 170 170 LEU LEU A . n 
A 1 191 LEU 191 171 171 LEU LEU A . n 
A 1 192 ASP 192 172 172 ASP ASP A . n 
A 1 193 ASN 193 173 173 ASN ASN A . n 
A 1 194 ALA 194 174 174 ALA ALA A . n 
A 1 195 LEU 195 175 175 LEU LEU A . n 
A 1 196 LEU 196 176 176 LEU LEU A . n 
A 1 197 SER 197 177 177 SER SER A . n 
A 1 198 VAL 198 178 178 VAL VAL A . n 
A 1 199 MET 199 179 179 MET MET A . n 
A 1 200 SER 200 180 180 SER SER A . n 
A 1 201 GLY 201 181 181 GLY GLY A . n 
A 1 202 VAL 202 182 182 VAL VAL A . n 
A 1 203 PHE 203 183 183 PHE PHE A . n 
A 1 204 GLU 204 184 184 GLU GLU A . n 
A 1 205 GLY 205 185 185 GLY GLY A . n 
A 1 206 TRP 206 186 186 TRP TRP A . n 
A 1 207 VAL 207 187 187 VAL VAL A . n 
A 1 208 GLN 208 188 188 GLN GLN A . n 
A 1 209 ALA 209 189 189 ALA ALA A . n 
A 1 210 LEU 210 190 190 LEU LEU A . n 
A 1 211 ALA 211 191 191 ALA ALA A . n 
A 1 212 ILE 212 192 192 ILE ILE A . n 
A 1 213 VAL 213 193 193 VAL VAL A . n 
A 1 214 GLY 214 194 194 GLY GLY A . n 
A 1 215 ALA 215 195 195 ALA ALA A . n 
A 1 216 ALA 216 196 196 ALA ALA A . n 
A 1 217 GLY 217 197 197 GLY GLY A . n 
A 1 218 GLU 218 198 198 GLU GLU 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 VAL 221 201 201 VAL VAL A . n 
A 1 222 ASP 222 202 202 ASP ASP A . n 
A 1 223 PHE 223 203 203 PHE PHE A . n 
A 1 224 ALA 224 204 204 ALA ALA A . n 
A 1 225 ALA 225 205 205 ALA ALA A . n 
A 1 226 LEU 226 206 206 LEU LEU A . n 
A 1 227 ALA 227 207 207 ALA ALA A . n 
A 1 228 SER 228 208 208 SER SER A . n 
A 1 229 PRO 229 209 209 PRO PRO A . n 
A 1 230 LEU 230 210 210 LEU LEU A . n 
A 1 231 VAL 231 211 211 VAL VAL A . n 
A 1 232 ALA 232 212 212 ALA ALA A . n 
A 1 233 SER 233 213 213 SER SER A . n 
A 1 234 MET 234 214 214 MET MET A . n 
A 1 235 ALA 235 215 215 ALA ALA A . n 
A 1 236 ASP 236 216 216 ASP ASP A . n 
A 1 237 GLN 237 217 217 GLN GLN A . n 
A 1 238 LEU 238 218 218 LEU LEU A . n 
A 1 239 PRO 239 219 219 PRO PRO A . n 
A 1 240 VAL 240 220 220 VAL VAL A . n 
A 1 241 ILE 241 221 221 ILE ILE A . n 
A 1 242 ALA 242 222 222 ALA ALA A . n 
A 1 243 GLY 243 223 223 GLY GLY A . n 
A 1 244 ARG 244 224 224 ARG ARG A . n 
A 1 245 VAL 245 225 225 VAL VAL A . n 
A 1 246 ARG 246 226 226 ARG ARG A . n 
A 1 247 GLU 247 227 227 GLU GLU A . n 
A 1 248 LYS 248 228 228 LYS LYS A . n 
A 1 249 GLN 249 229 229 GLN GLN A . n 
A 1 250 TYR 250 230 230 TYR TYR A . n 
A 1 251 VAL 251 231 231 VAL VAL A . n 
A 1 252 GLY 252 232 232 GLY GLY A . n 
A 1 253 GLY 253 233 233 GLY GLY A . n 
A 1 254 SER 254 234 234 SER SER A . n 
A 1 255 PRO 255 235 235 PRO PRO A . n 
A 1 256 ILE 256 236 236 ILE ILE A . n 
A 1 257 THR 257 237 237 THR THR A . n 
A 1 258 MET 258 238 238 MET MET A . n 
A 1 259 GLY 259 239 239 GLY GLY A . n 
A 1 260 LEU 260 240 240 LEU LEU A . n 
A 1 261 GLU 261 241 241 GLU GLU A . n 
A 1 262 ALA 262 242 242 ALA ALA A . n 
A 1 263 LEU 263 243 243 LEU LEU A . n 
A 1 264 GLU 264 244 244 GLU GLU A . n 
A 1 265 ASN 265 245 245 ASN ASN A . n 
A 1 266 ILE 266 246 246 ILE ILE A . n 
A 1 267 SER 267 247 247 SER SER A . n 
A 1 268 GLU 268 248 248 GLU GLU A . n 
A 1 269 THR 269 249 249 THR THR A . n 
A 1 270 SER 270 250 250 SER SER A . n 
A 1 271 ARG 271 251 251 ARG ARG A . n 
A 1 272 GLU 272 252 252 GLU GLU A . n 
A 1 273 LEU 273 253 253 LEU LEU A . n 
A 1 274 GLY 274 254 254 GLY GLY A . n 
A 1 275 VAL 275 255 255 VAL VAL A . n 
A 1 276 GLY 276 256 256 GLY GLY A . n 
A 1 277 VAL 277 257 257 VAL VAL A . n 
A 1 278 LEU 278 258 258 LEU LEU A . n 
A 1 279 LEU 279 259 259 LEU LEU A . n 
A 1 280 GLY 280 260 260 GLY GLY A . n 
A 1 281 SER 281 261 261 SER SER A . n 
A 1 282 MET 282 262 262 MET MET A . n 
A 1 283 ARG 283 263 263 ARG ARG A . n 
A 1 284 GLU 284 264 264 GLU GLU A . n 
A 1 285 VAL 285 265 265 VAL VAL A . n 
A 1 286 MET 286 266 266 MET MET A . n 
A 1 287 SER 287 267 267 SER SER A . n 
A 1 288 GLU 288 268 268 GLU GLU A . n 
A 1 289 ALA 289 269 269 ALA ALA A . n 
A 1 290 VAL 290 270 270 VAL VAL A . n 
A 1 291 LYS 291 271 271 LYS LYS A . n 
A 1 292 LYS 292 272 272 LYS LYS A . n 
A 1 293 GLY 293 273 273 GLY GLY A . n 
A 1 294 LYS 294 274 274 LYS LYS A . n 
A 1 295 GLY 295 275 275 GLY GLY A . n 
A 1 296 GLY 296 276 276 GLY GLY A . n 
A 1 297 GLU 297 277 277 GLU GLU A . n 
A 1 298 SER 298 278 278 SER SER A . n 
A 1 299 ILE 299 279 279 ILE ILE A . n 
A 1 300 ALA 300 280 280 ALA ALA A . n 
A 1 301 GLY 301 281 281 GLY GLY A . n 
A 1 302 LEU 302 282 282 LEU LEU A . n 
A 1 303 VAL 303 283 283 VAL VAL A . n 
A 1 304 PRO 304 284 284 PRO PRO A . n 
A 1 305 MET 305 285 285 MET MET A . n 
A 1 306 LEU 306 286 286 LEU LEU A . n 
A 1 307 THR 307 287 287 THR THR A . n 
A 1 308 GLU 308 288 288 GLU GLU A . n 
A 1 309 LEU 309 289 289 LEU LEU A . n 
A 1 310 ASP 310 290 290 ASP ASP A . n 
A 1 311 LYS 311 291 291 LYS LYS A . n 
A 1 312 LYS 312 292 292 LYS LYS A . n 
A 1 313 TRP 313 293 293 TRP TRP 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  GLU 14  -6  ?   ?   ?   B . n 
B 1 15  ASN 15  -5  ?   ?   ?   B . n 
B 1 16  LEU 16  -4  ?   ?   ?   B . n 
B 1 17  TYR 17  -3  ?   ?   ?   B . n 
B 1 18  PHE 18  -2  ?   ?   ?   B . n 
B 1 19  GLN 19  -1  ?   ?   ?   B . n 
B 1 20  GLY 20  0   ?   ?   ?   B . n 
B 1 21  MET 21  1   ?   ?   ?   B . n 
B 1 22  SER 22  2   ?   ?   ?   B . n 
B 1 23  SER 23  3   ?   ?   ?   B . n 
B 1 24  SER 24  4   ?   ?   ?   B . n 
B 1 25  ASN 25  5   ?   ?   ?   B . n 
B 1 26  LYS 26  6   ?   ?   ?   B . n 
B 1 27  PRO 27  7   7   PRO PRO B . n 
B 1 28  HIS 28  8   8   HIS HIS B . n 
B 1 29  VAL 29  9   9   VAL VAL B . n 
B 1 30  SER 30  10  10  SER SER B . n 
B 1 31  LEU 31  11  11  LEU LEU B . n 
B 1 32  ILE 32  12  12  ILE ILE B . n 
B 1 33  GLY 33  13  13  GLY GLY B . n 
B 1 34  LEU 34  14  14  LEU LEU B . n 
B 1 35  GLY 35  15  15  GLY GLY B . n 
B 1 36  ASN 36  16  16  ASN ASN B . n 
B 1 37  MET 37  17  17  MET MET B . n 
B 1 38  GLY 38  18  18  GLY GLY B . n 
B 1 39  LEU 39  19  19  LEU LEU B . n 
B 1 40  ALA 40  20  20  ALA ALA B . n 
B 1 41  ILE 41  21  21  ILE ILE B . n 
B 1 42  ALA 42  22  22  ALA ALA B . n 
B 1 43  ASN 43  23  23  ASN ASN B . n 
B 1 44  CYS 44  24  24  CYS CYS B . n 
B 1 45  LEU 45  25  25  LEU LEU B . n 
B 1 46  ILE 46  26  26  ILE ILE B . n 
B 1 47  LYS 47  27  27  LYS LYS B . n 
B 1 48  SER 48  28  28  SER SER B . n 
B 1 49  GLY 49  29  29  GLY GLY B . n 
B 1 50  CYS 50  30  30  CYS CYS B . n 
B 1 51  LYS 51  31  31  LYS LYS B . n 
B 1 52  LEU 52  32  32  LEU LEU B . n 
B 1 53  THR 53  33  33  THR THR B . n 
B 1 54  VAL 54  34  34  VAL VAL B . n 
B 1 55  TRP 55  35  35  TRP TRP B . n 
B 1 56  ASN 56  36  36  ASN ASN B . n 
B 1 57  ARG 57  37  37  ARG ARG B . n 
B 1 58  SER 58  38  38  SER SER B . n 
B 1 59  ALA 59  39  39  ALA ALA B . n 
B 1 60  GLU 60  40  40  GLU GLU B . n 
B 1 61  LYS 61  41  41  LYS LYS B . n 
B 1 62  ALA 62  42  42  ALA ALA B . n 
B 1 63  ALA 63  43  43  ALA ALA B . n 
B 1 64  SER 64  44  44  SER SER B . n 
B 1 65  LEU 65  45  45  LEU LEU B . n 
B 1 66  VAL 66  46  46  VAL VAL B . n 
B 1 67  PRO 67  47  47  PRO PRO B . n 
B 1 68  GLN 68  48  48  GLN GLN B . n 
B 1 69  GLY 69  49  49  GLY GLY B . n 
B 1 70  ALA 70  50  50  ALA ALA B . n 
B 1 71  THR 71  51  51  THR THR B . n 
B 1 72  VAL 72  52  52  VAL VAL B . n 
B 1 73  ALA 73  53  53  ALA ALA B . n 
B 1 74  ALA 74  54  54  ALA ALA B . n 
B 1 75  THR 75  55  55  THR THR B . n 
B 1 76  PRO 76  56  56  PRO PRO B . n 
B 1 77  ALA 77  57  57  ALA ALA B . n 
B 1 78  GLU 78  58  58  GLU GLU B . n 
B 1 79  CYS 79  59  59  CYS CYS B . n 
B 1 80  VAL 80  60  60  VAL VAL B . n 
B 1 81  ALA 81  61  61  ALA ALA B . n 
B 1 82  SER 82  62  62  SER SER B . n 
B 1 83  SER 83  63  63  SER SER B . n 
B 1 84  PRO 84  64  64  PRO PRO B . n 
B 1 85  THR 85  65  65  THR THR B . n 
B 1 86  ILE 86  66  66  ILE ILE B . n 
B 1 87  VAL 87  67  67  VAL VAL B . n 
B 1 88  ILE 88  68  68  ILE ILE B . n 
B 1 89  CYS 89  69  69  CYS CYS B . n 
B 1 90  LEU 90  70  70  LEU LEU B . n 
B 1 91  LEU 91  71  71  LEU LEU B . n 
B 1 92  ASN 92  72  72  ASN ASN B . n 
B 1 93  GLN 93  73  73  GLN GLN B . n 
B 1 94  ASP 94  74  74  ASP ASP B . n 
B 1 95  VAL 95  75  75  VAL VAL B . n 
B 1 96  VAL 96  76  76  VAL VAL B . n 
B 1 97  GLN 97  77  77  GLN GLN B . n 
B 1 98  GLN 98  78  78  GLN GLN B . n 
B 1 99  THR 99  79  79  THR THR B . n 
B 1 100 LEU 100 80  80  LEU LEU B . n 
B 1 101 ASP 101 81  81  ASP ASP B . n 
B 1 102 GLU 102 82  82  GLU GLU B . n 
B 1 103 VAL 103 83  83  VAL VAL B . n 
B 1 104 ILE 104 84  84  ILE ILE B . n 
B 1 105 ASP 105 85  85  ASP ASP B . n 
B 1 106 LEU 106 86  86  LEU LEU B . n 
B 1 107 SER 107 87  87  SER SER B . n 
B 1 108 GLY 108 88  88  GLY GLY B . n 
B 1 109 LYS 109 89  89  LYS LYS B . n 
B 1 110 THR 110 90  90  THR THR B . n 
B 1 111 ILE 111 91  91  ILE ILE B . n 
B 1 112 ILE 112 92  92  ILE ILE B . n 
B 1 113 ASN 113 93  93  ASN ASN B . n 
B 1 114 LEU 114 94  94  LEU LEU B . n 
B 1 115 THR 115 95  95  THR THR B . n 
B 1 116 ASN 116 96  96  ASN ASN B . n 
B 1 117 GLY 117 97  97  GLY GLY B . n 
B 1 118 THR 118 98  98  THR THR B . n 
B 1 119 PRO 119 99  99  PRO PRO B . n 
B 1 120 GLN 120 100 100 GLN GLN B . n 
B 1 121 GLN 121 101 101 GLN GLN B . n 
B 1 122 ALA 122 102 102 ALA ALA B . n 
B 1 123 VAL 123 103 103 VAL VAL B . n 
B 1 124 LYS 124 104 104 LYS LYS B . n 
B 1 125 VAL 125 105 105 VAL VAL B . n 
B 1 126 ALA 126 106 106 ALA ALA B . n 
B 1 127 THR 127 107 107 THR THR B . n 
B 1 128 LEU 128 108 108 LEU LEU B . n 
B 1 129 VAL 129 109 109 VAL VAL B . n 
B 1 130 GLN 130 110 110 GLN GLN B . n 
B 1 131 GLN 131 111 111 GLN GLN B . n 
B 1 132 ARG 132 112 112 ARG ARG B . n 
B 1 133 GLY 133 113 113 GLY GLY B . n 
B 1 134 ALA 134 114 114 ALA ALA B . n 
B 1 135 GLU 135 115 115 GLU GLU B . n 
B 1 136 SER 136 116 116 SER SER B . n 
B 1 137 TYR 137 117 117 TYR TYR B . n 
B 1 138 ILE 138 118 118 ILE ILE B . n 
B 1 139 HIS 139 119 119 HIS HIS B . n 
B 1 140 GLY 140 120 120 GLY GLY B . n 
B 1 141 ALA 141 121 121 ALA ALA B . n 
B 1 142 ILE 142 122 122 ILE ILE B . n 
B 1 143 MET 143 123 123 MET MET B . n 
B 1 144 THR 144 124 124 THR THR B . n 
B 1 145 THR 145 125 125 THR THR B . n 
B 1 146 PRO 146 126 126 PRO PRO B . n 
B 1 147 GLU 147 127 127 GLU GLU B . n 
B 1 148 TYR 148 128 128 TYR TYR B . n 
B 1 149 LEU 149 129 129 LEU LEU B . n 
B 1 150 GLY 150 130 130 GLY GLY B . n 
B 1 151 GLN 151 131 131 GLN GLN B . n 
B 1 152 PRO 152 132 132 PRO PRO B . n 
B 1 153 SER 153 133 133 SER SER B . n 
B 1 154 SER 154 134 134 SER SER B . n 
B 1 155 VAL 155 135 135 VAL VAL B . n 
B 1 156 THR 156 136 136 THR THR B . n 
B 1 157 LEU 157 137 137 LEU LEU B . n 
B 1 158 ILE 158 138 138 ILE ILE B . n 
B 1 159 SER 159 139 139 SER SER B . n 
B 1 160 GLY 160 140 140 GLY GLY B . n 
B 1 161 PRO 161 141 141 PRO PRO B . n 
B 1 162 LYS 162 142 142 LYS LYS B . n 
B 1 163 THR 163 143 143 THR THR B . n 
B 1 164 ALA 164 144 144 ALA ALA B . n 
B 1 165 TYR 165 145 145 TYR TYR B . n 
B 1 166 GLU 166 146 146 GLU GLU B . n 
B 1 167 SER 167 147 147 SER SER B . n 
B 1 168 GLN 168 148 148 GLN GLN B . n 
B 1 169 LYS 169 149 149 LYS LYS B . n 
B 1 170 GLU 170 150 150 GLU GLU B . n 
B 1 171 LEU 171 151 151 LEU LEU B . n 
B 1 172 LEU 172 152 152 LEU LEU B . n 
B 1 173 SER 173 153 153 SER SER B . n 
B 1 174 SER 174 154 154 SER SER B . n 
B 1 175 ILE 175 155 155 ILE ILE B . n 
B 1 176 GLY 176 156 156 GLY GLY B . n 
B 1 177 THR 177 157 157 THR THR B . n 
B 1 178 THR 178 158 158 THR THR B . n 
B 1 179 ARG 179 159 159 ARG ARG B . n 
B 1 180 HIS 180 160 160 HIS HIS B . n 
B 1 181 VAL 181 161 161 VAL VAL B . n 
B 1 182 SER 182 162 162 SER SER B . n 
B 1 183 ASP 183 163 163 ASP ASP B . n 
B 1 184 ASP 184 164 164 ASP ASP B . n 
B 1 185 ILE 185 165 165 ILE ILE B . n 
B 1 186 ALA 186 166 166 ALA ALA B . n 
B 1 187 LYS 187 167 167 LYS LYS B . n 
B 1 188 ALA 188 168 168 ALA ALA B . n 
B 1 189 SER 189 169 169 SER SER B . n 
B 1 190 LEU 190 170 170 LEU LEU B . n 
B 1 191 LEU 191 171 171 LEU LEU B . n 
B 1 192 ASP 192 172 172 ASP ASP B . n 
B 1 193 ASN 193 173 173 ASN ASN B . n 
B 1 194 ALA 194 174 174 ALA ALA B . n 
B 1 195 LEU 195 175 175 LEU LEU B . n 
B 1 196 LEU 196 176 176 LEU LEU B . n 
B 1 197 SER 197 177 177 SER SER B . n 
B 1 198 VAL 198 178 178 VAL VAL B . n 
B 1 199 MET 199 179 179 MET MET B . n 
B 1 200 SER 200 180 180 SER SER B . n 
B 1 201 GLY 201 181 181 GLY GLY B . n 
B 1 202 VAL 202 182 182 VAL VAL B . n 
B 1 203 PHE 203 183 183 PHE PHE B . n 
B 1 204 GLU 204 184 184 GLU GLU B . n 
B 1 205 GLY 205 185 185 GLY GLY B . n 
B 1 206 TRP 206 186 186 TRP TRP B . n 
B 1 207 VAL 207 187 187 VAL VAL B . n 
B 1 208 GLN 208 188 188 GLN GLN B . n 
B 1 209 ALA 209 189 189 ALA ALA B . n 
B 1 210 LEU 210 190 190 LEU LEU B . n 
B 1 211 ALA 211 191 191 ALA ALA B . n 
B 1 212 ILE 212 192 192 ILE ILE B . n 
B 1 213 VAL 213 193 193 VAL VAL B . n 
B 1 214 GLY 214 194 194 GLY GLY B . n 
B 1 215 ALA 215 195 195 ALA ALA B . n 
B 1 216 ALA 216 196 196 ALA ALA B . n 
B 1 217 GLY 217 197 197 GLY GLY B . n 
B 1 218 GLU 218 198 198 GLU GLU 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 VAL 221 201 201 VAL VAL B . n 
B 1 222 ASP 222 202 202 ASP ASP B . n 
B 1 223 PHE 223 203 203 PHE PHE B . n 
B 1 224 ALA 224 204 204 ALA ALA B . n 
B 1 225 ALA 225 205 205 ALA ALA B . n 
B 1 226 LEU 226 206 206 LEU LEU B . n 
B 1 227 ALA 227 207 207 ALA ALA B . n 
B 1 228 SER 228 208 208 SER SER B . n 
B 1 229 PRO 229 209 209 PRO PRO B . n 
B 1 230 LEU 230 210 210 LEU LEU B . n 
B 1 231 VAL 231 211 211 VAL VAL B . n 
B 1 232 ALA 232 212 212 ALA ALA B . n 
B 1 233 SER 233 213 213 SER SER B . n 
B 1 234 MET 234 214 214 MET MET B . n 
B 1 235 ALA 235 215 215 ALA ALA B . n 
B 1 236 ASP 236 216 216 ASP ASP B . n 
B 1 237 GLN 237 217 217 GLN GLN B . n 
B 1 238 LEU 238 218 218 LEU LEU B . n 
B 1 239 PRO 239 219 219 PRO PRO B . n 
B 1 240 VAL 240 220 220 VAL VAL B . n 
B 1 241 ILE 241 221 221 ILE ILE B . n 
B 1 242 ALA 242 222 222 ALA ALA B . n 
B 1 243 GLY 243 223 223 GLY GLY B . n 
B 1 244 ARG 244 224 224 ARG ARG B . n 
B 1 245 VAL 245 225 225 VAL VAL B . n 
B 1 246 ARG 246 226 226 ARG ARG B . n 
B 1 247 GLU 247 227 227 GLU GLU B . n 
B 1 248 LYS 248 228 228 LYS LYS B . n 
B 1 249 GLN 249 229 229 GLN GLN B . n 
B 1 250 TYR 250 230 230 TYR TYR B . n 
B 1 251 VAL 251 231 231 VAL VAL B . n 
B 1 252 GLY 252 232 232 GLY GLY B . n 
B 1 253 GLY 253 233 233 GLY GLY B . n 
B 1 254 SER 254 234 234 SER SER B . n 
B 1 255 PRO 255 235 235 PRO PRO B . n 
B 1 256 ILE 256 236 236 ILE ILE B . n 
B 1 257 THR 257 237 237 THR THR B . n 
B 1 258 MET 258 238 238 MET MET B . n 
B 1 259 GLY 259 239 239 GLY GLY B . n 
B 1 260 LEU 260 240 240 LEU LEU B . n 
B 1 261 GLU 261 241 241 GLU GLU B . n 
B 1 262 ALA 262 242 242 ALA ALA B . n 
B 1 263 LEU 263 243 243 LEU LEU B . n 
B 1 264 GLU 264 244 244 GLU GLU B . n 
B 1 265 ASN 265 245 245 ASN ASN B . n 
B 1 266 ILE 266 246 246 ILE ILE B . n 
B 1 267 SER 267 247 247 SER SER B . n 
B 1 268 GLU 268 248 248 GLU GLU B . n 
B 1 269 THR 269 249 249 THR THR B . n 
B 1 270 SER 270 250 250 SER SER B . n 
B 1 271 ARG 271 251 251 ARG ARG B . n 
B 1 272 GLU 272 252 252 GLU GLU B . n 
B 1 273 LEU 273 253 253 LEU LEU B . n 
B 1 274 GLY 274 254 254 GLY GLY B . n 
B 1 275 VAL 275 255 255 VAL VAL B . n 
B 1 276 GLY 276 256 256 GLY GLY B . n 
B 1 277 VAL 277 257 257 VAL VAL B . n 
B 1 278 LEU 278 258 258 LEU LEU B . n 
B 1 279 LEU 279 259 259 LEU LEU B . n 
B 1 280 GLY 280 260 260 GLY GLY B . n 
B 1 281 SER 281 261 261 SER SER B . n 
B 1 282 MET 282 262 262 MET MET B . n 
B 1 283 ARG 283 263 263 ARG ARG B . n 
B 1 284 GLU 284 264 264 GLU GLU B . n 
B 1 285 VAL 285 265 265 VAL VAL B . n 
B 1 286 MET 286 266 266 MET MET B . n 
B 1 287 SER 287 267 267 SER SER B . n 
B 1 288 GLU 288 268 268 GLU GLU B . n 
B 1 289 ALA 289 269 269 ALA ALA B . n 
B 1 290 VAL 290 270 270 VAL VAL B . n 
B 1 291 LYS 291 271 271 LYS LYS B . n 
B 1 292 LYS 292 272 272 LYS LYS B . n 
B 1 293 GLY 293 273 273 GLY GLY B . n 
B 1 294 LYS 294 274 274 LYS LYS B . n 
B 1 295 GLY 295 275 275 GLY GLY B . n 
B 1 296 GLY 296 276 276 GLY GLY B . n 
B 1 297 GLU 297 277 277 GLU GLU B . n 
B 1 298 SER 298 278 278 SER SER B . n 
B 1 299 ILE 299 279 279 ILE ILE B . n 
B 1 300 ALA 300 280 280 ALA ALA B . n 
B 1 301 GLY 301 281 281 GLY GLY B . n 
B 1 302 LEU 302 282 282 LEU LEU B . n 
B 1 303 VAL 303 283 283 VAL VAL B . n 
B 1 304 PRO 304 284 284 PRO PRO B . n 
B 1 305 MET 305 285 285 MET MET B . n 
B 1 306 LEU 306 286 286 LEU LEU B . n 
B 1 307 THR 307 287 287 THR THR B . n 
B 1 308 GLU 308 288 288 GLU GLU B . n 
B 1 309 LEU 309 289 289 LEU LEU B . n 
B 1 310 ASP 310 290 290 ASP ASP B . n 
B 1 311 LYS 311 291 291 LYS LYS B . n 
B 1 312 LYS 312 292 292 LYS LYS B . n 
B 1 313 TRP 313 293 293 TRP TRP B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NAP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NAP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 NAP 1   301 301 NAP NAP A . 
D 3 TRS 1   302 401 TRS TRS A . 
E 2 NAP 1   301 301 NAP NAP B . 
F 4 HOH 1   401 426 HOH HOH A . 
F 4 HOH 2   402 382 HOH HOH A . 
F 4 HOH 3   403 385 HOH HOH A . 
F 4 HOH 4   404 157 HOH HOH A . 
F 4 HOH 5   405 61  HOH HOH A . 
F 4 HOH 6   406 195 HOH HOH A . 
F 4 HOH 7   407 111 HOH HOH A . 
F 4 HOH 8   408 243 HOH HOH A . 
F 4 HOH 9   409 287 HOH HOH A . 
F 4 HOH 10  410 128 HOH HOH A . 
F 4 HOH 11  411 123 HOH HOH A . 
F 4 HOH 12  412 34  HOH HOH A . 
F 4 HOH 13  413 25  HOH HOH A . 
F 4 HOH 14  414 55  HOH HOH A . 
F 4 HOH 15  415 161 HOH HOH A . 
F 4 HOH 16  416 19  HOH HOH A . 
F 4 HOH 17  417 296 HOH HOH A . 
F 4 HOH 18  418 209 HOH HOH A . 
F 4 HOH 19  419 182 HOH HOH A . 
F 4 HOH 20  420 48  HOH HOH A . 
F 4 HOH 21  421 3   HOH HOH A . 
F 4 HOH 22  422 158 HOH HOH A . 
F 4 HOH 23  423 405 HOH HOH A . 
F 4 HOH 24  424 412 HOH HOH A . 
F 4 HOH 25  425 13  HOH HOH A . 
F 4 HOH 26  426 1   HOH HOH A . 
F 4 HOH 27  427 215 HOH HOH A . 
F 4 HOH 28  428 297 HOH HOH A . 
F 4 HOH 29  429 368 HOH HOH A . 
F 4 HOH 30  430 279 HOH HOH A . 
F 4 HOH 31  431 120 HOH HOH A . 
F 4 HOH 32  432 345 HOH HOH A . 
F 4 HOH 33  433 140 HOH HOH A . 
F 4 HOH 34  434 43  HOH HOH A . 
F 4 HOH 35  435 166 HOH HOH A . 
F 4 HOH 36  436 196 HOH HOH A . 
F 4 HOH 37  437 8   HOH HOH A . 
F 4 HOH 38  438 313 HOH HOH A . 
F 4 HOH 39  439 141 HOH HOH A . 
F 4 HOH 40  440 329 HOH HOH A . 
F 4 HOH 41  441 202 HOH HOH A . 
F 4 HOH 42  442 449 HOH HOH A . 
F 4 HOH 43  443 160 HOH HOH A . 
F 4 HOH 44  444 305 HOH HOH A . 
F 4 HOH 45  445 187 HOH HOH A . 
F 4 HOH 46  446 29  HOH HOH A . 
F 4 HOH 47  447 359 HOH HOH A . 
F 4 HOH 48  448 393 HOH HOH A . 
F 4 HOH 49  449 98  HOH HOH A . 
F 4 HOH 50  450 301 HOH HOH A . 
F 4 HOH 51  451 116 HOH HOH A . 
F 4 HOH 52  452 380 HOH HOH A . 
F 4 HOH 53  453 131 HOH HOH A . 
F 4 HOH 54  454 378 HOH HOH A . 
F 4 HOH 55  455 146 HOH HOH A . 
F 4 HOH 56  456 39  HOH HOH A . 
F 4 HOH 57  457 235 HOH HOH A . 
F 4 HOH 58  458 360 HOH HOH A . 
F 4 HOH 59  459 92  HOH HOH A . 
F 4 HOH 60  460 20  HOH HOH A . 
F 4 HOH 61  461 41  HOH HOH A . 
F 4 HOH 62  462 302 HOH HOH A . 
F 4 HOH 63  463 38  HOH HOH A . 
F 4 HOH 64  464 112 HOH HOH A . 
F 4 HOH 65  465 282 HOH HOH A . 
F 4 HOH 66  466 73  HOH HOH A . 
F 4 HOH 67  467 350 HOH HOH A . 
F 4 HOH 68  468 24  HOH HOH A . 
F 4 HOH 69  469 212 HOH HOH A . 
F 4 HOH 70  470 88  HOH HOH A . 
F 4 HOH 71  471 407 HOH HOH A . 
F 4 HOH 72  472 69  HOH HOH A . 
F 4 HOH 73  473 104 HOH HOH A . 
F 4 HOH 74  474 201 HOH HOH A . 
F 4 HOH 75  475 107 HOH HOH A . 
F 4 HOH 76  476 156 HOH HOH A . 
F 4 HOH 77  477 135 HOH HOH A . 
F 4 HOH 78  478 15  HOH HOH A . 
F 4 HOH 79  479 290 HOH HOH A . 
F 4 HOH 80  480 2   HOH HOH A . 
F 4 HOH 81  481 163 HOH HOH A . 
F 4 HOH 82  482 14  HOH HOH A . 
F 4 HOH 83  483 284 HOH HOH A . 
F 4 HOH 84  484 155 HOH HOH A . 
F 4 HOH 85  485 170 HOH HOH A . 
F 4 HOH 86  486 443 HOH HOH A . 
F 4 HOH 87  487 288 HOH HOH A . 
F 4 HOH 88  488 239 HOH HOH A . 
F 4 HOH 89  489 218 HOH HOH A . 
F 4 HOH 90  490 71  HOH HOH A . 
F 4 HOH 91  491 33  HOH HOH A . 
F 4 HOH 92  492 379 HOH HOH A . 
F 4 HOH 93  493 49  HOH HOH A . 
F 4 HOH 94  494 206 HOH HOH A . 
F 4 HOH 95  495 149 HOH HOH A . 
F 4 HOH 96  496 46  HOH HOH A . 
F 4 HOH 97  497 52  HOH HOH A . 
F 4 HOH 98  498 127 HOH HOH A . 
F 4 HOH 99  499 79  HOH HOH A . 
F 4 HOH 100 500 54  HOH HOH A . 
F 4 HOH 101 501 47  HOH HOH A . 
F 4 HOH 102 502 67  HOH HOH A . 
F 4 HOH 103 503 181 HOH HOH A . 
F 4 HOH 104 504 224 HOH HOH A . 
F 4 HOH 105 505 65  HOH HOH A . 
F 4 HOH 106 506 285 HOH HOH A . 
F 4 HOH 107 507 150 HOH HOH A . 
F 4 HOH 108 508 223 HOH HOH A . 
F 4 HOH 109 509 225 HOH HOH A . 
F 4 HOH 110 510 62  HOH HOH A . 
F 4 HOH 111 511 242 HOH HOH A . 
F 4 HOH 112 512 6   HOH HOH A . 
F 4 HOH 113 513 28  HOH HOH A . 
F 4 HOH 114 514 63  HOH HOH A . 
F 4 HOH 115 515 94  HOH HOH A . 
F 4 HOH 116 516 109 HOH HOH A . 
F 4 HOH 117 517 370 HOH HOH A . 
F 4 HOH 118 518 194 HOH HOH A . 
F 4 HOH 119 519 326 HOH HOH A . 
F 4 HOH 120 520 142 HOH HOH A . 
F 4 HOH 121 521 32  HOH HOH A . 
F 4 HOH 122 522 344 HOH HOH A . 
F 4 HOH 123 523 185 HOH HOH A . 
F 4 HOH 124 524 431 HOH HOH A . 
F 4 HOH 125 525 348 HOH HOH A . 
F 4 HOH 126 526 342 HOH HOH A . 
F 4 HOH 127 527 373 HOH HOH A . 
F 4 HOH 128 528 219 HOH HOH A . 
F 4 HOH 129 529 9   HOH HOH A . 
F 4 HOH 130 530 238 HOH HOH A . 
F 4 HOH 131 531 222 HOH HOH A . 
F 4 HOH 132 532 53  HOH HOH A . 
F 4 HOH 133 533 172 HOH HOH A . 
F 4 HOH 134 534 322 HOH HOH A . 
F 4 HOH 135 535 374 HOH HOH A . 
F 4 HOH 136 536 114 HOH HOH A . 
F 4 HOH 137 537 58  HOH HOH A . 
F 4 HOH 138 538 176 HOH HOH A . 
F 4 HOH 139 539 192 HOH HOH A . 
F 4 HOH 140 540 64  HOH HOH A . 
F 4 HOH 141 541 143 HOH HOH A . 
F 4 HOH 142 542 74  HOH HOH A . 
F 4 HOH 143 543 455 HOH HOH A . 
F 4 HOH 144 544 10  HOH HOH A . 
F 4 HOH 145 545 303 HOH HOH A . 
F 4 HOH 146 546 22  HOH HOH A . 
F 4 HOH 147 547 328 HOH HOH A . 
F 4 HOH 148 548 86  HOH HOH A . 
F 4 HOH 149 549 210 HOH HOH A . 
F 4 HOH 150 550 267 HOH HOH A . 
F 4 HOH 151 551 423 HOH HOH A . 
F 4 HOH 152 552 137 HOH HOH A . 
F 4 HOH 153 553 347 HOH HOH A . 
F 4 HOH 154 554 334 HOH HOH A . 
F 4 HOH 155 555 162 HOH HOH A . 
F 4 HOH 156 556 233 HOH HOH A . 
F 4 HOH 157 557 152 HOH HOH A . 
F 4 HOH 158 558 164 HOH HOH A . 
F 4 HOH 159 559 139 HOH HOH A . 
F 4 HOH 160 560 216 HOH HOH A . 
F 4 HOH 161 561 100 HOH HOH A . 
F 4 HOH 162 562 27  HOH HOH A . 
F 4 HOH 163 563 237 HOH HOH A . 
F 4 HOH 164 564 294 HOH HOH A . 
F 4 HOH 165 565 133 HOH HOH A . 
F 4 HOH 166 566 327 HOH HOH A . 
F 4 HOH 167 567 420 HOH HOH A . 
F 4 HOH 168 568 16  HOH HOH A . 
F 4 HOH 169 569 227 HOH HOH A . 
F 4 HOH 170 570 191 HOH HOH A . 
F 4 HOH 171 571 406 HOH HOH A . 
F 4 HOH 172 572 316 HOH HOH A . 
F 4 HOH 173 573 384 HOH HOH A . 
F 4 HOH 174 574 427 HOH HOH A . 
F 4 HOH 175 575 175 HOH HOH A . 
F 4 HOH 176 576 383 HOH HOH A . 
F 4 HOH 177 577 230 HOH HOH A . 
F 4 HOH 178 578 447 HOH HOH A . 
F 4 HOH 179 579 339 HOH HOH A . 
F 4 HOH 180 580 304 HOH HOH A . 
F 4 HOH 181 581 300 HOH HOH A . 
F 4 HOH 182 582 40  HOH HOH A . 
F 4 HOH 183 583 332 HOH HOH A . 
F 4 HOH 184 584 363 HOH HOH A . 
F 4 HOH 185 585 438 HOH HOH A . 
F 4 HOH 186 586 421 HOH HOH A . 
F 4 HOH 187 587 321 HOH HOH A . 
F 4 HOH 188 588 367 HOH HOH A . 
F 4 HOH 189 589 251 HOH HOH A . 
F 4 HOH 190 590 415 HOH HOH A . 
F 4 HOH 191 591 442 HOH HOH A . 
F 4 HOH 192 592 167 HOH HOH A . 
F 4 HOH 193 593 429 HOH HOH A . 
F 4 HOH 194 594 252 HOH HOH A . 
F 4 HOH 195 595 441 HOH HOH A . 
F 4 HOH 196 596 446 HOH HOH A . 
F 4 HOH 197 597 433 HOH HOH A . 
F 4 HOH 198 598 337 HOH HOH A . 
F 4 HOH 199 599 221 HOH HOH A . 
F 4 HOH 200 600 246 HOH HOH A . 
F 4 HOH 201 601 408 HOH HOH A . 
F 4 HOH 202 602 245 HOH HOH A . 
F 4 HOH 203 603 257 HOH HOH A . 
F 4 HOH 204 604 411 HOH HOH A . 
F 4 HOH 205 605 371 HOH HOH A . 
F 4 HOH 206 606 96  HOH HOH A . 
F 4 HOH 207 607 272 HOH HOH A . 
F 4 HOH 208 608 234 HOH HOH A . 
F 4 HOH 209 609 410 HOH HOH A . 
F 4 HOH 210 610 241 HOH HOH A . 
F 4 HOH 211 611 428 HOH HOH A . 
F 4 HOH 212 612 249 HOH HOH A . 
F 4 HOH 213 613 130 HOH HOH A . 
F 4 HOH 214 614 349 HOH HOH A . 
F 4 HOH 215 615 422 HOH HOH A . 
F 4 HOH 216 616 198 HOH HOH A . 
F 4 HOH 217 617 273 HOH HOH A . 
F 4 HOH 218 618 414 HOH HOH A . 
F 4 HOH 219 619 353 HOH HOH A . 
F 4 HOH 220 620 430 HOH HOH A . 
F 4 HOH 221 621 392 HOH HOH A . 
F 4 HOH 222 622 248 HOH HOH A . 
F 4 HOH 223 623 261 HOH HOH A . 
F 4 HOH 224 624 277 HOH HOH A . 
F 4 HOH 225 625 335 HOH HOH A . 
F 4 HOH 226 626 82  HOH HOH A . 
F 4 HOH 227 627 124 HOH HOH A . 
F 4 HOH 228 628 262 HOH HOH A . 
F 4 HOH 229 629 228 HOH HOH A . 
F 4 HOH 230 630 240 HOH HOH A . 
F 4 HOH 231 631 276 HOH HOH A . 
F 4 HOH 232 632 346 HOH HOH A . 
F 4 HOH 233 633 381 HOH HOH A . 
F 4 HOH 234 634 352 HOH HOH A . 
F 4 HOH 235 635 394 HOH HOH A . 
F 4 HOH 236 636 178 HOH HOH A . 
F 4 HOH 237 637 445 HOH HOH A . 
F 4 HOH 238 638 85  HOH HOH A . 
F 4 HOH 239 639 274 HOH HOH A . 
F 4 HOH 240 640 253 HOH HOH A . 
F 4 HOH 241 641 356 HOH HOH A . 
F 4 HOH 242 642 355 HOH HOH A . 
F 4 HOH 243 643 264 HOH HOH A . 
F 4 HOH 244 644 190 HOH HOH A . 
F 4 HOH 245 645 199 HOH HOH A . 
F 4 HOH 246 646 270 HOH HOH A . 
F 4 HOH 247 647 136 HOH HOH A . 
F 4 HOH 248 648 269 HOH HOH A . 
F 4 HOH 249 649 440 HOH HOH A . 
F 4 HOH 250 650 450 HOH HOH A . 
F 4 HOH 251 651 448 HOH HOH A . 
F 4 HOH 252 652 401 HOH HOH A . 
F 4 HOH 253 653 434 HOH HOH A . 
F 4 HOH 254 654 454 HOH HOH A . 
G 4 HOH 1   401 439 HOH HOH B . 
G 4 HOH 2   402 437 HOH HOH B . 
G 4 HOH 3   403 399 HOH HOH B . 
G 4 HOH 4   404 436 HOH HOH B . 
G 4 HOH 5   405 44  HOH HOH B . 
G 4 HOH 6   406 418 HOH HOH B . 
G 4 HOH 7   407 57  HOH HOH B . 
G 4 HOH 8   408 173 HOH HOH B . 
G 4 HOH 9   409 211 HOH HOH B . 
G 4 HOH 10  410 78  HOH HOH B . 
G 4 HOH 11  411 203 HOH HOH B . 
G 4 HOH 12  412 333 HOH HOH B . 
G 4 HOH 13  413 204 HOH HOH B . 
G 4 HOH 14  414 389 HOH HOH B . 
G 4 HOH 15  415 125 HOH HOH B . 
G 4 HOH 16  416 66  HOH HOH B . 
G 4 HOH 17  417 351 HOH HOH B . 
G 4 HOH 18  418 395 HOH HOH B . 
G 4 HOH 19  419 89  HOH HOH B . 
G 4 HOH 20  420 12  HOH HOH B . 
G 4 HOH 21  421 390 HOH HOH B . 
G 4 HOH 22  422 68  HOH HOH B . 
G 4 HOH 23  423 291 HOH HOH B . 
G 4 HOH 24  424 59  HOH HOH B . 
G 4 HOH 25  425 286 HOH HOH B . 
G 4 HOH 26  426 51  HOH HOH B . 
G 4 HOH 27  427 42  HOH HOH B . 
G 4 HOH 28  428 214 HOH HOH B . 
G 4 HOH 29  429 183 HOH HOH B . 
G 4 HOH 30  430 309 HOH HOH B . 
G 4 HOH 31  431 18  HOH HOH B . 
G 4 HOH 32  432 188 HOH HOH B . 
G 4 HOH 33  433 119 HOH HOH B . 
G 4 HOH 34  434 99  HOH HOH B . 
G 4 HOH 35  435 307 HOH HOH B . 
G 4 HOH 36  436 417 HOH HOH B . 
G 4 HOH 37  437 45  HOH HOH B . 
G 4 HOH 38  438 134 HOH HOH B . 
G 4 HOH 39  439 83  HOH HOH B . 
G 4 HOH 40  440 144 HOH HOH B . 
G 4 HOH 41  441 362 HOH HOH B . 
G 4 HOH 42  442 324 HOH HOH B . 
G 4 HOH 43  443 151 HOH HOH B . 
G 4 HOH 44  444 35  HOH HOH B . 
G 4 HOH 45  445 93  HOH HOH B . 
G 4 HOH 46  446 184 HOH HOH B . 
G 4 HOH 47  447 138 HOH HOH B . 
G 4 HOH 48  448 105 HOH HOH B . 
G 4 HOH 49  449 306 HOH HOH B . 
G 4 HOH 50  450 60  HOH HOH B . 
G 4 HOH 51  451 278 HOH HOH B . 
G 4 HOH 52  452 115 HOH HOH B . 
G 4 HOH 53  453 171 HOH HOH B . 
G 4 HOH 54  454 117 HOH HOH B . 
G 4 HOH 55  455 72  HOH HOH B . 
G 4 HOH 56  456 369 HOH HOH B . 
G 4 HOH 57  457 292 HOH HOH B . 
G 4 HOH 58  458 11  HOH HOH B . 
G 4 HOH 59  459 319 HOH HOH B . 
G 4 HOH 60  460 121 HOH HOH B . 
G 4 HOH 61  461 177 HOH HOH B . 
G 4 HOH 62  462 75  HOH HOH B . 
G 4 HOH 63  463 325 HOH HOH B . 
G 4 HOH 64  464 95  HOH HOH B . 
G 4 HOH 65  465 90  HOH HOH B . 
G 4 HOH 66  466 126 HOH HOH B . 
G 4 HOH 67  467 444 HOH HOH B . 
G 4 HOH 68  468 435 HOH HOH B . 
G 4 HOH 69  469 308 HOH HOH B . 
G 4 HOH 70  470 56  HOH HOH B . 
G 4 HOH 71  471 193 HOH HOH B . 
G 4 HOH 72  472 101 HOH HOH B . 
G 4 HOH 73  473 180 HOH HOH B . 
G 4 HOH 74  474 5   HOH HOH B . 
G 4 HOH 75  475 281 HOH HOH B . 
G 4 HOH 76  476 81  HOH HOH B . 
G 4 HOH 77  477 289 HOH HOH B . 
G 4 HOH 78  478 226 HOH HOH B . 
G 4 HOH 79  479 236 HOH HOH B . 
G 4 HOH 80  480 213 HOH HOH B . 
G 4 HOH 81  481 340 HOH HOH B . 
G 4 HOH 82  482 23  HOH HOH B . 
G 4 HOH 83  483 205 HOH HOH B . 
G 4 HOH 84  484 7   HOH HOH B . 
G 4 HOH 85  485 148 HOH HOH B . 
G 4 HOH 86  486 4   HOH HOH B . 
G 4 HOH 87  487 293 HOH HOH B . 
G 4 HOH 88  488 30  HOH HOH B . 
G 4 HOH 89  489 145 HOH HOH B . 
G 4 HOH 90  490 388 HOH HOH B . 
G 4 HOH 91  491 231 HOH HOH B . 
G 4 HOH 92  492 97  HOH HOH B . 
G 4 HOH 93  493 70  HOH HOH B . 
G 4 HOH 94  494 207 HOH HOH B . 
G 4 HOH 95  495 118 HOH HOH B . 
G 4 HOH 96  496 165 HOH HOH B . 
G 4 HOH 97  497 387 HOH HOH B . 
G 4 HOH 98  498 17  HOH HOH B . 
G 4 HOH 99  499 280 HOH HOH B . 
G 4 HOH 100 500 375 HOH HOH B . 
G 4 HOH 101 501 103 HOH HOH B . 
G 4 HOH 102 502 77  HOH HOH B . 
G 4 HOH 103 503 84  HOH HOH B . 
G 4 HOH 104 504 174 HOH HOH B . 
G 4 HOH 105 505 364 HOH HOH B . 
G 4 HOH 106 506 341 HOH HOH B . 
G 4 HOH 107 507 315 HOH HOH B . 
G 4 HOH 108 508 323 HOH HOH B . 
G 4 HOH 109 509 361 HOH HOH B . 
G 4 HOH 110 510 189 HOH HOH B . 
G 4 HOH 111 511 318 HOH HOH B . 
G 4 HOH 112 512 229 HOH HOH B . 
G 4 HOH 113 513 372 HOH HOH B . 
G 4 HOH 114 514 208 HOH HOH B . 
G 4 HOH 115 515 244 HOH HOH B . 
G 4 HOH 116 516 153 HOH HOH B . 
G 4 HOH 117 517 271 HOH HOH B . 
G 4 HOH 118 518 31  HOH HOH B . 
G 4 HOH 119 519 80  HOH HOH B . 
G 4 HOH 120 520 122 HOH HOH B . 
G 4 HOH 121 521 50  HOH HOH B . 
G 4 HOH 122 522 108 HOH HOH B . 
G 4 HOH 123 523 154 HOH HOH B . 
G 4 HOH 124 524 36  HOH HOH B . 
G 4 HOH 125 525 312 HOH HOH B . 
G 4 HOH 126 526 37  HOH HOH B . 
G 4 HOH 127 527 220 HOH HOH B . 
G 4 HOH 128 528 298 HOH HOH B . 
G 4 HOH 129 529 310 HOH HOH B . 
G 4 HOH 130 530 110 HOH HOH B . 
G 4 HOH 131 531 132 HOH HOH B . 
G 4 HOH 132 532 311 HOH HOH B . 
G 4 HOH 133 533 147 HOH HOH B . 
G 4 HOH 134 534 106 HOH HOH B . 
G 4 HOH 135 535 76  HOH HOH B . 
G 4 HOH 136 536 87  HOH HOH B . 
G 4 HOH 137 537 295 HOH HOH B . 
G 4 HOH 138 538 247 HOH HOH B . 
G 4 HOH 139 539 159 HOH HOH B . 
G 4 HOH 140 540 320 HOH HOH B . 
G 4 HOH 141 541 21  HOH HOH B . 
G 4 HOH 142 542 330 HOH HOH B . 
G 4 HOH 143 543 317 HOH HOH B . 
G 4 HOH 144 544 314 HOH HOH B . 
G 4 HOH 145 545 404 HOH HOH B . 
G 4 HOH 146 546 331 HOH HOH B . 
G 4 HOH 147 547 91  HOH HOH B . 
G 4 HOH 148 548 425 HOH HOH B . 
G 4 HOH 149 549 400 HOH HOH B . 
G 4 HOH 150 550 232 HOH HOH B . 
G 4 HOH 151 551 343 HOH HOH B . 
G 4 HOH 152 552 102 HOH HOH B . 
G 4 HOH 153 553 268 HOH HOH B . 
G 4 HOH 154 554 283 HOH HOH B . 
G 4 HOH 155 555 200 HOH HOH B . 
G 4 HOH 156 556 26  HOH HOH B . 
G 4 HOH 157 557 266 HOH HOH B . 
G 4 HOH 158 558 386 HOH HOH B . 
G 4 HOH 159 559 391 HOH HOH B . 
G 4 HOH 160 560 358 HOH HOH B . 
G 4 HOH 161 561 250 HOH HOH B . 
G 4 HOH 162 562 299 HOH HOH B . 
G 4 HOH 163 563 398 HOH HOH B . 
G 4 HOH 164 564 397 HOH HOH B . 
G 4 HOH 165 565 432 HOH HOH B . 
G 4 HOH 166 566 452 HOH HOH B . 
G 4 HOH 167 567 113 HOH HOH B . 
G 4 HOH 168 568 366 HOH HOH B . 
G 4 HOH 169 569 419 HOH HOH B . 
G 4 HOH 170 570 275 HOH HOH B . 
G 4 HOH 171 571 169 HOH HOH B . 
G 4 HOH 172 572 357 HOH HOH B . 
G 4 HOH 173 573 402 HOH HOH B . 
G 4 HOH 174 574 260 HOH HOH B . 
G 4 HOH 175 575 258 HOH HOH B . 
G 4 HOH 176 576 265 HOH HOH B . 
G 4 HOH 177 577 197 HOH HOH B . 
G 4 HOH 178 578 338 HOH HOH B . 
G 4 HOH 179 579 376 HOH HOH B . 
G 4 HOH 180 580 403 HOH HOH B . 
G 4 HOH 181 581 377 HOH HOH B . 
G 4 HOH 182 582 255 HOH HOH B . 
G 4 HOH 183 583 168 HOH HOH B . 
G 4 HOH 184 584 179 HOH HOH B . 
G 4 HOH 185 585 413 HOH HOH B . 
G 4 HOH 186 586 453 HOH HOH B . 
G 4 HOH 187 587 396 HOH HOH B . 
G 4 HOH 188 588 424 HOH HOH B . 
G 4 HOH 189 589 336 HOH HOH B . 
G 4 HOH 190 590 256 HOH HOH B . 
G 4 HOH 191 591 365 HOH HOH B . 
G 4 HOH 192 592 254 HOH HOH B . 
G 4 HOH 193 593 129 HOH HOH B . 
G 4 HOH 194 594 409 HOH HOH B . 
G 4 HOH 195 595 259 HOH HOH B . 
G 4 HOH 196 596 217 HOH HOH B . 
G 4 HOH 197 597 451 HOH HOH B . 
G 4 HOH 198 598 263 HOH HOH B . 
G 4 HOH 199 599 354 HOH HOH B . 
G 4 HOH 200 600 186 HOH HOH B . 
G 4 HOH 201 601 416 HOH HOH B . 
# 
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 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0258 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SAINT  ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? SAINT  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   100.89 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YVH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     37.398 
_cell.length_a_esd                 ? 
_cell.length_b                     117.950 
_cell.length_b_esd                 ? 
_cell.length_c                     63.529 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8YVH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   8YVH 
_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             2.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.37 
_exptl_crystal.description                  ? 
_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              8.5 
_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    'PEG3350, magnesium chloride, Tris-Hcl pH 8.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_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                         'Bruker PHOTON III' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-25 
_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   1.34138 
_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                      'LIQUID ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'BRUKER METALJET' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.34138 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YVH 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.00 
_reflns.d_resolution_low                               35.09 
_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                                     36140 
_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                           98.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.99 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.36 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.0638 
_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                                    2.00 
_reflns_shell.d_res_low                                     2.03 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.08 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1528 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               2.08 
_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                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          84.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.1661 
_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]                            1.54 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.41 
_refine.aniso_B[2][2]                            0.33 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.59 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               22.384 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.954 
_refine.correlation_coeff_Fo_to_Fc_free          0.906 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8YVH 
_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                            2.10 
_refine.ls_d_res_low                             35.09 
_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                     29740 
_refine.ls_number_reflns_R_free                  1596 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.35 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17061 
_refine.ls_R_factor_R_free                       0.24140 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16687 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.240 
_refine.pdbx_overall_ESU_R_Free                  0.207 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             5.368 
_refine.overall_SU_ML                            0.142 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        35.09 
_refine_hist.number_atoms_solvent             455 
_refine_hist.number_atoms_total               4782 
_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        4223 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         104 
_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' ? 0.008  0.013  4386 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  4211 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.580  1.661  5974 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.327  1.582  9799 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.042  5.000  578  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 37.845 24.771 153  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.556 15.000 753  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.943 15.000 14   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.071  0.200  614  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  4799 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  753  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.525  2.232  2319 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.526  2.232  2318 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.306  3.342  2894 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.305  3.342  2895 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.192  2.505  2067 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.192  2.505  2068 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.326  3.645  3081 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.084  28.677 5077 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.009  28.422 4987 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                          2.100 
_refine_ls_shell.d_res_low                           2.155 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                119 
_refine_ls_shell.number_reflns_R_work                2191 
_refine_ls_shell.percent_reflns_obs                  99.44 
_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                     0.209 
_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.correlation_coeff_Fo_to_Fc          ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free     ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work   ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free   ? 
_refine_ls_shell.pdbx_total_number_of_bins_used      20 
_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                     0.284 
# 
_struct.entry_id                     8YVH 
_struct.title                        'NADPH complex of Imine Reductase Mutant(M6) from Pochonia chlamydosporia 170' 
_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        8YVH 
_struct_keywords.text            'NADPH complex of Mutant(M6), Imine reductase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A179FZ20_METCM 
_struct_ref.pdbx_db_accession          A0A179FZ20 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSSSNKPHVSLIGLGNMGLAIANCLIKSGCKLTVWNRSASKAASLVAQGVTVAATPAECVASSPTIVICLLSYDVTQQTL
DEVIDLSGKTIINLTNGTPQQAVKVATLVQQRGAESYIHGAIMVPPILLGQPSSVTLISGPKTAYESQKELLSSIGTTRH
VSDDIAKASLLDNALLSIMGGVFEGWVQALAIVGKAGEDEVDFAALASPFVKSMADWLPRIAGHVREKQYVGGSPLTMQL
EALENISETSRELGVGVLLGSMREVMSEAVKKGKGGESIAGLVPMLTELDKKW
;
_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 8YVH A 21 ? 313 ? A0A179FZ20 1 ? 293 ? 1 293 
2 1 8YVH B 21 ? 313 ? A0A179FZ20 1 ? 293 ? 1 293 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8YVH MET A 1   ? UNP A0A179FZ20 ?   ?   'initiating methionine' -19 1  
1 8YVH GLY A 2   ? UNP A0A179FZ20 ?   ?   'expression tag'        -18 2  
1 8YVH SER A 3   ? UNP A0A179FZ20 ?   ?   'expression tag'        -17 3  
1 8YVH SER A 4   ? UNP A0A179FZ20 ?   ?   'expression tag'        -16 4  
1 8YVH HIS A 5   ? UNP A0A179FZ20 ?   ?   'expression tag'        -15 5  
1 8YVH HIS A 6   ? UNP A0A179FZ20 ?   ?   'expression tag'        -14 6  
1 8YVH HIS A 7   ? UNP A0A179FZ20 ?   ?   'expression tag'        -13 7  
1 8YVH HIS A 8   ? UNP A0A179FZ20 ?   ?   'expression tag'        -12 8  
1 8YVH HIS A 9   ? UNP A0A179FZ20 ?   ?   'expression tag'        -11 9  
1 8YVH HIS A 10  ? UNP A0A179FZ20 ?   ?   'expression tag'        -10 10 
1 8YVH SER A 11  ? UNP A0A179FZ20 ?   ?   'expression tag'        -9  11 
1 8YVH SER A 12  ? UNP A0A179FZ20 ?   ?   'expression tag'        -8  12 
1 8YVH GLY A 13  ? UNP A0A179FZ20 ?   ?   'expression tag'        -7  13 
1 8YVH GLU A 14  ? UNP A0A179FZ20 ?   ?   'expression tag'        -6  14 
1 8YVH ASN A 15  ? UNP A0A179FZ20 ?   ?   'expression tag'        -5  15 
1 8YVH LEU A 16  ? UNP A0A179FZ20 ?   ?   'expression tag'        -4  16 
1 8YVH TYR A 17  ? UNP A0A179FZ20 ?   ?   'expression tag'        -3  17 
1 8YVH PHE A 18  ? UNP A0A179FZ20 ?   ?   'expression tag'        -2  18 
1 8YVH GLN A 19  ? UNP A0A179FZ20 ?   ?   'expression tag'        -1  19 
1 8YVH GLY A 20  ? UNP A0A179FZ20 ?   ?   'expression tag'        0   20 
1 8YVH GLU A 60  ? UNP A0A179FZ20 SER 40  conflict                40  21 
1 8YVH PRO A 67  ? UNP A0A179FZ20 ALA 47  conflict                47  22 
1 8YVH ALA A 70  ? UNP A0A179FZ20 VAL 50  conflict                50  23 
1 8YVH ASN A 92  ? UNP A0A179FZ20 SER 72  conflict                72  24 
1 8YVH GLN A 93  ? UNP A0A179FZ20 TYR 73  conflict                73  25 
1 8YVH VAL A 96  ? UNP A0A179FZ20 THR 76  conflict                76  26 
1 8YVH THR A 144 ? UNP A0A179FZ20 VAL 124 conflict                124 27 
1 8YVH THR A 145 ? UNP A0A179FZ20 PRO 125 conflict                125 28 
1 8YVH GLU A 147 ? UNP A0A179FZ20 ILE 127 conflict                127 29 
1 8YVH TYR A 148 ? UNP A0A179FZ20 LEU 128 conflict                128 30 
1 8YVH VAL A 198 ? UNP A0A179FZ20 ILE 178 conflict                178 31 
1 8YVH SER A 200 ? UNP A0A179FZ20 GLY 180 conflict                180 32 
1 8YVH ALA A 215 ? UNP A0A179FZ20 LYS 195 conflict                195 33 
1 8YVH LEU A 230 ? UNP A0A179FZ20 PHE 210 conflict                210 34 
1 8YVH ALA A 232 ? UNP A0A179FZ20 LYS 212 conflict                212 35 
1 8YVH GLN A 237 ? UNP A0A179FZ20 TRP 217 conflict                217 36 
1 8YVH VAL A 240 ? UNP A0A179FZ20 ARG 220 conflict                220 37 
1 8YVH ARG A 244 ? UNP A0A179FZ20 HIS 224 conflict                224 38 
1 8YVH ILE A 256 ? UNP A0A179FZ20 LEU 236 conflict                236 39 
1 8YVH GLY A 259 ? UNP A0A179FZ20 GLN 239 conflict                239 40 
2 8YVH MET B 1   ? UNP A0A179FZ20 ?   ?   'initiating methionine' -19 41 
2 8YVH GLY B 2   ? UNP A0A179FZ20 ?   ?   'expression tag'        -18 42 
2 8YVH SER B 3   ? UNP A0A179FZ20 ?   ?   'expression tag'        -17 43 
2 8YVH SER B 4   ? UNP A0A179FZ20 ?   ?   'expression tag'        -16 44 
2 8YVH HIS B 5   ? UNP A0A179FZ20 ?   ?   'expression tag'        -15 45 
2 8YVH HIS B 6   ? UNP A0A179FZ20 ?   ?   'expression tag'        -14 46 
2 8YVH HIS B 7   ? UNP A0A179FZ20 ?   ?   'expression tag'        -13 47 
2 8YVH HIS B 8   ? UNP A0A179FZ20 ?   ?   'expression tag'        -12 48 
2 8YVH HIS B 9   ? UNP A0A179FZ20 ?   ?   'expression tag'        -11 49 
2 8YVH HIS B 10  ? UNP A0A179FZ20 ?   ?   'expression tag'        -10 50 
2 8YVH SER B 11  ? UNP A0A179FZ20 ?   ?   'expression tag'        -9  51 
2 8YVH SER B 12  ? UNP A0A179FZ20 ?   ?   'expression tag'        -8  52 
2 8YVH GLY B 13  ? UNP A0A179FZ20 ?   ?   'expression tag'        -7  53 
2 8YVH GLU B 14  ? UNP A0A179FZ20 ?   ?   'expression tag'        -6  54 
2 8YVH ASN B 15  ? UNP A0A179FZ20 ?   ?   'expression tag'        -5  55 
2 8YVH LEU B 16  ? UNP A0A179FZ20 ?   ?   'expression tag'        -4  56 
2 8YVH TYR B 17  ? UNP A0A179FZ20 ?   ?   'expression tag'        -3  57 
2 8YVH PHE B 18  ? UNP A0A179FZ20 ?   ?   'expression tag'        -2  58 
2 8YVH GLN B 19  ? UNP A0A179FZ20 ?   ?   'expression tag'        -1  59 
2 8YVH GLY B 20  ? UNP A0A179FZ20 ?   ?   'expression tag'        0   60 
2 8YVH GLU B 60  ? UNP A0A179FZ20 SER 40  conflict                40  61 
2 8YVH PRO B 67  ? UNP A0A179FZ20 ALA 47  conflict                47  62 
2 8YVH ALA B 70  ? UNP A0A179FZ20 VAL 50  conflict                50  63 
2 8YVH ASN B 92  ? UNP A0A179FZ20 SER 72  conflict                72  64 
2 8YVH GLN B 93  ? UNP A0A179FZ20 TYR 73  conflict                73  65 
2 8YVH VAL B 96  ? UNP A0A179FZ20 THR 76  conflict                76  66 
2 8YVH THR B 144 ? UNP A0A179FZ20 VAL 124 conflict                124 67 
2 8YVH THR B 145 ? UNP A0A179FZ20 PRO 125 conflict                125 68 
2 8YVH GLU B 147 ? UNP A0A179FZ20 ILE 127 conflict                127 69 
2 8YVH TYR B 148 ? UNP A0A179FZ20 LEU 128 conflict                128 70 
2 8YVH VAL B 198 ? UNP A0A179FZ20 ILE 178 conflict                178 71 
2 8YVH SER B 200 ? UNP A0A179FZ20 GLY 180 conflict                180 72 
2 8YVH ALA B 215 ? UNP A0A179FZ20 LYS 195 conflict                195 73 
2 8YVH LEU B 230 ? UNP A0A179FZ20 PHE 210 conflict                210 74 
2 8YVH ALA B 232 ? UNP A0A179FZ20 LYS 212 conflict                212 75 
2 8YVH GLN B 237 ? UNP A0A179FZ20 TRP 217 conflict                217 76 
2 8YVH VAL B 240 ? UNP A0A179FZ20 ARG 220 conflict                220 77 
2 8YVH ARG B 244 ? UNP A0A179FZ20 HIS 224 conflict                224 78 
2 8YVH ILE B 256 ? UNP A0A179FZ20 LEU 236 conflict                236 79 
2 8YVH GLY B 259 ? UNP A0A179FZ20 GLN 239 conflict                239 80 
# 
_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)' 10710 ? 
1 MORE         -86   ? 
1 'SSA (A^2)'  22520 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 35  ? SER A 48  ? GLY A 15  SER A 28  1 ? 14 
HELX_P HELX_P2  AA2 SER A 58  ? GLY A 69  ? SER A 38  GLY A 49  5 ? 12 
HELX_P HELX_P3  AA3 THR A 75  ? SER A 82  ? THR A 55  SER A 62  1 ? 8  
HELX_P HELX_P4  AA4 ASN A 92  ? ASP A 101 ? ASN A 72  ASP A 81  1 ? 10 
HELX_P HELX_P5  AA5 THR A 118 ? ARG A 132 ? THR A 98  ARG A 112 1 ? 15 
HELX_P HELX_P6  AA6 THR A 145 ? LEU A 149 ? THR A 125 LEU A 129 5 ? 5  
HELX_P HELX_P7  AA7 PRO A 161 ? SER A 173 ? PRO A 141 SER A 153 1 ? 13 
HELX_P HELX_P8  AA8 SER A 174 ? GLY A 176 ? SER A 154 GLY A 156 5 ? 3  
HELX_P HELX_P9  AA9 ALA A 186 ? ALA A 216 ? ALA A 166 ALA A 196 1 ? 31 
HELX_P HELX_P10 AB1 ASP A 219 ? GLU A 247 ? ASP A 199 GLU A 227 1 ? 29 
HELX_P HELX_P11 AB2 PRO A 255 ? LEU A 273 ? PRO A 235 LEU A 253 1 ? 19 
HELX_P HELX_P12 AB3 LEU A 279 ? LYS A 292 ? LEU A 259 LYS A 272 1 ? 14 
HELX_P HELX_P13 AB4 SER A 298 ? GLY A 301 ? SER A 278 GLY A 281 5 ? 4  
HELX_P HELX_P14 AB5 LEU A 302 ? GLU A 308 ? LEU A 282 GLU A 288 1 ? 7  
HELX_P HELX_P15 AB6 GLY B 35  ? GLY B 49  ? GLY B 15  GLY B 29  1 ? 15 
HELX_P HELX_P16 AB7 SER B 58  ? ALA B 63  ? SER B 38  ALA B 43  5 ? 6  
HELX_P HELX_P17 AB8 LEU B 65  ? GLY B 69  ? LEU B 45  GLY B 49  5 ? 5  
HELX_P HELX_P18 AB9 THR B 75  ? SER B 82  ? THR B 55  SER B 62  1 ? 8  
HELX_P HELX_P19 AC1 ASN B 92  ? LEU B 100 ? ASN B 72  LEU B 80  1 ? 9  
HELX_P HELX_P20 AC2 THR B 118 ? ARG B 132 ? THR B 98  ARG B 112 1 ? 15 
HELX_P HELX_P21 AC3 THR B 145 ? LEU B 149 ? THR B 125 LEU B 129 5 ? 5  
HELX_P HELX_P22 AC4 PRO B 161 ? SER B 174 ? PRO B 141 SER B 154 1 ? 14 
HELX_P HELX_P23 AC5 ALA B 186 ? ALA B 216 ? ALA B 166 ALA B 196 1 ? 31 
HELX_P HELX_P24 AC6 ASP B 219 ? GLU B 247 ? ASP B 199 GLU B 227 1 ? 29 
HELX_P HELX_P25 AC7 PRO B 255 ? LEU B 273 ? PRO B 235 LEU B 253 1 ? 19 
HELX_P HELX_P26 AC8 LEU B 279 ? LYS B 292 ? LEU B 259 LYS B 272 1 ? 14 
HELX_P HELX_P27 AC9 SER B 298 ? GLY B 301 ? SER B 278 GLY B 281 5 ? 4  
HELX_P HELX_P28 AD1 LEU B 302 ? GLU B 308 ? LEU B 282 GLU B 288 1 ? 7  
# 
_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 ? 8 ? 
AA2 ? 8 ? 
# 
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 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA2 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 71  ? VAL A 72  ? THR A 51  VAL A 52  
AA1 2 LYS A 51  ? TRP A 55  ? LYS A 31  TRP A 35  
AA1 3 HIS A 28  ? ILE A 32  ? HIS A 8   ILE A 12  
AA1 4 THR A 85  ? ILE A 88  ? THR A 65  ILE A 68  
AA1 5 THR A 110 ? ASN A 113 ? THR A 90  ASN A 93  
AA1 6 SER A 136 ? ILE A 142 ? SER A 116 ILE A 122 
AA1 7 VAL A 155 ? SER A 159 ? VAL A 135 SER A 139 
AA1 8 THR A 177 ? SER A 182 ? THR A 157 SER A 162 
AA2 1 THR B 71  ? VAL B 72  ? THR B 51  VAL B 52  
AA2 2 LYS B 51  ? TRP B 55  ? LYS B 31  TRP B 35  
AA2 3 HIS B 28  ? ILE B 32  ? HIS B 8   ILE B 12  
AA2 4 THR B 85  ? ILE B 88  ? THR B 65  ILE B 68  
AA2 5 THR B 110 ? ASN B 113 ? THR B 90  ASN B 93  
AA2 6 SER B 136 ? ILE B 142 ? SER B 116 ILE B 122 
AA2 7 VAL B 155 ? SER B 159 ? VAL B 135 SER B 139 
AA2 8 THR B 177 ? SER B 182 ? THR B 157 SER B 162 
# 
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 THR A 71  ? O THR A 51  N VAL A 54  ? N VAL A 34  
AA1 2 3 O LYS A 51  ? O LYS A 31  N VAL A 29  ? N VAL A 9   
AA1 3 4 N SER A 30  ? N SER A 10  O THR A 85  ? O THR A 65  
AA1 4 5 N ILE A 86  ? N ILE A 66  O ILE A 112 ? O ILE A 92  
AA1 5 6 N ILE A 111 ? N ILE A 91  O SER A 136 ? O SER A 116 
AA1 6 7 N ALA A 141 ? N ALA A 121 O LEU A 157 ? O LEU A 137 
AA1 7 8 N ILE A 158 ? N ILE A 138 O VAL A 181 ? O VAL A 161 
AA2 1 2 O THR B 71  ? O THR B 51  N LEU B 52  ? N LEU B 32  
AA2 2 3 O THR B 53  ? O THR B 33  N LEU B 31  ? N LEU B 11  
AA2 3 4 N SER B 30  ? N SER B 10  O VAL B 87  ? O VAL B 67  
AA2 4 5 N ILE B 86  ? N ILE B 66  O ILE B 112 ? O ILE B 92  
AA2 5 6 N ILE B 111 ? N ILE B 91  O SER B 136 ? O SER B 116 
AA2 6 7 N HIS B 139 ? N HIS B 119 O SER B 159 ? O SER B 139 
AA2 7 8 N ILE B 158 ? N ILE B 138 O ARG B 179 ? O ARG B 159 
# 
_pdbx_entry_details.entry_id                   8YVH 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 MET A 123 ? ? -105.07 47.39   
2 1 SER A 162 ? ? -174.30 149.22  
3 1 LEU A 258 ? ? -94.13  -159.85 
4 1 VAL B 83  ? ? -65.18  94.55   
5 1 MET B 123 ? ? -104.02 48.31   
6 1 LEU B 258 ? ? -96.30  -158.32 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 651 ? 6.03 . 
2 1 O ? A HOH 652 ? 6.59 . 
3 1 O ? A HOH 653 ? 6.64 . 
4 1 O ? A HOH 654 ? 8.52 . 
# 
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 GLU -6  ? A GLU 14 
15 1 Y 1 A ASN -5  ? A ASN 15 
16 1 Y 1 A LEU -4  ? A LEU 16 
17 1 Y 1 A TYR -3  ? A TYR 17 
18 1 Y 1 A PHE -2  ? A PHE 18 
19 1 Y 1 A GLN -1  ? A GLN 19 
20 1 Y 1 A GLY 0   ? A GLY 20 
21 1 Y 1 B MET -19 ? B MET 1  
22 1 Y 1 B GLY -18 ? B GLY 2  
23 1 Y 1 B SER -17 ? B SER 3  
24 1 Y 1 B SER -16 ? B SER 4  
25 1 Y 1 B HIS -15 ? B HIS 5  
26 1 Y 1 B HIS -14 ? B HIS 6  
27 1 Y 1 B HIS -13 ? B HIS 7  
28 1 Y 1 B HIS -12 ? B HIS 8  
29 1 Y 1 B HIS -11 ? B HIS 9  
30 1 Y 1 B HIS -10 ? B HIS 10 
31 1 Y 1 B SER -9  ? B SER 11 
32 1 Y 1 B SER -8  ? B SER 12 
33 1 Y 1 B GLY -7  ? B GLY 13 
34 1 Y 1 B GLU -6  ? B GLU 14 
35 1 Y 1 B ASN -5  ? B ASN 15 
36 1 Y 1 B LEU -4  ? B LEU 16 
37 1 Y 1 B TYR -3  ? B TYR 17 
38 1 Y 1 B PHE -2  ? B PHE 18 
39 1 Y 1 B GLN -1  ? B GLN 19 
40 1 Y 1 B GLY 0   ? B GLY 20 
41 1 Y 1 B MET 1   ? B MET 21 
42 1 Y 1 B SER 2   ? B SER 22 
43 1 Y 1 B SER 3   ? B SER 23 
44 1 Y 1 B SER 4   ? B SER 24 
45 1 Y 1 B ASN 5   ? B ASN 25 
46 1 Y 1 B LYS 6   ? B LYS 26 
# 
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  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
NAP PA   P N R 250 
NAP O1A  O N N 251 
NAP O2A  O N N 252 
NAP O5B  O N N 253 
NAP C5B  C N N 254 
NAP C4B  C N R 255 
NAP O4B  O N N 256 
NAP C3B  C N R 257 
NAP O3B  O N N 258 
NAP C2B  C N R 259 
NAP O2B  O N N 260 
NAP C1B  C N R 261 
NAP N9A  N Y N 262 
NAP C8A  C Y N 263 
NAP N7A  N Y N 264 
NAP C5A  C Y N 265 
NAP C6A  C Y N 266 
NAP N6A  N N N 267 
NAP N1A  N Y N 268 
NAP C2A  C Y N 269 
NAP N3A  N Y N 270 
NAP C4A  C Y N 271 
NAP O3   O N N 272 
NAP PN   P N N 273 
NAP O1N  O N N 274 
NAP O2N  O N N 275 
NAP O5D  O N N 276 
NAP C5D  C N N 277 
NAP C4D  C N R 278 
NAP O4D  O N N 279 
NAP C3D  C N S 280 
NAP O3D  O N N 281 
NAP C2D  C N R 282 
NAP O2D  O N N 283 
NAP C1D  C N R 284 
NAP N1N  N Y N 285 
NAP C2N  C Y N 286 
NAP C3N  C Y N 287 
NAP C7N  C N N 288 
NAP O7N  O N N 289 
NAP N7N  N N N 290 
NAP C4N  C Y N 291 
NAP C5N  C Y N 292 
NAP C6N  C Y N 293 
NAP P2B  P N N 294 
NAP O1X  O N N 295 
NAP O2X  O N N 296 
NAP O3X  O N N 297 
NAP HOA2 H N N 298 
NAP H51A H N N 299 
NAP H52A H N N 300 
NAP H4B  H N N 301 
NAP H3B  H N N 302 
NAP HO3A H N N 303 
NAP H2B  H N N 304 
NAP H1B  H N N 305 
NAP H8A  H N N 306 
NAP H61A H N N 307 
NAP H62A H N N 308 
NAP H2A  H N N 309 
NAP H51N H N N 310 
NAP H52N H N N 311 
NAP H4D  H N N 312 
NAP H3D  H N N 313 
NAP HO3N H N N 314 
NAP H2D  H N N 315 
NAP HO2N H N N 316 
NAP H1D  H N N 317 
NAP H2N  H N N 318 
NAP H71N H N N 319 
NAP H72N H N N 320 
NAP H4N  H N N 321 
NAP H5N  H N N 322 
NAP H6N  H N N 323 
NAP HOP2 H N N 324 
NAP HOP3 H N N 325 
PHE N    N N N 326 
PHE CA   C N S 327 
PHE C    C N N 328 
PHE O    O N N 329 
PHE CB   C N N 330 
PHE CG   C Y N 331 
PHE CD1  C Y N 332 
PHE CD2  C Y N 333 
PHE CE1  C Y N 334 
PHE CE2  C Y N 335 
PHE CZ   C Y N 336 
PHE OXT  O N N 337 
PHE H    H N N 338 
PHE H2   H N N 339 
PHE HA   H N N 340 
PHE HB2  H N N 341 
PHE HB3  H N N 342 
PHE HD1  H N N 343 
PHE HD2  H N N 344 
PHE HE1  H N N 345 
PHE HE2  H N N 346 
PHE HZ   H N N 347 
PHE HXT  H N N 348 
PRO N    N N N 349 
PRO CA   C N S 350 
PRO C    C N N 351 
PRO O    O N N 352 
PRO CB   C N N 353 
PRO CG   C N N 354 
PRO CD   C N N 355 
PRO OXT  O N N 356 
PRO H    H N N 357 
PRO HA   H N N 358 
PRO HB2  H N N 359 
PRO HB3  H N N 360 
PRO HG2  H N N 361 
PRO HG3  H N N 362 
PRO HD2  H N N 363 
PRO HD3  H N N 364 
PRO HXT  H N N 365 
SER N    N N N 366 
SER CA   C N S 367 
SER C    C N N 368 
SER O    O N N 369 
SER CB   C N N 370 
SER OG   O N N 371 
SER OXT  O N N 372 
SER H    H N N 373 
SER H2   H N N 374 
SER HA   H N N 375 
SER HB2  H N N 376 
SER HB3  H N N 377 
SER HG   H N N 378 
SER HXT  H N N 379 
THR N    N N N 380 
THR CA   C N S 381 
THR C    C N N 382 
THR O    O N N 383 
THR CB   C N R 384 
THR OG1  O N N 385 
THR CG2  C N N 386 
THR OXT  O N N 387 
THR H    H N N 388 
THR H2   H N N 389 
THR HA   H N N 390 
THR HB   H N N 391 
THR HG1  H N N 392 
THR HG21 H N N 393 
THR HG22 H N N 394 
THR HG23 H N N 395 
THR HXT  H N N 396 
TRP N    N N N 397 
TRP CA   C N S 398 
TRP C    C N N 399 
TRP O    O N N 400 
TRP CB   C N N 401 
TRP CG   C Y N 402 
TRP CD1  C Y N 403 
TRP CD2  C Y N 404 
TRP NE1  N Y N 405 
TRP CE2  C Y N 406 
TRP CE3  C Y N 407 
TRP CZ2  C Y N 408 
TRP CZ3  C Y N 409 
TRP CH2  C Y N 410 
TRP OXT  O N N 411 
TRP H    H N N 412 
TRP H2   H N N 413 
TRP HA   H N N 414 
TRP HB2  H N N 415 
TRP HB3  H N N 416 
TRP HD1  H N N 417 
TRP HE1  H N N 418 
TRP HE3  H N N 419 
TRP HZ2  H N N 420 
TRP HZ3  H N N 421 
TRP HH2  H N N 422 
TRP HXT  H N N 423 
TRS C    C N N 424 
TRS C1   C N N 425 
TRS C2   C N N 426 
TRS C3   C N N 427 
TRS N    N N N 428 
TRS O1   O N N 429 
TRS O2   O N N 430 
TRS O3   O N N 431 
TRS H11  H N N 432 
TRS H12  H N N 433 
TRS H21  H N N 434 
TRS H22  H N N 435 
TRS H31  H N N 436 
TRS H32  H N N 437 
TRS HN1  H N N 438 
TRS HN2  H N N 439 
TRS HN3  H N N 440 
TRS HO1  H N N 441 
TRS HO2  H N N 442 
TRS HO3  H N N 443 
TYR N    N N N 444 
TYR CA   C N S 445 
TYR C    C N N 446 
TYR O    O N N 447 
TYR CB   C N N 448 
TYR CG   C Y N 449 
TYR CD1  C Y N 450 
TYR CD2  C Y N 451 
TYR CE1  C Y N 452 
TYR CE2  C Y N 453 
TYR CZ   C Y N 454 
TYR OH   O N N 455 
TYR OXT  O N N 456 
TYR H    H N N 457 
TYR H2   H N N 458 
TYR HA   H N N 459 
TYR HB2  H N N 460 
TYR HB3  H N N 461 
TYR HD1  H N N 462 
TYR HD2  H N N 463 
TYR HE1  H N N 464 
TYR HE2  H N N 465 
TYR HH   H N N 466 
TYR HXT  H N N 467 
VAL N    N N N 468 
VAL CA   C N S 469 
VAL C    C N N 470 
VAL O    O N N 471 
VAL CB   C N N 472 
VAL CG1  C N N 473 
VAL CG2  C N N 474 
VAL OXT  O N N 475 
VAL H    H N N 476 
VAL H2   H N N 477 
VAL HA   H N N 478 
VAL HB   H N N 479 
VAL HG11 H N N 480 
VAL HG12 H N N 481 
VAL HG13 H N N 482 
VAL HG21 H N N 483 
VAL HG22 H N N 484 
VAL HG23 H N N 485 
VAL HXT  H N N 486 
# 
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  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
NAP PA  O1A  doub N N 237 
NAP PA  O2A  sing N N 238 
NAP PA  O5B  sing N N 239 
NAP PA  O3   sing N N 240 
NAP O2A HOA2 sing N N 241 
NAP O5B C5B  sing N N 242 
NAP C5B C4B  sing N N 243 
NAP C5B H51A sing N N 244 
NAP C5B H52A sing N N 245 
NAP C4B O4B  sing N N 246 
NAP C4B C3B  sing N N 247 
NAP C4B H4B  sing N N 248 
NAP O4B C1B  sing N N 249 
NAP C3B O3B  sing N N 250 
NAP C3B C2B  sing N N 251 
NAP C3B H3B  sing N N 252 
NAP O3B HO3A sing N N 253 
NAP C2B O2B  sing N N 254 
NAP C2B C1B  sing N N 255 
NAP C2B H2B  sing N N 256 
NAP O2B P2B  sing N N 257 
NAP C1B N9A  sing N N 258 
NAP C1B H1B  sing N N 259 
NAP N9A C8A  sing Y N 260 
NAP N9A C4A  sing Y N 261 
NAP C8A N7A  doub Y N 262 
NAP C8A H8A  sing N N 263 
NAP N7A C5A  sing Y N 264 
NAP C5A C6A  sing Y N 265 
NAP C5A C4A  doub Y N 266 
NAP C6A N6A  sing N N 267 
NAP C6A N1A  doub Y N 268 
NAP N6A H61A sing N N 269 
NAP N6A H62A sing N N 270 
NAP N1A C2A  sing Y N 271 
NAP C2A N3A  doub Y N 272 
NAP C2A H2A  sing N N 273 
NAP N3A C4A  sing Y N 274 
NAP O3  PN   sing N N 275 
NAP PN  O1N  doub N N 276 
NAP PN  O2N  sing N N 277 
NAP PN  O5D  sing N N 278 
NAP O5D C5D  sing N N 279 
NAP C5D C4D  sing N N 280 
NAP C5D H51N sing N N 281 
NAP C5D H52N sing N N 282 
NAP C4D O4D  sing N N 283 
NAP C4D C3D  sing N N 284 
NAP C4D H4D  sing N N 285 
NAP O4D C1D  sing N N 286 
NAP C3D O3D  sing N N 287 
NAP C3D C2D  sing N N 288 
NAP C3D H3D  sing N N 289 
NAP O3D HO3N sing N N 290 
NAP C2D O2D  sing N N 291 
NAP C2D C1D  sing N N 292 
NAP C2D H2D  sing N N 293 
NAP O2D HO2N sing N N 294 
NAP C1D N1N  sing N N 295 
NAP C1D H1D  sing N N 296 
NAP N1N C2N  sing Y N 297 
NAP N1N C6N  doub Y N 298 
NAP C2N C3N  doub Y N 299 
NAP C2N H2N  sing N N 300 
NAP C3N C7N  sing N N 301 
NAP C3N C4N  sing Y N 302 
NAP C7N O7N  doub N N 303 
NAP C7N N7N  sing N N 304 
NAP N7N H71N sing N N 305 
NAP N7N H72N sing N N 306 
NAP C4N C5N  doub Y N 307 
NAP C4N H4N  sing N N 308 
NAP C5N C6N  sing Y N 309 
NAP C5N H5N  sing N N 310 
NAP C6N H6N  sing N N 311 
NAP P2B O1X  doub N N 312 
NAP P2B O2X  sing N N 313 
NAP P2B O3X  sing N N 314 
NAP O2X HOP2 sing N N 315 
NAP O3X HOP3 sing N N 316 
PHE N   CA   sing N N 317 
PHE N   H    sing N N 318 
PHE N   H2   sing N N 319 
PHE CA  C    sing N N 320 
PHE CA  CB   sing N N 321 
PHE CA  HA   sing N N 322 
PHE C   O    doub N N 323 
PHE C   OXT  sing N N 324 
PHE CB  CG   sing N N 325 
PHE CB  HB2  sing N N 326 
PHE CB  HB3  sing N N 327 
PHE CG  CD1  doub Y N 328 
PHE CG  CD2  sing Y N 329 
PHE CD1 CE1  sing Y N 330 
PHE CD1 HD1  sing N N 331 
PHE CD2 CE2  doub Y N 332 
PHE CD2 HD2  sing N N 333 
PHE CE1 CZ   doub Y N 334 
PHE CE1 HE1  sing N N 335 
PHE CE2 CZ   sing Y N 336 
PHE CE2 HE2  sing N N 337 
PHE CZ  HZ   sing N N 338 
PHE OXT HXT  sing N N 339 
PRO N   CA   sing N N 340 
PRO N   CD   sing N N 341 
PRO N   H    sing N N 342 
PRO CA  C    sing N N 343 
PRO CA  CB   sing N N 344 
PRO CA  HA   sing N N 345 
PRO C   O    doub N N 346 
PRO C   OXT  sing N N 347 
PRO CB  CG   sing N N 348 
PRO CB  HB2  sing N N 349 
PRO CB  HB3  sing N N 350 
PRO CG  CD   sing N N 351 
PRO CG  HG2  sing N N 352 
PRO CG  HG3  sing N N 353 
PRO CD  HD2  sing N N 354 
PRO CD  HD3  sing N N 355 
PRO OXT HXT  sing N N 356 
SER N   CA   sing N N 357 
SER N   H    sing N N 358 
SER N   H2   sing N N 359 
SER CA  C    sing N N 360 
SER CA  CB   sing N N 361 
SER CA  HA   sing N N 362 
SER C   O    doub N N 363 
SER C   OXT  sing N N 364 
SER CB  OG   sing N N 365 
SER CB  HB2  sing N N 366 
SER CB  HB3  sing N N 367 
SER OG  HG   sing N N 368 
SER OXT HXT  sing N N 369 
THR N   CA   sing N N 370 
THR N   H    sing N N 371 
THR N   H2   sing N N 372 
THR CA  C    sing N N 373 
THR CA  CB   sing N N 374 
THR CA  HA   sing N N 375 
THR C   O    doub N N 376 
THR C   OXT  sing N N 377 
THR CB  OG1  sing N N 378 
THR CB  CG2  sing N N 379 
THR CB  HB   sing N N 380 
THR OG1 HG1  sing N N 381 
THR CG2 HG21 sing N N 382 
THR CG2 HG22 sing N N 383 
THR CG2 HG23 sing N N 384 
THR OXT HXT  sing N N 385 
TRP N   CA   sing N N 386 
TRP N   H    sing N N 387 
TRP N   H2   sing N N 388 
TRP CA  C    sing N N 389 
TRP CA  CB   sing N N 390 
TRP CA  HA   sing N N 391 
TRP C   O    doub N N 392 
TRP C   OXT  sing N N 393 
TRP CB  CG   sing N N 394 
TRP CB  HB2  sing N N 395 
TRP CB  HB3  sing N N 396 
TRP CG  CD1  doub Y N 397 
TRP CG  CD2  sing Y N 398 
TRP CD1 NE1  sing Y N 399 
TRP CD1 HD1  sing N N 400 
TRP CD2 CE2  doub Y N 401 
TRP CD2 CE3  sing Y N 402 
TRP NE1 CE2  sing Y N 403 
TRP NE1 HE1  sing N N 404 
TRP CE2 CZ2  sing Y N 405 
TRP CE3 CZ3  doub Y N 406 
TRP CE3 HE3  sing N N 407 
TRP CZ2 CH2  doub Y N 408 
TRP CZ2 HZ2  sing N N 409 
TRP CZ3 CH2  sing Y N 410 
TRP CZ3 HZ3  sing N N 411 
TRP CH2 HH2  sing N N 412 
TRP OXT HXT  sing N N 413 
TRS C   C1   sing N N 414 
TRS C   C2   sing N N 415 
TRS C   C3   sing N N 416 
TRS C   N    sing N N 417 
TRS C1  O1   sing N N 418 
TRS C1  H11  sing N N 419 
TRS C1  H12  sing N N 420 
TRS C2  O2   sing N N 421 
TRS C2  H21  sing N N 422 
TRS C2  H22  sing N N 423 
TRS C3  O3   sing N N 424 
TRS C3  H31  sing N N 425 
TRS C3  H32  sing N N 426 
TRS N   HN1  sing N N 427 
TRS N   HN2  sing N N 428 
TRS N   HN3  sing N N 429 
TRS O1  HO1  sing N N 430 
TRS O2  HO2  sing N N 431 
TRS O3  HO3  sing N N 432 
TYR N   CA   sing N N 433 
TYR N   H    sing N N 434 
TYR N   H2   sing N N 435 
TYR CA  C    sing N N 436 
TYR CA  CB   sing N N 437 
TYR CA  HA   sing N N 438 
TYR C   O    doub N N 439 
TYR C   OXT  sing N N 440 
TYR CB  CG   sing N N 441 
TYR CB  HB2  sing N N 442 
TYR CB  HB3  sing N N 443 
TYR CG  CD1  doub Y N 444 
TYR CG  CD2  sing Y N 445 
TYR CD1 CE1  sing Y N 446 
TYR CD1 HD1  sing N N 447 
TYR CD2 CE2  doub Y N 448 
TYR CD2 HD2  sing N N 449 
TYR CE1 CZ   doub Y N 450 
TYR CE1 HE1  sing N N 451 
TYR CE2 CZ   sing Y N 452 
TYR CE2 HE2  sing N N 453 
TYR CZ  OH   sing N N 454 
TYR OH  HH   sing N N 455 
TYR OXT HXT  sing N N 456 
VAL N   CA   sing N N 457 
VAL N   H    sing N N 458 
VAL N   H2   sing N N 459 
VAL CA  C    sing N N 460 
VAL CA  CB   sing N N 461 
VAL CA  HA   sing N N 462 
VAL C   O    doub N N 463 
VAL C   OXT  sing N N 464 
VAL CB  CG1  sing N N 465 
VAL CB  CG2  sing N N 466 
VAL CB  HB   sing N N 467 
VAL CG1 HG11 sing N N 468 
VAL CG1 HG12 sing N N 469 
VAL CG1 HG13 sing N N 470 
VAL CG2 HG21 sing N N 471 
VAL CG2 HG22 sing N N 472 
VAL CG2 HG23 sing N N 473 
VAL OXT HXT  sing N N 474 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YVH 
_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]   0.026739 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005146 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008478 
_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]   0.016030 
_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 
C 
N 
O 
P 
S 
# 
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   . MET A 1 21  ? -10.548 -28.383 15.037  1.00 35.89 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 21  ? -10.310 -29.818 15.390  1.00 35.61 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 21  ? -11.672 -30.431 15.695  1.00 35.97 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 21  ? -12.399 -29.861 16.544  1.00 33.93 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 21  ? -9.392  -29.985 16.607  1.00 35.64 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 21  ? -8.028  -29.320 16.454  1.00 37.01 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 21  ? -7.200  -29.682 14.873  1.00 38.18 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 21  ? -6.791  -31.417 15.057  1.00 36.13 ? 1   MET A CE  1 
ATOM   9    N N   . SER A 1 22  ? -12.018 -31.514 15.005  1.00 35.25 ? 2   SER A N   1 
ATOM   10   C CA  . SER A 1 22  ? -13.391 -32.076 14.997  1.00 36.53 ? 2   SER A CA  1 
ATOM   11   C C   . SER A 1 22  ? -13.691 -32.823 16.305  1.00 35.93 ? 2   SER A C   1 
ATOM   12   O O   . SER A 1 22  ? -14.896 -32.865 16.673  1.00 34.81 ? 2   SER A O   1 
ATOM   13   C CB  . SER A 1 22  ? -13.627 -32.950 13.784  1.00 41.22 ? 2   SER A CB  1 
ATOM   14   O OG  . SER A 1 22  ? -15.019 -33.152 13.571  1.00 42.76 ? 2   SER A OG  1 
ATOM   15   N N   . SER A 1 23  ? -12.687 -33.390 16.996  1.00 33.36 ? 3   SER A N   1 
ATOM   16   C CA  . SER A 1 23  ? -12.944 -34.219 18.208  1.00 33.88 ? 3   SER A CA  1 
ATOM   17   C C   . SER A 1 23  ? -13.236 -33.329 19.427  1.00 34.32 ? 3   SER A C   1 
ATOM   18   O O   . SER A 1 23  ? -12.659 -32.217 19.533  1.00 35.04 ? 3   SER A O   1 
ATOM   19   C CB  . SER A 1 23  ? -11.851 -35.211 18.509  1.00 35.26 ? 3   SER A CB  1 
ATOM   20   O OG  . SER A 1 23  ? -12.295 -36.103 19.530  1.00 33.41 ? 3   SER A OG  1 
ATOM   21   N N   . SER A 1 24  ? -14.122 -33.807 20.308  1.00 31.10 ? 4   SER A N   1 
ATOM   22   C CA  . SER A 1 24  ? -14.404 -33.208 21.639  1.00 29.22 ? 4   SER A CA  1 
ATOM   23   C C   . SER A 1 24  ? -13.183 -33.426 22.534  1.00 28.18 ? 4   SER A C   1 
ATOM   24   O O   . SER A 1 24  ? -13.038 -32.660 23.503  1.00 29.40 ? 4   SER A O   1 
ATOM   25   C CB  . SER A 1 24  ? -15.690 -33.760 22.266  1.00 27.98 ? 4   SER A CB  1 
ATOM   26   O OG  . SER A 1 24  ? -15.625 -35.158 22.550  1.00 21.80 ? 4   SER A OG  1 
ATOM   27   N N   . ASN A 1 25  ? -12.405 -34.478 22.243  1.00 27.84 ? 5   ASN A N   1 
ATOM   28   C CA  . ASN A 1 25  ? -11.082 -34.798 22.853  1.00 29.58 ? 5   ASN A CA  1 
ATOM   29   C C   . ASN A 1 25  ? -9.984  -34.052 22.072  1.00 30.60 ? 5   ASN A C   1 
ATOM   30   O O   . ASN A 1 25  ? -9.556  -34.526 20.973  1.00 27.32 ? 5   ASN A O   1 
ATOM   31   C CB  . ASN A 1 25  ? -10.805 -36.304 22.868  1.00 28.55 ? 5   ASN A CB  1 
ATOM   32   C CG  . ASN A 1 25  ? -9.441  -36.664 23.431  1.00 28.40 ? 5   ASN A CG  1 
ATOM   33   O OD1 . ASN A 1 25  ? -9.050  -36.177 24.490  1.00 25.53 ? 5   ASN A OD1 1 
ATOM   34   N ND2 . ASN A 1 25  ? -8.733  -37.549 22.741  1.00 27.28 ? 5   ASN A ND2 1 
ATOM   35   N N   . LYS A 1 26  ? -9.549  -32.921 22.624  1.00 30.34 ? 6   LYS A N   1 
ATOM   36   C CA  . LYS A 1 26  ? -8.646  -31.965 21.939  1.00 29.16 ? 6   LYS A CA  1 
ATOM   37   C C   . LYS A 1 26  ? -7.218  -32.495 22.001  1.00 27.10 ? 6   LYS A C   1 
ATOM   38   O O   . LYS A 1 26  ? -6.732  -32.875 23.064  1.00 21.52 ? 6   LYS A O   1 
ATOM   39   C CB  . LYS A 1 26  ? -8.809  -30.579 22.563  1.00 31.97 ? 6   LYS A CB  1 
ATOM   40   C CG  . LYS A 1 26  ? -10.134 -29.909 22.242  1.00 33.32 ? 6   LYS A CG  1 
ATOM   41   C CD  . LYS A 1 26  ? -10.424 -29.852 20.757  1.00 35.31 ? 6   LYS A CD  1 
ATOM   42   C CE  . LYS A 1 26  ? -11.763 -29.214 20.470  1.00 38.19 ? 6   LYS A CE  1 
ATOM   43   N NZ  . LYS A 1 26  ? -12.090 -29.255 19.026  1.00 41.96 ? 6   LYS A NZ  1 
ATOM   44   N N   . PRO A 1 27  ? -6.495  -32.510 20.860  1.00 25.65 ? 7   PRO A N   1 
ATOM   45   C CA  . PRO A 1 27  ? -5.133  -33.037 20.841  1.00 25.27 ? 7   PRO A CA  1 
ATOM   46   C C   . PRO A 1 27  ? -4.124  -32.053 21.453  1.00 24.09 ? 7   PRO A C   1 
ATOM   47   O O   . PRO A 1 27  ? -4.353  -30.831 21.458  1.00 23.61 ? 7   PRO A O   1 
ATOM   48   C CB  . PRO A 1 27  ? -4.901  -33.306 19.344  1.00 26.13 ? 7   PRO A CB  1 
ATOM   49   C CG  . PRO A 1 27  ? -5.738  -32.239 18.638  1.00 27.28 ? 7   PRO A CG  1 
ATOM   50   C CD  . PRO A 1 27  ? -6.931  -31.994 19.551  1.00 26.77 ? 7   PRO A CD  1 
ATOM   51   N N   . HIS A 1 28  ? -3.024  -32.604 21.960  1.00 23.76 ? 8   HIS A N   1 
ATOM   52   C CA  . HIS A 1 28  ? -1.894  -31.836 22.539  1.00 21.14 ? 8   HIS A CA  1 
ATOM   53   C C   . HIS A 1 28  ? -0.964  -31.432 21.401  1.00 17.94 ? 8   HIS A C   1 
ATOM   54   O O   . HIS A 1 28  ? -0.585  -32.330 20.589  1.00 14.72 ? 8   HIS A O   1 
ATOM   55   C CB  . HIS A 1 28  ? -1.140  -32.656 23.595  1.00 24.05 ? 8   HIS A CB  1 
ATOM   56   C CG  . HIS A 1 28  ? -1.896  -32.868 24.859  1.00 26.03 ? 8   HIS A CG  1 
ATOM   57   N ND1 . HIS A 1 28  ? -1.670  -32.106 25.996  1.00 28.18 ? 8   HIS A ND1 1 
ATOM   58   C CD2 . HIS A 1 28  ? -2.864  -33.757 25.173  1.00 27.71 ? 8   HIS A CD2 1 
ATOM   59   C CE1 . HIS A 1 28  ? -2.463  -32.536 26.960  1.00 28.98 ? 8   HIS A CE1 1 
ATOM   60   N NE2 . HIS A 1 28  ? -3.201  -33.546 26.476  1.00 28.04 ? 8   HIS A NE2 1 
ATOM   61   N N   . VAL A 1 29  ? -0.642  -30.138 21.337  1.00 15.55 ? 9   VAL A N   1 
ATOM   62   C CA  . VAL A 1 29  ? 0.318   -29.559 20.357  1.00 15.23 ? 9   VAL A CA  1 
ATOM   63   C C   . VAL A 1 29  ? 1.278   -28.643 21.118  1.00 15.52 ? 9   VAL A C   1 
ATOM   64   O O   . VAL A 1 29  ? 0.800   -27.813 21.943  1.00 15.78 ? 9   VAL A O   1 
ATOM   65   C CB  . VAL A 1 29  ? -0.426  -28.795 19.250  1.00 16.43 ? 9   VAL A CB  1 
ATOM   66   C CG1 . VAL A 1 29  ? 0.516   -28.355 18.140  1.00 15.67 ? 9   VAL A CG1 1 
ATOM   67   C CG2 . VAL A 1 29  ? -1.597  -29.592 18.702  1.00 17.26 ? 9   VAL A CG2 1 
ATOM   68   N N   . SER A 1 30  ? 2.576   -28.763 20.876  1.00 15.39 ? 10  SER A N   1 
ATOM   69   C CA  . SER A 1 30  ? 3.578   -27.809 21.412  1.00 15.28 ? 10  SER A CA  1 
ATOM   70   C C   . SER A 1 30  ? 3.962   -26.808 20.315  1.00 14.73 ? 10  SER A C   1 
ATOM   71   O O   . SER A 1 30  ? 3.959   -27.187 19.127  1.00 14.39 ? 10  SER A O   1 
ATOM   72   C CB  . SER A 1 30  ? 4.761   -28.526 21.972  1.00 15.22 ? 10  SER A CB  1 
ATOM   73   O OG  . SER A 1 30  ? 4.378   -29.288 23.115  1.00 16.15 ? 10  SER A OG  1 
ATOM   74   N N   . LEU A 1 31  ? 4.239   -25.565 20.701  1.00 14.24 ? 11  LEU A N   1 
ATOM   75   C CA  . LEU A 1 31  ? 4.735   -24.500 19.780  1.00 13.99 ? 11  LEU A CA  1 
ATOM   76   C C   . LEU A 1 31  ? 6.021   -23.886 20.352  1.00 13.93 ? 11  LEU A C   1 
ATOM   77   O O   . LEU A 1 31  ? 6.003   -23.452 21.499  1.00 13.69 ? 11  LEU A O   1 
ATOM   78   C CB  . LEU A 1 31  ? 3.651   -23.428 19.605  1.00 13.68 ? 11  LEU A CB  1 
ATOM   79   C CG  . LEU A 1 31  ? 4.054   -22.197 18.795  1.00 13.13 ? 11  LEU A CG  1 
ATOM   80   C CD1 . LEU A 1 31  ? 4.409   -22.580 17.373  1.00 13.32 ? 11  LEU A CD1 1 
ATOM   81   C CD2 . LEU A 1 31  ? 2.957   -21.143 18.807  1.00 13.99 ? 11  LEU A CD2 1 
ATOM   82   N N   . ILE A 1 32  ? 7.092   -23.856 19.558  1.00 15.28 ? 12  ILE A N   1 
ATOM   83   C CA  . ILE A 1 32  ? 8.393   -23.221 19.898  1.00 14.85 ? 12  ILE A CA  1 
ATOM   84   C C   . ILE A 1 32  ? 8.508   -21.951 19.050  1.00 14.84 ? 12  ILE A C   1 
ATOM   85   O O   . ILE A 1 32  ? 8.540   -22.070 17.801  1.00 13.34 ? 12  ILE A O   1 
ATOM   86   C CB  . ILE A 1 32  ? 9.549   -24.205 19.652  1.00 17.81 ? 12  ILE A CB  1 
ATOM   87   C CG1 . ILE A 1 32  ? 9.529   -25.350 20.671  1.00 18.26 ? 12  ILE A CG1 1 
ATOM   88   C CG2 . ILE A 1 32  ? 10.897  -23.476 19.612  1.00 17.03 ? 12  ILE A CG2 1 
ATOM   89   C CD1 . ILE A 1 32  ? 10.359  -26.529 20.246  1.00 19.87 ? 12  ILE A CD1 1 
ATOM   90   N N   . GLY A 1 33  ? 8.495   -20.772 19.692  1.00 13.57 ? 13  GLY A N   1 
ATOM   91   C CA  . GLY A 1 33  ? 8.572   -19.476 18.995  1.00 14.00 ? 13  GLY A CA  1 
ATOM   92   C C   . GLY A 1 33  ? 7.294   -18.675 19.119  1.00 14.62 ? 13  GLY A C   1 
ATOM   93   O O   . GLY A 1 33  ? 6.248   -19.140 18.621  1.00 16.28 ? 13  GLY A O   1 
ATOM   94   N N   . LEU A 1 34  ? 7.377   -17.476 19.693  1.00 15.44 ? 14  LEU A N   1 
ATOM   95   C CA  . LEU A 1 34  ? 6.198   -16.591 19.890  1.00 14.64 ? 14  LEU A CA  1 
ATOM   96   C C   . LEU A 1 34  ? 6.541   -15.166 19.438  1.00 14.02 ? 14  LEU A C   1 
ATOM   97   O O   . LEU A 1 34  ? 6.096   -14.254 20.111  1.00 13.64 ? 14  LEU A O   1 
ATOM   98   C CB  . LEU A 1 34  ? 5.726   -16.630 21.353  1.00 14.73 ? 14  LEU A CB  1 
ATOM   99   C CG  . LEU A 1 34  ? 5.144   -17.946 21.879  1.00 14.94 ? 14  LEU A CG  1 
ATOM   100  C CD1 . LEU A 1 34  ? 4.614   -17.764 23.304  1.00 16.12 ? 14  LEU A CD1 1 
ATOM   101  C CD2 . LEU A 1 34  ? 4.031   -18.487 20.987  1.00 13.28 ? 14  LEU A CD2 1 
ATOM   102  N N   . GLY A 1 35  ? 7.218   -15.012 18.291  1.00 13.68 ? 15  GLY A N   1 
ATOM   103  C CA  . GLY A 1 35  ? 7.294   -13.746 17.522  1.00 14.66 ? 15  GLY A CA  1 
ATOM   104  C C   . GLY A 1 35  ? 5.965   -13.451 16.831  1.00 15.31 ? 15  GLY A C   1 
ATOM   105  O O   . GLY A 1 35  ? 4.964   -14.118 17.173  1.00 15.71 ? 15  GLY A O   1 
ATOM   106  N N   . ASN A 1 36  ? 5.936   -12.528 15.864  1.00 15.91 ? 16  ASN A N   1 
ATOM   107  C CA  . ASN A 1 36  ? 4.675   -12.111 15.191  1.00 16.47 ? 16  ASN A CA  1 
ATOM   108  C C   . ASN A 1 36  ? 3.989   -13.310 14.525  1.00 16.00 ? 16  ASN A C   1 
ATOM   109  O O   . ASN A 1 36  ? 2.758   -13.435 14.632  1.00 15.39 ? 16  ASN A O   1 
ATOM   110  C CB  . ASN A 1 36  ? 4.903   -10.945 14.229  1.00 16.94 ? 16  ASN A CB  1 
ATOM   111  C CG  . ASN A 1 36  ? 5.300   -9.691  14.985  1.00 18.09 ? 16  ASN A CG  1 
ATOM   112  O OD1 . ASN A 1 36  ? 6.382   -9.148  14.784  1.00 20.83 ? 16  ASN A OD1 1 
ATOM   113  N ND2 . ASN A 1 36  ? 4.488   -9.299  15.949  1.00 19.65 ? 16  ASN A ND2 1 
ATOM   114  N N   . MET A 1 37  ? 4.744   -14.180 13.863  1.00 15.38 ? 17  MET A N   1 
ATOM   115  C CA  . MET A 1 37  ? 4.139   -15.338 13.167  1.00 15.48 ? 17  MET A CA  1 
ATOM   116  C C   . MET A 1 37  ? 3.853   -16.429 14.209  1.00 16.20 ? 17  MET A C   1 
ATOM   117  O O   . MET A 1 37  ? 2.710   -16.970 14.219  1.00 17.70 ? 17  MET A O   1 
ATOM   118  C CB  . MET A 1 37  ? 5.051   -15.839 12.044  1.00 14.90 ? 17  MET A CB  1 
ATOM   119  C CG  . MET A 1 37  ? 4.422   -16.886 11.156  1.00 14.80 ? 17  MET A CG  1 
ATOM   120  S SD  . MET A 1 37  ? 2.803   -16.402 10.490  1.00 13.92 ? 17  MET A SD  1 
ATOM   121  C CE  . MET A 1 37  ? 3.259   -15.676 8.926   1.00 13.98 ? 17  MET A CE  1 
ATOM   122  N N   . GLY A 1 38  ? 4.800   -16.707 15.108  1.00 16.46 ? 18  GLY A N   1 
ATOM   123  C CA  . GLY A 1 38  ? 4.590   -17.718 16.165  1.00 16.78 ? 18  GLY A CA  1 
ATOM   124  C C   . GLY A 1 38  ? 3.321   -17.437 16.975  1.00 17.76 ? 18  GLY A C   1 
ATOM   125  O O   . GLY A 1 38  ? 2.585   -18.383 17.313  1.00 17.06 ? 18  GLY A O   1 
ATOM   126  N N   . LEU A 1 39  ? 3.078   -16.173 17.336  1.00 18.50 ? 19  LEU A N   1 
ATOM   127  C CA  . LEU A 1 39  ? 1.901   -15.803 18.158  1.00 18.06 ? 19  LEU A CA  1 
ATOM   128  C C   . LEU A 1 39  ? 0.630   -15.953 17.303  1.00 17.09 ? 19  LEU A C   1 
ATOM   129  O O   . LEU A 1 39  ? -0.400  -16.413 17.848  1.00 16.82 ? 19  LEU A O   1 
ATOM   130  C CB  . LEU A 1 39  ? 2.107   -14.379 18.699  1.00 18.93 ? 19  LEU A CB  1 
ATOM   131  C CG  . LEU A 1 39  ? 1.365   -14.059 19.992  1.00 19.65 ? 19  LEU A CG  1 
ATOM   132  C CD1 . LEU A 1 39  ? 1.807   -14.993 21.113  1.00 20.53 ? 19  LEU A CD1 1 
ATOM   133  C CD2 . LEU A 1 39  ? 1.557   -12.588 20.389  1.00 20.53 ? 19  LEU A CD2 1 
ATOM   134  N N   . ALA A 1 40  ? 0.694   -15.621 16.011  1.00 15.56 ? 20  ALA A N   1 
ATOM   135  C CA  . ALA A 1 40  ? -0.396  -15.890 15.041  1.00 15.60 ? 20  ALA A CA  1 
ATOM   136  C C   . ALA A 1 40  ? -0.665  -17.401 14.984  1.00 15.35 ? 20  ALA A C   1 
ATOM   137  O O   . ALA A 1 40  ? -1.864  -17.802 15.008  1.00 15.40 ? 20  ALA A O   1 
ATOM   138  C CB  . ALA A 1 40  ? -0.048  -15.345 13.683  1.00 15.70 ? 20  ALA A CB  1 
ATOM   139  N N   . ILE A 1 41  ? 0.382   -18.226 14.920  1.00 14.38 ? 21  ILE A N   1 
ATOM   140  C CA  . ILE A 1 41  ? 0.191   -19.711 14.893  1.00 15.28 ? 21  ILE A CA  1 
ATOM   141  C C   . ILE A 1 41  ? -0.502  -20.148 16.192  1.00 15.73 ? 21  ILE A C   1 
ATOM   142  O O   . ILE A 1 41  ? -1.460  -20.912 16.113  1.00 15.61 ? 21  ILE A O   1 
ATOM   143  C CB  . ILE A 1 41  ? 1.521   -20.452 14.654  1.00 15.77 ? 21  ILE A CB  1 
ATOM   144  C CG1 . ILE A 1 41  ? 2.095   -20.115 13.274  1.00 16.25 ? 21  ILE A CG1 1 
ATOM   145  C CG2 . ILE A 1 41  ? 1.340   -21.956 14.832  1.00 15.67 ? 21  ILE A CG2 1 
ATOM   146  C CD1 . ILE A 1 41  ? 3.570   -20.368 13.132  1.00 16.80 ? 21  ILE A CD1 1 
ATOM   147  N N   . ALA A 1 42  ? -0.001  -19.703 17.344  1.00 16.45 ? 22  ALA A N   1 
ATOM   148  C CA  . ALA A 1 42  ? -0.571  -20.014 18.671  1.00 16.33 ? 22  ALA A CA  1 
ATOM   149  C C   . ALA A 1 42  ? -2.086  -19.769 18.657  1.00 17.48 ? 22  ALA A C   1 
ATOM   150  O O   . ALA A 1 42  ? -2.842  -20.668 19.056  1.00 14.96 ? 22  ALA A O   1 
ATOM   151  C CB  . ALA A 1 42  ? 0.097   -19.164 19.711  1.00 17.26 ? 22  ALA A CB  1 
ATOM   152  N N   . ASN A 1 43  ? -2.501  -18.566 18.262  1.00 17.84 ? 23  ASN A N   1 
ATOM   153  C CA  . ASN A 1 43  ? -3.928  -18.158 18.254  1.00 19.25 ? 23  ASN A CA  1 
ATOM   154  C C   . ASN A 1 43  ? -4.715  -19.044 17.293  1.00 20.25 ? 23  ASN A C   1 
ATOM   155  O O   . ASN A 1 43  ? -5.837  -19.429 17.648  1.00 22.28 ? 23  ASN A O   1 
ATOM   156  C CB  . ASN A 1 43  ? -4.077  -16.663 17.955  1.00 20.05 ? 23  ASN A CB  1 
ATOM   157  C CG  . ASN A 1 43  ? -3.735  -15.849 19.179  1.00 18.84 ? 23  ASN A CG  1 
ATOM   158  O OD1 . ASN A 1 43  ? -4.417  -15.976 20.190  1.00 20.15 ? 23  ASN A OD1 1 
ATOM   159  N ND2 . ASN A 1 43  ? -2.671  -15.065 19.129  1.00 18.22 ? 23  ASN A ND2 1 
ATOM   160  N N   . CYS A 1 44  ? -4.166  -19.378 16.125  1.00 20.82 ? 24  CYS A N   1 
ATOM   161  C CA  . CYS A 1 44  ? -4.802  -20.351 15.195  1.00 20.19 ? 24  CYS A CA  1 
ATOM   162  C C   . CYS A 1 44  ? -5.004  -21.699 15.899  1.00 19.69 ? 24  CYS A C   1 
ATOM   163  O O   . CYS A 1 44  ? -6.130  -22.234 15.830  1.00 18.33 ? 24  CYS A O   1 
ATOM   164  C CB  . CYS A 1 44  ? -4.024  -20.502 13.893  1.00 20.91 ? 24  CYS A CB  1 
ATOM   165  S SG  . CYS A 1 44  ? -4.117  -19.011 12.861  1.00 20.70 ? 24  CYS A SG  1 
ATOM   166  N N   . LEU A 1 45  ? -3.990  -22.214 16.599  1.00 18.79 ? 25  LEU A N   1 
ATOM   167  C CA  . LEU A 1 45  ? -4.058  -23.561 17.226  1.00 18.91 ? 25  LEU A CA  1 
ATOM   168  C C   . LEU A 1 45  ? -5.018  -23.507 18.426  1.00 20.85 ? 25  LEU A C   1 
ATOM   169  O O   . LEU A 1 45  ? -5.792  -24.459 18.581  1.00 20.65 ? 25  LEU A O   1 
ATOM   170  C CB  . LEU A 1 45  ? -2.653  -24.033 17.634  1.00 18.32 ? 25  LEU A CB  1 
ATOM   171  C CG  . LEU A 1 45  ? -1.652  -24.229 16.483  1.00 18.72 ? 25  LEU A CG  1 
ATOM   172  C CD1 . LEU A 1 45  ? -0.263  -24.566 17.011  1.00 17.47 ? 25  LEU A CD1 1 
ATOM   173  C CD2 . LEU A 1 45  ? -2.110  -25.318 15.521  1.00 18.18 ? 25  LEU A CD2 1 
ATOM   174  N N   . ILE A 1 46  ? -4.983  -22.447 19.250  1.00 20.84 ? 26  ILE A N   1 
ATOM   175  C CA  . ILE A 1 46  ? -5.926  -22.280 20.396  1.00 23.24 ? 26  ILE A CA  1 
ATOM   176  C C   . ILE A 1 46  ? -7.359  -22.185 19.843  1.00 25.71 ? 26  ILE A C   1 
ATOM   177  O O   . ILE A 1 46  ? -8.248  -22.842 20.413  1.00 27.07 ? 26  ILE A O   1 
ATOM   178  C CB  . ILE A 1 46  ? -5.555  -21.064 21.265  1.00 25.41 ? 26  ILE A CB  1 
ATOM   179  C CG1 . ILE A 1 46  ? -4.285  -21.301 22.088  1.00 25.43 ? 26  ILE A CG1 1 
ATOM   180  C CG2 . ILE A 1 46  ? -6.713  -20.632 22.156  1.00 24.46 ? 26  ILE A CG2 1 
ATOM   181  C CD1 . ILE A 1 46  ? -3.589  -20.000 22.464  1.00 25.88 ? 26  ILE A CD1 1 
ATOM   182  N N   . LYS A 1 47  ? -7.571  -21.426 18.763  1.00 26.96 ? 27  LYS A N   1 
ATOM   183  C CA  . LYS A 1 47  ? -8.909  -21.194 18.151  1.00 30.01 ? 27  LYS A CA  1 
ATOM   184  C C   . LYS A 1 47  ? -9.467  -22.516 17.599  1.00 30.27 ? 27  LYS A C   1 
ATOM   185  O O   . LYS A 1 47  ? -10.694 -22.687 17.613  1.00 29.69 ? 27  LYS A O   1 
ATOM   186  C CB  . LYS A 1 47  ? -8.824  -20.107 17.075  1.00 31.55 ? 27  LYS A CB  1 
ATOM   187  C CG  . LYS A 1 47  ? -10.165 -19.698 16.488  1.00 35.92 ? 27  LYS A CG  1 
ATOM   188  C CD  . LYS A 1 47  ? -10.094 -18.532 15.510  1.00 37.68 ? 27  LYS A CD  1 
ATOM   189  C CE  . LYS A 1 47  ? -11.397 -18.317 14.767  1.00 38.10 ? 27  LYS A CE  1 
ATOM   190  N NZ  . LYS A 1 47  ? -11.851 -19.564 14.110  1.00 40.23 ? 27  LYS A NZ  1 
ATOM   191  N N   . SER A 1 48  ? -8.604  -23.424 17.136  1.00 28.48 ? 28  SER A N   1 
ATOM   192  C CA  . SER A 1 48  ? -8.993  -24.764 16.632  1.00 27.32 ? 28  SER A CA  1 
ATOM   193  C C   . SER A 1 48  ? -9.225  -25.753 17.780  1.00 26.45 ? 28  SER A C   1 
ATOM   194  O O   . SER A 1 48  ? -9.520  -26.914 17.477  1.00 26.10 ? 28  SER A O   1 
ATOM   195  C CB  . SER A 1 48  ? -7.976  -25.289 15.679  1.00 29.28 ? 28  SER A CB  1 
ATOM   196  O OG  . SER A 1 48  ? -8.017  -24.534 14.484  1.00 34.97 ? 28  SER A OG  1 
ATOM   197  N N   . GLY A 1 49  ? -9.043  -25.339 19.036  1.00 24.66 ? 29  GLY A N   1 
ATOM   198  C CA  . GLY A 1 49  ? -9.358  -26.165 20.213  1.00 26.14 ? 29  GLY A CA  1 
ATOM   199  C C   . GLY A 1 49  ? -8.183  -26.969 20.764  1.00 25.78 ? 29  GLY A C   1 
ATOM   200  O O   . GLY A 1 49  ? -8.381  -27.615 21.797  1.00 26.12 ? 29  GLY A O   1 
ATOM   201  N N   . CYS A 1 50  ? -6.999  -26.945 20.144  1.00 25.35 ? 30  CYS A N   1 
ATOM   202  C CA  . CYS A 1 50  ? -5.797  -27.696 20.623  1.00 23.53 ? 30  CYS A CA  1 
ATOM   203  C C   . CYS A 1 50  ? -5.504  -27.397 22.107  1.00 20.66 ? 30  CYS A C   1 
ATOM   204  O O   . CYS A 1 50  ? -5.662  -26.240 22.506  1.00 18.91 ? 30  CYS A O   1 
ATOM   205  C CB  . CYS A 1 50  ? -4.578  -27.336 19.779  1.00 25.15 ? 30  CYS A CB  1 
ATOM   206  S SG  . CYS A 1 50  ? -4.870  -27.640 18.017  1.00 29.80 ? 30  CYS A SG  1 
ATOM   207  N N   . LYS A 1 51  ? -5.041  -28.393 22.870  1.00 18.84 ? 31  LYS A N   1 
ATOM   208  C CA  . LYS A 1 51  ? -4.316  -28.220 24.165  1.00 19.55 ? 31  LYS A CA  1 
ATOM   209  C C   . LYS A 1 51  ? -2.879  -27.786 23.870  1.00 17.53 ? 31  LYS A C   1 
ATOM   210  O O   . LYS A 1 51  ? -2.066  -28.644 23.483  1.00 17.18 ? 31  LYS A O   1 
ATOM   211  C CB  . LYS A 1 51  ? -4.369  -29.501 25.002  1.00 21.40 ? 31  LYS A CB  1 
ATOM   212  C CG  . LYS A 1 51  ? -5.775  -29.861 25.474  1.00 24.63 ? 31  LYS A CG  1 
ATOM   213  C CD  . LYS A 1 51  ? -5.886  -31.175 26.237  1.00 26.70 ? 31  LYS A CD  1 
ATOM   214  C CE  . LYS A 1 51  ? -7.332  -31.634 26.377  1.00 29.07 ? 31  LYS A CE  1 
ATOM   215  N NZ  . LYS A 1 51  ? -7.440  -32.998 26.952  1.00 29.57 ? 31  LYS A NZ  1 
ATOM   216  N N   . LEU A 1 52  ? -2.595  -26.484 23.994  1.00 16.70 ? 32  LEU A N   1 
ATOM   217  C CA  . LEU A 1 52  ? -1.346  -25.887 23.458  1.00 14.96 ? 32  LEU A CA  1 
ATOM   218  C C   . LEU A 1 52  ? -0.342  -25.667 24.589  1.00 15.29 ? 32  LEU A C   1 
ATOM   219  O O   . LEU A 1 52  ? -0.733  -25.074 25.640  1.00 15.21 ? 32  LEU A O   1 
ATOM   220  C CB  . LEU A 1 52  ? -1.651  -24.573 22.753  1.00 14.73 ? 32  LEU A CB  1 
ATOM   221  C CG  . LEU A 1 52  ? -0.411  -23.896 22.162  1.00 13.78 ? 32  LEU A CG  1 
ATOM   222  C CD1 . LEU A 1 52  ? 0.075   -24.665 20.956  1.00 13.46 ? 32  LEU A CD1 1 
ATOM   223  C CD2 . LEU A 1 52  ? -0.676  -22.449 21.797  1.00 13.51 ? 32  LEU A CD2 1 
ATOM   224  N N   . THR A 1 53  ? 0.870   -26.191 24.408  1.00 13.33 ? 33  THR A N   1 
ATOM   225  C CA  . THR A 1 53  ? 2.039   -25.893 25.269  1.00 14.38 ? 33  THR A CA  1 
ATOM   226  C C   . THR A 1 53  ? 2.989   -25.021 24.464  1.00 14.13 ? 33  THR A C   1 
ATOM   227  O O   . THR A 1 53  ? 3.293   -25.428 23.367  1.00 15.51 ? 33  THR A O   1 
ATOM   228  C CB  . THR A 1 53  ? 2.728   -27.157 25.793  1.00 13.50 ? 33  THR A CB  1 
ATOM   229  O OG1 . THR A 1 53  ? 1.734   -27.921 26.476  1.00 14.16 ? 33  THR A OG1 1 
ATOM   230  C CG2 . THR A 1 53  ? 3.848   -26.863 26.762  1.00 13.27 ? 33  THR A CG2 1 
ATOM   231  N N   . VAL A 1 54  ? 3.435   -23.882 25.005  1.00 13.90 ? 34  VAL A N   1 
ATOM   232  C CA  . VAL A 1 54  ? 4.334   -22.953 24.263  1.00 13.48 ? 34  VAL A CA  1 
ATOM   233  C C   . VAL A 1 54  ? 5.674   -22.821 24.996  1.00 15.28 ? 34  VAL A C   1 
ATOM   234  O O   . VAL A 1 54  ? 5.750   -23.043 26.238  1.00 15.42 ? 34  VAL A O   1 
ATOM   235  C CB  . VAL A 1 54  ? 3.628   -21.612 23.989  1.00 12.51 ? 34  VAL A CB  1 
ATOM   236  C CG1 . VAL A 1 54  ? 2.250   -21.840 23.368  1.00 11.96 ? 34  VAL A CG1 1 
ATOM   237  C CG2 . VAL A 1 54  ? 3.509   -20.748 25.220  1.00 12.53 ? 34  VAL A CG2 1 
ATOM   238  N N   . TRP A 1 55  ? 6.717   -22.514 24.230  1.00 15.62 ? 35  TRP A N   1 
ATOM   239  C CA  . TRP A 1 55  ? 7.995   -21.982 24.750  1.00 16.51 ? 35  TRP A CA  1 
ATOM   240  C C   . TRP A 1 55  ? 8.427   -20.814 23.869  1.00 16.61 ? 35  TRP A C   1 
ATOM   241  O O   . TRP A 1 55  ? 8.145   -20.833 22.671  1.00 15.82 ? 35  TRP A O   1 
ATOM   242  C CB  . TRP A 1 55  ? 9.070   -23.063 24.859  1.00 16.64 ? 35  TRP A CB  1 
ATOM   243  C CG  . TRP A 1 55  ? 10.345  -22.542 25.436  1.00 17.41 ? 35  TRP A CG  1 
ATOM   244  C CD1 . TRP A 1 55  ? 10.687  -22.461 26.755  1.00 18.11 ? 35  TRP A CD1 1 
ATOM   245  C CD2 . TRP A 1 55  ? 11.420  -21.937 24.700  1.00 17.39 ? 35  TRP A CD2 1 
ATOM   246  N NE1 . TRP A 1 55  ? 11.920  -21.893 26.888  1.00 17.92 ? 35  TRP A NE1 1 
ATOM   247  C CE2 . TRP A 1 55  ? 12.394  -21.559 25.641  1.00 17.85 ? 35  TRP A CE2 1 
ATOM   248  C CE3 . TRP A 1 55  ? 11.669  -21.732 23.338  1.00 17.32 ? 35  TRP A CE3 1 
ATOM   249  C CZ2 . TRP A 1 55  ? 13.593  -20.951 25.259  1.00 18.25 ? 35  TRP A CZ2 1 
ATOM   250  C CZ3 . TRP A 1 55  ? 12.844  -21.121 22.963  1.00 17.67 ? 35  TRP A CZ3 1 
ATOM   251  C CH2 . TRP A 1 55  ? 13.804  -20.759 23.912  1.00 18.37 ? 35  TRP A CH2 1 
ATOM   252  N N   . ASN A 1 56  ? 9.070   -19.827 24.476  1.00 17.47 ? 36  ASN A N   1 
ATOM   253  C CA  . ASN A 1 56  ? 9.742   -18.707 23.768  1.00 18.10 ? 36  ASN A CA  1 
ATOM   254  C C   . ASN A 1 56  ? 10.914  -18.235 24.638  1.00 19.21 ? 36  ASN A C   1 
ATOM   255  O O   . ASN A 1 56  ? 10.767  -18.242 25.876  1.00 18.75 ? 36  ASN A O   1 
ATOM   256  C CB  . ASN A 1 56  ? 8.749   -17.580 23.496  1.00 17.52 ? 36  ASN A CB  1 
ATOM   257  C CG  . ASN A 1 56  ? 9.278   -16.569 22.506  1.00 18.10 ? 36  ASN A CG  1 
ATOM   258  O OD1 . ASN A 1 56  ? 9.610   -16.934 21.374  1.00 18.12 ? 36  ASN A OD1 1 
ATOM   259  N ND2 . ASN A 1 56  ? 9.315   -15.303 22.912  1.00 16.72 ? 36  ASN A ND2 1 
ATOM   260  N N   . ARG A 1 57  ? 12.035  -17.839 24.029  1.00 20.49 ? 37  ARG A N   1 
ATOM   261  C CA  . ARG A 1 57  ? 13.183  -17.241 24.768  1.00 19.41 ? 37  ARG A CA  1 
ATOM   262  C C   . ARG A 1 57  ? 12.641  -16.165 25.717  1.00 18.12 ? 37  ARG A C   1 
ATOM   263  O O   . ARG A 1 57  ? 12.916  -16.217 26.929  1.00 18.48 ? 37  ARG A O   1 
ATOM   264  C CB  . ARG A 1 57  ? 14.204  -16.695 23.767  1.00 19.70 ? 37  ARG A CB  1 
ATOM   265  C CG  . ARG A 1 57  ? 15.356  -15.924 24.395  1.00 19.51 ? 37  ARG A CG  1 
ATOM   266  C CD  . ARG A 1 57  ? 16.311  -15.441 23.320  1.00 20.01 ? 37  ARG A CD  1 
ATOM   267  N NE  . ARG A 1 57  ? 15.670  -14.430 22.486  1.00 21.29 ? 37  ARG A NE  1 
ATOM   268  C CZ  . ARG A 1 57  ? 16.284  -13.648 21.606  1.00 21.04 ? 37  ARG A CZ  1 
ATOM   269  N NH1 . ARG A 1 57  ? 15.589  -12.758 20.918  1.00 21.95 ? 37  ARG A NH1 1 
ATOM   270  N NH2 . ARG A 1 57  ? 17.580  -13.757 21.403  1.00 20.52 ? 37  ARG A NH2 1 
ATOM   271  N N   . SER A 1 58  ? 11.869  -15.226 25.184  1.00 18.05 ? 38  SER A N   1 
ATOM   272  C CA  . SER A 1 58  ? 11.192  -14.173 25.985  1.00 17.86 ? 38  SER A CA  1 
ATOM   273  C C   . SER A 1 58  ? 9.850   -14.733 26.460  1.00 18.21 ? 38  SER A C   1 
ATOM   274  O O   . SER A 1 58  ? 8.883   -14.659 25.698  1.00 18.17 ? 38  SER A O   1 
ATOM   275  C CB  . SER A 1 58  ? 11.040  -12.899 25.197  1.00 17.20 ? 38  SER A CB  1 
ATOM   276  O OG  . SER A 1 58  ? 12.253  -12.587 24.553  1.00 17.62 ? 38  SER A OG  1 
ATOM   277  N N   . ALA A 1 59  ? 9.818   -15.332 27.658  1.00 20.32 ? 39  ALA A N   1 
ATOM   278  C CA  . ALA A 1 59  ? 8.697   -16.197 28.108  1.00 20.16 ? 39  ALA A CA  1 
ATOM   279  C C   . ALA A 1 59  ? 7.397   -15.380 28.151  1.00 19.89 ? 39  ALA A C   1 
ATOM   280  O O   . ALA A 1 59  ? 6.356   -15.965 27.870  1.00 16.75 ? 39  ALA A O   1 
ATOM   281  C CB  . ALA A 1 59  ? 9.018   -16.847 29.434  1.00 20.66 ? 39  ALA A CB  1 
ATOM   282  N N   . GLU A 1 60  ? 7.485   -14.069 28.443  1.00 21.57 ? 40  GLU A N   1 
ATOM   283  C CA  . GLU A 1 60  ? 6.336   -13.160 28.707  1.00 21.95 ? 40  GLU A CA  1 
ATOM   284  C C   . GLU A 1 60  ? 5.506   -12.913 27.444  1.00 21.16 ? 40  GLU A C   1 
ATOM   285  O O   . GLU A 1 60  ? 4.351   -12.493 27.600  1.00 21.96 ? 40  GLU A O   1 
ATOM   286  C CB  . GLU A 1 60  ? 6.794   -11.825 29.316  1.00 25.67 ? 40  GLU A CB  1 
ATOM   287  C CG  . GLU A 1 60  ? 7.504   -10.866 28.356  1.00 24.31 ? 40  GLU A CG  1 
ATOM   288  C CD  . GLU A 1 60  ? 8.977   -11.168 28.106  1.00 25.37 ? 40  GLU A CD  1 
ATOM   289  O OE1 . GLU A 1 60  ? 9.615   -10.392 27.389  1.00 29.21 ? 40  GLU A OE1 1 
ATOM   290  O OE2 . GLU A 1 60  ? 9.486   -12.173 28.616  1.00 23.77 ? 40  GLU A OE2 1 
ATOM   291  N N   . LYS A 1 61  ? 6.012   -13.205 26.248  1.00 21.27 ? 41  LYS A N   1 
ATOM   292  C CA  . LYS A 1 61  ? 5.193   -13.116 25.003  1.00 21.39 ? 41  LYS A CA  1 
ATOM   293  C C   . LYS A 1 61  ? 4.079   -14.183 25.021  1.00 20.91 ? 41  LYS A C   1 
ATOM   294  O O   . LYS A 1 61  ? 3.211   -14.119 24.159  1.00 19.86 ? 41  LYS A O   1 
ATOM   295  C CB  . LYS A 1 61  ? 6.080   -13.252 23.761  1.00 22.14 ? 41  LYS A CB  1 
ATOM   296  C CG  . LYS A 1 61  ? 7.013   -12.072 23.516  1.00 24.67 ? 41  LYS A CG  1 
ATOM   297  C CD  . LYS A 1 61  ? 7.653   -12.093 22.158  1.00 25.85 ? 41  LYS A CD  1 
ATOM   298  C CE  . LYS A 1 61  ? 8.738   -11.050 21.986  1.00 28.28 ? 41  LYS A CE  1 
ATOM   299  N NZ  . LYS A 1 61  ? 8.919   -10.743 20.550  1.00 29.49 ? 41  LYS A NZ  1 
ATOM   300  N N   . ALA A 1 62  ? 4.114   -15.156 25.941  1.00 20.36 ? 42  ALA A N   1 
ATOM   301  C CA  . ALA A 1 62  ? 3.023   -16.143 26.115  1.00 20.06 ? 42  ALA A CA  1 
ATOM   302  C C   . ALA A 1 62  ? 1.834   -15.527 26.870  1.00 19.23 ? 42  ALA A C   1 
ATOM   303  O O   . ALA A 1 62  ? 0.794   -16.212 26.919  1.00 18.43 ? 42  ALA A O   1 
ATOM   304  C CB  . ALA A 1 62  ? 3.522   -17.371 26.836  1.00 18.85 ? 42  ALA A CB  1 
ATOM   305  N N   . ALA A 1 63  ? 1.993   -14.334 27.474  1.00 18.48 ? 43  ALA A N   1 
ATOM   306  C CA  . ALA A 1 63  ? 1.062   -13.747 28.473  1.00 19.27 ? 43  ALA A CA  1 
ATOM   307  C C   . ALA A 1 63  ? -0.368  -13.687 27.904  1.00 18.57 ? 43  ALA A C   1 
ATOM   308  O O   . ALA A 1 63  ? -1.272  -14.125 28.626  1.00 19.49 ? 43  ALA A O   1 
ATOM   309  C CB  . ALA A 1 63  ? 1.544   -12.395 28.973  1.00 19.52 ? 43  ALA A CB  1 
ATOM   310  N N   . SER A 1 64  ? -0.551  -13.287 26.641  1.00 19.23 ? 44  SER A N   1 
ATOM   311  C CA  . SER A 1 64  ? -1.868  -13.174 25.945  1.00 19.78 ? 44  SER A CA  1 
ATOM   312  C C   . SER A 1 64  ? -2.499  -14.551 25.659  1.00 20.37 ? 44  SER A C   1 
ATOM   313  O O   . SER A 1 64  ? -3.666  -14.567 25.268  1.00 22.78 ? 44  SER A O   1 
ATOM   314  C CB  . SER A 1 64  ? -1.763  -12.385 24.641  1.00 20.54 ? 44  SER A CB  1 
ATOM   315  O OG  . SER A 1 64  ? -1.068  -13.114 23.612  1.00 21.38 ? 44  SER A OG  1 
ATOM   316  N N   . LEU A 1 65  ? -1.748  -15.653 25.744  1.00 19.60 ? 45  LEU A N   1 
ATOM   317  C CA  . LEU A 1 65  ? -2.262  -17.010 25.403  1.00 19.37 ? 45  LEU A CA  1 
ATOM   318  C C   . LEU A 1 65  ? -2.764  -17.711 26.671  1.00 20.07 ? 45  LEU A C   1 
ATOM   319  O O   . LEU A 1 65  ? -3.541  -18.669 26.574  1.00 19.02 ? 45  LEU A O   1 
ATOM   320  C CB  . LEU A 1 65  ? -1.125  -17.811 24.760  1.00 18.91 ? 45  LEU A CB  1 
ATOM   321  C CG  . LEU A 1 65  ? -0.400  -17.100 23.630  1.00 18.43 ? 45  LEU A CG  1 
ATOM   322  C CD1 . LEU A 1 65  ? 0.866   -17.835 23.259  1.00 18.80 ? 45  LEU A CD1 1 
ATOM   323  C CD2 . LEU A 1 65  ? -1.325  -16.940 22.437  1.00 20.01 ? 45  LEU A CD2 1 
ATOM   324  N N   . VAL A 1 66  ? -2.251  -17.302 27.824  1.00 20.61 ? 46  VAL A N   1 
ATOM   325  C CA  . VAL A 1 66  ? -2.506  -17.980 29.120  1.00 21.72 ? 46  VAL A CA  1 
ATOM   326  C C   . VAL A 1 66  ? -3.994  -17.873 29.448  1.00 23.33 ? 46  VAL A C   1 
ATOM   327  O O   . VAL A 1 66  ? -4.594  -18.895 29.773  1.00 22.38 ? 46  VAL A O   1 
ATOM   328  C CB  . VAL A 1 66  ? -1.588  -17.429 30.223  1.00 20.97 ? 46  VAL A CB  1 
ATOM   329  C CG1 . VAL A 1 66  ? -1.972  -17.940 31.608  1.00 21.44 ? 46  VAL A CG1 1 
ATOM   330  C CG2 . VAL A 1 66  ? -0.134  -17.749 29.910  1.00 21.49 ? 46  VAL A CG2 1 
ATOM   331  N N   . PRO A 1 67  ? -4.645  -16.682 29.378  1.00 24.21 ? 47  PRO A N   1 
ATOM   332  C CA  . PRO A 1 67  ? -6.086  -16.605 29.603  1.00 25.98 ? 47  PRO A CA  1 
ATOM   333  C C   . PRO A 1 67  ? -6.904  -17.344 28.532  1.00 27.57 ? 47  PRO A C   1 
ATOM   334  O O   . PRO A 1 67  ? -8.111  -17.470 28.719  1.00 27.80 ? 47  PRO A O   1 
ATOM   335  C CB  . PRO A 1 67  ? -6.428  -15.100 29.634  1.00 26.29 ? 47  PRO A CB  1 
ATOM   336  C CG  . PRO A 1 67  ? -5.199  -14.387 29.099  1.00 26.47 ? 47  PRO A CG  1 
ATOM   337  C CD  . PRO A 1 67  ? -4.034  -15.356 29.220  1.00 25.60 ? 47  PRO A CD  1 
ATOM   338  N N   . GLN A 1 68  ? -6.269  -17.795 27.437  1.00 25.54 ? 48  GLN A N   1 
ATOM   339  C CA  . GLN A 1 68  ? -6.940  -18.624 26.395  1.00 22.06 ? 48  GLN A CA  1 
ATOM   340  C C   . GLN A 1 68  ? -6.741  -20.124 26.681  1.00 19.79 ? 48  GLN A C   1 
ATOM   341  O O   . GLN A 1 68  ? -7.336  -20.933 25.959  1.00 20.60 ? 48  GLN A O   1 
ATOM   342  C CB  . GLN A 1 68  ? -6.435  -18.261 25.001  1.00 23.59 ? 48  GLN A CB  1 
ATOM   343  C CG  . GLN A 1 68  ? -6.363  -16.759 24.734  1.00 24.59 ? 48  GLN A CG  1 
ATOM   344  C CD  . GLN A 1 68  ? -6.078  -16.481 23.276  1.00 24.70 ? 48  GLN A CD  1 
ATOM   345  O OE1 . GLN A 1 68  ? -6.855  -16.841 22.391  1.00 22.77 ? 48  GLN A OE1 1 
ATOM   346  N NE2 . GLN A 1 68  ? -4.942  -15.848 23.018  1.00 24.23 ? 48  GLN A NE2 1 
ATOM   347  N N   . GLY A 1 69  ? -5.956  -20.507 27.694  1.00 18.67 ? 49  GLY A N   1 
ATOM   348  C CA  . GLY A 1 69  ? -5.818  -21.924 28.100  1.00 17.98 ? 49  GLY A CA  1 
ATOM   349  C C   . GLY A 1 69  ? -4.458  -22.523 27.718  1.00 16.84 ? 49  GLY A C   1 
ATOM   350  O O   . GLY A 1 69  ? -4.263  -23.726 27.899  1.00 15.44 ? 49  GLY A O   1 
ATOM   351  N N   . ALA A 1 70  ? -3.536  -21.721 27.212  1.00 16.94 ? 50  ALA A N   1 
ATOM   352  C CA  . ALA A 1 70  ? -2.170  -22.164 26.856  1.00 16.87 ? 50  ALA A CA  1 
ATOM   353  C C   . ALA A 1 70  ? -1.361  -22.398 28.136  1.00 17.35 ? 50  ALA A C   1 
ATOM   354  O O   . ALA A 1 70  ? -1.517  -21.628 29.112  1.00 15.99 ? 50  ALA A O   1 
ATOM   355  C CB  . ALA A 1 70  ? -1.525  -21.143 25.967  1.00 17.69 ? 50  ALA A CB  1 
ATOM   356  N N   . THR A 1 71  ? -0.568  -23.470 28.135  1.00 16.97 ? 51  THR A N   1 
ATOM   357  C CA  . THR A 1 71  ? 0.440   -23.804 29.169  1.00 17.49 ? 51  THR A CA  1 
ATOM   358  C C   . THR A 1 71  ? 1.798   -23.283 28.692  1.00 17.51 ? 51  THR A C   1 
ATOM   359  O O   . THR A 1 71  ? 2.141   -23.500 27.508  1.00 16.04 ? 51  THR A O   1 
ATOM   360  C CB  . THR A 1 71  ? 0.553   -25.320 29.358  1.00 17.32 ? 51  THR A CB  1 
ATOM   361  O OG1 . THR A 1 71  ? -0.740  -25.741 29.745  1.00 16.50 ? 51  THR A OG1 1 
ATOM   362  C CG2 . THR A 1 71  ? 1.585   -25.764 30.367  1.00 18.05 ? 51  THR A CG2 1 
ATOM   363  N N   . VAL A 1 72  ? 2.561   -22.679 29.588  1.00 16.76 ? 52  VAL A N   1 
ATOM   364  C CA  . VAL A 1 72  ? 3.923   -22.167 29.284  1.00 17.00 ? 52  VAL A CA  1 
ATOM   365  C C   . VAL A 1 72  ? 4.910   -23.160 29.897  1.00 17.29 ? 52  VAL A C   1 
ATOM   366  O O   . VAL A 1 72  ? 4.819   -23.393 31.106  1.00 17.47 ? 52  VAL A O   1 
ATOM   367  C CB  . VAL A 1 72  ? 4.121   -20.739 29.823  1.00 16.79 ? 52  VAL A CB  1 
ATOM   368  C CG1 . VAL A 1 72  ? 5.422   -20.125 29.320  1.00 16.55 ? 52  VAL A CG1 1 
ATOM   369  C CG2 . VAL A 1 72  ? 2.935   -19.862 29.467  1.00 16.44 ? 52  VAL A CG2 1 
ATOM   370  N N   . ALA A 1 73  ? 5.768   -23.753 29.067  1.00 18.62 ? 53  ALA A N   1 
ATOM   371  C CA  . ALA A 1 73  ? 6.856   -24.672 29.468  1.00 18.50 ? 53  ALA A CA  1 
ATOM   372  C C   . ALA A 1 73  ? 8.103   -23.834 29.766  1.00 18.60 ? 53  ALA A C   1 
ATOM   373  O O   . ALA A 1 73  ? 8.311   -22.767 29.111  1.00 18.36 ? 53  ALA A O   1 
ATOM   374  C CB  . ALA A 1 73  ? 7.089   -25.688 28.371  1.00 18.87 ? 53  ALA A CB  1 
ATOM   375  N N   . ALA A 1 74  ? 8.875   -24.248 30.765  1.00 20.32 ? 54  ALA A N   1 
ATOM   376  C CA  . ALA A 1 74  ? 10.085  -23.541 31.249  1.00 20.89 ? 54  ALA A CA  1 
ATOM   377  C C   . ALA A 1 74  ? 11.155  -23.570 30.158  1.00 19.17 ? 54  ALA A C   1 
ATOM   378  O O   . ALA A 1 74  ? 11.815  -22.533 29.915  1.00 18.49 ? 54  ALA A O   1 
ATOM   379  C CB  . ALA A 1 74  ? 10.584  -24.175 32.529  1.00 21.82 ? 54  ALA A CB  1 
ATOM   380  N N   . THR A 1 75  ? 11.296  -24.724 29.507  1.00 19.20 ? 55  THR A N   1 
ATOM   381  C CA  . THR A 1 75  ? 12.409  -25.054 28.583  1.00 19.08 ? 55  THR A CA  1 
ATOM   382  C C   . THR A 1 75  ? 11.863  -25.649 27.285  1.00 18.04 ? 55  THR A C   1 
ATOM   383  O O   . THR A 1 75  ? 10.719  -26.112 27.223  1.00 17.21 ? 55  THR A O   1 
ATOM   384  C CB  . THR A 1 75  ? 13.404  -26.004 29.266  1.00 21.16 ? 55  THR A CB  1 
ATOM   385  O OG1 . THR A 1 75  ? 12.826  -27.311 29.335  1.00 21.56 ? 55  THR A OG1 1 
ATOM   386  C CG2 . THR A 1 75  ? 13.810  -25.553 30.657  1.00 22.39 ? 55  THR A CG2 1 
ATOM   387  N N   . PRO A 1 76  ? 12.653  -25.614 26.190  1.00 17.57 ? 56  PRO A N   1 
ATOM   388  C CA  . PRO A 1 76  ? 12.314  -26.336 24.967  1.00 18.52 ? 56  PRO A CA  1 
ATOM   389  C C   . PRO A 1 76  ? 12.075  -27.831 25.221  1.00 17.79 ? 56  PRO A C   1 
ATOM   390  O O   . PRO A 1 76  ? 11.121  -28.342 24.707  1.00 16.18 ? 56  PRO A O   1 
ATOM   391  C CB  . PRO A 1 76  ? 13.552  -26.126 24.075  1.00 18.49 ? 56  PRO A CB  1 
ATOM   392  C CG  . PRO A 1 76  ? 14.119  -24.795 24.549  1.00 17.83 ? 56  PRO A CG  1 
ATOM   393  C CD  . PRO A 1 76  ? 13.873  -24.808 26.037  1.00 18.43 ? 56  PRO A CD  1 
ATOM   394  N N   . ALA A 1 77  ? 12.945  -28.476 26.006  1.00 18.07 ? 57  ALA A N   1 
ATOM   395  C CA  . ALA A 1 77  ? 12.829  -29.910 26.368  1.00 19.32 ? 57  ALA A CA  1 
ATOM   396  C C   . ALA A 1 77  ? 11.473  -30.170 27.022  1.00 19.18 ? 57  ALA A C   1 
ATOM   397  O O   . ALA A 1 77  ? 10.861  -31.204 26.718  1.00 17.84 ? 57  ALA A O   1 
ATOM   398  C CB  . ALA A 1 77  ? 13.948  -30.350 27.293  1.00 20.56 ? 57  ALA A CB  1 
ATOM   399  N N   . GLU A 1 78  ? 11.056  -29.299 27.940  1.00 20.14 ? 58  GLU A N   1 
ATOM   400  C CA  . GLU A 1 78  ? 9.775   -29.476 28.677  1.00 21.81 ? 58  GLU A CA  1 
ATOM   401  C C   . GLU A 1 78  ? 8.646   -29.294 27.671  1.00 18.34 ? 58  GLU A C   1 
ATOM   402  O O   . GLU A 1 78  ? 7.652   -30.027 27.730  1.00 17.25 ? 58  GLU A O   1 
ATOM   403  C CB  . GLU A 1 78  ? 9.629   -28.499 29.848  1.00 25.75 ? 58  GLU A CB  1 
ATOM   404  C CG  . GLU A 1 78  ? 10.294  -28.958 31.135  1.00 31.32 ? 58  GLU A CG  1 
ATOM   405  C CD  . GLU A 1 78  ? 10.074  -28.002 32.302  1.00 37.58 ? 58  GLU A CD  1 
ATOM   406  O OE1 . GLU A 1 78  ? 8.982   -27.367 32.349  1.00 43.11 ? 58  GLU A OE1 1 
ATOM   407  O OE2 . GLU A 1 78  ? 10.996  -27.868 33.140  1.00 40.46 ? 58  GLU A OE2 1 
ATOM   408  N N   . CYS A 1 79  ? 8.807   -28.314 26.789  1.00 17.14 ? 59  CYS A N   1 
ATOM   409  C CA  . CYS A 1 79  ? 7.820   -27.996 25.748  1.00 16.13 ? 59  CYS A CA  1 
ATOM   410  C C   . CYS A 1 79  ? 7.636   -29.244 24.894  1.00 15.40 ? 59  CYS A C   1 
ATOM   411  O O   . CYS A 1 79  ? 6.483   -29.708 24.740  1.00 15.58 ? 59  CYS A O   1 
ATOM   412  C CB  . CYS A 1 79  ? 8.237   -26.782 24.931  1.00 17.04 ? 59  CYS A CB  1 
ATOM   413  S SG  . CYS A 1 79  ? 6.866   -26.250 23.897  1.00 17.67 ? 59  CYS A SG  1 
ATOM   414  N N   . VAL A 1 80  ? 8.730   -29.842 24.451  1.00 14.35 ? 60  VAL A N   1 
ATOM   415  C CA  . VAL A 1 80  ? 8.678   -31.027 23.541  1.00 15.39 ? 60  VAL A CA  1 
ATOM   416  C C   . VAL A 1 80  ? 8.073   -32.237 24.267  1.00 16.27 ? 60  VAL A C   1 
ATOM   417  O O   . VAL A 1 80  ? 7.372   -33.051 23.599  1.00 16.57 ? 60  VAL A O   1 
ATOM   418  C CB  . VAL A 1 80  ? 10.067  -31.361 22.969  1.00 16.21 ? 60  VAL A CB  1 
ATOM   419  C CG1 . VAL A 1 80  ? 10.092  -32.761 22.397  1.00 16.64 ? 60  VAL A CG1 1 
ATOM   420  C CG2 . VAL A 1 80  ? 10.474  -30.325 21.925  1.00 17.09 ? 60  VAL A CG2 1 
ATOM   421  N N   . ALA A 1 81  ? 8.313   -32.374 25.571  1.00 16.95 ? 61  ALA A N   1 
ATOM   422  C CA  . ALA A 1 81  ? 7.776   -33.497 26.378  1.00 18.24 ? 61  ALA A CA  1 
ATOM   423  C C   . ALA A 1 81  ? 6.240   -33.434 26.460  1.00 18.73 ? 61  ALA A C   1 
ATOM   424  O O   . ALA A 1 81  ? 5.667   -34.478 26.738  1.00 19.62 ? 61  ALA A O   1 
ATOM   425  C CB  . ALA A 1 81  ? 8.375   -33.491 27.767  1.00 18.40 ? 61  ALA A CB  1 
ATOM   426  N N   . SER A 1 82  ? 5.614   -32.263 26.262  1.00 18.71 ? 62  SER A N   1 
ATOM   427  C CA  . SER A 1 82  ? 4.173   -31.990 26.549  1.00 18.54 ? 62  SER A CA  1 
ATOM   428  C C   . SER A 1 82  ? 3.224   -32.462 25.447  1.00 18.52 ? 62  SER A C   1 
ATOM   429  O O   . SER A 1 82  ? 1.986   -32.508 25.727  1.00 18.20 ? 62  SER A O   1 
ATOM   430  C CB  . SER A 1 82  ? 3.948   -30.530 26.779  1.00 19.90 ? 62  SER A CB  1 
ATOM   431  O OG  . SER A 1 82  ? 4.557   -30.150 27.988  1.00 20.37 ? 62  SER A OG  1 
ATOM   432  N N   . SER A 1 83  ? 3.736   -32.721 24.236  1.00 17.36 ? 63  SER A N   1 
ATOM   433  C CA  . SER A 1 83  ? 2.905   -32.986 23.035  1.00 17.74 ? 63  SER A CA  1 
ATOM   434  C C   . SER A 1 83  ? 3.604   -33.969 22.112  1.00 17.47 ? 63  SER A C   1 
ATOM   435  O O   . SER A 1 83  ? 4.829   -33.997 22.044  1.00 17.09 ? 63  SER A O   1 
ATOM   436  C CB  . SER A 1 83  ? 2.571   -31.717 22.292  1.00 17.77 ? 63  SER A CB  1 
ATOM   437  O OG  . SER A 1 83  ? 2.043   -30.744 23.167  1.00 16.23 ? 63  SER A OG  1 
ATOM   438  N N   . PRO A 1 84  ? 2.829   -34.778 21.361  1.00 16.92 ? 64  PRO A N   1 
ATOM   439  C CA  . PRO A 1 84  ? 3.378   -35.653 20.320  1.00 16.87 ? 64  PRO A CA  1 
ATOM   440  C C   . PRO A 1 84  ? 3.730   -34.891 19.037  1.00 16.13 ? 64  PRO A C   1 
ATOM   441  O O   . PRO A 1 84  ? 4.433   -35.448 18.207  1.00 15.78 ? 64  PRO A O   1 
ATOM   442  C CB  . PRO A 1 84  ? 2.235   -36.633 20.037  1.00 16.91 ? 64  PRO A CB  1 
ATOM   443  C CG  . PRO A 1 84  ? 0.956   -35.826 20.354  1.00 17.25 ? 64  PRO A CG  1 
ATOM   444  C CD  . PRO A 1 84  ? 1.368   -34.873 21.455  1.00 18.10 ? 64  PRO A CD  1 
ATOM   445  N N   . THR A 1 85  ? 3.215   -33.663 18.903  1.00 14.41 ? 65  THR A N   1 
ATOM   446  C CA  . THR A 1 85  ? 3.344   -32.814 17.699  1.00 16.02 ? 65  THR A CA  1 
ATOM   447  C C   . THR A 1 85  ? 3.996   -31.492 18.100  1.00 16.46 ? 65  THR A C   1 
ATOM   448  O O   . THR A 1 85  ? 3.405   -30.769 18.947  1.00 15.41 ? 65  THR A O   1 
ATOM   449  C CB  . THR A 1 85  ? 1.984   -32.576 17.010  1.00 16.69 ? 65  THR A CB  1 
ATOM   450  O OG1 . THR A 1 85  ? 1.314   -33.814 16.772  1.00 14.75 ? 65  THR A OG1 1 
ATOM   451  C CG2 . THR A 1 85  ? 2.130   -31.865 15.685  1.00 16.91 ? 65  THR A CG2 1 
ATOM   452  N N   . ILE A 1 86  ? 5.136   -31.172 17.476  1.00 15.76 ? 66  ILE A N   1 
ATOM   453  C CA  . ILE A 1 86  ? 5.936   -29.954 17.769  1.00 15.87 ? 66  ILE A CA  1 
ATOM   454  C C   . ILE A 1 86  ? 5.942   -29.037 16.542  1.00 15.42 ? 66  ILE A C   1 
ATOM   455  O O   . ILE A 1 86  ? 6.485   -29.416 15.505  1.00 15.05 ? 66  ILE A O   1 
ATOM   456  C CB  . ILE A 1 86  ? 7.373   -30.325 18.188  1.00 17.68 ? 66  ILE A CB  1 
ATOM   457  C CG1 . ILE A 1 86  ? 7.428   -31.547 19.118  1.00 19.14 ? 66  ILE A CG1 1 
ATOM   458  C CG2 . ILE A 1 86  ? 8.062   -29.106 18.766  1.00 17.92 ? 66  ILE A CG2 1 
ATOM   459  C CD1 . ILE A 1 86  ? 6.799   -31.326 20.471  1.00 20.05 ? 66  ILE A CD1 1 
ATOM   460  N N   . VAL A 1 87  ? 5.409   -27.833 16.690  1.00 14.02 ? 67  VAL A N   1 
ATOM   461  C CA  . VAL A 1 87  ? 5.420   -26.778 15.641  1.00 13.09 ? 67  VAL A CA  1 
ATOM   462  C C   . VAL A 1 87  ? 6.495   -25.777 16.049  1.00 12.71 ? 67  VAL A C   1 
ATOM   463  O O   . VAL A 1 87  ? 6.526   -25.363 17.227  1.00 13.12 ? 67  VAL A O   1 
ATOM   464  C CB  . VAL A 1 87  ? 4.050   -26.092 15.502  1.00 12.95 ? 67  VAL A CB  1 
ATOM   465  C CG1 . VAL A 1 87  ? 4.067   -25.022 14.421  1.00 12.41 ? 67  VAL A CG1 1 
ATOM   466  C CG2 . VAL A 1 87  ? 2.926   -27.107 15.273  1.00 12.69 ? 67  VAL A CG2 1 
ATOM   467  N N   . ILE A 1 88  ? 7.367   -25.438 15.119  1.00 12.28 ? 68  ILE A N   1 
ATOM   468  C CA  . ILE A 1 88  ? 8.497   -24.505 15.342  1.00 11.88 ? 68  ILE A CA  1 
ATOM   469  C C   . ILE A 1 88  ? 8.373   -23.347 14.361  1.00 11.41 ? 68  ILE A C   1 
ATOM   470  O O   . ILE A 1 88  ? 8.210   -23.581 13.143  1.00 10.97 ? 68  ILE A O   1 
ATOM   471  C CB  . ILE A 1 88  ? 9.840   -25.240 15.200  1.00 11.77 ? 68  ILE A CB  1 
ATOM   472  C CG1 . ILE A 1 88  ? 9.847   -26.543 16.006  1.00 11.94 ? 68  ILE A CG1 1 
ATOM   473  C CG2 . ILE A 1 88  ? 10.967  -24.318 15.606  1.00 11.92 ? 68  ILE A CG2 1 
ATOM   474  C CD1 . ILE A 1 88  ? 11.089  -27.388 15.827  1.00 11.96 ? 68  ILE A CD1 1 
ATOM   475  N N   . CYS A 1 89  ? 8.467   -22.131 14.874  1.00 12.95 ? 69  CYS A N   1 
ATOM   476  C CA  . CYS A 1 89  ? 8.461   -20.900 14.047  1.00 13.59 ? 69  CYS A CA  1 
ATOM   477  C C   . CYS A 1 89  ? 9.368   -19.873 14.709  1.00 14.10 ? 69  CYS A C   1 
ATOM   478  O O   . CYS A 1 89  ? 8.911   -19.106 15.577  1.00 14.12 ? 69  CYS A O   1 
ATOM   479  C CB  . CYS A 1 89  ? 7.045   -20.403 13.800  1.00 14.14 ? 69  CYS A CB  1 
ATOM   480  S SG  . CYS A 1 89  ? 7.024   -19.043 12.608  1.00 14.55 ? 69  CYS A SG  1 
ATOM   481  N N   . LEU A 1 90  ? 10.650  -19.943 14.353  1.00 15.67 ? 70  LEU A N   1 
ATOM   482  C CA  . LEU A 1 90  ? 11.728  -19.131 14.962  1.00 16.01 ? 70  LEU A CA  1 
ATOM   483  C C   . LEU A 1 90  ? 12.312  -18.221 13.866  1.00 17.61 ? 70  LEU A C   1 
ATOM   484  O O   . LEU A 1 90  ? 11.905  -18.358 12.676  1.00 17.72 ? 70  LEU A O   1 
ATOM   485  C CB  . LEU A 1 90  ? 12.759  -20.062 15.610  1.00 14.99 ? 70  LEU A CB  1 
ATOM   486  C CG  . LEU A 1 90  ? 12.321  -20.730 16.908  1.00 15.44 ? 70  LEU A CG  1 
ATOM   487  C CD1 . LEU A 1 90  ? 13.240  -21.882 17.295  1.00 15.89 ? 70  LEU A CD1 1 
ATOM   488  C CD2 . LEU A 1 90  ? 12.236  -19.717 18.054  1.00 15.93 ? 70  LEU A CD2 1 
ATOM   489  N N   . LEU A 1 91  ? 13.186  -17.290 14.259  1.00 18.39 ? 71  LEU A N   1 
ATOM   490  C CA  . LEU A 1 91  ? 13.798  -16.277 13.362  1.00 18.92 ? 71  LEU A CA  1 
ATOM   491  C C   . LEU A 1 91  ? 14.382  -16.955 12.110  1.00 17.80 ? 71  LEU A C   1 
ATOM   492  O O   . LEU A 1 91  ? 14.121  -16.506 10.974  1.00 16.79 ? 71  LEU A O   1 
ATOM   493  C CB  . LEU A 1 91  ? 14.896  -15.539 14.135  1.00 20.78 ? 71  LEU A CB  1 
ATOM   494  C CG  . LEU A 1 91  ? 15.575  -14.402 13.365  1.00 21.94 ? 71  LEU A CG  1 
ATOM   495  C CD1 . LEU A 1 91  ? 14.622  -13.234 13.184  1.00 22.34 ? 71  LEU A CD1 1 
ATOM   496  C CD2 . LEU A 1 91  ? 16.837  -13.964 14.072  1.00 21.79 ? 71  LEU A CD2 1 
ATOM   497  N N   . ASN A 1 92  ? 15.191  -17.981 12.302  1.00 17.93 ? 72  ASN A N   1 
ATOM   498  C CA  . ASN A 1 92  ? 15.960  -18.604 11.197  1.00 18.09 ? 72  ASN A CA  1 
ATOM   499  C C   . ASN A 1 92  ? 16.308  -20.032 11.630  1.00 17.68 ? 72  ASN A C   1 
ATOM   500  O O   . ASN A 1 92  ? 16.033  -20.365 12.787  1.00 18.54 ? 72  ASN A O   1 
ATOM   501  C CB  . ASN A 1 92  ? 17.174  -17.740 10.849  1.00 18.18 ? 72  ASN A CB  1 
ATOM   502  C CG  . ASN A 1 92  ? 18.132  -17.587 12.014  1.00 18.94 ? 72  ASN A CG  1 
ATOM   503  O OD1 . ASN A 1 92  ? 18.547  -18.580 12.604  1.00 20.31 ? 72  ASN A OD1 1 
ATOM   504  N ND2 . ASN A 1 92  ? 18.498  -16.360 12.354  1.00 19.70 ? 72  ASN A ND2 1 
ATOM   505  N N   . GLN A 1 93  ? 16.886  -20.834 10.741  1.00 18.01 ? 73  GLN A N   1 
ATOM   506  C CA  . GLN A 1 93  ? 17.186  -22.269 10.999  1.00 18.15 ? 73  GLN A CA  1 
ATOM   507  C C   . GLN A 1 93  ? 18.373  -22.418 11.974  1.00 18.86 ? 73  GLN A C   1 
ATOM   508  O O   . GLN A 1 93  ? 18.469  -23.485 12.625  1.00 16.09 ? 73  GLN A O   1 
ATOM   509  C CB  . GLN A 1 93  ? 17.428  -22.994 9.677   1.00 16.90 ? 73  GLN A CB  1 
ATOM   510  C CG  . GLN A 1 93  ? 16.177  -23.122 8.813   1.00 17.03 ? 73  GLN A CG  1 
ATOM   511  C CD  . GLN A 1 93  ? 15.292  -24.269 9.249   1.00 16.29 ? 73  GLN A CD  1 
ATOM   512  O OE1 . GLN A 1 93  ? 14.968  -24.415 10.432  1.00 16.70 ? 73  GLN A OE1 1 
ATOM   513  N NE2 . GLN A 1 93  ? 14.892  -25.098 8.300   1.00 14.79 ? 73  GLN A NE2 1 
ATOM   514  N N   . ASP A 1 94  ? 19.240  -21.415 12.103  1.00 19.88 ? 74  ASP A N   1 
ATOM   515  C CA  . ASP A 1 94  ? 20.339  -21.461 13.112  1.00 22.15 ? 74  ASP A CA  1 
ATOM   516  C C   . ASP A 1 94  ? 19.721  -21.396 14.525  1.00 21.27 ? 74  ASP A C   1 
ATOM   517  O O   . ASP A 1 94  ? 20.000  -22.270 15.309  1.00 20.33 ? 74  ASP A O   1 
ATOM   518  C CB  . ASP A 1 94  ? 21.388  -20.376 12.843  1.00 26.55 ? 74  ASP A CB  1 
ATOM   519  C CG  . ASP A 1 94  ? 22.404  -20.753 11.759  1.00 30.89 ? 74  ASP A CG  1 
ATOM   520  O OD1 . ASP A 1 94  ? 22.864  -21.942 11.730  1.00 32.03 ? 74  ASP A OD1 1 
ATOM   521  O OD2 . ASP A 1 94  ? 22.734  -19.865 10.937  1.00 31.41 ? 74  ASP A OD2 1 
ATOM   522  N N   . VAL A 1 95  ? 18.856  -20.421 14.814  1.00 20.59 ? 75  VAL A N   1 
ATOM   523  C CA  . VAL A 1 95  ? 18.119  -20.319 16.107  1.00 20.49 ? 75  VAL A CA  1 
ATOM   524  C C   . VAL A 1 95  ? 17.341  -21.634 16.355  1.00 21.17 ? 75  VAL A C   1 
ATOM   525  O O   . VAL A 1 95  ? 17.234  -22.062 17.522  1.00 23.03 ? 75  VAL A O   1 
ATOM   526  C CB  . VAL A 1 95  ? 17.213  -19.070 16.100  1.00 20.43 ? 75  VAL A CB  1 
ATOM   527  C CG1 . VAL A 1 95  ? 16.308  -19.034 17.313  1.00 21.51 ? 75  VAL A CG1 1 
ATOM   528  C CG2 . VAL A 1 95  ? 18.023  -17.770 15.983  1.00 20.97 ? 75  VAL A CG2 1 
ATOM   529  N N   . VAL A 1 96  ? 16.840  -22.297 15.313  1.00 21.11 ? 76  VAL A N   1 
ATOM   530  C CA  . VAL A 1 96  ? 16.085  -23.581 15.453  1.00 22.21 ? 76  VAL A CA  1 
ATOM   531  C C   . VAL A 1 96  ? 17.028  -24.620 16.057  1.00 23.28 ? 76  VAL A C   1 
ATOM   532  O O   . VAL A 1 96  ? 16.637  -25.292 17.052  1.00 21.84 ? 76  VAL A O   1 
ATOM   533  C CB  . VAL A 1 96  ? 15.478  -24.054 14.116  1.00 22.40 ? 76  VAL A CB  1 
ATOM   534  C CG1 . VAL A 1 96  ? 15.042  -25.508 14.177  1.00 23.57 ? 76  VAL A CG1 1 
ATOM   535  C CG2 . VAL A 1 96  ? 14.324  -23.164 13.679  1.00 22.79 ? 76  VAL A CG2 1 
ATOM   536  N N   . GLN A 1 97  ? 18.211  -24.768 15.451  1.00 25.18 ? 77  GLN A N   1 
ATOM   537  C CA  . GLN A 1 97  ? 19.293  -25.672 15.917  1.00 25.92 ? 77  GLN A CA  1 
ATOM   538  C C   . GLN A 1 97  ? 19.708  -25.302 17.339  1.00 25.23 ? 77  GLN A C   1 
ATOM   539  O O   . GLN A 1 97  ? 19.830  -26.222 18.151  1.00 25.56 ? 77  GLN A O   1 
ATOM   540  C CB  . GLN A 1 97  ? 20.510  -25.607 14.997  1.00 27.19 ? 77  GLN A CB  1 
ATOM   541  C CG  . GLN A 1 97  ? 20.245  -26.262 13.654  1.00 28.58 ? 77  GLN A CG  1 
ATOM   542  C CD  . GLN A 1 97  ? 21.407  -26.115 12.708  1.00 31.28 ? 77  GLN A CD  1 
ATOM   543  O OE1 . GLN A 1 97  ? 21.312  -25.452 11.683  1.00 34.69 ? 77  GLN A OE1 1 
ATOM   544  N NE2 . GLN A 1 97  ? 22.514  -26.749 13.048  1.00 34.62 ? 77  GLN A NE2 1 
ATOM   545  N N   . GLN A 1 98  ? 19.939  -24.019 17.621  1.00 26.07 ? 78  GLN A N   1 
ATOM   546  C CA  . GLN A 1 98  ? 20.350  -23.543 18.973  1.00 27.80 ? 78  GLN A CA  1 
ATOM   547  C C   . GLN A 1 98  ? 19.271  -23.950 19.995  1.00 28.39 ? 78  GLN A C   1 
ATOM   548  O O   . GLN A 1 98  ? 19.617  -24.393 21.121  1.00 27.06 ? 78  GLN A O   1 
ATOM   549  C CB  . GLN A 1 98  ? 20.569  -22.031 18.958  1.00 30.21 ? 78  GLN A CB  1 
ATOM   550  C CG  . GLN A 1 98  ? 21.733  -21.577 18.082  1.00 31.86 ? 78  GLN A CG  1 
ATOM   551  C CD  . GLN A 1 98  ? 21.804  -20.075 17.960  1.00 33.53 ? 78  GLN A CD  1 
ATOM   552  O OE1 . GLN A 1 98  ? 21.323  -19.344 18.821  1.00 40.92 ? 78  GLN A OE1 1 
ATOM   553  N NE2 . GLN A 1 98  ? 22.405  -19.594 16.883  1.00 33.35 ? 78  GLN A NE2 1 
ATOM   554  N N   . THR A 1 99  ? 17.996  -23.853 19.619  1.00 25.08 ? 79  THR A N   1 
ATOM   555  C CA  . THR A 1 99  ? 16.858  -24.109 20.539  1.00 25.87 ? 79  THR A CA  1 
ATOM   556  C C   . THR A 1 99  ? 16.695  -25.615 20.800  1.00 25.26 ? 79  THR A C   1 
ATOM   557  O O   . THR A 1 99  ? 16.272  -25.967 21.904  1.00 24.50 ? 79  THR A O   1 
ATOM   558  C CB  . THR A 1 99  ? 15.574  -23.493 19.988  1.00 25.40 ? 79  THR A CB  1 
ATOM   559  O OG1 . THR A 1 99  ? 15.785  -22.080 19.953  1.00 25.50 ? 79  THR A OG1 1 
ATOM   560  C CG2 . THR A 1 99  ? 14.371  -23.823 20.843  1.00 27.51 ? 79  THR A CG2 1 
ATOM   561  N N   . LEU A 1 100 ? 17.014  -26.465 19.827  1.00 24.82 ? 80  LEU A N   1 
ATOM   562  C CA  . LEU A 1 100 ? 16.914  -27.941 19.974  1.00 27.64 ? 80  LEU A CA  1 
ATOM   563  C C   . LEU A 1 100 ? 18.170  -28.488 20.668  1.00 29.25 ? 80  LEU A C   1 
ATOM   564  O O   . LEU A 1 100 ? 18.193  -29.694 20.970  1.00 29.33 ? 80  LEU A O   1 
ATOM   565  C CB  . LEU A 1 100 ? 16.732  -28.576 18.595  1.00 26.90 ? 80  LEU A CB  1 
ATOM   566  C CG  . LEU A 1 100 ? 15.406  -28.267 17.906  1.00 27.15 ? 80  LEU A CG  1 
ATOM   567  C CD1 . LEU A 1 100 ? 15.335  -28.939 16.547  1.00 27.32 ? 80  LEU A CD1 1 
ATOM   568  C CD2 . LEU A 1 100 ? 14.231  -28.673 18.762  1.00 29.30 ? 80  LEU A CD2 1 
ATOM   569  N N   . ASP A 1 101 ? 19.163  -27.639 20.930  1.00 32.64 ? 81  ASP A N   1 
ATOM   570  C CA  . ASP A 1 101 ? 20.486  -28.086 21.437  1.00 37.44 ? 81  ASP A CA  1 
ATOM   571  C C   . ASP A 1 101 ? 20.304  -29.080 22.587  1.00 35.86 ? 81  ASP A C   1 
ATOM   572  O O   . ASP A 1 101 ? 20.811  -30.190 22.452  1.00 37.25 ? 81  ASP A O   1 
ATOM   573  C CB  . ASP A 1 101 ? 21.352  -26.916 21.885  1.00 42.76 ? 81  ASP A CB  1 
ATOM   574  C CG  . ASP A 1 101 ? 22.741  -27.029 21.301  1.00 48.62 ? 81  ASP A CG  1 
ATOM   575  O OD1 . ASP A 1 101 ? 22.826  -27.221 20.075  1.00 53.19 ? 81  ASP A OD1 1 
ATOM   576  O OD2 . ASP A 1 101 ? 23.711  -26.973 22.081  1.00 58.61 ? 81  ASP A OD2 1 
ATOM   577  N N   . GLU A 1 102 ? 19.561  -28.708 23.636  1.00 33.35 ? 82  GLU A N   1 
ATOM   578  C CA  . GLU A 1 102 ? 19.461  -29.488 24.900  1.00 33.67 ? 82  GLU A CA  1 
ATOM   579  C C   . GLU A 1 102 ? 18.191  -30.353 24.936  1.00 29.93 ? 82  GLU A C   1 
ATOM   580  O O   . GLU A 1 102 ? 17.910  -30.946 26.026  1.00 28.48 ? 82  GLU A O   1 
ATOM   581  C CB  . GLU A 1 102 ? 19.560  -28.549 26.101  1.00 36.27 ? 82  GLU A CB  1 
ATOM   582  C CG  . GLU A 1 102 ? 20.899  -27.822 26.172  1.00 38.70 ? 82  GLU A CG  1 
ATOM   583  C CD  . GLU A 1 102 ? 21.066  -26.958 27.408  1.00 41.89 ? 82  GLU A CD  1 
ATOM   584  O OE1 . GLU A 1 102 ? 22.106  -26.264 27.504  1.00 47.28 ? 82  GLU A OE1 1 
ATOM   585  O OE2 . GLU A 1 102 ? 20.158  -26.985 28.270  1.00 36.80 ? 82  GLU A OE2 1 
ATOM   586  N N   . VAL A 1 103 ? 17.506  -30.496 23.793  1.00 24.70 ? 83  VAL A N   1 
ATOM   587  C CA  . VAL A 1 103 ? 16.439  -31.519 23.584  1.00 24.14 ? 83  VAL A CA  1 
ATOM   588  C C   . VAL A 1 103 ? 17.127  -32.860 23.265  1.00 24.05 ? 83  VAL A C   1 
ATOM   589  O O   . VAL A 1 103 ? 17.815  -32.967 22.243  1.00 24.81 ? 83  VAL A O   1 
ATOM   590  C CB  . VAL A 1 103 ? 15.440  -31.119 22.482  1.00 25.59 ? 83  VAL A CB  1 
ATOM   591  C CG1 . VAL A 1 103 ? 14.313  -32.136 22.365  1.00 25.21 ? 83  VAL A CG1 1 
ATOM   592  C CG2 . VAL A 1 103 ? 14.891  -29.705 22.681  1.00 24.25 ? 83  VAL A CG2 1 
ATOM   593  N N   . ILE A 1 104 ? 16.942  -33.849 24.133  1.00 22.56 ? 84  ILE A N   1 
ATOM   594  C CA  . ILE A 1 104 ? 17.671  -35.145 24.087  1.00 22.82 ? 84  ILE A CA  1 
ATOM   595  C C   . ILE A 1 104 ? 16.879  -36.115 23.211  1.00 20.55 ? 84  ILE A C   1 
ATOM   596  O O   . ILE A 1 104 ? 17.487  -36.835 22.392  1.00 19.69 ? 84  ILE A O   1 
ATOM   597  C CB  . ILE A 1 104 ? 17.872  -35.642 25.532  1.00 23.36 ? 84  ILE A CB  1 
ATOM   598  C CG1 . ILE A 1 104 ? 18.633  -34.592 26.355  1.00 24.48 ? 84  ILE A CG1 1 
ATOM   599  C CG2 . ILE A 1 104 ? 18.553  -36.997 25.544  1.00 24.98 ? 84  ILE A CG2 1 
ATOM   600  C CD1 . ILE A 1 104 ? 18.678  -34.865 27.854  1.00 24.76 ? 84  ILE A CD1 1 
ATOM   601  N N   . ASP A 1 105 ? 15.558  -36.133 23.385  1.00 19.71 ? 85  ASP A N   1 
ATOM   602  C CA  . ASP A 1 105 ? 14.724  -37.272 22.939  1.00 21.53 ? 85  ASP A CA  1 
ATOM   603  C C   . ASP A 1 105 ? 13.484  -36.751 22.216  1.00 20.52 ? 85  ASP A C   1 
ATOM   604  O O   . ASP A 1 105 ? 12.669  -36.037 22.854  1.00 21.21 ? 85  ASP A O   1 
ATOM   605  C CB  . ASP A 1 105 ? 14.356  -38.158 24.130  1.00 23.93 ? 85  ASP A CB  1 
ATOM   606  C CG  . ASP A 1 105 ? 13.910  -39.543 23.712  1.00 26.71 ? 85  ASP A CG  1 
ATOM   607  O OD1 . ASP A 1 105 ? 14.111  -39.901 22.525  1.00 25.36 ? 85  ASP A OD1 1 
ATOM   608  O OD2 . ASP A 1 105 ? 13.362  -40.250 24.578  1.00 34.82 ? 85  ASP A OD2 1 
ATOM   609  N N   . LEU A 1 106 ? 13.354  -37.124 20.946  1.00 19.52 ? 86  LEU A N   1 
ATOM   610  C CA  . LEU A 1 106 ? 12.198  -36.776 20.080  1.00 19.62 ? 86  LEU A CA  1 
ATOM   611  C C   . LEU A 1 106 ? 11.454  -38.055 19.678  1.00 19.05 ? 86  LEU A C   1 
ATOM   612  O O   . LEU A 1 106 ? 10.597  -37.999 18.767  1.00 19.83 ? 86  LEU A O   1 
ATOM   613  C CB  . LEU A 1 106 ? 12.728  -36.000 18.871  1.00 19.16 ? 86  LEU A CB  1 
ATOM   614  C CG  . LEU A 1 106 ? 13.313  -34.613 19.150  1.00 18.43 ? 86  LEU A CG  1 
ATOM   615  C CD1 . LEU A 1 106 ? 13.691  -33.914 17.851  1.00 19.51 ? 86  LEU A CD1 1 
ATOM   616  C CD2 . LEU A 1 106 ? 12.353  -33.755 19.941  1.00 19.52 ? 86  LEU A CD2 1 
ATOM   617  N N   . SER A 1 107 ? 11.727  -39.181 20.343  1.00 19.30 ? 87  SER A N   1 
ATOM   618  C CA  . SER A 1 107 ? 10.985  -40.452 20.134  1.00 20.04 ? 87  SER A CA  1 
ATOM   619  C C   . SER A 1 107 ? 9.473   -40.172 20.137  1.00 19.05 ? 87  SER A C   1 
ATOM   620  O O   . SER A 1 107 ? 9.001   -39.517 21.068  1.00 18.34 ? 87  SER A O   1 
ATOM   621  C CB  . SER A 1 107 ? 11.366  -41.488 21.164  1.00 21.34 ? 87  SER A CB  1 
ATOM   622  O OG  . SER A 1 107 ? 12.746  -41.794 21.036  1.00 24.21 ? 87  SER A OG  1 
ATOM   623  N N   . GLY A 1 108 ? 8.772   -40.631 19.099  1.00 19.97 ? 88  GLY A N   1 
ATOM   624  C CA  . GLY A 1 108 ? 7.318   -40.465 18.927  1.00 22.37 ? 88  GLY A CA  1 
ATOM   625  C C   . GLY A 1 108 ? 6.907   -39.032 18.619  1.00 23.69 ? 88  GLY A C   1 
ATOM   626  O O   . GLY A 1 108 ? 5.687   -38.762 18.645  1.00 27.76 ? 88  GLY A O   1 
ATOM   627  N N   . LYS A 1 109 ? 7.849   -38.124 18.341  1.00 22.48 ? 89  LYS A N   1 
ATOM   628  C CA  . LYS A 1 109 ? 7.494   -36.709 18.059  1.00 20.74 ? 89  LYS A CA  1 
ATOM   629  C C   . LYS A 1 109 ? 7.429   -36.496 16.546  1.00 19.46 ? 89  LYS A C   1 
ATOM   630  O O   . LYS A 1 109 ? 8.338   -36.924 15.840  1.00 17.75 ? 89  LYS A O   1 
ATOM   631  C CB  . LYS A 1 109 ? 8.471   -35.712 18.683  1.00 20.41 ? 89  LYS A CB  1 
ATOM   632  C CG  . LYS A 1 109 ? 8.765   -35.943 20.149  1.00 21.27 ? 89  LYS A CG  1 
ATOM   633  C CD  . LYS A 1 109 ? 7.581   -35.825 21.039  1.00 21.50 ? 89  LYS A CD  1 
ATOM   634  C CE  . LYS A 1 109 ? 7.975   -36.058 22.481  1.00 21.07 ? 89  LYS A CE  1 
ATOM   635  N NZ  . LYS A 1 109 ? 6.764   -36.143 23.321  1.00 21.49 ? 89  LYS A NZ  1 
ATOM   636  N N   . THR A 1 110 ? 6.394   -35.800 16.082  1.00 18.97 ? 90  THR A N   1 
ATOM   637  C CA  . THR A 1 110 ? 6.346   -35.239 14.710  1.00 18.37 ? 90  THR A CA  1 
ATOM   638  C C   . THR A 1 110 ? 6.715   -33.761 14.799  1.00 18.35 ? 90  THR A C   1 
ATOM   639  O O   . THR A 1 110 ? 6.054   -33.039 15.573  1.00 17.01 ? 90  THR A O   1 
ATOM   640  C CB  . THR A 1 110 ? 4.972   -35.470 14.079  1.00 18.90 ? 90  THR A CB  1 
ATOM   641  O OG1 . THR A 1 110 ? 4.787   -36.886 14.005  1.00 18.44 ? 90  THR A OG1 1 
ATOM   642  C CG2 . THR A 1 110 ? 4.861   -34.843 12.708  1.00 19.63 ? 90  THR A CG2 1 
ATOM   643  N N   . ILE A 1 111 ? 7.707   -33.340 14.007  1.00 19.29 ? 91  ILE A N   1 
ATOM   644  C CA  . ILE A 1 111 ? 8.248   -31.950 13.955  1.00 18.54 ? 91  ILE A CA  1 
ATOM   645  C C   . ILE A 1 111 ? 7.705   -31.285 12.693  1.00 18.19 ? 91  ILE A C   1 
ATOM   646  O O   . ILE A 1 111 ? 7.935   -31.844 11.597  1.00 19.05 ? 91  ILE A O   1 
ATOM   647  C CB  . ILE A 1 111 ? 9.791   -31.975 13.933  1.00 19.78 ? 91  ILE A CB  1 
ATOM   648  C CG1 . ILE A 1 111 ? 10.349  -32.824 15.079  1.00 20.57 ? 91  ILE A CG1 1 
ATOM   649  C CG2 . ILE A 1 111 ? 10.348  -30.557 13.938  1.00 19.15 ? 91  ILE A CG2 1 
ATOM   650  C CD1 . ILE A 1 111 ? 9.878   -32.362 16.443  1.00 20.40 ? 91  ILE A CD1 1 
ATOM   651  N N   . ILE A 1 112 ? 7.001   -30.163 12.861  1.00 16.28 ? 92  ILE A N   1 
ATOM   652  C CA  . ILE A 1 112 ? 6.463   -29.292 11.789  1.00 15.79 ? 92  ILE A CA  1 
ATOM   653  C C   . ILE A 1 112 ? 7.232   -27.979 11.901  1.00 15.09 ? 92  ILE A C   1 
ATOM   654  O O   . ILE A 1 112 ? 6.926   -27.157 12.793  1.00 13.78 ? 92  ILE A O   1 
ATOM   655  C CB  . ILE A 1 112 ? 4.928   -29.110 11.933  1.00 16.59 ? 92  ILE A CB  1 
ATOM   656  C CG1 . ILE A 1 112 ? 4.196   -30.452 12.070  1.00 16.75 ? 92  ILE A CG1 1 
ATOM   657  C CG2 . ILE A 1 112 ? 4.366   -28.284 10.793  1.00 16.58 ? 92  ILE A CG2 1 
ATOM   658  C CD1 . ILE A 1 112 ? 2.666   -30.333 12.191  1.00 16.59 ? 92  ILE A CD1 1 
ATOM   659  N N   . ASN A 1 113 ? 8.175   -27.771 10.998  1.00 14.37 ? 93  ASN A N   1 
ATOM   660  C CA  . ASN A 1 113 ? 9.029   -26.564 11.017  1.00 14.32 ? 93  ASN A CA  1 
ATOM   661  C C   . ASN A 1 113 ? 8.472   -25.546 10.019  1.00 13.12 ? 93  ASN A C   1 
ATOM   662  O O   . ASN A 1 113 ? 8.560   -25.819 8.810   1.00 12.59 ? 93  ASN A O   1 
ATOM   663  C CB  . ASN A 1 113 ? 10.477  -26.932 10.691  1.00 13.56 ? 93  ASN A CB  1 
ATOM   664  C CG  . ASN A 1 113 ? 11.440  -25.830 11.053  1.00 13.88 ? 93  ASN A CG  1 
ATOM   665  O OD1 . ASN A 1 113 ? 11.040  -24.812 11.654  1.00 13.35 ? 93  ASN A OD1 1 
ATOM   666  N ND2 . ASN A 1 113 ? 12.708  -26.076 10.758  1.00 12.12 ? 93  ASN A ND2 1 
ATOM   667  N N   . LEU A 1 114 ? 7.992   -24.403 10.510  1.00 13.33 ? 94  LEU A N   1 
ATOM   668  C CA  . LEU A 1 114 ? 7.491   -23.261 9.691   1.00 13.41 ? 94  LEU A CA  1 
ATOM   669  C C   . LEU A 1 114 ? 8.472   -22.084 9.706   1.00 14.27 ? 94  LEU A C   1 
ATOM   670  O O   . LEU A 1 114 ? 8.079   -20.981 9.266   1.00 15.77 ? 94  LEU A O   1 
ATOM   671  C CB  . LEU A 1 114 ? 6.119   -22.847 10.234  1.00 13.91 ? 94  LEU A CB  1 
ATOM   672  C CG  . LEU A 1 114 ? 5.139   -24.004 10.391  1.00 13.88 ? 94  LEU A CG  1 
ATOM   673  C CD1 . LEU A 1 114 ? 3.817   -23.516 10.939  1.00 13.68 ? 94  LEU A CD1 1 
ATOM   674  C CD2 . LEU A 1 114 ? 4.956   -24.746 9.062   1.00 14.38 ? 94  LEU A CD2 1 
ATOM   675  N N   . THR A 1 115 ? 9.699   -22.296 10.180  1.00 14.12 ? 95  THR A N   1 
ATOM   676  C CA  . THR A 1 115 ? 10.829  -21.331 10.111  1.00 13.67 ? 95  THR A CA  1 
ATOM   677  C C   . THR A 1 115 ? 11.346  -21.251 8.666   1.00 13.26 ? 95  THR A C   1 
ATOM   678  O O   . THR A 1 115 ? 11.642  -22.332 8.069   1.00 13.67 ? 95  THR A O   1 
ATOM   679  C CB  . THR A 1 115 ? 11.963  -21.789 11.031  1.00 12.96 ? 95  THR A CB  1 
ATOM   680  O OG1 . THR A 1 115 ? 11.436  -21.968 12.343  1.00 12.25 ? 95  THR A OG1 1 
ATOM   681  C CG2 . THR A 1 115 ? 13.142  -20.837 11.061  1.00 12.78 ? 95  THR A CG2 1 
ATOM   682  N N   . ASN A 1 116 ? 11.496  -20.046 8.121   1.00 12.89 ? 96  ASN A N   1 
ATOM   683  C CA  . ASN A 1 116 ? 11.969  -19.868 6.724   1.00 13.19 ? 96  ASN A CA  1 
ATOM   684  C C   . ASN A 1 116 ? 13.463  -20.150 6.721   1.00 12.81 ? 96  ASN A C   1 
ATOM   685  O O   . ASN A 1 116 ? 14.117  -19.884 7.739   1.00 14.00 ? 96  ASN A O   1 
ATOM   686  C CB  . ASN A 1 116 ? 11.655  -18.500 6.117   1.00 13.53 ? 96  ASN A CB  1 
ATOM   687  C CG  . ASN A 1 116 ? 10.233  -18.392 5.615   1.00 14.40 ? 96  ASN A CG  1 
ATOM   688  O OD1 . ASN A 1 116 ? 9.836   -17.334 5.113   1.00 16.03 ? 96  ASN A OD1 1 
ATOM   689  N ND2 . ASN A 1 116 ? 9.445   -19.442 5.792   1.00 13.13 ? 96  ASN A ND2 1 
ATOM   690  N N   . GLY A 1 117 ? 13.956  -20.729 5.635   1.00 12.65 ? 97  GLY A N   1 
ATOM   691  C CA  . GLY A 1 117 ? 15.391  -20.971 5.458   1.00 12.75 ? 97  GLY A CA  1 
ATOM   692  C C   . GLY A 1 117 ? 15.668  -21.534 4.078   1.00 13.47 ? 97  GLY A C   1 
ATOM   693  O O   . GLY A 1 117 ? 14.760  -21.546 3.236   1.00 12.78 ? 97  GLY A O   1 
ATOM   694  N N   . THR A 1 118 ? 16.886  -22.007 3.870   1.00 13.33 ? 98  THR A N   1 
ATOM   695  C CA  . THR A 1 118 ? 17.363  -22.525 2.574   1.00 14.32 ? 98  THR A CA  1 
ATOM   696  C C   . THR A 1 118 ? 17.022  -24.002 2.499   1.00 14.52 ? 98  THR A C   1 
ATOM   697  O O   . THR A 1 118 ? 16.812  -24.641 3.519   1.00 13.90 ? 98  THR A O   1 
ATOM   698  C CB  . THR A 1 118 ? 18.880  -22.350 2.441   1.00 14.57 ? 98  THR A CB  1 
ATOM   699  O OG1 . THR A 1 118 ? 19.470  -23.310 3.320   1.00 14.89 ? 98  THR A OG1 1 
ATOM   700  C CG2 . THR A 1 118 ? 19.330  -20.943 2.752   1.00 14.27 ? 98  THR A CG2 1 
ATOM   701  N N   . PRO A 1 119 ? 17.006  -24.597 1.289   1.00 16.52 ? 99  PRO A N   1 
ATOM   702  C CA  . PRO A 1 119 ? 16.876  -26.058 1.162   1.00 18.16 ? 99  PRO A CA  1 
ATOM   703  C C   . PRO A 1 119 ? 17.817  -26.891 2.067   1.00 18.66 ? 99  PRO A C   1 
ATOM   704  O O   . PRO A 1 119 ? 17.333  -27.803 2.752   1.00 21.51 ? 99  PRO A O   1 
ATOM   705  C CB  . PRO A 1 119 ? 17.153  -26.275 -0.333  1.00 17.68 ? 99  PRO A CB  1 
ATOM   706  C CG  . PRO A 1 119 ? 16.651  -24.966 -0.958  1.00 18.17 ? 99  PRO A CG  1 
ATOM   707  C CD  . PRO A 1 119 ? 17.144  -23.904 -0.004  1.00 16.31 ? 99  PRO A CD  1 
ATOM   708  N N   . GLN A 1 120 ? 19.114  -26.596 2.087   1.00 19.43 ? 100 GLN A N   1 
ATOM   709  C CA  . GLN A 1 120 ? 20.109  -27.420 2.843   1.00 20.86 ? 100 GLN A CA  1 
ATOM   710  C C   . GLN A 1 120 ? 20.005  -27.133 4.355   1.00 20.18 ? 100 GLN A C   1 
ATOM   711  O O   . GLN A 1 120 ? 20.377  -28.039 5.143   1.00 17.64 ? 100 GLN A O   1 
ATOM   712  C CB  . GLN A 1 120 ? 21.527  -27.228 2.295   1.00 22.01 ? 100 GLN A CB  1 
ATOM   713  C CG  . GLN A 1 120 ? 21.687  -27.659 0.838   1.00 22.74 ? 100 GLN A CG  1 
ATOM   714  C CD  . GLN A 1 120 ? 21.106  -29.026 0.589   1.00 24.89 ? 100 GLN A CD  1 
ATOM   715  O OE1 . GLN A 1 120 ? 20.252  -29.228 -0.284  1.00 27.27 ? 100 GLN A OE1 1 
ATOM   716  N NE2 . GLN A 1 120 ? 21.530  -29.979 1.401   1.00 23.84 ? 100 GLN A NE2 1 
ATOM   717  N N   . GLN A 1 121 ? 19.505  -25.954 4.770   1.00 19.27 ? 101 GLN A N   1 
ATOM   718  C CA  . GLN A 1 121 ? 19.239  -25.684 6.214   1.00 19.32 ? 101 GLN A CA  1 
ATOM   719  C C   . GLN A 1 121 ? 18.140  -26.656 6.676   1.00 18.71 ? 101 GLN A C   1 
ATOM   720  O O   . GLN A 1 121 ? 18.273  -27.220 7.766   1.00 21.82 ? 101 GLN A O   1 
ATOM   721  C CB  . GLN A 1 121 ? 18.834  -24.233 6.472   1.00 20.71 ? 101 GLN A CB  1 
ATOM   722  C CG  . GLN A 1 121 ? 19.986  -23.241 6.401   1.00 20.07 ? 101 GLN A CG  1 
ATOM   723  C CD  . GLN A 1 121 ? 19.510  -21.812 6.379   1.00 20.47 ? 101 GLN A CD  1 
ATOM   724  O OE1 . GLN A 1 121 ? 18.319  -21.510 6.288   1.00 18.43 ? 101 GLN A OE1 1 
ATOM   725  N NE2 . GLN A 1 121 ? 20.462  -20.900 6.420   1.00 23.19 ? 101 GLN A NE2 1 
ATOM   726  N N   . ALA A 1 122 ? 17.122  -26.903 5.851   1.00 18.04 ? 102 ALA A N   1 
ATOM   727  C CA  . ALA A 1 122 ? 16.017  -27.834 6.163   1.00 18.50 ? 102 ALA A CA  1 
ATOM   728  C C   . ALA A 1 122 ? 16.595  -29.250 6.291   1.00 19.64 ? 102 ALA A C   1 
ATOM   729  O O   . ALA A 1 122 ? 16.181  -29.973 7.221   1.00 17.55 ? 102 ALA A O   1 
ATOM   730  C CB  . ALA A 1 122 ? 14.913  -27.770 5.123   1.00 18.00 ? 102 ALA A CB  1 
ATOM   731  N N   . VAL A 1 123 ? 17.523  -29.622 5.401   1.00 20.66 ? 103 VAL A N   1 
ATOM   732  C CA  . VAL A 1 123 ? 18.204  -30.954 5.433   1.00 22.06 ? 103 VAL A CA  1 
ATOM   733  C C   . VAL A 1 123 ? 18.919  -31.084 6.777   1.00 22.49 ? 103 VAL A C   1 
ATOM   734  O O   . VAL A 1 123 ? 18.672  -32.084 7.457   1.00 26.19 ? 103 VAL A O   1 
ATOM   735  C CB  . VAL A 1 123 ? 19.177  -31.174 4.257   1.00 22.93 ? 103 VAL A CB  1 
ATOM   736  C CG1 . VAL A 1 123 ? 19.991  -32.455 4.433   1.00 22.85 ? 103 VAL A CG1 1 
ATOM   737  C CG2 . VAL A 1 123 ? 18.442  -31.196 2.936   1.00 23.20 ? 103 VAL A CG2 1 
ATOM   738  N N   . LYS A 1 124 ? 19.706  -30.078 7.149   1.00 23.66 ? 104 LYS A N   1 
ATOM   739  C CA  . LYS A 1 124 ? 20.517  -30.024 8.404   1.00 26.34 ? 104 LYS A CA  1 
ATOM   740  C C   . LYS A 1 124 ? 19.613  -30.117 9.645   1.00 25.77 ? 104 LYS A C   1 
ATOM   741  O O   . LYS A 1 124 ? 19.963  -30.864 10.581  1.00 24.02 ? 104 LYS A O   1 
ATOM   742  C CB  . LYS A 1 124 ? 21.349  -28.740 8.412   1.00 28.58 ? 104 LYS A CB  1 
ATOM   743  C CG  . LYS A 1 124 ? 22.214  -28.486 9.640   1.00 31.81 ? 104 LYS A CG  1 
ATOM   744  C CD  . LYS A 1 124 ? 23.633  -28.997 9.503   1.00 35.45 ? 104 LYS A CD  1 
ATOM   745  C CE  . LYS A 1 124 ? 24.482  -28.667 10.706  1.00 35.45 ? 104 LYS A CE  1 
ATOM   746  N NZ  . LYS A 1 124 ? 24.676  -27.202 10.817  1.00 37.09 ? 104 LYS A NZ  1 
ATOM   747  N N   . VAL A 1 125 ? 18.487  -29.404 9.667   1.00 23.86 ? 105 VAL A N   1 
ATOM   748  C CA  . VAL A 1 125 ? 17.530  -29.508 10.807  1.00 22.79 ? 105 VAL A CA  1 
ATOM   749  C C   . VAL A 1 125 ? 16.887  -30.902 10.798  1.00 21.52 ? 105 VAL A C   1 
ATOM   750  O O   . VAL A 1 125 ? 16.761  -31.482 11.891  1.00 21.08 ? 105 VAL A O   1 
ATOM   751  C CB  . VAL A 1 125 ? 16.485  -28.384 10.837  1.00 20.95 ? 105 VAL A CB  1 
ATOM   752  C CG1 . VAL A 1 125 ? 15.537  -28.588 11.993  1.00 21.95 ? 105 VAL A CG1 1 
ATOM   753  C CG2 . VAL A 1 125 ? 17.147  -27.016 10.922  1.00 20.89 ? 105 VAL A CG2 1 
ATOM   754  N N   . ALA A 1 126 ? 16.508  -31.430 9.639   1.00 22.54 ? 106 ALA A N   1 
ATOM   755  C CA  . ALA A 1 126 ? 15.860  -32.766 9.508   1.00 24.38 ? 106 ALA A CA  1 
ATOM   756  C C   . ALA A 1 126 ? 16.755  -33.878 10.094  1.00 26.68 ? 106 ALA A C   1 
ATOM   757  O O   . ALA A 1 126 ? 16.186  -34.868 10.648  1.00 27.42 ? 106 ALA A O   1 
ATOM   758  C CB  . ALA A 1 126 ? 15.498  -33.038 8.075   1.00 24.12 ? 106 ALA A CB  1 
ATOM   759  N N   . THR A 1 127 ? 18.085  -33.716 10.023  1.00 28.31 ? 107 THR A N   1 
ATOM   760  C CA  . THR A 1 127 ? 19.095  -34.643 10.601  1.00 29.07 ? 107 THR A CA  1 
ATOM   761  C C   . THR A 1 127 ? 19.225  -34.408 12.114  1.00 27.94 ? 107 THR A C   1 
ATOM   762  O O   . THR A 1 127 ? 19.361  -35.427 12.836  1.00 26.17 ? 107 THR A O   1 
ATOM   763  C CB  . THR A 1 127 ? 20.444  -34.571 9.857   1.00 32.32 ? 107 THR A CB  1 
ATOM   764  O OG1 . THR A 1 127 ? 21.131  -33.347 10.151  1.00 35.86 ? 107 THR A OG1 1 
ATOM   765  C CG2 . THR A 1 127 ? 20.270  -34.719 8.359   1.00 31.61 ? 107 THR A CG2 1 
ATOM   766  N N   . LEU A 1 128 ? 19.176  -33.162 12.610  1.00 23.81 ? 108 LEU A N   1 
ATOM   767  C CA  . LEU A 1 128 ? 19.149  -32.925 14.079  1.00 26.68 ? 108 LEU A CA  1 
ATOM   768  C C   . LEU A 1 128 ? 17.989  -33.742 14.673  1.00 26.50 ? 108 LEU A C   1 
ATOM   769  O O   . LEU A 1 128 ? 18.233  -34.471 15.659  1.00 25.13 ? 108 LEU A O   1 
ATOM   770  C CB  . LEU A 1 128 ? 19.016  -31.440 14.458  1.00 28.34 ? 108 LEU A CB  1 
ATOM   771  C CG  . LEU A 1 128 ? 20.310  -30.722 14.850  1.00 30.20 ? 108 LEU A CG  1 
ATOM   772  C CD1 . LEU A 1 128 ? 21.156  -30.400 13.615  1.00 30.76 ? 108 LEU A CD1 1 
ATOM   773  C CD2 . LEU A 1 128 ? 20.027  -29.441 15.647  1.00 29.34 ? 108 LEU A CD2 1 
ATOM   774  N N   . VAL A 1 129 ? 16.767  -33.628 14.129  1.00 22.50 ? 109 VAL A N   1 
ATOM   775  C CA  . VAL A 1 129 ? 15.581  -34.252 14.791  1.00 21.21 ? 109 VAL A CA  1 
ATOM   776  C C   . VAL A 1 129 ? 15.604  -35.766 14.542  1.00 21.55 ? 109 VAL A C   1 
ATOM   777  O O   . VAL A 1 129 ? 15.259  -36.497 15.474  1.00 20.77 ? 109 VAL A O   1 
ATOM   778  C CB  . VAL A 1 129 ? 14.248  -33.600 14.401  1.00 20.72 ? 109 VAL A CB  1 
ATOM   779  C CG1 . VAL A 1 129 ? 14.251  -32.121 14.765  1.00 21.78 ? 109 VAL A CG1 1 
ATOM   780  C CG2 . VAL A 1 129 ? 13.922  -33.780 12.934  1.00 20.62 ? 109 VAL A CG2 1 
ATOM   781  N N   . GLN A 1 130 ? 16.051  -36.230 13.376  1.00 22.60 ? 110 GLN A N   1 
ATOM   782  C CA  . GLN A 1 130 ? 16.156  -37.692 13.100  1.00 25.10 ? 110 GLN A CA  1 
ATOM   783  C C   . GLN A 1 130 ? 17.109  -38.349 14.106  1.00 25.99 ? 110 GLN A C   1 
ATOM   784  O O   . GLN A 1 130 ? 16.747  -39.390 14.642  1.00 25.32 ? 110 GLN A O   1 
ATOM   785  C CB  . GLN A 1 130 ? 16.652  -37.994 11.689  1.00 24.74 ? 110 GLN A CB  1 
ATOM   786  C CG  . GLN A 1 130 ? 16.538  -39.472 11.340  1.00 26.44 ? 110 GLN A CG  1 
ATOM   787  C CD  . GLN A 1 130 ? 17.649  -40.363 11.856  1.00 27.60 ? 110 GLN A CD  1 
ATOM   788  O OE1 . GLN A 1 130 ? 17.463  -41.570 12.021  1.00 29.36 ? 110 GLN A OE1 1 
ATOM   789  N NE2 . GLN A 1 130 ? 18.817  -39.793 12.115  1.00 24.05 ? 110 GLN A NE2 1 
ATOM   790  N N   . GLN A 1 131 ? 18.272  -37.744 14.348  1.00 27.59 ? 111 GLN A N   1 
ATOM   791  C CA  . GLN A 1 131 ? 19.300  -38.224 15.309  1.00 28.79 ? 111 GLN A CA  1 
ATOM   792  C C   . GLN A 1 131 ? 18.718  -38.308 16.723  1.00 28.11 ? 111 GLN A C   1 
ATOM   793  O O   . GLN A 1 131 ? 19.123  -39.235 17.451  1.00 28.77 ? 111 GLN A O   1 
ATOM   794  C CB  . GLN A 1 131 ? 20.517  -37.307 15.302  1.00 30.59 ? 111 GLN A CB  1 
ATOM   795  C CG  . GLN A 1 131 ? 21.412  -37.487 14.082  1.00 35.80 ? 111 GLN A CG  1 
ATOM   796  C CD  . GLN A 1 131 ? 22.694  -36.701 14.239  1.00 39.27 ? 111 GLN A CD  1 
ATOM   797  O OE1 . GLN A 1 131 ? 23.337  -36.726 15.291  1.00 40.42 ? 111 GLN A OE1 1 
ATOM   798  N NE2 . GLN A 1 131 ? 23.079  -35.995 13.190  1.00 41.74 ? 111 GLN A NE2 1 
ATOM   799  N N   . ARG A 1 132 ? 17.808  -37.392 17.081  1.00 26.30 ? 112 ARG A N   1 
ATOM   800  C CA  . ARG A 1 132 ? 17.082  -37.397 18.384  1.00 25.99 ? 112 ARG A CA  1 
ATOM   801  C C   . ARG A 1 132 ? 15.962  -38.442 18.383  1.00 22.79 ? 112 ARG A C   1 
ATOM   802  O O   . ARG A 1 132 ? 15.392  -38.637 19.460  1.00 19.76 ? 112 ARG A O   1 
ATOM   803  C CB  . ARG A 1 132 ? 16.441  -36.048 18.730  1.00 28.18 ? 112 ARG A CB  1 
ATOM   804  C CG  . ARG A 1 132 ? 17.341  -34.830 18.578  1.00 32.02 ? 112 ARG A CG  1 
ATOM   805  C CD  . ARG A 1 132 ? 18.419  -34.709 19.625  1.00 34.22 ? 112 ARG A CD  1 
ATOM   806  N NE  . ARG A 1 132 ? 18.810  -33.328 19.939  1.00 36.73 ? 112 ARG A NE  1 
ATOM   807  C CZ  . ARG A 1 132 ? 19.657  -32.584 19.232  1.00 36.06 ? 112 ARG A CZ  1 
ATOM   808  N NH1 . ARG A 1 132 ? 19.979  -31.381 19.663  1.00 36.59 ? 112 ARG A NH1 1 
ATOM   809  N NH2 . ARG A 1 132 ? 20.180  -33.029 18.101  1.00 35.42 ? 112 ARG A NH2 1 
ATOM   810  N N   . GLY A 1 133 ? 15.651  -39.057 17.234  1.00 21.65 ? 113 GLY A N   1 
ATOM   811  C CA  . GLY A 1 133 ? 14.662  -40.151 17.093  1.00 21.59 ? 113 GLY A CA  1 
ATOM   812  C C   . GLY A 1 133 ? 13.250  -39.651 16.798  1.00 20.58 ? 113 GLY A C   1 
ATOM   813  O O   . GLY A 1 133 ? 12.287  -40.397 17.062  1.00 18.04 ? 113 GLY A O   1 
ATOM   814  N N   . ALA A 1 134 ? 13.117  -38.436 16.264  1.00 20.06 ? 114 ALA A N   1 
ATOM   815  C CA  . ALA A 1 134 ? 11.825  -37.856 15.827  1.00 21.54 ? 114 ALA A CA  1 
ATOM   816  C C   . ALA A 1 134 ? 11.121  -38.852 14.904  1.00 21.26 ? 114 ALA A C   1 
ATOM   817  O O   . ALA A 1 134 ? 11.819  -39.510 14.120  1.00 20.73 ? 114 ALA A O   1 
ATOM   818  C CB  . ALA A 1 134 ? 12.071  -36.530 15.143  1.00 22.89 ? 114 ALA A CB  1 
ATOM   819  N N   . GLU A 1 135 ? 9.801   -38.991 15.030  1.00 21.60 ? 115 GLU A N   1 
ATOM   820  C CA  . GLU A 1 135 ? 8.967   -39.849 14.148  1.00 24.71 ? 115 GLU A CA  1 
ATOM   821  C C   . GLU A 1 135 ? 9.050   -39.358 12.687  1.00 24.28 ? 115 GLU A C   1 
ATOM   822  O O   . GLU A 1 135 ? 9.179   -40.185 11.772  1.00 22.74 ? 115 GLU A O   1 
ATOM   823  C CB  . GLU A 1 135 ? 7.539   -39.839 14.674  1.00 28.03 ? 115 GLU A CB  1 
ATOM   824  C CG  . GLU A 1 135 ? 6.619   -40.772 13.936  1.00 33.43 ? 115 GLU A CG  1 
ATOM   825  C CD  . GLU A 1 135 ? 6.974   -42.237 14.105  1.00 40.18 ? 115 GLU A CD  1 
ATOM   826  O OE1 . GLU A 1 135 ? 6.547   -43.027 13.234  1.00 43.72 ? 115 GLU A OE1 1 
ATOM   827  O OE2 . GLU A 1 135 ? 7.686   -42.581 15.103  1.00 39.54 ? 115 GLU A OE2 1 
ATOM   828  N N   . SER A 1 136 ? 8.947   -38.050 12.459  1.00 21.64 ? 116 SER A N   1 
ATOM   829  C CA  . SER A 1 136 ? 9.072   -37.443 11.118  1.00 21.67 ? 116 SER A CA  1 
ATOM   830  C C   . SER A 1 136 ? 9.256   -35.938 11.258  1.00 19.49 ? 116 SER A C   1 
ATOM   831  O O   . SER A 1 136 ? 9.084   -35.415 12.380  1.00 15.86 ? 116 SER A O   1 
ATOM   832  C CB  . SER A 1 136 ? 7.895   -37.750 10.227  1.00 24.53 ? 116 SER A CB  1 
ATOM   833  O OG  . SER A 1 136 ? 6.748   -37.065 10.681  1.00 29.48 ? 116 SER A OG  1 
ATOM   834  N N   . TYR A 1 137 ? 9.707   -35.354 10.144  1.00 18.35 ? 117 TYR A N   1 
ATOM   835  C CA  . TYR A 1 137 ? 9.948   -33.918 9.889   1.00 18.89 ? 117 TYR A CA  1 
ATOM   836  C C   . TYR A 1 137 ? 9.175   -33.560 8.628   1.00 17.78 ? 117 TYR A C   1 
ATOM   837  O O   . TYR A 1 137 ? 9.359   -34.215 7.616   1.00 15.41 ? 117 TYR A O   1 
ATOM   838  C CB  . TYR A 1 137 ? 11.446  -33.632 9.701   1.00 18.60 ? 117 TYR A CB  1 
ATOM   839  C CG  . TYR A 1 137 ? 11.818  -32.183 9.488   1.00 18.74 ? 117 TYR A CG  1 
ATOM   840  C CD1 . TYR A 1 137 ? 12.148  -31.355 10.549  1.00 19.47 ? 117 TYR A CD1 1 
ATOM   841  C CD2 . TYR A 1 137 ? 11.880  -31.646 8.213   1.00 19.60 ? 117 TYR A CD2 1 
ATOM   842  C CE1 . TYR A 1 137 ? 12.500  -30.025 10.354  1.00 19.33 ? 117 TYR A CE1 1 
ATOM   843  C CE2 . TYR A 1 137 ? 12.250  -30.329 7.994   1.00 19.81 ? 117 TYR A CE2 1 
ATOM   844  C CZ  . TYR A 1 137 ? 12.549  -29.507 9.073   1.00 19.01 ? 117 TYR A CZ  1 
ATOM   845  O OH  . TYR A 1 137 ? 12.897  -28.206 8.859   1.00 15.90 ? 117 TYR A OH  1 
ATOM   846  N N   . ILE A 1 138 ? 8.335   -32.543 8.711   1.00 16.93 ? 118 ILE A N   1 
ATOM   847  C CA  . ILE A 1 138 ? 7.821   -31.834 7.516   1.00 17.81 ? 118 ILE A CA  1 
ATOM   848  C C   . ILE A 1 138 ? 8.143   -30.353 7.711   1.00 17.01 ? 118 ILE A C   1 
ATOM   849  O O   . ILE A 1 138 ? 8.140   -29.873 8.856   1.00 13.97 ? 118 ILE A O   1 
ATOM   850  C CB  . ILE A 1 138 ? 6.320   -32.075 7.282   1.00 17.95 ? 118 ILE A CB  1 
ATOM   851  C CG1 . ILE A 1 138 ? 5.473   -31.432 8.377   1.00 19.08 ? 118 ILE A CG1 1 
ATOM   852  C CG2 . ILE A 1 138 ? 6.043   -33.563 7.111   1.00 18.99 ? 118 ILE A CG2 1 
ATOM   853  C CD1 . ILE A 1 138 ? 4.050   -31.962 8.489   1.00 20.20 ? 118 ILE A CD1 1 
ATOM   854  N N   . HIS A 1 139 ? 8.358   -29.683 6.592   1.00 17.42 ? 119 HIS A N   1 
ATOM   855  C CA  . HIS A 1 139 ? 8.631   -28.234 6.504   1.00 17.47 ? 119 HIS A CA  1 
ATOM   856  C C   . HIS A 1 139 ? 7.449   -27.540 5.847   1.00 16.69 ? 119 HIS A C   1 
ATOM   857  O O   . HIS A 1 139 ? 6.924   -28.105 4.889   1.00 16.63 ? 119 HIS A O   1 
ATOM   858  C CB  . HIS A 1 139 ? 9.891   -27.977 5.691   1.00 17.19 ? 119 HIS A CB  1 
ATOM   859  C CG  . HIS A 1 139 ? 10.457  -26.656 6.053   1.00 16.81 ? 119 HIS A CG  1 
ATOM   860  N ND1 . HIS A 1 139 ? 11.393  -26.524 7.043   1.00 17.00 ? 119 HIS A ND1 1 
ATOM   861  C CD2 . HIS A 1 139 ? 10.113  -25.409 5.668   1.00 16.61 ? 119 HIS A CD2 1 
ATOM   862  C CE1 . HIS A 1 139 ? 11.658  -25.239 7.203   1.00 16.35 ? 119 HIS A CE1 1 
ATOM   863  N NE2 . HIS A 1 139 ? 10.896  -24.541 6.356   1.00 15.60 ? 119 HIS A NE2 1 
ATOM   864  N N   . GLY A 1 140 ? 7.090   -26.360 6.360   1.00 17.07 ? 120 GLY A N   1 
ATOM   865  C CA  . GLY A 1 140 ? 6.008   -25.508 5.847   1.00 16.19 ? 120 GLY A CA  1 
ATOM   866  C C   . GLY A 1 140 ? 6.550   -24.141 5.492   1.00 15.93 ? 120 GLY A C   1 
ATOM   867  O O   . GLY A 1 140 ? 7.310   -23.605 6.282   1.00 15.11 ? 120 GLY A O   1 
ATOM   868  N N   . ALA A 1 141 ? 6.182   -23.603 4.333   1.00 15.83 ? 121 ALA A N   1 
ATOM   869  C CA  . ALA A 1 141 ? 6.449   -22.196 3.957   1.00 16.49 ? 121 ALA A CA  1 
ATOM   870  C C   . ALA A 1 141 ? 5.113   -21.472 3.924   1.00 16.32 ? 121 ALA A C   1 
ATOM   871  O O   . ALA A 1 141 ? 4.284   -21.757 3.000   1.00 18.11 ? 121 ALA A O   1 
ATOM   872  C CB  . ALA A 1 141 ? 7.156   -22.075 2.638   1.00 16.55 ? 121 ALA A CB  1 
ATOM   873  N N   . ILE A 1 142 ? 4.891   -20.649 4.944   1.00 16.14 ? 122 ILE A N   1 
ATOM   874  C CA  . ILE A 1 142 ? 3.664   -19.820 5.095   1.00 17.01 ? 122 ILE A CA  1 
ATOM   875  C C   . ILE A 1 142 ? 3.753   -18.699 4.050   1.00 17.32 ? 122 ILE A C   1 
ATOM   876  O O   . ILE A 1 142 ? 4.708   -17.907 4.115   1.00 14.86 ? 122 ILE A O   1 
ATOM   877  C CB  . ILE A 1 142 ? 3.537   -19.281 6.537   1.00 15.90 ? 122 ILE A CB  1 
ATOM   878  C CG1 . ILE A 1 142 ? 3.385   -20.394 7.579   1.00 14.97 ? 122 ILE A CG1 1 
ATOM   879  C CG2 . ILE A 1 142 ? 2.386   -18.285 6.627   1.00 16.27 ? 122 ILE A CG2 1 
ATOM   880  C CD1 . ILE A 1 142 ? 3.573   -19.933 9.027   1.00 14.99 ? 122 ILE A CD1 1 
ATOM   881  N N   . MET A 1 143 ? 2.790   -18.631 3.130   1.00 18.70 ? 123 MET A N   1 
ATOM   882  C CA  . MET A 1 143 ? 2.804   -17.649 2.013   1.00 18.82 ? 123 MET A CA  1 
ATOM   883  C C   . MET A 1 143 ? 1.794   -16.528 2.280   1.00 20.20 ? 123 MET A C   1 
ATOM   884  O O   . MET A 1 143 ? 0.985   -16.168 1.361   1.00 19.38 ? 123 MET A O   1 
ATOM   885  C CB  . MET A 1 143 ? 2.489   -18.358 0.703   1.00 19.66 ? 123 MET A CB  1 
ATOM   886  C CG  . MET A 1 143 ? 3.453   -19.483 0.424   1.00 20.54 ? 123 MET A CG  1 
ATOM   887  S SD  . MET A 1 143 ? 3.581   -19.830 -1.327  1.00 23.00 ? 123 MET A SD  1 
ATOM   888  C CE  . MET A 1 143 ? 1.910   -20.397 -1.647  1.00 24.17 ? 123 MET A CE  1 
ATOM   889  N N   . THR A 1 144 ? 1.838   -15.997 3.502   1.00 21.04 ? 124 THR A N   1 
ATOM   890  C CA  . THR A 1 144 ? 1.023   -14.839 3.940   1.00 20.47 ? 124 THR A CA  1 
ATOM   891  C C   . THR A 1 144 ? 1.623   -14.227 5.204   1.00 20.30 ? 124 THR A C   1 
ATOM   892  O O   . THR A 1 144 ? 2.652   -14.733 5.689   1.00 21.18 ? 124 THR A O   1 
ATOM   893  C CB  . THR A 1 144 ? -0.446  -15.212 4.147   1.00 21.21 ? 124 THR A CB  1 
ATOM   894  O OG1 . THR A 1 144 ? -1.078  -13.953 4.347   1.00 23.45 ? 124 THR A OG1 1 
ATOM   895  C CG2 . THR A 1 144 ? -0.708  -16.118 5.333   1.00 22.10 ? 124 THR A CG2 1 
ATOM   896  N N   . THR A 1 145 ? 0.997   -13.155 5.691   1.00 19.77 ? 125 THR A N   1 
ATOM   897  C CA  . THR A 1 145 ? 1.442   -12.385 6.870   1.00 21.01 ? 125 THR A CA  1 
ATOM   898  C C   . THR A 1 145 ? 0.629   -12.885 8.057   1.00 20.68 ? 125 THR A C   1 
ATOM   899  O O   . THR A 1 145 ? -0.399  -13.538 7.868   1.00 20.14 ? 125 THR A O   1 
ATOM   900  C CB  . THR A 1 145 ? 1.312   -10.870 6.653   1.00 21.13 ? 125 THR A CB  1 
ATOM   901  O OG1 . THR A 1 145 ? 0.016   -10.625 6.133   1.00 23.74 ? 125 THR A OG1 1 
ATOM   902  C CG2 . THR A 1 145 ? 2.324   -10.292 5.702   1.00 22.40 ? 125 THR A CG2 1 
ATOM   903  N N   . PRO A 1 146 ? 1.101   -12.652 9.300   1.00 20.64 ? 126 PRO A N   1 
ATOM   904  C CA  . PRO A 1 146 ? 0.426   -13.154 10.498  1.00 20.49 ? 126 PRO A CA  1 
ATOM   905  C C   . PRO A 1 146 ? -1.075  -12.843 10.615  1.00 21.14 ? 126 PRO A C   1 
ATOM   906  O O   . PRO A 1 146 ? -1.818  -13.712 11.043  1.00 18.53 ? 126 PRO A O   1 
ATOM   907  C CB  . PRO A 1 146 ? 1.218   -12.432 11.585  1.00 20.05 ? 126 PRO A CB  1 
ATOM   908  C CG  . PRO A 1 146 ? 2.607   -12.442 11.035  1.00 19.82 ? 126 PRO A CG  1 
ATOM   909  C CD  . PRO A 1 146 ? 2.372   -11.980 9.621   1.00 21.29 ? 126 PRO A CD  1 
ATOM   910  N N   . GLU A 1 147 ? -1.471  -11.631 10.225  1.00 23.38 ? 127 GLU A N   1 
ATOM   911  C CA  . GLU A 1 147 ? -2.866  -11.122 10.319  1.00 27.79 ? 127 GLU A CA  1 
ATOM   912  C C   . GLU A 1 147 ? -3.812  -11.976 9.459   1.00 26.12 ? 127 GLU A C   1 
ATOM   913  O O   . GLU A 1 147 ? -4.987  -12.035 9.809   1.00 24.41 ? 127 GLU A O   1 
ATOM   914  C CB  . GLU A 1 147 ? -2.935  -9.645  9.900   1.00 31.85 ? 127 GLU A CB  1 
ATOM   915  C CG  . GLU A 1 147 ? -2.735  -9.426  8.408   1.00 35.70 ? 127 GLU A CG  1 
ATOM   916  C CD  . GLU A 1 147 ? -2.133  -8.088  8.000   1.00 42.70 ? 127 GLU A CD  1 
ATOM   917  O OE1 . GLU A 1 147 ? -2.711  -7.041  8.381   1.00 46.24 ? 127 GLU A OE1 1 
ATOM   918  O OE2 . GLU A 1 147 ? -1.078  -8.097  7.293   1.00 46.59 ? 127 GLU A OE2 1 
ATOM   919  N N   . TYR A 1 148 ? -3.351  -12.601 8.367   1.00 24.78 ? 128 TYR A N   1 
ATOM   920  C CA  . TYR A 1 148 ? -4.232  -13.406 7.475   1.00 24.76 ? 128 TYR A CA  1 
ATOM   921  C C   . TYR A 1 148 ? -4.117  -14.906 7.802   1.00 23.98 ? 128 TYR A C   1 
ATOM   922  O O   . TYR A 1 148 ? -4.847  -15.713 7.185   1.00 21.83 ? 128 TYR A O   1 
ATOM   923  C CB  . TYR A 1 148 ? -3.947  -13.097 6.004   1.00 27.14 ? 128 TYR A CB  1 
ATOM   924  C CG  . TYR A 1 148 ? -4.195  -11.654 5.640   1.00 30.79 ? 128 TYR A CG  1 
ATOM   925  C CD1 . TYR A 1 148 ? -5.483  -11.154 5.571   1.00 34.08 ? 128 TYR A CD1 1 
ATOM   926  C CD2 . TYR A 1 148 ? -3.149  -10.777 5.413   1.00 32.79 ? 128 TYR A CD2 1 
ATOM   927  C CE1 . TYR A 1 148 ? -5.731  -9.828  5.258   1.00 34.61 ? 128 TYR A CE1 1 
ATOM   928  C CE2 . TYR A 1 148 ? -3.374  -9.444  5.111   1.00 35.13 ? 128 TYR A CE2 1 
ATOM   929  C CZ  . TYR A 1 148 ? -4.673  -8.970  5.035   1.00 36.66 ? 128 TYR A CZ  1 
ATOM   930  O OH  . TYR A 1 148 ? -4.927  -7.663  4.756   1.00 36.69 ? 128 TYR A OH  1 
ATOM   931  N N   . LEU A 1 149 ? -3.254  -15.290 8.745   1.00 20.91 ? 129 LEU A N   1 
ATOM   932  C CA  . LEU A 1 149 ? -3.062  -16.728 9.082   1.00 20.51 ? 129 LEU A CA  1 
ATOM   933  C C   . LEU A 1 149 ? -4.388  -17.275 9.629   1.00 20.29 ? 129 LEU A C   1 
ATOM   934  O O   . LEU A 1 149 ? -4.976  -16.605 10.480  1.00 20.02 ? 129 LEU A O   1 
ATOM   935  C CB  . LEU A 1 149 ? -1.930  -16.880 10.100  1.00 18.54 ? 129 LEU A CB  1 
ATOM   936  C CG  . LEU A 1 149 ? -1.363  -18.287 10.231  1.00 18.15 ? 129 LEU A CG  1 
ATOM   937  C CD1 . LEU A 1 149 ? -0.672  -18.709 8.942   1.00 18.19 ? 129 LEU A CD1 1 
ATOM   938  C CD2 . LEU A 1 149 ? -0.409  -18.370 11.409  1.00 18.92 ? 129 LEU A CD2 1 
ATOM   939  N N   . GLY A 1 150 ? -4.826  -18.429 9.138   1.00 21.09 ? 130 GLY A N   1 
ATOM   940  C CA  . GLY A 1 150 ? -6.019  -19.146 9.618   1.00 23.00 ? 130 GLY A CA  1 
ATOM   941  C C   . GLY A 1 150 ? -7.200  -19.009 8.667   1.00 24.02 ? 130 GLY A C   1 
ATOM   942  O O   . GLY A 1 150 ? -8.102  -19.814 8.782   1.00 25.54 ? 130 GLY A O   1 
ATOM   943  N N   . GLN A 1 151 ? -7.206  -17.999 7.797   1.00 25.42 ? 131 GLN A N   1 
ATOM   944  C CA  . GLN A 1 151 ? -8.149  -17.874 6.651   1.00 27.26 ? 131 GLN A CA  1 
ATOM   945  C C   . GLN A 1 151 ? -7.848  -18.958 5.615   1.00 26.21 ? 131 GLN A C   1 
ATOM   946  O O   . GLN A 1 151 ? -6.694  -19.153 5.234   1.00 27.24 ? 131 GLN A O   1 
ATOM   947  C CB  . GLN A 1 151 ? -8.015  -16.491 6.015   1.00 27.39 ? 131 GLN A CB  1 
ATOM   948  C CG  . GLN A 1 151 ? -8.535  -15.366 6.891   1.00 31.96 ? 131 GLN A CG  1 
ATOM   949  C CD  . GLN A 1 151 ? -8.117  -14.008 6.379   1.00 35.51 ? 131 GLN A CD  1 
ATOM   950  O OE1 . GLN A 1 151 ? -7.591  -13.876 5.278   1.00 42.34 ? 131 GLN A OE1 1 
ATOM   951  N NE2 . GLN A 1 151 ? -8.346  -12.978 7.181   1.00 39.31 ? 131 GLN A NE2 1 
ATOM   952  N N   . PRO A 1 152 ? -8.861  -19.656 5.052   1.00 27.92 ? 132 PRO A N   1 
ATOM   953  C CA  . PRO A 1 152 ? -8.599  -20.756 4.124   1.00 26.55 ? 132 PRO A CA  1 
ATOM   954  C C   . PRO A 1 152 ? -7.958  -20.273 2.817   1.00 24.21 ? 132 PRO A C   1 
ATOM   955  O O   . PRO A 1 152 ? -7.356  -21.090 2.144   1.00 24.45 ? 132 PRO A O   1 
ATOM   956  C CB  . PRO A 1 152 ? -9.974  -21.383 3.870   1.00 28.67 ? 132 PRO A CB  1 
ATOM   957  C CG  . PRO A 1 152 ? -10.852 -20.840 4.966   1.00 28.30 ? 132 PRO A CG  1 
ATOM   958  C CD  . PRO A 1 152 ? -10.310 -19.454 5.258   1.00 29.08 ? 132 PRO A CD  1 
ATOM   959  N N   . SER A 1 153 ? -8.064  -18.975 2.524   1.00 23.19 ? 133 SER A N   1 
ATOM   960  C CA  . SER A 1 153 ? -7.372  -18.299 1.391   1.00 23.53 ? 133 SER A CA  1 
ATOM   961  C C   . SER A 1 153 ? -5.860  -18.220 1.646   1.00 22.39 ? 133 SER A C   1 
ATOM   962  O O   . SER A 1 153 ? -5.150  -17.951 0.708   1.00 23.56 ? 133 SER A O   1 
ATOM   963  C CB  . SER A 1 153 ? -7.934  -16.918 1.126   1.00 24.59 ? 133 SER A CB  1 
ATOM   964  O OG  . SER A 1 153 ? -7.824  -16.086 2.282   1.00 24.79 ? 133 SER A OG  1 
ATOM   965  N N   . SER A 1 154 ? -5.401  -18.413 2.883   1.00 22.87 ? 134 SER A N   1 
ATOM   966  C CA  . SER A 1 154 ? -3.963  -18.372 3.280   1.00 20.93 ? 134 SER A CA  1 
ATOM   967  C C   . SER A 1 154 ? -3.323  -19.740 3.062   1.00 21.37 ? 134 SER A C   1 
ATOM   968  O O   . SER A 1 154 ? -3.767  -20.720 3.707   1.00 24.47 ? 134 SER A O   1 
ATOM   969  C CB  . SER A 1 154 ? -3.825  -17.936 4.686   1.00 18.52 ? 134 SER A CB  1 
ATOM   970  O OG  . SER A 1 154 ? -4.101  -16.555 4.776   1.00 19.43 ? 134 SER A OG  1 
ATOM   971  N N   . VAL A 1 155 ? -2.317  -19.802 2.189   1.00 21.98 ? 135 VAL A N   1 
ATOM   972  C CA  . VAL A 1 155 ? -1.719  -21.076 1.697   1.00 20.44 ? 135 VAL A CA  1 
ATOM   973  C C   . VAL A 1 155 ? -0.346  -21.267 2.335   1.00 20.07 ? 135 VAL A C   1 
ATOM   974  O O   . VAL A 1 155 ? 0.445   -20.328 2.328   1.00 20.56 ? 135 VAL A O   1 
ATOM   975  C CB  . VAL A 1 155 ? -1.602  -21.124 0.160   1.00 21.78 ? 135 VAL A CB  1 
ATOM   976  C CG1 . VAL A 1 155 ? -1.079  -22.492 -0.316  1.00 21.48 ? 135 VAL A CG1 1 
ATOM   977  C CG2 . VAL A 1 155 ? -2.939  -20.785 -0.509  1.00 21.11 ? 135 VAL A CG2 1 
ATOM   978  N N   . THR A 1 156 ? -0.099  -22.471 2.851   1.00 17.30 ? 136 THR A N   1 
ATOM   979  C CA  . THR A 1 156 ? 1.214   -22.925 3.320   1.00 16.80 ? 136 THR A CA  1 
ATOM   980  C C   . THR A 1 156 ? 1.648   -24.118 2.469   1.00 16.54 ? 136 THR A C   1 
ATOM   981  O O   . THR A 1 156 ? 0.961   -25.145 2.520   1.00 15.58 ? 136 THR A O   1 
ATOM   982  C CB  . THR A 1 156 ? 1.155   -23.253 4.810   1.00 16.07 ? 136 THR A CB  1 
ATOM   983  O OG1 . THR A 1 156 ? 0.821   -22.015 5.447   1.00 15.75 ? 136 THR A OG1 1 
ATOM   984  C CG2 . THR A 1 156 ? 2.458   -23.845 5.312   1.00 15.88 ? 136 THR A CG2 1 
ATOM   985  N N   . LEU A 1 157 ? 2.800   -24.015 1.814   1.00 16.77 ? 137 LEU A N   1 
ATOM   986  C CA  . LEU A 1 157 ? 3.435   -25.179 1.142   1.00 17.17 ? 137 LEU A CA  1 
ATOM   987  C C   . LEU A 1 157 ? 4.060   -26.082 2.201   1.00 17.29 ? 137 LEU A C   1 
ATOM   988  O O   . LEU A 1 157 ? 4.790   -25.585 3.091   1.00 18.15 ? 137 LEU A O   1 
ATOM   989  C CB  . LEU A 1 157 ? 4.497   -24.744 0.136   1.00 17.01 ? 137 LEU A CB  1 
ATOM   990  C CG  . LEU A 1 157 ? 4.140   -23.580 -0.784  1.00 17.45 ? 137 LEU A CG  1 
ATOM   991  C CD1 . LEU A 1 157 ? 5.276   -23.318 -1.747  1.00 18.90 ? 137 LEU A CD1 1 
ATOM   992  C CD2 . LEU A 1 157 ? 2.861   -23.839 -1.542  1.00 18.16 ? 137 LEU A CD2 1 
ATOM   993  N N   . ILE A 1 158 ? 3.864   -27.380 2.036   1.00 17.82 ? 138 ILE A N   1 
ATOM   994  C CA  . ILE A 1 158 ? 4.403   -28.420 2.956   1.00 17.36 ? 138 ILE A CA  1 
ATOM   995  C C   . ILE A 1 158 ? 5.250   -29.361 2.113   1.00 17.39 ? 138 ILE A C   1 
ATOM   996  O O   . ILE A 1 158 ? 4.787   -29.748 1.040   1.00 19.26 ? 138 ILE A O   1 
ATOM   997  C CB  . ILE A 1 158 ? 3.246   -29.155 3.667   1.00 17.31 ? 138 ILE A CB  1 
ATOM   998  C CG1 . ILE A 1 158 ? 2.334   -28.179 4.415   1.00 17.38 ? 138 ILE A CG1 1 
ATOM   999  C CG2 . ILE A 1 158 ? 3.784   -30.264 4.558   1.00 17.40 ? 138 ILE A CG2 1 
ATOM   1000 C CD1 . ILE A 1 158 ? 2.953   -27.584 5.658   1.00 18.48 ? 138 ILE A CD1 1 
ATOM   1001 N N   . SER A 1 159 ? 6.464   -29.685 2.555   1.00 16.52 ? 139 SER A N   1 
ATOM   1002 C CA  . SER A 1 159 ? 7.277   -30.750 1.927   1.00 15.84 ? 139 SER A CA  1 
ATOM   1003 C C   . SER A 1 159 ? 7.698   -31.754 3.002   1.00 16.00 ? 139 SER A C   1 
ATOM   1004 O O   . SER A 1 159 ? 7.831   -31.364 4.151   1.00 15.78 ? 139 SER A O   1 
ATOM   1005 C CB  . SER A 1 159 ? 8.431   -30.151 1.200   1.00 15.42 ? 139 SER A CB  1 
ATOM   1006 O OG  . SER A 1 159 ? 9.195   -29.330 2.064   1.00 13.69 ? 139 SER A OG  1 
ATOM   1007 N N   . GLY A 1 160 ? 7.861   -33.021 2.636   1.00 16.84 ? 140 GLY A N   1 
ATOM   1008 C CA  . GLY A 1 160 ? 8.117   -34.108 3.595   1.00 16.94 ? 140 GLY A CA  1 
ATOM   1009 C C   . GLY A 1 160 ? 7.258   -35.333 3.323   1.00 17.77 ? 140 GLY A C   1 
ATOM   1010 O O   . GLY A 1 160 ? 6.377   -35.313 2.465   1.00 17.39 ? 140 GLY A O   1 
ATOM   1011 N N   . PRO A 1 161 ? 7.496   -36.425 4.084   1.00 21.04 ? 141 PRO A N   1 
ATOM   1012 C CA  . PRO A 1 161 ? 6.735   -37.668 3.950   1.00 22.43 ? 141 PRO A CA  1 
ATOM   1013 C C   . PRO A 1 161 ? 5.219   -37.441 3.807   1.00 22.54 ? 141 PRO A C   1 
ATOM   1014 O O   . PRO A 1 161 ? 4.618   -36.844 4.694   1.00 21.14 ? 141 PRO A O   1 
ATOM   1015 C CB  . PRO A 1 161 ? 7.071   -38.360 5.270   1.00 22.63 ? 141 PRO A CB  1 
ATOM   1016 C CG  . PRO A 1 161 ? 8.502   -37.976 5.500   1.00 22.68 ? 141 PRO A CG  1 
ATOM   1017 C CD  . PRO A 1 161 ? 8.522   -36.507 5.136   1.00 21.45 ? 141 PRO A CD  1 
ATOM   1018 N N   . LYS A 1 162 ? 4.636   -37.907 2.699   1.00 23.27 ? 142 LYS A N   1 
ATOM   1019 C CA  . LYS A 1 162 ? 3.193   -37.697 2.410   1.00 25.13 ? 142 LYS A CA  1 
ATOM   1020 C C   . LYS A 1 162 ? 2.353   -38.300 3.542   1.00 22.95 ? 142 LYS A C   1 
ATOM   1021 O O   . LYS A 1 162 ? 1.328   -37.689 3.873   1.00 21.73 ? 142 LYS A O   1 
ATOM   1022 C CB  . LYS A 1 162 ? 2.740   -38.257 1.060   1.00 28.54 ? 142 LYS A CB  1 
ATOM   1023 C CG  . LYS A 1 162 ? 1.344   -37.787 0.659   1.00 32.05 ? 142 LYS A CG  1 
ATOM   1024 C CD  . LYS A 1 162 ? 0.956   -38.105 -0.756  1.00 37.15 ? 142 LYS A CD  1 
ATOM   1025 C CE  . LYS A 1 162 ? 1.446   -37.089 -1.768  1.00 41.35 ? 142 LYS A CE  1 
ATOM   1026 N NZ  . LYS A 1 162 ? 0.612   -35.863 -1.794  1.00 44.89 ? 142 LYS A NZ  1 
ATOM   1027 N N   . THR A 1 163 ? 2.759   -39.427 4.142   1.00 21.55 ? 143 THR A N   1 
ATOM   1028 C CA  . THR A 1 163 ? 2.005   -40.023 5.281   1.00 22.15 ? 143 THR A CA  1 
ATOM   1029 C C   . THR A 1 163 ? 2.014   -39.069 6.488   1.00 21.79 ? 143 THR A C   1 
ATOM   1030 O O   . THR A 1 163 ? 0.979   -38.971 7.137   1.00 21.92 ? 143 THR A O   1 
ATOM   1031 C CB  . THR A 1 163 ? 2.509   -41.419 5.672   1.00 24.49 ? 143 THR A CB  1 
ATOM   1032 O OG1 . THR A 1 163 ? 3.836   -41.267 6.169   1.00 27.76 ? 143 THR A OG1 1 
ATOM   1033 C CG2 . THR A 1 163 ? 2.476   -42.395 4.519   1.00 25.98 ? 143 THR A CG2 1 
ATOM   1034 N N   . ALA A 1 164 ? 3.124   -38.385 6.790   1.00 21.92 ? 144 ALA A N   1 
ATOM   1035 C CA  . ALA A 1 164 ? 3.190   -37.419 7.916   1.00 22.54 ? 144 ALA A CA  1 
ATOM   1036 C C   . ALA A 1 164 ? 2.294   -36.217 7.612   1.00 21.31 ? 144 ALA A C   1 
ATOM   1037 O O   . ALA A 1 164 ? 1.489   -35.844 8.493   1.00 21.78 ? 144 ALA A O   1 
ATOM   1038 C CB  . ALA A 1 164 ? 4.611   -36.998 8.201   1.00 25.06 ? 144 ALA A CB  1 
ATOM   1039 N N   . TYR A 1 165 ? 2.406   -35.653 6.405   1.00 22.40 ? 145 TYR A N   1 
ATOM   1040 C CA  . TYR A 1 165 ? 1.484   -34.613 5.868   1.00 22.80 ? 145 TYR A CA  1 
ATOM   1041 C C   . TYR A 1 165 ? 0.018   -35.020 6.108   1.00 24.40 ? 145 TYR A C   1 
ATOM   1042 O O   . TYR A 1 165 ? -0.741  -34.250 6.733   1.00 23.37 ? 145 TYR A O   1 
ATOM   1043 C CB  . TYR A 1 165 ? 1.702   -34.361 4.371   1.00 22.93 ? 145 TYR A CB  1 
ATOM   1044 C CG  . TYR A 1 165 ? 0.665   -33.423 3.808   1.00 22.90 ? 145 TYR A CG  1 
ATOM   1045 C CD1 . TYR A 1 165 ? 0.526   -32.162 4.362   1.00 22.38 ? 145 TYR A CD1 1 
ATOM   1046 C CD2 . TYR A 1 165 ? -0.249  -33.818 2.844   1.00 22.93 ? 145 TYR A CD2 1 
ATOM   1047 C CE1 . TYR A 1 165 ? -0.439  -31.287 3.923   1.00 23.40 ? 145 TYR A CE1 1 
ATOM   1048 C CE2 . TYR A 1 165 ? -1.239  -32.952 2.400   1.00 23.28 ? 145 TYR A CE2 1 
ATOM   1049 C CZ  . TYR A 1 165 ? -1.325  -31.681 2.946   1.00 22.40 ? 145 TYR A CZ  1 
ATOM   1050 O OH  . TYR A 1 165 ? -2.251  -30.769 2.571   1.00 23.43 ? 145 TYR A OH  1 
ATOM   1051 N N   . GLU A 1 166 ? -0.378  -36.204 5.630   1.00 26.64 ? 146 GLU A N   1 
ATOM   1052 C CA  . GLU A 1 166 ? -1.784  -36.703 5.736   1.00 27.49 ? 146 GLU A CA  1 
ATOM   1053 C C   . GLU A 1 166 ? -2.246  -36.695 7.203   1.00 24.29 ? 146 GLU A C   1 
ATOM   1054 O O   . GLU A 1 166 ? -3.355  -36.194 7.457   1.00 22.16 ? 146 GLU A O   1 
ATOM   1055 C CB  . GLU A 1 166 ? -1.928  -38.109 5.172   1.00 30.99 ? 146 GLU A CB  1 
ATOM   1056 C CG  . GLU A 1 166 ? -1.540  -38.226 3.716   1.00 36.89 ? 146 GLU A CG  1 
ATOM   1057 C CD  . GLU A 1 166 ? -2.647  -37.951 2.723   1.00 40.68 ? 146 GLU A CD  1 
ATOM   1058 O OE1 . GLU A 1 166 ? -3.037  -38.914 2.035   1.00 42.57 ? 146 GLU A OE1 1 
ATOM   1059 O OE2 . GLU A 1 166 ? -3.092  -36.773 2.628   1.00 40.79 ? 146 GLU A OE2 1 
ATOM   1060 N N   . SER A 1 167 ? -1.422  -37.215 8.119   1.00 22.55 ? 147 SER A N   1 
ATOM   1061 C CA  . SER A 1 167 ? -1.713  -37.295 9.577   1.00 22.89 ? 147 SER A CA  1 
ATOM   1062 C C   . SER A 1 167 ? -1.895  -35.902 10.193  1.00 22.74 ? 147 SER A C   1 
ATOM   1063 O O   . SER A 1 167 ? -2.686  -35.783 11.151  1.00 23.59 ? 147 SER A O   1 
ATOM   1064 C CB  . SER A 1 167 ? -0.649  -38.045 10.301  1.00 22.56 ? 147 SER A CB  1 
ATOM   1065 O OG  . SER A 1 167 ? -0.754  -39.419 10.020  1.00 24.39 ? 147 SER A OG  1 
ATOM   1066 N N   . GLN A 1 168 ? -1.185  -34.894 9.688   1.00 22.58 ? 148 GLN A N   1 
ATOM   1067 C CA  . GLN A 1 168 ? -1.109  -33.548 10.317  1.00 24.03 ? 148 GLN A CA  1 
ATOM   1068 C C   . GLN A 1 168 ? -2.046  -32.583 9.600   1.00 24.95 ? 148 GLN A C   1 
ATOM   1069 O O   . GLN A 1 168 ? -2.074  -31.398 9.974   1.00 22.54 ? 148 GLN A O   1 
ATOM   1070 C CB  . GLN A 1 168 ? 0.332   -33.026 10.257  1.00 24.68 ? 148 GLN A CB  1 
ATOM   1071 C CG  . GLN A 1 168 ? 1.314   -33.867 11.067  1.00 24.36 ? 148 GLN A CG  1 
ATOM   1072 C CD  . GLN A 1 168 ? 0.917   -33.915 12.521  1.00 23.29 ? 148 GLN A CD  1 
ATOM   1073 O OE1 . GLN A 1 168 ? 0.360   -32.968 13.076  1.00 23.53 ? 148 GLN A OE1 1 
ATOM   1074 N NE2 . GLN A 1 168 ? 1.183   -35.039 13.148  1.00 24.30 ? 148 GLN A NE2 1 
ATOM   1075 N N   . LYS A 1 169 ? -2.790  -33.078 8.609   1.00 26.82 ? 149 LYS A N   1 
ATOM   1076 C CA  . LYS A 1 169 ? -3.589  -32.227 7.697   1.00 26.06 ? 149 LYS A CA  1 
ATOM   1077 C C   . LYS A 1 169 ? -4.635  -31.470 8.514   1.00 24.90 ? 149 LYS A C   1 
ATOM   1078 O O   . LYS A 1 169 ? -4.766  -30.223 8.344   1.00 23.61 ? 149 LYS A O   1 
ATOM   1079 C CB  . LYS A 1 169 ? -4.196  -33.115 6.615   1.00 29.55 ? 149 LYS A CB  1 
ATOM   1080 C CG  . LYS A 1 169 ? -5.106  -32.410 5.626   1.00 32.86 ? 149 LYS A CG  1 
ATOM   1081 C CD  . LYS A 1 169 ? -4.379  -31.915 4.419   1.00 34.71 ? 149 LYS A CD  1 
ATOM   1082 C CE  . LYS A 1 169 ? -5.267  -31.808 3.197   1.00 35.69 ? 149 LYS A CE  1 
ATOM   1083 N NZ  . LYS A 1 169 ? -4.798  -30.704 2.327   1.00 38.63 ? 149 LYS A NZ  1 
ATOM   1084 N N   . GLU A 1 170 ? -5.386  -32.179 9.351   1.00 25.45 ? 150 GLU A N   1 
ATOM   1085 C CA  . GLU A 1 170 ? -6.484  -31.545 10.118  1.00 26.27 ? 150 GLU A CA  1 
ATOM   1086 C C   . GLU A 1 170 ? -5.863  -30.475 11.011  1.00 25.31 ? 150 GLU A C   1 
ATOM   1087 O O   . GLU A 1 170 ? -6.390  -29.335 11.018  1.00 24.75 ? 150 GLU A O   1 
ATOM   1088 C CB  . GLU A 1 170 ? -7.293  -32.531 10.966  1.00 29.76 ? 150 GLU A CB  1 
ATOM   1089 C CG  . GLU A 1 170 ? -8.352  -31.818 11.806  1.00 33.50 ? 150 GLU A CG  1 
ATOM   1090 C CD  . GLU A 1 170 ? -9.406  -32.684 12.487  1.00 41.08 ? 150 GLU A CD  1 
ATOM   1091 O OE1 . GLU A 1 170 ? -10.605 -32.266 12.499  1.00 42.39 ? 150 GLU A OE1 1 
ATOM   1092 O OE2 . GLU A 1 170 ? -9.038  -33.773 13.010  1.00 43.77 ? 150 GLU A OE2 1 
ATOM   1093 N N   . LEU A 1 171 ? -4.804  -30.833 11.756  1.00 24.27 ? 151 LEU A N   1 
ATOM   1094 C CA  . LEU A 1 171 ? -4.122  -29.883 12.666  1.00 22.93 ? 151 LEU A CA  1 
ATOM   1095 C C   . LEU A 1 171 ? -3.697  -28.660 11.841  1.00 22.08 ? 151 LEU A C   1 
ATOM   1096 O O   . LEU A 1 171 ? -3.923  -27.503 12.315  1.00 20.07 ? 151 LEU A O   1 
ATOM   1097 C CB  . LEU A 1 171 ? -2.914  -30.541 13.343  1.00 24.41 ? 151 LEU A CB  1 
ATOM   1098 C CG  . LEU A 1 171 ? -2.017  -29.570 14.112  1.00 24.81 ? 151 LEU A CG  1 
ATOM   1099 C CD1 . LEU A 1 171 ? -2.794  -28.881 15.226  1.00 26.14 ? 151 LEU A CD1 1 
ATOM   1100 C CD2 . LEU A 1 171 ? -0.806  -30.277 14.678  1.00 25.73 ? 151 LEU A CD2 1 
ATOM   1101 N N   . LEU A 1 172 ? -3.135  -28.898 10.646  1.00 20.06 ? 152 LEU A N   1 
ATOM   1102 C CA  . LEU A 1 172 ? -2.571  -27.823 9.783   1.00 20.72 ? 152 LEU A CA  1 
ATOM   1103 C C   . LEU A 1 172 ? -3.690  -26.929 9.221   1.00 19.24 ? 152 LEU A C   1 
ATOM   1104 O O   . LEU A 1 172 ? -3.441  -25.734 8.982   1.00 17.48 ? 152 LEU A O   1 
ATOM   1105 C CB  . LEU A 1 172 ? -1.711  -28.445 8.678   1.00 20.84 ? 152 LEU A CB  1 
ATOM   1106 C CG  . LEU A 1 172 ? -0.318  -28.916 9.117   1.00 21.47 ? 152 LEU A CG  1 
ATOM   1107 C CD1 . LEU A 1 172 ? 0.302   -29.813 8.063   1.00 22.50 ? 152 LEU A CD1 1 
ATOM   1108 C CD2 . LEU A 1 172 ? 0.602   -27.758 9.410   1.00 21.88 ? 152 LEU A CD2 1 
ATOM   1109 N N   . SER A 1 173 ? -4.903  -27.451 9.057   1.00 19.67 ? 153 SER A N   1 
ATOM   1110 C CA  . SER A 1 173 ? -6.050  -26.660 8.550   1.00 20.03 ? 153 SER A CA  1 
ATOM   1111 C C   . SER A 1 173 ? -6.330  -25.476 9.491   1.00 19.74 ? 153 SER A C   1 
ATOM   1112 O O   . SER A 1 173 ? -6.930  -24.507 9.028   1.00 19.99 ? 153 SER A O   1 
ATOM   1113 C CB  . SER A 1 173 ? -7.278  -27.517 8.322   1.00 21.65 ? 153 SER A CB  1 
ATOM   1114 O OG  . SER A 1 173 ? -7.940  -27.747 9.545   1.00 22.69 ? 153 SER A OG  1 
ATOM   1115 N N   . SER A 1 174 ? -5.854  -25.517 10.743  1.00 19.98 ? 154 SER A N   1 
ATOM   1116 C CA  . SER A 1 174 ? -5.882  -24.386 11.714  1.00 20.37 ? 154 SER A CA  1 
ATOM   1117 C C   . SER A 1 174 ? -5.264  -23.105 11.140  1.00 17.87 ? 154 SER A C   1 
ATOM   1118 O O   . SER A 1 174 ? -5.708  -22.056 11.560  1.00 15.55 ? 154 SER A O   1 
ATOM   1119 C CB  . SER A 1 174 ? -5.159  -24.738 12.988  1.00 22.66 ? 154 SER A CB  1 
ATOM   1120 O OG  . SER A 1 174 ? -5.619  -25.978 13.482  1.00 27.37 ? 154 SER A OG  1 
ATOM   1121 N N   . ILE A 1 175 ? -4.228  -23.188 10.286  1.00 17.22 ? 155 ILE A N   1 
ATOM   1122 C CA  . ILE A 1 175 ? -3.455  -22.003 9.806   1.00 16.69 ? 155 ILE A CA  1 
ATOM   1123 C C   . ILE A 1 175 ? -3.850  -21.677 8.370   1.00 17.30 ? 155 ILE A C   1 
ATOM   1124 O O   . ILE A 1 175 ? -3.282  -20.721 7.821   1.00 16.48 ? 155 ILE A O   1 
ATOM   1125 C CB  . ILE A 1 175 ? -1.927  -22.171 9.938   1.00 16.29 ? 155 ILE A CB  1 
ATOM   1126 C CG1 . ILE A 1 175 ? -1.331  -23.252 9.030   1.00 16.79 ? 155 ILE A CG1 1 
ATOM   1127 C CG2 . ILE A 1 175 ? -1.563  -22.403 11.389  1.00 17.38 ? 155 ILE A CG2 1 
ATOM   1128 C CD1 . ILE A 1 175 ? 0.200   -23.348 9.127   1.00 16.98 ? 155 ILE A CD1 1 
ATOM   1129 N N   . GLY A 1 176 ? -4.814  -22.409 7.820   1.00 18.30 ? 156 GLY A N   1 
ATOM   1130 C CA  . GLY A 1 176 ? -5.454  -22.111 6.526   1.00 18.70 ? 156 GLY A CA  1 
ATOM   1131 C C   . GLY A 1 176 ? -5.366  -23.311 5.617   1.00 19.77 ? 156 GLY A C   1 
ATOM   1132 O O   . GLY A 1 176 ? -5.561  -24.430 6.114   1.00 19.80 ? 156 GLY A O   1 
ATOM   1133 N N   . THR A 1 177 ? -5.064  -23.082 4.342   1.00 20.53 ? 157 THR A N   1 
ATOM   1134 C CA  . THR A 1 177 ? -5.041  -24.132 3.302   1.00 22.24 ? 157 THR A CA  1 
ATOM   1135 C C   . THR A 1 177 ? -3.581  -24.569 3.151   1.00 22.86 ? 157 THR A C   1 
ATOM   1136 O O   . THR A 1 177 ? -2.720  -23.685 3.039   1.00 21.72 ? 157 THR A O   1 
ATOM   1137 C CB  . THR A 1 177 ? -5.713  -23.638 2.013   1.00 24.44 ? 157 THR A CB  1 
ATOM   1138 O OG1 . THR A 1 177 ? -5.470  -24.577 0.970   1.00 28.32 ? 157 THR A OG1 1 
ATOM   1139 C CG2 . THR A 1 177 ? -5.172  -22.329 1.493   1.00 28.30 ? 157 THR A CG2 1 
ATOM   1140 N N   . THR A 1 178 ? -3.306  -25.874 3.188   1.00 21.89 ? 158 THR A N   1 
ATOM   1141 C CA  . THR A 1 178 ? -1.951  -26.418 2.951   1.00 22.95 ? 158 THR A CA  1 
ATOM   1142 C C   . THR A 1 178 ? -1.933  -27.095 1.583   1.00 23.77 ? 158 THR A C   1 
ATOM   1143 O O   . THR A 1 178 ? -2.987  -27.572 1.138   1.00 22.56 ? 158 THR A O   1 
ATOM   1144 C CB  . THR A 1 178 ? -1.499  -27.368 4.063   1.00 23.71 ? 158 THR A CB  1 
ATOM   1145 O OG1 . THR A 1 178 ? -2.365  -28.500 4.061   1.00 23.15 ? 158 THR A OG1 1 
ATOM   1146 C CG2 . THR A 1 178 ? -1.482  -26.693 5.420   1.00 24.07 ? 158 THR A CG2 1 
ATOM   1147 N N   . ARG A 1 179 ? -0.764  -27.105 0.955   1.00 23.39 ? 159 ARG A N   1 
ATOM   1148 C CA  . ARG A 1 179 ? -0.526  -27.725 -0.366  1.00 25.23 ? 159 ARG A CA  1 
ATOM   1149 C C   . ARG A 1 179 ? 0.734   -28.562 -0.230  1.00 24.35 ? 159 ARG A C   1 
ATOM   1150 O O   . ARG A 1 179 ? 1.825   -27.951 -0.055  1.00 22.15 ? 159 ARG A O   1 
ATOM   1151 C CB  . ARG A 1 179 ? -0.371  -26.644 -1.436  1.00 28.36 ? 159 ARG A CB  1 
ATOM   1152 C CG  . ARG A 1 179 ? 0.026   -27.145 -2.816  1.00 32.66 ? 159 ARG A CG  1 
ATOM   1153 C CD  . ARG A 1 179 ? 0.372   -25.955 -3.695  1.00 38.37 ? 159 ARG A CD  1 
ATOM   1154 N NE  . ARG A 1 179 ? -0.168  -26.037 -5.038  1.00 42.11 ? 159 ARG A NE  1 
ATOM   1155 C CZ  . ARG A 1 179 ? 0.368   -26.716 -6.047  1.00 45.38 ? 159 ARG A CZ  1 
ATOM   1156 N NH1 . ARG A 1 179 ? -0.238  -26.702 -7.222  1.00 49.07 ? 159 ARG A NH1 1 
ATOM   1157 N NH2 . ARG A 1 179 ? 1.487   -27.408 -5.900  1.00 46.95 ? 159 ARG A NH2 1 
ATOM   1158 N N   . HIS A 1 180 ? 0.594   -29.885 -0.283  1.00 22.84 ? 160 HIS A N   1 
ATOM   1159 C CA  . HIS A 1 180 ? 1.758   -30.805 -0.248  1.00 25.48 ? 160 HIS A CA  1 
ATOM   1160 C C   . HIS A 1 180 ? 2.482   -30.725 -1.589  1.00 26.14 ? 160 HIS A C   1 
ATOM   1161 O O   . HIS A 1 180 ? 1.898   -31.174 -2.580  1.00 27.54 ? 160 HIS A O   1 
ATOM   1162 C CB  . HIS A 1 180 ? 1.328   -32.226 0.116   1.00 24.36 ? 160 HIS A CB  1 
ATOM   1163 C CG  . HIS A 1 180 ? 2.485   -33.151 0.273   1.00 23.72 ? 160 HIS A CG  1 
ATOM   1164 N ND1 . HIS A 1 180 ? 2.798   -34.100 -0.672  1.00 24.89 ? 160 HIS A ND1 1 
ATOM   1165 C CD2 . HIS A 1 180 ? 3.410   -33.265 1.242   1.00 23.73 ? 160 HIS A CD2 1 
ATOM   1166 C CE1 . HIS A 1 180 ? 3.862   -34.767 -0.277  1.00 25.35 ? 160 HIS A CE1 1 
ATOM   1167 N NE2 . HIS A 1 180 ? 4.242   -34.292 0.899   1.00 24.32 ? 160 HIS A NE2 1 
ATOM   1168 N N   . VAL A 1 181 ? 3.693   -30.162 -1.623  1.00 25.72 ? 161 VAL A N   1 
ATOM   1169 C CA  . VAL A 1 181 ? 4.407   -29.889 -2.909  1.00 25.48 ? 161 VAL A CA  1 
ATOM   1170 C C   . VAL A 1 181 ? 5.362   -31.035 -3.249  1.00 26.79 ? 161 VAL A C   1 
ATOM   1171 O O   . VAL A 1 181 ? 5.679   -31.181 -4.447  1.00 26.27 ? 161 VAL A O   1 
ATOM   1172 C CB  . VAL A 1 181 ? 5.153   -28.544 -2.900  1.00 25.76 ? 161 VAL A CB  1 
ATOM   1173 C CG1 . VAL A 1 181 ? 4.180   -27.375 -2.903  1.00 25.38 ? 161 VAL A CG1 1 
ATOM   1174 C CG2 . VAL A 1 181 ? 6.160   -28.439 -1.757  1.00 25.71 ? 161 VAL A CG2 1 
ATOM   1175 N N   . SER A 1 182 ? 5.816   -31.810 -2.260  1.00 24.96 ? 162 SER A N   1 
ATOM   1176 C CA  . SER A 1 182 ? 6.881   -32.822 -2.466  1.00 23.86 ? 162 SER A CA  1 
ATOM   1177 C C   . SER A 1 182 ? 7.118   -33.669 -1.209  1.00 23.79 ? 162 SER A C   1 
ATOM   1178 O O   . SER A 1 182 ? 6.956   -33.131 -0.091  1.00 20.33 ? 162 SER A O   1 
ATOM   1179 C CB  . SER A 1 182 ? 8.140   -32.135 -2.890  1.00 23.00 ? 162 SER A CB  1 
ATOM   1180 O OG  . SER A 1 182 ? 9.168   -33.078 -3.093  1.00 21.47 ? 162 SER A OG  1 
ATOM   1181 N N   . ASP A 1 183 ? 7.524   -34.934 -1.401  1.00 23.97 ? 163 ASP A N   1 
ATOM   1182 C CA  . ASP A 1 183 ? 7.993   -35.841 -0.315  1.00 25.39 ? 163 ASP A CA  1 
ATOM   1183 C C   . ASP A 1 183 ? 9.405   -35.420 0.141   1.00 21.55 ? 163 ASP A C   1 
ATOM   1184 O O   . ASP A 1 183 ? 9.796   -35.787 1.253   1.00 20.11 ? 163 ASP A O   1 
ATOM   1185 C CB  . ASP A 1 183 ? 7.897   -37.322 -0.710  1.00 28.32 ? 163 ASP A CB  1 
ATOM   1186 C CG  . ASP A 1 183 ? 6.514   -37.925 -0.474  1.00 33.40 ? 163 ASP A CG  1 
ATOM   1187 O OD1 . ASP A 1 183 ? 5.524   -37.320 -0.934  1.00 34.74 ? 163 ASP A OD1 1 
ATOM   1188 O OD2 . ASP A 1 183 ? 6.424   -38.990 0.196   1.00 41.02 ? 163 ASP A OD2 1 
ATOM   1189 N N   . ASP A 1 184 ? 10.144  -34.656 -0.656  1.00 20.26 ? 164 ASP A N   1 
ATOM   1190 C CA  . ASP A 1 184 ? 11.493  -34.151 -0.264  1.00 20.44 ? 164 ASP A CA  1 
ATOM   1191 C C   . ASP A 1 184 ? 11.320  -32.954 0.691   1.00 19.72 ? 164 ASP A C   1 
ATOM   1192 O O   . ASP A 1 184 ? 10.751  -31.923 0.244   1.00 17.73 ? 164 ASP A O   1 
ATOM   1193 C CB  . ASP A 1 184 ? 12.282  -33.777 -1.513  1.00 22.10 ? 164 ASP A CB  1 
ATOM   1194 C CG  . ASP A 1 184 ? 13.642  -33.140 -1.286  1.00 22.28 ? 164 ASP A CG  1 
ATOM   1195 O OD1 . ASP A 1 184 ? 13.969  -32.782 -0.139  1.00 23.92 ? 164 ASP A OD1 1 
ATOM   1196 O OD2 . ASP A 1 184 ? 14.373  -33.014 -2.282  1.00 25.64 ? 164 ASP A OD2 1 
ATOM   1197 N N   . ILE A 1 185 ? 11.808  -33.069 1.932   1.00 18.29 ? 165 ILE A N   1 
ATOM   1198 C CA  . ILE A 1 185 ? 11.673  -32.042 3.010   1.00 20.93 ? 165 ILE A CA  1 
ATOM   1199 C C   . ILE A 1 185 ? 12.255  -30.674 2.582   1.00 20.99 ? 165 ILE A C   1 
ATOM   1200 O O   . ILE A 1 185 ? 11.763  -29.674 3.106   1.00 18.67 ? 165 ILE A O   1 
ATOM   1201 C CB  . ILE A 1 185 ? 12.296  -32.563 4.321   1.00 22.84 ? 165 ILE A CB  1 
ATOM   1202 C CG1 . ILE A 1 185 ? 13.799  -32.823 4.175   1.00 25.45 ? 165 ILE A CG1 1 
ATOM   1203 C CG2 . ILE A 1 185 ? 11.549  -33.808 4.815   1.00 23.01 ? 165 ILE A CG2 1 
ATOM   1204 C CD1 . ILE A 1 185 ? 14.682  -31.648 4.526   1.00 27.66 ? 165 ILE A CD1 1 
ATOM   1205 N N   . ALA A 1 186 ? 13.266  -30.618 1.696   1.00 20.64 ? 166 ALA A N   1 
ATOM   1206 C CA  . ALA A 1 186 ? 13.934  -29.374 1.221   1.00 21.11 ? 166 ALA A CA  1 
ATOM   1207 C C   . ALA A 1 186 ? 13.082  -28.559 0.231   1.00 21.42 ? 166 ALA A C   1 
ATOM   1208 O O   . ALA A 1 186 ? 13.465  -27.402 -0.047  1.00 23.59 ? 166 ALA A O   1 
ATOM   1209 C CB  . ALA A 1 186 ? 15.249  -29.710 0.558   1.00 22.67 ? 166 ALA A CB  1 
ATOM   1210 N N   . LYS A 1 187 ? 11.999  -29.110 -0.315  1.00 22.19 ? 167 LYS A N   1 
ATOM   1211 C CA  . LYS A 1 187 ? 11.309  -28.515 -1.490  1.00 23.63 ? 167 LYS A CA  1 
ATOM   1212 C C   . LYS A 1 187 ? 10.489  -27.265 -1.116  1.00 19.89 ? 167 LYS A C   1 
ATOM   1213 O O   . LYS A 1 187 ? 10.475  -26.341 -1.913  1.00 18.20 ? 167 LYS A O   1 
ATOM   1214 C CB  . LYS A 1 187 ? 10.419  -29.550 -2.179  1.00 27.35 ? 167 LYS A CB  1 
ATOM   1215 C CG  . LYS A 1 187 ? 10.076  -29.215 -3.626  1.00 31.59 ? 167 LYS A CG  1 
ATOM   1216 C CD  . LYS A 1 187 ? 11.259  -29.351 -4.570  1.00 34.21 ? 167 LYS A CD  1 
ATOM   1217 C CE  . LYS A 1 187 ? 11.702  -30.789 -4.754  1.00 37.56 ? 167 LYS A CE  1 
ATOM   1218 N NZ  . LYS A 1 187 ? 13.064  -30.861 -5.329  1.00 37.66 ? 167 LYS A NZ  1 
ATOM   1219 N N   . ALA A 1 188 ? 9.800   -27.242 0.019   1.00 18.26 ? 168 ALA A N   1 
ATOM   1220 C CA  . ALA A 1 188 ? 8.993   -26.077 0.444   1.00 18.13 ? 168 ALA A CA  1 
ATOM   1221 C C   . ALA A 1 188 ? 9.916   -24.858 0.460   1.00 17.43 ? 168 ALA A C   1 
ATOM   1222 O O   . ALA A 1 188 ? 9.547   -23.815 -0.091  1.00 17.47 ? 168 ALA A O   1 
ATOM   1223 C CB  . ALA A 1 188 ? 8.324   -26.333 1.781   1.00 18.60 ? 168 ALA A CB  1 
ATOM   1224 N N   . SER A 1 189 ? 11.115  -25.009 1.024   1.00 17.29 ? 169 SER A N   1 
ATOM   1225 C CA  . SER A 1 189 ? 12.126  -23.929 1.116   1.00 16.35 ? 169 SER A CA  1 
ATOM   1226 C C   . SER A 1 189 ? 12.647  -23.576 -0.279  1.00 16.10 ? 169 SER A C   1 
ATOM   1227 O O   . SER A 1 189 ? 12.816  -22.352 -0.557  1.00 16.22 ? 169 SER A O   1 
ATOM   1228 C CB  . SER A 1 189 ? 13.238  -24.301 2.068   1.00 16.78 ? 169 SER A CB  1 
ATOM   1229 O OG  . SER A 1 189 ? 12.730  -24.309 3.384   1.00 15.58 ? 169 SER A OG  1 
ATOM   1230 N N   . LEU A 1 190 ? 12.875  -24.566 -1.143  1.00 15.08 ? 170 LEU A N   1 
ATOM   1231 C CA  . LEU A 1 190 ? 13.369  -24.268 -2.520  1.00 15.12 ? 170 LEU A CA  1 
ATOM   1232 C C   . LEU A 1 190 ? 12.329  -23.389 -3.211  1.00 14.99 ? 170 LEU A C   1 
ATOM   1233 O O   . LEU A 1 190 ? 12.669  -22.301 -3.662  1.00 15.43 ? 170 LEU A O   1 
ATOM   1234 C CB  . LEU A 1 190 ? 13.585  -25.535 -3.339  1.00 15.09 ? 170 LEU A CB  1 
ATOM   1235 C CG  . LEU A 1 190 ? 13.921  -25.236 -4.802  1.00 15.31 ? 170 LEU A CG  1 
ATOM   1236 C CD1 . LEU A 1 190 ? 15.405  -24.914 -4.944  1.00 14.72 ? 170 LEU A CD1 1 
ATOM   1237 C CD2 . LEU A 1 190 ? 13.524  -26.387 -5.703  1.00 17.13 ? 170 LEU A CD2 1 
ATOM   1238 N N   . LEU A 1 191 ? 11.074  -23.835 -3.214  1.00 14.97 ? 171 LEU A N   1 
ATOM   1239 C CA  . LEU A 1 191 ? 10.006  -23.163 -3.985  1.00 14.61 ? 171 LEU A CA  1 
ATOM   1240 C C   . LEU A 1 191 ? 9.713   -21.789 -3.376  1.00 14.44 ? 171 LEU A C   1 
ATOM   1241 O O   . LEU A 1 191 ? 9.512   -20.836 -4.167  1.00 12.80 ? 171 LEU A O   1 
ATOM   1242 C CB  . LEU A 1 191 ? 8.774   -24.058 -4.040  1.00 15.03 ? 171 LEU A CB  1 
ATOM   1243 C CG  . LEU A 1 191 ? 8.984   -25.339 -4.838  1.00 16.03 ? 171 LEU A CG  1 
ATOM   1244 C CD1 . LEU A 1 191 ? 7.911   -26.347 -4.486  1.00 18.06 ? 171 LEU A CD1 1 
ATOM   1245 C CD2 . LEU A 1 191 ? 9.020   -25.073 -6.333  1.00 15.93 ? 171 LEU A CD2 1 
ATOM   1246 N N   . ASP A 1 192 ? 9.730   -21.681 -2.048  1.00 14.61 ? 172 ASP A N   1 
ATOM   1247 C CA  . ASP A 1 192 ? 9.396   -20.411 -1.360  1.00 15.48 ? 172 ASP A CA  1 
ATOM   1248 C C   . ASP A 1 192 ? 10.461  -19.361 -1.667  1.00 14.52 ? 172 ASP A C   1 
ATOM   1249 O O   . ASP A 1 192 ? 10.074  -18.243 -1.978  1.00 14.16 ? 172 ASP A O   1 
ATOM   1250 C CB  . ASP A 1 192 ? 9.154   -20.572 0.136   1.00 15.99 ? 172 ASP A CB  1 
ATOM   1251 C CG  . ASP A 1 192 ? 8.462   -19.353 0.737   1.00 16.96 ? 172 ASP A CG  1 
ATOM   1252 O OD1 . ASP A 1 192 ? 7.564   -18.788 0.073   1.00 17.13 ? 172 ASP A OD1 1 
ATOM   1253 O OD2 . ASP A 1 192 ? 8.792   -19.007 1.878   1.00 17.95 ? 172 ASP A OD2 1 
ATOM   1254 N N   . ASN A 1 193 ? 11.746  -19.716 -1.594  1.00 14.97 ? 173 ASN A N   1 
ATOM   1255 C CA  . ASN A 1 193 ? 12.855  -18.811 -1.968  1.00 15.39 ? 173 ASN A CA  1 
ATOM   1256 C C   . ASN A 1 193 ? 12.705  -18.397 -3.443  1.00 14.96 ? 173 ASN A C   1 
ATOM   1257 O O   . ASN A 1 193 ? 12.920  -17.205 -3.755  1.00 15.38 ? 173 ASN A O   1 
ATOM   1258 C CB  . ASN A 1 193 ? 14.222  -19.442 -1.703  1.00 16.81 ? 173 ASN A CB  1 
ATOM   1259 C CG  . ASN A 1 193 ? 14.679  -19.304 -0.265  1.00 20.07 ? 173 ASN A CG  1 
ATOM   1260 O OD1 . ASN A 1 193 ? 15.189  -18.251 0.121   1.00 24.75 ? 173 ASN A OD1 1 
ATOM   1261 N ND2 . ASN A 1 193 ? 14.520  -20.352 0.532   1.00 18.28 ? 173 ASN A ND2 1 
ATOM   1262 N N   . ALA A 1 194 ? 12.403  -19.324 -4.350  1.00 14.19 ? 174 ALA A N   1 
ATOM   1263 C CA  . ALA A 1 194 ? 12.157  -18.973 -5.768  1.00 15.13 ? 174 ALA A CA  1 
ATOM   1264 C C   . ALA A 1 194 ? 10.997  -17.974 -5.852  1.00 14.78 ? 174 ALA A C   1 
ATOM   1265 O O   . ALA A 1 194 ? 11.146  -16.955 -6.562  1.00 14.69 ? 174 ALA A O   1 
ATOM   1266 C CB  . ALA A 1 194 ? 11.882  -20.183 -6.611  1.00 15.75 ? 174 ALA A CB  1 
ATOM   1267 N N   . LEU A 1 195 ? 9.891   -18.223 -5.144  1.00 15.19 ? 175 LEU A N   1 
ATOM   1268 C CA  . LEU A 1 195 ? 8.734   -17.282 -5.134  1.00 15.80 ? 175 LEU A CA  1 
ATOM   1269 C C   . LEU A 1 195 ? 9.164   -15.908 -4.585  1.00 15.56 ? 175 LEU A C   1 
ATOM   1270 O O   . LEU A 1 195 ? 8.777   -14.905 -5.196  1.00 13.77 ? 175 LEU A O   1 
ATOM   1271 C CB  . LEU A 1 195 ? 7.578   -17.864 -4.317  1.00 16.69 ? 175 LEU A CB  1 
ATOM   1272 C CG  . LEU A 1 195 ? 6.812   -18.991 -5.001  1.00 18.96 ? 175 LEU A CG  1 
ATOM   1273 C CD1 . LEU A 1 195 ? 5.763   -19.585 -4.060  1.00 19.66 ? 175 LEU A CD1 1 
ATOM   1274 C CD2 . LEU A 1 195 ? 6.165   -18.514 -6.303  1.00 19.08 ? 175 LEU A CD2 1 
ATOM   1275 N N   . LEU A 1 196 ? 9.953   -15.876 -3.496  1.00 16.12 ? 176 LEU A N   1 
ATOM   1276 C CA  . LEU A 1 196 ? 10.393  -14.616 -2.850  1.00 16.08 ? 176 LEU A CA  1 
ATOM   1277 C C   . LEU A 1 196 ? 11.367  -13.857 -3.756  1.00 16.65 ? 176 LEU A C   1 
ATOM   1278 O O   . LEU A 1 196 ? 11.400  -12.643 -3.647  1.00 14.87 ? 176 LEU A O   1 
ATOM   1279 C CB  . LEU A 1 196 ? 10.985  -14.894 -1.465  1.00 16.52 ? 176 LEU A CB  1 
ATOM   1280 C CG  . LEU A 1 196 ? 9.957   -15.305 -0.400  1.00 17.25 ? 176 LEU A CG  1 
ATOM   1281 C CD1 . LEU A 1 196 ? 10.657  -15.897 0.805   1.00 17.62 ? 176 LEU A CD1 1 
ATOM   1282 C CD2 . LEU A 1 196 ? 9.079   -14.134 0.029   1.00 17.75 ? 176 LEU A CD2 1 
ATOM   1283 N N   . SER A 1 197 ? 12.149  -14.535 -4.596  1.00 17.48 ? 177 SER A N   1 
ATOM   1284 C CA  . SER A 1 197 ? 12.960  -13.882 -5.654  1.00 18.23 ? 177 SER A CA  1 
ATOM   1285 C C   . SER A 1 197 ? 12.054  -13.014 -6.530  1.00 18.63 ? 177 SER A C   1 
ATOM   1286 O O   . SER A 1 197 ? 12.352  -11.809 -6.697  1.00 16.81 ? 177 SER A O   1 
ATOM   1287 C CB  . SER A 1 197 ? 13.694  -14.877 -6.499  1.00 18.43 ? 177 SER A CB  1 
ATOM   1288 O OG  . SER A 1 197 ? 14.642  -15.573 -5.726  1.00 18.78 ? 177 SER A OG  1 
ATOM   1289 N N   . VAL A 1 198 ? 10.974  -13.598 -7.055  1.00 19.32 ? 178 VAL A N   1 
ATOM   1290 C CA  . VAL A 1 198 ? 10.055  -12.872 -7.977  1.00 19.36 ? 178 VAL A CA  1 
ATOM   1291 C C   . VAL A 1 198 ? 9.553   -11.631 -7.236  1.00 19.75 ? 178 VAL A C   1 
ATOM   1292 O O   . VAL A 1 198 ? 9.641   -10.504 -7.823  1.00 17.77 ? 178 VAL A O   1 
ATOM   1293 C CB  . VAL A 1 198 ? 8.877   -13.738 -8.456  1.00 20.57 ? 178 VAL A CB  1 
ATOM   1294 C CG1 . VAL A 1 198 ? 8.062   -12.995 -9.502  1.00 21.41 ? 178 VAL A CG1 1 
ATOM   1295 C CG2 . VAL A 1 198 ? 9.330   -15.079 -8.985  1.00 20.39 ? 178 VAL A CG2 1 
ATOM   1296 N N   . MET A 1 199 ? 9.055   -11.815 -6.006  1.00 18.94 ? 179 MET A N   1 
ATOM   1297 C CA  . MET A 1 199 ? 8.411   -10.715 -5.250  1.00 20.49 ? 179 MET A CA  1 
ATOM   1298 C C   . MET A 1 199 ? 9.463   -9.639  -4.971  1.00 19.50 ? 179 MET A C   1 
ATOM   1299 O O   . MET A 1 199 ? 9.129   -8.450  -5.081  1.00 17.68 ? 179 MET A O   1 
ATOM   1300 C CB  . MET A 1 199 ? 7.810   -11.188 -3.923  1.00 24.16 ? 179 MET A CB  1 
ATOM   1301 C CG  . MET A 1 199 ? 6.545   -12.009 -4.079  1.00 30.50 ? 179 MET A CG  1 
ATOM   1302 S SD  . MET A 1 199 ? 5.474   -11.537 -5.497  1.00 39.15 ? 179 MET A SD  1 
ATOM   1303 C CE  . MET A 1 199 ? 5.333   -9.763  -5.260  1.00 33.41 ? 179 MET A CE  1 
ATOM   1304 N N   . SER A 1 200 ? 10.692  -10.031 -4.618  1.00 19.35 ? 180 SER A N   1 
ATOM   1305 C CA  . SER A 1 200 ? 11.796  -9.073  -4.334  1.00 19.91 ? 180 SER A CA  1 
ATOM   1306 C C   . SER A 1 200 ? 12.035  -8.180  -5.554  1.00 17.30 ? 180 SER A C   1 
ATOM   1307 O O   . SER A 1 200 ? 12.172  -6.950  -5.373  1.00 15.32 ? 180 SER A O   1 
ATOM   1308 C CB  . SER A 1 200 ? 13.063  -9.772  -3.932  1.00 21.10 ? 180 SER A CB  1 
ATOM   1309 O OG  . SER A 1 200 ? 12.938  -10.297 -2.624  1.00 23.42 ? 180 SER A OG  1 
ATOM   1310 N N   . GLY A 1 201 ? 12.113  -8.782  -6.741  1.00 16.60 ? 181 GLY A N   1 
ATOM   1311 C CA  . GLY A 1 201 ? 12.307  -8.042  -8.011  1.00 16.14 ? 181 GLY A CA  1 
ATOM   1312 C C   . GLY A 1 201 ? 11.152  -7.087  -8.273  1.00 15.77 ? 181 GLY A C   1 
ATOM   1313 O O   . GLY A 1 201 ? 11.407  -5.929  -8.612  1.00 16.12 ? 181 GLY A O   1 
ATOM   1314 N N   . VAL A 1 202 ? 9.913   -7.546  -8.085  1.00 15.10 ? 182 VAL A N   1 
ATOM   1315 C CA  . VAL A 1 202 ? 8.689   -6.710  -8.248  1.00 15.50 ? 182 VAL A CA  1 
ATOM   1316 C C   . VAL A 1 202 ? 8.834   -5.463  -7.371  1.00 15.61 ? 182 VAL A C   1 
ATOM   1317 O O   . VAL A 1 202 ? 8.765   -4.371  -7.900  1.00 15.59 ? 182 VAL A O   1 
ATOM   1318 C CB  . VAL A 1 202 ? 7.408   -7.495  -7.915  1.00 15.51 ? 182 VAL A CB  1 
ATOM   1319 C CG1 . VAL A 1 202 ? 6.181   -6.594  -7.917  1.00 16.93 ? 182 VAL A CG1 1 
ATOM   1320 C CG2 . VAL A 1 202 ? 7.202   -8.659  -8.864  1.00 15.94 ? 182 VAL A CG2 1 
ATOM   1321 N N   . PHE A 1 203 ? 9.117   -5.650  -6.082  1.00 17.41 ? 183 PHE A N   1 
ATOM   1322 C CA  . PHE A 1 203 ? 9.262   -4.560  -5.082  1.00 18.17 ? 183 PHE A CA  1 
ATOM   1323 C C   . PHE A 1 203 ? 10.428  -3.629  -5.438  1.00 17.15 ? 183 PHE A C   1 
ATOM   1324 O O   . PHE A 1 203 ? 10.270  -2.417  -5.195  1.00 16.36 ? 183 PHE A O   1 
ATOM   1325 C CB  . PHE A 1 203 ? 9.427   -5.149  -3.680  1.00 20.28 ? 183 PHE A CB  1 
ATOM   1326 C CG  . PHE A 1 203 ? 8.187   -5.798  -3.107  1.00 22.80 ? 183 PHE A CG  1 
ATOM   1327 C CD1 . PHE A 1 203 ? 6.916   -5.509  -3.596  1.00 26.72 ? 183 PHE A CD1 1 
ATOM   1328 C CD2 . PHE A 1 203 ? 8.280   -6.650  -2.024  1.00 24.80 ? 183 PHE A CD2 1 
ATOM   1329 C CE1 . PHE A 1 203 ? 5.778   -6.089  -3.051  1.00 25.95 ? 183 PHE A CE1 1 
ATOM   1330 C CE2 . PHE A 1 203 ? 7.141   -7.217  -1.462  1.00 26.49 ? 183 PHE A CE2 1 
ATOM   1331 C CZ  . PHE A 1 203 ? 5.892   -6.945  -1.982  1.00 26.54 ? 183 PHE A CZ  1 
ATOM   1332 N N   . GLU A 1 204 ? 11.564  -4.174  -5.902  1.00 15.62 ? 184 GLU A N   1 
ATOM   1333 C CA  . GLU A 1 204 ? 12.746  -3.369  -6.295  1.00 16.79 ? 184 GLU A CA  1 
ATOM   1334 C C   . GLU A 1 204 ? 12.325  -2.416  -7.418  1.00 15.92 ? 184 GLU A C   1 
ATOM   1335 O O   . GLU A 1 204 ? 12.554  -1.219  -7.279  1.00 15.40 ? 184 GLU A O   1 
ATOM   1336 C CB  . GLU A 1 204 ? 13.915  -4.252  -6.735  1.00 16.00 ? 184 GLU A CB  1 
ATOM   1337 C CG  . GLU A 1 204 ? 15.187  -3.468  -7.015  1.00 17.26 ? 184 GLU A CG  1 
ATOM   1338 C CD  . GLU A 1 204 ? 16.339  -4.303  -7.547  1.00 17.68 ? 184 GLU A CD  1 
ATOM   1339 O OE1 . GLU A 1 204 ? 17.480  -3.827  -7.545  1.00 20.73 ? 184 GLU A OE1 1 
ATOM   1340 O OE2 . GLU A 1 204 ? 16.092  -5.447  -7.925  1.00 19.86 ? 184 GLU A OE2 1 
ATOM   1341 N N   . GLY A 1 205 ? 11.664  -2.952  -8.450  1.00 17.22 ? 185 GLY A N   1 
ATOM   1342 C CA  . GLY A 1 205 ? 11.123  -2.181  -9.591  1.00 17.19 ? 185 GLY A CA  1 
ATOM   1343 C C   . GLY A 1 205 ? 10.137  -1.124  -9.134  1.00 17.66 ? 185 GLY A C   1 
ATOM   1344 O O   . GLY A 1 205 ? 10.209  0.029   -9.616  1.00 15.40 ? 185 GLY A O   1 
ATOM   1345 N N   . TRP A 1 206 ? 9.289   -1.489  -8.185  1.00 17.96 ? 186 TRP A N   1 
ATOM   1346 C CA  . TRP A 1 206 ? 8.174   -0.637  -7.709  1.00 20.05 ? 186 TRP A CA  1 
ATOM   1347 C C   . TRP A 1 206 ? 8.728   0.588   -6.962  1.00 19.71 ? 186 TRP A C   1 
ATOM   1348 O O   . TRP A 1 206 ? 8.305   1.762   -7.238  1.00 17.16 ? 186 TRP A O   1 
ATOM   1349 C CB  . TRP A 1 206 ? 7.248   -1.507  -6.860  1.00 21.78 ? 186 TRP A CB  1 
ATOM   1350 C CG  . TRP A 1 206 ? 5.951   -0.831  -6.580  1.00 24.51 ? 186 TRP A CG  1 
ATOM   1351 C CD1 . TRP A 1 206 ? 5.397   -0.590  -5.360  1.00 25.80 ? 186 TRP A CD1 1 
ATOM   1352 C CD2 . TRP A 1 206 ? 5.096   -0.198  -7.544  1.00 28.04 ? 186 TRP A CD2 1 
ATOM   1353 N NE1 . TRP A 1 206 ? 4.225   0.107   -5.505  1.00 27.98 ? 186 TRP A NE1 1 
ATOM   1354 C CE2 . TRP A 1 206 ? 4.021   0.373   -6.830  1.00 30.11 ? 186 TRP A CE2 1 
ATOM   1355 C CE3 . TRP A 1 206 ? 5.123   -0.067  -8.934  1.00 31.10 ? 186 TRP A CE3 1 
ATOM   1356 C CZ2 . TRP A 1 206 ? 2.981   1.051   -7.461  1.00 31.92 ? 186 TRP A CZ2 1 
ATOM   1357 C CZ3 . TRP A 1 206 ? 4.100   0.604   -9.559  1.00 33.58 ? 186 TRP A CZ3 1 
ATOM   1358 C CH2 . TRP A 1 206 ? 3.047   1.160   -8.830  1.00 33.54 ? 186 TRP A CH2 1 
ATOM   1359 N N   . VAL A 1 207 ? 9.710   0.337   -6.092  1.00 18.88 ? 187 VAL A N   1 
ATOM   1360 C CA  . VAL A 1 207 ? 10.376  1.378   -5.271  1.00 17.75 ? 187 VAL A CA  1 
ATOM   1361 C C   . VAL A 1 207 ? 11.094  2.365   -6.211  1.00 17.59 ? 187 VAL A C   1 
ATOM   1362 O O   . VAL A 1 207 ? 10.995  3.588   -5.979  1.00 16.08 ? 187 VAL A O   1 
ATOM   1363 C CB  . VAL A 1 207 ? 11.328  0.717   -4.260  1.00 18.68 ? 187 VAL A CB  1 
ATOM   1364 C CG1 . VAL A 1 207 ? 12.342  1.691   -3.683  1.00 18.81 ? 187 VAL A CG1 1 
ATOM   1365 C CG2 . VAL A 1 207 ? 10.524  0.064   -3.158  1.00 19.28 ? 187 VAL A CG2 1 
ATOM   1366 N N   . GLN A 1 208 ? 11.784  1.852   -7.232  1.00 16.25 ? 188 GLN A N   1 
ATOM   1367 C CA  . GLN A 1 208 ? 12.424  2.685   -8.273  1.00 15.55 ? 188 GLN A CA  1 
ATOM   1368 C C   . GLN A 1 208 ? 11.362  3.529   -9.001  1.00 15.75 ? 188 GLN A C   1 
ATOM   1369 O O   . GLN A 1 208 ? 11.601  4.754   -9.156  1.00 16.62 ? 188 GLN A O   1 
ATOM   1370 C CB  . GLN A 1 208 ? 13.252  1.811   -9.210  1.00 15.77 ? 188 GLN A CB  1 
ATOM   1371 C CG  . GLN A 1 208 ? 14.042  2.619   -10.240 1.00 16.63 ? 188 GLN A CG  1 
ATOM   1372 C CD  . GLN A 1 208 ? 15.189  3.321   -9.569  1.00 17.35 ? 188 GLN A CD  1 
ATOM   1373 O OE1 . GLN A 1 208 ? 15.974  2.682   -8.891  1.00 22.81 ? 188 GLN A OE1 1 
ATOM   1374 N NE2 . GLN A 1 208 ? 15.262  4.631   -9.686  1.00 15.82 ? 188 GLN A NE2 1 
ATOM   1375 N N   . ALA A 1 209 ? 10.253  2.928   -9.450  1.00 13.99 ? 189 ALA A N   1 
ATOM   1376 C CA  . ALA A 1 209 ? 9.193   3.633   -10.213 1.00 14.15 ? 189 ALA A CA  1 
ATOM   1377 C C   . ALA A 1 209 ? 8.617   4.774   -9.358  1.00 13.51 ? 189 ALA A C   1 
ATOM   1378 O O   . ALA A 1 209 ? 8.509   5.925   -9.850  1.00 12.94 ? 189 ALA A O   1 
ATOM   1379 C CB  . ALA A 1 209 ? 8.116   2.678   -10.646 1.00 12.79 ? 189 ALA A CB  1 
ATOM   1380 N N   . LEU A 1 210 ? 8.344   4.466   -8.091  1.00 14.54 ? 190 LEU A N   1 
ATOM   1381 C CA  . LEU A 1 210 ? 7.661   5.376   -7.140  1.00 14.70 ? 190 LEU A CA  1 
ATOM   1382 C C   . LEU A 1 210 ? 8.582   6.532   -6.790  1.00 14.47 ? 190 LEU A C   1 
ATOM   1383 O O   . LEU A 1 210 ? 8.071   7.655   -6.674  1.00 14.39 ? 190 LEU A O   1 
ATOM   1384 C CB  . LEU A 1 210 ? 7.220   4.578   -5.913  1.00 15.08 ? 190 LEU A CB  1 
ATOM   1385 C CG  . LEU A 1 210 ? 5.970   3.708   -6.113  1.00 16.32 ? 190 LEU A CG  1 
ATOM   1386 C CD1 . LEU A 1 210 ? 5.354   3.316   -4.775  1.00 17.36 ? 190 LEU A CD1 1 
ATOM   1387 C CD2 . LEU A 1 210 ? 4.939   4.418   -6.965  1.00 15.82 ? 190 LEU A CD2 1 
ATOM   1388 N N   . ALA A 1 211 ? 9.886   6.279   -6.693  1.00 14.21 ? 191 ALA A N   1 
ATOM   1389 C CA  . ALA A 1 211 ? 10.897  7.321   -6.417  1.00 15.05 ? 191 ALA A CA  1 
ATOM   1390 C C   . ALA A 1 211 ? 10.986  8.306   -7.594  1.00 16.64 ? 191 ALA A C   1 
ATOM   1391 O O   . ALA A 1 211 ? 11.033  9.558   -7.353  1.00 15.76 ? 191 ALA A O   1 
ATOM   1392 C CB  . ALA A 1 211 ? 12.233  6.679   -6.136  1.00 15.55 ? 191 ALA A CB  1 
ATOM   1393 N N   . ILE A 1 212 ? 11.035  7.790   -8.828  1.00 15.24 ? 192 ILE A N   1 
ATOM   1394 C CA  . ILE A 1 212 ? 11.063  8.642   -10.050 1.00 15.56 ? 192 ILE A CA  1 
ATOM   1395 C C   . ILE A 1 212 ? 9.788   9.512   -10.093 1.00 17.38 ? 192 ILE A C   1 
ATOM   1396 O O   . ILE A 1 212 ? 9.890   10.762  -10.293 1.00 16.14 ? 192 ILE A O   1 
ATOM   1397 C CB  . ILE A 1 212 ? 11.247  7.754   -11.293 1.00 14.85 ? 192 ILE A CB  1 
ATOM   1398 C CG1 . ILE A 1 212 ? 12.664  7.167   -11.333 1.00 14.93 ? 192 ILE A CG1 1 
ATOM   1399 C CG2 . ILE A 1 212 ? 10.908  8.525   -12.553 1.00 15.11 ? 192 ILE A CG2 1 
ATOM   1400 C CD1 . ILE A 1 212 ? 12.862  6.076   -12.358 1.00 15.04 ? 192 ILE A CD1 1 
ATOM   1401 N N   . VAL A 1 213 ? 8.627   8.878   -9.944  1.00 18.17 ? 193 VAL A N   1 
ATOM   1402 C CA  . VAL A 1 213 ? 7.280   9.532   -10.024 1.00 20.22 ? 193 VAL A CA  1 
ATOM   1403 C C   . VAL A 1 213 ? 7.179   10.616  -8.939  1.00 20.21 ? 193 VAL A C   1 
ATOM   1404 O O   . VAL A 1 213 ? 6.792   11.760  -9.268  1.00 19.17 ? 193 VAL A O   1 
ATOM   1405 C CB  . VAL A 1 213 ? 6.163   8.472   -9.918  1.00 22.44 ? 193 VAL A CB  1 
ATOM   1406 C CG1 . VAL A 1 213 ? 4.886   8.968   -9.269  1.00 25.75 ? 193 VAL A CG1 1 
ATOM   1407 C CG2 . VAL A 1 213 ? 5.855   7.891   -11.286 1.00 24.91 ? 193 VAL A CG2 1 
ATOM   1408 N N   . GLY A 1 214 ? 7.511   10.267  -7.697  1.00 18.88 ? 194 GLY A N   1 
ATOM   1409 C CA  . GLY A 1 214 ? 7.451   11.177  -6.541  1.00 19.71 ? 194 GLY A CA  1 
ATOM   1410 C C   . GLY A 1 214 ? 8.354   12.385  -6.738  1.00 21.40 ? 194 GLY A C   1 
ATOM   1411 O O   . GLY A 1 214 ? 7.879   13.510  -6.526  1.00 19.17 ? 194 GLY A O   1 
ATOM   1412 N N   . ALA A 1 215 ? 9.613   12.153  -7.140  1.00 20.06 ? 195 ALA A N   1 
ATOM   1413 C CA  . ALA A 1 215 ? 10.641  13.196  -7.293  1.00 20.39 ? 195 ALA A CA  1 
ATOM   1414 C C   . ALA A 1 215 ? 10.275  14.159  -8.437  1.00 22.72 ? 195 ALA A C   1 
ATOM   1415 O O   . ALA A 1 215 ? 10.718  15.339  -8.378  1.00 22.94 ? 195 ALA A O   1 
ATOM   1416 C CB  . ALA A 1 215 ? 11.981  12.548  -7.522  1.00 20.11 ? 195 ALA A CB  1 
ATOM   1417 N N   . ALA A 1 216 ? 9.567   13.675  -9.463  1.00 21.25 ? 196 ALA A N   1 
ATOM   1418 C CA  . ALA A 1 216 ? 9.121   14.481  -10.620 1.00 21.99 ? 196 ALA A CA  1 
ATOM   1419 C C   . ALA A 1 216 ? 7.881   15.306  -10.242 1.00 22.88 ? 196 ALA A C   1 
ATOM   1420 O O   . ALA A 1 216 ? 7.521   16.166  -11.029 1.00 24.70 ? 196 ALA A O   1 
ATOM   1421 C CB  . ALA A 1 216 ? 8.858   13.591  -11.820 1.00 21.29 ? 196 ALA A CB  1 
ATOM   1422 N N   . GLY A 1 217 ? 7.249   15.047  -9.091  1.00 24.24 ? 197 GLY A N   1 
ATOM   1423 C CA  . GLY A 1 217 ? 6.020   15.738  -8.654  1.00 23.74 ? 197 GLY A CA  1 
ATOM   1424 C C   . GLY A 1 217 ? 4.754   15.037  -9.140  1.00 23.62 ? 197 GLY A C   1 
ATOM   1425 O O   . GLY A 1 217 ? 3.691   15.652  -9.070  1.00 22.85 ? 197 GLY A O   1 
ATOM   1426 N N   . GLU A 1 218 ? 4.813   13.783  -9.579  1.00 21.65 ? 198 GLU A N   1 
ATOM   1427 C CA  . GLU A 1 218 ? 3.602   13.090  -10.090 1.00 23.01 ? 198 GLU A CA  1 
ATOM   1428 C C   . GLU A 1 218 ? 2.947   12.375  -8.916  1.00 22.73 ? 198 GLU A C   1 
ATOM   1429 O O   . GLU A 1 218 ? 3.557   12.332  -7.851  1.00 22.41 ? 198 GLU A O   1 
ATOM   1430 C CB  . GLU A 1 218 ? 3.908   12.142  -11.246 1.00 26.68 ? 198 GLU A CB  1 
ATOM   1431 C CG  . GLU A 1 218 ? 4.474   12.859  -12.462 1.00 31.20 ? 198 GLU A CG  1 
ATOM   1432 C CD  . GLU A 1 218 ? 3.592   13.936  -13.066 1.00 31.68 ? 198 GLU A CD  1 
ATOM   1433 O OE1 . GLU A 1 218 ? 4.125   14.994  -13.433 1.00 36.81 ? 198 GLU A OE1 1 
ATOM   1434 O OE2 . GLU A 1 218 ? 2.383   13.713  -13.180 1.00 37.44 ? 198 GLU A OE2 1 
ATOM   1435 N N   . ASP A 1 219 ? 1.751   11.848  -9.131  1.00 24.69 ? 199 ASP A N   1 
ATOM   1436 C CA  . ASP A 1 219 ? 0.891   11.283  -8.064  1.00 25.37 ? 199 ASP A CA  1 
ATOM   1437 C C   . ASP A 1 219 ? 1.065   9.763   -8.023  1.00 22.79 ? 199 ASP A C   1 
ATOM   1438 O O   . ASP A 1 219 ? 0.654   9.093   -8.978  1.00 20.86 ? 199 ASP A O   1 
ATOM   1439 C CB  . ASP A 1 219 ? -0.572  11.672  -8.277  1.00 25.67 ? 199 ASP A CB  1 
ATOM   1440 C CG  . ASP A 1 219 ? -1.420  11.164  -7.136  1.00 26.56 ? 199 ASP A CG  1 
ATOM   1441 O OD1 . ASP A 1 219 ? -1.812  9.996   -7.191  1.00 30.87 ? 199 ASP A OD1 1 
ATOM   1442 O OD2 . ASP A 1 219 ? -1.589  11.911  -6.168  1.00 28.43 ? 199 ASP A OD2 1 
ATOM   1443 N N   . GLU A 1 220 ? 1.636   9.242   -6.936  1.00 23.01 ? 200 GLU A N   1 
ATOM   1444 C CA  . GLU A 1 220 ? 1.971   7.793   -6.815  1.00 23.11 ? 200 GLU A CA  1 
ATOM   1445 C C   . GLU A 1 220 ? 0.698   6.976   -7.052  1.00 21.71 ? 200 GLU A C   1 
ATOM   1446 O O   . GLU A 1 220 ? 0.769   5.942   -7.722  1.00 22.41 ? 200 GLU A O   1 
ATOM   1447 C CB  . GLU A 1 220 ? 2.626   7.476   -5.463  1.00 23.35 ? 200 GLU A CB  1 
ATOM   1448 C CG  . GLU A 1 220 ? 3.978   8.140   -5.257  1.00 22.51 ? 200 GLU A CG  1 
ATOM   1449 C CD  . GLU A 1 220 ? 3.903   9.573   -4.756  1.00 22.86 ? 200 GLU A CD  1 
ATOM   1450 O OE1 . GLU A 1 220 ? 4.937   10.098  -4.338  1.00 21.65 ? 200 GLU A OE1 1 
ATOM   1451 O OE2 . GLU A 1 220 ? 2.800   10.150  -4.793  1.00 19.83 ? 200 GLU A OE2 1 
ATOM   1452 N N   . VAL A 1 221 ? -0.449  7.428   -6.550  1.00 24.42 ? 201 VAL A N   1 
ATOM   1453 C CA  . VAL A 1 221 ? -1.722  6.647   -6.623  1.00 24.67 ? 201 VAL A CA  1 
ATOM   1454 C C   . VAL A 1 221 ? -2.192  6.590   -8.084  1.00 24.01 ? 201 VAL A C   1 
ATOM   1455 O O   . VAL A 1 221 ? -2.466  5.494   -8.570  1.00 26.28 ? 201 VAL A O   1 
ATOM   1456 C CB  . VAL A 1 221 ? -2.796  7.228   -5.685  1.00 25.98 ? 201 VAL A CB  1 
ATOM   1457 C CG1 . VAL A 1 221 ? -4.140  6.541   -5.891  1.00 26.63 ? 201 VAL A CG1 1 
ATOM   1458 C CG2 . VAL A 1 221 ? -2.357  7.145   -4.228  1.00 25.40 ? 201 VAL A CG2 1 
ATOM   1459 N N   . ASP A 1 222 ? -2.237  7.733   -8.765  1.00 25.69 ? 202 ASP A N   1 
ATOM   1460 C CA  . ASP A 1 222 ? -2.530  7.848   -10.220 1.00 24.75 ? 202 ASP A CA  1 
ATOM   1461 C C   . ASP A 1 222 ? -1.618  6.908   -11.018 1.00 24.03 ? 202 ASP A C   1 
ATOM   1462 O O   . ASP A 1 222 ? -2.135  6.131   -11.851 1.00 23.76 ? 202 ASP A O   1 
ATOM   1463 C CB  . ASP A 1 222 ? -2.381  9.304   -10.661 1.00 28.99 ? 202 ASP A CB  1 
ATOM   1464 C CG  . ASP A 1 222 ? -3.489  10.187  -10.121 1.00 31.62 ? 202 ASP A CG  1 
ATOM   1465 O OD1 . ASP A 1 222 ? -4.486  9.608   -9.627  1.00 34.10 ? 202 ASP A OD1 1 
ATOM   1466 O OD2 . ASP A 1 222 ? -3.333  11.433  -10.161 1.00 32.17 ? 202 ASP A OD2 1 
ATOM   1467 N N   . PHE A 1 223 ? -0.308  6.961   -10.769 1.00 22.47 ? 203 PHE A N   1 
ATOM   1468 C CA  . PHE A 1 223 ? 0.681   6.092   -11.451 1.00 22.30 ? 203 PHE A CA  1 
ATOM   1469 C C   . PHE A 1 223 ? 0.323   4.623   -11.215 1.00 22.20 ? 203 PHE A C   1 
ATOM   1470 O O   . PHE A 1 223 ? 0.392   3.845   -12.163 1.00 25.86 ? 203 PHE A O   1 
ATOM   1471 C CB  . PHE A 1 223 ? 2.109   6.406   -11.001 1.00 21.30 ? 203 PHE A CB  1 
ATOM   1472 C CG  . PHE A 1 223 ? 3.131   5.499   -11.637 1.00 21.77 ? 203 PHE A CG  1 
ATOM   1473 C CD1 . PHE A 1 223 ? 3.536   5.709   -12.942 1.00 20.38 ? 203 PHE A CD1 1 
ATOM   1474 C CD2 . PHE A 1 223 ? 3.643   4.396   -10.951 1.00 21.96 ? 203 PHE A CD2 1 
ATOM   1475 C CE1 . PHE A 1 223 ? 4.460   4.863   -13.532 1.00 19.86 ? 203 PHE A CE1 1 
ATOM   1476 C CE2 . PHE A 1 223 ? 4.576   3.559   -11.544 1.00 20.38 ? 203 PHE A CE2 1 
ATOM   1477 C CZ  . PHE A 1 223 ? 4.980   3.798   -12.834 1.00 20.37 ? 203 PHE A CZ  1 
ATOM   1478 N N   . ALA A 1 224 ? -0.081  4.239   -10.004 1.00 22.93 ? 204 ALA A N   1 
ATOM   1479 C CA  . ALA A 1 224 ? -0.418  2.833   -9.682  1.00 23.21 ? 204 ALA A CA  1 
ATOM   1480 C C   . ALA A 1 224 ? -1.574  2.365   -10.576 1.00 24.85 ? 204 ALA A C   1 
ATOM   1481 O O   . ALA A 1 224 ? -1.517  1.253   -11.109 1.00 24.87 ? 204 ALA A O   1 
ATOM   1482 C CB  . ALA A 1 224 ? -0.728  2.689   -8.219  1.00 23.35 ? 204 ALA A CB  1 
ATOM   1483 N N   . ALA A 1 225 ? -2.567  3.221   -10.789 1.00 28.02 ? 205 ALA A N   1 
ATOM   1484 C CA  . ALA A 1 225 ? -3.690  2.962   -11.714 1.00 28.03 ? 205 ALA A CA  1 
ATOM   1485 C C   . ALA A 1 225 ? -3.141  2.707   -13.118 1.00 30.43 ? 205 ALA A C   1 
ATOM   1486 O O   . ALA A 1 225 ? -3.614  1.770   -13.765 1.00 33.49 ? 205 ALA A O   1 
ATOM   1487 C CB  . ALA A 1 225 ? -4.659  4.115   -11.690 1.00 26.94 ? 205 ALA A CB  1 
ATOM   1488 N N   . LEU A 1 226 ? -2.159  3.490   -13.571 1.00 36.28 ? 206 LEU A N   1 
ATOM   1489 C CA  . LEU A 1 226 ? -1.582  3.354   -14.938 1.00 36.47 ? 206 LEU A CA  1 
ATOM   1490 C C   . LEU A 1 226 ? -0.788  2.044   -15.037 1.00 36.75 ? 206 LEU A C   1 
ATOM   1491 O O   . LEU A 1 226 ? -0.865  1.408   -16.105 1.00 41.29 ? 206 LEU A O   1 
ATOM   1492 C CB  . LEU A 1 226 ? -0.710  4.571   -15.268 1.00 37.63 ? 206 LEU A CB  1 
ATOM   1493 C CG  . LEU A 1 226 ? -0.017  4.540   -16.632 1.00 38.92 ? 206 LEU A CG  1 
ATOM   1494 C CD1 . LEU A 1 226 ? -1.020  4.715   -17.759 1.00 39.69 ? 206 LEU A CD1 1 
ATOM   1495 C CD2 . LEU A 1 226 ? 1.058   5.610   -16.730 1.00 39.95 ? 206 LEU A CD2 1 
ATOM   1496 N N   . ALA A 1 227 ? -0.101  1.641   -13.963 1.00 37.98 ? 207 ALA A N   1 
ATOM   1497 C CA  . ALA A 1 227 ? 0.945   0.587   -13.946 1.00 38.48 ? 207 ALA A CA  1 
ATOM   1498 C C   . ALA A 1 227 ? 0.434   -0.767  -13.424 1.00 42.21 ? 207 ALA A C   1 
ATOM   1499 O O   . ALA A 1 227 ? 1.127   -1.776  -13.659 1.00 40.06 ? 207 ALA A O   1 
ATOM   1500 C CB  . ALA A 1 227 ? 2.105   1.051   -13.101 1.00 39.28 ? 207 ALA A CB  1 
ATOM   1501 N N   . SER A 1 228 ? -0.687  -0.816  -12.698 1.00 46.01 ? 208 SER A N   1 
ATOM   1502 C CA  . SER A 1 228 ? -1.216  -2.085  -12.127 1.00 47.07 ? 208 SER A CA  1 
ATOM   1503 C C   . SER A 1 228 ? -1.611  -3.058  -13.241 1.00 44.36 ? 208 SER A C   1 
ATOM   1504 O O   . SER A 1 228 ? -1.402  -4.260  -13.100 1.00 41.13 ? 208 SER A O   1 
ATOM   1505 C CB  . SER A 1 228 ? -2.331  -1.819  -11.153 1.00 51.56 ? 208 SER A CB  1 
ATOM   1506 O OG  . SER A 1 228 ? -1.802  -1.223  -9.975  1.00 53.80 ? 208 SER A OG  1 
ATOM   1507 N N   . PRO A 1 229 ? -2.214  -2.587  -14.361 1.00 46.12 ? 209 PRO A N   1 
ATOM   1508 C CA  . PRO A 1 229 ? -2.337  -3.389  -15.583 1.00 43.03 ? 209 PRO A CA  1 
ATOM   1509 C C   . PRO A 1 229 ? -1.072  -4.110  -16.075 1.00 48.41 ? 209 PRO A C   1 
ATOM   1510 O O   . PRO A 1 229 ? -1.141  -5.298  -16.345 1.00 49.30 ? 209 PRO A O   1 
ATOM   1511 C CB  . PRO A 1 229 ? -2.749  -2.352  -16.635 1.00 45.45 ? 209 PRO A CB  1 
ATOM   1512 C CG  . PRO A 1 229 ? -3.578  -1.353  -15.839 1.00 48.52 ? 209 PRO A CG  1 
ATOM   1513 C CD  . PRO A 1 229 ? -2.927  -1.301  -14.467 1.00 47.39 ? 209 PRO A CD  1 
ATOM   1514 N N   . LEU A 1 230 ? 0.045   -3.391  -16.205 1.00 46.18 ? 210 LEU A N   1 
ATOM   1515 C CA  . LEU A 1 230 ? 1.333   -3.964  -16.674 1.00 40.11 ? 210 LEU A CA  1 
ATOM   1516 C C   . LEU A 1 230 ? 1.720   -5.161  -15.798 1.00 39.34 ? 210 LEU A C   1 
ATOM   1517 O O   . LEU A 1 230 ? 2.169   -6.165  -16.352 1.00 33.48 ? 210 LEU A O   1 
ATOM   1518 C CB  . LEU A 1 230 ? 2.405   -2.870  -16.652 1.00 41.92 ? 210 LEU A CB  1 
ATOM   1519 C CG  . LEU A 1 230 ? 3.857   -3.347  -16.699 1.00 42.68 ? 210 LEU A CG  1 
ATOM   1520 C CD1 . LEU A 1 230 ? 4.138   -4.102  -17.994 1.00 44.89 ? 210 LEU A CD1 1 
ATOM   1521 C CD2 . LEU A 1 230 ? 4.809   -2.168  -16.535 1.00 43.43 ? 210 LEU A CD2 1 
ATOM   1522 N N   . VAL A 1 231 ? 1.572   -5.077  -14.476 1.00 41.77 ? 211 VAL A N   1 
ATOM   1523 C CA  . VAL A 1 231 ? 2.032   -6.181  -13.579 1.00 47.14 ? 211 VAL A CA  1 
ATOM   1524 C C   . VAL A 1 231 ? 1.087   -7.379  -13.742 1.00 50.42 ? 211 VAL A C   1 
ATOM   1525 O O   . VAL A 1 231 ? 1.604   -8.521  -13.806 1.00 48.95 ? 211 VAL A O   1 
ATOM   1526 C CB  . VAL A 1 231 ? 2.199   -5.734  -12.114 1.00 51.55 ? 211 VAL A CB  1 
ATOM   1527 C CG1 . VAL A 1 231 ? 3.090   -4.501  -12.035 1.00 52.49 ? 211 VAL A CG1 1 
ATOM   1528 C CG2 . VAL A 1 231 ? 0.874   -5.496  -11.395 1.00 52.60 ? 211 VAL A CG2 1 
ATOM   1529 N N   . ALA A 1 232 ? -0.224  -7.119  -13.854 1.00 48.17 ? 212 ALA A N   1 
ATOM   1530 C CA  . ALA A 1 232 ? -1.277  -8.115  -14.169 1.00 47.23 ? 212 ALA A CA  1 
ATOM   1531 C C   . ALA A 1 232 ? -0.952  -8.799  -15.503 1.00 44.55 ? 212 ALA A C   1 
ATOM   1532 O O   . ALA A 1 232 ? -1.045  -10.040 -15.566 1.00 45.72 ? 212 ALA A O   1 
ATOM   1533 C CB  . ALA A 1 232 ? -2.636  -7.456  -14.204 1.00 44.61 ? 212 ALA A CB  1 
ATOM   1534 N N   . SER A 1 233 ? -0.576  -8.026  -16.523 1.00 42.86 ? 213 SER A N   1 
ATOM   1535 C CA  . SER A 1 233 ? -0.115  -8.551  -17.836 1.00 44.68 ? 213 SER A CA  1 
ATOM   1536 C C   . SER A 1 233 ? 0.865   -9.716  -17.616 1.00 44.75 ? 213 SER A C   1 
ATOM   1537 O O   . SER A 1 233 ? 0.768   -10.726 -18.353 1.00 41.98 ? 213 SER A O   1 
ATOM   1538 C CB  . SER A 1 233 ? 0.516   -7.469  -18.677 1.00 46.52 ? 213 SER A CB  1 
ATOM   1539 O OG  . SER A 1 233 ? 1.907   -7.346  -18.392 1.00 48.17 ? 213 SER A OG  1 
ATOM   1540 N N   . MET A 1 234 ? 1.766   -9.592  -16.631 1.00 45.52 ? 214 MET A N   1 
ATOM   1541 C CA  . MET A 1 234 ? 2.853   -10.577 -16.367 1.00 47.30 ? 214 MET A CA  1 
ATOM   1542 C C   . MET A 1 234 ? 2.282   -11.925 -15.898 1.00 43.56 ? 214 MET A C   1 
ATOM   1543 O O   . MET A 1 234 ? 3.038   -12.899 -15.880 1.00 39.43 ? 214 MET A O   1 
ATOM   1544 C CB  . MET A 1 234 ? 3.854   -10.033 -15.342 1.00 55.54 ? 214 MET A CB  1 
ATOM   1545 C CG  . MET A 1 234 ? 5.123   -9.492  -15.981 1.00 58.14 ? 214 MET A CG  1 
ATOM   1546 S SD  . MET A 1 234 ? 4.929   -7.938  -16.884 1.00 71.87 ? 214 MET A SD  1 
ATOM   1547 C CE  . MET A 1 234 ? 6.646   -7.432  -16.975 1.00 63.73 ? 214 MET A CE  1 
ATOM   1548 N N   . ALA A 1 235 ? 0.982   -12.013 -15.602 1.00 43.40 ? 215 ALA A N   1 
ATOM   1549 C CA  . ALA A 1 235 ? 0.247   -13.298 -15.489 1.00 43.41 ? 215 ALA A CA  1 
ATOM   1550 C C   . ALA A 1 235 ? 0.469   -14.130 -16.760 1.00 42.16 ? 215 ALA A C   1 
ATOM   1551 O O   . ALA A 1 235 ? 0.550   -15.364 -16.657 1.00 47.17 ? 215 ALA A O   1 
ATOM   1552 C CB  . ALA A 1 235 ? -1.227  -13.052 -15.252 1.00 42.03 ? 215 ALA A CB  1 
ATOM   1553 N N   . ASP A 1 236 ? 0.562   -13.475 -17.916 1.00 41.82 ? 216 ASP A N   1 
ATOM   1554 C CA  . ASP A 1 236 ? 0.726   -14.125 -19.245 1.00 41.02 ? 216 ASP A CA  1 
ATOM   1555 C C   . ASP A 1 236 ? 2.202   -14.184 -19.626 1.00 39.03 ? 216 ASP A C   1 
ATOM   1556 O O   . ASP A 1 236 ? 2.633   -15.250 -20.091 1.00 39.08 ? 216 ASP A O   1 
ATOM   1557 C CB  . ASP A 1 236 ? -0.056  -13.372 -20.318 1.00 43.21 ? 216 ASP A CB  1 
ATOM   1558 C CG  . ASP A 1 236 ? -1.523  -13.266 -19.959 1.00 46.64 ? 216 ASP A CG  1 
ATOM   1559 O OD1 . ASP A 1 236 ? -2.142  -14.339 -19.769 1.00 49.57 ? 216 ASP A OD1 1 
ATOM   1560 O OD2 . ASP A 1 236 ? -2.014  -12.121 -19.810 1.00 47.46 ? 216 ASP A OD2 1 
ATOM   1561 N N   . GLN A 1 237 ? 2.936   -13.081 -19.476 1.00 35.57 ? 217 GLN A N   1 
ATOM   1562 C CA  . GLN A 1 237 ? 4.331   -12.982 -19.982 1.00 37.81 ? 217 GLN A CA  1 
ATOM   1563 C C   . GLN A 1 237 ? 5.222   -14.010 -19.273 1.00 36.43 ? 217 GLN A C   1 
ATOM   1564 O O   . GLN A 1 237 ? 6.055   -14.615 -19.961 1.00 34.70 ? 217 GLN A O   1 
ATOM   1565 C CB  . GLN A 1 237 ? 4.883   -11.575 -19.797 1.00 40.94 ? 217 GLN A CB  1 
ATOM   1566 C CG  . GLN A 1 237 ? 4.173   -10.542 -20.653 1.00 45.43 ? 217 GLN A CG  1 
ATOM   1567 C CD  . GLN A 1 237 ? 4.809   -9.182  -20.497 1.00 46.77 ? 217 GLN A CD  1 
ATOM   1568 O OE1 . GLN A 1 237 ? 4.199   -8.251  -19.971 1.00 43.10 ? 217 GLN A OE1 1 
ATOM   1569 N NE2 . GLN A 1 237 ? 6.047   -9.068  -20.961 1.00 42.14 ? 217 GLN A NE2 1 
ATOM   1570 N N   . LEU A 1 238 ? 5.017   -14.224 -17.964 1.00 36.63 ? 218 LEU A N   1 
ATOM   1571 C CA  . LEU A 1 238 ? 5.913   -15.038 -17.093 1.00 34.61 ? 218 LEU A CA  1 
ATOM   1572 C C   . LEU A 1 238 ? 5.861   -16.511 -17.497 1.00 30.74 ? 218 LEU A C   1 
ATOM   1573 O O   . LEU A 1 238 ? 6.905   -17.120 -17.688 1.00 28.44 ? 218 LEU A O   1 
ATOM   1574 C CB  . LEU A 1 238 ? 5.564   -14.814 -15.613 1.00 36.58 ? 218 LEU A CB  1 
ATOM   1575 C CG  . LEU A 1 238 ? 6.388   -13.727 -14.911 1.00 37.71 ? 218 LEU A CG  1 
ATOM   1576 C CD1 . LEU A 1 238 ? 6.376   -12.425 -15.696 1.00 37.32 ? 218 LEU A CD1 1 
ATOM   1577 C CD2 . LEU A 1 238 ? 5.908   -13.492 -13.482 1.00 40.07 ? 218 LEU A CD2 1 
ATOM   1578 N N   . PRO A 1 239 ? 4.683   -17.157 -17.639 1.00 31.20 ? 219 PRO A N   1 
ATOM   1579 C CA  . PRO A 1 239 ? 4.642   -18.535 -18.137 1.00 28.43 ? 219 PRO A CA  1 
ATOM   1580 C C   . PRO A 1 239 ? 5.212   -18.675 -19.556 1.00 28.05 ? 219 PRO A C   1 
ATOM   1581 O O   . PRO A 1 239 ? 5.788   -19.704 -19.842 1.00 27.84 ? 219 PRO A O   1 
ATOM   1582 C CB  . PRO A 1 239 ? 3.165   -18.914 -18.102 1.00 29.92 ? 219 PRO A CB  1 
ATOM   1583 C CG  . PRO A 1 239 ? 2.570   -17.949 -17.099 1.00 29.91 ? 219 PRO A CG  1 
ATOM   1584 C CD  . PRO A 1 239 ? 3.356   -16.660 -17.251 1.00 30.28 ? 219 PRO A CD  1 
ATOM   1585 N N   . VAL A 1 240 ? 5.095   -17.633 -20.389 1.00 28.21 ? 220 VAL A N   1 
ATOM   1586 C CA  . VAL A 1 240 ? 5.732   -17.608 -21.743 1.00 27.07 ? 220 VAL A CA  1 
ATOM   1587 C C   . VAL A 1 240 ? 7.252   -17.733 -21.561 1.00 23.84 ? 220 VAL A C   1 
ATOM   1588 O O   . VAL A 1 240 ? 7.835   -18.676 -22.133 1.00 22.32 ? 220 VAL A O   1 
ATOM   1589 C CB  . VAL A 1 240 ? 5.324   -16.370 -22.573 1.00 28.48 ? 220 VAL A CB  1 
ATOM   1590 C CG1 . VAL A 1 240 ? 6.180   -16.226 -23.827 1.00 28.58 ? 220 VAL A CG1 1 
ATOM   1591 C CG2 . VAL A 1 240 ? 3.849   -16.419 -22.953 1.00 27.92 ? 220 VAL A CG2 1 
ATOM   1592 N N   . ILE A 1 241 ? 7.859   -16.870 -20.741 1.00 21.72 ? 221 ILE A N   1 
ATOM   1593 C CA  . ILE A 1 241 ? 9.332   -16.874 -20.456 1.00 20.67 ? 221 ILE A CA  1 
ATOM   1594 C C   . ILE A 1 241 ? 9.735   -18.231 -19.851 1.00 20.10 ? 221 ILE A C   1 
ATOM   1595 O O   . ILE A 1 241 ? 10.757  -18.790 -20.285 1.00 19.77 ? 221 ILE A O   1 
ATOM   1596 C CB  . ILE A 1 241 ? 9.721   -15.675 -19.565 1.00 21.55 ? 221 ILE A CB  1 
ATOM   1597 C CG1 . ILE A 1 241 ? 9.334   -14.357 -20.249 1.00 22.09 ? 221 ILE A CG1 1 
ATOM   1598 C CG2 . ILE A 1 241 ? 11.202  -15.714 -19.179 1.00 20.65 ? 221 ILE A CG2 1 
ATOM   1599 C CD1 . ILE A 1 241 ? 9.695   -13.100 -19.491 1.00 23.94 ? 221 ILE A CD1 1 
ATOM   1600 N N   . ALA A 1 242 ? 8.966   -18.767 -18.899 1.00 19.31 ? 222 ALA A N   1 
ATOM   1601 C CA  . ALA A 1 242 ? 9.246   -20.071 -18.245 1.00 18.06 ? 222 ALA A CA  1 
ATOM   1602 C C   . ALA A 1 242 ? 9.428   -21.157 -19.307 1.00 17.97 ? 222 ALA A C   1 
ATOM   1603 O O   . ALA A 1 242 ? 10.433  -21.892 -19.243 1.00 16.72 ? 222 ALA A O   1 
ATOM   1604 C CB  . ALA A 1 242 ? 8.138   -20.431 -17.292 1.00 18.72 ? 222 ALA A CB  1 
ATOM   1605 N N   . GLY A 1 243 ? 8.469   -21.245 -20.236 1.00 18.08 ? 223 GLY A N   1 
ATOM   1606 C CA  . GLY A 1 243 ? 8.474   -22.167 -21.398 1.00 18.79 ? 223 GLY A CA  1 
ATOM   1607 C C   . GLY A 1 243 ? 9.739   -22.055 -22.232 1.00 17.67 ? 223 GLY A C   1 
ATOM   1608 O O   . GLY A 1 243 ? 10.391  -23.095 -22.485 1.00 15.25 ? 223 GLY A O   1 
ATOM   1609 N N   . ARG A 1 244 ? 10.054  -20.832 -22.668 1.00 16.96 ? 224 ARG A N   1 
ATOM   1610 C CA  . ARG A 1 244 ? 11.293  -20.456 -23.397 1.00 17.54 ? 224 ARG A CA  1 
ATOM   1611 C C   . ARG A 1 244 ? 12.538  -20.951 -22.646 1.00 16.04 ? 224 ARG A C   1 
ATOM   1612 O O   . ARG A 1 244 ? 13.425  -21.558 -23.296 1.00 14.62 ? 224 ARG A O   1 
ATOM   1613 C CB  . ARG A 1 244 ? 11.319  -18.930 -23.569 1.00 19.14 ? 224 ARG A CB  1 
ATOM   1614 C CG  . ARG A 1 244 ? 10.415  -18.438 -24.681 1.00 23.43 ? 224 ARG A CG  1 
ATOM   1615 C CD  . ARG A 1 244 ? 10.361  -16.928 -24.710 1.00 27.19 ? 224 ARG A CD  1 
ATOM   1616 N NE  . ARG A 1 244 ? 9.699   -16.393 -25.901 1.00 32.78 ? 224 ARG A NE  1 
ATOM   1617 C CZ  . ARG A 1 244 ? 9.160   -15.165 -25.973 1.00 35.43 ? 224 ARG A CZ  1 
ATOM   1618 N NH1 . ARG A 1 244 ? 8.572   -14.759 -27.085 1.00 39.24 ? 224 ARG A NH1 1 
ATOM   1619 N NH2 . ARG A 1 244 ? 9.223   -14.341 -24.939 1.00 33.96 ? 224 ARG A NH2 1 
ATOM   1620 N N   . VAL A 1 245 ? 12.621  -20.695 -21.337 1.00 15.71 ? 225 VAL A N   1 
ATOM   1621 C CA  . VAL A 1 245 ? 13.760  -21.140 -20.478 1.00 16.36 ? 225 VAL A CA  1 
ATOM   1622 C C   . VAL A 1 245 ? 13.850  -22.678 -20.498 1.00 17.12 ? 225 VAL A C   1 
ATOM   1623 O O   . VAL A 1 245 ? 14.987  -23.201 -20.715 1.00 16.55 ? 225 VAL A O   1 
ATOM   1624 C CB  . VAL A 1 245 ? 13.656  -20.566 -19.050 1.00 17.78 ? 225 VAL A CB  1 
ATOM   1625 C CG1 . VAL A 1 245 ? 14.707  -21.164 -18.104 1.00 18.40 ? 225 VAL A CG1 1 
ATOM   1626 C CG2 . VAL A 1 245 ? 13.791  -19.052 -19.062 1.00 17.63 ? 225 VAL A CG2 1 
ATOM   1627 N N   . ARG A 1 246 ? 12.736  -23.396 -20.364 1.00 17.73 ? 226 ARG A N   1 
ATOM   1628 C CA  . ARG A 1 246 ? 12.791  -24.881 -20.261 1.00 20.73 ? 226 ARG A CA  1 
ATOM   1629 C C   . ARG A 1 246 ? 13.246  -25.486 -21.593 1.00 23.52 ? 226 ARG A C   1 
ATOM   1630 O O   . ARG A 1 246 ? 13.970  -26.482 -21.545 1.00 24.88 ? 226 ARG A O   1 
ATOM   1631 C CB  . ARG A 1 246 ? 11.465  -25.525 -19.862 1.00 21.87 ? 226 ARG A CB  1 
ATOM   1632 C CG  . ARG A 1 246 ? 11.633  -27.029 -19.676 1.00 24.09 ? 226 ARG A CG  1 
ATOM   1633 C CD  . ARG A 1 246 ? 10.352  -27.731 -19.334 1.00 25.82 ? 226 ARG A CD  1 
ATOM   1634 N NE  . ARG A 1 246 ? 9.388   -27.567 -20.408 1.00 28.79 ? 226 ARG A NE  1 
ATOM   1635 C CZ  . ARG A 1 246 ? 8.083   -27.785 -20.284 1.00 30.69 ? 226 ARG A CZ  1 
ATOM   1636 N NH1 . ARG A 1 246 ? 7.590   -28.208 -19.132 1.00 31.51 ? 226 ARG A NH1 1 
ATOM   1637 N NH2 . ARG A 1 246 ? 7.275   -27.595 -21.316 1.00 31.53 ? 226 ARG A NH2 1 
ATOM   1638 N N   . GLU A 1 247 ? 12.845  -24.903 -22.732 1.00 26.04 ? 227 GLU A N   1 
ATOM   1639 C CA  . GLU A 1 247 ? 13.232  -25.374 -24.099 1.00 25.83 ? 227 GLU A CA  1 
ATOM   1640 C C   . GLU A 1 247 ? 14.550  -24.735 -24.556 1.00 25.10 ? 227 GLU A C   1 
ATOM   1641 O O   . GLU A 1 247 ? 14.973  -25.018 -25.671 1.00 28.21 ? 227 GLU A O   1 
ATOM   1642 C CB  . GLU A 1 247 ? 12.136  -25.041 -25.105 1.00 27.48 ? 227 GLU A CB  1 
ATOM   1643 C CG  . GLU A 1 247 ? 10.743  -25.390 -24.617 1.00 30.62 ? 227 GLU A CG  1 
ATOM   1644 C CD  . GLU A 1 247 ? 10.538  -26.867 -24.369 1.00 32.74 ? 227 GLU A CD  1 
ATOM   1645 O OE1 . GLU A 1 247 ? 10.150  -27.236 -23.244 1.00 35.26 ? 227 GLU A OE1 1 
ATOM   1646 O OE2 . GLU A 1 247 ? 10.767  -27.628 -25.312 1.00 36.46 ? 227 GLU A OE2 1 
ATOM   1647 N N   . LYS A 1 248 ? 15.175  -23.876 -23.752 1.00 25.19 ? 228 LYS A N   1 
ATOM   1648 C CA  . LYS A 1 248 ? 16.451  -23.210 -24.118 1.00 24.87 ? 228 LYS A CA  1 
ATOM   1649 C C   . LYS A 1 248 ? 16.232  -22.441 -25.432 1.00 22.98 ? 228 LYS A C   1 
ATOM   1650 O O   . LYS A 1 248 ? 17.095  -22.498 -26.309 1.00 21.36 ? 228 LYS A O   1 
ATOM   1651 C CB  . LYS A 1 248 ? 17.560  -24.269 -24.174 1.00 28.21 ? 228 LYS A CB  1 
ATOM   1652 C CG  . LYS A 1 248 ? 17.570  -25.243 -22.995 1.00 33.07 ? 228 LYS A CG  1 
ATOM   1653 C CD  . LYS A 1 248 ? 18.956  -25.617 -22.448 1.00 37.49 ? 228 LYS A CD  1 
ATOM   1654 C CE  . LYS A 1 248 ? 19.959  -26.053 -23.499 1.00 40.80 ? 228 LYS A CE  1 
ATOM   1655 N NZ  . LYS A 1 248 ? 20.996  -25.017 -23.752 1.00 46.43 ? 228 LYS A NZ  1 
ATOM   1656 N N   . GLN A 1 249 ? 15.073  -21.784 -25.577 1.00 21.16 ? 229 GLN A N   1 
ATOM   1657 C CA  . GLN A 1 249 ? 14.729  -20.936 -26.752 1.00 20.74 ? 229 GLN A CA  1 
ATOM   1658 C C   . GLN A 1 249 ? 14.899  -19.467 -26.359 1.00 20.13 ? 229 GLN A C   1 
ATOM   1659 O O   . GLN A 1 249 ? 13.921  -18.861 -25.874 1.00 20.47 ? 229 GLN A O   1 
ATOM   1660 C CB  . GLN A 1 249 ? 13.331  -21.306 -27.252 1.00 19.78 ? 229 GLN A CB  1 
ATOM   1661 C CG  . GLN A 1 249 ? 13.320  -22.720 -27.840 1.00 19.53 ? 229 GLN A CG  1 
ATOM   1662 C CD  . GLN A 1 249 ? 14.035  -22.775 -29.166 1.00 18.34 ? 229 GLN A CD  1 
ATOM   1663 O OE1 . GLN A 1 249 ? 13.624  -22.104 -30.118 1.00 19.13 ? 229 GLN A OE1 1 
ATOM   1664 N NE2 . GLN A 1 249 ? 15.135  -23.525 -29.234 1.00 17.54 ? 229 GLN A NE2 1 
ATOM   1665 N N   . TYR A 1 250 ? 16.113  -18.943 -26.529 1.00 18.49 ? 230 TYR A N   1 
ATOM   1666 C CA  . TYR A 1 250 ? 16.515  -17.625 -25.988 1.00 20.22 ? 230 TYR A CA  1 
ATOM   1667 C C   . TYR A 1 250 ? 16.176  -16.542 -27.013 1.00 20.10 ? 230 TYR A C   1 
ATOM   1668 O O   . TYR A 1 250 ? 16.066  -15.388 -26.632 1.00 20.78 ? 230 TYR A O   1 
ATOM   1669 C CB  . TYR A 1 250 ? 17.984  -17.654 -25.548 1.00 20.74 ? 230 TYR A CB  1 
ATOM   1670 C CG  . TYR A 1 250 ? 18.297  -18.785 -24.596 1.00 20.94 ? 230 TYR A CG  1 
ATOM   1671 C CD1 . TYR A 1 250 ? 17.462  -19.068 -23.518 1.00 20.02 ? 230 TYR A CD1 1 
ATOM   1672 C CD2 . TYR A 1 250 ? 19.426  -19.575 -24.772 1.00 20.29 ? 230 TYR A CD2 1 
ATOM   1673 C CE1 . TYR A 1 250 ? 17.757  -20.096 -22.634 1.00 21.15 ? 230 TYR A CE1 1 
ATOM   1674 C CE2 . TYR A 1 250 ? 19.711  -20.634 -23.924 1.00 20.42 ? 230 TYR A CE2 1 
ATOM   1675 C CZ  . TYR A 1 250 ? 18.877  -20.888 -22.847 1.00 21.63 ? 230 TYR A CZ  1 
ATOM   1676 O OH  . TYR A 1 250 ? 19.146  -21.936 -22.025 1.00 22.38 ? 230 TYR A OH  1 
ATOM   1677 N N   . VAL A 1 251 ? 15.976  -16.917 -28.270 1.00 20.73 ? 231 VAL A N   1 
ATOM   1678 C CA  . VAL A 1 251 ? 15.625  -15.963 -29.356 1.00 21.67 ? 231 VAL A CA  1 
ATOM   1679 C C   . VAL A 1 251 ? 14.100  -15.844 -29.432 1.00 21.04 ? 231 VAL A C   1 
ATOM   1680 O O   . VAL A 1 251 ? 13.401  -16.880 -29.459 1.00 20.74 ? 231 VAL A O   1 
ATOM   1681 C CB  . VAL A 1 251 ? 16.257  -16.390 -30.695 1.00 22.12 ? 231 VAL A CB  1 
ATOM   1682 C CG1 . VAL A 1 251 ? 15.791  -15.503 -31.824 1.00 23.13 ? 231 VAL A CG1 1 
ATOM   1683 C CG2 . VAL A 1 251 ? 17.777  -16.372 -30.610 1.00 22.90 ? 231 VAL A CG2 1 
ATOM   1684 N N   . GLY A 1 252 ? 13.596  -14.608 -29.485 1.00 21.79 ? 232 GLY A N   1 
ATOM   1685 C CA  . GLY A 1 252 ? 12.147  -14.337 -29.465 1.00 21.44 ? 232 GLY A CA  1 
ATOM   1686 C C   . GLY A 1 252 ? 11.768  -13.594 -28.203 1.00 22.25 ? 232 GLY A C   1 
ATOM   1687 O O   . GLY A 1 252 ? 11.872  -14.157 -27.129 1.00 25.68 ? 232 GLY A O   1 
ATOM   1688 N N   . GLY A 1 253 ? 11.297  -12.366 -28.353 1.00 24.19 ? 233 GLY A N   1 
ATOM   1689 C CA  . GLY A 1 253 ? 11.085  -11.424 -27.247 1.00 22.78 ? 233 GLY A CA  1 
ATOM   1690 C C   . GLY A 1 253 ? 11.985  -10.237 -27.457 1.00 21.46 ? 233 GLY A C   1 
ATOM   1691 O O   . GLY A 1 253 ? 12.946  -10.368 -28.237 1.00 20.92 ? 233 GLY A O   1 
ATOM   1692 N N   . SER A 1 254 ? 11.725  -9.138  -26.755 1.00 21.01 ? 234 SER A N   1 
ATOM   1693 C CA  . SER A 1 254 ? 12.541  -7.912  -26.889 1.00 22.18 ? 234 SER A CA  1 
ATOM   1694 C C   . SER A 1 254 ? 13.954  -8.227  -26.420 1.00 19.93 ? 234 SER A C   1 
ATOM   1695 O O   . SER A 1 254 ? 14.168  -8.907  -25.434 1.00 19.96 ? 234 SER A O   1 
ATOM   1696 C CB  . SER A 1 254 ? 11.944  -6.751  -26.183 1.00 23.03 ? 234 SER A CB  1 
ATOM   1697 O OG  . SER A 1 254 ? 11.606  -7.127  -24.887 1.00 26.87 ? 234 SER A OG  1 
ATOM   1698 N N   . PRO A 1 255 ? 14.971  -7.812  -27.178 1.00 19.90 ? 235 PRO A N   1 
ATOM   1699 C CA  . PRO A 1 255 ? 16.330  -8.271  -26.907 1.00 19.40 ? 235 PRO A CA  1 
ATOM   1700 C C   . PRO A 1 255 ? 16.926  -7.627  -25.653 1.00 18.39 ? 235 PRO A C   1 
ATOM   1701 O O   . PRO A 1 255 ? 16.581  -6.492  -25.305 1.00 17.45 ? 235 PRO A O   1 
ATOM   1702 C CB  . PRO A 1 255 ? 17.100  -7.837  -28.155 1.00 19.29 ? 235 PRO A CB  1 
ATOM   1703 C CG  . PRO A 1 255 ? 16.322  -6.643  -28.679 1.00 19.85 ? 235 PRO A CG  1 
ATOM   1704 C CD  . PRO A 1 255 ? 14.867  -6.937  -28.352 1.00 19.80 ? 235 PRO A CD  1 
ATOM   1705 N N   . ILE A 1 256 ? 17.876  -8.340  -25.058 1.00 18.21 ? 236 ILE A N   1 
ATOM   1706 C CA  . ILE A 1 256 ? 18.679  -7.877  -23.890 1.00 17.84 ? 236 ILE A CA  1 
ATOM   1707 C C   . ILE A 1 256 ? 19.284  -6.487  -24.168 1.00 17.60 ? 236 ILE A C   1 
ATOM   1708 O O   . ILE A 1 256 ? 19.315  -5.684  -23.218 1.00 16.06 ? 236 ILE A O   1 
ATOM   1709 C CB  . ILE A 1 256 ? 19.730  -8.940  -23.494 1.00 18.57 ? 236 ILE A CB  1 
ATOM   1710 C CG1 . ILE A 1 256 ? 19.067  -10.183 -22.897 1.00 18.29 ? 236 ILE A CG1 1 
ATOM   1711 C CG2 . ILE A 1 256 ? 20.783  -8.361  -22.548 1.00 19.08 ? 236 ILE A CG2 1 
ATOM   1712 C CD1 . ILE A 1 256 ? 19.997  -11.373 -22.759 1.00 19.67 ? 236 ILE A CD1 1 
ATOM   1713 N N   . THR A 1 257 ? 19.760  -6.183  -25.381 1.00 18.12 ? 237 THR A N   1 
ATOM   1714 C CA  . THR A 1 257 ? 20.383  -4.855  -25.694 1.00 19.35 ? 237 THR A CA  1 
ATOM   1715 C C   . THR A 1 257 ? 19.373  -3.737  -25.404 1.00 18.86 ? 237 THR A C   1 
ATOM   1716 O O   . THR A 1 257 ? 19.730  -2.754  -24.703 1.00 18.09 ? 237 THR A O   1 
ATOM   1717 C CB  . THR A 1 257 ? 20.874  -4.753  -27.142 1.00 20.62 ? 237 THR A CB  1 
ATOM   1718 O OG1 . THR A 1 257 ? 19.797  -5.205  -27.952 1.00 21.01 ? 237 THR A OG1 1 
ATOM   1719 C CG2 . THR A 1 257 ? 22.096  -5.596  -27.428 1.00 21.84 ? 237 THR A CG2 1 
ATOM   1720 N N   . MET A 1 258 ? 18.141  -3.900  -25.888 1.00 20.04 ? 238 MET A N   1 
ATOM   1721 C CA  . MET A 1 258 ? 17.015  -2.965  -25.610 1.00 20.34 ? 238 MET A CA  1 
ATOM   1722 C C   . MET A 1 258 ? 16.680  -2.930  -24.113 1.00 18.75 ? 238 MET A C   1 
ATOM   1723 O O   . MET A 1 258 ? 16.467  -1.826  -23.580 1.00 17.09 ? 238 MET A O   1 
ATOM   1724 C CB  . MET A 1 258 ? 15.786  -3.354  -26.425 1.00 23.33 ? 238 MET A CB  1 
ATOM   1725 C CG  . MET A 1 258 ? 15.924  -2.889  -27.853 1.00 27.38 ? 238 MET A CG  1 
ATOM   1726 S SD  . MET A 1 258 ? 15.724  -1.094  -27.939 1.00 30.66 ? 238 MET A SD  1 
ATOM   1727 C CE  . MET A 1 258 ? 13.944  -1.134  -27.852 1.00 33.25 ? 238 MET A CE  1 
ATOM   1728 N N   . GLY A 1 259 ? 16.662  -4.078  -23.438 1.00 17.25 ? 239 GLY A N   1 
ATOM   1729 C CA  . GLY A 1 259 ? 16.538  -4.120  -21.963 1.00 17.79 ? 239 GLY A CA  1 
ATOM   1730 C C   . GLY A 1 259 ? 17.630  -3.292  -21.287 1.00 17.13 ? 239 GLY A C   1 
ATOM   1731 O O   . GLY A 1 259 ? 17.329  -2.544  -20.337 1.00 15.82 ? 239 GLY A O   1 
ATOM   1732 N N   . LEU A 1 260 ? 18.875  -3.422  -21.737 1.00 17.05 ? 240 LEU A N   1 
ATOM   1733 C CA  . LEU A 1 260 ? 20.027  -2.738  -21.099 1.00 18.26 ? 240 LEU A CA  1 
ATOM   1734 C C   . LEU A 1 260 ? 19.880  -1.224  -21.302 1.00 18.99 ? 240 LEU A C   1 
ATOM   1735 O O   . LEU A 1 260 ? 20.100  -0.477  -20.337 1.00 18.73 ? 240 LEU A O   1 
ATOM   1736 C CB  . LEU A 1 260 ? 21.330  -3.247  -21.706 1.00 18.68 ? 240 LEU A CB  1 
ATOM   1737 C CG  . LEU A 1 260 ? 22.580  -2.637  -21.087 1.00 19.79 ? 240 LEU A CG  1 
ATOM   1738 C CD1 . LEU A 1 260 ? 22.607  -2.909  -19.584 1.00 20.40 ? 240 LEU A CD1 1 
ATOM   1739 C CD2 . LEU A 1 260 ? 23.830  -3.148  -21.785 1.00 19.13 ? 240 LEU A CD2 1 
ATOM   1740 N N   . GLU A 1 261 ? 19.459  -0.799  -22.492 1.00 19.89 ? 241 GLU A N   1 
ATOM   1741 C CA  . GLU A 1 261 ? 19.309  0.644   -22.826 1.00 21.46 ? 241 GLU A CA  1 
ATOM   1742 C C   . GLU A 1 261 ? 18.149  1.232   -22.010 1.00 18.91 ? 241 GLU A C   1 
ATOM   1743 O O   . GLU A 1 261 ? 18.286  2.354   -21.530 1.00 17.81 ? 241 GLU A O   1 
ATOM   1744 C CB  . GLU A 1 261 ? 19.138  0.833   -24.336 1.00 24.77 ? 241 GLU A CB  1 
ATOM   1745 C CG  . GLU A 1 261 ? 19.322  2.263   -24.775 1.00 29.02 ? 241 GLU A CG  1 
ATOM   1746 C CD  . GLU A 1 261 ? 20.722  2.814   -24.575 1.00 31.78 ? 241 GLU A CD  1 
ATOM   1747 O OE1 . GLU A 1 261 ? 20.898  4.024   -24.781 1.00 32.59 ? 241 GLU A OE1 1 
ATOM   1748 O OE2 . GLU A 1 261 ? 21.638  2.020   -24.247 1.00 34.93 ? 241 GLU A OE2 1 
ATOM   1749 N N   . ALA A 1 262 ? 17.076  0.482   -21.789 1.00 18.68 ? 242 ALA A N   1 
ATOM   1750 C CA  . ALA A 1 262 ? 15.956  0.925   -20.919 1.00 18.03 ? 242 ALA A CA  1 
ATOM   1751 C C   . ALA A 1 262 ? 16.472  1.124   -19.488 1.00 16.78 ? 242 ALA A C   1 
ATOM   1752 O O   . ALA A 1 262 ? 16.087  2.097   -18.833 1.00 17.15 ? 242 ALA A O   1 
ATOM   1753 C CB  . ALA A 1 262 ? 14.805  -0.052  -20.973 1.00 17.32 ? 242 ALA A CB  1 
ATOM   1754 N N   . LEU A 1 263 ? 17.358  0.259   -19.026 1.00 16.69 ? 243 LEU A N   1 
ATOM   1755 C CA  . LEU A 1 263 ? 17.996  0.425   -17.685 1.00 17.31 ? 243 LEU A CA  1 
ATOM   1756 C C   . LEU A 1 263 ? 18.876  1.681   -17.693 1.00 16.19 ? 243 LEU A C   1 
ATOM   1757 O O   . LEU A 1 263 ? 18.805  2.409   -16.737 1.00 18.09 ? 243 LEU A O   1 
ATOM   1758 C CB  . LEU A 1 263 ? 18.770  -0.828  -17.278 1.00 16.11 ? 243 LEU A CB  1 
ATOM   1759 C CG  . LEU A 1 263 ? 17.893  -1.991  -16.825 1.00 16.38 ? 243 LEU A CG  1 
ATOM   1760 C CD1 . LEU A 1 263 ? 18.682  -3.277  -16.744 1.00 16.80 ? 243 LEU A CD1 1 
ATOM   1761 C CD2 . LEU A 1 263 ? 17.221  -1.689  -15.492 1.00 16.52 ? 243 LEU A CD2 1 
ATOM   1762 N N   . GLU A 1 264 ? 19.617  1.968   -18.748 1.00 17.15 ? 244 GLU A N   1 
ATOM   1763 C CA  . GLU A 1 264 ? 20.455  3.202   -18.809 1.00 17.77 ? 244 GLU A CA  1 
ATOM   1764 C C   . GLU A 1 264 ? 19.534  4.430   -18.847 1.00 15.92 ? 244 GLU A C   1 
ATOM   1765 O O   . GLU A 1 264 ? 19.862  5.437   -18.198 1.00 15.82 ? 244 GLU A O   1 
ATOM   1766 C CB  . GLU A 1 264 ? 21.418  3.156   -20.004 1.00 21.01 ? 244 GLU A CB  1 
ATOM   1767 C CG  . GLU A 1 264 ? 22.510  2.097   -19.877 1.00 25.43 ? 244 GLU A CG  1 
ATOM   1768 C CD  . GLU A 1 264 ? 23.506  2.247   -18.725 1.00 28.16 ? 244 GLU A CD  1 
ATOM   1769 O OE1 . GLU A 1 264 ? 24.138  1.221   -18.335 1.00 33.21 ? 244 GLU A OE1 1 
ATOM   1770 O OE2 . GLU A 1 264 ? 23.681  3.392   -18.231 1.00 33.61 ? 244 GLU A OE2 1 
ATOM   1771 N N   . ASN A 1 265 ? 18.401  4.353   -19.556 1.00 14.37 ? 245 ASN A N   1 
ATOM   1772 C CA  . ASN A 1 265 ? 17.397  5.441   -19.592 1.00 15.01 ? 245 ASN A CA  1 
ATOM   1773 C C   . ASN A 1 265 ? 16.877  5.681   -18.165 1.00 14.89 ? 245 ASN A C   1 
ATOM   1774 O O   . ASN A 1 265 ? 16.794  6.849   -17.757 1.00 14.67 ? 245 ASN A O   1 
ATOM   1775 C CB  . ASN A 1 265 ? 16.308  5.163   -20.647 1.00 15.51 ? 245 ASN A CB  1 
ATOM   1776 C CG  . ASN A 1 265 ? 16.814  5.389   -22.058 1.00 16.75 ? 245 ASN A CG  1 
ATOM   1777 O OD1 . ASN A 1 265 ? 17.928  5.873   -22.249 1.00 16.65 ? 245 ASN A OD1 1 
ATOM   1778 N ND2 . ASN A 1 265 ? 16.001  5.089   -23.061 1.00 17.76 ? 245 ASN A ND2 1 
ATOM   1779 N N   . ILE A 1 266 ? 16.543  4.610   -17.443 1.00 14.59 ? 246 ILE A N   1 
ATOM   1780 C CA  . ILE A 1 266 ? 16.051  4.643   -16.034 1.00 15.51 ? 246 ILE A CA  1 
ATOM   1781 C C   . ILE A 1 266 ? 17.089  5.286   -15.108 1.00 15.92 ? 246 ILE A C   1 
ATOM   1782 O O   . ILE A 1 266 ? 16.715  6.135   -14.324 1.00 14.82 ? 246 ILE A O   1 
ATOM   1783 C CB  . ILE A 1 266 ? 15.688  3.225   -15.559 1.00 15.13 ? 246 ILE A CB  1 
ATOM   1784 C CG1 . ILE A 1 266 ? 14.399  2.746   -16.236 1.00 15.03 ? 246 ILE A CG1 1 
ATOM   1785 C CG2 . ILE A 1 266 ? 15.593  3.187   -14.035 1.00 14.94 ? 246 ILE A CG2 1 
ATOM   1786 C CD1 . ILE A 1 266 ? 14.234  1.243   -16.234 1.00 15.33 ? 246 ILE A CD1 1 
ATOM   1787 N N   . SER A 1 267 ? 18.340  4.854   -15.183 1.00 17.35 ? 247 SER A N   1 
ATOM   1788 C CA  . SER A 1 267 ? 19.467  5.422   -14.393 1.00 19.88 ? 247 SER A CA  1 
ATOM   1789 C C   . SER A 1 267 ? 19.582  6.945   -14.603 1.00 19.69 ? 247 SER A C   1 
ATOM   1790 O O   . SER A 1 267 ? 19.721  7.694   -13.588 1.00 17.13 ? 247 SER A O   1 
ATOM   1791 C CB  . SER A 1 267 ? 20.749  4.716   -14.748 1.00 21.21 ? 247 SER A CB  1 
ATOM   1792 O OG  . SER A 1 267 ? 21.834  5.375   -14.141 1.00 26.71 ? 247 SER A OG  1 
ATOM   1793 N N   . GLU A 1 268 ? 19.489  7.390   -15.864 1.00 20.07 ? 248 GLU A N   1 
ATOM   1794 C CA  . GLU A 1 268 ? 19.684  8.810   -16.265 1.00 20.27 ? 248 GLU A CA  1 
ATOM   1795 C C   . GLU A 1 268 ? 18.429  9.621   -15.915 1.00 19.18 ? 248 GLU A C   1 
ATOM   1796 O O   . GLU A 1 268 ? 18.573  10.764  -15.455 1.00 19.52 ? 248 GLU A O   1 
ATOM   1797 C CB  . GLU A 1 268 ? 20.046  8.915   -17.750 1.00 21.48 ? 248 GLU A CB  1 
ATOM   1798 C CG  . GLU A 1 268 ? 20.344  10.341  -18.193 1.00 25.33 ? 248 GLU A CG  1 
ATOM   1799 C CD  . GLU A 1 268 ? 21.519  10.996  -17.472 1.00 29.10 ? 248 GLU A CD  1 
ATOM   1800 O OE1 . GLU A 1 268 ? 22.320  10.267  -16.839 1.00 29.79 ? 248 GLU A OE1 1 
ATOM   1801 O OE2 . GLU A 1 268 ? 21.607  12.245  -17.500 1.00 37.76 ? 248 GLU A OE2 1 
ATOM   1802 N N   . THR A 1 269 ? 17.233  9.071   -16.122 1.00 18.19 ? 249 THR A N   1 
ATOM   1803 C CA  . THR A 1 269 ? 15.978  9.707   -15.643 1.00 16.87 ? 249 THR A CA  1 
ATOM   1804 C C   . THR A 1 269 ? 16.146  9.974   -14.145 1.00 18.31 ? 249 THR A C   1 
ATOM   1805 O O   . THR A 1 269 ? 15.877  11.103  -13.682 1.00 15.28 ? 249 THR A O   1 
ATOM   1806 C CB  . THR A 1 269 ? 14.748  8.836   -15.920 1.00 16.23 ? 249 THR A CB  1 
ATOM   1807 O OG1 . THR A 1 269 ? 14.655  8.669   -17.334 1.00 14.56 ? 249 THR A OG1 1 
ATOM   1808 C CG2 . THR A 1 269 ? 13.464  9.444   -15.381 1.00 15.79 ? 249 THR A CG2 1 
ATOM   1809 N N   . SER A 1 270 ? 16.566  8.952   -13.391 1.00 18.84 ? 250 SER A N   1 
ATOM   1810 C CA  . SER A 1 270 ? 16.726  9.085   -11.924 1.00 19.02 ? 250 SER A CA  1 
ATOM   1811 C C   . SER A 1 270 ? 17.747  10.212  -11.617 1.00 20.46 ? 250 SER A C   1 
ATOM   1812 O O   . SER A 1 270 ? 17.431  11.068  -10.772 1.00 19.83 ? 250 SER A O   1 
ATOM   1813 C CB  . SER A 1 270 ? 17.083  7.760   -11.302 1.00 19.83 ? 250 SER A CB  1 
ATOM   1814 O OG  . SER A 1 270 ? 16.082  6.789   -11.565 1.00 18.55 ? 250 SER A OG  1 
ATOM   1815 N N   . ARG A 1 271 ? 18.898  10.235  -12.294 1.00 20.79 ? 251 ARG A N   1 
ATOM   1816 C CA  . ARG A 1 271 ? 20.006  11.205  -12.058 1.00 22.69 ? 251 ARG A CA  1 
ATOM   1817 C C   . ARG A 1 271 ? 19.501  12.632  -12.298 1.00 21.41 ? 251 ARG A C   1 
ATOM   1818 O O   . ARG A 1 271 ? 19.752  13.494  -11.454 1.00 20.80 ? 251 ARG A O   1 
ATOM   1819 C CB  . ARG A 1 271 ? 21.224  10.899  -12.943 1.00 25.91 ? 251 ARG A CB  1 
ATOM   1820 C CG  . ARG A 1 271 ? 22.560  11.259  -12.296 1.00 30.63 ? 251 ARG A CG  1 
ATOM   1821 C CD  . ARG A 1 271 ? 23.793  11.121  -13.194 1.00 32.55 ? 251 ARG A CD  1 
ATOM   1822 N NE  . ARG A 1 271 ? 23.579  11.790  -14.475 1.00 35.91 ? 251 ARG A NE  1 
ATOM   1823 C CZ  . ARG A 1 271 ? 24.045  12.994  -14.815 1.00 37.01 ? 251 ARG A CZ  1 
ATOM   1824 N NH1 . ARG A 1 271 ? 23.768  13.490  -16.008 1.00 35.53 ? 251 ARG A NH1 1 
ATOM   1825 N NH2 . ARG A 1 271 ? 24.809  13.685  -13.986 1.00 36.46 ? 251 ARG A NH2 1 
ATOM   1826 N N   . GLU A 1 272 ? 18.751  12.857  -13.382 1.00 20.44 ? 252 GLU A N   1 
ATOM   1827 C CA  . GLU A 1 272 ? 18.157  14.179  -13.705 1.00 18.36 ? 252 GLU A CA  1 
ATOM   1828 C C   . GLU A 1 272 ? 17.391  14.679  -12.483 1.00 18.46 ? 252 GLU A C   1 
ATOM   1829 O O   . GLU A 1 272 ? 17.390  15.891  -12.235 1.00 17.83 ? 252 GLU A O   1 
ATOM   1830 C CB  . GLU A 1 272 ? 17.269  14.062  -14.942 1.00 17.79 ? 252 GLU A CB  1 
ATOM   1831 C CG  . GLU A 1 272 ? 18.060  13.800  -16.209 1.00 17.00 ? 252 GLU A CG  1 
ATOM   1832 C CD  . GLU A 1 272 ? 17.250  13.445  -17.456 1.00 16.90 ? 252 GLU A CD  1 
ATOM   1833 O OE1 . GLU A 1 272 ? 17.886  13.187  -18.478 1.00 14.83 ? 252 GLU A OE1 1 
ATOM   1834 O OE2 . GLU A 1 272 ? 15.980  13.455  -17.413 1.00 17.99 ? 252 GLU A OE2 1 
ATOM   1835 N N   . LEU A 1 273 ? 16.777  13.770  -11.734 1.00 17.56 ? 253 LEU A N   1 
ATOM   1836 C CA  . LEU A 1 273 ? 15.809  14.101  -10.668 1.00 17.45 ? 253 LEU A CA  1 
ATOM   1837 C C   . LEU A 1 273 ? 16.471  14.043  -9.286  1.00 17.94 ? 253 LEU A C   1 
ATOM   1838 O O   . LEU A 1 273 ? 15.736  14.223  -8.324  1.00 18.10 ? 253 LEU A O   1 
ATOM   1839 C CB  . LEU A 1 273 ? 14.645  13.113  -10.760 1.00 18.86 ? 253 LEU A CB  1 
ATOM   1840 C CG  . LEU A 1 273 ? 13.630  13.387  -11.877 1.00 19.05 ? 253 LEU A CG  1 
ATOM   1841 C CD1 . LEU A 1 273 ? 12.717  12.188  -12.042 1.00 19.72 ? 253 LEU A CD1 1 
ATOM   1842 C CD2 . LEU A 1 273 ? 12.799  14.634  -11.608 1.00 18.66 ? 253 LEU A CD2 1 
ATOM   1843 N N   . GLY A 1 274 ? 17.786  13.790  -9.203  1.00 17.80 ? 254 GLY A N   1 
ATOM   1844 C CA  . GLY A 1 274 ? 18.537  13.623  -7.942  1.00 18.97 ? 254 GLY A CA  1 
ATOM   1845 C C   . GLY A 1 274 ? 18.142  12.339  -7.221  1.00 20.45 ? 254 GLY A C   1 
ATOM   1846 O O   . GLY A 1 274 ? 18.116  12.342  -5.983  1.00 20.80 ? 254 GLY A O   1 
ATOM   1847 N N   . VAL A 1 275 ? 17.755  11.303  -7.971  1.00 20.30 ? 255 VAL A N   1 
ATOM   1848 C CA  . VAL A 1 275 ? 17.136  10.076  -7.397  1.00 19.85 ? 255 VAL A CA  1 
ATOM   1849 C C   . VAL A 1 275 ? 18.120  8.925   -7.586  1.00 18.24 ? 255 VAL A C   1 
ATOM   1850 O O   . VAL A 1 275 ? 18.742  8.841   -8.642  1.00 18.45 ? 255 VAL A O   1 
ATOM   1851 C CB  . VAL A 1 275 ? 15.759  9.759   -8.013  1.00 19.31 ? 255 VAL A CB  1 
ATOM   1852 C CG1 . VAL A 1 275 ? 15.251  8.399   -7.560  1.00 19.79 ? 255 VAL A CG1 1 
ATOM   1853 C CG2 . VAL A 1 275 ? 14.717  10.820  -7.708  1.00 19.80 ? 255 VAL A CG2 1 
ATOM   1854 N N   . GLY A 1 276 ? 18.227  8.064   -6.586  1.00 18.97 ? 256 GLY A N   1 
ATOM   1855 C CA  . GLY A 1 276 ? 19.180  6.939   -6.595  1.00 18.10 ? 256 GLY A CA  1 
ATOM   1856 C C   . GLY A 1 276 ? 18.653  5.828   -7.470  1.00 18.16 ? 256 GLY A C   1 
ATOM   1857 O O   . GLY A 1 276 ? 17.500  5.925   -7.885  1.00 15.32 ? 256 GLY A O   1 
ATOM   1858 N N   . VAL A 1 277 ? 19.473  4.811   -7.751  1.00 19.59 ? 257 VAL A N   1 
ATOM   1859 C CA  . VAL A 1 277 ? 19.152  3.799   -8.793  1.00 19.64 ? 257 VAL A CA  1 
ATOM   1860 C C   . VAL A 1 277 ? 19.392  2.407   -8.225  1.00 18.32 ? 257 VAL A C   1 
ATOM   1861 O O   . VAL A 1 277 ? 20.495  2.145   -7.716  1.00 17.44 ? 257 VAL A O   1 
ATOM   1862 C CB  . VAL A 1 277 ? 19.968  4.046   -10.073 1.00 21.96 ? 257 VAL A CB  1 
ATOM   1863 C CG1 . VAL A 1 277 ? 19.449  3.209   -11.222 1.00 23.56 ? 257 VAL A CG1 1 
ATOM   1864 C CG2 . VAL A 1 277 ? 19.980  5.522   -10.445 1.00 23.45 ? 257 VAL A CG2 1 
ATOM   1865 N N   . LEU A 1 278 ? 18.371  1.564   -8.296  1.00 16.77 ? 258 LEU A N   1 
ATOM   1866 C CA  . LEU A 1 278 ? 18.460  0.113   -8.004  1.00 15.62 ? 258 LEU A CA  1 
ATOM   1867 C C   . LEU A 1 278 ? 18.699  -0.612  -9.334  1.00 14.33 ? 258 LEU A C   1 
ATOM   1868 O O   . LEU A 1 278 ? 19.178  0.029   -10.279 1.00 15.41 ? 258 LEU A O   1 
ATOM   1869 C CB  . LEU A 1 278 ? 17.167  -0.302  -7.287  1.00 15.25 ? 258 LEU A CB  1 
ATOM   1870 C CG  . LEU A 1 278 ? 16.844  0.508   -6.037  1.00 14.43 ? 258 LEU A CG  1 
ATOM   1871 C CD1 . LEU A 1 278 ? 15.559  0.051   -5.389  1.00 14.76 ? 258 LEU A CD1 1 
ATOM   1872 C CD2 . LEU A 1 278 ? 17.973  0.431   -5.023  1.00 15.48 ? 258 LEU A CD2 1 
ATOM   1873 N N   . LEU A 1 279 ? 18.411  -1.907  -9.394  1.00 14.75 ? 259 LEU A N   1 
ATOM   1874 C CA  . LEU A 1 279 ? 18.487  -2.751  -10.612 1.00 15.48 ? 259 LEU A CA  1 
ATOM   1875 C C   . LEU A 1 279 ? 19.937  -2.899  -11.100 1.00 14.59 ? 259 LEU A C   1 
ATOM   1876 O O   . LEU A 1 279 ? 20.123  -3.367  -12.224 1.00 15.42 ? 259 LEU A O   1 
ATOM   1877 C CB  . LEU A 1 279 ? 17.572  -2.162  -11.691 1.00 16.08 ? 259 LEU A CB  1 
ATOM   1878 C CG  . LEU A 1 279 ? 16.093  -2.043  -11.292 1.00 16.09 ? 259 LEU A CG  1 
ATOM   1879 C CD1 . LEU A 1 279 ? 15.294  -1.195  -12.261 1.00 15.81 ? 259 LEU A CD1 1 
ATOM   1880 C CD2 . LEU A 1 279 ? 15.458  -3.407  -11.181 1.00 16.68 ? 259 LEU A CD2 1 
ATOM   1881 N N   . GLY A 1 280 ? 20.934  -2.588  -10.274 1.00 15.33 ? 260 GLY A N   1 
ATOM   1882 C CA  . GLY A 1 280 ? 22.363  -2.719  -10.635 1.00 14.90 ? 260 GLY A CA  1 
ATOM   1883 C C   . GLY A 1 280 ? 22.700  -4.138  -11.088 1.00 15.72 ? 260 GLY A C   1 
ATOM   1884 O O   . GLY A 1 280 ? 23.288  -4.274  -12.168 1.00 16.07 ? 260 GLY A O   1 
ATOM   1885 N N   . SER A 1 281 ? 22.300  -5.173  -10.331 1.00 15.00 ? 261 SER A N   1 
ATOM   1886 C CA  . SER A 1 281 ? 22.640  -6.589  -10.643 1.00 15.58 ? 261 SER A CA  1 
ATOM   1887 C C   . SER A 1 281 ? 22.073  -6.938  -12.024 1.00 16.21 ? 261 SER A C   1 
ATOM   1888 O O   . SER A 1 281 ? 22.730  -7.704  -12.774 1.00 15.52 ? 261 SER A O   1 
ATOM   1889 C CB  . SER A 1 281 ? 22.155  -7.559  -9.584  1.00 16.69 ? 261 SER A CB  1 
ATOM   1890 O OG  . SER A 1 281 ? 22.602  -7.212  -8.274  1.00 16.66 ? 261 SER A OG  1 
ATOM   1891 N N   . MET A 1 282 ? 20.892  -6.406  -12.365 1.00 16.45 ? 262 MET A N   1 
ATOM   1892 C CA  . MET A 1 282 ? 20.265  -6.617  -13.699 1.00 16.11 ? 262 MET A CA  1 
ATOM   1893 C C   . MET A 1 282 ? 21.097  -5.920  -14.799 1.00 16.71 ? 262 MET A C   1 
ATOM   1894 O O   . MET A 1 282 ? 21.374  -6.520  -15.826 1.00 15.60 ? 262 MET A O   1 
ATOM   1895 C CB  . MET A 1 282 ? 18.843  -6.062  -13.697 1.00 16.52 ? 262 MET A CB  1 
ATOM   1896 C CG  . MET A 1 282 ? 17.973  -6.574  -14.838 1.00 16.85 ? 262 MET A CG  1 
ATOM   1897 S SD  . MET A 1 282 ? 17.948  -8.394  -14.943 1.00 15.49 ? 262 MET A SD  1 
ATOM   1898 C CE  . MET A 1 282 ? 16.481  -8.633  -15.955 1.00 16.78 ? 262 MET A CE  1 
ATOM   1899 N N   . ARG A 1 283 ? 21.437  -4.655  -14.589 1.00 18.98 ? 263 ARG A N   1 
ATOM   1900 C CA  . ARG A 1 283 ? 22.320  -3.862  -15.481 1.00 20.68 ? 263 ARG A CA  1 
ATOM   1901 C C   . ARG A 1 283 ? 23.603  -4.683  -15.734 1.00 19.96 ? 263 ARG A C   1 
ATOM   1902 O O   . ARG A 1 283 ? 23.974  -4.854  -16.892 1.00 18.98 ? 263 ARG A O   1 
ATOM   1903 C CB  . ARG A 1 283 ? 22.480  -2.494  -14.812 1.00 22.60 ? 263 ARG A CB  1 
ATOM   1904 C CG  . ARG A 1 283 ? 22.956  -1.357  -15.698 1.00 29.15 ? 263 ARG A CG  1 
ATOM   1905 C CD  . ARG A 1 283 ? 22.450  -0.020  -15.145 1.00 30.82 ? 263 ARG A CD  1 
ATOM   1906 N NE  . ARG A 1 283 ? 23.045  0.258   -13.836 1.00 31.97 ? 263 ARG A NE  1 
ATOM   1907 C CZ  . ARG A 1 283 ? 22.407  0.346   -12.666 1.00 31.27 ? 263 ARG A CZ  1 
ATOM   1908 N NH1 . ARG A 1 283 ? 23.122  0.580   -11.574 1.00 31.87 ? 263 ARG A NH1 1 
ATOM   1909 N NH2 . ARG A 1 283 ? 21.089  0.205   -12.570 1.00 27.78 ? 263 ARG A NH2 1 
ATOM   1910 N N   . GLU A 1 284 ? 24.226  -5.232  -14.684 1.00 20.68 ? 264 GLU A N   1 
ATOM   1911 C CA  . GLU A 1 284 ? 25.520  -5.964  -14.765 1.00 22.70 ? 264 GLU A CA  1 
ATOM   1912 C C   . GLU A 1 284 ? 25.348  -7.256  -15.563 1.00 21.21 ? 264 GLU A C   1 
ATOM   1913 O O   . GLU A 1 284 ? 26.169  -7.479  -16.475 1.00 18.51 ? 264 GLU A O   1 
ATOM   1914 C CB  . GLU A 1 284 ? 26.093  -6.289  -13.376 1.00 25.64 ? 264 GLU A CB  1 
ATOM   1915 C CG  . GLU A 1 284 ? 26.625  -5.063  -12.659 1.00 27.50 ? 264 GLU A CG  1 
ATOM   1916 C CD  . GLU A 1 284 ? 27.615  -4.286  -13.513 1.00 30.72 ? 264 GLU A CD  1 
ATOM   1917 O OE1 . GLU A 1 284 ? 28.466  -4.929  -14.150 1.00 32.19 ? 264 GLU A OE1 1 
ATOM   1918 O OE2 . GLU A 1 284 ? 27.478  -3.058  -13.601 1.00 35.75 ? 264 GLU A OE2 1 
ATOM   1919 N N   . VAL A 1 285 ? 24.345  -8.083  -15.254 1.00 18.15 ? 265 VAL A N   1 
ATOM   1920 C CA  . VAL A 1 285 ? 24.228  -9.392  -15.951 1.00 19.08 ? 265 VAL A CA  1 
ATOM   1921 C C   . VAL A 1 285 ? 23.847  -9.152  -17.426 1.00 19.10 ? 265 VAL A C   1 
ATOM   1922 O O   . VAL A 1 285 ? 24.386  -9.860  -18.291 1.00 17.80 ? 265 VAL A O   1 
ATOM   1923 C CB  . VAL A 1 285 ? 23.323  -10.389 -15.209 1.00 19.12 ? 265 VAL A CB  1 
ATOM   1924 C CG1 . VAL A 1 285 ? 21.859  -9.998  -15.291 1.00 18.69 ? 265 VAL A CG1 1 
ATOM   1925 C CG2 . VAL A 1 285 ? 23.559  -11.815 -15.690 1.00 18.44 ? 265 VAL A CG2 1 
ATOM   1926 N N   . MET A 1 286 ? 23.059  -8.124  -17.734 1.00 19.42 ? 266 MET A N   1 
ATOM   1927 C CA  . MET A 1 286 ? 22.646  -7.848  -19.138 1.00 20.04 ? 266 MET A CA  1 
ATOM   1928 C C   . MET A 1 286 ? 23.838  -7.303  -19.952 1.00 20.66 ? 266 MET A C   1 
ATOM   1929 O O   . MET A 1 286 ? 23.918  -7.634  -21.156 1.00 17.84 ? 266 MET A O   1 
ATOM   1930 C CB  . MET A 1 286 ? 21.473  -6.864  -19.200 1.00 19.64 ? 266 MET A CB  1 
ATOM   1931 C CG  . MET A 1 286 ? 20.176  -7.494  -18.736 1.00 21.87 ? 266 MET A CG  1 
ATOM   1932 S SD  . MET A 1 286 ? 18.728  -6.408  -18.770 1.00 19.93 ? 266 MET A SD  1 
ATOM   1933 C CE  . MET A 1 286 ? 18.188  -6.633  -20.459 1.00 23.50 ? 266 MET A CE  1 
ATOM   1934 N N   . SER A 1 287 ? 24.707  -6.493  -19.339 1.00 22.40 ? 267 SER A N   1 
ATOM   1935 C CA  . SER A 1 287 ? 25.959  -5.988  -19.974 1.00 25.17 ? 267 SER A CA  1 
ATOM   1936 C C   . SER A 1 287 ? 26.869  -7.156  -20.339 1.00 24.98 ? 267 SER A C   1 
ATOM   1937 O O   . SER A 1 287 ? 27.399  -7.161  -21.476 1.00 24.41 ? 267 SER A O   1 
ATOM   1938 C CB  . SER A 1 287 ? 26.695  -4.998  -19.127 1.00 25.39 ? 267 SER A CB  1 
ATOM   1939 O OG  . SER A 1 287 ? 26.094  -3.734  -19.276 1.00 30.56 ? 267 SER A OG  1 
ATOM   1940 N N   . GLU A 1 288 ? 27.055  -8.094  -19.416 1.00 24.51 ? 268 GLU A N   1 
ATOM   1941 C CA  . GLU A 1 288 ? 27.917  -9.272  -19.656 1.00 25.01 ? 268 GLU A CA  1 
ATOM   1942 C C   . GLU A 1 288 ? 27.330  -10.068 -20.813 1.00 24.96 ? 268 GLU A C   1 
ATOM   1943 O O   . GLU A 1 288 ? 28.100  -10.420 -21.711 1.00 22.37 ? 268 GLU A O   1 
ATOM   1944 C CB  . GLU A 1 288 ? 28.059  -10.131 -18.407 1.00 27.46 ? 268 GLU A CB  1 
ATOM   1945 C CG  . GLU A 1 288 ? 28.899  -11.370 -18.627 1.00 28.63 ? 268 GLU A CG  1 
ATOM   1946 C CD  . GLU A 1 288 ? 30.344  -11.096 -19.023 1.00 31.08 ? 268 GLU A CD  1 
ATOM   1947 O OE1 . GLU A 1 288 ? 30.843  -9.971  -18.762 1.00 30.08 ? 268 GLU A OE1 1 
ATOM   1948 O OE2 . GLU A 1 288 ? 30.964  -12.017 -19.603 1.00 31.77 ? 268 GLU A OE2 1 
ATOM   1949 N N   . ALA A 1 289 ? 26.011  -10.324 -20.783 1.00 24.14 ? 269 ALA A N   1 
ATOM   1950 C CA  . ALA A 1 289 ? 25.267  -11.009 -21.863 1.00 22.87 ? 269 ALA A CA  1 
ATOM   1951 C C   . ALA A 1 289 ? 25.663  -10.400 -23.218 1.00 22.69 ? 269 ALA A C   1 
ATOM   1952 O O   . ALA A 1 289 ? 25.984  -11.168 -24.124 1.00 22.70 ? 269 ALA A O   1 
ATOM   1953 C CB  . ALA A 1 289 ? 23.772  -10.922 -21.638 1.00 21.42 ? 269 ALA A CB  1 
ATOM   1954 N N   . VAL A 1 290 ? 25.622  -9.072  -23.336 1.00 22.67 ? 270 VAL A N   1 
ATOM   1955 C CA  . VAL A 1 290 ? 25.935  -8.323  -24.591 1.00 25.14 ? 270 VAL A CA  1 
ATOM   1956 C C   . VAL A 1 290 ? 27.372  -8.678  -24.990 1.00 28.07 ? 270 VAL A C   1 
ATOM   1957 O O   . VAL A 1 290 ? 27.548  -9.262  -26.086 1.00 25.07 ? 270 VAL A O   1 
ATOM   1958 C CB  . VAL A 1 290 ? 25.706  -6.808  -24.409 1.00 24.91 ? 270 VAL A CB  1 
ATOM   1959 C CG1 . VAL A 1 290 ? 26.240  -5.949  -25.558 1.00 24.06 ? 270 VAL A CG1 1 
ATOM   1960 C CG2 . VAL A 1 290 ? 24.226  -6.518  -24.212 1.00 25.29 ? 270 VAL A CG2 1 
ATOM   1961 N N   . LYS A 1 291 ? 28.332  -8.460  -24.077 1.00 31.11 ? 271 LYS A N   1 
ATOM   1962 C CA  . LYS A 1 291 ? 29.772  -8.778  -24.303 1.00 34.33 ? 271 LYS A CA  1 
ATOM   1963 C C   . LYS A 1 291 ? 29.882  -10.216 -24.818 1.00 32.57 ? 271 LYS A C   1 
ATOM   1964 O O   . LYS A 1 291 ? 30.566  -10.402 -25.795 1.00 31.28 ? 271 LYS A O   1 
ATOM   1965 C CB  . LYS A 1 291 ? 30.615  -8.503  -23.052 1.00 37.62 ? 271 LYS A CB  1 
ATOM   1966 C CG  . LYS A 1 291 ? 30.710  -7.024  -22.689 1.00 41.27 ? 271 LYS A CG  1 
ATOM   1967 C CD  . LYS A 1 291 ? 31.585  -6.719  -21.484 1.00 45.59 ? 271 LYS A CD  1 
ATOM   1968 C CE  . LYS A 1 291 ? 31.189  -5.422  -20.799 1.00 48.51 ? 271 LYS A CE  1 
ATOM   1969 N NZ  . LYS A 1 291 ? 32.118  -5.069  -19.699 1.00 52.78 ? 271 LYS A NZ  1 
ATOM   1970 N N   . LYS A 1 292 ? 29.113  -11.158 -24.266 1.00 32.96 ? 272 LYS A N   1 
ATOM   1971 C CA  . LYS A 1 292 ? 29.200  -12.600 -24.615 1.00 30.63 ? 272 LYS A CA  1 
ATOM   1972 C C   . LYS A 1 292 ? 28.388  -12.934 -25.880 1.00 29.03 ? 272 LYS A C   1 
ATOM   1973 O O   . LYS A 1 292 ? 28.300  -14.127 -26.201 1.00 28.12 ? 272 LYS A O   1 
ATOM   1974 C CB  . LYS A 1 292 ? 28.747  -13.447 -23.424 1.00 33.82 ? 272 LYS A CB  1 
ATOM   1975 C CG  . LYS A 1 292 ? 29.749  -13.522 -22.280 1.00 35.37 ? 272 LYS A CG  1 
ATOM   1976 C CD  . LYS A 1 292 ? 29.887  -14.913 -21.684 1.00 38.90 ? 272 LYS A CD  1 
ATOM   1977 C CE  . LYS A 1 292 ? 29.063  -15.104 -20.434 1.00 39.29 ? 272 LYS A CE  1 
ATOM   1978 N NZ  . LYS A 1 292 ? 29.677  -14.387 -19.295 1.00 40.19 ? 272 LYS A NZ  1 
ATOM   1979 N N   . GLY A 1 293 ? 27.846  -11.942 -26.595 1.00 26.71 ? 273 GLY A N   1 
ATOM   1980 C CA  . GLY A 1 293 ? 27.180  -12.152 -27.896 1.00 26.84 ? 273 GLY A CA  1 
ATOM   1981 C C   . GLY A 1 293 ? 25.723  -12.598 -27.780 1.00 27.03 ? 273 GLY A C   1 
ATOM   1982 O O   . GLY A 1 293 ? 25.195  -13.087 -28.801 1.00 26.34 ? 273 GLY A O   1 
ATOM   1983 N N   . LYS A 1 294 ? 25.078  -12.439 -26.610 1.00 23.58 ? 274 LYS A N   1 
ATOM   1984 C CA  . LYS A 1 294 ? 23.662  -12.858 -26.381 1.00 22.07 ? 274 LYS A CA  1 
ATOM   1985 C C   . LYS A 1 294 ? 22.723  -11.631 -26.383 1.00 20.72 ? 274 LYS A C   1 
ATOM   1986 O O   . LYS A 1 294 ? 21.528  -11.788 -26.056 1.00 22.38 ? 274 LYS A O   1 
ATOM   1987 C CB  . LYS A 1 294 ? 23.588  -13.684 -25.084 1.00 23.09 ? 274 LYS A CB  1 
ATOM   1988 C CG  . LYS A 1 294 ? 24.250  -15.065 -25.141 1.00 23.54 ? 274 LYS A CG  1 
ATOM   1989 C CD  . LYS A 1 294 ? 24.717  -15.658 -23.785 1.00 23.41 ? 274 LYS A CD  1 
ATOM   1990 C CE  . LYS A 1 294 ? 23.635  -15.759 -22.716 1.00 22.72 ? 274 LYS A CE  1 
ATOM   1991 N NZ  . LYS A 1 294 ? 22.552  -16.710 -23.076 1.00 21.56 ? 274 LYS A NZ  1 
ATOM   1992 N N   . GLY A 1 295 ? 23.220  -10.459 -26.766 1.00 20.07 ? 275 GLY A N   1 
ATOM   1993 C CA  . GLY A 1 295 ? 22.467  -9.194  -26.862 1.00 20.79 ? 275 GLY A CA  1 
ATOM   1994 C C   . GLY A 1 295 ? 21.147  -9.313  -27.619 1.00 20.47 ? 275 GLY A C   1 
ATOM   1995 O O   . GLY A 1 295 ? 20.227  -8.558  -27.276 1.00 20.11 ? 275 GLY A O   1 
ATOM   1996 N N   . GLY A 1 296 ? 21.074  -10.176 -28.643 1.00 20.07 ? 276 GLY A N   1 
ATOM   1997 C CA  . GLY A 1 296 ? 19.879  -10.374 -29.495 1.00 20.47 ? 276 GLY A CA  1 
ATOM   1998 C C   . GLY A 1 296 ? 18.847  -11.280 -28.839 1.00 18.70 ? 276 GLY A C   1 
ATOM   1999 O O   . GLY A 1 296 ? 17.706  -11.336 -29.320 1.00 17.88 ? 276 GLY A O   1 
ATOM   2000 N N   . GLU A 1 297 ? 19.234  -11.999 -27.788 1.00 17.86 ? 277 GLU A N   1 
ATOM   2001 C CA  . GLU A 1 297 ? 18.330  -12.937 -27.076 1.00 17.71 ? 277 GLU A CA  1 
ATOM   2002 C C   . GLU A 1 297 ? 17.370  -12.138 -26.188 1.00 17.64 ? 277 GLU A C   1 
ATOM   2003 O O   . GLU A 1 297 ? 17.663  -10.994 -25.860 1.00 16.20 ? 277 GLU A O   1 
ATOM   2004 C CB  . GLU A 1 297 ? 19.138  -13.926 -26.241 1.00 18.78 ? 277 GLU A CB  1 
ATOM   2005 C CG  . GLU A 1 297 ? 19.834  -14.988 -27.064 1.00 18.35 ? 277 GLU A CG  1 
ATOM   2006 C CD  . GLU A 1 297 ? 20.712  -15.934 -26.259 1.00 19.91 ? 277 GLU A CD  1 
ATOM   2007 O OE1 . GLU A 1 297 ? 20.764  -15.808 -25.022 1.00 19.13 ? 277 GLU A OE1 1 
ATOM   2008 O OE2 . GLU A 1 297 ? 21.365  -16.795 -26.886 1.00 20.81 ? 277 GLU A OE2 1 
ATOM   2009 N N   . SER A 1 298 ? 16.261  -12.749 -25.789 1.00 17.85 ? 278 SER A N   1 
ATOM   2010 C CA  . SER A 1 298 ? 15.361  -12.183 -24.755 1.00 17.60 ? 278 SER A CA  1 
ATOM   2011 C C   . SER A 1 298 ? 15.897  -12.503 -23.341 1.00 17.68 ? 278 SER A C   1 
ATOM   2012 O O   . SER A 1 298 ? 16.948  -13.177 -23.171 1.00 15.21 ? 278 SER A O   1 
ATOM   2013 C CB  . SER A 1 298 ? 13.943  -12.683 -24.959 1.00 17.42 ? 278 SER A CB  1 
ATOM   2014 O OG  . SER A 1 298 ? 13.849  -14.062 -24.620 1.00 17.88 ? 278 SER A OG  1 
ATOM   2015 N N   . ILE A 1 299 ? 15.175  -11.994 -22.344 1.00 17.77 ? 279 ILE A N   1 
ATOM   2016 C CA  . ILE A 1 299 ? 15.407  -12.184 -20.882 1.00 18.49 ? 279 ILE A CA  1 
ATOM   2017 C C   . ILE A 1 299 ? 15.667  -13.675 -20.559 1.00 17.24 ? 279 ILE A C   1 
ATOM   2018 O O   . ILE A 1 299 ? 16.497  -13.945 -19.671 1.00 15.64 ? 279 ILE A O   1 
ATOM   2019 C CB  . ILE A 1 299 ? 14.205  -11.522 -20.159 1.00 19.24 ? 279 ILE A CB  1 
ATOM   2020 C CG1 . ILE A 1 299 ? 14.636  -10.226 -19.474 1.00 20.94 ? 279 ILE A CG1 1 
ATOM   2021 C CG2 . ILE A 1 299 ? 13.483  -12.435 -19.195 1.00 19.09 ? 279 ILE A CG2 1 
ATOM   2022 C CD1 . ILE A 1 299 ? 15.481  -9.337  -20.308 1.00 20.08 ? 279 ILE A CD1 1 
ATOM   2023 N N   . ALA A 1 300 ? 15.039  -14.617 -21.268 1.00 18.53 ? 280 ALA A N   1 
ATOM   2024 C CA  . ALA A 1 300 ? 15.230  -16.081 -21.070 1.00 19.19 ? 280 ALA A CA  1 
ATOM   2025 C C   . ALA A 1 300 ? 16.721  -16.439 -21.119 1.00 18.87 ? 280 ALA A C   1 
ATOM   2026 O O   . ALA A 1 300 ? 17.157  -17.357 -20.401 1.00 19.86 ? 280 ALA A O   1 
ATOM   2027 C CB  . ALA A 1 300 ? 14.448  -16.864 -22.101 1.00 20.37 ? 280 ALA A CB  1 
ATOM   2028 N N   . GLY A 1 301 ? 17.487  -15.739 -21.940 1.00 18.09 ? 281 GLY A N   1 
ATOM   2029 C CA  . GLY A 1 301 ? 18.916  -16.014 -22.139 1.00 19.04 ? 281 GLY A CA  1 
ATOM   2030 C C   . GLY A 1 301 ? 19.726  -15.639 -20.914 1.00 17.92 ? 281 GLY A C   1 
ATOM   2031 O O   . GLY A 1 301 ? 20.905  -16.066 -20.814 1.00 17.42 ? 281 GLY A O   1 
ATOM   2032 N N   . LEU A 1 302 ? 19.145  -14.882 -19.988 1.00 16.97 ? 282 LEU A N   1 
ATOM   2033 C CA  . LEU A 1 302 ? 19.882  -14.520 -18.752 1.00 16.58 ? 282 LEU A CA  1 
ATOM   2034 C C   . LEU A 1 302 ? 19.879  -15.704 -17.777 1.00 16.41 ? 282 LEU A C   1 
ATOM   2035 O O   . LEU A 1 302 ? 20.782  -15.741 -16.932 1.00 17.49 ? 282 LEU A O   1 
ATOM   2036 C CB  . LEU A 1 302 ? 19.295  -13.261 -18.115 1.00 17.23 ? 282 LEU A CB  1 
ATOM   2037 C CG  . LEU A 1 302 ? 19.341  -12.013 -18.990 1.00 16.44 ? 282 LEU A CG  1 
ATOM   2038 C CD1 . LEU A 1 302 ? 18.549  -10.900 -18.344 1.00 16.97 ? 282 LEU A CD1 1 
ATOM   2039 C CD2 . LEU A 1 302 ? 20.772  -11.589 -19.282 1.00 16.24 ? 282 LEU A CD2 1 
ATOM   2040 N N   . VAL A 1 303 ? 18.910  -16.608 -17.852 1.00 14.88 ? 283 VAL A N   1 
ATOM   2041 C CA  . VAL A 1 303 ? 18.821  -17.738 -16.879 1.00 16.52 ? 283 VAL A CA  1 
ATOM   2042 C C   . VAL A 1 303 ? 20.094  -18.586 -16.927 1.00 17.13 ? 283 VAL A C   1 
ATOM   2043 O O   . VAL A 1 303 ? 20.683  -18.816 -15.873 1.00 17.48 ? 283 VAL A O   1 
ATOM   2044 C CB  . VAL A 1 303 ? 17.563  -18.585 -17.080 1.00 15.35 ? 283 VAL A CB  1 
ATOM   2045 C CG1 . VAL A 1 303 ? 17.637  -19.849 -16.237 1.00 16.23 ? 283 VAL A CG1 1 
ATOM   2046 C CG2 . VAL A 1 303 ? 16.301  -17.777 -16.758 1.00 14.98 ? 283 VAL A CG2 1 
ATOM   2047 N N   . PRO A 1 304 ? 20.582  -19.071 -18.095 1.00 19.46 ? 284 PRO A N   1 
ATOM   2048 C CA  . PRO A 1 304 ? 21.839  -19.830 -18.138 1.00 20.10 ? 284 PRO A CA  1 
ATOM   2049 C C   . PRO A 1 304 ? 23.059  -19.069 -17.604 1.00 20.34 ? 284 PRO A C   1 
ATOM   2050 O O   . PRO A 1 304 ? 23.996  -19.695 -17.156 1.00 22.23 ? 284 PRO A O   1 
ATOM   2051 C CB  . PRO A 1 304 ? 22.038  -20.191 -19.620 1.00 20.05 ? 284 PRO A CB  1 
ATOM   2052 C CG  . PRO A 1 304 ? 21.168  -19.205 -20.356 1.00 19.99 ? 284 PRO A CG  1 
ATOM   2053 C CD  . PRO A 1 304 ? 19.971  -18.994 -19.436 1.00 19.68 ? 284 PRO A CD  1 
ATOM   2054 N N   . MET A 1 305 ? 23.041  -17.746 -17.610 1.00 19.72 ? 285 MET A N   1 
ATOM   2055 C CA  . MET A 1 305 ? 24.207  -17.005 -17.075 1.00 20.22 ? 285 MET A CA  1 
ATOM   2056 C C   . MET A 1 305 ? 24.270  -17.099 -15.545 1.00 19.86 ? 285 MET A C   1 
ATOM   2057 O O   . MET A 1 305 ? 25.392  -17.109 -15.026 1.00 20.83 ? 285 MET A O   1 
ATOM   2058 C CB  . MET A 1 305 ? 24.176  -15.561 -17.545 1.00 21.02 ? 285 MET A CB  1 
ATOM   2059 C CG  . MET A 1 305 ? 24.546  -15.494 -19.018 1.00 22.45 ? 285 MET A CG  1 
ATOM   2060 S SD  . MET A 1 305 ? 24.422  -13.819 -19.486 1.00 24.96 ? 285 MET A SD  1 
ATOM   2061 C CE  . MET A 1 305 ? 25.971  -13.207 -18.827 1.00 24.83 ? 285 MET A CE  1 
ATOM   2062 N N   . LEU A 1 306 ? 23.131  -17.254 -14.872 1.00 18.26 ? 286 LEU A N   1 
ATOM   2063 C CA  . LEU A 1 306 ? 23.064  -17.503 -13.406 1.00 19.12 ? 286 LEU A CA  1 
ATOM   2064 C C   . LEU A 1 306 ? 23.428  -18.965 -13.117 1.00 18.09 ? 286 LEU A C   1 
ATOM   2065 O O   . LEU A 1 306 ? 24.237  -19.202 -12.206 1.00 18.56 ? 286 LEU A O   1 
ATOM   2066 C CB  . LEU A 1 306 ? 21.661  -17.168 -12.884 1.00 20.16 ? 286 LEU A CB  1 
ATOM   2067 C CG  . LEU A 1 306 ? 21.469  -15.746 -12.342 1.00 21.35 ? 286 LEU A CG  1 
ATOM   2068 C CD1 . LEU A 1 306 ? 22.220  -14.709 -13.153 1.00 22.86 ? 286 LEU A CD1 1 
ATOM   2069 C CD2 . LEU A 1 306 ? 20.004  -15.391 -12.219 1.00 20.57 ? 286 LEU A CD2 1 
ATOM   2070 N N   . THR A 1 307 ? 22.810  -19.906 -13.813 1.00 17.54 ? 287 THR A N   1 
ATOM   2071 C CA  . THR A 1 307 ? 22.957  -21.347 -13.500 1.00 20.05 ? 287 THR A CA  1 
ATOM   2072 C C   . THR A 1 307 ? 24.414  -21.770 -13.727 1.00 21.88 ? 287 THR A C   1 
ATOM   2073 O O   . THR A 1 307 ? 24.836  -22.722 -13.033 1.00 26.99 ? 287 THR A O   1 
ATOM   2074 C CB  . THR A 1 307 ? 21.974  -22.232 -14.269 1.00 18.93 ? 287 THR A CB  1 
ATOM   2075 O OG1 . THR A 1 307 ? 22.290  -22.165 -15.657 1.00 17.61 ? 287 THR A OG1 1 
ATOM   2076 C CG2 . THR A 1 307 ? 20.529  -21.856 -14.011 1.00 18.99 ? 287 THR A CG2 1 
ATOM   2077 N N   . GLU A 1 308 ? 25.160  -21.092 -14.608 1.00 22.73 ? 288 GLU A N   1 
ATOM   2078 C CA  . GLU A 1 308 ? 26.534  -21.534 -14.997 1.00 27.82 ? 288 GLU A CA  1 
ATOM   2079 C C   . GLU A 1 308 ? 27.585  -21.066 -13.980 1.00 26.15 ? 288 GLU A C   1 
ATOM   2080 O O   . GLU A 1 308 ? 28.706  -21.588 -14.011 1.00 25.91 ? 288 GLU A O   1 
ATOM   2081 C CB  . GLU A 1 308 ? 26.881  -21.053 -16.405 1.00 30.14 ? 288 GLU A CB  1 
ATOM   2082 C CG  . GLU A 1 308 ? 26.153  -21.863 -17.461 1.00 34.20 ? 288 GLU A CG  1 
ATOM   2083 C CD  . GLU A 1 308 ? 26.231  -21.351 -18.895 1.00 36.21 ? 288 GLU A CD  1 
ATOM   2084 O OE1 . GLU A 1 308 ? 25.541  -21.940 -19.753 1.00 36.73 ? 288 GLU A OE1 1 
ATOM   2085 O OE2 . GLU A 1 308 ? 26.974  -20.371 -19.155 1.00 40.43 ? 288 GLU A OE2 1 
ATOM   2086 N N   . LEU A 1 309 ? 27.277  -20.111 -13.114 1.00 25.94 ? 289 LEU A N   1 
ATOM   2087 C CA  . LEU A 1 309 ? 28.357  -19.403 -12.387 1.00 28.88 ? 289 LEU A CA  1 
ATOM   2088 C C   . LEU A 1 309 ? 27.855  -18.878 -11.042 1.00 29.03 ? 289 LEU A C   1 
ATOM   2089 O O   . LEU A 1 309 ? 26.893  -18.068 -11.038 1.00 22.75 ? 289 LEU A O   1 
ATOM   2090 C CB  . LEU A 1 309 ? 28.875  -18.256 -13.260 1.00 29.54 ? 289 LEU A CB  1 
ATOM   2091 C CG  . LEU A 1 309 ? 29.978  -17.418 -12.617 1.00 31.38 ? 289 LEU A CG  1 
ATOM   2092 C CD1 . LEU A 1 309 ? 31.275  -18.212 -12.528 1.00 32.81 ? 289 LEU A CD1 1 
ATOM   2093 C CD2 . LEU A 1 309 ? 30.189  -16.117 -13.383 1.00 31.51 ? 289 LEU A CD2 1 
ATOM   2094 N N   . ASP A 1 310 ? 28.535  -19.324 -9.976  1.00 27.35 ? 290 ASP A N   1 
ATOM   2095 C CA  . ASP A 1 310 ? 28.388  -18.853 -8.579  1.00 27.05 ? 290 ASP A CA  1 
ATOM   2096 C C   . ASP A 1 310 ? 29.051  -17.481 -8.503  1.00 28.08 ? 290 ASP A C   1 
ATOM   2097 O O   . ASP A 1 310 ? 30.278  -17.419 -8.293  1.00 28.98 ? 290 ASP A O   1 
ATOM   2098 C CB  . ASP A 1 310 ? 29.000  -19.873 -7.618  1.00 27.14 ? 290 ASP A CB  1 
ATOM   2099 C CG  . ASP A 1 310 ? 29.052  -19.457 -6.159  1.00 27.84 ? 290 ASP A CG  1 
ATOM   2100 O OD1 . ASP A 1 310 ? 28.537  -18.359 -5.823  1.00 26.15 ? 290 ASP A OD1 1 
ATOM   2101 O OD2 . ASP A 1 310 ? 29.604  -20.256 -5.361  1.00 27.90 ? 290 ASP A OD2 1 
ATOM   2102 N N   . LYS A 1 311 ? 28.266  -16.423 -8.699  1.00 27.18 ? 291 LYS A N   1 
ATOM   2103 C CA  . LYS A 1 311 ? 28.750  -15.024 -8.688  1.00 26.23 ? 291 LYS A CA  1 
ATOM   2104 C C   . LYS A 1 311 ? 27.618  -14.128 -8.184  1.00 27.97 ? 291 LYS A C   1 
ATOM   2105 O O   . LYS A 1 311 ? 26.417  -14.417 -8.509  1.00 27.41 ? 291 LYS A O   1 
ATOM   2106 C CB  . LYS A 1 311 ? 29.192  -14.631 -10.099 1.00 28.30 ? 291 LYS A CB  1 
ATOM   2107 C CG  . LYS A 1 311 ? 29.411  -13.140 -10.306 1.00 28.95 ? 291 LYS A CG  1 
ATOM   2108 C CD  . LYS A 1 311 ? 30.046  -12.782 -11.634 1.00 29.39 ? 291 LYS A CD  1 
ATOM   2109 C CE  . LYS A 1 311 ? 30.141  -11.284 -11.804 1.00 28.24 ? 291 LYS A CE  1 
ATOM   2110 N NZ  . LYS A 1 311 ? 30.348  -10.886 -13.214 1.00 29.44 ? 291 LYS A NZ  1 
ATOM   2111 N N   . LYS A 1 312 ? 27.970  -13.060 -7.469  1.00 27.60 ? 292 LYS A N   1 
ATOM   2112 C CA  . LYS A 1 312 ? 26.986  -12.042 -7.005  1.00 30.20 ? 292 LYS A CA  1 
ATOM   2113 C C   . LYS A 1 312 ? 27.122  -10.817 -7.928  1.00 26.52 ? 292 LYS A C   1 
ATOM   2114 O O   . LYS A 1 312 ? 28.231  -10.248 -7.989  1.00 25.84 ? 292 LYS A O   1 
ATOM   2115 C CB  . LYS A 1 312 ? 27.156  -11.842 -5.491  1.00 30.84 ? 292 LYS A CB  1 
ATOM   2116 C CG  . LYS A 1 312 ? 27.257  -13.165 -4.729  1.00 34.95 ? 292 LYS A CG  1 
ATOM   2117 C CD  . LYS A 1 312 ? 26.510  -13.240 -3.425  1.00 37.26 ? 292 LYS A CD  1 
ATOM   2118 C CE  . LYS A 1 312 ? 27.218  -12.512 -2.300  1.00 40.21 ? 292 LYS A CE  1 
ATOM   2119 N NZ  . LYS A 1 312 ? 26.279  -12.169 -1.202  1.00 39.80 ? 292 LYS A NZ  1 
ATOM   2120 N N   . TRP A 1 313 ? 26.030  -10.446 -8.622  1.00 20.98 ? 293 TRP A N   1 
ATOM   2121 C CA  . TRP A 1 313 ? 26.013  -9.493  -9.769  1.00 19.83 ? 293 TRP A CA  1 
ATOM   2122 C C   . TRP A 1 313 ? 25.806  -8.036  -9.315  1.00 18.65 ? 293 TRP A C   1 
ATOM   2123 O O   . TRP A 1 313 ? 25.138  -7.987  -8.275  1.00 20.10 ? 293 TRP A O   1 
ATOM   2124 C CB  . TRP A 1 313 ? 24.956  -9.942  -10.782 1.00 17.84 ? 293 TRP A CB  1 
ATOM   2125 C CG  . TRP A 1 313 ? 25.367  -11.178 -11.512 1.00 16.74 ? 293 TRP A CG  1 
ATOM   2126 C CD1 . TRP A 1 313 ? 25.120  -12.471 -11.160 1.00 17.29 ? 293 TRP A CD1 1 
ATOM   2127 C CD2 . TRP A 1 313 ? 26.160  -11.234 -12.710 1.00 17.68 ? 293 TRP A CD2 1 
ATOM   2128 N NE1 . TRP A 1 313 ? 25.672  -13.329 -12.078 1.00 17.25 ? 293 TRP A NE1 1 
ATOM   2129 C CE2 . TRP A 1 313 ? 26.338  -12.600 -13.024 1.00 17.05 ? 293 TRP A CE2 1 
ATOM   2130 C CE3 . TRP A 1 313 ? 26.738  -10.263 -13.544 1.00 17.85 ? 293 TRP A CE3 1 
ATOM   2131 C CZ2 . TRP A 1 313 ? 27.057  -13.016 -14.141 1.00 18.09 ? 293 TRP A CZ2 1 
ATOM   2132 C CZ3 . TRP A 1 313 ? 27.456  -10.679 -14.647 1.00 18.88 ? 293 TRP A CZ3 1 
ATOM   2133 C CH2 . TRP A 1 313 ? 27.596  -12.038 -14.947 1.00 17.99 ? 293 TRP A CH2 1 
ATOM   2134 N N   . PRO B 1 27  ? -2.483  12.815  -47.651 1.00 31.60 ? 7   PRO B N   1 
ATOM   2135 C CA  . PRO B 1 27  ? -1.696  13.328  -46.499 1.00 31.02 ? 7   PRO B CA  1 
ATOM   2136 C C   . PRO B 1 27  ? -0.210  12.954  -46.594 1.00 29.09 ? 7   PRO B C   1 
ATOM   2137 O O   . PRO B 1 27  ? 0.096   11.807  -46.763 1.00 26.65 ? 7   PRO B O   1 
ATOM   2138 C CB  . PRO B 1 27  ? -2.307  12.691  -45.242 1.00 31.71 ? 7   PRO B CB  1 
ATOM   2139 C CG  . PRO B 1 27  ? -3.000  11.438  -45.744 1.00 32.99 ? 7   PRO B CG  1 
ATOM   2140 C CD  . PRO B 1 27  ? -3.079  11.527  -47.262 1.00 32.41 ? 7   PRO B CD  1 
ATOM   2141 N N   . HIS B 1 28  ? 0.675   13.943  -46.519 1.00 29.15 ? 8   HIS B N   1 
ATOM   2142 C CA  . HIS B 1 28  ? 2.144   13.737  -46.613 1.00 29.18 ? 8   HIS B CA  1 
ATOM   2143 C C   . HIS B 1 28  ? 2.721   13.510  -45.215 1.00 25.85 ? 8   HIS B C   1 
ATOM   2144 O O   . HIS B 1 28  ? 2.573   14.424  -44.369 1.00 21.87 ? 8   HIS B O   1 
ATOM   2145 C CB  . HIS B 1 28  ? 2.805   14.925  -47.310 1.00 33.36 ? 8   HIS B CB  1 
ATOM   2146 C CG  . HIS B 1 28  ? 2.596   14.954  -48.786 1.00 37.41 ? 8   HIS B CG  1 
ATOM   2147 N ND1 . HIS B 1 28  ? 3.500   14.395  -49.666 1.00 39.09 ? 8   HIS B ND1 1 
ATOM   2148 C CD2 . HIS B 1 28  ? 1.603   15.479  -49.534 1.00 41.36 ? 8   HIS B CD2 1 
ATOM   2149 C CE1 . HIS B 1 28  ? 3.077   14.585  -50.896 1.00 45.04 ? 8   HIS B CE1 1 
ATOM   2150 N NE2 . HIS B 1 28  ? 1.910   15.245  -50.842 1.00 43.73 ? 8   HIS B NE2 1 
ATOM   2151 N N   . VAL B 1 29  ? 3.366   12.355  -44.997 1.00 22.13 ? 9   VAL B N   1 
ATOM   2152 C CA  . VAL B 1 29  ? 4.052   12.001  -43.718 1.00 21.24 ? 9   VAL B CA  1 
ATOM   2153 C C   . VAL B 1 29  ? 5.492   11.578  -44.023 1.00 21.75 ? 9   VAL B C   1 
ATOM   2154 O O   . VAL B 1 29  ? 5.714   10.788  -44.977 1.00 19.80 ? 9   VAL B O   1 
ATOM   2155 C CB  . VAL B 1 29  ? 3.290   10.893  -42.963 1.00 22.24 ? 9   VAL B CB  1 
ATOM   2156 C CG1 . VAL B 1 29  ? 3.967   10.533  -41.652 1.00 21.96 ? 9   VAL B CG1 1 
ATOM   2157 C CG2 . VAL B 1 29  ? 1.834   11.266  -42.725 1.00 22.85 ? 9   VAL B CG2 1 
ATOM   2158 N N   . SER B 1 30  ? 6.449   12.077  -43.234 1.00 21.84 ? 10  SER B N   1 
ATOM   2159 C CA  . SER B 1 30  ? 7.871   11.654  -43.285 1.00 19.65 ? 10  SER B CA  1 
ATOM   2160 C C   . SER B 1 30  ? 8.217   10.829  -42.037 1.00 20.55 ? 10  SER B C   1 
ATOM   2161 O O   . SER B 1 30  ? 7.733   11.152  -40.927 1.00 22.13 ? 10  SER B O   1 
ATOM   2162 C CB  . SER B 1 30  ? 8.777   12.842  -43.487 1.00 20.77 ? 10  SER B CB  1 
ATOM   2163 O OG  . SER B 1 30  ? 8.563   13.473  -44.758 1.00 20.19 ? 10  SER B OG  1 
ATOM   2164 N N   . LEU B 1 31  ? 8.997   9.756   -42.218 1.00 20.29 ? 11  LEU B N   1 
ATOM   2165 C CA  . LEU B 1 31  ? 9.526   8.893   -41.133 1.00 19.07 ? 11  LEU B CA  1 
ATOM   2166 C C   . LEU B 1 31  ? 11.053  8.884   -41.201 1.00 18.86 ? 11  LEU B C   1 
ATOM   2167 O O   . LEU B 1 31  ? 11.632  8.689   -42.295 1.00 17.88 ? 11  LEU B O   1 
ATOM   2168 C CB  . LEU B 1 31  ? 8.951   7.490   -41.284 1.00 19.88 ? 11  LEU B CB  1 
ATOM   2169 C CG  . LEU B 1 31  ? 9.573   6.428   -40.381 1.00 20.03 ? 11  LEU B CG  1 
ATOM   2170 C CD1 . LEU B 1 31  ? 9.359   6.743   -38.915 1.00 20.95 ? 11  LEU B CD1 1 
ATOM   2171 C CD2 . LEU B 1 31  ? 9.014   5.063   -40.726 1.00 20.02 ? 11  LEU B CD2 1 
ATOM   2172 N N   . ILE B 1 32  ? 11.689  9.126   -40.069 1.00 18.43 ? 12  ILE B N   1 
ATOM   2173 C CA  . ILE B 1 32  ? 13.175  9.123   -39.943 1.00 18.87 ? 12  ILE B CA  1 
ATOM   2174 C C   . ILE B 1 32  ? 13.541  7.927   -39.063 1.00 18.69 ? 12  ILE B C   1 
ATOM   2175 O O   . ILE B 1 32  ? 13.123  7.915   -37.891 1.00 19.79 ? 12  ILE B O   1 
ATOM   2176 C CB  . ILE B 1 32  ? 13.662  10.474  -39.400 1.00 18.30 ? 12  ILE B CB  1 
ATOM   2177 C CG1 . ILE B 1 32  ? 13.560  11.561  -40.472 1.00 18.98 ? 12  ILE B CG1 1 
ATOM   2178 C CG2 . ILE B 1 32  ? 15.081  10.358  -38.869 1.00 19.74 ? 12  ILE B CG2 1 
ATOM   2179 C CD1 . ILE B 1 32  ? 13.785  12.976  -39.935 1.00 19.60 ? 12  ILE B CD1 1 
ATOM   2180 N N   . GLY B 1 33  ? 14.154  6.902   -39.649 1.00 17.41 ? 13  GLY B N   1 
ATOM   2181 C CA  . GLY B 1 33  ? 14.613  5.712   -38.921 1.00 18.06 ? 13  GLY B CA  1 
ATOM   2182 C C   . GLY B 1 33  ? 13.818  4.492   -39.316 1.00 18.42 ? 13  GLY B C   1 
ATOM   2183 O O   . GLY B 1 33  ? 12.593  4.528   -39.204 1.00 18.37 ? 13  GLY B O   1 
ATOM   2184 N N   . LEU B 1 34  ? 14.518  3.430   -39.710 1.00 19.69 ? 14  LEU B N   1 
ATOM   2185 C CA  . LEU B 1 34  ? 13.926  2.209   -40.301 1.00 20.16 ? 14  LEU B CA  1 
ATOM   2186 C C   . LEU B 1 34  ? 14.497  0.953   -39.638 1.00 19.81 ? 14  LEU B C   1 
ATOM   2187 O O   . LEU B 1 34  ? 14.515  -0.079  -40.317 1.00 20.98 ? 14  LEU B O   1 
ATOM   2188 C CB  . LEU B 1 34  ? 14.201  2.245   -41.806 1.00 21.68 ? 14  LEU B CB  1 
ATOM   2189 C CG  . LEU B 1 34  ? 13.454  3.333   -42.582 1.00 22.60 ? 14  LEU B CG  1 
ATOM   2190 C CD1 . LEU B 1 34  ? 13.640  3.132   -44.082 1.00 22.89 ? 14  LEU B CD1 1 
ATOM   2191 C CD2 . LEU B 1 34  ? 11.958  3.348   -42.225 1.00 21.79 ? 14  LEU B CD2 1 
ATOM   2192 N N   . GLY B 1 35  ? 14.855  1.036   -38.348 1.00 20.25 ? 15  GLY B N   1 
ATOM   2193 C CA  . GLY B 1 35  ? 15.185  -0.108  -37.471 1.00 20.02 ? 15  GLY B CA  1 
ATOM   2194 C C   . GLY B 1 35  ? 14.002  -1.047  -37.339 1.00 20.17 ? 15  GLY B C   1 
ATOM   2195 O O   . GLY B 1 35  ? 13.038  -0.886  -38.114 1.00 22.32 ? 15  GLY B O   1 
ATOM   2196 N N   . ASN B 1 36  ? 14.011  -1.963  -36.370 1.00 19.30 ? 16  ASN B N   1 
ATOM   2197 C CA  . ASN B 1 36  ? 12.872  -2.900  -36.183 1.00 20.43 ? 16  ASN B CA  1 
ATOM   2198 C C   . ASN B 1 36  ? 11.589  -2.096  -35.905 1.00 21.12 ? 16  ASN B C   1 
ATOM   2199 O O   . ASN B 1 36  ? 10.535  -2.378  -36.527 1.00 20.09 ? 16  ASN B O   1 
ATOM   2200 C CB  . ASN B 1 36  ? 13.212  -3.948  -35.126 1.00 21.63 ? 16  ASN B CB  1 
ATOM   2201 C CG  . ASN B 1 36  ? 14.335  -4.839  -35.614 1.00 22.58 ? 16  ASN B CG  1 
ATOM   2202 O OD1 . ASN B 1 36  ? 15.403  -4.899  -35.014 1.00 25.13 ? 16  ASN B OD1 1 
ATOM   2203 N ND2 . ASN B 1 36  ? 14.133  -5.442  -36.772 1.00 23.57 ? 16  ASN B ND2 1 
ATOM   2204 N N   . MET B 1 37  ? 11.660  -1.110  -35.013 1.00 20.82 ? 17  MET B N   1 
ATOM   2205 C CA  . MET B 1 37  ? 10.467  -0.306  -34.675 1.00 20.60 ? 17  MET B CA  1 
ATOM   2206 C C   . MET B 1 37  ? 10.150  0.638   -35.848 1.00 19.14 ? 17  MET B C   1 
ATOM   2207 O O   . MET B 1 37  ? 9.008   0.687   -36.244 1.00 18.53 ? 17  MET B O   1 
ATOM   2208 C CB  . MET B 1 37  ? 10.658  0.453   -33.357 1.00 20.77 ? 17  MET B CB  1 
ATOM   2209 C CG  . MET B 1 37  ? 9.362   1.073   -32.824 1.00 20.07 ? 17  MET B CG  1 
ATOM   2210 S SD  . MET B 1 37  ? 7.926   -0.020  -32.816 1.00 21.05 ? 17  MET B SD  1 
ATOM   2211 C CE  . MET B 1 37  ? 8.185   -0.903  -31.278 1.00 20.80 ? 17  MET B CE  1 
ATOM   2212 N N   . GLY B 1 38  ? 11.136  1.312   -36.428 1.00 21.18 ? 18  GLY B N   1 
ATOM   2213 C CA  . GLY B 1 38  ? 10.946  2.236   -37.563 1.00 21.69 ? 18  GLY B CA  1 
ATOM   2214 C C   . GLY B 1 38  ? 10.201  1.602   -38.736 1.00 22.79 ? 18  GLY B C   1 
ATOM   2215 O O   . GLY B 1 38  ? 9.213   2.191   -39.197 1.00 20.34 ? 18  GLY B O   1 
ATOM   2216 N N   . LEU B 1 39  ? 10.685  0.454   -39.235 1.00 25.63 ? 19  LEU B N   1 
ATOM   2217 C CA  . LEU B 1 39  ? 10.004  -0.353  -40.284 1.00 23.73 ? 19  LEU B CA  1 
ATOM   2218 C C   . LEU B 1 39  ? 8.580   -0.707  -39.844 1.00 22.98 ? 19  LEU B C   1 
ATOM   2219 O O   . LEU B 1 39  ? 7.687   -0.637  -40.694 1.00 24.14 ? 19  LEU B O   1 
ATOM   2220 C CB  . LEU B 1 39  ? 10.786  -1.643  -40.557 1.00 26.06 ? 19  LEU B CB  1 
ATOM   2221 C CG  . LEU B 1 39  ? 11.454  -1.773  -41.920 1.00 29.07 ? 19  LEU B CG  1 
ATOM   2222 C CD1 . LEU B 1 39  ? 11.794  -3.244  -42.185 1.00 30.57 ? 19  LEU B CD1 1 
ATOM   2223 C CD2 . LEU B 1 39  ? 10.590  -1.207  -43.046 1.00 29.50 ? 19  LEU B CD2 1 
ATOM   2224 N N   . ALA B 1 40  ? 8.366   -1.109  -38.592 1.00 21.24 ? 20  ALA B N   1 
ATOM   2225 C CA  . ALA B 1 40  ? 7.011   -1.426  -38.081 1.00 20.83 ? 20  ALA B CA  1 
ATOM   2226 C C   . ALA B 1 40  ? 6.143   -0.179  -38.201 1.00 20.93 ? 20  ALA B C   1 
ATOM   2227 O O   . ALA B 1 40  ? 4.987   -0.285  -38.674 1.00 20.82 ? 20  ALA B O   1 
ATOM   2228 C CB  . ALA B 1 40  ? 7.051   -1.914  -36.669 1.00 22.10 ? 20  ALA B CB  1 
ATOM   2229 N N   . ILE B 1 41  ? 6.679   0.971   -37.805 1.00 20.35 ? 21  ILE B N   1 
ATOM   2230 C CA  . ILE B 1 41  ? 5.920   2.251   -37.894 1.00 19.76 ? 21  ILE B CA  1 
ATOM   2231 C C   . ILE B 1 41  ? 5.636   2.533   -39.376 1.00 19.83 ? 21  ILE B C   1 
ATOM   2232 O O   . ILE B 1 41  ? 4.452   2.783   -39.693 1.00 19.54 ? 21  ILE B O   1 
ATOM   2233 C CB  . ILE B 1 41  ? 6.652   3.411   -37.194 1.00 19.39 ? 21  ILE B CB  1 
ATOM   2234 C CG1 . ILE B 1 41  ? 6.893   3.150   -35.703 1.00 19.95 ? 21  ILE B CG1 1 
ATOM   2235 C CG2 . ILE B 1 41  ? 5.876   4.695   -37.394 1.00 19.52 ? 21  ILE B CG2 1 
ATOM   2236 C CD1 . ILE B 1 41  ? 7.907   4.095   -35.075 1.00 20.43 ? 21  ILE B CD1 1 
ATOM   2237 N N   . ALA B 1 42  ? 6.643   2.430   -40.253 1.00 18.43 ? 22  ALA B N   1 
ATOM   2238 C CA  . ALA B 1 42  ? 6.511   2.701   -41.715 1.00 21.38 ? 22  ALA B CA  1 
ATOM   2239 C C   . ALA B 1 42  ? 5.346   1.902   -42.314 1.00 22.48 ? 22  ALA B C   1 
ATOM   2240 O O   . ALA B 1 42  ? 4.530   2.467   -43.071 1.00 22.66 ? 22  ALA B O   1 
ATOM   2241 C CB  . ALA B 1 42  ? 7.792   2.372   -42.442 1.00 22.49 ? 22  ALA B CB  1 
ATOM   2242 N N   . ASN B 1 43  ? 5.305   0.607   -41.994 1.00 23.98 ? 23  ASN B N   1 
ATOM   2243 C CA  . ASN B 1 43  ? 4.269   -0.345  -42.440 1.00 23.16 ? 23  ASN B CA  1 
ATOM   2244 C C   . ASN B 1 43  ? 2.879   0.067   -41.935 1.00 22.72 ? 23  ASN B C   1 
ATOM   2245 O O   . ASN B 1 43  ? 1.913   -0.048  -42.719 1.00 20.93 ? 23  ASN B O   1 
ATOM   2246 C CB  . ASN B 1 43  ? 4.668   -1.751  -42.000 1.00 24.56 ? 23  ASN B CB  1 
ATOM   2247 C CG  . ASN B 1 43  ? 5.554   -2.374  -43.044 1.00 24.44 ? 23  ASN B CG  1 
ATOM   2248 O OD1 . ASN B 1 43  ? 5.109   -2.522  -44.172 1.00 25.56 ? 23  ASN B OD1 1 
ATOM   2249 N ND2 . ASN B 1 43  ? 6.810   -2.626  -42.716 1.00 25.14 ? 23  ASN B ND2 1 
ATOM   2250 N N   . CYS B 1 44  ? 2.765   0.473   -40.667 1.00 21.37 ? 24  CYS B N   1 
ATOM   2251 C CA  . CYS B 1 44  ? 1.501   0.981   -40.077 1.00 20.31 ? 24  CYS B CA  1 
ATOM   2252 C C   . CYS B 1 44  ? 1.046   2.242   -40.820 1.00 21.84 ? 24  CYS B C   1 
ATOM   2253 O O   . CYS B 1 44  ? -0.158  2.345   -41.112 1.00 23.41 ? 24  CYS B O   1 
ATOM   2254 C CB  . CYS B 1 44  ? 1.665   1.273   -38.592 1.00 21.14 ? 24  CYS B CB  1 
ATOM   2255 S SG  . CYS B 1 44  ? 1.693   -0.209  -37.553 1.00 21.83 ? 24  CYS B SG  1 
ATOM   2256 N N   . LEU B 1 45  ? 1.950   3.188   -41.101 1.00 22.92 ? 25  LEU B N   1 
ATOM   2257 C CA  . LEU B 1 45  ? 1.589   4.484   -41.749 1.00 24.80 ? 25  LEU B CA  1 
ATOM   2258 C C   . LEU B 1 45  ? 1.165   4.231   -43.204 1.00 28.16 ? 25  LEU B C   1 
ATOM   2259 O O   . LEU B 1 45  ? 0.130   4.778   -43.626 1.00 27.16 ? 25  LEU B O   1 
ATOM   2260 C CB  . LEU B 1 45  ? 2.765   5.466   -41.674 1.00 25.76 ? 25  LEU B CB  1 
ATOM   2261 C CG  . LEU B 1 45  ? 3.167   5.959   -40.276 1.00 24.49 ? 25  LEU B CG  1 
ATOM   2262 C CD1 . LEU B 1 45  ? 4.453   6.758   -40.357 1.00 23.84 ? 25  LEU B CD1 1 
ATOM   2263 C CD2 . LEU B 1 45  ? 2.069   6.799   -39.634 1.00 24.79 ? 25  LEU B CD2 1 
ATOM   2264 N N   . ILE B 1 46  ? 1.893   3.392   -43.947 1.00 32.37 ? 26  ILE B N   1 
ATOM   2265 C CA  . ILE B 1 46  ? 1.476   2.985   -45.328 1.00 34.39 ? 26  ILE B CA  1 
ATOM   2266 C C   . ILE B 1 46  ? 0.047   2.432   -45.268 1.00 36.40 ? 26  ILE B C   1 
ATOM   2267 O O   . ILE B 1 46  ? -0.793  2.890   -46.052 1.00 34.67 ? 26  ILE B O   1 
ATOM   2268 C CB  . ILE B 1 46  ? 2.440   1.965   -45.952 1.00 35.32 ? 26  ILE B CB  1 
ATOM   2269 C CG1 . ILE B 1 46  ? 3.772   2.617   -46.323 1.00 33.51 ? 26  ILE B CG1 1 
ATOM   2270 C CG2 . ILE B 1 46  ? 1.789   1.285   -47.158 1.00 36.16 ? 26  ILE B CG2 1 
ATOM   2271 C CD1 . ILE B 1 46  ? 4.923   1.644   -46.374 1.00 35.60 ? 26  ILE B CD1 1 
ATOM   2272 N N   . LYS B 1 47  ? -0.202  1.495   -44.350 1.00 39.43 ? 27  LYS B N   1 
ATOM   2273 C CA  . LYS B 1 47  ? -1.519  0.841   -44.140 1.00 41.11 ? 27  LYS B CA  1 
ATOM   2274 C C   . LYS B 1 47  ? -2.587  1.907   -43.844 1.00 41.15 ? 27  LYS B C   1 
ATOM   2275 O O   . LYS B 1 47  ? -3.717  1.682   -44.232 1.00 45.56 ? 27  LYS B O   1 
ATOM   2276 C CB  . LYS B 1 47  ? -1.387  -0.203  -43.030 1.00 42.50 ? 27  LYS B CB  1 
ATOM   2277 C CG  . LYS B 1 47  ? -2.474  -1.260  -42.996 1.00 43.15 ? 27  LYS B CG  1 
ATOM   2278 C CD  . LYS B 1 47  ? -2.032  -2.513  -42.279 1.00 46.05 ? 27  LYS B CD  1 
ATOM   2279 C CE  . LYS B 1 47  ? -3.183  -3.299  -41.690 1.00 48.40 ? 27  LYS B CE  1 
ATOM   2280 N NZ  . LYS B 1 47  ? -2.929  -4.759  -41.771 1.00 51.89 ? 27  LYS B NZ  1 
ATOM   2281 N N   . SER B 1 48  ? -2.225  3.039   -43.225 1.00 45.99 ? 28  SER B N   1 
ATOM   2282 C CA  . SER B 1 48  ? -3.115  4.201   -42.929 1.00 42.96 ? 28  SER B CA  1 
ATOM   2283 C C   . SER B 1 48  ? -3.568  4.913   -44.208 1.00 42.45 ? 28  SER B C   1 
ATOM   2284 O O   . SER B 1 48  ? -4.562  5.633   -44.131 1.00 47.13 ? 28  SER B O   1 
ATOM   2285 C CB  . SER B 1 48  ? -2.447  5.204   -42.014 1.00 42.82 ? 28  SER B CB  1 
ATOM   2286 O OG  . SER B 1 48  ? -1.711  6.190   -42.744 1.00 39.40 ? 28  SER B OG  1 
ATOM   2287 N N   . GLY B 1 49  ? -2.818  4.814   -45.309 1.00 40.20 ? 29  GLY B N   1 
ATOM   2288 C CA  . GLY B 1 49  ? -3.191  5.432   -46.597 1.00 37.86 ? 29  GLY B CA  1 
ATOM   2289 C C   . GLY B 1 49  ? -2.391  6.683   -46.909 1.00 37.15 ? 29  GLY B C   1 
ATOM   2290 O O   . GLY B 1 49  ? -2.661  7.325   -47.944 1.00 38.35 ? 29  GLY B O   1 
ATOM   2291 N N   . CYS B 1 50  ? -1.386  7.011   -46.103 1.00 35.10 ? 30  CYS B N   1 
ATOM   2292 C CA  . CYS B 1 50  ? -0.623  8.274   -46.268 1.00 33.09 ? 30  CYS B CA  1 
ATOM   2293 C C   . CYS B 1 50  ? 0.429   8.127   -47.380 1.00 31.71 ? 30  CYS B C   1 
ATOM   2294 O O   . CYS B 1 50  ? 0.813   6.988   -47.726 1.00 29.91 ? 30  CYS B O   1 
ATOM   2295 C CB  . CYS B 1 50  ? -0.018  8.699   -44.936 1.00 35.05 ? 30  CYS B CB  1 
ATOM   2296 S SG  . CYS B 1 50  ? 1.609   7.982   -44.603 1.00 35.02 ? 30  CYS B SG  1 
ATOM   2297 N N   . LYS B 1 51  ? 0.873   9.253   -47.932 1.00 29.24 ? 31  LYS B N   1 
ATOM   2298 C CA  . LYS B 1 51  ? 2.060   9.340   -48.822 1.00 32.48 ? 31  LYS B CA  1 
ATOM   2299 C C   . LYS B 1 51  ? 3.329   9.430   -47.958 1.00 29.84 ? 31  LYS B C   1 
ATOM   2300 O O   . LYS B 1 51  ? 3.557   10.488  -47.339 1.00 32.16 ? 31  LYS B O   1 
ATOM   2301 C CB  . LYS B 1 51  ? 1.936   10.566  -49.729 1.00 35.03 ? 31  LYS B CB  1 
ATOM   2302 C CG  . LYS B 1 51  ? 3.161   10.886  -50.573 1.00 40.82 ? 31  LYS B CG  1 
ATOM   2303 C CD  . LYS B 1 51  ? 3.198   10.195  -51.936 1.00 46.48 ? 31  LYS B CD  1 
ATOM   2304 C CE  . LYS B 1 51  ? 4.000   10.964  -52.971 1.00 48.20 ? 31  LYS B CE  1 
ATOM   2305 N NZ  . LYS B 1 51  ? 5.210   11.598  -52.387 1.00 49.84 ? 31  LYS B NZ  1 
ATOM   2306 N N   . LEU B 1 52  ? 4.151   8.387   -47.955 1.00 25.55 ? 32  LEU B N   1 
ATOM   2307 C CA  . LEU B 1 52  ? 5.273   8.232   -47.000 1.00 24.58 ? 32  LEU B CA  1 
ATOM   2308 C C   . LEU B 1 52  ? 6.611   8.540   -47.683 1.00 24.65 ? 32  LEU B C   1 
ATOM   2309 O O   . LEU B 1 52  ? 6.872   7.994   -48.790 1.00 25.21 ? 32  LEU B O   1 
ATOM   2310 C CB  . LEU B 1 52  ? 5.269   6.821   -46.415 1.00 23.53 ? 32  LEU B CB  1 
ATOM   2311 C CG  . LEU B 1 52  ? 6.236   6.643   -45.242 1.00 24.11 ? 32  LEU B CG  1 
ATOM   2312 C CD1 . LEU B 1 52  ? 5.792   7.500   -44.058 1.00 25.00 ? 32  LEU B CD1 1 
ATOM   2313 C CD2 . LEU B 1 52  ? 6.355   5.169   -44.833 1.00 23.62 ? 32  LEU B CD2 1 
ATOM   2314 N N   . THR B 1 53  ? 7.396   9.416   -47.052 1.00 22.02 ? 33  THR B N   1 
ATOM   2315 C CA  . THR B 1 53  ? 8.814   9.723   -47.388 1.00 23.01 ? 33  THR B CA  1 
ATOM   2316 C C   . THR B 1 53  ? 9.677   9.283   -46.198 1.00 23.93 ? 33  THR B C   1 
ATOM   2317 O O   . THR B 1 53  ? 9.338   9.657   -45.047 1.00 21.92 ? 33  THR B O   1 
ATOM   2318 C CB  . THR B 1 53  ? 8.999   11.207  -47.745 1.00 22.26 ? 33  THR B CB  1 
ATOM   2319 O OG1 . THR B 1 53  ? 8.002   11.536  -48.711 1.00 20.12 ? 33  THR B OG1 1 
ATOM   2320 C CG2 . THR B 1 53  ? 10.378  11.532  -48.282 1.00 23.12 ? 33  THR B CG2 1 
ATOM   2321 N N   . VAL B 1 54  ? 10.714  8.479   -46.468 1.00 23.38 ? 34  VAL B N   1 
ATOM   2322 C CA  . VAL B 1 54  ? 11.539  7.790   -45.439 1.00 22.09 ? 34  VAL B CA  1 
ATOM   2323 C C   . VAL B 1 54  ? 13.008  8.177   -45.630 1.00 23.17 ? 34  VAL B C   1 
ATOM   2324 O O   . VAL B 1 54  ? 13.440  8.375   -46.772 1.00 22.67 ? 34  VAL B O   1 
ATOM   2325 C CB  . VAL B 1 54  ? 11.302  6.268   -45.492 1.00 22.07 ? 34  VAL B CB  1 
ATOM   2326 C CG1 . VAL B 1 54  ? 9.834   5.935   -45.268 1.00 21.11 ? 34  VAL B CG1 1 
ATOM   2327 C CG2 . VAL B 1 54  ? 11.761  5.650   -46.800 1.00 23.14 ? 34  VAL B CG2 1 
ATOM   2328 N N   . TRP B 1 55  ? 13.744  8.301   -44.527 1.00 22.48 ? 35  TRP B N   1 
ATOM   2329 C CA  . TRP B 1 55  ? 15.224  8.372   -44.523 1.00 22.91 ? 35  TRP B CA  1 
ATOM   2330 C C   . TRP B 1 55  ? 15.753  7.447   -43.430 1.00 23.37 ? 35  TRP B C   1 
ATOM   2331 O O   . TRP B 1 55  ? 15.154  7.418   -42.324 1.00 22.20 ? 35  TRP B O   1 
ATOM   2332 C CB  . TRP B 1 55  ? 15.730  9.802   -44.313 1.00 24.34 ? 35  TRP B CB  1 
ATOM   2333 C CG  . TRP B 1 55  ? 17.225  9.882   -44.283 1.00 25.70 ? 35  TRP B CG  1 
ATOM   2334 C CD1 . TRP B 1 55  ? 18.041  10.189  -45.328 1.00 25.87 ? 35  TRP B CD1 1 
ATOM   2335 C CD2 . TRP B 1 55  ? 18.093  9.607   -43.164 1.00 29.27 ? 35  TRP B CD2 1 
ATOM   2336 N NE1 . TRP B 1 55  ? 19.350  10.167  -44.935 1.00 27.42 ? 35  TRP B NE1 1 
ATOM   2337 C CE2 . TRP B 1 55  ? 19.420  9.803   -43.616 1.00 28.55 ? 35  TRP B CE2 1 
ATOM   2338 C CE3 . TRP B 1 55  ? 17.889  9.246   -41.825 1.00 28.66 ? 35  TRP B CE3 1 
ATOM   2339 C CZ2 . TRP B 1 55  ? 20.528  9.655   -42.778 1.00 28.67 ? 35  TRP B CZ2 1 
ATOM   2340 C CZ3 . TRP B 1 55  ? 18.985  9.090   -41.000 1.00 28.67 ? 35  TRP B CZ3 1 
ATOM   2341 C CH2 . TRP B 1 55  ? 20.287  9.290   -41.471 1.00 28.80 ? 35  TRP B CH2 1 
ATOM   2342 N N   . ASN B 1 56  ? 16.828  6.718   -43.738 1.00 23.35 ? 36  ASN B N   1 
ATOM   2343 C CA  . ASN B 1 56  ? 17.621  5.917   -42.769 1.00 24.55 ? 36  ASN B CA  1 
ATOM   2344 C C   . ASN B 1 56  ? 19.100  6.025   -43.143 1.00 26.18 ? 36  ASN B C   1 
ATOM   2345 O O   . ASN B 1 56  ? 19.410  6.026   -44.365 1.00 25.42 ? 36  ASN B O   1 
ATOM   2346 C CB  . ASN B 1 56  ? 17.161  4.459   -42.750 1.00 23.61 ? 36  ASN B CB  1 
ATOM   2347 C CG  . ASN B 1 56  ? 17.673  3.694   -41.545 1.00 24.10 ? 36  ASN B CG  1 
ATOM   2348 O OD1 . ASN B 1 56  ? 17.310  4.012   -40.408 1.00 22.43 ? 36  ASN B OD1 1 
ATOM   2349 N ND2 . ASN B 1 56  ? 18.415  2.620   -41.790 1.00 23.16 ? 36  ASN B ND2 1 
ATOM   2350 N N   . ARG B 1 57  ? 19.976  6.081   -42.145 1.00 26.47 ? 37  ARG B N   1 
ATOM   2351 C CA  . ARG B 1 57  ? 21.452  6.011   -42.322 1.00 26.84 ? 37  ARG B CA  1 
ATOM   2352 C C   . ARG B 1 57  ? 21.774  4.907   -43.339 1.00 25.64 ? 37  ARG B C   1 
ATOM   2353 O O   . ARG B 1 57  ? 22.439  5.206   -44.338 1.00 24.26 ? 37  ARG B O   1 
ATOM   2354 C CB  . ARG B 1 57  ? 22.167  5.779   -40.983 1.00 27.00 ? 37  ARG B CB  1 
ATOM   2355 C CG  . ARG B 1 57  ? 23.671  5.560   -41.132 1.00 27.19 ? 37  ARG B CG  1 
ATOM   2356 C CD  . ARG B 1 57  ? 24.356  5.386   -39.798 1.00 27.31 ? 37  ARG B CD  1 
ATOM   2357 N NE  . ARG B 1 57  ? 23.874  4.198   -39.105 1.00 28.11 ? 37  ARG B NE  1 
ATOM   2358 C CZ  . ARG B 1 57  ? 24.329  3.786   -37.933 1.00 28.63 ? 37  ARG B CZ  1 
ATOM   2359 N NH1 . ARG B 1 57  ? 23.834  2.691   -37.388 1.00 29.87 ? 37  ARG B NH1 1 
ATOM   2360 N NH2 . ARG B 1 57  ? 25.294  4.450   -37.318 1.00 31.04 ? 37  ARG B NH2 1 
ATOM   2361 N N   . SER B 1 58  ? 21.296  3.685   -43.107 1.00 25.98 ? 38  SER B N   1 
ATOM   2362 C CA  . SER B 1 58  ? 21.396  2.548   -44.058 1.00 26.30 ? 38  SER B CA  1 
ATOM   2363 C C   . SER B 1 58  ? 20.141  2.534   -44.948 1.00 26.04 ? 38  SER B C   1 
ATOM   2364 O O   . SER B 1 58  ? 19.136  1.927   -44.548 1.00 29.23 ? 38  SER B O   1 
ATOM   2365 C CB  . SER B 1 58  ? 21.602  1.268   -43.304 1.00 26.55 ? 38  SER B CB  1 
ATOM   2366 O OG  . SER B 1 58  ? 22.591  1.455   -42.296 1.00 28.92 ? 38  SER B OG  1 
ATOM   2367 N N   . ALA B 1 59  ? 20.189  3.224   -46.096 1.00 27.36 ? 39  ALA B N   1 
ATOM   2368 C CA  . ALA B 1 59  ? 19.018  3.561   -46.959 1.00 28.87 ? 39  ALA B CA  1 
ATOM   2369 C C   . ALA B 1 59  ? 18.346  2.291   -47.512 1.00 29.26 ? 39  ALA B C   1 
ATOM   2370 O O   . ALA B 1 59  ? 17.114  2.324   -47.715 1.00 27.23 ? 39  ALA B O   1 
ATOM   2371 C CB  . ALA B 1 59  ? 19.421  4.509   -48.071 1.00 26.36 ? 39  ALA B CB  1 
ATOM   2372 N N   . GLU B 1 60  ? 19.114  1.210   -47.715 1.00 29.36 ? 40  GLU B N   1 
ATOM   2373 C CA  . GLU B 1 60  ? 18.629  -0.083  -48.272 1.00 30.30 ? 40  GLU B CA  1 
ATOM   2374 C C   . GLU B 1 60  ? 17.536  -0.723  -47.406 1.00 31.47 ? 40  GLU B C   1 
ATOM   2375 O O   . GLU B 1 60  ? 16.785  -1.573  -47.943 1.00 31.83 ? 40  GLU B O   1 
ATOM   2376 C CB  . GLU B 1 60  ? 19.792  -1.059  -48.461 1.00 33.64 ? 40  GLU B CB  1 
ATOM   2377 C CG  . GLU B 1 60  ? 20.288  -1.735  -47.194 1.00 34.48 ? 40  GLU B CG  1 
ATOM   2378 C CD  . GLU B 1 60  ? 21.445  -1.042  -46.486 1.00 36.13 ? 40  GLU B CD  1 
ATOM   2379 O OE1 . GLU B 1 60  ? 21.766  0.113   -46.836 1.00 36.21 ? 40  GLU B OE1 1 
ATOM   2380 O OE2 . GLU B 1 60  ? 22.008  -1.660  -45.563 1.00 43.06 ? 40  GLU B OE2 1 
ATOM   2381 N N   . LYS B 1 61  ? 17.435  -0.362  -46.123 1.00 32.22 ? 41  LYS B N   1 
ATOM   2382 C CA  . LYS B 1 61  ? 16.349  -0.854  -45.228 1.00 30.62 ? 41  LYS B CA  1 
ATOM   2383 C C   . LYS B 1 61  ? 14.984  -0.318  -45.697 1.00 27.38 ? 41  LYS B C   1 
ATOM   2384 O O   . LYS B 1 61  ? 13.956  -0.889  -45.279 1.00 26.39 ? 41  LYS B O   1 
ATOM   2385 C CB  . LYS B 1 61  ? 16.643  -0.477  -43.771 1.00 32.58 ? 41  LYS B CB  1 
ATOM   2386 C CG  . LYS B 1 61  ? 17.984  -0.988  -43.243 1.00 33.24 ? 41  LYS B CG  1 
ATOM   2387 C CD  . LYS B 1 61  ? 18.006  -1.243  -41.760 1.00 34.20 ? 41  LYS B CD  1 
ATOM   2388 C CE  . LYS B 1 61  ? 19.366  -1.653  -41.226 1.00 34.35 ? 41  LYS B CE  1 
ATOM   2389 N NZ  . LYS B 1 61  ? 19.354  -1.672  -39.740 1.00 33.12 ? 41  LYS B NZ  1 
ATOM   2390 N N   . ALA B 1 62  ? 14.941  0.692   -46.577 1.00 27.36 ? 42  ALA B N   1 
ATOM   2391 C CA  . ALA B 1 62  ? 13.673  1.145   -47.212 1.00 29.22 ? 42  ALA B CA  1 
ATOM   2392 C C   . ALA B 1 62  ? 13.244  0.149   -48.298 1.00 28.70 ? 42  ALA B C   1 
ATOM   2393 O O   . ALA B 1 62  ? 12.106  0.274   -48.770 1.00 28.06 ? 42  ALA B O   1 
ATOM   2394 C CB  . ALA B 1 62  ? 13.811  2.543   -47.772 1.00 29.59 ? 42  ALA B CB  1 
ATOM   2395 N N   . ALA B 1 63  ? 14.097  -0.825  -48.654 1.00 30.45 ? 43  ALA B N   1 
ATOM   2396 C CA  . ALA B 1 63  ? 13.903  -1.726  -49.818 1.00 30.16 ? 43  ALA B CA  1 
ATOM   2397 C C   . ALA B 1 63  ? 12.464  -2.245  -49.836 1.00 29.30 ? 43  ALA B C   1 
ATOM   2398 O O   . ALA B 1 63  ? 11.823  -2.127  -50.897 1.00 30.53 ? 43  ALA B O   1 
ATOM   2399 C CB  . ALA B 1 63  ? 14.914  -2.850  -49.818 1.00 31.23 ? 43  ALA B CB  1 
ATOM   2400 N N   . SER B 1 64  ? 11.964  -2.766  -48.710 1.00 26.72 ? 44  SER B N   1 
ATOM   2401 C CA  . SER B 1 64  ? 10.622  -3.392  -48.608 1.00 26.68 ? 44  SER B CA  1 
ATOM   2402 C C   . SER B 1 64  ? 9.508   -2.338  -48.669 1.00 26.90 ? 44  SER B C   1 
ATOM   2403 O O   . SER B 1 64  ? 8.360   -2.755  -48.773 1.00 26.50 ? 44  SER B O   1 
ATOM   2404 C CB  . SER B 1 64  ? 10.489  -4.231  -47.355 1.00 28.94 ? 44  SER B CB  1 
ATOM   2405 O OG  . SER B 1 64  ? 10.613  -3.429  -46.180 1.00 28.95 ? 44  SER B OG  1 
ATOM   2406 N N   . LEU B 1 65  ? 9.802   -1.035  -48.564 1.00 27.81 ? 45  LEU B N   1 
ATOM   2407 C CA  . LEU B 1 65  ? 8.733   0.013   -48.523 1.00 30.35 ? 45  LEU B CA  1 
ATOM   2408 C C   . LEU B 1 65  ? 8.455   0.611   -49.919 1.00 30.95 ? 45  LEU B C   1 
ATOM   2409 O O   . LEU B 1 65  ? 7.316   1.053   -50.144 1.00 31.39 ? 45  LEU B O   1 
ATOM   2410 C CB  . LEU B 1 65  ? 9.135   1.120   -47.551 1.00 29.18 ? 45  LEU B CB  1 
ATOM   2411 C CG  . LEU B 1 65  ? 9.380   0.692   -46.108 1.00 28.01 ? 45  LEU B CG  1 
ATOM   2412 C CD1 . LEU B 1 65  ? 9.911   1.874   -45.313 1.00 27.90 ? 45  LEU B CD1 1 
ATOM   2413 C CD2 . LEU B 1 65  ? 8.119   0.121   -45.475 1.00 27.07 ? 45  LEU B CD2 1 
ATOM   2414 N N   . VAL B 1 66  ? 9.449   0.624   -50.807 1.00 33.13 ? 46  VAL B N   1 
ATOM   2415 C CA  . VAL B 1 66  ? 9.357   1.105   -52.222 1.00 33.23 ? 46  VAL B CA  1 
ATOM   2416 C C   . VAL B 1 66  ? 8.200   0.419   -52.957 1.00 33.60 ? 46  VAL B C   1 
ATOM   2417 O O   . VAL B 1 66  ? 7.380   1.091   -53.571 1.00 35.21 ? 46  VAL B O   1 
ATOM   2418 C CB  . VAL B 1 66  ? 10.708  0.923   -52.934 1.00 34.84 ? 46  VAL B CB  1 
ATOM   2419 C CG1 . VAL B 1 66  ? 10.691  1.492   -54.345 1.00 37.19 ? 46  VAL B CG1 1 
ATOM   2420 C CG2 . VAL B 1 66  ? 11.838  1.540   -52.126 1.00 34.98 ? 46  VAL B CG2 1 
ATOM   2421 N N   . PRO B 1 67  ? 8.040   -0.923  -52.921 1.00 35.25 ? 47  PRO B N   1 
ATOM   2422 C CA  . PRO B 1 67  ? 6.869   -1.551  -53.533 1.00 33.92 ? 47  PRO B CA  1 
ATOM   2423 C C   . PRO B 1 67  ? 5.528   -1.188  -52.878 1.00 35.54 ? 47  PRO B C   1 
ATOM   2424 O O   . PRO B 1 67  ? 4.494   -1.507  -53.450 1.00 33.14 ? 47  PRO B O   1 
ATOM   2425 C CB  . PRO B 1 67  ? 7.087   -3.062  -53.355 1.00 34.20 ? 47  PRO B CB  1 
ATOM   2426 C CG  . PRO B 1 67  ? 8.559   -3.209  -53.026 1.00 34.56 ? 47  PRO B CG  1 
ATOM   2427 C CD  . PRO B 1 67  ? 8.985   -1.911  -52.381 1.00 34.62 ? 47  PRO B CD  1 
ATOM   2428 N N   . GLN B 1 68  ? 5.534   -0.591  -51.684 1.00 32.11 ? 48  GLN B N   1 
ATOM   2429 C CA  . GLN B 1 68  ? 4.266   -0.173  -51.033 1.00 30.36 ? 48  GLN B CA  1 
ATOM   2430 C C   . GLN B 1 68  ? 3.974   1.297   -51.387 1.00 29.18 ? 48  GLN B C   1 
ATOM   2431 O O   . GLN B 1 68  ? 2.889   1.768   -51.017 1.00 31.36 ? 48  GLN B O   1 
ATOM   2432 C CB  . GLN B 1 68  ? 4.322   -0.448  -49.530 1.00 31.94 ? 48  GLN B CB  1 
ATOM   2433 C CG  . GLN B 1 68  ? 4.611   -1.906  -49.182 1.00 31.91 ? 48  GLN B CG  1 
ATOM   2434 C CD  . GLN B 1 68  ? 4.614   -2.188  -47.701 1.00 31.02 ? 48  GLN B CD  1 
ATOM   2435 O OE1 . GLN B 1 68  ? 3.587   -2.084  -47.037 1.00 30.25 ? 48  GLN B OE1 1 
ATOM   2436 N NE2 . GLN B 1 68  ? 5.781   -2.548  -47.174 1.00 30.90 ? 48  GLN B NE2 1 
ATOM   2437 N N   . GLY B 1 69  ? 4.892   1.980   -52.080 1.00 26.93 ? 49  GLY B N   1 
ATOM   2438 C CA  . GLY B 1 69  ? 4.699   3.351   -52.593 1.00 28.06 ? 49  GLY B CA  1 
ATOM   2439 C C   . GLY B 1 69  ? 5.483   4.400   -51.819 1.00 27.44 ? 49  GLY B C   1 
ATOM   2440 O O   . GLY B 1 69  ? 5.244   5.609   -52.032 1.00 28.28 ? 49  GLY B O   1 
ATOM   2441 N N   . ALA B 1 70  ? 6.428   3.981   -50.985 1.00 28.17 ? 50  ALA B N   1 
ATOM   2442 C CA  . ALA B 1 70  ? 7.269   4.895   -50.185 1.00 26.74 ? 50  ALA B CA  1 
ATOM   2443 C C   . ALA B 1 70  ? 8.360   5.459   -51.090 1.00 26.62 ? 50  ALA B C   1 
ATOM   2444 O O   . ALA B 1 70  ? 8.967   4.687   -51.852 1.00 22.71 ? 50  ALA B O   1 
ATOM   2445 C CB  . ALA B 1 70  ? 7.846   4.190   -48.978 1.00 27.35 ? 50  ALA B CB  1 
ATOM   2446 N N   . THR B 1 71  ? 8.605   6.755   -50.948 1.00 25.68 ? 51  THR B N   1 
ATOM   2447 C CA  . THR B 1 71  ? 9.706   7.522   -51.564 1.00 27.34 ? 51  THR B CA  1 
ATOM   2448 C C   . THR B 1 71  ? 10.880  7.587   -50.583 1.00 27.86 ? 51  THR B C   1 
ATOM   2449 O O   . THR B 1 71  ? 10.623  7.915   -49.394 1.00 28.12 ? 51  THR B O   1 
ATOM   2450 C CB  . THR B 1 71  ? 9.213   8.944   -51.851 1.00 27.38 ? 51  THR B CB  1 
ATOM   2451 O OG1 . THR B 1 71  ? 8.037   8.732   -52.630 1.00 32.30 ? 51  THR B OG1 1 
ATOM   2452 C CG2 . THR B 1 71  ? 10.223  9.818   -52.560 1.00 27.88 ? 51  THR B CG2 1 
ATOM   2453 N N   . VAL B 1 72  ? 12.104  7.338   -51.058 1.00 25.05 ? 52  VAL B N   1 
ATOM   2454 C CA  . VAL B 1 72  ? 13.346  7.350   -50.235 1.00 27.24 ? 52  VAL B CA  1 
ATOM   2455 C C   . VAL B 1 72  ? 14.026  8.713   -50.386 1.00 28.31 ? 52  VAL B C   1 
ATOM   2456 O O   . VAL B 1 72  ? 14.377  9.091   -51.523 1.00 28.78 ? 52  VAL B O   1 
ATOM   2457 C CB  . VAL B 1 72  ? 14.276  6.191   -50.633 1.00 29.46 ? 52  VAL B CB  1 
ATOM   2458 C CG1 . VAL B 1 72  ? 15.572  6.204   -49.833 1.00 33.13 ? 52  VAL B CG1 1 
ATOM   2459 C CG2 . VAL B 1 72  ? 13.574  4.850   -50.494 1.00 29.39 ? 52  VAL B CG2 1 
ATOM   2460 N N   . ALA B 1 73  ? 14.178  9.445   -49.283 1.00 28.79 ? 53  ALA B N   1 
ATOM   2461 C CA  . ALA B 1 73  ? 14.844  10.764  -49.247 1.00 28.34 ? 53  ALA B CA  1 
ATOM   2462 C C   . ALA B 1 73  ? 16.346  10.547  -49.037 1.00 30.92 ? 53  ALA B C   1 
ATOM   2463 O O   . ALA B 1 73  ? 16.709  9.737   -48.167 1.00 33.87 ? 53  ALA B O   1 
ATOM   2464 C CB  . ALA B 1 73  ? 14.241  11.611  -48.158 1.00 27.82 ? 53  ALA B CB  1 
ATOM   2465 N N   . ALA B 1 74  ? 17.187  11.268  -49.779 1.00 31.45 ? 54  ALA B N   1 
ATOM   2466 C CA  . ALA B 1 74  ? 18.665  11.164  -49.729 1.00 31.28 ? 54  ALA B CA  1 
ATOM   2467 C C   . ALA B 1 74  ? 19.178  11.611  -48.355 1.00 30.06 ? 54  ALA B C   1 
ATOM   2468 O O   . ALA B 1 74  ? 20.138  11.026  -47.865 1.00 30.42 ? 54  ALA B O   1 
ATOM   2469 C CB  . ALA B 1 74  ? 19.273  11.987  -50.848 1.00 30.43 ? 54  ALA B CB  1 
ATOM   2470 N N   . THR B 1 75  ? 18.558  12.629  -47.760 1.00 32.41 ? 55  THR B N   1 
ATOM   2471 C CA  . THR B 1 75  ? 19.052  13.330  -46.546 1.00 31.57 ? 55  THR B CA  1 
ATOM   2472 C C   . THR B 1 75  ? 17.897  13.590  -45.577 1.00 29.90 ? 55  THR B C   1 
ATOM   2473 O O   . THR B 1 75  ? 16.744  13.724  -45.986 1.00 26.96 ? 55  THR B O   1 
ATOM   2474 C CB  . THR B 1 75  ? 19.740  14.653  -46.923 1.00 32.70 ? 55  THR B CB  1 
ATOM   2475 O OG1 . THR B 1 75  ? 18.745  15.570  -47.385 1.00 30.15 ? 55  THR B OG1 1 
ATOM   2476 C CG2 . THR B 1 75  ? 20.798  14.474  -47.993 1.00 34.18 ? 55  THR B CG2 1 
ATOM   2477 N N   . PRO B 1 76  ? 18.194  13.662  -44.261 1.00 30.88 ? 56  PRO B N   1 
ATOM   2478 C CA  . PRO B 1 76  ? 17.224  14.098  -43.259 1.00 32.39 ? 56  PRO B CA  1 
ATOM   2479 C C   . PRO B 1 76  ? 16.515  15.385  -43.700 1.00 32.24 ? 56  PRO B C   1 
ATOM   2480 O O   . PRO B 1 76  ? 15.286  15.412  -43.705 1.00 33.17 ? 56  PRO B O   1 
ATOM   2481 C CB  . PRO B 1 76  ? 18.095  14.356  -42.016 1.00 32.71 ? 56  PRO B CB  1 
ATOM   2482 C CG  . PRO B 1 76  ? 19.264  13.399  -42.167 1.00 32.10 ? 56  PRO B CG  1 
ATOM   2483 C CD  . PRO B 1 76  ? 19.500  13.321  -43.661 1.00 32.58 ? 56  PRO B CD  1 
ATOM   2484 N N   . ALA B 1 77  ? 17.304  16.387  -44.106 1.00 31.32 ? 57  ALA B N   1 
ATOM   2485 C CA  . ALA B 1 77  ? 16.829  17.715  -44.564 1.00 30.02 ? 57  ALA B CA  1 
ATOM   2486 C C   . ALA B 1 77  ? 15.767  17.535  -45.652 1.00 29.31 ? 57  ALA B C   1 
ATOM   2487 O O   . ALA B 1 77  ? 14.691  18.153  -45.557 1.00 28.45 ? 57  ALA B O   1 
ATOM   2488 C CB  . ALA B 1 77  ? 17.995  18.537  -45.047 1.00 29.79 ? 57  ALA B CB  1 
ATOM   2489 N N   . GLU B 1 78  ? 16.055  16.674  -46.620 1.00 30.07 ? 58  GLU B N   1 
ATOM   2490 C CA  . GLU B 1 78  ? 15.155  16.369  -47.761 1.00 32.75 ? 58  GLU B CA  1 
ATOM   2491 C C   . GLU B 1 78  ? 13.889  15.683  -47.248 1.00 28.75 ? 58  GLU B C   1 
ATOM   2492 O O   . GLU B 1 78  ? 12.785  16.042  -47.668 1.00 28.11 ? 58  GLU B O   1 
ATOM   2493 C CB  . GLU B 1 78  ? 15.867  15.441  -48.744 1.00 38.24 ? 58  GLU B CB  1 
ATOM   2494 C CG  . GLU B 1 78  ? 15.580  15.742  -50.192 1.00 42.33 ? 58  GLU B CG  1 
ATOM   2495 C CD  . GLU B 1 78  ? 16.514  14.964  -51.101 1.00 47.82 ? 58  GLU B CD  1 
ATOM   2496 O OE1 . GLU B 1 78  ? 17.522  15.554  -51.533 1.00 48.41 ? 58  GLU B OE1 1 
ATOM   2497 O OE2 . GLU B 1 78  ? 16.241  13.759  -51.343 1.00 51.92 ? 58  GLU B OE2 1 
ATOM   2498 N N   . CYS B 1 79  ? 14.047  14.684  -46.389 1.00 28.12 ? 59  CYS B N   1 
ATOM   2499 C CA  . CYS B 1 79  ? 12.914  13.910  -45.847 1.00 25.92 ? 59  CYS B CA  1 
ATOM   2500 C C   . CYS B 1 79  ? 11.947  14.888  -45.149 1.00 25.13 ? 59  CYS B C   1 
ATOM   2501 O O   . CYS B 1 79  ? 10.725  14.847  -45.402 1.00 21.66 ? 59  CYS B O   1 
ATOM   2502 C CB  . CYS B 1 79  ? 13.471  12.852  -44.916 1.00 25.96 ? 59  CYS B CB  1 
ATOM   2503 S SG  . CYS B 1 79  ? 12.210  11.690  -44.367 1.00 25.81 ? 59  CYS B SG  1 
ATOM   2504 N N   . VAL B 1 80  ? 12.500  15.804  -44.356 1.00 25.02 ? 60  VAL B N   1 
ATOM   2505 C CA  . VAL B 1 80  ? 11.735  16.826  -43.583 1.00 25.19 ? 60  VAL B CA  1 
ATOM   2506 C C   . VAL B 1 80  ? 11.013  17.767  -44.552 1.00 27.18 ? 60  VAL B C   1 
ATOM   2507 O O   . VAL B 1 80  ? 9.828   18.084  -44.286 1.00 26.95 ? 60  VAL B O   1 
ATOM   2508 C CB  . VAL B 1 80  ? 12.666  17.557  -42.599 1.00 25.03 ? 60  VAL B CB  1 
ATOM   2509 C CG1 . VAL B 1 80  ? 12.151  18.921  -42.155 1.00 26.16 ? 60  VAL B CG1 1 
ATOM   2510 C CG2 . VAL B 1 80  ? 12.936  16.675  -41.399 1.00 24.48 ? 60  VAL B CG2 1 
ATOM   2511 N N   . ALA B 1 81  ? 11.685  18.198  -45.624 1.00 27.79 ? 61  ALA B N   1 
ATOM   2512 C CA  . ALA B 1 81  ? 11.134  19.130  -46.637 1.00 28.98 ? 61  ALA B CA  1 
ATOM   2513 C C   . ALA B 1 81  ? 9.857   18.543  -47.251 1.00 28.10 ? 61  ALA B C   1 
ATOM   2514 O O   . ALA B 1 81  ? 8.948   19.330  -47.563 1.00 27.20 ? 61  ALA B O   1 
ATOM   2515 C CB  . ALA B 1 81  ? 12.172  19.422  -47.700 1.00 29.69 ? 61  ALA B CB  1 
ATOM   2516 N N   . SER B 1 82  ? 9.776   17.208  -47.376 1.00 27.68 ? 62  SER B N   1 
ATOM   2517 C CA  . SER B 1 82  ? 8.734   16.498  -48.160 1.00 27.46 ? 62  SER B CA  1 
ATOM   2518 C C   . SER B 1 82  ? 7.371   16.519  -47.454 1.00 25.31 ? 62  SER B C   1 
ATOM   2519 O O   . SER B 1 82  ? 6.368   16.252  -48.126 1.00 25.20 ? 62  SER B O   1 
ATOM   2520 C CB  . SER B 1 82  ? 9.151   15.081  -48.463 1.00 29.74 ? 62  SER B CB  1 
ATOM   2521 O OG  . SER B 1 82  ? 10.359  15.060  -49.206 1.00 31.48 ? 62  SER B OG  1 
ATOM   2522 N N   . SER B 1 83  ? 7.305   16.749  -46.140 1.00 23.97 ? 63  SER B N   1 
ATOM   2523 C CA  . SER B 1 83  ? 6.037   16.577  -45.383 1.00 20.74 ? 63  SER B CA  1 
ATOM   2524 C C   . SER B 1 83  ? 5.905   17.629  -44.292 1.00 19.87 ? 63  SER B C   1 
ATOM   2525 O O   . SER B 1 83  ? 6.905   18.129  -43.798 1.00 18.13 ? 63  SER B O   1 
ATOM   2526 C CB  . SER B 1 83  ? 5.956   15.186  -44.788 1.00 20.75 ? 63  SER B CB  1 
ATOM   2527 O OG  . SER B 1 83  ? 6.349   14.190  -45.727 1.00 21.05 ? 63  SER B OG  1 
ATOM   2528 N N   . PRO B 1 84  ? 4.665   17.946  -43.845 1.00 20.70 ? 64  PRO B N   1 
ATOM   2529 C CA  . PRO B 1 84  ? 4.453   18.814  -42.686 1.00 20.39 ? 64  PRO B CA  1 
ATOM   2530 C C   . PRO B 1 84  ? 4.446   18.046  -41.349 1.00 20.41 ? 64  PRO B C   1 
ATOM   2531 O O   . PRO B 1 84  ? 4.477   18.669  -40.304 1.00 19.99 ? 64  PRO B O   1 
ATOM   2532 C CB  . PRO B 1 84  ? 3.079   19.419  -43.012 1.00 21.11 ? 64  PRO B CB  1 
ATOM   2533 C CG  . PRO B 1 84  ? 2.340   18.275  -43.701 1.00 21.79 ? 64  PRO B CG  1 
ATOM   2534 C CD  . PRO B 1 84  ? 3.401   17.556  -44.499 1.00 20.66 ? 64  PRO B CD  1 
ATOM   2535 N N   . THR B 1 85  ? 4.441   16.710  -41.388 1.00 21.32 ? 65  THR B N   1 
ATOM   2536 C CA  . THR B 1 85  ? 4.415   15.839  -40.181 1.00 19.19 ? 65  THR B CA  1 
ATOM   2537 C C   . THR B 1 85  ? 5.623   14.898  -40.223 1.00 19.05 ? 65  THR B C   1 
ATOM   2538 O O   . THR B 1 85  ? 5.677   14.061  -41.166 1.00 19.24 ? 65  THR B O   1 
ATOM   2539 C CB  . THR B 1 85  ? 3.117   15.028  -40.064 1.00 19.78 ? 65  THR B CB  1 
ATOM   2540 O OG1 . THR B 1 85  ? 1.943   15.840  -40.143 1.00 20.77 ? 65  THR B OG1 1 
ATOM   2541 C CG2 . THR B 1 85  ? 3.063   14.252  -38.771 1.00 18.20 ? 65  THR B CG2 1 
ATOM   2542 N N   . ILE B 1 86  ? 6.561   15.038  -39.271 1.00 19.52 ? 66  ILE B N   1 
ATOM   2543 C CA  . ILE B 1 86  ? 7.851   14.275  -39.230 1.00 18.60 ? 66  ILE B CA  1 
ATOM   2544 C C   . ILE B 1 86  ? 7.818   13.292  -38.057 1.00 18.04 ? 66  ILE B C   1 
ATOM   2545 O O   . ILE B 1 86  ? 7.829   13.763  -36.884 1.00 16.24 ? 66  ILE B O   1 
ATOM   2546 C CB  . ILE B 1 86  ? 9.078   15.193  -39.107 1.00 20.48 ? 66  ILE B CB  1 
ATOM   2547 C CG1 . ILE B 1 86  ? 8.971   16.456  -39.963 1.00 20.65 ? 66  ILE B CG1 1 
ATOM   2548 C CG2 . ILE B 1 86  ? 10.352  14.400  -39.398 1.00 20.00 ? 66  ILE B CG2 1 
ATOM   2549 C CD1 . ILE B 1 86  ? 8.652   16.196  -41.395 1.00 21.25 ? 66  ILE B CD1 1 
ATOM   2550 N N   . VAL B 1 87  ? 7.738   11.991  -38.356 1.00 16.53 ? 67  VAL B N   1 
ATOM   2551 C CA  . VAL B 1 87  ? 7.830   10.899  -37.347 1.00 15.19 ? 67  VAL B CA  1 
ATOM   2552 C C   . VAL B 1 87  ? 9.300   10.479  -37.252 1.00 16.38 ? 67  VAL B C   1 
ATOM   2553 O O   . VAL B 1 87  ? 9.943   10.303  -38.330 1.00 15.45 ? 67  VAL B O   1 
ATOM   2554 C CB  . VAL B 1 87  ? 6.943   9.697   -37.683 1.00 14.45 ? 67  VAL B CB  1 
ATOM   2555 C CG1 . VAL B 1 87  ? 7.018   8.671   -36.564 1.00 14.31 ? 67  VAL B CG1 1 
ATOM   2556 C CG2 . VAL B 1 87  ? 5.508   10.117  -37.961 1.00 14.14 ? 67  VAL B CG2 1 
ATOM   2557 N N   . ILE B 1 88  ? 9.815   10.384  -36.027 1.00 15.32 ? 68  ILE B N   1 
ATOM   2558 C CA  . ILE B 1 88  ? 11.236  10.016  -35.735 1.00 16.10 ? 68  ILE B CA  1 
ATOM   2559 C C   . ILE B 1 88  ? 11.250  8.804   -34.795 1.00 15.51 ? 68  ILE B C   1 
ATOM   2560 O O   . ILE B 1 88  ? 10.554  8.822   -33.763 1.00 14.11 ? 68  ILE B O   1 
ATOM   2561 C CB  . ILE B 1 88  ? 12.042  11.191  -35.164 1.00 16.54 ? 68  ILE B CB  1 
ATOM   2562 C CG1 . ILE B 1 88  ? 11.748  12.498  -35.904 1.00 16.41 ? 68  ILE B CG1 1 
ATOM   2563 C CG2 . ILE B 1 88  ? 13.534  10.861  -35.181 1.00 17.22 ? 68  ILE B CG2 1 
ATOM   2564 C CD1 . ILE B 1 88  ? 12.534  13.675  -35.429 1.00 16.61 ? 68  ILE B CD1 1 
ATOM   2565 N N   . CYS B 1 89  ? 11.987  7.766   -35.178 1.00 14.41 ? 69  CYS B N   1 
ATOM   2566 C CA  . CYS B 1 89  ? 12.173  6.547   -34.360 1.00 14.88 ? 69  CYS B CA  1 
ATOM   2567 C C   . CYS B 1 89  ? 13.575  5.991   -34.617 1.00 15.74 ? 69  CYS B C   1 
ATOM   2568 O O   . CYS B 1 89  ? 13.745  5.149   -35.543 1.00 13.84 ? 69  CYS B O   1 
ATOM   2569 C CB  . CYS B 1 89  ? 11.117  5.501   -34.638 1.00 14.61 ? 69  CYS B CB  1 
ATOM   2570 S SG  . CYS B 1 89  ? 11.143  4.190   -33.390 1.00 15.58 ? 69  CYS B SG  1 
ATOM   2571 N N   . LEU B 1 90  ? 14.528  6.512   -33.838 1.00 16.48 ? 70  LEU B N   1 
ATOM   2572 C CA  . LEU B 1 90  ? 15.988  6.232   -33.920 1.00 17.35 ? 70  LEU B CA  1 
ATOM   2573 C C   . LEU B 1 90  ? 16.449  5.536   -32.625 1.00 17.94 ? 70  LEU B C   1 
ATOM   2574 O O   . LEU B 1 90  ? 15.604  5.409   -31.696 1.00 18.10 ? 70  LEU B O   1 
ATOM   2575 C CB  . LEU B 1 90  ? 16.676  7.584   -34.159 1.00 16.52 ? 70  LEU B CB  1 
ATOM   2576 C CG  . LEU B 1 90  ? 16.402  8.212   -35.526 1.00 16.28 ? 70  LEU B CG  1 
ATOM   2577 C CD1 . LEU B 1 90  ? 16.848  9.669   -35.576 1.00 16.49 ? 70  LEU B CD1 1 
ATOM   2578 C CD2 . LEU B 1 90  ? 17.103  7.409   -36.624 1.00 17.44 ? 70  LEU B CD2 1 
ATOM   2579 N N   . LEU B 1 91  ? 17.734  5.134   -32.535 1.00 18.45 ? 71  LEU B N   1 
ATOM   2580 C CA  . LEU B 1 91  ? 18.275  4.302   -31.413 1.00 19.18 ? 71  LEU B CA  1 
ATOM   2581 C C   . LEU B 1 91  ? 18.102  5.020   -30.073 1.00 17.33 ? 71  LEU B C   1 
ATOM   2582 O O   . LEU B 1 91  ? 17.762  4.356   -29.078 1.00 18.72 ? 71  LEU B O   1 
ATOM   2583 C CB  . LEU B 1 91  ? 19.763  4.000   -31.643 1.00 21.53 ? 71  LEU B CB  1 
ATOM   2584 C CG  . LEU B 1 91  ? 20.427  3.096   -30.600 1.00 22.80 ? 71  LEU B CG  1 
ATOM   2585 C CD1 . LEU B 1 91  ? 19.857  1.683   -30.659 1.00 23.94 ? 71  LEU B CD1 1 
ATOM   2586 C CD2 . LEU B 1 91  ? 21.941  3.058   -30.778 1.00 22.88 ? 71  LEU B CD2 1 
ATOM   2587 N N   . ASN B 1 92  ? 18.402  6.310   -30.042 1.00 16.16 ? 72  ASN B N   1 
ATOM   2588 C CA  . ASN B 1 92  ? 18.425  7.144   -28.818 1.00 16.95 ? 72  ASN B CA  1 
ATOM   2589 C C   . ASN B 1 92  ? 18.305  8.610   -29.235 1.00 16.77 ? 72  ASN B C   1 
ATOM   2590 O O   . ASN B 1 92  ? 18.470  8.902   -30.431 1.00 15.58 ? 72  ASN B O   1 
ATOM   2591 C CB  . ASN B 1 92  ? 19.707  6.950   -27.991 1.00 17.35 ? 72  ASN B CB  1 
ATOM   2592 C CG  . ASN B 1 92  ? 20.978  7.315   -28.738 1.00 16.84 ? 72  ASN B CG  1 
ATOM   2593 O OD1 . ASN B 1 92  ? 21.183  8.463   -29.116 1.00 17.51 ? 72  ASN B OD1 1 
ATOM   2594 N ND2 . ASN B 1 92  ? 21.849  6.348   -28.956 1.00 18.03 ? 72  ASN B ND2 1 
ATOM   2595 N N   . GLN B 1 93  ? 18.094  9.485   -28.258 1.00 17.40 ? 73  GLN B N   1 
ATOM   2596 C CA  . GLN B 1 93  ? 17.870  10.932  -28.468 1.00 19.21 ? 73  GLN B CA  1 
ATOM   2597 C C   . GLN B 1 93  ? 19.188  11.606  -28.852 1.00 21.09 ? 73  GLN B C   1 
ATOM   2598 O O   . GLN B 1 93  ? 19.142  12.701  -29.384 1.00 20.46 ? 73  GLN B O   1 
ATOM   2599 C CB  . GLN B 1 93  ? 17.309  11.566  -27.196 1.00 18.88 ? 73  GLN B CB  1 
ATOM   2600 C CG  . GLN B 1 93  ? 15.919  11.060  -26.853 1.00 17.31 ? 73  GLN B CG  1 
ATOM   2601 C CD  . GLN B 1 93  ? 14.852  11.874  -27.531 1.00 16.42 ? 73  GLN B CD  1 
ATOM   2602 O OE1 . GLN B 1 93  ? 13.924  12.343  -26.880 1.00 16.16 ? 73  GLN B OE1 1 
ATOM   2603 N NE2 . GLN B 1 93  ? 14.989  12.055  -28.835 1.00 13.27 ? 73  GLN B NE2 1 
ATOM   2604 N N   . ASP B 1 94  ? 20.327  10.988  -28.559 1.00 23.91 ? 74  ASP B N   1 
ATOM   2605 C CA  . ASP B 1 94  ? 21.622  11.539  -29.023 1.00 26.52 ? 74  ASP B CA  1 
ATOM   2606 C C   . ASP B 1 94  ? 21.659  11.473  -30.552 1.00 26.47 ? 74  ASP B C   1 
ATOM   2607 O O   . ASP B 1 94  ? 21.970  12.479  -31.192 1.00 25.24 ? 74  ASP B O   1 
ATOM   2608 C CB  . ASP B 1 94  ? 22.799  10.803  -28.392 1.00 31.10 ? 74  ASP B CB  1 
ATOM   2609 C CG  . ASP B 1 94  ? 23.700  11.809  -27.715 1.00 37.33 ? 74  ASP B CG  1 
ATOM   2610 O OD1 . ASP B 1 94  ? 23.309  12.288  -26.620 1.00 34.47 ? 74  ASP B OD1 1 
ATOM   2611 O OD2 . ASP B 1 94  ? 24.729  12.168  -28.336 1.00 42.83 ? 74  ASP B OD2 1 
ATOM   2612 N N   . VAL B 1 95  ? 21.295  10.323  -31.107 1.00 23.83 ? 75  VAL B N   1 
ATOM   2613 C CA  . VAL B 1 95  ? 21.228  10.099  -32.579 1.00 25.38 ? 75  VAL B CA  1 
ATOM   2614 C C   . VAL B 1 95  ? 20.211  11.073  -33.184 1.00 25.44 ? 75  VAL B C   1 
ATOM   2615 O O   . VAL B 1 95  ? 20.507  11.621  -34.276 1.00 27.80 ? 75  VAL B O   1 
ATOM   2616 C CB  . VAL B 1 95  ? 20.918  8.619   -32.876 1.00 22.41 ? 75  VAL B CB  1 
ATOM   2617 C CG1 . VAL B 1 95  ? 20.565  8.374   -34.340 1.00 22.27 ? 75  VAL B CG1 1 
ATOM   2618 C CG2 . VAL B 1 95  ? 22.088  7.757   -32.436 1.00 22.03 ? 75  VAL B CG2 1 
ATOM   2619 N N   . VAL B 1 96  ? 19.084  11.310  -32.495 1.00 24.17 ? 76  VAL B N   1 
ATOM   2620 C CA  . VAL B 1 96  ? 18.002  12.222  -32.976 1.00 22.41 ? 76  VAL B CA  1 
ATOM   2621 C C   . VAL B 1 96  ? 18.600  13.623  -33.165 1.00 25.20 ? 76  VAL B C   1 
ATOM   2622 O O   . VAL B 1 96  ? 18.376  14.221  -34.243 1.00 23.57 ? 76  VAL B O   1 
ATOM   2623 C CB  . VAL B 1 96  ? 16.772  12.251  -32.045 1.00 21.32 ? 76  VAL B CB  1 
ATOM   2624 C CG1 . VAL B 1 96  ? 15.770  13.302  -32.508 1.00 22.13 ? 76  VAL B CG1 1 
ATOM   2625 C CG2 . VAL B 1 96  ? 16.090  10.891  -31.966 1.00 20.69 ? 76  VAL B CG2 1 
ATOM   2626 N N   . GLN B 1 97  ? 19.347  14.115  -32.172 1.00 25.15 ? 77  GLN B N   1 
ATOM   2627 C CA  . GLN B 1 97  ? 19.984  15.456  -32.213 1.00 29.92 ? 77  GLN B CA  1 
ATOM   2628 C C   . GLN B 1 97  ? 21.010  15.518  -33.359 1.00 28.97 ? 77  GLN B C   1 
ATOM   2629 O O   . GLN B 1 97  ? 21.110  16.579  -33.981 1.00 26.92 ? 77  GLN B O   1 
ATOM   2630 C CB  . GLN B 1 97  ? 20.637  15.797  -30.868 1.00 34.95 ? 77  GLN B CB  1 
ATOM   2631 C CG  . GLN B 1 97  ? 19.728  15.561  -29.668 1.00 38.30 ? 77  GLN B CG  1 
ATOM   2632 C CD  . GLN B 1 97  ? 19.839  16.640  -28.620 1.00 44.02 ? 77  GLN B CD  1 
ATOM   2633 O OE1 . GLN B 1 97  ? 20.872  16.803  -27.970 1.00 48.38 ? 77  GLN B OE1 1 
ATOM   2634 N NE2 . GLN B 1 97  ? 18.753  17.374  -28.430 1.00 43.89 ? 77  GLN B NE2 1 
ATOM   2635 N N   . GLN B 1 98  ? 21.733  14.430  -33.633 1.00 29.28 ? 78  GLN B N   1 
ATOM   2636 C CA  . GLN B 1 98  ? 22.807  14.387  -34.671 1.00 31.36 ? 78  GLN B CA  1 
ATOM   2637 C C   . GLN B 1 98  ? 22.155  14.396  -36.052 1.00 32.29 ? 78  GLN B C   1 
ATOM   2638 O O   . GLN B 1 98  ? 22.632  15.126  -36.950 1.00 30.51 ? 78  GLN B O   1 
ATOM   2639 C CB  . GLN B 1 98  ? 23.726  13.182  -34.470 1.00 31.32 ? 78  GLN B CB  1 
ATOM   2640 C CG  . GLN B 1 98  ? 24.760  13.427  -33.370 1.00 32.52 ? 78  GLN B CG  1 
ATOM   2641 C CD  . GLN B 1 98  ? 25.272  12.205  -32.644 1.00 33.34 ? 78  GLN B CD  1 
ATOM   2642 O OE1 . GLN B 1 98  ? 25.087  11.069  -33.055 1.00 31.67 ? 78  GLN B OE1 1 
ATOM   2643 N NE2 . GLN B 1 98  ? 25.950  12.440  -31.528 1.00 46.12 ? 78  GLN B NE2 1 
ATOM   2644 N N   . THR B 1 99  ? 21.066  13.651  -36.200 1.00 31.44 ? 79  THR B N   1 
ATOM   2645 C CA  . THR B 1 99  ? 20.275  13.613  -37.449 1.00 29.51 ? 79  THR B CA  1 
ATOM   2646 C C   . THR B 1 99  ? 19.652  14.987  -37.706 1.00 29.54 ? 79  THR B C   1 
ATOM   2647 O O   . THR B 1 99  ? 19.696  15.426  -38.854 1.00 30.92 ? 79  THR B O   1 
ATOM   2648 C CB  . THR B 1 99  ? 19.241  12.492  -37.391 1.00 30.72 ? 79  THR B CB  1 
ATOM   2649 O OG1 . THR B 1 99  ? 19.959  11.289  -37.119 1.00 29.02 ? 79  THR B OG1 1 
ATOM   2650 C CG2 . THR B 1 99  ? 18.443  12.383  -38.670 1.00 31.87 ? 79  THR B CG2 1 
ATOM   2651 N N   . LEU B 1 100 ? 19.107  15.655  -36.690 1.00 28.78 ? 80  LEU B N   1 
ATOM   2652 C CA  . LEU B 1 100 ? 18.467  16.997  -36.855 1.00 32.45 ? 80  LEU B CA  1 
ATOM   2653 C C   . LEU B 1 100 ? 19.516  18.108  -37.007 1.00 36.38 ? 80  LEU B C   1 
ATOM   2654 O O   . LEU B 1 100 ? 19.112  19.268  -37.234 1.00 34.46 ? 80  LEU B O   1 
ATOM   2655 C CB  . LEU B 1 100 ? 17.569  17.286  -35.644 1.00 33.73 ? 80  LEU B CB  1 
ATOM   2656 C CG  . LEU B 1 100 ? 16.079  16.956  -35.790 1.00 34.98 ? 80  LEU B CG  1 
ATOM   2657 C CD1 . LEU B 1 100 ? 15.791  16.057  -36.984 1.00 34.92 ? 80  LEU B CD1 1 
ATOM   2658 C CD2 . LEU B 1 100 ? 15.532  16.343  -34.504 1.00 36.48 ? 80  LEU B CD2 1 
ATOM   2659 N N   . ASP B 1 101 ? 20.806  17.789  -36.868 1.00 40.21 ? 81  ASP B N   1 
ATOM   2660 C CA  . ASP B 1 101 ? 21.889  18.797  -36.738 1.00 44.86 ? 81  ASP B CA  1 
ATOM   2661 C C   . ASP B 1 101 ? 21.787  19.811  -37.883 1.00 47.62 ? 81  ASP B C   1 
ATOM   2662 O O   . ASP B 1 101 ? 21.583  21.003  -37.587 1.00 46.40 ? 81  ASP B O   1 
ATOM   2663 C CB  . ASP B 1 101 ? 23.268  18.140  -36.694 1.00 46.74 ? 81  ASP B CB  1 
ATOM   2664 C CG  . ASP B 1 101 ? 24.254  18.860  -35.793 1.00 52.82 ? 81  ASP B CG  1 
ATOM   2665 O OD1 . ASP B 1 101 ? 23.793  19.572  -34.861 1.00 54.03 ? 81  ASP B OD1 1 
ATOM   2666 O OD2 . ASP B 1 101 ? 25.477  18.703  -36.029 1.00 56.33 ? 81  ASP B OD2 1 
ATOM   2667 N N   . GLU B 1 102 ? 21.892  19.341  -39.131 1.00 50.99 ? 82  GLU B N   1 
ATOM   2668 C CA  . GLU B 1 102 ? 21.898  20.193  -40.349 1.00 51.80 ? 82  GLU B CA  1 
ATOM   2669 C C   . GLU B 1 102 ? 20.474  20.643  -40.696 1.00 49.81 ? 82  GLU B C   1 
ATOM   2670 O O   . GLU B 1 102 ? 20.354  21.670  -41.384 1.00 53.37 ? 82  GLU B O   1 
ATOM   2671 C CB  . GLU B 1 102 ? 22.519  19.462  -41.540 1.00 54.18 ? 82  GLU B CB  1 
ATOM   2672 C CG  . GLU B 1 102 ? 24.018  19.660  -41.664 1.00 55.81 ? 82  GLU B CG  1 
ATOM   2673 C CD  . GLU B 1 102 ? 24.625  18.947  -42.862 1.00 56.21 ? 82  GLU B CD  1 
ATOM   2674 O OE1 . GLU B 1 102 ? 24.225  19.254  -44.002 1.00 55.79 ? 82  GLU B OE1 1 
ATOM   2675 O OE2 . GLU B 1 102 ? 25.471  18.062  -42.651 1.00 60.64 ? 82  GLU B OE2 1 
ATOM   2676 N N   . VAL B 1 103 ? 19.437  19.925  -40.252 1.00 44.21 ? 83  VAL B N   1 
ATOM   2677 C CA  . VAL B 1 103 ? 18.025  20.304  -40.560 1.00 43.39 ? 83  VAL B CA  1 
ATOM   2678 C C   . VAL B 1 103 ? 17.728  21.647  -39.880 1.00 41.15 ? 83  VAL B C   1 
ATOM   2679 O O   . VAL B 1 103 ? 17.333  21.636  -38.702 1.00 39.41 ? 83  VAL B O   1 
ATOM   2680 C CB  . VAL B 1 103 ? 17.016  19.222  -40.132 1.00 41.67 ? 83  VAL B CB  1 
ATOM   2681 C CG1 . VAL B 1 103 ? 15.612  19.621  -40.525 1.00 41.78 ? 83  VAL B CG1 1 
ATOM   2682 C CG2 . VAL B 1 103 ? 17.351  17.854  -40.700 1.00 41.15 ? 83  VAL B CG2 1 
ATOM   2683 N N   . ILE B 1 104 ? 17.885  22.756  -40.608 1.00 44.52 ? 84  ILE B N   1 
ATOM   2684 C CA  . ILE B 1 104 ? 17.852  24.143  -40.043 1.00 47.14 ? 84  ILE B CA  1 
ATOM   2685 C C   . ILE B 1 104 ? 16.431  24.724  -40.113 1.00 44.03 ? 84  ILE B C   1 
ATOM   2686 O O   . ILE B 1 104 ? 16.123  25.566  -39.256 1.00 44.66 ? 84  ILE B O   1 
ATOM   2687 C CB  . ILE B 1 104 ? 18.901  25.077  -40.699 1.00 52.53 ? 84  ILE B CB  1 
ATOM   2688 C CG1 . ILE B 1 104 ? 18.953  24.981  -42.231 1.00 55.81 ? 84  ILE B CG1 1 
ATOM   2689 C CG2 . ILE B 1 104 ? 20.276  24.842  -40.086 1.00 52.57 ? 84  ILE B CG2 1 
ATOM   2690 C CD1 . ILE B 1 104 ? 17.782  25.625  -42.953 1.00 55.32 ? 84  ILE B CD1 1 
ATOM   2691 N N   . ASP B 1 105 ? 15.593  24.277  -41.056 1.00 43.41 ? 85  ASP B N   1 
ATOM   2692 C CA  . ASP B 1 105 ? 14.257  24.875  -41.342 1.00 42.90 ? 85  ASP B CA  1 
ATOM   2693 C C   . ASP B 1 105 ? 13.111  23.912  -40.981 1.00 39.31 ? 85  ASP B C   1 
ATOM   2694 O O   . ASP B 1 105 ? 12.755  23.044  -41.804 1.00 36.09 ? 85  ASP B O   1 
ATOM   2695 C CB  . ASP B 1 105 ? 14.150  25.288  -42.813 1.00 42.86 ? 85  ASP B CB  1 
ATOM   2696 C CG  . ASP B 1 105 ? 12.841  25.981  -43.149 1.00 45.07 ? 85  ASP B CG  1 
ATOM   2697 O OD1 . ASP B 1 105 ? 12.302  26.673  -42.255 1.00 46.55 ? 85  ASP B OD1 1 
ATOM   2698 O OD2 . ASP B 1 105 ? 12.378  25.836  -44.308 1.00 46.43 ? 85  ASP B OD2 1 
ATOM   2699 N N   . LEU B 1 106 ? 12.480  24.108  -39.824 1.00 35.47 ? 86  LEU B N   1 
ATOM   2700 C CA  . LEU B 1 106 ? 11.354  23.245  -39.386 1.00 32.90 ? 86  LEU B CA  1 
ATOM   2701 C C   . LEU B 1 106 ? 10.050  24.050  -39.343 1.00 30.21 ? 86  LEU B C   1 
ATOM   2702 O O   . LEU B 1 106 ? 9.031   23.492  -38.905 1.00 28.49 ? 86  LEU B O   1 
ATOM   2703 C CB  . LEU B 1 106 ? 11.719  22.626  -38.035 1.00 31.63 ? 86  LEU B CB  1 
ATOM   2704 C CG  . LEU B 1 106 ? 12.825  21.571  -38.101 1.00 34.51 ? 86  LEU B CG  1 
ATOM   2705 C CD1 . LEU B 1 106 ? 13.330  21.185  -36.714 1.00 35.01 ? 86  LEU B CD1 1 
ATOM   2706 C CD2 . LEU B 1 106 ? 12.345  20.338  -38.843 1.00 34.13 ? 86  LEU B CD2 1 
ATOM   2707 N N   . SER B 1 107 ? 10.071  25.318  -39.768 1.00 29.68 ? 87  SER B N   1 
ATOM   2708 C CA  . SER B 1 107 ? 8.860   26.171  -39.858 1.00 29.04 ? 87  SER B CA  1 
ATOM   2709 C C   . SER B 1 107 ? 7.721   25.348  -40.477 1.00 27.46 ? 87  SER B C   1 
ATOM   2710 O O   . SER B 1 107 ? 7.947   24.693  -41.504 1.00 28.57 ? 87  SER B O   1 
ATOM   2711 C CB  . SER B 1 107 ? 9.122   27.447  -40.627 1.00 30.53 ? 87  SER B CB  1 
ATOM   2712 O OG  . SER B 1 107 ? 9.662   27.167  -41.910 1.00 34.33 ? 87  SER B OG  1 
ATOM   2713 N N   . GLY B 1 108 ? 6.560   25.345  -39.835 1.00 26.61 ? 88  GLY B N   1 
ATOM   2714 C CA  . GLY B 1 108 ? 5.342   24.668  -40.313 1.00 27.59 ? 88  GLY B CA  1 
ATOM   2715 C C   . GLY B 1 108 ? 5.331   23.183  -39.968 1.00 28.24 ? 88  GLY B C   1 
ATOM   2716 O O   . GLY B 1 108 ? 4.297   22.524  -40.243 1.00 29.86 ? 88  GLY B O   1 
ATOM   2717 N N   . LYS B 1 109 ? 6.417   22.645  -39.395 1.00 25.43 ? 89  LYS B N   1 
ATOM   2718 C CA  . LYS B 1 109 ? 6.570   21.171  -39.239 1.00 25.70 ? 89  LYS B CA  1 
ATOM   2719 C C   . LYS B 1 109 ? 6.092   20.749  -37.848 1.00 24.04 ? 89  LYS B C   1 
ATOM   2720 O O   . LYS B 1 109 ? 6.425   21.413  -36.875 1.00 25.72 ? 89  LYS B O   1 
ATOM   2721 C CB  . LYS B 1 109 ? 8.013   20.707  -39.449 1.00 25.52 ? 89  LYS B CB  1 
ATOM   2722 C CG  . LYS B 1 109 ? 8.671   21.150  -40.751 1.00 26.27 ? 89  LYS B CG  1 
ATOM   2723 C CD  . LYS B 1 109 ? 8.267   20.373  -41.971 1.00 24.49 ? 89  LYS B CD  1 
ATOM   2724 C CE  . LYS B 1 109 ? 8.959   20.889  -43.215 1.00 24.77 ? 89  LYS B CE  1 
ATOM   2725 N NZ  . LYS B 1 109 ? 8.142   20.644  -44.421 1.00 25.31 ? 89  LYS B NZ  1 
ATOM   2726 N N   . THR B 1 110 ? 5.342   19.655  -37.779 1.00 23.52 ? 90  THR B N   1 
ATOM   2727 C CA  . THR B 1 110 ? 4.985   18.952  -36.528 1.00 21.18 ? 90  THR B CA  1 
ATOM   2728 C C   . THR B 1 110 ? 5.897   17.739  -36.412 1.00 21.57 ? 90  THR B C   1 
ATOM   2729 O O   . THR B 1 110 ? 5.904   16.891  -37.360 1.00 20.34 ? 90  THR B O   1 
ATOM   2730 C CB  . THR B 1 110 ? 3.513   18.560  -36.519 1.00 22.68 ? 90  THR B CB  1 
ATOM   2731 O OG1 . THR B 1 110 ? 2.825   19.812  -36.542 1.00 22.25 ? 90  THR B OG1 1 
ATOM   2732 C CG2 . THR B 1 110 ? 3.145   17.692  -35.334 1.00 23.92 ? 90  THR B CG2 1 
ATOM   2733 N N   . ILE B 1 111 ? 6.650   17.683  -35.314 1.00 19.60 ? 91  ILE B N   1 
ATOM   2734 C CA  . ILE B 1 111 ? 7.581   16.564  -35.016 1.00 20.14 ? 91  ILE B CA  1 
ATOM   2735 C C   . ILE B 1 111 ? 6.890   15.623  -34.036 1.00 18.40 ? 91  ILE B C   1 
ATOM   2736 O O   . ILE B 1 111 ? 6.461   16.100  -32.949 1.00 18.06 ? 91  ILE B O   1 
ATOM   2737 C CB  . ILE B 1 111 ? 8.908   17.097  -34.451 1.00 20.53 ? 91  ILE B CB  1 
ATOM   2738 C CG1 . ILE B 1 111 ? 9.464   18.236  -35.314 1.00 21.80 ? 91  ILE B CG1 1 
ATOM   2739 C CG2 . ILE B 1 111 ? 9.878   15.948  -34.263 1.00 21.07 ? 91  ILE B CG2 1 
ATOM   2740 C CD1 . ILE B 1 111 ? 9.814   17.837  -36.747 1.00 22.15 ? 91  ILE B CD1 1 
ATOM   2741 N N   . ILE B 1 112 ? 6.798   14.345  -34.411 1.00 16.18 ? 92  ILE B N   1 
ATOM   2742 C CA  . ILE B 1 112 ? 6.313   13.241  -33.543 1.00 15.68 ? 92  ILE B CA  1 
ATOM   2743 C C   . ILE B 1 112 ? 7.507   12.338  -33.239 1.00 15.86 ? 92  ILE B C   1 
ATOM   2744 O O   . ILE B 1 112 ? 7.901   11.551  -34.131 1.00 15.07 ? 92  ILE B O   1 
ATOM   2745 C CB  . ILE B 1 112 ? 5.154   12.471  -34.211 1.00 15.97 ? 92  ILE B CB  1 
ATOM   2746 C CG1 . ILE B 1 112 ? 4.049   13.403  -34.739 1.00 16.28 ? 92  ILE B CG1 1 
ATOM   2747 C CG2 . ILE B 1 112 ? 4.616   11.442  -33.245 1.00 16.53 ? 92  ILE B CG2 1 
ATOM   2748 C CD1 . ILE B 1 112 ? 2.837   12.690  -35.327 1.00 15.43 ? 92  ILE B CD1 1 
ATOM   2749 N N   . ASN B 1 113 ? 8.076   12.471  -32.043 1.00 14.86 ? 93  ASN B N   1 
ATOM   2750 C CA  . ASN B 1 113 ? 9.301   11.736  -31.653 1.00 14.76 ? 93  ASN B CA  1 
ATOM   2751 C C   . ASN B 1 113 ? 8.898   10.481  -30.885 1.00 13.95 ? 93  ASN B C   1 
ATOM   2752 O O   . ASN B 1 113 ? 8.436   10.615  -29.753 1.00 13.76 ? 93  ASN B O   1 
ATOM   2753 C CB  . ASN B 1 113 ? 10.270  12.612  -30.861 1.00 14.44 ? 93  ASN B CB  1 
ATOM   2754 C CG  . ASN B 1 113 ? 11.642  11.981  -30.774 1.00 15.39 ? 93  ASN B CG  1 
ATOM   2755 O OD1 . ASN B 1 113 ? 11.874  10.902  -31.342 1.00 16.35 ? 93  ASN B OD1 1 
ATOM   2756 N ND2 . ASN B 1 113 ? 12.539  12.611  -30.028 1.00 14.25 ? 93  ASN B ND2 1 
ATOM   2757 N N   . LEU B 1 114 ? 9.058   9.306   -31.493 1.00 13.99 ? 94  LEU B N   1 
ATOM   2758 C CA  . LEU B 1 114 ? 8.805   8.010   -30.813 1.00 14.68 ? 94  LEU B CA  1 
ATOM   2759 C C   . LEU B 1 114 ? 10.123  7.314   -30.430 1.00 15.10 ? 94  LEU B C   1 
ATOM   2760 O O   . LEU B 1 114 ? 10.066  6.106   -30.097 1.00 15.39 ? 94  LEU B O   1 
ATOM   2761 C CB  . LEU B 1 114 ? 7.953   7.142   -31.727 1.00 15.19 ? 94  LEU B CB  1 
ATOM   2762 C CG  . LEU B 1 114 ? 6.704   7.828   -32.264 1.00 15.77 ? 94  LEU B CG  1 
ATOM   2763 C CD1 . LEU B 1 114 ? 6.020   6.935   -33.277 1.00 16.00 ? 94  LEU B CD1 1 
ATOM   2764 C CD2 . LEU B 1 114 ? 5.748   8.199   -31.139 1.00 15.71 ? 94  LEU B CD2 1 
ATOM   2765 N N   . THR B 1 115 ? 11.242  8.056   -30.401 1.00 15.06 ? 95  THR B N   1 
ATOM   2766 C CA  . THR B 1 115 ? 12.556  7.624   -29.845 1.00 15.08 ? 95  THR B CA  1 
ATOM   2767 C C   . THR B 1 115 ? 12.509  7.655   -28.306 1.00 15.47 ? 95  THR B C   1 
ATOM   2768 O O   . THR B 1 115 ? 12.269  8.745   -27.720 1.00 14.91 ? 95  THR B O   1 
ATOM   2769 C CB  . THR B 1 115 ? 13.679  8.546   -30.319 1.00 14.85 ? 95  THR B CB  1 
ATOM   2770 O OG1 . THR B 1 115 ? 13.559  8.689   -31.741 1.00 14.49 ? 95  THR B OG1 1 
ATOM   2771 C CG2 . THR B 1 115 ? 15.052  8.054   -29.908 1.00 14.63 ? 95  THR B CG2 1 
ATOM   2772 N N   . ASN B 1 116 ? 12.721  6.516   -27.657 1.00 14.87 ? 96  ASN B N   1 
ATOM   2773 C CA  . ASN B 1 116 ? 12.767  6.421   -26.174 1.00 15.73 ? 96  ASN B CA  1 
ATOM   2774 C C   . ASN B 1 116 ? 13.985  7.184   -25.650 1.00 16.59 ? 96  ASN B C   1 
ATOM   2775 O O   . ASN B 1 116 ? 15.023  7.224   -26.346 1.00 16.38 ? 96  ASN B O   1 
ATOM   2776 C CB  . ASN B 1 116 ? 12.782  4.975   -25.671 1.00 15.78 ? 96  ASN B CB  1 
ATOM   2777 C CG  . ASN B 1 116 ? 11.434  4.326   -25.869 1.00 15.72 ? 96  ASN B CG  1 
ATOM   2778 O OD1 . ASN B 1 116 ? 10.560  4.925   -26.501 1.00 16.93 ? 96  ASN B OD1 1 
ATOM   2779 N ND2 . ASN B 1 116 ? 11.251  3.132   -25.324 1.00 14.37 ? 96  ASN B ND2 1 
ATOM   2780 N N   . GLY B 1 117 ? 13.827  7.789   -24.472 1.00 16.18 ? 97  GLY B N   1 
ATOM   2781 C CA  . GLY B 1 117 ? 14.923  8.441   -23.745 1.00 16.35 ? 97  GLY B CA  1 
ATOM   2782 C C   . GLY B 1 117 ? 14.443  9.016   -22.429 1.00 15.86 ? 97  GLY B C   1 
ATOM   2783 O O   . GLY B 1 117 ? 13.422  8.541   -21.898 1.00 17.56 ? 97  GLY B O   1 
ATOM   2784 N N   . THR B 1 118 ? 15.180  9.980   -21.895 1.00 15.87 ? 98  THR B N   1 
ATOM   2785 C CA  . THR B 1 118 ? 14.895  10.589  -20.578 1.00 16.38 ? 98  THR B CA  1 
ATOM   2786 C C   . THR B 1 118 ? 13.981  11.803  -20.753 1.00 15.48 ? 98  THR B C   1 
ATOM   2787 O O   . THR B 1 118 ? 13.908  12.388  -21.833 1.00 14.54 ? 98  THR B O   1 
ATOM   2788 C CB  . THR B 1 118 ? 16.203  10.901  -19.864 1.00 16.10 ? 98  THR B CB  1 
ATOM   2789 O OG1 . THR B 1 118 ? 16.697  12.101  -20.435 1.00 15.61 ? 98  THR B OG1 1 
ATOM   2790 C CG2 . THR B 1 118 ? 17.215  9.791   -19.992 1.00 16.84 ? 98  THR B CG2 1 
ATOM   2791 N N   . PRO B 1 119 ? 13.258  12.221  -19.697 1.00 15.09 ? 99  PRO B N   1 
ATOM   2792 C CA  . PRO B 1 119 ? 12.532  13.492  -19.719 1.00 15.67 ? 99  PRO B CA  1 
ATOM   2793 C C   . PRO B 1 119 ? 13.363  14.690  -20.225 1.00 15.68 ? 99  PRO B C   1 
ATOM   2794 O O   . PRO B 1 119 ? 12.885  15.431  -21.013 1.00 15.19 ? 99  PRO B O   1 
ATOM   2795 C CB  . PRO B 1 119 ? 12.145  13.659  -18.244 1.00 15.76 ? 99  PRO B CB  1 
ATOM   2796 C CG  . PRO B 1 119 ? 11.926  12.229  -17.789 1.00 16.08 ? 99  PRO B CG  1 
ATOM   2797 C CD  . PRO B 1 119 ? 13.106  11.512  -18.414 1.00 16.40 ? 99  PRO B CD  1 
ATOM   2798 N N   . GLN B 1 120 ? 14.584  14.875  -19.729 1.00 17.22 ? 100 GLN B N   1 
ATOM   2799 C CA  . GLN B 1 120 ? 15.409  16.074  -20.071 1.00 18.44 ? 100 GLN B CA  1 
ATOM   2800 C C   . GLN B 1 120 ? 15.958  15.948  -21.492 1.00 16.23 ? 100 GLN B C   1 
ATOM   2801 O O   . GLN B 1 120 ? 16.226  16.997  -22.121 1.00 15.26 ? 100 GLN B O   1 
ATOM   2802 C CB  . GLN B 1 120 ? 16.504  16.272  -19.026 1.00 19.49 ? 100 GLN B CB  1 
ATOM   2803 C CG  . GLN B 1 120 ? 15.938  16.647  -17.655 1.00 22.16 ? 100 GLN B CG  1 
ATOM   2804 C CD  . GLN B 1 120 ? 14.777  17.624  -17.691 1.00 23.39 ? 100 GLN B CD  1 
ATOM   2805 O OE1 . GLN B 1 120 ? 13.649  17.322  -17.264 1.00 23.35 ? 100 GLN B OE1 1 
ATOM   2806 N NE2 . GLN B 1 120 ? 15.037  18.800  -18.241 1.00 23.20 ? 100 GLN B NE2 1 
ATOM   2807 N N   . GLN B 1 121 ? 16.079  14.720  -21.996 1.00 15.29 ? 101 GLN B N   1 
ATOM   2808 C CA  . GLN B 1 121 ? 16.482  14.451  -23.401 1.00 15.80 ? 101 GLN B CA  1 
ATOM   2809 C C   . GLN B 1 121 ? 15.366  14.925  -24.322 1.00 15.08 ? 101 GLN B C   1 
ATOM   2810 O O   . GLN B 1 121 ? 15.658  15.619  -25.338 1.00 15.10 ? 101 GLN B O   1 
ATOM   2811 C CB  . GLN B 1 121 ? 16.770  12.971  -23.621 1.00 16.48 ? 101 GLN B CB  1 
ATOM   2812 C CG  . GLN B 1 121 ? 18.189  12.582  -23.270 1.00 18.42 ? 101 GLN B CG  1 
ATOM   2813 C CD  . GLN B 1 121 ? 18.419  11.091  -23.360 1.00 20.67 ? 101 GLN B CD  1 
ATOM   2814 O OE1 . GLN B 1 121 ? 17.498  10.270  -23.545 1.00 19.59 ? 101 GLN B OE1 1 
ATOM   2815 N NE2 . GLN B 1 121 ? 19.688  10.738  -23.266 1.00 23.42 ? 101 GLN B NE2 1 
ATOM   2816 N N   . ALA B 1 122 ? 14.122  14.606  -23.968 1.00 14.48 ? 102 ALA B N   1 
ATOM   2817 C CA  . ALA B 1 122 ? 12.933  15.080  -24.695 1.00 14.71 ? 102 ALA B CA  1 
ATOM   2818 C C   . ALA B 1 122 ? 12.928  16.616  -24.592 1.00 16.48 ? 102 ALA B C   1 
ATOM   2819 O O   . ALA B 1 122 ? 12.638  17.238  -25.608 1.00 16.05 ? 102 ALA B O   1 
ATOM   2820 C CB  . ALA B 1 122 ? 11.662  14.456  -24.155 1.00 13.71 ? 102 ALA B CB  1 
ATOM   2821 N N   . VAL B 1 123 ? 13.279  17.194  -23.436 1.00 17.03 ? 103 VAL B N   1 
ATOM   2822 C CA  . VAL B 1 123 ? 13.295  18.682  -23.254 1.00 18.60 ? 103 VAL B CA  1 
ATOM   2823 C C   . VAL B 1 123 ? 14.275  19.280  -24.265 1.00 20.07 ? 103 VAL B C   1 
ATOM   2824 O O   . VAL B 1 123 ? 13.874  20.217  -24.957 1.00 21.28 ? 103 VAL B O   1 
ATOM   2825 C CB  . VAL B 1 123 ? 13.621  19.152  -21.820 1.00 18.01 ? 103 VAL B CB  1 
ATOM   2826 C CG1 . VAL B 1 123 ? 14.034  20.628  -21.797 1.00 18.77 ? 103 VAL B CG1 1 
ATOM   2827 C CG2 . VAL B 1 123 ? 12.446  18.924  -20.874 1.00 17.92 ? 103 VAL B CG2 1 
ATOM   2828 N N   . LYS B 1 124 ? 15.494  18.724  -24.382 1.00 20.66 ? 104 LYS B N   1 
ATOM   2829 C CA  . LYS B 1 124 ? 16.568  19.324  -25.216 1.00 20.54 ? 104 LYS B CA  1 
ATOM   2830 C C   . LYS B 1 124 ? 16.143  19.228  -26.685 1.00 19.58 ? 104 LYS B C   1 
ATOM   2831 O O   . LYS B 1 124 ? 16.296  20.228  -27.389 1.00 19.86 ? 104 LYS B O   1 
ATOM   2832 C CB  . LYS B 1 124 ? 17.938  18.675  -24.976 1.00 20.45 ? 104 LYS B CB  1 
ATOM   2833 C CG  . LYS B 1 124 ? 18.504  18.852  -23.574 1.00 22.01 ? 104 LYS B CG  1 
ATOM   2834 C CD  . LYS B 1 124 ? 19.902  18.272  -23.446 1.00 23.37 ? 104 LYS B CD  1 
ATOM   2835 C CE  . LYS B 1 124 ? 20.541  18.465  -22.086 1.00 25.28 ? 104 LYS B CE  1 
ATOM   2836 N NZ  . LYS B 1 124 ? 19.644  18.080  -20.972 1.00 29.19 ? 104 LYS B NZ  1 
ATOM   2837 N N   . VAL B 1 125 ? 15.575  18.096  -27.113 1.00 18.78 ? 105 VAL B N   1 
ATOM   2838 C CA  . VAL B 1 125 ? 15.115  17.888  -28.525 1.00 18.48 ? 105 VAL B CA  1 
ATOM   2839 C C   . VAL B 1 125 ? 13.942  18.826  -28.839 1.00 17.10 ? 105 VAL B C   1 
ATOM   2840 O O   . VAL B 1 125 ? 13.964  19.472  -29.929 1.00 17.64 ? 105 VAL B O   1 
ATOM   2841 C CB  . VAL B 1 125 ? 14.726  16.428  -28.800 1.00 18.81 ? 105 VAL B CB  1 
ATOM   2842 C CG1 . VAL B 1 125 ? 14.057  16.276  -30.150 1.00 18.85 ? 105 VAL B CG1 1 
ATOM   2843 C CG2 . VAL B 1 125 ? 15.925  15.504  -28.688 1.00 19.79 ? 105 VAL B CG2 1 
ATOM   2844 N N   . ALA B 1 126 ? 12.954  18.915  -27.948 1.00 16.33 ? 106 ALA B N   1 
ATOM   2845 C CA  . ALA B 1 126 ? 11.794  19.817  -28.137 1.00 16.98 ? 106 ALA B CA  1 
ATOM   2846 C C   . ALA B 1 126 ? 12.277  21.270  -28.220 1.00 17.36 ? 106 ALA B C   1 
ATOM   2847 O O   . ALA B 1 126 ? 11.772  22.008  -29.071 1.00 18.87 ? 106 ALA B O   1 
ATOM   2848 C CB  . ALA B 1 126 ? 10.774  19.655  -27.053 1.00 16.96 ? 106 ALA B CB  1 
ATOM   2849 N N   . THR B 1 127 ? 13.216  21.687  -27.373 1.00 18.29 ? 107 THR B N   1 
ATOM   2850 C CA  . THR B 1 127 ? 13.715  23.082  -27.419 1.00 19.23 ? 107 THR B CA  1 
ATOM   2851 C C   . THR B 1 127 ? 14.439  23.302  -28.759 1.00 21.19 ? 107 THR B C   1 
ATOM   2852 O O   . THR B 1 127 ? 14.172  24.323  -29.394 1.00 21.58 ? 107 THR B O   1 
ATOM   2853 C CB  . THR B 1 127 ? 14.545  23.446  -26.187 1.00 18.28 ? 107 THR B CB  1 
ATOM   2854 O OG1 . THR B 1 127 ? 13.759  23.140  -25.034 1.00 15.91 ? 107 THR B OG1 1 
ATOM   2855 C CG2 . THR B 1 127 ? 14.935  24.913  -26.201 1.00 18.30 ? 107 THR B CG2 1 
ATOM   2856 N N   . LEU B 1 128 ? 15.302  22.376  -29.174 1.00 24.27 ? 108 LEU B N   1 
ATOM   2857 C CA  . LEU B 1 128 ? 16.092  22.463  -30.436 1.00 26.64 ? 108 LEU B CA  1 
ATOM   2858 C C   . LEU B 1 128 ? 15.145  22.660  -31.623 1.00 27.08 ? 108 LEU B C   1 
ATOM   2859 O O   . LEU B 1 128 ? 15.357  23.615  -32.372 1.00 28.21 ? 108 LEU B O   1 
ATOM   2860 C CB  . LEU B 1 128 ? 16.944  21.198  -30.611 1.00 29.82 ? 108 LEU B CB  1 
ATOM   2861 C CG  . LEU B 1 128 ? 17.748  21.121  -31.915 1.00 31.81 ? 108 LEU B CG  1 
ATOM   2862 C CD1 . LEU B 1 128 ? 18.899  22.111  -31.894 1.00 32.57 ? 108 LEU B CD1 1 
ATOM   2863 C CD2 . LEU B 1 128 ? 18.261  19.709  -32.167 1.00 32.55 ? 108 LEU B CD2 1 
ATOM   2864 N N   . VAL B 1 129 ? 14.113  21.824  -31.777 1.00 27.70 ? 109 VAL B N   1 
ATOM   2865 C CA  . VAL B 1 129 ? 13.224  21.879  -32.981 1.00 26.47 ? 109 VAL B CA  1 
ATOM   2866 C C   . VAL B 1 129 ? 12.374  23.151  -32.950 1.00 28.34 ? 109 VAL B C   1 
ATOM   2867 O O   . VAL B 1 129 ? 12.102  23.700  -34.026 1.00 30.69 ? 109 VAL B O   1 
ATOM   2868 C CB  . VAL B 1 129 ? 12.334  20.636  -33.151 1.00 25.25 ? 109 VAL B CB  1 
ATOM   2869 C CG1 . VAL B 1 129 ? 13.166  19.380  -33.309 1.00 26.70 ? 109 VAL B CG1 1 
ATOM   2870 C CG2 . VAL B 1 129 ? 11.284  20.488  -32.065 1.00 24.23 ? 109 VAL B CG2 1 
ATOM   2871 N N   . GLN B 1 130 ? 11.935  23.584  -31.775 1.00 30.48 ? 110 GLN B N   1 
ATOM   2872 C CA  . GLN B 1 130 ? 11.090  24.795  -31.622 1.00 33.59 ? 110 GLN B CA  1 
ATOM   2873 C C   . GLN B 1 130 ? 11.913  26.054  -31.951 1.00 33.38 ? 110 GLN B C   1 
ATOM   2874 O O   . GLN B 1 130 ? 11.344  26.948  -32.607 1.00 30.17 ? 110 GLN B O   1 
ATOM   2875 C CB  . GLN B 1 130 ? 10.451  24.808  -30.234 1.00 38.08 ? 110 GLN B CB  1 
ATOM   2876 C CG  . GLN B 1 130 ? 9.467   23.654  -30.027 1.00 45.54 ? 110 GLN B CG  1 
ATOM   2877 C CD  . GLN B 1 130 ? 8.048   23.998  -30.415 1.00 48.03 ? 110 GLN B CD  1 
ATOM   2878 O OE1 . GLN B 1 130 ? 7.528   23.550  -31.433 1.00 54.02 ? 110 GLN B OE1 1 
ATOM   2879 N NE2 . GLN B 1 130 ? 7.406   24.815  -29.598 1.00 50.52 ? 110 GLN B NE2 1 
ATOM   2880 N N   . GLN B 1 131 ? 13.198  26.110  -31.568 1.00 29.87 ? 111 GLN B N   1 
ATOM   2881 C CA  . GLN B 1 131 ? 14.108  27.245  -31.905 1.00 30.44 ? 111 GLN B CA  1 
ATOM   2882 C C   . GLN B 1 131 ? 14.327  27.290  -33.424 1.00 30.66 ? 111 GLN B C   1 
ATOM   2883 O O   . GLN B 1 131 ? 14.552  28.389  -33.949 1.00 31.18 ? 111 GLN B O   1 
ATOM   2884 C CB  . GLN B 1 131 ? 15.449  27.138  -31.164 1.00 30.67 ? 111 GLN B CB  1 
ATOM   2885 C CG  . GLN B 1 131 ? 15.369  27.481  -29.676 1.00 28.75 ? 111 GLN B CG  1 
ATOM   2886 C CD  . GLN B 1 131 ? 16.713  27.334  -28.997 1.00 26.68 ? 111 GLN B CD  1 
ATOM   2887 O OE1 . GLN B 1 131 ? 17.713  27.072  -29.647 1.00 23.70 ? 111 GLN B OE1 1 
ATOM   2888 N NE2 . GLN B 1 131 ? 16.749  27.488  -27.678 1.00 23.81 ? 111 GLN B NE2 1 
ATOM   2889 N N   . ARG B 1 132 ? 14.180  26.156  -34.118 1.00 31.12 ? 112 ARG B N   1 
ATOM   2890 C CA  . ARG B 1 132 ? 14.360  26.065  -35.590 1.00 29.31 ? 112 ARG B CA  1 
ATOM   2891 C C   . ARG B 1 132 ? 13.043  26.233  -36.364 1.00 26.53 ? 112 ARG B C   1 
ATOM   2892 O O   . ARG B 1 132 ? 13.068  26.028  -37.585 1.00 27.34 ? 112 ARG B O   1 
ATOM   2893 C CB  . ARG B 1 132 ? 15.052  24.742  -35.911 1.00 33.77 ? 112 ARG B CB  1 
ATOM   2894 C CG  . ARG B 1 132 ? 16.490  24.727  -35.428 1.00 34.78 ? 112 ARG B CG  1 
ATOM   2895 C CD  . ARG B 1 132 ? 17.222  23.464  -35.771 1.00 37.42 ? 112 ARG B CD  1 
ATOM   2896 N NE  . ARG B 1 132 ? 18.594  23.595  -35.306 1.00 38.08 ? 112 ARG B NE  1 
ATOM   2897 C CZ  . ARG B 1 132 ? 19.583  22.777  -35.638 1.00 40.97 ? 112 ARG B CZ  1 
ATOM   2898 N NH1 . ARG B 1 132 ? 19.361  21.748  -36.442 1.00 42.99 ? 112 ARG B NH1 1 
ATOM   2899 N NH2 . ARG B 1 132 ? 20.794  22.992  -35.154 1.00 41.33 ? 112 ARG B NH2 1 
ATOM   2900 N N   . GLY B 1 133 ? 11.934  26.573  -35.710 1.00 24.05 ? 113 GLY B N   1 
ATOM   2901 C CA  . GLY B 1 133 ? 10.673  26.916  -36.396 1.00 25.23 ? 113 GLY B CA  1 
ATOM   2902 C C   . GLY B 1 133 ? 9.532   25.925  -36.193 1.00 23.94 ? 113 GLY B C   1 
ATOM   2903 O O   . GLY B 1 133 ? 8.396   26.274  -36.566 1.00 23.75 ? 113 GLY B O   1 
ATOM   2904 N N   . ALA B 1 134 ? 9.788   24.722  -35.669 1.00 24.87 ? 114 ALA B N   1 
ATOM   2905 C CA  . ALA B 1 134 ? 8.775   23.644  -35.602 1.00 23.47 ? 114 ALA B CA  1 
ATOM   2906 C C   . ALA B 1 134 ? 7.493   24.234  -35.014 1.00 25.83 ? 114 ALA B C   1 
ATOM   2907 O O   . ALA B 1 134 ? 7.587   25.010  -34.022 1.00 23.70 ? 114 ALA B O   1 
ATOM   2908 C CB  . ALA B 1 134 ? 9.263   22.437  -34.818 1.00 22.64 ? 114 ALA B CB  1 
ATOM   2909 N N   . GLU B 1 135 ? 6.358   23.901  -35.638 1.00 26.01 ? 115 GLU B N   1 
ATOM   2910 C CA  . GLU B 1 135 ? 4.983   24.211  -35.160 1.00 28.78 ? 115 GLU B CA  1 
ATOM   2911 C C   . GLU B 1 135 ? 4.739   23.574  -33.785 1.00 28.86 ? 115 GLU B C   1 
ATOM   2912 O O   . GLU B 1 135 ? 4.170   24.243  -32.895 1.00 26.97 ? 115 GLU B O   1 
ATOM   2913 C CB  . GLU B 1 135 ? 3.963   23.656  -36.158 1.00 33.93 ? 115 GLU B CB  1 
ATOM   2914 C CG  . GLU B 1 135 ? 2.550   24.139  -35.906 1.00 40.95 ? 115 GLU B CG  1 
ATOM   2915 C CD  . GLU B 1 135 ? 2.294   25.545  -36.420 1.00 48.43 ? 115 GLU B CD  1 
ATOM   2916 O OE1 . GLU B 1 135 ? 1.112   25.859  -36.684 1.00 52.60 ? 115 GLU B OE1 1 
ATOM   2917 O OE2 . GLU B 1 135 ? 3.283   26.319  -36.575 1.00 52.05 ? 115 GLU B OE2 1 
ATOM   2918 N N   . SER B 1 136 ? 5.052   22.288  -33.630 1.00 25.23 ? 116 SER B N   1 
ATOM   2919 C CA  . SER B 1 136 ? 4.967   21.618  -32.312 1.00 24.46 ? 116 SER B CA  1 
ATOM   2920 C C   . SER B 1 136 ? 5.845   20.373  -32.271 1.00 21.47 ? 116 SER B C   1 
ATOM   2921 O O   . SER B 1 136 ? 6.298   19.879  -33.328 1.00 21.04 ? 116 SER B O   1 
ATOM   2922 C CB  . SER B 1 136 ? 3.532   21.313  -31.910 1.00 26.16 ? 116 SER B CB  1 
ATOM   2923 O OG  . SER B 1 136 ? 2.925   20.459  -32.852 1.00 31.40 ? 116 SER B OG  1 
ATOM   2924 N N   . TYR B 1 137 ? 6.096   19.937  -31.040 1.00 19.20 ? 117 TYR B N   1 
ATOM   2925 C CA  . TYR B 1 137 ? 6.797   18.692  -30.684 1.00 18.09 ? 117 TYR B CA  1 
ATOM   2926 C C   . TYR B 1 137 ? 5.822   17.901  -29.825 1.00 16.80 ? 117 TYR B C   1 
ATOM   2927 O O   . TYR B 1 137 ? 5.250   18.470  -28.887 1.00 15.96 ? 117 TYR B O   1 
ATOM   2928 C CB  . TYR B 1 137 ? 8.105   18.983  -29.938 1.00 16.78 ? 117 TYR B CB  1 
ATOM   2929 C CG  . TYR B 1 137 ? 8.862   17.756  -29.493 1.00 17.84 ? 117 TYR B CG  1 
ATOM   2930 C CD1 . TYR B 1 137 ? 8.483   17.054  -28.359 1.00 17.42 ? 117 TYR B CD1 1 
ATOM   2931 C CD2 . TYR B 1 137 ? 9.984   17.310  -30.184 1.00 17.51 ? 117 TYR B CD2 1 
ATOM   2932 C CE1 . TYR B 1 137 ? 9.175   15.920  -27.944 1.00 17.80 ? 117 TYR B CE1 1 
ATOM   2933 C CE2 . TYR B 1 137 ? 10.700  16.193  -29.767 1.00 17.83 ? 117 TYR B CE2 1 
ATOM   2934 C CZ  . TYR B 1 137 ? 10.289  15.490  -28.648 1.00 17.41 ? 117 TYR B CZ  1 
ATOM   2935 O OH  . TYR B 1 137 ? 10.958  14.373  -28.237 1.00 17.41 ? 117 TYR B OH  1 
ATOM   2936 N N   . ILE B 1 138 ? 5.634   16.641  -30.146 1.00 16.28 ? 118 ILE B N   1 
ATOM   2937 C CA  . ILE B 1 138 ? 4.920   15.694  -29.248 1.00 17.22 ? 118 ILE B CA  1 
ATOM   2938 C C   . ILE B 1 138 ? 5.775   14.442  -29.153 1.00 16.09 ? 118 ILE B C   1 
ATOM   2939 O O   . ILE B 1 138 ? 6.383   14.055  -30.162 1.00 15.18 ? 118 ILE B O   1 
ATOM   2940 C CB  . ILE B 1 138 ? 3.463   15.414  -29.678 1.00 20.13 ? 118 ILE B CB  1 
ATOM   2941 C CG1 . ILE B 1 138 ? 3.328   14.658  -30.994 1.00 22.16 ? 118 ILE B CG1 1 
ATOM   2942 C CG2 . ILE B 1 138 ? 2.646   16.697  -29.722 1.00 21.14 ? 118 ILE B CG2 1 
ATOM   2943 C CD1 . ILE B 1 138 ? 1.883   14.366  -31.343 1.00 22.78 ? 118 ILE B CD1 1 
ATOM   2944 N N   . HIS B 1 139 ? 5.862   13.884  -27.948 1.00 15.32 ? 119 HIS B N   1 
ATOM   2945 C CA  . HIS B 1 139 ? 6.628   12.655  -27.657 1.00 14.56 ? 119 HIS B CA  1 
ATOM   2946 C C   . HIS B 1 139 ? 5.662   11.492  -27.471 1.00 14.04 ? 119 HIS B C   1 
ATOM   2947 O O   . HIS B 1 139 ? 4.627   11.688  -26.805 1.00 14.35 ? 119 HIS B O   1 
ATOM   2948 C CB  . HIS B 1 139 ? 7.498   12.824  -26.413 1.00 15.46 ? 119 HIS B CB  1 
ATOM   2949 C CG  . HIS B 1 139 ? 8.685   11.933  -26.504 1.00 14.87 ? 119 HIS B CG  1 
ATOM   2950 N ND1 . HIS B 1 139 ? 9.850   12.352  -27.089 1.00 13.73 ? 119 HIS B ND1 1 
ATOM   2951 C CD2 . HIS B 1 139 ? 8.828   10.611  -26.234 1.00 15.06 ? 119 HIS B CD2 1 
ATOM   2952 C CE1 . HIS B 1 139 ? 10.701  11.341  -27.119 1.00 13.68 ? 119 HIS B CE1 1 
ATOM   2953 N NE2 . HIS B 1 139 ? 10.108  10.253  -26.574 1.00 13.26 ? 119 HIS B NE2 1 
ATOM   2954 N N   . GLY B 1 140 ? 6.019   10.340  -28.031 1.00 13.41 ? 120 GLY B N   1 
ATOM   2955 C CA  . GLY B 1 140 ? 5.332   9.054   -27.847 1.00 13.40 ? 120 GLY B CA  1 
ATOM   2956 C C   . GLY B 1 140 ? 6.274   8.001   -27.286 1.00 13.70 ? 120 GLY B C   1 
ATOM   2957 O O   . GLY B 1 140 ? 7.442   7.917   -27.746 1.00 13.56 ? 120 GLY B O   1 
ATOM   2958 N N   . ALA B 1 141 ? 5.796   7.251   -26.300 1.00 13.86 ? 121 ALA B N   1 
ATOM   2959 C CA  . ALA B 1 141 ? 6.407   6.008   -25.787 1.00 14.56 ? 121 ALA B CA  1 
ATOM   2960 C C   . ALA B 1 141 ? 5.526   4.840   -26.212 1.00 14.22 ? 121 ALA B C   1 
ATOM   2961 O O   . ALA B 1 141 ? 4.421   4.689   -25.659 1.00 13.74 ? 121 ALA B O   1 
ATOM   2962 C CB  . ALA B 1 141 ? 6.578   6.050   -24.288 1.00 14.40 ? 121 ALA B CB  1 
ATOM   2963 N N   . ILE B 1 142 ? 6.013   4.062   -27.172 1.00 14.76 ? 122 ILE B N   1 
ATOM   2964 C CA  . ILE B 1 142 ? 5.341   2.816   -27.636 1.00 16.01 ? 122 ILE B CA  1 
ATOM   2965 C C   . ILE B 1 142 ? 5.545   1.770   -26.548 1.00 16.26 ? 122 ILE B C   1 
ATOM   2966 O O   . ILE B 1 142 ? 6.700   1.479   -26.253 1.00 16.04 ? 122 ILE B O   1 
ATOM   2967 C CB  . ILE B 1 142 ? 5.897   2.341   -28.986 1.00 15.42 ? 122 ILE B CB  1 
ATOM   2968 C CG1 . ILE B 1 142 ? 5.711   3.398   -30.074 1.00 15.17 ? 122 ILE B CG1 1 
ATOM   2969 C CG2 . ILE B 1 142 ? 5.288   1.000   -29.380 1.00 15.41 ? 122 ILE B CG2 1 
ATOM   2970 C CD1 . ILE B 1 142 ? 6.738   3.315   -31.171 1.00 15.69 ? 122 ILE B CD1 1 
ATOM   2971 N N   . MET B 1 143 ? 4.459   1.232   -25.991 1.00 16.93 ? 123 MET B N   1 
ATOM   2972 C CA  . MET B 1 143 ? 4.537   0.215   -24.918 1.00 18.66 ? 123 MET B CA  1 
ATOM   2973 C C   . MET B 1 143 ? 4.228   -1.182  -25.469 1.00 18.54 ? 123 MET B C   1 
ATOM   2974 O O   . MET B 1 143 ? 3.437   -1.922  -24.874 1.00 18.97 ? 123 MET B O   1 
ATOM   2975 C CB  . MET B 1 143 ? 3.573   0.585   -23.801 1.00 21.60 ? 123 MET B CB  1 
ATOM   2976 C CG  . MET B 1 143 ? 3.752   2.022   -23.363 1.00 23.28 ? 123 MET B CG  1 
ATOM   2977 S SD  . MET B 1 143 ? 2.983   2.268   -21.773 1.00 25.28 ? 123 MET B SD  1 
ATOM   2978 C CE  . MET B 1 143 ? 1.297   1.743   -22.072 1.00 29.09 ? 123 MET B CE  1 
ATOM   2979 N N   . THR B 1 144 ? 4.850   -1.549  -26.569 1.00 18.95 ? 124 THR B N   1 
ATOM   2980 C CA  . THR B 1 144 ? 4.733   -2.902  -27.165 1.00 20.34 ? 124 THR B CA  1 
ATOM   2981 C C   . THR B 1 144 ? 5.997   -3.136  -27.993 1.00 20.96 ? 124 THR B C   1 
ATOM   2982 O O   . THR B 1 144 ? 6.808   -2.231  -28.045 1.00 19.57 ? 124 THR B O   1 
ATOM   2983 C CB  . THR B 1 144 ? 3.423   -3.048  -27.947 1.00 21.17 ? 124 THR B CB  1 
ATOM   2984 O OG1 . THR B 1 144 ? 3.209   -4.447  -28.164 1.00 24.28 ? 124 THR B OG1 1 
ATOM   2985 C CG2 . THR B 1 144 ? 3.425   -2.310  -29.268 1.00 21.90 ? 124 THR B CG2 1 
ATOM   2986 N N   . THR B 1 145 ? 6.150   -4.320  -28.593 1.00 21.35 ? 125 THR B N   1 
ATOM   2987 C CA  . THR B 1 145 ? 7.251   -4.658  -29.524 1.00 20.39 ? 125 THR B CA  1 
ATOM   2988 C C   . THR B 1 145 ? 6.769   -4.406  -30.947 1.00 20.21 ? 125 THR B C   1 
ATOM   2989 O O   . THR B 1 145 ? 5.563   -4.266  -31.171 1.00 19.35 ? 125 THR B O   1 
ATOM   2990 C CB  . THR B 1 145 ? 7.679   -6.113  -29.303 1.00 19.85 ? 125 THR B CB  1 
ATOM   2991 O OG1 . THR B 1 145 ? 6.481   -6.855  -29.499 1.00 20.08 ? 125 THR B OG1 1 
ATOM   2992 C CG2 . THR B 1 145 ? 8.219   -6.354  -27.913 1.00 20.89 ? 125 THR B CG2 1 
ATOM   2993 N N   . PRO B 1 146 ? 7.689   -4.336  -31.939 1.00 20.86 ? 126 PRO B N   1 
ATOM   2994 C CA  . PRO B 1 146 ? 7.324   -4.053  -33.328 1.00 22.85 ? 126 PRO B CA  1 
ATOM   2995 C C   . PRO B 1 146 ? 6.239   -4.954  -33.928 1.00 25.41 ? 126 PRO B C   1 
ATOM   2996 O O   . PRO B 1 146 ? 5.417   -4.476  -34.717 1.00 28.10 ? 126 PRO B O   1 
ATOM   2997 C CB  . PRO B 1 146 ? 8.650   -4.233  -34.074 1.00 21.78 ? 126 PRO B CB  1 
ATOM   2998 C CG  . PRO B 1 146 ? 9.680   -3.794  -33.063 1.00 20.58 ? 126 PRO B CG  1 
ATOM   2999 C CD  . PRO B 1 146 ? 9.146   -4.339  -31.753 1.00 21.31 ? 126 PRO B CD  1 
ATOM   3000 N N   . GLU B 1 147 ? 6.229   -6.221  -33.543 1.00 27.59 ? 127 GLU B N   1 
ATOM   3001 C CA  . GLU B 1 147 ? 5.354   -7.222  -34.189 1.00 28.85 ? 127 GLU B CA  1 
ATOM   3002 C C   . GLU B 1 147 ? 3.899   -6.987  -33.793 1.00 26.46 ? 127 GLU B C   1 
ATOM   3003 O O   . GLU B 1 147 ? 3.058   -7.317  -34.597 1.00 26.31 ? 127 GLU B O   1 
ATOM   3004 C CB  . GLU B 1 147 ? 5.828   -8.638  -33.889 1.00 32.41 ? 127 GLU B CB  1 
ATOM   3005 C CG  . GLU B 1 147 ? 5.691   -9.078  -32.456 1.00 34.58 ? 127 GLU B CG  1 
ATOM   3006 C CD  . GLU B 1 147 ? 6.206   -10.499 -32.303 1.00 39.76 ? 127 GLU B CD  1 
ATOM   3007 O OE1 . GLU B 1 147 ? 5.376   -11.391 -31.980 1.00 44.38 ? 127 GLU B OE1 1 
ATOM   3008 O OE2 . GLU B 1 147 ? 7.426   -10.719 -32.568 1.00 39.21 ? 127 GLU B OE2 1 
ATOM   3009 N N   . TYR B 1 148 ? 3.607   -6.398  -32.637 1.00 26.89 ? 128 TYR B N   1 
ATOM   3010 C CA  . TYR B 1 148 ? 2.210   -6.056  -32.254 1.00 26.65 ? 128 TYR B CA  1 
ATOM   3011 C C   . TYR B 1 148 ? 1.874   -4.590  -32.589 1.00 25.18 ? 128 TYR B C   1 
ATOM   3012 O O   . TYR B 1 148 ? 0.706   -4.184  -32.341 1.00 24.29 ? 128 TYR B O   1 
ATOM   3013 C CB  . TYR B 1 148 ? 1.976   -6.375  -30.778 1.00 31.37 ? 128 TYR B CB  1 
ATOM   3014 C CG  . TYR B 1 148 ? 2.409   -7.763  -30.391 1.00 35.39 ? 128 TYR B CG  1 
ATOM   3015 C CD1 . TYR B 1 148 ? 1.631   -8.867  -30.697 1.00 39.92 ? 128 TYR B CD1 1 
ATOM   3016 C CD2 . TYR B 1 148 ? 3.625   -7.981  -29.768 1.00 36.79 ? 128 TYR B CD2 1 
ATOM   3017 C CE1 . TYR B 1 148 ? 2.025   -10.150 -30.355 1.00 40.99 ? 128 TYR B CE1 1 
ATOM   3018 C CE2 . TYR B 1 148 ? 4.042   -9.258  -29.433 1.00 40.90 ? 128 TYR B CE2 1 
ATOM   3019 C CZ  . TYR B 1 148 ? 3.238   -10.346 -29.722 1.00 41.11 ? 128 TYR B CZ  1 
ATOM   3020 O OH  . TYR B 1 148 ? 3.650   -11.604 -29.389 1.00 46.63 ? 128 TYR B OH  1 
ATOM   3021 N N   . LEU B 1 149 ? 2.806   -3.793  -33.131 1.00 22.63 ? 129 LEU B N   1 
ATOM   3022 C CA  . LEU B 1 149 ? 2.480   -2.370  -33.407 1.00 22.18 ? 129 LEU B CA  1 
ATOM   3023 C C   . LEU B 1 149 ? 1.285   -2.338  -34.366 1.00 24.36 ? 129 LEU B C   1 
ATOM   3024 O O   . LEU B 1 149 ? 1.248   -3.155  -35.301 1.00 25.01 ? 129 LEU B O   1 
ATOM   3025 C CB  . LEU B 1 149 ? 3.672   -1.607  -33.985 1.00 21.14 ? 129 LEU B CB  1 
ATOM   3026 C CG  . LEU B 1 149 ? 3.500   -0.088  -33.943 1.00 19.36 ? 129 LEU B CG  1 
ATOM   3027 C CD1 . LEU B 1 149 ? 3.622   0.421   -32.523 1.00 18.62 ? 129 LEU B CD1 1 
ATOM   3028 C CD2 . LEU B 1 149 ? 4.485   0.616   -34.852 1.00 19.65 ? 129 LEU B CD2 1 
ATOM   3029 N N   . GLY B 1 150 ? 0.319   -1.456  -34.123 1.00 25.08 ? 130 GLY B N   1 
ATOM   3030 C CA  . GLY B 1 150 ? -0.831  -1.280  -35.024 1.00 26.55 ? 130 GLY B CA  1 
ATOM   3031 C C   . GLY B 1 150 ? -2.079  -1.958  -34.502 1.00 28.55 ? 130 GLY B C   1 
ATOM   3032 O O   . GLY B 1 150 ? -3.151  -1.619  -34.986 1.00 30.13 ? 130 GLY B O   1 
ATOM   3033 N N   . GLN B 1 151 ? -1.952  -2.875  -33.544 1.00 30.93 ? 131 GLN B N   1 
ATOM   3034 C CA  . GLN B 1 151 ? -3.112  -3.505  -32.869 1.00 33.09 ? 131 GLN B CA  1 
ATOM   3035 C C   . GLN B 1 151 ? -3.699  -2.537  -31.838 1.00 34.06 ? 131 GLN B C   1 
ATOM   3036 O O   . GLN B 1 151 ? -2.964  -1.844  -31.124 1.00 33.68 ? 131 GLN B O   1 
ATOM   3037 C CB  . GLN B 1 151 ? -2.679  -4.832  -32.259 1.00 33.62 ? 131 GLN B CB  1 
ATOM   3038 C CG  . GLN B 1 151 ? -2.125  -5.801  -33.299 1.00 36.88 ? 131 GLN B CG  1 
ATOM   3039 C CD  . GLN B 1 151 ? -1.706  -7.116  -32.691 1.00 37.38 ? 131 GLN B CD  1 
ATOM   3040 O OE1 . GLN B 1 151 ? -1.227  -8.017  -33.380 1.00 42.58 ? 131 GLN B OE1 1 
ATOM   3041 N NE2 . GLN B 1 151 ? -1.891  -7.240  -31.389 1.00 38.25 ? 131 GLN B NE2 1 
ATOM   3042 N N   . PRO B 1 152 ? -5.047  -2.470  -31.701 1.00 35.99 ? 132 PRO B N   1 
ATOM   3043 C CA  . PRO B 1 152 ? -5.679  -1.582  -30.714 1.00 36.09 ? 132 PRO B CA  1 
ATOM   3044 C C   . PRO B 1 152 ? -5.205  -1.845  -29.273 1.00 34.48 ? 132 PRO B C   1 
ATOM   3045 O O   . PRO B 1 152 ? -5.158  -0.908  -28.482 1.00 35.80 ? 132 PRO B O   1 
ATOM   3046 C CB  . PRO B 1 152 ? -7.190  -1.846  -30.857 1.00 36.48 ? 132 PRO B CB  1 
ATOM   3047 C CG  . PRO B 1 152 ? -7.278  -3.168  -31.611 1.00 38.85 ? 132 PRO B CG  1 
ATOM   3048 C CD  . PRO B 1 152 ? -6.035  -3.235  -32.479 1.00 36.67 ? 132 PRO B CD  1 
ATOM   3049 N N   . SER B 1 153 ? -4.856  -3.095  -28.953 1.00 29.48 ? 133 SER B N   1 
ATOM   3050 C CA  . SER B 1 153 ? -4.324  -3.482  -27.620 1.00 30.00 ? 133 SER B CA  1 
ATOM   3051 C C   . SER B 1 153 ? -2.939  -2.844  -27.398 1.00 28.07 ? 133 SER B C   1 
ATOM   3052 O O   . SER B 1 153 ? -2.450  -2.864  -26.255 1.00 29.33 ? 133 SER B O   1 
ATOM   3053 C CB  . SER B 1 153 ? -4.246  -4.984  -27.489 1.00 29.02 ? 133 SER B CB  1 
ATOM   3054 O OG  . SER B 1 153 ? -3.166  -5.484  -28.272 1.00 26.69 ? 133 SER B OG  1 
ATOM   3055 N N   . SER B 1 154 ? -2.279  -2.381  -28.455 1.00 27.04 ? 134 SER B N   1 
ATOM   3056 C CA  . SER B 1 154 ? -0.956  -1.712  -28.362 1.00 28.67 ? 134 SER B CA  1 
ATOM   3057 C C   . SER B 1 154 ? -1.151  -0.234  -28.016 1.00 25.04 ? 134 SER B C   1 
ATOM   3058 O O   . SER B 1 154 ? -1.705  0.499   -28.831 1.00 28.56 ? 134 SER B O   1 
ATOM   3059 C CB  . SER B 1 154 ? -0.190  -1.888  -29.626 1.00 29.48 ? 134 SER B CB  1 
ATOM   3060 O OG  . SER B 1 154 ? 0.030   -3.269  -29.840 1.00 34.10 ? 134 SER B OG  1 
ATOM   3061 N N   . VAL B 1 155 ? -0.724  0.175   -26.833 1.00 24.11 ? 135 VAL B N   1 
ATOM   3062 C CA  . VAL B 1 155 ? -0.884  1.568   -26.337 1.00 22.94 ? 135 VAL B CA  1 
ATOM   3063 C C   . VAL B 1 155 ? 0.440   2.312   -26.518 1.00 23.11 ? 135 VAL B C   1 
ATOM   3064 O O   . VAL B 1 155 ? 1.513   1.786   -26.089 1.00 21.12 ? 135 VAL B O   1 
ATOM   3065 C CB  . VAL B 1 155 ? -1.371  1.578   -24.876 1.00 25.58 ? 135 VAL B CB  1 
ATOM   3066 C CG1 . VAL B 1 155 ? -1.585  2.993   -24.338 1.00 25.64 ? 135 VAL B CG1 1 
ATOM   3067 C CG2 . VAL B 1 155 ? -2.655  0.769   -24.722 1.00 27.02 ? 135 VAL B CG2 1 
ATOM   3068 N N   . THR B 1 156 ? 0.357   3.508   -27.098 1.00 20.13 ? 136 THR B N   1 
ATOM   3069 C CA  . THR B 1 156 ? 1.437   4.516   -27.098 1.00 19.40 ? 136 THR B CA  1 
ATOM   3070 C C   . THR B 1 156 ? 1.019   5.694   -26.205 1.00 19.00 ? 136 THR B C   1 
ATOM   3071 O O   . THR B 1 156 ? -0.013  6.314   -26.492 1.00 19.25 ? 136 THR B O   1 
ATOM   3072 C CB  . THR B 1 156 ? 1.766   4.874   -28.546 1.00 20.06 ? 136 THR B CB  1 
ATOM   3073 O OG1 . THR B 1 156 ? 2.328   3.677   -29.110 1.00 24.35 ? 136 THR B OG1 1 
ATOM   3074 C CG2 . THR B 1 156 ? 2.709   6.044   -28.672 1.00 19.55 ? 136 THR B CG2 1 
ATOM   3075 N N   . LEU B 1 157 ? 1.808   5.994   -25.167 1.00 16.95 ? 137 LEU B N   1 
ATOM   3076 C CA  . LEU B 1 157 ? 1.634   7.213   -24.346 1.00 16.33 ? 137 LEU B CA  1 
ATOM   3077 C C   . LEU B 1 157 ? 2.139   8.396   -25.173 1.00 14.61 ? 137 LEU B C   1 
ATOM   3078 O O   . LEU B 1 157 ? 3.224   8.288   -25.774 1.00 13.27 ? 137 LEU B O   1 
ATOM   3079 C CB  . LEU B 1 157 ? 2.396   7.097   -23.021 1.00 17.13 ? 137 LEU B CB  1 
ATOM   3080 C CG  . LEU B 1 157 ? 2.092   5.864   -22.172 1.00 19.08 ? 137 LEU B CG  1 
ATOM   3081 C CD1 . LEU B 1 157 ? 2.859   5.930   -20.873 1.00 20.40 ? 137 LEU B CD1 1 
ATOM   3082 C CD2 . LEU B 1 157 ? 0.598   5.724   -21.890 1.00 19.83 ? 137 LEU B CD2 1 
ATOM   3083 N N   . ILE B 1 158 ? 1.357   9.461   -25.221 1.00 13.23 ? 138 ILE B N   1 
ATOM   3084 C CA  . ILE B 1 158 ? 1.684   10.703  -25.989 1.00 13.67 ? 138 ILE B CA  1 
ATOM   3085 C C   . ILE B 1 158 ? 1.753   11.852  -24.996 1.00 13.69 ? 138 ILE B C   1 
ATOM   3086 O O   . ILE B 1 158 ? 0.817   11.993  -24.174 1.00 14.48 ? 138 ILE B O   1 
ATOM   3087 C CB  . ILE B 1 158 ? 0.655   10.990  -27.098 1.00 13.21 ? 138 ILE B CB  1 
ATOM   3088 C CG1 . ILE B 1 158 ? 0.534   9.831   -28.096 1.00 14.20 ? 138 ILE B CG1 1 
ATOM   3089 C CG2 . ILE B 1 158 ? 0.960   12.314  -27.799 1.00 13.25 ? 138 ILE B CG2 1 
ATOM   3090 C CD1 . ILE B 1 158 ? 1.793   9.545   -28.890 1.00 14.80 ? 138 ILE B CD1 1 
ATOM   3091 N N   . SER B 1 159 ? 2.815   12.646  -25.048 1.00 14.18 ? 139 SER B N   1 
ATOM   3092 C CA  . SER B 1 159 ? 2.858   13.904  -24.268 1.00 13.96 ? 139 SER B CA  1 
ATOM   3093 C C   . SER B 1 159 ? 3.214   15.073  -25.186 1.00 14.67 ? 139 SER B C   1 
ATOM   3094 O O   . SER B 1 159 ? 4.012   14.884  -26.141 1.00 13.65 ? 139 SER B O   1 
ATOM   3095 C CB  . SER B 1 159 ? 3.736   13.771  -23.067 1.00 13.26 ? 139 SER B CB  1 
ATOM   3096 O OG  . SER B 1 159 ? 5.075   13.511  -23.421 1.00 12.49 ? 139 SER B OG  1 
ATOM   3097 N N   . GLY B 1 160 ? 2.551   16.211  -24.951 1.00 15.17 ? 140 GLY B N   1 
ATOM   3098 C CA  . GLY B 1 160 ? 2.720   17.460  -25.716 1.00 14.68 ? 140 GLY B CA  1 
ATOM   3099 C C   . GLY B 1 160 ? 1.398   18.201  -25.905 1.00 15.10 ? 140 GLY B C   1 
ATOM   3100 O O   . GLY B 1 160 ? 0.346   17.749  -25.426 1.00 14.24 ? 140 GLY B O   1 
ATOM   3101 N N   . PRO B 1 161 ? 1.426   19.365  -26.600 1.00 15.42 ? 141 PRO B N   1 
ATOM   3102 C CA  . PRO B 1 161 ? 0.245   20.217  -26.736 1.00 16.52 ? 141 PRO B CA  1 
ATOM   3103 C C   . PRO B 1 161 ? -0.996  19.415  -27.157 1.00 18.44 ? 141 PRO B C   1 
ATOM   3104 O O   . PRO B 1 161 ? -0.915  18.610  -28.085 1.00 21.29 ? 141 PRO B O   1 
ATOM   3105 C CB  . PRO B 1 161 ? 0.696   21.295  -27.742 1.00 16.88 ? 141 PRO B CB  1 
ATOM   3106 C CG  . PRO B 1 161 ? 2.191   21.415  -27.470 1.00 16.55 ? 141 PRO B CG  1 
ATOM   3107 C CD  . PRO B 1 161 ? 2.626   19.983  -27.188 1.00 15.91 ? 141 PRO B CD  1 
ATOM   3108 N N   . LYS B 1 162 ? -2.094  19.606  -26.426 1.00 19.52 ? 142 LYS B N   1 
ATOM   3109 C CA  . LYS B 1 162 ? -3.403  18.937  -26.665 1.00 21.81 ? 142 LYS B CA  1 
ATOM   3110 C C   . LYS B 1 162 ? -3.821  19.112  -28.138 1.00 21.69 ? 142 LYS B C   1 
ATOM   3111 O O   . LYS B 1 162 ? -4.114  18.078  -28.804 1.00 20.67 ? 142 LYS B O   1 
ATOM   3112 C CB  . LYS B 1 162 ? -4.442  19.500  -25.693 1.00 24.36 ? 142 LYS B CB  1 
ATOM   3113 C CG  . LYS B 1 162 ? -5.873  19.042  -25.910 1.00 26.15 ? 142 LYS B CG  1 
ATOM   3114 C CD  . LYS B 1 162 ? -6.055  17.565  -25.850 1.00 28.25 ? 142 LYS B CD  1 
ATOM   3115 C CE  . LYS B 1 162 ? -7.518  17.167  -25.941 1.00 31.84 ? 142 LYS B CE  1 
ATOM   3116 N NZ  . LYS B 1 162 ? -8.303  17.761  -24.833 1.00 31.75 ? 142 LYS B NZ  1 
ATOM   3117 N N   . THR B 1 163 ? -3.806  20.351  -28.646 1.00 19.69 ? 143 THR B N   1 
ATOM   3118 C CA  . THR B 1 163 ? -4.266  20.679  -30.016 1.00 21.55 ? 143 THR B CA  1 
ATOM   3119 C C   . THR B 1 163 ? -3.403  19.918  -31.027 1.00 20.60 ? 143 THR B C   1 
ATOM   3120 O O   . THR B 1 163 ? -3.991  19.406  -31.970 1.00 19.76 ? 143 THR B O   1 
ATOM   3121 C CB  . THR B 1 163 ? -4.350  22.195  -30.249 1.00 22.20 ? 143 THR B CB  1 
ATOM   3122 O OG1 . THR B 1 163 ? -3.079  22.768  -29.971 1.00 27.01 ? 143 THR B OG1 1 
ATOM   3123 C CG2 . THR B 1 163 ? -5.381  22.852  -29.364 1.00 20.80 ? 143 THR B CG2 1 
ATOM   3124 N N   . ALA B 1 164 ? -2.082  19.804  -30.815 1.00 21.57 ? 144 ALA B N   1 
ATOM   3125 C CA  . ALA B 1 164 ? -1.161  19.010  -31.672 1.00 21.67 ? 144 ALA B CA  1 
ATOM   3126 C C   . ALA B 1 164 ? -1.517  17.516  -31.604 1.00 22.47 ? 144 ALA B C   1 
ATOM   3127 O O   . ALA B 1 164 ? -1.562  16.873  -32.672 1.00 23.94 ? 144 ALA B O   1 
ATOM   3128 C CB  . ALA B 1 164 ? 0.284   19.251  -31.290 1.00 23.21 ? 144 ALA B CB  1 
ATOM   3129 N N   . TYR B 1 165 ? -1.774  16.964  -30.416 1.00 21.93 ? 145 TYR B N   1 
ATOM   3130 C CA  . TYR B 1 165 ? -2.265  15.570  -30.261 1.00 21.07 ? 145 TYR B CA  1 
ATOM   3131 C C   . TYR B 1 165 ? -3.544  15.366  -31.083 1.00 23.74 ? 145 TYR B C   1 
ATOM   3132 O O   . TYR B 1 165 ? -3.660  14.345  -31.832 1.00 22.99 ? 145 TYR B O   1 
ATOM   3133 C CB  . TYR B 1 165 ? -2.581  15.220  -28.810 1.00 20.29 ? 145 TYR B CB  1 
ATOM   3134 C CG  . TYR B 1 165 ? -3.211  13.864  -28.618 1.00 19.83 ? 145 TYR B CG  1 
ATOM   3135 C CD1 . TYR B 1 165 ? -2.560  12.701  -29.006 1.00 21.12 ? 145 TYR B CD1 1 
ATOM   3136 C CD2 . TYR B 1 165 ? -4.458  13.735  -28.041 1.00 20.33 ? 145 TYR B CD2 1 
ATOM   3137 C CE1 . TYR B 1 165 ? -3.123  11.451  -28.811 1.00 20.29 ? 145 TYR B CE1 1 
ATOM   3138 C CE2 . TYR B 1 165 ? -5.045  12.497  -27.860 1.00 20.61 ? 145 TYR B CE2 1 
ATOM   3139 C CZ  . TYR B 1 165 ? -4.380  11.350  -28.251 1.00 20.66 ? 145 TYR B CZ  1 
ATOM   3140 O OH  . TYR B 1 165 ? -4.969  10.137  -28.048 1.00 23.96 ? 145 TYR B OH  1 
ATOM   3141 N N   . GLU B 1 166 ? -4.496  16.288  -30.939 1.00 23.63 ? 146 GLU B N   1 
ATOM   3142 C CA  . GLU B 1 166 ? -5.834  16.173  -31.581 1.00 25.68 ? 146 GLU B CA  1 
ATOM   3143 C C   . GLU B 1 166 ? -5.652  16.191  -33.104 1.00 22.72 ? 146 GLU B C   1 
ATOM   3144 O O   . GLU B 1 166 ? -6.216  15.327  -33.738 1.00 23.09 ? 146 GLU B O   1 
ATOM   3145 C CB  . GLU B 1 166 ? -6.789  17.255  -31.061 1.00 27.66 ? 146 GLU B CB  1 
ATOM   3146 C CG  . GLU B 1 166 ? -7.329  16.970  -29.669 1.00 29.84 ? 146 GLU B CG  1 
ATOM   3147 C CD  . GLU B 1 166 ? -8.184  15.723  -29.515 1.00 35.18 ? 146 GLU B CD  1 
ATOM   3148 O OE1 . GLU B 1 166 ? -8.031  15.025  -28.501 1.00 39.26 ? 146 GLU B OE1 1 
ATOM   3149 O OE2 . GLU B 1 166 ? -9.022  15.456  -30.403 1.00 45.31 ? 146 GLU B OE2 1 
ATOM   3150 N N   . SER B 1 167 ? -4.843  17.090  -33.666 1.00 23.39 ? 147 SER B N   1 
ATOM   3151 C CA  . SER B 1 167 ? -4.525  17.112  -35.121 1.00 24.65 ? 147 SER B CA  1 
ATOM   3152 C C   . SER B 1 167 ? -3.980  15.754  -35.584 1.00 23.13 ? 147 SER B C   1 
ATOM   3153 O O   . SER B 1 167 ? -4.388  15.315  -36.653 1.00 26.50 ? 147 SER B O   1 
ATOM   3154 C CB  . SER B 1 167 ? -3.564  18.200  -35.477 1.00 25.36 ? 147 SER B CB  1 
ATOM   3155 O OG  . SER B 1 167 ? -4.171  19.442  -35.217 1.00 33.03 ? 147 SER B OG  1 
ATOM   3156 N N   . GLN B 1 168 ? -3.136  15.103  -34.788 1.00 21.80 ? 148 GLN B N   1 
ATOM   3157 C CA  . GLN B 1 168 ? -2.359  13.889  -35.183 1.00 21.73 ? 148 GLN B CA  1 
ATOM   3158 C C   . GLN B 1 168 ? -3.019  12.584  -34.711 1.00 22.49 ? 148 GLN B C   1 
ATOM   3159 O O   . GLN B 1 168 ? -2.537  11.507  -35.110 1.00 19.52 ? 148 GLN B O   1 
ATOM   3160 C CB  . GLN B 1 168 ? -0.948  13.989  -34.595 1.00 20.94 ? 148 GLN B CB  1 
ATOM   3161 C CG  . GLN B 1 168 ? -0.149  15.181  -35.093 1.00 20.42 ? 148 GLN B CG  1 
ATOM   3162 C CD  . GLN B 1 168 ? 0.017   15.216  -36.595 1.00 20.55 ? 148 GLN B CD  1 
ATOM   3163 O OE1 . GLN B 1 168 ? -0.045  14.191  -37.262 1.00 19.76 ? 148 GLN B OE1 1 
ATOM   3164 N NE2 . GLN B 1 168 ? 0.248   16.399  -37.138 1.00 19.79 ? 148 GLN B NE2 1 
ATOM   3165 N N   . LYS B 1 169 ? -4.070  12.658  -33.888 1.00 24.73 ? 149 LYS B N   1 
ATOM   3166 C CA  . LYS B 1 169 ? -4.737  11.481  -33.264 1.00 27.35 ? 149 LYS B CA  1 
ATOM   3167 C C   . LYS B 1 169 ? -5.113  10.449  -34.341 1.00 25.33 ? 149 LYS B C   1 
ATOM   3168 O O   . LYS B 1 169 ? -4.851  9.246   -34.146 1.00 24.24 ? 149 LYS B O   1 
ATOM   3169 C CB  . LYS B 1 169 ? -5.966  11.949  -32.480 1.00 31.20 ? 149 LYS B CB  1 
ATOM   3170 C CG  . LYS B 1 169 ? -6.575  10.923  -31.542 1.00 35.66 ? 149 LYS B CG  1 
ATOM   3171 C CD  . LYS B 1 169 ? -7.857  11.402  -30.886 1.00 39.57 ? 149 LYS B CD  1 
ATOM   3172 C CE  . LYS B 1 169 ? -7.676  11.906  -29.470 1.00 44.60 ? 149 LYS B CE  1 
ATOM   3173 N NZ  . LYS B 1 169 ? -8.967  12.274  -28.828 1.00 47.76 ? 149 LYS B NZ  1 
ATOM   3174 N N   . GLU B 1 170 ? -5.705  10.898  -35.444 1.00 25.89 ? 150 GLU B N   1 
ATOM   3175 C CA  . GLU B 1 170 ? -6.182  9.991   -36.513 1.00 26.29 ? 150 GLU B CA  1 
ATOM   3176 C C   . GLU B 1 170 ? -4.965  9.248   -37.081 1.00 24.55 ? 150 GLU B C   1 
ATOM   3177 O O   . GLU B 1 170 ? -4.989  7.997   -37.061 1.00 21.89 ? 150 GLU B O   1 
ATOM   3178 C CB  . GLU B 1 170 ? -6.959  10.782  -37.562 1.00 28.99 ? 150 GLU B CB  1 
ATOM   3179 C CG  . GLU B 1 170 ? -7.370  9.947   -38.756 1.00 32.99 ? 150 GLU B CG  1 
ATOM   3180 C CD  . GLU B 1 170 ? -8.628  10.435  -39.458 1.00 35.41 ? 150 GLU B CD  1 
ATOM   3181 O OE1 . GLU B 1 170 ? -8.553  10.764  -40.643 1.00 36.34 ? 150 GLU B OE1 1 
ATOM   3182 O OE2 . GLU B 1 170 ? -9.679  10.497  -38.802 1.00 43.48 ? 150 GLU B OE2 1 
ATOM   3183 N N   . LEU B 1 171 ? -3.941  9.985   -37.539 1.00 22.21 ? 151 LEU B N   1 
ATOM   3184 C CA  . LEU B 1 171 ? -2.673  9.402   -38.064 1.00 22.06 ? 151 LEU B CA  1 
ATOM   3185 C C   . LEU B 1 171 ? -2.105  8.409   -37.051 1.00 21.70 ? 151 LEU B C   1 
ATOM   3186 O O   . LEU B 1 171 ? -1.780  7.265   -37.448 1.00 19.28 ? 151 LEU B O   1 
ATOM   3187 C CB  . LEU B 1 171 ? -1.652  10.496  -38.379 1.00 23.88 ? 151 LEU B CB  1 
ATOM   3188 C CG  . LEU B 1 171 ? -0.351  9.997   -39.015 1.00 24.33 ? 151 LEU B CG  1 
ATOM   3189 C CD1 . LEU B 1 171 ? -0.642  9.364   -40.370 1.00 23.75 ? 151 LEU B CD1 1 
ATOM   3190 C CD2 . LEU B 1 171 ? 0.695   11.107  -39.120 1.00 23.67 ? 151 LEU B CD2 1 
ATOM   3191 N N   . LEU B 1 172 ? -2.025  8.812   -35.785 1.00 21.65 ? 152 LEU B N   1 
ATOM   3192 C CA  . LEU B 1 172 ? -1.383  8.004   -34.717 1.00 21.72 ? 152 LEU B CA  1 
ATOM   3193 C C   . LEU B 1 172 ? -2.195  6.726   -34.472 1.00 22.44 ? 152 LEU B C   1 
ATOM   3194 O O   . LEU B 1 172 ? -1.594  5.753   -33.982 1.00 21.82 ? 152 LEU B O   1 
ATOM   3195 C CB  . LEU B 1 172 ? -1.260  8.827   -33.431 1.00 22.53 ? 152 LEU B CB  1 
ATOM   3196 C CG  . LEU B 1 172 ? -0.098  9.819   -33.373 1.00 23.30 ? 152 LEU B CG  1 
ATOM   3197 C CD1 . LEU B 1 172 ? -0.207  10.720  -32.151 1.00 22.34 ? 152 LEU B CD1 1 
ATOM   3198 C CD2 . LEU B 1 172 ? 1.243   9.102   -33.378 1.00 24.19 ? 152 LEU B CD2 1 
ATOM   3199 N N   . SER B 1 173 ? -3.494  6.695   -34.793 1.00 20.19 ? 153 SER B N   1 
ATOM   3200 C CA  . SER B 1 173 ? -4.318  5.485   -34.555 1.00 20.86 ? 153 SER B CA  1 
ATOM   3201 C C   . SER B 1 173 ? -3.740  4.332   -35.389 1.00 21.44 ? 153 SER B C   1 
ATOM   3202 O O   . SER B 1 173 ? -3.823  3.194   -34.950 1.00 21.55 ? 153 SER B O   1 
ATOM   3203 C CB  . SER B 1 173 ? -5.802  5.705   -34.819 1.00 20.31 ? 153 SER B CB  1 
ATOM   3204 O OG  . SER B 1 173 ? -6.028  6.079   -36.167 1.00 19.63 ? 153 SER B OG  1 
ATOM   3205 N N   . SER B 1 174 ? -3.104  4.627   -36.521 1.00 24.18 ? 154 SER B N   1 
ATOM   3206 C CA  . SER B 1 174 ? -2.445  3.609   -37.389 1.00 26.34 ? 154 SER B CA  1 
ATOM   3207 C C   . SER B 1 174 ? -1.455  2.746   -36.589 1.00 26.13 ? 154 SER B C   1 
ATOM   3208 O O   . SER B 1 174 ? -1.242  1.592   -37.006 1.00 25.58 ? 154 SER B O   1 
ATOM   3209 C CB  . SER B 1 174 ? -1.782  4.236   -38.592 1.00 26.32 ? 154 SER B CB  1 
ATOM   3210 O OG  . SER B 1 174 ? -0.624  4.955   -38.232 1.00 27.74 ? 154 SER B OG  1 
ATOM   3211 N N   . ILE B 1 175 ? -0.888  3.233   -35.476 1.00 24.81 ? 155 ILE B N   1 
ATOM   3212 C CA  . ILE B 1 175 ? 0.096   2.419   -34.701 1.00 25.18 ? 155 ILE B CA  1 
ATOM   3213 C C   . ILE B 1 175 ? -0.571  1.760   -33.490 1.00 26.61 ? 155 ILE B C   1 
ATOM   3214 O O   . ILE B 1 175 ? 0.139   1.026   -32.783 1.00 24.79 ? 155 ILE B O   1 
ATOM   3215 C CB  . ILE B 1 175 ? 1.351   3.220   -34.308 1.00 25.68 ? 155 ILE B CB  1 
ATOM   3216 C CG1 . ILE B 1 175 ? 1.106   4.313   -33.265 1.00 25.69 ? 155 ILE B CG1 1 
ATOM   3217 C CG2 . ILE B 1 175 ? 2.040   3.784   -35.529 1.00 26.14 ? 155 ILE B CG2 1 
ATOM   3218 C CD1 . ILE B 1 175 ? 2.402   4.829   -32.649 1.00 25.52 ? 155 ILE B CD1 1 
ATOM   3219 N N   . GLY B 1 176 ? -1.875  1.967   -33.272 1.00 27.42 ? 156 GLY B N   1 
ATOM   3220 C CA  . GLY B 1 176 ? -2.618  1.332   -32.166 1.00 26.73 ? 156 GLY B CA  1 
ATOM   3221 C C   . GLY B 1 176 ? -3.414  2.356   -31.373 1.00 27.66 ? 156 GLY B C   1 
ATOM   3222 O O   . GLY B 1 176 ? -3.963  3.273   -31.993 1.00 27.95 ? 156 GLY B O   1 
ATOM   3223 N N   . THR B 1 177 ? -3.466  2.205   -30.050 1.00 28.45 ? 157 THR B N   1 
ATOM   3224 C CA  . THR B 1 177 ? -4.231  3.068   -29.112 1.00 27.96 ? 157 THR B CA  1 
ATOM   3225 C C   . THR B 1 177 ? -3.279  4.094   -28.490 1.00 28.23 ? 157 THR B C   1 
ATOM   3226 O O   . THR B 1 177 ? -2.336  3.668   -27.798 1.00 26.12 ? 157 THR B O   1 
ATOM   3227 C CB  . THR B 1 177 ? -4.922  2.207   -28.052 1.00 28.21 ? 157 THR B CB  1 
ATOM   3228 O OG1 . THR B 1 177 ? -5.848  1.413   -28.779 1.00 28.96 ? 157 THR B OG1 1 
ATOM   3229 C CG2 . THR B 1 177 ? -5.666  2.986   -26.991 1.00 29.88 ? 157 THR B CG2 1 
ATOM   3230 N N   . THR B 1 178 ? -3.520  5.387   -28.726 1.00 25.68 ? 158 THR B N   1 
ATOM   3231 C CA  . THR B 1 178 ? -2.762  6.492   -28.087 1.00 24.54 ? 158 THR B CA  1 
ATOM   3232 C C   . THR B 1 178 ? -3.456  6.908   -26.792 1.00 24.46 ? 158 THR B C   1 
ATOM   3233 O O   . THR B 1 178 ? -4.698  6.842   -26.732 1.00 29.48 ? 158 THR B O   1 
ATOM   3234 C CB  . THR B 1 178 ? -2.604  7.684   -29.031 1.00 23.97 ? 158 THR B CB  1 
ATOM   3235 O OG1 . THR B 1 178 ? -3.906  8.043   -29.487 1.00 22.63 ? 158 THR B OG1 1 
ATOM   3236 C CG2 . THR B 1 178 ? -1.685  7.367   -30.187 1.00 24.17 ? 158 THR B CG2 1 
ATOM   3237 N N   . ARG B 1 179 ? -2.667  7.279   -25.788 1.00 24.54 ? 159 ARG B N   1 
ATOM   3238 C CA  . ARG B 1 179 ? -3.141  7.853   -24.503 1.00 24.33 ? 159 ARG B CA  1 
ATOM   3239 C C   . ARG B 1 179 ? -2.374  9.154   -24.264 1.00 22.13 ? 159 ARG B C   1 
ATOM   3240 O O   . ARG B 1 179 ? -1.146  9.067   -24.038 1.00 21.26 ? 159 ARG B O   1 
ATOM   3241 C CB  . ARG B 1 179 ? -2.953  6.849   -23.364 1.00 25.51 ? 159 ARG B CB  1 
ATOM   3242 C CG  . ARG B 1 179 ? -3.162  7.427   -21.970 1.00 28.74 ? 159 ARG B CG  1 
ATOM   3243 C CD  . ARG B 1 179 ? -3.341  6.311   -20.962 1.00 32.57 ? 159 ARG B CD  1 
ATOM   3244 N NE  . ARG B 1 179 ? -3.896  6.719   -19.676 1.00 35.13 ? 159 ARG B NE  1 
ATOM   3245 C CZ  . ARG B 1 179 ? -4.209  5.875   -18.687 1.00 36.64 ? 159 ARG B CZ  1 
ATOM   3246 N NH1 . ARG B 1 179 ? -4.706  6.344   -17.555 1.00 39.45 ? 159 ARG B NH1 1 
ATOM   3247 N NH2 . ARG B 1 179 ? -3.997  4.570   -18.812 1.00 36.28 ? 159 ARG B NH2 1 
ATOM   3248 N N   . HIS B 1 180 ? -3.060  10.304  -24.366 1.00 20.98 ? 160 HIS B N   1 
ATOM   3249 C CA  . HIS B 1 180 ? -2.500  11.647  -24.043 1.00 19.35 ? 160 HIS B CA  1 
ATOM   3250 C C   . HIS B 1 180 ? -2.360  11.757  -22.522 1.00 17.30 ? 160 HIS B C   1 
ATOM   3251 O O   . HIS B 1 180 ? -3.389  11.820  -21.839 1.00 17.05 ? 160 HIS B O   1 
ATOM   3252 C CB  . HIS B 1 180 ? -3.363  12.779  -24.609 1.00 19.39 ? 160 HIS B CB  1 
ATOM   3253 C CG  . HIS B 1 180 ? -2.709  14.118  -24.513 1.00 19.06 ? 160 HIS B CG  1 
ATOM   3254 N ND1 . HIS B 1 180 ? -3.249  15.156  -23.799 1.00 20.76 ? 160 HIS B ND1 1 
ATOM   3255 C CD2 . HIS B 1 180 ? -1.579  14.602  -25.070 1.00 18.79 ? 160 HIS B CD2 1 
ATOM   3256 C CE1 . HIS B 1 180 ? -2.463  16.217  -23.898 1.00 20.89 ? 160 HIS B CE1 1 
ATOM   3257 N NE2 . HIS B 1 180 ? -1.430  15.905  -24.674 1.00 17.84 ? 160 HIS B NE2 1 
ATOM   3258 N N   . VAL B 1 181 ? -1.134  11.718  -22.014 1.00 16.03 ? 161 VAL B N   1 
ATOM   3259 C CA  . VAL B 1 181 ? -0.846  11.653  -20.553 1.00 16.19 ? 161 VAL B CA  1 
ATOM   3260 C C   . VAL B 1 181 ? -0.676  13.076  -20.002 1.00 16.78 ? 161 VAL B C   1 
ATOM   3261 O O   . VAL B 1 181 ? -0.930  13.280  -18.763 1.00 15.13 ? 161 VAL B O   1 
ATOM   3262 C CB  . VAL B 1 181 ? 0.368   10.757  -20.241 1.00 16.80 ? 161 VAL B CB  1 
ATOM   3263 C CG1 . VAL B 1 181 ? 0.038   9.290   -20.500 1.00 16.20 ? 161 VAL B CG1 1 
ATOM   3264 C CG2 . VAL B 1 181 ? 1.626   11.182  -20.996 1.00 17.28 ? 161 VAL B CG2 1 
ATOM   3265 N N   . SER B 1 182 ? -0.308  14.046  -20.852 1.00 14.81 ? 162 SER B N   1 
ATOM   3266 C CA  . SER B 1 182 ? 0.048   15.403  -20.369 1.00 15.15 ? 162 SER B CA  1 
ATOM   3267 C C   . SER B 1 182 ? 0.346   16.345  -21.539 1.00 14.15 ? 162 SER B C   1 
ATOM   3268 O O   . SER B 1 182 ? 0.726   15.845  -22.603 1.00 13.41 ? 162 SER B O   1 
ATOM   3269 C CB  . SER B 1 182 ? 1.228   15.296  -19.428 1.00 15.50 ? 162 SER B CB  1 
ATOM   3270 O OG  . SER B 1 182 ? 1.688   16.563  -19.006 1.00 14.33 ? 162 SER B OG  1 
ATOM   3271 N N   . ASP B 1 183 ? 0.206   17.654  -21.317 1.00 13.80 ? 163 ASP B N   1 
ATOM   3272 C CA  . ASP B 1 183 ? 0.609   18.712  -22.279 1.00 15.06 ? 163 ASP B CA  1 
ATOM   3273 C C   . ASP B 1 183 ? 2.123   18.934  -22.177 1.00 15.14 ? 163 ASP B C   1 
ATOM   3274 O O   . ASP B 1 183 ? 2.684   19.513  -23.118 1.00 16.02 ? 163 ASP B O   1 
ATOM   3275 C CB  . ASP B 1 183 ? -0.171  20.026  -22.092 1.00 15.34 ? 163 ASP B CB  1 
ATOM   3276 C CG  . ASP B 1 183 ? -1.454  20.078  -22.936 1.00 16.09 ? 163 ASP B CG  1 
ATOM   3277 O OD1 . ASP B 1 183 ? -2.358  19.255  -22.659 1.00 16.54 ? 163 ASP B OD1 1 
ATOM   3278 O OD2 . ASP B 1 183 ? -1.504  20.862  -23.911 1.00 13.37 ? 163 ASP B OD2 1 
ATOM   3279 N N   . ASP B 1 184 ? 2.747   18.506  -21.080 1.00 15.01 ? 164 ASP B N   1 
ATOM   3280 C CA  . ASP B 1 184 ? 4.214   18.623  -20.881 1.00 15.35 ? 164 ASP B CA  1 
ATOM   3281 C C   . ASP B 1 184 ? 4.906   17.560  -21.750 1.00 15.29 ? 164 ASP B C   1 
ATOM   3282 O O   . ASP B 1 184 ? 4.668   16.372  -21.517 1.00 13.12 ? 164 ASP B O   1 
ATOM   3283 C CB  . ASP B 1 184 ? 4.539   18.487  -19.401 1.00 16.35 ? 164 ASP B CB  1 
ATOM   3284 C CG  . ASP B 1 184 ? 6.024   18.489  -19.088 1.00 18.08 ? 164 ASP B CG  1 
ATOM   3285 O OD1 . ASP B 1 184 ? 6.851   18.435  -20.026 1.00 18.98 ? 164 ASP B OD1 1 
ATOM   3286 O OD2 . ASP B 1 184 ? 6.330   18.528  -17.907 1.00 22.14 ? 164 ASP B OD2 1 
ATOM   3287 N N   . ILE B 1 185 ? 5.747   17.965  -22.703 1.00 15.49 ? 165 ILE B N   1 
ATOM   3288 C CA  . ILE B 1 185 ? 6.353   17.022  -23.694 1.00 16.74 ? 165 ILE B CA  1 
ATOM   3289 C C   . ILE B 1 185 ? 7.175   15.937  -22.983 1.00 16.49 ? 165 ILE B C   1 
ATOM   3290 O O   . ILE B 1 185 ? 7.340   14.883  -23.581 1.00 16.53 ? 165 ILE B O   1 
ATOM   3291 C CB  . ILE B 1 185 ? 7.193   17.744  -24.761 1.00 18.08 ? 165 ILE B CB  1 
ATOM   3292 C CG1 . ILE B 1 185 ? 8.474   18.344  -24.179 1.00 20.21 ? 165 ILE B CG1 1 
ATOM   3293 C CG2 . ILE B 1 185 ? 6.380   18.787  -25.507 1.00 19.01 ? 165 ILE B CG2 1 
ATOM   3294 C CD1 . ILE B 1 185 ? 9.674   17.480  -24.425 1.00 21.30 ? 165 ILE B CD1 1 
ATOM   3295 N N   . ALA B 1 186 ? 7.698   16.188  -21.780 1.00 16.49 ? 166 ALA B N   1 
ATOM   3296 C CA  . ALA B 1 186 ? 8.653   15.283  -21.083 1.00 18.21 ? 166 ALA B CA  1 
ATOM   3297 C C   . ALA B 1 186 ? 7.946   14.122  -20.340 1.00 17.49 ? 166 ALA B C   1 
ATOM   3298 O O   . ALA B 1 186 ? 8.677   13.213  -19.845 1.00 17.93 ? 166 ALA B O   1 
ATOM   3299 C CB  . ALA B 1 186 ? 9.518   16.090  -20.129 1.00 17.92 ? 166 ALA B CB  1 
ATOM   3300 N N   . LYS B 1 187 ? 6.609   14.110  -20.272 1.00 16.60 ? 167 LYS B N   1 
ATOM   3301 C CA  . LYS B 1 187 ? 5.832   13.170  -19.416 1.00 17.22 ? 167 LYS B CA  1 
ATOM   3302 C C   . LYS B 1 187 ? 5.763   11.755  -19.999 1.00 14.75 ? 167 LYS B C   1 
ATOM   3303 O O   . LYS B 1 187 ? 5.753   10.835  -19.197 1.00 14.23 ? 167 LYS B O   1 
ATOM   3304 C CB  . LYS B 1 187 ? 4.427   13.701  -19.124 1.00 19.47 ? 167 LYS B CB  1 
ATOM   3305 C CG  . LYS B 1 187 ? 4.376   14.852  -18.131 1.00 22.49 ? 167 LYS B CG  1 
ATOM   3306 C CD  . LYS B 1 187 ? 5.188   14.609  -16.879 1.00 25.29 ? 167 LYS B CD  1 
ATOM   3307 C CE  . LYS B 1 187 ? 5.040   15.703  -15.844 1.00 27.64 ? 167 LYS B CE  1 
ATOM   3308 N NZ  . LYS B 1 187 ? 6.276   15.819  -15.031 1.00 28.72 ? 167 LYS B NZ  1 
ATOM   3309 N N   . ALA B 1 188 ? 5.692   11.553  -21.313 1.00 13.51 ? 168 ALA B N   1 
ATOM   3310 C CA  . ALA B 1 188 ? 5.656   10.167  -21.847 1.00 12.48 ? 168 ALA B CA  1 
ATOM   3311 C C   . ALA B 1 188 ? 6.937   9.455   -21.416 1.00 11.58 ? 168 ALA B C   1 
ATOM   3312 O O   . ALA B 1 188 ? 6.868   8.286   -20.973 1.00 11.06 ? 168 ALA B O   1 
ATOM   3313 C CB  . ALA B 1 188 ? 5.483   10.155  -23.344 1.00 11.54 ? 168 ALA B CB  1 
ATOM   3314 N N   . SER B 1 189 ? 8.086   10.115  -21.563 1.00 11.02 ? 169 SER B N   1 
ATOM   3315 C CA  . SER B 1 189 ? 9.396   9.517   -21.193 1.00 10.95 ? 169 SER B CA  1 
ATOM   3316 C C   . SER B 1 189 ? 9.448   9.271   -19.679 1.00 11.32 ? 169 SER B C   1 
ATOM   3317 O O   . SER B 1 189 ? 9.891   8.156   -19.267 1.00 10.48 ? 169 SER B O   1 
ATOM   3318 C CB  . SER B 1 189 ? 10.545  10.346  -21.685 1.00 11.05 ? 169 SER B CB  1 
ATOM   3319 O OG  . SER B 1 189 ? 10.636  10.268  -23.111 1.00 11.32 ? 169 SER B OG  1 
ATOM   3320 N N   . LEU B 1 190 ? 8.962   10.219  -18.870 1.00 11.68 ? 170 LEU B N   1 
ATOM   3321 C CA  . LEU B 1 190 ? 8.989   10.058  -17.389 1.00 12.50 ? 170 LEU B CA  1 
ATOM   3322 C C   . LEU B 1 190 ? 8.198   8.806   -17.029 1.00 13.46 ? 170 LEU B C   1 
ATOM   3323 O O   . LEU B 1 190 ? 8.775   7.940   -16.345 1.00 12.17 ? 170 LEU B O   1 
ATOM   3324 C CB  . LEU B 1 190 ? 8.417   11.273  -16.658 1.00 12.49 ? 170 LEU B CB  1 
ATOM   3325 C CG  . LEU B 1 190 ? 8.305   11.056  -15.152 1.00 12.61 ? 170 LEU B CG  1 
ATOM   3326 C CD1 . LEU B 1 190 ? 9.668   11.268  -14.503 1.00 12.42 ? 170 LEU B CD1 1 
ATOM   3327 C CD2 . LEU B 1 190 ? 7.219   11.931  -14.518 1.00 13.14 ? 170 LEU B CD2 1 
ATOM   3328 N N   . LEU B 1 191 ? 6.956   8.705   -17.547 1.00 14.50 ? 171 LEU B N   1 
ATOM   3329 C CA  . LEU B 1 191 ? 6.039   7.607   -17.206 1.00 15.01 ? 171 LEU B CA  1 
ATOM   3330 C C   . LEU B 1 191 ? 6.616   6.297   -17.744 1.00 14.78 ? 171 LEU B C   1 
ATOM   3331 O O   . LEU B 1 191 ? 6.616   5.335   -16.985 1.00 14.66 ? 171 LEU B O   1 
ATOM   3332 C CB  . LEU B 1 191 ? 4.634   7.881   -17.743 1.00 16.68 ? 171 LEU B CB  1 
ATOM   3333 C CG  . LEU B 1 191 ? 3.878   8.982   -16.993 1.00 19.01 ? 171 LEU B CG  1 
ATOM   3334 C CD1 . LEU B 1 191 ? 2.496   9.189   -17.585 1.00 21.34 ? 171 LEU B CD1 1 
ATOM   3335 C CD2 . LEU B 1 191 ? 3.744   8.657   -15.512 1.00 18.71 ? 171 LEU B CD2 1 
ATOM   3336 N N   . ASP B 1 192 ? 7.088   6.270   -18.990 1.00 14.94 ? 172 ASP B N   1 
ATOM   3337 C CA  . ASP B 1 192 ? 7.546   5.016   -19.632 1.00 16.12 ? 172 ASP B CA  1 
ATOM   3338 C C   . ASP B 1 192 ? 8.789   4.515   -18.891 1.00 15.98 ? 172 ASP B C   1 
ATOM   3339 O O   . ASP B 1 192 ? 8.878   3.306   -18.673 1.00 16.65 ? 172 ASP B O   1 
ATOM   3340 C CB  . ASP B 1 192 ? 7.735   5.161   -21.143 1.00 16.31 ? 172 ASP B CB  1 
ATOM   3341 C CG  . ASP B 1 192 ? 7.890   3.828   -21.868 1.00 16.66 ? 172 ASP B CG  1 
ATOM   3342 O OD1 . ASP B 1 192 ? 7.173   2.857   -21.508 1.00 17.36 ? 172 ASP B OD1 1 
ATOM   3343 O OD2 . ASP B 1 192 ? 8.722   3.767   -22.777 1.00 16.24 ? 172 ASP B OD2 1 
ATOM   3344 N N   . ASN B 1 193 ? 9.690   5.408   -18.485 1.00 16.52 ? 173 ASN B N   1 
ATOM   3345 C CA  . ASN B 1 193 ? 10.871  5.038   -17.664 1.00 17.15 ? 173 ASN B CA  1 
ATOM   3346 C C   . ASN B 1 193 ? 10.387  4.480   -16.323 1.00 17.00 ? 173 ASN B C   1 
ATOM   3347 O O   . ASN B 1 193 ? 10.959  3.480   -15.881 1.00 17.79 ? 173 ASN B O   1 
ATOM   3348 C CB  . ASN B 1 193 ? 11.841  6.210   -17.506 1.00 19.08 ? 173 ASN B CB  1 
ATOM   3349 C CG  . ASN B 1 193 ? 12.764  6.297   -18.695 1.00 20.22 ? 173 ASN B CG  1 
ATOM   3350 O OD1 . ASN B 1 193 ? 13.748  5.575   -18.746 1.00 24.55 ? 173 ASN B OD1 1 
ATOM   3351 N ND2 . ASN B 1 193 ? 12.419  7.107   -19.680 1.00 20.29 ? 173 ASN B ND2 1 
ATOM   3352 N N   . ALA B 1 194 ? 9.361   5.072   -15.704 1.00 15.97 ? 174 ALA B N   1 
ATOM   3353 C CA  . ALA B 1 194 ? 8.832   4.539   -14.427 1.00 15.87 ? 174 ALA B CA  1 
ATOM   3354 C C   . ALA B 1 194 ? 8.308   3.121   -14.673 1.00 16.14 ? 174 ALA B C   1 
ATOM   3355 O O   . ALA B 1 194 ? 8.588   2.251   -13.831 1.00 15.24 ? 174 ALA B O   1 
ATOM   3356 C CB  . ALA B 1 194 ? 7.784   5.431   -13.815 1.00 14.83 ? 174 ALA B CB  1 
ATOM   3357 N N   . LEU B 1 195 ? 7.608   2.895   -15.790 1.00 14.91 ? 175 LEU B N   1 
ATOM   3358 C CA  . LEU B 1 195 ? 6.923   1.607   -16.046 1.00 15.78 ? 175 LEU B CA  1 
ATOM   3359 C C   . LEU B 1 195 ? 7.980   0.553   -16.347 1.00 15.38 ? 175 LEU B C   1 
ATOM   3360 O O   . LEU B 1 195 ? 7.825   -0.596  -15.906 1.00 15.57 ? 175 LEU B O   1 
ATOM   3361 C CB  . LEU B 1 195 ? 5.922   1.756   -17.201 1.00 15.26 ? 175 LEU B CB  1 
ATOM   3362 C CG  . LEU B 1 195 ? 4.652   2.516   -16.847 1.00 16.12 ? 175 LEU B CG  1 
ATOM   3363 C CD1 . LEU B 1 195 ? 3.895   2.950   -18.092 1.00 16.54 ? 175 LEU B CD1 1 
ATOM   3364 C CD2 . LEU B 1 195 ? 3.746   1.689   -15.944 1.00 16.71 ? 175 LEU B CD2 1 
ATOM   3365 N N   . LEU B 1 196 ? 9.032   0.954   -17.056 1.00 14.91 ? 176 LEU B N   1 
ATOM   3366 C CA  . LEU B 1 196 ? 10.155  0.054   -17.410 1.00 15.27 ? 176 LEU B CA  1 
ATOM   3367 C C   . LEU B 1 196 ? 10.943  -0.350  -16.155 1.00 15.74 ? 176 LEU B C   1 
ATOM   3368 O O   . LEU B 1 196 ? 11.469  -1.493  -16.141 1.00 15.17 ? 176 LEU B O   1 
ATOM   3369 C CB  . LEU B 1 196 ? 11.032  0.745   -18.453 1.00 14.67 ? 176 LEU B CB  1 
ATOM   3370 C CG  . LEU B 1 196 ? 10.470  0.724   -19.867 1.00 15.15 ? 176 LEU B CG  1 
ATOM   3371 C CD1 . LEU B 1 196 ? 11.184  1.746   -20.737 1.00 15.21 ? 176 LEU B CD1 1 
ATOM   3372 C CD2 . LEU B 1 196 ? 10.586  -0.662  -20.484 1.00 16.65 ? 176 LEU B CD2 1 
ATOM   3373 N N   . SER B 1 197 ? 10.992  0.497   -15.120 1.00 15.96 ? 177 SER B N   1 
ATOM   3374 C CA  . SER B 1 197 ? 11.593  0.129   -13.808 1.00 16.43 ? 177 SER B CA  1 
ATOM   3375 C C   . SER B 1 197 ? 10.858  -1.097  -13.250 1.00 17.19 ? 177 SER B C   1 
ATOM   3376 O O   . SER B 1 197 ? 11.527  -2.068  -12.864 1.00 16.26 ? 177 SER B O   1 
ATOM   3377 C CB  . SER B 1 197 ? 11.557  1.269   -12.831 1.00 16.70 ? 177 SER B CB  1 
ATOM   3378 O OG  . SER B 1 197 ? 12.231  2.394   -13.361 1.00 18.84 ? 177 SER B OG  1 
ATOM   3379 N N   . VAL B 1 198 ? 9.527   -1.022  -13.179 1.00 17.66 ? 178 VAL B N   1 
ATOM   3380 C CA  . VAL B 1 198 ? 8.653   -2.107  -12.652 1.00 19.59 ? 178 VAL B CA  1 
ATOM   3381 C C   . VAL B 1 198 ? 8.936   -3.401  -13.420 1.00 19.54 ? 178 VAL B C   1 
ATOM   3382 O O   . VAL B 1 198 ? 9.163   -4.438  -12.775 1.00 18.93 ? 178 VAL B O   1 
ATOM   3383 C CB  . VAL B 1 198 ? 7.156   -1.755  -12.781 1.00 20.63 ? 178 VAL B CB  1 
ATOM   3384 C CG1 . VAL B 1 198 ? 6.310   -2.877  -12.195 1.00 23.13 ? 178 VAL B CG1 1 
ATOM   3385 C CG2 . VAL B 1 198 ? 6.816   -0.414  -12.159 1.00 19.36 ? 178 VAL B CG2 1 
ATOM   3386 N N   . MET B 1 199 ? 8.836   -3.332  -14.749 1.00 21.13 ? 179 MET B N   1 
ATOM   3387 C CA  . MET B 1 199 ? 9.032   -4.469  -15.687 1.00 23.80 ? 179 MET B CA  1 
ATOM   3388 C C   . MET B 1 199 ? 10.426  -5.067  -15.449 1.00 20.67 ? 179 MET B C   1 
ATOM   3389 O O   . MET B 1 199 ? 10.534  -6.291  -15.302 1.00 18.71 ? 179 MET B O   1 
ATOM   3390 C CB  . MET B 1 199 ? 8.902   -3.999  -17.142 1.00 25.99 ? 179 MET B CB  1 
ATOM   3391 C CG  . MET B 1 199 ? 9.372   -5.028  -18.171 1.00 33.87 ? 179 MET B CG  1 
ATOM   3392 S SD  . MET B 1 199 ? 9.385   -4.448  -19.924 1.00 44.78 ? 179 MET B SD  1 
ATOM   3393 C CE  . MET B 1 199 ? 11.120  -4.036  -20.139 1.00 41.03 ? 179 MET B CE  1 
ATOM   3394 N N   . SER B 1 200 ? 11.450  -4.224  -15.440 1.00 19.11 ? 180 SER B N   1 
ATOM   3395 C CA  . SER B 1 200 ? 12.865  -4.614  -15.185 1.00 18.96 ? 180 SER B CA  1 
ATOM   3396 C C   . SER B 1 200 ? 12.993  -5.359  -13.849 1.00 16.69 ? 180 SER B C   1 
ATOM   3397 O O   . SER B 1 200 ? 13.640  -6.404  -13.823 1.00 16.12 ? 180 SER B O   1 
ATOM   3398 C CB  . SER B 1 200 ? 13.769  -3.409  -15.208 1.00 19.86 ? 180 SER B CB  1 
ATOM   3399 O OG  . SER B 1 200 ? 13.758  -2.804  -16.486 1.00 19.98 ? 180 SER B OG  1 
ATOM   3400 N N   . GLY B 1 201 ? 12.365  -4.850  -12.798 1.00 15.18 ? 181 GLY B N   1 
ATOM   3401 C CA  . GLY B 1 201 ? 12.343  -5.490  -11.478 1.00 15.45 ? 181 GLY B CA  1 
ATOM   3402 C C   . GLY B 1 201 ? 11.726  -6.868  -11.551 1.00 16.23 ? 181 GLY B C   1 
ATOM   3403 O O   . GLY B 1 201 ? 12.323  -7.833  -11.020 1.00 15.66 ? 181 GLY B O   1 
ATOM   3404 N N   . VAL B 1 202 ? 10.606  -6.968  -12.260 1.00 16.45 ? 182 VAL B N   1 
ATOM   3405 C CA  . VAL B 1 202 ? 9.822   -8.215  -12.363 1.00 17.46 ? 182 VAL B CA  1 
ATOM   3406 C C   . VAL B 1 202 ? 10.705  -9.253  -13.050 1.00 17.81 ? 182 VAL B C   1 
ATOM   3407 O O   . VAL B 1 202 ? 10.757  -10.378 -12.574 1.00 18.86 ? 182 VAL B O   1 
ATOM   3408 C CB  . VAL B 1 202 ? 8.512   -7.978  -13.125 1.00 16.45 ? 182 VAL B CB  1 
ATOM   3409 C CG1 . VAL B 1 202 ? 7.840   -9.278  -13.491 1.00 18.05 ? 182 VAL B CG1 1 
ATOM   3410 C CG2 . VAL B 1 202 ? 7.584   -7.086  -12.318 1.00 18.09 ? 182 VAL B CG2 1 
ATOM   3411 N N   . PHE B 1 203 ? 11.360  -8.862  -14.133 1.00 18.53 ? 183 PHE B N   1 
ATOM   3412 C CA  . PHE B 1 203 ? 12.210  -9.757  -14.958 1.00 18.50 ? 183 PHE B CA  1 
ATOM   3413 C C   . PHE B 1 203 ? 13.420  -10.192 -14.135 1.00 16.51 ? 183 PHE B C   1 
ATOM   3414 O O   . PHE B 1 203 ? 13.737  -11.358 -14.227 1.00 16.57 ? 183 PHE B O   1 
ATOM   3415 C CB  . PHE B 1 203 ? 12.604  -9.102  -16.286 1.00 19.83 ? 183 PHE B CB  1 
ATOM   3416 C CG  . PHE B 1 203 ? 11.469  -8.990  -17.282 1.00 22.33 ? 183 PHE B CG  1 
ATOM   3417 C CD1 . PHE B 1 203 ? 10.384  -9.852  -17.238 1.00 23.77 ? 183 PHE B CD1 1 
ATOM   3418 C CD2 . PHE B 1 203 ? 11.482  -8.015  -18.262 1.00 23.85 ? 183 PHE B CD2 1 
ATOM   3419 C CE1 . PHE B 1 203 ? 9.334   -9.727  -18.140 1.00 25.91 ? 183 PHE B CE1 1 
ATOM   3420 C CE2 . PHE B 1 203 ? 10.445  -7.908  -19.175 1.00 23.92 ? 183 PHE B CE2 1 
ATOM   3421 C CZ  . PHE B 1 203 ? 9.371   -8.758  -19.107 1.00 23.48 ? 183 PHE B CZ  1 
ATOM   3422 N N   . GLU B 1 204 ? 14.037  -9.292  -13.368 1.00 15.80 ? 184 GLU B N   1 
ATOM   3423 C CA  . GLU B 1 204 ? 15.235  -9.609  -12.532 1.00 15.56 ? 184 GLU B CA  1 
ATOM   3424 C C   . GLU B 1 204 ? 14.852  -10.728 -11.553 1.00 14.89 ? 184 GLU B C   1 
ATOM   3425 O O   . GLU B 1 204 ? 15.558  -11.739 -11.521 1.00 14.19 ? 184 GLU B O   1 
ATOM   3426 C CB  . GLU B 1 204 ? 15.741  -8.387  -11.777 1.00 15.66 ? 184 GLU B CB  1 
ATOM   3427 C CG  . GLU B 1 204 ? 17.051  -8.627  -11.039 1.00 17.89 ? 184 GLU B CG  1 
ATOM   3428 C CD  . GLU B 1 204 ? 17.580  -7.478  -10.181 1.00 19.85 ? 184 GLU B CD  1 
ATOM   3429 O OE1 . GLU B 1 204 ? 18.740  -7.525  -9.749  1.00 19.70 ? 184 GLU B OE1 1 
ATOM   3430 O OE2 . GLU B 1 204 ? 16.806  -6.558  -9.910  1.00 26.19 ? 184 GLU B OE2 1 
ATOM   3431 N N   . GLY B 1 205 ? 13.743  -10.562 -10.820 1.00 14.34 ? 185 GLY B N   1 
ATOM   3432 C CA  . GLY B 1 205 ? 13.269  -11.552 -9.840  1.00 14.83 ? 185 GLY B CA  1 
ATOM   3433 C C   . GLY B 1 205 ? 12.917  -12.871 -10.501 1.00 15.10 ? 185 GLY B C   1 
ATOM   3434 O O   . GLY B 1 205 ? 13.199  -13.917 -9.888  1.00 14.35 ? 185 GLY B O   1 
ATOM   3435 N N   . TRP B 1 206 ? 12.312  -12.807 -11.701 1.00 15.57 ? 186 TRP B N   1 
ATOM   3436 C CA  . TRP B 1 206 ? 11.834  -13.975 -12.479 1.00 17.27 ? 186 TRP B CA  1 
ATOM   3437 C C   . TRP B 1 206 ? 13.020  -14.790 -13.013 1.00 15.92 ? 186 TRP B C   1 
ATOM   3438 O O   . TRP B 1 206 ? 13.010  -16.035 -12.889 1.00 15.33 ? 186 TRP B O   1 
ATOM   3439 C CB  . TRP B 1 206 ? 10.909  -13.524 -13.620 1.00 19.82 ? 186 TRP B CB  1 
ATOM   3440 C CG  . TRP B 1 206 ? 10.189  -14.659 -14.274 1.00 21.48 ? 186 TRP B CG  1 
ATOM   3441 C CD1 . TRP B 1 206 ? 10.224  -15.014 -15.588 1.00 23.66 ? 186 TRP B CD1 1 
ATOM   3442 C CD2 . TRP B 1 206 ? 9.304   -15.597 -13.636 1.00 23.93 ? 186 TRP B CD2 1 
ATOM   3443 N NE1 . TRP B 1 206 ? 9.423   -16.105 -15.810 1.00 23.42 ? 186 TRP B NE1 1 
ATOM   3444 C CE2 . TRP B 1 206 ? 8.850   -16.485 -14.629 1.00 24.29 ? 186 TRP B CE2 1 
ATOM   3445 C CE3 . TRP B 1 206 ? 8.850   -15.768 -12.325 1.00 27.10 ? 186 TRP B CE3 1 
ATOM   3446 C CZ2 . TRP B 1 206 ? 7.962   -17.519 -14.353 1.00 26.54 ? 186 TRP B CZ2 1 
ATOM   3447 C CZ3 . TRP B 1 206 ? 7.972   -16.792 -12.048 1.00 27.86 ? 186 TRP B CZ3 1 
ATOM   3448 C CH2 . TRP B 1 206 ? 7.536   -17.656 -13.052 1.00 28.22 ? 186 TRP B CH2 1 
ATOM   3449 N N   . VAL B 1 207 ? 14.016  -14.124 -13.588 1.00 13.59 ? 187 VAL B N   1 
ATOM   3450 C CA  . VAL B 1 207 ? 15.266  -14.824 -14.011 1.00 13.35 ? 187 VAL B CA  1 
ATOM   3451 C C   . VAL B 1 207 ? 15.887  -15.546 -12.799 1.00 13.53 ? 187 VAL B C   1 
ATOM   3452 O O   . VAL B 1 207 ? 16.235  -16.780 -12.919 1.00 12.73 ? 187 VAL B O   1 
ATOM   3453 C CB  . VAL B 1 207 ? 16.215  -13.825 -14.691 1.00 12.76 ? 187 VAL B CB  1 
ATOM   3454 C CG1 . VAL B 1 207 ? 17.646  -14.348 -14.785 1.00 12.46 ? 187 VAL B CG1 1 
ATOM   3455 C CG2 . VAL B 1 207 ? 15.631  -13.472 -16.060 1.00 12.43 ? 187 VAL B CG2 1 
ATOM   3456 N N   . GLN B 1 208 ? 15.972  -14.855 -11.654 1.00 13.41 ? 188 GLN B N   1 
ATOM   3457 C CA  . GLN B 1 208 ? 16.578  -15.444 -10.438 1.00 13.42 ? 188 GLN B CA  1 
ATOM   3458 C C   . GLN B 1 208 ? 15.784  -16.707 -10.050 1.00 13.03 ? 188 GLN B C   1 
ATOM   3459 O O   . GLN B 1 208 ? 16.409  -17.734 -9.833  1.00 13.26 ? 188 GLN B O   1 
ATOM   3460 C CB  . GLN B 1 208 ? 16.611  -14.440 -9.293  1.00 13.41 ? 188 GLN B CB  1 
ATOM   3461 C CG  . GLN B 1 208 ? 17.243  -15.021 -8.037  1.00 13.88 ? 188 GLN B CG  1 
ATOM   3462 C CD  . GLN B 1 208 ? 18.731  -15.130 -8.232  1.00 14.93 ? 188 GLN B CD  1 
ATOM   3463 O OE1 . GLN B 1 208 ? 19.377  -14.128 -8.534  1.00 17.51 ? 188 GLN B OE1 1 
ATOM   3464 N NE2 . GLN B 1 208 ? 19.265  -16.339 -8.124  1.00 13.30 ? 188 GLN B NE2 1 
ATOM   3465 N N   . ALA B 1 209 ? 14.450  -16.611 -10.008 1.00 12.11 ? 189 ALA B N   1 
ATOM   3466 C CA  . ALA B 1 209 ? 13.522  -17.683 -9.630  1.00 12.19 ? 189 ALA B CA  1 
ATOM   3467 C C   . ALA B 1 209 ? 13.727  -18.877 -10.555 1.00 12.96 ? 189 ALA B C   1 
ATOM   3468 O O   . ALA B 1 209 ? 13.783  -20.027 -10.051 1.00 12.12 ? 189 ALA B O   1 
ATOM   3469 C CB  . ALA B 1 209 ? 12.108  -17.172 -9.697  1.00 12.74 ? 189 ALA B CB  1 
ATOM   3470 N N   . LEU B 1 210 ? 13.785  -18.633 -11.866 1.00 13.84 ? 190 LEU B N   1 
ATOM   3471 C CA  . LEU B 1 210 ? 13.858  -19.737 -12.844 1.00 14.35 ? 190 LEU B CA  1 
ATOM   3472 C C   . LEU B 1 210 ? 15.258  -20.357 -12.784 1.00 14.05 ? 190 LEU B C   1 
ATOM   3473 O O   . LEU B 1 210 ? 15.343  -21.568 -12.850 1.00 16.34 ? 190 LEU B O   1 
ATOM   3474 C CB  . LEU B 1 210 ? 13.454  -19.234 -14.233 1.00 14.74 ? 190 LEU B CB  1 
ATOM   3475 C CG  . LEU B 1 210 ? 11.967  -18.903 -14.383 1.00 16.38 ? 190 LEU B CG  1 
ATOM   3476 C CD1 . LEU B 1 210 ? 11.677  -18.383 -15.782 1.00 17.86 ? 190 LEU B CD1 1 
ATOM   3477 C CD2 . LEU B 1 210 ? 11.105  -20.110 -14.051 1.00 16.52 ? 190 LEU B CD2 1 
ATOM   3478 N N   . ALA B 1 211 ? 16.311  -19.584 -12.595 1.00 14.52 ? 191 ALA B N   1 
ATOM   3479 C CA  . ALA B 1 211 ? 17.675  -20.147 -12.397 1.00 14.62 ? 191 ALA B CA  1 
ATOM   3480 C C   . ALA B 1 211 ? 17.648  -21.136 -11.216 1.00 14.98 ? 191 ALA B C   1 
ATOM   3481 O O   . ALA B 1 211 ? 18.058  -22.308 -11.422 1.00 14.69 ? 191 ALA B O   1 
ATOM   3482 C CB  . ALA B 1 211 ? 18.667  -19.055 -12.182 1.00 14.20 ? 191 ALA B CB  1 
ATOM   3483 N N   . ILE B 1 212 ? 17.115  -20.723 -10.053 1.00 14.69 ? 192 ILE B N   1 
ATOM   3484 C CA  . ILE B 1 212 ? 17.023  -21.575 -8.822  1.00 16.25 ? 192 ILE B CA  1 
ATOM   3485 C C   . ILE B 1 212 ? 16.238  -22.859 -9.149  1.00 18.36 ? 192 ILE B C   1 
ATOM   3486 O O   . ILE B 1 212 ? 16.736  -23.966 -8.872  1.00 17.74 ? 192 ILE B O   1 
ATOM   3487 C CB  . ILE B 1 212 ? 16.375  -20.787 -7.660  1.00 17.42 ? 192 ILE B CB  1 
ATOM   3488 C CG1 . ILE B 1 212 ? 17.274  -19.635 -7.195  1.00 17.51 ? 192 ILE B CG1 1 
ATOM   3489 C CG2 . ILE B 1 212 ? 16.010  -21.709 -6.505  1.00 17.03 ? 192 ILE B CG2 1 
ATOM   3490 C CD1 . ILE B 1 212 ? 16.615  -18.652 -6.280  1.00 16.71 ? 192 ILE B CD1 1 
ATOM   3491 N N   . VAL B 1 213 ? 15.023  -22.707 -9.695  1.00 18.61 ? 193 VAL B N   1 
ATOM   3492 C CA  . VAL B 1 213 ? 14.084  -23.825 -9.992  1.00 18.45 ? 193 VAL B CA  1 
ATOM   3493 C C   . VAL B 1 213 ? 14.767  -24.787 -10.983 1.00 16.99 ? 193 VAL B C   1 
ATOM   3494 O O   . VAL B 1 213 ? 14.810  -26.001 -10.720 1.00 15.20 ? 193 VAL B O   1 
ATOM   3495 C CB  . VAL B 1 213 ? 12.735  -23.249 -10.466 1.00 19.56 ? 193 VAL B CB  1 
ATOM   3496 C CG1 . VAL B 1 213 ? 11.883  -24.236 -11.236 1.00 22.50 ? 193 VAL B CG1 1 
ATOM   3497 C CG2 . VAL B 1 213 ? 11.942  -22.711 -9.296  1.00 20.78 ? 193 VAL B CG2 1 
ATOM   3498 N N   . GLY B 1 214 ? 15.346  -24.257 -12.051 1.00 16.78 ? 194 GLY B N   1 
ATOM   3499 C CA  . GLY B 1 214 ? 16.050  -25.049 -13.076 1.00 18.57 ? 194 GLY B CA  1 
ATOM   3500 C C   . GLY B 1 214 ? 17.212  -25.852 -12.500 1.00 18.54 ? 194 GLY B C   1 
ATOM   3501 O O   . GLY B 1 214 ? 17.275  -27.100 -12.740 1.00 16.97 ? 194 GLY B O   1 
ATOM   3502 N N   . ALA B 1 215 ? 18.091  -25.192 -11.749 1.00 18.08 ? 195 ALA B N   1 
ATOM   3503 C CA  . ALA B 1 215 ? 19.274  -25.840 -11.147 1.00 18.80 ? 195 ALA B CA  1 
ATOM   3504 C C   . ALA B 1 215 ? 18.858  -26.905 -10.115 1.00 20.44 ? 195 ALA B C   1 
ATOM   3505 O O   . ALA B 1 215 ? 19.642  -27.865 -9.925  1.00 20.06 ? 195 ALA B O   1 
ATOM   3506 C CB  . ALA B 1 215 ? 20.179  -24.805 -10.549 1.00 19.77 ? 195 ALA B CB  1 
ATOM   3507 N N   . ALA B 1 216 ? 17.682  -26.787 -9.492  1.00 19.31 ? 196 ALA B N   1 
ATOM   3508 C CA  . ALA B 1 216 ? 17.199  -27.754 -8.481  1.00 21.24 ? 196 ALA B CA  1 
ATOM   3509 C C   . ALA B 1 216 ? 16.534  -28.965 -9.157  1.00 23.34 ? 196 ALA B C   1 
ATOM   3510 O O   . ALA B 1 216 ? 16.088  -29.870 -8.431  1.00 22.78 ? 196 ALA B O   1 
ATOM   3511 C CB  . ALA B 1 216 ? 16.262  -27.080 -7.513  1.00 21.11 ? 196 ALA B CB  1 
ATOM   3512 N N   . GLY B 1 217 ? 16.486  -29.002 -10.494 1.00 23.98 ? 197 GLY B N   1 
ATOM   3513 C CA  . GLY B 1 217 ? 15.883  -30.100 -11.263 1.00 23.45 ? 197 GLY B CA  1 
ATOM   3514 C C   . GLY B 1 217 ? 14.378  -29.951 -11.324 1.00 23.48 ? 197 GLY B C   1 
ATOM   3515 O O   . GLY B 1 217 ? 13.714  -30.913 -11.683 1.00 26.45 ? 197 GLY B O   1 
ATOM   3516 N N   . GLU B 1 218 ? 13.834  -28.776 -11.018 1.00 23.57 ? 198 GLU B N   1 
ATOM   3517 C CA  . GLU B 1 218 ? 12.361  -28.562 -11.062 1.00 23.02 ? 198 GLU B CA  1 
ATOM   3518 C C   . GLU B 1 218 ? 11.955  -28.121 -12.472 1.00 22.58 ? 198 GLU B C   1 
ATOM   3519 O O   . GLU B 1 218 ? 12.850  -27.856 -13.331 1.00 20.72 ? 198 GLU B O   1 
ATOM   3520 C CB  . GLU B 1 218 ? 11.921  -27.566 -9.987  1.00 26.15 ? 198 GLU B CB  1 
ATOM   3521 C CG  . GLU B 1 218 ? 12.106  -28.072 -8.572  1.00 28.17 ? 198 GLU B CG  1 
ATOM   3522 C CD  . GLU B 1 218 ? 11.322  -29.330 -8.228  1.00 33.54 ? 198 GLU B CD  1 
ATOM   3523 O OE1 . GLU B 1 218 ? 11.935  -30.273 -7.646  1.00 35.45 ? 198 GLU B OE1 1 
ATOM   3524 O OE2 . GLU B 1 218 ? 10.102  -29.377 -8.549  1.00 35.09 ? 198 GLU B OE2 1 
ATOM   3525 N N   . ASP B 1 219 ? 10.649  -28.097 -12.717 1.00 21.49 ? 199 ASP B N   1 
ATOM   3526 C CA  . ASP B 1 219 ? 10.060  -27.768 -14.034 1.00 22.61 ? 199 ASP B CA  1 
ATOM   3527 C C   . ASP B 1 219 ? 9.589   -26.311 -14.013 1.00 20.20 ? 199 ASP B C   1 
ATOM   3528 O O   . ASP B 1 219 ? 8.795   -25.962 -13.128 1.00 17.61 ? 199 ASP B O   1 
ATOM   3529 C CB  . ASP B 1 219 ? 8.915   -28.707 -14.398 1.00 24.58 ? 199 ASP B CB  1 
ATOM   3530 C CG  . ASP B 1 219 ? 8.469   -28.512 -15.839 1.00 24.27 ? 199 ASP B CG  1 
ATOM   3531 O OD1 . ASP B 1 219 ? 7.731   -27.564 -16.093 1.00 23.35 ? 199 ASP B OD1 1 
ATOM   3532 O OD2 . ASP B 1 219 ? 8.900   -29.297 -16.686 1.00 26.59 ? 199 ASP B OD2 1 
ATOM   3533 N N   . GLU B 1 220 ? 10.120  -25.516 -14.948 1.00 18.76 ? 200 GLU B N   1 
ATOM   3534 C CA  . GLU B 1 220 ? 9.960   -24.041 -15.042 1.00 18.82 ? 200 GLU B CA  1 
ATOM   3535 C C   . GLU B 1 220 ? 8.475   -23.731 -15.283 1.00 20.02 ? 200 GLU B C   1 
ATOM   3536 O O   . GLU B 1 220 ? 7.950   -22.765 -14.681 1.00 19.97 ? 200 GLU B O   1 
ATOM   3537 C CB  . GLU B 1 220 ? 10.878  -23.494 -16.143 1.00 18.11 ? 200 GLU B CB  1 
ATOM   3538 C CG  . GLU B 1 220 ? 12.347  -23.462 -15.750 1.00 18.61 ? 200 GLU B CG  1 
ATOM   3539 C CD  . GLU B 1 220 ? 13.145  -24.681 -16.162 1.00 20.40 ? 200 GLU B CD  1 
ATOM   3540 O OE1 . GLU B 1 220 ? 14.405  -24.619 -16.128 1.00 20.21 ? 200 GLU B OE1 1 
ATOM   3541 O OE2 . GLU B 1 220 ? 12.506  -25.680 -16.529 1.00 21.29 ? 200 GLU B OE2 1 
ATOM   3542 N N   . VAL B 1 221 ? 7.814   -24.561 -16.090 1.00 20.01 ? 201 VAL B N   1 
ATOM   3543 C CA  . VAL B 1 221 ? 6.414   -24.329 -16.545 1.00 21.63 ? 201 VAL B CA  1 
ATOM   3544 C C   . VAL B 1 221 ? 5.476   -24.580 -15.364 1.00 20.85 ? 201 VAL B C   1 
ATOM   3545 O O   . VAL B 1 221 ? 4.723   -23.671 -15.019 1.00 20.44 ? 201 VAL B O   1 
ATOM   3546 C CB  . VAL B 1 221 ? 6.082   -25.216 -17.761 1.00 22.39 ? 201 VAL B CB  1 
ATOM   3547 C CG1 . VAL B 1 221 ? 4.622   -25.045 -18.208 1.00 22.19 ? 201 VAL B CG1 1 
ATOM   3548 C CG2 . VAL B 1 221 ? 7.055   -24.926 -18.899 1.00 21.86 ? 201 VAL B CG2 1 
ATOM   3549 N N   . ASP B 1 222 ? 5.593   -25.748 -14.729 1.00 23.43 ? 202 ASP B N   1 
ATOM   3550 C CA  . ASP B 1 222 ? 4.921   -26.071 -13.438 1.00 22.34 ? 202 ASP B CA  1 
ATOM   3551 C C   . ASP B 1 222 ? 5.138   -24.953 -12.414 1.00 22.01 ? 202 ASP B C   1 
ATOM   3552 O O   . ASP B 1 222 ? 4.125   -24.535 -11.774 1.00 19.62 ? 202 ASP B O   1 
ATOM   3553 C CB  . ASP B 1 222 ? 5.449   -27.376 -12.850 1.00 23.99 ? 202 ASP B CB  1 
ATOM   3554 C CG  . ASP B 1 222 ? 5.066   -28.586 -13.679 1.00 25.65 ? 202 ASP B CG  1 
ATOM   3555 O OD1 . ASP B 1 222 ? 4.196   -28.445 -14.543 1.00 28.79 ? 202 ASP B OD1 1 
ATOM   3556 O OD2 . ASP B 1 222 ? 5.650   -29.639 -13.458 1.00 28.08 ? 202 ASP B OD2 1 
ATOM   3557 N N   . PHE B 1 223 ? 6.388   -24.486 -12.236 1.00 19.59 ? 203 PHE B N   1 
ATOM   3558 C CA  . PHE B 1 223 ? 6.681   -23.421 -11.238 1.00 19.88 ? 203 PHE B CA  1 
ATOM   3559 C C   . PHE B 1 223 ? 5.879   -22.167 -11.610 1.00 20.02 ? 203 PHE B C   1 
ATOM   3560 O O   . PHE B 1 223 ? 5.214   -21.588 -10.721 1.00 20.38 ? 203 PHE B O   1 
ATOM   3561 C CB  . PHE B 1 223 ? 8.175   -23.132 -11.066 1.00 18.25 ? 203 PHE B CB  1 
ATOM   3562 C CG  . PHE B 1 223 ? 8.437   -21.917 -10.211 1.00 17.92 ? 203 PHE B CG  1 
ATOM   3563 C CD1 . PHE B 1 223 ? 8.395   -21.995 -8.826  1.00 18.76 ? 203 PHE B CD1 1 
ATOM   3564 C CD2 . PHE B 1 223 ? 8.722   -20.691 -10.782 1.00 17.81 ? 203 PHE B CD2 1 
ATOM   3565 C CE1 . PHE B 1 223 ? 8.632   -20.885 -8.030  1.00 16.58 ? 203 PHE B CE1 1 
ATOM   3566 C CE2 . PHE B 1 223 ? 8.953   -19.580 -9.983  1.00 17.99 ? 203 PHE B CE2 1 
ATOM   3567 C CZ  . PHE B 1 223 ? 8.901   -19.673 -8.609  1.00 16.78 ? 203 PHE B CZ  1 
ATOM   3568 N N   . ALA B 1 224 ? 5.886   -21.770 -12.886 1.00 19.88 ? 204 ALA B N   1 
ATOM   3569 C CA  . ALA B 1 224 ? 5.131   -20.584 -13.345 1.00 20.03 ? 204 ALA B CA  1 
ATOM   3570 C C   . ALA B 1 224 ? 3.647   -20.752 -12.980 1.00 21.90 ? 204 ALA B C   1 
ATOM   3571 O O   . ALA B 1 224 ? 3.005   -19.733 -12.590 1.00 19.04 ? 204 ALA B O   1 
ATOM   3572 C CB  . ALA B 1 224 ? 5.333   -20.335 -14.815 1.00 19.99 ? 204 ALA B CB  1 
ATOM   3573 N N   . ALA B 1 225 ? 3.122   -21.980 -13.062 1.00 24.74 ? 205 ALA B N   1 
ATOM   3574 C CA  . ALA B 1 225 ? 1.707   -22.281 -12.728 1.00 27.87 ? 205 ALA B CA  1 
ATOM   3575 C C   . ALA B 1 225 ? 1.446   -21.880 -11.269 1.00 30.55 ? 205 ALA B C   1 
ATOM   3576 O O   . ALA B 1 225 ? 0.347   -21.386 -10.965 1.00 32.64 ? 205 ALA B O   1 
ATOM   3577 C CB  . ALA B 1 225 ? 1.392   -23.741 -12.981 1.00 27.98 ? 205 ALA B CB  1 
ATOM   3578 N N   . LEU B 1 226 ? 2.442   -22.094 -10.406 1.00 34.13 ? 206 LEU B N   1 
ATOM   3579 C CA  . LEU B 1 226 ? 2.414   -21.799 -8.952  1.00 34.14 ? 206 LEU B CA  1 
ATOM   3580 C C   . LEU B 1 226 ? 2.661   -20.299 -8.740  1.00 37.33 ? 206 LEU B C   1 
ATOM   3581 O O   . LEU B 1 226 ? 1.967   -19.707 -7.895  1.00 39.45 ? 206 LEU B O   1 
ATOM   3582 C CB  . LEU B 1 226 ? 3.514   -22.634 -8.288  1.00 36.48 ? 206 LEU B CB  1 
ATOM   3583 C CG  . LEU B 1 226 ? 3.245   -23.204 -6.895  1.00 37.55 ? 206 LEU B CG  1 
ATOM   3584 C CD1 . LEU B 1 226 ? 4.533   -23.211 -6.097  1.00 37.73 ? 206 LEU B CD1 1 
ATOM   3585 C CD2 . LEU B 1 226 ? 2.166   -22.452 -6.136  1.00 40.60 ? 206 LEU B CD2 1 
ATOM   3586 N N   . ALA B 1 227 ? 3.602   -19.708 -9.486  1.00 32.23 ? 207 ALA B N   1 
ATOM   3587 C CA  . ALA B 1 227 ? 4.151   -18.350 -9.250  1.00 34.62 ? 207 ALA B CA  1 
ATOM   3588 C C   . ALA B 1 227 ? 3.273   -17.254 -9.871  1.00 38.70 ? 207 ALA B C   1 
ATOM   3589 O O   . ALA B 1 227 ? 2.911   -16.284 -9.157  1.00 33.22 ? 207 ALA B O   1 
ATOM   3590 C CB  . ALA B 1 227 ? 5.551   -18.276 -9.795  1.00 32.35 ? 207 ALA B CB  1 
ATOM   3591 N N   . SER B 1 228 ? 2.997   -17.365 -11.171 1.00 44.00 ? 208 SER B N   1 
ATOM   3592 C CA  . SER B 1 228 ? 2.278   -16.343 -11.977 1.00 47.60 ? 208 SER B CA  1 
ATOM   3593 C C   . SER B 1 228 ? 1.032   -15.852 -11.238 1.00 48.10 ? 208 SER B C   1 
ATOM   3594 O O   . SER B 1 228 ? 0.804   -14.642 -11.180 1.00 49.54 ? 208 SER B O   1 
ATOM   3595 C CB  . SER B 1 228 ? 1.971   -16.859 -13.368 1.00 50.54 ? 208 SER B CB  1 
ATOM   3596 O OG  . SER B 1 228 ? 3.177   -17.135 -14.065 1.00 50.37 ? 208 SER B OG  1 
ATOM   3597 N N   . PRO B 1 229 ? 0.201   -16.751 -10.651 1.00 47.98 ? 209 PRO B N   1 
ATOM   3598 C CA  . PRO B 1 229 ? -0.904  -16.345 -9.777  1.00 47.02 ? 209 PRO B CA  1 
ATOM   3599 C C   . PRO B 1 229 ? -0.558  -15.341 -8.674  1.00 47.70 ? 209 PRO B C   1 
ATOM   3600 O O   . PRO B 1 229 ? -1.320  -14.412 -8.470  1.00 53.40 ? 209 PRO B O   1 
ATOM   3601 C CB  . PRO B 1 229 ? -1.302  -17.668 -9.100  1.00 47.42 ? 209 PRO B CB  1 
ATOM   3602 C CG  . PRO B 1 229 ? -1.061  -18.690 -10.185 1.00 47.41 ? 209 PRO B CG  1 
ATOM   3603 C CD  . PRO B 1 229 ? 0.204   -18.210 -10.874 1.00 47.69 ? 209 PRO B CD  1 
ATOM   3604 N N   . LEU B 1 230 ? 0.540   -15.574 -7.953  1.00 42.53 ? 210 LEU B N   1 
ATOM   3605 C CA  . LEU B 1 230 ? 0.945   -14.701 -6.826  1.00 39.74 ? 210 LEU B CA  1 
ATOM   3606 C C   . LEU B 1 230 ? 1.473   -13.362 -7.390  1.00 39.11 ? 210 LEU B C   1 
ATOM   3607 O O   . LEU B 1 230 ? 1.301   -12.326 -6.726  1.00 36.95 ? 210 LEU B O   1 
ATOM   3608 C CB  . LEU B 1 230 ? 1.950   -15.446 -5.932  1.00 41.03 ? 210 LEU B CB  1 
ATOM   3609 C CG  . LEU B 1 230 ? 1.402   -16.540 -4.991  1.00 41.70 ? 210 LEU B CG  1 
ATOM   3610 C CD1 . LEU B 1 230 ? -0.019  -16.253 -4.492  1.00 41.52 ? 210 LEU B CD1 1 
ATOM   3611 C CD2 . LEU B 1 230 ? 1.456   -17.927 -5.623  1.00 38.00 ? 210 LEU B CD2 1 
ATOM   3612 N N   . VAL B 1 231 ? 2.002   -13.333 -8.615  1.00 37.66 ? 211 VAL B N   1 
ATOM   3613 C CA  . VAL B 1 231 ? 2.428   -12.051 -9.253  1.00 39.10 ? 211 VAL B CA  1 
ATOM   3614 C C   . VAL B 1 231 ? 1.185   -11.265 -9.687  1.00 40.97 ? 211 VAL B C   1 
ATOM   3615 O O   . VAL B 1 231 ? 1.214   -10.024 -9.552  1.00 38.84 ? 211 VAL B O   1 
ATOM   3616 C CB  . VAL B 1 231 ? 3.411   -12.267 -10.416 1.00 40.44 ? 211 VAL B CB  1 
ATOM   3617 C CG1 . VAL B 1 231 ? 3.812   -10.943 -11.063 1.00 43.66 ? 211 VAL B CG1 1 
ATOM   3618 C CG2 . VAL B 1 231 ? 4.646   -13.025 -9.949  1.00 38.53 ? 211 VAL B CG2 1 
ATOM   3619 N N   . ALA B 1 232 ? 0.142   -11.953 -10.174 1.00 43.26 ? 212 ALA B N   1 
ATOM   3620 C CA  . ALA B 1 232 ? -1.215  -11.396 -10.395 1.00 41.60 ? 212 ALA B CA  1 
ATOM   3621 C C   . ALA B 1 232 ? -1.601  -10.576 -9.167  1.00 41.28 ? 212 ALA B C   1 
ATOM   3622 O O   . ALA B 1 232 ? -1.892  -9.376  -9.339  1.00 45.04 ? 212 ALA B O   1 
ATOM   3623 C CB  . ALA B 1 232 ? -2.238  -12.479 -10.648 1.00 40.86 ? 212 ALA B CB  1 
ATOM   3624 N N   . SER B 1 233 ? -1.554  -11.207 -7.985  1.00 42.92 ? 213 SER B N   1 
ATOM   3625 C CA  . SER B 1 233 ? -1.882  -10.622 -6.652  1.00 41.45 ? 213 SER B CA  1 
ATOM   3626 C C   . SER B 1 233 ? -1.308  -9.212  -6.492  1.00 40.34 ? 213 SER B C   1 
ATOM   3627 O O   . SER B 1 233 ? -1.965  -8.416  -5.817  1.00 37.12 ? 213 SER B O   1 
ATOM   3628 C CB  . SER B 1 233 ? -1.370  -11.466 -5.515  1.00 40.56 ? 213 SER B CB  1 
ATOM   3629 O OG  . SER B 1 233 ? -0.178  -10.894 -4.973  1.00 37.44 ? 213 SER B OG  1 
ATOM   3630 N N   . MET B 1 234 ? -0.085  -8.963  -6.981  1.00 42.05 ? 214 MET B N   1 
ATOM   3631 C CA  . MET B 1 234 ? 0.656   -7.682  -6.793  1.00 44.91 ? 214 MET B CA  1 
ATOM   3632 C C   . MET B 1 234 ? -0.130  -6.506  -7.357  1.00 42.30 ? 214 MET B C   1 
ATOM   3633 O O   . MET B 1 234 ? -0.051  -5.428  -6.743  1.00 43.25 ? 214 MET B O   1 
ATOM   3634 C CB  . MET B 1 234 ? 2.028   -7.710  -7.464  1.00 52.71 ? 214 MET B CB  1 
ATOM   3635 C CG  . MET B 1 234 ? 3.061   -8.390  -6.617  1.00 58.13 ? 214 MET B CG  1 
ATOM   3636 S SD  . MET B 1 234 ? 2.316   -9.451  -5.342  1.00 71.59 ? 214 MET B SD  1 
ATOM   3637 C CE  . MET B 1 234 ? 2.467   -8.407  -3.891  1.00 66.79 ? 214 MET B CE  1 
ATOM   3638 N N   . ALA B 1 235 ? -0.845  -6.705  -8.467  1.00 43.86 ? 215 ALA B N   1 
ATOM   3639 C CA  . ALA B 1 235 ? -1.820  -5.736  -9.024  1.00 42.15 ? 215 ALA B CA  1 
ATOM   3640 C C   . ALA B 1 235 ? -2.577  -5.078  -7.865  1.00 41.99 ? 215 ALA B C   1 
ATOM   3641 O O   . ALA B 1 235 ? -2.713  -3.845  -7.863  1.00 42.28 ? 215 ALA B O   1 
ATOM   3642 C CB  . ALA B 1 235 ? -2.762  -6.428  -9.981  1.00 41.74 ? 215 ALA B CB  1 
ATOM   3643 N N   . ASP B 1 236 ? -2.999  -5.884  -6.889  1.00 40.48 ? 216 ASP B N   1 
ATOM   3644 C CA  . ASP B 1 236 ? -3.742  -5.432  -5.682  1.00 44.89 ? 216 ASP B CA  1 
ATOM   3645 C C   . ASP B 1 236 ? -2.828  -4.636  -4.745  1.00 43.43 ? 216 ASP B C   1 
ATOM   3646 O O   . ASP B 1 236 ? -3.257  -3.568  -4.288  1.00 45.54 ? 216 ASP B O   1 
ATOM   3647 C CB  . ASP B 1 236 ? -4.360  -6.623  -4.950  1.00 46.04 ? 216 ASP B CB  1 
ATOM   3648 C CG  . ASP B 1 236 ? -5.260  -7.432  -5.863  1.00 49.65 ? 216 ASP B CG  1 
ATOM   3649 O OD1 . ASP B 1 236 ? -6.119  -6.808  -6.507  1.00 53.77 ? 216 ASP B OD1 1 
ATOM   3650 O OD2 . ASP B 1 236 ? -5.059  -8.662  -5.960  1.00 50.59 ? 216 ASP B OD2 1 
ATOM   3651 N N   . GLN B 1 237 ? -1.624  -5.136  -4.466  1.00 45.15 ? 217 GLN B N   1 
ATOM   3652 C CA  . GLN B 1 237 ? -0.748  -4.612  -3.384  1.00 44.87 ? 217 GLN B CA  1 
ATOM   3653 C C   . GLN B 1 237 ? 0.011   -3.352  -3.828  1.00 41.84 ? 217 GLN B C   1 
ATOM   3654 O O   . GLN B 1 237 ? 0.334   -2.537  -2.949  1.00 41.12 ? 217 GLN B O   1 
ATOM   3655 C CB  . GLN B 1 237 ? 0.188   -5.719  -2.901  1.00 50.97 ? 217 GLN B CB  1 
ATOM   3656 C CG  . GLN B 1 237 ? -0.276  -6.333  -1.585  1.00 60.95 ? 217 GLN B CG  1 
ATOM   3657 C CD  . GLN B 1 237 ? -0.157  -7.837  -1.519  1.00 69.04 ? 217 GLN B CD  1 
ATOM   3658 O OE1 . GLN B 1 237 ? 0.178   -8.406  -0.479  1.00 72.84 ? 217 GLN B OE1 1 
ATOM   3659 N NE2 . GLN B 1 237 ? -0.466  -8.497  -2.625  1.00 74.90 ? 217 GLN B NE2 1 
ATOM   3660 N N   . LEU B 1 238 ? 0.297   -3.176  -5.119  1.00 39.59 ? 218 LEU B N   1 
ATOM   3661 C CA  . LEU B 1 238 ? 1.159   -2.056  -5.596  1.00 38.67 ? 218 LEU B CA  1 
ATOM   3662 C C   . LEU B 1 238 ? 0.452   -0.720  -5.390  1.00 34.32 ? 218 LEU B C   1 
ATOM   3663 O O   . LEU B 1 238 ? 1.091   0.260   -5.020  1.00 33.29 ? 218 LEU B O   1 
ATOM   3664 C CB  . LEU B 1 238 ? 1.579   -2.276  -7.054  1.00 39.21 ? 218 LEU B CB  1 
ATOM   3665 C CG  . LEU B 1 238 ? 2.402   -3.539  -7.320  1.00 39.74 ? 218 LEU B CG  1 
ATOM   3666 C CD1 . LEU B 1 238 ? 2.704   -3.658  -8.800  1.00 41.40 ? 218 LEU B CD1 1 
ATOM   3667 C CD2 . LEU B 1 238 ? 3.694   -3.590  -6.508  1.00 39.81 ? 218 LEU B CD2 1 
ATOM   3668 N N   . PRO B 1 239 ? -0.874  -0.614  -5.623  1.00 34.35 ? 219 PRO B N   1 
ATOM   3669 C CA  . PRO B 1 239 ? -1.629  0.581   -5.255  1.00 34.13 ? 219 PRO B CA  1 
ATOM   3670 C C   . PRO B 1 239 ? -1.620  0.933   -3.761  1.00 36.15 ? 219 PRO B C   1 
ATOM   3671 O O   . PRO B 1 239 ? -1.624  2.111   -3.428  1.00 36.60 ? 219 PRO B O   1 
ATOM   3672 C CB  . PRO B 1 239 ? -3.073  0.215   -5.645  1.00 35.85 ? 219 PRO B CB  1 
ATOM   3673 C CG  . PRO B 1 239 ? -2.917  -0.778  -6.748  1.00 33.78 ? 219 PRO B CG  1 
ATOM   3674 C CD  . PRO B 1 239 ? -1.702  -1.583  -6.350  1.00 37.16 ? 219 PRO B CD  1 
ATOM   3675 N N   . VAL B 1 240 ? -1.690  -0.092  -2.906  1.00 35.61 ? 220 VAL B N   1 
ATOM   3676 C CA  . VAL B 1 240 ? -1.634  0.052   -1.425  1.00 33.65 ? 220 VAL B CA  1 
ATOM   3677 C C   . VAL B 1 240 ? -0.279  0.676   -1.083  1.00 29.63 ? 220 VAL B C   1 
ATOM   3678 O O   . VAL B 1 240 ? -0.258  1.681   -0.365  1.00 26.97 ? 220 VAL B O   1 
ATOM   3679 C CB  . VAL B 1 240 ? -1.859  -1.295  -0.704  1.00 36.39 ? 220 VAL B CB  1 
ATOM   3680 C CG1 . VAL B 1 240 ? -1.574  -1.198  0.783   1.00 37.83 ? 220 VAL B CG1 1 
ATOM   3681 C CG2 . VAL B 1 240 ? -3.266  -1.844  -0.927  1.00 37.61 ? 220 VAL B CG2 1 
ATOM   3682 N N   . ILE B 1 241 ? 0.815   0.111   -1.597  1.00 28.00 ? 221 ILE B N   1 
ATOM   3683 C CA  . ILE B 1 241 ? 2.192   0.606   -1.314  1.00 27.12 ? 221 ILE B CA  1 
ATOM   3684 C C   . ILE B 1 241 ? 2.298   2.066   -1.794  1.00 23.76 ? 221 ILE B C   1 
ATOM   3685 O O   . ILE B 1 241 ? 2.949   2.868   -1.124  1.00 23.75 ? 221 ILE B O   1 
ATOM   3686 C CB  . ILE B 1 241 ? 3.241   -0.304  -1.983  1.00 27.70 ? 221 ILE B CB  1 
ATOM   3687 C CG1 . ILE B 1 241 ? 3.237   -1.717  -1.393  1.00 30.20 ? 221 ILE B CG1 1 
ATOM   3688 C CG2 . ILE B 1 241 ? 4.619   0.324   -1.901  1.00 28.19 ? 221 ILE B CG2 1 
ATOM   3689 C CD1 . ILE B 1 241 ? 3.734   -2.778  -2.351  1.00 30.48 ? 221 ILE B CD1 1 
ATOM   3690 N N   . ALA B 1 242 ? 1.713   2.378   -2.945  1.00 23.86 ? 222 ALA B N   1 
ATOM   3691 C CA  . ALA B 1 242 ? 1.774   3.711   -3.598  1.00 25.06 ? 222 ALA B CA  1 
ATOM   3692 C C   . ALA B 1 242 ? 1.074   4.747   -2.714  1.00 25.57 ? 222 ALA B C   1 
ATOM   3693 O O   . ALA B 1 242 ? 1.602   5.860   -2.589  1.00 26.47 ? 222 ALA B O   1 
ATOM   3694 C CB  . ALA B 1 242 ? 1.139   3.656   -4.971  1.00 26.11 ? 222 ALA B CB  1 
ATOM   3695 N N   . GLY B 1 243 ? -0.080  4.378   -2.148  1.00 26.42 ? 223 GLY B N   1 
ATOM   3696 C CA  . GLY B 1 243 ? -0.848  5.214   -1.203  1.00 27.93 ? 223 GLY B CA  1 
ATOM   3697 C C   . GLY B 1 243 ? -0.038  5.534   0.035   1.00 26.65 ? 223 GLY B C   1 
ATOM   3698 O O   . GLY B 1 243 ? 0.020   6.714   0.419   1.00 24.79 ? 223 GLY B O   1 
ATOM   3699 N N   . ARG B 1 244 ? 0.612   4.517   0.603   1.00 27.33 ? 224 ARG B N   1 
ATOM   3700 C CA  . ARG B 1 244 ? 1.464   4.635   1.818   1.00 30.16 ? 224 ARG B CA  1 
ATOM   3701 C C   . ARG B 1 244 ? 2.624   5.583   1.542   1.00 28.05 ? 224 ARG B C   1 
ATOM   3702 O O   . ARG B 1 244 ? 2.945   6.380   2.423   1.00 26.60 ? 224 ARG B O   1 
ATOM   3703 C CB  . ARG B 1 244 ? 2.081   3.296   2.237   1.00 33.23 ? 224 ARG B CB  1 
ATOM   3704 C CG  . ARG B 1 244 ? 1.089   2.238   2.699   1.00 38.84 ? 224 ARG B CG  1 
ATOM   3705 C CD  . ARG B 1 244 ? 1.846   1.177   3.474   1.00 45.07 ? 224 ARG B CD  1 
ATOM   3706 N NE  . ARG B 1 244 ? 1.593   -0.202  3.082   1.00 50.58 ? 224 ARG B NE  1 
ATOM   3707 C CZ  . ARG B 1 244 ? 0.847   -1.081  3.758   1.00 51.87 ? 224 ARG B CZ  1 
ATOM   3708 N NH1 . ARG B 1 244 ? 0.714   -2.316  3.299   1.00 51.78 ? 224 ARG B NH1 1 
ATOM   3709 N NH2 . ARG B 1 244 ? 0.240   -0.734  4.879   1.00 50.48 ? 224 ARG B NH2 1 
ATOM   3710 N N   . VAL B 1 245 ? 3.280   5.418   0.391   1.00 26.20 ? 225 VAL B N   1 
ATOM   3711 C CA  . VAL B 1 245 ? 4.429   6.266   -0.030  1.00 24.10 ? 225 VAL B CA  1 
ATOM   3712 C C   . VAL B 1 245 ? 3.975   7.734   -0.113  1.00 22.48 ? 225 VAL B C   1 
ATOM   3713 O O   . VAL B 1 245 ? 4.675   8.585   0.421   1.00 21.15 ? 225 VAL B O   1 
ATOM   3714 C CB  . VAL B 1 245 ? 5.020   5.784   -1.366  1.00 23.80 ? 225 VAL B CB  1 
ATOM   3715 C CG1 . VAL B 1 245 ? 5.879   6.853   -2.000  1.00 23.89 ? 225 VAL B CG1 1 
ATOM   3716 C CG2 . VAL B 1 245 ? 5.816   4.496   -1.191  1.00 24.37 ? 225 VAL B CG2 1 
ATOM   3717 N N   . ARG B 1 246 ? 2.873   8.028   -0.788  1.00 23.44 ? 226 ARG B N   1 
ATOM   3718 C CA  . ARG B 1 246 ? 2.407   9.431   -0.940  1.00 26.66 ? 226 ARG B CA  1 
ATOM   3719 C C   . ARG B 1 246 ? 2.203   10.067  0.444   1.00 28.44 ? 226 ARG B C   1 
ATOM   3720 O O   . ARG B 1 246 ? 2.831   11.119  0.692   1.00 28.14 ? 226 ARG B O   1 
ATOM   3721 C CB  . ARG B 1 246 ? 1.110   9.517   -1.732  1.00 27.56 ? 226 ARG B CB  1 
ATOM   3722 C CG  . ARG B 1 246 ? 0.684   10.961  -1.970  1.00 29.19 ? 226 ARG B CG  1 
ATOM   3723 C CD  . ARG B 1 246 ? -0.455  11.031  -2.951  1.00 29.94 ? 226 ARG B CD  1 
ATOM   3724 N NE  . ARG B 1 246 ? -1.638  10.408  -2.383  1.00 32.14 ? 226 ARG B NE  1 
ATOM   3725 C CZ  . ARG B 1 246 ? -2.770  10.222  -3.044  1.00 32.22 ? 226 ARG B CZ  1 
ATOM   3726 N NH1 . ARG B 1 246 ? -2.865  10.610  -4.304  1.00 33.23 ? 226 ARG B NH1 1 
ATOM   3727 N NH2 . ARG B 1 246 ? -3.797  9.650   -2.442  1.00 32.08 ? 226 ARG B NH2 1 
ATOM   3728 N N   . GLU B 1 247 ? 1.438   9.405   1.332   1.00 30.62 ? 227 GLU B N   1 
ATOM   3729 C CA  . GLU B 1 247 ? 1.091   9.903   2.699   1.00 30.49 ? 227 GLU B CA  1 
ATOM   3730 C C   . GLU B 1 247 ? 2.296   9.770   3.647   1.00 31.53 ? 227 GLU B C   1 
ATOM   3731 O O   . GLU B 1 247 ? 2.157   10.154  4.804   1.00 31.90 ? 227 GLU B O   1 
ATOM   3732 C CB  . GLU B 1 247 ? -0.116  9.169   3.285   1.00 32.93 ? 227 GLU B CB  1 
ATOM   3733 C CG  . GLU B 1 247 ? -1.306  9.021   2.346   1.00 39.02 ? 227 GLU B CG  1 
ATOM   3734 C CD  . GLU B 1 247 ? -2.034  10.298  1.946   1.00 45.05 ? 227 GLU B CD  1 
ATOM   3735 O OE1 . GLU B 1 247 ? -1.380  11.360  1.853   1.00 45.53 ? 227 GLU B OE1 1 
ATOM   3736 O OE2 . GLU B 1 247 ? -3.266  10.226  1.722   1.00 48.93 ? 227 GLU B OE2 1 
ATOM   3737 N N   . LYS B 1 248 ? 3.437   9.254   3.174   1.00 33.63 ? 228 LYS B N   1 
ATOM   3738 C CA  . LYS B 1 248 ? 4.668   8.960   3.970   1.00 32.65 ? 228 LYS B CA  1 
ATOM   3739 C C   . LYS B 1 248 ? 4.307   8.144   5.225   1.00 30.91 ? 228 LYS B C   1 
ATOM   3740 O O   . LYS B 1 248 ? 4.785   8.484   6.321   1.00 33.55 ? 228 LYS B O   1 
ATOM   3741 C CB  . LYS B 1 248 ? 5.420   10.251  4.307   1.00 33.99 ? 228 LYS B CB  1 
ATOM   3742 C CG  . LYS B 1 248 ? 5.591   11.222  3.145   1.00 35.35 ? 228 LYS B CG  1 
ATOM   3743 C CD  . LYS B 1 248 ? 6.815   12.114  3.281   1.00 39.48 ? 228 LYS B CD  1 
ATOM   3744 C CE  . LYS B 1 248 ? 6.682   13.440  2.561   1.00 38.60 ? 228 LYS B CE  1 
ATOM   3745 N NZ  . LYS B 1 248 ? 6.214   13.265  1.165   1.00 40.99 ? 228 LYS B NZ  1 
ATOM   3746 N N   . GLN B 1 249 ? 3.492   7.103   5.050   1.00 25.85 ? 229 GLN B N   1 
ATOM   3747 C CA  . GLN B 1 249 ? 3.141   6.107   6.090   1.00 24.82 ? 229 GLN B CA  1 
ATOM   3748 C C   . GLN B 1 249 ? 4.001   4.850   5.875   1.00 22.69 ? 229 GLN B C   1 
ATOM   3749 O O   . GLN B 1 249 ? 3.537   3.955   5.172   1.00 22.22 ? 229 GLN B O   1 
ATOM   3750 C CB  . GLN B 1 249 ? 1.637   5.822   6.017   1.00 25.05 ? 229 GLN B CB  1 
ATOM   3751 C CG  . GLN B 1 249 ? 0.780   7.014   6.437   1.00 25.63 ? 229 GLN B CG  1 
ATOM   3752 C CD  . GLN B 1 249 ? 0.979   7.329   7.900   1.00 24.51 ? 229 GLN B CD  1 
ATOM   3753 O OE1 . GLN B 1 249 ? 0.617   6.544   8.765   1.00 24.08 ? 229 GLN B OE1 1 
ATOM   3754 N NE2 . GLN B 1 249 ? 1.578   8.472   8.192   1.00 21.99 ? 229 GLN B NE2 1 
ATOM   3755 N N   . TYR B 1 250 ? 5.211   4.808   6.451   1.00 22.58 ? 230 TYR B N   1 
ATOM   3756 C CA  . TYR B 1 250 ? 6.260   3.790   6.176   1.00 24.77 ? 230 TYR B CA  1 
ATOM   3757 C C   . TYR B 1 250 ? 6.079   2.590   7.111   1.00 26.98 ? 230 TYR B C   1 
ATOM   3758 O O   . TYR B 1 250 ? 6.698   1.541   6.854   1.00 26.79 ? 230 TYR B O   1 
ATOM   3759 C CB  . TYR B 1 250 ? 7.660   4.409   6.273   1.00 26.69 ? 230 TYR B CB  1 
ATOM   3760 C CG  . TYR B 1 250 ? 7.844   5.624   5.396   1.00 28.95 ? 230 TYR B CG  1 
ATOM   3761 C CD1 . TYR B 1 250 ? 7.348   5.654   4.099   1.00 28.94 ? 230 TYR B CD1 1 
ATOM   3762 C CD2 . TYR B 1 250 ? 8.509   6.750   5.858   1.00 31.50 ? 230 TYR B CD2 1 
ATOM   3763 C CE1 . TYR B 1 250 ? 7.505   6.769   3.291   1.00 30.03 ? 230 TYR B CE1 1 
ATOM   3764 C CE2 . TYR B 1 250 ? 8.670   7.877   5.064   1.00 31.59 ? 230 TYR B CE2 1 
ATOM   3765 C CZ  . TYR B 1 250 ? 8.152   7.888   3.782   1.00 30.39 ? 230 TYR B CZ  1 
ATOM   3766 O OH  . TYR B 1 250 ? 8.286   8.997   3.004   1.00 31.30 ? 230 TYR B OH  1 
ATOM   3767 N N   . VAL B 1 251 ? 5.229   2.736   8.136   1.00 28.27 ? 231 VAL B N   1 
ATOM   3768 C CA  . VAL B 1 251 ? 4.886   1.679   9.132   1.00 27.14 ? 231 VAL B CA  1 
ATOM   3769 C C   . VAL B 1 251 ? 3.596   0.993   8.679   1.00 24.66 ? 231 VAL B C   1 
ATOM   3770 O O   . VAL B 1 251 ? 2.677   1.684   8.232   1.00 22.95 ? 231 VAL B O   1 
ATOM   3771 C CB  . VAL B 1 251 ? 4.783   2.271   10.553  1.00 28.32 ? 231 VAL B CB  1 
ATOM   3772 C CG1 . VAL B 1 251 ? 3.998   1.367   11.489  1.00 30.42 ? 231 VAL B CG1 1 
ATOM   3773 C CG2 . VAL B 1 251 ? 6.161   2.569   11.126  1.00 29.61 ? 231 VAL B CG2 1 
ATOM   3774 N N   . GLY B 1 252 ? 3.557   -0.331  8.769   1.00 25.88 ? 232 GLY B N   1 
ATOM   3775 C CA  . GLY B 1 252 ? 2.453   -1.164  8.253   1.00 28.79 ? 232 GLY B CA  1 
ATOM   3776 C C   . GLY B 1 252 ? 2.890   -1.923  7.007   1.00 29.97 ? 232 GLY B C   1 
ATOM   3777 O O   . GLY B 1 252 ? 3.251   -1.266  6.006   1.00 34.15 ? 232 GLY B O   1 
ATOM   3778 N N   . GLY B 1 253 ? 2.879   -3.255  7.073   1.00 30.39 ? 233 GLY B N   1 
ATOM   3779 C CA  . GLY B 1 253 ? 3.418   -4.159  6.038   1.00 29.87 ? 233 GLY B CA  1 
ATOM   3780 C C   . GLY B 1 253 ? 4.674   -4.877  6.520   1.00 29.46 ? 233 GLY B C   1 
ATOM   3781 O O   . GLY B 1 253 ? 5.345   -4.369  7.447   1.00 30.91 ? 233 GLY B O   1 
ATOM   3782 N N   . SER B 1 254 ? 4.998   -6.012  5.904   1.00 26.85 ? 234 SER B N   1 
ATOM   3783 C CA  . SER B 1 254 ? 6.164   -6.852  6.264   1.00 25.42 ? 234 SER B CA  1 
ATOM   3784 C C   . SER B 1 254 ? 7.393   -5.965  6.420   1.00 23.05 ? 234 SER B C   1 
ATOM   3785 O O   . SER B 1 254 ? 7.701   -5.119  5.576   1.00 23.65 ? 234 SER B O   1 
ATOM   3786 C CB  . SER B 1 254 ? 6.379   -7.951  5.255   1.00 27.68 ? 234 SER B CB  1 
ATOM   3787 O OG  . SER B 1 254 ? 7.545   -8.690  5.591   1.00 31.41 ? 234 SER B OG  1 
ATOM   3788 N N   . PRO B 1 255 ? 8.124   -6.088  7.540   1.00 20.94 ? 235 PRO B N   1 
ATOM   3789 C CA  . PRO B 1 255 ? 9.262   -5.214  7.785   1.00 20.19 ? 235 PRO B CA  1 
ATOM   3790 C C   . PRO B 1 255 ? 10.422  -5.437  6.808   1.00 18.88 ? 235 PRO B C   1 
ATOM   3791 O O   . PRO B 1 255 ? 10.633  -6.552  6.330   1.00 17.65 ? 235 PRO B O   1 
ATOM   3792 C CB  . PRO B 1 255 ? 9.701   -5.551  9.214   1.00 20.35 ? 235 PRO B CB  1 
ATOM   3793 C CG  . PRO B 1 255 ? 9.181   -6.955  9.429   1.00 21.65 ? 235 PRO B CG  1 
ATOM   3794 C CD  . PRO B 1 255 ? 7.884   -7.023  8.645   1.00 21.46 ? 235 PRO B CD  1 
ATOM   3795 N N   . ILE B 1 256 ? 11.183  -4.372  6.601   1.00 17.97 ? 236 ILE B N   1 
ATOM   3796 C CA  . ILE B 1 256 ? 12.412  -4.390  5.768   1.00 19.19 ? 236 ILE B CA  1 
ATOM   3797 C C   . ILE B 1 256 ? 13.386  -5.445  6.305   1.00 18.78 ? 236 ILE B C   1 
ATOM   3798 O O   . ILE B 1 256 ? 14.000  -6.099  5.490   1.00 18.68 ? 236 ILE B O   1 
ATOM   3799 C CB  . ILE B 1 256 ? 13.043  -2.993  5.678   1.00 18.27 ? 236 ILE B CB  1 
ATOM   3800 C CG1 . ILE B 1 256 ? 12.270  -2.106  4.699   1.00 19.97 ? 236 ILE B CG1 1 
ATOM   3801 C CG2 . ILE B 1 256 ? 14.502  -3.101  5.290   1.00 18.65 ? 236 ILE B CG2 1 
ATOM   3802 C CD1 . ILE B 1 256 ? 12.525  -0.632  4.881   1.00 20.84 ? 236 ILE B CD1 1 
ATOM   3803 N N   . THR B 1 257 ? 13.571  -5.582  7.618   1.00 19.71 ? 237 THR B N   1 
ATOM   3804 C CA  . THR B 1 257 ? 14.464  -6.637  8.189   1.00 21.78 ? 237 THR B CA  1 
ATOM   3805 C C   . THR B 1 257 ? 14.061  -8.020  7.657   1.00 21.49 ? 237 THR B C   1 
ATOM   3806 O O   . THR B 1 257 ? 14.947  -8.870  7.441   1.00 19.75 ? 237 THR B O   1 
ATOM   3807 C CB  . THR B 1 257 ? 14.433  -6.649  9.726   1.00 22.65 ? 237 THR B CB  1 
ATOM   3808 O OG1 . THR B 1 257 ? 13.063  -6.516  10.134  1.00 23.31 ? 237 THR B OG1 1 
ATOM   3809 C CG2 . THR B 1 257 ? 15.282  -5.535  10.293  1.00 22.77 ? 237 THR B CG2 1 
ATOM   3810 N N   . MET B 1 258 ? 12.761  -8.244  7.486   1.00 22.23 ? 238 MET B N   1 
ATOM   3811 C CA  . MET B 1 258 ? 12.202  -9.544  7.045   1.00 23.39 ? 238 MET B CA  1 
ATOM   3812 C C   . MET B 1 258 ? 12.559  -9.717  5.568   1.00 21.60 ? 238 MET B C   1 
ATOM   3813 O O   . MET B 1 258 ? 12.969  -10.812 5.183   1.00 19.66 ? 238 MET B O   1 
ATOM   3814 C CB  . MET B 1 258 ? 10.684  -9.551  7.228   1.00 26.03 ? 238 MET B CB  1 
ATOM   3815 C CG  . MET B 1 258 ? 10.016  -10.802 6.772   1.00 30.88 ? 238 MET B CG  1 
ATOM   3816 S SD  . MET B 1 258 ? 9.375   -11.710 8.178   1.00 39.37 ? 238 MET B SD  1 
ATOM   3817 C CE  . MET B 1 258 ? 10.938  -12.291 8.837   1.00 31.11 ? 238 MET B CE  1 
ATOM   3818 N N   . GLY B 1 259 ? 12.434  -8.636  4.801   1.00 19.76 ? 239 GLY B N   1 
ATOM   3819 C CA  . GLY B 1 259 ? 12.699  -8.609  3.352   1.00 18.85 ? 239 GLY B CA  1 
ATOM   3820 C C   . GLY B 1 259 ? 14.170  -8.864  3.106   1.00 19.17 ? 239 GLY B C   1 
ATOM   3821 O O   . GLY B 1 259 ? 14.489  -9.600  2.160   1.00 18.09 ? 239 GLY B O   1 
ATOM   3822 N N   . LEU B 1 260 ? 15.042  -8.280  3.934   1.00 18.52 ? 240 LEU B N   1 
ATOM   3823 C CA  . LEU B 1 260 ? 16.510  -8.476  3.796   1.00 19.44 ? 240 LEU B CA  1 
ATOM   3824 C C   . LEU B 1 260 ? 16.851  -9.943  4.119   1.00 18.37 ? 240 LEU B C   1 
ATOM   3825 O O   . LEU B 1 260 ? 17.533  -10.560 3.286   1.00 18.00 ? 240 LEU B O   1 
ATOM   3826 C CB  . LEU B 1 260 ? 17.232  -7.477  4.698   1.00 20.08 ? 240 LEU B CB  1 
ATOM   3827 C CG  . LEU B 1 260 ? 18.757  -7.507  4.673   1.00 20.76 ? 240 LEU B CG  1 
ATOM   3828 C CD1 . LEU B 1 260 ? 19.270  -7.281  3.266   1.00 21.02 ? 240 LEU B CD1 1 
ATOM   3829 C CD2 . LEU B 1 260 ? 19.330  -6.449  5.631   1.00 22.05 ? 240 LEU B CD2 1 
ATOM   3830 N N   . GLU B 1 261 ? 16.299  -10.523 5.188   1.00 18.55 ? 241 GLU B N   1 
ATOM   3831 C CA  . GLU B 1 261 ? 16.534  -11.960 5.506   1.00 20.00 ? 241 GLU B CA  1 
ATOM   3832 C C   . GLU B 1 261 ? 16.130  -12.813 4.313   1.00 18.79 ? 241 GLU B C   1 
ATOM   3833 O O   . GLU B 1 261 ? 16.910  -13.743 3.971   1.00 19.47 ? 241 GLU B O   1 
ATOM   3834 C CB  . GLU B 1 261 ? 15.746  -12.533 6.689   1.00 22.74 ? 241 GLU B CB  1 
ATOM   3835 C CG  . GLU B 1 261 ? 16.584  -12.947 7.893   1.00 27.27 ? 241 GLU B CG  1 
ATOM   3836 C CD  . GLU B 1 261 ? 17.929  -13.637 7.707   1.00 27.47 ? 241 GLU B CD  1 
ATOM   3837 O OE1 . GLU B 1 261 ? 18.911  -12.932 7.456   1.00 33.64 ? 241 GLU B OE1 1 
ATOM   3838 O OE2 . GLU B 1 261 ? 18.001  -14.872 7.869   1.00 31.34 ? 241 GLU B OE2 1 
ATOM   3839 N N   . ALA B 1 262 ? 14.913  -12.599 3.792   1.00 16.97 ? 242 ALA B N   1 
ATOM   3840 C CA  . ALA B 1 262 ? 14.457  -13.242 2.544   1.00 15.66 ? 242 ALA B CA  1 
ATOM   3841 C C   . ALA B 1 262 ? 15.586  -13.212 1.497   1.00 15.30 ? 242 ALA B C   1 
ATOM   3842 O O   . ALA B 1 262 ? 15.918  -14.293 0.947   1.00 15.49 ? 242 ALA B O   1 
ATOM   3843 C CB  . ALA B 1 262 ? 13.204  -12.601 2.028   1.00 15.38 ? 242 ALA B CB  1 
ATOM   3844 N N   . LEU B 1 263 ? 16.165  -12.046 1.221   1.00 14.81 ? 243 LEU B N   1 
ATOM   3845 C CA  . LEU B 1 263 ? 17.197  -11.923 0.156   1.00 16.45 ? 243 LEU B CA  1 
ATOM   3846 C C   . LEU B 1 263 ? 18.452  -12.742 0.489   1.00 16.97 ? 243 LEU B C   1 
ATOM   3847 O O   . LEU B 1 263 ? 19.065  -13.298 -0.467  1.00 15.58 ? 243 LEU B O   1 
ATOM   3848 C CB  . LEU B 1 263 ? 17.503  -10.443 -0.081  1.00 16.90 ? 243 LEU B CB  1 
ATOM   3849 C CG  . LEU B 1 263 ? 16.428  -9.717  -0.880  1.00 17.15 ? 243 LEU B CG  1 
ATOM   3850 C CD1 . LEU B 1 263 ? 16.520  -8.224  -0.731  1.00 17.84 ? 243 LEU B CD1 1 
ATOM   3851 C CD2 . LEU B 1 263 ? 16.511  -10.135 -2.351  1.00 18.50 ? 243 LEU B CD2 1 
ATOM   3852 N N   . GLU B 1 264 ? 18.811  -12.845 1.779   1.00 18.51 ? 244 GLU B N   1 
ATOM   3853 C CA  . GLU B 1 264 ? 19.954  -13.659 2.261   1.00 18.72 ? 244 GLU B CA  1 
ATOM   3854 C C   . GLU B 1 264 ? 19.657  -15.150 2.073   1.00 16.74 ? 244 GLU B C   1 
ATOM   3855 O O   . GLU B 1 264 ? 20.596  -15.871 1.703   1.00 14.20 ? 244 GLU B O   1 
ATOM   3856 C CB  . GLU B 1 264 ? 20.276  -13.406 3.737   1.00 22.24 ? 244 GLU B CB  1 
ATOM   3857 C CG  . GLU B 1 264 ? 20.758  -11.999 4.040   1.00 26.43 ? 244 GLU B CG  1 
ATOM   3858 C CD  . GLU B 1 264 ? 21.915  -11.472 3.203   1.00 29.77 ? 244 GLU B CD  1 
ATOM   3859 O OE1 . GLU B 1 264 ? 21.998  -10.223 3.056   1.00 31.77 ? 244 GLU B OE1 1 
ATOM   3860 O OE2 . GLU B 1 264 ? 22.731  -12.290 2.709   1.00 26.53 ? 244 GLU B OE2 1 
ATOM   3861 N N   . ASN B 1 265 ? 18.418  -15.607 2.331   1.00 16.08 ? 245 ASN B N   1 
ATOM   3862 C CA  . ASN B 1 265 ? 18.014  -17.017 2.048   1.00 15.84 ? 245 ASN B CA  1 
ATOM   3863 C C   . ASN B 1 265 ? 18.061  -17.251 0.527   1.00 15.59 ? 245 ASN B C   1 
ATOM   3864 O O   . ASN B 1 265 ? 18.406  -18.365 0.120   1.00 13.91 ? 245 ASN B O   1 
ATOM   3865 C CB  . ASN B 1 265 ? 16.642  -17.411 2.630   1.00 15.83 ? 245 ASN B CB  1 
ATOM   3866 C CG  . ASN B 1 265 ? 16.591  -17.303 4.139   1.00 17.03 ? 245 ASN B CG  1 
ATOM   3867 O OD1 . ASN B 1 265 ? 15.510  -17.321 4.736   1.00 17.47 ? 245 ASN B OD1 1 
ATOM   3868 N ND2 . ASN B 1 265 ? 17.757  -17.199 4.760   1.00 15.32 ? 245 ASN B ND2 1 
ATOM   3869 N N   . ILE B 1 266 ? 17.702  -16.253 -0.287  1.00 15.35 ? 246 ILE B N   1 
ATOM   3870 C CA  . ILE B 1 266 ? 17.703  -16.400 -1.776  1.00 15.68 ? 246 ILE B CA  1 
ATOM   3871 C C   . ILE B 1 266 ? 19.157  -16.580 -2.229  1.00 15.22 ? 246 ILE B C   1 
ATOM   3872 O O   . ILE B 1 266 ? 19.408  -17.547 -2.976  1.00 14.11 ? 246 ILE B O   1 
ATOM   3873 C CB  . ILE B 1 266 ? 16.976  -15.244 -2.492  1.00 15.41 ? 246 ILE B CB  1 
ATOM   3874 C CG1 . ILE B 1 266 ? 15.456  -15.354 -2.333  1.00 15.07 ? 246 ILE B CG1 1 
ATOM   3875 C CG2 . ILE B 1 266 ? 17.356  -15.175 -3.959  1.00 15.85 ? 246 ILE B CG2 1 
ATOM   3876 C CD1 . ILE B 1 266 ? 14.727  -14.016 -2.420  1.00 15.05 ? 246 ILE B CD1 1 
ATOM   3877 N N   . SER B 1 267 ? 20.089  -15.740 -1.761  1.00 17.61 ? 247 SER B N   1 
ATOM   3878 C CA  . SER B 1 267 ? 21.521  -15.786 -2.174  1.00 18.17 ? 247 SER B CA  1 
ATOM   3879 C C   . SER B 1 267 ? 22.109  -17.148 -1.811  1.00 18.11 ? 247 SER B C   1 
ATOM   3880 O O   . SER B 1 267 ? 22.784  -17.725 -2.673  1.00 17.55 ? 247 SER B O   1 
ATOM   3881 C CB  . SER B 1 267 ? 22.367  -14.677 -1.600  1.00 19.92 ? 247 SER B CB  1 
ATOM   3882 O OG  . SER B 1 267 ? 21.736  -13.423 -1.799  1.00 30.11 ? 247 SER B OG  1 
ATOM   3883 N N   . GLU B 1 268 ? 21.837  -17.641 -0.595  1.00 18.33 ? 248 GLU B N   1 
ATOM   3884 C CA  . GLU B 1 268 ? 22.404  -18.914 -0.075  1.00 18.85 ? 248 GLU B CA  1 
ATOM   3885 C C   . GLU B 1 268 ? 21.694  -20.125 -0.709  1.00 18.37 ? 248 GLU B C   1 
ATOM   3886 O O   . GLU B 1 268 ? 22.360  -21.134 -0.905  1.00 19.00 ? 248 GLU B O   1 
ATOM   3887 C CB  . GLU B 1 268 ? 22.352  -18.917 1.460   1.00 19.61 ? 248 GLU B CB  1 
ATOM   3888 C CG  . GLU B 1 268 ? 23.065  -20.102 2.088   1.00 21.77 ? 248 GLU B CG  1 
ATOM   3889 C CD  . GLU B 1 268 ? 24.467  -20.357 1.560   1.00 21.07 ? 248 GLU B CD  1 
ATOM   3890 O OE1 . GLU B 1 268 ? 25.106  -19.390 1.139   1.00 20.04 ? 248 GLU B OE1 1 
ATOM   3891 O OE2 . GLU B 1 268 ? 24.884  -21.522 1.520   1.00 22.37 ? 248 GLU B OE2 1 
ATOM   3892 N N   . THR B 1 269 ? 20.378  -20.072 -0.965  1.00 17.14 ? 249 THR B N   1 
ATOM   3893 C CA  . THR B 1 269 ? 19.640  -21.103 -1.743  1.00 16.09 ? 249 THR B CA  1 
ATOM   3894 C C   . THR B 1 269 ? 20.327  -21.233 -3.107  1.00 15.67 ? 249 THR B C   1 
ATOM   3895 O O   . THR B 1 269 ? 20.582  -22.381 -3.564  1.00 13.67 ? 249 THR B O   1 
ATOM   3896 C CB  . THR B 1 269 ? 18.149  -20.753 -1.870  1.00 16.99 ? 249 THR B CB  1 
ATOM   3897 O OG1 . THR B 1 269 ? 17.553  -20.776 -0.574  1.00 16.53 ? 249 THR B OG1 1 
ATOM   3898 C CG2 . THR B 1 269 ? 17.399  -21.711 -2.768  1.00 16.34 ? 249 THR B CG2 1 
ATOM   3899 N N   . SER B 1 270 ? 20.660  -20.082 -3.708  1.00 15.36 ? 250 SER B N   1 
ATOM   3900 C CA  . SER B 1 270 ? 21.380  -19.984 -4.998  1.00 16.83 ? 250 SER B CA  1 
ATOM   3901 C C   . SER B 1 270 ? 22.797  -20.584 -4.869  1.00 17.21 ? 250 SER B C   1 
ATOM   3902 O O   . SER B 1 270 ? 23.127  -21.495 -5.656  1.00 17.00 ? 250 SER B O   1 
ATOM   3903 C CB  . SER B 1 270 ? 21.371  -18.542 -5.512  1.00 17.04 ? 250 SER B CB  1 
ATOM   3904 O OG  . SER B 1 270 ? 20.024  -18.111 -5.804  1.00 16.14 ? 250 SER B OG  1 
ATOM   3905 N N   . ARG B 1 271 ? 23.582  -20.155 -3.886  1.00 17.91 ? 251 ARG B N   1 
ATOM   3906 C CA  . ARG B 1 271 ? 24.997  -20.609 -3.738  1.00 19.56 ? 251 ARG B CA  1 
ATOM   3907 C C   . ARG B 1 271 ? 25.018  -22.135 -3.547  1.00 19.48 ? 251 ARG B C   1 
ATOM   3908 O O   . ARG B 1 271 ? 25.689  -22.798 -4.341  1.00 18.23 ? 251 ARG B O   1 
ATOM   3909 C CB  . ARG B 1 271 ? 25.699  -19.875 -2.589  1.00 20.30 ? 251 ARG B CB  1 
ATOM   3910 C CG  . ARG B 1 271 ? 27.224  -19.922 -2.661  1.00 20.41 ? 251 ARG B CG  1 
ATOM   3911 C CD  . ARG B 1 271 ? 27.870  -19.616 -1.321  1.00 21.87 ? 251 ARG B CD  1 
ATOM   3912 N NE  . ARG B 1 271 ? 27.428  -20.590 -0.347  1.00 23.14 ? 251 ARG B NE  1 
ATOM   3913 C CZ  . ARG B 1 271 ? 27.836  -21.857 -0.278  1.00 24.31 ? 251 ARG B CZ  1 
ATOM   3914 N NH1 . ARG B 1 271 ? 28.766  -22.330 -1.093  1.00 25.24 ? 251 ARG B NH1 1 
ATOM   3915 N NH2 . ARG B 1 271 ? 27.305  -22.657 0.623   1.00 26.23 ? 251 ARG B NH2 1 
ATOM   3916 N N   . GLU B 1 272 ? 24.206  -22.673 -2.625  1.00 19.64 ? 252 GLU B N   1 
ATOM   3917 C CA  . GLU B 1 272 ? 24.035  -24.138 -2.412  1.00 20.17 ? 252 GLU B CA  1 
ATOM   3918 C C   . GLU B 1 272 ? 23.887  -24.870 -3.767  1.00 20.91 ? 252 GLU B C   1 
ATOM   3919 O O   . GLU B 1 272 ? 24.337  -26.016 -3.842  1.00 23.01 ? 252 GLU B O   1 
ATOM   3920 C CB  . GLU B 1 272 ? 22.806  -24.450 -1.538  1.00 20.71 ? 252 GLU B CB  1 
ATOM   3921 C CG  . GLU B 1 272 ? 22.887  -24.033 -0.064  1.00 19.44 ? 252 GLU B CG  1 
ATOM   3922 C CD  . GLU B 1 272 ? 21.578  -24.177 0.735   1.00 18.84 ? 252 GLU B CD  1 
ATOM   3923 O OE1 . GLU B 1 272 ? 21.553  -23.782 1.932   1.00 17.22 ? 252 GLU B OE1 1 
ATOM   3924 O OE2 . GLU B 1 272 ? 20.577  -24.690 0.187   1.00 15.61 ? 252 GLU B OE2 1 
ATOM   3925 N N   . LEU B 1 273 ? 23.224  -24.277 -4.776  1.00 20.99 ? 253 LEU B N   1 
ATOM   3926 C CA  . LEU B 1 273 ? 22.973  -24.897 -6.105  1.00 20.52 ? 253 LEU B CA  1 
ATOM   3927 C C   . LEU B 1 273 ? 24.015  -24.439 -7.140  1.00 20.96 ? 253 LEU B C   1 
ATOM   3928 O O   . LEU B 1 273 ? 23.833  -24.762 -8.342  1.00 19.95 ? 253 LEU B O   1 
ATOM   3929 C CB  . LEU B 1 273 ? 21.573  -24.512 -6.589  1.00 20.31 ? 253 LEU B CB  1 
ATOM   3930 C CG  . LEU B 1 273 ? 20.387  -25.117 -5.837  1.00 21.59 ? 253 LEU B CG  1 
ATOM   3931 C CD1 . LEU B 1 273 ? 19.084  -24.402 -6.200  1.00 21.39 ? 253 LEU B CD1 1 
ATOM   3932 C CD2 . LEU B 1 273 ? 20.250  -26.603 -6.143  1.00 21.69 ? 253 LEU B CD2 1 
ATOM   3933 N N   . GLY B 1 274 ? 25.037  -23.683 -6.729  1.00 21.93 ? 254 GLY B N   1 
ATOM   3934 C CA  . GLY B 1 274 ? 26.055  -23.116 -7.644  1.00 22.00 ? 254 GLY B CA  1 
ATOM   3935 C C   . GLY B 1 274 ? 25.452  -22.101 -8.607  1.00 22.92 ? 254 GLY B C   1 
ATOM   3936 O O   . GLY B 1 274 ? 26.080  -21.857 -9.675  1.00 22.17 ? 254 GLY B O   1 
ATOM   3937 N N   . VAL B 1 275 ? 24.295  -21.510 -8.242  1.00 21.17 ? 255 VAL B N   1 
ATOM   3938 C CA  . VAL B 1 275 ? 23.559  -20.514 -9.066  1.00 18.65 ? 255 VAL B CA  1 
ATOM   3939 C C   . VAL B 1 275 ? 23.956  -19.098 -8.636  1.00 17.85 ? 255 VAL B C   1 
ATOM   3940 O O   . VAL B 1 275 ? 24.080  -18.857 -7.428  1.00 17.84 ? 255 VAL B O   1 
ATOM   3941 C CB  . VAL B 1 275 ? 22.038  -20.737 -8.954  1.00 20.84 ? 255 VAL B CB  1 
ATOM   3942 C CG1 . VAL B 1 275 ? 21.244  -19.688 -9.732  1.00 20.22 ? 255 VAL B CG1 1 
ATOM   3943 C CG2 . VAL B 1 275 ? 21.661  -22.154 -9.393  1.00 21.05 ? 255 VAL B CG2 1 
ATOM   3944 N N   . GLY B 1 276 ? 24.116  -18.187 -9.597  1.00 16.37 ? 256 GLY B N   1 
ATOM   3945 C CA  . GLY B 1 276 ? 24.459  -16.776 -9.341  1.00 17.80 ? 256 GLY B CA  1 
ATOM   3946 C C   . GLY B 1 276 ? 23.272  -16.011 -8.781  1.00 17.98 ? 256 GLY B C   1 
ATOM   3947 O O   . GLY B 1 276 ? 22.187  -16.596 -8.725  1.00 20.31 ? 256 GLY B O   1 
ATOM   3948 N N   . VAL B 1 277 ? 23.441  -14.761 -8.355  1.00 18.27 ? 257 VAL B N   1 
ATOM   3949 C CA  . VAL B 1 277 ? 22.306  -14.036 -7.721  1.00 18.78 ? 257 VAL B CA  1 
ATOM   3950 C C   . VAL B 1 277 ? 22.278  -12.583 -8.182  1.00 17.22 ? 257 VAL B C   1 
ATOM   3951 O O   . VAL B 1 277 ? 23.326  -11.888 -8.223  1.00 15.41 ? 257 VAL B O   1 
ATOM   3952 C CB  . VAL B 1 277 ? 22.287  -14.150 -6.181  1.00 20.76 ? 257 VAL B CB  1 
ATOM   3953 C CG1 . VAL B 1 277 ? 22.959  -15.424 -5.697  1.00 22.50 ? 257 VAL B CG1 1 
ATOM   3954 C CG2 . VAL B 1 277 ? 22.897  -12.944 -5.509  1.00 22.43 ? 257 VAL B CG2 1 
ATOM   3955 N N   . LEU B 1 278 ? 21.068  -12.132 -8.474  1.00 15.14 ? 258 LEU B N   1 
ATOM   3956 C CA  . LEU B 1 278 ? 20.770  -10.722 -8.792  1.00 15.60 ? 258 LEU B CA  1 
ATOM   3957 C C   . LEU B 1 278 ? 20.287  -10.067 -7.508  1.00 15.90 ? 258 LEU B C   1 
ATOM   3958 O O   . LEU B 1 278 ? 20.625  -10.591 -6.414  1.00 16.05 ? 258 LEU B O   1 
ATOM   3959 C CB  . LEU B 1 278 ? 19.751  -10.691 -9.933  1.00 15.08 ? 258 LEU B CB  1 
ATOM   3960 C CG  . LEU B 1 278 ? 20.145  -11.551 -11.132 1.00 14.50 ? 258 LEU B CG  1 
ATOM   3961 C CD1 . LEU B 1 278 ? 19.055  -11.554 -12.186 1.00 15.07 ? 258 LEU B CD1 1 
ATOM   3962 C CD2 . LEU B 1 278 ? 21.452  -11.065 -11.734 1.00 15.75 ? 258 LEU B CD2 1 
ATOM   3963 N N   . LEU B 1 279 ? 19.558  -8.961  -7.642  1.00 16.90 ? 259 LEU B N   1 
ATOM   3964 C CA  . LEU B 1 279 ? 18.865  -8.267  -6.538  1.00 16.38 ? 259 LEU B CA  1 
ATOM   3965 C C   . LEU B 1 279 ? 19.877  -7.659  -5.557  1.00 16.32 ? 259 LEU B C   1 
ATOM   3966 O O   . LEU B 1 279 ? 19.450  -7.342  -4.432  1.00 15.51 ? 259 LEU B O   1 
ATOM   3967 C CB  . LEU B 1 279 ? 17.959  -9.277  -5.834  1.00 16.55 ? 259 LEU B CB  1 
ATOM   3968 C CG  . LEU B 1 279 ? 16.911  -9.963  -6.703  1.00 16.35 ? 259 LEU B CG  1 
ATOM   3969 C CD1 . LEU B 1 279 ? 16.215  -11.058 -5.932  1.00 16.67 ? 259 LEU B CD1 1 
ATOM   3970 C CD2 . LEU B 1 279 ? 15.893  -8.988  -7.214  1.00 16.51 ? 259 LEU B CD2 1 
ATOM   3971 N N   . GLY B 1 280 ? 21.153  -7.523  -5.952  1.00 16.51 ? 260 GLY B N   1 
ATOM   3972 C CA  . GLY B 1 280 ? 22.207  -6.862  -5.157  1.00 17.62 ? 260 GLY B CA  1 
ATOM   3973 C C   . GLY B 1 280 ? 21.833  -5.465  -4.675  1.00 18.13 ? 260 GLY B C   1 
ATOM   3974 O O   . GLY B 1 280 ? 22.058  -5.160  -3.484  1.00 18.40 ? 260 GLY B O   1 
ATOM   3975 N N   . SER B 1 281 ? 21.319  -4.610  -5.558  1.00 18.95 ? 261 SER B N   1 
ATOM   3976 C CA  . SER B 1 281 ? 20.934  -3.215  -5.209  1.00 18.40 ? 261 SER B CA  1 
ATOM   3977 C C   . SER B 1 281 ? 19.849  -3.275  -4.125  1.00 19.65 ? 261 SER B C   1 
ATOM   3978 O O   . SER B 1 281 ? 19.833  -2.373  -3.250  1.00 17.77 ? 261 SER B O   1 
ATOM   3979 C CB  . SER B 1 281 ? 20.444  -2.431  -6.395  1.00 18.57 ? 261 SER B CB  1 
ATOM   3980 O OG  . SER B 1 281 ? 21.381  -2.392  -7.461  1.00 18.01 ? 261 SER B OG  1 
ATOM   3981 N N   . MET B 1 282 ? 18.948  -4.267  -4.201  1.00 18.25 ? 262 MET B N   1 
ATOM   3982 C CA  . MET B 1 282 ? 17.788  -4.348  -3.265  1.00 19.22 ? 262 MET B CA  1 
ATOM   3983 C C   . MET B 1 282 ? 18.351  -4.670  -1.878  1.00 19.63 ? 262 MET B C   1 
ATOM   3984 O O   . MET B 1 282 ? 18.039  -3.923  -0.945  1.00 18.38 ? 262 MET B O   1 
ATOM   3985 C CB  . MET B 1 282 ? 16.767  -5.392  -3.712  1.00 18.08 ? 262 MET B CB  1 
ATOM   3986 C CG  . MET B 1 282 ? 15.386  -5.250  -3.113  1.00 17.66 ? 262 MET B CG  1 
ATOM   3987 S SD  . MET B 1 282 ? 14.734  -3.558  -3.047  1.00 16.71 ? 262 MET B SD  1 
ATOM   3988 C CE  . MET B 1 282 ? 13.035  -3.941  -2.619  1.00 15.79 ? 262 MET B CE  1 
ATOM   3989 N N   . ARG B 1 283 ? 19.260  -5.646  -1.803  1.00 20.75 ? 263 ARG B N   1 
ATOM   3990 C CA  . ARG B 1 283 ? 20.000  -6.024  -0.561  1.00 21.98 ? 263 ARG B CA  1 
ATOM   3991 C C   . ARG B 1 283 ? 20.718  -4.812  0.022   1.00 20.45 ? 263 ARG B C   1 
ATOM   3992 O O   . ARG B 1 283 ? 20.545  -4.571  1.227   1.00 17.95 ? 263 ARG B O   1 
ATOM   3993 C CB  . ARG B 1 283 ? 21.038  -7.119  -0.818  1.00 23.74 ? 263 ARG B CB  1 
ATOM   3994 C CG  . ARG B 1 283 ? 20.434  -8.510  -0.910  1.00 26.94 ? 263 ARG B CG  1 
ATOM   3995 C CD  . ARG B 1 283 ? 21.436  -9.621  -0.647  1.00 28.08 ? 263 ARG B CD  1 
ATOM   3996 N NE  . ARG B 1 283 ? 22.612  -9.486  -1.501  1.00 29.56 ? 263 ARG B NE  1 
ATOM   3997 C CZ  . ARG B 1 283 ? 22.660  -9.745  -2.805  1.00 28.22 ? 263 ARG B CZ  1 
ATOM   3998 N NH1 . ARG B 1 283 ? 23.802  -9.568  -3.450  1.00 27.06 ? 263 ARG B NH1 1 
ATOM   3999 N NH2 . ARG B 1 283 ? 21.580  -10.142 -3.471  1.00 26.36 ? 263 ARG B NH2 1 
ATOM   4000 N N   . GLU B 1 284 ? 21.489  -4.093  -0.799  1.00 20.56 ? 264 GLU B N   1 
ATOM   4001 C CA  . GLU B 1 284 ? 22.332  -2.947  -0.356  1.00 20.34 ? 264 GLU B CA  1 
ATOM   4002 C C   . GLU B 1 284 ? 21.436  -1.845  0.219   1.00 19.84 ? 264 GLU B C   1 
ATOM   4003 O O   . GLU B 1 284 ? 21.708  -1.375  1.356   1.00 17.38 ? 264 GLU B O   1 
ATOM   4004 C CB  . GLU B 1 284 ? 23.227  -2.443  -1.492  1.00 22.37 ? 264 GLU B CB  1 
ATOM   4005 C CG  . GLU B 1 284 ? 24.425  -3.362  -1.745  1.00 23.68 ? 264 GLU B CG  1 
ATOM   4006 C CD  . GLU B 1 284 ? 25.317  -3.579  -0.530  1.00 24.82 ? 264 GLU B CD  1 
ATOM   4007 O OE1 . GLU B 1 284 ? 25.477  -2.637  0.272   1.00 26.16 ? 264 GLU B OE1 1 
ATOM   4008 O OE2 . GLU B 1 284 ? 25.786  -4.710  -0.338  1.00 27.82 ? 264 GLU B OE2 1 
ATOM   4009 N N   . VAL B 1 285 ? 20.342  -1.494  -0.457  1.00 18.07 ? 265 VAL B N   1 
ATOM   4010 C CA  . VAL B 1 285 ? 19.482  -0.378  0.023   1.00 18.20 ? 265 VAL B CA  1 
ATOM   4011 C C   . VAL B 1 285 ? 18.730  -0.786  1.300   1.00 19.99 ? 265 VAL B C   1 
ATOM   4012 O O   . VAL B 1 285 ? 18.510  0.097   2.156   1.00 19.88 ? 265 VAL B O   1 
ATOM   4013 C CB  . VAL B 1 285 ? 18.526  0.146   -1.059  1.00 18.76 ? 265 VAL B CB  1 
ATOM   4014 C CG1 . VAL B 1 285 ? 17.367  -0.791  -1.315  1.00 17.48 ? 265 VAL B CG1 1 
ATOM   4015 C CG2 . VAL B 1 285 ? 18.037  1.539   -0.691  1.00 18.01 ? 265 VAL B CG2 1 
ATOM   4016 N N   . MET B 1 286 ? 18.312  -2.051  1.405   1.00 19.43 ? 266 MET B N   1 
ATOM   4017 C CA  . MET B 1 286 ? 17.603  -2.590  2.591   1.00 19.32 ? 266 MET B CA  1 
ATOM   4018 C C   . MET B 1 286 ? 18.587  -2.696  3.774   1.00 20.27 ? 266 MET B C   1 
ATOM   4019 O O   . MET B 1 286 ? 18.195  -2.362  4.924   1.00 17.48 ? 266 MET B O   1 
ATOM   4020 C CB  . MET B 1 286 ? 16.956  -3.939  2.257   1.00 18.44 ? 266 MET B CB  1 
ATOM   4021 C CG  . MET B 1 286 ? 15.757  -3.787  1.287   1.00 18.00 ? 266 MET B CG  1 
ATOM   4022 S SD  . MET B 1 286 ? 14.911  -5.318  0.913   1.00 17.66 ? 266 MET B SD  1 
ATOM   4023 C CE  . MET B 1 286 ? 13.490  -5.256  1.998   1.00 20.15 ? 266 MET B CE  1 
ATOM   4024 N N   . SER B 1 287 ? 19.832  -3.095  3.521   1.00 20.39 ? 267 SER B N   1 
ATOM   4025 C CA  . SER B 1 287 ? 20.875  -3.162  4.580   1.00 22.13 ? 267 SER B CA  1 
ATOM   4026 C C   . SER B 1 287 ? 21.110  -1.759  5.152   1.00 21.53 ? 267 SER B C   1 
ATOM   4027 O O   . SER B 1 287 ? 21.129  -1.616  6.381   1.00 21.98 ? 267 SER B O   1 
ATOM   4028 C CB  . SER B 1 287 ? 22.138  -3.789  4.076   1.00 23.58 ? 267 SER B CB  1 
ATOM   4029 O OG  . SER B 1 287 ? 23.111  -3.813  5.106   1.00 28.03 ? 267 SER B OG  1 
ATOM   4030 N N   . GLU B 1 288 ? 21.209  -0.749  4.296   1.00 20.86 ? 268 GLU B N   1 
ATOM   4031 C CA  . GLU B 1 288 ? 21.480  0.637   4.726   1.00 22.83 ? 268 GLU B CA  1 
ATOM   4032 C C   . GLU B 1 288 ? 20.263  1.151   5.490   1.00 25.04 ? 268 GLU B C   1 
ATOM   4033 O O   . GLU B 1 288 ? 20.473  1.825   6.532   1.00 23.37 ? 268 GLU B O   1 
ATOM   4034 C CB  . GLU B 1 288 ? 21.833  1.516   3.531   1.00 25.59 ? 268 GLU B CB  1 
ATOM   4035 C CG  . GLU B 1 288 ? 22.224  2.934   3.908   1.00 28.76 ? 268 GLU B CG  1 
ATOM   4036 C CD  . GLU B 1 288 ? 23.383  3.060   4.883   1.00 29.76 ? 268 GLU B CD  1 
ATOM   4037 O OE1 . GLU B 1 288 ? 24.237  2.150   4.922   1.00 31.69 ? 268 GLU B OE1 1 
ATOM   4038 O OE2 . GLU B 1 288 ? 23.425  4.071   5.590   1.00 34.62 ? 268 GLU B OE2 1 
ATOM   4039 N N   . ALA B 1 289 ? 19.045  0.824   5.025   1.00 23.30 ? 269 ALA B N   1 
ATOM   4040 C CA  . ALA B 1 289 ? 17.794  1.197   5.727   1.00 26.14 ? 269 ALA B CA  1 
ATOM   4041 C C   . ALA B 1 289 ? 17.856  0.707   7.186   1.00 27.07 ? 269 ALA B C   1 
ATOM   4042 O O   . ALA B 1 289 ? 17.524  1.509   8.091   1.00 25.11 ? 269 ALA B O   1 
ATOM   4043 C CB  . ALA B 1 289 ? 16.571  0.686   5.000   1.00 25.20 ? 269 ALA B CB  1 
ATOM   4044 N N   . VAL B 1 290 ? 18.252  -0.555  7.413   1.00 28.25 ? 270 VAL B N   1 
ATOM   4045 C CA  . VAL B 1 290 ? 18.371  -1.152  8.783   1.00 28.75 ? 270 VAL B CA  1 
ATOM   4046 C C   . VAL B 1 290 ? 19.407  -0.344  9.583   1.00 28.78 ? 270 VAL B C   1 
ATOM   4047 O O   . VAL B 1 290 ? 19.115  -0.031  10.752  1.00 27.65 ? 270 VAL B O   1 
ATOM   4048 C CB  . VAL B 1 290 ? 18.746  -2.650  8.751   1.00 29.46 ? 270 VAL B CB  1 
ATOM   4049 C CG1 . VAL B 1 290 ? 19.207  -3.165  10.120  1.00 27.51 ? 270 VAL B CG1 1 
ATOM   4050 C CG2 . VAL B 1 290 ? 17.619  -3.510  8.204   1.00 27.00 ? 270 VAL B CG2 1 
ATOM   4051 N N   . LYS B 1 291 ? 20.569  -0.053  8.990   1.00 27.94 ? 271 LYS B N   1 
ATOM   4052 C CA  . LYS B 1 291 ? 21.633  0.784   9.611   1.00 32.67 ? 271 LYS B CA  1 
ATOM   4053 C C   . LYS B 1 291 ? 21.068  2.167   9.962   1.00 32.95 ? 271 LYS B C   1 
ATOM   4054 O O   . LYS B 1 291 ? 21.500  2.717   10.991  1.00 35.97 ? 271 LYS B O   1 
ATOM   4055 C CB  . LYS B 1 291 ? 22.863  0.961   8.711   1.00 32.82 ? 271 LYS B CB  1 
ATOM   4056 C CG  . LYS B 1 291 ? 23.799  -0.234  8.649   1.00 35.02 ? 271 LYS B CG  1 
ATOM   4057 C CD  . LYS B 1 291 ? 24.936  -0.060  7.653   1.00 36.96 ? 271 LYS B CD  1 
ATOM   4058 C CE  . LYS B 1 291 ? 25.235  -1.315  6.853   1.00 38.64 ? 271 LYS B CE  1 
ATOM   4059 N NZ  . LYS B 1 291 ? 25.039  -2.545  7.659   1.00 41.38 ? 271 LYS B NZ  1 
ATOM   4060 N N   . LYS B 1 292 ? 20.144  2.703   9.160   1.00 30.94 ? 272 LYS B N   1 
ATOM   4061 C CA  . LYS B 1 292 ? 19.518  4.029   9.412   1.00 32.40 ? 272 LYS B CA  1 
ATOM   4062 C C   . LYS B 1 292 ? 18.334  3.896   10.388  1.00 30.94 ? 272 LYS B C   1 
ATOM   4063 O O   . LYS B 1 292 ? 17.751  4.937   10.732  1.00 30.92 ? 272 LYS B O   1 
ATOM   4064 C CB  . LYS B 1 292 ? 19.132  4.685   8.083   1.00 35.59 ? 272 LYS B CB  1 
ATOM   4065 C CG  . LYS B 1 292 ? 20.333  5.072   7.227   1.00 35.64 ? 272 LYS B CG  1 
ATOM   4066 C CD  . LYS B 1 292 ? 19.998  5.513   5.813   1.00 39.75 ? 272 LYS B CD  1 
ATOM   4067 C CE  . LYS B 1 292 ? 20.045  7.016   5.620   1.00 40.74 ? 272 LYS B CE  1 
ATOM   4068 N NZ  . LYS B 1 292 ? 18.712  7.626   5.854   1.00 39.81 ? 272 LYS B NZ  1 
ATOM   4069 N N   . GLY B 1 293 ? 18.020  2.685   10.856  1.00 27.50 ? 273 GLY B N   1 
ATOM   4070 C CA  . GLY B 1 293 ? 16.961  2.430   11.857  1.00 26.79 ? 273 GLY B CA  1 
ATOM   4071 C C   . GLY B 1 293 ? 15.564  2.345   11.252  1.00 26.44 ? 273 GLY B C   1 
ATOM   4072 O O   . GLY B 1 293 ? 14.589  2.536   11.990  1.00 27.05 ? 273 GLY B O   1 
ATOM   4073 N N   . LYS B 1 294 ? 15.443  2.017   9.967   1.00 26.43 ? 274 LYS B N   1 
ATOM   4074 C CA  . LYS B 1 294 ? 14.135  1.867   9.269   1.00 25.91 ? 274 LYS B CA  1 
ATOM   4075 C C   . LYS B 1 294 ? 13.807  0.375   9.114   1.00 25.92 ? 274 LYS B C   1 
ATOM   4076 O O   . LYS B 1 294 ? 12.855  0.059   8.384   1.00 25.92 ? 274 LYS B O   1 
ATOM   4077 C CB  . LYS B 1 294 ? 14.195  2.618   7.932   1.00 26.31 ? 274 LYS B CB  1 
ATOM   4078 C CG  . LYS B 1 294 ? 14.344  4.129   8.076   1.00 27.83 ? 274 LYS B CG  1 
ATOM   4079 C CD  . LYS B 1 294 ? 14.772  4.882   6.814   1.00 27.79 ? 274 LYS B CD  1 
ATOM   4080 C CE  . LYS B 1 294 ? 13.917  4.595   5.594   1.00 25.94 ? 274 LYS B CE  1 
ATOM   4081 N NZ  . LYS B 1 294 ? 12.621  5.316   5.626   1.00 25.58 ? 274 LYS B NZ  1 
ATOM   4082 N N   . GLY B 1 295 ? 14.536  -0.498  9.817   1.00 25.88 ? 275 GLY B N   1 
ATOM   4083 C CA  . GLY B 1 295 ? 14.401  -1.967  9.731   1.00 25.56 ? 275 GLY B CA  1 
ATOM   4084 C C   . GLY B 1 295 ? 12.962  -2.420  9.921   1.00 24.29 ? 275 GLY B C   1 
ATOM   4085 O O   . GLY B 1 295 ? 12.593  -3.447  9.341   1.00 21.71 ? 275 GLY B O   1 
ATOM   4086 N N   . GLY B 1 296 ? 12.176  -1.698  10.728  1.00 22.85 ? 276 GLY B N   1 
ATOM   4087 C CA  . GLY B 1 296 ? 10.774  -2.064  11.048  1.00 21.59 ? 276 GLY B CA  1 
ATOM   4088 C C   . GLY B 1 296 ? 9.755   -1.457  10.096  1.00 20.89 ? 276 GLY B C   1 
ATOM   4089 O O   . GLY B 1 296 ? 8.575   -1.820  10.178  1.00 22.17 ? 276 GLY B O   1 
ATOM   4090 N N   . GLU B 1 297 ? 10.177  -0.550  9.210   1.00 21.38 ? 277 GLU B N   1 
ATOM   4091 C CA  . GLU B 1 297 ? 9.303   0.025   8.156   1.00 21.58 ? 277 GLU B CA  1 
ATOM   4092 C C   . GLU B 1 297 ? 9.069   -1.015  7.055   1.00 21.81 ? 277 GLU B C   1 
ATOM   4093 O O   . GLU B 1 297 ? 9.899   -1.931  6.929   1.00 21.79 ? 277 GLU B O   1 
ATOM   4094 C CB  . GLU B 1 297 ? 9.953   1.277   7.578   1.00 23.22 ? 277 GLU B CB  1 
ATOM   4095 C CG  . GLU B 1 297 ? 10.191  2.349   8.624   1.00 22.94 ? 277 GLU B CG  1 
ATOM   4096 C CD  . GLU B 1 297 ? 10.686  3.634   8.007   1.00 24.86 ? 277 GLU B CD  1 
ATOM   4097 O OE1 . GLU B 1 297 ? 10.985  3.616   6.784   1.00 26.96 ? 277 GLU B OE1 1 
ATOM   4098 O OE2 . GLU B 1 297 ? 10.794  4.637   8.737   1.00 24.67 ? 277 GLU B OE2 1 
ATOM   4099 N N   . SER B 1 298 ? 7.970   -0.877  6.311   1.00 21.91 ? 278 SER B N   1 
ATOM   4100 C CA  . SER B 1 298 ? 7.655   -1.645  5.081   1.00 22.72 ? 278 SER B CA  1 
ATOM   4101 C C   . SER B 1 298 ? 8.498   -1.111  3.913   1.00 21.68 ? 278 SER B C   1 
ATOM   4102 O O   . SER B 1 298 ? 9.220   -0.117  4.093   1.00 20.32 ? 278 SER B O   1 
ATOM   4103 C CB  . SER B 1 298 ? 6.183   -1.586  4.768   1.00 23.51 ? 278 SER B CB  1 
ATOM   4104 O OG  . SER B 1 298 ? 5.862   -0.298  4.263   1.00 25.80 ? 278 SER B OG  1 
ATOM   4105 N N   . ILE B 1 299 ? 8.419   -1.757  2.748   1.00 22.93 ? 279 ILE B N   1 
ATOM   4106 C CA  . ILE B 1 299 ? 9.245   -1.378  1.559   1.00 23.17 ? 279 ILE B CA  1 
ATOM   4107 C C   . ILE B 1 299 ? 8.898   0.065   1.138   1.00 20.31 ? 279 ILE B C   1 
ATOM   4108 O O   . ILE B 1 299 ? 9.748   0.691   0.505   1.00 18.01 ? 279 ILE B O   1 
ATOM   4109 C CB  . ILE B 1 299 ? 9.096   -2.385  0.401   1.00 26.01 ? 279 ILE B CB  1 
ATOM   4110 C CG1 . ILE B 1 299 ? 7.659   -2.407  -0.125  1.00 26.58 ? 279 ILE B CG1 1 
ATOM   4111 C CG2 . ILE B 1 299 ? 9.643   -3.777  0.784   1.00 26.08 ? 279 ILE B CG2 1 
ATOM   4112 C CD1 . ILE B 1 299 ? 7.081   -3.781  -0.301  1.00 30.61 ? 279 ILE B CD1 1 
ATOM   4113 N N   . ALA B 1 300 ? 7.722   0.590   1.498   1.00 18.68 ? 280 ALA B N   1 
ATOM   4114 C CA  . ALA B 1 300 ? 7.362   2.015   1.258   1.00 18.87 ? 280 ALA B CA  1 
ATOM   4115 C C   . ALA B 1 300 ? 8.464   2.944   1.782   1.00 18.29 ? 280 ALA B C   1 
ATOM   4116 O O   . ALA B 1 300 ? 8.756   3.980   1.124   1.00 19.06 ? 280 ALA B O   1 
ATOM   4117 C CB  . ALA B 1 300 ? 6.007   2.335   1.842   1.00 18.62 ? 280 ALA B CB  1 
ATOM   4118 N N   . GLY B 1 301 ? 9.098   2.585   2.897   1.00 19.46 ? 281 GLY B N   1 
ATOM   4119 C CA  . GLY B 1 301 ? 10.219  3.338   3.494   1.00 18.93 ? 281 GLY B CA  1 
ATOM   4120 C C   . GLY B 1 301 ? 11.509  3.316   2.673   1.00 19.80 ? 281 GLY B C   1 
ATOM   4121 O O   . GLY B 1 301 ? 12.418  4.117   2.990   1.00 18.10 ? 281 GLY B O   1 
ATOM   4122 N N   . LEU B 1 302 ? 11.644  2.435   1.674   1.00 18.83 ? 282 LEU B N   1 
ATOM   4123 C CA  . LEU B 1 302 ? 12.831  2.443   0.758   1.00 18.84 ? 282 LEU B CA  1 
ATOM   4124 C C   . LEU B 1 302 ? 12.727  3.637   -0.228  1.00 19.50 ? 282 LEU B C   1 
ATOM   4125 O O   . LEU B 1 302 ? 13.771  4.059   -0.753  1.00 18.37 ? 282 LEU B O   1 
ATOM   4126 C CB  . LEU B 1 302 ? 12.943  1.101   0.002   1.00 18.22 ? 282 LEU B CB  1 
ATOM   4127 C CG  . LEU B 1 302 ? 13.181  -0.137  0.880   1.00 18.51 ? 282 LEU B CG  1 
ATOM   4128 C CD1 . LEU B 1 302 ? 13.168  -1.439  0.083   1.00 17.41 ? 282 LEU B CD1 1 
ATOM   4129 C CD2 . LEU B 1 302 ? 14.492  -0.004  1.650   1.00 19.01 ? 282 LEU B CD2 1 
ATOM   4130 N N   . VAL B 1 303 ? 11.527  4.165   -0.507  1.00 18.69 ? 283 VAL B N   1 
ATOM   4131 C CA  . VAL B 1 303 ? 11.384  5.216   -1.557  1.00 20.16 ? 283 VAL B CA  1 
ATOM   4132 C C   . VAL B 1 303 ? 12.215  6.433   -1.131  1.00 21.14 ? 283 VAL B C   1 
ATOM   4133 O O   . VAL B 1 303 ? 13.101  6.856   -1.853  1.00 23.78 ? 283 VAL B O   1 
ATOM   4134 C CB  . VAL B 1 303 ? 9.902   5.521   -1.855  1.00 19.45 ? 283 VAL B CB  1 
ATOM   4135 C CG1 . VAL B 1 303 ? 9.716   6.791   -2.673  1.00 19.62 ? 283 VAL B CG1 1 
ATOM   4136 C CG2 . VAL B 1 303 ? 9.228   4.336   -2.531  1.00 19.61 ? 283 VAL B CG2 1 
ATOM   4137 N N   . PRO B 1 304 ? 12.041  7.025   0.067   1.00 23.43 ? 284 PRO B N   1 
ATOM   4138 C CA  . PRO B 1 304 ? 12.889  8.149   0.468   1.00 23.53 ? 284 PRO B CA  1 
ATOM   4139 C C   . PRO B 1 304 ? 14.400  7.857   0.485   1.00 23.66 ? 284 PRO B C   1 
ATOM   4140 O O   . PRO B 1 304 ? 15.149  8.801   0.348   1.00 23.01 ? 284 PRO B O   1 
ATOM   4141 C CB  . PRO B 1 304 ? 12.390  8.525   1.877   1.00 22.99 ? 284 PRO B CB  1 
ATOM   4142 C CG  . PRO B 1 304 ? 11.511  7.358   2.316   1.00 22.83 ? 284 PRO B CG  1 
ATOM   4143 C CD  . PRO B 1 304 ? 10.970  6.752   1.045   1.00 23.03 ? 284 PRO B CD  1 
ATOM   4144 N N   . MET B 1 305 ? 14.816  6.596   0.629   1.00 22.34 ? 285 MET B N   1 
ATOM   4145 C CA  . MET B 1 305 ? 16.249  6.216   0.502   1.00 23.76 ? 285 MET B CA  1 
ATOM   4146 C C   . MET B 1 305 ? 16.731  6.645   -0.889  1.00 21.15 ? 285 MET B C   1 
ATOM   4147 O O   . MET B 1 305 ? 17.895  7.008   -1.020  1.00 20.44 ? 285 MET B O   1 
ATOM   4148 C CB  . MET B 1 305 ? 16.498  4.707   0.619   1.00 26.14 ? 285 MET B CB  1 
ATOM   4149 C CG  . MET B 1 305 ? 15.943  4.018   1.854   1.00 29.09 ? 285 MET B CG  1 
ATOM   4150 S SD  . MET B 1 305 ? 17.006  4.022   3.304   1.00 30.76 ? 285 MET B SD  1 
ATOM   4151 C CE  . MET B 1 305 ? 18.663  3.700   2.698   1.00 28.35 ? 285 MET B CE  1 
ATOM   4152 N N   . LEU B 1 306 ? 15.859  6.542   -1.892  1.00 19.87 ? 286 LEU B N   1 
ATOM   4153 C CA  . LEU B 1 306 ? 16.188  6.863   -3.305  1.00 21.09 ? 286 LEU B CA  1 
ATOM   4154 C C   . LEU B 1 306 ? 16.018  8.366   -3.548  1.00 19.31 ? 286 LEU B C   1 
ATOM   4155 O O   . LEU B 1 306 ? 16.950  8.973   -4.118  1.00 18.39 ? 286 LEU B O   1 
ATOM   4156 C CB  . LEU B 1 306 ? 15.299  6.042   -4.246  1.00 20.75 ? 286 LEU B CB  1 
ATOM   4157 C CG  . LEU B 1 306 ? 15.463  4.526   -4.155  1.00 20.89 ? 286 LEU B CG  1 
ATOM   4158 C CD1 . LEU B 1 306 ? 14.701  3.863   -5.293  1.00 21.72 ? 286 LEU B CD1 1 
ATOM   4159 C CD2 . LEU B 1 306 ? 16.936  4.118   -4.191  1.00 21.67 ? 286 LEU B CD2 1 
ATOM   4160 N N   . THR B 1 307 ? 14.876  8.943   -3.181  1.00 21.25 ? 287 THR B N   1 
ATOM   4161 C CA  . THR B 1 307 ? 14.557  10.365  -3.521  1.00 22.85 ? 287 THR B CA  1 
ATOM   4162 C C   . THR B 1 307 ? 15.558  11.317  -2.857  1.00 23.31 ? 287 THR B C   1 
ATOM   4163 O O   . THR B 1 307 ? 15.642  12.463  -3.299  1.00 23.92 ? 287 THR B O   1 
ATOM   4164 C CB  . THR B 1 307 ? 13.132  10.807  -3.146  1.00 22.73 ? 287 THR B CB  1 
ATOM   4165 O OG1 . THR B 1 307 ? 12.951  10.754  -1.729  1.00 21.99 ? 287 THR B OG1 1 
ATOM   4166 C CG2 . THR B 1 307 ? 12.058  10.005  -3.843  1.00 21.62 ? 287 THR B CG2 1 
ATOM   4167 N N   . GLU B 1 308 ? 16.284  10.875  -1.833  1.00 27.56 ? 288 GLU B N   1 
ATOM   4168 C CA  . GLU B 1 308 ? 17.107  11.777  -0.988  1.00 30.79 ? 288 GLU B CA  1 
ATOM   4169 C C   . GLU B 1 308 ? 18.577  11.784  -1.421  1.00 31.45 ? 288 GLU B C   1 
ATOM   4170 O O   . GLU B 1 308 ? 19.297  12.657  -0.912  1.00 31.64 ? 288 GLU B O   1 
ATOM   4171 C CB  . GLU B 1 308 ? 17.035  11.366  0.483   1.00 34.20 ? 288 GLU B CB  1 
ATOM   4172 C CG  . GLU B 1 308 ? 15.726  11.729  1.154   1.00 37.40 ? 288 GLU B CG  1 
ATOM   4173 C CD  . GLU B 1 308 ? 15.602  11.193  2.575   1.00 42.09 ? 288 GLU B CD  1 
ATOM   4174 O OE1 . GLU B 1 308 ? 14.532  11.399  3.194   1.00 37.82 ? 288 GLU B OE1 1 
ATOM   4175 O OE2 . GLU B 1 308 ? 16.580  10.564  3.062   1.00 42.66 ? 288 GLU B OE2 1 
ATOM   4176 N N   . LEU B 1 309 ? 19.038  10.867  -2.273  1.00 27.09 ? 289 LEU B N   1 
ATOM   4177 C CA  . LEU B 1 309 ? 20.499  10.748  -2.544  1.00 28.18 ? 289 LEU B CA  1 
ATOM   4178 C C   . LEU B 1 309 ? 20.758  10.188  -3.947  1.00 27.35 ? 289 LEU B C   1 
ATOM   4179 O O   . LEU B 1 309 ? 20.170  9.145   -4.291  1.00 23.21 ? 289 LEU B O   1 
ATOM   4180 C CB  . LEU B 1 309 ? 21.116  9.845   -1.470  1.00 30.12 ? 289 LEU B CB  1 
ATOM   4181 C CG  . LEU B 1 309 ? 22.620  9.573   -1.581  1.00 31.81 ? 289 LEU B CG  1 
ATOM   4182 C CD1 . LEU B 1 309 ? 23.423  10.867  -1.453  1.00 33.01 ? 289 LEU B CD1 1 
ATOM   4183 C CD2 . LEU B 1 309 ? 23.052  8.561   -0.526  1.00 31.48 ? 289 LEU B CD2 1 
ATOM   4184 N N   . ASP B 1 310 ? 21.656  10.846  -4.689  1.00 27.25 ? 290 ASP B N   1 
ATOM   4185 C CA  . ASP B 1 310 ? 22.112  10.456  -6.047  1.00 26.17 ? 290 ASP B CA  1 
ATOM   4186 C C   . ASP B 1 310 ? 23.153  9.355   -5.883  1.00 26.18 ? 290 ASP B C   1 
ATOM   4187 O O   . ASP B 1 310 ? 24.350  9.678   -5.831  1.00 27.94 ? 290 ASP B O   1 
ATOM   4188 C CB  . ASP B 1 310 ? 22.661  11.670  -6.796  1.00 27.16 ? 290 ASP B CB  1 
ATOM   4189 C CG  . ASP B 1 310 ? 23.086  11.425  -8.233  1.00 28.72 ? 290 ASP B CG  1 
ATOM   4190 O OD1 . ASP B 1 310 ? 23.105  10.243  -8.675  1.00 30.48 ? 290 ASP B OD1 1 
ATOM   4191 O OD2 . ASP B 1 310 ? 23.407  12.423  -8.909  1.00 34.00 ? 290 ASP B OD2 1 
ATOM   4192 N N   . LYS B 1 311 ? 22.720  8.094   -5.842  1.00 25.88 ? 291 LYS B N   1 
ATOM   4193 C CA  . LYS B 1 311 ? 23.641  6.955   -5.592  1.00 25.92 ? 291 LYS B CA  1 
ATOM   4194 C C   . LYS B 1 311 ? 23.183  5.746   -6.401  1.00 24.33 ? 291 LYS B C   1 
ATOM   4195 O O   . LYS B 1 311 ? 21.975  5.477   -6.381  1.00 21.84 ? 291 LYS B O   1 
ATOM   4196 C CB  . LYS B 1 311 ? 23.667  6.652   -4.089  1.00 25.97 ? 291 LYS B CB  1 
ATOM   4197 C CG  . LYS B 1 311 ? 24.450  5.417   -3.667  1.00 25.13 ? 291 LYS B CG  1 
ATOM   4198 C CD  . LYS B 1 311 ? 24.523  5.273   -2.168  1.00 25.72 ? 291 LYS B CD  1 
ATOM   4199 C CE  . LYS B 1 311 ? 24.981  3.905   -1.728  1.00 26.20 ? 291 LYS B CE  1 
ATOM   4200 N NZ  . LYS B 1 311 ? 24.958  3.793   -0.246  1.00 29.43 ? 291 LYS B NZ  1 
ATOM   4201 N N   . LYS B 1 312 ? 24.119  5.053   -7.055  1.00 24.63 ? 292 LYS B N   1 
ATOM   4202 C CA  . LYS B 1 312 ? 23.879  3.735   -7.704  1.00 27.09 ? 292 LYS B CA  1 
ATOM   4203 C C   . LYS B 1 312 ? 24.118  2.620   -6.673  1.00 25.44 ? 292 LYS B C   1 
ATOM   4204 O O   . LYS B 1 312 ? 25.248  2.407   -6.253  1.00 25.94 ? 292 LYS B O   1 
ATOM   4205 C CB  . LYS B 1 312 ? 24.714  3.647   -8.986  1.00 31.01 ? 292 LYS B CB  1 
ATOM   4206 C CG  . LYS B 1 312 ? 24.443  4.789   -9.963  1.00 34.75 ? 292 LYS B CG  1 
ATOM   4207 C CD  . LYS B 1 312 ? 24.685  4.473   -11.438 1.00 41.06 ? 292 LYS B CD  1 
ATOM   4208 C CE  . LYS B 1 312 ? 24.601  5.694   -12.340 1.00 43.70 ? 292 LYS B CE  1 
ATOM   4209 N NZ  . LYS B 1 312 ? 23.506  6.631   -11.958 1.00 45.39 ? 292 LYS B NZ  1 
ATOM   4210 N N   . TRP B 1 313 ? 23.056  1.944   -6.236  1.00 24.03 ? 293 TRP B N   1 
ATOM   4211 C CA  . TRP B 1 313 ? 23.083  0.945   -5.136  1.00 20.80 ? 293 TRP B CA  1 
ATOM   4212 C C   . TRP B 1 313 ? 23.585  -0.432  -5.616  1.00 20.18 ? 293 TRP B C   1 
ATOM   4213 O O   . TRP B 1 313 ? 23.410  -0.745  -6.817  1.00 19.76 ? 293 TRP B O   1 
ATOM   4214 C CB  . TRP B 1 313 ? 21.689  0.882   -4.516  1.00 21.02 ? 293 TRP B CB  1 
ATOM   4215 C CG  . TRP B 1 313 ? 21.343  2.096   -3.711  1.00 20.46 ? 293 TRP B CG  1 
ATOM   4216 C CD1 . TRP B 1 313 ? 20.750  3.246   -4.142  1.00 20.75 ? 293 TRP B CD1 1 
ATOM   4217 C CD2 . TRP B 1 313 ? 21.588  2.278   -2.309  1.00 20.92 ? 293 TRP B CD2 1 
ATOM   4218 N NE1 . TRP B 1 313 ? 20.571  4.115   -3.097  1.00 20.30 ? 293 TRP B NE1 1 
ATOM   4219 C CE2 . TRP B 1 313 ? 21.104  3.562   -1.966  1.00 20.20 ? 293 TRP B CE2 1 
ATOM   4220 C CE3 . TRP B 1 313 ? 22.167  1.480   -1.313  1.00 21.15 ? 293 TRP B CE3 1 
ATOM   4221 C CZ2 . TRP B 1 313 ? 21.188  4.064   -0.671  1.00 20.33 ? 293 TRP B CZ2 1 
ATOM   4222 C CZ3 . TRP B 1 313 ? 22.241  1.976   -0.027  1.00 21.03 ? 293 TRP B CZ3 1 
ATOM   4223 C CH2 . TRP B 1 313 ? 21.759  3.252   0.284   1.00 21.44 ? 293 TRP B CH2 1 
HETATM 4224 P PA  . NAP C 2 .   ? 9.866   -12.302 14.952  1.00 19.86 ? 301 NAP A PA  1 
HETATM 4225 O O1A . NAP C 2 .   ? 8.593   -11.635 15.277  1.00 20.52 ? 301 NAP A O1A 1 
HETATM 4226 O O2A . NAP C 2 .   ? 11.177  -11.607 14.839  1.00 20.85 ? 301 NAP A O2A 1 
HETATM 4227 O O5B . NAP C 2 .   ? 10.083  -13.615 15.861  1.00 20.40 ? 301 NAP A O5B 1 
HETATM 4228 C C5B . NAP C 2 .   ? 11.409  -14.100 16.068  1.00 19.23 ? 301 NAP A C5B 1 
HETATM 4229 C C4B . NAP C 2 .   ? 11.331  -15.328 16.955  1.00 17.95 ? 301 NAP A C4B 1 
HETATM 4230 O O4B . NAP C 2 .   ? 12.611  -15.979 16.972  1.00 17.01 ? 301 NAP A O4B 1 
HETATM 4231 C C3B . NAP C 2 .   ? 11.005  -14.971 18.386  1.00 16.95 ? 301 NAP A C3B 1 
HETATM 4232 O O3B . NAP C 2 .   ? 10.364  -16.090 19.018  1.00 16.98 ? 301 NAP A O3B 1 
HETATM 4233 C C2B . NAP C 2 .   ? 12.390  -14.775 18.991  1.00 16.97 ? 301 NAP A C2B 1 
HETATM 4234 O O2B . NAP C 2 .   ? 12.474  -14.844 20.407  1.00 16.07 ? 301 NAP A O2B 1 
HETATM 4235 C C1B . NAP C 2 .   ? 13.083  -15.946 18.340  1.00 17.75 ? 301 NAP A C1B 1 
HETATM 4236 N N9A . NAP C 2 .   ? 14.546  -15.807 18.466  1.00 20.30 ? 301 NAP A N9A 1 
HETATM 4237 C C8A . NAP C 2 .   ? 15.348  -14.898 17.845  1.00 20.29 ? 301 NAP A C8A 1 
HETATM 4238 N N7A . NAP C 2 .   ? 16.649  -15.128 18.179  1.00 20.85 ? 301 NAP A N7A 1 
HETATM 4239 C C5A . NAP C 2 .   ? 16.657  -16.181 19.013  1.00 21.31 ? 301 NAP A C5A 1 
HETATM 4240 C C6A . NAP C 2 .   ? 17.680  -16.900 19.771  1.00 23.07 ? 301 NAP A C6A 1 
HETATM 4241 N N6A . NAP C 2 .   ? 18.976  -16.545 19.631  1.00 23.77 ? 301 NAP A N6A 1 
HETATM 4242 N N1A . NAP C 2 .   ? 17.294  -17.925 20.539  1.00 22.82 ? 301 NAP A N1A 1 
HETATM 4243 C C2A . NAP C 2 .   ? 15.991  -18.304 20.666  1.00 24.75 ? 301 NAP A C2A 1 
HETATM 4244 N N3A . NAP C 2 .   ? 14.990  -17.691 20.016  1.00 23.45 ? 301 NAP A N3A 1 
HETATM 4245 C C4A . NAP C 2 .   ? 15.278  -16.620 19.214  1.00 21.10 ? 301 NAP A C4A 1 
HETATM 4246 O O3  . NAP C 2 .   ? 9.727   -13.012 13.495  1.00 18.93 ? 301 NAP A O3  1 
HETATM 4247 P PN  . NAP C 2 .   ? 8.403   -13.745 12.924  1.00 17.99 ? 301 NAP A PN  1 
HETATM 4248 O O1N . NAP C 2 .   ? 7.758   -14.506 14.096  1.00 17.09 ? 301 NAP A O1N 1 
HETATM 4249 O O2N . NAP C 2 .   ? 7.579   -12.757 12.186  1.00 17.74 ? 301 NAP A O2N 1 
HETATM 4250 O O5D . NAP C 2 .   ? 8.949   -14.809 11.879  1.00 16.63 ? 301 NAP A O5D 1 
HETATM 4251 C C5D . NAP C 2 .   ? 9.380   -16.096 12.350  1.00 15.80 ? 301 NAP A C5D 1 
HETATM 4252 C C4D . NAP C 2 .   ? 9.548   -17.055 11.190  1.00 15.63 ? 301 NAP A C4D 1 
HETATM 4253 O O4D . NAP C 2 .   ? 8.342   -17.067 10.443  1.00 17.16 ? 301 NAP A O4D 1 
HETATM 4254 C C3D . NAP C 2 .   ? 10.641  -16.614 10.227  1.00 16.36 ? 301 NAP A C3D 1 
HETATM 4255 O O3D . NAP C 2 .   ? 11.424  -17.721 9.796   1.00 16.08 ? 301 NAP A O3D 1 
HETATM 4256 C C2D . NAP C 2 .   ? 9.891   -15.934 9.095   1.00 16.61 ? 301 NAP A C2D 1 
HETATM 4257 O O2D . NAP C 2 .   ? 10.602  -15.830 7.834   1.00 16.23 ? 301 NAP A O2D 1 
HETATM 4258 C C1D . NAP C 2 .   ? 8.610   -16.763 9.072   1.00 16.92 ? 301 NAP A C1D 1 
HETATM 4259 N N1N . NAP C 2 .   ? 7.553   -16.034 8.374   1.00 17.62 ? 301 NAP A N1N 1 
HETATM 4260 C C2N . NAP C 2 .   ? 7.215   -14.766 8.764   1.00 16.99 ? 301 NAP A C2N 1 
HETATM 4261 C C3N . NAP C 2 .   ? 6.237   -14.050 8.093   1.00 17.00 ? 301 NAP A C3N 1 
HETATM 4262 C C7N . NAP C 2 .   ? 5.865   -12.667 8.570   1.00 17.02 ? 301 NAP A C7N 1 
HETATM 4263 O O7N . NAP C 2 .   ? 6.069   -12.276 9.736   1.00 19.77 ? 301 NAP A O7N 1 
HETATM 4264 N N7N . NAP C 2 .   ? 5.296   -11.860 7.750   1.00 14.75 ? 301 NAP A N7N 1 
HETATM 4265 C C4N . NAP C 2 .   ? 5.625   -14.623 6.961   1.00 18.05 ? 301 NAP A C4N 1 
HETATM 4266 C C5N . NAP C 2 .   ? 5.968   -15.946 6.577   1.00 16.88 ? 301 NAP A C5N 1 
HETATM 4267 C C6N . NAP C 2 .   ? 6.954   -16.620 7.297   1.00 17.04 ? 301 NAP A C6N 1 
HETATM 4268 P P2B . NAP C 2 .   ? 12.060  -13.564 21.328  1.00 20.07 ? 301 NAP A P2B 1 
HETATM 4269 O O1X . NAP C 2 .   ? 10.575  -13.545 21.244  1.00 17.75 ? 301 NAP A O1X 1 
HETATM 4270 O O2X . NAP C 2 .   ? 12.770  -12.402 20.669  1.00 19.14 ? 301 NAP A O2X 1 
HETATM 4271 O O3X . NAP C 2 .   ? 12.629  -13.943 22.687  1.00 19.74 ? 301 NAP A O3X 1 
HETATM 4272 C C   . TRS D 3 .   ? 4.598   13.955  -4.087  1.00 29.05 ? 302 TRS A C   1 
HETATM 4273 C C1  . TRS D 3 .   ? 3.226   13.792  -4.734  1.00 29.59 ? 302 TRS A C1  1 
HETATM 4274 C C2  . TRS D 3 .   ? 5.597   14.455  -5.115  1.00 30.93 ? 302 TRS A C2  1 
HETATM 4275 C C3  . TRS D 3 .   ? 4.538   14.905  -2.899  1.00 33.62 ? 302 TRS A C3  1 
HETATM 4276 N N   . TRS D 3 .   ? 5.078   12.614  -3.613  1.00 30.02 ? 302 TRS A N   1 
HETATM 4277 O O1  . TRS D 3 .   ? 2.599   12.563  -4.419  1.00 26.46 ? 302 TRS A O1  1 
HETATM 4278 O O2  . TRS D 3 .   ? 5.410   13.776  -6.349  1.00 29.12 ? 302 TRS A O2  1 
HETATM 4279 O O3  . TRS D 3 .   ? 3.448   14.609  -2.044  1.00 32.81 ? 302 TRS A O3  1 
HETATM 4280 P PA  . NAP E 2 .   ? 17.145  -0.606  -34.031 1.00 20.49 ? 301 NAP B PA  1 
HETATM 4281 O O1A . NAP E 2 .   ? 16.480  -1.727  -34.758 1.00 20.31 ? 301 NAP B O1A 1 
HETATM 4282 O O2A . NAP E 2 .   ? 18.545  -0.681  -33.469 1.00 20.99 ? 301 NAP B O2A 1 
HETATM 4283 O O5B . NAP E 2 .   ? 17.287  0.668   -34.939 1.00 19.81 ? 301 NAP B O5B 1 
HETATM 4284 C C5B . NAP E 2 .   ? 18.181  1.708   -34.600 1.00 21.63 ? 301 NAP B C5B 1 
HETATM 4285 C C4B . NAP E 2 .   ? 17.885  2.907   -35.526 1.00 22.03 ? 301 NAP B C4B 1 
HETATM 4286 O O4B . NAP E 2 .   ? 18.772  3.984   -35.210 1.00 22.75 ? 301 NAP B O4B 1 
HETATM 4287 C C3B . NAP E 2 .   ? 18.147  2.604   -37.009 1.00 23.13 ? 301 NAP B C3B 1 
HETATM 4288 O O3B . NAP E 2 .   ? 17.356  3.397   -37.903 1.00 21.39 ? 301 NAP B O3B 1 
HETATM 4289 C C2B . NAP E 2 .   ? 19.603  2.992   -37.146 1.00 23.67 ? 301 NAP B C2B 1 
HETATM 4290 O O2B . NAP E 2 .   ? 20.056  3.152   -38.478 1.00 26.46 ? 301 NAP B O2B 1 
HETATM 4291 C C1B . NAP E 2 .   ? 19.603  4.277   -36.384 1.00 23.58 ? 301 NAP B C1B 1 
HETATM 4292 N N9A . NAP E 2 .   ? 20.952  4.707   -35.973 1.00 24.23 ? 301 NAP B N9A 1 
HETATM 4293 C C8A . NAP E 2 .   ? 21.711  4.134   -35.003 1.00 25.73 ? 301 NAP B C8A 1 
HETATM 4294 N N7A . NAP E 2 .   ? 22.856  4.830   -34.816 1.00 25.20 ? 301 NAP B N7A 1 
HETATM 4295 C C5A . NAP E 2 .   ? 22.798  5.865   -35.682 1.00 24.46 ? 301 NAP B C5A 1 
HETATM 4296 C C6A . NAP E 2 .   ? 23.671  6.982   -36.016 1.00 26.58 ? 301 NAP B C6A 1 
HETATM 4297 N N6A . NAP E 2 .   ? 24.833  7.076   -35.347 1.00 26.74 ? 301 NAP B N6A 1 
HETATM 4298 N N1A . NAP E 2 .   ? 23.279  7.860   -36.973 1.00 27.68 ? 301 NAP B N1A 1 
HETATM 4299 C C2A . NAP E 2 .   ? 22.114  7.726   -37.627 1.00 26.44 ? 301 NAP B C2A 1 
HETATM 4300 N N3A . NAP E 2 .   ? 21.255  6.734   -37.358 1.00 24.91 ? 301 NAP B N3A 1 
HETATM 4301 C C4A . NAP E 2 .   ? 21.555  5.794   -36.428 1.00 24.75 ? 301 NAP B C4A 1 
HETATM 4302 O O3  . NAP E 2 .   ? 16.201  -0.068  -32.826 1.00 18.00 ? 301 NAP B O3  1 
HETATM 4303 P PN  . NAP E 2 .   ? 14.571  -0.115  -32.873 1.00 18.14 ? 301 NAP B PN  1 
HETATM 4304 O O1N . NAP E 2 .   ? 14.126  -1.427  -32.197 1.00 17.87 ? 301 NAP B O1N 1 
HETATM 4305 O O2N . NAP E 2 .   ? 14.101  0.331   -34.244 1.00 16.44 ? 301 NAP B O2N 1 
HETATM 4306 O O5D . NAP E 2 .   ? 14.130  1.065   -31.863 1.00 17.00 ? 301 NAP B O5D 1 
HETATM 4307 C C5D . NAP E 2 .   ? 14.153  2.471   -32.164 1.00 15.85 ? 301 NAP B C5D 1 
HETATM 4308 C C4D . NAP E 2 .   ? 13.568  3.247   -30.995 1.00 15.59 ? 301 NAP B C4D 1 
HETATM 4309 O O4D . NAP E 2 .   ? 12.284  2.707   -30.695 1.00 14.94 ? 301 NAP B O4D 1 
HETATM 4310 C C3D . NAP E 2 .   ? 14.439  3.165   -29.709 1.00 15.59 ? 301 NAP B C3D 1 
HETATM 4311 O O3D . NAP E 2 .   ? 14.420  4.406   -28.952 1.00 14.67 ? 301 NAP B O3D 1 
HETATM 4312 C C2D . NAP E 2 .   ? 13.732  2.138   -28.903 1.00 16.49 ? 301 NAP B C2D 1 
HETATM 4313 O O2D . NAP E 2 .   ? 14.011  2.330   -27.498 1.00 18.60 ? 301 NAP B O2D 1 
HETATM 4314 C C1D . NAP E 2 .   ? 12.249  2.381   -29.325 1.00 16.01 ? 301 NAP B C1D 1 
HETATM 4315 N N1N . NAP E 2 .   ? 11.402  1.250   -29.032 1.00 16.65 ? 301 NAP B N1N 1 
HETATM 4316 C C2N . NAP E 2 .   ? 11.755  -0.017  -29.423 1.00 15.98 ? 301 NAP B C2N 1 
HETATM 4317 C C3N . NAP E 2 .   ? 11.021  -1.140  -29.077 1.00 15.74 ? 301 NAP B C3N 1 
HETATM 4318 C C7N . NAP E 2 .   ? 11.474  -2.525  -29.543 1.00 16.05 ? 301 NAP B C7N 1 
HETATM 4319 O O7N . NAP E 2 .   ? 12.310  -2.659  -30.462 1.00 16.61 ? 301 NAP B O7N 1 
HETATM 4320 N N7N . NAP E 2 .   ? 10.961  -3.585  -28.952 1.00 14.76 ? 301 NAP B N7N 1 
HETATM 4321 C C4N . NAP E 2 .   ? 9.860   -0.958  -28.302 1.00 17.06 ? 301 NAP B C4N 1 
HETATM 4322 C C5N . NAP E 2 .   ? 9.479   0.360   -27.942 1.00 17.15 ? 301 NAP B C5N 1 
HETATM 4323 C C6N . NAP E 2 .   ? 10.257  1.452   -28.318 1.00 16.53 ? 301 NAP B C6N 1 
HETATM 4324 P P2B . NAP E 2 .   ? 20.676  1.874   -39.272 1.00 25.62 ? 301 NAP B P2B 1 
HETATM 4325 O O1X . NAP E 2 .   ? 21.520  2.623   -40.293 1.00 24.61 ? 301 NAP B O1X 1 
HETATM 4326 O O2X . NAP E 2 .   ? 19.439  1.094   -39.736 1.00 20.90 ? 301 NAP B O2X 1 
HETATM 4327 O O3X . NAP E 2 .   ? 21.487  1.166   -38.257 1.00 23.12 ? 301 NAP B O3X 1 
HETATM 4328 O O   . HOH F 4 .   ? -11.546 -26.758 13.836  1.00 29.62 ? 401 HOH A O   1 
HETATM 4329 O O   . HOH F 4 .   ? -9.897  -16.604 3.104   1.00 42.23 ? 402 HOH A O   1 
HETATM 4330 O O   . HOH F 4 .   ? 20.399  13.595  -18.957 1.00 18.41 ? 403 HOH A O   1 
HETATM 4331 O O   . HOH F 4 .   ? 15.132  -42.259 12.171  1.00 39.49 ? 404 HOH A O   1 
HETATM 4332 O O   . HOH F 4 .   ? 12.904  -15.111 7.495   1.00 19.98 ? 405 HOH A O   1 
HETATM 4333 O O   . HOH F 4 .   ? 18.820  14.068  -4.381  1.00 34.79 ? 406 HOH A O   1 
HETATM 4334 O O   . HOH F 4 .   ? 17.208  -22.289 -20.143 1.00 28.43 ? 407 HOH A O   1 
HETATM 4335 O O   . HOH F 4 .   ? -5.709  -28.433 1.922   1.00 35.41 ? 408 HOH A O   1 
HETATM 4336 O O   . HOH F 4 .   ? -2.427  -12.895 21.530  1.00 21.42 ? 409 HOH A O   1 
HETATM 4337 O O   . HOH F 4 .   ? 22.844  0.137   -23.110 1.00 39.93 ? 410 HOH A O   1 
HETATM 4338 O O   . HOH F 4 .   ? -7.644  -24.692 22.425  1.00 26.81 ? 411 HOH A O   1 
HETATM 4339 O O   . HOH F 4 .   ? 6.324   -16.634 0.514   1.00 20.28 ? 412 HOH A O   1 
HETATM 4340 O O   . HOH F 4 .   ? 22.466  0.665   -9.131  1.00 21.95 ? 413 HOH A O   1 
HETATM 4341 O O   . HOH F 4 .   ? -5.504  -15.264 2.908   1.00 24.48 ? 414 HOH A O   1 
HETATM 4342 O O   . HOH F 4 .   ? 19.446  -22.911 -27.182 1.00 25.98 ? 415 HOH A O   1 
HETATM 4343 O O   . HOH F 4 .   ? 16.446  -32.686 0.436   1.00 32.90 ? 416 HOH A O   1 
HETATM 4344 O O   . HOH F 4 .   ? 4.002   -37.978 16.169  1.00 21.73 ? 417 HOH A O   1 
HETATM 4345 O O   . HOH F 4 .   ? 9.801   -38.760 23.369  1.00 34.31 ? 418 HOH A O   1 
HETATM 4346 O O   . HOH F 4 .   ? 10.884  -36.236 7.278   1.00 31.77 ? 419 HOH A O   1 
HETATM 4347 O O   . HOH F 4 .   ? -6.234  -38.059 22.926  1.00 13.98 ? 420 HOH A O   1 
HETATM 4348 O O   . HOH F 4 .   ? 11.867  -27.122 2.956   1.00 12.73 ? 421 HOH A O   1 
HETATM 4349 O O   . HOH F 4 .   ? 13.191  -10.174 21.861  1.00 23.77 ? 422 HOH A O   1 
HETATM 4350 O O   . HOH F 4 .   ? 4.891   -9.361  8.163   1.00 15.70 ? 423 HOH A O   1 
HETATM 4351 O O   . HOH F 4 .   ? 0.468   13.701  -5.292  1.00 29.91 ? 424 HOH A O   1 
HETATM 4352 O O   . HOH F 4 .   ? -1.661  -21.355 5.514   1.00 16.76 ? 425 HOH A O   1 
HETATM 4353 O O   . HOH F 4 .   ? 19.520  -5.225  -8.265  1.00 11.64 ? 426 HOH A O   1 
HETATM 4354 O O   . HOH F 4 .   ? -3.266  13.865  -6.086  1.00 40.84 ? 427 HOH A O   1 
HETATM 4355 O O   . HOH F 4 .   ? 28.157  -5.019  -22.694 1.00 30.77 ? 428 HOH A O   1 
HETATM 4356 O O   . HOH F 4 .   ? 13.133  -16.394 -25.793 1.00 26.42 ? 429 HOH A O   1 
HETATM 4357 O O   . HOH F 4 .   ? 26.028  -16.115 -12.505 1.00 22.19 ? 430 HOH A O   1 
HETATM 4358 O O   . HOH F 4 .   ? 6.808   -20.332 -23.846 1.00 26.47 ? 431 HOH A O   1 
HETATM 4359 O O   . HOH F 4 .   ? 23.009  -18.582 -25.971 1.00 26.96 ? 432 HOH A O   1 
HETATM 4360 O O   . HOH F 4 .   ? 22.099  -1.839  -25.237 1.00 25.07 ? 433 HOH A O   1 
HETATM 4361 O O   . HOH F 4 .   ? -17.359 -36.856 21.621  1.00 16.10 ? 434 HOH A O   1 
HETATM 4362 O O   . HOH F 4 .   ? 17.218  -31.393 28.493  1.00 32.12 ? 435 HOH A O   1 
HETATM 4363 O O   . HOH F 4 .   ? 11.191  -21.309 -30.595 1.00 20.25 ? 436 HOH A O   1 
HETATM 4364 O O   . HOH F 4 .   ? 0.984   -11.962 15.850  1.00 18.61 ? 437 HOH A O   1 
HETATM 4365 O O   . HOH F 4 .   ? 10.522  -42.415 11.600  1.00 34.12 ? 438 HOH A O   1 
HETATM 4366 O O   . HOH F 4 .   ? 1.133   -28.982 28.783  1.00 26.33 ? 439 HOH A O   1 
HETATM 4367 O O   . HOH F 4 .   ? -7.807  -36.164 19.938  1.00 26.40 ? 440 HOH A O   1 
HETATM 4368 O O   . HOH F 4 .   ? -5.730  -18.424 -1.795  1.00 33.73 ? 441 HOH A O   1 
HETATM 4369 O O   . HOH F 4 .   ? -10.049 -32.979 27.092  1.00 44.06 ? 442 HOH A O   1 
HETATM 4370 O O   . HOH F 4 .   ? 21.452  14.300  -9.640  1.00 34.13 ? 443 HOH A O   1 
HETATM 4371 O O   . HOH F 4 .   ? 13.010  -9.855  -23.291 1.00 23.69 ? 444 HOH A O   1 
HETATM 4372 O O   . HOH F 4 .   ? -14.601 -29.815 18.539  1.00 33.58 ? 445 HOH A O   1 
HETATM 4373 O O   . HOH F 4 .   ? 30.324  -7.409  -18.592 1.00 38.53 ? 446 HOH A O   1 
HETATM 4374 O O   . HOH F 4 .   ? 10.819  -20.131 29.588  1.00 23.47 ? 447 HOH A O   1 
HETATM 4375 O O   . HOH F 4 .   ? 21.543  -16.806 -29.504 1.00 22.48 ? 448 HOH A O   1 
HETATM 4376 O O   . HOH F 4 .   ? 20.386  -23.239 -17.111 1.00 25.82 ? 449 HOH A O   1 
HETATM 4377 O O   . HOH F 4 .   ? 21.503  -23.111 -21.943 1.00 26.79 ? 450 HOH A O   1 
HETATM 4378 O O   . HOH F 4 .   ? -4.030  -14.649 12.138  1.00 20.80 ? 451 HOH A O   1 
HETATM 4379 O O   . HOH F 4 .   ? 11.571  -21.981 3.849   1.00 11.99 ? 452 HOH A O   1 
HETATM 4380 O O   . HOH F 4 .   ? -7.046  -23.440 25.178  1.00 31.33 ? 453 HOH A O   1 
HETATM 4381 O O   . HOH F 4 .   ? 1.260   -12.308 24.567  1.00 32.12 ? 454 HOH A O   1 
HETATM 4382 O O   . HOH F 4 .   ? 21.522  3.755   -27.336 1.00 23.11 ? 455 HOH A O   1 
HETATM 4383 O O   . HOH F 4 .   ? 17.364  -19.849 8.111   1.00 21.41 ? 456 HOH A O   1 
HETATM 4384 O O   . HOH F 4 .   ? -5.577  -36.572 6.056   1.00 32.58 ? 457 HOH A O   1 
HETATM 4385 O O   . HOH F 4 .   ? -8.295  -23.944 6.822   1.00 31.63 ? 458 HOH A O   1 
HETATM 4386 O O   . HOH F 4 .   ? 17.598  -26.975 24.084  1.00 23.44 ? 459 HOH A O   1 
HETATM 4387 O O   . HOH F 4 .   ? 6.618   -36.862 26.045  1.00 30.78 ? 460 HOH A O   1 
HETATM 4388 O O   . HOH F 4 .   ? -9.478  -20.498 24.441  1.00 23.76 ? 461 HOH A O   1 
HETATM 4389 O O   . HOH F 4 .   ? -3.945  3.527   -7.548  1.00 42.39 ? 462 HOH A O   1 
HETATM 4390 O O   . HOH F 4 .   ? 7.333   -17.503 3.525   1.00 20.22 ? 463 HOH A O   1 
HETATM 4391 O O   . HOH F 4 .   ? 28.717  -6.905  -15.944 1.00 26.42 ? 464 HOH A O   1 
HETATM 4392 O O   . HOH F 4 .   ? 16.815  -9.774  -31.290 1.00 23.27 ? 465 HOH A O   1 
HETATM 4393 O O   . HOH F 4 .   ? 25.716  -9.452  -28.021 1.00 19.48 ? 466 HOH A O   1 
HETATM 4394 O O   . HOH F 4 .   ? 30.965  -12.932 -14.829 1.00 36.47 ? 467 HOH A O   1 
HETATM 4395 O O   . HOH F 4 .   ? 9.560   -22.235 5.786   1.00 16.30 ? 468 HOH A O   1 
HETATM 4396 O O   . HOH F 4 .   ? 4.112   -37.953 -3.123  1.00 40.17 ? 469 HOH A O   1 
HETATM 4397 O O   . HOH F 4 .   ? 31.376  -21.902 -13.994 1.00 41.01 ? 470 HOH A O   1 
HETATM 4398 O O   . HOH F 4 .   ? 7.888   -10.090 12.042  1.00 13.45 ? 471 HOH A O   1 
HETATM 4399 O O   . HOH F 4 .   ? 1.766   -36.451 16.494  1.00 17.04 ? 472 HOH A O   1 
HETATM 4400 O O   . HOH F 4 .   ? -2.173  -26.659 27.660  1.00 21.74 ? 473 HOH A O   1 
HETATM 4401 O O   . HOH F 4 .   ? 0.668   -34.772 26.374  1.00 28.60 ? 474 HOH A O   1 
HETATM 4402 O O   . HOH F 4 .   ? 0.166   -29.397 24.848  1.00 14.88 ? 475 HOH A O   1 
HETATM 4403 O O   . HOH F 4 .   ? 27.708  -16.730 -16.366 1.00 34.18 ? 476 HOH A O   1 
HETATM 4404 O O   . HOH F 4 .   ? 20.241  -18.343 5.562   1.00 35.86 ? 477 HOH A O   1 
HETATM 4405 O O   . HOH F 4 .   ? 12.092  -33.435 25.786  1.00 27.11 ? 478 HOH A O   1 
HETATM 4406 O O   . HOH F 4 .   ? -4.061  -33.557 11.891  1.00 19.43 ? 479 HOH A O   1 
HETATM 4407 O O   . HOH F 4 .   ? 7.678   -16.584 15.855  1.00 10.44 ? 480 HOH A O   1 
HETATM 4408 O O   . HOH F 4 .   ? 11.538  -15.519 4.001   1.00 26.44 ? 481 HOH A O   1 
HETATM 4409 O O   . HOH F 4 .   ? 14.704  -19.263 -29.709 1.00 22.51 ? 482 HOH A O   1 
HETATM 4410 O O   . HOH F 4 .   ? 10.824  -35.290 24.722  1.00 37.53 ? 483 HOH A O   1 
HETATM 4411 O O   . HOH F 4 .   ? 5.113   -11.752 19.633  1.00 20.29 ? 484 HOH A O   1 
HETATM 4412 O O   . HOH F 4 .   ? -3.629  -37.846 12.672  1.00 37.98 ? 485 HOH A O   1 
HETATM 4413 O O   . HOH F 4 .   ? 16.933  -25.695 -27.450 1.00 39.22 ? 486 HOH A O   1 
HETATM 4414 O O   . HOH F 4 .   ? 2.443   -10.542 17.273  1.00 37.17 ? 487 HOH A O   1 
HETATM 4415 O O   . HOH F 4 .   ? 21.238  8.370   -9.657  1.00 25.08 ? 488 HOH A O   1 
HETATM 4416 O O   . HOH F 4 .   ? -7.320  -17.820 19.295  1.00 26.67 ? 489 HOH A O   1 
HETATM 4417 O O   . HOH F 4 .   ? -9.313  -18.051 22.590  1.00 29.47 ? 490 HOH A O   1 
HETATM 4418 O O   . HOH F 4 .   ? -1.448  -31.382 -1.351  1.00 34.94 ? 491 HOH A O   1 
HETATM 4419 O O   . HOH F 4 .   ? 11.365  -19.609 2.661   1.00 15.97 ? 492 HOH A O   1 
HETATM 4420 O O   . HOH F 4 .   ? 14.932  -24.108 5.463   1.00 18.69 ? 493 HOH A O   1 
HETATM 4421 O O   . HOH F 4 .   ? -0.025  -10.420 3.384   1.00 28.56 ? 494 HOH A O   1 
HETATM 4422 O O   . HOH F 4 .   ? 23.772  -19.185 -23.103 1.00 25.77 ? 495 HOH A O   1 
HETATM 4423 O O   . HOH F 4 .   ? 16.939  5.061   -25.658 1.00 17.56 ? 496 HOH A O   1 
HETATM 4424 O O   . HOH F 4 .   ? 6.870   -20.011 6.978   1.00 14.53 ? 497 HOH A O   1 
HETATM 4425 O O   . HOH F 4 .   ? -1.093  -33.719 18.252  1.00 23.70 ? 498 HOH A O   1 
HETATM 4426 O O   . HOH F 4 .   ? 14.836  -12.148 -29.221 1.00 18.31 ? 499 HOH A O   1 
HETATM 4427 O O   . HOH F 4 .   ? -5.213  -34.943 9.431   1.00 25.90 ? 500 HOH A O   1 
HETATM 4428 O O   . HOH F 4 .   ? 7.409   8.696   -4.172  1.00 19.49 ? 501 HOH A O   1 
HETATM 4429 O O   . HOH F 4 .   ? 9.296   -13.928 6.255   1.00 28.76 ? 502 HOH A O   1 
HETATM 4430 O O   . HOH F 4 .   ? 22.737  -12.289 -29.889 1.00 23.29 ? 503 HOH A O   1 
HETATM 4431 O O   . HOH F 4 .   ? -7.691  -21.347 13.413  1.00 21.94 ? 504 HOH A O   1 
HETATM 4432 O O   . HOH F 4 .   ? 25.901  -17.413 -5.645  1.00 20.42 ? 505 HOH A O   1 
HETATM 4433 O O   . HOH F 4 .   ? -4.316  -28.612 6.077   1.00 25.16 ? 506 HOH A O   1 
HETATM 4434 O O   . HOH F 4 .   ? 30.734  -13.146 -6.983  1.00 41.40 ? 507 HOH A O   1 
HETATM 4435 O O   . HOH F 4 .   ? 9.650   -10.403 17.858  1.00 36.14 ? 508 HOH A O   1 
HETATM 4436 O O   . HOH F 4 .   ? 14.815  -17.155 7.497   1.00 26.64 ? 509 HOH A O   1 
HETATM 4437 O O   . HOH F 4 .   ? 14.410  -12.416 26.373  1.00 35.79 ? 510 HOH A O   1 
HETATM 4438 O O   . HOH F 4 .   ? -9.707  -33.667 15.756  1.00 33.54 ? 511 HOH A O   1 
HETATM 4439 O O   . HOH F 4 .   ? 12.122  -18.202 21.073  1.00 15.55 ? 512 HOH A O   1 
HETATM 4440 O O   . HOH F 4 .   ? -3.908  -15.855 14.796  1.00 24.17 ? 513 HOH A O   1 
HETATM 4441 O O   . HOH F 4 .   ? 12.757  -9.121  -0.054  1.00 27.01 ? 514 HOH A O   1 
HETATM 4442 O O   . HOH F 4 .   ? -4.470  -24.720 25.175  1.00 22.43 ? 515 HOH A O   1 
HETATM 4443 O O   . HOH F 4 .   ? -5.938  -12.871 25.237  1.00 31.73 ? 516 HOH A O   1 
HETATM 4444 O O   . HOH F 4 .   ? -9.740  -26.107 11.001  1.00 39.76 ? 517 HOH A O   1 
HETATM 4445 O O   . HOH F 4 .   ? 3.620   -40.327 19.838  1.00 34.88 ? 518 HOH A O   1 
HETATM 4446 O O   . HOH F 4 .   ? 11.765  -8.890  15.487  1.00 41.24 ? 519 HOH A O   1 
HETATM 4447 O O   . HOH F 4 .   ? 13.697  -36.037 9.879   1.00 27.47 ? 520 HOH A O   1 
HETATM 4448 O O   . HOH F 4 .   ? 3.245   -35.990 26.699  1.00 19.24 ? 521 HOH A O   1 
HETATM 4449 O O   . HOH F 4 .   ? 11.728  -14.305 -22.718 1.00 30.85 ? 522 HOH A O   1 
HETATM 4450 O O   . HOH F 4 .   ? 22.683  7.891   -15.282 1.00 41.64 ? 523 HOH A O   1 
HETATM 4451 O O   . HOH F 4 .   ? 0.320   -0.767  -17.543 1.00 30.96 ? 524 HOH A O   1 
HETATM 4452 O O   . HOH F 4 .   ? 13.833  16.366  -8.291  1.00 33.12 ? 525 HOH A O   1 
HETATM 4453 O O   . HOH F 4 .   ? 22.038  -23.552 22.407  1.00 35.12 ? 526 HOH A O   1 
HETATM 4454 O O   . HOH F 4 .   ? 1.050   -13.702 -0.137  1.00 39.81 ? 527 HOH A O   1 
HETATM 4455 O O   . HOH F 4 .   ? 13.415  4.142   -22.191 1.00 25.28 ? 528 HOH A O   1 
HETATM 4456 O O   . HOH F 4 .   ? 4.781   -40.987 2.783   1.00 35.04 ? 529 HOH A O   1 
HETATM 4457 O O   . HOH F 4 .   ? 6.681   -18.608 26.714  1.00 26.25 ? 530 HOH A O   1 
HETATM 4458 O O   . HOH F 4 .   ? 21.537  -32.726 0.455   1.00 37.03 ? 531 HOH A O   1 
HETATM 4459 O O   . HOH F 4 .   ? 14.630  -33.955 25.890  1.00 28.82 ? 532 HOH A O   1 
HETATM 4460 O O   . HOH F 4 .   ? 22.682  6.123   -18.017 1.00 34.57 ? 533 HOH A O   1 
HETATM 4461 O O   . HOH F 4 .   ? 2.544   -37.358 12.033  1.00 28.15 ? 534 HOH A O   1 
HETATM 4462 O O   . HOH F 4 .   ? -2.175  -12.404 30.799  1.00 37.63 ? 535 HOH A O   1 
HETATM 4463 O O   . HOH F 4 .   ? 14.074  12.833  -15.295 1.00 20.84 ? 536 HOH A O   1 
HETATM 4464 O O   . HOH F 4 .   ? -2.688  -35.469 21.497  1.00 18.67 ? 537 HOH A O   1 
HETATM 4465 O O   . HOH F 4 .   ? -1.159  -40.964 6.971   1.00 29.08 ? 538 HOH A O   1 
HETATM 4466 O O   . HOH F 4 .   ? 10.635  -30.024 -22.491 1.00 38.14 ? 539 HOH A O   1 
HETATM 4467 O O   . HOH F 4 .   ? -1.590  -17.422 0.645   1.00 21.12 ? 540 HOH A O   1 
HETATM 4468 O O   . HOH F 4 .   ? 12.055  -15.658 29.690  1.00 24.06 ? 541 HOH A O   1 
HETATM 4469 O O   . HOH F 4 .   ? 30.504  -21.514 -10.049 1.00 30.42 ? 542 HOH A O   1 
HETATM 4470 O O   . HOH F 4 .   ? 17.739  -11.335 19.438  1.00 41.45 ? 543 HOH A O   1 
HETATM 4471 O O   . HOH F 4 .   ? -1.219  -13.309 17.201  1.00 19.70 ? 544 HOH A O   1 
HETATM 4472 O O   . HOH F 4 .   ? 20.040  -19.682 9.654   1.00 25.47 ? 545 HOH A O   1 
HETATM 4473 O O   . HOH F 4 .   ? 15.748  -27.480 26.461  1.00 25.24 ? 546 HOH A O   1 
HETATM 4474 O O   . HOH F 4 .   ? 3.575   -31.574 -6.578  1.00 35.53 ? 547 HOH A O   1 
HETATM 4475 O O   . HOH F 4 .   ? 19.606  -27.341 -2.554  1.00 21.82 ? 548 HOH A O   1 
HETATM 4476 O O   . HOH F 4 .   ? 7.462   -25.082 -22.987 1.00 44.91 ? 549 HOH A O   1 
HETATM 4477 O O   . HOH F 4 .   ? 20.194  7.771   -21.596 1.00 29.96 ? 550 HOH A O   1 
HETATM 4478 O O   . HOH F 4 .   ? -0.938  12.149  -11.874 1.00 39.97 ? 551 HOH A O   1 
HETATM 4479 O O   . HOH F 4 .   ? 33.802  -9.364  -19.042 1.00 25.29 ? 552 HOH A O   1 
HETATM 4480 O O   . HOH F 4 .   ? 0.525   -31.615 28.248  1.00 33.76 ? 553 HOH A O   1 
HETATM 4481 O O   . HOH F 4 .   ? 9.030   -9.299  -25.336 1.00 33.12 ? 554 HOH A O   1 
HETATM 4482 O O   . HOH F 4 .   ? 25.210  -16.139 -29.020 1.00 42.58 ? 555 HOH A O   1 
HETATM 4483 O O   . HOH F 4 .   ? -4.739  -26.758 27.697  1.00 29.33 ? 556 HOH A O   1 
HETATM 4484 O O   . HOH F 4 .   ? 11.480  -9.608  24.326  1.00 49.66 ? 557 HOH A O   1 
HETATM 4485 O O   . HOH F 4 .   ? 13.370  -35.722 2.232   1.00 28.35 ? 558 HOH A O   1 
HETATM 4486 O O   . HOH F 4 .   ? 24.852  -0.038  -21.091 1.00 32.15 ? 559 HOH A O   1 
HETATM 4487 O O   . HOH F 4 .   ? 0.870   15.324  -7.793  1.00 36.96 ? 560 HOH A O   1 
HETATM 4488 O O   . HOH F 4 .   ? 8.424   -40.233 8.751   1.00 39.25 ? 561 HOH A O   1 
HETATM 4489 O O   . HOH F 4 .   ? -1.324  -23.302 -4.096  1.00 36.31 ? 562 HOH A O   1 
HETATM 4490 O O   . HOH F 4 .   ? -15.867 -36.097 19.117  1.00 28.33 ? 563 HOH A O   1 
HETATM 4491 O O   . HOH F 4 .   ? 20.192  -7.012  -30.465 1.00 30.35 ? 564 HOH A O   1 
HETATM 4492 O O   . HOH F 4 .   ? 17.558  17.022  -9.324  1.00 33.95 ? 565 HOH A O   1 
HETATM 4493 O O   . HOH F 4 .   ? 12.559  -7.450  -21.915 1.00 25.44 ? 566 HOH A O   1 
HETATM 4494 O O   . HOH F 4 .   ? 18.543  -31.876 -0.652  1.00 37.05 ? 567 HOH A O   1 
HETATM 4495 O O   . HOH F 4 .   ? 0.587   -9.236  9.814   1.00 28.33 ? 568 HOH A O   1 
HETATM 4496 O O   . HOH F 4 .   ? 18.058  -20.264 -28.720 1.00 36.36 ? 569 HOH A O   1 
HETATM 4497 O O   . HOH F 4 .   ? 8.601   -19.873 27.734  1.00 21.64 ? 570 HOH A O   1 
HETATM 4498 O O   . HOH F 4 .   ? 5.717   -9.229  10.832  1.00 22.06 ? 571 HOH A O   1 
HETATM 4499 O O   . HOH F 4 .   ? 14.762  -22.218 28.487  1.00 28.14 ? 572 HOH A O   1 
HETATM 4500 O O   . HOH F 4 .   ? 8.665   12.576  -3.483  1.00 40.43 ? 573 HOH A O   1 
HETATM 4501 O O   . HOH F 4 .   ? 19.495  -15.503 23.415  1.00 25.83 ? 574 HOH A O   1 
HETATM 4502 O O   . HOH F 4 .   ? 7.030   -41.571 5.472   1.00 42.96 ? 575 HOH A O   1 
HETATM 4503 O O   . HOH F 4 .   ? 7.856   -36.216 -4.422  1.00 23.33 ? 576 HOH A O   1 
HETATM 4504 O O   . HOH F 4 .   ? -6.427  -17.300 14.911  1.00 29.52 ? 577 HOH A O   1 
HETATM 4505 O O   . HOH F 4 .   ? 0.931   9.488   -12.504 1.00 33.89 ? 578 HOH A O   1 
HETATM 4506 O O   . HOH F 4 .   ? 11.538  -10.453 -31.228 1.00 29.17 ? 579 HOH A O   1 
HETATM 4507 O O   . HOH F 4 .   ? 8.743   -40.512 -1.638  1.00 42.41 ? 580 HOH A O   1 
HETATM 4508 O O   . HOH F 4 .   ? -12.966 -32.460 10.157  1.00 36.98 ? 581 HOH A O   1 
HETATM 4509 O O   . HOH F 4 .   ? 25.342  -4.661  -8.401  1.00 34.89 ? 582 HOH A O   1 
HETATM 4510 O O   . HOH F 4 .   ? -1.669  -29.380 27.964  1.00 35.03 ? 583 HOH A O   1 
HETATM 4511 O O   . HOH F 4 .   ? 16.244  -35.808 -1.877  1.00 37.37 ? 584 HOH A O   1 
HETATM 4512 O O   . HOH F 4 .   ? 14.148  -9.663  -31.342 1.00 44.43 ? 585 HOH A O   1 
HETATM 4513 O O   . HOH F 4 .   ? 3.646   16.427  -5.135  1.00 28.05 ? 586 HOH A O   1 
HETATM 4514 O O   . HOH F 4 .   ? -10.167 -12.132 9.939   1.00 48.40 ? 587 HOH A O   1 
HETATM 4515 O O   . HOH F 4 .   ? -2.220  -36.371 14.491  1.00 29.85 ? 588 HOH A O   1 
HETATM 4516 O O   . HOH F 4 .   ? -2.981  -15.288 1.025   1.00 27.28 ? 589 HOH A O   1 
HETATM 4517 O O   . HOH F 4 .   ? 6.945   -25.188 34.112  1.00 28.90 ? 590 HOH A O   1 
HETATM 4518 O O   . HOH F 4 .   ? 16.325  -11.939 24.825  1.00 45.09 ? 591 HOH A O   1 
HETATM 4519 O O   . HOH F 4 .   ? 4.510   -27.725 -7.635  1.00 43.05 ? 592 HOH A O   1 
HETATM 4520 O O   . HOH F 4 .   ? 0.668   -7.295  4.321   1.00 42.86 ? 593 HOH A O   1 
HETATM 4521 O O   . HOH F 4 .   ? 27.014  -25.140 -14.438 1.00 39.31 ? 594 HOH A O   1 
HETATM 4522 O O   . HOH F 4 .   ? 13.247  -3.497  -22.568 1.00 34.39 ? 595 HOH A O   1 
HETATM 4523 O O   . HOH F 4 .   ? -1.371  -11.207 13.770  1.00 34.29 ? 596 HOH A O   1 
HETATM 4524 O O   . HOH F 4 .   ? 2.484   -19.776 -21.650 1.00 42.37 ? 597 HOH A O   1 
HETATM 4525 O O   . HOH F 4 .   ? -6.487  -14.014 17.956  1.00 41.65 ? 598 HOH A O   1 
HETATM 4526 O O   . HOH F 4 .   ? 10.755  -11.598 -23.131 1.00 29.41 ? 599 HOH A O   1 
HETATM 4527 O O   . HOH F 4 .   ? -4.938  -12.362 22.006  1.00 30.09 ? 600 HOH A O   1 
HETATM 4528 O O   . HOH F 4 .   ? 10.109  -9.167  12.371  1.00 26.55 ? 601 HOH A O   1 
HETATM 4529 O O   . HOH F 4 .   ? 21.636  -28.865 -3.628  1.00 26.88 ? 602 HOH A O   1 
HETATM 4530 O O   . HOH F 4 .   ? 7.646   -22.554 -24.816 1.00 27.08 ? 603 HOH A O   1 
HETATM 4531 O O   . HOH F 4 .   ? 11.890  -33.482 29.379  1.00 35.09 ? 604 HOH A O   1 
HETATM 4532 O O   . HOH F 4 .   ? 31.570  -20.053 -15.689 1.00 37.17 ? 605 HOH A O   1 
HETATM 4533 O O   . HOH F 4 .   ? -1.875  -11.495 19.306  1.00 28.77 ? 606 HOH A O   1 
HETATM 4534 O O   . HOH F 4 .   ? 9.957   -24.717 -27.388 1.00 29.72 ? 607 HOH A O   1 
HETATM 4535 O O   . HOH F 4 .   ? -1.529  -33.281 -3.283  1.00 36.98 ? 608 HOH A O   1 
HETATM 4536 O O   . HOH F 4 .   ? -3.483  -13.530 15.888  1.00 26.75 ? 609 HOH A O   1 
HETATM 4537 O O   . HOH F 4 .   ? 3.537   -34.164 -4.754  1.00 42.09 ? 610 HOH A O   1 
HETATM 4538 O O   . HOH F 4 .   ? 2.479   -7.767  8.210   1.00 18.66 ? 611 HOH A O   1 
HETATM 4539 O O   . HOH F 4 .   ? 10.068  -8.339  -29.956 1.00 23.97 ? 612 HOH A O   1 
HETATM 4540 O O   . HOH F 4 .   ? -4.688  -36.860 25.532  1.00 28.39 ? 613 HOH A O   1 
HETATM 4541 O O   . HOH F 4 .   ? 29.384  -16.300 -2.741  1.00 37.11 ? 614 HOH A O   1 
HETATM 4542 O O   . HOH F 4 .   ? 19.483  -12.345 24.385  1.00 36.58 ? 615 HOH A O   1 
HETATM 4543 O O   . HOH F 4 .   ? -6.870  -25.934 26.116  1.00 31.32 ? 616 HOH A O   1 
HETATM 4544 O O   . HOH F 4 .   ? -8.833  -24.557 4.147   1.00 31.57 ? 617 HOH A O   1 
HETATM 4545 O O   . HOH F 4 .   ? 4.053   -21.189 -22.908 1.00 37.74 ? 618 HOH A O   1 
HETATM 4546 O O   . HOH F 4 .   ? 7.085   -14.970 3.476   1.00 25.72 ? 619 HOH A O   1 
HETATM 4547 O O   . HOH F 4 .   ? -0.700  8.979   -14.023 1.00 41.13 ? 620 HOH A O   1 
HETATM 4548 O O   . HOH F 4 .   ? 8.311   -21.201 33.164  1.00 27.25 ? 621 HOH A O   1 
HETATM 4549 O O   . HOH F 4 .   ? -7.498  -18.830 12.950  1.00 28.69 ? 622 HOH A O   1 
HETATM 4550 O O   . HOH F 4 .   ? 16.361  -29.095 29.149  1.00 48.50 ? 623 HOH A O   1 
HETATM 4551 O O   . HOH F 4 .   ? -0.679  -5.315  -20.615 1.00 37.52 ? 624 HOH A O   1 
HETATM 4552 O O   . HOH F 4 .   ? 3.916   -40.548 15.269  1.00 35.18 ? 625 HOH A O   1 
HETATM 4553 O O   . HOH F 4 .   ? 8.324   9.912   -2.223  1.00 26.34 ? 626 HOH A O   1 
HETATM 4554 O O   . HOH F 4 .   ? 22.151  -24.226 -19.085 1.00 32.35 ? 627 HOH A O   1 
HETATM 4555 O O   . HOH F 4 .   ? 9.811   -22.334 -26.422 1.00 17.84 ? 628 HOH A O   1 
HETATM 4556 O O   . HOH F 4 .   ? 4.315   -14.455 -0.433  1.00 35.99 ? 629 HOH A O   1 
HETATM 4557 O O   . HOH F 4 .   ? 5.745   17.949  -6.168  1.00 39.92 ? 630 HOH A O   1 
HETATM 4558 O O   . HOH F 4 .   ? 22.215  -13.961 20.340  1.00 41.19 ? 631 HOH A O   1 
HETATM 4559 O O   . HOH F 4 .   ? 25.433  -17.880 -26.576 1.00 36.46 ? 632 HOH A O   1 
HETATM 4560 O O   . HOH F 4 .   ? 16.321  -28.644 -3.788  1.00 26.74 ? 633 HOH A O   1 
HETATM 4561 O O   . HOH F 4 .   ? 29.631  -4.275  -10.116 1.00 38.32 ? 634 HOH A O   1 
HETATM 4562 O O   . HOH F 4 .   ? 20.610  -19.318 -30.365 1.00 20.91 ? 635 HOH A O   1 
HETATM 4563 O O   . HOH F 4 .   ? 2.367   -9.034  12.096  1.00 28.37 ? 636 HOH A O   1 
HETATM 4564 O O   . HOH F 4 .   ? 18.234  -7.570  -31.548 1.00 34.41 ? 637 HOH A O   1 
HETATM 4565 O O   . HOH F 4 .   ? -2.074  -36.325 19.083  1.00 16.34 ? 638 HOH A O   1 
HETATM 4566 O O   . HOH F 4 .   ? 20.971  -35.518 5.519   1.00 35.41 ? 639 HOH A O   1 
HETATM 4567 O O   . HOH F 4 .   ? -0.308  -37.974 17.756  1.00 23.74 ? 640 HOH A O   1 
HETATM 4568 O O   . HOH F 4 .   ? 33.540  -14.163 -13.196 1.00 35.61 ? 641 HOH A O   1 
HETATM 4569 O O   . HOH F 4 .   ? 13.577  18.157  -10.615 1.00 43.06 ? 642 HOH A O   1 
HETATM 4570 O O   . HOH F 4 .   ? 9.735   -20.377 -28.294 1.00 26.66 ? 643 HOH A O   1 
HETATM 4571 O O   . HOH F 4 .   ? -3.167  -32.620 16.700  1.00 26.22 ? 644 HOH A O   1 
HETATM 4572 O O   . HOH F 4 .   ? 24.363  -2.652  -25.510 1.00 33.33 ? 645 HOH A O   1 
HETATM 4573 O O   . HOH F 4 .   ? 14.976  -40.647 7.880   1.00 31.18 ? 646 HOH A O   1 
HETATM 4574 O O   . HOH F 4 .   ? -3.993  -10.014 18.579  1.00 33.68 ? 647 HOH A O   1 
HETATM 4575 O O   . HOH F 4 .   ? -5.063  -33.845 -2.043  1.00 37.26 ? 648 HOH A O   1 
HETATM 4576 O O   . HOH F 4 .   ? 7.040   -11.095 -0.657  1.00 33.01 ? 649 HOH A O   1 
HETATM 4577 O O   . HOH F 4 .   ? -1.499  -35.153 -7.153  1.00 41.56 ? 650 HOH A O   1 
HETATM 4578 O O   . HOH F 4 .   ? 31.982  -26.066 -16.373 1.00 37.09 ? 651 HOH A O   1 
HETATM 4579 O O   . HOH F 4 .   ? 21.548  -38.126 5.629   1.00 39.91 ? 652 HOH A O   1 
HETATM 4580 O O   . HOH F 4 .   ? 5.894   -22.528 -27.554 1.00 39.90 ? 653 HOH A O   1 
HETATM 4581 O O   . HOH F 4 .   ? 29.337  -29.451 -18.449 1.00 36.23 ? 654 HOH A O   1 
HETATM 4582 O O   . HOH G 4 .   ? -1.570  14.104  -38.986 1.00 26.91 ? 401 HOH B O   1 
HETATM 4583 O O   . HOH G 4 .   ? 15.000  -28.376 -13.998 1.00 25.39 ? 402 HOH B O   1 
HETATM 4584 O O   . HOH G 4 .   ? 21.115  -0.354  -36.541 1.00 29.44 ? 403 HOH B O   1 
HETATM 4585 O O   . HOH G 4 .   ? 15.780  -26.329 -16.889 1.00 26.39 ? 404 HOH B O   1 
HETATM 4586 O O   . HOH G 4 .   ? -4.686  7.943   -31.696 1.00 20.82 ? 405 HOH B O   1 
HETATM 4587 O O   . HOH G 4 .   ? -1.004  1.260   4.794   1.00 43.65 ? 406 HOH B O   1 
HETATM 4588 O O   . HOH G 4 .   ? 11.159  -29.996 -16.820 1.00 25.94 ? 407 HOH B O   1 
HETATM 4589 O O   . HOH G 4 .   ? -0.800  -5.383  -28.147 1.00 29.08 ? 408 HOH B O   1 
HETATM 4590 O O   . HOH G 4 .   ? 14.732  20.447  -44.808 1.00 29.50 ? 409 HOH B O   1 
HETATM 4591 O O   . HOH G 4 .   ? 0.106   4.725   -48.229 1.00 24.35 ? 410 HOH B O   1 
HETATM 4592 O O   . HOH G 4 .   ? -2.197  2.488   0.849   1.00 32.76 ? 411 HOH B O   1 
HETATM 4593 O O   . HOH G 4 .   ? 24.233  14.049  -29.794 1.00 46.40 ? 412 HOH B O   1 
HETATM 4594 O O   . HOH G 4 .   ? 14.789  -2.504  -40.153 1.00 30.09 ? 413 HOH B O   1 
HETATM 4595 O O   . HOH G 4 .   ? 13.032  -3.087  -45.999 1.00 27.02 ? 414 HOH B O   1 
HETATM 4596 O O   . HOH G 4 .   ? 11.548  6.922   8.261   1.00 31.26 ? 415 HOH B O   1 
HETATM 4597 O O   . HOH G 4 .   ? 17.744  -17.260 7.347   1.00 24.48 ? 416 HOH B O   1 
HETATM 4598 O O   . HOH G 4 .   ? 19.170  -1.740  -31.309 1.00 40.56 ? 417 HOH B O   1 
HETATM 4599 O O   . HOH G 4 .   ? 15.851  -22.683 -15.506 1.00 18.01 ? 418 HOH B O   1 
HETATM 4600 O O   . HOH G 4 .   ? 21.774  13.289  -4.174  1.00 32.35 ? 419 HOH B O   1 
HETATM 4601 O O   . HOH G 4 .   ? 2.672   20.634  -38.904 1.00 22.84 ? 420 HOH B O   1 
HETATM 4602 O O   . HOH G 4 .   ? 5.751   12.352  -47.955 1.00 25.84 ? 421 HOH B O   1 
HETATM 4603 O O   . HOH G 4 .   ? 10.662  7.848   -23.791 1.00 12.08 ? 422 HOH B O   1 
HETATM 4604 O O   . HOH G 4 .   ? 15.001  -3.777  -32.015 1.00 22.37 ? 423 HOH B O   1 
HETATM 4605 O O   . HOH G 4 .   ? 23.747  -23.311 3.069   1.00 28.53 ? 424 HOH B O   1 
HETATM 4606 O O   . HOH G 4 .   ? 1.537   18.259  -39.574 1.00 20.15 ? 425 HOH B O   1 
HETATM 4607 O O   . HOH G 4 .   ? 11.316  -6.052  -29.313 1.00 21.39 ? 426 HOH B O   1 
HETATM 4608 O O   . HOH G 4 .   ? 0.742   16.873  -16.692 1.00 29.72 ? 427 HOH B O   1 
HETATM 4609 O O   . HOH G 4 .   ? 2.786   -26.365 -10.665 1.00 38.23 ? 428 HOH B O   1 
HETATM 4610 O O   . HOH G 4 .   ? 17.290  -8.956  8.386   1.00 19.80 ? 429 HOH B O   1 
HETATM 4611 O O   . HOH G 4 .   ? 9.450   -8.123  4.029   1.00 38.39 ? 430 HOH B O   1 
HETATM 4612 O O   . HOH G 4 .   ? -3.945  12.572  1.062   1.00 44.45 ? 431 HOH B O   1 
HETATM 4613 O O   . HOH G 4 .   ? 1.836   -1.615  -44.706 1.00 31.58 ? 432 HOH B O   1 
HETATM 4614 O O   . HOH G 4 .   ? 24.177  -1.109  1.925   1.00 29.09 ? 433 HOH B O   1 
HETATM 4615 O O   . HOH G 4 .   ? 7.053   0.358   -22.013 1.00 23.59 ? 434 HOH B O   1 
HETATM 4616 O O   . HOH G 4 .   ? 10.014  -4.305  -38.119 1.00 23.97 ? 435 HOH B O   1 
HETATM 4617 O O   . HOH G 4 .   ? 5.838   8.991   -51.346 1.00 30.09 ? 436 HOH B O   1 
HETATM 4618 O O   . HOH G 4 .   ? 1.423   -1.934  -48.398 1.00 41.28 ? 437 HOH B O   1 
HETATM 4619 O O   . HOH G 4 .   ? 24.620  4.661   -32.967 1.00 40.07 ? 438 HOH B O   1 
HETATM 4620 O O   . HOH G 4 .   ? 8.887   2.034   -24.660 1.00 18.53 ? 439 HOH B O   1 
HETATM 4621 O O   . HOH G 4 .   ? 9.902   10.789  3.873   1.00 27.91 ? 440 HOH B O   1 
HETATM 4622 O O   . HOH G 4 .   ? 23.763  1.719   -46.667 1.00 36.88 ? 441 HOH B O   1 
HETATM 4623 O O   . HOH G 4 .   ? 23.292  -27.235 -8.802  1.00 46.65 ? 442 HOH B O   1 
HETATM 4624 O O   . HOH G 4 .   ? 9.053   -29.370 -10.900 1.00 27.34 ? 443 HOH B O   1 
HETATM 4625 O O   . HOH G 4 .   ? 8.661   4.557   -28.204 1.00 16.12 ? 444 HOH B O   1 
HETATM 4626 O O   . HOH G 4 .   ? 14.955  -3.702  -18.587 1.00 17.79 ? 445 HOH B O   1 
HETATM 4627 O O   . HOH G 4 .   ? 19.166  -10.373 7.247   1.00 27.21 ? 446 HOH B O   1 
HETATM 4628 O O   . HOH G 4 .   ? 7.120   -4.506  3.130   1.00 22.95 ? 447 HOH B O   1 
HETATM 4629 O O   . HOH G 4 .   ? 17.857  8.575   -25.484 1.00 16.84 ? 448 HOH B O   1 
HETATM 4630 O O   . HOH G 4 .   ? 7.455   8.744   0.553   1.00 28.72 ? 449 HOH B O   1 
HETATM 4631 O O   . HOH G 4 .   ? 9.689   24.538  -43.440 1.00 29.42 ? 450 HOH B O   1 
HETATM 4632 O O   . HOH G 4 .   ? 9.496   7.411   -26.212 1.00 17.70 ? 451 HOH B O   1 
HETATM 4633 O O   . HOH G 4 .   ? 2.716   21.974  -24.007 1.00 21.00 ? 452 HOH B O   1 
HETATM 4634 O O   . HOH G 4 .   ? 14.579  -33.360 -11.328 1.00 39.06 ? 453 HOH B O   1 
HETATM 4635 O O   . HOH G 4 .   ? 8.852   20.129  -19.999 1.00 33.58 ? 454 HOH B O   1 
HETATM 4636 O O   . HOH G 4 .   ? 0.124   22.880  -24.320 1.00 14.94 ? 455 HOH B O   1 
HETATM 4637 O O   . HOH G 4 .   ? 3.494   -3.616  -52.231 1.00 37.96 ? 456 HOH B O   1 
HETATM 4638 O O   . HOH G 4 .   ? 27.844  -23.191 -11.117 1.00 33.19 ? 457 HOH B O   1 
HETATM 4639 O O   . HOH G 4 .   ? -4.257  12.892  -37.694 1.00 28.78 ? 458 HOH B O   1 
HETATM 4640 O O   . HOH G 4 .   ? 12.155  -5.230  12.259  1.00 30.15 ? 459 HOH B O   1 
HETATM 4641 O O   . HOH G 4 .   ? 0.607   15.041  -42.281 1.00 22.16 ? 460 HOH B O   1 
HETATM 4642 O O   . HOH G 4 .   ? 3.189   -22.338 -16.720 1.00 32.35 ? 461 HOH B O   1 
HETATM 4643 O O   . HOH G 4 .   ? 6.786   -11.215 5.302   1.00 30.83 ? 462 HOH B O   1 
HETATM 4644 O O   . HOH G 4 .   ? 8.857   27.435  -33.391 1.00 27.00 ? 463 HOH B O   1 
HETATM 4645 O O   . HOH G 4 .   ? 22.043  -28.472 -10.882 1.00 43.56 ? 464 HOH B O   1 
HETATM 4646 O O   . HOH G 4 .   ? -6.381  19.689  -33.097 1.00 36.52 ? 465 HOH B O   1 
HETATM 4647 O O   . HOH G 4 .   ? 13.183  -4.876  -39.193 1.00 28.24 ? 466 HOH B O   1 
HETATM 4648 O O   . HOH G 4 .   ? 8.592   -4.115  -44.589 1.00 40.14 ? 467 HOH B O   1 
HETATM 4649 O O   . HOH G 4 .   ? 13.671  -28.061 -16.786 1.00 27.61 ? 468 HOH B O   1 
HETATM 4650 O O   . HOH G 4 .   ? 5.699   -2.142  8.878   1.00 26.73 ? 469 HOH B O   1 
HETATM 4651 O O   . HOH G 4 .   ? 13.979  21.219  -17.827 1.00 23.65 ? 470 HOH B O   1 
HETATM 4652 O O   . HOH G 4 .   ? 15.155  13.641  -5.654  1.00 25.81 ? 471 HOH B O   1 
HETATM 4653 O O   . HOH G 4 .   ? 28.182  -22.600 -5.323  1.00 39.26 ? 472 HOH B O   1 
HETATM 4654 O O   . HOH G 4 .   ? 11.391  -3.845  -26.301 1.00 29.61 ? 473 HOH B O   1 
HETATM 4655 O O   . HOH G 4 .   ? 13.991  2.430   -35.937 1.00 15.62 ? 474 HOH B O   1 
HETATM 4656 O O   . HOH G 4 .   ? 3.746   1.252   5.169   1.00 24.30 ? 475 HOH B O   1 
HETATM 4657 O O   . HOH G 4 .   ? 16.617  -0.554  11.635  1.00 30.06 ? 476 HOH B O   1 
HETATM 4658 O O   . HOH G 4 .   ? 24.521  10.228  -36.586 1.00 44.49 ? 477 HOH B O   1 
HETATM 4659 O O   . HOH G 4 .   ? 7.580   -3.743  11.797  1.00 28.48 ? 478 HOH B O   1 
HETATM 4660 O O   . HOH G 4 .   ? 12.619  8.003   5.927   1.00 30.07 ? 479 HOH B O   1 
HETATM 4661 O O   . HOH G 4 .   ? 2.655   23.105  -42.314 1.00 31.92 ? 480 HOH B O   1 
HETATM 4662 O O   . HOH G 4 .   ? 10.855  5.438   -22.691 1.00 17.78 ? 481 HOH B O   1 
HETATM 4663 O O   . HOH G 4 .   ? 19.513  -24.594 -2.309  1.00 24.13 ? 482 HOH B O   1 
HETATM 4664 O O   . HOH G 4 .   ? -6.422  5.804   -24.904 1.00 39.10 ? 483 HOH B O   1 
HETATM 4665 O O   . HOH G 4 .   ? 8.441   12.416  -23.255 1.00 13.50 ? 484 HOH B O   1 
HETATM 4666 O O   . HOH G 4 .   ? 23.838  -24.511 -11.054 1.00 23.55 ? 485 HOH B O   1 
HETATM 4667 O O   . HOH G 4 .   ? 19.724  6.741   -3.085  1.00 13.89 ? 486 HOH B O   1 
HETATM 4668 O O   . HOH G 4 .   ? 21.611  24.537  -33.057 1.00 47.40 ? 487 HOH B O   1 
HETATM 4669 O O   . HOH G 4 .   ? -3.325  22.900  -24.064 1.00 20.96 ? 488 HOH B O   1 
HETATM 4670 O O   . HOH G 4 .   ? 17.145  -3.241  -39.302 1.00 38.27 ? 489 HOH B O   1 
HETATM 4671 O O   . HOH G 4 .   ? 3.420   -4.360  -36.614 1.00 16.97 ? 490 HOH B O   1 
HETATM 4672 O O   . HOH G 4 .   ? -2.871  2.770   -20.572 1.00 41.92 ? 491 HOH B O   1 
HETATM 4673 O O   . HOH G 4 .   ? 19.574  7.152   1.169   1.00 21.30 ? 492 HOH B O   1 
HETATM 4674 O O   . HOH G 4 .   ? 0.403   -1.699  -25.142 1.00 15.46 ? 493 HOH B O   1 
HETATM 4675 O O   . HOH G 4 .   ? 28.295  -5.717  0.261   1.00 34.06 ? 494 HOH B O   1 
HETATM 4676 O O   . HOH G 4 .   ? 26.830  6.549   -38.281 1.00 36.76 ? 495 HOH B O   1 
HETATM 4677 O O   . HOH G 4 .   ? 16.169  4.591   -46.426 1.00 29.82 ? 496 HOH B O   1 
HETATM 4678 O O   . HOH G 4 .   ? 4.021   -2.889  -38.642 1.00 20.54 ? 497 HOH B O   1 
HETATM 4679 O O   . HOH G 4 .   ? 13.206  11.273  -24.282 1.00 14.11 ? 498 HOH B O   1 
HETATM 4680 O O   . HOH G 4 .   ? 2.581   4.435   8.656   1.00 32.44 ? 499 HOH B O   1 
HETATM 4681 O O   . HOH G 4 .   ? 20.011  17.191  -18.358 1.00 28.03 ? 500 HOH B O   1 
HETATM 4682 O O   . HOH G 4 .   ? 12.331  0.727   12.093  1.00 20.50 ? 501 HOH B O   1 
HETATM 4683 O O   . HOH G 4 .   ? 23.734  -9.712  -6.525  1.00 24.40 ? 502 HOH B O   1 
HETATM 4684 O O   . HOH G 4 .   ? 2.407   4.122   -49.593 1.00 32.80 ? 503 HOH B O   1 
HETATM 4685 O O   . HOH G 4 .   ? 18.435  -2.204  -36.696 1.00 31.48 ? 504 HOH B O   1 
HETATM 4686 O O   . HOH G 4 .   ? 26.855  8.788   -36.247 1.00 32.86 ? 505 HOH B O   1 
HETATM 4687 O O   . HOH G 4 .   ? 0.274   2.095   -30.170 1.00 23.02 ? 506 HOH B O   1 
HETATM 4688 O O   . HOH G 4 .   ? 3.669   6.230   -49.696 1.00 28.46 ? 507 HOH B O   1 
HETATM 4689 O O   . HOH G 4 .   ? 12.231  -9.146  10.753  1.00 37.17 ? 508 HOH B O   1 
HETATM 4690 O O   . HOH G 4 .   ? 12.481  10.262  4.787   1.00 39.02 ? 509 HOH B O   1 
HETATM 4691 O O   . HOH G 4 .   ? 22.341  -3.564  8.050   1.00 32.21 ? 510 HOH B O   1 
HETATM 4692 O O   . HOH G 4 .   ? -5.531  5.754   -30.695 1.00 43.38 ? 511 HOH B O   1 
HETATM 4693 O O   . HOH G 4 .   ? 4.086   -0.892  1.900   1.00 32.19 ? 512 HOH B O   1 
HETATM 4694 O O   . HOH G 4 .   ? 25.079  -6.567  1.697   1.00 34.49 ? 513 HOH B O   1 
HETATM 4695 O O   . HOH G 4 .   ? 19.711  15.303  -21.587 1.00 32.50 ? 514 HOH B O   1 
HETATM 4696 O O   . HOH G 4 .   ? 12.127  -3.900  -53.112 1.00 34.46 ? 515 HOH B O   1 
HETATM 4697 O O   . HOH G 4 .   ? 22.490  10.916  -38.387 1.00 34.64 ? 516 HOH B O   1 
HETATM 4698 O O   . HOH G 4 .   ? -7.192  6.806   -28.130 1.00 40.51 ? 517 HOH B O   1 
HETATM 4699 O O   . HOH G 4 .   ? -4.888  20.543  -22.316 1.00 18.43 ? 518 HOH B O   1 
HETATM 4700 O O   . HOH G 4 .   ? 29.513  -25.055 -1.536  1.00 35.08 ? 519 HOH B O   1 
HETATM 4701 O O   . HOH G 4 .   ? 13.115  15.317  -15.292 1.00 18.30 ? 520 HOH B O   1 
HETATM 4702 O O   . HOH G 4 .   ? 5.557   21.245  -28.224 1.00 22.93 ? 521 HOH B O   1 
HETATM 4703 O O   . HOH G 4 .   ? 24.533  6.769   -29.898 1.00 35.69 ? 522 HOH B O   1 
HETATM 4704 O O   . HOH G 4 .   ? 3.633   14.171  2.052   1.00 39.66 ? 523 HOH B O   1 
HETATM 4705 O O   . HOH G 4 .   ? -0.096  18.863  -35.677 1.00 38.29 ? 524 HOH B O   1 
HETATM 4706 O O   . HOH G 4 .   ? 25.840  -27.447 -5.861  1.00 38.71 ? 525 HOH B O   1 
HETATM 4707 O O   . HOH G 4 .   ? -6.636  13.594  -36.045 1.00 19.40 ? 526 HOH B O   1 
HETATM 4708 O O   . HOH G 4 .   ? 21.855  -9.330  5.821   1.00 34.46 ? 527 HOH B O   1 
HETATM 4709 O O   . HOH G 4 .   ? 8.031   -9.280  -29.043 1.00 32.63 ? 528 HOH B O   1 
HETATM 4710 O O   . HOH G 4 .   ? 23.494  1.334   12.610  1.00 41.20 ? 529 HOH B O   1 
HETATM 4711 O O   . HOH G 4 .   ? -1.018  18.710  -18.865 1.00 20.04 ? 530 HOH B O   1 
HETATM 4712 O O   . HOH G 4 .   ? 3.231   -6.710  3.664   1.00 26.23 ? 531 HOH B O   1 
HETATM 4713 O O   . HOH G 4 .   ? 9.944   22.450  -45.886 1.00 31.21 ? 532 HOH B O   1 
HETATM 4714 O O   . HOH G 4 .   ? 18.415  15.168  -26.318 1.00 31.68 ? 533 HOH B O   1 
HETATM 4715 O O   . HOH G 4 .   ? 13.085  -17.405 3.039   1.00 24.18 ? 534 HOH B O   1 
HETATM 4716 O O   . HOH G 4 .   ? 17.101  19.648  -20.200 1.00 25.11 ? 535 HOH B O   1 
HETATM 4717 O O   . HOH G 4 .   ? 8.704   -7.653  -32.649 1.00 34.68 ? 536 HOH B O   1 
HETATM 4718 O O   . HOH G 4 .   ? 26.990  5.900   -6.798  1.00 29.05 ? 537 HOH B O   1 
HETATM 4719 O O   . HOH G 4 .   ? 0.017   -4.321  -25.301 1.00 23.86 ? 538 HOH B O   1 
HETATM 4720 O O   . HOH G 4 .   ? 6.483   2.186   -56.251 1.00 49.41 ? 539 HOH B O   1 
HETATM 4721 O O   . HOH G 4 .   ? -4.464  -2.634  -23.996 1.00 47.01 ? 540 HOH B O   1 
HETATM 4722 O O   . HOH G 4 .   ? -0.326  16.799  -46.217 1.00 26.26 ? 541 HOH B O   1 
HETATM 4723 O O   . HOH G 4 .   ? -4.379  2.247   -16.874 1.00 41.67 ? 542 HOH B O   1 
HETATM 4724 O O   . HOH G 4 .   ? 11.662  28.018  -29.665 1.00 37.43 ? 543 HOH B O   1 
HETATM 4725 O O   . HOH G 4 .   ? 3.418   -7.859  -37.630 1.00 43.22 ? 544 HOH B O   1 
HETATM 4726 O O   . HOH G 4 .   ? -4.289  14.685  -20.900 1.00 41.51 ? 545 HOH B O   1 
HETATM 4727 O O   . HOH G 4 .   ? -4.670  6.332   -39.678 1.00 30.76 ? 546 HOH B O   1 
HETATM 4728 O O   . HOH G 4 .   ? 2.424   -5.061  9.581   1.00 35.79 ? 547 HOH B O   1 
HETATM 4729 O O   . HOH G 4 .   ? -4.689  12.819  -49.890 1.00 35.49 ? 548 HOH B O   1 
HETATM 4730 O O   . HOH G 4 .   ? 12.502  -0.030  -26.048 1.00 30.27 ? 549 HOH B O   1 
HETATM 4731 O O   . HOH G 4 .   ? 7.650   -29.641 -6.566  1.00 40.82 ? 550 HOH B O   1 
HETATM 4732 O O   . HOH G 4 .   ? 5.016   -7.111  -26.667 1.00 42.83 ? 551 HOH B O   1 
HETATM 4733 O O   . HOH G 4 .   ? 20.421  16.676  -43.426 1.00 25.90 ? 552 HOH B O   1 
HETATM 4734 O O   . HOH G 4 .   ? 13.587  2.007   -23.410 1.00 24.73 ? 553 HOH B O   1 
HETATM 4735 O O   . HOH G 4 .   ? 9.395   15.232  -15.712 1.00 31.97 ? 554 HOH B O   1 
HETATM 4736 O O   . HOH G 4 .   ? 2.098   23.733  -30.448 1.00 31.41 ? 555 HOH B O   1 
HETATM 4737 O O   . HOH G 4 .   ? -5.487  -5.665  -30.844 1.00 33.75 ? 556 HOH B O   1 
HETATM 4738 O O   . HOH G 4 .   ? 5.799   19.866  -46.876 1.00 35.78 ? 557 HOH B O   1 
HETATM 4739 O O   . HOH G 4 .   ? 8.287   -4.083  -40.114 1.00 25.18 ? 558 HOH B O   1 
HETATM 4740 O O   . HOH G 4 .   ? -8.655  9.725   -34.373 1.00 32.90 ? 559 HOH B O   1 
HETATM 4741 O O   . HOH G 4 .   ? 2.759   -11.350 -34.076 1.00 51.55 ? 560 HOH B O   1 
HETATM 4742 O O   . HOH G 4 .   ? -2.591  5.011   1.706   1.00 35.31 ? 561 HOH B O   1 
HETATM 4743 O O   . HOH G 4 .   ? 24.593  -3.845  -5.999  1.00 26.02 ? 562 HOH B O   1 
HETATM 4744 O O   . HOH G 4 .   ? 21.546  0.751   -34.361 1.00 28.34 ? 563 HOH B O   1 
HETATM 4745 O O   . HOH G 4 .   ? 13.392  -33.213 -9.126  1.00 45.91 ? 564 HOH B O   1 
HETATM 4746 O O   . HOH G 4 .   ? 6.101   -4.696  -16.362 1.00 36.53 ? 565 HOH B O   1 
HETATM 4747 O O   . HOH G 4 .   ? 2.723   -6.068  -0.289  1.00 40.74 ? 566 HOH B O   1 
HETATM 4748 O O   . HOH G 4 .   ? 13.423  -5.696  -31.789 1.00 22.99 ? 567 HOH B O   1 
HETATM 4749 O O   . HOH G 4 .   ? 1.280   -2.731  -40.234 1.00 34.57 ? 568 HOH B O   1 
HETATM 4750 O O   . HOH G 4 .   ? -3.204  13.695  -2.562  1.00 45.80 ? 569 HOH B O   1 
HETATM 4751 O O   . HOH G 4 .   ? -0.072  14.214  -53.621 1.00 48.93 ? 570 HOH B O   1 
HETATM 4752 O O   . HOH G 4 .   ? 3.841   -3.769  2.382   1.00 35.18 ? 571 HOH B O   1 
HETATM 4753 O O   . HOH G 4 .   ? 22.001  1.684   -50.066 1.00 30.42 ? 572 HOH B O   1 
HETATM 4754 O O   . HOH G 4 .   ? 6.026   -4.650  -39.812 1.00 26.53 ? 573 HOH B O   1 
HETATM 4755 O O   . HOH G 4 .   ? -1.271  5.894   3.787   1.00 23.84 ? 574 HOH B O   1 
HETATM 4756 O O   . HOH G 4 .   ? 13.768  -11.319 9.993   1.00 22.05 ? 575 HOH B O   1 
HETATM 4757 O O   . HOH G 4 .   ? 6.051   -26.423 -9.030  1.00 38.28 ? 576 HOH B O   1 
HETATM 4758 O O   . HOH G 4 .   ? 10.875  19.819  -17.740 1.00 40.54 ? 577 HOH B O   1 
HETATM 4759 O O   . HOH G 4 .   ? 9.938   -11.046 2.885   1.00 34.51 ? 578 HOH B O   1 
HETATM 4760 O O   . HOH G 4 .   ? 9.240   -5.549  -42.198 1.00 31.63 ? 579 HOH B O   1 
HETATM 4761 O O   . HOH G 4 .   ? 9.878   -0.411  -24.353 1.00 26.60 ? 580 HOH B O   1 
HETATM 4762 O O   . HOH G 4 .   ? 2.129   -12.069 -1.969  1.00 34.45 ? 581 HOH B O   1 
HETATM 4763 O O   . HOH G 4 .   ? 16.450  -11.016 10.426  1.00 36.06 ? 582 HOH B O   1 
HETATM 4764 O O   . HOH G 4 .   ? 25.730  -0.058  -3.071  1.00 25.70 ? 583 HOH B O   1 
HETATM 4765 O O   . HOH G 4 .   ? 1.800   18.011  -47.865 1.00 35.56 ? 584 HOH B O   1 
HETATM 4766 O O   . HOH G 4 .   ? 12.355  14.672  -4.322  1.00 29.30 ? 585 HOH B O   1 
HETATM 4767 O O   . HOH G 4 .   ? -1.409  10.154  -16.149 1.00 48.95 ? 586 HOH B O   1 
HETATM 4768 O O   . HOH G 4 .   ? 32.294  -22.801 -3.149  1.00 32.95 ? 587 HOH B O   1 
HETATM 4769 O O   . HOH G 4 .   ? 17.996  -22.892 -17.253 1.00 34.83 ? 588 HOH B O   1 
HETATM 4770 O O   . HOH G 4 .   ? 5.240   22.227  -20.603 1.00 26.79 ? 589 HOH B O   1 
HETATM 4771 O O   . HOH G 4 .   ? 11.455  -6.767  -33.860 1.00 23.66 ? 590 HOH B O   1 
HETATM 4772 O O   . HOH G 4 .   ? -1.000  -2.212  -39.010 1.00 28.07 ? 591 HOH B O   1 
HETATM 4773 O O   . HOH G 4 .   ? 10.540  12.375  1.471   1.00 29.84 ? 592 HOH B O   1 
HETATM 4774 O O   . HOH G 4 .   ? 5.827   -2.308  -21.206 1.00 39.89 ? 593 HOH B O   1 
HETATM 4775 O O   . HOH G 4 .   ? 22.018  6.236   1.926   1.00 30.14 ? 594 HOH B O   1 
HETATM 4776 O O   . HOH G 4 .   ? 9.615   -5.340  12.665  1.00 30.01 ? 595 HOH B O   1 
HETATM 4777 O O   . HOH G 4 .   ? 21.226  -5.670  8.711   1.00 36.68 ? 596 HOH B O   1 
HETATM 4778 O O   . HOH G 4 .   ? -1.071  16.797  -43.325 1.00 34.38 ? 597 HOH B O   1 
HETATM 4779 O O   . HOH G 4 .   ? 22.538  -2.875  -36.415 1.00 42.60 ? 598 HOH B O   1 
HETATM 4780 O O   . HOH G 4 .   ? 0.758   26.786  -30.867 1.00 31.84 ? 599 HOH B O   1 
HETATM 4781 O O   . HOH G 4 .   ? 30.120  18.629  -40.650 1.00 43.32 ? 600 HOH B O   1 
HETATM 4782 O O   . HOH G 4 .   ? -4.088  -11.844 -30.640 1.00 44.58 ? 601 HOH B O   1 
# 
