data_3S5J
# 
_entry.id   3S5J 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3S5J         
RCSB  RCSB065787   
WWPDB D_1000065787 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3S5J 
_pdbx_database_status.recvd_initial_deposition_date   2011-05-23 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Chen, P.' 1 
'Teng, M.' 2 
'Li, X.'   3 
# 
_citation.id                        primary 
_citation.title                     
;Crystal and EM Structures of Human Phosphoribosyl Pyrophosphate Synthase I (PRS1) Provide Novel Insights into the Disease-Associated Mutations
;
_citation.journal_abbrev            'Plos One' 
_citation.journal_volume            10 
_citation.page_first                e0120304 
_citation.page_last                 e0120304 
_citation.year                      2015 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1932-6203 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25781187 
_citation.pdbx_database_id_DOI      10.1371/journal.pone.0120304 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Chen, P.'  1  
primary 'Liu, Z.'   2  
primary 'Wang, X.'  3  
primary 'Peng, J.'  4  
primary 'Sun, Q.'   5  
primary 'Li, J.'    6  
primary 'Wang, M.'  7  
primary 'Niu, L.'   8  
primary 'Zhang, Z.' 9  
primary 'Cai, G.'   10 
primary 'Teng, M.'  11 
primary 'Li, X.'    12 
# 
_cell.entry_id           3S5J 
_cell.length_a           170.536 
_cell.length_b           170.536 
_cell.length_c           61.778 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              18 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3S5J 
_symmetry.space_group_name_H-M             'H 3' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_symmetry.space_group_name_Hall            ? 
# 
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 'Ribose-phosphate pyrophosphokinase 1' 35950.375 2   2.7.6.1 ? ? ? 
2 non-polymer syn 'SULFATE ION'                          96.063    6   ?       ? ? ? 
3 water       nat water                                  18.015    178 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'PPRibP, Phosphoribosyl pyrophosphate synthase I, PRS-I' 
# 
_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       
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_strand_id                 B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
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   PRO n 
1 3   ASN n 
1 4   ILE n 
1 5   LYS n 
1 6   ILE n 
1 7   PHE n 
1 8   SER n 
1 9   GLY n 
1 10  SER n 
1 11  SER n 
1 12  HIS n 
1 13  GLN n 
1 14  ASP n 
1 15  LEU n 
1 16  SER n 
1 17  GLN n 
1 18  LYS n 
1 19  ILE n 
1 20  ALA n 
1 21  ASP n 
1 22  ARG n 
1 23  LEU n 
1 24  GLY n 
1 25  LEU n 
1 26  GLU n 
1 27  LEU n 
1 28  GLY n 
1 29  LYS n 
1 30  VAL n 
1 31  VAL n 
1 32  THR n 
1 33  LYS n 
1 34  LYS n 
1 35  PHE n 
1 36  SER n 
1 37  ASN n 
1 38  GLN n 
1 39  GLU n 
1 40  THR n 
1 41  CYS n 
1 42  VAL n 
1 43  GLU n 
1 44  ILE n 
1 45  GLY n 
1 46  GLU n 
1 47  SER n 
1 48  VAL n 
1 49  ARG n 
1 50  GLY n 
1 51  GLU n 
1 52  ASP n 
1 53  VAL n 
1 54  TYR n 
1 55  ILE n 
1 56  VAL n 
1 57  GLN n 
1 58  SER n 
1 59  GLY n 
1 60  CYS n 
1 61  GLY n 
1 62  GLU n 
1 63  ILE n 
1 64  ASN n 
1 65  ASP n 
1 66  ASN n 
1 67  LEU n 
1 68  MET n 
1 69  GLU n 
1 70  LEU n 
1 71  LEU n 
1 72  ILE n 
1 73  MET n 
1 74  ILE n 
1 75  ASN n 
1 76  ALA n 
1 77  CYS n 
1 78  LYS n 
1 79  ILE n 
1 80  ALA n 
1 81  SER n 
1 82  ALA n 
1 83  SER n 
1 84  ARG n 
1 85  VAL n 
1 86  THR n 
1 87  ALA n 
1 88  VAL n 
1 89  ILE n 
1 90  PRO n 
1 91  CYS n 
1 92  PHE n 
1 93  PRO n 
1 94  TYR n 
1 95  ALA n 
1 96  ARG n 
1 97  GLN n 
1 98  ASP n 
1 99  LYS n 
1 100 LYS n 
1 101 ASP n 
1 102 LYS n 
1 103 SER n 
1 104 ARG n 
1 105 ALA n 
1 106 PRO n 
1 107 ILE n 
1 108 SER n 
1 109 ALA n 
1 110 LYS n 
1 111 LEU n 
1 112 VAL n 
1 113 ALA n 
1 114 ASN n 
1 115 MET n 
1 116 LEU n 
1 117 SER n 
1 118 VAL n 
1 119 ALA n 
1 120 GLY n 
1 121 ALA n 
1 122 ASP n 
1 123 HIS n 
1 124 ILE n 
1 125 ILE n 
1 126 THR n 
1 127 MET n 
1 128 ASP n 
1 129 LEU n 
1 130 HIS n 
1 131 ALA n 
1 132 SER n 
1 133 GLN n 
1 134 ILE n 
1 135 GLN n 
1 136 GLY n 
1 137 PHE n 
1 138 PHE n 
1 139 ASP n 
1 140 ILE n 
1 141 PRO n 
1 142 VAL n 
1 143 ASP n 
1 144 ASN n 
1 145 LEU n 
1 146 TYR n 
1 147 ALA n 
1 148 GLU n 
1 149 PRO n 
1 150 ALA n 
1 151 VAL n 
1 152 LEU n 
1 153 LYS n 
1 154 TRP n 
1 155 ILE n 
1 156 ARG n 
1 157 GLU n 
1 158 ASN n 
1 159 ILE n 
1 160 SER n 
1 161 GLU n 
1 162 TRP n 
1 163 ARG n 
1 164 ASN n 
1 165 CYS n 
1 166 THR n 
1 167 ILE n 
1 168 VAL n 
1 169 SER n 
1 170 PRO n 
1 171 ASP n 
1 172 ALA n 
1 173 GLY n 
1 174 GLY n 
1 175 ALA n 
1 176 LYS n 
1 177 ARG n 
1 178 VAL n 
1 179 THR n 
1 180 SER n 
1 181 ILE n 
1 182 ALA n 
1 183 ASP n 
1 184 ARG n 
1 185 LEU n 
1 186 ASN n 
1 187 VAL n 
1 188 ASP n 
1 189 PHE n 
1 190 ALA n 
1 191 LEU n 
1 192 ILE n 
1 193 HIS n 
1 194 LYS n 
1 195 GLU n 
1 196 ARG n 
1 197 LYS n 
1 198 LYS n 
1 199 ALA n 
1 200 ASN n 
1 201 GLU n 
1 202 VAL n 
1 203 ASP n 
1 204 ARG n 
1 205 MET n 
1 206 VAL n 
1 207 LEU n 
1 208 VAL n 
1 209 GLY n 
1 210 ASP n 
1 211 VAL n 
1 212 LYS n 
1 213 ASP n 
1 214 ARG n 
1 215 VAL n 
1 216 ALA n 
1 217 ILE n 
1 218 LEU n 
1 219 VAL n 
1 220 ASP n 
1 221 ASP n 
1 222 MET n 
1 223 ALA n 
1 224 ASP n 
1 225 THR n 
1 226 CYS n 
1 227 GLY n 
1 228 THR n 
1 229 ILE n 
1 230 CYS n 
1 231 HIS n 
1 232 ALA n 
1 233 ALA n 
1 234 ASP n 
1 235 LYS n 
1 236 LEU n 
1 237 LEU n 
1 238 SER n 
1 239 ALA n 
1 240 GLY n 
1 241 ALA n 
1 242 THR n 
1 243 ARG n 
1 244 VAL n 
1 245 TYR n 
1 246 ALA n 
1 247 ILE n 
1 248 LEU n 
1 249 THR n 
1 250 HIS n 
1 251 GLY n 
1 252 ILE n 
1 253 PHE n 
1 254 SER n 
1 255 GLY n 
1 256 PRO n 
1 257 ALA n 
1 258 ILE n 
1 259 SER n 
1 260 ARG n 
1 261 ILE n 
1 262 ASN n 
1 263 ASN n 
1 264 ALA n 
1 265 CYS n 
1 266 PHE n 
1 267 GLU n 
1 268 ALA n 
1 269 VAL n 
1 270 VAL n 
1 271 VAL n 
1 272 THR n 
1 273 ASN n 
1 274 THR n 
1 275 ILE n 
1 276 PRO n 
1 277 GLN n 
1 278 GLU n 
1 279 ASP n 
1 280 LYS n 
1 281 MET n 
1 282 LYS n 
1 283 HIS n 
1 284 CYS n 
1 285 SER n 
1 286 LYS n 
1 287 ILE n 
1 288 GLN n 
1 289 VAL n 
1 290 ILE n 
1 291 ASP n 
1 292 ILE n 
1 293 SER n 
1 294 MET n 
1 295 ILE n 
1 296 LEU n 
1 297 ALA n 
1 298 GLU n 
1 299 ALA n 
1 300 ILE n 
1 301 ARG n 
1 302 ARG n 
1 303 THR n 
1 304 HIS n 
1 305 ASN n 
1 306 GLY n 
1 307 GLU n 
1 308 SER n 
1 309 VAL n 
1 310 SER n 
1 311 TYR n 
1 312 LEU n 
1 313 PHE n 
1 314 SER n 
1 315 HIS n 
1 316 VAL n 
1 317 PRO n 
1 318 LEU n 
1 319 LEU n 
1 320 GLU n 
1 321 HIS n 
1 322 HIS n 
1 323 HIS n 
1 324 HIS n 
1 325 HIS n 
1 326 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PRPS1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET22b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PRPS1_HUMAN 
_struct_ref.pdbx_db_accession          P60891 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPL
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
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 3S5J B 1 ? 318 ? P60891 1 ? 318 ? 1 318 
2 1 3S5J A 1 ? 318 ? P60891 1 ? 318 ? 1 318 
# 
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 3S5J LEU B 319 ? UNP P60891 ? ? 'EXPRESSION TAG' 319 1  
1 3S5J GLU B 320 ? UNP P60891 ? ? 'EXPRESSION TAG' 320 2  
1 3S5J HIS B 321 ? UNP P60891 ? ? 'EXPRESSION TAG' 321 3  
1 3S5J HIS B 322 ? UNP P60891 ? ? 'EXPRESSION TAG' 322 4  
1 3S5J HIS B 323 ? UNP P60891 ? ? 'EXPRESSION TAG' 323 5  
1 3S5J HIS B 324 ? UNP P60891 ? ? 'EXPRESSION TAG' 324 6  
1 3S5J HIS B 325 ? UNP P60891 ? ? 'EXPRESSION TAG' 325 7  
1 3S5J HIS B 326 ? UNP P60891 ? ? 'EXPRESSION TAG' 326 8  
2 3S5J LEU A 319 ? UNP P60891 ? ? 'EXPRESSION TAG' 319 9  
2 3S5J GLU A 320 ? UNP P60891 ? ? 'EXPRESSION TAG' 320 10 
2 3S5J HIS A 321 ? UNP P60891 ? ? 'EXPRESSION TAG' 321 11 
2 3S5J HIS A 322 ? UNP P60891 ? ? 'EXPRESSION TAG' 322 12 
2 3S5J HIS A 323 ? UNP P60891 ? ? 'EXPRESSION TAG' 323 13 
2 3S5J HIS A 324 ? UNP P60891 ? ? 'EXPRESSION TAG' 324 14 
2 3S5J HIS A 325 ? UNP P60891 ? ? 'EXPRESSION TAG' 325 15 
2 3S5J HIS A 326 ? UNP P60891 ? ? 'EXPRESSION TAG' 326 16 
# 
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 
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 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          3S5J 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.40 
_exptl_crystal.density_percent_sol   48.85 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pdbx_details    'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'RAYONIX MX225HE' 
_diffrn_detector.pdbx_collection_date   2010-09-22 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRF BEAMLINE BL17U' 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_synchrotron_beamline   BL17U 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0 
# 
_reflns.entry_id                     3S5J 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             85.27 
_reflns.d_resolution_high            2.02 
_reflns.number_obs                   41673 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         ? 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_refine.entry_id                                 3S5J 
_refine.ls_number_reflns_obs                     41673 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             49.23 
_refine.ls_d_res_high                            2.02 
_refine.ls_percent_reflns_obs                    99.84 
_refine.ls_R_factor_obs                          0.21683 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.21477 
_refine.ls_R_factor_R_free                       0.25607 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  2205 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.928 
_refine.correlation_coeff_Fo_to_Fc_free          0.911 
_refine.B_iso_mean                               35.624 
_refine.aniso_B[1][1]                            0.55 
_refine.aniso_B[2][2]                            0.55 
_refine.aniso_B[3][3]                            -0.82 
_refine.aniso_B[1][2]                            0.27 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      'PDB ENTRY 2HCR' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R_Free                  0.180 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4680 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             178 
_refine_hist.number_atoms_total               4888 
_refine_hist.d_res_high                       2.02 
_refine_hist.d_res_low                        49.23 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       0.008  0.022  ? 4770 ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    1.149  1.960  ? 6453 ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 5.230  5.000  ? 608  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 38.451 24.523 ? 199  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 16.050 15.000 ? 855  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 18.401 15.000 ? 30   ? 'X-RAY DIFFRACTION' 
r_chiral_restr         0.078  0.200  ? 763  ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   0.004  0.021  ? 3478 ? 'X-RAY DIFFRACTION' 
r_mcbond_it            2.987  1.500  ? 3039 ? 'X-RAY DIFFRACTION' 
r_mcangle_it           3.930  2.000  ? 4916 ? 'X-RAY DIFFRACTION' 
r_scbond_it            4.176  3.000  ? 1731 ? 'X-RAY DIFFRACTION' 
r_scangle_it           5.545  4.500  ? 1537 ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.020 
_refine_ls_shell.d_res_low                        2.073 
_refine_ls_shell.number_reflns_R_work             3053 
_refine_ls_shell.R_factor_R_work                  0.267 
_refine_ls_shell.percent_reflns_obs               98.83 
_refine_ls_shell.R_factor_R_free                  0.303 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             148 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
# 
_struct.entry_id                  3S5J 
_struct.title                     '2.0A Crystal structure of human phosphoribosyl pyrophosphate synthetase 1' 
_struct.pdbx_descriptor           'Ribose-phosphate pyrophosphokinase 1 (E.C.2.7.6.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3S5J 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            'nucleotide synthesis, TRANSFERASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 3 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  1  GLN A 13  ? LEU A 23  ? GLN B 13  LEU B 23  1 ? 11 
HELX_P HELX_P2  2  GLU A 62  ? ALA A 80  ? GLU B 62  ALA B 80  1 ? 19 
HELX_P HELX_P3  3  ILE A 107 ? GLY A 120 ? ILE B 107 GLY B 120 1 ? 14 
HELX_P HELX_P4  4  ALA A 131 ? PHE A 138 ? ALA B 131 PHE B 138 5 ? 8  
HELX_P HELX_P5  5  ALA A 147 ? ILE A 159 ? ALA B 147 ILE B 159 1 ? 13 
HELX_P HELX_P6  6  GLU A 161 ? ASN A 164 ? GLU B 161 ASN B 164 5 ? 4  
HELX_P HELX_P7  7  ASP A 171 ? GLY A 173 ? ASP B 171 GLY B 173 5 ? 3  
HELX_P HELX_P8  8  GLY A 174 ? ASN A 186 ? GLY B 174 ASN B 186 1 ? 13 
HELX_P HELX_P9  9  CYS A 226 ? ALA A 239 ? CYS B 226 ALA B 239 1 ? 14 
HELX_P HELX_P10 10 PRO A 256 ? ALA A 264 ? PRO B 256 ALA B 264 1 ? 9  
HELX_P HELX_P11 11 GLN A 277 ? HIS A 283 ? GLN B 277 HIS B 283 1 ? 7  
HELX_P HELX_P12 12 ILE A 292 ? GLY A 306 ? ILE B 292 GLY B 306 1 ? 15 
HELX_P HELX_P13 13 VAL A 309 ? SER A 314 ? VAL B 309 SER B 314 5 ? 6  
HELX_P HELX_P14 14 GLN B 13  ? LEU B 23  ? GLN A 13  LEU A 23  1 ? 11 
HELX_P HELX_P15 15 GLU B 62  ? ALA B 80  ? GLU A 62  ALA A 80  1 ? 19 
HELX_P HELX_P16 16 ILE B 107 ? GLY B 120 ? ILE A 107 GLY A 120 1 ? 14 
HELX_P HELX_P17 17 ALA B 131 ? PHE B 138 ? ALA A 131 PHE A 138 5 ? 8  
HELX_P HELX_P18 18 ALA B 147 ? ILE B 159 ? ALA A 147 ILE A 159 1 ? 13 
HELX_P HELX_P19 19 GLU B 161 ? ASN B 164 ? GLU A 161 ASN A 164 5 ? 4  
HELX_P HELX_P20 20 ASP B 171 ? GLY B 173 ? ASP A 171 GLY A 173 5 ? 3  
HELX_P HELX_P21 21 GLY B 174 ? ASN B 186 ? GLY A 174 ASN A 186 1 ? 13 
HELX_P HELX_P22 22 CYS B 226 ? ALA B 239 ? CYS A 226 ALA A 239 1 ? 14 
HELX_P HELX_P23 23 PRO B 256 ? ASN B 263 ? PRO A 256 ASN A 263 1 ? 8  
HELX_P HELX_P24 24 GLN B 277 ? LYS B 282 ? GLN A 277 LYS A 282 1 ? 6  
HELX_P HELX_P25 25 ILE B 292 ? GLY B 306 ? ILE A 292 GLY A 306 1 ? 15 
HELX_P HELX_P26 26 VAL B 309 ? PHE B 313 ? VAL A 309 PHE A 313 5 ? 5  
# 
_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 
A ? 5 ? 
B ? 2 ? 
C ? 7 ? 
D ? 5 ? 
E ? 2 ? 
F ? 7 ? 
# 
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 
A 1 2 ? parallel      
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? parallel      
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? parallel      
C 3 4 ? parallel      
C 4 5 ? parallel      
C 5 6 ? parallel      
C 6 7 ? parallel      
D 1 2 ? parallel      
D 2 3 ? parallel      
D 3 4 ? parallel      
D 4 5 ? parallel      
E 1 2 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? parallel      
F 3 4 ? parallel      
F 4 5 ? parallel      
F 5 6 ? parallel      
F 6 7 ? 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 
A 1 ILE A 4   ? SER A 8   ? ILE B 4   SER B 8   
A 2 ASP A 52  ? VAL A 56  ? ASP B 52  VAL B 56  
A 3 ARG A 84  ? ILE A 89  ? ARG B 84  ILE B 89  
A 4 HIS A 123 ? MET A 127 ? HIS B 123 MET B 127 
A 5 VAL A 142 ? LEU A 145 ? VAL B 142 LEU B 145 
B 1 VAL A 30  ? LYS A 34  ? VAL B 30  LYS B 34  
B 2 THR A 40  ? ILE A 44  ? THR B 40  ILE B 44  
C 1 MET A 205 ? VAL A 208 ? MET B 205 VAL B 208 
C 2 ASP A 188 ? LYS A 194 ? ASP B 188 LYS B 194 
C 3 THR A 166 ? SER A 169 ? THR B 166 SER B 169 
C 4 VAL A 215 ? ALA A 223 ? VAL B 215 ALA B 223 
C 5 ARG A 243 ? GLY A 251 ? ARG B 243 GLY B 251 
C 6 ALA A 268 ? THR A 272 ? ALA B 268 THR B 272 
C 7 ILE A 287 ? ILE A 290 ? ILE B 287 ILE B 290 
D 1 ILE B 4   ? SER B 8   ? ILE A 4   SER A 8   
D 2 ASP B 52  ? VAL B 56  ? ASP A 52  VAL A 56  
D 3 ARG B 84  ? ILE B 89  ? ARG A 84  ILE A 89  
D 4 HIS B 123 ? MET B 127 ? HIS A 123 MET A 127 
D 5 VAL B 142 ? LEU B 145 ? VAL A 142 LEU A 145 
E 1 VAL B 30  ? LYS B 34  ? VAL A 30  LYS A 34  
E 2 THR B 40  ? ILE B 44  ? THR A 40  ILE A 44  
F 1 MET B 205 ? VAL B 208 ? MET A 205 VAL A 208 
F 2 ASP B 188 ? LYS B 194 ? ASP A 188 LYS A 194 
F 3 THR B 166 ? SER B 169 ? THR A 166 SER A 169 
F 4 ALA B 216 ? ALA B 223 ? ALA A 216 ALA A 223 
F 5 VAL B 244 ? GLY B 251 ? VAL A 244 GLY A 251 
F 6 ALA B 268 ? THR B 272 ? ALA A 268 THR A 272 
F 7 ILE B 287 ? ILE B 290 ? ILE A 287 ILE A 290 
# 
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 
A 1 2 N LYS A 5   ? N LYS B 5   O TYR A 54  ? O TYR B 54  
A 2 3 N VAL A 53  ? N VAL B 53  O THR A 86  ? O THR B 86  
A 3 4 N ILE A 89  ? N ILE B 89  O ILE A 125 ? O ILE B 125 
A 4 5 N THR A 126 ? N THR B 126 O LEU A 145 ? O LEU B 145 
B 1 2 N LYS A 33  ? N LYS B 33  O CYS A 41  ? O CYS B 41  
C 1 2 O VAL A 208 ? O VAL B 208 N LEU A 191 ? N LEU B 191 
C 2 3 O ILE A 192 ? O ILE B 192 N SER A 169 ? N SER B 169 
C 3 4 N VAL A 168 ? N VAL B 168 O ILE A 217 ? O ILE B 217 
C 4 5 N LEU A 218 ? N LEU B 218 O ILE A 247 ? O ILE B 247 
C 5 6 N ALA A 246 ? N ALA B 246 O VAL A 270 ? O VAL B 270 
C 6 7 N VAL A 271 ? N VAL B 271 O ILE A 290 ? O ILE B 290 
D 1 2 N LYS B 5   ? N LYS A 5   O TYR B 54  ? O TYR A 54  
D 2 3 N VAL B 53  ? N VAL A 53  O THR B 86  ? O THR A 86  
D 3 4 N ALA B 87  ? N ALA A 87  O ILE B 125 ? O ILE A 125 
D 4 5 N THR B 126 ? N THR A 126 O LEU B 145 ? O LEU A 145 
E 1 2 N LYS B 33  ? N LYS A 33  O CYS B 41  ? O CYS A 41  
F 1 2 O VAL B 208 ? O VAL A 208 N LEU B 191 ? N LEU A 191 
F 2 3 O ILE B 192 ? O ILE A 192 N SER B 169 ? N SER A 169 
F 3 4 N VAL B 168 ? N VAL A 168 O ILE B 217 ? O ILE A 217 
F 4 5 N LEU B 218 ? N LEU A 218 O ILE B 247 ? O ILE A 247 
F 5 6 N LEU B 248 ? N LEU A 248 O VAL B 270 ? O VAL A 270 
F 6 7 N VAL B 271 ? N VAL A 271 O ILE B 290 ? O ILE A 290 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 B 1002' 
AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 B 1003' 
AC3 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE SO4 B 1005' 
AC4 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 A 1001' 
AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 1004' 
AC6 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 A 1006' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 8 ARG B 104 ? ARG A 104  . ? 2_555 ? 
2  AC1 8 SER A 47  ? SER B 47   . ? 2_555 ? 
3  AC1 8 ARG A 49  ? ARG B 49   . ? 2_555 ? 
4  AC1 8 SER A 308 ? SER B 308  . ? 1_555 ? 
5  AC1 8 VAL A 309 ? VAL B 309  . ? 1_555 ? 
6  AC1 8 SER A 310 ? SER B 310  . ? 1_555 ? 
7  AC1 8 HOH I .   ? HOH B 3002 . ? 2_555 ? 
8  AC1 8 HOH I .   ? HOH B 3137 . ? 1_555 ? 
9  AC2 7 ALA A 223 ? ALA B 223  . ? 1_555 ? 
10 AC2 7 ASP A 224 ? ASP B 224  . ? 1_555 ? 
11 AC2 7 THR A 225 ? THR B 225  . ? 1_555 ? 
12 AC2 7 CYS A 226 ? CYS B 226  . ? 1_555 ? 
13 AC2 7 GLY A 227 ? GLY B 227  . ? 1_555 ? 
14 AC2 7 THR A 228 ? THR B 228  . ? 1_555 ? 
15 AC2 7 HOH I .   ? HOH B 3144 . ? 1_555 ? 
16 AC3 9 LYS B 99  ? LYS A 99   . ? 2_555 ? 
17 AC3 9 LYS B 100 ? LYS A 100  . ? 2_555 ? 
18 AC3 9 ASP B 101 ? ASP A 101  . ? 2_555 ? 
19 AC3 9 LYS B 102 ? LYS A 102  . ? 2_555 ? 
20 AC3 9 SER A 132 ? SER B 132  . ? 1_555 ? 
21 AC3 9 GLN A 135 ? GLN B 135  . ? 1_555 ? 
22 AC3 9 ASN A 144 ? ASN B 144  . ? 1_555 ? 
23 AC3 9 TYR A 146 ? TYR B 146  . ? 1_555 ? 
24 AC3 9 HOH I .   ? HOH B 3010 . ? 1_555 ? 
25 AC4 8 SER B 47  ? SER A 47   . ? 3_555 ? 
26 AC4 8 ARG B 49  ? ARG A 49   . ? 3_555 ? 
27 AC4 8 SER B 308 ? SER A 308  . ? 1_555 ? 
28 AC4 8 VAL B 309 ? VAL A 309  . ? 1_555 ? 
29 AC4 8 SER B 310 ? SER A 310  . ? 1_555 ? 
30 AC4 8 HOH J .   ? HOH A 3027 . ? 1_555 ? 
31 AC4 8 HOH J .   ? HOH A 3036 . ? 3_555 ? 
32 AC4 8 ARG A 104 ? ARG B 104  . ? 3_555 ? 
33 AC5 5 ASP B 224 ? ASP A 224  . ? 1_555 ? 
34 AC5 5 THR B 225 ? THR A 225  . ? 1_555 ? 
35 AC5 5 CYS B 226 ? CYS A 226  . ? 1_555 ? 
36 AC5 5 GLY B 227 ? GLY A 227  . ? 1_555 ? 
37 AC5 5 THR B 228 ? THR A 228  . ? 1_555 ? 
38 AC6 8 SER B 132 ? SER A 132  . ? 1_555 ? 
39 AC6 8 GLN B 135 ? GLN A 135  . ? 1_555 ? 
40 AC6 8 ASN B 144 ? ASN A 144  . ? 1_555 ? 
41 AC6 8 TYR B 146 ? TYR A 146  . ? 1_555 ? 
42 AC6 8 HOH J .   ? HOH A 3056 . ? 1_555 ? 
43 AC6 8 LYS A 100 ? LYS B 100  . ? 3_555 ? 
44 AC6 8 ASP A 101 ? ASP B 101  . ? 3_555 ? 
45 AC6 8 LYS A 102 ? LYS B 102  . ? 3_555 ? 
# 
_database_PDB_matrix.entry_id          3S5J 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3S5J 
_atom_sites.fract_transf_matrix[1][1]   0.005864 
_atom_sites.fract_transf_matrix[1][2]   0.003386 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006771 
_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]   0.016187 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
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   . ASN A 1 3   ? -11.539 -0.554  25.645  0.40  34.59 ? 3    ASN B N   1 
ATOM   2    C CA  . ASN A 1 3   ? -10.750 -0.603  24.453  0.40  30.98 ? 3    ASN B CA  1 
ATOM   3    C C   . ASN A 1 3   ? -11.620 -1.410  23.493  0.40  28.86 ? 3    ASN B C   1 
ATOM   4    O O   . ASN A 1 3   ? -11.561 -1.137  22.367  0.40  29.10 ? 3    ASN B O   1 
ATOM   5    C CB  . ASN A 1 3   ? -9.365  -1.252  24.674  0.40  32.40 ? 3    ASN B CB  1 
ATOM   6    C CG  . ASN A 1 3   ? -8.167  -0.340  24.331  0.40  36.09 ? 3    ASN B CG  1 
ATOM   7    O OD1 . ASN A 1 3   ? -7.343  -0.048  25.182  0.40  36.87 ? 3    ASN B OD1 1 
ATOM   8    N ND2 . ASN A 1 3   ? -8.015  0.022   23.091  0.40  34.42 ? 3    ASN B ND2 1 
ATOM   9    N N   . ILE A 1 4   ? -12.445 -2.348  23.941  1.00  27.22 ? 4    ILE B N   1 
ATOM   10   C CA  . ILE A 1 4   ? -13.247 -3.179  23.034  1.00  29.36 ? 4    ILE B CA  1 
ATOM   11   C C   . ILE A 1 4   ? -14.633 -2.612  22.720  1.00  30.98 ? 4    ILE B C   1 
ATOM   12   O O   . ILE A 1 4   ? -15.329 -2.256  23.617  1.00  26.47 ? 4    ILE B O   1 
ATOM   13   C CB  . ILE A 1 4   ? -13.353 -4.638  23.525  1.00  30.17 ? 4    ILE B CB  1 
ATOM   14   C CG1 . ILE A 1 4   ? -13.754 -5.587  22.431  1.00  30.02 ? 4    ILE B CG1 1 
ATOM   15   C CG2 . ILE A 1 4   ? -14.370 -4.776  24.503  1.00  40.56 ? 4    ILE B CG2 1 
ATOM   16   C CD1 . ILE A 1 4   ? -15.138 -5.561  22.098  1.00  28.05 ? 4    ILE B CD1 1 
ATOM   17   N N   . LYS A 1 5   ? -14.989 -2.489  21.435  0.40  16.70 ? 5    LYS B N   1 
ATOM   18   C CA  . LYS A 1 5   ? -16.298 -1.960  21.102  0.40  16.09 ? 5    LYS B CA  1 
ATOM   19   C C   . LYS A 1 5   ? -16.882 -2.850  20.016  0.40  21.73 ? 5    LYS B C   1 
ATOM   20   O O   . LYS A 1 5   ? -16.221 -3.141  19.018  0.40  13.91 ? 5    LYS B O   1 
ATOM   21   C CB  . LYS A 1 5   ? -16.200 -0.513  20.624  0.40  17.23 ? 5    LYS B CB  1 
ATOM   22   C CG  . LYS A 1 5   ? -17.416 0.334   20.997  0.40  26.82 ? 5    LYS B CG  1 
ATOM   23   C CD  . LYS A 1 5   ? -17.203 1.035   22.342  0.40  27.40 ? 5    LYS B CD  1 
ATOM   24   C CE  . LYS A 1 5   ? -18.459 1.047   23.211  0.40  30.88 ? 5    LYS B CE  1 
ATOM   25   N NZ  . LYS A 1 5   ? -19.657 0.448   22.553  0.40  32.10 ? 5    LYS B NZ  1 
ATOM   26   N N   . ILE A 1 6   ? -18.117 -3.297  20.216  1.00  22.36 ? 6    ILE B N   1 
ATOM   27   C CA  . ILE A 1 6   ? -18.749 -4.210  19.261  1.00  24.12 ? 6    ILE B CA  1 
ATOM   28   C C   . ILE A 1 6   ? -19.947 -3.539  18.639  1.00  22.49 ? 6    ILE B C   1 
ATOM   29   O O   . ILE A 1 6   ? -20.814 -3.050  19.354  1.00  25.45 ? 6    ILE B O   1 
ATOM   30   C CB  . ILE A 1 6   ? -19.284 -5.471  19.934  1.00  25.12 ? 6    ILE B CB  1 
ATOM   31   C CG1 . ILE A 1 6   ? -18.174 -6.223  20.654  1.00  33.37 ? 6    ILE B CG1 1 
ATOM   32   C CG2 . ILE A 1 6   ? -19.956 -6.391  18.893  1.00  23.60 ? 6    ILE B CG2 1 
ATOM   33   C CD1 . ILE A 1 6   ? -18.688 -7.033  21.805  1.00  36.96 ? 6    ILE B CD1 1 
ATOM   34   N N   . PHE A 1 7   ? -20.007 -3.540  17.312  1.00  21.66 ? 7    PHE B N   1 
ATOM   35   C CA  . PHE A 1 7   ? -21.150 -3.003  16.580  1.00  22.49 ? 7    PHE B CA  1 
ATOM   36   C C   . PHE A 1 7   ? -21.817 -4.099  15.763  1.00  25.40 ? 7    PHE B C   1 
ATOM   37   O O   . PHE A 1 7   ? -21.175 -5.047  15.317  1.00  22.55 ? 7    PHE B O   1 
ATOM   38   C CB  . PHE A 1 7   ? -20.736 -1.880  15.616  1.00  25.61 ? 7    PHE B CB  1 
ATOM   39   C CG  . PHE A 1 7   ? -20.290 -0.617  16.297  1.00  25.70 ? 7    PHE B CG  1 
ATOM   40   C CD1 . PHE A 1 7   ? -18.954 -0.412  16.586  1.00  25.26 ? 7    PHE B CD1 1 
ATOM   41   C CD2 . PHE A 1 7   ? -21.197 0.364   16.632  1.00  24.89 ? 7    PHE B CD2 1 
ATOM   42   C CE1 . PHE A 1 7   ? -18.530 0.754   17.219  1.00  28.34 ? 7    PHE B CE1 1 
ATOM   43   C CE2 . PHE A 1 7   ? -20.790 1.530   17.250  1.00  27.40 ? 7    PHE B CE2 1 
ATOM   44   C CZ  . PHE A 1 7   ? -19.448 1.727   17.548  1.00  29.88 ? 7    PHE B CZ  1 
ATOM   45   N N   . SER A 1 8   ? -23.111 -3.955  15.556  1.00  20.00 ? 8    SER B N   1 
ATOM   46   C CA  . SER A 1 8   ? -23.844 -4.895  14.727  1.00  27.60 ? 8    SER B CA  1 
ATOM   47   C C   . SER A 1 8   ? -24.253 -4.229  13.424  1.00  29.59 ? 8    SER B C   1 
ATOM   48   O O   . SER A 1 8   ? -24.621 -3.051  13.413  1.00  29.79 ? 8    SER B O   1 
ATOM   49   C CB  . SER A 1 8   ? -25.109 -5.370  15.435  1.00  30.40 ? 8    SER B CB  1 
ATOM   50   O OG  . SER A 1 8   ? -25.723 -6.414  14.701  1.00  36.26 ? 8    SER B OG  1 
ATOM   51   N N   . GLY A 1 9   ? -24.188 -4.992  12.332  1.00  37.77 ? 9    GLY B N   1 
ATOM   52   C CA  . GLY A 1 9   ? -24.799 -4.587  11.070  1.00  36.45 ? 9    GLY B CA  1 
ATOM   53   C C   . GLY A 1 9   ? -26.314 -4.759  11.121  1.00  43.69 ? 9    GLY B C   1 
ATOM   54   O O   . GLY A 1 9   ? -26.817 -5.609  11.862  1.00  46.92 ? 9    GLY B O   1 
ATOM   55   N N   . SER A 1 10  ? -27.032 -3.936  10.361  0.10  41.87 ? 10   SER B N   1 
ATOM   56   C CA  . SER A 1 10  ? -28.490 -4.013  10.231  0.10  43.86 ? 10   SER B CA  1 
ATOM   57   C C   . SER A 1 10  ? -29.379 -3.956  11.472  0.10  44.59 ? 10   SER B C   1 
ATOM   58   O O   . SER A 1 10  ? -29.161 -3.147  12.370  0.10  44.96 ? 10   SER B O   1 
ATOM   59   C CB  . SER A 1 10  ? -28.886 -5.170  9.314   0.10  43.27 ? 10   SER B CB  1 
ATOM   60   O OG  . SER A 1 10  ? -29.178 -6.334  10.082  0.10  43.07 ? 10   SER B OG  1 
ATOM   61   N N   . SER A 1 11  ? -30.390 -4.825  11.497  0.20  45.01 ? 11   SER B N   1 
ATOM   62   C CA  . SER A 1 11  ? -31.310 -4.926  12.628  0.20  46.66 ? 11   SER B CA  1 
ATOM   63   C C   . SER A 1 11  ? -31.510 -6.415  12.905  0.20  45.83 ? 11   SER B C   1 
ATOM   64   O O   . SER A 1 11  ? -32.385 -6.795  13.684  0.20  46.00 ? 11   SER B O   1 
ATOM   65   C CB  . SER A 1 11  ? -32.666 -4.238  12.450  0.20  47.23 ? 11   SER B CB  1 
ATOM   66   O OG  . SER A 1 11  ? -33.495 -4.422  13.579  0.20  46.38 ? 11   SER B OG  1 
ATOM   67   N N   . HIS A 1 12  ? -30.712 -7.258  12.253  0.76  47.71 ? 12   HIS B N   1 
ATOM   68   C CA  . HIS A 1 12  ? -30.687 -8.683  12.585  0.76  41.74 ? 12   HIS B CA  1 
ATOM   69   C C   . HIS A 1 12  ? -29.647 -8.923  13.674  0.76  41.65 ? 12   HIS B C   1 
ATOM   70   O O   . HIS A 1 12  ? -28.735 -9.724  13.510  0.76  39.60 ? 12   HIS B O   1 
ATOM   71   C CB  . HIS A 1 12  ? -30.349 -9.526  11.358  0.76  47.62 ? 12   HIS B CB  1 
ATOM   72   C CG  . HIS A 1 12  ? -31.503 -9.734  10.425  0.76  48.26 ? 12   HIS B CG  1 
ATOM   73   N ND1 . HIS A 1 12  ? -32.239 -10.894 10.407  0.76  50.03 ? 12   HIS B ND1 1 
ATOM   74   C CD2 . HIS A 1 12  ? -32.034 -8.927  9.475   0.76  46.73 ? 12   HIS B CD2 1 
ATOM   75   C CE1 . HIS A 1 12  ? -33.183 -10.797 9.481   0.76  53.61 ? 12   HIS B CE1 1 
ATOM   76   N NE2 . HIS A 1 12  ? -33.080 -9.616  8.904   0.76  48.64 ? 12   HIS B NE2 1 
ATOM   77   N N   . GLN A 1 13  ? -29.796 -8.231  14.796  1.00  44.20 ? 13   GLN B N   1 
ATOM   78   C CA  . GLN A 1 13  ? -28.741 -8.185  15.791  1.00  40.65 ? 13   GLN B CA  1 
ATOM   79   C C   . GLN A 1 13  ? -28.681 -9.372  16.767  1.00  32.39 ? 13   GLN B C   1 
ATOM   80   O O   . GLN A 1 13  ? -27.926 -9.314  17.734  1.00  31.87 ? 13   GLN B O   1 
ATOM   81   C CB  . GLN A 1 13  ? -28.827 -6.862  16.567  1.00  46.22 ? 13   GLN B CB  1 
ATOM   82   C CG  . GLN A 1 13  ? -28.962 -5.635  15.650  1.00  48.47 ? 13   GLN B CG  1 
ATOM   83   C CD  . GLN A 1 13  ? -28.709 -4.323  16.374  1.00  50.72 ? 13   GLN B CD  1 
ATOM   84   O OE1 . GLN A 1 13  ? -27.562 -3.922  16.570  1.00  50.99 ? 13   GLN B OE1 1 
ATOM   85   N NE2 . GLN A 1 13  ? -29.780 -3.643  16.768  1.00  57.98 ? 13   GLN B NE2 1 
ATOM   86   N N   . ASP A 1 14  ? -29.435 -10.441 16.524  0.40  28.09 ? 14   ASP B N   1 
ATOM   87   C CA  . ASP A 1 14  ? -29.494 -11.523 17.508  0.40  25.57 ? 14   ASP B CA  1 
ATOM   88   C C   . ASP A 1 14  ? -28.121 -12.117 17.830  0.40  26.87 ? 14   ASP B C   1 
ATOM   89   O O   . ASP A 1 14  ? -27.722 -12.151 18.993  0.40  20.98 ? 14   ASP B O   1 
ATOM   90   C CB  . ASP A 1 14  ? -30.480 -12.621 17.109  0.40  27.11 ? 14   ASP B CB  1 
ATOM   91   C CG  . ASP A 1 14  ? -30.875 -13.495 18.290  0.40  30.59 ? 14   ASP B CG  1 
ATOM   92   O OD1 . ASP A 1 14  ? -31.821 -13.120 19.014  0.40  33.84 ? 14   ASP B OD1 1 
ATOM   93   O OD2 . ASP A 1 14  ? -30.233 -14.544 18.505  0.40  32.41 ? 14   ASP B OD2 1 
ATOM   94   N N   . LEU A 1 15  ? -27.402 -12.586 16.808  1.00  29.57 ? 15   LEU B N   1 
ATOM   95   C CA  . LEU A 1 15  ? -26.046 -13.093 17.016  1.00  28.55 ? 15   LEU B CA  1 
ATOM   96   C C   . LEU A 1 15  ? -25.215 -12.000 17.672  1.00  25.90 ? 15   LEU B C   1 
ATOM   97   O O   . LEU A 1 15  ? -24.530 -12.238 18.660  1.00  24.35 ? 15   LEU B O   1 
ATOM   98   C CB  . LEU A 1 15  ? -25.399 -13.473 15.681  1.00  28.03 ? 15   LEU B CB  1 
ATOM   99   C CG  . LEU A 1 15  ? -24.446 -14.669 15.619  1.00  36.27 ? 15   LEU B CG  1 
ATOM   100  C CD1 . LEU A 1 15  ? -23.409 -14.482 14.492  1.00  29.97 ? 15   LEU B CD1 1 
ATOM   101  C CD2 . LEU A 1 15  ? -23.760 -14.992 16.945  1.00  26.37 ? 15   LEU B CD2 1 
ATOM   102  N N   . SER A 1 16  ? -25.260 -10.807 17.093  1.00  22.57 ? 16   SER B N   1 
ATOM   103  C CA  . SER A 1 16  ? -24.449 -9.697  17.582  1.00  28.04 ? 16   SER B CA  1 
ATOM   104  C C   . SER A 1 16  ? -24.699 -9.458  19.060  1.00  27.09 ? 16   SER B C   1 
ATOM   105  O O   . SER A 1 16  ? -23.768 -9.229  19.825  1.00  25.65 ? 16   SER B O   1 
ATOM   106  C CB  . SER A 1 16  ? -24.756 -8.427  16.799  1.00  29.26 ? 16   SER B CB  1 
ATOM   107  O OG  . SER A 1 16  ? -24.486 -8.608  15.427  1.00  34.35 ? 16   SER B OG  1 
ATOM   108  N N   . GLN A 1 17  ? -25.965 -9.527  19.459  1.00  29.75 ? 17   GLN B N   1 
ATOM   109  C CA  . GLN A 1 17  ? -26.332 -9.262  20.844  1.00  27.66 ? 17   GLN B CA  1 
ATOM   110  C C   . GLN A 1 17  ? -25.875 -10.402 21.734  1.00  24.83 ? 17   GLN B C   1 
ATOM   111  O O   . GLN A 1 17  ? -25.416 -10.173 22.847  1.00  26.69 ? 17   GLN B O   1 
ATOM   112  C CB  . GLN A 1 17  ? -27.848 -9.025  20.972  1.00  31.92 ? 17   GLN B CB  1 
ATOM   113  C CG  . GLN A 1 17  ? -28.326 -8.692  22.384  1.00  33.05 ? 17   GLN B CG  1 
ATOM   114  C CD  . GLN A 1 17  ? -27.722 -7.407  22.937  1.00  37.91 ? 17   GLN B CD  1 
ATOM   115  O OE1 . GLN A 1 17  ? -27.886 -6.325  22.367  1.00  39.24 ? 17   GLN B OE1 1 
ATOM   116  N NE2 . GLN A 1 17  ? -27.019 -7.527  24.063  1.00  37.89 ? 17   GLN B NE2 1 
ATOM   117  N N   . LYS A 1 18  ? -25.981 -11.630 21.243  1.00  23.19 ? 18   LYS B N   1 
ATOM   118  C CA  . LYS A 1 18  ? -25.485 -12.782 21.991  1.00  28.16 ? 18   LYS B CA  1 
ATOM   119  C C   . LYS A 1 18  ? -23.994 -12.674 22.260  1.00  28.82 ? 18   LYS B C   1 
ATOM   120  O O   . LYS A 1 18  ? -23.514 -13.064 23.334  1.00  27.88 ? 18   LYS B O   1 
ATOM   121  C CB  . LYS A 1 18  ? -25.770 -14.085 21.251  1.00  30.89 ? 18   LYS B CB  1 
ATOM   122  C CG  . LYS A 1 18  ? -27.125 -14.698 21.555  1.00  32.47 ? 18   LYS B CG  1 
ATOM   123  C CD  . LYS A 1 18  ? -27.323 -15.936 20.700  1.00  33.76 ? 18   LYS B CD  1 
ATOM   124  C CE  . LYS A 1 18  ? -28.578 -16.701 21.086  1.00  41.39 ? 18   LYS B CE  1 
ATOM   125  N NZ  . LYS A 1 18  ? -28.874 -17.731 20.053  1.00  49.89 ? 18   LYS B NZ  1 
ATOM   126  N N   . ILE A 1 19  ? -23.251 -12.164 21.278  1.00  26.82 ? 19   ILE B N   1 
ATOM   127  C CA  . ILE A 1 19  ? -21.801 -12.042 21.430  1.00  27.15 ? 19   ILE B CA  1 
ATOM   128  C C   . ILE A 1 19  ? -21.475 -10.926 22.425  1.00  23.66 ? 19   ILE B C   1 
ATOM   129  O O   . ILE A 1 19  ? -20.622 -11.085 23.302  1.00  22.36 ? 19   ILE B O   1 
ATOM   130  C CB  . ILE A 1 19  ? -21.105 -11.754 20.084  1.00  25.32 ? 19   ILE B CB  1 
ATOM   131  C CG1 . ILE A 1 19  ? -21.221 -12.970 19.158  1.00  23.88 ? 19   ILE B CG1 1 
ATOM   132  C CG2 . ILE A 1 19  ? -19.652 -11.373 20.315  1.00  23.54 ? 19   ILE B CG2 1 
ATOM   133  C CD1 . ILE A 1 19  ? -21.185 -12.625 17.663  1.00  23.09 ? 19   ILE B CD1 1 
ATOM   134  N N   . ALA A 1 20  ? -22.158 -9.796  22.274  1.00  24.00 ? 20   ALA B N   1 
ATOM   135  C CA  . ALA A 1 20  ? -21.953 -8.669  23.171  1.00  27.60 ? 20   ALA B CA  1 
ATOM   136  C C   . ALA A 1 20  ? -22.276 -9.102  24.604  1.00  26.30 ? 20   ALA B C   1 
ATOM   137  O O   . ALA A 1 20  ? -21.468 -8.874  25.507  1.00  27.50 ? 20   ALA B O   1 
ATOM   138  C CB  . ALA A 1 20  ? -22.786 -7.471  22.746  1.00  24.11 ? 20   ALA B CB  1 
ATOM   139  N N   . ASP A 1 21  ? -23.427 -9.746  24.794  0.40  23.59 ? 21   ASP B N   1 
ATOM   140  C CA  . ASP A 1 21  ? -23.809 -10.285 26.099  0.40  25.57 ? 21   ASP B CA  1 
ATOM   141  C C   . ASP A 1 21  ? -22.686 -11.118 26.719  0.40  28.08 ? 21   ASP B C   1 
ATOM   142  O O   . ASP A 1 21  ? -22.301 -10.893 27.867  0.40  24.55 ? 21   ASP B O   1 
ATOM   143  C CB  . ASP A 1 21  ? -25.075 -11.145 26.001  0.40  24.73 ? 21   ASP B CB  1 
ATOM   144  C CG  . ASP A 1 21  ? -26.340 -10.324 25.854  0.40  26.34 ? 21   ASP B CG  1 
ATOM   145  O OD1 . ASP A 1 21  ? -26.284 -9.092  26.025  0.40  26.21 ? 21   ASP B OD1 1 
ATOM   146  O OD2 . ASP A 1 21  ? -27.406 -10.918 25.584  0.40  27.32 ? 21   ASP B OD2 1 
ATOM   147  N N   . ARG A 1 22  ? -22.164 -12.083 25.963  1.00  29.62 ? 22   ARG B N   1 
ATOM   148  C CA  . ARG A 1 22  ? -21.121 -12.964 26.494  1.00  30.78 ? 22   ARG B CA  1 
ATOM   149  C C   . ARG A 1 22  ? -19.851 -12.196 26.889  1.00  32.41 ? 22   ARG B C   1 
ATOM   150  O O   . ARG A 1 22  ? -19.093 -12.622 27.763  1.00  32.95 ? 22   ARG B O   1 
ATOM   151  C CB  . ARG A 1 22  ? -20.818 -14.105 25.520  1.00  30.33 ? 22   ARG B CB  1 
ATOM   152  C CG  . ARG A 1 22  ? -22.020 -15.011 25.290  1.00  35.12 ? 22   ARG B CG  1 
ATOM   153  C CD  . ARG A 1 22  ? -21.743 -16.116 24.282  1.00  35.87 ? 22   ARG B CD  1 
ATOM   154  N NE  . ARG A 1 22  ? -21.515 -17.389 24.948  1.00  50.88 ? 22   ARG B NE  1 
ATOM   155  C CZ  . ARG A 1 22  ? -22.478 -18.246 25.279  1.00  52.79 ? 22   ARG B CZ  1 
ATOM   156  N NH1 . ARG A 1 22  ? -23.746 -17.971 24.993  1.00  50.05 ? 22   ARG B NH1 1 
ATOM   157  N NH2 . ARG A 1 22  ? -22.171 -19.381 25.890  1.00  45.22 ? 22   ARG B NH2 1 
ATOM   158  N N   . LEU A 1 23  ? -19.649 -11.043 26.273  1.00  27.94 ? 23   LEU B N   1 
ATOM   159  C CA  . LEU A 1 23  ? -18.480 -10.228 26.584  1.00  30.26 ? 23   LEU B CA  1 
ATOM   160  C C   . LEU A 1 23  ? -18.744 -9.204  27.674  1.00  28.81 ? 23   LEU B C   1 
ATOM   161  O O   . LEU A 1 23  ? -17.845 -8.449  28.025  1.00  30.62 ? 23   LEU B O   1 
ATOM   162  C CB  . LEU A 1 23  ? -17.984 -9.505  25.337  1.00  26.37 ? 23   LEU B CB  1 
ATOM   163  C CG  . LEU A 1 23  ? -17.403 -10.379 24.211  1.00  30.17 ? 23   LEU B CG  1 
ATOM   164  C CD1 . LEU A 1 23  ? -17.111 -9.534  22.974  1.00  31.54 ? 23   LEU B CD1 1 
ATOM   165  C CD2 . LEU A 1 23  ? -16.161 -11.103 24.659  1.00  31.72 ? 23   LEU B CD2 1 
ATOM   166  N N   . GLY A 1 24  ? -19.976 -9.152  28.177  1.00  28.75 ? 24   GLY B N   1 
ATOM   167  C CA  . GLY A 1 24  ? -20.344 -8.170  29.188  1.00  30.00 ? 24   GLY B CA  1 
ATOM   168  C C   . GLY A 1 24  ? -20.484 -6.758  28.646  1.00  30.23 ? 24   GLY B C   1 
ATOM   169  O O   . GLY A 1 24  ? -20.339 -5.788  29.396  1.00  26.28 ? 24   GLY B O   1 
ATOM   170  N N   . LEU A 1 25  ? -20.775 -6.637  27.348  1.00  27.93 ? 25   LEU B N   1 
ATOM   171  C CA  . LEU A 1 25  ? -20.883 -5.329  26.686  1.00  26.04 ? 25   LEU B CA  1 
ATOM   172  C C   . LEU A 1 25  ? -22.268 -5.029  26.094  1.00  27.17 ? 25   LEU B C   1 
ATOM   173  O O   . LEU A 1 25  ? -23.021 -5.938  25.771  1.00  23.11 ? 25   LEU B O   1 
ATOM   174  C CB  . LEU A 1 25  ? -19.847 -5.221  25.557  1.00  26.70 ? 25   LEU B CB  1 
ATOM   175  C CG  . LEU A 1 25  ? -18.379 -5.475  25.884  1.00  32.78 ? 25   LEU B CG  1 
ATOM   176  C CD1 . LEU A 1 25  ? -17.552 -5.427  24.604  1.00  27.35 ? 25   LEU B CD1 1 
ATOM   177  C CD2 . LEU A 1 25  ? -17.862 -4.465  26.916  1.00  22.29 ? 25   LEU B CD2 1 
ATOM   178  N N   . GLU A 1 26  ? -22.591 -3.743  25.957  0.94  21.84 ? 26   GLU B N   1 
ATOM   179  C CA  . GLU A 1 26  ? -23.673 -3.315  25.086  0.94  27.94 ? 26   GLU B CA  1 
ATOM   180  C C   . GLU A 1 26  ? -23.123 -3.108  23.672  0.94  25.26 ? 26   GLU B C   1 
ATOM   181  O O   . GLU A 1 26  ? -21.968 -2.727  23.508  0.94  23.07 ? 26   GLU B O   1 
ATOM   182  C CB  . GLU A 1 26  ? -24.292 -2.006  25.576  0.94  27.44 ? 26   GLU B CB  1 
ATOM   183  C CG  . GLU A 1 26  ? -25.153 -2.152  26.815  0.94  34.10 ? 26   GLU B CG  1 
ATOM   184  C CD  . GLU A 1 26  ? -25.789 -0.834  27.223  0.94  41.18 ? 26   GLU B CD  1 
ATOM   185  O OE1 . GLU A 1 26  ? -25.462 0.209   26.596  0.94  42.29 ? 26   GLU B OE1 1 
ATOM   186  O OE2 . GLU A 1 26  ? -26.619 -0.845  28.163  0.94  44.40 ? 26   GLU B OE2 1 
ATOM   187  N N   . LEU A 1 27  ? -23.953 -3.368  22.669  1.00  24.74 ? 27   LEU B N   1 
ATOM   188  C CA  . LEU A 1 27  ? -23.620 -3.043  21.281  1.00  25.66 ? 27   LEU B CA  1 
ATOM   189  C C   . LEU A 1 27  ? -23.468 -1.537  21.142  1.00  26.82 ? 27   LEU B C   1 
ATOM   190  O O   . LEU A 1 27  ? -24.247 -0.783  21.704  1.00  25.20 ? 27   LEU B O   1 
ATOM   191  C CB  . LEU A 1 27  ? -24.732 -3.510  20.342  1.00  24.80 ? 27   LEU B CB  1 
ATOM   192  C CG  . LEU A 1 27  ? -24.779 -5.016  20.087  1.00  27.52 ? 27   LEU B CG  1 
ATOM   193  C CD1 . LEU A 1 27  ? -26.042 -5.378  19.291  1.00  33.39 ? 27   LEU B CD1 1 
ATOM   194  C CD2 . LEU A 1 27  ? -23.513 -5.456  19.350  1.00  25.12 ? 27   LEU B CD2 1 
ATOM   195  N N   . GLY A 1 28  ? -22.466 -1.100  20.392  1.00  25.40 ? 28   GLY B N   1 
ATOM   196  C CA  . GLY A 1 28  ? -22.249 0.322   20.186  1.00  24.94 ? 28   GLY B CA  1 
ATOM   197  C C   . GLY A 1 28  ? -23.431 0.939   19.463  1.00  29.21 ? 28   GLY B C   1 
ATOM   198  O O   . GLY A 1 28  ? -24.168 0.247   18.744  1.00  25.89 ? 28   GLY B O   1 
ATOM   199  N N   . LYS A 1 29  ? -23.624 2.241   19.660  1.00  25.92 ? 29   LYS B N   1 
ATOM   200  C CA  . LYS A 1 29  ? -24.741 2.944   19.048  1.00  28.98 ? 29   LYS B CA  1 
ATOM   201  C C   . LYS A 1 29  ? -24.439 3.237   17.582  1.00  29.95 ? 29   LYS B C   1 
ATOM   202  O O   . LYS A 1 29  ? -23.399 3.812   17.266  1.00  25.31 ? 29   LYS B O   1 
ATOM   203  C CB  . LYS A 1 29  ? -24.980 4.255   19.774  1.00  30.82 ? 29   LYS B CB  1 
ATOM   204  C CG  . LYS A 1 29  ? -24.920 4.115   21.295  1.00  40.78 ? 29   LYS B CG  1 
ATOM   205  C CD  . LYS A 1 29  ? -24.840 5.483   21.982  1.00  43.48 ? 29   LYS B CD  1 
ATOM   206  C CE  . LYS A 1 29  ? -24.725 5.337   23.499  1.00  52.76 ? 29   LYS B CE  1 
ATOM   207  N NZ  . LYS A 1 29  ? -25.949 4.720   24.078  1.00  50.90 ? 29   LYS B NZ  1 
ATOM   208  N N   . VAL A 1 30  ? -25.355 2.845   16.702  1.00  32.26 ? 30   VAL B N   1 
ATOM   209  C CA  . VAL A 1 30  ? -25.241 3.150   15.281  1.00  35.29 ? 30   VAL B CA  1 
ATOM   210  C C   . VAL A 1 30  ? -26.584 3.524   14.668  1.00  42.43 ? 30   VAL B C   1 
ATOM   211  O O   . VAL A 1 30  ? -27.582 2.847   14.900  1.00  40.30 ? 30   VAL B O   1 
ATOM   212  C CB  . VAL A 1 30  ? -24.758 1.950   14.480  1.00  35.73 ? 30   VAL B CB  1 
ATOM   213  C CG1 . VAL A 1 30  ? -24.575 2.358   13.026  1.00  41.08 ? 30   VAL B CG1 1 
ATOM   214  C CG2 . VAL A 1 30  ? -23.479 1.417   15.041  1.00  36.56 ? 30   VAL B CG2 1 
ATOM   215  N N   . VAL A 1 31  ? -26.597 4.591   13.877  1.00  37.25 ? 31   VAL B N   1 
ATOM   216  C CA  . VAL A 1 31  ? -27.772 4.961   13.088  1.00  47.98 ? 31   VAL B CA  1 
ATOM   217  C C   . VAL A 1 31  ? -27.620 4.395   11.675  1.00  50.11 ? 31   VAL B C   1 
ATOM   218  O O   . VAL A 1 31  ? -26.876 4.950   10.870  1.00  49.21 ? 31   VAL B O   1 
ATOM   219  C CB  . VAL A 1 31  ? -27.896 6.488   12.949  1.00  48.19 ? 31   VAL B CB  1 
ATOM   220  C CG1 . VAL A 1 31  ? -29.231 6.849   12.319  1.00  50.48 ? 31   VAL B CG1 1 
ATOM   221  C CG2 . VAL A 1 31  ? -27.724 7.178   14.300  1.00  49.41 ? 31   VAL B CG2 1 
ATOM   222  N N   . THR A 1 32  ? -28.326 3.305   11.377  0.71  51.23 ? 32   THR B N   1 
ATOM   223  C CA  . THR A 1 32  ? -28.083 2.524   10.160  0.71  48.63 ? 32   THR B CA  1 
ATOM   224  C C   . THR A 1 32  ? -29.332 2.280   9.304   0.71  52.18 ? 32   THR B C   1 
ATOM   225  O O   . THR A 1 32  ? -30.024 1.274   9.474   0.71  53.57 ? 32   THR B O   1 
ATOM   226  C CB  . THR A 1 32  ? -27.455 1.157   10.514  0.71  49.41 ? 32   THR B CB  1 
ATOM   227  O OG1 . THR A 1 32  ? -27.566 0.265   9.398   0.71  50.51 ? 32   THR B OG1 1 
ATOM   228  C CG2 . THR A 1 32  ? -28.169 0.533   11.714  0.71  53.67 ? 32   THR B CG2 1 
ATOM   229  N N   . LYS A 1 33  ? -29.601 3.183   8.364   0.010 50.48 ? 33   LYS B N   1 
ATOM   230  C CA  . LYS A 1 33  ? -30.829 3.114   7.571   0.010 50.40 ? 33   LYS B CA  1 
ATOM   231  C C   . LYS A 1 33  ? -30.574 3.112   6.060   0.010 49.12 ? 33   LYS B C   1 
ATOM   232  O O   . LYS A 1 33  ? -29.578 3.659   5.596   0.010 46.90 ? 33   LYS B O   1 
ATOM   233  C CB  . LYS A 1 33  ? -31.747 4.286   7.933   0.010 50.92 ? 33   LYS B CB  1 
ATOM   234  C CG  . LYS A 1 33  ? -31.356 5.606   7.279   0.010 50.43 ? 33   LYS B CG  1 
ATOM   235  C CD  . LYS A 1 33  ? -31.705 6.802   8.154   0.010 51.16 ? 33   LYS B CD  1 
ATOM   236  C CE  . LYS A 1 33  ? -31.153 8.092   7.559   0.010 50.91 ? 33   LYS B CE  1 
ATOM   237  N NZ  . LYS A 1 33  ? -31.264 9.259   8.485   0.010 51.18 ? 33   LYS B NZ  1 
ATOM   238  N N   . LYS A 1 34  ? -31.477 2.490   5.300   1.00  55.90 ? 34   LYS B N   1 
ATOM   239  C CA  . LYS A 1 34  ? -31.437 2.561   3.837   1.00  45.92 ? 34   LYS B CA  1 
ATOM   240  C C   . LYS A 1 34  ? -32.252 3.747   3.331   1.00  48.95 ? 34   LYS B C   1 
ATOM   241  O O   . LYS A 1 34  ? -33.442 3.870   3.630   1.00  51.60 ? 34   LYS B O   1 
ATOM   242  C CB  . LYS A 1 34  ? -31.960 1.271   3.201   1.00  47.57 ? 34   LYS B CB  1 
ATOM   243  C CG  . LYS A 1 34  ? -30.927 0.153   3.104   1.00  50.37 ? 34   LYS B CG  1 
ATOM   244  C CD  . LYS A 1 34  ? -30.839 -0.383  1.674   1.00  44.56 ? 34   LYS B CD  1 
ATOM   245  C CE  . LYS A 1 34  ? -32.208 -0.860  1.184   1.00  48.57 ? 34   LYS B CE  1 
ATOM   246  N NZ  . LYS A 1 34  ? -32.149 -1.362  -0.218  1.00  48.65 ? 34   LYS B NZ  1 
ATOM   247  N N   . PHE A 1 35  ? -31.611 4.617   2.559   0.010 43.50 ? 35   PHE B N   1 
ATOM   248  C CA  . PHE A 1 35  ? -32.268 5.818   2.057   0.010 43.48 ? 35   PHE B CA  1 
ATOM   249  C C   . PHE A 1 35  ? -33.385 5.509   1.070   0.010 43.61 ? 35   PHE B C   1 
ATOM   250  O O   . PHE A 1 35  ? -33.684 4.350   0.781   0.010 43.17 ? 35   PHE B O   1 
ATOM   251  C CB  . PHE A 1 35  ? -31.256 6.755   1.397   0.010 41.80 ? 35   PHE B CB  1 
ATOM   252  C CG  . PHE A 1 35  ? -30.307 7.403   2.362   0.010 41.98 ? 35   PHE B CG  1 
ATOM   253  C CD1 . PHE A 1 35  ? -28.965 7.065   2.362   0.010 39.93 ? 35   PHE B CD1 1 
ATOM   254  C CD2 . PHE A 1 35  ? -30.756 8.352   3.267   0.010 43.32 ? 35   PHE B CD2 1 
ATOM   255  C CE1 . PHE A 1 35  ? -28.088 7.665   3.242   0.010 40.90 ? 35   PHE B CE1 1 
ATOM   256  C CE2 . PHE A 1 35  ? -29.884 8.953   4.153   0.010 44.46 ? 35   PHE B CE2 1 
ATOM   257  C CZ  . PHE A 1 35  ? -28.548 8.612   4.140   0.010 43.42 ? 35   PHE B CZ  1 
ATOM   258  N N   . SER A 1 36  ? -33.992 6.572   0.555   0.010 44.99 ? 36   SER B N   1 
ATOM   259  C CA  . SER A 1 36  ? -35.059 6.458   -0.423  0.010 45.82 ? 36   SER B CA  1 
ATOM   260  C C   . SER A 1 36  ? -34.593 5.716   -1.670  0.010 44.17 ? 36   SER B C   1 
ATOM   261  O O   . SER A 1 36  ? -35.296 4.845   -2.177  0.010 43.49 ? 36   SER B O   1 
ATOM   262  C CB  . SER A 1 36  ? -35.559 7.849   -0.806  0.010 48.19 ? 36   SER B CB  1 
ATOM   263  O OG  . SER A 1 36  ? -36.973 7.895   -0.844  0.010 50.72 ? 36   SER B OG  1 
ATOM   264  N N   . ASN A 1 37  ? -33.407 6.067   -2.161  0.010 42.98 ? 37   ASN B N   1 
ATOM   265  C CA  . ASN A 1 37  ? -32.890 5.489   -3.400  0.010 41.50 ? 37   ASN B CA  1 
ATOM   266  C C   . ASN A 1 37  ? -31.982 4.282   -3.176  0.010 38.39 ? 37   ASN B C   1 
ATOM   267  O O   . ASN A 1 37  ? -31.083 4.012   -3.974  0.010 36.97 ? 37   ASN B O   1 
ATOM   268  C CB  . ASN A 1 37  ? -32.175 6.553   -4.238  0.010 41.74 ? 37   ASN B CB  1 
ATOM   269  C CG  . ASN A 1 37  ? -30.772 6.844   -3.742  0.010 39.07 ? 37   ASN B CG  1 
ATOM   270  O OD1 . ASN A 1 37  ? -30.585 7.512   -2.725  0.010 39.13 ? 37   ASN B OD1 1 
ATOM   271  N ND2 . ASN A 1 37  ? -29.776 6.352   -4.470  0.010 37.19 ? 37   ASN B ND2 1 
ATOM   272  N N   . GLN A 1 38  ? -32.229 3.567   -2.081  0.10  38.10 ? 38   GLN B N   1 
ATOM   273  C CA  . GLN A 1 38  ? -31.571 2.292   -1.793  0.10  36.49 ? 38   GLN B CA  1 
ATOM   274  C C   . GLN A 1 38  ? -30.179 2.446   -1.178  0.10  34.82 ? 38   GLN B C   1 
ATOM   275  O O   . GLN A 1 38  ? -29.612 1.473   -0.683  0.10  33.48 ? 38   GLN B O   1 
ATOM   276  C CB  . GLN A 1 38  ? -31.494 1.405   -3.046  0.10  35.02 ? 38   GLN B CB  1 
ATOM   277  C CG  . GLN A 1 38  ? -32.723 1.450   -3.949  0.10  35.57 ? 38   GLN B CG  1 
ATOM   278  C CD  . GLN A 1 38  ? -34.018 1.635   -3.181  0.10  38.72 ? 38   GLN B CD  1 
ATOM   279  O OE1 . GLN A 1 38  ? -34.506 2.754   -3.034  0.10  39.27 ? 38   GLN B OE1 1 
ATOM   280  N NE2 . GLN A 1 38  ? -34.585 0.537   -2.696  0.10  37.86 ? 38   GLN B NE2 1 
ATOM   281  N N   . GLU A 1 39  ? -29.633 3.657   -1.206  0.40  30.87 ? 39   GLU B N   1 
ATOM   282  C CA  . GLU A 1 39  ? -28.303 3.875   -0.658  0.40  31.21 ? 39   GLU B CA  1 
ATOM   283  C C   . GLU A 1 39  ? -28.313 3.610   0.838   0.40  33.39 ? 39   GLU B C   1 
ATOM   284  O O   . GLU A 1 39  ? -29.265 3.970   1.530   0.40  31.53 ? 39   GLU B O   1 
ATOM   285  C CB  . GLU A 1 39  ? -27.815 5.297   -0.920  0.40  28.74 ? 39   GLU B CB  1 
ATOM   286  C CG  . GLU A 1 39  ? -27.726 5.656   -2.382  0.40  32.27 ? 39   GLU B CG  1 
ATOM   287  C CD  . GLU A 1 39  ? -26.832 6.847   -2.638  0.40  29.47 ? 39   GLU B CD  1 
ATOM   288  O OE1 . GLU A 1 39  ? -26.494 7.562   -1.670  0.40  26.97 ? 39   GLU B OE1 1 
ATOM   289  O OE2 . GLU A 1 39  ? -26.459 7.059   -3.814  0.40  34.87 ? 39   GLU B OE2 1 
ATOM   290  N N   . THR A 1 40  ? -27.256 2.974   1.334   1.00  33.55 ? 40   THR B N   1 
ATOM   291  C CA  . THR A 1 40  ? -27.129 2.727   2.771   1.00  36.08 ? 40   THR B CA  1 
ATOM   292  C C   . THR A 1 40  ? -26.616 3.948   3.506   1.00  37.60 ? 40   THR B C   1 
ATOM   293  O O   . THR A 1 40  ? -25.595 4.526   3.126   1.00  32.72 ? 40   THR B O   1 
ATOM   294  C CB  . THR A 1 40  ? -26.163 1.573   3.088   1.00  38.15 ? 40   THR B CB  1 
ATOM   295  O OG1 . THR A 1 40  ? -26.562 0.401   2.374   1.00  41.04 ? 40   THR B OG1 1 
ATOM   296  C CG2 . THR A 1 40  ? -26.177 1.275   4.598   1.00  39.14 ? 40   THR B CG2 1 
ATOM   297  N N   . CYS A 1 41  ? -27.326 4.315   4.570   1.00  39.19 ? 41   CYS B N   1 
ATOM   298  C CA  . CYS A 1 41  ? -26.908 5.363   5.491   1.00  41.35 ? 41   CYS B CA  1 
ATOM   299  C C   . CYS A 1 41  ? -26.345 4.751   6.771   1.00  44.67 ? 41   CYS B C   1 
ATOM   300  O O   . CYS A 1 41  ? -26.959 3.860   7.360   1.00  50.41 ? 41   CYS B O   1 
ATOM   301  C CB  . CYS A 1 41  ? -28.104 6.214   5.907   1.00  48.25 ? 41   CYS B CB  1 
ATOM   302  S SG  . CYS A 1 41  ? -28.264 6.333   7.723   1.00  65.42 ? 41   CYS B SG  1 
ATOM   303  N N   . VAL A 1 42  ? -25.195 5.246   7.212   1.00  40.20 ? 42   VAL B N   1 
ATOM   304  C CA  . VAL A 1 42  ? -24.612 4.805   8.476   1.00  44.47 ? 42   VAL B CA  1 
ATOM   305  C C   . VAL A 1 42  ? -24.071 5.989   9.259   1.00  40.87 ? 42   VAL B C   1 
ATOM   306  O O   . VAL A 1 42  ? -23.509 6.920   8.680   1.00  41.52 ? 42   VAL B O   1 
ATOM   307  C CB  . VAL A 1 42  ? -23.473 3.791   8.258   1.00  42.40 ? 42   VAL B CB  1 
ATOM   308  C CG1 . VAL A 1 42  ? -22.660 3.607   9.532   1.00  36.46 ? 42   VAL B CG1 1 
ATOM   309  C CG2 . VAL A 1 42  ? -24.042 2.462   7.800   1.00  43.68 ? 42   VAL B CG2 1 
ATOM   310  N N   . GLU A 1 43  ? -24.248 5.962   10.573  0.40  36.71 ? 43   GLU B N   1 
ATOM   311  C CA  . GLU A 1 43  ? -23.678 6.997   11.421  0.40  35.36 ? 43   GLU B CA  1 
ATOM   312  C C   . GLU A 1 43  ? -23.324 6.436   12.792  0.40  34.85 ? 43   GLU B C   1 
ATOM   313  O O   . GLU A 1 43  ? -24.195 6.046   13.560  0.40  28.46 ? 43   GLU B O   1 
ATOM   314  C CB  . GLU A 1 43  ? -24.629 8.185   11.552  0.40  37.97 ? 43   GLU B CB  1 
ATOM   315  C CG  . GLU A 1 43  ? -24.000 9.391   12.227  0.40  37.88 ? 43   GLU B CG  1 
ATOM   316  C CD  . GLU A 1 43  ? -25.002 10.495  12.507  0.40  43.14 ? 43   GLU B CD  1 
ATOM   317  O OE1 . GLU A 1 43  ? -24.865 11.167  13.551  0.40  45.95 ? 43   GLU B OE1 1 
ATOM   318  O OE2 . GLU A 1 43  ? -25.924 10.692  11.687  0.40  44.75 ? 43   GLU B OE2 1 
ATOM   319  N N   . ILE A 1 44  ? -22.029 6.393   13.079  1.00  40.73 ? 44   ILE B N   1 
ATOM   320  C CA  . ILE A 1 44  ? -21.524 5.863   14.346  1.00  36.96 ? 44   ILE B CA  1 
ATOM   321  C C   . ILE A 1 44  ? -21.910 6.832   15.452  1.00  34.39 ? 44   ILE B C   1 
ATOM   322  O O   . ILE A 1 44  ? -21.526 7.997   15.421  1.00  40.76 ? 44   ILE B O   1 
ATOM   323  C CB  . ILE A 1 44  ? -19.998 5.684   14.297  1.00  34.42 ? 44   ILE B CB  1 
ATOM   324  C CG1 . ILE A 1 44  ? -19.604 4.797   13.110  1.00  32.95 ? 44   ILE B CG1 1 
ATOM   325  C CG2 . ILE A 1 44  ? -19.486 5.062   15.583  1.00  33.22 ? 44   ILE B CG2 1 
ATOM   326  C CD1 . ILE A 1 44  ? -20.100 3.354   13.232  1.00  41.91 ? 44   ILE B CD1 1 
ATOM   327  N N   . GLY A 1 45  ? -22.683 6.362   16.421  1.00  31.69 ? 45   GLY B N   1 
ATOM   328  C CA  . GLY A 1 45  ? -23.295 7.258   17.387  1.00  29.25 ? 45   GLY B CA  1 
ATOM   329  C C   . GLY A 1 45  ? -22.464 7.531   18.626  1.00  33.76 ? 45   GLY B C   1 
ATOM   330  O O   . GLY A 1 45  ? -22.962 8.068   19.606  1.00  33.12 ? 45   GLY B O   1 
ATOM   331  N N   . GLU A 1 46  ? -21.197 7.150   18.591  1.00  32.74 ? 46   GLU B N   1 
ATOM   332  C CA  . GLU A 1 46  ? -20.316 7.391   19.716  1.00  34.12 ? 46   GLU B CA  1 
ATOM   333  C C   . GLU A 1 46  ? -18.884 7.383   19.214  1.00  32.70 ? 46   GLU B C   1 
ATOM   334  O O   . GLU A 1 46  ? -18.605 6.790   18.185  1.00  27.20 ? 46   GLU B O   1 
ATOM   335  C CB  . GLU A 1 46  ? -20.510 6.307   20.774  1.00  35.36 ? 46   GLU B CB  1 
ATOM   336  C CG  . GLU A 1 46  ? -20.329 4.871   20.261  1.00  32.53 ? 46   GLU B CG  1 
ATOM   337  C CD  . GLU A 1 46  ? -20.617 3.834   21.349  1.00  37.49 ? 46   GLU B CD  1 
ATOM   338  O OE1 . GLU A 1 46  ? -19.680 3.484   22.096  1.00  43.53 ? 46   GLU B OE1 1 
ATOM   339  O OE2 . GLU A 1 46  ? -21.778 3.384   21.479  1.00  35.79 ? 46   GLU B OE2 1 
ATOM   340  N N   . SER A 1 47  ? -17.973 8.035   19.931  1.00  31.41 ? 47   SER B N   1 
ATOM   341  C CA  . SER A 1 47  ? -16.572 8.023   19.518  1.00  34.67 ? 47   SER B CA  1 
ATOM   342  C C   . SER A 1 47  ? -16.014 6.602   19.548  1.00  29.73 ? 47   SER B C   1 
ATOM   343  O O   . SER A 1 47  ? -16.314 5.829   20.462  1.00  28.47 ? 47   SER B O   1 
ATOM   344  C CB  . SER A 1 47  ? -15.732 8.943   20.410  1.00  30.64 ? 47   SER B CB  1 
ATOM   345  O OG  . SER A 1 47  ? -14.347 8.711   20.215  1.00  27.38 ? 47   SER B OG  1 
ATOM   346  N N   . VAL A 1 48  ? -15.200 6.258   18.549  1.00  23.68 ? 48   VAL B N   1 
ATOM   347  C CA  . VAL A 1 48  ? -14.451 5.005   18.574  1.00  23.89 ? 48   VAL B CA  1 
ATOM   348  C C   . VAL A 1 48  ? -12.956 5.287   18.579  1.00  25.15 ? 48   VAL B C   1 
ATOM   349  O O   . VAL A 1 48  ? -12.148 4.387   18.388  1.00  22.54 ? 48   VAL B O   1 
ATOM   350  C CB  . VAL A 1 48  ? -14.774 4.116   17.346  1.00  21.93 ? 48   VAL B CB  1 
ATOM   351  C CG1 . VAL A 1 48  ? -16.216 3.597   17.431  1.00  23.24 ? 48   VAL B CG1 1 
ATOM   352  C CG2 . VAL A 1 48  ? -14.523 4.888   16.041  1.00  20.68 ? 48   VAL B CG2 1 
ATOM   353  N N   . ARG A 1 49  ? -12.591 6.547   18.791  1.00  24.55 ? 49   ARG B N   1 
ATOM   354  C CA  . ARG A 1 49  ? -11.177 6.948   18.772  1.00  23.34 ? 49   ARG B CA  1 
ATOM   355  C C   . ARG A 1 49  ? -10.322 6.102   19.727  1.00  27.70 ? 49   ARG B C   1 
ATOM   356  O O   . ARG A 1 49  ? -10.665 5.911   20.899  1.00  24.91 ? 49   ARG B O   1 
ATOM   357  C CB  . ARG A 1 49  ? -11.045 8.445   19.085  1.00  26.29 ? 49   ARG B CB  1 
ATOM   358  C CG  . ARG A 1 49  ? -9.670  9.063   18.778  1.00  28.07 ? 49   ARG B CG  1 
ATOM   359  C CD  . ARG A 1 49  ? -9.699  10.584  18.945  1.00  27.62 ? 49   ARG B CD  1 
ATOM   360  N NE  . ARG A 1 49  ? -10.669 11.218  18.050  1.00  26.14 ? 49   ARG B NE  1 
ATOM   361  C CZ  . ARG A 1 49  ? -10.355 11.797  16.890  1.00  25.57 ? 49   ARG B CZ  1 
ATOM   362  N NH1 . ARG A 1 49  ? -9.096  11.846  16.485  1.00  24.33 ? 49   ARG B NH1 1 
ATOM   363  N NH2 . ARG A 1 49  ? -11.294 12.340  16.134  1.00  25.30 ? 49   ARG B NH2 1 
ATOM   364  N N   . GLY A 1 50  ? -9.216  5.582   19.210  1.00  24.02 ? 50   GLY B N   1 
ATOM   365  C CA  . GLY A 1 50  ? -8.334  4.720   19.982  1.00  22.77 ? 50   GLY B CA  1 
ATOM   366  C C   . GLY A 1 50  ? -8.899  3.361   20.385  1.00  24.51 ? 50   GLY B C   1 
ATOM   367  O O   . GLY A 1 50  ? -8.233  2.636   21.120  1.00  28.66 ? 50   GLY B O   1 
ATOM   368  N N   . GLU A 1 51  ? -10.100 3.002   19.927  0.40  18.38 ? 51   GLU B N   1 
ATOM   369  C CA  . GLU A 1 51  ? -10.738 1.750   20.372  0.40  18.88 ? 51   GLU B CA  1 
ATOM   370  C C   . GLU A 1 51  ? -10.459 0.508   19.495  0.40  19.16 ? 51   GLU B C   1 
ATOM   371  O O   . GLU A 1 51  ? -10.159 0.629   18.311  0.40  13.30 ? 51   GLU B O   1 
ATOM   372  C CB  . GLU A 1 51  ? -12.252 1.938   20.514  0.40  19.43 ? 51   GLU B CB  1 
ATOM   373  C CG  . GLU A 1 51  ? -12.693 3.113   21.399  0.40  20.69 ? 51   GLU B CG  1 
ATOM   374  C CD  . GLU A 1 51  ? -12.548 2.842   22.882  0.40  31.93 ? 51   GLU B CD  1 
ATOM   375  O OE1 . GLU A 1 51  ? -11.420 2.560   23.332  0.40  28.72 ? 51   GLU B OE1 1 
ATOM   376  O OE2 . GLU A 1 51  ? -13.565 2.915   23.609  0.40  37.49 ? 51   GLU B OE2 1 
ATOM   377  N N   . ASP A 1 52  ? -10.569 -0.677  20.102  1.00  21.55 ? 52   ASP B N   1 
ATOM   378  C CA  . ASP A 1 52  ? -10.472 -1.962  19.393  1.00  22.48 ? 52   ASP B CA  1 
ATOM   379  C C   . ASP A 1 52  ? -11.880 -2.333  18.902  1.00  24.83 ? 52   ASP B C   1 
ATOM   380  O O   . ASP A 1 52  ? -12.712 -2.876  19.655  1.00  19.45 ? 52   ASP B O   1 
ATOM   381  C CB  . ASP A 1 52  ? -9.881  -3.049  20.310  1.00  19.61 ? 52   ASP B CB  1 
ATOM   382  C CG  . ASP A 1 52  ? -9.369  -4.268  19.552  1.00  24.20 ? 52   ASP B CG  1 
ATOM   383  O OD1 . ASP A 1 52  ? -9.152  -4.200  18.308  1.00  22.43 ? 52   ASP B OD1 1 
ATOM   384  O OD2 . ASP A 1 52  ? -9.163  -5.311  20.214  1.00  26.82 ? 52   ASP B OD2 1 
ATOM   385  N N   . VAL A 1 53  ? -12.160 -2.007  17.638  1.00  18.86 ? 53   VAL B N   1 
ATOM   386  C CA  . VAL A 1 53  ? -13.541 -2.108  17.110  1.00  16.75 ? 53   VAL B CA  1 
ATOM   387  C C   . VAL A 1 53  ? -13.829 -3.443  16.400  1.00  22.93 ? 53   VAL B C   1 
ATOM   388  O O   . VAL A 1 53  ? -13.047 -3.890  15.541  1.00  22.46 ? 53   VAL B O   1 
ATOM   389  C CB  . VAL A 1 53  ? -13.848 -0.916  16.157  1.00  19.07 ? 53   VAL B CB  1 
ATOM   390  C CG1 . VAL A 1 53  ? -15.242 -1.088  15.454  1.00  21.11 ? 53   VAL B CG1 1 
ATOM   391  C CG2 . VAL A 1 53  ? -13.760 0.409   16.921  1.00  18.77 ? 53   VAL B CG2 1 
ATOM   392  N N   . TYR A 1 54  ? -14.968 -4.053  16.725  1.00  16.44 ? 54   TYR B N   1 
ATOM   393  C CA  . TYR A 1 54  ? -15.401 -5.289  16.078  1.00  16.10 ? 54   TYR B CA  1 
ATOM   394  C C   . TYR A 1 54  ? -16.769 -5.067  15.467  1.00  19.48 ? 54   TYR B C   1 
ATOM   395  O O   . TYR A 1 54  ? -17.696 -4.651  16.158  1.00  22.36 ? 54   TYR B O   1 
ATOM   396  C CB  . TYR A 1 54  ? -15.454 -6.449  17.102  1.00  18.44 ? 54   TYR B CB  1 
ATOM   397  C CG  . TYR A 1 54  ? -14.079 -6.771  17.616  1.00  19.42 ? 54   TYR B CG  1 
ATOM   398  C CD1 . TYR A 1 54  ? -13.491 -5.978  18.595  1.00  20.93 ? 54   TYR B CD1 1 
ATOM   399  C CD2 . TYR A 1 54  ? -13.345 -7.823  17.092  1.00  17.36 ? 54   TYR B CD2 1 
ATOM   400  C CE1 . TYR A 1 54  ? -12.220 -6.238  19.068  1.00  19.88 ? 54   TYR B CE1 1 
ATOM   401  C CE2 . TYR A 1 54  ? -12.066 -8.091  17.555  1.00  20.28 ? 54   TYR B CE2 1 
ATOM   402  C CZ  . TYR A 1 54  ? -11.514 -7.296  18.549  1.00  21.94 ? 54   TYR B CZ  1 
ATOM   403  O OH  . TYR A 1 54  ? -10.245 -7.537  19.008  1.00  21.26 ? 54   TYR B OH  1 
ATOM   404  N N   . ILE A 1 55  ? -16.904 -5.333  14.169  1.00  19.83 ? 55   ILE B N   1 
ATOM   405  C CA  . ILE A 1 55  ? -18.189 -5.140  13.502  1.00  18.56 ? 55   ILE B CA  1 
ATOM   406  C C   . ILE A 1 55  ? -18.693 -6.491  13.037  1.00  19.56 ? 55   ILE B C   1 
ATOM   407  O O   . ILE A 1 55  ? -18.043 -7.164  12.249  1.00  19.58 ? 55   ILE B O   1 
ATOM   408  C CB  . ILE A 1 55  ? -18.090 -4.179  12.290  1.00  19.17 ? 55   ILE B CB  1 
ATOM   409  C CG1 . ILE A 1 55  ? -17.663 -2.787  12.766  1.00  23.49 ? 55   ILE B CG1 1 
ATOM   410  C CG2 . ILE A 1 55  ? -19.474 -4.101  11.552  1.00  18.19 ? 55   ILE B CG2 1 
ATOM   411  C CD1 . ILE A 1 55  ? -16.824 -2.023  11.784  1.00  18.46 ? 55   ILE B CD1 1 
ATOM   412  N N   . VAL A 1 56  ? -19.863 -6.880  13.523  1.00  17.57 ? 56   VAL B N   1 
ATOM   413  C CA  . VAL A 1 56  ? -20.407 -8.195  13.221  1.00  20.67 ? 56   VAL B CA  1 
ATOM   414  C C   . VAL A 1 56  ? -21.388 -8.092  12.050  1.00  21.56 ? 56   VAL B C   1 
ATOM   415  O O   . VAL A 1 56  ? -22.335 -7.298  12.118  1.00  26.17 ? 56   VAL B O   1 
ATOM   416  C CB  . VAL A 1 56  ? -21.149 -8.791  14.434  1.00  21.98 ? 56   VAL B CB  1 
ATOM   417  C CG1 . VAL A 1 56  ? -21.644 -10.197 14.106  1.00  21.52 ? 56   VAL B CG1 1 
ATOM   418  C CG2 . VAL A 1 56  ? -20.236 -8.835  15.632  1.00  18.31 ? 56   VAL B CG2 1 
ATOM   419  N N   . GLN A 1 57  ? -21.155 -8.894  11.011  0.20  19.45 ? 57   GLN B N   1 
ATOM   420  C CA  . GLN A 1 57  ? -21.959 -8.874  9.793   0.20  25.25 ? 57   GLN B CA  1 
ATOM   421  C C   . GLN A 1 57  ? -23.409 -9.281  10.052  0.20  30.30 ? 57   GLN B C   1 
ATOM   422  O O   . GLN A 1 57  ? -23.677 -10.279 10.722  0.20  30.42 ? 57   GLN B O   1 
ATOM   423  C CB  . GLN A 1 57  ? -21.341 -9.787  8.724   0.20  24.75 ? 57   GLN B CB  1 
ATOM   424  C CG  . GLN A 1 57  ? -22.207 -10.983 8.354   0.20  27.46 ? 57   GLN B CG  1 
ATOM   425  C CD  . GLN A 1 57  ? -22.612 -10.991 6.890   0.20  29.07 ? 57   GLN B CD  1 
ATOM   426  O OE1 . GLN A 1 57  ? -23.737 -11.360 6.545   0.20  26.57 ? 57   GLN B OE1 1 
ATOM   427  N NE2 . GLN A 1 57  ? -21.692 -10.590 6.021   0.20  25.53 ? 57   GLN B NE2 1 
ATOM   428  N N   . SER A 1 58  ? -24.344 -8.496  9.519   1.00  40.62 ? 58   SER B N   1 
ATOM   429  C CA  . SER A 1 58  ? -25.768 -8.799  9.647   1.00  42.33 ? 58   SER B CA  1 
ATOM   430  C C   . SER A 1 58  ? -26.255 -9.907  8.724   1.00  42.26 ? 58   SER B C   1 
ATOM   431  O O   . SER A 1 58  ? -25.757 -10.064 7.614   1.00  48.26 ? 58   SER B O   1 
ATOM   432  C CB  . SER A 1 58  ? -26.606 -7.548  9.403   1.00  45.15 ? 58   SER B CB  1 
ATOM   433  O OG  . SER A 1 58  ? -27.925 -7.920  9.053   1.00  46.56 ? 58   SER B OG  1 
ATOM   434  N N   . GLY A 1 59  ? -27.252 -10.658 9.183   0.010 41.92 ? 59   GLY B N   1 
ATOM   435  C CA  . GLY A 1 59  ? -27.816 -11.749 8.410   0.010 43.00 ? 59   GLY B CA  1 
ATOM   436  C C   . GLY A 1 59  ? -29.179 -11.421 7.828   0.010 44.13 ? 59   GLY B C   1 
ATOM   437  O O   . GLY A 1 59  ? -30.050 -12.286 7.746   0.010 43.94 ? 59   GLY B O   1 
ATOM   438  N N   . CYS A 1 60  ? -29.358 -10.166 7.427   0.10  44.26 ? 60   CYS B N   1 
ATOM   439  C CA  . CYS A 1 60  ? -30.603 -9.711  6.815   0.10  42.98 ? 60   CYS B CA  1 
ATOM   440  C C   . CYS A 1 60  ? -31.089 -10.645 5.711   0.10  43.54 ? 60   CYS B C   1 
ATOM   441  O O   . CYS A 1 60  ? -32.254 -11.050 5.690   0.10  42.99 ? 60   CYS B O   1 
ATOM   442  C CB  . CYS A 1 60  ? -30.434 -8.297  6.262   0.10  40.14 ? 60   CYS B CB  1 
ATOM   443  S SG  . CYS A 1 60  ? -31.512 -7.903  4.864   0.10  44.22 ? 60   CYS B SG  1 
ATOM   444  N N   . GLY A 1 61  ? -30.189 -10.979 4.794   1.00  48.34 ? 61   GLY B N   1 
ATOM   445  C CA  . GLY A 1 61  ? -30.522 -11.821 3.659   1.00  43.76 ? 61   GLY B CA  1 
ATOM   446  C C   . GLY A 1 61  ? -30.069 -11.224 2.342   1.00  39.49 ? 61   GLY B C   1 
ATOM   447  O O   . GLY A 1 61  ? -29.530 -11.940 1.489   1.00  39.87 ? 61   GLY B O   1 
ATOM   448  N N   . GLU A 1 62  ? -30.289 -9.921  2.173   0.50  32.04 ? 62   GLU B N   1 
ATOM   449  C CA  . GLU A 1 62  ? -29.834 -9.222  0.979   0.50  27.87 ? 62   GLU B CA  1 
ATOM   450  C C   . GLU A 1 62  ? -28.334 -9.023  1.059   0.50  24.91 ? 62   GLU B C   1 
ATOM   451  O O   . GLU A 1 62  ? -27.853 -8.066  1.648   0.50  19.50 ? 62   GLU B O   1 
ATOM   452  C CB  . GLU A 1 62  ? -30.530 -7.871  0.826   0.50  28.68 ? 62   GLU B CB  1 
ATOM   453  C CG  . GLU A 1 62  ? -31.004 -7.568  -0.589  0.50  28.24 ? 62   GLU B CG  1 
ATOM   454  C CD  . GLU A 1 62  ? -29.885 -7.234  -1.575  0.50  29.23 ? 62   GLU B CD  1 
ATOM   455  O OE1 . GLU A 1 62  ? -28.705 -7.138  -1.174  0.50  23.31 ? 62   GLU B OE1 1 
ATOM   456  O OE2 . GLU A 1 62  ? -30.202 -7.058  -2.770  0.50  28.61 ? 62   GLU B OE2 1 
ATOM   457  N N   . ILE A 1 63  ? -27.596 -9.943  0.454   1.00  26.89 ? 63   ILE B N   1 
ATOM   458  C CA  . ILE A 1 63  ? -26.153 -9.969  0.596   1.00  24.08 ? 63   ILE B CA  1 
ATOM   459  C C   . ILE A 1 63  ? -25.454 -8.670  0.137   1.00  27.09 ? 63   ILE B C   1 
ATOM   460  O O   . ILE A 1 63  ? -24.552 -8.176  0.807   1.00  23.39 ? 63   ILE B O   1 
ATOM   461  C CB  . ILE A 1 63  ? -25.568 -11.197 -0.098  1.00  28.52 ? 63   ILE B CB  1 
ATOM   462  C CG1 . ILE A 1 63  ? -24.087 -11.323 0.214   1.00  30.91 ? 63   ILE B CG1 1 
ATOM   463  C CG2 . ILE A 1 63  ? -25.770 -11.121 -1.609  1.00  33.66 ? 63   ILE B CG2 1 
ATOM   464  C CD1 . ILE A 1 63  ? -23.392 -12.304 -0.695  1.00  38.31 ? 63   ILE B CD1 1 
ATOM   465  N N   . ASN A 1 64  ? -25.879 -8.086  -0.979  1.00  23.80 ? 64   ASN B N   1 
ATOM   466  C CA  . ASN A 1 64  ? -25.198 -6.879  -1.432  1.00  24.46 ? 64   ASN B CA  1 
ATOM   467  C C   . ASN A 1 64  ? -25.413 -5.708  -0.471  1.00  23.42 ? 64   ASN B C   1 
ATOM   468  O O   . ASN A 1 64  ? -24.482 -4.926  -0.222  1.00  22.11 ? 64   ASN B O   1 
ATOM   469  C CB  . ASN A 1 64  ? -25.554 -6.525  -2.886  1.00  21.23 ? 64   ASN B CB  1 
ATOM   470  C CG  . ASN A 1 64  ? -25.097 -7.589  -3.873  1.00  21.33 ? 64   ASN B CG  1 
ATOM   471  O OD1 . ASN A 1 64  ? -25.785 -7.875  -4.848  1.00  30.20 ? 64   ASN B OD1 1 
ATOM   472  N ND2 . ASN A 1 64  ? -23.956 -8.216  -3.595  1.00  21.33 ? 64   ASN B ND2 1 
ATOM   473  N N   . ASP A 1 65  ? -26.623 -5.584  0.071   1.00  21.84 ? 65   ASP B N   1 
ATOM   474  C CA  . ASP A 1 65  ? -26.911 -4.526  1.042   1.00  25.55 ? 65   ASP B CA  1 
ATOM   475  C C   . ASP A 1 65  ? -26.097 -4.750  2.314   1.00  22.34 ? 65   ASP B C   1 
ATOM   476  O O   . ASP A 1 65  ? -25.583 -3.807  2.899   1.00  21.62 ? 65   ASP B O   1 
ATOM   477  C CB  . ASP A 1 65  ? -28.394 -4.480  1.453   1.00  26.37 ? 65   ASP B CB  1 
ATOM   478  C CG  . ASP A 1 65  ? -29.326 -4.132  0.304   1.00  29.58 ? 65   ASP B CG  1 
ATOM   479  O OD1 . ASP A 1 65  ? -28.882 -3.487  -0.671  1.00  24.70 ? 65   ASP B OD1 1 
ATOM   480  O OD2 . ASP A 1 65  ? -30.519 -4.503  0.393   1.00  29.73 ? 65   ASP B OD2 1 
ATOM   481  N N   . ASN A 1 66  ? -26.053 -5.991  2.773   1.00  23.40 ? 66   ASN B N   1 
ATOM   482  C CA  . ASN A 1 66  ? -25.312 -6.319  3.989   1.00  23.98 ? 66   ASN B CA  1 
ATOM   483  C C   . ASN A 1 66  ? -23.806 -6.098  3.823   1.00  22.23 ? 66   ASN B C   1 
ATOM   484  O O   . ASN A 1 66  ? -23.122 -5.606  4.719   1.00  21.23 ? 66   ASN B O   1 
ATOM   485  C CB  . ASN A 1 66  ? -25.610 -7.764  4.382   1.00  25.38 ? 66   ASN B CB  1 
ATOM   486  C CG  . ASN A 1 66  ? -26.990 -7.927  5.006   1.00  32.89 ? 66   ASN B CG  1 
ATOM   487  O OD1 . ASN A 1 66  ? -27.530 -6.995  5.599   1.00  34.17 ? 66   ASN B OD1 1 
ATOM   488  N ND2 . ASN A 1 66  ? -27.560 -9.115  4.877   1.00  37.79 ? 66   ASN B ND2 1 
ATOM   489  N N   . LEU A 1 67  ? -23.283 -6.457  2.663   1.00  20.60 ? 67   LEU B N   1 
ATOM   490  C CA  . LEU A 1 67  ? -21.865 -6.227  2.402   1.00  18.38 ? 67   LEU B CA  1 
ATOM   491  C C   . LEU A 1 67  ? -21.505 -4.735  2.364   1.00  19.31 ? 67   LEU B C   1 
ATOM   492  O O   . LEU A 1 67  ? -20.524 -4.317  3.003   1.00  16.88 ? 67   LEU B O   1 
ATOM   493  C CB  . LEU A 1 67  ? -21.432 -6.930  1.113   1.00  17.85 ? 67   LEU B CB  1 
ATOM   494  C CG  . LEU A 1 67  ? -20.024 -6.573  0.633   1.00  20.06 ? 67   LEU B CG  1 
ATOM   495  C CD1 . LEU A 1 67  ? -18.953 -7.197  1.556   1.00  18.35 ? 67   LEU B CD1 1 
ATOM   496  C CD2 . LEU A 1 67  ? -19.841 -7.002  -0.830  1.00  26.56 ? 67   LEU B CD2 1 
ATOM   497  N N   . MET A 1 68  ? -22.276 -3.937  1.634   0.10  16.67 ? 68   MET B N   1 
ATOM   498  C CA  . MET A 1 68  ? -21.995 -2.510  1.544   0.10  16.39 ? 68   MET B CA  1 
ATOM   499  C C   . MET A 1 68  ? -22.098 -1.840  2.911   0.10  16.24 ? 68   MET B C   1 
ATOM   500  O O   . MET A 1 68  ? -21.281 -1.001  3.262   0.10  13.81 ? 68   MET B O   1 
ATOM   501  C CB  . MET A 1 68  ? -22.923 -1.824  0.545   0.10  16.23 ? 68   MET B CB  1 
ATOM   502  C CG  . MET A 1 68  ? -22.637 -2.171  -0.904  0.10  16.16 ? 68   MET B CG  1 
ATOM   503  S SD  . MET A 1 68  ? -20.942 -1.786  -1.378  0.10  8.32  ? 68   MET B SD  1 
ATOM   504  C CE  . MET A 1 68  ? -20.790 -0.118  -0.744  0.10  14.55 ? 68   MET B CE  1 
ATOM   505  N N   . GLU A 1 69  ? -23.108 -2.228  3.678   1.00  19.01 ? 69   GLU B N   1 
ATOM   506  C CA  . GLU A 1 69  ? -23.305 -1.711  5.041   1.00  21.17 ? 69   GLU B CA  1 
ATOM   507  C C   . GLU A 1 69  ? -22.068 -1.966  5.896   1.00  18.96 ? 69   GLU B C   1 
ATOM   508  O O   . GLU A 1 69  ? -21.592 -1.082  6.596   1.00  21.65 ? 69   GLU B O   1 
ATOM   509  C CB  . GLU A 1 69  ? -24.538 -2.357  5.692   1.00  21.67 ? 69   GLU B CB  1 
ATOM   510  C CG  . GLU A 1 69  ? -24.814 -1.875  7.120   1.00  29.23 ? 69   GLU B CG  1 
ATOM   511  C CD  . GLU A 1 69  ? -26.098 -2.473  7.688   1.00  41.31 ? 69   GLU B CD  1 
ATOM   512  O OE1 . GLU A 1 69  ? -26.140 -3.701  7.925   1.00  37.24 ? 69   GLU B OE1 1 
ATOM   513  O OE2 . GLU A 1 69  ? -27.074 -1.720  7.872   1.00  45.37 ? 69   GLU B OE2 1 
ATOM   514  N N   . LEU A 1 70  ? -21.541 -3.175  5.802   1.00  17.47 ? 70   LEU B N   1 
ATOM   515  C CA  . LEU A 1 70  ? -20.337 -3.570  6.520   1.00  19.60 ? 70   LEU B CA  1 
ATOM   516  C C   . LEU A 1 70  ? -19.120 -2.747  6.091   1.00  21.57 ? 70   LEU B C   1 
ATOM   517  O O   . LEU A 1 70  ? -18.356 -2.260  6.937   1.00  16.55 ? 70   LEU B O   1 
ATOM   518  C CB  . LEU A 1 70  ? -20.068 -5.048  6.286   1.00  14.56 ? 70   LEU B CB  1 
ATOM   519  C CG  . LEU A 1 70  ? -18.719 -5.538  6.816   1.00  20.65 ? 70   LEU B CG  1 
ATOM   520  C CD1 . LEU A 1 70  ? -18.560 -5.352  8.343   1.00  17.64 ? 70   LEU B CD1 1 
ATOM   521  C CD2 . LEU A 1 70  ? -18.569 -6.986  6.434   1.00  20.19 ? 70   LEU B CD2 1 
ATOM   522  N N   . LEU A 1 71  ? -18.954 -2.588  4.780   1.00  18.47 ? 71   LEU B N   1 
ATOM   523  C CA  . LEU A 1 71  ? -17.840 -1.827  4.240   1.00  18.52 ? 71   LEU B CA  1 
ATOM   524  C C   . LEU A 1 71  ? -17.903 -0.388  4.686   1.00  17.00 ? 71   LEU B C   1 
ATOM   525  O O   . LEU A 1 71  ? -16.879 0.220   5.004   1.00  18.36 ? 71   LEU B O   1 
ATOM   526  C CB  . LEU A 1 71  ? -17.824 -1.895  2.709   1.00  16.16 ? 71   LEU B CB  1 
ATOM   527  C CG  . LEU A 1 71  ? -17.478 -3.298  2.215   1.00  19.08 ? 71   LEU B CG  1 
ATOM   528  C CD1 . LEU A 1 71  ? -17.718 -3.450  0.733   1.00  21.79 ? 71   LEU B CD1 1 
ATOM   529  C CD2 . LEU A 1 71  ? -16.038 -3.649  2.561   1.00  17.98 ? 71   LEU B CD2 1 
ATOM   530  N N   . ILE A 1 72  ? -19.108 0.158   4.684   1.00  19.24 ? 72   ILE B N   1 
ATOM   531  C CA  . ILE A 1 72  ? -19.321 1.557   5.049   1.00  19.11 ? 72   ILE B CA  1 
ATOM   532  C C   . ILE A 1 72  ? -19.046 1.760   6.548   1.00  18.30 ? 72   ILE B C   1 
ATOM   533  O O   . ILE A 1 72  ? -18.424 2.747   6.939   1.00  19.54 ? 72   ILE B O   1 
ATOM   534  C CB  . ILE A 1 72  ? -20.748 2.017   4.666   1.00  19.43 ? 72   ILE B CB  1 
ATOM   535  C CG1 . ILE A 1 72  ? -20.901 2.128   3.147   1.00  21.04 ? 72   ILE B CG1 1 
ATOM   536  C CG2 . ILE A 1 72  ? -21.097 3.345   5.289   1.00  19.46 ? 72   ILE B CG2 1 
ATOM   537  C CD1 . ILE A 1 72  ? -22.362 2.150   2.716   1.00  22.73 ? 72   ILE B CD1 1 
ATOM   538  N N   . MET A 1 73  ? -19.462 0.825   7.370   0.97  18.30 ? 73   MET B N   1 
ATOM   539  C CA  . MET A 1 73  ? -19.179 0.857   8.796   0.97  19.80 ? 73   MET B CA  1 
ATOM   540  C C   . MET A 1 73  ? -17.685 0.748   9.092   0.97  17.38 ? 73   MET B C   1 
ATOM   541  O O   . MET A 1 73  ? -17.185 1.429   9.926   0.97  18.14 ? 73   MET B O   1 
ATOM   542  C CB  . MET A 1 73  ? -19.931 -0.213  9.547   0.97  17.54 ? 73   MET B CB  1 
ATOM   543  C CG  . MET A 1 73  ? -21.357 0.041   9.697   0.97  26.33 ? 73   MET B CG  1 
ATOM   544  S SD  . MET A 1 73  ? -22.185 -1.333  10.419  0.97  36.01 ? 73   MET B SD  1 
ATOM   545  C CE  . MET A 1 73  ? -21.760 -1.048  12.067  0.97  37.61 ? 73   MET B CE  1 
ATOM   546  N N   . ILE A 1 74  ? -17.009 -0.129  8.385   1.00  18.90 ? 74   ILE B N   1 
ATOM   547  C CA  . ILE A 1 74  ? -15.555 -0.227  8.513   1.00  16.96 ? 74   ILE B CA  1 
ATOM   548  C C   . ILE A 1 74  ? -14.885 1.112   8.194   1.00  21.62 ? 74   ILE B C   1 
ATOM   549  O O   . ILE A 1 74  ? -14.019 1.571   8.939   1.00  19.78 ? 74   ILE B O   1 
ATOM   550  C CB  . ILE A 1 74  ? -14.996 -1.363  7.601   1.00  18.45 ? 74   ILE B CB  1 
ATOM   551  C CG1 . ILE A 1 74  ? -15.430 -2.732  8.135   1.00  20.76 ? 74   ILE B CG1 1 
ATOM   552  C CG2 . ILE A 1 74  ? -13.468 -1.287  7.506   1.00  20.48 ? 74   ILE B CG2 1 
ATOM   553  C CD1 . ILE A 1 74  ? -15.223 -3.913  7.156   1.00  19.99 ? 74   ILE B CD1 1 
ATOM   554  N N   . ASN A 1 75  ? -15.303 1.732   7.086   1.00  18.82 ? 75   ASN B N   1 
ATOM   555  C CA  . ASN A 1 75  ? -14.776 3.023   6.630   1.00  24.00 ? 75   ASN B CA  1 
ATOM   556  C C   . ASN A 1 75  ? -14.969 4.110   7.671   1.00  23.31 ? 75   ASN B C   1 
ATOM   557  O O   . ASN A 1 75  ? -14.033 4.831   8.009   1.00  19.81 ? 75   ASN B O   1 
ATOM   558  C CB  . ASN A 1 75  ? -15.450 3.446   5.315   1.00  23.57 ? 75   ASN B CB  1 
ATOM   559  C CG  . ASN A 1 75  ? -15.046 4.851   4.863   1.00  29.98 ? 75   ASN B CG  1 
ATOM   560  O OD1 . ASN A 1 75  ? -13.885 5.096   4.535   1.00  31.00 ? 75   ASN B OD1 1 
ATOM   561  N ND2 . ASN A 1 75  ? -16.008 5.772   4.832   1.00  25.43 ? 75   ASN B ND2 1 
ATOM   562  N N   . ALA A 1 76  ? -16.192 4.201   8.192   1.00  22.06 ? 76   ALA B N   1 
ATOM   563  C CA  . ALA A 1 76  ? -16.521 5.200   9.195   1.00  22.93 ? 76   ALA B CA  1 
ATOM   564  C C   . ALA A 1 76  ? -15.624 5.040   10.421  1.00  21.55 ? 76   ALA B C   1 
ATOM   565  O O   . ALA A 1 76  ? -15.083 6.010   10.932  1.00  25.59 ? 76   ALA B O   1 
ATOM   566  C CB  . ALA A 1 76  ? -18.000 5.112   9.576   1.00  24.11 ? 76   ALA B CB  1 
ATOM   567  N N   . CYS A 1 77  ? -15.436 3.815   10.890  1.00  19.28 ? 77   CYS B N   1 
ATOM   568  C CA  . CYS A 1 77  ? -14.650 3.632   12.104  1.00  20.23 ? 77   CYS B CA  1 
ATOM   569  C C   . CYS A 1 77  ? -13.182 3.968   11.861  1.00  22.49 ? 77   CYS B C   1 
ATOM   570  O O   . CYS A 1 77  ? -12.519 4.558   12.704  1.00  20.26 ? 77   CYS B O   1 
ATOM   571  C CB  . CYS A 1 77  ? -14.804 2.211   12.644  1.00  21.20 ? 77   CYS B CB  1 
ATOM   572  S SG  . CYS A 1 77  ? -16.460 1.877   13.284  1.00  24.85 ? 77   CYS B SG  1 
ATOM   573  N N   . LYS A 1 78  ? -12.676 3.596   10.693  1.00  20.88 ? 78   LYS B N   1 
ATOM   574  C CA  . LYS A 1 78  ? -11.280 3.850   10.369  1.00  20.91 ? 78   LYS B CA  1 
ATOM   575  C C   . LYS A 1 78  ? -10.999 5.345   10.288  1.00  25.22 ? 78   LYS B C   1 
ATOM   576  O O   . LYS A 1 78  ? -9.995  5.841   10.816  1.00  23.74 ? 78   LYS B O   1 
ATOM   577  C CB  . LYS A 1 78  ? -10.911 3.151   9.056   1.00  25.12 ? 78   LYS B CB  1 
ATOM   578  C CG  . LYS A 1 78  ? -10.306 1.746   9.234   1.00  29.40 ? 78   LYS B CG  1 
ATOM   579  C CD  . LYS A 1 78  ? -8.974  1.866   9.950   1.00  30.46 ? 78   LYS B CD  1 
ATOM   580  C CE  . LYS A 1 78  ? -8.110  0.620   9.856   1.00  34.35 ? 78   LYS B CE  1 
ATOM   581  N NZ  . LYS A 1 78  ? -7.367  0.432   11.152  1.00  36.06 ? 78   LYS B NZ  1 
ATOM   582  N N   . ILE A 1 79  ? -11.888 6.085   9.648   1.00  20.78 ? 79   ILE B N   1 
ATOM   583  C CA  . ILE A 1 79  ? -11.616 7.500   9.479   1.00  21.76 ? 79   ILE B CA  1 
ATOM   584  C C   . ILE A 1 79  ? -12.000 8.262   10.739  1.00  26.23 ? 79   ILE B C   1 
ATOM   585  O O   . ILE A 1 79  ? -11.667 9.438   10.874  1.00  27.27 ? 79   ILE B O   1 
ATOM   586  C CB  . ILE A 1 79  ? -12.265 8.105   8.206   1.00  26.33 ? 79   ILE B CB  1 
ATOM   587  C CG1 . ILE A 1 79  ? -13.784 8.215   8.333   1.00  30.01 ? 79   ILE B CG1 1 
ATOM   588  C CG2 . ILE A 1 79  ? -11.866 7.294   6.962   1.00  28.72 ? 79   ILE B CG2 1 
ATOM   589  C CD1 . ILE A 1 79  ? -14.476 8.624   7.007   1.00  31.08 ? 79   ILE B CD1 1 
ATOM   590  N N   . ALA A 1 80  ? -12.693 7.578   11.657  1.00  24.62 ? 80   ALA B N   1 
ATOM   591  C CA  . ALA A 1 80  ? -12.954 8.117   12.999  1.00  22.81 ? 80   ALA B CA  1 
ATOM   592  C C   . ALA A 1 80  ? -11.877 7.689   14.000  1.00  23.09 ? 80   ALA B C   1 
ATOM   593  O O   . ALA A 1 80  ? -12.059 7.811   15.214  1.00  20.99 ? 80   ALA B O   1 
ATOM   594  C CB  . ALA A 1 80  ? -14.361 7.728   13.498  1.00  23.07 ? 80   ALA B CB  1 
ATOM   595  N N   . SER A 1 81  ? -10.757 7.195   13.476  1.00  21.32 ? 81   SER B N   1 
ATOM   596  C CA  . SER A 1 81  ? -9.540  6.888   14.245  1.00  21.20 ? 81   SER B CA  1 
ATOM   597  C C   . SER A 1 81  ? -9.614  5.737   15.244  1.00  25.12 ? 81   SER B C   1 
ATOM   598  O O   . SER A 1 81  ? -8.906  5.753   16.242  1.00  22.19 ? 81   SER B O   1 
ATOM   599  C CB  . SER A 1 81  ? -8.958  8.132   14.948  1.00  24.21 ? 81   SER B CB  1 
ATOM   600  O OG  . SER A 1 81  ? -8.603  9.139   14.021  1.00  24.69 ? 81   SER B OG  1 
ATOM   601  N N   . ALA A 1 82  ? -10.432 4.727   14.980  1.00  22.57 ? 82   ALA B N   1 
ATOM   602  C CA  . ALA A 1 82  ? -10.342 3.518   15.787  1.00  23.23 ? 82   ALA B CA  1 
ATOM   603  C C   . ALA A 1 82  ? -8.890  3.024   15.811  1.00  22.42 ? 82   ALA B C   1 
ATOM   604  O O   . ALA A 1 82  ? -8.147  3.199   14.855  1.00  23.13 ? 82   ALA B O   1 
ATOM   605  C CB  . ALA A 1 82  ? -11.259 2.430   15.240  1.00  19.17 ? 82   ALA B CB  1 
ATOM   606  N N   . SER A 1 83  ? -8.488  2.394   16.905  1.00  22.41 ? 83   SER B N   1 
ATOM   607  C CA  . SER A 1 83  ? -7.158  1.814   16.980  1.00  26.57 ? 83   SER B CA  1 
ATOM   608  C C   . SER A 1 83  ? -7.031  0.628   16.011  1.00  30.62 ? 83   SER B C   1 
ATOM   609  O O   . SER A 1 83  ? -5.993  0.434   15.369  1.00  26.82 ? 83   SER B O   1 
ATOM   610  C CB  . SER A 1 83  ? -6.890  1.359   18.420  1.00  27.54 ? 83   SER B CB  1 
ATOM   611  O OG  . SER A 1 83  ? -5.644  0.710   18.509  1.00  35.35 ? 83   SER B OG  1 
ATOM   612  N N   . ARG A 1 84  ? -8.092  -0.167  15.908  1.00  23.02 ? 84   ARG B N   1 
ATOM   613  C CA  . ARG A 1 84  ? -8.104  -1.332  15.013  1.00  22.19 ? 84   ARG B CA  1 
ATOM   614  C C   . ARG A 1 84  ? -9.554  -1.641  14.663  1.00  24.09 ? 84   ARG B C   1 
ATOM   615  O O   . ARG A 1 84  ? -10.451 -1.380  15.462  1.00  20.42 ? 84   ARG B O   1 
ATOM   616  C CB  . ARG A 1 84  ? -7.432  -2.543  15.685  1.00  26.66 ? 84   ARG B CB  1 
ATOM   617  C CG  . ARG A 1 84  ? -7.408  -3.841  14.852  1.00  28.23 ? 84   ARG B CG  1 
ATOM   618  C CD  . ARG A 1 84  ? -6.564  -4.964  15.514  1.00  27.04 ? 84   ARG B CD  1 
ATOM   619  N NE  . ARG A 1 84  ? -7.018  -5.276  16.872  1.00  32.66 ? 84   ARG B NE  1 
ATOM   620  C CZ  . ARG A 1 84  ? -6.395  -6.109  17.705  1.00  34.39 ? 84   ARG B CZ  1 
ATOM   621  N NH1 . ARG A 1 84  ? -5.283  -6.733  17.332  1.00  36.74 ? 84   ARG B NH1 1 
ATOM   622  N NH2 . ARG A 1 84  ? -6.882  -6.322  18.913  1.00  31.89 ? 84   ARG B NH2 1 
ATOM   623  N N   . VAL A 1 85  ? -9.778  -2.174  13.458  1.00  21.96 ? 85   VAL B N   1 
ATOM   624  C CA  . VAL A 1 85  ? -11.109 -2.568  13.026  1.00  20.76 ? 85   VAL B CA  1 
ATOM   625  C C   . VAL A 1 85  ? -11.100 -4.005  12.539  1.00  21.55 ? 85   VAL B C   1 
ATOM   626  O O   . VAL A 1 85  ? -10.405 -4.352  11.589  1.00  19.81 ? 85   VAL B O   1 
ATOM   627  C CB  . VAL A 1 85  ? -11.658 -1.654  11.910  1.00  25.11 ? 85   VAL B CB  1 
ATOM   628  C CG1 . VAL A 1 85  ? -13.087 -2.068  11.541  1.00  23.01 ? 85   VAL B CG1 1 
ATOM   629  C CG2 . VAL A 1 85  ? -11.632 -0.193  12.371  1.00  20.04 ? 85   VAL B CG2 1 
ATOM   630  N N   . THR A 1 86  ? -11.881 -4.841  13.199  1.00  17.30 ? 86   THR B N   1 
ATOM   631  C CA  . THR A 1 86  ? -11.958 -6.236  12.826  1.00  15.45 ? 86   THR B CA  1 
ATOM   632  C C   . THR A 1 86  ? -13.324 -6.499  12.259  1.00  16.95 ? 86   THR B C   1 
ATOM   633  O O   . THR A 1 86  ? -14.341 -6.112  12.850  1.00  17.74 ? 86   THR B O   1 
ATOM   634  C CB  . THR A 1 86  ? -11.684 -7.131  14.044  1.00  19.05 ? 86   THR B CB  1 
ATOM   635  O OG1 . THR A 1 86  ? -10.314 -6.959  14.412  1.00  19.37 ? 86   THR B OG1 1 
ATOM   636  C CG2 . THR A 1 86  ? -11.955 -8.595  13.731  1.00  16.19 ? 86   THR B CG2 1 
ATOM   637  N N   . ALA A 1 87  ? -13.356 -7.131  11.089  1.00  16.73 ? 87   ALA B N   1 
ATOM   638  C CA  . ALA A 1 87  ? -14.630 -7.581  10.539  1.00  16.66 ? 87   ALA B CA  1 
ATOM   639  C C   . ALA A 1 87  ? -14.914 -8.992  11.021  1.00  17.77 ? 87   ALA B C   1 
ATOM   640  O O   . ALA A 1 87  ? -14.121 -9.906  10.803  1.00  18.90 ? 87   ALA B O   1 
ATOM   641  C CB  . ALA A 1 87  ? -14.618 -7.542  9.041   1.00  16.46 ? 87   ALA B CB  1 
ATOM   642  N N   . VAL A 1 88  ? -16.046 -9.159  11.695  1.00  17.95 ? 88   VAL B N   1 
ATOM   643  C CA  . VAL A 1 88  ? -16.464 -10.461 12.179  1.00  17.28 ? 88   VAL B CA  1 
ATOM   644  C C   . VAL A 1 88  ? -17.560 -10.916 11.230  1.00  17.98 ? 88   VAL B C   1 
ATOM   645  O O   . VAL A 1 88  ? -18.670 -10.411 11.268  1.00  20.14 ? 88   VAL B O   1 
ATOM   646  C CB  . VAL A 1 88  ? -16.997 -10.373 13.638  1.00  18.82 ? 88   VAL B CB  1 
ATOM   647  C CG1 . VAL A 1 88  ? -17.428 -11.748 14.143  1.00  18.51 ? 88   VAL B CG1 1 
ATOM   648  C CG2 . VAL A 1 88  ? -15.919 -9.742  14.580  1.00  19.87 ? 88   VAL B CG2 1 
ATOM   649  N N   . ILE A 1 89  ? -17.240 -11.867 10.364  1.00  18.36 ? 89   ILE B N   1 
ATOM   650  C CA  . ILE A 1 89  ? -18.134 -12.202 9.271   1.00  17.57 ? 89   ILE B CA  1 
ATOM   651  C C   . ILE A 1 89  ? -18.442 -13.674 9.372   1.00  19.75 ? 89   ILE B C   1 
ATOM   652  O O   . ILE A 1 89  ? -17.757 -14.498 8.758   1.00  19.23 ? 89   ILE B O   1 
ATOM   653  C CB  . ILE A 1 89  ? -17.459 -11.941 7.895   1.00  22.02 ? 89   ILE B CB  1 
ATOM   654  C CG1 . ILE A 1 89  ? -16.888 -10.532 7.826   1.00  16.78 ? 89   ILE B CG1 1 
ATOM   655  C CG2 . ILE A 1 89  ? -18.443 -12.167 6.733   1.00  20.27 ? 89   ILE B CG2 1 
ATOM   656  C CD1 . ILE A 1 89  ? -16.245 -10.212 6.462   1.00  20.35 ? 89   ILE B CD1 1 
ATOM   657  N N   . PRO A 1 90  ? -19.481 -14.018 10.135  1.00  20.93 ? 90   PRO B N   1 
ATOM   658  C CA  . PRO A 1 90  ? -19.690 -15.437 10.423  1.00  27.53 ? 90   PRO B CA  1 
ATOM   659  C C   . PRO A 1 90  ? -19.784 -16.280 9.149   1.00  23.08 ? 90   PRO B C   1 
ATOM   660  O O   . PRO A 1 90  ? -19.110 -17.300 9.053   1.00  24.14 ? 90   PRO B O   1 
ATOM   661  C CB  . PRO A 1 90  ? -20.991 -15.430 11.232  1.00  28.50 ? 90   PRO B CB  1 
ATOM   662  C CG  . PRO A 1 90  ? -20.952 -14.087 11.939  1.00  26.11 ? 90   PRO B CG  1 
ATOM   663  C CD  . PRO A 1 90  ? -20.450 -13.167 10.843  1.00  25.48 ? 90   PRO B CD  1 
ATOM   664  N N   . CYS A 1 91  ? -20.574 -15.844 8.175   1.00  23.48 ? 91   CYS B N   1 
ATOM   665  C CA  . CYS A 1 91  ? -20.655 -16.539 6.887   1.00  27.34 ? 91   CYS B CA  1 
ATOM   666  C C   . CYS A 1 91  ? -20.101 -15.606 5.825   1.00  23.24 ? 91   CYS B C   1 
ATOM   667  O O   . CYS A 1 91  ? -20.652 -14.540 5.599   1.00  25.61 ? 91   CYS B O   1 
ATOM   668  C CB  . CYS A 1 91  ? -22.100 -16.923 6.557   1.00  26.49 ? 91   CYS B CB  1 
ATOM   669  S SG  . CYS A 1 91  ? -22.252 -17.942 5.068   1.00  32.08 ? 91   CYS B SG  1 
ATOM   670  N N   . PHE A 1 92  ? -18.988 -15.986 5.203   1.00  23.68 ? 92   PHE B N   1 
ATOM   671  C CA  . PHE A 1 92  ? -18.280 -15.091 4.288   1.00  22.60 ? 92   PHE B CA  1 
ATOM   672  C C   . PHE A 1 92  ? -19.000 -15.026 2.930   1.00  24.95 ? 92   PHE B C   1 
ATOM   673  O O   . PHE A 1 92  ? -19.218 -16.033 2.293   1.00  28.14 ? 92   PHE B O   1 
ATOM   674  C CB  . PHE A 1 92  ? -16.833 -15.564 4.096   1.00  22.41 ? 92   PHE B CB  1 
ATOM   675  C CG  . PHE A 1 92  ? -15.928 -14.548 3.440   1.00  18.26 ? 92   PHE B CG  1 
ATOM   676  C CD1 . PHE A 1 92  ? -15.137 -13.698 4.209   1.00  21.42 ? 92   PHE B CD1 1 
ATOM   677  C CD2 . PHE A 1 92  ? -15.856 -14.462 2.057   1.00  21.63 ? 92   PHE B CD2 1 
ATOM   678  C CE1 . PHE A 1 92  ? -14.298 -12.761 3.600   1.00  24.86 ? 92   PHE B CE1 1 
ATOM   679  C CE2 . PHE A 1 92  ? -15.015 -13.536 1.436   1.00  22.87 ? 92   PHE B CE2 1 
ATOM   680  C CZ  . PHE A 1 92  ? -14.234 -12.687 2.208   1.00  18.94 ? 92   PHE B CZ  1 
ATOM   681  N N   . PRO A 1 93  ? -19.374 -13.826 2.505   1.00  22.22 ? 93   PRO B N   1 
ATOM   682  C CA  . PRO A 1 93  ? -20.149 -13.634 1.270   1.00  29.49 ? 93   PRO B CA  1 
ATOM   683  C C   . PRO A 1 93  ? -19.342 -13.915 -0.010  1.00  26.95 ? 93   PRO B C   1 
ATOM   684  O O   . PRO A 1 93  ? -18.143 -13.631 -0.063  1.00  25.54 ? 93   PRO B O   1 
ATOM   685  C CB  . PRO A 1 93  ? -20.551 -12.162 1.345   1.00  31.44 ? 93   PRO B CB  1 
ATOM   686  C CG  . PRO A 1 93  ? -19.515 -11.522 2.191   1.00  28.44 ? 93   PRO B CG  1 
ATOM   687  C CD  . PRO A 1 93  ? -19.127 -12.559 3.215   1.00  24.79 ? 93   PRO B CD  1 
ATOM   688  N N   . TYR A 1 94  ? -20.004 -14.493 -1.011  1.00  24.88 ? 94   TYR B N   1 
ATOM   689  C CA  . TYR A 1 94  ? -19.387 -14.835 -2.287  1.00  28.57 ? 94   TYR B CA  1 
ATOM   690  C C   . TYR A 1 94  ? -18.292 -15.889 -2.147  1.00  28.10 ? 94   TYR B C   1 
ATOM   691  O O   . TYR A 1 94  ? -17.494 -16.082 -3.051  1.00  24.53 ? 94   TYR B O   1 
ATOM   692  C CB  . TYR A 1 94  ? -18.867 -13.575 -3.011  1.00  26.07 ? 94   TYR B CB  1 
ATOM   693  C CG  . TYR A 1 94  ? -19.988 -12.695 -3.523  1.00  26.58 ? 94   TYR B CG  1 
ATOM   694  C CD1 . TYR A 1 94  ? -20.516 -11.685 -2.731  1.00  25.86 ? 94   TYR B CD1 1 
ATOM   695  C CD2 . TYR A 1 94  ? -20.552 -12.913 -4.780  1.00  24.59 ? 94   TYR B CD2 1 
ATOM   696  C CE1 . TYR A 1 94  ? -21.547 -10.892 -3.183  1.00  25.95 ? 94   TYR B CE1 1 
ATOM   697  C CE2 . TYR A 1 94  ? -21.590 -12.132 -5.242  1.00  24.47 ? 94   TYR B CE2 1 
ATOM   698  C CZ  . TYR A 1 94  ? -22.078 -11.114 -4.436  1.00  25.26 ? 94   TYR B CZ  1 
ATOM   699  O OH  . TYR A 1 94  ? -23.098 -10.318 -4.871  1.00  23.90 ? 94   TYR B OH  1 
ATOM   700  N N   . ALA A 1 95  ? -18.280 -16.586 -1.012  1.00  31.33 ? 95   ALA B N   1 
ATOM   701  C CA  . ALA A 1 95  ? -17.253 -17.588 -0.731  1.00  29.10 ? 95   ALA B CA  1 
ATOM   702  C C   . ALA A 1 95  ? -17.226 -18.733 -1.749  1.00  31.48 ? 95   ALA B C   1 
ATOM   703  O O   . ALA A 1 95  ? -16.162 -19.273 -2.050  1.00  32.66 ? 95   ALA B O   1 
ATOM   704  C CB  . ALA A 1 95  ? -17.419 -18.138 0.680   1.00  25.71 ? 95   ALA B CB  1 
ATOM   705  N N   . ARG A 1 96  ? -18.386 -19.103 -2.272  0.95  28.61 ? 96   ARG B N   1 
ATOM   706  C CA  . ARG A 1 96  ? -18.452 -20.108 -3.334  0.95  33.51 ? 96   ARG B CA  1 
ATOM   707  C C   . ARG A 1 96  ? -17.931 -19.592 -4.682  0.95  36.49 ? 96   ARG B C   1 
ATOM   708  O O   . ARG A 1 96  ? -17.836 -20.353 -5.634  0.95  38.87 ? 96   ARG B O   1 
ATOM   709  C CB  . ARG A 1 96  ? -19.876 -20.633 -3.495  0.95  38.60 ? 96   ARG B CB  1 
ATOM   710  C CG  . ARG A 1 96  ? -20.379 -21.456 -2.316  0.95  37.79 ? 96   ARG B CG  1 
ATOM   711  C CD  . ARG A 1 96  ? -21.886 -21.682 -2.397  0.95  47.44 ? 96   ARG B CD  1 
ATOM   712  N NE  . ARG A 1 96  ? -22.626 -20.420 -2.378  0.95  49.01 ? 96   ARG B NE  1 
ATOM   713  C CZ  . ARG A 1 96  ? -23.810 -20.237 -2.957  0.95  47.99 ? 96   ARG B CZ  1 
ATOM   714  N NH1 . ARG A 1 96  ? -24.396 -21.232 -3.610  0.95  46.57 ? 96   ARG B NH1 1 
ATOM   715  N NH2 . ARG A 1 96  ? -24.407 -19.055 -2.887  0.95  50.88 ? 96   ARG B NH2 1 
ATOM   716  N N   . GLN A 1 97  ? -17.606 -18.303 -4.765  0.73  32.37 ? 97   GLN B N   1 
ATOM   717  C CA  . GLN A 1 97  ? -16.974 -17.758 -5.973  0.73  31.11 ? 97   GLN B CA  1 
ATOM   718  C C   . GLN A 1 97  ? -15.476 -17.502 -5.744  0.73  27.65 ? 97   GLN B C   1 
ATOM   719  O O   . GLN A 1 97  ? -15.017 -16.360 -5.739  0.73  29.01 ? 97   GLN B O   1 
ATOM   720  C CB  . GLN A 1 97  ? -17.707 -16.500 -6.466  0.73  30.91 ? 97   GLN B CB  1 
ATOM   721  C CG  . GLN A 1 97  ? -19.016 -16.802 -7.210  0.73  36.44 ? 97   GLN B CG  1 
ATOM   722  C CD  . GLN A 1 97  ? -19.850 -15.564 -7.514  0.73  36.77 ? 97   GLN B CD  1 
ATOM   723  O OE1 . GLN A 1 97  ? -19.368 -14.602 -8.116  0.73  36.71 ? 97   GLN B OE1 1 
ATOM   724  N NE2 . GLN A 1 97  ? -21.113 -15.586 -7.098  0.73  35.92 ? 97   GLN B NE2 1 
ATOM   725  N N   . ASP A 1 98  ? -14.726 -18.586 -5.571  0.10  28.22 ? 98   ASP B N   1 
ATOM   726  C CA  . ASP A 1 98  ? -13.335 -18.507 -5.146  0.10  27.89 ? 98   ASP B CA  1 
ATOM   727  C C   . ASP A 1 98  ? -12.365 -19.053 -6.190  0.10  28.25 ? 98   ASP B C   1 
ATOM   728  O O   . ASP A 1 98  ? -11.183 -19.246 -5.906  0.10  26.53 ? 98   ASP B O   1 
ATOM   729  C CB  . ASP A 1 98  ? -13.151 -19.260 -3.831  0.10  27.13 ? 98   ASP B CB  1 
ATOM   730  C CG  . ASP A 1 98  ? -13.535 -20.723 -3.941  0.10  28.60 ? 98   ASP B CG  1 
ATOM   731  O OD1 . ASP A 1 98  ? -14.391 -21.062 -4.782  0.10  29.08 ? 98   ASP B OD1 1 
ATOM   732  O OD2 . ASP A 1 98  ? -12.980 -21.540 -3.184  0.10  27.54 ? 98   ASP B OD2 1 
ATOM   733  N N   . LYS A 1 99  ? -12.869 -19.304 -7.393  0.10  29.72 ? 99   LYS B N   1 
ATOM   734  C CA  . LYS A 1 99  ? -12.030 -19.772 -8.492  0.10  33.70 ? 99   LYS B CA  1 
ATOM   735  C C   . LYS A 1 99  ? -12.718 -19.545 -9.832  0.10  36.47 ? 99   LYS B C   1 
ATOM   736  O O   . LYS A 1 99  ? -13.892 -19.183 -9.879  0.10  34.27 ? 99   LYS B O   1 
ATOM   737  C CB  . LYS A 1 99  ? -11.669 -21.247 -8.313  0.10  33.75 ? 99   LYS B CB  1 
ATOM   738  C CG  . LYS A 1 99  ? -12.856 -22.193 -8.215  0.10  34.58 ? 99   LYS B CG  1 
ATOM   739  C CD  . LYS A 1 99  ? -12.384 -23.605 -7.904  0.10  34.72 ? 99   LYS B CD  1 
ATOM   740  C CE  . LYS A 1 99  ? -13.438 -24.399 -7.154  0.10  34.13 ? 99   LYS B CE  1 
ATOM   741  N NZ  . LYS A 1 99  ? -12.847 -25.581 -6.458  0.10  35.77 ? 99   LYS B NZ  1 
ATOM   742  N N   . LYS A 1 100 ? -11.985 -19.755 -10.920 1.00  39.77 ? 100  LYS B N   1 
ATOM   743  C CA  . LYS A 1 100 ? -12.530 -19.510 -12.258 1.00  41.36 ? 100  LYS B CA  1 
ATOM   744  C C   . LYS A 1 100 ? -13.327 -20.691 -12.816 1.00  46.80 ? 100  LYS B C   1 
ATOM   745  O O   . LYS A 1 100 ? -14.236 -20.502 -13.631 1.00  52.63 ? 100  LYS B O   1 
ATOM   746  C CB  . LYS A 1 100 ? -11.430 -19.116 -13.247 1.00  46.01 ? 100  LYS B CB  1 
ATOM   747  C CG  . LYS A 1 100 ? -10.950 -17.671 -13.163 1.00  43.58 ? 100  LYS B CG  1 
ATOM   748  C CD  . LYS A 1 100 ? -10.060 -17.366 -14.374 1.00  41.78 ? 100  LYS B CD  1 
ATOM   749  C CE  . LYS A 1 100 ? -9.381  -16.013 -14.278 1.00  40.11 ? 100  LYS B CE  1 
ATOM   750  N NZ  . LYS A 1 100 ? -8.421  -15.821 -15.412 1.00  46.48 ? 100  LYS B NZ  1 
ATOM   751  N N   . ASP A 1 101 ? -12.979 -21.901 -12.394 0.010 45.21 ? 101  ASP B N   1 
ATOM   752  C CA  . ASP A 1 101 ? -13.697 -23.100 -12.817 0.010 47.11 ? 101  ASP B CA  1 
ATOM   753  C C   . ASP A 1 101 ? -13.705 -23.293 -14.334 0.010 49.25 ? 101  ASP B C   1 
ATOM   754  O O   . ASP A 1 101 ? -14.693 -23.762 -14.899 0.010 50.26 ? 101  ASP B O   1 
ATOM   755  C CB  . ASP A 1 101 ? -15.136 -23.072 -12.291 0.010 45.65 ? 101  ASP B CB  1 
ATOM   756  C CG  . ASP A 1 101 ? -15.212 -23.218 -10.784 0.010 43.20 ? 101  ASP B CG  1 
ATOM   757  O OD1 . ASP A 1 101 ? -14.416 -23.995 -10.219 0.010 42.37 ? 101  ASP B OD1 1 
ATOM   758  O OD2 . ASP A 1 101 ? -16.074 -22.559 -10.163 0.010 42.59 ? 101  ASP B OD2 1 
ATOM   759  N N   . LYS A 1 102 ? -12.601 -22.936 -14.983 1.00  50.75 ? 102  LYS B N   1 
ATOM   760  C CA  . LYS A 1 102 ? -12.464 -23.059 -16.437 1.00  51.47 ? 102  LYS B CA  1 
ATOM   761  C C   . LYS A 1 102 ? -13.369 -22.107 -17.220 1.00  53.34 ? 102  LYS B C   1 
ATOM   762  O O   . LYS A 1 102 ? -13.677 -22.357 -18.387 1.00  54.98 ? 102  LYS B O   1 
ATOM   763  C CB  . LYS A 1 102 ? -12.720 -24.498 -16.905 1.00  53.77 ? 102  LYS B CB  1 
ATOM   764  C CG  . LYS A 1 102 ? -11.611 -25.489 -16.581 1.00  55.84 ? 102  LYS B CG  1 
ATOM   765  C CD  . LYS A 1 102 ? -11.658 -26.670 -17.539 1.00  58.58 ? 102  LYS B CD  1 
ATOM   766  C CE  . LYS A 1 102 ? -13.059 -27.256 -17.627 1.00  68.68 ? 102  LYS B CE  1 
ATOM   767  N NZ  . LYS A 1 102 ? -13.129 -28.388 -18.604 1.00  74.46 ? 102  LYS B NZ  1 
ATOM   768  N N   . SER A 1 103 ? -13.787 -21.016 -16.588 0.68  49.37 ? 103  SER B N   1 
ATOM   769  C CA  . SER A 1 103 ? -14.685 -20.067 -17.234 0.68  46.97 ? 103  SER B CA  1 
ATOM   770  C C   . SER A 1 103 ? -14.177 -18.636 -17.103 0.68  44.87 ? 103  SER B C   1 
ATOM   771  O O   . SER A 1 103 ? -13.318 -18.352 -16.278 0.68  43.05 ? 103  SER B O   1 
ATOM   772  C CB  . SER A 1 103 ? -16.095 -20.182 -16.646 0.68  47.00 ? 103  SER B CB  1 
ATOM   773  O OG  . SER A 1 103 ? -16.925 -19.128 -17.112 0.68  48.09 ? 103  SER B OG  1 
ATOM   774  N N   . ARG A 1 104 ? -14.712 -17.736 -17.925 1.00  47.12 ? 104  ARG B N   1 
ATOM   775  C CA  . ARG A 1 104 ? -14.331 -16.327 -17.870 1.00  41.80 ? 104  ARG B CA  1 
ATOM   776  C C   . ARG A 1 104 ? -15.049 -15.682 -16.687 1.00  45.75 ? 104  ARG B C   1 
ATOM   777  O O   . ARG A 1 104 ? -15.780 -14.700 -16.836 1.00  44.37 ? 104  ARG B O   1 
ATOM   778  C CB  . ARG A 1 104 ? -14.694 -15.625 -19.183 1.00  45.29 ? 104  ARG B CB  1 
ATOM   779  C CG  . ARG A 1 104 ? -13.622 -14.675 -19.717 1.00  46.57 ? 104  ARG B CG  1 
ATOM   780  C CD  . ARG A 1 104 ? -13.192 -15.053 -21.131 1.00  44.39 ? 104  ARG B CD  1 
ATOM   781  N NE  . ARG A 1 104 ? -14.362 -15.328 -21.943 1.00  49.00 ? 104  ARG B NE  1 
ATOM   782  C CZ  . ARG A 1 104 ? -14.371 -16.073 -23.040 1.00  41.56 ? 104  ARG B CZ  1 
ATOM   783  N NH1 . ARG A 1 104 ? -13.259 -16.630 -23.493 1.00  43.57 ? 104  ARG B NH1 1 
ATOM   784  N NH2 . ARG A 1 104 ? -15.512 -16.258 -23.684 1.00  45.53 ? 104  ARG B NH2 1 
ATOM   785  N N   . ALA A 1 105 ? -14.842 -16.257 -15.507 1.00  41.25 ? 105  ALA B N   1 
ATOM   786  C CA  . ALA A 1 105 ? -15.588 -15.865 -14.316 1.00  42.96 ? 105  ALA B CA  1 
ATOM   787  C C   . ALA A 1 105 ? -14.787 -14.940 -13.396 1.00  39.30 ? 105  ALA B C   1 
ATOM   788  O O   . ALA A 1 105 ? -13.552 -14.962 -13.389 1.00  38.05 ? 105  ALA B O   1 
ATOM   789  C CB  . ALA A 1 105 ? -16.045 -17.108 -13.556 1.00  44.92 ? 105  ALA B CB  1 
ATOM   790  N N   . PRO A 1 106 ? -15.490 -14.126 -12.604 0.86  36.71 ? 106  PRO B N   1 
ATOM   791  C CA  . PRO A 1 106 ? -14.757 -13.330 -11.628 0.86  34.12 ? 106  PRO B CA  1 
ATOM   792  C C   . PRO A 1 106 ? -14.416 -14.226 -10.441 0.86  33.00 ? 106  PRO B C   1 
ATOM   793  O O   . PRO A 1 106 ? -15.128 -15.187 -10.173 0.86  24.66 ? 106  PRO B O   1 
ATOM   794  C CB  . PRO A 1 106 ? -15.800 -12.299 -11.205 0.86  33.12 ? 106  PRO B CB  1 
ATOM   795  C CG  . PRO A 1 106 ? -17.081 -13.088 -11.226 0.86  35.32 ? 106  PRO B CG  1 
ATOM   796  C CD  . PRO A 1 106 ? -16.951 -14.024 -12.414 0.86  37.21 ? 106  PRO B CD  1 
ATOM   797  N N   . ILE A 1 107 ? -13.335 -13.942 -9.735  1.00  35.21 ? 107  ILE B N   1 
ATOM   798  C CA  . ILE A 1 107 ? -13.137 -14.611 -8.457  1.00  27.18 ? 107  ILE B CA  1 
ATOM   799  C C   . ILE A 1 107 ? -13.722 -13.680 -7.409  1.00  24.35 ? 107  ILE B C   1 
ATOM   800  O O   . ILE A 1 107 ? -12.995 -12.948 -6.750  1.00  26.03 ? 107  ILE B O   1 
ATOM   801  C CB  . ILE A 1 107 ? -11.664 -14.875 -8.177  1.00  32.72 ? 107  ILE B CB  1 
ATOM   802  C CG1 . ILE A 1 107 ? -11.043 -15.622 -9.357  1.00  36.81 ? 107  ILE B CG1 1 
ATOM   803  C CG2 . ILE A 1 107 ? -11.497 -15.668 -6.873  1.00  24.24 ? 107  ILE B CG2 1 
ATOM   804  C CD1 . ILE A 1 107 ? -9.539  -15.823 -9.226  1.00  36.12 ? 107  ILE B CD1 1 
ATOM   805  N N   . SER A 1 108 ? -15.044 -13.688 -7.285  1.00  24.64 ? 108  SER B N   1 
ATOM   806  C CA  . SER A 1 108 ? -15.738 -12.668 -6.499  1.00  27.90 ? 108  SER B CA  1 
ATOM   807  C C   . SER A 1 108 ? -15.300 -12.640 -5.037  1.00  22.57 ? 108  SER B C   1 
ATOM   808  O O   . SER A 1 108 ? -15.387 -11.603 -4.365  1.00  23.13 ? 108  SER B O   1 
ATOM   809  C CB  . SER A 1 108 ? -17.254 -12.861 -6.603  1.00  30.87 ? 108  SER B CB  1 
ATOM   810  O OG  . SER A 1 108 ? -17.703 -12.656 -7.936  1.00  32.09 ? 108  SER B OG  1 
ATOM   811  N N   . ALA A 1 109 ? -14.816 -13.775 -4.541  1.00  21.20 ? 109  ALA B N   1 
ATOM   812  C CA  . ALA A 1 109 ? -14.398 -13.840 -3.150  1.00  21.04 ? 109  ALA B CA  1 
ATOM   813  C C   . ALA A 1 109 ? -13.108 -13.060 -2.957  1.00  21.96 ? 109  ALA B C   1 
ATOM   814  O O   . ALA A 1 109 ? -12.881 -12.492 -1.882  1.00  20.94 ? 109  ALA B O   1 
ATOM   815  C CB  . ALA A 1 109 ? -14.229 -15.274 -2.699  1.00  21.46 ? 109  ALA B CB  1 
ATOM   816  N N   . LYS A 1 110 ? -12.255 -13.044 -3.984  1.00  17.03 ? 110  LYS B N   1 
ATOM   817  C CA  . LYS A 1 110 ? -11.040 -12.246 -3.934  1.00  17.72 ? 110  LYS B CA  1 
ATOM   818  C C   . LYS A 1 110 ? -11.425 -10.780 -4.055  1.00  19.81 ? 110  LYS B C   1 
ATOM   819  O O   . LYS A 1 110 ? -10.841 -9.927  -3.403  1.00  18.25 ? 110  LYS B O   1 
ATOM   820  C CB  . LYS A 1 110 ? -10.056 -12.636 -5.044  1.00  20.96 ? 110  LYS B CB  1 
ATOM   821  C CG  . LYS A 1 110 ? -8.844  -11.696 -5.181  1.00  25.23 ? 110  LYS B CG  1 
ATOM   822  C CD  . LYS A 1 110 ? -8.001  -11.621 -3.875  1.00  21.96 ? 110  LYS B CD  1 
ATOM   823  C CE  . LYS A 1 110 ? -6.849  -10.615 -4.005  1.00  25.65 ? 110  LYS B CE  1 
ATOM   824  N NZ  . LYS A 1 110 ? -5.886  -11.021 -5.061  1.00  26.20 ? 110  LYS B NZ  1 
ATOM   825  N N   . LEU A 1 111 ? -12.409 -10.484 -4.900  1.00  20.28 ? 111  LEU B N   1 
ATOM   826  C CA  . LEU A 1 111 ? -12.896 -9.116  -4.973  1.00  20.53 ? 111  LEU B CA  1 
ATOM   827  C C   . LEU A 1 111 ? -13.415 -8.629  -3.600  1.00  18.25 ? 111  LEU B C   1 
ATOM   828  O O   . LEU A 1 111 ? -13.121 -7.528  -3.179  1.00  18.37 ? 111  LEU B O   1 
ATOM   829  C CB  . LEU A 1 111 ? -13.972 -8.992  -6.045  1.00  23.18 ? 111  LEU B CB  1 
ATOM   830  C CG  . LEU A 1 111 ? -14.743 -7.666  -6.117  1.00  24.95 ? 111  LEU B CG  1 
ATOM   831  C CD1 . LEU A 1 111 ? -13.830 -6.470  -6.459  1.00  23.81 ? 111  LEU B CD1 1 
ATOM   832  C CD2 . LEU A 1 111 ? -15.924 -7.800  -7.121  1.00  27.01 ? 111  LEU B CD2 1 
ATOM   833  N N   . VAL A 1 112 ? -14.217 -9.448  -2.935  1.00  19.51 ? 112  VAL B N   1 
ATOM   834  C CA  . VAL A 1 112 ? -14.724 -9.117  -1.600  1.00  22.63 ? 112  VAL B CA  1 
ATOM   835  C C   . VAL A 1 112 ? -13.576 -8.865  -0.611  1.00  16.18 ? 112  VAL B C   1 
ATOM   836  O O   . VAL A 1 112 ? -13.612 -7.908  0.152   1.00  19.13 ? 112  VAL B O   1 
ATOM   837  C CB  . VAL A 1 112 ? -15.739 -10.196 -1.089  1.00  16.22 ? 112  VAL B CB  1 
ATOM   838  C CG1 . VAL A 1 112 ? -16.081 -10.013 0.409   1.00  15.53 ? 112  VAL B CG1 1 
ATOM   839  C CG2 . VAL A 1 112 ? -17.007 -10.147 -1.928  1.00  20.97 ? 112  VAL B CG2 1 
ATOM   840  N N   . ALA A 1 113 ? -12.542 -9.701  -0.649  1.00  17.18 ? 113  ALA B N   1 
ATOM   841  C CA  . ALA A 1 113 ? -11.389 -9.533  0.227   1.00  20.29 ? 113  ALA B CA  1 
ATOM   842  C C   . ALA A 1 113 ? -10.713 -8.195  -0.033  1.00  20.46 ? 113  ALA B C   1 
ATOM   843  O O   . ALA A 1 113 ? -10.352 -7.491  0.901   1.00  17.10 ? 113  ALA B O   1 
ATOM   844  C CB  . ALA A 1 113 ? -10.391 -10.667 0.022   1.00  17.76 ? 113  ALA B CB  1 
ATOM   845  N N   . ASN A 1 114 ? -10.544 -7.856  -1.312  1.00  19.66 ? 114  ASN B N   1 
ATOM   846  C CA  . ASN A 1 114 ? -9.969  -6.568  -1.672  1.00  19.41 ? 114  ASN B CA  1 
ATOM   847  C C   . ASN A 1 114 ? -10.825 -5.405  -1.218  1.00  16.41 ? 114  ASN B C   1 
ATOM   848  O O   . ASN A 1 114 ? -10.309 -4.365  -0.794  1.00  22.82 ? 114  ASN B O   1 
ATOM   849  C CB  . ASN A 1 114 ? -9.710  -6.468  -3.185  1.00  15.82 ? 114  ASN B CB  1 
ATOM   850  C CG  . ASN A 1 114 ? -8.473  -7.209  -3.596  1.00  21.26 ? 114  ASN B CG  1 
ATOM   851  O OD1 . ASN A 1 114 ? -7.583  -7.446  -2.780  1.00  25.82 ? 114  ASN B OD1 1 
ATOM   852  N ND2 . ASN A 1 114 ? -8.403  -7.588  -4.855  1.00  22.83 ? 114  ASN B ND2 1 
ATOM   853  N N   . MET A 1 115 ? -12.137 -5.569  -1.301  0.90  15.62 ? 115  MET B N   1 
ATOM   854  C CA  . MET A 1 115 ? -13.017 -4.495  -0.867  0.90  17.25 ? 115  MET B CA  1 
ATOM   855  C C   . MET A 1 115 ? -12.896 -4.304  0.652   0.90  15.08 ? 115  MET B C   1 
ATOM   856  O O   . MET A 1 115 ? -12.757 -3.190  1.138   0.90  15.84 ? 115  MET B O   1 
ATOM   857  C CB  . MET A 1 115 ? -14.456 -4.785  -1.283  0.90  14.31 ? 115  MET B CB  1 
ATOM   858  C CG  . MET A 1 115 ? -14.674 -4.831  -2.815  0.90  20.28 ? 115  MET B CG  1 
ATOM   859  S SD  . MET A 1 115 ? -16.350 -5.302  -3.179  0.90  30.25 ? 115  MET B SD  1 
ATOM   860  C CE  . MET A 1 115 ? -16.237 -7.045  -3.416  0.90  29.56 ? 115  MET B CE  1 
ATOM   861  N N   . LEU A 1 116 ? -12.930 -5.404  1.395   1.00  16.40 ? 116  LEU B N   1 
ATOM   862  C CA  . LEU A 1 116 ? -12.776 -5.331  2.846   1.00  17.17 ? 116  LEU B CA  1 
ATOM   863  C C   . LEU A 1 116 ? -11.453 -4.662  3.199   1.00  17.42 ? 116  LEU B C   1 
ATOM   864  O O   . LEU A 1 116 ? -11.391 -3.813  4.087   1.00  18.88 ? 116  LEU B O   1 
ATOM   865  C CB  . LEU A 1 116 ? -12.829 -6.731  3.459   1.00  16.71 ? 116  LEU B CB  1 
ATOM   866  C CG  . LEU A 1 116 ? -14.216 -7.355  3.392   1.00  15.90 ? 116  LEU B CG  1 
ATOM   867  C CD1 . LEU A 1 116 ? -14.102 -8.900  3.481   1.00  16.11 ? 116  LEU B CD1 1 
ATOM   868  C CD2 . LEU A 1 116 ? -15.057 -6.807  4.546   1.00  18.54 ? 116  LEU B CD2 1 
ATOM   869  N N   . SER A 1 117 ? -10.406 -5.039  2.477   1.00  19.78 ? 117  SER B N   1 
ATOM   870  C CA  . SER A 1 117 ? -9.076  -4.509  2.719   1.00  20.90 ? 117  SER B CA  1 
ATOM   871  C C   . SER A 1 117 ? -9.003  -2.996  2.447   1.00  19.85 ? 117  SER B C   1 
ATOM   872  O O   . SER A 1 117 ? -8.555  -2.225  3.293   1.00  23.36 ? 117  SER B O   1 
ATOM   873  C CB  . SER A 1 117 ? -8.039  -5.274  1.886   1.00  23.55 ? 117  SER B CB  1 
ATOM   874  O OG  . SER A 1 117 ? -7.989  -6.654  2.243   1.00  25.88 ? 117  SER B OG  1 
ATOM   875  N N   . VAL A 1 118 ? -9.464  -2.553  1.288   1.00  20.82 ? 118  VAL B N   1 
ATOM   876  C CA  . VAL A 1 118 ? -9.419  -1.111  1.011   1.00  20.59 ? 118  VAL B CA  1 
ATOM   877  C C   . VAL A 1 118 ? -10.361 -0.299  1.909   1.00  20.99 ? 118  VAL B C   1 
ATOM   878  O O   . VAL A 1 118 ? -10.091 0.870   2.196   1.00  22.70 ? 118  VAL B O   1 
ATOM   879  C CB  . VAL A 1 118 ? -9.677  -0.750  -0.485  1.00  21.15 ? 118  VAL B CB  1 
ATOM   880  C CG1 . VAL A 1 118 ? -8.714  -1.493  -1.398  1.00  25.55 ? 118  VAL B CG1 1 
ATOM   881  C CG2 . VAL A 1 118 ? -11.141 -1.020  -0.887  1.00  22.28 ? 118  VAL B CG2 1 
ATOM   882  N N   . ALA A 1 119 ? -11.460 -0.899  2.353   1.00  19.81 ? 119  ALA B N   1 
ATOM   883  C CA  . ALA A 1 119 ? -12.367 -0.170  3.237   1.00  21.05 ? 119  ALA B CA  1 
ATOM   884  C C   . ALA A 1 119 ? -11.639 0.086   4.547   1.00  18.64 ? 119  ALA B C   1 
ATOM   885  O O   . ALA A 1 119 ? -11.972 1.013   5.274   1.00  19.78 ? 119  ALA B O   1 
ATOM   886  C CB  . ALA A 1 119 ? -13.697 -0.929  3.454   1.00  20.11 ? 119  ALA B CB  1 
ATOM   887  N N   . GLY A 1 120 ? -10.622 -0.727  4.824   1.00  20.27 ? 120  GLY B N   1 
ATOM   888  C CA  . GLY A 1 120 ? -9.781  -0.538  5.993   1.00  24.54 ? 120  GLY B CA  1 
ATOM   889  C C   . GLY A 1 120 ? -9.798  -1.613  7.078   1.00  22.85 ? 120  GLY B C   1 
ATOM   890  O O   . GLY A 1 120 ? -9.391  -1.353  8.200   1.00  22.64 ? 120  GLY B O   1 
ATOM   891  N N   . ALA A 1 121 ? -10.258 -2.820  6.778   1.00  21.74 ? 121  ALA B N   1 
ATOM   892  C CA  . ALA A 1 121 ? -10.216 -3.873  7.793   1.00  22.09 ? 121  ALA B CA  1 
ATOM   893  C C   . ALA A 1 121 ? -8.773  -4.257  8.130   1.00  21.44 ? 121  ALA B C   1 
ATOM   894  O O   . ALA A 1 121 ? -7.947  -4.413  7.240   1.00  18.20 ? 121  ALA B O   1 
ATOM   895  C CB  . ALA A 1 121 ? -11.003 -5.088  7.351   1.00  20.36 ? 121  ALA B CB  1 
ATOM   896  N N   . ASP A 1 122 ? -8.478  -4.410  9.421   1.00  19.27 ? 122  ASP B N   1 
ATOM   897  C CA  . ASP A 1 122 ? -7.157  -4.826  9.852   1.00  20.94 ? 122  ASP B CA  1 
ATOM   898  C C   . ASP A 1 122 ? -7.122  -6.318  10.125  1.00  19.03 ? 122  ASP B C   1 
ATOM   899  O O   . ASP A 1 122 ? -6.055  -6.925  10.201  1.00  16.57 ? 122  ASP B O   1 
ATOM   900  C CB  . ASP A 1 122 ? -6.763  -4.080  11.121  1.00  21.95 ? 122  ASP B CB  1 
ATOM   901  C CG  . ASP A 1 122 ? -6.718  -2.577  10.920  1.00  27.47 ? 122  ASP B CG  1 
ATOM   902  O OD1 . ASP A 1 122 ? -5.904  -2.098  10.087  1.00  23.27 ? 122  ASP B OD1 1 
ATOM   903  O OD2 . ASP A 1 122 ? -7.501  -1.874  11.592  1.00  24.85 ? 122  ASP B OD2 1 
ATOM   904  N N   . HIS A 1 123 ? -8.290  -6.915  10.276  1.00  18.53 ? 123  HIS B N   1 
ATOM   905  C CA  . HIS A 1 123 ? -8.346  -8.288  10.765  1.00  18.10 ? 123  HIS B CA  1 
ATOM   906  C C   . HIS A 1 123 ? -9.701  -8.871  10.396  1.00  15.97 ? 123  HIS B C   1 
ATOM   907  O O   . HIS A 1 123 ? -10.695 -8.160  10.416  1.00  17.93 ? 123  HIS B O   1 
ATOM   908  C CB  . HIS A 1 123 ? -8.168  -8.270  12.294  1.00  20.16 ? 123  HIS B CB  1 
ATOM   909  C CG  . HIS A 1 123 ? -8.164  -9.630  12.937  1.00  21.40 ? 123  HIS B CG  1 
ATOM   910  N ND1 . HIS A 1 123 ? -7.594  -10.731 12.348  1.00  30.77 ? 123  HIS B ND1 1 
ATOM   911  C CD2 . HIS A 1 123 ? -8.649  -10.049 14.131  1.00  27.97 ? 123  HIS B CD2 1 
ATOM   912  C CE1 . HIS A 1 123 ? -7.725  -11.781 13.148  1.00  25.34 ? 123  HIS B CE1 1 
ATOM   913  N NE2 . HIS A 1 123 ? -8.358  -11.390 14.235  1.00  28.17 ? 123  HIS B NE2 1 
ATOM   914  N N   . ILE A 1 124 ? -9.741  -10.152 10.052  1.00  14.05 ? 124  ILE B N   1 
ATOM   915  C CA  . ILE A 1 124 ? -11.009 -10.827 9.777   1.00  18.00 ? 124  ILE B CA  1 
ATOM   916  C C   . ILE A 1 124 ? -11.200 -11.992 10.736  1.00  17.95 ? 124  ILE B C   1 
ATOM   917  O O   . ILE A 1 124 ? -10.259 -12.753 10.992  1.00  19.88 ? 124  ILE B O   1 
ATOM   918  C CB  . ILE A 1 124 ? -11.081 -11.378 8.319   1.00  17.94 ? 124  ILE B CB  1 
ATOM   919  C CG1 . ILE A 1 124 ? -10.674 -10.299 7.301   1.00  17.34 ? 124  ILE B CG1 1 
ATOM   920  C CG2 . ILE A 1 124 ? -12.477 -11.925 8.007   1.00  18.96 ? 124  ILE B CG2 1 
ATOM   921  C CD1 . ILE A 1 124 ? -11.557 -9.057  7.326   1.00  18.59 ? 124  ILE B CD1 1 
ATOM   922  N N   . ILE A 1 125 ? -12.404 -12.114 11.283  1.00  14.67 ? 125  ILE B N   1 
ATOM   923  C CA  . ILE A 1 125 ? -12.783 -13.325 11.993  1.00  18.17 ? 125  ILE B CA  1 
ATOM   924  C C   . ILE A 1 125 ? -13.975 -13.925 11.271  1.00  17.09 ? 125  ILE B C   1 
ATOM   925  O O   . ILE A 1 125 ? -14.990 -13.260 11.076  1.00  17.69 ? 125  ILE B O   1 
ATOM   926  C CB  . ILE A 1 125 ? -13.190 -13.055 13.449  1.00  17.40 ? 125  ILE B CB  1 
ATOM   927  C CG1 . ILE A 1 125 ? -12.019 -12.485 14.251  1.00  22.04 ? 125  ILE B CG1 1 
ATOM   928  C CG2 . ILE A 1 125 ? -13.609 -14.363 14.106  1.00  15.78 ? 125  ILE B CG2 1 
ATOM   929  C CD1 . ILE A 1 125 ? -12.432 -11.968 15.637  1.00  21.87 ? 125  ILE B CD1 1 
ATOM   930  N N   . THR A 1 126 ? -13.848 -15.186 10.870  1.00  19.08 ? 126  THR B N   1 
ATOM   931  C CA  . THR A 1 126 ? -14.908 -15.856 10.124  1.00  16.63 ? 126  THR B CA  1 
ATOM   932  C C   . THR A 1 126 ? -15.014 -17.324 10.570  1.00  18.94 ? 126  THR B C   1 
ATOM   933  O O   . THR A 1 126 ? -14.177 -17.816 11.342  1.00  19.45 ? 126  THR B O   1 
ATOM   934  C CB  . THR A 1 126 ? -14.689 -15.727 8.583   1.00  21.61 ? 126  THR B CB  1 
ATOM   935  O OG1 . THR A 1 126 ? -15.859 -16.169 7.884   1.00  25.60 ? 126  THR B OG1 1 
ATOM   936  C CG2 . THR A 1 126 ? -13.525 -16.541 8.137   1.00  19.30 ? 126  THR B CG2 1 
ATOM   937  N N   . MET A 1 127 ? -16.060 -18.015 10.132  1.00  23.16 ? 127  MET B N   1 
ATOM   938  C CA  . MET A 1 127 ? -16.206 -19.427 10.472  1.00  20.63 ? 127  MET B CA  1 
ATOM   939  C C   . MET A 1 127 ? -16.372 -20.306 9.247   1.00  21.61 ? 127  MET B C   1 
ATOM   940  O O   . MET A 1 127 ? -17.204 -20.042 8.382   1.00  21.67 ? 127  MET B O   1 
ATOM   941  C CB  . MET A 1 127 ? -17.384 -19.655 11.429  1.00  22.64 ? 127  MET B CB  1 
ATOM   942  C CG  . MET A 1 127 ? -17.564 -21.135 11.806  1.00  26.64 ? 127  MET B CG  1 
ATOM   943  S SD  . MET A 1 127 ? -18.715 -21.419 13.171  1.00  32.80 ? 127  MET B SD  1 
ATOM   944  C CE  . MET A 1 127 ? -17.683 -20.903 14.534  1.00  27.90 ? 127  MET B CE  1 
ATOM   945  N N   . ASP A 1 128 ? -15.570 -21.365 9.187   1.00  20.59 ? 128  ASP B N   1 
ATOM   946  C CA  . ASP A 1 128 ? -15.666 -22.353 8.127   1.00  22.14 ? 128  ASP B CA  1 
ATOM   947  C C   . ASP A 1 128 ? -15.753 -21.759 6.733   1.00  26.25 ? 128  ASP B C   1 
ATOM   948  O O   . ASP A 1 128 ? -16.763 -21.918 6.037   1.00  21.36 ? 128  ASP B O   1 
ATOM   949  C CB  . ASP A 1 128 ? -16.829 -23.307 8.381   1.00  29.20 ? 128  ASP B CB  1 
ATOM   950  C CG  . ASP A 1 128 ? -16.550 -24.250 9.533   1.00  30.54 ? 128  ASP B CG  1 
ATOM   951  O OD1 . ASP A 1 128 ? -15.472 -24.869 9.540   1.00  29.81 ? 128  ASP B OD1 1 
ATOM   952  O OD2 . ASP A 1 128 ? -17.397 -24.348 10.438  1.00  34.29 ? 128  ASP B OD2 1 
ATOM   953  N N   . LEU A 1 129 ? -14.675 -21.096 6.323   1.00  23.56 ? 129  LEU B N   1 
ATOM   954  C CA  . LEU A 1 129 ? -14.560 -20.624 4.950   1.00  21.14 ? 129  LEU B CA  1 
ATOM   955  C C   . LEU A 1 129 ? -14.808 -21.789 3.985   1.00  23.80 ? 129  LEU B C   1 
ATOM   956  O O   . LEU A 1 129 ? -14.347 -22.916 4.227   1.00  21.83 ? 129  LEU B O   1 
ATOM   957  C CB  . LEU A 1 129 ? -13.167 -20.050 4.713   1.00  24.35 ? 129  LEU B CB  1 
ATOM   958  C CG  . LEU A 1 129 ? -12.917 -18.645 5.269   1.00  22.75 ? 129  LEU B CG  1 
ATOM   959  C CD1 . LEU A 1 129 ? -11.418 -18.298 5.203   1.00  21.60 ? 129  LEU B CD1 1 
ATOM   960  C CD2 . LEU A 1 129 ? -13.766 -17.580 4.542   1.00  22.31 ? 129  LEU B CD2 1 
ATOM   961  N N   . HIS A 1 130 ? -15.546 -21.524 2.912   1.00  22.77 ? 130  HIS B N   1 
ATOM   962  C CA  . HIS A 1 130 ? -15.885 -22.562 1.936   1.00  25.92 ? 130  HIS B CA  1 
ATOM   963  C C   . HIS A 1 130 ? -14.635 -23.221 1.410   1.00  27.72 ? 130  HIS B C   1 
ATOM   964  O O   . HIS A 1 130 ? -14.615 -24.423 1.203   1.00  24.35 ? 130  HIS B O   1 
ATOM   965  C CB  . HIS A 1 130 ? -16.670 -21.969 0.762   1.00  30.57 ? 130  HIS B CB  1 
ATOM   966  C CG  . HIS A 1 130 ? -16.956 -22.951 -0.336  1.00  32.52 ? 130  HIS B CG  1 
ATOM   967  N ND1 . HIS A 1 130 ? -17.872 -23.974 -0.204  1.00  35.10 ? 130  HIS B ND1 1 
ATOM   968  C CD2 . HIS A 1 130 ? -16.453 -23.056 -1.591  1.00  30.44 ? 130  HIS B CD2 1 
ATOM   969  C CE1 . HIS A 1 130 ? -17.926 -24.665 -1.332  1.00  33.85 ? 130  HIS B CE1 1 
ATOM   970  N NE2 . HIS A 1 130 ? -17.072 -24.130 -2.188  1.00  33.49 ? 130  HIS B NE2 1 
ATOM   971  N N   . ALA A 1 131 ? -13.595 -22.420 1.170   1.00  25.89 ? 131  ALA B N   1 
ATOM   972  C CA  . ALA A 1 131 ? -12.280 -22.958 0.821   1.00  26.37 ? 131  ALA B CA  1 
ATOM   973  C C   . ALA A 1 131 ? -11.263 -22.228 1.657   1.00  26.86 ? 131  ALA B C   1 
ATOM   974  O O   . ALA A 1 131 ? -11.258 -21.001 1.685   1.00  26.50 ? 131  ALA B O   1 
ATOM   975  C CB  . ALA A 1 131 ? -11.974 -22.758 -0.663  1.00  26.09 ? 131  ALA B CB  1 
ATOM   976  N N   . SER A 1 132 ? -10.407 -22.987 2.329   1.00  29.31 ? 132  SER B N   1 
ATOM   977  C CA  . SER A 1 132 ? -9.428  -22.428 3.265   1.00  29.90 ? 132  SER B CA  1 
ATOM   978  C C   . SER A 1 132 ? -8.493  -21.452 2.566   1.00  29.74 ? 132  SER B C   1 
ATOM   979  O O   . SER A 1 132 ? -7.973  -20.519 3.196   1.00  25.16 ? 132  SER B O   1 
ATOM   980  C CB  . SER A 1 132 ? -8.615  -23.551 3.908   1.00  29.72 ? 132  SER B CB  1 
ATOM   981  O OG  . SER A 1 132 ? -9.483  -24.422 4.615   1.00  47.40 ? 132  SER B OG  1 
ATOM   982  N N   . GLN A 1 133 ? -8.290  -21.674 1.266   1.00  24.53 ? 133  GLN B N   1 
ATOM   983  C CA  . GLN A 1 133 ? -7.430  -20.810 0.468   1.00  28.13 ? 133  GLN B CA  1 
ATOM   984  C C   . GLN A 1 133 ? -7.908  -19.372 0.477   1.00  24.07 ? 133  GLN B C   1 
ATOM   985  O O   . GLN A 1 133 ? -7.144  -18.476 0.135   1.00  24.40 ? 133  GLN B O   1 
ATOM   986  C CB  . GLN A 1 133 ? -7.305  -21.297 -0.984  1.00  27.71 ? 133  GLN B CB  1 
ATOM   987  C CG  . GLN A 1 133 ? -6.495  -22.578 -1.158  1.00  32.55 ? 133  GLN B CG  1 
ATOM   988  C CD  . GLN A 1 133 ? -7.336  -23.822 -0.970  1.00  35.76 ? 133  GLN B CD  1 
ATOM   989  O OE1 . GLN A 1 133 ? -8.562  -23.743 -0.815  1.00  33.62 ? 133  GLN B OE1 1 
ATOM   990  N NE2 . GLN A 1 133 ? -6.683  -24.983 -0.981  1.00  39.23 ? 133  GLN B NE2 1 
ATOM   991  N N   . ILE A 1 134 ? -9.163  -19.139 0.860   1.00  22.49 ? 134  ILE B N   1 
ATOM   992  C CA  . ILE A 1 134 ? -9.682  -17.771 0.881   1.00  22.32 ? 134  ILE B CA  1 
ATOM   993  C C   . ILE A 1 134 ? -8.898  -16.906 1.879   1.00  23.67 ? 134  ILE B C   1 
ATOM   994  O O   . ILE A 1 134 ? -8.830  -15.681 1.738   1.00  19.09 ? 134  ILE B O   1 
ATOM   995  C CB  . ILE A 1 134 ? -11.198 -17.729 1.194   1.00  23.16 ? 134  ILE B CB  1 
ATOM   996  C CG1 . ILE A 1 134 ? -12.009 -18.325 0.036   1.00  27.87 ? 134  ILE B CG1 1 
ATOM   997  C CG2 . ILE A 1 134 ? -11.657 -16.311 1.478   1.00  20.99 ? 134  ILE B CG2 1 
ATOM   998  C CD1 . ILE A 1 134 ? -13.493 -18.514 0.373   1.00  27.09 ? 134  ILE B CD1 1 
ATOM   999  N N   . GLN A 1 135 ? -8.290  -17.541 2.876   1.00  22.05 ? 135  GLN B N   1 
ATOM   1000 C CA  . GLN A 1 135 ? -7.401  -16.810 3.783   1.00  23.29 ? 135  GLN B CA  1 
ATOM   1001 C C   . GLN A 1 135 ? -6.259  -16.161 3.023   1.00  21.93 ? 135  GLN B C   1 
ATOM   1002 O O   . GLN A 1 135 ? -5.804  -15.088 3.379   1.00  21.71 ? 135  GLN B O   1 
ATOM   1003 C CB  . GLN A 1 135 ? -6.799  -17.742 4.822   1.00  25.41 ? 135  GLN B CB  1 
ATOM   1004 C CG  . GLN A 1 135 ? -7.680  -18.044 5.990   1.00  31.02 ? 135  GLN B CG  1 
ATOM   1005 C CD  . GLN A 1 135 ? -6.850  -18.397 7.222   1.00  34.27 ? 135  GLN B CD  1 
ATOM   1006 O OE1 . GLN A 1 135 ? -5.934  -17.664 7.589   1.00  37.53 ? 135  GLN B OE1 1 
ATOM   1007 N NE2 . GLN A 1 135 ? -7.158  -19.520 7.850   1.00  32.85 ? 135  GLN B NE2 1 
ATOM   1008 N N   . GLY A 1 136 ? -5.766  -16.849 1.995   1.00  21.20 ? 136  GLY B N   1 
ATOM   1009 C CA  . GLY A 1 136 ? -4.768  -16.288 1.096   1.00  22.75 ? 136  GLY B CA  1 
ATOM   1010 C C   . GLY A 1 136 ? -5.220  -15.121 0.230   1.00  19.66 ? 136  GLY B C   1 
ATOM   1011 O O   . GLY A 1 136 ? -4.396  -14.466 -0.395  1.00  21.93 ? 136  GLY B O   1 
ATOM   1012 N N   . PHE A 1 137 ? -6.521  -14.836 0.198   1.00  19.89 ? 137  PHE B N   1 
ATOM   1013 C CA  . PHE A 1 137 ? -7.014  -13.715 -0.612  1.00  19.85 ? 137  PHE B CA  1 
ATOM   1014 C C   . PHE A 1 137 ? -6.751  -12.382 0.062   1.00  21.93 ? 137  PHE B C   1 
ATOM   1015 O O   . PHE A 1 137 ? -6.938  -11.344 -0.556  1.00  19.27 ? 137  PHE B O   1 
ATOM   1016 C CB  . PHE A 1 137 ? -8.516  -13.847 -0.890  1.00  23.36 ? 137  PHE B CB  1 
ATOM   1017 C CG  . PHE A 1 137 ? -8.857  -14.960 -1.831  1.00  20.19 ? 137  PHE B CG  1 
ATOM   1018 C CD1 . PHE A 1 137 ? -10.175 -15.259 -2.129  1.00  21.71 ? 137  PHE B CD1 1 
ATOM   1019 C CD2 . PHE A 1 137 ? -7.854  -15.705 -2.428  1.00  20.95 ? 137  PHE B CD2 1 
ATOM   1020 C CE1 . PHE A 1 137 ? -10.486 -16.288 -2.998  1.00  22.71 ? 137  PHE B CE1 1 
ATOM   1021 C CE2 . PHE A 1 137 ? -8.155  -16.729 -3.290  1.00  21.25 ? 137  PHE B CE2 1 
ATOM   1022 C CZ  . PHE A 1 137 ? -9.469  -17.027 -3.577  1.00  22.50 ? 137  PHE B CZ  1 
ATOM   1023 N N   . PHE A 1 138 ? -6.351  -12.429 1.339   1.00  18.97 ? 138  PHE B N   1 
ATOM   1024 C CA  . PHE A 1 138 ? -6.025  -11.244 2.132   1.00  18.79 ? 138  PHE B CA  1 
ATOM   1025 C C   . PHE A 1 138 ? -4.513  -11.164 2.378   1.00  19.40 ? 138  PHE B C   1 
ATOM   1026 O O   . PHE A 1 138 ? -3.810  -12.176 2.263   1.00  18.42 ? 138  PHE B O   1 
ATOM   1027 C CB  . PHE A 1 138 ? -6.712  -11.321 3.513   1.00  19.67 ? 138  PHE B CB  1 
ATOM   1028 C CG  . PHE A 1 138 ? -8.219  -11.304 3.459   1.00  19.00 ? 138  PHE B CG  1 
ATOM   1029 C CD1 . PHE A 1 138 ? -8.936  -12.478 3.275   1.00  19.73 ? 138  PHE B CD1 1 
ATOM   1030 C CD2 . PHE A 1 138 ? -8.914  -10.105 3.590   1.00  18.60 ? 138  PHE B CD2 1 
ATOM   1031 C CE1 . PHE A 1 138 ? -10.321 -12.453 3.243   1.00  21.76 ? 138  PHE B CE1 1 
ATOM   1032 C CE2 . PHE A 1 138 ? -10.303 -10.071 3.560   1.00  17.91 ? 138  PHE B CE2 1 
ATOM   1033 C CZ  . PHE A 1 138 ? -11.002 -11.248 3.386   1.00  16.28 ? 138  PHE B CZ  1 
ATOM   1034 N N   . ASP A 1 139 ? -4.020  -9.990  2.759   0.50  13.53 ? 139  ASP B N   1 
ATOM   1035 C CA  . ASP A 1 139 ? -2.685  -9.905  3.326   0.50  17.79 ? 139  ASP B CA  1 
ATOM   1036 C C   . ASP A 1 139 ? -2.754  -9.648  4.846   0.50  18.47 ? 139  ASP B C   1 
ATOM   1037 O O   . ASP A 1 139 ? -1.803  -9.910  5.574   0.50  23.31 ? 139  ASP B O   1 
ATOM   1038 C CB  . ASP A 1 139 ? -1.838  -8.851  2.611   0.50  20.38 ? 139  ASP B CB  1 
ATOM   1039 C CG  . ASP A 1 139 ? -1.340  -9.327  1.252   0.50  22.16 ? 139  ASP B CG  1 
ATOM   1040 O OD1 . ASP A 1 139 ? -0.892  -10.490 1.140   0.50  17.09 ? 139  ASP B OD1 1 
ATOM   1041 O OD2 . ASP A 1 139 ? -1.408  -8.528  0.299   0.50  22.91 ? 139  ASP B OD2 1 
ATOM   1042 N N   . ILE A 1 140 ? -3.898  -9.157  5.306   1.00  21.51 ? 140  ILE B N   1 
ATOM   1043 C CA  . ILE A 1 140 ? -4.160  -8.980  6.739   1.00  19.08 ? 140  ILE B CA  1 
ATOM   1044 C C   . ILE A 1 140 ? -4.479  -10.337 7.344   1.00  18.48 ? 140  ILE B C   1 
ATOM   1045 O O   . ILE A 1 140 ? -4.857  -11.265 6.634   1.00  18.33 ? 140  ILE B O   1 
ATOM   1046 C CB  . ILE A 1 140 ? -5.348  -8.034  6.996   1.00  18.04 ? 140  ILE B CB  1 
ATOM   1047 C CG1 . ILE A 1 140 ? -6.605  -8.531  6.272   1.00  19.57 ? 140  ILE B CG1 1 
ATOM   1048 C CG2 . ILE A 1 140 ? -5.000  -6.582  6.581   1.00  19.35 ? 140  ILE B CG2 1 
ATOM   1049 C CD1 . ILE A 1 140 ? -7.873  -7.705  6.564   1.00  19.71 ? 140  ILE B CD1 1 
ATOM   1050 N N   . PRO A 1 141 ? -4.327  -10.464 8.671   1.00  22.07 ? 141  PRO B N   1 
ATOM   1051 C CA  . PRO A 1 141 ? -4.660  -11.762 9.256   1.00  19.67 ? 141  PRO B CA  1 
ATOM   1052 C C   . PRO A 1 141 ? -6.143  -12.092 9.240   1.00  21.36 ? 141  PRO B C   1 
ATOM   1053 O O   . PRO A 1 141 ? -7.007  -11.233 9.408   1.00  20.04 ? 141  PRO B O   1 
ATOM   1054 C CB  . PRO A 1 141 ? -4.115  -11.672 10.694  1.00  25.79 ? 141  PRO B CB  1 
ATOM   1055 C CG  . PRO A 1 141 ? -3.839  -10.253 10.944  1.00  24.19 ? 141  PRO B CG  1 
ATOM   1056 C CD  . PRO A 1 141 ? -3.685  -9.548  9.631   1.00  23.52 ? 141  PRO B CD  1 
ATOM   1057 N N   . VAL A 1 142 ? -6.413  -13.374 9.032   1.00  19.94 ? 142  VAL B N   1 
ATOM   1058 C CA  . VAL A 1 142 ? -7.753  -13.925 9.095   1.00  20.99 ? 142  VAL B CA  1 
ATOM   1059 C C   . VAL A 1 142 ? -7.772  -15.082 10.111  1.00  23.61 ? 142  VAL B C   1 
ATOM   1060 O O   . VAL A 1 142 ? -6.937  -15.969 10.066  1.00  23.90 ? 142  VAL B O   1 
ATOM   1061 C CB  . VAL A 1 142 ? -8.150  -14.507 7.730   1.00  23.72 ? 142  VAL B CB  1 
ATOM   1062 C CG1 . VAL A 1 142 ? -9.549  -15.158 7.802   1.00  19.34 ? 142  VAL B CG1 1 
ATOM   1063 C CG2 . VAL A 1 142 ? -8.037  -13.431 6.593   1.00  17.65 ? 142  VAL B CG2 1 
ATOM   1064 N N   . ASP A 1 143 ? -8.709  -15.063 11.041  1.00  20.39 ? 143  ASP B N   1 
ATOM   1065 C CA  . ASP A 1 143 ? -8.926  -16.232 11.876  1.00  21.27 ? 143  ASP B CA  1 
ATOM   1066 C C   . ASP A 1 143 ? -10.167 -16.938 11.353  1.00  21.06 ? 143  ASP B C   1 
ATOM   1067 O O   . ASP A 1 143 ? -11.255 -16.388 11.380  1.00  21.35 ? 143  ASP B O   1 
ATOM   1068 C CB  . ASP A 1 143 ? -9.068  -15.829 13.336  1.00  26.24 ? 143  ASP B CB  1 
ATOM   1069 C CG  . ASP A 1 143 ? -7.776  -15.289 13.898  1.00  25.33 ? 143  ASP B CG  1 
ATOM   1070 O OD1 . ASP A 1 143 ? -6.712  -15.873 13.601  1.00  25.52 ? 143  ASP B OD1 1 
ATOM   1071 O OD2 . ASP A 1 143 ? -7.826  -14.271 14.598  1.00  25.61 ? 143  ASP B OD2 1 
ATOM   1072 N N   . ASN A 1 144 ? -9.953  -18.126 10.808  1.00  18.89 ? 144  ASN B N   1 
ATOM   1073 C CA  . ASN A 1 144 ? -10.991 -18.974 10.250  1.00  22.88 ? 144  ASN B CA  1 
ATOM   1074 C C   . ASN A 1 144 ? -11.349 -20.026 11.311  1.00  25.58 ? 144  ASN B C   1 
ATOM   1075 O O   . ASN A 1 144 ? -10.636 -21.014 11.506  1.00  21.71 ? 144  ASN B O   1 
ATOM   1076 C CB  . ASN A 1 144 ? -10.475 -19.633 8.959   1.00  24.28 ? 144  ASN B CB  1 
ATOM   1077 C CG  . ASN A 1 144 ? -11.511 -20.515 8.280   1.00  24.22 ? 144  ASN B CG  1 
ATOM   1078 O OD1 . ASN A 1 144 ? -12.708 -20.243 8.328   1.00  21.62 ? 144  ASN B OD1 1 
ATOM   1079 N ND2 . ASN A 1 144 ? -11.046 -21.588 7.647   1.00  26.82 ? 144  ASN B ND2 1 
ATOM   1080 N N   . LEU A 1 145 ? -12.440 -19.782 12.027  1.00  20.67 ? 145  LEU B N   1 
ATOM   1081 C CA  . LEU A 1 145 ? -12.840 -20.671 13.108  1.00  23.73 ? 145  LEU B CA  1 
ATOM   1082 C C   . LEU A 1 145 ? -13.571 -21.882 12.544  1.00  25.95 ? 145  LEU B C   1 
ATOM   1083 O O   . LEU A 1 145 ? -14.110 -21.834 11.438  1.00  23.56 ? 145  LEU B O   1 
ATOM   1084 C CB  . LEU A 1 145 ? -13.748 -19.937 14.083  1.00  19.39 ? 145  LEU B CB  1 
ATOM   1085 C CG  . LEU A 1 145 ? -13.258 -18.607 14.640  1.00  23.57 ? 145  LEU B CG  1 
ATOM   1086 C CD1 . LEU A 1 145 ? -14.413 -17.871 15.275  1.00  21.26 ? 145  LEU B CD1 1 
ATOM   1087 C CD2 . LEU A 1 145 ? -12.153 -18.867 15.640  1.00  30.09 ? 145  LEU B CD2 1 
ATOM   1088 N N   . TYR A 1 146 ? -13.595 -22.970 13.306  0.60  26.48 ? 146  TYR B N   1 
ATOM   1089 C CA  . TYR A 1 146 ? -14.290 -24.181 12.868  0.60  25.15 ? 146  TYR B CA  1 
ATOM   1090 C C   . TYR A 1 146 ? -15.499 -24.529 13.704  0.60  30.61 ? 146  TYR B C   1 
ATOM   1091 O O   . TYR A 1 146 ? -15.497 -24.371 14.919  0.60  24.63 ? 146  TYR B O   1 
ATOM   1092 C CB  . TYR A 1 146 ? -13.335 -25.354 12.848  0.60  28.30 ? 146  TYR B CB  1 
ATOM   1093 C CG  . TYR A 1 146 ? -12.148 -25.088 11.974  0.60  35.58 ? 146  TYR B CG  1 
ATOM   1094 C CD1 . TYR A 1 146 ? -10.926 -24.730 12.529  0.60  39.16 ? 146  TYR B CD1 1 
ATOM   1095 C CD2 . TYR A 1 146 ? -12.254 -25.149 10.592  0.60  34.19 ? 146  TYR B CD2 1 
ATOM   1096 C CE1 . TYR A 1 146 ? -9.839  -24.473 11.733  0.60  41.50 ? 146  TYR B CE1 1 
ATOM   1097 C CE2 . TYR A 1 146 ? -11.169 -24.896 9.785   0.60  35.91 ? 146  TYR B CE2 1 
ATOM   1098 C CZ  . TYR A 1 146 ? -9.967  -24.563 10.365  0.60  40.08 ? 146  TYR B CZ  1 
ATOM   1099 O OH  . TYR A 1 146 ? -8.876  -24.312 9.579   0.60  49.78 ? 146  TYR B OH  1 
ATOM   1100 N N   . ALA A 1 147 ? -16.544 -25.007 13.036  1.00  29.27 ? 147  ALA B N   1 
ATOM   1101 C CA  . ALA A 1 147 ? -17.710 -25.496 13.747  1.00  32.74 ? 147  ALA B CA  1 
ATOM   1102 C C   . ALA A 1 147 ? -17.471 -26.942 14.203  1.00  27.88 ? 147  ALA B C   1 
ATOM   1103 O O   . ALA A 1 147 ? -18.200 -27.460 15.039  1.00  28.82 ? 147  ALA B O   1 
ATOM   1104 C CB  . ALA A 1 147 ? -18.936 -25.414 12.857  1.00  30.15 ? 147  ALA B CB  1 
ATOM   1105 N N   . GLU A 1 148 ? -16.435 -27.566 13.659  1.00  25.65 ? 148  GLU B N   1 
ATOM   1106 C CA  . GLU A 1 148 ? -16.172 -28.991 13.875  1.00  30.50 ? 148  GLU B CA  1 
ATOM   1107 C C   . GLU A 1 148 ? -16.222 -29.444 15.339  1.00  30.61 ? 148  GLU B C   1 
ATOM   1108 O O   . GLU A 1 148 ? -16.881 -30.426 15.650  1.00  27.53 ? 148  GLU B O   1 
ATOM   1109 C CB  . GLU A 1 148 ? -14.868 -29.440 13.201  1.00  29.85 ? 148  GLU B CB  1 
ATOM   1110 C CG  . GLU A 1 148 ? -14.554 -30.909 13.439  1.00  32.60 ? 148  GLU B CG  1 
ATOM   1111 C CD  . GLU A 1 148 ? -13.378 -31.433 12.635  1.00  44.49 ? 148  GLU B CD  1 
ATOM   1112 O OE1 . GLU A 1 148 ? -13.157 -30.971 11.496  1.00  51.67 ? 148  GLU B OE1 1 
ATOM   1113 O OE2 . GLU A 1 148 ? -12.684 -32.339 13.137  1.00  46.29 ? 148  GLU B OE2 1 
ATOM   1114 N N   . PRO A 1 149 ? -15.541 -28.723 16.248  1.00  30.08 ? 149  PRO B N   1 
ATOM   1115 C CA  . PRO A 1 149 ? -15.652 -29.164 17.645  1.00  30.95 ? 149  PRO B CA  1 
ATOM   1116 C C   . PRO A 1 149 ? -17.106 -29.183 18.118  1.00  32.05 ? 149  PRO B C   1 
ATOM   1117 O O   . PRO A 1 149 ? -17.516 -30.147 18.752  1.00  29.54 ? 149  PRO B O   1 
ATOM   1118 C CB  . PRO A 1 149 ? -14.826 -28.117 18.408  1.00  36.08 ? 149  PRO B CB  1 
ATOM   1119 C CG  . PRO A 1 149 ? -13.801 -27.673 17.395  1.00  36.75 ? 149  PRO B CG  1 
ATOM   1120 C CD  . PRO A 1 149 ? -14.574 -27.619 16.094  1.00  29.73 ? 149  PRO B CD  1 
ATOM   1121 N N   . ALA A 1 150 ? -17.882 -28.155 17.787  1.00  27.50 ? 150  ALA B N   1 
ATOM   1122 C CA  . ALA A 1 150 ? -19.284 -28.104 18.196  1.00  29.10 ? 150  ALA B CA  1 
ATOM   1123 C C   . ALA A 1 150 ? -20.136 -29.172 17.492  1.00  27.66 ? 150  ALA B C   1 
ATOM   1124 O O   . ALA A 1 150 ? -21.104 -29.691 18.065  1.00  28.09 ? 150  ALA B O   1 
ATOM   1125 C CB  . ALA A 1 150 ? -19.864 -26.707 17.966  1.00  29.11 ? 150  ALA B CB  1 
ATOM   1126 N N   . VAL A 1 151 ? -19.765 -29.499 16.261  1.00  27.16 ? 151  VAL B N   1 
ATOM   1127 C CA  . VAL A 1 151 ? -20.450 -30.533 15.492  1.00  28.88 ? 151  VAL B CA  1 
ATOM   1128 C C   . VAL A 1 151 ? -20.174 -31.946 16.054  1.00  26.74 ? 151  VAL B C   1 
ATOM   1129 O O   . VAL A 1 151 ? -21.088 -32.753 16.224  1.00  25.93 ? 151  VAL B O   1 
ATOM   1130 C CB  . VAL A 1 151 ? -20.040 -30.470 14.022  1.00  25.00 ? 151  VAL B CB  1 
ATOM   1131 C CG1 . VAL A 1 151 ? -20.511 -31.701 13.279  1.00  24.16 ? 151  VAL B CG1 1 
ATOM   1132 C CG2 . VAL A 1 151 ? -20.586 -29.180 13.365  1.00  23.29 ? 151  VAL B CG2 1 
ATOM   1133 N N   . LEU A 1 152 ? -18.912 -32.236 16.332  1.00  26.79 ? 152  LEU B N   1 
ATOM   1134 C CA  . LEU A 1 152 ? -18.548 -33.506 16.975  1.00  29.78 ? 152  LEU B CA  1 
ATOM   1135 C C   . LEU A 1 152 ? -19.277 -33.703 18.301  1.00  30.33 ? 152  LEU B C   1 
ATOM   1136 O O   . LEU A 1 152 ? -19.815 -34.779 18.576  1.00  30.00 ? 152  LEU B O   1 
ATOM   1137 C CB  . LEU A 1 152 ? -17.043 -33.558 17.206  1.00  30.10 ? 152  LEU B CB  1 
ATOM   1138 C CG  . LEU A 1 152 ? -16.202 -33.636 15.933  1.00  31.65 ? 152  LEU B CG  1 
ATOM   1139 C CD1 . LEU A 1 152 ? -14.730 -33.374 16.232  1.00  34.51 ? 152  LEU B CD1 1 
ATOM   1140 C CD2 . LEU A 1 152 ? -16.394 -34.982 15.256  1.00  31.56 ? 152  LEU B CD2 1 
ATOM   1141 N N   . LYS A 1 153 ? -19.285 -32.664 19.131  1.00  29.22 ? 153  LYS B N   1 
ATOM   1142 C CA  . LYS A 1 153 ? -20.009 -32.712 20.391  1.00  30.71 ? 153  LYS B CA  1 
ATOM   1143 C C   . LYS A 1 153 ? -21.487 -32.998 20.169  1.00  31.97 ? 153  LYS B C   1 
ATOM   1144 O O   . LYS A 1 153 ? -22.072 -33.847 20.858  1.00  28.92 ? 153  LYS B O   1 
ATOM   1145 C CB  . LYS A 1 153 ? -19.836 -31.410 21.175  1.00  35.23 ? 153  LYS B CB  1 
ATOM   1146 C CG  . LYS A 1 153 ? -20.671 -31.326 22.443  1.00  33.66 ? 153  LYS B CG  1 
ATOM   1147 C CD  . LYS A 1 153 ? -20.357 -30.035 23.205  1.00  40.85 ? 153  LYS B CD  1 
ATOM   1148 C CE  . LYS A 1 153 ? -21.130 -29.930 24.511  1.00  41.40 ? 153  LYS B CE  1 
ATOM   1149 N NZ  . LYS A 1 153 ? -22.553 -29.553 24.279  1.00  48.64 ? 153  LYS B NZ  1 
ATOM   1150 N N   . TRP A 1 154 ? -22.097 -32.306 19.209  1.00  28.87 ? 154  TRP B N   1 
ATOM   1151 C CA  . TRP A 1 154 ? -23.510 -32.523 18.909  1.00  25.63 ? 154  TRP B CA  1 
ATOM   1152 C C   . TRP A 1 154 ? -23.759 -33.982 18.474  1.00  28.79 ? 154  TRP B C   1 
ATOM   1153 O O   . TRP A 1 154 ? -24.722 -34.607 18.903  1.00  29.03 ? 154  TRP B O   1 
ATOM   1154 C CB  . TRP A 1 154 ? -24.028 -31.556 17.830  1.00  27.62 ? 154  TRP B CB  1 
ATOM   1155 C CG  . TRP A 1 154 ? -25.521 -31.614 17.673  1.00  27.87 ? 154  TRP B CG  1 
ATOM   1156 C CD1 . TRP A 1 154 ? -26.436 -30.741 18.209  1.00  29.21 ? 154  TRP B CD1 1 
ATOM   1157 C CD2 . TRP A 1 154 ? -26.286 -32.612 16.971  1.00  29.86 ? 154  TRP B CD2 1 
ATOM   1158 N NE1 . TRP A 1 154 ? -27.713 -31.121 17.859  1.00  29.62 ? 154  TRP B NE1 1 
ATOM   1159 C CE2 . TRP A 1 154 ? -27.648 -32.266 17.107  1.00  28.96 ? 154  TRP B CE2 1 
ATOM   1160 C CE3 . TRP A 1 154 ? -25.950 -33.751 16.221  1.00  30.02 ? 154  TRP B CE3 1 
ATOM   1161 C CZ2 . TRP A 1 154 ? -28.675 -33.026 16.539  1.00  28.25 ? 154  TRP B CZ2 1 
ATOM   1162 C CZ3 . TRP A 1 154 ? -26.977 -34.504 15.658  1.00  28.95 ? 154  TRP B CZ3 1 
ATOM   1163 C CH2 . TRP A 1 154 ? -28.323 -34.134 15.823  1.00  26.87 ? 154  TRP B CH2 1 
ATOM   1164 N N   . ILE A 1 155 ? -22.891 -34.508 17.621  1.00  27.94 ? 155  ILE B N   1 
ATOM   1165 C CA  . ILE A 1 155 ? -23.047 -35.875 17.135  1.00  28.00 ? 155  ILE B CA  1 
ATOM   1166 C C   . ILE A 1 155 ? -22.961 -36.844 18.321  1.00  30.61 ? 155  ILE B C   1 
ATOM   1167 O O   . ILE A 1 155 ? -23.873 -37.638 18.563  1.00  27.54 ? 155  ILE B O   1 
ATOM   1168 C CB  . ILE A 1 155 ? -21.976 -36.229 16.089  1.00  27.45 ? 155  ILE B CB  1 
ATOM   1169 C CG1 . ILE A 1 155 ? -22.282 -35.537 14.758  1.00  27.25 ? 155  ILE B CG1 1 
ATOM   1170 C CG2 . ILE A 1 155 ? -21.917 -37.735 15.870  1.00  28.43 ? 155  ILE B CG2 1 
ATOM   1171 C CD1 . ILE A 1 155 ? -21.117 -35.551 13.772  1.00  25.37 ? 155  ILE B CD1 1 
ATOM   1172 N N   . ARG A 1 156 ? -21.873 -36.754 19.075  1.00  28.63 ? 156  ARG B N   1 
ATOM   1173 C CA  . ARG A 1 156 ? -21.715 -37.620 20.243  1.00  35.72 ? 156  ARG B CA  1 
ATOM   1174 C C   . ARG A 1 156 ? -22.873 -37.532 21.241  1.00  30.18 ? 156  ARG B C   1 
ATOM   1175 O O   . ARG A 1 156 ? -23.201 -38.525 21.879  1.00  38.91 ? 156  ARG B O   1 
ATOM   1176 C CB  . ARG A 1 156 ? -20.389 -37.357 20.947  1.00  35.34 ? 156  ARG B CB  1 
ATOM   1177 C CG  . ARG A 1 156 ? -19.170 -37.709 20.116  1.00  32.90 ? 156  ARG B CG  1 
ATOM   1178 C CD  . ARG A 1 156 ? -17.931 -37.606 20.985  1.00  36.41 ? 156  ARG B CD  1 
ATOM   1179 N NE  . ARG A 1 156 ? -16.709 -37.984 20.285  1.00  37.84 ? 156  ARG B NE  1 
ATOM   1180 C CZ  . ARG A 1 156 ? -15.803 -37.115 19.847  1.00  43.42 ? 156  ARG B CZ  1 
ATOM   1181 N NH1 . ARG A 1 156 ? -15.988 -35.818 20.032  1.00  41.47 ? 156  ARG B NH1 1 
ATOM   1182 N NH2 . ARG A 1 156 ? -14.710 -37.540 19.232  1.00  37.00 ? 156  ARG B NH2 1 
ATOM   1183 N N   . GLU A 1 157 ? -23.508 -36.374 21.380  0.40  25.89 ? 157  GLU B N   1 
ATOM   1184 C CA  . GLU A 1 157 ? -24.578 -36.248 22.371  0.40  27.72 ? 157  GLU B CA  1 
ATOM   1185 C C   . GLU A 1 157 ? -25.996 -36.496 21.835  0.40  27.97 ? 157  GLU B C   1 
ATOM   1186 O O   . GLU A 1 157 ? -26.945 -36.584 22.613  0.40  23.50 ? 157  GLU B O   1 
ATOM   1187 C CB  . GLU A 1 157 ? -24.503 -34.895 23.090  0.40  28.58 ? 157  GLU B CB  1 
ATOM   1188 C CG  . GLU A 1 157 ? -24.905 -33.719 22.226  0.40  32.46 ? 157  GLU B CG  1 
ATOM   1189 C CD  . GLU A 1 157 ? -24.810 -32.385 22.947  0.40  33.77 ? 157  GLU B CD  1 
ATOM   1190 O OE1 . GLU A 1 157 ? -25.543 -31.453 22.553  0.40  31.56 ? 157  GLU B OE1 1 
ATOM   1191 O OE2 . GLU A 1 157 ? -24.002 -32.264 23.896  0.40  32.81 ? 157  GLU B OE2 1 
ATOM   1192 N N   . ASN A 1 158 ? -26.141 -36.622 20.517  1.00  28.60 ? 158  ASN B N   1 
ATOM   1193 C CA  . ASN A 1 158 ? -27.469 -36.722 19.907  1.00  30.08 ? 158  ASN B CA  1 
ATOM   1194 C C   . ASN A 1 158 ? -27.702 -37.962 19.062  1.00  31.18 ? 158  ASN B C   1 
ATOM   1195 O O   . ASN A 1 158 ? -28.843 -38.301 18.769  1.00  33.11 ? 158  ASN B O   1 
ATOM   1196 C CB  . ASN A 1 158 ? -27.765 -35.489 19.045  1.00  31.89 ? 158  ASN B CB  1 
ATOM   1197 C CG  . ASN A 1 158 ? -27.991 -34.251 19.868  1.00  34.96 ? 158  ASN B CG  1 
ATOM   1198 O OD1 . ASN A 1 158 ? -29.098 -33.997 20.331  1.00  37.57 ? 158  ASN B OD1 1 
ATOM   1199 N ND2 . ASN A 1 158 ? -26.944 -33.465 20.050  1.00  32.59 ? 158  ASN B ND2 1 
ATOM   1200 N N   . ILE A 1 159 ? -26.629 -38.612 18.629  1.00  26.62 ? 159  ILE B N   1 
ATOM   1201 C CA  . ILE A 1 159 ? -26.764 -39.806 17.807  1.00  30.06 ? 159  ILE B CA  1 
ATOM   1202 C C   . ILE A 1 159 ? -26.209 -41.014 18.554  1.00  29.84 ? 159  ILE B C   1 
ATOM   1203 O O   . ILE A 1 159 ? -25.008 -41.128 18.737  1.00  28.61 ? 159  ILE B O   1 
ATOM   1204 C CB  . ILE A 1 159 ? -26.063 -39.647 16.443  1.00  30.91 ? 159  ILE B CB  1 
ATOM   1205 C CG1 . ILE A 1 159 ? -26.654 -38.445 15.699  1.00  29.32 ? 159  ILE B CG1 1 
ATOM   1206 C CG2 . ILE A 1 159 ? -26.205 -40.927 15.616  1.00  29.63 ? 159  ILE B CG2 1 
ATOM   1207 C CD1 . ILE A 1 159 ? -25.941 -38.096 14.429  1.00  29.22 ? 159  ILE B CD1 1 
ATOM   1208 N N   . SER A 1 160 ? -27.104 -41.895 19.001  1.00  34.06 ? 160  SER B N   1 
ATOM   1209 C CA  . SER A 1 160 ? -26.735 -43.065 19.806  1.00  36.77 ? 160  SER B CA  1 
ATOM   1210 C C   . SER A 1 160 ? -25.679 -43.921 19.125  1.00  32.69 ? 160  SER B C   1 
ATOM   1211 O O   . SER A 1 160 ? -24.731 -44.397 19.763  1.00  31.18 ? 160  SER B O   1 
ATOM   1212 C CB  . SER A 1 160 ? -27.978 -43.924 20.089  1.00  38.40 ? 160  SER B CB  1 
ATOM   1213 O OG  . SER A 1 160 ? -29.076 -43.115 20.488  1.00  44.73 ? 160  SER B OG  1 
ATOM   1214 N N   . GLU A 1 161 ? -25.842 -44.092 17.819  1.00  31.49 ? 161  GLU B N   1 
ATOM   1215 C CA  . GLU A 1 161 ? -25.008 -44.994 17.041  1.00  31.62 ? 161  GLU B CA  1 
ATOM   1216 C C   . GLU A 1 161 ? -23.795 -44.313 16.420  1.00  32.69 ? 161  GLU B C   1 
ATOM   1217 O O   . GLU A 1 161 ? -23.292 -44.780 15.400  1.00  28.97 ? 161  GLU B O   1 
ATOM   1218 C CB  . GLU A 1 161 ? -25.834 -45.634 15.914  1.00  31.52 ? 161  GLU B CB  1 
ATOM   1219 C CG  . GLU A 1 161 ? -27.151 -46.226 16.364  1.00  33.00 ? 161  GLU B CG  1 
ATOM   1220 C CD  . GLU A 1 161 ? -28.318 -45.258 16.234  1.00  37.11 ? 161  GLU B CD  1 
ATOM   1221 O OE1 . GLU A 1 161 ? -28.118 -44.027 16.373  1.00  36.88 ? 161  GLU B OE1 1 
ATOM   1222 O OE2 . GLU A 1 161 ? -29.442 -45.736 15.979  1.00  44.52 ? 161  GLU B OE2 1 
ATOM   1223 N N   . TRP A 1 162 ? -23.329 -43.212 17.010  1.00  33.73 ? 162  TRP B N   1 
ATOM   1224 C CA  . TRP A 1 162 ? -22.245 -42.456 16.369  1.00  31.21 ? 162  TRP B CA  1 
ATOM   1225 C C   . TRP A 1 162 ? -20.961 -43.262 16.185  1.00  33.83 ? 162  TRP B C   1 
ATOM   1226 O O   . TRP A 1 162 ? -20.229 -43.068 15.202  1.00  32.06 ? 162  TRP B O   1 
ATOM   1227 C CB  . TRP A 1 162 ? -21.960 -41.121 17.080  1.00  33.30 ? 162  TRP B CB  1 
ATOM   1228 C CG  . TRP A 1 162 ? -21.398 -41.204 18.477  1.00  28.64 ? 162  TRP B CG  1 
ATOM   1229 C CD1 . TRP A 1 162 ? -22.101 -41.125 19.649  1.00  31.54 ? 162  TRP B CD1 1 
ATOM   1230 C CD2 . TRP A 1 162 ? -20.014 -41.331 18.848  1.00  34.37 ? 162  TRP B CD2 1 
ATOM   1231 N NE1 . TRP A 1 162 ? -21.244 -41.210 20.718  1.00  28.42 ? 162  TRP B NE1 1 
ATOM   1232 C CE2 . TRP A 1 162 ? -19.960 -41.337 20.259  1.00  32.04 ? 162  TRP B CE2 1 
ATOM   1233 C CE3 . TRP A 1 162 ? -18.818 -41.449 18.125  1.00  29.48 ? 162  TRP B CE3 1 
ATOM   1234 C CZ2 . TRP A 1 162 ? -18.757 -41.463 20.961  1.00  35.26 ? 162  TRP B CZ2 1 
ATOM   1235 C CZ3 . TRP A 1 162 ? -17.626 -41.571 18.825  1.00  32.76 ? 162  TRP B CZ3 1 
ATOM   1236 C CH2 . TRP A 1 162 ? -17.604 -41.573 20.226  1.00  31.14 ? 162  TRP B CH2 1 
ATOM   1237 N N   . ARG A 1 163 ? -20.691 -44.177 17.112  1.00  30.39 ? 163  ARG B N   1 
ATOM   1238 C CA  . ARG A 1 163 ? -19.505 -45.015 17.001  1.00  31.02 ? 163  ARG B CA  1 
ATOM   1239 C C   . ARG A 1 163 ? -19.552 -45.941 15.803  1.00  30.69 ? 163  ARG B C   1 
ATOM   1240 O O   . ARG A 1 163 ? -18.515 -46.452 15.382  1.00  33.12 ? 163  ARG B O   1 
ATOM   1241 C CB  . ARG A 1 163 ? -19.273 -45.821 18.275  1.00  30.30 ? 163  ARG B CB  1 
ATOM   1242 C CG  . ARG A 1 163 ? -18.946 -44.967 19.468  1.00  31.03 ? 163  ARG B CG  1 
ATOM   1243 C CD  . ARG A 1 163 ? -18.818 -45.835 20.710  1.00  33.91 ? 163  ARG B CD  1 
ATOM   1244 N NE  . ARG A 1 163 ? -18.706 -45.029 21.922  1.00  30.45 ? 163  ARG B NE  1 
ATOM   1245 C CZ  . ARG A 1 163 ? -19.730 -44.428 22.520  1.00  34.52 ? 163  ARG B CZ  1 
ATOM   1246 N NH1 . ARG A 1 163 ? -20.957 -44.513 22.008  1.00  33.35 ? 163  ARG B NH1 1 
ATOM   1247 N NH2 . ARG A 1 163 ? -19.524 -43.728 23.632  1.00  37.03 ? 163  ARG B NH2 1 
ATOM   1248 N N   . ASN A 1 164 ? -20.743 -46.147 15.248  1.00  29.32 ? 164  ASN B N   1 
ATOM   1249 C CA  . ASN A 1 164 ? -20.893 -46.997 14.067  1.00  33.84 ? 164  ASN B CA  1 
ATOM   1250 C C   . ASN A 1 164 ? -21.483 -46.307 12.837  1.00  35.54 ? 164  ASN B C   1 
ATOM   1251 O O   . ASN A 1 164 ? -21.993 -46.979 11.940  1.00  37.01 ? 164  ASN B O   1 
ATOM   1252 C CB  . ASN A 1 164 ? -21.759 -48.217 14.395  1.00  34.90 ? 164  ASN B CB  1 
ATOM   1253 C CG  . ASN A 1 164 ? -21.027 -49.231 15.223  1.00  35.73 ? 164  ASN B CG  1 
ATOM   1254 O OD1 . ASN A 1 164 ? -20.355 -50.116 14.683  1.00  39.27 ? 164  ASN B OD1 1 
ATOM   1255 N ND2 . ASN A 1 164 ? -21.131 -49.105 16.547  1.00  31.15 ? 164  ASN B ND2 1 
ATOM   1256 N N   . CYS A 1 165 ? -21.435 -44.980 12.788  1.00  30.54 ? 165  CYS B N   1 
ATOM   1257 C CA  . CYS A 1 165 ? -22.077 -44.279 11.692  1.00  29.53 ? 165  CYS B CA  1 
ATOM   1258 C C   . CYS A 1 165 ? -21.110 -44.087 10.536  1.00  28.10 ? 165  CYS B C   1 
ATOM   1259 O O   . CYS A 1 165 ? -19.955 -44.498 10.604  1.00  28.69 ? 165  CYS B O   1 
ATOM   1260 C CB  . CYS A 1 165 ? -22.611 -42.922 12.156  1.00  28.30 ? 165  CYS B CB  1 
ATOM   1261 S SG  . CYS A 1 165 ? -21.290 -41.721 12.487  1.00  30.85 ? 165  CYS B SG  1 
ATOM   1262 N N   . THR A 1 166 ? -21.602 -43.475 9.465   1.00  27.87 ? 166  THR B N   1 
ATOM   1263 C CA  . THR A 1 166 ? -20.750 -43.056 8.358   1.00  29.04 ? 166  THR B CA  1 
ATOM   1264 C C   . THR A 1 166 ? -20.969 -41.581 8.088   1.00  30.50 ? 166  THR B C   1 
ATOM   1265 O O   . THR A 1 166 ? -22.113 -41.107 8.019   1.00  28.16 ? 166  THR B O   1 
ATOM   1266 C CB  . THR A 1 166 ? -21.054 -43.818 7.071   1.00  28.44 ? 166  THR B CB  1 
ATOM   1267 O OG1 . THR A 1 166 ? -20.927 -45.218 7.315   1.00  30.34 ? 166  THR B OG1 1 
ATOM   1268 C CG2 . THR A 1 166 ? -20.075 -43.407 5.951   1.00  27.63 ? 166  THR B CG2 1 
ATOM   1269 N N   . ILE A 1 167 ? -19.862 -40.859 7.962   1.00  26.38 ? 167  ILE B N   1 
ATOM   1270 C CA  . ILE A 1 167 ? -19.897 -39.453 7.626   1.00  24.95 ? 167  ILE B CA  1 
ATOM   1271 C C   . ILE A 1 167 ? -19.816 -39.342 6.112   1.00  25.27 ? 167  ILE B C   1 
ATOM   1272 O O   . ILE A 1 167 ? -18.936 -39.929 5.480   1.00  26.04 ? 167  ILE B O   1 
ATOM   1273 C CB  . ILE A 1 167 ? -18.737 -38.687 8.290   1.00  27.01 ? 167  ILE B CB  1 
ATOM   1274 C CG1 . ILE A 1 167 ? -18.650 -39.033 9.787   1.00  27.61 ? 167  ILE B CG1 1 
ATOM   1275 C CG2 . ILE A 1 167 ? -18.906 -37.186 8.097   1.00  24.72 ? 167  ILE B CG2 1 
ATOM   1276 C CD1 . ILE A 1 167 ? -19.931 -38.696 10.594  1.00  23.99 ? 167  ILE B CD1 1 
ATOM   1277 N N   . VAL A 1 168 ? -20.757 -38.603 5.535   1.00  26.68 ? 168  VAL B N   1 
ATOM   1278 C CA  . VAL A 1 168 ? -20.929 -38.563 4.097   1.00  24.36 ? 168  VAL B CA  1 
ATOM   1279 C C   . VAL A 1 168 ? -20.813 -37.155 3.524   1.00  25.44 ? 168  VAL B C   1 
ATOM   1280 O O   . VAL A 1 168 ? -21.441 -36.218 4.010   1.00  24.71 ? 168  VAL B O   1 
ATOM   1281 C CB  . VAL A 1 168 ? -22.300 -39.115 3.671   1.00  26.61 ? 168  VAL B CB  1 
ATOM   1282 C CG1 . VAL A 1 168 ? -22.318 -39.353 2.161   1.00  22.82 ? 168  VAL B CG1 1 
ATOM   1283 C CG2 . VAL A 1 168 ? -22.604 -40.396 4.399   1.00  25.21 ? 168  VAL B CG2 1 
ATOM   1284 N N   . SER A 1 169 ? -20.003 -37.022 2.484   1.00  23.50 ? 169  SER B N   1 
ATOM   1285 C CA  . SER A 1 169 ? -19.889 -35.764 1.763   1.00  28.72 ? 169  SER B CA  1 
ATOM   1286 C C   . SER A 1 169 ? -20.931 -35.787 0.661   1.00  25.05 ? 169  SER B C   1 
ATOM   1287 O O   . SER A 1 169 ? -21.068 -36.791 -0.029  1.00  27.97 ? 169  SER B O   1 
ATOM   1288 C CB  . SER A 1 169 ? -18.481 -35.610 1.157   1.00  29.10 ? 169  SER B CB  1 
ATOM   1289 O OG  . SER A 1 169 ? -18.324 -34.352 0.511   1.00  27.27 ? 169  SER B OG  1 
ATOM   1290 N N   . PRO A 1 170 ? -21.686 -34.691 0.510   1.00  27.74 ? 170  PRO B N   1 
ATOM   1291 C CA  . PRO A 1 170 ? -22.688 -34.594 -0.560  1.00  28.79 ? 170  PRO B CA  1 
ATOM   1292 C C   . PRO A 1 170 ? -22.084 -34.325 -1.938  1.00  32.12 ? 170  PRO B C   1 
ATOM   1293 O O   . PRO A 1 170 ? -22.816 -34.367 -2.918  1.00  35.06 ? 170  PRO B O   1 
ATOM   1294 C CB  . PRO A 1 170 ? -23.560 -33.407 -0.128  1.00  33.18 ? 170  PRO B CB  1 
ATOM   1295 C CG  . PRO A 1 170 ? -22.722 -32.627 0.814   1.00  35.72 ? 170  PRO B CG  1 
ATOM   1296 C CD  . PRO A 1 170 ? -21.829 -33.613 1.505   1.00  30.95 ? 170  PRO B CD  1 
ATOM   1297 N N   . ASP A 1 171 ? -20.787 -34.048 -2.011  1.00  27.85 ? 171  ASP B N   1 
ATOM   1298 C CA  . ASP A 1 171 ? -20.132 -33.842 -3.297  1.00  31.81 ? 171  ASP B CA  1 
ATOM   1299 C C   . ASP A 1 171 ? -18.648 -34.135 -3.223  1.00  32.43 ? 171  ASP B C   1 
ATOM   1300 O O   . ASP A 1 171 ? -18.122 -34.508 -2.175  1.00  29.08 ? 171  ASP B O   1 
ATOM   1301 C CB  . ASP A 1 171 ? -20.392 -32.429 -3.844  1.00  39.44 ? 171  ASP B CB  1 
ATOM   1302 C CG  . ASP A 1 171 ? -20.025 -31.337 -2.852  1.00  36.66 ? 171  ASP B CG  1 
ATOM   1303 O OD1 . ASP A 1 171 ? -19.056 -31.522 -2.091  1.00  42.65 ? 171  ASP B OD1 1 
ATOM   1304 O OD2 . ASP A 1 171 ? -20.713 -30.294 -2.831  1.00  48.07 ? 171  ASP B OD2 1 
ATOM   1305 N N   . ALA A 1 172 ? -17.977 -33.986 -4.357  1.00  34.86 ? 172  ALA B N   1 
ATOM   1306 C CA  . ALA A 1 172 ? -16.566 -34.323 -4.467  1.00  33.82 ? 172  ALA B CA  1 
ATOM   1307 C C   . ALA A 1 172 ? -15.694 -33.381 -3.651  1.00  33.84 ? 172  ALA B C   1 
ATOM   1308 O O   . ALA A 1 172 ? -14.681 -33.795 -3.089  1.00  38.40 ? 172  ALA B O   1 
ATOM   1309 C CB  . ALA A 1 172 ? -16.141 -34.297 -5.926  1.00  41.41 ? 172  ALA B CB  1 
ATOM   1310 N N   . GLY A 1 173 ? -16.101 -32.118 -3.577  1.00  36.34 ? 173  GLY B N   1 
ATOM   1311 C CA  . GLY A 1 173 ? -15.301 -31.102 -2.915  1.00  41.13 ? 173  GLY B CA  1 
ATOM   1312 C C   . GLY A 1 173 ? -15.356 -31.127 -1.393  1.00  39.45 ? 173  GLY B C   1 
ATOM   1313 O O   . GLY A 1 173 ? -14.623 -30.396 -0.730  1.00  38.60 ? 173  GLY B O   1 
ATOM   1314 N N   . GLY A 1 174 ? -16.220 -31.966 -0.831  1.00  38.21 ? 174  GLY B N   1 
ATOM   1315 C CA  . GLY A 1 174 ? -16.378 -32.017 0.615   1.00  30.53 ? 174  GLY B CA  1 
ATOM   1316 C C   . GLY A 1 174 ? -15.616 -33.163 1.244   1.00  31.22 ? 174  GLY B C   1 
ATOM   1317 O O   . GLY A 1 174 ? -15.788 -33.455 2.424   1.00  35.39 ? 174  GLY B O   1 
ATOM   1318 N N   . ALA A 1 175 ? -14.773 -33.816 0.451   1.00  29.19 ? 175  ALA B N   1 
ATOM   1319 C CA  . ALA A 1 175 ? -14.071 -35.017 0.897   1.00  32.35 ? 175  ALA B CA  1 
ATOM   1320 C C   . ALA A 1 175 ? -13.246 -34.805 2.166   1.00  35.27 ? 175  ALA B C   1 
ATOM   1321 O O   . ALA A 1 175 ? -13.451 -35.501 3.159   1.00  37.59 ? 175  ALA B O   1 
ATOM   1322 C CB  . ALA A 1 175 ? -13.193 -35.566 -0.219  1.00  37.10 ? 175  ALA B CB  1 
ATOM   1323 N N   . LYS A 1 176 ? -12.313 -33.859 2.131   0.10  33.11 ? 176  LYS B N   1 
ATOM   1324 C CA  . LYS A 1 176 ? -11.435 -33.615 3.274   0.10  33.18 ? 176  LYS B CA  1 
ATOM   1325 C C   . LYS A 1 176 ? -12.207 -33.267 4.543   0.10  31.95 ? 176  LYS B C   1 
ATOM   1326 O O   . LYS A 1 176 ? -11.868 -33.722 5.633   0.10  30.74 ? 176  LYS B O   1 
ATOM   1327 C CB  . LYS A 1 176 ? -10.416 -32.520 2.951   0.10  33.96 ? 176  LYS B CB  1 
ATOM   1328 C CG  . LYS A 1 176 ? -9.113  -33.052 2.378   0.10  36.79 ? 176  LYS B CG  1 
ATOM   1329 C CD  . LYS A 1 176 ? -8.121  -31.934 2.104   0.10  38.59 ? 176  LYS B CD  1 
ATOM   1330 C CE  . LYS A 1 176 ? -6.700  -32.470 2.079   0.10  40.16 ? 176  LYS B CE  1 
ATOM   1331 N NZ  . LYS A 1 176 ? -6.609  -33.773 1.361   0.10  41.46 ? 176  LYS B NZ  1 
ATOM   1332 N N   . ARG A 1 177 ? -13.246 -32.456 4.385   0.60  31.64 ? 177  ARG B N   1 
ATOM   1333 C CA  . ARG A 1 177 ? -14.112 -32.066 5.488   0.60  29.65 ? 177  ARG B CA  1 
ATOM   1334 C C   . ARG A 1 177 ? -14.729 -33.276 6.190   0.60  29.93 ? 177  ARG B C   1 
ATOM   1335 O O   . ARG A 1 177 ? -14.752 -33.329 7.414   0.60  29.90 ? 177  ARG B O   1 
ATOM   1336 C CB  . ARG A 1 177 ? -15.205 -31.125 4.978   0.60  34.18 ? 177  ARG B CB  1 
ATOM   1337 C CG  . ARG A 1 177 ? -16.111 -30.548 6.042   0.60  33.62 ? 177  ARG B CG  1 
ATOM   1338 C CD  . ARG A 1 177 ? -17.120 -29.569 5.432   0.60  31.84 ? 177  ARG B CD  1 
ATOM   1339 N NE  . ARG A 1 177 ? -16.478 -28.378 4.886   0.60  34.57 ? 177  ARG B NE  1 
ATOM   1340 C CZ  . ARG A 1 177 ? -15.985 -27.391 5.633   0.60  36.15 ? 177  ARG B CZ  1 
ATOM   1341 N NH1 . ARG A 1 177 ? -16.063 -27.458 6.953   0.60  30.31 ? 177  ARG B NH1 1 
ATOM   1342 N NH2 . ARG A 1 177 ? -15.417 -26.334 5.064   0.60  31.86 ? 177  ARG B NH2 1 
ATOM   1343 N N   . VAL A 1 178 ? -15.228 -34.251 5.431   1.00  32.84 ? 178  VAL B N   1 
ATOM   1344 C CA  . VAL A 1 178 ? -15.822 -35.419 6.076   1.00  32.49 ? 178  VAL B CA  1 
ATOM   1345 C C   . VAL A 1 178 ? -14.776 -36.395 6.603   1.00  31.24 ? 178  VAL B C   1 
ATOM   1346 O O   . VAL A 1 178 ? -14.944 -36.915 7.696   1.00  31.60 ? 178  VAL B O   1 
ATOM   1347 C CB  . VAL A 1 178 ? -16.863 -36.184 5.201   1.00  32.62 ? 178  VAL B CB  1 
ATOM   1348 C CG1 . VAL A 1 178 ? -17.975 -35.238 4.709   1.00  25.03 ? 178  VAL B CG1 1 
ATOM   1349 C CG2 . VAL A 1 178 ? -16.192 -36.921 4.063   1.00  34.82 ? 178  VAL B CG2 1 
ATOM   1350 N N   . THR A 1 179 ? -13.698 -36.645 5.854   1.00  32.74 ? 179  THR B N   1 
ATOM   1351 C CA  . THR A 1 179 ? -12.665 -37.560 6.362   1.00  34.21 ? 179  THR B CA  1 
ATOM   1352 C C   . THR A 1 179 ? -12.101 -37.055 7.696   1.00  34.03 ? 179  THR B C   1 
ATOM   1353 O O   . THR A 1 179 ? -11.809 -37.833 8.599   1.00  35.64 ? 179  THR B O   1 
ATOM   1354 C CB  . THR A 1 179 ? -11.500 -37.827 5.353   1.00  36.30 ? 179  THR B CB  1 
ATOM   1355 O OG1 . THR A 1 179 ? -10.816 -36.607 5.046   1.00  38.62 ? 179  THR B OG1 1 
ATOM   1356 C CG2 . THR A 1 179 ? -12.014 -38.456 4.067   1.00  34.73 ? 179  THR B CG2 1 
ATOM   1357 N N   . SER A 1 180 ? -11.967 -35.743 7.816   1.00  33.76 ? 180  SER B N   1 
ATOM   1358 C CA  . SER A 1 180 ? -11.492 -35.139 9.056   1.00  35.41 ? 180  SER B CA  1 
ATOM   1359 C C   . SER A 1 180 ? -12.383 -35.537 10.240  1.00  36.84 ? 180  SER B C   1 
ATOM   1360 O O   . SER A 1 180 ? -11.891 -35.993 11.283  1.00  32.95 ? 180  SER B O   1 
ATOM   1361 C CB  . SER A 1 180 ? -11.440 -33.612 8.897   1.00  33.99 ? 180  SER B CB  1 
ATOM   1362 O OG  . SER A 1 180 ? -10.956 -32.980 10.069  1.00  40.55 ? 180  SER B OG  1 
ATOM   1363 N N   . ILE A 1 181 ? -13.695 -35.380 10.069  1.00  32.94 ? 181  ILE B N   1 
ATOM   1364 C CA  . ILE A 1 181 ? -14.661 -35.784 11.097  1.00  32.50 ? 181  ILE B CA  1 
ATOM   1365 C C   . ILE A 1 181 ? -14.673 -37.291 11.312  1.00  31.02 ? 181  ILE B C   1 
ATOM   1366 O O   . ILE A 1 181 ? -14.672 -37.766 12.450  1.00  32.79 ? 181  ILE B O   1 
ATOM   1367 C CB  . ILE A 1 181 ? -16.097 -35.301 10.772  1.00  31.71 ? 181  ILE B CB  1 
ATOM   1368 C CG1 . ILE A 1 181 ? -16.152 -33.772 10.768  1.00  40.44 ? 181  ILE B CG1 1 
ATOM   1369 C CG2 . ILE A 1 181 ? -17.098 -35.838 11.795  1.00  29.42 ? 181  ILE B CG2 1 
ATOM   1370 C CD1 . ILE A 1 181 ? -17.536 -33.213 10.534  1.00  34.76 ? 181  ILE B CD1 1 
ATOM   1371 N N   . ALA A 1 182 ? -14.693 -38.053 10.229  1.00  32.81 ? 182  ALA B N   1 
ATOM   1372 C CA  . ALA A 1 182 ? -14.697 -39.508 10.353  1.00  32.40 ? 182  ALA B CA  1 
ATOM   1373 C C   . ALA A 1 182 ? -13.467 -40.006 11.125  1.00  36.94 ? 182  ALA B C   1 
ATOM   1374 O O   . ALA A 1 182 ? -13.579 -40.864 12.012  1.00  34.76 ? 182  ALA B O   1 
ATOM   1375 C CB  . ALA A 1 182 ? -14.780 -40.157 8.993   1.00  28.81 ? 182  ALA B CB  1 
ATOM   1376 N N   . ASP A 1 183 ? -12.301 -39.452 10.803  0.60  32.76 ? 183  ASP B N   1 
ATOM   1377 C CA  . ASP A 1 183 ? -11.072 -39.835 11.490  0.60  32.27 ? 183  ASP B CA  1 
ATOM   1378 C C   . ASP A 1 183 ? -11.129 -39.507 12.979  0.60  31.52 ? 183  ASP B C   1 
ATOM   1379 O O   . ASP A 1 183 ? -10.720 -40.321 13.803  0.60  28.66 ? 183  ASP B O   1 
ATOM   1380 C CB  . ASP A 1 183 ? -9.841  -39.193 10.840  0.60  29.73 ? 183  ASP B CB  1 
ATOM   1381 C CG  . ASP A 1 183 ? -9.537  -39.770 9.466   0.60  36.02 ? 183  ASP B CG  1 
ATOM   1382 O OD1 . ASP A 1 183 ? -10.148 -40.794 9.093   0.60  36.01 ? 183  ASP B OD1 1 
ATOM   1383 O OD2 . ASP A 1 183 ? -8.681  -39.203 8.759   0.60  38.18 ? 183  ASP B OD2 1 
ATOM   1384 N N   . ARG A 1 184 ? -11.633 -38.325 13.326  0.70  30.62 ? 184  ARG B N   1 
ATOM   1385 C CA  . ARG A 1 184 ? -11.737 -37.943 14.734  0.70  35.38 ? 184  ARG B CA  1 
ATOM   1386 C C   . ARG A 1 184 ? -12.695 -38.838 15.509  0.70  32.21 ? 184  ARG B C   1 
ATOM   1387 O O   . ARG A 1 184 ? -12.398 -39.252 16.624  0.70  30.51 ? 184  ARG B O   1 
ATOM   1388 C CB  . ARG A 1 184 ? -12.121 -36.469 14.892  0.70  37.09 ? 184  ARG B CB  1 
ATOM   1389 C CG  . ARG A 1 184 ? -10.996 -35.520 14.504  0.70  39.19 ? 184  ARG B CG  1 
ATOM   1390 C CD  . ARG A 1 184 ? -11.137 -34.149 15.140  0.70  41.01 ? 184  ARG B CD  1 
ATOM   1391 N NE  . ARG A 1 184 ? -10.062 -33.252 14.713  0.70  47.83 ? 184  ARG B NE  1 
ATOM   1392 C CZ  . ARG A 1 184 ? -9.806  -32.939 13.444  0.70  44.88 ? 184  ARG B CZ  1 
ATOM   1393 N NH1 . ARG A 1 184 ? -10.545 -33.447 12.467  0.70  41.86 ? 184  ARG B NH1 1 
ATOM   1394 N NH2 . ARG A 1 184 ? -8.808  -32.117 13.146  0.70  48.40 ? 184  ARG B NH2 1 
ATOM   1395 N N   . LEU A 1 185 ? -13.842 -39.138 14.911  1.00  31.51 ? 185  LEU B N   1 
ATOM   1396 C CA  . LEU A 1 185 ? -14.804 -40.056 15.514  1.00  32.64 ? 185  LEU B CA  1 
ATOM   1397 C C   . LEU A 1 185 ? -14.337 -41.511 15.401  1.00  35.15 ? 185  LEU B C   1 
ATOM   1398 O O   . LEU A 1 185 ? -14.908 -42.403 16.023  1.00  35.29 ? 185  LEU B O   1 
ATOM   1399 C CB  . LEU A 1 185 ? -16.178 -39.912 14.839  1.00  34.16 ? 185  LEU B CB  1 
ATOM   1400 C CG  . LEU A 1 185 ? -16.929 -38.579 14.989  1.00  34.73 ? 185  LEU B CG  1 
ATOM   1401 C CD1 . LEU A 1 185 ? -18.164 -38.530 14.082  1.00  30.76 ? 185  LEU B CD1 1 
ATOM   1402 C CD2 . LEU A 1 185 ? -17.320 -38.335 16.434  1.00  32.20 ? 185  LEU B CD2 1 
ATOM   1403 N N   . ASN A 1 186 ? -13.317 -41.756 14.585  1.00  35.96 ? 186  ASN B N   1 
ATOM   1404 C CA  . ASN A 1 186 ? -12.918 -43.127 14.277  1.00  36.70 ? 186  ASN B CA  1 
ATOM   1405 C C   . ASN A 1 186 ? -14.038 -43.955 13.647  1.00  36.09 ? 186  ASN B C   1 
ATOM   1406 O O   . ASN A 1 186 ? -14.354 -45.046 14.124  1.00  38.24 ? 186  ASN B O   1 
ATOM   1407 C CB  . ASN A 1 186 ? -12.415 -43.841 15.537  1.00  38.72 ? 186  ASN B CB  1 
ATOM   1408 C CG  . ASN A 1 186 ? -11.683 -45.129 15.219  1.00  49.93 ? 186  ASN B CG  1 
ATOM   1409 O OD1 . ASN A 1 186 ? -11.957 -46.180 15.809  1.00  53.86 ? 186  ASN B OD1 1 
ATOM   1410 N ND2 . ASN A 1 186 ? -10.751 -45.060 14.266  1.00  49.14 ? 186  ASN B ND2 1 
ATOM   1411 N N   . VAL A 1 187 ? -14.630 -43.446 12.573  1.00  32.31 ? 187  VAL B N   1 
ATOM   1412 C CA  . VAL A 1 187 ? -15.684 -44.171 11.866  1.00  33.96 ? 187  VAL B CA  1 
ATOM   1413 C C   . VAL A 1 187 ? -15.437 -44.091 10.361  1.00  35.53 ? 187  VAL B C   1 
ATOM   1414 O O   . VAL A 1 187 ? -14.427 -43.540 9.927   1.00  33.29 ? 187  VAL B O   1 
ATOM   1415 C CB  . VAL A 1 187 ? -17.087 -43.615 12.207  1.00  34.17 ? 187  VAL B CB  1 
ATOM   1416 C CG1 . VAL A 1 187 ? -17.347 -43.724 13.697  1.00  31.89 ? 187  VAL B CG1 1 
ATOM   1417 C CG2 . VAL A 1 187 ? -17.215 -42.163 11.751  1.00  28.73 ? 187  VAL B CG2 1 
ATOM   1418 N N   . ASP A 1 188 ? -16.350 -44.637 9.567   1.00  30.45 ? 188  ASP B N   1 
ATOM   1419 C CA  . ASP A 1 188 ? -16.187 -44.648 8.118   1.00  34.36 ? 188  ASP B CA  1 
ATOM   1420 C C   . ASP A 1 188 ? -16.677 -43.360 7.473   1.00  31.12 ? 188  ASP B C   1 
ATOM   1421 O O   . ASP A 1 188 ? -17.363 -42.554 8.100   1.00  29.03 ? 188  ASP B O   1 
ATOM   1422 C CB  . ASP A 1 188 ? -16.936 -45.835 7.495   1.00  35.14 ? 188  ASP B CB  1 
ATOM   1423 C CG  . ASP A 1 188 ? -16.523 -47.165 8.093   1.00  46.72 ? 188  ASP B CG  1 
ATOM   1424 O OD1 . ASP A 1 188 ? -15.363 -47.283 8.542   1.00  50.54 ? 188  ASP B OD1 1 
ATOM   1425 O OD2 . ASP A 1 188 ? -17.356 -48.095 8.111   1.00  50.39 ? 188  ASP B OD2 1 
ATOM   1426 N N   . PHE A 1 189 ? -16.338 -43.183 6.202   1.00  32.88 ? 189  PHE B N   1 
ATOM   1427 C CA  . PHE A 1 189 ? -16.838 -42.046 5.450   1.00  31.12 ? 189  PHE B CA  1 
ATOM   1428 C C   . PHE A 1 189 ? -17.301 -42.537 4.110   1.00  28.65 ? 189  PHE B C   1 
ATOM   1429 O O   . PHE A 1 189 ? -16.965 -43.646 3.689   1.00  31.94 ? 189  PHE B O   1 
ATOM   1430 C CB  . PHE A 1 189 ? -15.760 -40.975 5.263   1.00  32.42 ? 189  PHE B CB  1 
ATOM   1431 C CG  . PHE A 1 189 ? -14.736 -41.334 4.234   1.00  35.11 ? 189  PHE B CG  1 
ATOM   1432 C CD1 . PHE A 1 189 ? -14.906 -40.965 2.915   1.00  34.35 ? 189  PHE B CD1 1 
ATOM   1433 C CD2 . PHE A 1 189 ? -13.610 -42.061 4.585   1.00  36.70 ? 189  PHE B CD2 1 
ATOM   1434 C CE1 . PHE A 1 189 ? -13.963 -41.310 1.958   1.00  41.00 ? 189  PHE B CE1 1 
ATOM   1435 C CE2 . PHE A 1 189 ? -12.662 -42.407 3.633   1.00  39.06 ? 189  PHE B CE2 1 
ATOM   1436 C CZ  . PHE A 1 189 ? -12.838 -42.032 2.324   1.00  40.75 ? 189  PHE B CZ  1 
ATOM   1437 N N   . ALA A 1 190 ? -18.073 -41.700 3.433   1.00  29.84 ? 190  ALA B N   1 
ATOM   1438 C CA  . ALA A 1 190 ? -18.577 -42.031 2.116   1.00  31.32 ? 190  ALA B CA  1 
ATOM   1439 C C   . ALA A 1 190 ? -18.684 -40.746 1.320   1.00  27.31 ? 190  ALA B C   1 
ATOM   1440 O O   . ALA A 1 190 ? -18.666 -39.652 1.883   1.00  28.31 ? 190  ALA B O   1 
ATOM   1441 C CB  . ALA A 1 190 ? -19.929 -42.712 2.230   1.00  28.00 ? 190  ALA B CB  1 
ATOM   1442 N N   . LEU A 1 191 ? -18.784 -40.877 0.012   1.00  27.09 ? 191  LEU B N   1 
ATOM   1443 C CA  . LEU A 1 191 ? -18.809 -39.713 -0.857  1.00  30.26 ? 191  LEU B CA  1 
ATOM   1444 C C   . LEU A 1 191 ? -19.826 -39.852 -1.972  1.00  29.34 ? 191  LEU B C   1 
ATOM   1445 O O   . LEU A 1 191 ? -19.852 -40.844 -2.689  1.00  33.56 ? 191  LEU B O   1 
ATOM   1446 C CB  . LEU A 1 191 ? -17.431 -39.471 -1.464  1.00  33.42 ? 191  LEU B CB  1 
ATOM   1447 C CG  . LEU A 1 191 ? -17.323 -38.195 -2.301  1.00  38.31 ? 191  LEU B CG  1 
ATOM   1448 C CD1 . LEU A 1 191 ? -16.079 -37.410 -1.894  1.00  40.79 ? 191  LEU B CD1 1 
ATOM   1449 C CD2 . LEU A 1 191 ? -17.316 -38.510 -3.801  1.00  38.44 ? 191  LEU B CD2 1 
ATOM   1450 N N   . ILE A 1 192 ? -20.646 -38.823 -2.117  1.00  25.71 ? 192  ILE B N   1 
ATOM   1451 C CA  . ILE A 1 192 ? -21.558 -38.725 -3.226  1.00  31.02 ? 192  ILE B CA  1 
ATOM   1452 C C   . ILE A 1 192 ? -21.003 -37.772 -4.269  1.00  34.82 ? 192  ILE B C   1 
ATOM   1453 O O   . ILE A 1 192 ? -20.412 -36.744 -3.933  1.00  32.26 ? 192  ILE B O   1 
ATOM   1454 C CB  . ILE A 1 192 ? -22.928 -38.260 -2.729  1.00  34.75 ? 192  ILE B CB  1 
ATOM   1455 C CG1 . ILE A 1 192 ? -23.510 -39.352 -1.816  1.00  33.23 ? 192  ILE B CG1 1 
ATOM   1456 C CG2 . ILE A 1 192 ? -23.840 -37.914 -3.900  1.00  31.87 ? 192  ILE B CG2 1 
ATOM   1457 C CD1 . ILE A 1 192 ? -24.876 -39.087 -1.273  1.00  31.18 ? 192  ILE B CD1 1 
ATOM   1458 N N   . HIS A 1 193 ? -21.180 -38.133 -5.534  1.00  29.90 ? 193  HIS B N   1 
ATOM   1459 C CA  . HIS A 1 193 ? -20.769 -37.293 -6.647  1.00  32.98 ? 193  HIS B CA  1 
ATOM   1460 C C   . HIS A 1 193 ? -21.899 -37.255 -7.659  1.00  34.33 ? 193  HIS B C   1 
ATOM   1461 O O   . HIS A 1 193 ? -22.399 -38.307 -8.054  1.00  34.83 ? 193  HIS B O   1 
ATOM   1462 C CB  . HIS A 1 193 ? -19.517 -37.866 -7.310  1.00  36.79 ? 193  HIS B CB  1 
ATOM   1463 C CG  . HIS A 1 193 ? -19.255 -37.315 -8.677  1.00  35.59 ? 193  HIS B CG  1 
ATOM   1464 N ND1 . HIS A 1 193 ? -19.112 -35.965 -8.919  1.00  43.31 ? 193  HIS B ND1 1 
ATOM   1465 C CD2 . HIS A 1 193 ? -19.115 -37.927 -9.874  1.00  41.03 ? 193  HIS B CD2 1 
ATOM   1466 C CE1 . HIS A 1 193 ? -18.897 -35.769 -10.209 1.00  41.03 ? 193  HIS B CE1 1 
ATOM   1467 N NE2 . HIS A 1 193 ? -18.894 -36.943 -10.813 1.00  42.89 ? 193  HIS B NE2 1 
ATOM   1468 N N   . LYS A 1 194 ? -22.307 -36.056 -8.062  0.20  32.58 ? 194  LYS B N   1 
ATOM   1469 C CA  . LYS A 1 194 ? -23.341 -35.912 -9.074  0.20  36.09 ? 194  LYS B CA  1 
ATOM   1470 C C   . LYS A 1 194 ? -22.726 -35.773 -10.460 0.20  38.07 ? 194  LYS B C   1 
ATOM   1471 O O   . LYS A 1 194 ? -21.875 -34.914 -10.695 0.20  35.70 ? 194  LYS B O   1 
ATOM   1472 C CB  . LYS A 1 194 ? -24.247 -34.719 -8.774  0.20  37.29 ? 194  LYS B CB  1 
ATOM   1473 C CG  . LYS A 1 194 ? -25.392 -34.561 -9.763  0.20  39.49 ? 194  LYS B CG  1 
ATOM   1474 C CD  . LYS A 1 194 ? -26.534 -33.766 -9.162  0.20  39.40 ? 194  LYS B CD  1 
ATOM   1475 C CE  . LYS A 1 194 ? -27.817 -33.962 -9.961  0.20  44.43 ? 194  LYS B CE  1 
ATOM   1476 N NZ  . LYS A 1 194 ? -29.012 -33.364 -9.287  0.20  45.83 ? 194  LYS B NZ  1 
ATOM   1477 N N   . GLU A 1 195 ? -23.165 -36.632 -11.371 1.00  43.65 ? 195  GLU B N   1 
ATOM   1478 C CA  . GLU A 1 195 ? -22.671 -36.644 -12.750 1.00  49.28 ? 195  GLU B CA  1 
ATOM   1479 C C   . GLU A 1 195 ? -23.462 -35.714 -13.672 1.00  46.10 ? 195  GLU B C   1 
ATOM   1480 O O   . GLU A 1 195 ? -23.802 -34.587 -13.306 1.00  45.75 ? 195  GLU B O   1 
ATOM   1481 C CB  . GLU A 1 195 ? -22.712 -38.070 -13.305 1.00  47.03 ? 195  GLU B CB  1 
ATOM   1482 C CG  . GLU A 1 195 ? -21.673 -39.000 -12.713 1.00  47.26 ? 195  GLU B CG  1 
ATOM   1483 C CD  . GLU A 1 195 ? -22.185 -40.408 -12.606 1.00  57.06 ? 195  GLU B CD  1 
ATOM   1484 O OE1 . GLU A 1 195 ? -23.386 -40.564 -12.292 1.00  57.44 ? 195  GLU B OE1 1 
ATOM   1485 O OE2 . GLU A 1 195 ? -21.405 -41.360 -12.832 1.00  63.42 ? 195  GLU B OE2 1 
ATOM   1486 N N   . ASP A 1 203 ? -27.321 -36.717 -14.956 0.010 45.13 ? 203  ASP B N   1 
ATOM   1487 C CA  . ASP A 1 203 ? -28.116 -36.040 -13.941 0.010 44.83 ? 203  ASP B CA  1 
ATOM   1488 C C   . ASP A 1 203 ? -28.402 -36.988 -12.785 0.010 43.39 ? 203  ASP B C   1 
ATOM   1489 O O   . ASP A 1 203 ? -29.535 -37.089 -12.315 0.010 43.79 ? 203  ASP B O   1 
ATOM   1490 C CB  . ASP A 1 203 ? -29.431 -35.545 -14.541 0.010 46.46 ? 203  ASP B CB  1 
ATOM   1491 C CG  . ASP A 1 203 ? -29.881 -34.225 -13.947 0.010 47.40 ? 203  ASP B CG  1 
ATOM   1492 O OD1 . ASP A 1 203 ? -30.334 -34.219 -12.784 0.010 47.34 ? 203  ASP B OD1 1 
ATOM   1493 O OD2 . ASP A 1 203 ? -29.785 -33.197 -14.647 0.010 47.96 ? 203  ASP B OD2 1 
ATOM   1494 N N   . ARG A 1 204 ? -27.361 -37.673 -12.326 0.40  41.39 ? 204  ARG B N   1 
ATOM   1495 C CA  . ARG A 1 204 ? -27.508 -38.727 -11.331 0.40  40.62 ? 204  ARG B CA  1 
ATOM   1496 C C   . ARG A 1 204 ? -26.400 -38.695 -10.283 0.40  38.73 ? 204  ARG B C   1 
ATOM   1497 O O   . ARG A 1 204 ? -25.285 -38.263 -10.552 0.40  36.61 ? 204  ARG B O   1 
ATOM   1498 C CB  . ARG A 1 204 ? -27.497 -40.088 -12.019 0.40  39.95 ? 204  ARG B CB  1 
ATOM   1499 C CG  . ARG A 1 204 ? -28.712 -40.375 -12.881 0.40  42.71 ? 204  ARG B CG  1 
ATOM   1500 C CD  . ARG A 1 204 ? -29.855 -40.951 -12.064 0.40  38.67 ? 204  ARG B CD  1 
ATOM   1501 N NE  . ARG A 1 204 ? -29.440 -42.018 -11.148 0.40  43.74 ? 204  ARG B NE  1 
ATOM   1502 C CZ  . ARG A 1 204 ? -28.512 -42.942 -11.401 0.40  39.03 ? 204  ARG B CZ  1 
ATOM   1503 N NH1 . ARG A 1 204 ? -27.864 -42.962 -12.558 0.40  38.29 ? 204  ARG B NH1 1 
ATOM   1504 N NH2 . ARG A 1 204 ? -28.226 -43.853 -10.482 0.40  37.86 ? 204  ARG B NH2 1 
ATOM   1505 N N   . MET A 1 205 ? -26.718 -39.169 -9.086  1.00  40.30 ? 205  MET B N   1 
ATOM   1506 C CA  . MET A 1 205 ? -25.731 -39.289 -8.030  1.00  40.57 ? 205  MET B CA  1 
ATOM   1507 C C   . MET A 1 205 ? -25.149 -40.682 -7.978  1.00  40.14 ? 205  MET B C   1 
ATOM   1508 O O   . MET A 1 205 ? -25.858 -41.673 -8.185  1.00  42.00 ? 205  MET B O   1 
ATOM   1509 C CB  . MET A 1 205 ? -26.351 -38.958 -6.675  1.00  35.61 ? 205  MET B CB  1 
ATOM   1510 C CG  . MET A 1 205 ? -26.550 -37.484 -6.448  1.00  39.81 ? 205  MET B CG  1 
ATOM   1511 S SD  . MET A 1 205 ? -27.461 -37.161 -4.935  1.00  37.95 ? 205  MET B SD  1 
ATOM   1512 C CE  . MET A 1 205 ? -27.001 -35.443 -4.696  1.00  35.65 ? 205  MET B CE  1 
ATOM   1513 N N   . VAL A 1 206 ? -23.853 -40.751 -7.702  1.00  35.98 ? 206  VAL B N   1 
ATOM   1514 C CA  . VAL A 1 206 ? -23.219 -42.017 -7.403  1.00  37.74 ? 206  VAL B CA  1 
ATOM   1515 C C   . VAL A 1 206 ? -22.569 -41.934 -6.035  1.00  38.38 ? 206  VAL B C   1 
ATOM   1516 O O   . VAL A 1 206 ? -22.113 -40.871 -5.612  1.00  35.82 ? 206  VAL B O   1 
ATOM   1517 C CB  . VAL A 1 206 ? -22.167 -42.394 -8.444  1.00  41.57 ? 206  VAL B CB  1 
ATOM   1518 C CG1 . VAL A 1 206 ? -22.816 -42.537 -9.808  1.00  47.84 ? 206  VAL B CG1 1 
ATOM   1519 C CG2 . VAL A 1 206 ? -21.058 -41.365 -8.473  1.00  40.76 ? 206  VAL B CG2 1 
ATOM   1520 N N   . LEU A 1 207 ? -22.545 -43.062 -5.341  1.00  34.44 ? 207  LEU B N   1 
ATOM   1521 C CA  . LEU A 1 207 ? -22.044 -43.113 -3.986  1.00  34.34 ? 207  LEU B CA  1 
ATOM   1522 C C   . LEU A 1 207 ? -20.886 -44.089 -3.928  1.00  38.13 ? 207  LEU B C   1 
ATOM   1523 O O   . LEU A 1 207 ? -21.010 -45.235 -4.358  1.00  35.58 ? 207  LEU B O   1 
ATOM   1524 C CB  . LEU A 1 207 ? -23.158 -43.572 -3.045  1.00  34.05 ? 207  LEU B CB  1 
ATOM   1525 C CG  . LEU A 1 207 ? -22.856 -43.855 -1.571  1.00  35.61 ? 207  LEU B CG  1 
ATOM   1526 C CD1 . LEU A 1 207 ? -22.579 -42.574 -0.791  1.00  26.06 ? 207  LEU B CD1 1 
ATOM   1527 C CD2 . LEU A 1 207 ? -24.044 -44.577 -0.974  1.00  31.86 ? 207  LEU B CD2 1 
ATOM   1528 N N   . VAL A 1 208 ? -19.752 -43.632 -3.413  1.00  30.71 ? 208  VAL B N   1 
ATOM   1529 C CA  . VAL A 1 208 ? -18.674 -44.545 -3.100  1.00  30.27 ? 208  VAL B CA  1 
ATOM   1530 C C   . VAL A 1 208 ? -18.549 -44.617 -1.585  1.00  34.39 ? 208  VAL B C   1 
ATOM   1531 O O   . VAL A 1 208 ? -18.542 -43.586 -0.909  1.00  34.34 ? 208  VAL B O   1 
ATOM   1532 C CB  . VAL A 1 208 ? -17.343 -44.123 -3.750  1.00  31.23 ? 208  VAL B CB  1 
ATOM   1533 C CG1 . VAL A 1 208 ? -17.457 -44.191 -5.266  1.00  36.97 ? 208  VAL B CG1 1 
ATOM   1534 C CG2 . VAL A 1 208 ? -16.935 -42.728 -3.298  1.00  32.05 ? 208  VAL B CG2 1 
ATOM   1535 N N   . GLY A 1 209 ? -18.475 -45.837 -1.058  1.00  32.63 ? 209  GLY B N   1 
ATOM   1536 C CA  . GLY A 1 209 ? -18.343 -46.061 0.369   1.00  30.75 ? 209  GLY B CA  1 
ATOM   1537 C C   . GLY A 1 209 ? -19.577 -46.752 0.934   1.00  32.68 ? 209  GLY B C   1 
ATOM   1538 O O   . GLY A 1 209 ? -20.681 -46.557 0.444   1.00  38.10 ? 209  GLY B O   1 
ATOM   1539 N N   . ASP A 1 210 ? -19.396 -47.544 1.980   0.50  32.64 ? 210  ASP B N   1 
ATOM   1540 C CA  . ASP A 1 210 ? -20.492 -48.335 2.522   0.50  32.35 ? 210  ASP B CA  1 
ATOM   1541 C C   . ASP A 1 210 ? -21.291 -47.590 3.591   0.50  28.71 ? 210  ASP B C   1 
ATOM   1542 O O   . ASP A 1 210 ? -20.727 -47.062 4.547   0.50  28.30 ? 210  ASP B O   1 
ATOM   1543 C CB  . ASP A 1 210 ? -19.957 -49.657 3.076   0.50  34.50 ? 210  ASP B CB  1 
ATOM   1544 C CG  . ASP A 1 210 ? -21.057 -50.566 3.565   0.50  34.69 ? 210  ASP B CG  1 
ATOM   1545 O OD1 . ASP A 1 210 ? -21.089 -50.871 4.776   0.50  36.42 ? 210  ASP B OD1 1 
ATOM   1546 O OD2 . ASP A 1 210 ? -21.902 -50.968 2.736   0.50  38.57 ? 210  ASP B OD2 1 
ATOM   1547 N N   . VAL A 1 211 ? -22.608 -47.545 3.414   1.00  29.12 ? 211  VAL B N   1 
ATOM   1548 C CA  . VAL A 1 211 ? -23.481 -46.951 4.416   1.00  32.87 ? 211  VAL B CA  1 
ATOM   1549 C C   . VAL A 1 211 ? -24.540 -47.943 4.907   1.00  32.38 ? 211  VAL B C   1 
ATOM   1550 O O   . VAL A 1 211 ? -25.424 -47.576 5.675   1.00  26.24 ? 211  VAL B O   1 
ATOM   1551 C CB  . VAL A 1 211 ? -24.186 -45.681 3.881   1.00  32.06 ? 211  VAL B CB  1 
ATOM   1552 C CG1 . VAL A 1 211 ? -23.152 -44.634 3.469   1.00  29.76 ? 211  VAL B CG1 1 
ATOM   1553 C CG2 . VAL A 1 211 ? -25.112 -46.041 2.707   1.00  27.02 ? 211  VAL B CG2 1 
ATOM   1554 N N   . LYS A 1 212 ? -24.446 -49.191 4.463   0.40  25.89 ? 212  LYS B N   1 
ATOM   1555 C CA  . LYS A 1 212 ? -25.521 -50.147 4.696   0.40  29.64 ? 212  LYS B CA  1 
ATOM   1556 C C   . LYS A 1 212 ? -25.741 -50.463 6.176   0.40  29.10 ? 212  LYS B C   1 
ATOM   1557 O O   . LYS A 1 212 ? -24.802 -50.762 6.910   0.40  24.53 ? 212  LYS B O   1 
ATOM   1558 C CB  . LYS A 1 212 ? -25.296 -51.432 3.898   0.40  31.06 ? 212  LYS B CB  1 
ATOM   1559 C CG  . LYS A 1 212 ? -26.477 -52.385 3.947   0.40  32.44 ? 212  LYS B CG  1 
ATOM   1560 C CD  . LYS A 1 212 ? -26.241 -53.620 3.102   0.40  37.80 ? 212  LYS B CD  1 
ATOM   1561 C CE  . LYS A 1 212 ? -27.434 -54.558 3.165   0.40  41.28 ? 212  LYS B CE  1 
ATOM   1562 N NZ  . LYS A 1 212 ? -28.684 -53.894 2.704   0.40  44.43 ? 212  LYS B NZ  1 
ATOM   1563 N N   . ASP A 1 213 ? -26.997 -50.374 6.601   0.94  32.08 ? 213  ASP B N   1 
ATOM   1564 C CA  . ASP A 1 213 ? -27.379 -50.697 7.974   0.94  32.87 ? 213  ASP B CA  1 
ATOM   1565 C C   . ASP A 1 213 ? -26.657 -49.855 9.031   0.94  35.45 ? 213  ASP B C   1 
ATOM   1566 O O   . ASP A 1 213 ? -26.530 -50.283 10.177  0.94  38.61 ? 213  ASP B O   1 
ATOM   1567 C CB  . ASP A 1 213 ? -27.155 -52.193 8.260   0.94  34.81 ? 213  ASP B CB  1 
ATOM   1568 C CG  . ASP A 1 213 ? -28.119 -53.098 7.482   0.94  44.98 ? 213  ASP B CG  1 
ATOM   1569 O OD1 . ASP A 1 213 ? -27.682 -54.171 7.008   0.94  45.18 ? 213  ASP B OD1 1 
ATOM   1570 O OD2 . ASP A 1 213 ? -29.312 -52.738 7.351   0.94  46.61 ? 213  ASP B OD2 1 
ATOM   1571 N N   . ARG A 1 214 ? -26.179 -48.674 8.641   0.94  33.48 ? 214  ARG B N   1 
ATOM   1572 C CA  . ARG A 1 214 ? -25.585 -47.716 9.581   0.94  34.92 ? 214  ARG B CA  1 
ATOM   1573 C C   . ARG A 1 214 ? -26.319 -46.380 9.516   0.94  31.17 ? 214  ARG B C   1 
ATOM   1574 O O   . ARG A 1 214 ? -26.996 -46.069 8.534   0.94  29.83 ? 214  ARG B O   1 
ATOM   1575 C CB  . ARG A 1 214 ? -24.117 -47.450 9.235   0.94  31.75 ? 214  ARG B CB  1 
ATOM   1576 C CG  . ARG A 1 214 ? -23.220 -48.679 9.132   0.94  41.18 ? 214  ARG B CG  1 
ATOM   1577 C CD  . ARG A 1 214 ? -21.891 -48.327 8.450   0.94  36.27 ? 214  ARG B CD  1 
ATOM   1578 N NE  . ARG A 1 214 ? -20.783 -49.080 9.026   0.94  52.62 ? 214  ARG B NE  1 
ATOM   1579 C CZ  . ARG A 1 214 ? -19.913 -48.587 9.907   0.94  50.37 ? 214  ARG B CZ  1 
ATOM   1580 N NH1 . ARG A 1 214 ? -20.002 -47.322 10.310  0.94  46.81 ? 214  ARG B NH1 1 
ATOM   1581 N NH2 . ARG A 1 214 ? -18.945 -49.358 10.381  0.94  52.98 ? 214  ARG B NH2 1 
ATOM   1582 N N   . VAL A 1 215 ? -26.164 -45.568 10.551  1.00  28.86 ? 215  VAL B N   1 
ATOM   1583 C CA  . VAL A 1 215 ? -26.633 -44.189 10.485  1.00  28.63 ? 215  VAL B CA  1 
ATOM   1584 C C   . VAL A 1 215 ? -25.687 -43.395 9.577   1.00  26.35 ? 215  VAL B C   1 
ATOM   1585 O O   . VAL A 1 215 ? -24.468 -43.538 9.678   1.00  27.97 ? 215  VAL B O   1 
ATOM   1586 C CB  . VAL A 1 215 ? -26.675 -43.567 11.885  1.00  26.45 ? 215  VAL B CB  1 
ATOM   1587 C CG1 . VAL A 1 215 ? -27.001 -42.089 11.815  1.00  26.38 ? 215  VAL B CG1 1 
ATOM   1588 C CG2 . VAL A 1 215 ? -27.686 -44.323 12.763  1.00  30.51 ? 215  VAL B CG2 1 
ATOM   1589 N N   . ALA A 1 216 ? -26.242 -42.596 8.667   1.00  23.12 ? 216  ALA B N   1 
ATOM   1590 C CA  . ALA A 1 216 ? -25.418 -41.752 7.806   1.00  23.81 ? 216  ALA B CA  1 
ATOM   1591 C C   . ALA A 1 216 ? -25.575 -40.278 8.189   1.00  26.31 ? 216  ALA B C   1 
ATOM   1592 O O   . ALA A 1 216 ? -26.686 -39.782 8.387   1.00  26.83 ? 216  ALA B O   1 
ATOM   1593 C CB  . ALA A 1 216 ? -25.751 -41.961 6.313   1.00  25.75 ? 216  ALA B CB  1 
ATOM   1594 N N   . ILE A 1 217 ? -24.452 -39.579 8.284   1.00  21.95 ? 217  ILE B N   1 
ATOM   1595 C CA  . ILE A 1 217 ? -24.485 -38.160 8.580   1.00  23.59 ? 217  ILE B CA  1 
ATOM   1596 C C   . ILE A 1 217 ? -23.889 -37.389 7.417   1.00  24.48 ? 217  ILE B C   1 
ATOM   1597 O O   . ILE A 1 217 ? -22.671 -37.441 7.180   1.00  22.65 ? 217  ILE B O   1 
ATOM   1598 C CB  . ILE A 1 217 ? -23.690 -37.831 9.835   1.00  20.82 ? 217  ILE B CB  1 
ATOM   1599 C CG1 . ILE A 1 217 ? -24.145 -38.727 10.978  1.00  26.69 ? 217  ILE B CG1 1 
ATOM   1600 C CG2 . ILE A 1 217 ? -23.871 -36.346 10.196  1.00  22.43 ? 217  ILE B CG2 1 
ATOM   1601 C CD1 . ILE A 1 217 ? -23.421 -38.461 12.292  1.00  26.75 ? 217  ILE B CD1 1 
ATOM   1602 N N   . LEU A 1 218 ? -24.748 -36.686 6.689   1.00  22.78 ? 218  LEU B N   1 
ATOM   1603 C CA  . LEU A 1 218 ? -24.281 -35.791 5.638   1.00  24.02 ? 218  LEU B CA  1 
ATOM   1604 C C   . LEU A 1 218 ? -23.704 -34.559 6.307   1.00  26.44 ? 218  LEU B C   1 
ATOM   1605 O O   . LEU A 1 218 ? -24.370 -33.919 7.125   1.00  24.18 ? 218  LEU B O   1 
ATOM   1606 C CB  . LEU A 1 218 ? -25.422 -35.359 4.719   1.00  26.80 ? 218  LEU B CB  1 
ATOM   1607 C CG  . LEU A 1 218 ? -25.898 -36.375 3.679   1.00  30.17 ? 218  LEU B CG  1 
ATOM   1608 C CD1 . LEU A 1 218 ? -27.293 -36.028 3.174   1.00  30.66 ? 218  LEU B CD1 1 
ATOM   1609 C CD2 . LEU A 1 218 ? -24.912 -36.482 2.526   1.00  24.29 ? 218  LEU B CD2 1 
ATOM   1610 N N   . VAL A 1 219 ? -22.468 -34.231 5.945   1.00  23.40 ? 219  VAL B N   1 
ATOM   1611 C CA  . VAL A 1 219 ? -21.797 -33.061 6.493   1.00  24.30 ? 219  VAL B CA  1 
ATOM   1612 C C   . VAL A 1 219 ? -21.286 -32.187 5.367   1.00  30.00 ? 219  VAL B C   1 
ATOM   1613 O O   . VAL A 1 219 ? -20.561 -32.665 4.483   1.00  27.52 ? 219  VAL B O   1 
ATOM   1614 C CB  . VAL A 1 219 ? -20.612 -33.464 7.378   1.00  24.28 ? 219  VAL B CB  1 
ATOM   1615 C CG1 . VAL A 1 219 ? -19.790 -32.225 7.770   1.00  29.72 ? 219  VAL B CG1 1 
ATOM   1616 C CG2 . VAL A 1 219 ? -21.110 -34.188 8.622   1.00  22.23 ? 219  VAL B CG2 1 
ATOM   1617 N N   . ASP A 1 220 ? -21.668 -30.914 5.399   1.00  26.53 ? 220  ASP B N   1 
ATOM   1618 C CA  . ASP A 1 220 ? -21.211 -29.941 4.413   1.00  30.61 ? 220  ASP B CA  1 
ATOM   1619 C C   . ASP A 1 220 ? -20.981 -28.582 5.085   1.00  32.50 ? 220  ASP B C   1 
ATOM   1620 O O   . ASP A 1 220 ? -21.408 -28.367 6.223   1.00  25.45 ? 220  ASP B O   1 
ATOM   1621 C CB  . ASP A 1 220 ? -22.255 -29.820 3.298   1.00  32.72 ? 220  ASP B CB  1 
ATOM   1622 C CG  . ASP A 1 220 ? -21.639 -29.522 1.940   1.00  41.34 ? 220  ASP B CG  1 
ATOM   1623 O OD1 . ASP A 1 220 ? -20.420 -29.748 1.757   1.00  37.28 ? 220  ASP B OD1 1 
ATOM   1624 O OD2 . ASP A 1 220 ? -22.391 -29.078 1.046   1.00  44.82 ? 220  ASP B OD2 1 
ATOM   1625 N N   . ASP A 1 221 ? -20.309 -27.661 4.395   0.94  28.24 ? 221  ASP B N   1 
ATOM   1626 C CA  . ASP A 1 221 ? -20.099 -26.327 4.962   0.94  28.87 ? 221  ASP B CA  1 
ATOM   1627 C C   . ASP A 1 221 ? -21.364 -25.482 4.881   0.94  26.57 ? 221  ASP B C   1 
ATOM   1628 O O   . ASP A 1 221 ? -21.662 -24.693 5.772   0.94  27.80 ? 221  ASP B O   1 
ATOM   1629 C CB  . ASP A 1 221 ? -18.921 -25.598 4.298   0.94  27.16 ? 221  ASP B CB  1 
ATOM   1630 C CG  . ASP A 1 221 ? -19.114 -25.412 2.811   0.94  31.83 ? 221  ASP B CG  1 
ATOM   1631 O OD1 . ASP A 1 221 ? -19.563 -26.365 2.137   0.94  33.14 ? 221  ASP B OD1 1 
ATOM   1632 O OD2 . ASP A 1 221 ? -18.812 -24.306 2.314   0.94  36.70 ? 221  ASP B OD2 1 
ATOM   1633 N N   . MET A 1 222 ? -22.128 -25.651 3.815   1.00  30.06 ? 222  MET B N   1 
ATOM   1634 C CA  . MET A 1 222 ? -23.311 -24.841 3.670   1.00  26.37 ? 222  MET B CA  1 
ATOM   1635 C C   . MET A 1 222 ? -24.402 -25.540 2.871   1.00  34.19 ? 222  MET B C   1 
ATOM   1636 O O   . MET A 1 222 ? -24.133 -26.452 2.080   1.00  33.12 ? 222  MET B O   1 
ATOM   1637 C CB  . MET A 1 222 ? -22.951 -23.496 3.036   1.00  29.00 ? 222  MET B CB  1 
ATOM   1638 C CG  . MET A 1 222 ? -22.718 -23.530 1.540   1.00  38.47 ? 222  MET B CG  1 
ATOM   1639 S SD  . MET A 1 222 ? -22.357 -21.864 0.911   1.00  50.22 ? 222  MET B SD  1 
ATOM   1640 C CE  . MET A 1 222 ? -20.707 -21.570 1.569   1.00  38.59 ? 222  MET B CE  1 
ATOM   1641 N N   . ALA A 1 223 ? -25.637 -25.115 3.103   1.00  29.88 ? 223  ALA B N   1 
ATOM   1642 C CA  . ALA A 1 223 ? -26.758 -25.583 2.317   1.00  34.00 ? 223  ALA B CA  1 
ATOM   1643 C C   . ALA A 1 223 ? -27.570 -24.378 1.928   1.00  31.49 ? 223  ALA B C   1 
ATOM   1644 O O   . ALA A 1 223 ? -27.956 -23.562 2.770   1.00  32.78 ? 223  ALA B O   1 
ATOM   1645 C CB  . ALA A 1 223 ? -27.603 -26.561 3.105   1.00  32.36 ? 223  ALA B CB  1 
ATOM   1646 N N   . ASP A 1 224 ? -27.820 -24.266 0.635   1.00  34.62 ? 224  ASP B N   1 
ATOM   1647 C CA  . ASP A 1 224 ? -28.572 -23.150 0.121   1.00  35.78 ? 224  ASP B CA  1 
ATOM   1648 C C   . ASP A 1 224 ? -30.018 -23.346 -0.319  1.00  38.21 ? 224  ASP B C   1 
ATOM   1649 O O   . ASP A 1 224 ? -30.934 -22.799 0.290   1.00  35.45 ? 224  ASP B O   1 
ATOM   1650 C CB  . ASP A 1 224 ? -27.887 -22.603 -1.115  1.00  36.98 ? 224  ASP B CB  1 
ATOM   1651 C CG  . ASP A 1 224 ? -28.525 -21.343 -1.602  1.00  42.77 ? 224  ASP B CG  1 
ATOM   1652 O OD1 . ASP A 1 224 ? -29.363 -20.792 -0.852  1.00  37.71 ? 224  ASP B OD1 1 
ATOM   1653 O OD2 . ASP A 1 224 ? -28.183 -20.910 -2.727  1.00  43.99 ? 224  ASP B OD2 1 
ATOM   1654 N N   . THR A 1 225 ? -30.218 -24.130 -1.372  1.00  34.79 ? 225  THR B N   1 
ATOM   1655 C CA  . THR A 1 225 ? -31.567 -24.411 -1.858  1.00  39.94 ? 225  THR B CA  1 
ATOM   1656 C C   . THR A 1 225 ? -31.841 -25.851 -1.400  1.00  40.92 ? 225  THR B C   1 
ATOM   1657 O O   . THR A 1 225 ? -32.979 -26.313 -1.441  1.00  40.79 ? 225  THR B O   1 
ATOM   1658 C CB  . THR A 1 225 ? -31.753 -24.330 -3.372  1.00  38.70 ? 225  THR B CB  1 
ATOM   1659 O OG1 . THR A 1 225 ? -31.124 -25.455 -3.996  1.00  44.74 ? 225  THR B OG1 1 
ATOM   1660 C CG2 . THR A 1 225 ? -31.139 -23.042 -3.925  1.00  36.89 ? 225  THR B CG2 1 
ATOM   1661 N N   . CYS A 1 226 ? -30.792 -26.561 -0.985  1.00  40.03 ? 226  CYS B N   1 
ATOM   1662 C CA  . CYS A 1 226 ? -30.936 -27.877 -0.358  1.00  35.28 ? 226  CYS B CA  1 
ATOM   1663 C C   . CYS A 1 226 ? -31.308 -28.991 -1.321  1.00  38.55 ? 226  CYS B C   1 
ATOM   1664 O O   . CYS A 1 226 ? -31.618 -30.099 -0.888  1.00  38.87 ? 226  CYS B O   1 
ATOM   1665 C CB  . CYS A 1 226 ? -31.954 -27.826 0.785   1.00  33.26 ? 226  CYS B CB  1 
ATOM   1666 S SG  . CYS A 1 226 ? -31.358 -26.966 2.250   1.00  37.59 ? 226  CYS B SG  1 
ATOM   1667 N N   . GLY A 1 227 ? -31.292 -28.697 -2.618  1.00  38.19 ? 227  GLY B N   1 
ATOM   1668 C CA  . GLY A 1 227 ? -31.543 -29.716 -3.615  1.00  37.08 ? 227  GLY B CA  1 
ATOM   1669 C C   . GLY A 1 227 ? -30.570 -30.869 -3.454  1.00  40.31 ? 227  GLY B C   1 
ATOM   1670 O O   . GLY A 1 227 ? -30.965 -32.039 -3.519  1.00  36.54 ? 227  GLY B O   1 
ATOM   1671 N N   . THR A 1 228 ? -29.296 -30.550 -3.226  1.00  35.53 ? 228  THR B N   1 
ATOM   1672 C CA  . THR A 1 228 ? -28.276 -31.589 -3.133  1.00  39.82 ? 228  THR B CA  1 
ATOM   1673 C C   . THR A 1 228 ? -28.449 -32.478 -1.897  1.00  33.08 ? 228  THR B C   1 
ATOM   1674 O O   . THR A 1 228 ? -28.559 -33.693 -2.034  1.00  35.24 ? 228  THR B O   1 
ATOM   1675 C CB  . THR A 1 228 ? -26.830 -31.021 -3.173  1.00  49.85 ? 228  THR B CB  1 
ATOM   1676 O OG1 . THR A 1 228 ? -26.671 -30.170 -4.314  1.00  48.64 ? 228  THR B OG1 1 
ATOM   1677 C CG2 . THR A 1 228 ? -25.818 -32.159 -3.260  1.00  44.86 ? 228  THR B CG2 1 
ATOM   1678 N N   . ILE A 1 229 ? -28.490 -31.898 -0.699  1.00  32.18 ? 229  ILE B N   1 
ATOM   1679 C CA  . ILE A 1 229 ? -28.641 -32.735 0.499   1.00  34.13 ? 229  ILE B CA  1 
ATOM   1680 C C   . ILE A 1 229 ? -29.932 -33.554 0.462   1.00  30.63 ? 229  ILE B C   1 
ATOM   1681 O O   . ILE A 1 229 ? -29.968 -34.684 0.957   1.00  29.36 ? 229  ILE B O   1 
ATOM   1682 C CB  . ILE A 1 229 ? -28.573 -31.950 1.836   1.00  32.83 ? 229  ILE B CB  1 
ATOM   1683 C CG1 . ILE A 1 229 ? -29.540 -30.764 1.818   1.00  36.16 ? 229  ILE B CG1 1 
ATOM   1684 C CG2 . ILE A 1 229 ? -27.128 -31.520 2.154   1.00  34.82 ? 229  ILE B CG2 1 
ATOM   1685 C CD1 . ILE A 1 229 ? -29.726 -30.125 3.178   1.00  37.31 ? 229  ILE B CD1 1 
ATOM   1686 N N   . CYS A 1 230 ? -30.987 -32.993 -0.121  1.00  31.46 ? 230  CYS B N   1 
ATOM   1687 C CA  . CYS A 1 230 ? -32.244 -33.730 -0.197  1.00  33.99 ? 230  CYS B CA  1 
ATOM   1688 C C   . CYS A 1 230 ? -32.092 -34.946 -1.098  1.00  27.98 ? 230  CYS B C   1 
ATOM   1689 O O   . CYS A 1 230 ? -32.457 -36.050 -0.700  1.00  28.45 ? 230  CYS B O   1 
ATOM   1690 C CB  . CYS A 1 230 ? -33.404 -32.844 -0.632  1.00  32.56 ? 230  CYS B CB  1 
ATOM   1691 S SG  . CYS A 1 230 ? -33.908 -31.707 0.654   1.00  36.68 ? 230  CYS B SG  1 
ATOM   1692 N N   . HIS A 1 231 ? -31.524 -34.754 -2.285  0.60  28.41 ? 231  HIS B N   1 
ATOM   1693 C CA  . HIS A 1 231 ? -31.241 -35.875 -3.178  0.60  26.82 ? 231  HIS B CA  1 
ATOM   1694 C C   . HIS A 1 231 ? -30.235 -36.856 -2.567  0.60  27.70 ? 231  HIS B C   1 
ATOM   1695 O O   . HIS A 1 231 ? -30.381 -38.064 -2.713  0.60  24.19 ? 231  HIS B O   1 
ATOM   1696 C CB  . HIS A 1 231 ? -30.725 -35.383 -4.534  0.60  28.18 ? 231  HIS B CB  1 
ATOM   1697 C CG  . HIS A 1 231 ? -31.790 -34.823 -5.425  0.60  33.86 ? 231  HIS B CG  1 
ATOM   1698 N ND1 . HIS A 1 231 ? -32.487 -33.673 -5.124  0.60  39.07 ? 231  HIS B ND1 1 
ATOM   1699 C CD2 . HIS A 1 231 ? -32.272 -35.255 -6.614  0.60  35.23 ? 231  HIS B CD2 1 
ATOM   1700 C CE1 . HIS A 1 231 ? -33.351 -33.419 -6.091  0.60  35.70 ? 231  HIS B CE1 1 
ATOM   1701 N NE2 . HIS A 1 231 ? -33.244 -34.366 -7.004  0.60  38.91 ? 231  HIS B NE2 1 
ATOM   1702 N N   . ALA A 1 232 ? -29.213 -36.330 -1.891  1.00  27.10 ? 232  ALA B N   1 
ATOM   1703 C CA  . ALA A 1 232 ? -28.230 -37.169 -1.206  1.00  26.63 ? 232  ALA B CA  1 
ATOM   1704 C C   . ALA A 1 232 ? -28.861 -38.093 -0.154  1.00  21.69 ? 232  ALA B C   1 
ATOM   1705 O O   . ALA A 1 232 ? -28.462 -39.245 -0.034  1.00  26.45 ? 232  ALA B O   1 
ATOM   1706 C CB  . ALA A 1 232 ? -27.107 -36.308 -0.575  1.00  27.62 ? 232  ALA B CB  1 
ATOM   1707 N N   . ALA A 1 233 ? -29.829 -37.589 0.606   1.00  25.22 ? 233  ALA B N   1 
ATOM   1708 C CA  . ALA A 1 233 ? -30.490 -38.389 1.643   1.00  29.36 ? 233  ALA B CA  1 
ATOM   1709 C C   . ALA A 1 233 ? -31.260 -39.580 1.060   1.00  28.97 ? 233  ALA B C   1 
ATOM   1710 O O   . ALA A 1 233 ? -31.165 -40.704 1.570   1.00  28.13 ? 233  ALA B O   1 
ATOM   1711 C CB  . ALA A 1 233 ? -31.427 -37.531 2.471   1.00  28.24 ? 233  ALA B CB  1 
ATOM   1712 N N   . ASP A 1 234 ? -32.046 -39.312 0.023   1.00  26.69 ? 234  ASP B N   1 
ATOM   1713 C CA  . ASP A 1 234 ? -32.687 -40.365 -0.788  1.00  30.48 ? 234  ASP B CA  1 
ATOM   1714 C C   . ASP A 1 234 ? -31.705 -41.465 -1.164  1.00  28.34 ? 234  ASP B C   1 
ATOM   1715 O O   . ASP A 1 234 ? -31.917 -42.647 -0.892  1.00  28.58 ? 234  ASP B O   1 
ATOM   1716 C CB  . ASP A 1 234 ? -33.201 -39.782 -2.108  1.00  32.76 ? 234  ASP B CB  1 
ATOM   1717 C CG  . ASP A 1 234 ? -34.504 -39.037 -1.955  1.00  38.57 ? 234  ASP B CG  1 
ATOM   1718 O OD1 . ASP A 1 234 ? -35.096 -39.130 -0.868  1.00  35.80 ? 234  ASP B OD1 1 
ATOM   1719 O OD2 . ASP A 1 234 ? -34.931 -38.365 -2.933  1.00  42.66 ? 234  ASP B OD2 1 
ATOM   1720 N N   . LYS A 1 235 ? -30.637 -41.052 -1.833  1.00  30.93 ? 235  LYS B N   1 
ATOM   1721 C CA  . LYS A 1 235 ? -29.577 -41.954 -2.247  1.00  26.69 ? 235  LYS B CA  1 
ATOM   1722 C C   . LYS A 1 235 ? -29.047 -42.794 -1.091  1.00  28.57 ? 235  LYS B C   1 
ATOM   1723 O O   . LYS A 1 235 ? -28.864 -44.003 -1.217  1.00  30.01 ? 235  LYS B O   1 
ATOM   1724 C CB  . LYS A 1 235 ? -28.435 -41.145 -2.874  1.00  31.83 ? 235  LYS B CB  1 
ATOM   1725 C CG  . LYS A 1 235 ? -27.370 -41.987 -3.546  1.00  32.26 ? 235  LYS B CG  1 
ATOM   1726 C CD  . LYS A 1 235 ? -27.873 -42.497 -4.879  1.00  31.18 ? 235  LYS B CD  1 
ATOM   1727 C CE  . LYS A 1 235 ? -26.928 -43.549 -5.453  1.00  39.23 ? 235  LYS B CE  1 
ATOM   1728 N NZ  . LYS A 1 235 ? -27.286 -43.941 -6.857  1.00  44.32 ? 235  LYS B NZ  1 
ATOM   1729 N N   . LEU A 1 236 ? -28.789 -42.158 0.041   1.00  24.78 ? 236  LEU B N   1 
ATOM   1730 C CA  . LEU A 1 236 ? -28.232 -42.880 1.172   1.00  24.17 ? 236  LEU B CA  1 
ATOM   1731 C C   . LEU A 1 236 ? -29.200 -43.945 1.711   1.00  27.83 ? 236  LEU B C   1 
ATOM   1732 O O   . LEU A 1 236 ? -28.784 -45.054 2.007   1.00  25.25 ? 236  LEU B O   1 
ATOM   1733 C CB  . LEU A 1 236 ? -27.831 -41.904 2.282   1.00  22.41 ? 236  LEU B CB  1 
ATOM   1734 C CG  . LEU A 1 236 ? -26.592 -41.072 1.923   1.00  24.72 ? 236  LEU B CG  1 
ATOM   1735 C CD1 . LEU A 1 236 ? -26.408 -39.887 2.890   1.00  22.89 ? 236  LEU B CD1 1 
ATOM   1736 C CD2 . LEU A 1 236 ? -25.357 -41.965 1.912   1.00  23.40 ? 236  LEU B CD2 1 
ATOM   1737 N N   . LEU A 1 237 ? -30.477 -43.590 1.856   1.00  23.26 ? 237  LEU B N   1 
ATOM   1738 C CA  . LEU A 1 237 ? -31.514 -44.551 2.254   1.00  27.50 ? 237  LEU B CA  1 
ATOM   1739 C C   . LEU A 1 237 ? -31.601 -45.713 1.261   1.00  28.35 ? 237  LEU B C   1 
ATOM   1740 O O   . LEU A 1 237 ? -31.627 -46.871 1.665   1.00  27.97 ? 237  LEU B O   1 
ATOM   1741 C CB  . LEU A 1 237 ? -32.877 -43.864 2.410   1.00  25.45 ? 237  LEU B CB  1 
ATOM   1742 C CG  . LEU A 1 237 ? -33.088 -42.941 3.619   1.00  29.69 ? 237  LEU B CG  1 
ATOM   1743 C CD1 . LEU A 1 237 ? -34.538 -42.495 3.692   1.00  37.15 ? 237  LEU B CD1 1 
ATOM   1744 C CD2 . LEU A 1 237 ? -32.708 -43.641 4.922   1.00  26.82 ? 237  LEU B CD2 1 
ATOM   1745 N N   . SER A 1 238 ? -31.614 -45.397 -0.036  1.00  28.68 ? 238  SER B N   1 
ATOM   1746 C CA  . SER A 1 238 ? -31.548 -46.416 -1.094  1.00  30.35 ? 238  SER B CA  1 
ATOM   1747 C C   . SER A 1 238 ? -30.359 -47.355 -0.955  1.00  33.18 ? 238  SER B C   1 
ATOM   1748 O O   . SER A 1 238 ? -30.426 -48.522 -1.366  1.00  29.02 ? 238  SER B O   1 
ATOM   1749 C CB  . SER A 1 238 ? -31.479 -45.770 -2.482  1.00  27.56 ? 238  SER B CB  1 
ATOM   1750 O OG  . SER A 1 238 ? -32.708 -45.173 -2.810  1.00  33.00 ? 238  SER B OG  1 
ATOM   1751 N N   . ALA A 1 239 ? -29.255 -46.841 -0.414  1.00  27.49 ? 239  ALA B N   1 
ATOM   1752 C CA  . ALA A 1 239 ? -28.054 -47.653 -0.273  1.00  30.89 ? 239  ALA B CA  1 
ATOM   1753 C C   . ALA A 1 239 ? -28.113 -48.412 1.048   1.00  29.22 ? 239  ALA B C   1 
ATOM   1754 O O   . ALA A 1 239 ? -27.180 -49.116 1.410   1.00  31.41 ? 239  ALA B O   1 
ATOM   1755 C CB  . ALA A 1 239 ? -26.802 -46.792 -0.344  1.00  31.48 ? 239  ALA B CB  1 
ATOM   1756 N N   . GLY A 1 240 ? -29.215 -48.257 1.770   1.00  25.91 ? 240  GLY B N   1 
ATOM   1757 C CA  . GLY A 1 240 ? -29.424 -49.022 2.988   1.00  28.53 ? 240  GLY B CA  1 
ATOM   1758 C C   . GLY A 1 240 ? -29.101 -48.337 4.312   1.00  34.40 ? 240  GLY B C   1 
ATOM   1759 O O   . GLY A 1 240 ? -29.123 -48.987 5.364   1.00  31.32 ? 240  GLY B O   1 
ATOM   1760 N N   . ALA A 1 241 ? -28.814 -47.037 4.299   1.00  28.75 ? 241  ALA B N   1 
ATOM   1761 C CA  . ALA A 1 241 ? -28.615 -46.348 5.577   1.00  28.28 ? 241  ALA B CA  1 
ATOM   1762 C C   . ALA A 1 241 ? -29.868 -46.526 6.419   1.00  32.04 ? 241  ALA B C   1 
ATOM   1763 O O   . ALA A 1 241 ? -30.981 -46.575 5.886   1.00  30.12 ? 241  ALA B O   1 
ATOM   1764 C CB  . ALA A 1 241 ? -28.314 -44.864 5.377   1.00  26.66 ? 241  ALA B CB  1 
ATOM   1765 N N   . THR A 1 242 ? -29.677 -46.627 7.733   1.00  28.68 ? 242  THR B N   1 
ATOM   1766 C CA  . THR A 1 242 ? -30.772 -46.785 8.686   1.00  29.76 ? 242  THR B CA  1 
ATOM   1767 C C   . THR A 1 242 ? -31.555 -45.486 8.763   1.00  33.10 ? 242  THR B C   1 
ATOM   1768 O O   . THR A 1 242 ? -32.778 -45.462 8.739   1.00  25.68 ? 242  THR B O   1 
ATOM   1769 C CB  . THR A 1 242 ? -30.226 -47.080 10.077  1.00  29.83 ? 242  THR B CB  1 
ATOM   1770 O OG1 . THR A 1 242 ? -29.386 -48.239 10.016  1.00  43.63 ? 242  THR B OG1 1 
ATOM   1771 C CG2 . THR A 1 242 ? -31.370 -47.341 11.037  1.00  39.95 ? 242  THR B CG2 1 
ATOM   1772 N N   . ARG A 1 243 ? -30.824 -44.393 8.883   1.00  26.91 ? 243  ARG B N   1 
ATOM   1773 C CA  . ARG A 1 243 ? -31.417 -43.088 8.708   1.00  29.05 ? 243  ARG B CA  1 
ATOM   1774 C C   . ARG A 1 243 ? -30.321 -42.081 8.446   1.00  25.19 ? 243  ARG B C   1 
ATOM   1775 O O   . ARG A 1 243 ? -29.129 -42.419 8.504   1.00  24.51 ? 243  ARG B O   1 
ATOM   1776 C CB  . ARG A 1 243 ? -32.301 -42.680 9.888   1.00  34.11 ? 243  ARG B CB  1 
ATOM   1777 C CG  . ARG A 1 243 ? -31.611 -42.695 11.203  1.00  36.11 ? 243  ARG B CG  1 
ATOM   1778 C CD  . ARG A 1 243 ? -32.479 -43.293 12.309  1.00  39.80 ? 243  ARG B CD  1 
ATOM   1779 N NE  . ARG A 1 243 ? -31.619 -43.477 13.467  1.00  41.70 ? 243  ARG B NE  1 
ATOM   1780 C CZ  . ARG A 1 243 ? -31.266 -42.474 14.249  1.00  47.68 ? 243  ARG B CZ  1 
ATOM   1781 N NH1 . ARG A 1 243 ? -31.766 -41.282 13.981  1.00  49.38 ? 243  ARG B NH1 1 
ATOM   1782 N NH2 . ARG A 1 243 ? -30.445 -42.653 15.283  1.00  41.11 ? 243  ARG B NH2 1 
ATOM   1783 N N   . VAL A 1 244 ? -30.746 -40.858 8.148   1.00  21.94 ? 244  VAL B N   1 
ATOM   1784 C CA  . VAL A 1 244 ? -29.888 -39.824 7.583   1.00  24.45 ? 244  VAL B CA  1 
ATOM   1785 C C   . VAL A 1 244 ? -30.066 -38.522 8.342   1.00  26.21 ? 244  VAL B C   1 
ATOM   1786 O O   . VAL A 1 244 ? -31.186 -38.076 8.593   1.00  27.62 ? 244  VAL B O   1 
ATOM   1787 C CB  . VAL A 1 244 ? -30.226 -39.559 6.102   1.00  28.24 ? 244  VAL B CB  1 
ATOM   1788 C CG1 . VAL A 1 244 ? -29.273 -38.516 5.507   1.00  29.06 ? 244  VAL B CG1 1 
ATOM   1789 C CG2 . VAL A 1 244 ? -30.154 -40.856 5.289   1.00  24.22 ? 244  VAL B CG2 1 
ATOM   1790 N N   . TYR A 1 245 ? -28.942 -37.942 8.739   1.00  24.45 ? 245  TYR B N   1 
ATOM   1791 C CA  . TYR A 1 245 ? -28.906 -36.617 9.342   1.00  25.30 ? 245  TYR B CA  1 
ATOM   1792 C C   . TYR A 1 245 ? -28.170 -35.711 8.365   1.00  26.34 ? 245  TYR B C   1 
ATOM   1793 O O   . TYR A 1 245 ? -27.413 -36.192 7.531   1.00  26.07 ? 245  TYR B O   1 
ATOM   1794 C CB  . TYR A 1 245 ? -28.140 -36.667 10.649  1.00  25.35 ? 245  TYR B CB  1 
ATOM   1795 C CG  . TYR A 1 245 ? -28.854 -37.419 11.739  1.00  29.79 ? 245  TYR B CG  1 
ATOM   1796 C CD1 . TYR A 1 245 ? -28.757 -38.805 11.839  1.00  25.04 ? 245  TYR B CD1 1 
ATOM   1797 C CD2 . TYR A 1 245 ? -29.613 -36.742 12.675  1.00  27.78 ? 245  TYR B CD2 1 
ATOM   1798 C CE1 . TYR A 1 245 ? -29.396 -39.491 12.853  1.00  31.21 ? 245  TYR B CE1 1 
ATOM   1799 C CE2 . TYR A 1 245 ? -30.271 -37.418 13.680  1.00  33.29 ? 245  TYR B CE2 1 
ATOM   1800 C CZ  . TYR A 1 245 ? -30.156 -38.787 13.765  1.00  35.11 ? 245  TYR B CZ  1 
ATOM   1801 O OH  . TYR A 1 245 ? -30.808 -39.436 14.777  1.00  35.88 ? 245  TYR B OH  1 
ATOM   1802 N N   . ALA A 1 246 ? -28.414 -34.411 8.441   1.00  26.52 ? 246  ALA B N   1 
ATOM   1803 C CA  . ALA A 1 246 ? -27.585 -33.458 7.705   1.00  25.21 ? 246  ALA B CA  1 
ATOM   1804 C C   . ALA A 1 246 ? -27.101 -32.388 8.672   1.00  23.15 ? 246  ALA B C   1 
ATOM   1805 O O   . ALA A 1 246 ? -27.883 -31.808 9.403   1.00  23.39 ? 246  ALA B O   1 
ATOM   1806 C CB  . ALA A 1 246 ? -28.351 -32.840 6.548   1.00  27.57 ? 246  ALA B CB  1 
ATOM   1807 N N   . ILE A 1 247 ? -25.796 -32.158 8.690   1.00  23.86 ? 247  ILE B N   1 
ATOM   1808 C CA  . ILE A 1 247 ? -25.219 -31.158 9.568   1.00  24.04 ? 247  ILE B CA  1 
ATOM   1809 C C   . ILE A 1 247 ? -24.432 -30.181 8.714   1.00  24.98 ? 247  ILE B C   1 
ATOM   1810 O O   . ILE A 1 247 ? -23.541 -30.588 7.974   1.00  25.47 ? 247  ILE B O   1 
ATOM   1811 C CB  . ILE A 1 247 ? -24.288 -31.776 10.629  1.00  24.43 ? 247  ILE B CB  1 
ATOM   1812 C CG1 . ILE A 1 247 ? -25.019 -32.861 11.428  1.00  21.57 ? 247  ILE B CG1 1 
ATOM   1813 C CG2 . ILE A 1 247 ? -23.803 -30.690 11.588  1.00  21.62 ? 247  ILE B CG2 1 
ATOM   1814 C CD1 . ILE A 1 247 ? -24.175 -33.455 12.526  1.00  27.91 ? 247  ILE B CD1 1 
ATOM   1815 N N   . LEU A 1 248 ? -24.787 -28.902 8.790   1.00  23.51 ? 248  LEU B N   1 
ATOM   1816 C CA  . LEU A 1 248 ? -24.119 -27.876 7.980   1.00  27.82 ? 248  LEU B CA  1 
ATOM   1817 C C   . LEU A 1 248 ? -23.659 -26.787 8.908   1.00  30.97 ? 248  LEU B C   1 
ATOM   1818 O O   . LEU A 1 248 ? -24.330 -26.526 9.903   1.00  31.35 ? 248  LEU B O   1 
ATOM   1819 C CB  . LEU A 1 248 ? -25.080 -27.236 6.983   1.00  30.49 ? 248  LEU B CB  1 
ATOM   1820 C CG  . LEU A 1 248 ? -25.687 -28.063 5.854   1.00  36.08 ? 248  LEU B CG  1 
ATOM   1821 C CD1 . LEU A 1 248 ? -24.718 -29.145 5.428   1.00  33.84 ? 248  LEU B CD1 1 
ATOM   1822 C CD2 . LEU A 1 248 ? -27.006 -28.667 6.300   1.00  32.90 ? 248  LEU B CD2 1 
ATOM   1823 N N   . THR A 1 249 ? -22.557 -26.108 8.614   1.00  26.10 ? 249  THR B N   1 
ATOM   1824 C CA  . THR A 1 249 ? -22.336 -24.925 9.439   1.00  25.59 ? 249  THR B CA  1 
ATOM   1825 C C   . THR A 1 249 ? -23.251 -23.736 9.066   1.00  25.77 ? 249  THR B C   1 
ATOM   1826 O O   . THR A 1 249 ? -23.935 -23.194 9.938   1.00  25.04 ? 249  THR B O   1 
ATOM   1827 C CB  . THR A 1 249 ? -20.834 -24.583 9.742   1.00  30.13 ? 249  THR B CB  1 
ATOM   1828 O OG1 . THR A 1 249 ? -20.552 -23.203 9.472   1.00  39.60 ? 249  THR B OG1 1 
ATOM   1829 C CG2 . THR A 1 249 ? -19.870 -25.496 9.032   1.00  25.15 ? 249  THR B CG2 1 
ATOM   1830 N N   . HIS A 1 250 ? -23.318 -23.383 7.780   1.00  23.81 ? 250  HIS B N   1 
ATOM   1831 C CA  . HIS A 1 250 ? -24.096 -22.230 7.327   1.00  25.67 ? 250  HIS B CA  1 
ATOM   1832 C C   . HIS A 1 250 ? -25.432 -22.645 6.680   1.00  28.26 ? 250  HIS B C   1 
ATOM   1833 O O   . HIS A 1 250 ? -25.445 -23.234 5.588   1.00  27.73 ? 250  HIS B O   1 
ATOM   1834 C CB  . HIS A 1 250 ? -23.269 -21.369 6.330   1.00  26.59 ? 250  HIS B CB  1 
ATOM   1835 C CG  . HIS A 1 250 ? -21.873 -21.051 6.797   1.00  29.53 ? 250  HIS B CG  1 
ATOM   1836 N ND1 . HIS A 1 250 ? -21.604 -20.186 7.840   1.00  28.77 ? 250  HIS B ND1 1 
ATOM   1837 C CD2 . HIS A 1 250 ? -20.664 -21.483 6.352   1.00  27.63 ? 250  HIS B CD2 1 
ATOM   1838 C CE1 . HIS A 1 250 ? -20.297 -20.107 8.023   1.00  21.90 ? 250  HIS B CE1 1 
ATOM   1839 N NE2 . HIS A 1 250 ? -19.704 -20.886 7.131   1.00  23.84 ? 250  HIS B NE2 1 
ATOM   1840 N N   . GLY A 1 251 ? -26.546 -22.330 7.340   1.00  28.30 ? 251  GLY B N   1 
ATOM   1841 C CA  . GLY A 1 251 ? -27.864 -22.567 6.767   1.00  29.43 ? 251  GLY B CA  1 
ATOM   1842 C C   . GLY A 1 251 ? -28.436 -21.355 6.038   1.00  28.57 ? 251  GLY B C   1 
ATOM   1843 O O   . GLY A 1 251 ? -29.110 -20.512 6.628   1.00  29.23 ? 251  GLY B O   1 
ATOM   1844 N N   . ILE A 1 252 ? -28.143 -21.255 4.750   1.00  27.42 ? 252  ILE B N   1 
ATOM   1845 C CA  . ILE A 1 252 ? -28.697 -20.187 3.914   1.00  32.32 ? 252  ILE B CA  1 
ATOM   1846 C C   . ILE A 1 252 ? -30.191 -20.434 3.658   1.00  31.25 ? 252  ILE B C   1 
ATOM   1847 O O   . ILE A 1 252 ? -31.025 -19.546 3.818   1.00  33.37 ? 252  ILE B O   1 
ATOM   1848 C CB  . ILE A 1 252 ? -27.920 -20.075 2.581   1.00  38.11 ? 252  ILE B CB  1 
ATOM   1849 C CG1 . ILE A 1 252 ? -26.464 -19.691 2.862   1.00  35.61 ? 252  ILE B CG1 1 
ATOM   1850 C CG2 . ILE A 1 252 ? -28.579 -19.061 1.656   1.00  36.40 ? 252  ILE B CG2 1 
ATOM   1851 C CD1 . ILE A 1 252 ? -25.536 -19.819 1.665   1.00  38.86 ? 252  ILE B CD1 1 
ATOM   1852 N N   . PHE A 1 253 ? -30.520 -21.655 3.256   1.00  32.79 ? 253  PHE B N   1 
ATOM   1853 C CA  . PHE A 1 253 ? -31.909 -22.068 3.146   1.00  32.20 ? 253  PHE B CA  1 
ATOM   1854 C C   . PHE A 1 253 ? -32.750 -21.068 2.346   1.00  36.69 ? 253  PHE B C   1 
ATOM   1855 O O   . PHE A 1 253 ? -33.767 -20.587 2.842   1.00  32.04 ? 253  PHE B O   1 
ATOM   1856 C CB  . PHE A 1 253 ? -32.503 -22.245 4.553   1.00  32.78 ? 253  PHE B CB  1 
ATOM   1857 C CG  . PHE A 1 253 ? -31.857 -23.346 5.356   1.00  30.88 ? 253  PHE B CG  1 
ATOM   1858 C CD1 . PHE A 1 253 ? -31.719 -23.234 6.735   1.00  33.64 ? 253  PHE B CD1 1 
ATOM   1859 C CD2 . PHE A 1 253 ? -31.413 -24.499 4.742   1.00  33.22 ? 253  PHE B CD2 1 
ATOM   1860 C CE1 . PHE A 1 253 ? -31.130 -24.246 7.470   1.00  28.12 ? 253  PHE B CE1 1 
ATOM   1861 C CE2 . PHE A 1 253 ? -30.822 -25.515 5.480   1.00  28.34 ? 253  PHE B CE2 1 
ATOM   1862 C CZ  . PHE A 1 253 ? -30.690 -25.388 6.840   1.00  29.99 ? 253  PHE B CZ  1 
ATOM   1863 N N   . SER A 1 254 ? -32.338 -20.743 1.117   1.00  34.92 ? 254  SER B N   1 
ATOM   1864 C CA  . SER A 1 254 ? -33.128 -19.808 0.311   1.00  39.08 ? 254  SER B CA  1 
ATOM   1865 C C   . SER A 1 254 ? -34.093 -20.533 -0.637  1.00  41.02 ? 254  SER B C   1 
ATOM   1866 O O   . SER A 1 254 ? -34.148 -21.765 -0.660  1.00  38.17 ? 254  SER B O   1 
ATOM   1867 C CB  . SER A 1 254 ? -32.224 -18.841 -0.469  1.00  41.18 ? 254  SER B CB  1 
ATOM   1868 O OG  . SER A 1 254 ? -31.529 -19.503 -1.509  1.00  34.41 ? 254  SER B OG  1 
ATOM   1869 N N   . GLY A 1 255 ? -34.849 -19.767 -1.418  1.00  41.45 ? 255  GLY B N   1 
ATOM   1870 C CA  . GLY A 1 255 ? -35.768 -20.352 -2.383  1.00  40.80 ? 255  GLY B CA  1 
ATOM   1871 C C   . GLY A 1 255 ? -36.668 -21.409 -1.763  1.00  39.95 ? 255  GLY B C   1 
ATOM   1872 O O   . GLY A 1 255 ? -37.324 -21.159 -0.756  1.00  38.04 ? 255  GLY B O   1 
ATOM   1873 N N   . PRO A 1 256 ? -36.696 -22.610 -2.358  1.00  37.33 ? 256  PRO B N   1 
ATOM   1874 C CA  . PRO A 1 256 ? -37.592 -23.671 -1.892  1.00  42.91 ? 256  PRO B CA  1 
ATOM   1875 C C   . PRO A 1 256 ? -36.975 -24.552 -0.794  1.00  44.64 ? 256  PRO B C   1 
ATOM   1876 O O   . PRO A 1 256 ? -37.507 -25.623 -0.509  1.00  44.43 ? 256  PRO B O   1 
ATOM   1877 C CB  . PRO A 1 256 ? -37.796 -24.501 -3.157  1.00  40.18 ? 256  PRO B CB  1 
ATOM   1878 C CG  . PRO A 1 256 ? -36.475 -24.413 -3.850  1.00  40.64 ? 256  PRO B CG  1 
ATOM   1879 C CD  . PRO A 1 256 ? -35.894 -23.045 -3.512  1.00  44.24 ? 256  PRO B CD  1 
ATOM   1880 N N   . ALA A 1 257 ? -35.879 -24.115 -0.182  1.00  43.13 ? 257  ALA B N   1 
ATOM   1881 C CA  . ALA A 1 257 ? -35.198 -24.955 0.803   1.00  42.95 ? 257  ALA B CA  1 
ATOM   1882 C C   . ALA A 1 257 ? -36.152 -25.507 1.862   1.00  39.29 ? 257  ALA B C   1 
ATOM   1883 O O   . ALA A 1 257 ? -36.207 -26.717 2.081   1.00  39.22 ? 257  ALA B O   1 
ATOM   1884 C CB  . ALA A 1 257 ? -34.044 -24.201 1.463   1.00  37.44 ? 257  ALA B CB  1 
ATOM   1885 N N   . ILE A 1 258 ? -36.892 -24.621 2.523   1.00  38.08 ? 258  ILE B N   1 
ATOM   1886 C CA  . ILE A 1 258 ? -37.714 -25.031 3.654   1.00  39.50 ? 258  ILE B CA  1 
ATOM   1887 C C   . ILE A 1 258 ? -38.779 -26.038 3.230   1.00  43.29 ? 258  ILE B C   1 
ATOM   1888 O O   . ILE A 1 258 ? -39.102 -26.962 3.981   1.00  41.06 ? 258  ILE B O   1 
ATOM   1889 C CB  . ILE A 1 258 ? -38.326 -23.829 4.402   1.00  42.59 ? 258  ILE B CB  1 
ATOM   1890 C CG1 . ILE A 1 258 ? -37.212 -22.963 5.011   1.00  42.58 ? 258  ILE B CG1 1 
ATOM   1891 C CG2 . ILE A 1 258 ? -39.280 -24.292 5.498   1.00  40.27 ? 258  ILE B CG2 1 
ATOM   1892 C CD1 . ILE A 1 258 ? -36.145 -23.750 5.747   1.00  37.23 ? 258  ILE B CD1 1 
ATOM   1893 N N   . SER A 1 259 ? -39.295 -25.879 2.013   1.00  40.46 ? 259  SER B N   1 
ATOM   1894 C CA  . SER A 1 259 ? -40.241 -26.845 1.460   1.00  43.59 ? 259  SER B CA  1 
ATOM   1895 C C   . SER A 1 259 ? -39.555 -28.183 1.208   1.00  44.28 ? 259  SER B C   1 
ATOM   1896 O O   . SER A 1 259 ? -40.074 -29.238 1.579   1.00  44.30 ? 259  SER B O   1 
ATOM   1897 C CB  . SER A 1 259 ? -40.857 -26.320 0.158   1.00  49.13 ? 259  SER B CB  1 
ATOM   1898 O OG  . SER A 1 259 ? -41.651 -25.165 0.392   1.00  52.26 ? 259  SER B OG  1 
ATOM   1899 N N   . ARG A 1 260 ? -38.386 -28.130 0.575   1.00  43.54 ? 260  ARG B N   1 
ATOM   1900 C CA  . ARG A 1 260 ? -37.598 -29.328 0.282   1.00  43.50 ? 260  ARG B CA  1 
ATOM   1901 C C   . ARG A 1 260 ? -37.243 -30.131 1.534   1.00  39.35 ? 260  ARG B C   1 
ATOM   1902 O O   . ARG A 1 260 ? -37.263 -31.361 1.520   1.00  40.80 ? 260  ARG B O   1 
ATOM   1903 C CB  . ARG A 1 260 ? -36.323 -28.955 -0.473  1.00  42.58 ? 260  ARG B CB  1 
ATOM   1904 C CG  . ARG A 1 260 ? -36.264 -29.508 -1.884  1.00  46.40 ? 260  ARG B CG  1 
ATOM   1905 C CD  . ARG A 1 260 ? -36.499 -28.431 -2.904  1.00  44.45 ? 260  ARG B CD  1 
ATOM   1906 N NE  . ARG A 1 260 ? -35.255 -27.748 -3.224  1.00  46.00 ? 260  ARG B NE  1 
ATOM   1907 C CZ  . ARG A 1 260 ? -34.716 -27.706 -4.437  1.00  44.25 ? 260  ARG B CZ  1 
ATOM   1908 N NH1 . ARG A 1 260 ? -35.324 -28.300 -5.451  1.00  45.86 ? 260  ARG B NH1 1 
ATOM   1909 N NH2 . ARG A 1 260 ? -33.574 -27.060 -4.637  1.00  38.85 ? 260  ARG B NH2 1 
ATOM   1910 N N   . ILE A 1 261 ? -36.925 -29.426 2.612   1.00  37.95 ? 261  ILE B N   1 
ATOM   1911 C CA  . ILE A 1 261 ? -36.558 -30.061 3.871   1.00  40.99 ? 261  ILE B CA  1 
ATOM   1912 C C   . ILE A 1 261 ? -37.754 -30.751 4.530   1.00  44.29 ? 261  ILE B C   1 
ATOM   1913 O O   . ILE A 1 261 ? -37.658 -31.892 4.985   1.00  40.13 ? 261  ILE B O   1 
ATOM   1914 C CB  . ILE A 1 261 ? -35.955 -29.029 4.837   1.00  37.90 ? 261  ILE B CB  1 
ATOM   1915 C CG1 . ILE A 1 261 ? -34.593 -28.554 4.311   1.00  34.17 ? 261  ILE B CG1 1 
ATOM   1916 C CG2 . ILE A 1 261 ? -35.830 -29.608 6.244   1.00  42.89 ? 261  ILE B CG2 1 
ATOM   1917 C CD1 . ILE A 1 261 ? -33.984 -27.457 5.143   1.00  35.29 ? 261  ILE B CD1 1 
ATOM   1918 N N   . ASN A 1 262 ? -38.879 -30.047 4.583   1.00  43.92 ? 262  ASN B N   1 
ATOM   1919 C CA  . ASN A 1 262 ? -40.112 -30.610 5.115   1.00  45.24 ? 262  ASN B CA  1 
ATOM   1920 C C   . ASN A 1 262 ? -40.516 -31.917 4.434   1.00  42.16 ? 262  ASN B C   1 
ATOM   1921 O O   . ASN A 1 262 ? -41.141 -32.778 5.053   1.00  46.20 ? 262  ASN B O   1 
ATOM   1922 C CB  . ASN A 1 262 ? -41.241 -29.597 4.995   1.00  44.19 ? 262  ASN B CB  1 
ATOM   1923 C CG  . ASN A 1 262 ? -41.080 -28.437 5.952   1.00  46.39 ? 262  ASN B CG  1 
ATOM   1924 O OD1 . ASN A 1 262 ? -40.502 -28.581 7.035   1.00  46.21 ? 262  ASN B OD1 1 
ATOM   1925 N ND2 . ASN A 1 262 ? -41.595 -27.279 5.563   1.00  46.50 ? 262  ASN B ND2 1 
ATOM   1926 N N   . ASN A 1 263 ? -40.148 -32.070 3.167   1.00  40.21 ? 263  ASN B N   1 
ATOM   1927 C CA  . ASN A 1 263 ? -40.503 -33.265 2.413   1.00  42.22 ? 263  ASN B CA  1 
ATOM   1928 C C   . ASN A 1 263 ? -39.397 -34.309 2.395   1.00  46.25 ? 263  ASN B C   1 
ATOM   1929 O O   . ASN A 1 263 ? -39.603 -35.438 1.943   1.00  48.83 ? 263  ASN B O   1 
ATOM   1930 C CB  . ASN A 1 263 ? -40.887 -32.908 0.973   1.00  44.29 ? 263  ASN B CB  1 
ATOM   1931 C CG  . ASN A 1 263 ? -42.085 -31.964 0.901   1.00  49.93 ? 263  ASN B CG  1 
ATOM   1932 O OD1 . ASN A 1 263 ? -42.198 -31.151 -0.020  1.00  50.74 ? 263  ASN B OD1 1 
ATOM   1933 N ND2 . ASN A 1 263 ? -42.975 -32.057 1.887   1.00  45.47 ? 263  ASN B ND2 1 
ATOM   1934 N N   . ALA A 1 264 ? -38.224 -33.938 2.887   1.00  43.26 ? 264  ALA B N   1 
ATOM   1935 C CA  . ALA A 1 264 ? -37.072 -34.817 2.779   1.00  40.07 ? 264  ALA B CA  1 
ATOM   1936 C C   . ALA A 1 264 ? -37.055 -35.870 3.879   1.00  38.94 ? 264  ALA B C   1 
ATOM   1937 O O   . ALA A 1 264 ? -37.662 -35.706 4.941   1.00  40.10 ? 264  ALA B O   1 
ATOM   1938 C CB  . ALA A 1 264 ? -35.786 -34.010 2.786   1.00  39.82 ? 264  ALA B CB  1 
ATOM   1939 N N   . CYS A 1 265 ? -36.336 -36.946 3.606   1.00  35.84 ? 265  CYS B N   1 
ATOM   1940 C CA  . CYS A 1 265 ? -36.277 -38.084 4.491   1.00  38.31 ? 265  CYS B CA  1 
ATOM   1941 C C   . CYS A 1 265 ? -35.198 -37.927 5.569   1.00  43.72 ? 265  CYS B C   1 
ATOM   1942 O O   . CYS A 1 265 ? -34.740 -38.921 6.131   1.00  43.95 ? 265  CYS B O   1 
ATOM   1943 C CB  . CYS A 1 265 ? -36.034 -39.346 3.661   1.00  37.29 ? 265  CYS B CB  1 
ATOM   1944 S SG  . CYS A 1 265 ? -34.564 -39.270 2.567   1.00  51.07 ? 265  CYS B SG  1 
ATOM   1945 N N   . PHE A 1 266 ? -34.794 -36.688 5.857   1.00  39.36 ? 266  PHE B N   1 
ATOM   1946 C CA  . PHE A 1 266 ? -33.858 -36.420 6.954   1.00  39.54 ? 266  PHE B CA  1 
ATOM   1947 C C   . PHE A 1 266 ? -34.524 -36.680 8.277   1.00  37.56 ? 266  PHE B C   1 
ATOM   1948 O O   . PHE A 1 266 ? -35.702 -36.390 8.449   1.00  40.45 ? 266  PHE B O   1 
ATOM   1949 C CB  . PHE A 1 266 ? -33.423 -34.949 7.001   1.00  36.36 ? 266  PHE B CB  1 
ATOM   1950 C CG  . PHE A 1 266 ? -32.682 -34.488 5.797   1.00  36.60 ? 266  PHE B CG  1 
ATOM   1951 C CD1 . PHE A 1 266 ? -33.217 -33.506 4.984   1.00  39.46 ? 266  PHE B CD1 1 
ATOM   1952 C CD2 . PHE A 1 266 ? -31.445 -35.016 5.490   1.00  37.08 ? 266  PHE B CD2 1 
ATOM   1953 C CE1 . PHE A 1 266 ? -32.539 -33.065 3.881   1.00  38.96 ? 266  PHE B CE1 1 
ATOM   1954 C CE2 . PHE A 1 266 ? -30.750 -34.579 4.379   1.00  38.95 ? 266  PHE B CE2 1 
ATOM   1955 C CZ  . PHE A 1 266 ? -31.298 -33.599 3.574   1.00  38.49 ? 266  PHE B CZ  1 
ATOM   1956 N N   . GLU A 1 267 ? -33.753 -37.175 9.232   1.00  36.06 ? 267  GLU B N   1 
ATOM   1957 C CA  . GLU A 1 267 ? -34.235 -37.273 10.599  1.00  34.49 ? 267  GLU B CA  1 
ATOM   1958 C C   . GLU A 1 267 ? -34.166 -35.872 11.218  1.00  38.07 ? 267  GLU B C   1 
ATOM   1959 O O   . GLU A 1 267 ? -35.069 -35.457 11.939  1.00  39.66 ? 267  GLU B O   1 
ATOM   1960 C CB  . GLU A 1 267 ? -33.382 -38.284 11.375  1.00  32.87 ? 267  GLU B CB  1 
ATOM   1961 C CG  . GLU A 1 267 ? -33.790 -38.516 12.816  1.00  44.72 ? 267  GLU B CG  1 
ATOM   1962 C CD  . GLU A 1 267 ? -34.626 -39.779 12.993  1.00  50.21 ? 267  GLU B CD  1 
ATOM   1963 O OE1 . GLU A 1 267 ? -35.107 -40.330 11.976  1.00  46.17 ? 267  GLU B OE1 1 
ATOM   1964 O OE2 . GLU A 1 267 ? -34.789 -40.227 14.153  1.00  57.26 ? 267  GLU B OE2 1 
ATOM   1965 N N   . ALA A 1 268 ? -33.097 -35.140 10.909  1.00  31.48 ? 268  ALA B N   1 
ATOM   1966 C CA  . ALA A 1 268 ? -32.898 -33.772 11.397  1.00  30.32 ? 268  ALA B CA  1 
ATOM   1967 C C   . ALA A 1 268 ? -31.878 -33.038 10.528  1.00  32.87 ? 268  ALA B C   1 
ATOM   1968 O O   . ALA A 1 268 ? -30.990 -33.660 9.942   1.00  30.13 ? 268  ALA B O   1 
ATOM   1969 C CB  . ALA A 1 268 ? -32.437 -33.774 12.851  1.00  29.23 ? 268  ALA B CB  1 
ATOM   1970 N N   . VAL A 1 269 ? -32.019 -31.719 10.441  1.00  27.82 ? 269  VAL B N   1 
ATOM   1971 C CA  . VAL A 1 269 ? -31.066 -30.890 9.733   1.00  29.66 ? 269  VAL B CA  1 
ATOM   1972 C C   . VAL A 1 269 ? -30.465 -29.934 10.735  1.00  28.04 ? 269  VAL B C   1 
ATOM   1973 O O   . VAL A 1 269 ? -31.156 -29.094 11.303  1.00  28.92 ? 269  VAL B O   1 
ATOM   1974 C CB  . VAL A 1 269 ? -31.736 -30.096 8.590   1.00  30.84 ? 269  VAL B CB  1 
ATOM   1975 C CG1 . VAL A 1 269 ? -30.699 -29.324 7.806   1.00  28.77 ? 269  VAL B CG1 1 
ATOM   1976 C CG2 . VAL A 1 269 ? -32.510 -31.048 7.689   1.00  33.73 ? 269  VAL B CG2 1 
ATOM   1977 N N   . VAL A 1 270 ? -29.163 -30.060 10.946  1.00  23.73 ? 270  VAL B N   1 
ATOM   1978 C CA  . VAL A 1 270 ? -28.506 -29.319 12.009  1.00  24.41 ? 270  VAL B CA  1 
ATOM   1979 C C   . VAL A 1 270 ? -27.629 -28.230 11.407  1.00  26.44 ? 270  VAL B C   1 
ATOM   1980 O O   . VAL A 1 270 ? -26.814 -28.505 10.531  1.00  27.17 ? 270  VAL B O   1 
ATOM   1981 C CB  . VAL A 1 270 ? -27.648 -30.274 12.866  1.00  22.10 ? 270  VAL B CB  1 
ATOM   1982 C CG1 . VAL A 1 270 ? -26.887 -29.512 13.930  1.00  23.69 ? 270  VAL B CG1 1 
ATOM   1983 C CG2 . VAL A 1 270 ? -28.531 -31.353 13.488  1.00  27.88 ? 270  VAL B CG2 1 
ATOM   1984 N N   . VAL A 1 271 ? -27.794 -27.000 11.882  1.00  24.81 ? 271  VAL B N   1 
ATOM   1985 C CA  . VAL A 1 271 ? -26.996 -25.881 11.391  1.00  25.36 ? 271  VAL B CA  1 
ATOM   1986 C C   . VAL A 1 271 ? -26.525 -25.003 12.548  1.00  28.91 ? 271  VAL B C   1 
ATOM   1987 O O   . VAL A 1 271 ? -26.980 -25.164 13.685  1.00  27.86 ? 271  VAL B O   1 
ATOM   1988 C CB  . VAL A 1 271 ? -27.794 -25.037 10.372  1.00  25.73 ? 271  VAL B CB  1 
ATOM   1989 C CG1 . VAL A 1 271 ? -28.103 -25.872 9.127   1.00  31.24 ? 271  VAL B CG1 1 
ATOM   1990 C CG2 . VAL A 1 271 ? -29.084 -24.542 11.008  1.00  24.52 ? 271  VAL B CG2 1 
ATOM   1991 N N   . THR A 1 272 ? -25.594 -24.088 12.285  1.00  25.82 ? 272  THR B N   1 
ATOM   1992 C CA  . THR A 1 272 ? -25.185 -23.153 13.333  1.00  25.87 ? 272  THR B CA  1 
ATOM   1993 C C   . THR A 1 272 ? -25.994 -21.875 13.169  1.00  24.15 ? 272  THR B C   1 
ATOM   1994 O O   . THR A 1 272 ? -26.745 -21.737 12.218  1.00  20.98 ? 272  THR B O   1 
ATOM   1995 C CB  . THR A 1 272 ? -23.675 -22.807 13.315  1.00  22.55 ? 272  THR B CB  1 
ATOM   1996 O OG1 . THR A 1 272 ? -23.380 -21.977 12.186  1.00  25.25 ? 272  THR B OG1 1 
ATOM   1997 C CG2 . THR A 1 272 ? -22.821 -24.048 13.262  1.00  24.49 ? 272  THR B CG2 1 
ATOM   1998 N N   . ASN A 1 273 ? -25.854 -20.944 14.099  1.00  24.00 ? 273  ASN B N   1 
ATOM   1999 C CA  . ASN A 1 273 ? -26.554 -19.670 13.960  1.00  23.57 ? 273  ASN B CA  1 
ATOM   2000 C C   . ASN A 1 273 ? -25.692 -18.560 13.331  1.00  25.69 ? 273  ASN B C   1 
ATOM   2001 O O   . ASN A 1 273 ? -25.856 -17.389 13.662  1.00  24.94 ? 273  ASN B O   1 
ATOM   2002 C CB  . ASN A 1 273 ? -27.164 -19.217 15.303  1.00  25.43 ? 273  ASN B CB  1 
ATOM   2003 C CG  . ASN A 1 273 ? -26.129 -19.048 16.401  1.00  27.50 ? 273  ASN B CG  1 
ATOM   2004 O OD1 . ASN A 1 273 ? -24.989 -19.486 16.266  1.00  29.39 ? 273  ASN B OD1 1 
ATOM   2005 N ND2 . ASN A 1 273 ? -26.532 -18.424 17.515  1.00  30.48 ? 273  ASN B ND2 1 
ATOM   2006 N N   . THR A 1 274 ? -24.781 -18.924 12.427  1.00  27.67 ? 274  THR B N   1 
ATOM   2007 C CA  . THR A 1 274 ? -23.994 -17.925 11.704  1.00  24.78 ? 274  THR B CA  1 
ATOM   2008 C C   . THR A 1 274 ? -24.922 -17.125 10.797  1.00  30.37 ? 274  THR B C   1 
ATOM   2009 O O   . THR A 1 274 ? -24.614 -16.007 10.376  1.00  24.00 ? 274  THR B O   1 
ATOM   2010 C CB  . THR A 1 274 ? -22.882 -18.551 10.822  1.00  24.48 ? 274  THR B CB  1 
ATOM   2011 O OG1 . THR A 1 274 ? -23.444 -19.527 9.935   1.00  22.92 ? 274  THR B OG1 1 
ATOM   2012 C CG2 . THR A 1 274 ? -21.797 -19.211 11.676  1.00  26.05 ? 274  THR B CG2 1 
ATOM   2013 N N   . ILE A 1 275 ? -26.059 -17.729 10.491  1.00  27.70 ? 275  ILE B N   1 
ATOM   2014 C CA  . ILE A 1 275 ? -27.109 -17.081 9.737   1.00  27.36 ? 275  ILE B CA  1 
ATOM   2015 C C   . ILE A 1 275 ? -28.356 -17.261 10.579  1.00  30.60 ? 275  ILE B C   1 
ATOM   2016 O O   . ILE A 1 275 ? -28.539 -18.315 11.185  1.00  28.63 ? 275  ILE B O   1 
ATOM   2017 C CB  . ILE A 1 275 ? -27.291 -17.752 8.360   1.00  28.86 ? 275  ILE B CB  1 
ATOM   2018 C CG1 . ILE A 1 275 ? -26.032 -17.549 7.512   1.00  28.42 ? 275  ILE B CG1 1 
ATOM   2019 C CG2 . ILE A 1 275 ? -28.499 -17.192 7.631   1.00  31.96 ? 275  ILE B CG2 1 
ATOM   2020 C CD1 . ILE A 1 275 ? -26.096 -18.188 6.162   1.00  31.44 ? 275  ILE B CD1 1 
ATOM   2021 N N   . PRO A 1 276 ? -29.201 -16.228 10.658  1.00  29.61 ? 276  PRO B N   1 
ATOM   2022 C CA  . PRO A 1 276 ? -30.386 -16.341 11.519  1.00  32.80 ? 276  PRO B CA  1 
ATOM   2023 C C   . PRO A 1 276 ? -31.356 -17.435 11.052  1.00  33.51 ? 276  PRO B C   1 
ATOM   2024 O O   . PRO A 1 276 ? -31.651 -17.560 9.855   1.00  33.11 ? 276  PRO B O   1 
ATOM   2025 C CB  . PRO A 1 276 ? -31.030 -14.950 11.432  1.00  34.49 ? 276  PRO B CB  1 
ATOM   2026 C CG  . PRO A 1 276 ? -30.366 -14.259 10.272  1.00  39.05 ? 276  PRO B CG  1 
ATOM   2027 C CD  . PRO A 1 276 ? -29.011 -14.867 10.131  1.00  34.54 ? 276  PRO B CD  1 
ATOM   2028 N N   . GLN A 1 277 ? -31.834 -18.225 12.004  1.00  29.75 ? 277  GLN B N   1 
ATOM   2029 C CA  . GLN A 1 277 ? -32.625 -19.414 11.704  1.00  30.09 ? 277  GLN B CA  1 
ATOM   2030 C C   . GLN A 1 277 ? -34.031 -19.358 12.296  1.00  34.56 ? 277  GLN B C   1 
ATOM   2031 O O   . GLN A 1 277 ? -34.898 -20.151 11.929  1.00  36.61 ? 277  GLN B O   1 
ATOM   2032 C CB  . GLN A 1 277 ? -31.907 -20.654 12.245  1.00  27.19 ? 277  GLN B CB  1 
ATOM   2033 C CG  . GLN A 1 277 ? -30.479 -20.832 11.717  1.00  31.22 ? 277  GLN B CG  1 
ATOM   2034 C CD  . GLN A 1 277 ? -30.415 -20.925 10.194  1.00  34.44 ? 277  GLN B CD  1 
ATOM   2035 O OE1 . GLN A 1 277 ? -29.354 -20.743 9.590   1.00  31.49 ? 277  GLN B OE1 1 
ATOM   2036 N NE2 . GLN A 1 277 ? -31.557 -21.207 9.568   1.00  32.93 ? 277  GLN B NE2 1 
ATOM   2037 N N   . GLU A 1 278 ? -34.243 -18.425 13.212  0.20  32.67 ? 278  GLU B N   1 
ATOM   2038 C CA  . GLU A 1 278 ? -35.443 -18.404 14.039  0.20  35.17 ? 278  GLU B CA  1 
ATOM   2039 C C   . GLU A 1 278 ? -36.745 -18.440 13.231  0.20  37.91 ? 278  GLU B C   1 
ATOM   2040 O O   . GLU A 1 278 ? -37.652 -19.212 13.536  0.20  38.92 ? 278  GLU B O   1 
ATOM   2041 C CB  . GLU A 1 278 ? -35.392 -17.198 14.981  0.20  32.45 ? 278  GLU B CB  1 
ATOM   2042 C CG  . GLU A 1 278 ? -34.078 -17.097 15.768  0.20  32.06 ? 278  GLU B CG  1 
ATOM   2043 C CD  . GLU A 1 278 ? -32.866 -16.840 14.874  0.20  33.15 ? 278  GLU B CD  1 
ATOM   2044 O OE1 . GLU A 1 278 ? -32.940 -15.938 14.014  0.20  30.60 ? 278  GLU B OE1 1 
ATOM   2045 O OE2 . GLU A 1 278 ? -31.849 -17.553 15.022  0.20  33.86 ? 278  GLU B OE2 1 
ATOM   2046 N N   . ASP A 1 279 ? -36.823 -17.614 12.195  0.96  40.85 ? 279  ASP B N   1 
ATOM   2047 C CA  . ASP A 1 279 ? -37.989 -17.556 11.313  0.96  45.06 ? 279  ASP B CA  1 
ATOM   2048 C C   . ASP A 1 279 ? -38.122 -18.841 10.489  0.96  47.76 ? 279  ASP B C   1 
ATOM   2049 O O   . ASP A 1 279 ? -39.229 -19.337 10.276  0.96  51.01 ? 279  ASP B O   1 
ATOM   2050 C CB  . ASP A 1 279 ? -37.883 -16.327 10.389  0.96  51.26 ? 279  ASP B CB  1 
ATOM   2051 C CG  . ASP A 1 279 ? -39.146 -16.086 9.571   0.96  58.82 ? 279  ASP B CG  1 
ATOM   2052 O OD1 . ASP A 1 279 ? -39.021 -15.774 8.363   0.96  62.82 ? 279  ASP B OD1 1 
ATOM   2053 O OD2 . ASP A 1 279 ? -40.261 -16.200 10.130  0.96  59.53 ? 279  ASP B OD2 1 
ATOM   2054 N N   . LYS A 1 280 ? -36.990 -19.367 10.027  1.00  44.76 ? 280  LYS B N   1 
ATOM   2055 C CA  . LYS A 1 280 ? -36.955 -20.619 9.271   1.00  46.42 ? 280  LYS B CA  1 
ATOM   2056 C C   . LYS A 1 280 ? -37.510 -21.782 10.096  1.00  45.44 ? 280  LYS B C   1 
ATOM   2057 O O   . LYS A 1 280 ? -38.220 -22.641 9.578   1.00  47.74 ? 280  LYS B O   1 
ATOM   2058 C CB  . LYS A 1 280 ? -35.522 -20.944 8.834   1.00  43.03 ? 280  LYS B CB  1 
ATOM   2059 C CG  . LYS A 1 280 ? -34.908 -19.953 7.838   1.00  45.23 ? 280  LYS B CG  1 
ATOM   2060 C CD  . LYS A 1 280 ? -35.396 -20.217 6.430   1.00  43.38 ? 280  LYS B CD  1 
ATOM   2061 C CE  . LYS A 1 280 ? -35.065 -19.071 5.482   1.00  45.48 ? 280  LYS B CE  1 
ATOM   2062 N NZ  . LYS A 1 280 ? -33.600 -18.816 5.310   1.00  39.32 ? 280  LYS B NZ  1 
ATOM   2063 N N   . MET A 1 281 ? -37.177 -21.810 11.379  1.00  44.54 ? 281  MET B N   1 
ATOM   2064 C CA  . MET A 1 281 ? -37.567 -22.926 12.233  1.00  45.31 ? 281  MET B CA  1 
ATOM   2065 C C   . MET A 1 281 ? -39.076 -22.994 12.438  1.00  46.98 ? 281  MET B C   1 
ATOM   2066 O O   . MET A 1 281 ? -39.647 -24.082 12.509  1.00  47.52 ? 281  MET B O   1 
ATOM   2067 C CB  . MET A 1 281 ? -36.821 -22.877 13.567  1.00  33.34 ? 281  MET B CB  1 
ATOM   2068 C CG  . MET A 1 281 ? -35.323 -23.145 13.413  1.00  38.00 ? 281  MET B CG  1 
ATOM   2069 S SD  . MET A 1 281 ? -34.322 -22.657 14.833  1.00  45.97 ? 281  MET B SD  1 
ATOM   2070 C CE  . MET A 1 281 ? -34.873 -23.824 16.082  1.00  44.97 ? 281  MET B CE  1 
ATOM   2071 N N   . LYS A 1 282 ? -39.725 -21.835 12.508  0.99  45.54 ? 282  LYS B N   1 
ATOM   2072 C CA  . LYS A 1 282 ? -41.182 -21.800 12.641  0.99  45.51 ? 282  LYS B CA  1 
ATOM   2073 C C   . LYS A 1 282 ? -41.867 -22.578 11.520  0.99  47.96 ? 282  LYS B C   1 
ATOM   2074 O O   . LYS A 1 282 ? -42.901 -23.205 11.732  0.99  51.10 ? 282  LYS B O   1 
ATOM   2075 C CB  . LYS A 1 282 ? -41.690 -20.356 12.675  0.99  50.23 ? 282  LYS B CB  1 
ATOM   2076 C CG  . LYS A 1 282 ? -41.215 -19.565 13.882  0.99  51.96 ? 282  LYS B CG  1 
ATOM   2077 C CD  . LYS A 1 282 ? -41.718 -18.120 13.864  0.99  53.56 ? 282  LYS B CD  1 
ATOM   2078 C CE  . LYS A 1 282 ? -41.167 -17.347 15.066  0.99  64.32 ? 282  LYS B CE  1 
ATOM   2079 N NZ  . LYS A 1 282 ? -41.859 -16.042 15.298  0.99  67.65 ? 282  LYS B NZ  1 
ATOM   2080 N N   . HIS A 1 283 ? -41.286 -22.547 10.327  1.00  46.71 ? 283  HIS B N   1 
ATOM   2081 C CA  . HIS A 1 283 ? -41.871 -23.256 9.191   1.00  48.57 ? 283  HIS B CA  1 
ATOM   2082 C C   . HIS A 1 283 ? -41.211 -24.609 8.928   1.00  45.96 ? 283  HIS B C   1 
ATOM   2083 O O   . HIS A 1 283 ? -41.541 -25.284 7.954   1.00  46.22 ? 283  HIS B O   1 
ATOM   2084 C CB  . HIS A 1 283 ? -41.806 -22.394 7.929   1.00  49.74 ? 283  HIS B CB  1 
ATOM   2085 C CG  . HIS A 1 283 ? -42.506 -21.078 8.064   1.00  56.84 ? 283  HIS B CG  1 
ATOM   2086 N ND1 . HIS A 1 283 ? -43.840 -20.976 8.397   1.00  51.70 ? 283  HIS B ND1 1 
ATOM   2087 C CD2 . HIS A 1 283 ? -42.057 -19.810 7.911   1.00  55.85 ? 283  HIS B CD2 1 
ATOM   2088 C CE1 . HIS A 1 283 ? -44.182 -19.700 8.447   1.00  57.96 ? 283  HIS B CE1 1 
ATOM   2089 N NE2 . HIS A 1 283 ? -43.118 -18.972 8.155   1.00  59.01 ? 283  HIS B NE2 1 
ATOM   2090 N N   . CYS A 1 284 ? -40.288 -25.008 9.799   1.00  44.59 ? 284  CYS B N   1 
ATOM   2091 C CA  . CYS A 1 284 ? -39.517 -26.219 9.556   1.00  45.74 ? 284  CYS B CA  1 
ATOM   2092 C C   . CYS A 1 284 ? -39.006 -26.856 10.848  1.00  43.57 ? 284  CYS B C   1 
ATOM   2093 O O   . CYS A 1 284 ? -37.957 -26.477 11.373  1.00  37.93 ? 284  CYS B O   1 
ATOM   2094 C CB  . CYS A 1 284 ? -38.352 -25.908 8.619   1.00  40.07 ? 284  CYS B CB  1 
ATOM   2095 S SG  . CYS A 1 284 ? -37.448 -27.356 8.089   1.00  44.91 ? 284  CYS B SG  1 
ATOM   2096 N N   . SER A 1 285 ? -39.751 -27.839 11.343  1.00  41.73 ? 285  SER B N   1 
ATOM   2097 C CA  . SER A 1 285 ? -39.466 -28.441 12.643  1.00  41.56 ? 285  SER B CA  1 
ATOM   2098 C C   . SER A 1 285 ? -38.228 -29.348 12.643  1.00  39.82 ? 285  SER B C   1 
ATOM   2099 O O   . SER A 1 285 ? -37.715 -29.705 13.705  1.00  39.29 ? 285  SER B O   1 
ATOM   2100 C CB  . SER A 1 285 ? -40.688 -29.227 13.130  1.00  45.37 ? 285  SER B CB  1 
ATOM   2101 O OG  . SER A 1 285 ? -41.119 -30.146 12.138  1.00  47.89 ? 285  SER B OG  1 
ATOM   2102 N N   . LYS A 1 286 ? -37.759 -29.728 11.459  1.00  34.89 ? 286  LYS B N   1 
ATOM   2103 C CA  . LYS A 1 286 ? -36.573 -30.572 11.368  1.00  36.82 ? 286  LYS B CA  1 
ATOM   2104 C C   . LYS A 1 286 ? -35.284 -29.842 11.729  1.00  32.79 ? 286  LYS B C   1 
ATOM   2105 O O   . LYS A 1 286 ? -34.293 -30.464 12.103  1.00  33.72 ? 286  LYS B O   1 
ATOM   2106 C CB  . LYS A 1 286 ? -36.451 -31.185 9.977   1.00  33.57 ? 286  LYS B CB  1 
ATOM   2107 C CG  . LYS A 1 286 ? -37.406 -32.352 9.746   1.00  38.36 ? 286  LYS B CG  1 
ATOM   2108 C CD  . LYS A 1 286 ? -36.872 -33.257 8.643   1.00  45.05 ? 286  LYS B CD  1 
ATOM   2109 C CE  . LYS A 1 286 ? -37.890 -34.308 8.239   1.00  46.75 ? 286  LYS B CE  1 
ATOM   2110 N NZ  . LYS A 1 286 ? -38.552 -33.917 6.966   1.00  50.53 ? 286  LYS B NZ  1 
ATOM   2111 N N   . ILE A 1 287 ? -35.289 -28.523 11.613  1.00  27.93 ? 287  ILE B N   1 
ATOM   2112 C CA  . ILE A 1 287 ? -34.078 -27.754 11.871  1.00  28.69 ? 287  ILE B CA  1 
ATOM   2113 C C   . ILE A 1 287 ? -33.751 -27.626 13.354  1.00  33.21 ? 287  ILE B C   1 
ATOM   2114 O O   . ILE A 1 287 ? -34.596 -27.266 14.171  1.00  31.21 ? 287  ILE B O   1 
ATOM   2115 C CB  . ILE A 1 287 ? -34.148 -26.347 11.242  1.00  33.15 ? 287  ILE B CB  1 
ATOM   2116 C CG1 . ILE A 1 287 ? -34.356 -26.456 9.730   1.00  33.24 ? 287  ILE B CG1 1 
ATOM   2117 C CG2 . ILE A 1 287 ? -32.881 -25.567 11.558  1.00  28.55 ? 287  ILE B CG2 1 
ATOM   2118 C CD1 . ILE A 1 287 ? -34.503 -25.128 9.036   1.00  38.97 ? 287  ILE B CD1 1 
ATOM   2119 N N   . GLN A 1 288 ? -32.508 -27.941 13.689  1.00  25.80 ? 288  GLN B N   1 
ATOM   2120 C CA  . GLN A 1 288 ? -31.990 -27.699 15.007  1.00  25.61 ? 288  GLN B CA  1 
ATOM   2121 C C   . GLN A 1 288 ? -30.765 -26.817 14.863  1.00  27.92 ? 288  GLN B C   1 
ATOM   2122 O O   . GLN A 1 288 ? -30.041 -26.910 13.870  1.00  30.62 ? 288  GLN B O   1 
ATOM   2123 C CB  . GLN A 1 288 ? -31.632 -29.025 15.692  1.00  28.05 ? 288  GLN B CB  1 
ATOM   2124 C CG  . GLN A 1 288 ? -32.871 -29.878 15.995  1.00  30.75 ? 288  GLN B CG  1 
ATOM   2125 C CD  . GLN A 1 288 ? -32.531 -31.153 16.728  1.00  32.49 ? 288  GLN B CD  1 
ATOM   2126 O OE1 . GLN A 1 288 ? -32.957 -32.235 16.336  1.00  36.03 ? 288  GLN B OE1 1 
ATOM   2127 N NE2 . GLN A 1 288 ? -31.752 -31.034 17.799  1.00  35.26 ? 288  GLN B NE2 1 
ATOM   2128 N N   . VAL A 1 289 ? -30.542 -25.963 15.852  1.00  28.67 ? 289  VAL B N   1 
ATOM   2129 C CA  . VAL A 1 289 ? -29.502 -24.940 15.774  1.00  27.92 ? 289  VAL B CA  1 
ATOM   2130 C C   . VAL A 1 289 ? -28.439 -25.109 16.840  1.00  32.10 ? 289  VAL B C   1 
ATOM   2131 O O   . VAL A 1 289 ? -28.750 -25.310 18.022  1.00  36.04 ? 289  VAL B O   1 
ATOM   2132 C CB  . VAL A 1 289 ? -30.102 -23.528 15.904  1.00  32.03 ? 289  VAL B CB  1 
ATOM   2133 C CG1 . VAL A 1 289 ? -29.010 -22.477 15.909  1.00  30.19 ? 289  VAL B CG1 1 
ATOM   2134 C CG2 . VAL A 1 289 ? -31.073 -23.268 14.769  1.00  33.57 ? 289  VAL B CG2 1 
ATOM   2135 N N   . ILE A 1 290 ? -27.181 -25.049 16.415  1.00  28.64 ? 290  ILE B N   1 
ATOM   2136 C CA  . ILE A 1 290 ? -26.059 -24.973 17.327  1.00  26.18 ? 290  ILE B CA  1 
ATOM   2137 C C   . ILE A 1 290 ? -25.660 -23.508 17.475  1.00  32.01 ? 290  ILE B C   1 
ATOM   2138 O O   . ILE A 1 290 ? -25.379 -22.824 16.491  1.00  26.91 ? 290  ILE B O   1 
ATOM   2139 C CB  . ILE A 1 290 ? -24.866 -25.803 16.817  1.00  28.96 ? 290  ILE B CB  1 
ATOM   2140 C CG1 . ILE A 1 290 ? -25.222 -27.294 16.757  1.00  26.29 ? 290  ILE B CG1 1 
ATOM   2141 C CG2 . ILE A 1 290 ? -23.618 -25.597 17.698  1.00  31.02 ? 290  ILE B CG2 1 
ATOM   2142 C CD1 . ILE A 1 290 ? -24.117 -28.143 16.127  1.00  29.32 ? 290  ILE B CD1 1 
ATOM   2143 N N   . ASP A 1 291 ? -25.647 -23.027 18.710  1.00  28.48 ? 291  ASP B N   1 
ATOM   2144 C CA  . ASP A 1 291 ? -25.280 -21.645 18.987  1.00  31.74 ? 291  ASP B CA  1 
ATOM   2145 C C   . ASP A 1 291 ? -23.761 -21.492 18.949  1.00  31.70 ? 291  ASP B C   1 
ATOM   2146 O O   . ASP A 1 291 ? -23.047 -22.144 19.697  1.00  30.89 ? 291  ASP B O   1 
ATOM   2147 C CB  . ASP A 1 291 ? -25.835 -21.235 20.350  1.00  32.16 ? 291  ASP B CB  1 
ATOM   2148 C CG  . ASP A 1 291 ? -25.431 -19.829 20.758  1.00  36.21 ? 291  ASP B CG  1 
ATOM   2149 O OD1 . ASP A 1 291 ? -24.946 -19.050 19.909  1.00  29.44 ? 291  ASP B OD1 1 
ATOM   2150 O OD2 . ASP A 1 291 ? -25.629 -19.499 21.942  1.00  37.13 ? 291  ASP B OD2 1 
ATOM   2151 N N   . ILE A 1 292 ? -23.261 -20.647 18.058  1.00  28.68 ? 292  ILE B N   1 
ATOM   2152 C CA  . ILE A 1 292 ? -21.817 -20.461 17.959  1.00  28.20 ? 292  ILE B CA  1 
ATOM   2153 C C   . ILE A 1 292 ? -21.349 -19.114 18.512  1.00  27.98 ? 292  ILE B C   1 
ATOM   2154 O O   . ILE A 1 292 ? -20.175 -18.734 18.371  1.00  24.15 ? 292  ILE B O   1 
ATOM   2155 C CB  . ILE A 1 292 ? -21.287 -20.716 16.513  1.00  30.51 ? 292  ILE B CB  1 
ATOM   2156 C CG1 . ILE A 1 292 ? -22.126 -19.973 15.469  1.00  25.88 ? 292  ILE B CG1 1 
ATOM   2157 C CG2 . ILE A 1 292 ? -21.287 -22.211 16.202  1.00  26.64 ? 292  ILE B CG2 1 
ATOM   2158 C CD1 . ILE A 1 292 ? -21.912 -18.459 15.438  1.00  23.75 ? 292  ILE B CD1 1 
ATOM   2159 N N   . SER A 1 293 ? -22.261 -18.401 19.168  1.00  26.35 ? 293  SER B N   1 
ATOM   2160 C CA  . SER A 1 293 ? -21.925 -17.087 19.706  1.00  26.68 ? 293  SER B CA  1 
ATOM   2161 C C   . SER A 1 293 ? -20.765 -17.130 20.705  1.00  24.19 ? 293  SER B C   1 
ATOM   2162 O O   . SER A 1 293 ? -19.969 -16.195 20.769  1.00  26.36 ? 293  SER B O   1 
ATOM   2163 C CB  . SER A 1 293 ? -23.140 -16.422 20.342  1.00  28.09 ? 293  SER B CB  1 
ATOM   2164 O OG  . SER A 1 293 ? -23.624 -17.163 21.440  1.00  29.97 ? 293  SER B OG  1 
ATOM   2165 N N   . MET A 1 294 ? -20.671 -18.206 21.477  0.80  23.94 ? 294  MET B N   1 
ATOM   2166 C CA  . MET A 1 294 ? -19.623 -18.306 22.492  0.80  28.56 ? 294  MET B CA  1 
ATOM   2167 C C   . MET A 1 294 ? -18.264 -18.480 21.833  0.80  24.29 ? 294  MET B C   1 
ATOM   2168 O O   . MET A 1 294 ? -17.246 -17.968 22.308  0.80  18.33 ? 294  MET B O   1 
ATOM   2169 C CB  . MET A 1 294 ? -19.911 -19.459 23.469  0.80  30.79 ? 294  MET B CB  1 
ATOM   2170 C CG  . MET A 1 294 ? -19.783 -20.860 22.867  0.80  36.13 ? 294  MET B CG  1 
ATOM   2171 S SD  . MET A 1 294 ? -20.967 -21.173 21.544  0.80  45.46 ? 294  MET B SD  1 
ATOM   2172 C CE  . MET A 1 294 ? -22.499 -20.723 22.378  0.80  38.11 ? 294  MET B CE  1 
ATOM   2173 N N   . ILE A 1 295 ? -18.250 -19.196 20.712  1.00  24.14 ? 295  ILE B N   1 
ATOM   2174 C CA  . ILE A 1 295 ? -17.011 -19.367 19.973  1.00  24.08 ? 295  ILE B CA  1 
ATOM   2175 C C   . ILE A 1 295 ? -16.554 -18.036 19.378  1.00  21.27 ? 295  ILE B C   1 
ATOM   2176 O O   . ILE A 1 295 ? -15.381 -17.657 19.479  1.00  25.93 ? 295  ILE B O   1 
ATOM   2177 C CB  . ILE A 1 295 ? -17.153 -20.441 18.881  1.00  23.96 ? 295  ILE B CB  1 
ATOM   2178 C CG1 . ILE A 1 295 ? -17.451 -21.797 19.528  1.00  33.07 ? 295  ILE B CG1 1 
ATOM   2179 C CG2 . ILE A 1 295 ? -15.881 -20.505 18.045  1.00  25.07 ? 295  ILE B CG2 1 
ATOM   2180 C CD1 . ILE A 1 295 ? -18.014 -22.849 18.574  1.00  32.36 ? 295  ILE B CD1 1 
ATOM   2181 N N   . LEU A 1 296 ? -17.482 -17.315 18.765  1.00  22.11 ? 296  LEU B N   1 
ATOM   2182 C CA  . LEU A 1 296 ? -17.150 -15.999 18.241  1.00  21.44 ? 296  LEU B CA  1 
ATOM   2183 C C   . LEU A 1 296 ? -16.730 -15.015 19.359  1.00  22.70 ? 296  LEU B C   1 
ATOM   2184 O O   . LEU A 1 296 ? -15.727 -14.329 19.225  1.00  22.89 ? 296  LEU B O   1 
ATOM   2185 C CB  . LEU A 1 296 ? -18.316 -15.446 17.416  1.00  19.28 ? 296  LEU B CB  1 
ATOM   2186 C CG  . LEU A 1 296 ? -18.537 -16.110 16.050  1.00  21.20 ? 296  LEU B CG  1 
ATOM   2187 C CD1 . LEU A 1 296 ? -19.754 -15.523 15.410  1.00  25.59 ? 296  LEU B CD1 1 
ATOM   2188 C CD2 . LEU A 1 296 ? -17.319 -15.907 15.132  1.00  22.25 ? 296  LEU B CD2 1 
ATOM   2189 N N   . ALA A 1 297 ? -17.494 -14.966 20.454  1.00  21.72 ? 297  ALA B N   1 
ATOM   2190 C CA  . ALA A 1 297 ? -17.185 -14.085 21.586  1.00  25.54 ? 297  ALA B CA  1 
ATOM   2191 C C   . ALA A 1 297 ? -15.784 -14.346 22.125  1.00  21.26 ? 297  ALA B C   1 
ATOM   2192 O O   . ALA A 1 297 ? -15.048 -13.405 22.444  1.00  27.06 ? 297  ALA B O   1 
ATOM   2193 C CB  . ALA A 1 297 ? -18.236 -14.238 22.710  1.00  22.64 ? 297  ALA B CB  1 
ATOM   2194 N N   . GLU A 1 298 ? -15.416 -15.618 22.205  0.50  18.93 ? 298  GLU B N   1 
ATOM   2195 C CA  . GLU A 1 298 ? -14.104 -16.020 22.687  0.50  20.68 ? 298  GLU B CA  1 
ATOM   2196 C C   . GLU A 1 298 ? -12.972 -15.623 21.727  0.50  21.52 ? 298  GLU B C   1 
ATOM   2197 O O   . GLU A 1 298 ? -11.927 -15.168 22.157  0.50  19.12 ? 298  GLU B O   1 
ATOM   2198 C CB  . GLU A 1 298 ? -14.093 -17.523 22.943  0.50  23.96 ? 298  GLU B CB  1 
ATOM   2199 C CG  . GLU A 1 298 ? -12.910 -18.028 23.728  0.50  32.42 ? 298  GLU B CG  1 
ATOM   2200 C CD  . GLU A 1 298 ? -12.932 -17.611 25.192  0.50  33.63 ? 298  GLU B CD  1 
ATOM   2201 O OE1 . GLU A 1 298 ? -13.755 -16.752 25.581  0.50  29.25 ? 298  GLU B OE1 1 
ATOM   2202 O OE2 . GLU A 1 298 ? -12.112 -18.154 25.955  0.50  36.83 ? 298  GLU B OE2 1 
ATOM   2203 N N   . ALA A 1 299 ? -13.195 -15.787 20.426  1.00  22.42 ? 299  ALA B N   1 
ATOM   2204 C CA  . ALA A 1 299 ? -12.206 -15.397 19.421  1.00  24.77 ? 299  ALA B CA  1 
ATOM   2205 C C   . ALA A 1 299 ? -11.950 -13.890 19.500  1.00  23.11 ? 299  ALA B C   1 
ATOM   2206 O O   . ALA A 1 299 ? -10.821 -13.435 19.338  1.00  26.28 ? 299  ALA B O   1 
ATOM   2207 C CB  . ALA A 1 299 ? -12.668 -15.813 18.013  1.00  22.15 ? 299  ALA B CB  1 
ATOM   2208 N N   . ILE A 1 300 ? -13.003 -13.127 19.768  1.00  22.70 ? 300  ILE B N   1 
ATOM   2209 C CA  . ILE A 1 300 ? -12.909 -11.678 19.877  1.00  23.80 ? 300  ILE B CA  1 
ATOM   2210 C C   . ILE A 1 300 ? -12.175 -11.284 21.150  1.00  26.37 ? 300  ILE B C   1 
ATOM   2211 O O   . ILE A 1 300 ? -11.326 -10.398 21.146  1.00  23.05 ? 300  ILE B O   1 
ATOM   2212 C CB  . ILE A 1 300 ? -14.301 -11.034 19.942  1.00  21.49 ? 300  ILE B CB  1 
ATOM   2213 C CG1 . ILE A 1 300 ? -15.020 -11.110 18.589  1.00  23.86 ? 300  ILE B CG1 1 
ATOM   2214 C CG2 . ILE A 1 300 ? -14.175 -9.593  20.351  1.00  21.92 ? 300  ILE B CG2 1 
ATOM   2215 C CD1 . ILE A 1 300 ? -16.512 -10.842 18.696  1.00  21.12 ? 300  ILE B CD1 1 
ATOM   2216 N N   . ARG A 1 301 ? -12.510 -11.960 22.242  1.00  23.38 ? 301  ARG B N   1 
ATOM   2217 C CA  . ARG A 1 301 ? -11.847 -11.716 23.513  1.00  24.88 ? 301  ARG B CA  1 
ATOM   2218 C C   . ARG A 1 301 ? -10.367 -12.091 23.436  1.00  26.41 ? 301  ARG B C   1 
ATOM   2219 O O   . ARG A 1 301 ? -9.508  -11.335 23.897  1.00  29.33 ? 301  ARG B O   1 
ATOM   2220 C CB  . ARG A 1 301 ? -12.550 -12.511 24.614  1.00  24.46 ? 301  ARG B CB  1 
ATOM   2221 C CG  . ARG A 1 301 ? -11.773 -12.627 25.918  1.00  33.67 ? 301  ARG B CG  1 
ATOM   2222 C CD  . ARG A 1 301 ? -12.397 -13.701 26.817  1.00  35.92 ? 301  ARG B CD  1 
ATOM   2223 N NE  . ARG A 1 301 ? -11.512 -14.057 27.923  1.00  49.05 ? 301  ARG B NE  1 
ATOM   2224 C CZ  . ARG A 1 301 ? -10.540 -14.962 27.858  1.00  48.98 ? 301  ARG B CZ  1 
ATOM   2225 N NH1 . ARG A 1 301 ? -10.308 -15.622 26.736  1.00  46.19 ? 301  ARG B NH1 1 
ATOM   2226 N NH2 . ARG A 1 301 ? -9.795  -15.211 28.926  1.00  58.70 ? 301  ARG B NH2 1 
ATOM   2227 N N   . ARG A 1 302 ? -10.067 -13.250 22.857  0.70  24.35 ? 302  ARG B N   1 
ATOM   2228 C CA  . ARG A 1 302 ? -8.674  -13.678 22.700  0.70  29.73 ? 302  ARG B CA  1 
ATOM   2229 C C   . ARG A 1 302 ? -7.902  -12.685 21.825  0.70  29.53 ? 302  ARG B C   1 
ATOM   2230 O O   . ARG A 1 302 ? -6.787  -12.280 22.156  0.70  33.36 ? 302  ARG B O   1 
ATOM   2231 C CB  . ARG A 1 302 ? -8.582  -15.080 22.087  0.70  29.40 ? 302  ARG B CB  1 
ATOM   2232 C CG  . ARG A 1 302 ? -9.387  -16.174 22.783  0.70  31.80 ? 302  ARG B CG  1 
ATOM   2233 C CD  . ARG A 1 302 ? -8.722  -16.695 24.044  0.70  41.20 ? 302  ARG B CD  1 
ATOM   2234 N NE  . ARG A 1 302 ? -9.549  -17.700 24.715  0.70  43.87 ? 302  ARG B NE  1 
ATOM   2235 C CZ  . ARG A 1 302 ? -9.159  -18.942 24.994  0.70  44.37 ? 302  ARG B CZ  1 
ATOM   2236 N NH1 . ARG A 1 302 ? -7.938  -19.356 24.667  0.70  36.36 ? 302  ARG B NH1 1 
ATOM   2237 N NH2 . ARG A 1 302 ? -9.990  -19.771 25.610  0.70  45.35 ? 302  ARG B NH2 1 
ATOM   2238 N N   . THR A 1 303 ? -8.514  -12.299 20.707  1.00  26.19 ? 303  THR B N   1 
ATOM   2239 C CA  . THR A 1 303 ? -7.935  -11.338 19.772  1.00  29.55 ? 303  THR B CA  1 
ATOM   2240 C C   . THR A 1 303 ? -7.594  -10.022 20.454  1.00  30.17 ? 303  THR B C   1 
ATOM   2241 O O   . THR A 1 303 ? -6.536  -9.441  20.219  1.00  32.16 ? 303  THR B O   1 
ATOM   2242 C CB  . THR A 1 303 ? -8.927  -11.016 18.622  1.00  29.23 ? 303  THR B CB  1 
ATOM   2243 O OG1 . THR A 1 303 ? -9.324  -12.226 17.974  1.00  35.00 ? 303  THR B OG1 1 
ATOM   2244 C CG2 . THR A 1 303 ? -8.299  -10.104 17.612  1.00  32.19 ? 303  THR B CG2 1 
ATOM   2245 N N   . HIS A 1 304 ? -8.511  -9.528  21.273  1.00  27.66 ? 304  HIS B N   1 
ATOM   2246 C CA  . HIS A 1 304 ? -8.275  -8.274  21.978  1.00  26.33 ? 304  HIS B CA  1 
ATOM   2247 C C   . HIS A 1 304 ? -7.139  -8.445  23.004  1.00  30.19 ? 304  HIS B C   1 
ATOM   2248 O O   . HIS A 1 304 ? -6.320  -7.552  23.162  1.00  31.45 ? 304  HIS B O   1 
ATOM   2249 C CB  . HIS A 1 304 ? -9.563  -7.788  22.645  1.00  27.01 ? 304  HIS B CB  1 
ATOM   2250 C CG  . HIS A 1 304 ? -9.399  -6.522  23.430  1.00  30.81 ? 304  HIS B CG  1 
ATOM   2251 N ND1 . HIS A 1 304 ? -9.292  -5.280  22.835  1.00  27.75 ? 304  HIS B ND1 1 
ATOM   2252 C CD2 . HIS A 1 304 ? -9.318  -6.308  24.766  1.00  28.40 ? 304  HIS B CD2 1 
ATOM   2253 C CE1 . HIS A 1 304 ? -9.157  -4.357  23.771  1.00  30.96 ? 304  HIS B CE1 1 
ATOM   2254 N NE2 . HIS A 1 304 ? -9.164  -4.955  24.951  1.00  29.30 ? 304  HIS B NE2 1 
ATOM   2255 N N   . ASN A 1 305 ? -7.076  -9.601  23.665  1.00  32.24 ? 305  ASN B N   1 
ATOM   2256 C CA  . ASN A 1 305 ? -6.104  -9.833  24.753  1.00  34.46 ? 305  ASN B CA  1 
ATOM   2257 C C   . ASN A 1 305 ? -4.747  -10.334 24.302  1.00  38.32 ? 305  ASN B C   1 
ATOM   2258 O O   . ASN A 1 305 ? -3.802  -10.375 25.090  1.00  39.79 ? 305  ASN B O   1 
ATOM   2259 C CB  . ASN A 1 305 ? -6.636  -10.853 25.758  1.00  36.51 ? 305  ASN B CB  1 
ATOM   2260 C CG  . ASN A 1 305 ? -7.797  -10.337 26.547  1.00  38.30 ? 305  ASN B CG  1 
ATOM   2261 O OD1 . ASN A 1 305 ? -8.023  -9.137  26.616  1.00  38.15 ? 305  ASN B OD1 1 
ATOM   2262 N ND2 . ASN A 1 305 ? -8.544  -11.246 27.162  1.00  47.11 ? 305  ASN B ND2 1 
ATOM   2263 N N   . GLY A 1 306 ? -4.645  -10.752 23.046  1.00  41.06 ? 306  GLY B N   1 
ATOM   2264 C CA  . GLY A 1 306 ? -3.420  -11.380 22.577  1.00  38.15 ? 306  GLY B CA  1 
ATOM   2265 C C   . GLY A 1 306 ? -3.279  -12.822 23.046  1.00  38.42 ? 306  GLY B C   1 
ATOM   2266 O O   . GLY A 1 306 ? -2.175  -13.356 23.126  1.00  38.64 ? 306  GLY B O   1 
ATOM   2267 N N   . GLU A 1 307 ? -4.404  -13.456 23.358  1.00  37.96 ? 307  GLU B N   1 
ATOM   2268 C CA  . GLU A 1 307 ? -4.404  -14.859 23.744  1.00  41.16 ? 307  GLU B CA  1 
ATOM   2269 C C   . GLU A 1 307 ? -4.682  -15.739 22.541  1.00  40.93 ? 307  GLU B C   1 
ATOM   2270 O O   . GLU A 1 307 ? -5.197  -15.258 21.529  1.00  32.93 ? 307  GLU B O   1 
ATOM   2271 C CB  . GLU A 1 307 ? -5.458  -15.116 24.809  1.00  37.27 ? 307  GLU B CB  1 
ATOM   2272 C CG  . GLU A 1 307 ? -5.144  -14.453 26.131  1.00  45.63 ? 307  GLU B CG  1 
ATOM   2273 C CD  . GLU A 1 307 ? -6.340  -14.421 27.054  1.00  49.70 ? 307  GLU B CD  1 
ATOM   2274 O OE1 . GLU A 1 307 ? -6.508  -13.413 27.779  1.00  57.73 ? 307  GLU B OE1 1 
ATOM   2275 O OE2 . GLU A 1 307 ? -7.115  -15.402 27.056  1.00  49.28 ? 307  GLU B OE2 1 
ATOM   2276 N N   . SER A 1 308 ? -4.371  -17.028 22.681  1.00  40.08 ? 308  SER B N   1 
ATOM   2277 C CA  . SER A 1 308 ? -4.465  -17.999 21.591  1.00  39.62 ? 308  SER B CA  1 
ATOM   2278 C C   . SER A 1 308 ? -5.899  -18.287 21.153  1.00  37.57 ? 308  SER B C   1 
ATOM   2279 O O   . SER A 1 308 ? -6.734  -18.700 21.951  1.00  42.91 ? 308  SER B O   1 
ATOM   2280 C CB  . SER A 1 308 ? -3.756  -19.304 21.977  1.00  42.06 ? 308  SER B CB  1 
ATOM   2281 O OG  . SER A 1 308 ? -4.093  -20.352 21.077  1.00  46.80 ? 308  SER B OG  1 
ATOM   2282 N N   . VAL A 1 309 ? -6.171  -18.061 19.874  1.00  37.44 ? 309  VAL B N   1 
ATOM   2283 C CA  . VAL A 1 309 ? -7.496  -18.288 19.291  1.00  36.79 ? 309  VAL B CA  1 
ATOM   2284 C C   . VAL A 1 309 ? -7.591  -19.737 18.799  1.00  40.61 ? 309  VAL B C   1 
ATOM   2285 O O   . VAL A 1 309 ? -8.682  -20.304 18.694  1.00  39.32 ? 309  VAL B O   1 
ATOM   2286 C CB  . VAL A 1 309 ? -7.749  -17.295 18.134  1.00  35.68 ? 309  VAL B CB  1 
ATOM   2287 C CG1 . VAL A 1 309 ? -9.040  -17.630 17.367  1.00  34.56 ? 309  VAL B CG1 1 
ATOM   2288 C CG2 . VAL A 1 309 ? -7.786  -15.860 18.662  1.00  30.28 ? 309  VAL B CG2 1 
ATOM   2289 N N   . SER A 1 310 ? -6.425  -20.327 18.535  1.00  41.87 ? 310  SER B N   1 
ATOM   2290 C CA  . SER A 1 310 ? -6.296  -21.682 17.996  1.00  42.89 ? 310  SER B CA  1 
ATOM   2291 C C   . SER A 1 310 ? -6.827  -22.744 18.951  1.00  42.73 ? 310  SER B C   1 
ATOM   2292 O O   . SER A 1 310 ? -7.230  -23.826 18.533  1.00  45.10 ? 310  SER B O   1 
ATOM   2293 C CB  . SER A 1 310 ? -4.825  -21.977 17.686  1.00  43.39 ? 310  SER B CB  1 
ATOM   2294 O OG  . SER A 1 310 ? -4.257  -20.919 16.927  1.00  56.09 ? 310  SER B OG  1 
ATOM   2295 N N   . TYR A 1 311 ? -6.786  -22.442 20.240  0.50  40.86 ? 311  TYR B N   1 
ATOM   2296 C CA  . TYR A 1 311 ? -7.413  -23.279 21.249  0.50  39.54 ? 311  TYR B CA  1 
ATOM   2297 C C   . TYR A 1 311 ? -8.825  -23.681 20.792  0.50  39.37 ? 311  TYR B C   1 
ATOM   2298 O O   . TYR A 1 311 ? -9.264  -24.816 20.979  0.50  35.04 ? 311  TYR B O   1 
ATOM   2299 C CB  . TYR A 1 311 ? -7.449  -22.493 22.559  0.50  37.86 ? 311  TYR B CB  1 
ATOM   2300 C CG  . TYR A 1 311 ? -8.442  -22.957 23.589  0.50  40.70 ? 311  TYR B CG  1 
ATOM   2301 C CD1 . TYR A 1 311 ? -8.148  -24.012 24.439  0.50  45.05 ? 311  TYR B CD1 1 
ATOM   2302 C CD2 . TYR A 1 311 ? -9.656  -22.306 23.748  0.50  41.16 ? 311  TYR B CD2 1 
ATOM   2303 C CE1 . TYR A 1 311 ? -9.050  -24.426 25.398  0.50  46.61 ? 311  TYR B CE1 1 
ATOM   2304 C CE2 . TYR A 1 311 ? -10.563 -22.710 24.704  0.50  43.41 ? 311  TYR B CE2 1 
ATOM   2305 C CZ  . TYR A 1 311 ? -10.256 -23.770 25.528  0.50  48.50 ? 311  TYR B CZ  1 
ATOM   2306 O OH  . TYR A 1 311 ? -11.158 -24.180 26.486  0.50  56.10 ? 311  TYR B OH  1 
ATOM   2307 N N   . LEU A 1 312 ? -9.512  -22.736 20.163  1.00  37.02 ? 312  LEU B N   1 
ATOM   2308 C CA  . LEU A 1 312 ? -10.891 -22.917 19.707  1.00  38.59 ? 312  LEU B CA  1 
ATOM   2309 C C   . LEU A 1 312 ? -11.042 -23.859 18.517  1.00  41.96 ? 312  LEU B C   1 
ATOM   2310 O O   . LEU A 1 312 ? -12.159 -24.284 18.203  1.00  42.56 ? 312  LEU B O   1 
ATOM   2311 C CB  . LEU A 1 312 ? -11.503 -21.561 19.347  1.00  30.07 ? 312  LEU B CB  1 
ATOM   2312 C CG  . LEU A 1 312 ? -11.713 -20.592 20.508  1.00  36.52 ? 312  LEU B CG  1 
ATOM   2313 C CD1 . LEU A 1 312 ? -12.129 -19.216 19.986  1.00  31.16 ? 312  LEU B CD1 1 
ATOM   2314 C CD2 . LEU A 1 312 ? -12.755 -21.168 21.450  1.00  34.86 ? 312  LEU B CD2 1 
ATOM   2315 N N   . PHE A 1 313 ? -9.940  -24.174 17.838  1.00  39.56 ? 313  PHE B N   1 
ATOM   2316 C CA  . PHE A 1 313 ? -10.030 -25.010 16.636  1.00  46.13 ? 313  PHE B CA  1 
ATOM   2317 C C   . PHE A 1 313 ? -10.412 -26.468 16.924  1.00  43.97 ? 313  PHE B C   1 
ATOM   2318 O O   . PHE A 1 313 ? -10.921 -27.162 16.042  1.00  48.43 ? 313  PHE B O   1 
ATOM   2319 C CB  . PHE A 1 313 ? -8.737  -24.946 15.807  1.00  44.84 ? 313  PHE B CB  1 
ATOM   2320 C CG  . PHE A 1 313 ? -8.489  -23.609 15.167  1.00  45.05 ? 313  PHE B CG  1 
ATOM   2321 C CD1 . PHE A 1 313 ? -9.437  -22.598 15.251  1.00  44.62 ? 313  PHE B CD1 1 
ATOM   2322 C CD2 . PHE A 1 313 ? -7.309  -23.359 14.483  1.00  45.04 ? 313  PHE B CD2 1 
ATOM   2323 C CE1 . PHE A 1 313 ? -9.210  -21.368 14.671  1.00  40.17 ? 313  PHE B CE1 1 
ATOM   2324 C CE2 . PHE A 1 313 ? -7.077  -22.128 13.893  1.00  40.29 ? 313  PHE B CE2 1 
ATOM   2325 C CZ  . PHE A 1 313 ? -8.031  -21.133 13.985  1.00  42.04 ? 313  PHE B CZ  1 
ATOM   2326 N N   . SER A 1 314 ? -10.174 -26.933 18.146  0.50  41.60 ? 314  SER B N   1 
ATOM   2327 C CA  . SER A 1 314 ? -10.475 -28.321 18.484  0.50  42.28 ? 314  SER B CA  1 
ATOM   2328 C C   . SER A 1 314 ? -11.243 -28.435 19.795  0.50  44.08 ? 314  SER B C   1 
ATOM   2329 O O   . SER A 1 314 ? -11.631 -29.529 20.210  0.50  45.37 ? 314  SER B O   1 
ATOM   2330 C CB  . SER A 1 314 ? -9.194  -29.148 18.568  0.50  46.15 ? 314  SER B CB  1 
ATOM   2331 O OG  . SER A 1 314 ? -8.661  -29.124 19.880  0.50  47.30 ? 314  SER B OG  1 
ATOM   2332 N N   . HIS A 1 315 ? -11.470 -27.298 20.439  0.50  42.70 ? 315  HIS B N   1 
ATOM   2333 C CA  . HIS A 1 315 ? -12.121 -27.280 21.737  0.50  43.51 ? 315  HIS B CA  1 
ATOM   2334 C C   . HIS A 1 315 ? -13.340 -26.375 21.712  0.50  45.49 ? 315  HIS B C   1 
ATOM   2335 O O   . HIS A 1 315 ? -13.279 -25.253 21.212  0.50  41.23 ? 315  HIS B O   1 
ATOM   2336 C CB  . HIS A 1 315 ? -11.140 -26.806 22.812  0.50  45.10 ? 315  HIS B CB  1 
ATOM   2337 C CG  . HIS A 1 315 ? -11.648 -26.994 24.216  0.50  47.87 ? 315  HIS B CG  1 
ATOM   2338 N ND1 . HIS A 1 315 ? -12.914 -27.438 24.493  0.50  50.63 ? 315  HIS B ND1 1 
ATOM   2339 C CD2 . HIS A 1 315 ? -11.032 -26.803 25.409  0.50  49.48 ? 315  HIS B CD2 1 
ATOM   2340 C CE1 . HIS A 1 315 ? -13.073 -27.509 25.812  0.50  49.65 ? 315  HIS B CE1 1 
ATOM   2341 N NE2 . HIS A 1 315 ? -11.953 -27.131 26.383  0.50  46.87 ? 315  HIS B NE2 1 
ATOM   2342 N N   . VAL A 1 316 ? -14.446 -26.871 22.256  1.00  47.96 ? 316  VAL B N   1 
ATOM   2343 C CA  . VAL A 1 316 ? -15.662 -26.083 22.368  1.00  45.78 ? 316  VAL B CA  1 
ATOM   2344 C C   . VAL A 1 316 ? -15.625 -25.309 23.677  1.00  49.26 ? 316  VAL B C   1 
ATOM   2345 O O   . VAL A 1 316 ? -15.603 -25.914 24.753  1.00  56.68 ? 316  VAL B O   1 
ATOM   2346 C CB  . VAL A 1 316 ? -16.911 -26.981 22.373  1.00  47.18 ? 316  VAL B CB  1 
ATOM   2347 C CG1 . VAL A 1 316 ? -18.133 -26.170 21.989  1.00  54.19 ? 316  VAL B CG1 1 
ATOM   2348 C CG2 . VAL A 1 316 ? -16.735 -28.153 21.414  1.00  42.62 ? 316  VAL B CG2 1 
ATOM   2349 N N   . PRO A 1 317 ? -15.632 -23.970 23.602  0.80  45.68 ? 317  PRO B N   1 
ATOM   2350 C CA  . PRO A 1 317 ? -15.516 -23.179 24.833  0.80  49.03 ? 317  PRO B CA  1 
ATOM   2351 C C   . PRO A 1 317 ? -16.690 -23.440 25.775  0.80  51.03 ? 317  PRO B C   1 
ATOM   2352 O O   . PRO A 1 317 ? -16.574 -24.340 26.607  0.80  49.58 ? 317  PRO B O   1 
ATOM   2353 C CB  . PRO A 1 317 ? -15.553 -21.736 24.324  0.80  44.62 ? 317  PRO B CB  1 
ATOM   2354 C CG  . PRO A 1 317 ? -16.290 -21.816 23.048  0.80  38.70 ? 317  PRO B CG  1 
ATOM   2355 C CD  . PRO A 1 317 ? -15.943 -23.133 22.433  0.80  41.69 ? 317  PRO B CD  1 
ATOM   2356 N N   . ASN B 1 3   ? -12.010 -3.747  -31.217 1.00  46.37 ? 3    ASN A N   1 
ATOM   2357 C CA  . ASN B 1 3   ? -11.093 -3.245  -30.203 1.00  37.85 ? 3    ASN A CA  1 
ATOM   2358 C C   . ASN B 1 3   ? -11.886 -2.648  -29.067 1.00  36.33 ? 3    ASN A C   1 
ATOM   2359 O O   . ASN B 1 3   ? -11.700 -3.047  -27.924 1.00  32.48 ? 3    ASN A O   1 
ATOM   2360 C CB  . ASN B 1 3   ? -10.122 -2.223  -30.781 1.00  41.28 ? 3    ASN A CB  1 
ATOM   2361 C CG  . ASN B 1 3   ? -8.924  -1.997  -29.896 1.00  42.24 ? 3    ASN A CG  1 
ATOM   2362 O OD1 . ASN B 1 3   ? -8.090  -2.886  -29.708 1.00  49.30 ? 3    ASN A OD1 1 
ATOM   2363 N ND2 . ASN B 1 3   ? -8.813  -0.795  -29.362 1.00  45.83 ? 3    ASN A ND2 1 
ATOM   2364 N N   . ILE B 1 4   ? -12.788 -1.721  -29.374 1.00  29.95 ? 4    ILE A N   1 
ATOM   2365 C CA  . ILE B 1 4   ? -13.778 -1.316  -28.370 1.00  33.03 ? 4    ILE A CA  1 
ATOM   2366 C C   . ILE B 1 4   ? -14.831 -2.394  -28.144 1.00  38.11 ? 4    ILE A C   1 
ATOM   2367 O O   . ILE B 1 4   ? -15.394 -2.960  -29.095 1.00  32.28 ? 4    ILE A O   1 
ATOM   2368 C CB  . ILE B 1 4   ? -14.503 -0.002  -28.699 1.00  33.39 ? 4    ILE A CB  1 
ATOM   2369 C CG1 . ILE B 1 4   ? -15.652 0.198   -27.707 1.00  31.38 ? 4    ILE A CG1 1 
ATOM   2370 C CG2 . ILE B 1 4   ? -15.068 -0.044  -30.089 1.00  42.90 ? 4    ILE A CG2 1 
ATOM   2371 C CD1 . ILE B 1 4   ? -16.393 1.498   -27.880 1.00  37.87 ? 4    ILE A CD1 1 
ATOM   2372 N N   . LYS B 1 5   ? -15.086 -2.677  -26.870 1.00  29.68 ? 5    LYS A N   1 
ATOM   2373 C CA  . LYS B 1 5   ? -16.140 -3.594  -26.475 1.00  25.00 ? 5    LYS A CA  1 
ATOM   2374 C C   . LYS B 1 5   ? -16.980 -2.918  -25.399 1.00  29.36 ? 5    LYS A C   1 
ATOM   2375 O O   . LYS B 1 5   ? -16.444 -2.449  -24.395 1.00  26.02 ? 5    LYS A O   1 
ATOM   2376 C CB  . LYS B 1 5   ? -15.540 -4.900  -25.958 1.00  26.44 ? 5    LYS A CB  1 
ATOM   2377 C CG  . LYS B 1 5   ? -15.581 -6.052  -26.955 1.00  40.65 ? 5    LYS A CG  1 
ATOM   2378 C CD  . LYS B 1 5   ? -17.018 -6.514  -27.196 1.00  39.42 ? 5    LYS A CD  1 
ATOM   2379 C CE  . LYS B 1 5   ? -17.116 -7.414  -28.411 1.00  42.97 ? 5    LYS A CE  1 
ATOM   2380 N NZ  . LYS B 1 5   ? -18.523 -7.805  -28.703 1.00  44.22 ? 5    LYS A NZ  1 
ATOM   2381 N N   . ILE B 1 6   ? -18.292 -2.870  -25.603 1.00  24.76 ? 6    ILE A N   1 
ATOM   2382 C CA  . ILE B 1 6   ? -19.196 -2.234  -24.650 1.00  27.76 ? 6    ILE A CA  1 
ATOM   2383 C C   . ILE B 1 6   ? -20.142 -3.267  -24.033 1.00  29.35 ? 6    ILE A C   1 
ATOM   2384 O O   . ILE B 1 6   ? -20.801 -4.017  -24.757 1.00  23.08 ? 6    ILE A O   1 
ATOM   2385 C CB  . ILE B 1 6   ? -20.060 -1.156  -25.316 1.00  28.58 ? 6    ILE A CB  1 
ATOM   2386 C CG1 . ILE B 1 6   ? -19.180 -0.107  -25.990 1.00  33.85 ? 6    ILE A CG1 1 
ATOM   2387 C CG2 . ILE B 1 6   ? -20.964 -0.475  -24.272 1.00  27.53 ? 6    ILE A CG2 1 
ATOM   2388 C CD1 . ILE B 1 6   ? -19.958 1.081   -26.497 1.00  39.01 ? 6    ILE A CD1 1 
ATOM   2389 N N   . PHE B 1 7   ? -20.183 -3.308  -22.701 1.00  23.38 ? 7    PHE A N   1 
ATOM   2390 C CA  . PHE B 1 7   ? -21.073 -4.204  -21.969 1.00  22.49 ? 7    PHE A CA  1 
ATOM   2391 C C   . PHE B 1 7   ? -22.049 -3.402  -21.128 1.00  28.05 ? 7    PHE A C   1 
ATOM   2392 O O   . PHE B 1 7   ? -21.727 -2.315  -20.663 1.00  24.20 ? 7    PHE A O   1 
ATOM   2393 C CB  . PHE B 1 7   ? -20.280 -5.111  -21.027 1.00  26.20 ? 7    PHE A CB  1 
ATOM   2394 C CG  . PHE B 1 7   ? -19.412 -6.110  -21.720 1.00  25.57 ? 7    PHE A CG  1 
ATOM   2395 C CD1 . PHE B 1 7   ? -18.096 -5.802  -22.039 1.00  28.42 ? 7    PHE A CD1 1 
ATOM   2396 C CD2 . PHE B 1 7   ? -19.895 -7.369  -22.023 1.00  23.58 ? 7    PHE A CD2 1 
ATOM   2397 C CE1 . PHE B 1 7   ? -17.286 -6.728  -22.670 1.00  28.43 ? 7    PHE A CE1 1 
ATOM   2398 C CE2 . PHE B 1 7   ? -19.094 -8.299  -22.657 1.00  26.27 ? 7    PHE A CE2 1 
ATOM   2399 C CZ  . PHE B 1 7   ? -17.783 -7.982  -22.971 1.00  30.82 ? 7    PHE A CZ  1 
ATOM   2400 N N   . SER B 1 8   ? -23.240 -3.947  -20.920 1.00  25.53 ? 8    SER A N   1 
ATOM   2401 C CA  . SER B 1 8   ? -24.242 -3.275  -20.114 1.00  29.05 ? 8    SER A CA  1 
ATOM   2402 C C   . SER B 1 8   ? -24.438 -3.956  -18.769 1.00  29.72 ? 8    SER A C   1 
ATOM   2403 O O   . SER B 1 8   ? -24.364 -5.180  -18.676 1.00  34.30 ? 8    SER A O   1 
ATOM   2404 C CB  . SER B 1 8   ? -25.589 -3.252  -20.833 1.00  33.01 ? 8    SER A CB  1 
ATOM   2405 O OG  . SER B 1 8   ? -26.574 -2.696  -19.981 1.00  36.20 ? 8    SER A OG  1 
ATOM   2406 N N   . GLY B 1 9   ? -24.706 -3.152  -17.737 1.00  41.16 ? 9    GLY A N   1 
ATOM   2407 C CA  . GLY B 1 9   ? -25.149 -3.648  -16.431 1.00  39.03 ? 9    GLY A CA  1 
ATOM   2408 C C   . GLY B 1 9   ? -26.522 -4.327  -16.443 1.00  46.76 ? 9    GLY A C   1 
ATOM   2409 O O   . GLY B 1 9   ? -27.239 -4.281  -17.456 1.00  52.97 ? 9    GLY A O   1 
ATOM   2410 N N   . SER B 1 10  ? -26.898 -4.907  -15.302 1.00  51.41 ? 10   SER A N   1 
ATOM   2411 C CA  . SER B 1 10  ? -27.912 -5.977  -15.203 1.00  57.86 ? 10   SER A CA  1 
ATOM   2412 C C   . SER B 1 10  ? -29.195 -6.322  -15.939 1.00  60.65 ? 10   SER A C   1 
ATOM   2413 O O   . SER B 1 10  ? -29.385 -7.448  -16.408 1.00  66.94 ? 10   SER A O   1 
ATOM   2414 C CB  . SER B 1 10  ? -28.551 -6.022  -13.811 1.00  49.95 ? 10   SER A CB  1 
ATOM   2415 O OG  . SER B 1 10  ? -29.050 -4.754  -13.418 1.00  58.14 ? 10   SER A OG  1 
ATOM   2416 N N   . SER B 1 11  ? -30.100 -5.358  -15.987 1.00  61.44 ? 11   SER A N   1 
ATOM   2417 C CA  . SER B 1 11  ? -31.306 -5.531  -16.775 1.00  61.91 ? 11   SER A CA  1 
ATOM   2418 C C   . SER B 1 11  ? -31.578 -4.253  -17.547 1.00  60.41 ? 11   SER A C   1 
ATOM   2419 O O   . SER B 1 11  ? -32.008 -4.296  -18.699 1.00  66.07 ? 11   SER A O   1 
ATOM   2420 C CB  . SER B 1 11  ? -32.485 -5.865  -15.858 1.00  59.80 ? 11   SER A CB  1 
ATOM   2421 O OG  . SER B 1 11  ? -33.626 -6.175  -16.610 1.00  66.06 ? 11   SER A OG  1 
ATOM   2422 N N   . HIS B 1 12  ? -31.349 -3.123  -16.883 0.58  53.22 ? 12   HIS A N   1 
ATOM   2423 C CA  . HIS B 1 12  ? -31.389 -1.822  -17.523 0.58  51.56 ? 12   HIS A CA  1 
ATOM   2424 C C   . HIS B 1 12  ? -30.358 -1.807  -18.642 0.58  51.88 ? 12   HIS A C   1 
ATOM   2425 O O   . HIS B 1 12  ? -29.154 -1.921  -18.401 0.58  51.10 ? 12   HIS A O   1 
ATOM   2426 C CB  . HIS B 1 12  ? -31.081 -0.724  -16.504 0.58  50.05 ? 12   HIS A CB  1 
ATOM   2427 C CG  . HIS B 1 12  ? -30.583 0.551   -17.116 0.58  48.57 ? 12   HIS A CG  1 
ATOM   2428 N ND1 . HIS B 1 12  ? -29.244 0.855   -17.219 0.58  47.50 ? 12   HIS A ND1 1 
ATOM   2429 C CD2 . HIS B 1 12  ? -31.248 1.599   -17.659 0.58  48.95 ? 12   HIS A CD2 1 
ATOM   2430 C CE1 . HIS B 1 12  ? -29.102 2.038   -17.795 0.58  47.22 ? 12   HIS A CE1 1 
ATOM   2431 N NE2 . HIS B 1 12  ? -30.305 2.512   -18.070 0.58  49.61 ? 12   HIS A NE2 1 
ATOM   2432 N N   . GLN B 1 13  ? -30.843 -1.689  -19.869 1.00  47.77 ? 13   GLN A N   1 
ATOM   2433 C CA  . GLN B 1 13  ? -29.993 -1.807  -21.035 1.00  46.59 ? 13   GLN A CA  1 
ATOM   2434 C C   . GLN B 1 13  ? -30.283 -0.709  -22.035 1.00  40.95 ? 13   GLN A C   1 
ATOM   2435 O O   . GLN B 1 13  ? -29.552 -0.559  -23.015 1.00  38.81 ? 13   GLN A O   1 
ATOM   2436 C CB  . GLN B 1 13  ? -30.212 -3.160  -21.718 1.00  53.31 ? 13   GLN A CB  1 
ATOM   2437 C CG  . GLN B 1 13  ? -28.990 -4.066  -21.749 1.00  53.45 ? 13   GLN A CG  1 
ATOM   2438 C CD  . GLN B 1 13  ? -29.081 -5.116  -22.843 1.00  54.88 ? 13   GLN A CD  1 
ATOM   2439 O OE1 . GLN B 1 13  ? -28.554 -6.220  -22.706 1.00  57.75 ? 13   GLN A OE1 1 
ATOM   2440 N NE2 . GLN B 1 13  ? -29.743 -4.767  -23.944 1.00  54.52 ? 13   GLN A NE2 1 
ATOM   2441 N N   . ASP B 1 14  ? -31.340 0.063   -21.800 1.00  37.76 ? 14   ASP A N   1 
ATOM   2442 C CA  . ASP B 1 14  ? -31.803 0.982   -22.839 1.00  41.84 ? 14   ASP A CA  1 
ATOM   2443 C C   . ASP B 1 14  ? -30.758 2.045   -23.157 1.00  36.83 ? 14   ASP A C   1 
ATOM   2444 O O   . ASP B 1 14  ? -30.480 2.318   -24.314 1.00  38.25 ? 14   ASP A O   1 
ATOM   2445 C CB  . ASP B 1 14  ? -33.137 1.633   -22.471 1.00  42.58 ? 14   ASP A CB  1 
ATOM   2446 C CG  . ASP B 1 14  ? -33.664 2.539   -23.573 1.00  49.70 ? 14   ASP A CG  1 
ATOM   2447 O OD1 . ASP B 1 14  ? -34.194 3.622   -23.246 1.00  52.11 ? 14   ASP A OD1 1 
ATOM   2448 O OD2 . ASP B 1 14  ? -33.553 2.166   -24.767 1.00  54.30 ? 14   ASP A OD2 1 
ATOM   2449 N N   . LEU B 1 15  ? -30.179 2.643   -22.125 1.00  33.00 ? 15   LEU A N   1 
ATOM   2450 C CA  . LEU B 1 15  ? -29.119 3.625   -22.325 1.00  33.84 ? 15   LEU A CA  1 
ATOM   2451 C C   . LEU B 1 15  ? -27.915 2.935   -22.963 1.00  31.70 ? 15   LEU A C   1 
ATOM   2452 O O   . LEU B 1 15  ? -27.337 3.431   -23.921 1.00  29.82 ? 15   LEU A O   1 
ATOM   2453 C CB  . LEU B 1 15  ? -28.716 4.240   -20.984 1.00  31.49 ? 15   LEU A CB  1 
ATOM   2454 C CG  . LEU B 1 15  ? -28.178 5.673   -20.919 1.00  37.69 ? 15   LEU A CG  1 
ATOM   2455 C CD1 . LEU B 1 15  ? -27.113 5.780   -19.826 1.00  31.05 ? 15   LEU A CD1 1 
ATOM   2456 C CD2 . LEU B 1 15  ? -27.647 6.178   -22.270 1.00  33.75 ? 15   LEU A CD2 1 
ATOM   2457 N N   . SER B 1 16  ? -27.534 1.790   -22.414 1.00  27.96 ? 16   SER A N   1 
ATOM   2458 C CA  . SER B 1 16  ? -26.415 1.025   -22.951 1.00  30.25 ? 16   SER A CA  1 
ATOM   2459 C C   . SER B 1 16  ? -26.618 0.687   -24.436 1.00  33.21 ? 16   SER A C   1 
ATOM   2460 O O   . SER B 1 16  ? -25.708 0.857   -25.245 1.00  27.33 ? 16   SER A O   1 
ATOM   2461 C CB  . SER B 1 16  ? -26.198 -0.255  -22.143 1.00  31.63 ? 16   SER A CB  1 
ATOM   2462 O OG  . SER B 1 16  ? -25.770 0.065   -20.836 1.00  38.41 ? 16   SER A OG  1 
ATOM   2463 N N   . GLN B 1 17  ? -27.810 0.222   -24.790 1.00  30.64 ? 17   GLN A N   1 
ATOM   2464 C CA  . GLN B 1 17  ? -28.126 -0.060  -26.189 1.00  34.31 ? 17   GLN A CA  1 
ATOM   2465 C C   . GLN B 1 17  ? -28.030 1.184   -27.077 1.00  34.66 ? 17   GLN A C   1 
ATOM   2466 O O   . GLN B 1 17  ? -27.520 1.115   -28.188 1.00  36.81 ? 17   GLN A O   1 
ATOM   2467 C CB  . GLN B 1 17  ? -29.513 -0.694  -26.328 1.00  35.71 ? 17   GLN A CB  1 
ATOM   2468 C CG  . GLN B 1 17  ? -29.772 -1.261  -27.729 1.00  41.46 ? 17   GLN A CG  1 
ATOM   2469 C CD  . GLN B 1 17  ? -28.790 -2.364  -28.096 1.00  40.85 ? 17   GLN A CD  1 
ATOM   2470 O OE1 . GLN B 1 17  ? -28.793 -3.434  -27.495 1.00  40.95 ? 17   GLN A OE1 1 
ATOM   2471 N NE2 . GLN B 1 17  ? -27.934 -2.098  -29.082 1.00  43.77 ? 17   GLN A NE2 1 
ATOM   2472 N N   . LYS B 1 18  ? -28.530 2.313   -26.590 1.00  32.72 ? 18   LYS A N   1 
ATOM   2473 C CA  . LYS B 1 18  ? -28.458 3.552   -27.353 1.00  36.01 ? 18   LYS A CA  1 
ATOM   2474 C C   . LYS B 1 18  ? -27.005 3.912   -27.620 1.00  35.80 ? 18   LYS A C   1 
ATOM   2475 O O   . LYS B 1 18  ? -26.641 4.302   -28.726 1.00  32.55 ? 18   LYS A O   1 
ATOM   2476 C CB  . LYS B 1 18  ? -29.148 4.696   -26.609 1.00  36.17 ? 18   LYS A CB  1 
ATOM   2477 C CG  . LYS B 1 18  ? -30.664 4.688   -26.703 1.00  39.80 ? 18   LYS A CG  1 
ATOM   2478 C CD  . LYS B 1 18  ? -31.254 5.927   -26.036 1.00  41.20 ? 18   LYS A CD  1 
ATOM   2479 C CE  . LYS B 1 18  ? -32.748 6.037   -26.304 1.00  50.17 ? 18   LYS A CE  1 
ATOM   2480 N NZ  . LYS B 1 18  ? -33.479 4.778   -25.920 1.00  50.69 ? 18   LYS A NZ  1 
ATOM   2481 N N   . ILE B 1 19  ? -26.167 3.770   -26.601 1.00  28.89 ? 19   ILE A N   1 
ATOM   2482 C CA  . ILE B 1 19  ? -24.745 4.051   -26.753 1.00  27.19 ? 19   ILE A CA  1 
ATOM   2483 C C   . ILE B 1 19  ? -24.094 3.121   -27.786 1.00  30.50 ? 19   ILE A C   1 
ATOM   2484 O O   . ILE B 1 19  ? -23.360 3.566   -28.680 1.00  28.48 ? 19   ILE A O   1 
ATOM   2485 C CB  . ILE B 1 19  ? -24.030 3.931   -25.387 1.00  28.04 ? 19   ILE A CB  1 
ATOM   2486 C CG1 . ILE B 1 19  ? -24.436 5.099   -24.480 1.00  25.63 ? 19   ILE A CG1 1 
ATOM   2487 C CG2 . ILE B 1 19  ? -22.536 3.872   -25.567 1.00  26.61 ? 19   ILE A CG2 1 
ATOM   2488 C CD1 . ILE B 1 19  ? -24.126 4.870   -23.007 1.00  27.98 ? 19   ILE A CD1 1 
ATOM   2489 N N   . ALA B 1 20  ? -24.355 1.823   -27.673 1.00  26.43 ? 20   ALA A N   1 
ATOM   2490 C CA  . ALA B 1 20  ? -23.758 0.896   -28.614 1.00  28.80 ? 20   ALA A CA  1 
ATOM   2491 C C   . ALA B 1 20  ? -24.208 1.233   -30.047 1.00  28.22 ? 20   ALA A C   1 
ATOM   2492 O O   . ALA B 1 20  ? -23.423 1.142   -30.986 1.00  30.69 ? 20   ALA A O   1 
ATOM   2493 C CB  . ALA B 1 20  ? -24.090 -0.535  -28.255 1.00  30.36 ? 20   ALA A CB  1 
ATOM   2494 N N   . ASP B 1 21  ? -25.462 1.642   -30.198 1.00  31.47 ? 21   ASP A N   1 
ATOM   2495 C CA  . ASP B 1 21  ? -26.015 1.969   -31.512 1.00  37.61 ? 21   ASP A CA  1 
ATOM   2496 C C   . ASP B 1 21  ? -25.256 3.097   -32.169 1.00  34.99 ? 21   ASP A C   1 
ATOM   2497 O O   . ASP B 1 21  ? -24.974 3.055   -33.374 1.00  34.26 ? 21   ASP A O   1 
ATOM   2498 C CB  . ASP B 1 21  ? -27.484 2.380   -31.401 1.00  37.17 ? 21   ASP A CB  1 
ATOM   2499 C CG  . ASP B 1 21  ? -28.396 1.208   -31.172 1.00  39.72 ? 21   ASP A CG  1 
ATOM   2500 O OD1 . ASP B 1 21  ? -27.908 0.065   -31.287 1.00  40.29 ? 21   ASP A OD1 1 
ATOM   2501 O OD2 . ASP B 1 21  ? -29.598 1.423   -30.880 1.00  42.69 ? 21   ASP A OD2 1 
ATOM   2502 N N   . ARG B 1 22  ? -24.942 4.119   -31.380 0.80  30.13 ? 22   ARG A N   1 
ATOM   2503 C CA  . ARG B 1 22  ? -24.287 5.301   -31.911 0.80  30.91 ? 22   ARG A CA  1 
ATOM   2504 C C   . ARG B 1 22  ? -22.853 5.012   -32.317 0.80  32.79 ? 22   ARG A C   1 
ATOM   2505 O O   . ARG B 1 22  ? -22.273 5.706   -33.146 0.80  31.25 ? 22   ARG A O   1 
ATOM   2506 C CB  . ARG B 1 22  ? -24.337 6.444   -30.899 0.80  32.70 ? 22   ARG A CB  1 
ATOM   2507 C CG  . ARG B 1 22  ? -25.744 6.912   -30.583 0.80  32.90 ? 22   ARG A CG  1 
ATOM   2508 C CD  . ARG B 1 22  ? -25.719 8.221   -29.820 0.80  31.50 ? 22   ARG A CD  1 
ATOM   2509 N NE  . ARG B 1 22  ? -27.054 8.683   -29.445 0.80  34.24 ? 22   ARG A NE  1 
ATOM   2510 C CZ  . ARG B 1 22  ? -27.801 9.519   -30.167 0.80  39.91 ? 22   ARG A CZ  1 
ATOM   2511 N NH1 . ARG B 1 22  ? -27.353 9.987   -31.327 0.80  37.66 ? 22   ARG A NH1 1 
ATOM   2512 N NH2 . ARG B 1 22  ? -29.001 9.883   -29.731 0.80  38.38 ? 22   ARG A NH2 1 
ATOM   2513 N N   . LEU B 1 23  ? -22.287 3.971   -31.728 1.00  33.13 ? 23   LEU A N   1 
ATOM   2514 C CA  . LEU B 1 23  ? -20.903 3.610   -31.979 1.00  33.70 ? 23   LEU A CA  1 
ATOM   2515 C C   . LEU B 1 23  ? -20.809 2.524   -33.051 1.00  31.05 ? 23   LEU A C   1 
ATOM   2516 O O   . LEU B 1 23  ? -19.709 2.088   -33.399 1.00  29.86 ? 23   LEU A O   1 
ATOM   2517 C CB  . LEU B 1 23  ? -20.254 3.121   -30.677 1.00  32.42 ? 23   LEU A CB  1 
ATOM   2518 C CG  . LEU B 1 23  ? -19.936 4.201   -29.632 1.00  34.04 ? 23   LEU A CG  1 
ATOM   2519 C CD1 . LEU B 1 23  ? -19.450 3.583   -28.353 1.00  32.50 ? 23   LEU A CD1 1 
ATOM   2520 C CD2 . LEU B 1 23  ? -18.893 5.187   -30.160 1.00  34.49 ? 23   LEU A CD2 1 
ATOM   2521 N N   . GLY B 1 24  ? -21.964 2.079   -33.543 1.00  30.14 ? 24   GLY A N   1 
ATOM   2522 C CA  . GLY B 1 24  ? -22.035 1.006   -34.521 1.00  28.23 ? 24   GLY A CA  1 
ATOM   2523 C C   . GLY B 1 24  ? -21.672 -0.361  -33.975 1.00  29.77 ? 24   GLY A C   1 
ATOM   2524 O O   . GLY B 1 24  ? -21.154 -1.209  -34.706 1.00  25.84 ? 24   GLY A O   1 
ATOM   2525 N N   . LEU B 1 25  ? -21.927 -0.584  -32.686 1.00  29.95 ? 25   LEU A N   1 
ATOM   2526 C CA  . LEU B 1 25  ? -21.568 -1.855  -32.051 1.00  28.86 ? 25   LEU A CA  1 
ATOM   2527 C C   . LEU B 1 25  ? -22.778 -2.572  -31.475 1.00  24.43 ? 25   LEU A C   1 
ATOM   2528 O O   . LEU B 1 25  ? -23.794 -1.954  -31.194 1.00  25.40 ? 25   LEU A O   1 
ATOM   2529 C CB  . LEU B 1 25  ? -20.565 -1.638  -30.910 1.00  29.27 ? 25   LEU A CB  1 
ATOM   2530 C CG  . LEU B 1 25  ? -19.303 -0.823  -31.171 1.00  35.21 ? 25   LEU A CG  1 
ATOM   2531 C CD1 . LEU B 1 25  ? -18.529 -0.680  -29.865 1.00  31.64 ? 25   LEU A CD1 1 
ATOM   2532 C CD2 . LEU B 1 25  ? -18.438 -1.474  -32.230 1.00  30.20 ? 25   LEU A CD2 1 
ATOM   2533 N N   . GLU B 1 26  ? -22.657 -3.881  -31.308 0.40  22.38 ? 26   GLU A N   1 
ATOM   2534 C CA  . GLU B 1 26  ? -23.594 -4.638  -30.500 0.40  21.75 ? 26   GLU A CA  1 
ATOM   2535 C C   . GLU B 1 26  ? -23.021 -4.727  -29.083 0.40  24.68 ? 26   GLU A C   1 
ATOM   2536 O O   . GLU B 1 26  ? -21.799 -4.749  -28.912 0.40  18.86 ? 26   GLU A O   1 
ATOM   2537 C CB  . GLU B 1 26  ? -23.779 -6.047  -31.070 0.40  24.50 ? 26   GLU A CB  1 
ATOM   2538 C CG  . GLU B 1 26  ? -24.378 -6.084  -32.482 0.40  28.43 ? 26   GLU A CG  1 
ATOM   2539 C CD  . GLU B 1 26  ? -24.412 -7.493  -33.064 0.40  35.66 ? 26   GLU A CD  1 
ATOM   2540 O OE1 . GLU B 1 26  ? -23.965 -8.443  -32.373 0.40  34.23 ? 26   GLU A OE1 1 
ATOM   2541 O OE2 . GLU B 1 26  ? -24.885 -7.645  -34.215 0.40  41.35 ? 26   GLU A OE2 1 
ATOM   2542 N N   . LEU B 1 27  ? -23.895 -4.756  -28.077 1.00  25.44 ? 27   LEU A N   1 
ATOM   2543 C CA  . LEU B 1 27  ? -23.458 -4.994  -26.696 1.00  25.66 ? 27   LEU A CA  1 
ATOM   2544 C C   . LEU B 1 27  ? -22.764 -6.344  -26.566 1.00  27.06 ? 27   LEU A C   1 
ATOM   2545 O O   . LEU B 1 27  ? -23.221 -7.338  -27.115 1.00  26.74 ? 27   LEU A O   1 
ATOM   2546 C CB  . LEU B 1 27  ? -24.634 -4.904  -25.716 1.00  24.38 ? 27   LEU A CB  1 
ATOM   2547 C CG  . LEU B 1 27  ? -25.225 -3.504  -25.551 1.00  24.52 ? 27   LEU A CG  1 
ATOM   2548 C CD1 . LEU B 1 27  ? -26.518 -3.528  -24.740 1.00  30.06 ? 27   LEU A CD1 1 
ATOM   2549 C CD2 . LEU B 1 27  ? -24.189 -2.557  -24.932 1.00  26.10 ? 27   LEU A CD2 1 
ATOM   2550 N N   . GLY B 1 28  ? -21.657 -6.380  -25.830 1.00  25.83 ? 28   GLY A N   1 
ATOM   2551 C CA  . GLY B 1 28  ? -20.940 -7.621  -25.608 1.00  24.68 ? 28   GLY A CA  1 
ATOM   2552 C C   . GLY B 1 28  ? -21.784 -8.649  -24.879 1.00  28.24 ? 28   GLY A C   1 
ATOM   2553 O O   . GLY B 1 28  ? -22.693 -8.279  -24.134 1.00  24.91 ? 28   GLY A O   1 
ATOM   2554 N N   . LYS B 1 29  ? -21.493 -9.929  -25.095 0.40  19.03 ? 29   LYS A N   1 
ATOM   2555 C CA  . LYS B 1 29  ? -22.292 -10.991 -24.503 0.40  23.94 ? 29   LYS A CA  1 
ATOM   2556 C C   . LYS B 1 29  ? -21.957 -11.151 -23.026 0.40  25.31 ? 29   LYS A C   1 
ATOM   2557 O O   . LYS B 1 29  ? -20.798 -11.314 -22.656 0.40  20.90 ? 29   LYS A O   1 
ATOM   2558 C CB  . LYS B 1 29  ? -22.052 -12.319 -25.224 0.40  25.09 ? 29   LYS A CB  1 
ATOM   2559 C CG  . LYS B 1 29  ? -22.398 -12.308 -26.706 0.40  26.96 ? 29   LYS A CG  1 
ATOM   2560 C CD  . LYS B 1 29  ? -22.336 -13.716 -27.289 0.40  29.44 ? 29   LYS A CD  1 
ATOM   2561 C CE  . LYS B 1 29  ? -20.906 -14.140 -27.618 0.40  29.39 ? 29   LYS A CE  1 
ATOM   2562 N NZ  . LYS B 1 29  ? -20.406 -13.544 -28.895 0.40  35.88 ? 29   LYS A NZ  1 
ATOM   2563 N N   . VAL B 1 30  ? -22.972 -11.098 -22.178 1.00  26.76 ? 30   VAL A N   1 
ATOM   2564 C CA  . VAL B 1 30  ? -22.747 -11.346 -20.754 1.00  32.61 ? 30   VAL A CA  1 
ATOM   2565 C C   . VAL B 1 30  ? -23.999 -11.884 -20.075 1.00  35.41 ? 30   VAL A C   1 
ATOM   2566 O O   . VAL B 1 30  ? -25.104 -11.446 -20.367 1.00  40.76 ? 30   VAL A O   1 
ATOM   2567 C CB  . VAL B 1 30  ? -22.221 -10.090 -20.011 1.00  33.07 ? 30   VAL A CB  1 
ATOM   2568 C CG1 . VAL B 1 30  ? -23.249 -8.970  -20.026 1.00  33.71 ? 30   VAL A CG1 1 
ATOM   2569 C CG2 . VAL B 1 30  ? -21.848 -10.449 -18.562 1.00  37.68 ? 30   VAL A CG2 1 
ATOM   2570 N N   . VAL B 1 31  ? -23.817 -12.851 -19.185 1.00  39.94 ? 31   VAL A N   1 
ATOM   2571 C CA  . VAL B 1 31  ? -24.925 -13.437 -18.423 1.00  49.56 ? 31   VAL A CA  1 
ATOM   2572 C C   . VAL B 1 31  ? -24.971 -12.913 -16.988 1.00  50.92 ? 31   VAL A C   1 
ATOM   2573 O O   . VAL B 1 31  ? -24.251 -13.419 -16.134 1.00  54.37 ? 31   VAL A O   1 
ATOM   2574 C CB  . VAL B 1 31  ? -24.767 -14.962 -18.326 1.00  51.90 ? 31   VAL A CB  1 
ATOM   2575 C CG1 . VAL B 1 31  ? -26.026 -15.585 -17.746 1.00  59.46 ? 31   VAL A CG1 1 
ATOM   2576 C CG2 . VAL B 1 31  ? -24.441 -15.555 -19.681 1.00  49.50 ? 31   VAL A CG2 1 
ATOM   2577 N N   . THR B 1 32  ? -25.809 -11.911 -16.722 1.00  51.03 ? 32   THR A N   1 
ATOM   2578 C CA  . THR B 1 32  ? -25.925 -11.346 -15.378 1.00  49.49 ? 32   THR A CA  1 
ATOM   2579 C C   . THR B 1 32  ? -27.235 -11.702 -14.698 1.00  56.78 ? 32   THR A C   1 
ATOM   2580 O O   . THR B 1 32  ? -28.319 -11.383 -15.200 1.00  55.60 ? 32   THR A O   1 
ATOM   2581 C CB  . THR B 1 32  ? -25.794 -9.804  -15.358 1.00  57.06 ? 32   THR A CB  1 
ATOM   2582 O OG1 . THR B 1 32  ? -26.623 -9.225  -16.378 1.00  60.26 ? 32   THR A OG1 1 
ATOM   2583 C CG2 . THR B 1 32  ? -24.341 -9.378  -15.556 1.00  53.76 ? 32   THR A CG2 1 
ATOM   2584 N N   . LYS B 1 33  ? -27.125 -12.336 -13.535 0.010 50.02 ? 33   LYS A N   1 
ATOM   2585 C CA  . LYS B 1 33  ? -28.292 -12.749 -12.769 0.010 49.24 ? 33   LYS A CA  1 
ATOM   2586 C C   . LYS B 1 33  ? -28.096 -12.584 -11.263 0.010 47.26 ? 33   LYS A C   1 
ATOM   2587 O O   . LYS B 1 33  ? -27.160 -11.925 -10.808 0.010 44.63 ? 33   LYS A O   1 
ATOM   2588 C CB  . LYS B 1 33  ? -28.653 -14.203 -13.090 0.010 49.64 ? 33   LYS A CB  1 
ATOM   2589 C CG  . LYS B 1 33  ? -27.458 -15.104 -13.377 0.010 49.74 ? 33   LYS A CG  1 
ATOM   2590 C CD  . LYS B 1 33  ? -27.743 -16.539 -12.952 0.010 50.96 ? 33   LYS A CD  1 
ATOM   2591 C CE  . LYS B 1 33  ? -26.883 -17.542 -13.711 0.010 51.85 ? 33   LYS A CE  1 
ATOM   2592 N NZ  . LYS B 1 33  ? -27.403 -17.803 -15.084 0.010 51.63 ? 33   LYS A NZ  1 
ATOM   2593 N N   . LYS B 1 34  ? -29.002 -13.186 -10.502 1.00  53.22 ? 34   LYS A N   1 
ATOM   2594 C CA  . LYS B 1 34  ? -28.935 -13.201 -9.052  1.00  47.11 ? 34   LYS A CA  1 
ATOM   2595 C C   . LYS B 1 34  ? -29.387 -14.565 -8.553  1.00  50.98 ? 34   LYS A C   1 
ATOM   2596 O O   . LYS B 1 34  ? -30.538 -14.952 -8.756  1.00  49.66 ? 34   LYS A O   1 
ATOM   2597 C CB  . LYS B 1 34  ? -29.836 -12.116 -8.463  1.00  47.22 ? 34   LYS A CB  1 
ATOM   2598 C CG  . LYS B 1 34  ? -29.279 -10.711 -8.575  1.00  52.57 ? 34   LYS A CG  1 
ATOM   2599 C CD  . LYS B 1 34  ? -29.459 -9.945  -7.270  1.00  47.61 ? 34   LYS A CD  1 
ATOM   2600 C CE  . LYS B 1 34  ? -30.931 -9.793  -6.913  1.00  45.95 ? 34   LYS A CE  1 
ATOM   2601 N NZ  . LYS B 1 34  ? -31.106 -9.143  -5.575  1.00  55.07 ? 34   LYS A NZ  1 
ATOM   2602 N N   . PHE B 1 35  ? -28.487 -15.304 -7.914  1.00  49.83 ? 35   PHE A N   1 
ATOM   2603 C CA  . PHE B 1 35  ? -28.863 -16.606 -7.387  1.00  50.08 ? 35   PHE A CA  1 
ATOM   2604 C C   . PHE B 1 35  ? -29.975 -16.459 -6.356  1.00  48.57 ? 35   PHE A C   1 
ATOM   2605 O O   . PHE B 1 35  ? -30.184 -15.380 -5.782  1.00  48.16 ? 35   PHE A O   1 
ATOM   2606 C CB  . PHE B 1 35  ? -27.668 -17.331 -6.766  1.00  49.10 ? 35   PHE A CB  1 
ATOM   2607 C CG  . PHE B 1 35  ? -26.484 -17.439 -7.673  1.00  53.20 ? 35   PHE A CG  1 
ATOM   2608 C CD1 . PHE B 1 35  ? -25.301 -16.796 -7.358  1.00  49.89 ? 35   PHE A CD1 1 
ATOM   2609 C CD2 . PHE B 1 35  ? -26.548 -18.186 -8.836  1.00  54.55 ? 35   PHE A CD2 1 
ATOM   2610 C CE1 . PHE B 1 35  ? -24.199 -16.890 -8.190  1.00  53.43 ? 35   PHE A CE1 1 
ATOM   2611 C CE2 . PHE B 1 35  ? -25.456 -18.292 -9.667  1.00  55.29 ? 35   PHE A CE2 1 
ATOM   2612 C CZ  . PHE B 1 35  ? -24.275 -17.643 -9.343  1.00  57.06 ? 35   PHE A CZ  1 
ATOM   2613 N N   . SER B 1 36  ? -30.685 -17.555 -6.123  0.010 45.93 ? 36   SER A N   1 
ATOM   2614 C CA  . SER B 1 36  ? -31.775 -17.573 -5.163  0.010 43.71 ? 36   SER A CA  1 
ATOM   2615 C C   . SER B 1 36  ? -31.393 -16.848 -3.876  0.010 42.54 ? 36   SER A C   1 
ATOM   2616 O O   . SER B 1 36  ? -32.197 -16.109 -3.310  0.010 42.47 ? 36   SER A O   1 
ATOM   2617 C CB  . SER B 1 36  ? -32.180 -19.013 -4.854  0.010 42.33 ? 36   SER A CB  1 
ATOM   2618 O OG  . SER B 1 36  ? -33.298 -19.052 -3.990  0.010 41.24 ? 36   SER A OG  1 
ATOM   2619 N N   . ASN B 1 37  ? -30.159 -17.048 -3.426  0.50  40.22 ? 37   ASN A N   1 
ATOM   2620 C CA  . ASN B 1 37  ? -29.711 -16.460 -2.168  0.50  40.95 ? 37   ASN A CA  1 
ATOM   2621 C C   . ASN B 1 37  ? -29.088 -15.054 -2.282  0.50  40.58 ? 37   ASN A C   1 
ATOM   2622 O O   . ASN B 1 37  ? -28.278 -14.652 -1.451  0.50  37.26 ? 37   ASN A O   1 
ATOM   2623 C CB  . ASN B 1 37  ? -28.810 -17.435 -1.396  0.50  40.00 ? 37   ASN A CB  1 
ATOM   2624 C CG  . ASN B 1 37  ? -27.454 -17.640 -2.043  0.50  42.99 ? 37   ASN A CG  1 
ATOM   2625 O OD1 . ASN B 1 37  ? -27.326 -17.684 -3.263  0.50  44.97 ? 37   ASN A OD1 1 
ATOM   2626 N ND2 . ASN B 1 37  ? -26.428 -17.779 -1.211  0.50  45.96 ? 37   ASN A ND2 1 
ATOM   2627 N N   . GLN B 1 38  ? -29.484 -14.322 -3.322  1.00  42.31 ? 38   GLN A N   1 
ATOM   2628 C CA  . GLN B 1 38  ? -29.178 -12.892 -3.478  1.00  42.54 ? 38   GLN A CA  1 
ATOM   2629 C C   . GLN B 1 38  ? -27.782 -12.528 -4.034  1.00  40.41 ? 38   GLN A C   1 
ATOM   2630 O O   . GLN B 1 38  ? -27.551 -11.380 -4.414  1.00  41.23 ? 38   GLN A O   1 
ATOM   2631 C CB  . GLN B 1 38  ? -29.438 -12.136 -2.171  1.00  41.17 ? 38   GLN A CB  1 
ATOM   2632 C CG  . GLN B 1 38  ? -30.725 -12.528 -1.440  1.00  47.78 ? 38   GLN A CG  1 
ATOM   2633 C CD  . GLN B 1 38  ? -31.958 -11.812 -1.968  1.00  50.70 ? 38   GLN A CD  1 
ATOM   2634 O OE1 . GLN B 1 38  ? -32.188 -11.752 -3.176  1.00  53.52 ? 38   GLN A OE1 1 
ATOM   2635 N NE2 . GLN B 1 38  ? -32.758 -11.258 -1.056  1.00  49.61 ? 38   GLN A NE2 1 
ATOM   2636 N N   . GLU B 1 39  ? -26.857 -13.481 -4.085  1.00  36.94 ? 39   GLU A N   1 
ATOM   2637 C CA  . GLU B 1 39  ? -25.525 -13.218 -4.641  1.00  34.55 ? 39   GLU A CA  1 
ATOM   2638 C C   . GLU B 1 39  ? -25.572 -12.884 -6.130  1.00  39.24 ? 39   GLU A C   1 
ATOM   2639 O O   . GLU B 1 39  ? -26.268 -13.554 -6.889  1.00  35.10 ? 39   GLU A O   1 
ATOM   2640 C CB  . GLU B 1 39  ? -24.632 -14.441 -4.486  1.00  33.19 ? 39   GLU A CB  1 
ATOM   2641 C CG  . GLU B 1 39  ? -24.371 -14.836 -3.076  1.00  40.85 ? 39   GLU A CG  1 
ATOM   2642 C CD  . GLU B 1 39  ? -23.124 -15.671 -2.960  1.00  41.19 ? 39   GLU A CD  1 
ATOM   2643 O OE1 . GLU B 1 39  ? -22.665 -16.216 -3.983  1.00  39.13 ? 39   GLU A OE1 1 
ATOM   2644 O OE2 . GLU B 1 39  ? -22.583 -15.758 -1.844  1.00  48.19 ? 39   GLU A OE2 1 
ATOM   2645 N N   . THR B 1 40  ? -24.801 -11.881 -6.549  1.00  27.93 ? 40   THR A N   1 
ATOM   2646 C CA  . THR B 1 40  ? -24.739 -11.527 -7.963  1.00  31.54 ? 40   THR A CA  1 
ATOM   2647 C C   . THR B 1 40  ? -23.920 -12.543 -8.749  1.00  31.40 ? 40   THR A C   1 
ATOM   2648 O O   . THR B 1 40  ? -22.792 -12.893 -8.373  1.00  31.30 ? 40   THR A O   1 
ATOM   2649 C CB  . THR B 1 40  ? -24.098 -10.151 -8.198  1.00  34.53 ? 40   THR A CB  1 
ATOM   2650 O OG1 . THR B 1 40  ? -24.788 -9.154  -7.432  1.00  33.51 ? 40   THR A OG1 1 
ATOM   2651 C CG2 . THR B 1 40  ? -24.156 -9.797  -9.699  1.00  31.10 ? 40   THR A CG2 1 
ATOM   2652 N N   . CYS B 1 41  ? -24.478 -12.999 -9.860  0.89  33.98 ? 41   CYS A N   1 
ATOM   2653 C CA  . CYS B 1 41  ? -23.770 -13.909 -10.736 0.89  36.12 ? 41   CYS A CA  1 
ATOM   2654 C C   . CYS B 1 41  ? -23.483 -13.236 -12.073 0.89  40.04 ? 41   CYS A C   1 
ATOM   2655 O O   . CYS B 1 41  ? -24.402 -12.747 -12.734 0.89  37.05 ? 41   CYS A O   1 
ATOM   2656 C CB  . CYS B 1 41  ? -24.608 -15.157 -10.975 0.89  47.54 ? 41   CYS A CB  1 
ATOM   2657 S SG  . CYS B 1 41  ? -23.976 -16.189 -12.311 0.89  55.95 ? 41   CYS A SG  1 
ATOM   2658 N N   . VAL B 1 42  ? -22.210 -13.217 -12.460 1.00  38.25 ? 42   VAL A N   1 
ATOM   2659 C CA  . VAL B 1 42  ? -21.792 -12.627 -13.733 1.00  40.34 ? 42   VAL A CA  1 
ATOM   2660 C C   . VAL B 1 42  ? -20.876 -13.559 -14.513 1.00  40.48 ? 42   VAL A C   1 
ATOM   2661 O O   . VAL B 1 42  ? -20.043 -14.263 -13.936 1.00  43.95 ? 42   VAL A O   1 
ATOM   2662 C CB  . VAL B 1 42  ? -21.082 -11.279 -13.543 1.00  41.02 ? 42   VAL A CB  1 
ATOM   2663 C CG1 . VAL B 1 42  ? -20.316 -10.902 -14.803 1.00  40.28 ? 42   VAL A CG1 1 
ATOM   2664 C CG2 . VAL B 1 42  ? -22.093 -10.192 -13.171 1.00  41.16 ? 42   VAL A CG2 1 
ATOM   2665 N N   . GLU B 1 43  ? -21.035 -13.561 -15.833 0.40  36.32 ? 43   GLU A N   1 
ATOM   2666 C CA  . GLU B 1 43  ? -20.288 -14.462 -16.687 0.40  33.88 ? 43   GLU A CA  1 
ATOM   2667 C C   . GLU B 1 43  ? -20.086 -13.832 -18.066 0.40  36.07 ? 43   GLU A C   1 
ATOM   2668 O O   . GLU B 1 43  ? -20.983 -13.866 -18.902 0.40  30.80 ? 43   GLU A O   1 
ATOM   2669 C CB  . GLU B 1 43  ? -21.048 -15.782 -16.821 0.40  38.53 ? 43   GLU A CB  1 
ATOM   2670 C CG  . GLU B 1 43  ? -20.199 -16.971 -17.228 0.40  38.96 ? 43   GLU A CG  1 
ATOM   2671 C CD  . GLU B 1 43  ? -19.561 -17.658 -16.041 0.40  40.53 ? 43   GLU A CD  1 
ATOM   2672 O OE1 . GLU B 1 43  ? -19.701 -18.895 -15.923 0.40  45.97 ? 43   GLU A OE1 1 
ATOM   2673 O OE2 . GLU B 1 43  ? -18.925 -16.963 -15.223 0.40  44.96 ? 43   GLU A OE2 1 
ATOM   2674 N N   . ILE B 1 44  ? -18.908 -13.254 -18.289 1.00  35.73 ? 44   ILE A N   1 
ATOM   2675 C CA  . ILE B 1 44  ? -18.571 -12.605 -19.560 1.00  37.88 ? 44   ILE A CA  1 
ATOM   2676 C C   . ILE B 1 44  ? -18.608 -13.624 -20.701 1.00  36.74 ? 44   ILE A C   1 
ATOM   2677 O O   . ILE B 1 44  ? -17.827 -14.573 -20.718 1.00  35.49 ? 44   ILE A O   1 
ATOM   2678 C CB  . ILE B 1 44  ? -17.169 -11.933 -19.502 1.00  33.91 ? 44   ILE A CB  1 
ATOM   2679 C CG1 . ILE B 1 44  ? -17.096 -10.881 -18.383 1.00  37.17 ? 44   ILE A CG1 1 
ATOM   2680 C CG2 . ILE B 1 44  ? -16.828 -11.270 -20.830 1.00  33.82 ? 44   ILE A CG2 1 
ATOM   2681 C CD1 . ILE B 1 44  ? -17.821 -9.564  -18.702 1.00  37.13 ? 44   ILE A CD1 1 
ATOM   2682 N N   . GLY B 1 45  ? -19.504 -13.418 -21.662 1.00  34.18 ? 45   GLY A N   1 
ATOM   2683 C CA  . GLY B 1 45  ? -19.776 -14.429 -22.667 1.00  35.12 ? 45   GLY A CA  1 
ATOM   2684 C C   . GLY B 1 45  ? -18.845 -14.470 -23.865 1.00  38.36 ? 45   GLY A C   1 
ATOM   2685 O O   . GLY B 1 45  ? -19.076 -15.227 -24.802 1.00  36.75 ? 45   GLY A O   1 
ATOM   2686 N N   . GLU B 1 46  ? -17.793 -13.662 -23.843 0.88  32.27 ? 46   GLU A N   1 
ATOM   2687 C CA  . GLU B 1 46  ? -16.832 -13.651 -24.934 0.88  33.45 ? 46   GLU A CA  1 
ATOM   2688 C C   . GLU B 1 46  ? -15.469 -13.178 -24.448 0.88  36.50 ? 46   GLU A C   1 
ATOM   2689 O O   . GLU B 1 46  ? -15.348 -12.615 -23.363 0.88  29.48 ? 46   GLU A O   1 
ATOM   2690 C CB  . GLU B 1 46  ? -17.314 -12.769 -26.083 0.88  31.81 ? 46   GLU A CB  1 
ATOM   2691 C CG  . GLU B 1 46  ? -17.673 -11.338 -25.682 0.88  32.50 ? 46   GLU A CG  1 
ATOM   2692 C CD  . GLU B 1 46  ? -18.263 -10.556 -26.841 0.88  32.55 ? 46   GLU A CD  1 
ATOM   2693 O OE1 . GLU B 1 46  ? -17.511 -10.247 -27.794 0.88  39.86 ? 46   GLU A OE1 1 
ATOM   2694 O OE2 . GLU B 1 46  ? -19.476 -10.269 -26.814 0.88  30.20 ? 46   GLU A OE2 1 
ATOM   2695 N N   . SER B 1 47  ? -14.449 -13.416 -25.259 1.00  30.94 ? 47   SER A N   1 
ATOM   2696 C CA  . SER B 1 47  ? -13.099 -13.012 -24.913 1.00  36.28 ? 47   SER A CA  1 
ATOM   2697 C C   . SER B 1 47  ? -12.981 -11.499 -24.946 1.00  33.85 ? 47   SER A C   1 
ATOM   2698 O O   . SER B 1 47  ? -13.496 -10.852 -25.859 1.00  25.86 ? 47   SER A O   1 
ATOM   2699 C CB  . SER B 1 47  ? -12.081 -13.616 -25.877 1.00  32.12 ? 47   SER A CB  1 
ATOM   2700 O OG  . SER B 1 47  ? -10.776 -13.178 -25.524 1.00  34.53 ? 47   SER A OG  1 
ATOM   2701 N N   . VAL B 1 48  ? -12.304 -10.927 -23.953 1.00  24.56 ? 48   VAL A N   1 
ATOM   2702 C CA  . VAL B 1 48  ? -12.050 -9.486  -23.976 1.00  25.40 ? 48   VAL A CA  1 
ATOM   2703 C C   . VAL B 1 48  ? -10.553 -9.194  -23.977 1.00  29.81 ? 48   VAL A C   1 
ATOM   2704 O O   . VAL B 1 48  ? -10.117 -8.055  -23.797 1.00  27.62 ? 48   VAL A O   1 
ATOM   2705 C CB  . VAL B 1 48  ? -12.746 -8.774  -22.817 1.00  27.78 ? 48   VAL A CB  1 
ATOM   2706 C CG1 . VAL B 1 48  ? -14.259 -8.822  -23.025 1.00  27.42 ? 48   VAL A CG1 1 
ATOM   2707 C CG2 . VAL B 1 48  ? -12.341 -9.394  -21.475 1.00  26.12 ? 48   VAL A CG2 1 
ATOM   2708 N N   . ARG B 1 49  ? -9.770  -10.243 -24.205 1.00  25.02 ? 49   ARG A N   1 
ATOM   2709 C CA  . ARG B 1 49  ? -8.313  -10.156 -24.179 1.00  28.94 ? 49   ARG A CA  1 
ATOM   2710 C C   . ARG B 1 49  ? -7.824  -9.076  -25.144 1.00  33.78 ? 49   ARG A C   1 
ATOM   2711 O O   . ARG B 1 49  ? -8.158  -9.104  -26.327 1.00  28.93 ? 49   ARG A O   1 
ATOM   2712 C CB  . ARG B 1 49  ? -7.724  -11.525 -24.547 1.00  30.81 ? 49   ARG A CB  1 
ATOM   2713 C CG  . ARG B 1 49  ? -6.279  -11.742 -24.143 1.00  35.43 ? 49   ARG A CG  1 
ATOM   2714 C CD  . ARG B 1 49  ? -5.837  -13.169 -24.445 1.00  37.10 ? 49   ARG A CD  1 
ATOM   2715 N NE  . ARG B 1 49  ? -6.455  -14.132 -23.542 1.00  36.42 ? 49   ARG A NE  1 
ATOM   2716 C CZ  . ARG B 1 49  ? -5.936  -14.487 -22.369 1.00  31.85 ? 49   ARG A CZ  1 
ATOM   2717 N NH1 . ARG B 1 49  ? -4.778  -13.969 -21.968 1.00  37.70 ? 49   ARG A NH1 1 
ATOM   2718 N NH2 . ARG B 1 49  ? -6.560  -15.373 -21.606 1.00  31.30 ? 49   ARG A NH2 1 
ATOM   2719 N N   . GLY B 1 50  ? -7.054  -8.116  -24.638 1.00  30.71 ? 50   GLY A N   1 
ATOM   2720 C CA  . GLY B 1 50  ? -6.474  -7.086  -25.486 1.00  29.19 ? 50   GLY A CA  1 
ATOM   2721 C C   . GLY B 1 50  ? -7.454  -6.009  -25.931 1.00  34.28 ? 50   GLY A C   1 
ATOM   2722 O O   . GLY B 1 50  ? -7.108  -5.100  -26.693 1.00  30.02 ? 50   GLY A O   1 
ATOM   2723 N N   . GLU B 1 51  ? -8.685  -6.087  -25.445 1.00  26.52 ? 51   GLU A N   1 
ATOM   2724 C CA  . GLU B 1 51  ? -9.688  -5.117  -25.871 1.00  29.16 ? 51   GLU A CA  1 
ATOM   2725 C C   . GLU B 1 51  ? -9.864  -3.919  -24.922 1.00  25.98 ? 51   GLU A C   1 
ATOM   2726 O O   . GLU B 1 51  ? -9.507  -3.990  -23.745 1.00  23.88 ? 51   GLU A O   1 
ATOM   2727 C CB  . GLU B 1 51  ? -11.011 -5.828  -26.114 1.00  26.47 ? 51   GLU A CB  1 
ATOM   2728 C CG  . GLU B 1 51  ? -10.877 -7.007  -27.076 1.00  28.32 ? 51   GLU A CG  1 
ATOM   2729 C CD  . GLU B 1 51  ? -12.215 -7.473  -27.597 1.00  42.59 ? 51   GLU A CD  1 
ATOM   2730 O OE1 . GLU B 1 51  ? -13.090 -7.772  -26.760 1.00  46.30 ? 51   GLU A OE1 1 
ATOM   2731 O OE2 . GLU B 1 51  ? -12.406 -7.517  -28.836 1.00  47.92 ? 51   GLU A OE2 1 
ATOM   2732 N N   . ASP B 1 52  ? -10.403 -2.829  -25.467 1.00  29.00 ? 52   ASP A N   1 
ATOM   2733 C CA  . ASP B 1 52  ? -10.689 -1.598  -24.733 1.00  27.96 ? 52   ASP A CA  1 
ATOM   2734 C C   . ASP B 1 52  ? -12.139 -1.697  -24.241 1.00  26.34 ? 52   ASP A C   1 
ATOM   2735 O O   . ASP B 1 52  ? -13.085 -1.443  -24.983 1.00  25.36 ? 52   ASP A O   1 
ATOM   2736 C CB  . ASP B 1 52  ? -10.483 -0.384  -25.663 1.00  25.29 ? 52   ASP A CB  1 
ATOM   2737 C CG  . ASP B 1 52  ? -10.411 0.956   -24.918 1.00  31.03 ? 52   ASP A CG  1 
ATOM   2738 O OD1 . ASP B 1 52  ? -10.244 0.984   -23.668 1.00  26.72 ? 52   ASP A OD1 1 
ATOM   2739 O OD2 . ASP B 1 52  ? -10.505 2.002   -25.599 1.00  27.10 ? 52   ASP A OD2 1 
ATOM   2740 N N   . VAL B 1 53  ? -12.313 -2.107  -22.992 1.00  25.59 ? 53   VAL A N   1 
ATOM   2741 C CA  . VAL B 1 53  ? -13.655 -2.432  -22.472 1.00  25.40 ? 53   VAL A CA  1 
ATOM   2742 C C   . VAL B 1 53  ? -14.345 -1.285  -21.723 1.00  25.30 ? 53   VAL A C   1 
ATOM   2743 O O   . VAL B 1 53  ? -13.752 -0.642  -20.847 1.00  23.57 ? 53   VAL A O   1 
ATOM   2744 C CB  . VAL B 1 53  ? -13.596 -3.692  -21.578 1.00  22.20 ? 53   VAL A CB  1 
ATOM   2745 C CG1 . VAL B 1 53  ? -14.952 -3.965  -20.920 1.00  23.86 ? 53   VAL A CG1 1 
ATOM   2746 C CG2 . VAL B 1 53  ? -13.108 -4.902  -22.398 1.00  24.84 ? 53   VAL A CG2 1 
ATOM   2747 N N   . TYR B 1 54  ? -15.601 -1.036  -22.081 1.00  23.14 ? 54   TYR A N   1 
ATOM   2748 C CA  . TYR B 1 54  ? -16.426 -0.032  -21.426 1.00  20.03 ? 54   TYR A CA  1 
ATOM   2749 C C   . TYR B 1 54  ? -17.648 -0.699  -20.814 1.00  25.07 ? 54   TYR A C   1 
ATOM   2750 O O   . TYR B 1 54  ? -18.436 -1.330  -21.516 1.00  23.00 ? 54   TYR A O   1 
ATOM   2751 C CB  . TYR B 1 54  ? -16.861 1.055   -22.419 1.00  23.11 ? 54   TYR A CB  1 
ATOM   2752 C CG  . TYR B 1 54  ? -15.680 1.810   -22.979 1.00  24.67 ? 54   TYR A CG  1 
ATOM   2753 C CD1 . TYR B 1 54  ? -14.841 1.218   -23.913 1.00  26.66 ? 54   TYR A CD1 1 
ATOM   2754 C CD2 . TYR B 1 54  ? -15.365 3.093   -22.533 1.00  25.33 ? 54   TYR A CD2 1 
ATOM   2755 C CE1 . TYR B 1 54  ? -13.732 1.889   -24.419 1.00  26.13 ? 54   TYR A CE1 1 
ATOM   2756 C CE2 . TYR B 1 54  ? -14.253 3.770   -23.033 1.00  27.95 ? 54   TYR A CE2 1 
ATOM   2757 C CZ  . TYR B 1 54  ? -13.451 3.164   -23.980 1.00  27.85 ? 54   TYR A CZ  1 
ATOM   2758 O OH  . TYR B 1 54  ? -12.346 3.816   -24.485 1.00  26.00 ? 54   TYR A OH  1 
ATOM   2759 N N   . ILE B 1 55  ? -17.809 -0.560  -19.499 1.00  21.45 ? 55   ILE A N   1 
ATOM   2760 C CA  . ILE B 1 55  ? -18.977 -1.131  -18.838 1.00  22.01 ? 55   ILE A CA  1 
ATOM   2761 C C   . ILE B 1 55  ? -19.890 -0.022  -18.381 1.00  24.10 ? 55   ILE A C   1 
ATOM   2762 O O   . ILE B 1 55  ? -19.489 0.844   -17.605 1.00  24.37 ? 55   ILE A O   1 
ATOM   2763 C CB  . ILE B 1 55  ? -18.596 -2.019  -17.647 1.00  23.21 ? 55   ILE A CB  1 
ATOM   2764 C CG1 . ILE B 1 55  ? -17.731 -3.172  -18.147 1.00  24.04 ? 55   ILE A CG1 1 
ATOM   2765 C CG2 . ILE B 1 55  ? -19.867 -2.561  -16.975 1.00  22.70 ? 55   ILE A CG2 1 
ATOM   2766 C CD1 . ILE B 1 55  ? -16.670 -3.641  -17.166 1.00  23.31 ? 55   ILE A CD1 1 
ATOM   2767 N N   . VAL B 1 56  ? -21.114 -0.045  -18.896 1.00  20.17 ? 56   VAL A N   1 
ATOM   2768 C CA  . VAL B 1 56  ? -22.081 0.994   -18.631 1.00  25.54 ? 56   VAL A CA  1 
ATOM   2769 C C   . VAL B 1 56  ? -22.957 0.509   -17.497 1.00  29.53 ? 56   VAL A C   1 
ATOM   2770 O O   . VAL B 1 56  ? -23.597 -0.533  -17.588 1.00  29.31 ? 56   VAL A O   1 
ATOM   2771 C CB  . VAL B 1 56  ? -22.917 1.323   -19.886 1.00  27.08 ? 56   VAL A CB  1 
ATOM   2772 C CG1 . VAL B 1 56  ? -23.904 2.442   -19.599 1.00  26.15 ? 56   VAL A CG1 1 
ATOM   2773 C CG2 . VAL B 1 56  ? -22.006 1.717   -21.028 1.00  27.75 ? 56   VAL A CG2 1 
ATOM   2774 N N   . GLN B 1 57  ? -22.956 1.281   -16.421 1.00  26.03 ? 57   GLN A N   1 
ATOM   2775 C CA  . GLN B 1 57  ? -23.577 0.878   -15.172 1.00  38.13 ? 57   GLN A CA  1 
ATOM   2776 C C   . GLN B 1 57  ? -25.047 0.595   -15.413 1.00  43.24 ? 57   GLN A C   1 
ATOM   2777 O O   . GLN B 1 57  ? -25.618 1.098   -16.375 1.00  49.88 ? 57   GLN A O   1 
ATOM   2778 C CB  . GLN B 1 57  ? -23.377 1.977   -14.129 1.00  36.56 ? 57   GLN A CB  1 
ATOM   2779 C CG  . GLN B 1 57  ? -24.632 2.395   -13.430 1.00  45.10 ? 57   GLN A CG  1 
ATOM   2780 C CD  . GLN B 1 57  ? -25.357 3.496   -14.153 1.00  47.11 ? 57   GLN A CD  1 
ATOM   2781 O OE1 . GLN B 1 57  ? -25.635 4.553   -13.576 1.00  43.67 ? 57   GLN A OE1 1 
ATOM   2782 N NE2 . GLN B 1 57  ? -25.676 3.264   -15.424 1.00  45.86 ? 57   GLN A NE2 1 
ATOM   2783 N N   . SER B 1 58  ? -25.652 -0.227  -14.560 0.10  41.76 ? 58   SER A N   1 
ATOM   2784 C CA  . SER B 1 58  ? -27.045 -0.612  -14.749 0.10  43.41 ? 58   SER A CA  1 
ATOM   2785 C C   . SER B 1 58  ? -28.000 0.372   -14.091 0.10  42.59 ? 58   SER A C   1 
ATOM   2786 O O   . SER B 1 58  ? -27.588 1.411   -13.579 0.10  42.91 ? 58   SER A O   1 
ATOM   2787 C CB  . SER B 1 58  ? -27.298 -2.022  -14.211 0.10  44.86 ? 58   SER A CB  1 
ATOM   2788 O OG  . SER B 1 58  ? -28.563 -2.504  -14.628 0.10  45.54 ? 58   SER A OG  1 
ATOM   2789 N N   . GLY B 1 59  ? -29.284 0.035   -14.116 0.010 44.00 ? 59   GLY A N   1 
ATOM   2790 C CA  . GLY B 1 59  ? -30.308 0.865   -13.514 0.010 43.12 ? 59   GLY A CA  1 
ATOM   2791 C C   . GLY B 1 59  ? -31.414 0.018   -12.920 0.010 41.85 ? 59   GLY A C   1 
ATOM   2792 O O   . GLY B 1 59  ? -32.589 0.371   -13.005 0.010 41.42 ? 59   GLY A O   1 
ATOM   2793 N N   . CYS B 1 60  ? -31.040 -1.109  -12.322 0.010 40.92 ? 60   CYS A N   1 
ATOM   2794 C CA  . CYS B 1 60  ? -32.009 -1.986  -11.675 0.010 39.83 ? 60   CYS A CA  1 
ATOM   2795 C C   . CYS B 1 60  ? -32.471 -1.420  -10.336 0.010 36.73 ? 60   CYS A C   1 
ATOM   2796 O O   . CYS B 1 60  ? -32.899 -2.165  -9.458  0.010 35.84 ? 60   CYS A O   1 
ATOM   2797 C CB  . CYS B 1 60  ? -31.432 -3.391  -11.485 0.010 41.42 ? 60   CYS A CB  1 
ATOM   2798 S SG  . CYS B 1 60  ? -32.110 -4.632  -12.605 0.010 47.60 ? 60   CYS A SG  1 
ATOM   2799 N N   . GLY B 1 61  ? -32.375 -0.102  -10.186 0.010 36.12 ? 61   GLY A N   1 
ATOM   2800 C CA  . GLY B 1 61  ? -32.848 0.576   -8.991  0.010 34.03 ? 61   GLY A CA  1 
ATOM   2801 C C   . GLY B 1 61  ? -32.049 0.272   -7.740  0.010 31.80 ? 61   GLY A C   1 
ATOM   2802 O O   . GLY B 1 61  ? -31.589 1.183   -7.053  0.010 31.48 ? 61   GLY A O   1 
ATOM   2803 N N   . GLU B 1 62  ? -31.894 -1.013  -7.439  0.10  30.26 ? 62   GLU A N   1 
ATOM   2804 C CA  . GLU B 1 62  ? -31.169 -1.437  -6.249  0.10  28.57 ? 62   GLU A CA  1 
ATOM   2805 C C   . GLU B 1 62  ? -29.699 -1.038  -6.353  0.10  27.10 ? 62   GLU A C   1 
ATOM   2806 O O   . GLU B 1 62  ? -28.908 -1.700  -7.022  0.10  24.93 ? 62   GLU A O   1 
ATOM   2807 C CB  . GLU B 1 62  ? -31.308 -2.947  -6.050  0.10  27.80 ? 62   GLU A CB  1 
ATOM   2808 C CG  . GLU B 1 62  ? -31.688 -3.357  -4.633  0.10  28.14 ? 62   GLU A CG  1 
ATOM   2809 C CD  . GLU B 1 62  ? -30.531 -3.253  -3.655  0.10  26.58 ? 62   GLU A CD  1 
ATOM   2810 O OE1 . GLU B 1 62  ? -29.424 -2.871  -4.077  0.10  24.60 ? 62   GLU A OE1 1 
ATOM   2811 O OE2 . GLU B 1 62  ? -30.741 -3.558  -2.467  0.10  26.36 ? 62   GLU A OE2 1 
ATOM   2812 N N   . ILE B 1 63  ? -29.343 0.046   -5.675  1.00  29.14 ? 63   ILE A N   1 
ATOM   2813 C CA  . ILE B 1 63  ? -28.012 0.642   -5.814  1.00  28.58 ? 63   ILE A CA  1 
ATOM   2814 C C   . ILE B 1 63  ? -26.860 -0.269  -5.391  1.00  28.30 ? 63   ILE A C   1 
ATOM   2815 O O   . ILE B 1 63  ? -25.790 -0.226  -5.993  1.00  23.32 ? 63   ILE A O   1 
ATOM   2816 C CB  . ILE B 1 63  ? -27.867 1.950   -5.042  1.00  31.23 ? 63   ILE A CB  1 
ATOM   2817 C CG1 . ILE B 1 63  ? -26.541 2.610   -5.407  1.00  31.25 ? 63   ILE A CG1 1 
ATOM   2818 C CG2 . ILE B 1 63  ? -27.891 1.698   -3.548  1.00  34.27 ? 63   ILE A CG2 1 
ATOM   2819 C CD1 . ILE B 1 63  ? -26.275 3.888   -4.666  1.00  39.09 ? 63   ILE A CD1 1 
ATOM   2820 N N   . ASN B 1 64  ? -27.060 -1.079  -4.354  1.00  21.00 ? 64   ASN A N   1 
ATOM   2821 C CA  . ASN B 1 64  ? -25.979 -1.954  -3.918  1.00  25.77 ? 64   ASN A CA  1 
ATOM   2822 C C   . ASN B 1 64  ? -25.775 -3.145  -4.860  1.00  26.61 ? 64   ASN A C   1 
ATOM   2823 O O   . ASN B 1 64  ? -24.639 -3.571  -5.101  1.00  20.42 ? 64   ASN A O   1 
ATOM   2824 C CB  . ASN B 1 64  ? -26.179 -2.411  -2.473  1.00  23.57 ? 64   ASN A CB  1 
ATOM   2825 C CG  . ASN B 1 64  ? -26.142 -1.255  -1.484  1.00  24.80 ? 64   ASN A CG  1 
ATOM   2826 O OD1 . ASN B 1 64  ? -25.308 -0.357  -1.593  1.00  22.48 ? 64   ASN A OD1 1 
ATOM   2827 N ND2 . ASN B 1 64  ? -27.049 -1.278  -0.506  1.00  28.02 ? 64   ASN A ND2 1 
ATOM   2828 N N   . ASP B 1 65  ? -26.872 -3.684  -5.384  1.00  24.12 ? 65   ASP A N   1 
ATOM   2829 C CA  . ASP B 1 65  ? -26.800 -4.772  -6.351  1.00  26.31 ? 65   ASP A CA  1 
ATOM   2830 C C   . ASP B 1 65  ? -26.126 -4.285  -7.636  1.00  23.36 ? 65   ASP A C   1 
ATOM   2831 O O   . ASP B 1 65  ? -25.317 -4.994  -8.241  1.00  21.60 ? 65   ASP A O   1 
ATOM   2832 C CB  . ASP B 1 65  ? -28.202 -5.275  -6.712  1.00  26.46 ? 65   ASP A CB  1 
ATOM   2833 C CG  . ASP B 1 65  ? -28.897 -5.977  -5.553  1.00  32.17 ? 65   ASP A CG  1 
ATOM   2834 O OD1 . ASP B 1 65  ? -28.211 -6.543  -4.659  1.00  26.56 ? 65   ASP A OD1 1 
ATOM   2835 O OD2 . ASP B 1 65  ? -30.144 -5.969  -5.554  1.00  32.68 ? 65   ASP A OD2 1 
ATOM   2836 N N   . ASN B 1 66  ? -26.490 -3.081  -8.055  1.00  22.73 ? 66   ASN A N   1 
ATOM   2837 C CA  . ASN B 1 66  ? -25.917 -2.509  -9.265  1.00  27.02 ? 66   ASN A CA  1 
ATOM   2838 C C   . ASN B 1 66  ? -24.435 -2.177  -9.109  1.00  23.16 ? 66   ASN A C   1 
ATOM   2839 O O   . ASN B 1 66  ? -23.640 -2.408  -10.022 1.00  21.82 ? 66   ASN A O   1 
ATOM   2840 C CB  . ASN B 1 66  ? -26.715 -1.286  -9.702  1.00  29.44 ? 66   ASN A CB  1 
ATOM   2841 C CG  . ASN B 1 66  ? -28.053 -1.660  -10.318 1.00  36.00 ? 66   ASN A CG  1 
ATOM   2842 O OD1 . ASN B 1 66  ? -28.216 -2.745  -10.878 1.00  39.14 ? 66   ASN A OD1 1 
ATOM   2843 N ND2 . ASN B 1 66  ? -29.016 -0.765  -10.209 1.00  37.94 ? 66   ASN A ND2 1 
ATOM   2844 N N   . LEU B 1 67  ? -24.057 -1.656  -7.943  1.00  22.63 ? 67   LEU A N   1 
ATOM   2845 C CA  . LEU B 1 67  ? -22.638 -1.424  -7.653  1.00  20.58 ? 67   LEU A CA  1 
ATOM   2846 C C   . LEU B 1 67  ? -21.845 -2.740  -7.635  1.00  19.61 ? 67   LEU A C   1 
ATOM   2847 O O   . LEU B 1 67  ? -20.790 -2.850  -8.272  1.00  18.58 ? 67   LEU A O   1 
ATOM   2848 C CB  . LEU B 1 67  ? -22.464 -0.675  -6.324  1.00  24.66 ? 67   LEU A CB  1 
ATOM   2849 C CG  . LEU B 1 67  ? -21.011 -0.457  -5.896  1.00  22.28 ? 67   LEU A CG  1 
ATOM   2850 C CD1 . LEU B 1 67  ? -20.143 0.231   -6.983  1.00  23.21 ? 67   LEU A CD1 1 
ATOM   2851 C CD2 . LEU B 1 67  ? -20.969 0.313   -4.611  1.00  23.23 ? 67   LEU A CD2 1 
ATOM   2852 N N   . MET B 1 68  ? -22.347 -3.752  -6.937  0.70  17.57 ? 68   MET A N   1 
ATOM   2853 C CA  . MET B 1 68  ? -21.651 -5.039  -6.925  0.70  16.74 ? 68   MET A CA  1 
ATOM   2854 C C   . MET B 1 68  ? -21.574 -5.693  -8.314  0.70  16.05 ? 68   MET A C   1 
ATOM   2855 O O   . MET B 1 68  ? -20.556 -6.240  -8.688  0.70  12.86 ? 68   MET A O   1 
ATOM   2856 C CB  . MET B 1 68  ? -22.296 -6.011  -5.942  0.70  18.70 ? 68   MET A CB  1 
ATOM   2857 C CG  . MET B 1 68  ? -21.936 -5.734  -4.486  0.70  25.66 ? 68   MET A CG  1 
ATOM   2858 S SD  . MET B 1 68  ? -20.141 -5.713  -4.217  0.70  31.38 ? 68   MET A SD  1 
ATOM   2859 C CE  . MET B 1 68  ? -19.653 -7.238  -5.000  0.70  14.13 ? 68   MET A CE  1 
ATOM   2860 N N   . GLU B 1 69  ? -22.666 -5.664  -9.066  1.00  19.65 ? 69   GLU A N   1 
ATOM   2861 C CA  . GLU B 1 69  ? -22.621 -6.205  -10.433 1.00  21.07 ? 69   GLU A CA  1 
ATOM   2862 C C   . GLU B 1 69  ? -21.535 -5.486  -11.247 1.00  19.69 ? 69   GLU A C   1 
ATOM   2863 O O   . GLU B 1 69  ? -20.752 -6.124  -11.938 1.00  19.95 ? 69   GLU A O   1 
ATOM   2864 C CB  . GLU B 1 69  ? -23.987 -6.095  -11.103 1.00  26.48 ? 69   GLU A CB  1 
ATOM   2865 C CG  . GLU B 1 69  ? -24.039 -6.615  -12.534 1.00  34.44 ? 69   GLU A CG  1 
ATOM   2866 C CD  . GLU B 1 69  ? -25.425 -6.456  -13.126 1.00  43.78 ? 69   GLU A CD  1 
ATOM   2867 O OE1 . GLU B 1 69  ? -25.870 -5.302  -13.277 1.00  42.84 ? 69   GLU A OE1 1 
ATOM   2868 O OE2 . GLU B 1 69  ? -26.078 -7.478  -13.403 1.00  48.58 ? 69   GLU A OE2 1 
ATOM   2869 N N   . LEU B 1 70  ? -21.458 -4.170  -11.132 1.00  17.45 ? 70   LEU A N   1 
ATOM   2870 C CA  . LEU B 1 70  ? -20.415 -3.432  -11.854 1.00  15.35 ? 70   LEU A CA  1 
ATOM   2871 C C   . LEU B 1 70  ? -18.988 -3.813  -11.418 1.00  20.12 ? 70   LEU A C   1 
ATOM   2872 O O   . LEU B 1 70  ? -18.122 -4.036  -12.262 1.00  17.49 ? 70   LEU A O   1 
ATOM   2873 C CB  . LEU B 1 70  ? -20.635 -1.936  -11.709 1.00  19.58 ? 70   LEU A CB  1 
ATOM   2874 C CG  . LEU B 1 70  ? -19.544 -0.992  -12.218 1.00  24.24 ? 70   LEU A CG  1 
ATOM   2875 C CD1 . LEU B 1 70  ? -19.448 -1.003  -13.761 1.00  20.01 ? 70   LEU A CD1 1 
ATOM   2876 C CD2 . LEU B 1 70  ? -19.853 0.393   -11.694 1.00  22.07 ? 70   LEU A CD2 1 
ATOM   2877 N N   . LEU B 1 71  ? -18.748 -3.892  -10.107 1.00  16.17 ? 71   LEU A N   1 
ATOM   2878 C CA  . LEU B 1 71  ? -17.431 -4.237  -9.581  1.00  17.42 ? 71   LEU A CA  1 
ATOM   2879 C C   . LEU B 1 71  ? -17.018 -5.626  -10.059 1.00  18.27 ? 71   LEU A C   1 
ATOM   2880 O O   . LEU B 1 71  ? -15.881 -5.845  -10.462 1.00  19.29 ? 71   LEU A O   1 
ATOM   2881 C CB  . LEU B 1 71  ? -17.444 -4.176  -8.043  1.00  14.86 ? 71   LEU A CB  1 
ATOM   2882 C CG  . LEU B 1 71  ? -17.689 -2.772  -7.467  1.00  17.30 ? 71   LEU A CG  1 
ATOM   2883 C CD1 . LEU B 1 71  ? -17.842 -2.803  -5.953  1.00  21.06 ? 71   LEU A CD1 1 
ATOM   2884 C CD2 . LEU B 1 71  ? -16.553 -1.849  -7.852  1.00  18.57 ? 71   LEU A CD2 1 
ATOM   2885 N N   . ILE B 1 72  ? -17.967 -6.554  -10.041 1.00  17.98 ? 72   ILE A N   1 
ATOM   2886 C CA  . ILE B 1 72  ? -17.712 -7.926  -10.454 1.00  21.41 ? 72   ILE A CA  1 
ATOM   2887 C C   . ILE B 1 72  ? -17.364 -7.989  -11.955 1.00  19.98 ? 72   ILE A C   1 
ATOM   2888 O O   . ILE B 1 72  ? -16.421 -8.667  -12.366 1.00  24.02 ? 72   ILE A O   1 
ATOM   2889 C CB  . ILE B 1 72  ? -18.926 -8.820  -10.124 1.00  23.88 ? 72   ILE A CB  1 
ATOM   2890 C CG1 . ILE B 1 72  ? -19.040 -9.044  -8.609  1.00  25.81 ? 72   ILE A CG1 1 
ATOM   2891 C CG2 . ILE B 1 72  ? -18.838 -10.152 -10.859 1.00  27.10 ? 72   ILE A CG2 1 
ATOM   2892 C CD1 . ILE B 1 72  ? -20.417 -9.584  -8.174  1.00  22.73 ? 72   ILE A CD1 1 
ATOM   2893 N N   . MET B 1 73  ? -18.117 -7.267  -12.771 1.00  22.89 ? 73   MET A N   1 
ATOM   2894 C CA  . MET B 1 73  ? -17.825 -7.186  -14.207 1.00  23.12 ? 73   MET A CA  1 
ATOM   2895 C C   . MET B 1 73  ? -16.472 -6.540  -14.509 1.00  23.91 ? 73   MET A C   1 
ATOM   2896 O O   . MET B 1 73  ? -15.763 -6.938  -15.446 1.00  22.21 ? 73   MET A O   1 
ATOM   2897 C CB  . MET B 1 73  ? -18.937 -6.406  -14.918 1.00  18.31 ? 73   MET A CB  1 
ATOM   2898 C CG  . MET B 1 73  ? -20.250 -7.168  -14.994 1.00  26.96 ? 73   MET A CG  1 
ATOM   2899 S SD  . MET B 1 73  ? -21.529 -6.246  -15.871 1.00  38.70 ? 73   MET A SD  1 
ATOM   2900 C CE  . MET B 1 73  ? -20.769 -6.171  -17.488 1.00  25.55 ? 73   MET A CE  1 
ATOM   2901 N N   . ILE B 1 74  ? -16.123 -5.503  -13.758 1.00  20.32 ? 74   ILE A N   1 
ATOM   2902 C CA  . ILE B 1 74  ? -14.804 -4.899  -13.935 1.00  20.58 ? 74   ILE A CA  1 
ATOM   2903 C C   . ILE B 1 74  ? -13.704 -5.920  -13.652 1.00  24.56 ? 74   ILE A C   1 
ATOM   2904 O O   . ILE B 1 74  ? -12.758 -6.087  -14.439 1.00  25.09 ? 74   ILE A O   1 
ATOM   2905 C CB  . ILE B 1 74  ? -14.634 -3.670  -13.029 1.00  18.16 ? 74   ILE A CB  1 
ATOM   2906 C CG1 . ILE B 1 74  ? -15.547 -2.554  -13.519 1.00  19.94 ? 74   ILE A CG1 1 
ATOM   2907 C CG2 . ILE B 1 74  ? -13.178 -3.196  -13.020 1.00  19.57 ? 74   ILE A CG2 1 
ATOM   2908 C CD1 . ILE B 1 74  ? -15.635 -1.351  -12.606 1.00  22.53 ? 74   ILE A CD1 1 
ATOM   2909 N N   . ASN B 1 75  ? -13.826 -6.605  -12.520 1.00  20.59 ? 75   ASN A N   1 
ATOM   2910 C CA  . ASN B 1 75  ? -12.836 -7.587  -12.118 1.00  23.68 ? 75   ASN A CA  1 
ATOM   2911 C C   . ASN B 1 75  ? -12.702 -8.724  -13.147 1.00  26.56 ? 75   ASN A C   1 
ATOM   2912 O O   . ASN B 1 75  ? -11.584 -9.097  -13.542 1.00  24.03 ? 75   ASN A O   1 
ATOM   2913 C CB  . ASN B 1 75  ? -13.185 -8.132  -10.728 1.00  23.41 ? 75   ASN A CB  1 
ATOM   2914 C CG  . ASN B 1 75  ? -12.139 -9.089  -10.196 1.00  28.11 ? 75   ASN A CG  1 
ATOM   2915 O OD1 . ASN B 1 75  ? -12.427 -10.254 -9.942  1.00  30.77 ? 75   ASN A OD1 1 
ATOM   2916 N ND2 . ASN B 1 75  ? -10.909 -8.607  -10.060 1.00  33.50 ? 75   ASN A ND2 1 
ATOM   2917 N N   . ALA B 1 76  ? -13.843 -9.264  -13.575 1.00  25.26 ? 76   ALA A N   1 
ATOM   2918 C CA  . ALA B 1 76  ? -13.861 -10.339 -14.564 1.00  25.41 ? 76   ALA A CA  1 
ATOM   2919 C C   . ALA B 1 76  ? -13.103 -9.929  -15.827 1.00  25.13 ? 76   ALA A C   1 
ATOM   2920 O O   . ALA B 1 76  ? -12.306 -10.700 -16.342 1.00  25.91 ? 76   ALA A O   1 
ATOM   2921 C CB  . ALA B 1 76  ? -15.300 -10.745 -14.905 1.00  28.32 ? 76   ALA A CB  1 
ATOM   2922 N N   . CYS B 1 77  ? -13.346 -8.715  -16.316 1.00  21.35 ? 77   CYS A N   1 
ATOM   2923 C CA  . CYS B 1 77  ? -12.637 -8.214  -17.501 1.00  26.08 ? 77   CYS A CA  1 
ATOM   2924 C C   . CYS B 1 77  ? -11.143 -7.995  -17.250 1.00  27.70 ? 77   CYS A C   1 
ATOM   2925 O O   . CYS B 1 77  ? -10.322 -8.203  -18.140 1.00  25.68 ? 77   CYS A O   1 
ATOM   2926 C CB  . CYS B 1 77  ? -13.280 -6.927  -18.018 1.00  22.78 ? 77   CYS A CB  1 
ATOM   2927 S SG  . CYS B 1 77  ? -14.960 -7.197  -18.684 1.00  27.69 ? 77   CYS A SG  1 
ATOM   2928 N N   . LYS B 1 78  ? -10.787 -7.584  -16.037 1.00  23.88 ? 78   LYS A N   1 
ATOM   2929 C CA  . LYS B 1 78  ? -9.386  -7.331  -15.723 1.00  24.93 ? 78   LYS A CA  1 
ATOM   2930 C C   . LYS B 1 78  ? -8.621  -8.646  -15.703 1.00  24.38 ? 78   LYS A C   1 
ATOM   2931 O O   . LYS B 1 78  ? -7.556  -8.773  -16.308 1.00  28.63 ? 78   LYS A O   1 
ATOM   2932 C CB  . LYS B 1 78  ? -9.248  -6.578  -14.390 1.00  28.06 ? 78   LYS A CB  1 
ATOM   2933 C CG  . LYS B 1 78  ? -7.945  -5.786  -14.230 1.00  36.45 ? 78   LYS A CG  1 
ATOM   2934 C CD  . LYS B 1 78  ? -7.896  -4.614  -15.220 1.00  38.56 ? 78   LYS A CD  1 
ATOM   2935 C CE  . LYS B 1 78  ? -6.593  -3.823  -15.117 1.00  36.64 ? 78   LYS A CE  1 
ATOM   2936 N NZ  . LYS B 1 78  ? -6.656  -2.712  -14.119 1.00  41.42 ? 78   LYS A NZ  1 
ATOM   2937 N N   . ILE B 1 79  ? -9.182  -9.659  -15.054 1.00  23.53 ? 79   ILE A N   1 
ATOM   2938 C CA  . ILE B 1 79  ? -8.456  -10.914 -14.936 1.00  27.08 ? 79   ILE A CA  1 
ATOM   2939 C C   . ILE B 1 79  ? -8.560  -11.755 -16.205 1.00  28.81 ? 79   ILE A C   1 
ATOM   2940 O O   . ILE B 1 79  ? -7.893  -12.780 -16.325 1.00  28.72 ? 79   ILE A O   1 
ATOM   2941 C CB  . ILE B 1 79  ? -8.889  -11.731 -13.710 1.00  31.08 ? 79   ILE A CB  1 
ATOM   2942 C CG1 . ILE B 1 79  ? -10.316 -12.244 -13.883 1.00  31.27 ? 79   ILE A CG1 1 
ATOM   2943 C CG2 . ILE B 1 79  ? -8.772  -10.889 -12.454 1.00  26.21 ? 79   ILE A CG2 1 
ATOM   2944 C CD1 . ILE B 1 79  ? -10.756 -13.172 -12.765 1.00  39.21 ? 79   ILE A CD1 1 
ATOM   2945 N N   . ALA B 1 80  ? -9.396  -11.316 -17.143 1.00  26.19 ? 80   ALA A N   1 
ATOM   2946 C CA  . ALA B 1 80  ? -9.480  -11.948 -18.471 1.00  27.91 ? 80   ALA A CA  1 
ATOM   2947 C C   . ALA B 1 80  ? -8.624  -11.173 -19.476 1.00  25.79 ? 80   ALA A C   1 
ATOM   2948 O O   . ALA B 1 80  ? -8.794  -11.288 -20.699 1.00  28.81 ? 80   ALA A O   1 
ATOM   2949 C CB  . ALA B 1 80  ? -10.933 -12.024 -18.936 1.00  27.25 ? 80   ALA A CB  1 
ATOM   2950 N N   . SER B 1 81  ? -7.731  -10.347 -18.941 1.00  23.30 ? 81   SER A N   1 
ATOM   2951 C CA  . SER B 1 81  ? -6.686  -9.672  -19.702 1.00  24.14 ? 81   SER A CA  1 
ATOM   2952 C C   . SER B 1 81  ? -7.149  -8.599  -20.675 1.00  28.70 ? 81   SER A C   1 
ATOM   2953 O O   . SER B 1 81  ? -6.493  -8.356  -21.681 1.00  26.85 ? 81   SER A O   1 
ATOM   2954 C CB  . SER B 1 81  ? -5.789  -10.685 -20.419 1.00  30.64 ? 81   SER A CB  1 
ATOM   2955 O OG  . SER B 1 81  ? -5.154  -11.546 -19.492 1.00  29.33 ? 81   SER A OG  1 
ATOM   2956 N N   . ALA B 1 82  ? -8.260  -7.931  -20.378 1.00  26.95 ? 82   ALA A N   1 
ATOM   2957 C CA  . ALA B 1 82  ? -8.616  -6.745  -21.148 1.00  28.03 ? 82   ALA A CA  1 
ATOM   2958 C C   . ALA B 1 82  ? -7.424  -5.792  -21.162 1.00  28.05 ? 82   ALA A C   1 
ATOM   2959 O O   . ALA B 1 82  ? -6.665  -5.734  -20.202 1.00  27.55 ? 82   ALA A O   1 
ATOM   2960 C CB  . ALA B 1 82  ? -9.832  -6.061  -20.536 1.00  26.37 ? 82   ALA A CB  1 
ATOM   2961 N N   . SER B 1 83  ? -7.266  -5.041  -22.244 1.00  30.41 ? 83   SER A N   1 
ATOM   2962 C CA  . SER B 1 83  ? -6.192  -4.061  -22.337 1.00  31.80 ? 83   SER A CA  1 
ATOM   2963 C C   . SER B 1 83  ? -6.479  -2.849  -21.434 1.00  34.17 ? 83   SER A C   1 
ATOM   2964 O O   . SER B 1 83  ? -5.579  -2.298  -20.803 1.00  29.40 ? 83   SER A O   1 
ATOM   2965 C CB  . SER B 1 83  ? -6.020  -3.622  -23.782 1.00  31.78 ? 83   SER A CB  1 
ATOM   2966 O OG  . SER B 1 83  ? -5.347  -2.382  -23.843 1.00  46.00 ? 83   SER A OG  1 
ATOM   2967 N N   . ARG B 1 84  ? -7.740  -2.440  -21.371 1.00  28.10 ? 84   ARG A N   1 
ATOM   2968 C CA  . ARG B 1 84  ? -8.136  -1.354  -20.480 1.00  26.48 ? 84   ARG A CA  1 
ATOM   2969 C C   . ARG B 1 84  ? -9.595  -1.543  -20.106 1.00  26.80 ? 84   ARG A C   1 
ATOM   2970 O O   . ARG B 1 84  ? -10.372 -2.078  -20.907 1.00  26.79 ? 84   ARG A O   1 
ATOM   2971 C CB  . ARG B 1 84  ? -7.907  0.006   -21.152 1.00  30.32 ? 84   ARG A CB  1 
ATOM   2972 C CG  . ARG B 1 84  ? -8.332  1.219   -20.317 1.00  30.82 ? 84   ARG A CG  1 
ATOM   2973 C CD  . ARG B 1 84  ? -7.794  2.530   -20.932 1.00  34.99 ? 84   ARG A CD  1 
ATOM   2974 N NE  . ARG B 1 84  ? -8.393  2.806   -22.238 1.00  40.07 ? 84   ARG A NE  1 
ATOM   2975 C CZ  . ARG B 1 84  ? -7.985  3.762   -23.070 1.00  44.07 ? 84   ARG A CZ  1 
ATOM   2976 N NH1 . ARG B 1 84  ? -6.955  4.540   -22.749 1.00  43.52 ? 84   ARG A NH1 1 
ATOM   2977 N NH2 . ARG B 1 84  ? -8.602  3.933   -24.230 1.00  36.80 ? 84   ARG A NH2 1 
ATOM   2978 N N   . VAL B 1 85  ? -9.956  -1.138  -18.887 1.00  23.30 ? 85   VAL A N   1 
ATOM   2979 C CA  . VAL B 1 85  ? -11.351 -1.166  -18.448 1.00  22.37 ? 85   VAL A CA  1 
ATOM   2980 C C   . VAL B 1 85  ? -11.815 0.200   -17.943 1.00  21.65 ? 85   VAL A C   1 
ATOM   2981 O O   . VAL B 1 85  ? -11.236 0.755   -17.028 1.00  21.72 ? 85   VAL A O   1 
ATOM   2982 C CB  . VAL B 1 85  ? -11.587 -2.190  -17.326 1.00  21.20 ? 85   VAL A CB  1 
ATOM   2983 C CG1 . VAL B 1 85  ? -13.085 -2.194  -16.919 1.00  23.57 ? 85   VAL A CG1 1 
ATOM   2984 C CG2 . VAL B 1 85  ? -11.131 -3.588  -17.749 1.00  21.77 ? 85   VAL A CG2 1 
ATOM   2985 N N   . THR B 1 86  ? -12.863 0.733   -18.549 1.00  19.38 ? 86   THR A N   1 
ATOM   2986 C CA  . THR B 1 86  ? -13.432 2.008   -18.143 1.00  20.53 ? 86   THR A CA  1 
ATOM   2987 C C   . THR B 1 86  ? -14.806 1.774   -17.559 1.00  24.78 ? 86   THR A C   1 
ATOM   2988 O O   . THR B 1 86  ? -15.614 1.039   -18.146 1.00  23.70 ? 86   THR A O   1 
ATOM   2989 C CB  . THR B 1 86  ? -13.593 2.952   -19.349 1.00  20.60 ? 86   THR A CB  1 
ATOM   2990 O OG1 . THR B 1 86  ? -12.299 3.302   -19.834 1.00  23.60 ? 86   THR A OG1 1 
ATOM   2991 C CG2 . THR B 1 86  ? -14.334 4.233   -18.952 1.00  21.38 ? 86   THR A CG2 1 
ATOM   2992 N N   . ALA B 1 87  ? -15.079 2.401   -16.412 1.00  21.24 ? 87   ALA A N   1 
ATOM   2993 C CA  . ALA B 1 87  ? -16.441 2.425   -15.870 1.00  21.20 ? 87   ALA A CA  1 
ATOM   2994 C C   . ALA B 1 87  ? -17.206 3.643   -16.363 1.00  19.48 ? 87   ALA A C   1 
ATOM   2995 O O   . ALA B 1 87  ? -16.812 4.783   -16.130 1.00  20.28 ? 87   ALA A O   1 
ATOM   2996 C CB  . ALA B 1 87  ? -16.425 2.378   -14.340 1.00  21.32 ? 87   ALA A CB  1 
ATOM   2997 N N   . VAL B 1 88  ? -18.293 3.389   -17.077 1.00  21.29 ? 88   VAL A N   1 
ATOM   2998 C CA  . VAL B 1 88  ? -19.158 4.450   -17.543 1.00  20.58 ? 88   VAL A CA  1 
ATOM   2999 C C   . VAL B 1 88  ? -20.323 4.488   -16.577 1.00  21.63 ? 88   VAL A C   1 
ATOM   3000 O O   . VAL B 1 88  ? -21.170 3.611   -16.591 1.00  21.01 ? 88   VAL A O   1 
ATOM   3001 C CB  . VAL B 1 88  ? -19.654 4.186   -18.979 1.00  19.66 ? 88   VAL A CB  1 
ATOM   3002 C CG1 . VAL B 1 88  ? -20.624 5.260   -19.407 1.00  18.92 ? 88   VAL A CG1 1 
ATOM   3003 C CG2 . VAL B 1 88  ? -18.449 4.096   -19.935 1.00  23.73 ? 88   VAL A CG2 1 
ATOM   3004 N N   . ILE B 1 89  ? -20.343 5.495   -15.716 1.00  21.42 ? 89   ILE A N   1 
ATOM   3005 C CA  . ILE B 1 89  ? -21.322 5.551   -14.629 1.00  22.98 ? 89   ILE A CA  1 
ATOM   3006 C C   . ILE B 1 89  ? -22.038 6.895   -14.655 1.00  23.96 ? 89   ILE A C   1 
ATOM   3007 O O   . ILE B 1 89  ? -21.619 7.833   -13.989 1.00  22.16 ? 89   ILE A O   1 
ATOM   3008 C CB  . ILE B 1 89  ? -20.604 5.439   -13.253 1.00  28.01 ? 89   ILE A CB  1 
ATOM   3009 C CG1 . ILE B 1 89  ? -19.690 4.224   -13.192 1.00  24.44 ? 89   ILE A CG1 1 
ATOM   3010 C CG2 . ILE B 1 89  ? -21.599 5.383   -12.098 1.00  25.19 ? 89   ILE A CG2 1 
ATOM   3011 C CD1 . ILE B 1 89  ? -18.688 4.321   -12.012 1.00  26.00 ? 89   ILE A CD1 1 
ATOM   3012 N N   . PRO B 1 90  ? -23.122 7.003   -15.427 1.00  29.70 ? 90   PRO A N   1 
ATOM   3013 C CA  . PRO B 1 90  ? -23.781 8.309   -15.597 1.00  31.05 ? 90   PRO A CA  1 
ATOM   3014 C C   . PRO B 1 90  ? -24.174 8.960   -14.258 1.00  28.11 ? 90   PRO A C   1 
ATOM   3015 O O   . PRO B 1 90  ? -24.006 10.164  -14.062 1.00  27.52 ? 90   PRO A O   1 
ATOM   3016 C CB  . PRO B 1 90  ? -25.023 7.957   -16.418 1.00  32.87 ? 90   PRO A CB  1 
ATOM   3017 C CG  . PRO B 1 90  ? -24.603 6.718   -17.183 1.00  32.75 ? 90   PRO A CG  1 
ATOM   3018 C CD  . PRO B 1 90  ? -23.784 5.940   -16.200 1.00  33.51 ? 90   PRO A CD  1 
ATOM   3019 N N   . CYS B 1 91  ? -24.699 8.169   -13.332 1.00  28.63 ? 91   CYS A N   1 
ATOM   3020 C CA  . CYS B 1 91  ? -25.035 8.713   -12.020 1.00  26.75 ? 91   CYS A CA  1 
ATOM   3021 C C   . CYS B 1 91  ? -24.217 7.981   -10.954 1.00  27.72 ? 91   CYS A C   1 
ATOM   3022 O O   . CYS B 1 91  ? -24.456 6.820   -10.684 1.00  26.23 ? 91   CYS A O   1 
ATOM   3023 C CB  . CYS B 1 91  ? -26.539 8.607   -11.744 1.00  30.37 ? 91   CYS A CB  1 
ATOM   3024 S SG  . CYS B 1 91  ? -27.025 9.239   -10.109 1.00  37.35 ? 91   CYS A SG  1 
ATOM   3025 N N   . PHE B 1 92  ? -23.242 8.671   -10.376 1.00  27.71 ? 92   PHE A N   1 
ATOM   3026 C CA  . PHE B 1 92  ? -22.236 8.042   -9.521  1.00  22.91 ? 92   PHE A CA  1 
ATOM   3027 C C   . PHE B 1 92  ? -22.841 7.658   -8.153  1.00  27.22 ? 92   PHE A C   1 
ATOM   3028 O O   . PHE B 1 92  ? -23.448 8.484   -7.482  1.00  24.22 ? 92   PHE A O   1 
ATOM   3029 C CB  . PHE B 1 92  ? -21.040 8.994   -9.366  1.00  23.24 ? 92   PHE A CB  1 
ATOM   3030 C CG  . PHE B 1 92  ? -19.835 8.368   -8.718  1.00  23.99 ? 92   PHE A CG  1 
ATOM   3031 C CD1 . PHE B 1 92  ? -18.818 7.831   -9.478  1.00  22.90 ? 92   PHE A CD1 1 
ATOM   3032 C CD2 . PHE B 1 92  ? -19.723 8.329   -7.333  1.00  26.54 ? 92   PHE A CD2 1 
ATOM   3033 C CE1 . PHE B 1 92  ? -17.709 7.256   -8.869  1.00  25.29 ? 92   PHE A CE1 1 
ATOM   3034 C CE2 . PHE B 1 92  ? -18.618 7.775   -6.722  1.00  23.19 ? 92   PHE A CE2 1 
ATOM   3035 C CZ  . PHE B 1 92  ? -17.615 7.238   -7.479  1.00  21.90 ? 92   PHE A CZ  1 
ATOM   3036 N N   . PRO B 1 93  ? -22.698 6.385   -7.762  1.00  26.05 ? 93   PRO A N   1 
ATOM   3037 C CA  . PRO B 1 93  ? -23.340 5.854   -6.553  1.00  28.32 ? 93   PRO A CA  1 
ATOM   3038 C C   . PRO B 1 93  ? -22.723 6.430   -5.288  1.00  26.57 ? 93   PRO A C   1 
ATOM   3039 O O   . PRO B 1 93  ? -21.503 6.552   -5.238  1.00  26.84 ? 93   PRO A O   1 
ATOM   3040 C CB  . PRO B 1 93  ? -23.089 4.342   -6.653  1.00  29.47 ? 93   PRO A CB  1 
ATOM   3041 C CG  . PRO B 1 93  ? -21.936 4.194   -7.596  1.00  31.88 ? 93   PRO A CG  1 
ATOM   3042 C CD  . PRO B 1 93  ? -21.983 5.351   -8.535  1.00  28.42 ? 93   PRO A CD  1 
ATOM   3043 N N   . TYR B 1 94  ? -23.558 6.794   -4.313  1.00  26.80 ? 94   TYR A N   1 
ATOM   3044 C CA  . TYR B 1 94  ? -23.127 7.365   -3.038  1.00  26.73 ? 94   TYR A CA  1 
ATOM   3045 C C   . TYR B 1 94  ? -22.462 8.727   -3.179  1.00  25.37 ? 94   TYR A C   1 
ATOM   3046 O O   . TYR B 1 94  ? -21.733 9.148   -2.294  1.00  28.33 ? 94   TYR A O   1 
ATOM   3047 C CB  . TYR B 1 94  ? -22.207 6.399   -2.261  1.00  25.14 ? 94   TYR A CB  1 
ATOM   3048 C CG  . TYR B 1 94  ? -22.959 5.207   -1.724  1.00  25.61 ? 94   TYR A CG  1 
ATOM   3049 C CD1 . TYR B 1 94  ? -23.177 4.097   -2.521  1.00  25.03 ? 94   TYR A CD1 1 
ATOM   3050 C CD2 . TYR B 1 94  ? -23.483 5.208   -0.430  1.00  27.92 ? 94   TYR A CD2 1 
ATOM   3051 C CE1 . TYR B 1 94  ? -23.873 3.009   -2.056  1.00  25.68 ? 94   TYR A CE1 1 
ATOM   3052 C CE2 . TYR B 1 94  ? -24.191 4.113   0.051   1.00  26.49 ? 94   TYR A CE2 1 
ATOM   3053 C CZ  . TYR B 1 94  ? -24.378 3.018   -0.779  1.00  27.67 ? 94   TYR A CZ  1 
ATOM   3054 O OH  . TYR B 1 94  ? -25.069 1.925   -0.352  1.00  26.68 ? 94   TYR A OH  1 
ATOM   3055 N N   . ALA B 1 95  ? -22.718 9.421   -4.282  1.00  27.39 ? 95   ALA A N   1 
ATOM   3056 C CA  . ALA B 1 95  ? -22.115 10.740  -4.496  1.00  31.18 ? 95   ALA A CA  1 
ATOM   3057 C C   . ALA B 1 95  ? -22.429 11.735  -3.383  1.00  25.85 ? 95   ALA A C   1 
ATOM   3058 O O   . ALA B 1 95  ? -21.580 12.547  -3.046  1.00  29.95 ? 95   ALA A O   1 
ATOM   3059 C CB  . ALA B 1 95  ? -22.511 11.341  -5.873  1.00  21.34 ? 95   ALA A CB  1 
ATOM   3060 N N   . ARG B 1 96  ? -23.632 11.700  -2.825  0.20  24.84 ? 96   ARG A N   1 
ATOM   3061 C CA  . ARG B 1 96  ? -23.968 12.656  -1.771  0.20  28.35 ? 96   ARG A CA  1 
ATOM   3062 C C   . ARG B 1 96  ? -23.183 12.409  -0.482  0.20  27.20 ? 96   ARG A C   1 
ATOM   3063 O O   . ARG B 1 96  ? -23.081 13.291  0.368   0.20  23.73 ? 96   ARG A O   1 
ATOM   3064 C CB  . ARG B 1 96  ? -25.469 12.670  -1.486  0.20  29.14 ? 96   ARG A CB  1 
ATOM   3065 C CG  . ARG B 1 96  ? -26.292 13.231  -2.623  0.20  32.22 ? 96   ARG A CG  1 
ATOM   3066 C CD  . ARG B 1 96  ? -27.256 12.188  -3.141  0.20  33.82 ? 96   ARG A CD  1 
ATOM   3067 N NE  . ARG B 1 96  ? -28.594 12.354  -2.588  0.20  38.35 ? 96   ARG A NE  1 
ATOM   3068 C CZ  . ARG B 1 96  ? -29.441 11.352  -2.381  0.20  39.11 ? 96   ARG A CZ  1 
ATOM   3069 N NH1 . ARG B 1 96  ? -29.079 10.110  -2.669  0.20  36.58 ? 96   ARG A NH1 1 
ATOM   3070 N NH2 . ARG B 1 96  ? -30.645 11.591  -1.877  0.20  40.35 ? 96   ARG A NH2 1 
ATOM   3071 N N   . GLN B 1 97  ? -22.634 11.207  -0.346  0.81  27.70 ? 97   GLN A N   1 
ATOM   3072 C CA  . GLN B 1 97  ? -21.834 10.855  0.826   0.81  29.07 ? 97   GLN A CA  1 
ATOM   3073 C C   . GLN B 1 97  ? -20.348 11.151  0.583   0.81  26.79 ? 97   GLN A C   1 
ATOM   3074 O O   . GLN B 1 97  ? -19.512 10.246  0.572   0.81  25.17 ? 97   GLN A O   1 
ATOM   3075 C CB  . GLN B 1 97  ? -22.091 9.386   1.216   0.81  25.69 ? 97   GLN A CB  1 
ATOM   3076 C CG  . GLN B 1 97  ? -23.578 9.137   1.555   0.81  30.69 ? 97   GLN A CG  1 
ATOM   3077 C CD  . GLN B 1 97  ? -23.881 7.762   2.138   0.81  36.85 ? 97   GLN A CD  1 
ATOM   3078 O OE1 . GLN B 1 97  ? -23.061 7.164   2.846   0.81  33.27 ? 97   GLN A OE1 1 
ATOM   3079 N NE2 . GLN B 1 97  ? -25.082 7.256   1.846   0.81  33.81 ? 97   GLN A NE2 1 
ATOM   3080 N N   . ASP B 1 98  ? -20.029 12.437  0.418   1.00  29.81 ? 98   ASP A N   1 
ATOM   3081 C CA  . ASP B 1 98  ? -18.710 12.858  -0.059  1.00  28.73 ? 98   ASP A CA  1 
ATOM   3082 C C   . ASP B 1 98  ? -17.934 13.684  0.966   1.00  33.50 ? 98   ASP A C   1 
ATOM   3083 O O   . ASP B 1 98  ? -16.874 14.222  0.656   1.00  33.20 ? 98   ASP A O   1 
ATOM   3084 C CB  . ASP B 1 98  ? -18.847 13.648  -1.359  1.00  29.70 ? 98   ASP A CB  1 
ATOM   3085 C CG  . ASP B 1 98  ? -19.560 14.985  -1.162  1.00  35.59 ? 98   ASP A CG  1 
ATOM   3086 O OD1 . ASP B 1 98  ? -20.302 15.140  -0.170  1.00  40.31 ? 98   ASP A OD1 1 
ATOM   3087 O OD2 . ASP B 1 98  ? -19.384 15.882  -2.005  1.00  35.66 ? 98   ASP A OD2 1 
ATOM   3088 N N   . LYS B 1 99  ? -18.474 13.784  2.180   1.00  34.57 ? 99   LYS A N   1 
ATOM   3089 C CA  . LYS B 1 99  ? -17.804 14.475  3.281   1.00  35.08 ? 99   LYS A CA  1 
ATOM   3090 C C   . LYS B 1 99  ? -18.461 14.062  4.597   1.00  36.98 ? 99   LYS A C   1 
ATOM   3091 O O   . LYS B 1 99  ? -19.567 13.523  4.588   1.00  37.20 ? 99   LYS A O   1 
ATOM   3092 C CB  . LYS B 1 99  ? -17.901 15.987  3.097   1.00  29.62 ? 99   LYS A CB  1 
ATOM   3093 C CG  . LYS B 1 99  ? -19.314 16.509  3.215   1.00  36.71 ? 99   LYS A CG  1 
ATOM   3094 C CD  . LYS B 1 99  ? -19.451 17.886  2.600   1.00  43.65 ? 99   LYS A CD  1 
ATOM   3095 C CE  . LYS B 1 99  ? -20.772 18.500  2.984   1.00  47.39 ? 99   LYS A CE  1 
ATOM   3096 N NZ  . LYS B 1 99  ? -21.893 17.515  2.882   1.00  50.70 ? 99   LYS A NZ  1 
ATOM   3097 N N   . LYS B 1 100 ? -17.798 14.320  5.723   0.87  35.55 ? 100  LYS A N   1 
ATOM   3098 C CA  . LYS B 1 100 ? -18.331 13.902  7.027   0.87  40.66 ? 100  LYS A CA  1 
ATOM   3099 C C   . LYS B 1 100 ? -19.469 14.777  7.549   0.87  42.86 ? 100  LYS A C   1 
ATOM   3100 O O   . LYS B 1 100 ? -20.324 14.304  8.309   0.87  37.74 ? 100  LYS A O   1 
ATOM   3101 C CB  . LYS B 1 100 ? -17.230 13.852  8.089   0.87  39.83 ? 100  LYS A CB  1 
ATOM   3102 C CG  . LYS B 1 100 ? -16.232 12.726  7.933   0.87  35.49 ? 100  LYS A CG  1 
ATOM   3103 C CD  . LYS B 1 100 ? -15.289 12.731  9.110   0.87  31.52 ? 100  LYS A CD  1 
ATOM   3104 C CE  . LYS B 1 100 ? -14.089 11.852  8.862   0.87  32.01 ? 100  LYS A CE  1 
ATOM   3105 N NZ  . LYS B 1 100 ? -12.991 12.191  9.819   0.87  31.89 ? 100  LYS A NZ  1 
ATOM   3106 N N   . ASP B 1 101 ? -19.458 16.051  7.171   0.10  38.74 ? 101  ASP A N   1 
ATOM   3107 C CA  . ASP B 1 101 ? -20.513 16.984  7.557   0.10  39.87 ? 101  ASP A CA  1 
ATOM   3108 C C   . ASP B 1 101 ? -20.670 17.097  9.076   0.10  40.23 ? 101  ASP A C   1 
ATOM   3109 O O   . ASP B 1 101 ? -21.788 17.122  9.592   0.10  39.89 ? 101  ASP A O   1 
ATOM   3110 C CB  . ASP B 1 101 ? -21.842 16.580  6.912   0.10  39.86 ? 101  ASP A CB  1 
ATOM   3111 C CG  . ASP B 1 101 ? -22.874 17.689  6.956   0.10  39.34 ? 101  ASP A CG  1 
ATOM   3112 O OD1 . ASP B 1 101 ? -22.485 18.869  6.850   0.10  39.00 ? 101  ASP A OD1 1 
ATOM   3113 O OD2 . ASP B 1 101 ? -24.074 17.381  7.094   0.10  38.39 ? 101  ASP A OD2 1 
ATOM   3114 N N   . LYS B 1 102 ? -19.542 17.165  9.780   0.10  40.03 ? 102  LYS A N   1 
ATOM   3115 C CA  . LYS B 1 102 ? -19.519 17.339  11.235  0.10  41.10 ? 102  LYS A CA  1 
ATOM   3116 C C   . LYS B 1 102 ? -19.944 16.101  12.024  0.10  40.15 ? 102  LYS A C   1 
ATOM   3117 O O   . LYS B 1 102 ? -19.970 16.122  13.254  0.10  39.39 ? 102  LYS A O   1 
ATOM   3118 C CB  . LYS B 1 102 ? -20.359 18.545  11.666  0.10  41.15 ? 102  LYS A CB  1 
ATOM   3119 C CG  . LYS B 1 102 ? -19.552 19.811  11.896  0.10  42.09 ? 102  LYS A CG  1 
ATOM   3120 C CD  . LYS B 1 102 ? -19.952 20.517  13.187  0.10  43.29 ? 102  LYS A CD  1 
ATOM   3121 C CE  . LYS B 1 102 ? -21.327 21.158  13.084  0.10  43.55 ? 102  LYS A CE  1 
ATOM   3122 N NZ  . LYS B 1 102 ? -21.705 21.859  14.347  0.10  44.51 ? 102  LYS A NZ  1 
ATOM   3123 N N   . SER B 1 103 ? -20.270 15.027  11.314  1.00  39.22 ? 103  SER A N   1 
ATOM   3124 C CA  . SER B 1 103 ? -20.713 13.785  11.944  1.00  42.34 ? 103  SER A CA  1 
ATOM   3125 C C   . SER B 1 103 ? -19.652 12.688  11.894  1.00  39.29 ? 103  SER A C   1 
ATOM   3126 O O   . SER B 1 103 ? -18.656 12.800  11.178  1.00  38.26 ? 103  SER A O   1 
ATOM   3127 C CB  . SER B 1 103 ? -21.995 13.281  11.277  1.00  42.32 ? 103  SER A CB  1 
ATOM   3128 O OG  . SER B 1 103 ? -23.110 14.059  11.676  1.00  52.89 ? 103  SER A OG  1 
ATOM   3129 N N   . ARG B 1 104 ? -19.869 11.631  12.670  1.00  32.14 ? 104  ARG A N   1 
ATOM   3130 C CA  . ARG B 1 104 ? -19.018 10.450  12.594  1.00  39.87 ? 104  ARG A CA  1 
ATOM   3131 C C   . ARG B 1 104 ? -19.549 9.581   11.464  1.00  39.39 ? 104  ARG A C   1 
ATOM   3132 O O   . ARG B 1 104 ? -20.031 8.472   11.680  1.00  40.14 ? 104  ARG A O   1 
ATOM   3133 C CB  . ARG B 1 104 ? -18.989 9.694   13.928  1.00  41.20 ? 104  ARG A CB  1 
ATOM   3134 C CG  . ARG B 1 104 ? -17.803 10.072  14.815  1.00  44.17 ? 104  ARG A CG  1 
ATOM   3135 C CD  . ARG B 1 104 ? -17.855 9.424   16.206  1.00  38.37 ? 104  ARG A CD  1 
ATOM   3136 N NE  . ARG B 1 104 ? -19.087 9.768   16.910  1.00  42.06 ? 104  ARG A NE  1 
ATOM   3137 C CZ  . ARG B 1 104 ? -19.165 10.588  17.947  1.00  38.46 ? 104  ARG A CZ  1 
ATOM   3138 N NH1 . ARG B 1 104 ? -18.075 11.166  18.436  1.00  39.34 ? 104  ARG A NH1 1 
ATOM   3139 N NH2 . ARG B 1 104 ? -20.345 10.822  18.507  1.00  48.78 ? 104  ARG A NH2 1 
ATOM   3140 N N   . ALA B 1 105 ? -19.472 10.122  10.251  1.00  34.28 ? 105  ALA A N   1 
ATOM   3141 C CA  . ALA B 1 105 ? -20.073 9.497   9.083   1.00  35.99 ? 105  ALA A CA  1 
ATOM   3142 C C   . ALA B 1 105 ? -19.028 8.906   8.135   1.00  32.22 ? 105  ALA A C   1 
ATOM   3143 O O   . ALA B 1 105 ? -17.867 9.304   8.137   1.00  32.11 ? 105  ALA A O   1 
ATOM   3144 C CB  . ALA B 1 105 ? -20.951 10.513  8.349   1.00  37.39 ? 105  ALA A CB  1 
ATOM   3145 N N   . PRO B 1 106 ? -19.437 7.938   7.318   1.00  31.13 ? 106  PRO A N   1 
ATOM   3146 C CA  . PRO B 1 106 ? -18.493 7.468   6.313   1.00  28.74 ? 106  PRO A CA  1 
ATOM   3147 C C   . PRO B 1 106 ? -18.358 8.513   5.202   1.00  27.69 ? 106  PRO A C   1 
ATOM   3148 O O   . PRO B 1 106 ? -19.261 9.328   5.019   1.00  27.07 ? 106  PRO A O   1 
ATOM   3149 C CB  . PRO B 1 106 ? -19.193 6.223   5.763   1.00  29.00 ? 106  PRO A CB  1 
ATOM   3150 C CG  . PRO B 1 106 ? -20.643 6.544   5.891   1.00  32.08 ? 106  PRO A CG  1 
ATOM   3151 C CD  . PRO B 1 106 ? -20.771 7.319   7.169   1.00  30.68 ? 106  PRO A CD  1 
ATOM   3152 N N   . ILE B 1 107 ? -17.245 8.498   4.479   1.00  27.92 ? 107  ILE A N   1 
ATOM   3153 C CA  . ILE B 1 107 ? -17.170 9.217   3.207   1.00  24.26 ? 107  ILE A CA  1 
ATOM   3154 C C   . ILE B 1 107 ? -17.361 8.141   2.145   1.00  23.87 ? 107  ILE A C   1 
ATOM   3155 O O   . ILE B 1 107 ? -16.400 7.666   1.549   1.00  26.34 ? 107  ILE A O   1 
ATOM   3156 C CB  . ILE B 1 107 ? -15.813 9.879   3.027   1.00  29.28 ? 107  ILE A CB  1 
ATOM   3157 C CG1 . ILE B 1 107 ? -15.473 10.718  4.261   1.00  27.61 ? 107  ILE A CG1 1 
ATOM   3158 C CG2 . ILE B 1 107 ? -15.775 10.687  1.720   1.00  28.80 ? 107  ILE A CG2 1 
ATOM   3159 C CD1 . ILE B 1 107 ? -14.225 11.584  4.116   1.00  30.05 ? 107  ILE A CD1 1 
ATOM   3160 N N   . SER B 1 108 ? -18.607 7.728   1.949   1.00  23.04 ? 108  SER A N   1 
ATOM   3161 C CA  . SER B 1 108 ? -18.901 6.554   1.140   1.00  23.72 ? 108  SER A CA  1 
ATOM   3162 C C   . SER B 1 108 ? -18.553 6.763   -0.337  1.00  19.18 ? 108  SER A C   1 
ATOM   3163 O O   . SER B 1 108 ? -18.267 5.807   -1.045  1.00  24.47 ? 108  SER A O   1 
ATOM   3164 C CB  . SER B 1 108 ? -20.373 6.160   1.295   1.00  28.40 ? 108  SER A CB  1 
ATOM   3165 O OG  . SER B 1 108 ? -20.682 5.870   2.651   1.00  29.06 ? 108  SER A OG  1 
ATOM   3166 N N   . ALA B 1 109 ? -18.557 8.013   -0.800  1.00  24.88 ? 109  ALA A N   1 
ATOM   3167 C CA  . ALA B 1 109 ? -18.147 8.288   -2.177  1.00  22.85 ? 109  ALA A CA  1 
ATOM   3168 C C   . ALA B 1 109 ? -16.681 7.894   -2.390  1.00  20.38 ? 109  ALA A C   1 
ATOM   3169 O O   . ALA B 1 109 ? -16.301 7.396   -3.464  1.00  21.30 ? 109  ALA A O   1 
ATOM   3170 C CB  . ALA B 1 109 ? -18.382 9.762   -2.537  1.00  23.47 ? 109  ALA A CB  1 
ATOM   3171 N N   . LYS B 1 110 ? -15.859 8.099   -1.359  1.00  19.60 ? 110  LYS A N   1 
ATOM   3172 C CA  . LYS B 1 110 ? -14.449 7.751   -1.439  1.00  19.16 ? 110  LYS A CA  1 
ATOM   3173 C C   . LYS B 1 110 ? -14.302 6.240   -1.361  1.00  20.38 ? 110  LYS A C   1 
ATOM   3174 O O   . LYS B 1 110 ? -13.490 5.655   -2.061  1.00  18.24 ? 110  LYS A O   1 
ATOM   3175 C CB  . LYS B 1 110 ? -13.641 8.456   -0.331  1.00  24.21 ? 110  LYS A CB  1 
ATOM   3176 C CG  . LYS B 1 110 ? -12.186 7.991   -0.230  1.00  22.19 ? 110  LYS A CG  1 
ATOM   3177 C CD  . LYS B 1 110 ? -11.451 8.192   -1.583  1.00  21.13 ? 110  LYS A CD  1 
ATOM   3178 C CE  . LYS B 1 110 ? -9.987  7.725   -1.519  1.00  23.17 ? 110  LYS A CE  1 
ATOM   3179 N NZ  . LYS B 1 110 ? -9.201  8.547   -0.556  1.00  29.11 ? 110  LYS A NZ  1 
ATOM   3180 N N   . LEU B 1 111 ? -15.122 5.602   -0.533  1.00  19.11 ? 111  LEU A N   1 
ATOM   3181 C CA  . LEU B 1 111 ? -15.128 4.150   -0.451  1.00  21.66 ? 111  LEU A CA  1 
ATOM   3182 C C   . LEU B 1 111 ? -15.457 3.563   -1.832  1.00  19.52 ? 111  LEU A C   1 
ATOM   3183 O O   . LEU B 1 111 ? -14.801 2.641   -2.295  1.00  18.41 ? 111  LEU A O   1 
ATOM   3184 C CB  . LEU B 1 111 ? -16.184 3.705   0.555   1.00  22.03 ? 111  LEU A CB  1 
ATOM   3185 C CG  . LEU B 1 111 ? -16.172 2.330   1.230   1.00  28.89 ? 111  LEU A CG  1 
ATOM   3186 C CD1 . LEU B 1 111 ? -17.625 1.846   1.423   1.00  23.85 ? 111  LEU A CD1 1 
ATOM   3187 C CD2 . LEU B 1 111 ? -15.320 1.280   0.540   1.00  26.44 ? 111  LEU A CD2 1 
ATOM   3188 N N   . VAL B 1 112 ? -16.471 4.123   -2.478  1.00  15.31 ? 112  VAL A N   1 
ATOM   3189 C CA  . VAL B 1 112 ? -16.904 3.637   -3.772  1.00  18.90 ? 112  VAL A CA  1 
ATOM   3190 C C   . VAL B 1 112 ? -15.768 3.801   -4.771  1.00  18.10 ? 112  VAL A C   1 
ATOM   3191 O O   . VAL B 1 112 ? -15.492 2.895   -5.535  1.00  19.25 ? 112  VAL A O   1 
ATOM   3192 C CB  . VAL B 1 112 ? -18.182 4.335   -4.263  1.00  16.95 ? 112  VAL A CB  1 
ATOM   3193 C CG1 . VAL B 1 112 ? -18.488 3.918   -5.715  1.00  20.83 ? 112  VAL A CG1 1 
ATOM   3194 C CG2 . VAL B 1 112 ? -19.365 3.934   -3.364  1.00  18.18 ? 112  VAL A CG2 1 
ATOM   3195 N N   . ALA B 1 113 ? -15.081 4.940   -4.733  1.00  17.11 ? 113  ALA A N   1 
ATOM   3196 C CA  . ALA B 1 113 ? -13.927 5.163   -5.618  1.00  21.71 ? 113  ALA A CA  1 
ATOM   3197 C C   . ALA B 1 113 ? -12.790 4.157   -5.388  1.00  18.61 ? 113  ALA A C   1 
ATOM   3198 O O   . ALA B 1 113 ? -12.190 3.651   -6.353  1.00  19.00 ? 113  ALA A O   1 
ATOM   3199 C CB  . ALA B 1 113 ? -13.420 6.606   -5.490  1.00  15.99 ? 113  ALA A CB  1 
ATOM   3200 N N   . ASN B 1 114 ? -12.472 3.876   -4.123  1.00  21.13 ? 114  ASN A N   1 
ATOM   3201 C CA  . ASN B 1 114 ? -11.471 2.858   -3.822  1.00  19.26 ? 114  ASN A CA  1 
ATOM   3202 C C   . ASN B 1 114 ? -11.882 1.471   -4.282  1.00  17.76 ? 114  ASN A C   1 
ATOM   3203 O O   . ASN B 1 114 ? -11.059 0.684   -4.733  1.00  20.98 ? 114  ASN A O   1 
ATOM   3204 C CB  . ASN B 1 114 ? -11.160 2.807   -2.324  1.00  20.62 ? 114  ASN A CB  1 
ATOM   3205 C CG  . ASN B 1 114 ? -10.346 3.995   -1.856  1.00  25.41 ? 114  ASN A CG  1 
ATOM   3206 O OD1 . ASN B 1 114 ? -9.714  4.703   -2.647  1.00  24.01 ? 114  ASN A OD1 1 
ATOM   3207 N ND2 . ASN B 1 114 ? -10.327 4.193   -0.559  1.00  22.70 ? 114  ASN A ND2 1 
ATOM   3208 N N   . MET B 1 115 ? -13.152 1.143   -4.133  1.00  19.64 ? 115  MET A N   1 
ATOM   3209 C CA  . MET B 1 115 ? -13.613 -0.154  -4.609  1.00  21.36 ? 115  MET A CA  1 
ATOM   3210 C C   . MET B 1 115 ? -13.521 -0.305  -6.120  1.00  18.52 ? 115  MET A C   1 
ATOM   3211 O O   . MET B 1 115 ? -13.064 -1.332  -6.622  1.00  19.02 ? 115  MET A O   1 
ATOM   3212 C CB  . MET B 1 115 ? -15.019 -0.414  -4.128  1.00  18.24 ? 115  MET A CB  1 
ATOM   3213 C CG  . MET B 1 115 ? -15.023 -0.704  -2.622  1.00  25.70 ? 115  MET A CG  1 
ATOM   3214 S SD  . MET B 1 115 ? -16.635 -1.229  -2.147  1.00  37.67 ? 115  MET A SD  1 
ATOM   3215 C CE  . MET B 1 115 ? -17.465 0.312   -2.132  1.00  20.86 ? 115  MET A CE  1 
ATOM   3216 N N   . LEU B 1 116 ? -13.959 0.716   -6.851  1.00  18.97 ? 116  LEU A N   1 
ATOM   3217 C CA  . LEU B 1 116 ? -13.830 0.684   -8.302  1.00  19.54 ? 116  LEU A CA  1 
ATOM   3218 C C   . LEU B 1 116 ? -12.368 0.516   -8.699  1.00  19.59 ? 116  LEU A C   1 
ATOM   3219 O O   . LEU B 1 116 ? -12.057 -0.221  -9.637  1.00  22.75 ? 116  LEU A O   1 
ATOM   3220 C CB  . LEU B 1 116 ? -14.410 1.955   -8.925  1.00  20.33 ? 116  LEU A CB  1 
ATOM   3221 C CG  . LEU B 1 116 ? -15.941 2.022   -8.913  1.00  19.37 ? 116  LEU A CG  1 
ATOM   3222 C CD1 . LEU B 1 116 ? -16.431 3.457   -8.932  1.00  17.87 ? 116  LEU A CD1 1 
ATOM   3223 C CD2 . LEU B 1 116 ? -16.520 1.240   -10.109 1.00  19.64 ? 116  LEU A CD2 1 
ATOM   3224 N N   . SER B 1 117 ? -11.474 1.188   -7.982  1.00  16.35 ? 117  SER A N   1 
ATOM   3225 C CA  . SER B 1 117 ? -10.059 1.131   -8.307  1.00  20.46 ? 117  SER A CA  1 
ATOM   3226 C C   . SER B 1 117 ? -9.468  -0.248  -8.040  1.00  21.21 ? 117  SER A C   1 
ATOM   3227 O O   . SER B 1 117 ? -8.773  -0.814  -8.889  1.00  21.37 ? 117  SER A O   1 
ATOM   3228 C CB  . SER B 1 117 ? -9.281  2.202   -7.530  1.00  26.29 ? 117  SER A CB  1 
ATOM   3229 O OG  . SER B 1 117 ? -9.784  3.500   -7.822  1.00  25.03 ? 117  SER A OG  1 
ATOM   3230 N N   . VAL B 1 118 ? -9.769  -0.816  -6.880  1.00  17.78 ? 118  VAL A N   1 
ATOM   3231 C CA  . VAL B 1 118 ? -9.198  -2.116  -6.563  1.00  19.90 ? 118  VAL A CA  1 
ATOM   3232 C C   . VAL B 1 118 ? -9.808  -3.201  -7.448  1.00  22.03 ? 118  VAL A C   1 
ATOM   3233 O O   . VAL B 1 118 ? -9.162  -4.190  -7.757  1.00  22.52 ? 118  VAL A O   1 
ATOM   3234 C CB  . VAL B 1 118 ? -9.328  -2.474  -5.074  1.00  23.61 ? 118  VAL A CB  1 
ATOM   3235 C CG1 . VAL B 1 118 ? -10.758 -2.883  -4.732  1.00  20.63 ? 118  VAL A CG1 1 
ATOM   3236 C CG2 . VAL B 1 118 ? -8.368  -3.585  -4.752  1.00  30.94 ? 118  VAL A CG2 1 
ATOM   3237 N N   . ALA B 1 119 ? -11.043 -2.979  -7.888  1.00  20.07 ? 119  ALA A N   1 
ATOM   3238 C CA  . ALA B 1 119 ? -11.704 -3.915  -8.773  1.00  19.89 ? 119  ALA A CA  1 
ATOM   3239 C C   . ALA B 1 119 ? -10.952 -3.961  -10.080 1.00  21.97 ? 119  ALA A C   1 
ATOM   3240 O O   . ALA B 1 119 ? -10.980 -4.967  -10.759 1.00  22.19 ? 119  ALA A O   1 
ATOM   3241 C CB  . ALA B 1 119 ? -13.178 -3.535  -9.005  1.00  20.37 ? 119  ALA A CB  1 
ATOM   3242 N N   . GLY B 1 120 ? -10.287 -2.866  -10.437 1.00  21.22 ? 120  GLY A N   1 
ATOM   3243 C CA  . GLY B 1 120 ? -9.481  -2.837  -11.646 1.00  22.79 ? 120  GLY A CA  1 
ATOM   3244 C C   . GLY B 1 120 ? -9.829  -1.771  -12.682 1.00  25.20 ? 120  GLY A C   1 
ATOM   3245 O O   . GLY B 1 120 ? -9.334  -1.823  -13.807 1.00  24.83 ? 120  GLY A O   1 
ATOM   3246 N N   . ALA B 1 121 ? -10.665 -0.801  -12.328 1.00  20.97 ? 121  ALA A N   1 
ATOM   3247 C CA  . ALA B 1 121 ? -11.040 0.242   -13.284 1.00  18.55 ? 121  ALA A CA  1 
ATOM   3248 C C   . ALA B 1 121 ? -9.819  1.095   -13.633 1.00  24.10 ? 121  ALA A C   1 
ATOM   3249 O O   . ALA B 1 121 ? -9.071  1.503   -12.736 1.00  19.58 ? 121  ALA A O   1 
ATOM   3250 C CB  . ALA B 1 121 ? -12.117 1.108   -12.729 1.00  18.30 ? 121  ALA A CB  1 
ATOM   3251 N N   . ASP B 1 122 ? -9.624  1.367   -14.922 0.50  14.40 ? 122  ASP A N   1 
ATOM   3252 C CA  . ASP B 1 122 ? -8.500  2.188   -15.360 0.50  17.28 ? 122  ASP A CA  1 
ATOM   3253 C C   . ASP B 1 122 ? -8.933  3.619   -15.622 0.50  16.25 ? 122  ASP A C   1 
ATOM   3254 O O   . ASP B 1 122 ? -8.121  4.523   -15.682 0.50  12.53 ? 122  ASP A O   1 
ATOM   3255 C CB  . ASP B 1 122 ? -7.872  1.611   -16.625 0.50  18.38 ? 122  ASP A CB  1 
ATOM   3256 C CG  . ASP B 1 122 ? -7.335  0.215   -16.419 0.50  22.01 ? 122  ASP A CG  1 
ATOM   3257 O OD1 . ASP B 1 122 ? -7.828  -0.711  -17.096 0.50  17.79 ? 122  ASP A OD1 1 
ATOM   3258 O OD2 . ASP B 1 122 ? -6.421  0.050   -15.580 0.50  19.62 ? 122  ASP A OD2 1 
ATOM   3259 N N   . HIS B 1 123 ? -10.233 3.815   -15.764 1.00  17.49 ? 123  HIS A N   1 
ATOM   3260 C CA  . HIS B 1 123 ? -10.752 5.089   -16.242 1.00  18.03 ? 123  HIS A CA  1 
ATOM   3261 C C   . HIS B 1 123 ? -12.221 5.159   -15.849 1.00  20.07 ? 123  HIS A C   1 
ATOM   3262 O O   . HIS B 1 123 ? -12.918 4.144   -15.861 1.00  22.22 ? 123  HIS A O   1 
ATOM   3263 C CB  . HIS B 1 123 ? -10.554 5.163   -17.776 1.00  24.92 ? 123  HIS A CB  1 
ATOM   3264 C CG  . HIS B 1 123 ? -11.006 6.448   -18.394 1.00  27.43 ? 123  HIS A CG  1 
ATOM   3265 N ND1 . HIS B 1 123 ? -11.874 6.496   -19.462 1.00  38.79 ? 123  HIS A ND1 1 
ATOM   3266 C CD2 . HIS B 1 123 ? -10.704 7.734   -18.099 1.00  32.47 ? 123  HIS A CD2 1 
ATOM   3267 C CE1 . HIS B 1 123 ? -12.100 7.757   -19.790 1.00  35.84 ? 123  HIS A CE1 1 
ATOM   3268 N NE2 . HIS B 1 123 ? -11.403 8.528   -18.975 1.00  33.15 ? 123  HIS A NE2 1 
ATOM   3269 N N   . ILE B 1 124 ? -12.682 6.337   -15.460 1.00  19.18 ? 124  ILE A N   1 
ATOM   3270 C CA  . ILE B 1 124 ? -14.084 6.542   -15.161 1.00  16.84 ? 124  ILE A CA  1 
ATOM   3271 C C   . ILE B 1 124 ? -14.655 7.577   -16.110 1.00  24.32 ? 124  ILE A C   1 
ATOM   3272 O O   . ILE B 1 124 ? -14.026 8.626   -16.347 1.00  22.96 ? 124  ILE A O   1 
ATOM   3273 C CB  . ILE B 1 124 ? -14.320 7.110   -13.740 1.00  20.09 ? 124  ILE A CB  1 
ATOM   3274 C CG1 . ILE B 1 124 ? -13.603 6.285   -12.666 1.00  20.63 ? 124  ILE A CG1 1 
ATOM   3275 C CG2 . ILE B 1 124 ? -15.833 7.213   -13.463 1.00  20.54 ? 124  ILE A CG2 1 
ATOM   3276 C CD1 . ILE B 1 124 ? -14.091 4.846   -12.523 1.00  18.96 ? 124  ILE A CD1 1 
ATOM   3277 N N   . ILE B 1 125 ? -15.853 7.300   -16.625 1.00  20.06 ? 125  ILE A N   1 
ATOM   3278 C CA  . ILE B 1 125 ? -16.653 8.324   -17.299 1.00  22.26 ? 125  ILE A CA  1 
ATOM   3279 C C   . ILE B 1 125 ? -17.965 8.514   -16.545 1.00  22.39 ? 125  ILE A C   1 
ATOM   3280 O O   . ILE B 1 125 ? -18.702 7.558   -16.318 1.00  20.72 ? 125  ILE A O   1 
ATOM   3281 C CB  . ILE B 1 125 ? -16.947 7.936   -18.769 1.00  22.94 ? 125  ILE A CB  1 
ATOM   3282 C CG1 . ILE B 1 125 ? -15.646 7.887   -19.588 1.00  25.08 ? 125  ILE A CG1 1 
ATOM   3283 C CG2 . ILE B 1 125 ? -17.923 8.914   -19.400 1.00  21.91 ? 125  ILE A CG2 1 
ATOM   3284 C CD1 . ILE B 1 125 ? -15.814 7.310   -21.000 1.00  26.00 ? 125  ILE A CD1 1 
ATOM   3285 N N   . THR B 1 126 ? -18.263 9.748   -16.147 1.00  20.52 ? 126  THR A N   1 
ATOM   3286 C CA  . THR B 1 126 ? -19.497 10.004  -15.425 1.00  20.47 ? 126  THR A CA  1 
ATOM   3287 C C   . THR B 1 126 ? -20.072 11.342  -15.833 1.00  25.09 ? 126  THR A C   1 
ATOM   3288 O O   . THR B 1 126 ? -19.457 12.078  -16.610 1.00  24.74 ? 126  THR A O   1 
ATOM   3289 C CB  . THR B 1 126 ? -19.273 9.959   -13.881 1.00  26.31 ? 126  THR A CB  1 
ATOM   3290 O OG1 . THR B 1 126 ? -20.533 9.863   -13.207 1.00  26.80 ? 126  THR A OG1 1 
ATOM   3291 C CG2 . THR B 1 126 ? -18.505 11.190  -13.399 1.00  22.27 ? 126  THR A CG2 1 
ATOM   3292 N N   . MET B 1 127 ? -21.261 11.655  -15.322 1.00  24.40 ? 127  MET A N   1 
ATOM   3293 C CA  . MET B 1 127 ? -21.936 12.903  -15.674 1.00  30.44 ? 127  MET A CA  1 
ATOM   3294 C C   . MET B 1 127 ? -22.427 13.679  -14.456 1.00  26.64 ? 127  MET A C   1 
ATOM   3295 O O   . MET B 1 127 ? -23.133 13.136  -13.614 1.00  30.36 ? 127  MET A O   1 
ATOM   3296 C CB  . MET B 1 127 ? -23.120 12.639  -16.610 1.00  26.06 ? 127  MET A CB  1 
ATOM   3297 C CG  . MET B 1 127 ? -23.980 13.875  -16.827 1.00  34.22 ? 127  MET A CG  1 
ATOM   3298 S SD  . MET B 1 127 ? -24.996 13.811  -18.325 1.00  41.45 ? 127  MET A SD  1 
ATOM   3299 C CE  . MET B 1 127 ? -23.731 13.557  -19.576 1.00  36.46 ? 127  MET A CE  1 
ATOM   3300 N N   . ASP B 1 128 ? -22.057 14.954  -14.383 0.95  25.40 ? 128  ASP A N   1 
ATOM   3301 C CA  . ASP B 1 128 ? -22.488 15.840  -13.296 0.95  31.61 ? 128  ASP A CA  1 
ATOM   3302 C C   . ASP B 1 128 ? -22.315 15.261  -11.892 0.95  30.49 ? 128  ASP A C   1 
ATOM   3303 O O   . ASP B 1 128 ? -23.287 15.075  -11.161 0.95  30.49 ? 128  ASP A O   1 
ATOM   3304 C CB  . ASP B 1 128 ? -23.933 16.298  -13.502 0.95  33.68 ? 128  ASP A CB  1 
ATOM   3305 C CG  . ASP B 1 128 ? -24.068 17.255  -14.671 0.95  38.96 ? 128  ASP A CG  1 
ATOM   3306 O OD1 . ASP B 1 128 ? -24.976 17.071  -15.508 0.95  41.12 ? 128  ASP A OD1 1 
ATOM   3307 O OD2 . ASP B 1 128 ? -23.248 18.189  -14.758 0.95  38.91 ? 128  ASP A OD2 1 
ATOM   3308 N N   . LEU B 1 129 ? -21.071 14.990  -11.523 1.00  27.89 ? 129  LEU A N   1 
ATOM   3309 C CA  . LEU B 1 129 ? -20.767 14.565  -10.160 1.00  29.76 ? 129  LEU A CA  1 
ATOM   3310 C C   . LEU B 1 129 ? -21.397 15.534  -9.167  1.00  31.41 ? 129  LEU A C   1 
ATOM   3311 O O   . LEU B 1 129 ? -21.300 16.752  -9.350  1.00  27.45 ? 129  LEU A O   1 
ATOM   3312 C CB  . LEU B 1 129 ? -19.256 14.531  -9.954  1.00  29.06 ? 129  LEU A CB  1 
ATOM   3313 C CG  . LEU B 1 129 ? -18.559 13.323  -10.576 1.00  29.82 ? 129  LEU A CG  1 
ATOM   3314 C CD1 . LEU B 1 129 ? -17.054 13.504  -10.522 1.00  28.95 ? 129  LEU A CD1 1 
ATOM   3315 C CD2 . LEU B 1 129 ? -18.973 12.052  -9.856  1.00  27.98 ? 129  LEU A CD2 1 
ATOM   3316 N N   . HIS B 1 130 ? -22.049 15.005  -8.131  1.00  30.85 ? 130  HIS A N   1 
ATOM   3317 C CA  . HIS B 1 130 ? -22.676 15.860  -7.125  1.00  30.13 ? 130  HIS A CA  1 
ATOM   3318 C C   . HIS B 1 130 ? -21.663 16.881  -6.622  1.00  32.35 ? 130  HIS A C   1 
ATOM   3319 O O   . HIS B 1 130 ? -21.986 18.052  -6.454  1.00  34.13 ? 130  HIS A O   1 
ATOM   3320 C CB  . HIS B 1 130 ? -23.220 15.027  -5.961  1.00  37.10 ? 130  HIS A CB  1 
ATOM   3321 C CG  . HIS B 1 130 ? -23.778 15.846  -4.837  1.00  36.53 ? 130  HIS A CG  1 
ATOM   3322 N ND1 . HIS B 1 130 ? -25.029 16.421  -4.882  1.00  35.77 ? 130  HIS A ND1 1 
ATOM   3323 C CD2 . HIS B 1 130 ? -23.254 16.179  -3.632  1.00  36.84 ? 130  HIS A CD2 1 
ATOM   3324 C CE1 . HIS B 1 130 ? -25.254 17.074  -3.755  1.00  39.88 ? 130  HIS A CE1 1 
ATOM   3325 N NE2 . HIS B 1 130 ? -24.191 16.944  -2.980  1.00  36.86 ? 130  HIS A NE2 1 
ATOM   3326 N N   . ALA B 1 131 ? -20.432 16.434  -6.389  1.00  26.44 ? 131  ALA A N   1 
ATOM   3327 C CA  . ALA B 1 131 ? -19.330 17.356  -6.106  1.00  30.39 ? 131  ALA A CA  1 
ATOM   3328 C C   . ALA B 1 131 ? -18.126 17.061  -6.990  1.00  30.98 ? 131  ALA A C   1 
ATOM   3329 O O   . ALA B 1 131 ? -17.659 15.927  -7.074  1.00  31.13 ? 131  ALA A O   1 
ATOM   3330 C CB  . ALA B 1 131 ? -18.938 17.304  -4.642  1.00  33.40 ? 131  ALA A CB  1 
ATOM   3331 N N   . SER B 1 132 ? -17.636 18.097  -7.651  1.00  29.76 ? 132  SER A N   1 
ATOM   3332 C CA  . SER B 1 132 ? -16.492 17.995  -8.543  1.00  33.20 ? 132  SER A CA  1 
ATOM   3333 C C   . SER B 1 132 ? -15.248 17.417  -7.849  1.00  31.57 ? 132  SER A C   1 
ATOM   3334 O O   . SER B 1 132 ? -14.385 16.808  -8.497  1.00  32.97 ? 132  SER A O   1 
ATOM   3335 C CB  . SER B 1 132 ? -16.185 19.385  -9.105  1.00  34.43 ? 132  SER A CB  1 
ATOM   3336 O OG  . SER B 1 132 ? -14.893 19.411  -9.674  1.00  46.64 ? 132  SER A OG  1 
ATOM   3337 N N   . GLN B 1 133 ? -15.155 17.607  -6.535  0.95  28.16 ? 133  GLN A N   1 
ATOM   3338 C CA  . GLN B 1 133 ? -14.011 17.097  -5.771  0.95  28.90 ? 133  GLN A CA  1 
ATOM   3339 C C   . GLN B 1 133 ? -13.944 15.565  -5.824  0.95  26.58 ? 133  GLN A C   1 
ATOM   3340 O O   . GLN B 1 133 ? -12.885 14.969  -5.631  0.95  27.27 ? 133  GLN A O   1 
ATOM   3341 C CB  . GLN B 1 133 ? -14.071 17.576  -4.313  0.95  26.75 ? 133  GLN A CB  1 
ATOM   3342 C CG  . GLN B 1 133 ? -13.778 19.067  -4.123  0.95  28.80 ? 133  GLN A CG  1 
ATOM   3343 C CD  . GLN B 1 133 ? -14.975 19.943  -4.408  0.95  35.86 ? 133  GLN A CD  1 
ATOM   3344 O OE1 . GLN B 1 133 ? -16.046 19.449  -4.751  0.95  34.82 ? 133  GLN A OE1 1 
ATOM   3345 N NE2 . GLN B 1 133 ? -14.801 21.253  -4.268  0.95  32.63 ? 133  GLN A NE2 1 
ATOM   3346 N N   . ILE B 1 134 ? -15.080 14.934  -6.089  1.00  26.14 ? 134  ILE A N   1 
ATOM   3347 C CA  . ILE B 1 134 ? -15.131 13.483  -6.218  1.00  27.04 ? 134  ILE A CA  1 
ATOM   3348 C C   . ILE B 1 134 ? -14.117 12.953  -7.247  1.00  25.79 ? 134  ILE A C   1 
ATOM   3349 O O   . ILE B 1 134 ? -13.631 11.833  -7.120  1.00  26.19 ? 134  ILE A O   1 
ATOM   3350 C CB  . ILE B 1 134 ? -16.575 12.990  -6.516  1.00  26.43 ? 134  ILE A CB  1 
ATOM   3351 C CG1 . ILE B 1 134 ? -17.490 13.351  -5.341  1.00  29.30 ? 134  ILE A CG1 1 
ATOM   3352 C CG2 . ILE B 1 134 ? -16.598 11.478  -6.791  1.00  25.02 ? 134  ILE A CG2 1 
ATOM   3353 C CD1 . ILE B 1 134 ? -18.872 12.757  -5.397  1.00  26.77 ? 134  ILE A CD1 1 
ATOM   3354 N N   . GLN B 1 135 ? -13.765 13.745  -8.253  1.00  27.39 ? 135  GLN A N   1 
ATOM   3355 C CA  . GLN B 1 135 ? -12.673 13.331  -9.161  1.00  24.86 ? 135  GLN A CA  1 
ATOM   3356 C C   . GLN B 1 135 ? -11.374 13.140  -8.386  1.00  26.26 ? 135  GLN A C   1 
ATOM   3357 O O   . GLN B 1 135 ? -10.537 12.293  -8.708  1.00  24.64 ? 135  GLN A O   1 
ATOM   3358 C CB  . GLN B 1 135 ? -12.452 14.385  -10.242 1.00  27.71 ? 135  GLN A CB  1 
ATOM   3359 C CG  . GLN B 1 135 ? -13.644 14.573  -11.148 1.00  30.44 ? 135  GLN A CG  1 
ATOM   3360 C CD  . GLN B 1 135 ? -13.345 15.494  -12.316 1.00  42.05 ? 135  GLN A CD  1 
ATOM   3361 O OE1 . GLN B 1 135 ? -12.572 15.152  -13.212 1.00  39.58 ? 135  GLN A OE1 1 
ATOM   3362 N NE2 . GLN B 1 135 ? -13.952 16.674  -12.306 1.00  38.96 ? 135  GLN A NE2 1 
ATOM   3363 N N   . GLY B 1 136 ? -11.197 13.952  -7.355  1.00  24.96 ? 136  GLY A N   1 
ATOM   3364 C CA  . GLY B 1 136 ? -10.055 13.786  -6.473  1.00  26.20 ? 136  GLY A CA  1 
ATOM   3365 C C   . GLY B 1 136 ? -10.059 12.530  -5.619  1.00  21.28 ? 136  GLY A C   1 
ATOM   3366 O O   . GLY B 1 136 ? -9.067  12.222  -4.985  1.00  22.69 ? 136  GLY A O   1 
ATOM   3367 N N   . PHE B 1 137 ? -11.173 11.809  -5.576  1.00  20.95 ? 137  PHE A N   1 
ATOM   3368 C CA  . PHE B 1 137 ? -11.240 10.579  -4.782  1.00  20.86 ? 137  PHE A CA  1 
ATOM   3369 C C   . PHE B 1 137 ? -10.547 9.429   -5.498  1.00  22.46 ? 137  PHE A C   1 
ATOM   3370 O O   . PHE B 1 137 ? -10.312 8.352   -4.925  1.00  18.61 ? 137  PHE A O   1 
ATOM   3371 C CB  . PHE B 1 137 ? -12.702 10.211  -4.517  1.00  22.66 ? 137  PHE A CB  1 
ATOM   3372 C CG  . PHE B 1 137 ? -13.381 11.105  -3.517  1.00  23.72 ? 137  PHE A CG  1 
ATOM   3373 C CD1 . PHE B 1 137 ? -14.696 10.886  -3.159  1.00  21.59 ? 137  PHE A CD1 1 
ATOM   3374 C CD2 . PHE B 1 137 ? -12.714 12.177  -2.959  1.00  23.81 ? 137  PHE A CD2 1 
ATOM   3375 C CE1 . PHE B 1 137 ? -15.323 11.714  -2.262  1.00  22.78 ? 137  PHE A CE1 1 
ATOM   3376 C CE2 . PHE B 1 137 ? -13.345 13.004  -2.065  1.00  24.07 ? 137  PHE A CE2 1 
ATOM   3377 C CZ  . PHE B 1 137 ? -14.656 12.763  -1.713  1.00  25.03 ? 137  PHE A CZ  1 
ATOM   3378 N N   . PHE B 1 138 ? -10.219 9.657   -6.764  1.00  20.75 ? 138  PHE A N   1 
ATOM   3379 C CA  . PHE B 1 138 ? -9.554  8.650   -7.573  1.00  19.96 ? 138  PHE A CA  1 
ATOM   3380 C C   . PHE B 1 138 ? -8.126  9.052   -7.838  1.00  21.76 ? 138  PHE A C   1 
ATOM   3381 O O   . PHE B 1 138 ? -7.790  10.236  -7.758  1.00  23.28 ? 138  PHE A O   1 
ATOM   3382 C CB  . PHE B 1 138 ? -10.247 8.525   -8.930  1.00  20.45 ? 138  PHE A CB  1 
ATOM   3383 C CG  . PHE B 1 138 ? -11.608 7.929   -8.863  1.00  22.66 ? 138  PHE A CG  1 
ATOM   3384 C CD1 . PHE B 1 138 ? -12.722 8.731   -8.683  1.00  21.07 ? 138  PHE A CD1 1 
ATOM   3385 C CD2 . PHE B 1 138 ? -11.778 6.559   -8.991  1.00  22.38 ? 138  PHE A CD2 1 
ATOM   3386 C CE1 . PHE B 1 138 ? -13.993 8.175   -8.651  1.00  23.20 ? 138  PHE A CE1 1 
ATOM   3387 C CE2 . PHE B 1 138 ? -13.035 5.998   -8.950  1.00  22.56 ? 138  PHE A CE2 1 
ATOM   3388 C CZ  . PHE B 1 138 ? -14.152 6.813   -8.791  1.00  18.30 ? 138  PHE A CZ  1 
ATOM   3389 N N   . ASP B 1 139 ? -7.287  8.072   -8.172  1.00  23.60 ? 139  ASP A N   1 
ATOM   3390 C CA  . ASP B 1 139 ? -5.970  8.362   -8.739  1.00  23.54 ? 139  ASP A CA  1 
ATOM   3391 C C   . ASP B 1 139 ? -5.953  8.073   -10.260 1.00  26.02 ? 139  ASP A C   1 
ATOM   3392 O O   . ASP B 1 139 ? -5.003  8.417   -10.965 1.00  29.15 ? 139  ASP A O   1 
ATOM   3393 C CB  . ASP B 1 139 ? -4.878  7.561   -8.035  1.00  28.21 ? 139  ASP A CB  1 
ATOM   3394 C CG  . ASP B 1 139 ? -4.596  8.060   -6.616  1.00  34.35 ? 139  ASP A CG  1 
ATOM   3395 O OD1 . ASP B 1 139 ? -4.543  9.290   -6.399  1.00  29.72 ? 139  ASP A OD1 1 
ATOM   3396 O OD2 . ASP B 1 139 ? -4.406  7.211   -5.727  1.00  38.32 ? 139  ASP A OD2 1 
ATOM   3397 N N   . ILE B 1 140 ? -7.012  7.452   -10.758 1.00  27.00 ? 140  ILE A N   1 
ATOM   3398 C CA  . ILE B 1 140 ? -7.138  7.205   -12.188 1.00  19.74 ? 140  ILE A CA  1 
ATOM   3399 C C   . ILE B 1 140 ? -7.865  8.377   -12.805 1.00  19.55 ? 140  ILE A C   1 
ATOM   3400 O O   . ILE B 1 140 ? -8.587  9.105   -12.111 1.00  22.81 ? 140  ILE A O   1 
ATOM   3401 C CB  . ILE B 1 140 ? -7.900  5.882   -12.490 1.00  18.85 ? 140  ILE A CB  1 
ATOM   3402 C CG1 . ILE B 1 140 ? -9.276  5.908   -11.807 1.00  21.97 ? 140  ILE A CG1 1 
ATOM   3403 C CG2 . ILE B 1 140 ? -7.083  4.686   -12.038 1.00  21.66 ? 140  ILE A CG2 1 
ATOM   3404 C CD1 . ILE B 1 140 ? -10.117 4.658   -11.991 1.00  19.31 ? 140  ILE A CD1 1 
ATOM   3405 N N   . PRO B 1 141 ? -7.691  8.577   -14.127 1.00  25.79 ? 141  PRO A N   1 
ATOM   3406 C CA  . PRO B 1 141 ? -8.400  9.676   -14.780 1.00  23.31 ? 141  PRO A CA  1 
ATOM   3407 C C   . PRO B 1 141 ? -9.921  9.520   -14.684 1.00  23.18 ? 141  PRO A C   1 
ATOM   3408 O O   . PRO B 1 141 ? -10.468 8.422   -14.871 1.00  23.05 ? 141  PRO A O   1 
ATOM   3409 C CB  . PRO B 1 141 ? -7.972  9.559   -16.245 1.00  22.41 ? 141  PRO A CB  1 
ATOM   3410 C CG  . PRO B 1 141 ? -6.740  8.785   -16.241 1.00  26.56 ? 141  PRO A CG  1 
ATOM   3411 C CD  . PRO B 1 141 ? -6.789  7.866   -15.048 1.00  20.08 ? 141  PRO A CD  1 
ATOM   3412 N N   . VAL B 1 142 ? -10.593 10.629  -14.412 1.00  21.59 ? 142  VAL A N   1 
ATOM   3413 C CA  . VAL B 1 142 ? -12.045 10.685  -14.451 1.00  22.06 ? 142  VAL A CA  1 
ATOM   3414 C C   . VAL B 1 142 ? -12.448 11.759  -15.472 1.00  30.70 ? 142  VAL A C   1 
ATOM   3415 O O   . VAL B 1 142 ? -11.939 12.882  -15.435 1.00  27.86 ? 142  VAL A O   1 
ATOM   3416 C CB  . VAL B 1 142 ? -12.607 11.067  -13.076 1.00  25.84 ? 142  VAL A CB  1 
ATOM   3417 C CG1 . VAL B 1 142 ? -14.147 11.040  -13.086 1.00  22.51 ? 142  VAL A CG1 1 
ATOM   3418 C CG2 . VAL B 1 142 ? -12.074 10.127  -11.999 1.00  18.08 ? 142  VAL A CG2 1 
ATOM   3419 N N   . ASP B 1 143 ? -13.338 11.411  -16.395 0.93  23.01 ? 143  ASP A N   1 
ATOM   3420 C CA  . ASP B 1 143 ? -13.976 12.422  -17.223 0.93  25.71 ? 143  ASP A CA  1 
ATOM   3421 C C   . ASP B 1 143 ? -15.381 12.671  -16.695 0.93  28.69 ? 143  ASP A C   1 
ATOM   3422 O O   . ASP B 1 143 ? -16.229 11.784  -16.721 0.93  27.11 ? 143  ASP A O   1 
ATOM   3423 C CB  . ASP B 1 143 ? -14.015 11.995  -18.691 0.93  28.56 ? 143  ASP A CB  1 
ATOM   3424 C CG  . ASP B 1 143 ? -12.627 11.805  -19.277 0.93  32.84 ? 143  ASP A CG  1 
ATOM   3425 O OD1 . ASP B 1 143 ? -11.742 12.659  -19.039 0.93  35.83 ? 143  ASP A OD1 1 
ATOM   3426 O OD2 . ASP B 1 143 ? -12.406 10.787  -19.962 0.93  35.83 ? 143  ASP A OD2 1 
ATOM   3427 N N   . ASN B 1 144 ? -15.615 13.887  -16.221 1.00  22.63 ? 144  ASN A N   1 
ATOM   3428 C CA  . ASN B 1 144 ? -16.893 14.287  -15.654 1.00  25.16 ? 144  ASN A CA  1 
ATOM   3429 C C   . ASN B 1 144 ? -17.663 15.159  -16.650 1.00  33.75 ? 144  ASN A C   1 
ATOM   3430 O O   . ASN B 1 144 ? -17.383 16.344  -16.802 1.00  33.49 ? 144  ASN A O   1 
ATOM   3431 C CB  . ASN B 1 144 ? -16.643 15.054  -14.354 1.00  28.73 ? 144  ASN A CB  1 
ATOM   3432 C CG  . ASN B 1 144 ? -17.925 15.515  -13.670 1.00  30.89 ? 144  ASN A CG  1 
ATOM   3433 O OD1 . ASN B 1 144 ? -18.972 14.871  -13.753 1.00  27.73 ? 144  ASN A OD1 1 
ATOM   3434 N ND2 . ASN B 1 144 ? -17.835 16.643  -12.978 1.00  29.39 ? 144  ASN A ND2 1 
ATOM   3435 N N   . LEU B 1 145 ? -18.632 14.566  -17.337 1.00  28.57 ? 145  LEU A N   1 
ATOM   3436 C CA  . LEU B 1 145 ? -19.360 15.293  -18.370 1.00  35.09 ? 145  LEU A CA  1 
ATOM   3437 C C   . LEU B 1 145 ? -20.440 16.171  -17.741 1.00  36.72 ? 145  LEU A C   1 
ATOM   3438 O O   . LEU B 1 145 ? -20.864 15.932  -16.610 1.00  33.69 ? 145  LEU A O   1 
ATOM   3439 C CB  . LEU B 1 145 ? -19.969 14.313  -19.371 1.00  30.32 ? 145  LEU A CB  1 
ATOM   3440 C CG  . LEU B 1 145 ? -18.965 13.280  -19.869 1.00  32.23 ? 145  LEU A CG  1 
ATOM   3441 C CD1 . LEU B 1 145 ? -19.658 12.131  -20.593 1.00  31.97 ? 145  LEU A CD1 1 
ATOM   3442 C CD2 . LEU B 1 145 ? -17.918 13.934  -20.740 1.00  31.43 ? 145  LEU A CD2 1 
ATOM   3443 N N   . TYR B 1 146 ? -20.874 17.193  -18.472 1.00  38.42 ? 146  TYR A N   1 
ATOM   3444 C CA  . TYR B 1 146 ? -21.891 18.109  -17.969 1.00  36.02 ? 146  TYR A CA  1 
ATOM   3445 C C   . TYR B 1 146 ? -23.121 18.048  -18.839 1.00  37.82 ? 146  TYR A C   1 
ATOM   3446 O O   . TYR B 1 146 ? -23.015 17.923  -20.058 1.00  36.03 ? 146  TYR A O   1 
ATOM   3447 C CB  . TYR B 1 146 ? -21.347 19.537  -17.947 1.00  42.99 ? 146  TYR A CB  1 
ATOM   3448 C CG  . TYR B 1 146 ? -20.004 19.610  -17.280 1.00  42.27 ? 146  TYR A CG  1 
ATOM   3449 C CD1 . TYR B 1 146 ? -18.840 19.555  -18.028 1.00  43.29 ? 146  TYR A CD1 1 
ATOM   3450 C CD2 . TYR B 1 146 ? -19.900 19.683  -15.898 1.00  44.97 ? 146  TYR A CD2 1 
ATOM   3451 C CE1 . TYR B 1 146 ? -17.603 19.596  -17.424 1.00  47.00 ? 146  TYR A CE1 1 
ATOM   3452 C CE2 . TYR B 1 146 ? -18.665 19.730  -15.276 1.00  46.44 ? 146  TYR A CE2 1 
ATOM   3453 C CZ  . TYR B 1 146 ? -17.520 19.684  -16.047 1.00  48.28 ? 146  TYR A CZ  1 
ATOM   3454 O OH  . TYR B 1 146 ? -16.285 19.721  -15.439 1.00  52.18 ? 146  TYR A OH  1 
ATOM   3455 N N   . ALA B 1 147 ? -24.288 18.132  -18.208 1.00  36.60 ? 147  ALA A N   1 
ATOM   3456 C CA  . ALA B 1 147 ? -25.536 18.273  -18.941 1.00  40.17 ? 147  ALA A CA  1 
ATOM   3457 C C   . ALA B 1 147 ? -25.846 19.748  -19.186 1.00  36.65 ? 147  ALA A C   1 
ATOM   3458 O O   . ALA B 1 147 ? -26.782 20.062  -19.902 1.00  36.08 ? 147  ALA A O   1 
ATOM   3459 C CB  . ALA B 1 147 ? -26.679 17.624  -18.181 1.00  41.00 ? 147  ALA A CB  1 
ATOM   3460 N N   . GLU B 1 148 ? -25.062 20.635  -18.576 1.00  37.61 ? 148  GLU A N   1 
ATOM   3461 C CA  . GLU B 1 148 ? -25.280 22.079  -18.678 1.00  39.73 ? 148  GLU A CA  1 
ATOM   3462 C C   . GLU B 1 148 ? -25.637 22.530  -20.099 1.00  39.41 ? 148  GLU A C   1 
ATOM   3463 O O   . GLU B 1 148 ? -26.692 23.134  -20.304 1.00  41.73 ? 148  GLU A O   1 
ATOM   3464 C CB  . GLU B 1 148 ? -24.066 22.862  -18.163 1.00  44.38 ? 148  GLU A CB  1 
ATOM   3465 C CG  . GLU B 1 148 ? -24.247 24.380  -18.236 1.00  48.51 ? 148  GLU A CG  1 
ATOM   3466 C CD  . GLU B 1 148 ? -23.138 25.145  -17.531 1.00  58.63 ? 148  GLU A CD  1 
ATOM   3467 O OE1 . GLU B 1 148 ? -22.167 24.505  -17.077 1.00  64.11 ? 148  GLU A OE1 1 
ATOM   3468 O OE2 . GLU B 1 148 ? -23.237 26.388  -17.436 1.00  56.59 ? 148  GLU A OE2 1 
ATOM   3469 N N   . PRO B 1 149 ? -24.770 22.227  -21.083 1.00  39.18 ? 149  PRO A N   1 
ATOM   3470 C CA  . PRO B 1 149 ? -25.063 22.656  -22.455 1.00  43.19 ? 149  PRO A CA  1 
ATOM   3471 C C   . PRO B 1 149 ? -26.407 22.121  -22.942 1.00  41.11 ? 149  PRO A C   1 
ATOM   3472 O O   . PRO B 1 149 ? -27.148 22.838  -23.613 1.00  38.08 ? 149  PRO A O   1 
ATOM   3473 C CB  . PRO B 1 149 ? -23.922 22.040  -23.263 1.00  39.01 ? 149  PRO A CB  1 
ATOM   3474 C CG  . PRO B 1 149 ? -22.828 21.851  -22.284 1.00  43.94 ? 149  PRO A CG  1 
ATOM   3475 C CD  . PRO B 1 149 ? -23.511 21.467  -21.014 1.00  38.02 ? 149  PRO A CD  1 
ATOM   3476 N N   . ALA B 1 150 ? -26.725 20.878  -22.598 1.00  37.62 ? 150  ALA A N   1 
ATOM   3477 C CA  . ALA B 1 150 ? -28.013 20.304  -22.975 1.00  38.01 ? 150  ALA A CA  1 
ATOM   3478 C C   . ALA B 1 150 ? -29.174 21.027  -22.299 1.00  40.47 ? 150  ALA A C   1 
ATOM   3479 O O   . ALA B 1 150 ? -30.254 21.188  -22.881 1.00  40.75 ? 150  ALA A O   1 
ATOM   3480 C CB  . ALA B 1 150 ? -28.052 18.825  -22.648 1.00  38.71 ? 150  ALA A CB  1 
ATOM   3481 N N   . VAL B 1 151 ? -28.951 21.457  -21.063 1.00  38.18 ? 151  VAL A N   1 
ATOM   3482 C CA  . VAL B 1 151 ? -30.006 22.082  -20.268 1.00  38.20 ? 151  VAL A CA  1 
ATOM   3483 C C   . VAL B 1 151 ? -30.305 23.504  -20.754 1.00  41.19 ? 151  VAL A C   1 
ATOM   3484 O O   . VAL B 1 151 ? -31.461 23.940  -20.781 1.00  39.83 ? 151  VAL A O   1 
ATOM   3485 C CB  . VAL B 1 151 ? -29.618 22.137  -18.790 1.00  36.49 ? 151  VAL A CB  1 
ATOM   3486 C CG1 . VAL B 1 151 ? -30.631 22.966  -18.004 1.00  41.54 ? 151  VAL A CG1 1 
ATOM   3487 C CG2 . VAL B 1 151 ? -29.513 20.720  -18.222 1.00  38.82 ? 151  VAL A CG2 1 
ATOM   3488 N N   . LEU B 1 152 ? -29.247 24.221  -21.113 1.00  34.91 ? 152  LEU A N   1 
ATOM   3489 C CA  . LEU B 1 152 ? -29.386 25.581  -21.595 1.00  42.19 ? 152  LEU A CA  1 
ATOM   3490 C C   . LEU B 1 152 ? -30.200 25.533  -22.870 1.00  42.96 ? 152  LEU A C   1 
ATOM   3491 O O   . LEU B 1 152 ? -31.208 26.228  -23.001 1.00  45.71 ? 152  LEU A O   1 
ATOM   3492 C CB  . LEU B 1 152 ? -28.015 26.203  -21.853 1.00  36.07 ? 152  LEU A CB  1 
ATOM   3493 C CG  . LEU B 1 152 ? -27.451 27.010  -20.679 1.00  45.39 ? 152  LEU A CG  1 
ATOM   3494 C CD1 . LEU B 1 152 ? -27.975 26.481  -19.356 1.00  44.36 ? 152  LEU A CD1 1 
ATOM   3495 C CD2 . LEU B 1 152 ? -25.930 27.026  -20.707 1.00  40.02 ? 152  LEU A CD2 1 
ATOM   3496 N N   . LYS B 1 153 ? -29.755 24.687  -23.792 0.60  40.49 ? 153  LYS A N   1 
ATOM   3497 C CA  . LYS B 1 153 ? -30.451 24.471  -25.049 0.60  40.26 ? 153  LYS A CA  1 
ATOM   3498 C C   . LYS B 1 153 ? -31.932 24.247  -24.802 0.60  40.41 ? 153  LYS A C   1 
ATOM   3499 O O   . LYS B 1 153 ? -32.777 24.873  -25.443 0.60  43.91 ? 153  LYS A O   1 
ATOM   3500 C CB  . LYS B 1 153 ? -29.848 23.278  -25.794 0.60  37.99 ? 153  LYS A CB  1 
ATOM   3501 C CG  . LYS B 1 153 ? -30.557 22.930  -27.087 0.60  39.42 ? 153  LYS A CG  1 
ATOM   3502 C CD  . LYS B 1 153 ? -29.626 22.222  -28.048 0.60  40.45 ? 153  LYS A CD  1 
ATOM   3503 C CE  . LYS B 1 153 ? -30.236 22.120  -29.446 0.60  47.06 ? 153  LYS A CE  1 
ATOM   3504 N NZ  . LYS B 1 153 ? -31.500 21.323  -29.467 0.60  47.67 ? 153  LYS A NZ  1 
ATOM   3505 N N   . TRP B 1 154 ? -32.251 23.362  -23.864 1.00  39.54 ? 154  TRP A N   1 
ATOM   3506 C CA  . TRP B 1 154 ? -33.650 23.033  -23.604 1.00  42.38 ? 154  TRP A CA  1 
ATOM   3507 C C   . TRP B 1 154 ? -34.432 24.247  -23.100 1.00  44.28 ? 154  TRP A C   1 
ATOM   3508 O O   . TRP B 1 154 ? -35.589 24.453  -23.478 1.00  42.49 ? 154  TRP A O   1 
ATOM   3509 C CB  . TRP B 1 154 ? -33.778 21.871  -22.612 1.00  42.63 ? 154  TRP A CB  1 
ATOM   3510 C CG  . TRP B 1 154 ? -35.179 21.329  -22.518 1.00  42.53 ? 154  TRP A CG  1 
ATOM   3511 C CD1 . TRP B 1 154 ? -35.692 20.255  -23.191 1.00  38.77 ? 154  TRP A CD1 1 
ATOM   3512 C CD2 . TRP B 1 154 ? -36.253 21.852  -21.719 1.00  43.04 ? 154  TRP A CD2 1 
ATOM   3513 N NE1 . TRP B 1 154 ? -37.015 20.070  -22.853 1.00  45.22 ? 154  TRP A NE1 1 
ATOM   3514 C CE2 . TRP B 1 154 ? -37.382 21.034  -21.951 1.00  44.41 ? 154  TRP A CE2 1 
ATOM   3515 C CE3 . TRP B 1 154 ? -36.365 22.924  -20.828 1.00  44.29 ? 154  TRP A CE3 1 
ATOM   3516 C CZ2 . TRP B 1 154 ? -38.610 21.262  -21.324 1.00  44.84 ? 154  TRP A CZ2 1 
ATOM   3517 C CZ3 . TRP B 1 154 ? -37.588 23.146  -20.202 1.00  41.87 ? 154  TRP A CZ3 1 
ATOM   3518 C CH2 . TRP B 1 154 ? -38.690 22.319  -20.454 1.00  41.80 ? 154  TRP A CH2 1 
ATOM   3519 N N   . ILE B 1 155 ? -33.802 25.043  -22.239 1.00  42.89 ? 155  ILE A N   1 
ATOM   3520 C CA  . ILE B 1 155 ? -34.462 26.214  -21.673 1.00  43.63 ? 155  ILE A CA  1 
ATOM   3521 C C   . ILE B 1 155 ? -34.757 27.260  -22.748 1.00  41.57 ? 155  ILE A C   1 
ATOM   3522 O O   . ILE B 1 155 ? -35.851 27.803  -22.818 1.00  43.52 ? 155  ILE A O   1 
ATOM   3523 C CB  . ILE B 1 155 ? -33.619 26.852  -20.559 1.00  40.07 ? 155  ILE A CB  1 
ATOM   3524 C CG1 . ILE B 1 155 ? -33.560 25.931  -19.341 1.00  40.84 ? 155  ILE A CG1 1 
ATOM   3525 C CG2 . ILE B 1 155 ? -34.194 28.198  -20.160 1.00  41.05 ? 155  ILE A CG2 1 
ATOM   3526 C CD1 . ILE B 1 155 ? -32.611 26.436  -18.276 1.00  39.21 ? 155  ILE A CD1 1 
ATOM   3527 N N   . ARG B 1 156 ? -33.775 27.544  -23.583 1.00  42.13 ? 156  ARG A N   1 
ATOM   3528 C CA  . ARG B 1 156 ? -33.994 28.498  -24.653 1.00  51.28 ? 156  ARG A CA  1 
ATOM   3529 C C   . ARG B 1 156 ? -35.128 28.021  -25.566 1.00  49.72 ? 156  ARG A C   1 
ATOM   3530 O O   . ARG B 1 156 ? -36.039 28.784  -25.899 1.00  52.76 ? 156  ARG A O   1 
ATOM   3531 C CB  . ARG B 1 156 ? -32.704 28.726  -25.440 1.00  44.55 ? 156  ARG A CB  1 
ATOM   3532 C CG  . ARG B 1 156 ? -31.583 29.268  -24.590 1.00  47.40 ? 156  ARG A CG  1 
ATOM   3533 C CD  . ARG B 1 156 ? -30.460 29.823  -25.435 1.00  51.86 ? 156  ARG A CD  1 
ATOM   3534 N NE  . ARG B 1 156 ? -29.402 30.416  -24.622 1.00  52.32 ? 156  ARG A NE  1 
ATOM   3535 C CZ  . ARG B 1 156 ? -28.203 29.868  -24.436 1.00  57.81 ? 156  ARG A CZ  1 
ATOM   3536 N NH1 . ARG B 1 156 ? -27.900 28.712  -25.017 1.00  56.38 ? 156  ARG A NH1 1 
ATOM   3537 N NH2 . ARG B 1 156 ? -27.300 30.483  -23.674 1.00  55.14 ? 156  ARG A NH2 1 
ATOM   3538 N N   . GLU B 1 157 ? -35.091 26.743  -25.926 1.00  47.56 ? 157  GLU A N   1 
ATOM   3539 C CA  . GLU B 1 157 ? -36.015 26.206  -26.915 1.00  49.30 ? 157  GLU A CA  1 
ATOM   3540 C C   . GLU B 1 157 ? -37.414 25.906  -26.392 1.00  48.40 ? 157  GLU A C   1 
ATOM   3541 O O   . GLU B 1 157 ? -38.315 25.625  -27.180 1.00  53.77 ? 157  GLU A O   1 
ATOM   3542 C CB  . GLU B 1 157 ? -35.427 24.950  -27.562 1.00  47.76 ? 157  GLU A CB  1 
ATOM   3543 C CG  . GLU B 1 157 ? -34.075 25.180  -28.215 1.00  51.44 ? 157  GLU A CG  1 
ATOM   3544 C CD  . GLU B 1 157 ? -33.593 23.978  -29.008 1.00  54.74 ? 157  GLU A CD  1 
ATOM   3545 O OE1 . GLU B 1 157 ? -32.714 24.151  -29.881 1.00  49.76 ? 157  GLU A OE1 1 
ATOM   3546 O OE2 . GLU B 1 157 ? -34.099 22.863  -28.759 1.00  57.07 ? 157  GLU A OE2 1 
ATOM   3547 N N   . ASN B 1 158 ? -37.613 25.955  -25.080 1.00  45.76 ? 158  ASN A N   1 
ATOM   3548 C CA  . ASN B 1 158 ? -38.886 25.512  -24.524 1.00  43.60 ? 158  ASN A CA  1 
ATOM   3549 C C   . ASN B 1 158 ? -39.567 26.513  -23.601 1.00  45.02 ? 158  ASN A C   1 
ATOM   3550 O O   . ASN B 1 158 ? -40.744 26.361  -23.268 1.00  44.53 ? 158  ASN A O   1 
ATOM   3551 C CB  . ASN B 1 158 ? -38.728 24.167  -23.810 1.00  45.66 ? 158  ASN A CB  1 
ATOM   3552 C CG  . ASN B 1 158 ? -38.425 23.034  -24.768 1.00  49.32 ? 158  ASN A CG  1 
ATOM   3553 O OD1 . ASN B 1 158 ? -37.274 22.825  -25.165 1.00  51.36 ? 158  ASN A OD1 1 
ATOM   3554 N ND2 . ASN B 1 158 ? -39.457 22.294  -25.147 1.00  47.78 ? 158  ASN A ND2 1 
ATOM   3555 N N   . ILE B 1 159 ? -38.829 27.532  -23.185 1.00  45.04 ? 159  ILE A N   1 
ATOM   3556 C CA  . ILE B 1 159 ? -39.379 28.529  -22.282 1.00  43.34 ? 159  ILE A CA  1 
ATOM   3557 C C   . ILE B 1 159 ? -39.392 29.888  -22.980 1.00  43.57 ? 159  ILE A C   1 
ATOM   3558 O O   . ILE B 1 159 ? -38.348 30.522  -23.134 1.00  42.31 ? 159  ILE A O   1 
ATOM   3559 C CB  . ILE B 1 159 ? -38.552 28.592  -20.982 1.00  46.05 ? 159  ILE A CB  1 
ATOM   3560 C CG1 . ILE B 1 159 ? -38.516 27.205  -20.327 1.00  46.17 ? 159  ILE A CG1 1 
ATOM   3561 C CG2 . ILE B 1 159 ? -39.112 29.642  -20.033 1.00  43.50 ? 159  ILE A CG2 1 
ATOM   3562 C CD1 . ILE B 1 159 ? -37.949 27.197  -18.913 1.00  46.30 ? 159  ILE A CD1 1 
ATOM   3563 N N   . SER B 1 160 ? -40.568 30.320  -23.429 1.00  42.63 ? 160  SER A N   1 
ATOM   3564 C CA  . SER B 1 160 ? -40.669 31.555  -24.208 1.00  47.28 ? 160  SER A CA  1 
ATOM   3565 C C   . SER B 1 160 ? -40.140 32.788  -23.469 1.00  43.02 ? 160  SER A C   1 
ATOM   3566 O O   . SER B 1 160 ? -39.483 33.639  -24.062 1.00  44.97 ? 160  SER A O   1 
ATOM   3567 C CB  . SER B 1 160 ? -42.106 31.793  -24.694 1.00  45.14 ? 160  SER A CB  1 
ATOM   3568 O OG  . SER B 1 160 ? -43.022 31.897  -23.615 1.00  51.53 ? 160  SER A OG  1 
ATOM   3569 N N   . GLU B 1 161 ? -40.418 32.874  -22.175 0.95  45.12 ? 161  GLU A N   1 
ATOM   3570 C CA  . GLU B 1 161 ? -40.004 34.028  -21.376 0.95  48.37 ? 161  GLU A CA  1 
ATOM   3571 C C   . GLU B 1 161 ? -38.600 33.879  -20.792 0.95  48.78 ? 161  GLU A C   1 
ATOM   3572 O O   . GLU B 1 161 ? -38.250 34.572  -19.837 0.95  50.18 ? 161  GLU A O   1 
ATOM   3573 C CB  . GLU B 1 161 ? -40.992 34.249  -20.225 0.95  45.90 ? 161  GLU A CB  1 
ATOM   3574 C CG  . GLU B 1 161 ? -42.450 34.120  -20.612 0.95  47.66 ? 161  GLU A CG  1 
ATOM   3575 C CD  . GLU B 1 161 ? -42.895 32.676  -20.720 0.95  54.50 ? 161  GLU A CD  1 
ATOM   3576 O OE1 . GLU B 1 161 ? -42.020 31.784  -20.754 0.95  53.16 ? 161  GLU A OE1 1 
ATOM   3577 O OE2 . GLU B 1 161 ? -44.121 32.427  -20.763 0.95  56.26 ? 161  GLU A OE2 1 
ATOM   3578 N N   . TRP B 1 162 ? -37.791 32.985  -21.357 1.00  48.47 ? 162  TRP A N   1 
ATOM   3579 C CA  . TRP B 1 162 ? -36.531 32.614  -20.712 1.00  49.37 ? 162  TRP A CA  1 
ATOM   3580 C C   . TRP B 1 162 ? -35.565 33.784  -20.513 1.00  51.21 ? 162  TRP A C   1 
ATOM   3581 O O   . TRP B 1 162 ? -34.796 33.813  -19.542 1.00  46.54 ? 162  TRP A O   1 
ATOM   3582 C CB  . TRP B 1 162 ? -35.845 31.447  -21.437 1.00  46.24 ? 162  TRP A CB  1 
ATOM   3583 C CG  . TRP B 1 162 ? -35.255 31.779  -22.777 1.00  45.57 ? 162  TRP A CG  1 
ATOM   3584 C CD1 . TRP B 1 162 ? -35.826 31.562  -24.003 1.00  46.18 ? 162  TRP A CD1 1 
ATOM   3585 C CD2 . TRP B 1 162 ? -33.971 32.355  -23.032 1.00  43.04 ? 162  TRP A CD2 1 
ATOM   3586 N NE1 . TRP B 1 162 ? -34.979 31.974  -25.002 1.00  45.04 ? 162  TRP A NE1 1 
ATOM   3587 C CE2 . TRP B 1 162 ? -33.835 32.469  -24.435 1.00  44.69 ? 162  TRP A CE2 1 
ATOM   3588 C CE3 . TRP B 1 162 ? -32.926 32.796  -22.213 1.00  44.14 ? 162  TRP A CE3 1 
ATOM   3589 C CZ2 . TRP B 1 162 ? -32.695 33.004  -25.035 1.00  48.30 ? 162  TRP A CZ2 1 
ATOM   3590 C CZ3 . TRP B 1 162 ? -31.791 33.325  -22.812 1.00  45.85 ? 162  TRP A CZ3 1 
ATOM   3591 C CH2 . TRP B 1 162 ? -31.686 33.425  -24.210 1.00  48.39 ? 162  TRP A CH2 1 
ATOM   3592 N N   . ARG B 1 163 ? -35.615 34.752  -21.421 1.00  49.86 ? 163  ARG A N   1 
ATOM   3593 C CA  . ARG B 1 163 ? -34.685 35.874  -21.385 1.00  47.48 ? 163  ARG A CA  1 
ATOM   3594 C C   . ARG B 1 163 ? -34.823 36.715  -20.122 1.00  46.45 ? 163  ARG A C   1 
ATOM   3595 O O   . ARG B 1 163 ? -33.911 37.465  -19.768 1.00  41.63 ? 163  ARG A O   1 
ATOM   3596 C CB  . ARG B 1 163 ? -34.846 36.737  -22.633 1.00  50.17 ? 163  ARG A CB  1 
ATOM   3597 C CG  . ARG B 1 163 ? -34.577 35.959  -23.910 1.00  51.09 ? 163  ARG A CG  1 
ATOM   3598 C CD  . ARG B 1 163 ? -34.455 36.872  -25.112 1.00  52.48 ? 163  ARG A CD  1 
ATOM   3599 N NE  . ARG B 1 163 ? -34.229 36.119  -26.343 1.00  48.04 ? 163  ARG A NE  1 
ATOM   3600 C CZ  . ARG B 1 163 ? -33.037 35.938  -26.903 1.00  46.94 ? 163  ARG A CZ  1 
ATOM   3601 N NH1 . ARG B 1 163 ? -31.950 36.457  -26.348 1.00  44.33 ? 163  ARG A NH1 1 
ATOM   3602 N NH2 . ARG B 1 163 ? -32.936 35.243  -28.029 1.00  54.11 ? 163  ARG A NH2 1 
ATOM   3603 N N   . ASN B 1 164 ? -35.957 36.581  -19.444 0.94  45.07 ? 164  ASN A N   1 
ATOM   3604 C CA  . ASN B 1 164 ? -36.190 37.298  -18.199 0.94  44.96 ? 164  ASN A CA  1 
ATOM   3605 C C   . ASN B 1 164 ? -36.545 36.376  -17.034 0.94  48.63 ? 164  ASN A C   1 
ATOM   3606 O O   . ASN B 1 164 ? -37.199 36.807  -16.085 0.94  49.49 ? 164  ASN A O   1 
ATOM   3607 C CB  . ASN B 1 164 ? -37.303 38.339  -18.374 0.94  56.24 ? 164  ASN A CB  1 
ATOM   3608 C CG  . ASN B 1 164 ? -36.919 39.460  -19.317 0.94  52.96 ? 164  ASN A CG  1 
ATOM   3609 O OD1 . ASN B 1 164 ? -37.673 39.794  -20.229 0.94  58.92 ? 164  ASN A OD1 1 
ATOM   3610 N ND2 . ASN B 1 164 ? -35.747 40.050  -19.102 0.94  55.21 ? 164  ASN A ND2 1 
ATOM   3611 N N   . CYS B 1 165 ? -36.119 35.115  -17.097 1.00  43.95 ? 165  CYS A N   1 
ATOM   3612 C CA  . CYS B 1 165 ? -36.443 34.169  -16.028 1.00  46.82 ? 165  CYS A CA  1 
ATOM   3613 C C   . CYS B 1 165 ? -35.453 34.267  -14.872 1.00  45.94 ? 165  CYS A C   1 
ATOM   3614 O O   . CYS B 1 165 ? -34.489 35.028  -14.927 1.00  42.55 ? 165  CYS A O   1 
ATOM   3615 C CB  . CYS B 1 165 ? -36.438 32.735  -16.548 1.00  44.17 ? 165  CYS A CB  1 
ATOM   3616 S SG  . CYS B 1 165 ? -34.788 32.164  -16.943 1.00  41.89 ? 165  CYS A SG  1 
ATOM   3617 N N   . THR B 1 166 ? -35.702 33.485  -13.827 1.00  41.48 ? 166  THR A N   1 
ATOM   3618 C CA  . THR B 1 166 ? -34.758 33.373  -12.725 1.00  44.65 ? 166  THR A CA  1 
ATOM   3619 C C   . THR B 1 166 ? -34.428 31.917  -12.464 1.00  42.21 ? 166  THR A C   1 
ATOM   3620 O O   . THR B 1 166 ? -35.319 31.103  -12.203 1.00  41.03 ? 166  THR A O   1 
ATOM   3621 C CB  . THR B 1 166 ? -35.307 33.965  -11.419 1.00  43.64 ? 166  THR A CB  1 
ATOM   3622 O OG1 . THR B 1 166 ? -35.728 35.315  -11.641 1.00  47.08 ? 166  THR A OG1 1 
ATOM   3623 C CG2 . THR B 1 166 ? -34.231 33.939  -10.333 1.00  41.13 ? 166  THR A CG2 1 
ATOM   3624 N N   . ILE B 1 167 ? -33.138 31.602  -12.522 1.00  37.28 ? 167  ILE A N   1 
ATOM   3625 C CA  . ILE B 1 167 ? -32.661 30.287  -12.138 1.00  34.28 ? 167  ILE A CA  1 
ATOM   3626 C C   . ILE B 1 167 ? -32.607 30.198  -10.623 1.00  36.08 ? 167  ILE A C   1 
ATOM   3627 O O   . ILE B 1 167 ? -31.986 31.038  -9.980  1.00  39.17 ? 167  ILE A O   1 
ATOM   3628 C CB  . ILE B 1 167 ? -31.272 30.043  -12.689 1.00  34.65 ? 167  ILE A CB  1 
ATOM   3629 C CG1 . ILE B 1 167 ? -31.226 30.450  -14.168 1.00  37.38 ? 167  ILE A CG1 1 
ATOM   3630 C CG2 . ILE B 1 167 ? -30.881 28.580  -12.471 1.00  34.96 ? 167  ILE A CG2 1 
ATOM   3631 C CD1 . ILE B 1 167 ? -32.348 29.842  -14.999 1.00  38.02 ? 167  ILE A CD1 1 
ATOM   3632 N N   . VAL B 1 168 ? -33.256 29.186  -10.054 1.00  35.21 ? 168  VAL A N   1 
ATOM   3633 C CA  . VAL B 1 168 ? -33.418 29.091  -8.608  1.00  35.80 ? 168  VAL A CA  1 
ATOM   3634 C C   . VAL B 1 168 ? -32.809 27.815  -8.057  1.00  36.21 ? 168  VAL A C   1 
ATOM   3635 O O   . VAL B 1 168 ? -33.078 26.724  -8.561  1.00  31.89 ? 168  VAL A O   1 
ATOM   3636 C CB  . VAL B 1 168 ? -34.910 29.076  -8.198  1.00  36.53 ? 168  VAL A CB  1 
ATOM   3637 C CG1 . VAL B 1 168 ? -35.038 29.001  -6.686  1.00  38.32 ? 168  VAL A CG1 1 
ATOM   3638 C CG2 . VAL B 1 168 ? -35.639 30.288  -8.736  1.00  37.38 ? 168  VAL A CG2 1 
ATOM   3639 N N   . SER B 1 169 ? -31.996 27.955  -7.013  1.00  36.12 ? 169  SER A N   1 
ATOM   3640 C CA  . SER B 1 169 ? -31.448 26.799  -6.317  1.00  35.18 ? 169  SER A CA  1 
ATOM   3641 C C   . SER B 1 169 ? -32.339 26.419  -5.147  1.00  34.86 ? 169  SER A C   1 
ATOM   3642 O O   . SER B 1 169 ? -32.686 27.276  -4.333  1.00  33.67 ? 169  SER A O   1 
ATOM   3643 C CB  . SER B 1 169 ? -30.042 27.091  -5.782  1.00  36.38 ? 169  SER A CB  1 
ATOM   3644 O OG  . SER B 1 169 ? -29.607 26.008  -4.971  1.00  35.60 ? 169  SER A OG  1 
ATOM   3645 N N   . PRO B 1 170 ? -32.671 25.120  -5.041  1.00  32.08 ? 170  PRO A N   1 
ATOM   3646 C CA  . PRO B 1 170 ? -33.511 24.546  -3.986  1.00  35.93 ? 170  PRO A CA  1 
ATOM   3647 C C   . PRO B 1 170 ? -32.824 24.583  -2.625  1.00  37.84 ? 170  PRO A C   1 
ATOM   3648 O O   . PRO B 1 170 ? -33.478 24.381  -1.613  1.00  39.31 ? 170  PRO A O   1 
ATOM   3649 C CB  . PRO B 1 170 ? -33.668 23.083  -4.416  1.00  40.27 ? 170  PRO A CB  1 
ATOM   3650 C CG  . PRO B 1 170 ? -33.201 23.027  -5.850  1.00  41.50 ? 170  PRO A CG  1 
ATOM   3651 C CD  . PRO B 1 170 ? -32.178 24.090  -5.970  1.00  35.90 ? 170  PRO A CD  1 
ATOM   3652 N N   . ASP B 1 171 ? -31.518 24.808  -2.605  1.00  37.42 ? 171  ASP A N   1 
ATOM   3653 C CA  . ASP B 1 171 ? -30.789 24.867  -1.342  1.00  37.48 ? 171  ASP A CA  1 
ATOM   3654 C C   . ASP B 1 171 ? -29.592 25.784  -1.442  1.00  40.36 ? 171  ASP A C   1 
ATOM   3655 O O   . ASP B 1 171 ? -29.270 26.292  -2.520  1.00  37.55 ? 171  ASP A O   1 
ATOM   3656 C CB  . ASP B 1 171 ? -30.362 23.472  -0.860  1.00  42.23 ? 171  ASP A CB  1 
ATOM   3657 C CG  . ASP B 1 171 ? -29.631 22.671  -1.928  1.00  45.74 ? 171  ASP A CG  1 
ATOM   3658 O OD1 . ASP B 1 171 ? -29.663 21.423  -1.855  1.00  51.42 ? 171  ASP A OD1 1 
ATOM   3659 O OD2 . ASP B 1 171 ? -29.027 23.276  -2.841  1.00  43.60 ? 171  ASP A OD2 1 
ATOM   3660 N N   . ALA B 1 172 ? -28.942 26.000  -0.305  1.00  42.60 ? 172  ALA A N   1 
ATOM   3661 C CA  . ALA B 1 172 ? -27.774 26.861  -0.232  1.00  42.47 ? 172  ALA A CA  1 
ATOM   3662 C C   . ALA B 1 172 ? -26.607 26.257  -1.003  1.00  40.97 ? 172  ALA A C   1 
ATOM   3663 O O   . ALA B 1 172 ? -25.895 26.956  -1.725  1.00  45.74 ? 172  ALA A O   1 
ATOM   3664 C CB  . ALA B 1 172 ? -27.385 27.085  1.219   1.00  45.08 ? 172  ALA A CB  1 
ATOM   3665 N N   . GLY B 1 173 ? -26.426 24.952  -0.851  1.00  45.41 ? 173  GLY A N   1 
ATOM   3666 C CA  . GLY B 1 173 ? -25.312 24.260  -1.466  1.00  47.13 ? 173  GLY A CA  1 
ATOM   3667 C C   . GLY B 1 173 ? -25.332 24.271  -2.983  1.00  45.87 ? 173  GLY A C   1 
ATOM   3668 O O   . GLY B 1 173 ? -24.318 23.986  -3.624  1.00  51.49 ? 173  GLY A O   1 
ATOM   3669 N N   . GLY B 1 174 ? -26.479 24.602  -3.565  1.00  40.99 ? 174  GLY A N   1 
ATOM   3670 C CA  . GLY B 1 174 ? -26.625 24.568  -5.010  1.00  42.74 ? 174  GLY A CA  1 
ATOM   3671 C C   . GLY B 1 174 ? -26.278 25.884  -5.673  1.00  39.08 ? 174  GLY A C   1 
ATOM   3672 O O   . GLY B 1 174 ? -26.443 26.044  -6.881  1.00  36.66 ? 174  GLY A O   1 
ATOM   3673 N N   . ALA B 1 175 ? -25.791 26.833  -4.880  1.00  37.47 ? 175  ALA A N   1 
ATOM   3674 C CA  . ALA B 1 175 ? -25.539 28.183  -5.375  1.00  38.82 ? 175  ALA A CA  1 
ATOM   3675 C C   . ALA B 1 175 ? -24.680 28.225  -6.635  1.00  39.94 ? 175  ALA A C   1 
ATOM   3676 O O   . ALA B 1 175 ? -25.043 28.877  -7.618  1.00  40.66 ? 175  ALA A O   1 
ATOM   3677 C CB  . ALA B 1 175 ? -24.916 29.032  -4.290  1.00  40.55 ? 175  ALA A CB  1 
ATOM   3678 N N   . LYS B 1 176 ? -23.541 27.543  -6.604  0.80  36.39 ? 176  LYS A N   1 
ATOM   3679 C CA  . LYS B 1 176 ? -22.582 27.586  -7.711  0.80  36.92 ? 176  LYS A CA  1 
ATOM   3680 C C   . LYS B 1 176 ? -23.196 27.128  -9.029  0.80  35.32 ? 176  LYS A C   1 
ATOM   3681 O O   . LYS B 1 176 ? -22.978 27.732  -10.085 0.80  33.30 ? 176  LYS A O   1 
ATOM   3682 C CB  . LYS B 1 176 ? -21.375 26.710  -7.381  0.80  38.75 ? 176  LYS A CB  1 
ATOM   3683 C CG  . LYS B 1 176 ? -20.042 27.360  -7.668  0.80  43.79 ? 176  LYS A CG  1 
ATOM   3684 C CD  . LYS B 1 176 ? -18.989 26.895  -6.669  0.80  49.46 ? 176  LYS A CD  1 
ATOM   3685 C CE  . LYS B 1 176 ? -17.659 27.595  -6.908  0.80  53.79 ? 176  LYS A CE  1 
ATOM   3686 N NZ  . LYS B 1 176 ? -17.795 29.081  -6.838  0.80  56.00 ? 176  LYS A NZ  1 
ATOM   3687 N N   . ARG B 1 177 ? -23.953 26.043  -8.953  0.70  34.74 ? 177  ARG A N   1 
ATOM   3688 C CA  . ARG B 1 177 ? -24.591 25.451  -10.116 0.70  34.64 ? 177  ARG A CA  1 
ATOM   3689 C C   . ARG B 1 177 ? -25.530 26.438  -10.810 0.70  37.25 ? 177  ARG A C   1 
ATOM   3690 O O   . ARG B 1 177 ? -25.495 26.592  -12.032 0.70  37.65 ? 177  ARG A O   1 
ATOM   3691 C CB  . ARG B 1 177 ? -25.363 24.209  -9.682  0.70  32.89 ? 177  ARG A CB  1 
ATOM   3692 C CG  . ARG B 1 177 ? -25.816 23.306  -10.802 0.70  36.28 ? 177  ARG A CG  1 
ATOM   3693 C CD  . ARG B 1 177 ? -26.607 22.106  -10.269 0.70  36.70 ? 177  ARG A CD  1 
ATOM   3694 N NE  . ARG B 1 177 ? -25.765 21.138  -9.567  0.70  38.15 ? 177  ARG A NE  1 
ATOM   3695 C CZ  . ARG B 1 177 ? -25.630 21.065  -8.244  0.70  41.10 ? 177  ARG A CZ  1 
ATOM   3696 N NH1 . ARG B 1 177 ? -26.284 21.908  -7.451  0.70  34.10 ? 177  ARG A NH1 1 
ATOM   3697 N NH2 . ARG B 1 177 ? -24.839 20.142  -7.708  0.70  37.57 ? 177  ARG A NH2 1 
ATOM   3698 N N   . VAL B 1 178 ? -26.367 27.109  -10.027 1.00  33.83 ? 178  VAL A N   1 
ATOM   3699 C CA  . VAL B 1 178 ? -27.375 28.002  -10.598 1.00  39.53 ? 178  VAL A CA  1 
ATOM   3700 C C   . VAL B 1 178 ? -26.813 29.344  -11.086 1.00  40.16 ? 178  VAL A C   1 
ATOM   3701 O O   . VAL B 1 178 ? -27.235 29.843  -12.129 1.00  38.36 ? 178  VAL A O   1 
ATOM   3702 C CB  . VAL B 1 178 ? -28.574 28.236  -9.639  1.00  39.46 ? 178  VAL A CB  1 
ATOM   3703 C CG1 . VAL B 1 178 ? -29.097 26.907  -9.108  1.00  35.89 ? 178  VAL A CG1 1 
ATOM   3704 C CG2 . VAL B 1 178 ? -28.189 29.164  -8.503  1.00  36.47 ? 178  VAL A CG2 1 
ATOM   3705 N N   . THR B 1 179 ? -25.874 29.935  -10.344 1.00  34.68 ? 179  THR A N   1 
ATOM   3706 C CA  . THR B 1 179 ? -25.240 31.157  -10.824 1.00  35.00 ? 179  THR A CA  1 
ATOM   3707 C C   . THR B 1 179 ? -24.496 30.893  -12.128 1.00  38.19 ? 179  THR A C   1 
ATOM   3708 O O   . THR B 1 179 ? -24.411 31.764  -12.994 1.00  41.50 ? 179  THR A O   1 
ATOM   3709 C CB  . THR B 1 179 ? -24.282 31.797  -9.798  1.00  37.27 ? 179  THR A CB  1 
ATOM   3710 O OG1 . THR B 1 179 ? -23.246 30.871  -9.444  1.00  34.90 ? 179  THR A OG1 1 
ATOM   3711 C CG2 . THR B 1 179 ? -25.042 32.222  -8.555  1.00  34.09 ? 179  THR A CG2 1 
ATOM   3712 N N   . SER B 1 180 ? -23.962 29.687  -12.263 1.00  34.06 ? 180  SER A N   1 
ATOM   3713 C CA  . SER B 1 180 ? -23.314 29.287  -13.505 1.00  40.27 ? 180  SER A CA  1 
ATOM   3714 C C   . SER B 1 180 ? -24.302 29.337  -14.665 1.00  41.62 ? 180  SER A C   1 
ATOM   3715 O O   . SER B 1 180 ? -23.994 29.855  -15.734 1.00  45.38 ? 180  SER A O   1 
ATOM   3716 C CB  . SER B 1 180 ? -22.724 27.883  -13.384 1.00  40.11 ? 180  SER A CB  1 
ATOM   3717 O OG  . SER B 1 180 ? -22.265 27.431  -14.644 1.00  48.44 ? 180  SER A OG  1 
ATOM   3718 N N   . ILE B 1 181 ? -25.497 28.809  -14.443 1.00  40.81 ? 181  ILE A N   1 
ATOM   3719 C CA  . ILE B 1 181 ? -26.506 28.758  -15.489 1.00  40.95 ? 181  ILE A CA  1 
ATOM   3720 C C   . ILE B 1 181 ? -27.103 30.129  -15.755 1.00  43.73 ? 181  ILE A C   1 
ATOM   3721 O O   . ILE B 1 181 ? -27.284 30.526  -16.912 1.00  43.55 ? 181  ILE A O   1 
ATOM   3722 C CB  . ILE B 1 181 ? -27.631 27.774  -15.132 1.00  43.33 ? 181  ILE A CB  1 
ATOM   3723 C CG1 . ILE B 1 181 ? -27.071 26.349  -15.067 1.00  44.33 ? 181  ILE A CG1 1 
ATOM   3724 C CG2 . ILE B 1 181 ? -28.773 27.859  -16.150 1.00  42.71 ? 181  ILE A CG2 1 
ATOM   3725 C CD1 . ILE B 1 181 ? -28.125 25.295  -14.892 1.00  39.85 ? 181  ILE A CD1 1 
ATOM   3726 N N   . ALA B 1 182 ? -27.417 30.843  -14.679 1.00  39.47 ? 182  ALA A N   1 
ATOM   3727 C CA  . ALA B 1 182 ? -27.977 32.183  -14.786 1.00  42.23 ? 182  ALA A CA  1 
ATOM   3728 C C   . ALA B 1 182 ? -27.012 33.114  -15.519 1.00  43.54 ? 182  ALA A C   1 
ATOM   3729 O O   . ALA B 1 182 ? -27.434 34.012  -16.251 1.00  43.65 ? 182  ALA A O   1 
ATOM   3730 C CB  . ALA B 1 182 ? -28.308 32.733  -13.398 1.00  38.12 ? 182  ALA A CB  1 
ATOM   3731 N N   . ASP B 1 183 ? -25.717 32.895  -15.321 1.00  40.75 ? 183  ASP A N   1 
ATOM   3732 C CA  . ASP B 1 183 ? -24.708 33.727  -15.963 1.00  41.95 ? 183  ASP A CA  1 
ATOM   3733 C C   . ASP B 1 183 ? -24.625 33.469  -17.465 1.00  43.80 ? 183  ASP A C   1 
ATOM   3734 O O   . ASP B 1 183 ? -24.530 34.411  -18.253 1.00  43.41 ? 183  ASP A O   1 
ATOM   3735 C CB  . ASP B 1 183 ? -23.342 33.535  -15.316 1.00  42.47 ? 183  ASP A CB  1 
ATOM   3736 C CG  . ASP B 1 183 ? -23.159 34.390  -14.079 1.00  47.09 ? 183  ASP A CG  1 
ATOM   3737 O OD1 . ASP B 1 183 ? -24.053 35.212  -13.784 1.00  46.69 ? 183  ASP A OD1 1 
ATOM   3738 O OD2 . ASP B 1 183 ? -22.109 34.253  -13.414 1.00  46.28 ? 183  ASP A OD2 1 
ATOM   3739 N N   . ARG B 1 184 ? -24.667 32.198  -17.855 0.40  41.96 ? 184  ARG A N   1 
ATOM   3740 C CA  . ARG B 1 184 ? -24.634 31.823  -19.268 0.40  42.26 ? 184  ARG A CA  1 
ATOM   3741 C C   . ARG B 1 184 ? -25.826 32.389  -20.023 0.40  41.05 ? 184  ARG A C   1 
ATOM   3742 O O   . ARG B 1 184 ? -25.709 32.794  -21.177 0.40  41.04 ? 184  ARG A O   1 
ATOM   3743 C CB  . ARG B 1 184 ? -24.611 30.303  -19.420 0.40  41.43 ? 184  ARG A CB  1 
ATOM   3744 C CG  . ARG B 1 184 ? -23.218 29.703  -19.435 0.40  44.77 ? 184  ARG A CG  1 
ATOM   3745 C CD  . ARG B 1 184 ? -22.404 30.194  -18.249 0.40  47.72 ? 184  ARG A CD  1 
ATOM   3746 N NE  . ARG B 1 184 ? -21.374 29.240  -17.840 0.40  51.69 ? 184  ARG A NE  1 
ATOM   3747 C CZ  . ARG B 1 184 ? -20.514 29.452  -16.848 0.40  51.86 ? 184  ARG A CZ  1 
ATOM   3748 N NH1 . ARG B 1 184 ? -20.552 30.590  -16.162 0.40  40.87 ? 184  ARG A NH1 1 
ATOM   3749 N NH2 . ARG B 1 184 ? -19.609 28.528  -16.546 0.40  52.25 ? 184  ARG A NH2 1 
ATOM   3750 N N   . LEU B 1 185 ? -26.973 32.404  -19.355 1.00  42.04 ? 185  LEU A N   1 
ATOM   3751 C CA  . LEU B 1 185 ? -28.215 32.887  -19.941 1.00  40.12 ? 185  LEU A CA  1 
ATOM   3752 C C   . LEU B 1 185 ? -28.324 34.395  -19.807 1.00  46.65 ? 185  LEU A C   1 
ATOM   3753 O O   . LEU B 1 185 ? -29.181 35.021  -20.428 1.00  48.10 ? 185  LEU A O   1 
ATOM   3754 C CB  . LEU B 1 185 ? -29.404 32.262  -19.221 1.00  41.72 ? 185  LEU A CB  1 
ATOM   3755 C CG  . LEU B 1 185 ? -29.693 30.775  -19.389 1.00  42.31 ? 185  LEU A CG  1 
ATOM   3756 C CD1 . LEU B 1 185 ? -30.952 30.407  -18.621 1.00  39.69 ? 185  LEU A CD1 1 
ATOM   3757 C CD2 . LEU B 1 185 ? -29.850 30.440  -20.867 1.00  48.15 ? 185  LEU A CD2 1 
ATOM   3758 N N   . ASN B 1 186 ? -27.459 34.971  -18.978 1.00  44.59 ? 186  ASN A N   1 
ATOM   3759 C CA  . ASN B 1 186 ? -27.580 36.377  -18.601 1.00  49.85 ? 186  ASN A CA  1 
ATOM   3760 C C   . ASN B 1 186 ? -28.941 36.737  -17.999 1.00  45.56 ? 186  ASN A C   1 
ATOM   3761 O O   . ASN B 1 186 ? -29.608 37.663  -18.459 1.00  43.88 ? 186  ASN A O   1 
ATOM   3762 C CB  . ASN B 1 186 ? -27.264 37.288  -19.785 1.00  50.95 ? 186  ASN A CB  1 
ATOM   3763 C CG  . ASN B 1 186 ? -26.021 38.115  -19.551 1.00  59.88 ? 186  ASN A CG  1 
ATOM   3764 O OD1 . ASN B 1 186 ? -26.097 39.249  -19.074 1.00  61.60 ? 186  ASN A OD1 1 
ATOM   3765 N ND2 . ASN B 1 186 ? -24.861 37.542  -19.859 1.00  61.07 ? 186  ASN A ND2 1 
ATOM   3766 N N   . VAL B 1 187 ? -29.345 35.996  -16.972 1.00  42.07 ? 187  VAL A N   1 
ATOM   3767 C CA  . VAL B 1 187 ? -30.584 36.275  -16.260 1.00  38.99 ? 187  VAL A CA  1 
ATOM   3768 C C   . VAL B 1 187 ? -30.350 36.266  -14.743 1.00  43.43 ? 187  VAL A C   1 
ATOM   3769 O O   . VAL B 1 187 ? -29.217 36.164  -14.284 1.00  41.38 ? 187  VAL A O   1 
ATOM   3770 C CB  . VAL B 1 187 ? -31.673 35.257  -16.601 1.00  43.51 ? 187  VAL A CB  1 
ATOM   3771 C CG1 . VAL B 1 187 ? -31.867 35.181  -18.114 1.00  45.04 ? 187  VAL A CG1 1 
ATOM   3772 C CG2 . VAL B 1 187 ? -31.319 33.894  -16.020 1.00  42.38 ? 187  VAL A CG2 1 
ATOM   3773 N N   . ASP B 1 188 ? -31.426 36.371  -13.972 0.90  41.15 ? 188  ASP A N   1 
ATOM   3774 C CA  . ASP B 1 188 ? -31.315 36.436  -12.522 0.90  43.24 ? 188  ASP A CA  1 
ATOM   3775 C C   . ASP B 1 188 ? -31.176 35.055  -11.898 0.90  41.56 ? 188  ASP A C   1 
ATOM   3776 O O   . ASP B 1 188 ? -31.542 34.045  -12.494 0.90  44.23 ? 188  ASP A O   1 
ATOM   3777 C CB  . ASP B 1 188 ? -32.541 37.128  -11.915 0.90  47.50 ? 188  ASP A CB  1 
ATOM   3778 C CG  . ASP B 1 188 ? -32.634 38.593  -12.294 0.90  50.62 ? 188  ASP A CG  1 
ATOM   3779 O OD1 . ASP B 1 188 ? -31.582 39.208  -12.559 0.90  48.60 ? 188  ASP A OD1 1 
ATOM   3780 O OD2 . ASP B 1 188 ? -33.763 39.129  -12.325 0.90  55.33 ? 188  ASP A OD2 1 
ATOM   3781 N N   . PHE B 1 189 ? -30.657 35.019  -10.681 1.00  37.99 ? 189  PHE A N   1 
ATOM   3782 C CA  . PHE B 1 189 ? -30.666 33.785  -9.916  1.00  41.32 ? 189  PHE A CA  1 
ATOM   3783 C C   . PHE B 1 189 ? -31.232 34.093  -8.551  1.00  36.74 ? 189  PHE A C   1 
ATOM   3784 O O   . PHE B 1 189 ? -31.241 35.249  -8.121  1.00  37.07 ? 189  PHE A O   1 
ATOM   3785 C CB  . PHE B 1 189 ? -29.257 33.194  -9.788  1.00  37.29 ? 189  PHE A CB  1 
ATOM   3786 C CG  . PHE B 1 189 ? -28.393 33.900  -8.784  1.00  36.09 ? 189  PHE A CG  1 
ATOM   3787 C CD1 . PHE B 1 189 ? -28.270 33.411  -7.489  1.00  41.52 ? 189  PHE A CD1 1 
ATOM   3788 C CD2 . PHE B 1 189 ? -27.698 35.045  -9.136  1.00  38.54 ? 189  PHE A CD2 1 
ATOM   3789 C CE1 . PHE B 1 189 ? -27.473 34.063  -6.556  1.00  43.24 ? 189  PHE A CE1 1 
ATOM   3790 C CE2 . PHE B 1 189 ? -26.900 35.704  -8.210  1.00  38.54 ? 189  PHE A CE2 1 
ATOM   3791 C CZ  . PHE B 1 189 ? -26.790 35.209  -6.914  1.00  39.03 ? 189  PHE A CZ  1 
ATOM   3792 N N   . ALA B 1 190 ? -31.713 33.061  -7.876  1.00  39.31 ? 190  ALA A N   1 
ATOM   3793 C CA  . ALA B 1 190 ? -32.166 33.197  -6.497  1.00  37.95 ? 190  ALA A CA  1 
ATOM   3794 C C   . ALA B 1 190 ? -31.922 31.886  -5.776  1.00  36.33 ? 190  ALA A C   1 
ATOM   3795 O O   . ALA B 1 190 ? -31.534 30.888  -6.385  1.00  39.72 ? 190  ALA A O   1 
ATOM   3796 C CB  . ALA B 1 190 ? -33.631 33.574  -6.443  1.00  39.17 ? 190  ALA A CB  1 
ATOM   3797 N N   . LEU B 1 191 ? -32.142 31.881  -4.474  1.00  39.83 ? 191  LEU A N   1 
ATOM   3798 C CA  . LEU B 1 191 ? -31.814 30.701  -3.703  1.00  35.01 ? 191  LEU A CA  1 
ATOM   3799 C C   . LEU B 1 191 ? -32.776 30.490  -2.567  1.00  36.79 ? 191  LEU A C   1 
ATOM   3800 O O   . LEU B 1 191 ? -33.239 31.443  -1.942  1.00  40.63 ? 191  LEU A O   1 
ATOM   3801 C CB  . LEU B 1 191 ? -30.379 30.785  -3.187  1.00  42.11 ? 191  LEU A CB  1 
ATOM   3802 C CG  . LEU B 1 191 ? -29.933 29.523  -2.454  1.00  42.38 ? 191  LEU A CG  1 
ATOM   3803 C CD1 . LEU B 1 191 ? -28.504 29.155  -2.825  1.00  46.59 ? 191  LEU A CD1 1 
ATOM   3804 C CD2 . LEU B 1 191 ? -30.112 29.698  -0.942  1.00  43.14 ? 191  LEU A CD2 1 
ATOM   3805 N N   . ILE B 1 192 ? -33.066 29.221  -2.307  1.00  37.41 ? 192  ILE A N   1 
ATOM   3806 C CA  . ILE B 1 192 ? -33.923 28.824  -1.209  1.00  36.80 ? 192  ILE A CA  1 
ATOM   3807 C C   . ILE B 1 192 ? -33.124 28.091  -0.135  1.00  40.38 ? 192  ILE A C   1 
ATOM   3808 O O   . ILE B 1 192 ? -32.200 27.333  -0.432  1.00  38.19 ? 192  ILE A O   1 
ATOM   3809 C CB  . ILE B 1 192 ? -35.061 27.929  -1.714  1.00  39.31 ? 192  ILE A CB  1 
ATOM   3810 C CG1 . ILE B 1 192 ? -35.969 28.731  -2.651  1.00  41.92 ? 192  ILE A CG1 1 
ATOM   3811 C CG2 . ILE B 1 192 ? -35.849 27.354  -0.542  1.00  38.42 ? 192  ILE A CG2 1 
ATOM   3812 C CD1 . ILE B 1 192 ? -37.045 27.907  -3.299  1.00  45.99 ? 192  ILE A CD1 1 
ATOM   3813 N N   . HIS B 1 193 ? -33.485 28.333  1.117   1.00  36.31 ? 193  HIS A N   1 
ATOM   3814 C CA  . HIS B 1 193 ? -32.815 27.714  2.244   1.00  37.25 ? 193  HIS A CA  1 
ATOM   3815 C C   . HIS B 1 193 ? -33.862 27.279  3.254   1.00  41.36 ? 193  HIS A C   1 
ATOM   3816 O O   . HIS B 1 193 ? -34.772 28.045  3.569   1.00  43.26 ? 193  HIS A O   1 
ATOM   3817 C CB  . HIS B 1 193 ? -31.847 28.711  2.888   1.00  41.29 ? 193  HIS A CB  1 
ATOM   3818 C CG  . HIS B 1 193 ? -31.294 28.252  4.201   1.00  37.45 ? 193  HIS A CG  1 
ATOM   3819 N ND1 . HIS B 1 193 ? -30.518 27.124  4.328   1.00  37.55 ? 193  HIS A ND1 1 
ATOM   3820 C CD2 . HIS B 1 193 ? -31.415 28.766  5.450   1.00  40.62 ? 193  HIS A CD2 1 
ATOM   3821 C CE1 . HIS B 1 193 ? -30.173 26.962  5.594   1.00  38.08 ? 193  HIS A CE1 1 
ATOM   3822 N NE2 . HIS B 1 193 ? -30.707 27.948  6.295   1.00  42.65 ? 193  HIS A NE2 1 
ATOM   3823 N N   . LYS B 1 194 ? -33.747 26.053  3.753   0.30  38.69 ? 194  LYS A N   1 
ATOM   3824 C CA  . LYS B 1 194 ? -34.662 25.590  4.783   0.30  40.18 ? 194  LYS A CA  1 
ATOM   3825 C C   . LYS B 1 194 ? -34.093 25.875  6.168   0.30  43.11 ? 194  LYS A C   1 
ATOM   3826 O O   . LYS B 1 194 ? -33.097 25.281  6.583   0.30  41.33 ? 194  LYS A O   1 
ATOM   3827 C CB  . LYS B 1 194 ? -34.992 24.103  4.628   0.30  44.64 ? 194  LYS A CB  1 
ATOM   3828 C CG  . LYS B 1 194 ? -36.317 23.717  5.280   0.30  47.91 ? 194  LYS A CG  1 
ATOM   3829 C CD  . LYS B 1 194 ? -36.608 22.227  5.196   0.30  46.99 ? 194  LYS A CD  1 
ATOM   3830 C CE  . LYS B 1 194 ? -38.028 21.925  5.673   0.30  51.01 ? 194  LYS A CE  1 
ATOM   3831 N NZ  . LYS B 1 194 ? -38.326 20.464  5.771   0.30  52.48 ? 194  LYS A NZ  1 
ATOM   3832 N N   . GLU B 1 195 ? -34.736 26.803  6.869   0.80  44.72 ? 195  GLU A N   1 
ATOM   3833 C CA  . GLU B 1 195 ? -34.337 27.185  8.219   0.80  47.84 ? 195  GLU A CA  1 
ATOM   3834 C C   . GLU B 1 195 ? -34.368 25.985  9.160   0.80  50.13 ? 195  GLU A C   1 
ATOM   3835 O O   . GLU B 1 195 ? -35.376 25.281  9.251   0.80  51.53 ? 195  GLU A O   1 
ATOM   3836 C CB  . GLU B 1 195 ? -35.270 28.268  8.751   0.80  49.07 ? 195  GLU A CB  1 
ATOM   3837 C CG  . GLU B 1 195 ? -34.564 29.434  9.417   0.80  55.17 ? 195  GLU A CG  1 
ATOM   3838 C CD  . GLU B 1 195 ? -34.209 30.529  8.431   0.80  55.74 ? 195  GLU A CD  1 
ATOM   3839 O OE1 . GLU B 1 195 ? -33.521 30.226  7.428   0.80  57.23 ? 195  GLU A OE1 1 
ATOM   3840 O OE2 . GLU B 1 195 ? -34.627 31.688  8.652   0.80  52.25 ? 195  GLU A OE2 1 
ATOM   3841 N N   . ASP B 1 203 ? -39.767 22.899  9.491   0.010 51.38 ? 203  ASP A N   1 
ATOM   3842 C CA  . ASP B 1 203 ? -39.010 24.094  9.139   0.010 50.67 ? 203  ASP A CA  1 
ATOM   3843 C C   . ASP B 1 203 ? -39.834 25.040  8.277   0.010 50.00 ? 203  ASP A C   1 
ATOM   3844 O O   . ASP B 1 203 ? -40.939 24.709  7.845   0.010 49.81 ? 203  ASP A O   1 
ATOM   3845 C CB  . ASP B 1 203 ? -37.742 23.721  8.371   0.010 50.39 ? 203  ASP A CB  1 
ATOM   3846 C CG  . ASP B 1 203 ? -36.890 22.704  9.100   0.010 51.58 ? 203  ASP A CG  1 
ATOM   3847 O OD1 . ASP B 1 203 ? -36.631 22.896  10.305  0.010 52.15 ? 203  ASP A OD1 1 
ATOM   3848 O OD2 . ASP B 1 203 ? -36.475 21.713  8.462   0.010 51.52 ? 203  ASP A OD2 1 
ATOM   3849 N N   . ARG B 1 204 ? -39.280 26.222  8.030   0.010 49.28 ? 204  ARG A N   1 
ATOM   3850 C CA  . ARG B 1 204 ? -39.835 27.145  7.053   0.010 47.97 ? 204  ARG A CA  1 
ATOM   3851 C C   . ARG B 1 204 ? -38.790 27.358  5.970   0.010 46.08 ? 204  ARG A C   1 
ATOM   3852 O O   . ARG B 1 204 ? -37.597 27.189  6.215   0.010 45.97 ? 204  ARG A O   1 
ATOM   3853 C CB  . ARG B 1 204 ? -40.178 28.480  7.706   0.010 49.07 ? 204  ARG A CB  1 
ATOM   3854 C CG  . ARG B 1 204 ? -39.109 29.543  7.519   0.010 49.75 ? 204  ARG A CG  1 
ATOM   3855 C CD  . ARG B 1 204 ? -39.291 30.694  8.491   0.010 51.97 ? 204  ARG A CD  1 
ATOM   3856 N NE  . ARG B 1 204 ? -38.461 31.842  8.141   0.010 53.73 ? 204  ARG A NE  1 
ATOM   3857 C CZ  . ARG B 1 204 ? -38.322 32.922  8.901   0.010 54.90 ? 204  ARG A CZ  1 
ATOM   3858 N NH1 . ARG B 1 204 ? -38.950 33.004  10.066  0.010 55.51 ? 204  ARG A NH1 1 
ATOM   3859 N NH2 . ARG B 1 204 ? -37.550 33.921  8.499   0.010 55.61 ? 204  ARG A NH2 1 
ATOM   3860 N N   . MET B 1 205 ? -39.236 27.713  4.772   0.60  41.43 ? 205  MET A N   1 
ATOM   3861 C CA  . MET B 1 205 ? -38.317 28.004  3.681   0.60  42.45 ? 205  MET A CA  1 
ATOM   3862 C C   . MET B 1 205 ? -38.141 29.505  3.486   0.60  45.78 ? 205  MET A C   1 
ATOM   3863 O O   . MET B 1 205 ? -39.109 30.264  3.484   0.60  44.29 ? 205  MET A O   1 
ATOM   3864 C CB  . MET B 1 205 ? -38.796 27.366  2.371   0.60  42.13 ? 205  MET A CB  1 
ATOM   3865 C CG  . MET B 1 205 ? -38.466 25.891  2.220   0.60  39.10 ? 205  MET A CG  1 
ATOM   3866 S SD  . MET B 1 205 ? -38.743 25.315  0.525   0.60  49.72 ? 205  MET A SD  1 
ATOM   3867 C CE  . MET B 1 205 ? -37.850 23.762  0.525   0.60  48.43 ? 205  MET A CE  1 
ATOM   3868 N N   . VAL B 1 206 ? -36.898 29.930  3.312   1.00  45.04 ? 206  VAL A N   1 
ATOM   3869 C CA  . VAL B 1 206 ? -36.610 31.325  3.024   1.00  44.27 ? 206  VAL A CA  1 
ATOM   3870 C C   . VAL B 1 206 ? -36.129 31.453  1.590   1.00  42.58 ? 206  VAL A C   1 
ATOM   3871 O O   . VAL B 1 206 ? -35.414 30.586  1.091   1.00  40.39 ? 206  VAL A O   1 
ATOM   3872 C CB  . VAL B 1 206 ? -35.529 31.876  3.965   1.00  49.46 ? 206  VAL A CB  1 
ATOM   3873 C CG1 . VAL B 1 206 ? -35.146 33.292  3.564   1.00  49.81 ? 206  VAL A CG1 1 
ATOM   3874 C CG2 . VAL B 1 206 ? -36.008 31.825  5.406   1.00  48.34 ? 206  VAL A CG2 1 
ATOM   3875 N N   . LEU B 1 207 ? -36.526 32.533  0.929   1.00  45.83 ? 207  LEU A N   1 
ATOM   3876 C CA  . LEU B 1 207 ? -36.086 32.799  -0.434  1.00  44.38 ? 207  LEU A CA  1 
ATOM   3877 C C   . LEU B 1 207 ? -35.263 34.079  -0.518  1.00  45.84 ? 207  LEU A C   1 
ATOM   3878 O O   . LEU B 1 207 ? -35.705 35.136  -0.047  1.00  44.46 ? 207  LEU A O   1 
ATOM   3879 C CB  . LEU B 1 207 ? -37.296 32.913  -1.358  1.00  45.54 ? 207  LEU A CB  1 
ATOM   3880 C CG  . LEU B 1 207 ? -37.027 32.944  -2.866  1.00  45.73 ? 207  LEU A CG  1 
ATOM   3881 C CD1 . LEU B 1 207 ? -38.294 32.590  -3.619  1.00  50.45 ? 207  LEU A CD1 1 
ATOM   3882 C CD2 . LEU B 1 207 ? -36.495 34.301  -3.306  1.00  44.65 ? 207  LEU A CD2 1 
ATOM   3883 N N   . VAL B 1 208 ? -34.076 33.990  -1.123  1.00  39.98 ? 208  VAL A N   1 
ATOM   3884 C CA  . VAL B 1 208 ? -33.271 35.177  -1.391  1.00  40.79 ? 208  VAL A CA  1 
ATOM   3885 C C   . VAL B 1 208 ? -33.096 35.410  -2.888  1.00  41.44 ? 208  VAL A C   1 
ATOM   3886 O O   . VAL B 1 208 ? -32.645 34.530  -3.625  1.00  41.30 ? 208  VAL A O   1 
ATOM   3887 C CB  . VAL B 1 208 ? -31.894 35.135  -0.679  1.00  42.66 ? 208  VAL A CB  1 
ATOM   3888 C CG1 . VAL B 1 208 ? -32.052 34.622  0.746   1.00  42.38 ? 208  VAL A CG1 1 
ATOM   3889 C CG2 . VAL B 1 208 ? -30.893 34.285  -1.455  1.00  39.65 ? 208  VAL A CG2 1 
ATOM   3890 N N   . GLY B 1 209 ? -33.463 36.603  -3.336  1.00  41.24 ? 209  GLY A N   1 
ATOM   3891 C CA  . GLY B 1 209 ? -33.411 36.926  -4.747  1.00  45.46 ? 209  GLY A CA  1 
ATOM   3892 C C   . GLY B 1 209 ? -34.804 37.161  -5.290  1.00  47.66 ? 209  GLY A C   1 
ATOM   3893 O O   . GLY B 1 209 ? -35.793 36.768  -4.678  1.00  48.64 ? 209  GLY A O   1 
ATOM   3894 N N   . ASP B 1 210 ? -34.888 37.803  -6.447  1.00  49.44 ? 210  ASP A N   1 
ATOM   3895 C CA  . ASP B 1 210 ? -36.181 38.227  -6.962  1.00  54.58 ? 210  ASP A CA  1 
ATOM   3896 C C   . ASP B 1 210 ? -36.760 37.231  -7.954  1.00  49.18 ? 210  ASP A C   1 
ATOM   3897 O O   . ASP B 1 210 ? -36.070 36.798  -8.878  1.00  52.38 ? 210  ASP A O   1 
ATOM   3898 C CB  . ASP B 1 210 ? -36.065 39.597  -7.621  1.00  56.22 ? 210  ASP A CB  1 
ATOM   3899 C CG  . ASP B 1 210 ? -37.413 40.204  -7.913  1.00  59.89 ? 210  ASP A CG  1 
ATOM   3900 O OD1 . ASP B 1 210 ? -38.325 40.024  -7.072  1.00  53.56 ? 210  ASP A OD1 1 
ATOM   3901 O OD2 . ASP B 1 210 ? -37.560 40.846  -8.980  1.00  61.84 ? 210  ASP A OD2 1 
ATOM   3902 N N   . VAL B 1 211 ? -38.030 36.882  -7.763  1.00  48.27 ? 211  VAL A N   1 
ATOM   3903 C CA  . VAL B 1 211 ? -38.725 35.964  -8.665  1.00  50.58 ? 211  VAL A CA  1 
ATOM   3904 C C   . VAL B 1 211 ? -40.091 36.494  -9.104  1.00  51.34 ? 211  VAL A C   1 
ATOM   3905 O O   . VAL B 1 211 ? -40.765 35.881  -9.931  1.00  53.79 ? 211  VAL A O   1 
ATOM   3906 C CB  . VAL B 1 211 ? -38.947 34.595  -8.002  1.00  48.32 ? 211  VAL A CB  1 
ATOM   3907 C CG1 . VAL B 1 211 ? -37.647 34.095  -7.368  1.00  49.12 ? 211  VAL A CG1 1 
ATOM   3908 C CG2 . VAL B 1 211 ? -40.063 34.682  -6.970  1.00  48.95 ? 211  VAL A CG2 1 
ATOM   3909 N N   . LYS B 1 212 ? -40.490 37.628  -8.541  0.40  49.30 ? 212  LYS A N   1 
ATOM   3910 C CA  . LYS B 1 212 ? -41.816 38.188  -8.761  0.40  49.00 ? 212  LYS A CA  1 
ATOM   3911 C C   . LYS B 1 212 ? -42.106 38.457  -10.240 0.40  50.98 ? 212  LYS A C   1 
ATOM   3912 O O   . LYS B 1 212 ? -41.370 39.185  -10.908 0.40  47.67 ? 212  LYS A O   1 
ATOM   3913 C CB  . LYS B 1 212 ? -41.964 39.480  -7.948  0.40  51.56 ? 212  LYS A CB  1 
ATOM   3914 C CG  . LYS B 1 212 ? -43.385 39.994  -7.809  0.40  52.25 ? 212  LYS A CG  1 
ATOM   3915 C CD  . LYS B 1 212 ? -44.254 39.020  -7.031  0.40  52.17 ? 212  LYS A CD  1 
ATOM   3916 C CE  . LYS B 1 212 ? -45.615 39.623  -6.721  0.40  51.61 ? 212  LYS A CE  1 
ATOM   3917 N NZ  . LYS B 1 212 ? -46.574 38.607  -6.199  0.40  50.41 ? 212  LYS A NZ  1 
ATOM   3918 N N   . ASP B 1 213 ? -43.183 37.854  -10.739 1.00  52.29 ? 213  ASP A N   1 
ATOM   3919 C CA  . ASP B 1 213 ? -43.681 38.098  -12.094 1.00  54.61 ? 213  ASP A CA  1 
ATOM   3920 C C   . ASP B 1 213 ? -42.751 37.575  -13.182 1.00  55.70 ? 213  ASP A C   1 
ATOM   3921 O O   . ASP B 1 213 ? -42.724 38.105  -14.293 1.00  57.61 ? 213  ASP A O   1 
ATOM   3922 C CB  . ASP B 1 213 ? -43.954 39.589  -12.326 1.00  55.65 ? 213  ASP A CB  1 
ATOM   3923 C CG  . ASP B 1 213 ? -44.989 40.149  -11.369 1.00  61.17 ? 213  ASP A CG  1 
ATOM   3924 O OD1 . ASP B 1 213 ? -44.967 41.376  -11.128 1.00  65.84 ? 213  ASP A OD1 1 
ATOM   3925 O OD2 . ASP B 1 213 ? -45.822 39.368  -10.854 1.00  59.81 ? 213  ASP A OD2 1 
ATOM   3926 N N   . ARG B 1 214 ? -41.992 36.534  -12.868 0.40  54.74 ? 214  ARG A N   1 
ATOM   3927 C CA  . ARG B 1 214 ? -41.082 35.952  -13.849 0.40  55.53 ? 214  ARG A CA  1 
ATOM   3928 C C   . ARG B 1 214 ? -41.081 34.416  -13.784 0.40  51.78 ? 214  ARG A C   1 
ATOM   3929 O O   . ARG B 1 214 ? -41.421 33.823  -12.762 0.40  47.79 ? 214  ARG A O   1 
ATOM   3930 C CB  . ARG B 1 214 ? -39.670 36.541  -13.687 0.40  57.32 ? 214  ARG A CB  1 
ATOM   3931 C CG  . ARG B 1 214 ? -39.163 36.555  -12.243 0.40  56.81 ? 214  ARG A CG  1 
ATOM   3932 C CD  . ARG B 1 214 ? -38.146 37.669  -11.970 0.40  56.48 ? 214  ARG A CD  1 
ATOM   3933 N NE  . ARG B 1 214 ? -36.939 37.530  -12.778 0.40  53.21 ? 214  ARG A NE  1 
ATOM   3934 C CZ  . ARG B 1 214 ? -36.551 38.396  -13.709 0.40  57.77 ? 214  ARG A CZ  1 
ATOM   3935 N NH1 . ARG B 1 214 ? -37.275 39.482  -13.952 0.40  60.80 ? 214  ARG A NH1 1 
ATOM   3936 N NH2 . ARG B 1 214 ? -35.430 38.178  -14.396 0.40  53.27 ? 214  ARG A NH2 1 
ATOM   3937 N N   . VAL B 1 215 ? -40.735 33.777  -14.896 1.00  49.17 ? 215  VAL A N   1 
ATOM   3938 C CA  . VAL B 1 215 ? -40.637 32.328  -14.924 1.00  48.28 ? 215  VAL A CA  1 
ATOM   3939 C C   . VAL B 1 215 ? -39.550 31.876  -13.952 1.00  46.76 ? 215  VAL A C   1 
ATOM   3940 O O   . VAL B 1 215 ? -38.449 32.421  -13.949 1.00  46.90 ? 215  VAL A O   1 
ATOM   3941 C CB  . VAL B 1 215 ? -40.312 31.822  -16.341 1.00  48.13 ? 215  VAL A CB  1 
ATOM   3942 C CG1 . VAL B 1 215 ? -40.039 30.320  -16.329 1.00  44.16 ? 215  VAL A CG1 1 
ATOM   3943 C CG2 . VAL B 1 215 ? -41.459 32.154  -17.287 1.00  51.12 ? 215  VAL A CG2 1 
ATOM   3944 N N   . ALA B 1 216 ? -39.864 30.898  -13.112 1.00  41.30 ? 216  ALA A N   1 
ATOM   3945 C CA  . ALA B 1 216 ? -38.869 30.359  -12.189 1.00  45.26 ? 216  ALA A CA  1 
ATOM   3946 C C   . ALA B 1 216 ? -38.438 28.948  -12.580 1.00  43.89 ? 216  ALA A C   1 
ATOM   3947 O O   . ALA B 1 216 ? -39.270 28.045  -12.681 1.00  45.60 ? 216  ALA A O   1 
ATOM   3948 C CB  . ALA B 1 216 ? -39.395 30.372  -10.765 1.00  39.63 ? 216  ALA A CB  1 
ATOM   3949 N N   . ILE B 1 217 ? -37.138 28.767  -12.791 1.00  39.13 ? 217  ILE A N   1 
ATOM   3950 C CA  . ILE B 1 217 ? -36.590 27.453  -13.121 1.00  41.16 ? 217  ILE A CA  1 
ATOM   3951 C C   . ILE B 1 217 ? -35.748 26.887  -11.974 1.00  36.57 ? 217  ILE A C   1 
ATOM   3952 O O   . ILE B 1 217 ? -34.623 27.331  -11.743 1.00  34.37 ? 217  ILE A O   1 
ATOM   3953 C CB  . ILE B 1 217 ? -35.732 27.515  -14.403 1.00  38.17 ? 217  ILE A CB  1 
ATOM   3954 C CG1 . ILE B 1 217 ? -36.506 28.215  -15.518 1.00  36.17 ? 217  ILE A CG1 1 
ATOM   3955 C CG2 . ILE B 1 217 ? -35.310 26.120  -14.845 1.00  39.77 ? 217  ILE A CG2 1 
ATOM   3956 C CD1 . ILE B 1 217 ? -35.629 28.629  -16.685 1.00  37.47 ? 217  ILE A CD1 1 
ATOM   3957 N N   . LEU B 1 218 ? -36.295 25.916  -11.250 1.00  36.41 ? 218  LEU A N   1 
ATOM   3958 C CA  . LEU B 1 218 ? -35.513 25.216  -10.237 1.00  35.84 ? 218  LEU A CA  1 
ATOM   3959 C C   . LEU B 1 218 ? -34.534 24.279  -10.920 1.00  38.13 ? 218  LEU A C   1 
ATOM   3960 O O   . LEU B 1 218 ? -34.925 23.446  -11.742 1.00  36.82 ? 218  LEU A O   1 
ATOM   3961 C CB  . LEU B 1 218 ? -36.412 24.420  -9.292  1.00  35.29 ? 218  LEU A CB  1 
ATOM   3962 C CG  . LEU B 1 218 ? -36.990 25.142  -8.071  1.00  38.96 ? 218  LEU A CG  1 
ATOM   3963 C CD1 . LEU B 1 218 ? -38.267 24.451  -7.589  1.00  41.51 ? 218  LEU A CD1 1 
ATOM   3964 C CD2 . LEU B 1 218 ? -35.965 25.236  -6.935  1.00  37.74 ? 218  LEU A CD2 1 
ATOM   3965 N N   . VAL B 1 219 ? -33.260 24.417  -10.574 1.00  36.14 ? 219  VAL A N   1 
ATOM   3966 C CA  . VAL B 1 219 ? -32.220 23.581  -11.149 1.00  38.48 ? 219  VAL A CA  1 
ATOM   3967 C C   . VAL B 1 219 ? -31.442 22.888  -10.036 1.00  41.03 ? 219  VAL A C   1 
ATOM   3968 O O   . VAL B 1 219 ? -31.015 23.526  -9.063  1.00  39.21 ? 219  VAL A O   1 
ATOM   3969 C CB  . VAL B 1 219 ? -31.275 24.409  -12.041 1.00  41.45 ? 219  VAL A CB  1 
ATOM   3970 C CG1 . VAL B 1 219 ? -30.113 23.555  -12.555 1.00  39.66 ? 219  VAL A CG1 1 
ATOM   3971 C CG2 . VAL B 1 219 ? -32.047 25.021  -13.194 1.00  35.30 ? 219  VAL A CG2 1 
ATOM   3972 N N   . ASP B 1 220 ? -31.280 21.577  -10.174 1.00  40.25 ? 220  ASP A N   1 
ATOM   3973 C CA  . ASP B 1 220 ? -30.589 20.773  -9.171  1.00  41.11 ? 220  ASP A CA  1 
ATOM   3974 C C   . ASP B 1 220 ? -29.869 19.629  -9.871  1.00  44.30 ? 220  ASP A C   1 
ATOM   3975 O O   . ASP B 1 220 ? -30.247 19.237  -10.980 1.00  38.55 ? 220  ASP A O   1 
ATOM   3976 C CB  . ASP B 1 220 ? -31.590 20.218  -8.158  1.00  37.25 ? 220  ASP A CB  1 
ATOM   3977 C CG  . ASP B 1 220 ? -30.992 20.064  -6.771  1.00  47.00 ? 220  ASP A CG  1 
ATOM   3978 O OD1 . ASP B 1 220 ? -29.941 20.687  -6.496  1.00  46.01 ? 220  ASP A OD1 1 
ATOM   3979 O OD2 . ASP B 1 220 ? -31.579 19.328  -5.949  1.00  51.10 ? 220  ASP A OD2 1 
ATOM   3980 N N   . ASP B 1 221 ? -28.835 19.081  -9.241  1.00  39.79 ? 221  ASP A N   1 
ATOM   3981 C CA  . ASP B 1 221 ? -28.102 18.000  -9.896  1.00  41.51 ? 221  ASP A CA  1 
ATOM   3982 C C   . ASP B 1 221 ? -28.910 16.712  -9.855  1.00  39.27 ? 221  ASP A C   1 
ATOM   3983 O O   . ASP B 1 221 ? -28.818 15.881  -10.760 1.00  40.69 ? 221  ASP A O   1 
ATOM   3984 C CB  . ASP B 1 221 ? -26.719 17.794  -9.283  1.00  39.22 ? 221  ASP A CB  1 
ATOM   3985 C CG  . ASP B 1 221 ? -26.784 17.398  -7.831  1.00  40.83 ? 221  ASP A CG  1 
ATOM   3986 O OD1 . ASP B 1 221 ? -26.056 16.459  -7.442  1.00  42.56 ? 221  ASP A OD1 1 
ATOM   3987 O OD2 . ASP B 1 221 ? -27.567 18.023  -7.084  1.00  41.61 ? 221  ASP A OD2 1 
ATOM   3988 N N   . MET B 1 222 ? -29.712 16.559  -8.808  0.81  40.80 ? 222  MET A N   1 
ATOM   3989 C CA  . MET B 1 222 ? -30.529 15.371  -8.664  0.81  39.92 ? 222  MET A CA  1 
ATOM   3990 C C   . MET B 1 222 ? -31.736 15.616  -7.765  0.81  44.69 ? 222  MET A C   1 
ATOM   3991 O O   . MET B 1 222 ? -31.757 16.560  -6.977  0.81  43.12 ? 222  MET A O   1 
ATOM   3992 C CB  . MET B 1 222 ? -29.693 14.214  -8.113  0.81  44.44 ? 222  MET A CB  1 
ATOM   3993 C CG  . MET B 1 222 ? -29.397 14.309  -6.633  0.81  42.88 ? 222  MET A CG  1 
ATOM   3994 S SD  . MET B 1 222 ? -28.391 12.919  -6.084  0.81  51.05 ? 222  MET A SD  1 
ATOM   3995 C CE  . MET B 1 222 ? -26.737 13.530  -6.404  0.81  39.59 ? 222  MET A CE  1 
ATOM   3996 N N   . ALA B 1 223 ? -32.744 14.760  -7.908  1.00  42.50 ? 223  ALA A N   1 
ATOM   3997 C CA  . ALA B 1 223 ? -33.945 14.817  -7.086  1.00  42.82 ? 223  ALA A CA  1 
ATOM   3998 C C   . ALA B 1 223 ? -34.369 13.403  -6.730  1.00  48.17 ? 223  ALA A C   1 
ATOM   3999 O O   . ALA B 1 223 ? -34.555 12.554  -7.606  1.00  46.76 ? 223  ALA A O   1 
ATOM   4000 C CB  . ALA B 1 223 ? -35.057 15.530  -7.809  1.00  45.86 ? 223  ALA A CB  1 
ATOM   4001 N N   . ASP B 1 224 ? -34.502 13.157  -5.434  1.00  47.45 ? 224  ASP A N   1 
ATOM   4002 C CA  . ASP B 1 224 ? -34.814 11.831  -4.940  1.00  52.83 ? 224  ASP A CA  1 
ATOM   4003 C C   . ASP B 1 224 ? -36.212 11.525  -4.432  1.00  53.75 ? 224  ASP A C   1 
ATOM   4004 O O   . ASP B 1 224 ? -36.885 10.629  -4.945  1.00  56.03 ? 224  ASP A O   1 
ATOM   4005 C CB  . ASP B 1 224 ? -33.951 11.496  -3.727  1.00  53.79 ? 224  ASP A CB  1 
ATOM   4006 C CG  . ASP B 1 224 ? -34.139 10.068  -3.272  1.00  52.81 ? 224  ASP A CG  1 
ATOM   4007 O OD1 . ASP B 1 224 ? -34.697 9.281   -4.062  1.00  48.99 ? 224  ASP A OD1 1 
ATOM   4008 O OD2 . ASP B 1 224 ? -33.723 9.736   -2.140  1.00  53.78 ? 224  ASP A OD2 1 
ATOM   4009 N N   . THR B 1 225 ? -36.643 12.272  -3.425  1.00  48.24 ? 225  THR A N   1 
ATOM   4010 C CA  . THR B 1 225 ? -37.979 12.098  -2.869  1.00  55.19 ? 225  THR A CA  1 
ATOM   4011 C C   . THR B 1 225 ? -38.712 13.315  -3.419  1.00  55.15 ? 225  THR A C   1 
ATOM   4012 O O   . THR B 1 225 ? -39.942 13.338  -3.487  1.00  55.91 ? 225  THR A O   1 
ATOM   4013 C CB  . THR B 1 225 ? -38.070 12.103  -1.331  1.00  51.62 ? 225  THR A CB  1 
ATOM   4014 O OG1 . THR B 1 225 ? -37.458 13.287  -0.810  1.00  55.88 ? 225  THR A OG1 1 
ATOM   4015 C CG2 . THR B 1 225 ? -37.359 10.887  -0.752  1.00  53.59 ? 225  THR A CG2 1 
ATOM   4016 N N   . CYS B 1 226 ? -37.945 14.331  -3.802  1.00  49.93 ? 226  CYS A N   1 
ATOM   4017 C CA  . CYS B 1 226 ? -38.507 15.537  -4.398  1.00  54.57 ? 226  CYS A CA  1 
ATOM   4018 C C   . CYS B 1 226 ? -39.223 16.394  -3.366  1.00  50.59 ? 226  CYS A C   1 
ATOM   4019 O O   . CYS B 1 226 ? -39.832 17.398  -3.711  1.00  51.10 ? 226  CYS A O   1 
ATOM   4020 C CB  . CYS B 1 226 ? -39.463 15.184  -5.545  1.00  53.43 ? 226  CYS A CB  1 
ATOM   4021 S SG  . CYS B 1 226 ? -38.657 14.652  -7.074  1.00  51.69 ? 226  CYS A SG  1 
ATOM   4022 N N   . GLY B 1 227 ? -39.145 15.988  -2.103  1.00  52.16 ? 227  GLY A N   1 
ATOM   4023 C CA  . GLY B 1 227 ? -39.761 16.739  -1.026  1.00  57.78 ? 227  GLY A CA  1 
ATOM   4024 C C   . GLY B 1 227 ? -39.254 18.165  -0.992  1.00  55.29 ? 227  GLY A C   1 
ATOM   4025 O O   . GLY B 1 227 ? -40.022 19.114  -0.836  1.00  56.92 ? 227  GLY A O   1 
ATOM   4026 N N   . THR B 1 228 ? -37.947 18.316  -1.147  1.00  56.50 ? 228  THR A N   1 
ATOM   4027 C CA  . THR B 1 228 ? -37.343 19.637  -1.152  1.00  54.45 ? 228  THR A CA  1 
ATOM   4028 C C   . THR B 1 228 ? -37.739 20.419  -2.401  1.00  51.58 ? 228  THR A C   1 
ATOM   4029 O O   . THR B 1 228 ? -38.113 21.587  -2.317  1.00  51.55 ? 228  THR A O   1 
ATOM   4030 C CB  . THR B 1 228 ? -35.808 19.554  -1.035  1.00  57.63 ? 228  THR A CB  1 
ATOM   4031 O OG1 . THR B 1 228 ? -35.457 19.177  0.304   1.00  57.81 ? 228  THR A OG1 1 
ATOM   4032 C CG2 . THR B 1 228 ? -35.171 20.901  -1.355  1.00  51.00 ? 228  THR A CG2 1 
ATOM   4033 N N   . ILE B 1 229 ? -37.676 19.772  -3.560  1.00  52.15 ? 229  ILE A N   1 
ATOM   4034 C CA  . ILE B 1 229 ? -37.941 20.482  -4.806  1.00  51.10 ? 229  ILE A CA  1 
ATOM   4035 C C   . ILE B 1 229 ? -39.407 20.882  -4.935  1.00  51.71 ? 229  ILE A C   1 
ATOM   4036 O O   . ILE B 1 229 ? -39.725 21.894  -5.566  1.00  48.46 ? 229  ILE A O   1 
ATOM   4037 C CB  . ILE B 1 229 ? -37.517 19.679  -6.044  1.00  50.71 ? 229  ILE A CB  1 
ATOM   4038 C CG1 . ILE B 1 229 ? -37.352 20.619  -7.237  1.00  52.81 ? 229  ILE A CG1 1 
ATOM   4039 C CG2 . ILE B 1 229 ? -38.538 18.584  -6.349  1.00  47.93 ? 229  ILE A CG2 1 
ATOM   4040 C CD1 . ILE B 1 229 ? -36.119 20.358  -8.058  1.00  50.53 ? 229  ILE A CD1 1 
ATOM   4041 N N   . CYS B 1 230 ? -40.289 20.093  -4.326  1.00  51.46 ? 230  CYS A N   1 
ATOM   4042 C CA  . CYS B 1 230 ? -41.723 20.365  -4.384  1.00  53.93 ? 230  CYS A CA  1 
ATOM   4043 C C   . CYS B 1 230 ? -42.132 21.464  -3.418  1.00  52.67 ? 230  CYS A C   1 
ATOM   4044 O O   . CYS B 1 230 ? -42.977 22.302  -3.739  1.00  50.13 ? 230  CYS A O   1 
ATOM   4045 C CB  . CYS B 1 230 ? -42.532 19.094  -4.130  1.00  51.75 ? 230  CYS A CB  1 
ATOM   4046 S SG  . CYS B 1 230 ? -42.564 17.979  -5.555  1.00  57.62 ? 230  CYS A SG  1 
ATOM   4047 N N   . HIS B 1 231 ? -41.539 21.459  -2.231  1.00  53.73 ? 231  HIS A N   1 
ATOM   4048 C CA  . HIS B 1 231 ? -41.711 22.578  -1.314  1.00  53.10 ? 231  HIS A CA  1 
ATOM   4049 C C   . HIS B 1 231 ? -41.229 23.869  -1.973  1.00  53.97 ? 231  HIS A C   1 
ATOM   4050 O O   . HIS B 1 231 ? -41.941 24.878  -1.988  1.00  54.19 ? 231  HIS A O   1 
ATOM   4051 C CB  . HIS B 1 231 ? -40.951 22.328  -0.013  1.00  59.29 ? 231  HIS A CB  1 
ATOM   4052 C CG  . HIS B 1 231 ? -41.648 21.380  0.914   1.00  60.72 ? 231  HIS A CG  1 
ATOM   4053 N ND1 . HIS B 1 231 ? -42.923 20.920  0.683   1.00  62.90 ? 231  HIS A ND1 1 
ATOM   4054 C CD2 . HIS B 1 231 ? -41.244 20.817  2.080   1.00  68.30 ? 231  HIS A CD2 1 
ATOM   4055 C CE1 . HIS B 1 231 ? -43.281 20.107  1.667   1.00  64.93 ? 231  HIS A CE1 1 
ATOM   4056 N NE2 . HIS B 1 231 ? -42.282 20.029  2.524   1.00  65.96 ? 231  HIS A NE2 1 
ATOM   4057 N N   . ALA B 1 232 ? -40.021 23.830  -2.528  1.00  49.99 ? 232  ALA A N   1 
ATOM   4058 C CA  . ALA B 1 232 ? -39.446 25.001  -3.173  1.00  46.26 ? 232  ALA A CA  1 
ATOM   4059 C C   . ALA B 1 232 ? -40.411 25.573  -4.195  1.00  49.44 ? 232  ALA A C   1 
ATOM   4060 O O   . ALA B 1 232 ? -40.579 26.790  -4.283  1.00  47.03 ? 232  ALA A O   1 
ATOM   4061 C CB  . ALA B 1 232 ? -38.120 24.657  -3.828  1.00  48.84 ? 232  ALA A CB  1 
ATOM   4062 N N   . ALA B 1 233 ? -41.039 24.690  -4.970  1.00  50.08 ? 233  ALA A N   1 
ATOM   4063 C CA  . ALA B 1 233 ? -42.029 25.106  -5.961  1.00  49.18 ? 233  ALA A CA  1 
ATOM   4064 C C   . ALA B 1 233 ? -43.182 25.877  -5.312  1.00  51.18 ? 233  ALA A C   1 
ATOM   4065 O O   . ALA B 1 233 ? -43.659 26.879  -5.853  1.00  50.22 ? 233  ALA A O   1 
ATOM   4066 C CB  . ALA B 1 233 ? -42.558 23.898  -6.726  1.00  48.77 ? 233  ALA A CB  1 
ATOM   4067 N N   . ASP B 1 234 ? -43.625 25.408  -4.152  1.00  47.78 ? 234  ASP A N   1 
ATOM   4068 C CA  . ASP B 1 234 ? -44.669 26.107  -3.416  1.00  52.93 ? 234  ASP A CA  1 
ATOM   4069 C C   . ASP B 1 234 ? -44.196 27.496  -3.012  1.00  50.43 ? 234  ASP A C   1 
ATOM   4070 O O   . ASP B 1 234 ? -44.903 28.487  -3.216  1.00  47.25 ? 234  ASP A O   1 
ATOM   4071 C CB  . ASP B 1 234 ? -45.094 25.309  -2.187  1.00  51.81 ? 234  ASP A CB  1 
ATOM   4072 C CG  . ASP B 1 234 ? -45.495 23.883  -2.531  1.00  58.82 ? 234  ASP A CG  1 
ATOM   4073 O OD1 . ASP B 1 234 ? -45.890 23.635  -3.696  1.00  57.81 ? 234  ASP A OD1 1 
ATOM   4074 O OD2 . ASP B 1 234 ? -45.413 23.009  -1.638  1.00  61.06 ? 234  ASP A OD2 1 
ATOM   4075 N N   . LYS B 1 235 ? -42.993 27.563  -2.449  1.00  49.39 ? 235  LYS A N   1 
ATOM   4076 C CA  . LYS B 1 235 ? -42.404 28.836  -2.040  1.00  46.59 ? 235  LYS A CA  1 
ATOM   4077 C C   . LYS B 1 235 ? -42.370 29.812  -3.206  1.00  46.45 ? 235  LYS A C   1 
ATOM   4078 O O   . LYS B 1 235 ? -42.812 30.957  -3.092  1.00  47.57 ? 235  LYS A O   1 
ATOM   4079 C CB  . LYS B 1 235 ? -40.979 28.625  -1.521  1.00  49.66 ? 235  LYS A CB  1 
ATOM   4080 C CG  . LYS B 1 235 ? -40.688 29.309  -0.192  1.00  52.39 ? 235  LYS A CG  1 
ATOM   4081 C CD  . LYS B 1 235 ? -40.959 30.799  -0.254  1.00  54.25 ? 235  LYS A CD  1 
ATOM   4082 C CE  . LYS B 1 235 ? -40.574 31.481  1.050   1.00  55.77 ? 235  LYS A CE  1 
ATOM   4083 N NZ  . LYS B 1 235 ? -40.747 32.963  0.986   1.00  57.30 ? 235  LYS A NZ  1 
ATOM   4084 N N   . LEU B 1 236 ? -41.841 29.351  -4.332  1.00  44.46 ? 236  LEU A N   1 
ATOM   4085 C CA  . LEU B 1 236 ? -41.711 30.194  -5.511  1.00  46.23 ? 236  LEU A CA  1 
ATOM   4086 C C   . LEU B 1 236 ? -43.053 30.770  -5.979  1.00  47.36 ? 236  LEU A C   1 
ATOM   4087 O O   . LEU B 1 236 ? -43.143 31.949  -6.312  1.00  47.33 ? 236  LEU A O   1 
ATOM   4088 C CB  . LEU B 1 236 ? -41.017 29.426  -6.639  1.00  47.20 ? 236  LEU A CB  1 
ATOM   4089 C CG  . LEU B 1 236 ? -39.520 29.185  -6.401  1.00  44.68 ? 236  LEU A CG  1 
ATOM   4090 C CD1 . LEU B 1 236 ? -38.921 28.276  -7.483  1.00  42.00 ? 236  LEU A CD1 1 
ATOM   4091 C CD2 . LEU B 1 236 ? -38.775 30.512  -6.331  1.00  39.54 ? 236  LEU A CD2 1 
ATOM   4092 N N   . LEU B 1 237 ? -44.091 29.944  -6.008  1.00  49.54 ? 237  LEU A N   1 
ATOM   4093 C CA  . LEU B 1 237 ? -45.413 30.442  -6.373  1.00  54.61 ? 237  LEU A CA  1 
ATOM   4094 C C   . LEU B 1 237 ? -45.825 31.558  -5.420  1.00  53.02 ? 237  LEU A C   1 
ATOM   4095 O O   . LEU B 1 237 ? -46.273 32.625  -5.847  1.00  55.14 ? 237  LEU A O   1 
ATOM   4096 C CB  . LEU B 1 237 ? -46.459 29.321  -6.362  1.00  52.76 ? 237  LEU A CB  1 
ATOM   4097 C CG  . LEU B 1 237 ? -46.523 28.391  -7.580  1.00  54.03 ? 237  LEU A CG  1 
ATOM   4098 C CD1 . LEU B 1 237 ? -47.889 27.751  -7.669  1.00  57.76 ? 237  LEU A CD1 1 
ATOM   4099 C CD2 . LEU B 1 237 ? -46.229 29.150  -8.864  1.00  53.89 ? 237  LEU A CD2 1 
ATOM   4100 N N   . SER B 1 238 ? -45.658 31.297  -4.128  1.00  54.07 ? 238  SER A N   1 
ATOM   4101 C CA  . SER B 1 238 ? -45.982 32.261  -3.082  1.00  53.48 ? 238  SER A CA  1 
ATOM   4102 C C   . SER B 1 238 ? -45.277 33.596  -3.286  1.00  54.14 ? 238  SER A C   1 
ATOM   4103 O O   . SER B 1 238 ? -45.806 34.649  -2.922  1.00  55.57 ? 238  SER A O   1 
ATOM   4104 C CB  . SER B 1 238 ? -45.612 31.692  -1.716  1.00  52.40 ? 238  SER A CB  1 
ATOM   4105 O OG  . SER B 1 238 ? -46.212 30.422  -1.522  1.00  60.80 ? 238  SER A OG  1 
ATOM   4106 N N   . ALA B 1 239 ? -44.079 33.551  -3.859  1.00  49.47 ? 239  ALA A N   1 
ATOM   4107 C CA  . ALA B 1 239 ? -43.303 34.763  -4.096  1.00  44.65 ? 239  ALA A CA  1 
ATOM   4108 C C   . ALA B 1 239 ? -43.613 35.379  -5.461  1.00  51.79 ? 239  ALA A C   1 
ATOM   4109 O O   . ALA B 1 239 ? -42.932 36.304  -5.904  1.00  50.53 ? 239  ALA A O   1 
ATOM   4110 C CB  . ALA B 1 239 ? -41.816 34.478  -3.960  1.00  43.83 ? 239  ALA A CB  1 
ATOM   4111 N N   . GLY B 1 240 ? -44.631 34.848  -6.132  1.00  52.22 ? 240  GLY A N   1 
ATOM   4112 C CA  . GLY B 1 240 ? -45.151 35.457  -7.342  1.00  47.65 ? 240  GLY A CA  1 
ATOM   4113 C C   . GLY B 1 240 ? -44.485 35.066  -8.648  1.00  53.22 ? 240  GLY A C   1 
ATOM   4114 O O   . GLY B 1 240 ? -44.604 35.782  -9.642  1.00  45.46 ? 240  GLY A O   1 
ATOM   4115 N N   . ALA B 1 241 ? -43.779 33.941  -8.661  1.00  50.62 ? 241  ALA A N   1 
ATOM   4116 C CA  . ALA B 1 241 ? -43.219 33.454  -9.909  1.00  49.96 ? 241  ALA A CA  1 
ATOM   4117 C C   . ALA B 1 241 ? -44.384 33.173  -10.844 1.00  51.14 ? 241  ALA A C   1 
ATOM   4118 O O   . ALA B 1 241 ? -45.400 32.622  -10.423 1.00  50.14 ? 241  ALA A O   1 
ATOM   4119 C CB  . ALA B 1 241 ? -42.400 32.187  -9.678  1.00  48.47 ? 241  ALA A CB  1 
ATOM   4120 N N   . THR B 1 242 ? -44.242 33.559  -12.107 1.00  51.87 ? 242  THR A N   1 
ATOM   4121 C CA  . THR B 1 242 ? -45.299 33.331  -13.091 1.00  50.65 ? 242  THR A CA  1 
ATOM   4122 C C   . THR B 1 242 ? -45.582 31.842  -13.263 1.00  54.17 ? 242  THR A C   1 
ATOM   4123 O O   . THR B 1 242 ? -46.729 31.403  -13.214 1.00  56.11 ? 242  THR A O   1 
ATOM   4124 C CB  . THR B 1 242 ? -44.928 33.921  -14.454 1.00  52.95 ? 242  THR A CB  1 
ATOM   4125 O OG1 . THR B 1 242 ? -44.999 35.352  -14.394 1.00  60.13 ? 242  THR A OG1 1 
ATOM   4126 C CG2 . THR B 1 242 ? -45.889 33.415  -15.523 1.00  59.50 ? 242  THR A CG2 1 
ATOM   4127 N N   . ARG B 1 243 ? -44.518 31.074  -13.472 1.00  51.56 ? 243  ARG A N   1 
ATOM   4128 C CA  . ARG B 1 243 ? -44.606 29.629  -13.646 1.00  55.18 ? 243  ARG A CA  1 
ATOM   4129 C C   . ARG B 1 243 ? -43.311 29.015  -13.125 1.00  49.82 ? 243  ARG A C   1 
ATOM   4130 O O   . ARG B 1 243 ? -42.256 29.646  -13.194 1.00  50.26 ? 243  ARG A O   1 
ATOM   4131 C CB  . ARG B 1 243 ? -44.793 29.288  -15.129 1.00  51.84 ? 243  ARG A CB  1 
ATOM   4132 C CG  . ARG B 1 243 ? -46.073 29.862  -15.714 1.00  62.65 ? 243  ARG A CG  1 
ATOM   4133 C CD  . ARG B 1 243 ? -46.241 29.550  -17.187 1.00  58.43 ? 243  ARG A CD  1 
ATOM   4134 N NE  . ARG B 1 243 ? -45.218 30.180  -18.016 1.00  60.50 ? 243  ARG A NE  1 
ATOM   4135 C CZ  . ARG B 1 243 ? -44.369 29.494  -18.770 1.00  56.90 ? 243  ARG A CZ  1 
ATOM   4136 N NH1 . ARG B 1 243 ? -44.442 28.172  -18.779 1.00  55.36 ? 243  ARG A NH1 1 
ATOM   4137 N NH2 . ARG B 1 243 ? -43.459 30.117  -19.509 1.00  52.13 ? 243  ARG A NH2 1 
ATOM   4138 N N   . VAL B 1 244 ? -43.380 27.795  -12.604 1.00  47.09 ? 244  VAL A N   1 
ATOM   4139 C CA  . VAL B 1 244 ? -42.173 27.151  -12.097 1.00  48.17 ? 244  VAL A CA  1 
ATOM   4140 C C   . VAL B 1 244 ? -41.827 25.870  -12.852 1.00  46.54 ? 244  VAL A C   1 
ATOM   4141 O O   . VAL B 1 244 ? -42.697 25.035  -13.113 1.00  48.18 ? 244  VAL A O   1 
ATOM   4142 C CB  . VAL B 1 244 ? -42.258 26.857  -10.581 1.00  47.68 ? 244  VAL A CB  1 
ATOM   4143 C CG1 . VAL B 1 244 ? -43.389 25.908  -10.290 1.00  53.24 ? 244  VAL A CG1 1 
ATOM   4144 C CG2 . VAL B 1 244 ? -40.941 26.272  -10.084 1.00  46.03 ? 244  VAL A CG2 1 
ATOM   4145 N N   . TYR B 1 245 ? -40.553 25.735  -13.205 0.50  41.45 ? 245  TYR A N   1 
ATOM   4146 C CA  . TYR B 1 245 ? -40.037 24.519  -13.812 0.50  41.81 ? 245  TYR A CA  1 
ATOM   4147 C C   . TYR B 1 245 ? -39.024 23.889  -12.867 0.50  40.47 ? 245  TYR A C   1 
ATOM   4148 O O   . TYR B 1 245 ? -38.486 24.561  -11.989 0.50  36.65 ? 245  TYR A O   1 
ATOM   4149 C CB  . TYR B 1 245 ? -39.338 24.829  -15.133 0.50  40.63 ? 245  TYR A CB  1 
ATOM   4150 C CG  . TYR B 1 245 ? -40.241 25.318  -16.243 0.50  43.19 ? 245  TYR A CG  1 
ATOM   4151 C CD1 . TYR B 1 245 ? -40.709 26.624  -16.257 0.50  41.80 ? 245  TYR A CD1 1 
ATOM   4152 C CD2 . TYR B 1 245 ? -40.599 24.481  -17.291 0.50  41.74 ? 245  TYR A CD2 1 
ATOM   4153 C CE1 . TYR B 1 245 ? -41.522 27.080  -17.269 0.50  43.09 ? 245  TYR A CE1 1 
ATOM   4154 C CE2 . TYR B 1 245 ? -41.413 24.930  -18.311 0.50  41.86 ? 245  TYR A CE2 1 
ATOM   4155 C CZ  . TYR B 1 245 ? -41.871 26.232  -18.293 0.50  45.74 ? 245  TYR A CZ  1 
ATOM   4156 O OH  . TYR B 1 245 ? -42.677 26.689  -19.304 0.50  44.38 ? 245  TYR A OH  1 
ATOM   4157 N N   . ALA B 1 246 ? -38.758 22.602  -13.062 1.00  41.57 ? 246  ALA A N   1 
ATOM   4158 C CA  . ALA B 1 246 ? -37.702 21.912  -12.324 1.00  42.14 ? 246  ALA A CA  1 
ATOM   4159 C C   . ALA B 1 246 ? -36.802 21.160  -13.296 1.00  44.21 ? 246  ALA A C   1 
ATOM   4160 O O   . ALA B 1 246 ? -37.276 20.329  -14.074 1.00  40.20 ? 246  ALA A O   1 
ATOM   4161 C CB  . ALA B 1 246 ? -38.295 20.962  -11.308 1.00  42.87 ? 246  ALA A CB  1 
ATOM   4162 N N   . ILE B 1 247 ? -35.507 21.468  -13.262 1.00  36.78 ? 247  ILE A N   1 
ATOM   4163 C CA  . ILE B 1 247 ? -34.538 20.814  -14.140 1.00  38.86 ? 247  ILE A CA  1 
ATOM   4164 C C   . ILE B 1 247 ? -33.498 20.072  -13.305 1.00  40.09 ? 247  ILE A C   1 
ATOM   4165 O O   . ILE B 1 247 ? -32.786 20.665  -12.481 1.00  39.81 ? 247  ILE A O   1 
ATOM   4166 C CB  . ILE B 1 247 ? -33.875 21.816  -15.108 1.00  37.74 ? 247  ILE A CB  1 
ATOM   4167 C CG1 . ILE B 1 247 ? -34.955 22.596  -15.868 1.00  38.75 ? 247  ILE A CG1 1 
ATOM   4168 C CG2 . ILE B 1 247 ? -32.955 21.101  -16.094 1.00  35.28 ? 247  ILE A CG2 1 
ATOM   4169 C CD1 . ILE B 1 247 ? -34.417 23.414  -17.020 1.00  38.37 ? 247  ILE A CD1 1 
ATOM   4170 N N   . LEU B 1 248 ? -33.452 18.762  -13.499 1.00  38.58 ? 248  LEU A N   1 
ATOM   4171 C CA  . LEU B 1 248 ? -32.634 17.873  -12.687 1.00  35.84 ? 248  LEU A CA  1 
ATOM   4172 C C   . LEU B 1 248 ? -31.830 17.040  -13.651 1.00  43.29 ? 248  LEU A C   1 
ATOM   4173 O O   . LEU B 1 248 ? -32.373 16.554  -14.648 1.00  43.59 ? 248  LEU A O   1 
ATOM   4174 C CB  . LEU B 1 248 ? -33.535 16.946  -11.886 1.00  37.50 ? 248  LEU A CB  1 
ATOM   4175 C CG  . LEU B 1 248 ? -34.639 17.648  -11.096 1.00  43.39 ? 248  LEU A CG  1 
ATOM   4176 C CD1 . LEU B 1 248 ? -35.801 16.714  -10.813 1.00  45.41 ? 248  LEU A CD1 1 
ATOM   4177 C CD2 . LEU B 1 248 ? -34.066 18.219  -9.803  1.00  48.19 ? 248  LEU A CD2 1 
ATOM   4178 N N   . THR B 1 249 ? -30.540 16.865  -13.398 1.00  38.17 ? 249  THR A N   1 
ATOM   4179 C CA  . THR B 1 249 ? -29.787 16.036  -14.327 1.00  40.15 ? 249  THR A CA  1 
ATOM   4180 C C   . THR B 1 249 ? -30.055 14.552  -14.053 1.00  39.07 ? 249  THR A C   1 
ATOM   4181 O O   . THR B 1 249 ? -30.274 13.757  -14.986 1.00  38.84 ? 249  THR A O   1 
ATOM   4182 C CB  . THR B 1 249 ? -28.294 16.392  -14.361 1.00  37.68 ? 249  THR A CB  1 
ATOM   4183 O OG1 . THR B 1 249 ? -27.512 15.194  -14.297 1.00  45.61 ? 249  THR A OG1 1 
ATOM   4184 C CG2 . THR B 1 249 ? -27.949 17.307  -13.213 1.00  44.91 ? 249  THR A CG2 1 
ATOM   4185 N N   . HIS B 1 250 ? -30.085 14.197  -12.772 1.00  38.77 ? 250  HIS A N   1 
ATOM   4186 C CA  . HIS B 1 250 ? -30.341 12.828  -12.357 1.00  38.27 ? 250  HIS A CA  1 
ATOM   4187 C C   . HIS B 1 250 ? -31.709 12.747  -11.705 1.00  38.93 ? 250  HIS A C   1 
ATOM   4188 O O   . HIS B 1 250 ? -31.901 13.242  -10.588 1.00  41.05 ? 250  HIS A O   1 
ATOM   4189 C CB  . HIS B 1 250 ? -29.269 12.363  -11.366 1.00  37.78 ? 250  HIS A CB  1 
ATOM   4190 C CG  . HIS B 1 250 ? -27.869 12.482  -11.886 1.00  36.32 ? 250  HIS A CG  1 
ATOM   4191 N ND1 . HIS B 1 250 ? -27.393 11.718  -12.928 1.00  34.39 ? 250  HIS A ND1 1 
ATOM   4192 C CD2 . HIS B 1 250 ? -26.835 13.273  -11.498 1.00  35.68 ? 250  HIS A CD2 1 
ATOM   4193 C CE1 . HIS B 1 250 ? -26.133 12.040  -13.173 1.00  32.15 ? 250  HIS A CE1 1 
ATOM   4194 N NE2 . HIS B 1 250 ? -25.774 12.982  -12.317 1.00  34.74 ? 250  HIS A NE2 1 
ATOM   4195 N N   . GLY B 1 251 ? -32.662 12.133  -12.401 1.00  40.40 ? 251  GLY A N   1 
ATOM   4196 C CA  . GLY B 1 251 ? -34.006 11.958  -11.863 1.00  43.61 ? 251  GLY A CA  1 
ATOM   4197 C C   . GLY B 1 251 ? -34.193 10.633  -11.138 1.00  48.36 ? 251  GLY A C   1 
ATOM   4198 O O   . GLY B 1 251 ? -34.650 9.647   -11.724 1.00  42.41 ? 251  GLY A O   1 
ATOM   4199 N N   . ILE B 1 252 ? -33.831 10.598  -9.858  1.00  43.08 ? 252  ILE A N   1 
ATOM   4200 C CA  . ILE B 1 252 ? -33.985 9.381   -9.066  1.00  45.56 ? 252  ILE A CA  1 
ATOM   4201 C C   . ILE B 1 252 ? -35.469 9.094   -8.792  1.00  47.43 ? 252  ILE A C   1 
ATOM   4202 O O   . ILE B 1 252 ? -35.946 7.983   -9.012  1.00  46.46 ? 252  ILE A O   1 
ATOM   4203 C CB  . ILE B 1 252 ? -33.174 9.458   -7.755  1.00  49.13 ? 252  ILE A CB  1 
ATOM   4204 C CG1 . ILE B 1 252 ? -31.706 9.777   -8.076  1.00  48.14 ? 252  ILE A CG1 1 
ATOM   4205 C CG2 . ILE B 1 252 ? -33.302 8.156   -6.969  1.00  45.42 ? 252  ILE A CG2 1 
ATOM   4206 C CD1 . ILE B 1 252 ? -30.824 9.993   -6.871  1.00  50.15 ? 252  ILE A CD1 1 
ATOM   4207 N N   . PHE B 1 253 ? -36.196 10.104  -8.328  1.00  45.93 ? 253  PHE A N   1 
ATOM   4208 C CA  . PHE B 1 253 ? -37.655 10.015  -8.190  1.00  49.10 ? 253  PHE A CA  1 
ATOM   4209 C C   . PHE B 1 253 ? -38.159 8.785   -7.436  1.00  50.64 ? 253  PHE A C   1 
ATOM   4210 O O   . PHE B 1 253 ? -39.034 8.073   -7.926  1.00  47.38 ? 253  PHE A O   1 
ATOM   4211 C CB  . PHE B 1 253 ? -38.319 10.054  -9.568  1.00  48.36 ? 253  PHE A CB  1 
ATOM   4212 C CG  . PHE B 1 253 ? -38.076 11.330  -10.322 1.00  47.66 ? 253  PHE A CG  1 
ATOM   4213 C CD1 . PHE B 1 253 ? -38.056 11.339  -11.706 1.00  50.98 ? 253  PHE A CD1 1 
ATOM   4214 C CD2 . PHE B 1 253 ? -37.878 12.520  -9.649  1.00  48.60 ? 253  PHE A CD2 1 
ATOM   4215 C CE1 . PHE B 1 253 ? -37.841 12.513  -12.404 1.00  47.78 ? 253  PHE A CE1 1 
ATOM   4216 C CE2 . PHE B 1 253 ? -37.662 13.695  -10.344 1.00  49.06 ? 253  PHE A CE2 1 
ATOM   4217 C CZ  . PHE B 1 253 ? -37.640 13.691  -11.717 1.00  47.36 ? 253  PHE A CZ  1 
ATOM   4218 N N   . SER B 1 254 ? -37.627 8.537   -6.245  1.00  47.10 ? 254  SER A N   1 
ATOM   4219 C CA  . SER B 1 254 ? -38.085 7.387   -5.471  1.00  53.91 ? 254  SER A CA  1 
ATOM   4220 C C   . SER B 1 254 ? -39.118 7.783   -4.424  1.00  59.14 ? 254  SER A C   1 
ATOM   4221 O O   . SER B 1 254 ? -39.313 8.968   -4.138  1.00  59.46 ? 254  SER A O   1 
ATOM   4222 C CB  . SER B 1 254 ? -36.910 6.682   -4.797  1.00  51.84 ? 254  SER A CB  1 
ATOM   4223 O OG  . SER B 1 254 ? -36.373 7.478   -3.758  1.00  53.58 ? 254  SER A OG  1 
ATOM   4224 N N   . GLY B 1 255 ? -39.771 6.779   -3.848  1.00  60.95 ? 255  GLY A N   1 
ATOM   4225 C CA  . GLY B 1 255 ? -40.766 7.011   -2.819  1.00  60.81 ? 255  GLY A CA  1 
ATOM   4226 C C   . GLY B 1 255 ? -41.959 7.778   -3.356  1.00  60.78 ? 255  GLY A C   1 
ATOM   4227 O O   . GLY B 1 255 ? -42.477 7.459   -4.432  1.00  59.24 ? 255  GLY A O   1 
ATOM   4228 N N   . PRO B 1 256 ? -42.395 8.805   -2.610  1.00  60.04 ? 256  PRO A N   1 
ATOM   4229 C CA  . PRO B 1 256 ? -43.529 9.668   -2.963  1.00  59.41 ? 256  PRO A CA  1 
ATOM   4230 C C   . PRO B 1 256 ? -43.216 10.629  -4.114  1.00  60.01 ? 256  PRO A C   1 
ATOM   4231 O O   . PRO B 1 256 ? -44.107 11.348  -4.565  1.00  60.02 ? 256  PRO A O   1 
ATOM   4232 C CB  . PRO B 1 256 ? -43.765 10.461  -1.677  1.00  59.32 ? 256  PRO A CB  1 
ATOM   4233 C CG  . PRO B 1 256 ? -42.431 10.500  -1.015  1.00  63.44 ? 256  PRO A CG  1 
ATOM   4234 C CD  . PRO B 1 256 ? -41.804 9.171   -1.311  1.00  60.56 ? 256  PRO A CD  1 
ATOM   4235 N N   . ALA B 1 257 ? -41.970 10.634  -4.579  1.00  59.68 ? 257  ALA A N   1 
ATOM   4236 C CA  . ALA B 1 257 ? -41.527 11.587  -5.596  1.00  56.92 ? 257  ALA A CA  1 
ATOM   4237 C C   . ALA B 1 257 ? -42.591 11.842  -6.650  1.00  59.26 ? 257  ALA A C   1 
ATOM   4238 O O   . ALA B 1 257 ? -43.081 12.961  -6.797  1.00  58.89 ? 257  ALA A O   1 
ATOM   4239 C CB  . ALA B 1 257 ? -40.238 11.108  -6.255  1.00  53.94 ? 257  ALA A CB  1 
ATOM   4240 N N   . ILE B 1 258 ? -42.950 10.789  -7.377  1.00  60.70 ? 258  ILE A N   1 
ATOM   4241 C CA  . ILE B 1 258 ? -43.825 10.916  -8.537  1.00  60.44 ? 258  ILE A CA  1 
ATOM   4242 C C   . ILE B 1 258 ? -45.195 11.537  -8.226  1.00  63.17 ? 258  ILE A C   1 
ATOM   4243 O O   . ILE B 1 258 ? -45.728 12.308  -9.026  1.00  59.33 ? 258  ILE A O   1 
ATOM   4244 C CB  . ILE B 1 258 ? -44.016 9.561   -9.230  1.00  62.11 ? 258  ILE A CB  1 
ATOM   4245 C CG1 . ILE B 1 258 ? -42.673 9.054   -9.762  1.00  59.22 ? 258  ILE A CG1 1 
ATOM   4246 C CG2 . ILE B 1 258 ? -45.034 9.680   -10.357 1.00  63.98 ? 258  ILE A CG2 1 
ATOM   4247 C CD1 . ILE B 1 258 ? -42.008 9.999   -10.745 1.00  56.52 ? 258  ILE A CD1 1 
ATOM   4248 N N   . SER B 1 259 ? -45.759 11.207  -7.068  1.00  61.01 ? 259  SER A N   1 
ATOM   4249 C CA  . SER B 1 259 ? -47.061 11.741  -6.695  1.00  62.88 ? 259  SER A CA  1 
ATOM   4250 C C   . SER B 1 259 ? -46.918 13.149  -6.134  1.00  61.23 ? 259  SER A C   1 
ATOM   4251 O O   . SER B 1 259 ? -47.844 13.952  -6.199  1.00  59.39 ? 259  SER A O   1 
ATOM   4252 C CB  . SER B 1 259 ? -47.760 10.835  -5.678  1.00  62.17 ? 259  SER A CB  1 
ATOM   4253 O OG  . SER B 1 259 ? -47.138 10.918  -4.406  1.00  60.02 ? 259  SER A OG  1 
ATOM   4254 N N   . ARG B 1 260 ? -45.753 13.444  -5.571  1.00  61.63 ? 260  ARG A N   1 
ATOM   4255 C CA  . ARG B 1 260 ? -45.474 14.796  -5.113  1.00  63.67 ? 260  ARG A CA  1 
ATOM   4256 C C   . ARG B 1 260 ? -45.381 15.739  -6.319  1.00  60.10 ? 260  ARG A C   1 
ATOM   4257 O O   . ARG B 1 260 ? -45.741 16.911  -6.232  1.00  57.45 ? 260  ARG A O   1 
ATOM   4258 C CB  . ARG B 1 260 ? -44.184 14.838  -4.281  1.00  63.02 ? 260  ARG A CB  1 
ATOM   4259 C CG  . ARG B 1 260 ? -44.293 14.162  -2.914  1.00  63.15 ? 260  ARG A CG  1 
ATOM   4260 C CD  . ARG B 1 260 ? -42.957 14.173  -2.177  1.00  60.96 ? 260  ARG A CD  1 
ATOM   4261 N NE  . ARG B 1 260 ? -43.089 13.773  -0.774  1.00  66.66 ? 260  ARG A NE  1 
ATOM   4262 C CZ  . ARG B 1 260 ? -42.068 13.644  0.072   1.00  63.87 ? 260  ARG A CZ  1 
ATOM   4263 N NH1 . ARG B 1 260 ? -40.827 13.873  -0.340  1.00  58.10 ? 260  ARG A NH1 1 
ATOM   4264 N NH2 . ARG B 1 260 ? -42.286 13.277  1.329   1.00  62.86 ? 260  ARG A NH2 1 
ATOM   4265 N N   . ILE B 1 261 ? -44.918 15.212  -7.451  1.00  59.81 ? 261  ILE A N   1 
ATOM   4266 C CA  . ILE B 1 261 ? -44.718 16.032  -8.645  1.00  59.86 ? 261  ILE A CA  1 
ATOM   4267 C C   . ILE B 1 261 ? -46.029 16.413  -9.329  1.00  60.95 ? 261  ILE A C   1 
ATOM   4268 O O   . ILE B 1 261 ? -46.303 17.595  -9.539  1.00  62.58 ? 261  ILE A O   1 
ATOM   4269 C CB  . ILE B 1 261 ? -43.798 15.355  -9.662  1.00  55.64 ? 261  ILE A CB  1 
ATOM   4270 C CG1 . ILE B 1 261 ? -42.386 15.214  -9.095  1.00  57.85 ? 261  ILE A CG1 1 
ATOM   4271 C CG2 . ILE B 1 261 ? -43.754 16.159  -10.939 1.00  51.95 ? 261  ILE A CG2 1 
ATOM   4272 C CD1 . ILE B 1 261 ? -41.383 14.692  -10.104 1.00  53.28 ? 261  ILE A CD1 1 
ATOM   4273 N N   . ASN B 1 262 ? -46.828 15.417  -9.695  1.00  60.88 ? 262  ASN A N   1 
ATOM   4274 C CA  . ASN B 1 262 ? -48.176 15.687  -10.185 1.00  60.33 ? 262  ASN A CA  1 
ATOM   4275 C C   . ASN B 1 262 ? -48.853 16.677  -9.248  1.00  63.22 ? 262  ASN A C   1 
ATOM   4276 O O   . ASN B 1 262 ? -49.319 17.733  -9.673  1.00  65.34 ? 262  ASN A O   1 
ATOM   4277 C CB  . ASN B 1 262 ? -49.001 14.403  -10.236 1.00  61.36 ? 262  ASN A CB  1 
ATOM   4278 C CG  . ASN B 1 262 ? -48.409 13.364  -11.168 1.00  65.25 ? 262  ASN A CG  1 
ATOM   4279 O OD1 . ASN B 1 262 ? -48.069 13.656  -12.321 1.00  61.69 ? 262  ASN A OD1 1 
ATOM   4280 N ND2 . ASN B 1 262 ? -48.277 12.139  -10.669 1.00  62.99 ? 262  ASN A ND2 1 
ATOM   4281 N N   . ASN B 1 263 ? -48.874 16.322  -7.964  1.00  60.63 ? 263  ASN A N   1 
ATOM   4282 C CA  . ASN B 1 263 ? -49.478 17.136  -6.912  1.00  62.40 ? 263  ASN A CA  1 
ATOM   4283 C C   . ASN B 1 263 ? -48.889 18.534  -6.756  1.00  65.22 ? 263  ASN A C   1 
ATOM   4284 O O   . ASN B 1 263 ? -49.317 19.300  -5.885  1.00  63.30 ? 263  ASN A O   1 
ATOM   4285 C CB  . ASN B 1 263 ? -49.368 16.416  -5.571  1.00  61.44 ? 263  ASN A CB  1 
ATOM   4286 C CG  . ASN B 1 263 ? -50.652 15.738  -5.171  1.00  67.10 ? 263  ASN A CG  1 
ATOM   4287 O OD1 . ASN B 1 263 ? -51.736 16.157  -5.576  1.00  67.33 ? 263  ASN A OD1 1 
ATOM   4288 N ND2 . ASN B 1 263 ? -50.544 14.685  -4.365  1.00  72.36 ? 263  ASN A ND2 1 
ATOM   4289 N N   . ALA B 1 264 ? -47.899 18.857  -7.582  1.00  61.77 ? 264  ALA A N   1 
ATOM   4290 C CA  . ALA B 1 264 ? -47.233 20.149  -7.496  1.00  61.26 ? 264  ALA A CA  1 
ATOM   4291 C C   . ALA B 1 264 ? -47.521 20.990  -8.730  1.00  59.41 ? 264  ALA A C   1 
ATOM   4292 O O   . ALA B 1 264 ? -48.136 20.520  -9.690  1.00  60.29 ? 264  ALA A O   1 
ATOM   4293 C CB  . ALA B 1 264 ? -45.729 19.965  -7.309  1.00  61.56 ? 264  ALA A CB  1 
ATOM   4294 N N   . CYS B 1 265 ? -47.061 22.235  -8.701  1.00  54.32 ? 265  CYS A N   1 
ATOM   4295 C CA  . CYS B 1 265 ? -47.407 23.205  -9.731  1.00  56.46 ? 265  CYS A CA  1 
ATOM   4296 C C   . CYS B 1 265 ? -46.418 23.238  -10.895 1.00  59.11 ? 265  CYS A C   1 
ATOM   4297 O O   . CYS B 1 265 ? -46.534 24.085  -11.785 1.00  60.09 ? 265  CYS A O   1 
ATOM   4298 C CB  . CYS B 1 265 ? -47.508 24.593  -9.108  1.00  57.11 ? 265  CYS A CB  1 
ATOM   4299 S SG  . CYS B 1 265 ? -46.106 24.972  -8.023  1.00  72.21 ? 265  CYS A SG  1 
ATOM   4300 N N   . PHE B 1 266 ? -45.445 22.329  -10.898 1.00  52.39 ? 266  PHE A N   1 
ATOM   4301 C CA  . PHE B 1 266 ? -44.452 22.335  -11.964 1.00  51.20 ? 266  PHE A CA  1 
ATOM   4302 C C   . PHE B 1 266 ? -45.131 22.365  -13.323 1.00  50.31 ? 266  PHE A C   1 
ATOM   4303 O O   . PHE B 1 266 ? -45.952 21.506  -13.632 1.00  53.48 ? 266  PHE A O   1 
ATOM   4304 C CB  . PHE B 1 266 ? -43.518 21.119  -11.878 1.00  50.65 ? 266  PHE A CB  1 
ATOM   4305 C CG  . PHE B 1 266 ? -42.700 21.068  -10.619 1.00  47.88 ? 266  PHE A CG  1 
ATOM   4306 C CD1 . PHE B 1 266 ? -42.880 20.044  -9.705  1.00  45.55 ? 266  PHE A CD1 1 
ATOM   4307 C CD2 . PHE B 1 266 ? -41.753 22.048  -10.349 1.00  45.56 ? 266  PHE A CD2 1 
ATOM   4308 C CE1 . PHE B 1 266 ? -42.131 19.993  -8.539  1.00  51.09 ? 266  PHE A CE1 1 
ATOM   4309 C CE2 . PHE B 1 266 ? -40.999 22.004  -9.180  1.00  47.36 ? 266  PHE A CE2 1 
ATOM   4310 C CZ  . PHE B 1 266 ? -41.192 20.978  -8.276  1.00  44.53 ? 266  PHE A CZ  1 
ATOM   4311 N N   . GLU B 1 267 ? -44.798 23.371  -14.121 1.00  50.38 ? 267  GLU A N   1 
ATOM   4312 C CA  . GLU B 1 267 ? -45.186 23.394  -15.518 1.00  45.67 ? 267  GLU A CA  1 
ATOM   4313 C C   . GLU B 1 267 ? -44.580 22.187  -16.223 1.00  51.55 ? 267  GLU A C   1 
ATOM   4314 O O   . GLU B 1 267 ? -45.119 21.679  -17.209 1.00  49.77 ? 267  GLU A O   1 
ATOM   4315 C CB  . GLU B 1 267 ? -44.698 24.680  -16.177 1.00  47.55 ? 267  GLU A CB  1 
ATOM   4316 C CG  . GLU B 1 267 ? -44.862 24.691  -17.686 1.00  54.43 ? 267  GLU A CG  1 
ATOM   4317 C CD  . GLU B 1 267 ? -46.301 24.440  -18.122 1.00  57.24 ? 267  GLU A CD  1 
ATOM   4318 O OE1 . GLU B 1 267 ? -47.210 24.549  -17.271 1.00  54.11 ? 267  GLU A OE1 1 
ATOM   4319 O OE2 . GLU B 1 267 ? -46.516 24.130  -19.313 1.00  59.41 ? 267  GLU A OE2 1 
ATOM   4320 N N   . ALA B 1 268 ? -43.448 21.730  -15.702 1.00  47.48 ? 268  ALA A N   1 
ATOM   4321 C CA  . ALA B 1 268 ? -42.763 20.566  -16.245 1.00  47.85 ? 268  ALA A CA  1 
ATOM   4322 C C   . ALA B 1 268 ? -41.590 20.177  -15.346 1.00  49.44 ? 268  ALA A C   1 
ATOM   4323 O O   . ALA B 1 268 ? -41.096 20.990  -14.550 1.00  42.90 ? 268  ALA A O   1 
ATOM   4324 C CB  . ALA B 1 268 ? -42.277 20.844  -17.657 1.00  46.06 ? 268  ALA A CB  1 
ATOM   4325 N N   . VAL B 1 269 ? -41.165 18.926  -15.470 1.00  44.00 ? 269  VAL A N   1 
ATOM   4326 C CA  . VAL B 1 269 ? -39.973 18.440  -14.790 1.00  42.27 ? 269  VAL A CA  1 
ATOM   4327 C C   . VAL B 1 269 ? -39.061 17.788  -15.817 1.00  42.71 ? 269  VAL A C   1 
ATOM   4328 O O   . VAL B 1 269 ? -39.419 16.780  -16.418 1.00  43.76 ? 269  VAL A O   1 
ATOM   4329 C CB  . VAL B 1 269 ? -40.329 17.439  -13.677 1.00  47.33 ? 269  VAL A CB  1 
ATOM   4330 C CG1 . VAL B 1 269 ? -39.062 16.881  -13.023 1.00  43.67 ? 269  VAL A CG1 1 
ATOM   4331 C CG2 . VAL B 1 269 ? -41.231 18.103  -12.634 1.00  44.46 ? 269  VAL A CG2 1 
ATOM   4332 N N   . VAL B 1 270 ? -37.889 18.377  -16.028 1.00  37.45 ? 270  VAL A N   1 
ATOM   4333 C CA  . VAL B 1 270 ? -36.961 17.898  -17.040 1.00  36.94 ? 270  VAL A CA  1 
ATOM   4334 C C   . VAL B 1 270 ? -35.786 17.152  -16.396 1.00  38.33 ? 270  VAL A C   1 
ATOM   4335 O O   . VAL B 1 270 ? -35.143 17.666  -15.481 1.00  37.65 ? 270  VAL A O   1 
ATOM   4336 C CB  . VAL B 1 270 ? -36.396 19.063  -17.871 1.00  37.03 ? 270  VAL A CB  1 
ATOM   4337 C CG1 . VAL B 1 270 ? -35.582 18.533  -19.032 1.00  38.17 ? 270  VAL A CG1 1 
ATOM   4338 C CG2 . VAL B 1 270 ? -37.514 19.976  -18.366 1.00  40.39 ? 270  VAL A CG2 1 
ATOM   4339 N N   . VAL B 1 271 ? -35.510 15.943  -16.875 1.00  37.37 ? 271  VAL A N   1 
ATOM   4340 C CA  . VAL B 1 271 ? -34.340 15.188  -16.428 1.00  35.14 ? 271  VAL A CA  1 
ATOM   4341 C C   . VAL B 1 271 ? -33.629 14.566  -17.618 1.00  35.92 ? 271  VAL A C   1 
ATOM   4342 O O   . VAL B 1 271 ? -34.178 14.526  -18.719 1.00  35.39 ? 271  VAL A O   1 
ATOM   4343 C CB  . VAL B 1 271 ? -34.707 14.095  -15.405 1.00  36.12 ? 271  VAL A CB  1 
ATOM   4344 C CG1 . VAL B 1 271 ? -35.338 14.717  -14.176 1.00  42.28 ? 271  VAL A CG1 1 
ATOM   4345 C CG2 . VAL B 1 271 ? -35.639 13.060  -16.011 1.00  40.47 ? 271  VAL A CG2 1 
ATOM   4346 N N   . THR B 1 272 ? -32.401 14.101  -17.410 1.00  30.46 ? 272  THR A N   1 
ATOM   4347 C CA  . THR B 1 272 ? -31.699 13.361  -18.455 1.00  33.13 ? 272  THR A CA  1 
ATOM   4348 C C   . THR B 1 272 ? -32.053 11.897  -18.299 1.00  32.53 ? 272  THR A C   1 
ATOM   4349 O O   . THR B 1 272 ? -32.674 11.513  -17.314 1.00  31.82 ? 272  THR A O   1 
ATOM   4350 C CB  . THR B 1 272 ? -30.175 13.483  -18.342 1.00  34.47 ? 272  THR A CB  1 
ATOM   4351 O OG1 . THR B 1 272 ? -29.727 12.748  -17.193 1.00  32.61 ? 272  THR A OG1 1 
ATOM   4352 C CG2 . THR B 1 272 ? -29.746 14.951  -18.223 1.00  36.23 ? 272  THR A CG2 1 
ATOM   4353 N N   . ASN B 1 273 ? -31.653 11.071  -19.259 1.00  32.74 ? 273  ASN A N   1 
ATOM   4354 C CA  . ASN B 1 273 ? -31.825 9.633   -19.095 1.00  36.17 ? 273  ASN A CA  1 
ATOM   4355 C C   . ASN B 1 273 ? -30.589 8.949   -18.484 1.00  34.59 ? 273  ASN A C   1 
ATOM   4356 O O   . ASN B 1 273 ? -30.224 7.843   -18.872 1.00  35.78 ? 273  ASN A O   1 
ATOM   4357 C CB  . ASN B 1 273 ? -32.272 8.962   -20.407 1.00  35.55 ? 273  ASN A CB  1 
ATOM   4358 C CG  . ASN B 1 273 ? -31.265 9.139   -21.549 1.00  39.49 ? 273  ASN A CG  1 
ATOM   4359 O OD1 . ASN B 1 273 ? -31.326 8.432   -22.563 1.00  41.70 ? 273  ASN A OD1 1 
ATOM   4360 N ND2 . ASN B 1 273 ? -30.345 10.082  -21.393 1.00  32.54 ? 273  ASN A ND2 1 
ATOM   4361 N N   . THR B 1 274 ? -29.940 9.609   -17.527 1.00  35.79 ? 274  THR A N   1 
ATOM   4362 C CA  . THR B 1 274 ? -28.844 8.950   -16.814 1.00  35.39 ? 274  THR A CA  1 
ATOM   4363 C C   . THR B 1 274 ? -29.406 7.813   -15.966 1.00  37.56 ? 274  THR A C   1 
ATOM   4364 O O   . THR B 1 274 ? -28.708 6.849   -15.646 1.00  32.44 ? 274  THR A O   1 
ATOM   4365 C CB  . THR B 1 274 ? -28.011 9.928   -15.944 1.00  35.39 ? 274  THR A CB  1 
ATOM   4366 O OG1 . THR B 1 274 ? -28.831 10.517  -14.925 1.00  35.20 ? 274  THR A OG1 1 
ATOM   4367 C CG2 . THR B 1 274 ? -27.390 11.023  -16.811 1.00  32.75 ? 274  THR A CG2 1 
ATOM   4368 N N   . ILE B 1 275 ? -30.683 7.943   -15.623 1.00  36.15 ? 275  ILE A N   1 
ATOM   4369 C CA  . ILE B 1 275 ? -31.441 6.911   -14.925 1.00  39.23 ? 275  ILE A CA  1 
ATOM   4370 C C   . ILE B 1 275 ? -32.677 6.635   -15.774 1.00  41.44 ? 275  ILE A C   1 
ATOM   4371 O O   . ILE B 1 275 ? -33.247 7.565   -16.354 1.00  40.97 ? 275  ILE A O   1 
ATOM   4372 C CB  . ILE B 1 275 ? -31.866 7.398   -13.519 1.00  40.29 ? 275  ILE A CB  1 
ATOM   4373 C CG1 . ILE B 1 275 ? -30.647 7.514   -12.601 1.00  39.65 ? 275  ILE A CG1 1 
ATOM   4374 C CG2 . ILE B 1 275 ? -32.926 6.483   -12.896 1.00  40.83 ? 275  ILE A CG2 1 
ATOM   4375 C CD1 . ILE B 1 275 ? -30.973 8.095   -11.228 1.00  43.66 ? 275  ILE A CD1 1 
ATOM   4376 N N   . PRO B 1 276 ? -33.075 5.357   -15.890 1.00  43.57 ? 276  PRO A N   1 
ATOM   4377 C CA  . PRO B 1 276 ? -34.250 5.008   -16.699 1.00  45.58 ? 276  PRO A CA  1 
ATOM   4378 C C   . PRO B 1 276 ? -35.464 5.815   -16.257 1.00  47.73 ? 276  PRO A C   1 
ATOM   4379 O O   . PRO B 1 276 ? -35.656 6.025   -15.056 1.00  43.69 ? 276  PRO A O   1 
ATOM   4380 C CB  . PRO B 1 276 ? -34.462 3.525   -16.385 1.00  47.68 ? 276  PRO A CB  1 
ATOM   4381 C CG  . PRO B 1 276 ? -33.131 3.033   -16.000 1.00  45.01 ? 276  PRO A CG  1 
ATOM   4382 C CD  . PRO B 1 276 ? -32.452 4.166   -15.286 1.00  44.67 ? 276  PRO A CD  1 
ATOM   4383 N N   . GLN B 1 277 ? -36.262 6.273   -17.215 0.95  43.74 ? 277  GLN A N   1 
ATOM   4384 C CA  . GLN B 1 277 ? -37.367 7.176   -16.903 0.95  50.94 ? 277  GLN A CA  1 
ATOM   4385 C C   . GLN B 1 277 ? -38.697 6.703   -17.482 0.95  51.90 ? 277  GLN A C   1 
ATOM   4386 O O   . GLN B 1 277 ? -39.756 7.196   -17.103 0.95  50.66 ? 277  GLN A O   1 
ATOM   4387 C CB  . GLN B 1 277 ? -37.051 8.584   -17.429 0.95  45.83 ? 277  GLN A CB  1 
ATOM   4388 C CG  . GLN B 1 277 ? -35.770 9.183   -16.870 0.95  43.39 ? 277  GLN A CG  1 
ATOM   4389 C CD  . GLN B 1 277 ? -35.834 9.375   -15.361 0.95  45.14 ? 277  GLN A CD  1 
ATOM   4390 O OE1 . GLN B 1 277 ? -34.805 9.424   -14.675 0.95  41.84 ? 277  GLN A OE1 1 
ATOM   4391 N NE2 . GLN B 1 277 ? -37.049 9.492   -14.838 0.95  46.72 ? 277  GLN A NE2 1 
ATOM   4392 N N   . GLU B 1 278 ? -38.627 5.745   -18.398 0.20  50.73 ? 278  GLU A N   1 
ATOM   4393 C CA  . GLU B 1 278 ? -39.783 5.331   -19.186 0.20  52.12 ? 278  GLU A CA  1 
ATOM   4394 C C   . GLU B 1 278 ? -40.961 4.863   -18.329 0.20  55.92 ? 278  GLU A C   1 
ATOM   4395 O O   . GLU B 1 278 ? -42.120 5.068   -18.685 0.20  56.53 ? 278  GLU A O   1 
ATOM   4396 C CB  . GLU B 1 278 ? -39.372 4.253   -20.191 0.20  50.94 ? 278  GLU A CB  1 
ATOM   4397 C CG  . GLU B 1 278 ? -38.160 4.637   -21.042 0.20  49.98 ? 278  GLU A CG  1 
ATOM   4398 C CD  . GLU B 1 278 ? -36.859 4.655   -20.250 0.20  48.53 ? 278  GLU A CD  1 
ATOM   4399 O OE1 . GLU B 1 278 ? -36.275 5.748   -20.086 0.20  49.14 ? 278  GLU A OE1 1 
ATOM   4400 O OE2 . GLU B 1 278 ? -36.425 3.577   -19.793 0.20  46.10 ? 278  GLU A OE2 1 
ATOM   4401 N N   . ASP B 1 279 ? -40.653 4.241   -17.198 1.00  58.43 ? 279  ASP A N   1 
ATOM   4402 C CA  . ASP B 1 279 ? -41.668 3.771   -16.258 1.00  60.68 ? 279  ASP A CA  1 
ATOM   4403 C C   . ASP B 1 279 ? -42.410 4.927   -15.578 1.00  61.72 ? 279  ASP A C   1 
ATOM   4404 O O   . ASP B 1 279 ? -43.641 4.924   -15.497 1.00  63.05 ? 279  ASP A O   1 
ATOM   4405 C CB  . ASP B 1 279 ? -41.013 2.865   -15.207 1.00  66.14 ? 279  ASP A CB  1 
ATOM   4406 C CG  . ASP B 1 279 ? -42.014 2.277   -14.213 1.00  74.96 ? 279  ASP A CG  1 
ATOM   4407 O OD1 . ASP B 1 279 ? -43.048 2.921   -13.920 1.00  74.30 ? 279  ASP A OD1 1 
ATOM   4408 O OD2 . ASP B 1 279 ? -41.752 1.161   -13.710 1.00  78.94 ? 279  ASP A OD2 1 
ATOM   4409 N N   . LYS B 1 280 ? -41.659 5.911   -15.092 0.10  58.76 ? 280  LYS A N   1 
ATOM   4410 C CA  . LYS B 1 280 ? -42.244 7.015   -14.334 0.10  58.76 ? 280  LYS A CA  1 
ATOM   4411 C C   . LYS B 1 280 ? -42.941 8.048   -15.216 0.10  58.11 ? 280  LYS A C   1 
ATOM   4412 O O   . LYS B 1 280 ? -43.796 8.797   -14.747 0.10  58.67 ? 280  LYS A O   1 
ATOM   4413 C CB  . LYS B 1 280 ? -41.180 7.692   -13.467 0.10  55.86 ? 280  LYS A CB  1 
ATOM   4414 C CG  . LYS B 1 280 ? -40.638 6.812   -12.355 0.10  54.93 ? 280  LYS A CG  1 
ATOM   4415 C CD  . LYS B 1 280 ? -39.398 7.423   -11.731 0.10  51.35 ? 280  LYS A CD  1 
ATOM   4416 C CE  . LYS B 1 280 ? -38.667 6.426   -10.842 0.10  50.35 ? 280  LYS A CE  1 
ATOM   4417 N NZ  . LYS B 1 280 ? -39.477 5.996   -9.673  0.10  49.69 ? 280  LYS A NZ  1 
ATOM   4418 N N   . MET B 1 281 ? -42.569 8.095   -16.489 1.00  57.56 ? 281  MET A N   1 
ATOM   4419 C CA  . MET B 1 281 ? -43.208 9.007   -17.433 1.00  60.78 ? 281  MET A CA  1 
ATOM   4420 C C   . MET B 1 281 ? -44.645 8.577   -17.724 1.00  62.35 ? 281  MET A C   1 
ATOM   4421 O O   . MET B 1 281 ? -45.499 9.402   -18.056 1.00  60.79 ? 281  MET A O   1 
ATOM   4422 C CB  . MET B 1 281 ? -42.400 9.116   -18.729 1.00  56.10 ? 281  MET A CB  1 
ATOM   4423 C CG  . MET B 1 281 ? -41.053 9.797   -18.544 1.00  53.42 ? 281  MET A CG  1 
ATOM   4424 S SD  . MET B 1 281 ? -40.169 10.026  -20.101 1.00  69.71 ? 281  MET A SD  1 
ATOM   4425 C CE  . MET B 1 281 ? -39.836 8.332   -20.573 1.00  60.91 ? 281  MET A CE  1 
ATOM   4426 N N   . LYS B 1 282 ? -44.906 7.283   -17.589 0.84  59.47 ? 282  LYS A N   1 
ATOM   4427 C CA  . LYS B 1 282 ? -46.261 6.772   -17.713 0.84  62.82 ? 282  LYS A CA  1 
ATOM   4428 C C   . LYS B 1 282 ? -47.101 7.191   -16.503 0.84  65.00 ? 282  LYS A C   1 
ATOM   4429 O O   . LYS B 1 282 ? -48.325 7.279   -16.589 0.84  65.01 ? 282  LYS A O   1 
ATOM   4430 C CB  . LYS B 1 282 ? -46.248 5.248   -17.865 0.84  65.82 ? 282  LYS A CB  1 
ATOM   4431 C CG  . LYS B 1 282 ? -45.545 4.765   -19.130 0.84  67.05 ? 282  LYS A CG  1 
ATOM   4432 C CD  . LYS B 1 282 ? -45.396 3.252   -19.152 0.84  73.00 ? 282  LYS A CD  1 
ATOM   4433 C CE  . LYS B 1 282 ? -44.583 2.795   -20.358 0.84  74.50 ? 282  LYS A CE  1 
ATOM   4434 N NZ  . LYS B 1 282 ? -44.401 1.312   -20.389 0.84  75.91 ? 282  LYS A NZ  1 
ATOM   4435 N N   . HIS B 1 283 ? -46.443 7.459   -15.379 0.20  61.13 ? 283  HIS A N   1 
ATOM   4436 C CA  . HIS B 1 283 ? -47.155 7.855   -14.166 0.20  61.80 ? 283  HIS A CA  1 
ATOM   4437 C C   . HIS B 1 283 ? -47.058 9.358   -13.897 0.20  60.97 ? 283  HIS A C   1 
ATOM   4438 O O   . HIS B 1 283 ? -47.606 9.852   -12.914 0.20  59.89 ? 283  HIS A O   1 
ATOM   4439 C CB  . HIS B 1 283 ? -46.645 7.068   -12.955 0.20  61.78 ? 283  HIS A CB  1 
ATOM   4440 C CG  . HIS B 1 283 ? -47.726 6.374   -12.185 0.20  63.00 ? 283  HIS A CG  1 
ATOM   4441 N ND1 . HIS B 1 283 ? -48.577 7.039   -11.328 0.20  62.90 ? 283  HIS A ND1 1 
ATOM   4442 C CD2 . HIS B 1 283 ? -48.092 5.070   -12.139 0.20  63.04 ? 283  HIS A CD2 1 
ATOM   4443 C CE1 . HIS B 1 283 ? -49.421 6.176   -10.789 0.20  63.54 ? 283  HIS A CE1 1 
ATOM   4444 N NE2 . HIS B 1 283 ? -49.147 4.974   -11.265 0.20  64.12 ? 283  HIS A NE2 1 
ATOM   4445 N N   . CYS B 1 284 ? -46.367 10.081  -14.775 0.78  61.63 ? 284  CYS A N   1 
ATOM   4446 C CA  . CYS B 1 284 ? -46.192 11.524  -14.609 0.78  59.80 ? 284  CYS A CA  1 
ATOM   4447 C C   . CYS B 1 284 ? -46.005 12.231  -15.948 0.78  58.98 ? 284  CYS A C   1 
ATOM   4448 O O   . CYS B 1 284 ? -44.998 12.037  -16.640 0.78  56.37 ? 284  CYS A O   1 
ATOM   4449 C CB  . CYS B 1 284 ? -45.012 11.827  -13.680 0.78  60.68 ? 284  CYS A CB  1 
ATOM   4450 S SG  . CYS B 1 284 ? -44.814 13.585  -13.290 0.78  61.87 ? 284  CYS A SG  1 
ATOM   4451 N N   . SER B 1 285 ? -46.975 13.070  -16.298 1.00  60.07 ? 285  SER A N   1 
ATOM   4452 C CA  . SER B 1 285 ? -47.033 13.685  -17.624 1.00  56.72 ? 285  SER A CA  1 
ATOM   4453 C C   . SER B 1 285 ? -46.130 14.903  -17.797 1.00  54.17 ? 285  SER A C   1 
ATOM   4454 O O   . SER B 1 285 ? -45.771 15.263  -18.920 1.00  53.59 ? 285  SER A O   1 
ATOM   4455 C CB  . SER B 1 285 ? -48.474 14.071  -17.965 1.00  64.41 ? 285  SER A CB  1 
ATOM   4456 O OG  . SER B 1 285 ? -48.532 14.727  -19.217 1.00  62.30 ? 285  SER A OG  1 
ATOM   4457 N N   . LYS B 1 286 ? -45.764 15.545  -16.695 1.00  56.56 ? 286  LYS A N   1 
ATOM   4458 C CA  . LYS B 1 286 ? -44.913 16.729  -16.786 1.00  55.39 ? 286  LYS A CA  1 
ATOM   4459 C C   . LYS B 1 286 ? -43.418 16.412  -16.972 1.00  50.86 ? 286  LYS A C   1 
ATOM   4460 O O   . LYS B 1 286 ? -42.617 17.312  -17.238 1.00  48.58 ? 286  LYS A O   1 
ATOM   4461 C CB  . LYS B 1 286 ? -45.142 17.660  -15.596 1.00  56.12 ? 286  LYS A CB  1 
ATOM   4462 C CG  . LYS B 1 286 ? -45.196 16.965  -14.254 1.00  56.58 ? 286  LYS A CG  1 
ATOM   4463 C CD  . LYS B 1 286 ? -45.371 17.974  -13.122 1.00  54.38 ? 286  LYS A CD  1 
ATOM   4464 C CE  . LYS B 1 286 ? -46.832 18.259  -12.828 1.00  55.50 ? 286  LYS A CE  1 
ATOM   4465 N NZ  . LYS B 1 286 ? -47.409 19.264  -13.753 1.00  58.82 ? 286  LYS A NZ  1 
ATOM   4466 N N   . ILE B 1 287 ? -43.048 15.138  -16.859 1.00  49.22 ? 287  ILE A N   1 
ATOM   4467 C CA  . ILE B 1 287 ? -41.656 14.740  -17.065 1.00  45.71 ? 287  ILE A CA  1 
ATOM   4468 C C   . ILE B 1 287 ? -41.222 14.725  -18.526 1.00  46.93 ? 287  ILE A C   1 
ATOM   4469 O O   . ILE B 1 287 ? -41.815 14.037  -19.359 1.00  48.84 ? 287  ILE A O   1 
ATOM   4470 C CB  . ILE B 1 287 ? -41.347 13.352  -16.475 1.00  54.26 ? 287  ILE A CB  1 
ATOM   4471 C CG1 . ILE B 1 287 ? -41.484 13.364  -14.951 1.00  56.14 ? 287  ILE A CG1 1 
ATOM   4472 C CG2 . ILE B 1 287 ? -39.936 12.922  -16.870 1.00  49.26 ? 287  ILE A CG2 1 
ATOM   4473 C CD1 . ILE B 1 287 ? -41.125 12.040  -14.299 1.00  55.74 ? 287  ILE A CD1 1 
ATOM   4474 N N   . GLN B 1 288 ? -40.174 15.479  -18.834 1.00  39.20 ? 288  GLN A N   1 
ATOM   4475 C CA  . GLN B 1 288 ? -39.541 15.387  -20.140 1.00  45.72 ? 288  GLN A CA  1 
ATOM   4476 C C   . GLN B 1 288 ? -38.094 14.932  -19.962 1.00  43.00 ? 288  GLN A C   1 
ATOM   4477 O O   . GLN B 1 288 ? -37.442 15.302  -18.987 1.00  42.01 ? 288  GLN A O   1 
ATOM   4478 C CB  . GLN B 1 288 ? -39.598 16.735  -20.868 1.00  43.55 ? 288  GLN A CB  1 
ATOM   4479 C CG  . GLN B 1 288 ? -40.977 17.393  -20.819 1.00  48.79 ? 288  GLN A CG  1 
ATOM   4480 C CD  . GLN B 1 288 ? -41.193 18.396  -21.944 1.00  53.81 ? 288  GLN A CD  1 
ATOM   4481 O OE1 . GLN B 1 288 ? -40.521 18.347  -22.982 1.00  51.72 ? 288  GLN A OE1 1 
ATOM   4482 N NE2 . GLN B 1 288 ? -42.138 19.313  -21.743 1.00  54.97 ? 288  GLN A NE2 1 
ATOM   4483 N N   . VAL B 1 289 ? -37.590 14.128  -20.894 1.00  44.62 ? 289  VAL A N   1 
ATOM   4484 C CA  . VAL B 1 289 ? -36.206 13.679  -20.802 1.00  42.49 ? 289  VAL A CA  1 
ATOM   4485 C C   . VAL B 1 289 ? -35.295 14.228  -21.902 1.00  44.66 ? 289  VAL A C   1 
ATOM   4486 O O   . VAL B 1 289 ? -35.654 14.284  -23.088 1.00  48.01 ? 289  VAL A O   1 
ATOM   4487 C CB  . VAL B 1 289 ? -36.082 12.142  -20.780 1.00  45.49 ? 289  VAL A CB  1 
ATOM   4488 C CG1 . VAL B 1 289 ? -37.111 11.537  -19.853 1.00  48.10 ? 289  VAL A CG1 1 
ATOM   4489 C CG2 . VAL B 1 289 ? -36.232 11.587  -22.178 1.00  52.93 ? 289  VAL A CG2 1 
ATOM   4490 N N   . ILE B 1 290 ? -34.109 14.636  -21.477 1.00  35.12 ? 290  ILE A N   1 
ATOM   4491 C CA  . ILE B 1 290 ? -33.022 14.969  -22.373 1.00  40.54 ? 290  ILE A CA  1 
ATOM   4492 C C   . ILE B 1 290 ? -32.149 13.733  -22.542 1.00  42.68 ? 290  ILE A C   1 
ATOM   4493 O O   . ILE B 1 290 ? -31.592 13.214  -21.570 1.00  38.19 ? 290  ILE A O   1 
ATOM   4494 C CB  . ILE B 1 290 ? -32.151 16.079  -21.788 1.00  39.42 ? 290  ILE A CB  1 
ATOM   4495 C CG1 . ILE B 1 290 ? -32.998 17.314  -21.490 1.00  41.19 ? 290  ILE A CG1 1 
ATOM   4496 C CG2 . ILE B 1 290 ? -30.988 16.396  -22.730 1.00  41.28 ? 290  ILE A CG2 1 
ATOM   4497 C CD1 . ILE B 1 290 ? -32.205 18.468  -20.938 1.00  40.34 ? 290  ILE A CD1 1 
ATOM   4498 N N   . ASP B 1 291 ? -32.033 13.272  -23.779 1.00  39.33 ? 291  ASP A N   1 
ATOM   4499 C CA  . ASP B 1 291 ? -31.237 12.097  -24.109 1.00  43.33 ? 291  ASP A CA  1 
ATOM   4500 C C   . ASP B 1 291 ? -29.753 12.435  -24.050 1.00  40.57 ? 291  ASP A C   1 
ATOM   4501 O O   . ASP B 1 291 ? -29.300 13.355  -24.725 1.00  40.33 ? 291  ASP A O   1 
ATOM   4502 C CB  . ASP B 1 291 ? -31.615 11.620  -25.512 1.00  42.16 ? 291  ASP A CB  1 
ATOM   4503 C CG  . ASP B 1 291 ? -30.800 10.434  -25.972 1.00  43.39 ? 291  ASP A CG  1 
ATOM   4504 O OD1 . ASP B 1 291 ? -30.121 9.797   -25.140 1.00  39.81 ? 291  ASP A OD1 1 
ATOM   4505 O OD2 . ASP B 1 291 ? -30.857 10.128  -27.181 1.00  44.70 ? 291  ASP A OD2 1 
ATOM   4506 N N   . ILE B 1 292 ? -28.985 11.706  -23.248 1.00  33.83 ? 292  ILE A N   1 
ATOM   4507 C CA  . ILE B 1 292 ? -27.559 12.020  -23.163 1.00  36.04 ? 292  ILE A CA  1 
ATOM   4508 C C   . ILE B 1 292 ? -26.664 10.906  -23.680 1.00  34.68 ? 292  ILE A C   1 
ATOM   4509 O O   . ILE B 1 292 ? -25.452 10.922  -23.477 1.00  33.03 ? 292  ILE A O   1 
ATOM   4510 C CB  . ILE B 1 292 ? -27.130 12.545  -21.758 1.00  38.54 ? 292  ILE A CB  1 
ATOM   4511 C CG1 . ILE B 1 292 ? -27.556 11.610  -20.622 1.00  29.29 ? 292  ILE A CG1 1 
ATOM   4512 C CG2 . ILE B 1 292 ? -27.736 13.918  -21.520 1.00  36.07 ? 292  ILE A CG2 1 
ATOM   4513 C CD1 . ILE B 1 292 ? -27.051 10.185  -20.737 1.00  30.47 ? 292  ILE A CD1 1 
ATOM   4514 N N   . SER B 1 293 ? -27.275 9.948   -24.375 1.00  33.77 ? 293  SER A N   1 
ATOM   4515 C CA  . SER B 1 293 ? -26.533 8.839   -24.957 1.00  30.25 ? 293  SER A CA  1 
ATOM   4516 C C   . SER B 1 293 ? -25.492 9.314   -25.968 1.00  31.77 ? 293  SER A C   1 
ATOM   4517 O O   . SER B 1 293 ? -24.451 8.670   -26.140 1.00  32.67 ? 293  SER A O   1 
ATOM   4518 C CB  . SER B 1 293 ? -27.483 7.843   -25.627 1.00  35.82 ? 293  SER A CB  1 
ATOM   4519 O OG  . SER B 1 293 ? -28.180 8.445   -26.703 1.00  36.12 ? 293  SER A OG  1 
ATOM   4520 N N   . MET B 1 294 ? -25.747 10.429  -26.642 0.73  27.83 ? 294  MET A N   1 
ATOM   4521 C CA  . MET B 1 294 ? -24.799 10.862  -27.666 0.73  31.85 ? 294  MET A CA  1 
ATOM   4522 C C   . MET B 1 294 ? -23.538 11.443  -27.035 0.73  28.26 ? 294  MET A C   1 
ATOM   4523 O O   . MET B 1 294 ? -22.429 11.231  -27.507 0.73  28.88 ? 294  MET A O   1 
ATOM   4524 C CB  . MET B 1 294 ? -25.416 11.877  -28.626 0.73  33.83 ? 294  MET A CB  1 
ATOM   4525 C CG  . MET B 1 294 ? -24.395 12.422  -29.612 0.73  38.54 ? 294  MET A CG  1 
ATOM   4526 S SD  . MET B 1 294 ? -23.563 11.123  -30.572 0.73  53.50 ? 294  MET A SD  1 
ATOM   4527 C CE  . MET B 1 294 ? -24.651 10.988  -31.994 0.73  45.05 ? 294  MET A CE  1 
ATOM   4528 N N   . ILE B 1 295 ? -23.725 12.186  -25.960 1.00  29.11 ? 295  ILE A N   1 
ATOM   4529 C CA  . ILE B 1 295 ? -22.605 12.674  -25.163 1.00  32.80 ? 295  ILE A CA  1 
ATOM   4530 C C   . ILE B 1 295 ? -21.774 11.500  -24.646 1.00  26.54 ? 295  ILE A C   1 
ATOM   4531 O O   . ILE B 1 295 ? -20.545 11.492  -24.750 1.00  29.62 ? 295  ILE A O   1 
ATOM   4532 C CB  . ILE B 1 295 ? -23.133 13.517  -23.995 1.00  32.81 ? 295  ILE A CB  1 
ATOM   4533 C CG1 . ILE B 1 295 ? -24.106 14.567  -24.534 1.00  35.74 ? 295  ILE A CG1 1 
ATOM   4534 C CG2 . ILE B 1 295 ? -21.995 14.149  -23.230 1.00  36.22 ? 295  ILE A CG2 1 
ATOM   4535 C CD1 . ILE B 1 295 ? -24.789 15.407  -23.466 1.00  35.89 ? 295  ILE A CD1 1 
ATOM   4536 N N   . LEU B 1 296 ? -22.442 10.496  -24.101 1.00  29.10 ? 296  LEU A N   1 
ATOM   4537 C CA  . LEU B 1 296 ? -21.719 9.356   -23.539 1.00  28.78 ? 296  LEU A CA  1 
ATOM   4538 C C   . LEU B 1 296 ? -21.000 8.569   -24.625 1.00  29.77 ? 296  LEU A C   1 
ATOM   4539 O O   . LEU B 1 296 ? -19.829 8.244   -24.482 1.00  26.76 ? 296  LEU A O   1 
ATOM   4540 C CB  . LEU B 1 296 ? -22.651 8.454   -22.740 1.00  25.68 ? 296  LEU A CB  1 
ATOM   4541 C CG  . LEU B 1 296 ? -23.108 9.014   -21.388 1.00  28.27 ? 296  LEU A CG  1 
ATOM   4542 C CD1 . LEU B 1 296 ? -24.126 8.071   -20.773 1.00  25.70 ? 296  LEU A CD1 1 
ATOM   4543 C CD2 . LEU B 1 296 ? -21.909 9.238   -20.435 1.00  26.67 ? 296  LEU A CD2 1 
ATOM   4544 N N   . ALA B 1 297 ? -21.698 8.269   -25.721 1.00  29.76 ? 297  ALA A N   1 
ATOM   4545 C CA  . ALA B 1 297 ? -21.067 7.562   -26.833 1.00  30.18 ? 297  ALA A CA  1 
ATOM   4546 C C   . ALA B 1 297 ? -19.834 8.331   -27.324 1.00  29.61 ? 297  ALA A C   1 
ATOM   4547 O O   . ALA B 1 297 ? -18.766 7.754   -27.574 1.00  29.88 ? 297  ALA A O   1 
ATOM   4548 C CB  . ALA B 1 297 ? -22.078 7.350   -27.972 1.00  27.66 ? 297  ALA A CB  1 
ATOM   4549 N N   . GLU B 1 298 ? -19.976 9.643   -27.435 0.99  29.34 ? 298  GLU A N   1 
ATOM   4550 C CA  . GLU B 1 298 ? -18.895 10.469  -27.967 0.99  35.51 ? 298  GLU A CA  1 
ATOM   4551 C C   . GLU B 1 298 ? -17.715 10.542  -26.997 0.99  34.00 ? 298  GLU A C   1 
ATOM   4552 O O   . GLU B 1 298 ? -16.562 10.651  -27.417 0.99  31.22 ? 298  GLU A O   1 
ATOM   4553 C CB  . GLU B 1 298 ? -19.412 11.860  -28.335 0.99  35.86 ? 298  GLU A CB  1 
ATOM   4554 C CG  . GLU B 1 298 ? -18.412 12.744  -29.064 0.99  42.56 ? 298  GLU A CG  1 
ATOM   4555 C CD  . GLU B 1 298 ? -18.158 12.302  -30.500 0.99  45.41 ? 298  GLU A CD  1 
ATOM   4556 O OE1 . GLU B 1 298 ? -18.776 11.306  -30.948 0.99  41.97 ? 298  GLU A OE1 1 
ATOM   4557 O OE2 . GLU B 1 298 ? -17.330 12.950  -31.181 0.99  48.63 ? 298  GLU A OE2 1 
ATOM   4558 N N   . ALA B 1 299 ? -17.998 10.463  -25.698 1.00  31.52 ? 299  ALA A N   1 
ATOM   4559 C CA  . ALA B 1 299 ? -16.940 10.385  -24.697 1.00  26.63 ? 299  ALA A CA  1 
ATOM   4560 C C   . ALA B 1 299 ? -16.182 9.062   -24.831 1.00  29.27 ? 299  ALA A C   1 
ATOM   4561 O O   . ALA B 1 299 ? -14.955 9.019   -24.712 1.00  28.67 ? 299  ALA A O   1 
ATOM   4562 C CB  . ALA B 1 299 ? -17.511 10.551  -23.290 1.00  30.38 ? 299  ALA A CB  1 
ATOM   4563 N N   . ILE B 1 300 ? -16.909 7.984   -25.105 1.00  25.35 ? 300  ILE A N   1 
ATOM   4564 C CA  . ILE B 1 300 ? -16.268 6.688   -25.273 1.00  30.86 ? 300  ILE A CA  1 
ATOM   4565 C C   . ILE B 1 300 ? -15.408 6.642   -26.539 1.00  28.46 ? 300  ILE A C   1 
ATOM   4566 O O   . ILE B 1 300 ? -14.253 6.224   -26.495 1.00  27.02 ? 300  ILE A O   1 
ATOM   4567 C CB  . ILE B 1 300 ? -17.286 5.531   -25.278 1.00  26.63 ? 300  ILE A CB  1 
ATOM   4568 C CG1 . ILE B 1 300 ? -17.898 5.362   -23.881 1.00  27.58 ? 300  ILE A CG1 1 
ATOM   4569 C CG2 . ILE B 1 300 ? -16.610 4.232   -25.693 1.00  28.45 ? 300  ILE A CG2 1 
ATOM   4570 C CD1 . ILE B 1 300 ? -19.188 4.589   -23.894 1.00  27.49 ? 300  ILE A CD1 1 
ATOM   4571 N N   . ARG B 1 301 ? -15.968 7.069   -27.666 0.98  28.33 ? 301  ARG A N   1 
ATOM   4572 C CA  . ARG B 1 301 ? -15.195 7.083   -28.896 0.98  30.74 ? 301  ARG A CA  1 
ATOM   4573 C C   . ARG B 1 301 ? -13.959 7.956   -28.731 0.98  31.25 ? 301  ARG A C   1 
ATOM   4574 O O   . ARG B 1 301 ? -12.853 7.552   -29.097 0.98  36.15 ? 301  ARG A O   1 
ATOM   4575 C CB  . ARG B 1 301 ? -16.031 7.576   -30.077 0.98  35.53 ? 301  ARG A CB  1 
ATOM   4576 C CG  . ARG B 1 301 ? -15.440 7.160   -31.419 0.98  40.20 ? 301  ARG A CG  1 
ATOM   4577 C CD  . ARG B 1 301 ? -16.201 7.734   -32.596 0.98  42.56 ? 301  ARG A CD  1 
ATOM   4578 N NE  . ARG B 1 301 ? -15.549 8.944   -33.081 0.98  52.74 ? 301  ARG A NE  1 
ATOM   4579 C CZ  . ARG B 1 301 ? -15.841 10.155  -32.637 0.98  49.49 ? 301  ARG A CZ  1 
ATOM   4580 N NH1 . ARG B 1 301 ? -16.775 10.288  -31.709 0.98  49.13 ? 301  ARG A NH1 1 
ATOM   4581 N NH2 . ARG B 1 301 ? -15.211 11.222  -33.110 0.98  48.74 ? 301  ARG A NH2 1 
ATOM   4582 N N   . ARG B 1 302 ? -14.135 9.146   -28.171 0.50  27.50 ? 302  ARG A N   1 
ATOM   4583 C CA  . ARG B 1 302 ? -13.003 10.048  -28.007 0.50  32.76 ? 302  ARG A CA  1 
ATOM   4584 C C   . ARG B 1 302 ? -11.972 9.489   -27.028 0.50  30.98 ? 302  ARG A C   1 
ATOM   4585 O O   . ARG B 1 302 ? -10.779 9.541   -27.293 0.50  32.33 ? 302  ARG A O   1 
ATOM   4586 C CB  . ARG B 1 302 ? -13.465 11.461  -27.650 0.50  33.15 ? 302  ARG A CB  1 
ATOM   4587 C CG  . ARG B 1 302 ? -14.141 12.156  -28.828 0.50  41.46 ? 302  ARG A CG  1 
ATOM   4588 C CD  . ARG B 1 302 ? -14.874 13.423  -28.432 0.50  41.81 ? 302  ARG A CD  1 
ATOM   4589 N NE  . ARG B 1 302 ? -15.491 14.063  -29.589 0.50  42.50 ? 302  ARG A NE  1 
ATOM   4590 C CZ  . ARG B 1 302 ? -14.947 15.068  -30.266 0.50  46.99 ? 302  ARG A CZ  1 
ATOM   4591 N NH1 . ARG B 1 302 ? -13.771 15.559  -29.900 0.50  45.00 ? 302  ARG A NH1 1 
ATOM   4592 N NH2 . ARG B 1 302 ? -15.580 15.584  -31.310 0.50  45.72 ? 302  ARG A NH2 1 
ATOM   4593 N N   . THR B 1 303 ? -12.442 8.927   -25.914 1.00  31.67 ? 303  THR A N   1 
ATOM   4594 C CA  . THR B 1 303 ? -11.572 8.189   -24.994 1.00  32.83 ? 303  THR A CA  1 
ATOM   4595 C C   . THR B 1 303 ? -10.799 7.105   -25.727 1.00  35.13 ? 303  THR A C   1 
ATOM   4596 O O   . THR B 1 303 ? -9.621  6.863   -25.455 1.00  34.47 ? 303  THR A O   1 
ATOM   4597 C CB  . THR B 1 303 ? -12.386 7.455   -23.900 1.00  33.70 ? 303  THR A CB  1 
ATOM   4598 O OG1 . THR B 1 303 ? -13.112 8.397   -23.108 1.00  34.71 ? 303  THR A OG1 1 
ATOM   4599 C CG2 . THR B 1 303 ? -11.471 6.656   -23.012 1.00  34.29 ? 303  THR A CG2 1 
ATOM   4600 N N   . HIS B 1 304 ? -11.482 6.420   -26.636 1.00  29.55 ? 304  HIS A N   1 
ATOM   4601 C CA  . HIS B 1 304 ? -10.859 5.315   -27.344 1.00  32.81 ? 304  HIS A CA  1 
ATOM   4602 C C   . HIS B 1 304 ? -9.812  5.798   -28.343 1.00  33.66 ? 304  HIS A C   1 
ATOM   4603 O O   . HIS B 1 304 ? -8.779  5.153   -28.515 1.00  34.31 ? 304  HIS A O   1 
ATOM   4604 C CB  . HIS B 1 304 ? -11.902 4.467   -28.067 1.00  30.93 ? 304  HIS A CB  1 
ATOM   4605 C CG  . HIS B 1 304 ? -11.310 3.345   -28.855 1.00  34.56 ? 304  HIS A CG  1 
ATOM   4606 N ND1 . HIS B 1 304 ? -10.698 2.262   -28.265 1.00  29.78 ? 304  HIS A ND1 1 
ATOM   4607 C CD2 . HIS B 1 304 ? -11.201 3.154   -30.193 1.00  36.54 ? 304  HIS A CD2 1 
ATOM   4608 C CE1 . HIS B 1 304 ? -10.264 1.437   -29.199 1.00  35.42 ? 304  HIS A CE1 1 
ATOM   4609 N NE2 . HIS B 1 304 ? -10.552 1.960   -30.378 1.00  36.87 ? 304  HIS A NE2 1 
ATOM   4610 N N   . ASN B 1 305 ? -10.097 6.921   -28.999 1.00  32.71 ? 305  ASN A N   1 
ATOM   4611 C CA  . ASN B 1 305 ? -9.246  7.446   -30.077 1.00  39.43 ? 305  ASN A CA  1 
ATOM   4612 C C   . ASN B 1 305 ? -8.229  8.506   -29.655 1.00  42.77 ? 305  ASN A C   1 
ATOM   4613 O O   . ASN B 1 305 ? -7.623  9.148   -30.506 1.00  45.56 ? 305  ASN A O   1 
ATOM   4614 C CB  . ASN B 1 305 ? -10.112 8.062   -31.176 1.00  36.67 ? 305  ASN A CB  1 
ATOM   4615 C CG  . ASN B 1 305 ? -11.064 7.072   -31.786 1.00  40.32 ? 305  ASN A CG  1 
ATOM   4616 O OD1 . ASN B 1 305 ? -10.701 5.927   -32.042 1.00  46.27 ? 305  ASN A OD1 1 
ATOM   4617 N ND2 . ASN B 1 305 ? -12.298 7.499   -32.011 1.00  43.03 ? 305  ASN A ND2 1 
ATOM   4618 N N   . GLY B 1 306 ? -8.062  8.728   -28.358 1.00  44.80 ? 306  GLY A N   1 
ATOM   4619 C CA  . GLY B 1 306 ? -7.153  9.773   -27.911 1.00  38.31 ? 306  GLY A CA  1 
ATOM   4620 C C   . GLY B 1 306 ? -7.603  11.153  -28.354 1.00  39.07 ? 306  GLY A C   1 
ATOM   4621 O O   . GLY B 1 306 ? -6.831  12.112  -28.330 1.00  38.72 ? 306  GLY A O   1 
ATOM   4622 N N   . GLU B 1 307 ? -8.864  11.258  -28.757 1.00  40.09 ? 307  GLU A N   1 
ATOM   4623 C CA  . GLU B 1 307 ? -9.448  12.541  -29.140 1.00  45.78 ? 307  GLU A CA  1 
ATOM   4624 C C   . GLU B 1 307 ? -9.885  13.340  -27.911 1.00  50.45 ? 307  GLU A C   1 
ATOM   4625 O O   . GLU B 1 307 ? -10.105 12.774  -26.836 1.00  39.64 ? 307  GLU A O   1 
ATOM   4626 C CB  . GLU B 1 307 ? -10.649 12.322  -30.061 1.00  44.43 ? 307  GLU A CB  1 
ATOM   4627 C CG  . GLU B 1 307 ? -11.353 13.600  -30.509 1.00  49.87 ? 307  GLU A CG  1 
ATOM   4628 C CD  . GLU B 1 307 ? -10.678 14.252  -31.706 1.00  59.43 ? 307  GLU A CD  1 
ATOM   4629 O OE1 . GLU B 1 307 ? -9.537  13.853  -32.031 1.00  58.65 ? 307  GLU A OE1 1 
ATOM   4630 O OE2 . GLU B 1 307 ? -11.291 15.151  -32.328 1.00  55.83 ? 307  GLU A OE2 1 
ATOM   4631 N N   . SER B 1 308 ? -10.027 14.652  -28.083 1.00  48.37 ? 308  SER A N   1 
ATOM   4632 C CA  . SER B 1 308 ? -10.415 15.527  -26.984 1.00  48.56 ? 308  SER A CA  1 
ATOM   4633 C C   . SER B 1 308 ? -11.837 15.258  -26.497 1.00  46.53 ? 308  SER A C   1 
ATOM   4634 O O   . SER B 1 308 ? -12.781 15.236  -27.281 1.00  51.53 ? 308  SER A O   1 
ATOM   4635 C CB  . SER B 1 308 ? -10.280 16.996  -27.386 1.00  49.88 ? 308  SER A CB  1 
ATOM   4636 O OG  . SER B 1 308 ? -10.768 17.837  -26.349 1.00  54.22 ? 308  SER A OG  1 
ATOM   4637 N N   . VAL B 1 309 ? -11.978 15.058  -25.195 1.00  40.36 ? 309  VAL A N   1 
ATOM   4638 C CA  . VAL B 1 309 ? -13.288 14.903  -24.581 1.00  41.07 ? 309  VAL A CA  1 
ATOM   4639 C C   . VAL B 1 309 ? -13.780 16.235  -24.008 1.00  42.44 ? 309  VAL A C   1 
ATOM   4640 O O   . VAL B 1 309 ? -14.985 16.486  -23.949 1.00  45.13 ? 309  VAL A O   1 
ATOM   4641 C CB  . VAL B 1 309 ? -13.247 13.836  -23.477 1.00  43.95 ? 309  VAL A CB  1 
ATOM   4642 C CG1 . VAL B 1 309 ? -14.514 13.865  -22.642 1.00  40.23 ? 309  VAL A CG1 1 
ATOM   4643 C CG2 . VAL B 1 309 ? -13.013 12.454  -24.085 1.00  36.34 ? 309  VAL A CG2 1 
ATOM   4644 N N   . SER B 1 310 ? -12.847 17.097  -23.619 0.010 42.99 ? 310  SER A N   1 
ATOM   4645 C CA  . SER B 1 310 ? -13.194 18.372  -23.000 0.010 42.79 ? 310  SER A CA  1 
ATOM   4646 C C   . SER B 1 310 ? -14.102 19.222  -23.886 0.010 43.11 ? 310  SER A C   1 
ATOM   4647 O O   . SER B 1 310 ? -14.834 20.077  -23.392 0.010 42.71 ? 310  SER A O   1 
ATOM   4648 C CB  . SER B 1 310 ? -11.933 19.159  -22.639 0.010 42.86 ? 310  SER A CB  1 
ATOM   4649 O OG  . SER B 1 310 ? -11.320 19.696  -23.797 0.010 43.65 ? 310  SER A OG  1 
ATOM   4650 N N   . TYR B 1 311 ? -14.048 18.991  -25.194 0.20  43.55 ? 311  TYR A N   1 
ATOM   4651 C CA  . TYR B 1 311 ? -14.914 19.703  -26.129 0.20  44.75 ? 311  TYR A CA  1 
ATOM   4652 C C   . TYR B 1 311 ? -16.382 19.612  -25.712 0.20  43.50 ? 311  TYR A C   1 
ATOM   4653 O O   . TYR B 1 311 ? -17.102 20.609  -25.724 0.20  41.97 ? 311  TYR A O   1 
ATOM   4654 C CB  . TYR B 1 311 ? -14.729 19.164  -27.551 0.20  45.83 ? 311  TYR A CB  1 
ATOM   4655 C CG  . TYR B 1 311 ? -15.819 19.581  -28.514 0.20  47.33 ? 311  TYR A CG  1 
ATOM   4656 C CD1 . TYR B 1 311 ? -16.252 20.900  -28.574 0.20  48.25 ? 311  TYR A CD1 1 
ATOM   4657 C CD2 . TYR B 1 311 ? -16.407 18.659  -29.371 0.20  46.89 ? 311  TYR A CD2 1 
ATOM   4658 C CE1 . TYR B 1 311 ? -17.246 21.287  -29.450 0.20  48.26 ? 311  TYR A CE1 1 
ATOM   4659 C CE2 . TYR B 1 311 ? -17.401 19.039  -30.255 0.20  49.35 ? 311  TYR A CE2 1 
ATOM   4660 C CZ  . TYR B 1 311 ? -17.816 20.357  -30.287 0.20  50.94 ? 311  TYR A CZ  1 
ATOM   4661 O OH  . TYR B 1 311 ? -18.806 20.745  -31.162 0.20  52.93 ? 311  TYR A OH  1 
ATOM   4662 N N   . LEU B 1 312 ? -16.811 18.411  -25.337 1.00  43.90 ? 312  LEU A N   1 
ATOM   4663 C CA  . LEU B 1 312 ? -18.196 18.158  -24.946 1.00  41.02 ? 312  LEU A CA  1 
ATOM   4664 C C   . LEU B 1 312 ? -18.624 18.936  -23.702 1.00  44.78 ? 312  LEU A C   1 
ATOM   4665 O O   . LEU B 1 312 ? -19.820 19.070  -23.441 1.00  50.86 ? 312  LEU A O   1 
ATOM   4666 C CB  . LEU B 1 312 ? -18.413 16.669  -24.672 1.00  33.70 ? 312  LEU A CB  1 
ATOM   4667 C CG  . LEU B 1 312 ? -18.203 15.601  -25.748 1.00  43.68 ? 312  LEU A CG  1 
ATOM   4668 C CD1 . LEU B 1 312 ? -18.262 14.211  -25.111 1.00  33.10 ? 312  LEU A CD1 1 
ATOM   4669 C CD2 . LEU B 1 312 ? -19.244 15.733  -26.862 1.00  40.79 ? 312  LEU A CD2 1 
ATOM   4670 N N   . PHE B 1 313 ? -17.663 19.424  -22.922 0.40  41.93 ? 313  PHE A N   1 
ATOM   4671 C CA  . PHE B 1 313 ? -17.986 20.098  -21.664 0.40  42.85 ? 313  PHE A CA  1 
ATOM   4672 C C   . PHE B 1 313 ? -18.888 21.309  -21.881 0.40  43.64 ? 313  PHE A C   1 
ATOM   4673 O O   . PHE B 1 313 ? -19.265 21.991  -20.925 0.40  39.81 ? 313  PHE A O   1 
ATOM   4674 C CB  . PHE B 1 313 ? -16.719 20.516  -20.911 0.40  43.29 ? 313  PHE A CB  1 
ATOM   4675 C CG  . PHE B 1 313 ? -15.918 19.363  -20.377 0.40  41.97 ? 313  PHE A CG  1 
ATOM   4676 C CD1 . PHE B 1 313 ? -14.652 19.568  -19.852 0.40  39.93 ? 313  PHE A CD1 1 
ATOM   4677 C CD2 . PHE B 1 313 ? -16.428 18.075  -20.402 0.40  40.17 ? 313  PHE A CD2 1 
ATOM   4678 C CE1 . PHE B 1 313 ? -13.913 18.511  -19.357 0.40  39.41 ? 313  PHE A CE1 1 
ATOM   4679 C CE2 . PHE B 1 313 ? -15.693 17.015  -19.911 0.40  37.44 ? 313  PHE A CE2 1 
ATOM   4680 C CZ  . PHE B 1 313 ? -14.433 17.231  -19.389 0.40  38.87 ? 313  PHE A CZ  1 
HETATM 4681 S S   . SO4 C 2 .   ? -2.907  -18.433 18.111  1.00  33.45 ? 1002 SO4 B S   1 
HETATM 4682 O O1  . SO4 C 2 .   ? -2.785  -17.211 18.891  1.00  33.17 ? 1002 SO4 B O1  1 
HETATM 4683 O O2  . SO4 C 2 .   ? -2.666  -19.596 18.955  1.00  34.51 ? 1002 SO4 B O2  1 
HETATM 4684 O O3  . SO4 C 2 .   ? -4.259  -18.509 17.571  1.00  39.66 ? 1002 SO4 B O3  1 
HETATM 4685 O O4  . SO4 C 2 .   ? -1.941  -18.443 17.026  1.00  32.51 ? 1002 SO4 B O4  1 
HETATM 4686 S S   . SO4 D 2 .   ? -27.648 -26.526 -2.564  1.00  50.29 ? 1003 SO4 B S   1 
HETATM 4687 O O1  . SO4 D 2 .   ? -28.152 -25.281 -3.148  1.00  44.60 ? 1003 SO4 B O1  1 
HETATM 4688 O O2  . SO4 D 2 .   ? -27.810 -26.496 -1.104  1.00  34.42 ? 1003 SO4 B O2  1 
HETATM 4689 O O3  . SO4 D 2 .   ? -28.403 -27.649 -3.124  1.00  41.24 ? 1003 SO4 B O3  1 
HETATM 4690 O O4  . SO4 D 2 .   ? -26.232 -26.655 -2.905  1.00  52.31 ? 1003 SO4 B O4  1 
HETATM 4691 S S   . SO4 E 2 .   ? -7.329  -23.439 7.349   0.53  42.68 ? 1005 SO4 B S   1 
HETATM 4692 O O1  . SO4 E 2 .   ? -7.845  -22.075 7.424   0.53  30.11 ? 1005 SO4 B O1  1 
HETATM 4693 O O2  . SO4 E 2 .   ? -6.593  -23.761 8.574   0.53  43.06 ? 1005 SO4 B O2  1 
HETATM 4694 O O3  . SO4 E 2 .   ? -8.455  -24.352 7.175   0.53  39.82 ? 1005 SO4 B O3  1 
HETATM 4695 O O4  . SO4 E 2 .   ? -6.419  -23.572 6.218   0.53  38.97 ? 1005 SO4 B O4  1 
HETATM 4696 S S   . SO4 F 2 .   ? -8.940  16.381  -23.511 1.00  38.23 ? 1001 SO4 A S   1 
HETATM 4697 O O1  . SO4 F 2 .   ? -8.079  16.668  -22.386 1.00  37.18 ? 1001 SO4 A O1  1 
HETATM 4698 O O2  . SO4 F 2 .   ? -10.261 16.018  -23.020 1.00  40.61 ? 1001 SO4 A O2  1 
HETATM 4699 O O3  . SO4 F 2 .   ? -9.038  17.557  -24.360 1.00  44.49 ? 1001 SO4 A O3  1 
HETATM 4700 O O4  . SO4 F 2 .   ? -8.392  15.279  -24.290 1.00  38.71 ? 1001 SO4 A O4  1 
HETATM 4701 S S   . SO4 G 2 .   ? -34.927 15.229  -1.929  0.68  57.85 ? 1004 SO4 A S   1 
HETATM 4702 O O1  . SO4 G 2 .   ? -33.527 15.636  -1.807  0.68  57.01 ? 1004 SO4 A O1  1 
HETATM 4703 O O2  . SO4 G 2 .   ? -35.757 16.033  -1.027  0.68  58.57 ? 1004 SO4 A O2  1 
HETATM 4704 O O3  . SO4 G 2 .   ? -35.351 15.423  -3.319  0.68  54.09 ? 1004 SO4 A O3  1 
HETATM 4705 O O4  . SO4 G 2 .   ? -35.060 13.823  -1.552  0.68  51.59 ? 1004 SO4 A O4  1 
HETATM 4706 S S   . SO4 H 2 .   ? -14.762 19.769  -12.863 0.47  47.27 ? 1006 SO4 A S   1 
HETATM 4707 O O1  . SO4 H 2 .   ? -13.829 19.970  -11.759 0.47  42.46 ? 1006 SO4 A O1  1 
HETATM 4708 O O2  . SO4 H 2 .   ? -15.682 20.903  -12.927 0.47  50.68 ? 1006 SO4 A O2  1 
HETATM 4709 O O3  . SO4 H 2 .   ? -13.989 19.688  -14.104 0.47  49.79 ? 1006 SO4 A O3  1 
HETATM 4710 O O4  . SO4 H 2 .   ? -15.539 18.544  -12.686 0.47  33.33 ? 1006 SO4 A O4  1 
HETATM 4711 O O   . HOH I 3 .   ? -26.093 -20.717 9.692   1.00  24.62 ? 3001 HOH B O   1 
HETATM 4712 O O   . HOH I 3 .   ? -14.256 8.250   16.921  1.00  23.09 ? 3002 HOH B O   1 
HETATM 4713 O O   . HOH I 3 .   ? -33.750 -40.605 7.885   1.00  30.10 ? 3003 HOH B O   1 
HETATM 4714 O O   . HOH I 3 .   ? -17.236 -18.342 6.319   1.00  24.89 ? 3004 HOH B O   1 
HETATM 4715 O O   . HOH I 3 .   ? -19.920 -33.625 -6.957  1.00  36.67 ? 3005 HOH B O   1 
HETATM 4716 O O   . HOH I 3 .   ? -15.396 -27.134 10.786  1.00  30.17 ? 3006 HOH B O   1 
HETATM 4717 O O   . HOH I 3 .   ? -23.869 -5.815  7.526   1.00  31.17 ? 3007 HOH B O   1 
HETATM 4718 O O   . HOH I 3 .   ? -7.315  -8.652  -0.311  1.00  27.37 ? 3009 HOH B O   1 
HETATM 4719 O O   . HOH I 3 .   ? -5.948  -20.922 5.320   1.00  36.98 ? 3010 HOH B O   1 
HETATM 4720 O O   . HOH I 3 .   ? -18.958 -1.102  25.214  1.00  25.32 ? 3012 HOH B O   1 
HETATM 4721 O O   . HOH I 3 .   ? -6.943  -2.947  5.180   1.00  24.54 ? 3015 HOH B O   1 
HETATM 4722 O O   . HOH I 3 .   ? -5.593  -7.545  2.718   1.00  25.71 ? 3018 HOH B O   1 
HETATM 4723 O O   . HOH I 3 .   ? -19.393 -2.294  22.559  1.00  28.18 ? 3021 HOH B O   1 
HETATM 4724 O O   . HOH I 3 .   ? -22.191 -45.234 19.521  1.00  32.66 ? 3024 HOH B O   1 
HETATM 4725 O O   . HOH I 3 .   ? -18.433 -31.889 3.139   1.00  32.53 ? 3025 HOH B O   1 
HETATM 4726 O O   . HOH I 3 .   ? -10.036 -6.793  -6.953  1.00  26.48 ? 3028 HOH B O   1 
HETATM 4727 O O   . HOH I 3 .   ? -13.736 -30.425 2.005   1.00  36.05 ? 3030 HOH B O   1 
HETATM 4728 O O   . HOH I 3 .   ? -37.181 -25.923 13.703  1.00  33.06 ? 3031 HOH B O   1 
HETATM 4729 O O   . HOH I 3 .   ? 0.263   -12.646 2.757   1.00  37.48 ? 3032 HOH B O   1 
HETATM 4730 O O   . HOH I 3 .   ? -24.518 -2.023  17.000  1.00  28.38 ? 3034 HOH B O   1 
HETATM 4731 O O   . HOH I 3 .   ? -18.627 -21.936 3.843   1.00  31.62 ? 3035 HOH B O   1 
HETATM 4732 O O   . HOH I 3 .   ? -7.223  -19.410 10.947  1.00  29.51 ? 3038 HOH B O   1 
HETATM 4733 O O   . HOH I 3 .   ? -7.816  4.809   11.821  1.00  29.87 ? 3039 HOH B O   1 
HETATM 4734 O O   . HOH I 3 .   ? -12.554 -23.606 6.127   1.00  29.05 ? 3041 HOH B O   1 
HETATM 4735 O O   . HOH I 3 .   ? -16.187 8.708   10.588  1.00  32.44 ? 3043 HOH B O   1 
HETATM 4736 O O   . HOH I 3 .   ? -3.836  -3.318  8.912   1.00  33.21 ? 3044 HOH B O   1 
HETATM 4737 O O   . HOH I 3 .   ? -16.492 -25.570 17.255  1.00  33.47 ? 3045 HOH B O   1 
HETATM 4738 O O   . HOH I 3 .   ? -26.634 -10.354 14.305  1.00  32.17 ? 3046 HOH B O   1 
HETATM 4739 O O   . HOH I 3 .   ? -4.296  -13.861 5.804   1.00  29.36 ? 3047 HOH B O   1 
HETATM 4740 O O   . HOH I 3 .   ? -17.384 -34.688 21.591  1.00  41.14 ? 3048 HOH B O   1 
HETATM 4741 O O   . HOH I 3 .   ? -14.161 -26.313 -0.756  1.00  48.53 ? 3049 HOH B O   1 
HETATM 4742 O O   . HOH I 3 .   ? -15.076 -24.464 19.347  1.00  35.14 ? 3052 HOH B O   1 
HETATM 4743 O O   . HOH I 3 .   ? -26.777 -4.342  23.333  1.00  37.35 ? 3055 HOH B O   1 
HETATM 4744 O O   . HOH I 3 .   ? -22.820 1.203   23.726  1.00  37.85 ? 3057 HOH B O   1 
HETATM 4745 O O   . HOH I 3 .   ? -18.337 -5.135  31.351  1.00  34.60 ? 3058 HOH B O   1 
HETATM 4746 O O   . HOH I 3 .   ? -22.479 -28.582 20.276  1.00  29.59 ? 3059 HOH B O   1 
HETATM 4747 O O   . HOH I 3 .   ? -37.901 -32.742 -0.424  1.00  43.96 ? 3060 HOH B O   1 
HETATM 4748 O O   . HOH I 3 .   ? -24.167 -13.661 8.877   1.00  42.09 ? 3061 HOH B O   1 
HETATM 4749 O O   . HOH I 3 .   ? -28.469 -13.519 14.040  1.00  34.15 ? 3064 HOH B O   1 
HETATM 4750 O O   . HOH I 3 .   ? -15.807 -1.240  26.006  1.00  31.73 ? 3066 HOH B O   1 
HETATM 4751 O O   . HOH I 3 .   ? -15.108 -2.375  28.190  1.00  32.74 ? 3067 HOH B O   1 
HETATM 4752 O O   . HOH I 3 .   ? -8.735  2.404   4.406   1.00  39.11 ? 3068 HOH B O   1 
HETATM 4753 O O   . HOH I 3 .   ? -31.482 -19.397 6.989   1.00  33.33 ? 3069 HOH B O   1 
HETATM 4754 O O   . HOH I 3 .   ? -27.404 -10.397 11.718  1.00  44.64 ? 3072 HOH B O   1 
HETATM 4755 O O   . HOH I 3 .   ? -4.386  -14.552 13.187  1.00  30.25 ? 3075 HOH B O   1 
HETATM 4756 O O   . HOH I 3 .   ? -14.291 -25.429 7.389   1.00  38.27 ? 3076 HOH B O   1 
HETATM 4757 O O   . HOH I 3 .   ? -34.543 -17.346 9.636   1.00  43.77 ? 3079 HOH B O   1 
HETATM 4758 O O   . HOH I 3 .   ? -6.869  9.975   17.530  1.00  36.12 ? 3081 HOH B O   1 
HETATM 4759 O O   . HOH I 3 .   ? -20.265 -18.256 2.868   1.00  41.09 ? 3084 HOH B O   1 
HETATM 4760 O O   . HOH I 3 .   ? -2.594  -14.249 3.608   1.00  29.75 ? 3086 HOH B O   1 
HETATM 4761 O O   . HOH I 3 .   ? -26.034 -24.769 20.940  1.00  38.03 ? 3089 HOH B O   1 
HETATM 4762 O O   . HOH I 3 .   ? -9.455  3.078   24.834  1.00  44.04 ? 3090 HOH B O   1 
HETATM 4763 O O   . HOH I 3 .   ? -17.429 -46.117 4.166   1.00  39.86 ? 3092 HOH B O   1 
HETATM 4764 O O   . HOH I 3 .   ? -31.473 -4.994  2.684   1.00  42.61 ? 3093 HOH B O   1 
HETATM 4765 O O   . HOH I 3 .   ? -3.332  -10.072 -4.359  1.00  30.76 ? 3094 HOH B O   1 
HETATM 4766 O O   . HOH I 3 .   ? -3.554  -5.771  10.256  1.00  31.72 ? 3095 HOH B O   1 
HETATM 4767 O O   . HOH I 3 .   ? -15.164 -7.762  27.474  1.00  47.26 ? 3096 HOH B O   1 
HETATM 4768 O O   . HOH I 3 .   ? -30.068 -41.361 18.634  1.00  46.03 ? 3097 HOH B O   1 
HETATM 4769 O O   . HOH I 3 .   ? -10.198 -7.784  27.786  1.00  41.16 ? 3099 HOH B O   1 
HETATM 4770 O O   . HOH I 3 .   ? -18.839 9.230   22.476  1.00  39.49 ? 3101 HOH B O   1 
HETATM 4771 O O   . HOH I 3 .   ? -17.523 -29.200 2.415   1.00  39.66 ? 3102 HOH B O   1 
HETATM 4772 O O   . HOH I 3 .   ? -3.617  -11.729 27.993  1.00  49.15 ? 3105 HOH B O   1 
HETATM 4773 O O   . HOH I 3 .   ? -24.052 -43.597 22.508  1.00  37.18 ? 3106 HOH B O   1 
HETATM 4774 O O   . HOH I 3 .   ? -31.835 -16.265 7.248   1.00  38.39 ? 3107 HOH B O   1 
HETATM 4775 O O   . HOH I 3 .   ? -0.014  -14.878 22.361  1.00  35.47 ? 3108 HOH B O   1 
HETATM 4776 O O   . HOH I 3 .   ? -15.844 -45.338 16.476  1.00  42.03 ? 3110 HOH B O   1 
HETATM 4777 O O   . HOH I 3 .   ? -39.263 -23.078 1.029   1.00  45.20 ? 3112 HOH B O   1 
HETATM 4778 O O   . HOH I 3 .   ? -9.182  5.337   23.786  1.00  44.21 ? 3113 HOH B O   1 
HETATM 4779 O O   . HOH I 3 .   ? -6.246  7.442   18.727  1.00  41.35 ? 3115 HOH B O   1 
HETATM 4780 O O   . HOH I 3 .   ? -31.415 -38.915 -5.122  1.00  38.56 ? 3116 HOH B O   1 
HETATM 4781 O O   . HOH I 3 .   ? -35.439 -15.617 7.822   1.00  45.55 ? 3117 HOH B O   1 
HETATM 4782 O O   . HOH I 3 .   ? -27.645 -1.624  3.097   1.00  35.80 ? 3120 HOH B O   1 
HETATM 4783 O O   . HOH I 3 .   ? -15.863 -26.988 2.440   1.00  41.43 ? 3123 HOH B O   1 
HETATM 4784 O O   . HOH I 3 .   ? -32.438 -26.006 17.932  1.00  35.99 ? 3124 HOH B O   1 
HETATM 4785 O O   . HOH I 3 .   ? -17.636 -19.306 3.491   1.00  30.49 ? 3126 HOH B O   1 
HETATM 4786 O O   . HOH I 3 .   ? -23.967 -45.550 -6.286  1.00  42.85 ? 3127 HOH B O   1 
HETATM 4787 O O   . HOH I 3 .   ? -1.036  -8.586  -1.973  1.00  33.55 ? 3128 HOH B O   1 
HETATM 4788 O O   . HOH I 3 .   ? 0.582   -10.803 4.093   1.00  37.85 ? 3131 HOH B O   1 
HETATM 4789 O O   . HOH I 3 .   ? -14.152 -45.367 4.912   1.00  38.28 ? 3132 HOH B O   1 
HETATM 4790 O O   . HOH I 3 .   ? -12.236 3.552   4.614   1.00  34.85 ? 3133 HOH B O   1 
HETATM 4791 O O   . HOH I 3 .   ? -2.711  -18.324 14.128  1.00  42.63 ? 3137 HOH B O   1 
HETATM 4792 O O   . HOH I 3 .   ? -34.865 -15.543 11.859  1.00  42.77 ? 3139 HOH B O   1 
HETATM 4793 O O   . HOH I 3 .   ? -36.791 -21.736 1.674   1.00  42.84 ? 3140 HOH B O   1 
HETATM 4794 O O   . HOH I 3 .   ? -35.304 -35.622 -3.540  1.00  47.90 ? 3141 HOH B O   1 
HETATM 4795 O O   . HOH I 3 .   ? -27.847 -28.871 -0.512  1.00  41.37 ? 3144 HOH B O   1 
HETATM 4796 O O   . HOH I 3 .   ? -29.521 -23.104 19.933  1.00  44.09 ? 3145 HOH B O   1 
HETATM 4797 O O   . HOH I 3 .   ? -14.683 -31.230 9.112   1.00  40.93 ? 3146 HOH B O   1 
HETATM 4798 O O   . HOH I 3 .   ? -10.225 -26.337 -0.993  1.00  49.16 ? 3149 HOH B O   1 
HETATM 4799 O O   . HOH I 3 .   ? -12.667 -31.396 18.081  1.00  45.89 ? 3151 HOH B O   1 
HETATM 4800 O O   . HOH I 3 .   ? -24.438 -23.784 -2.257  1.00  50.21 ? 3153 HOH B O   1 
HETATM 4801 O O   . HOH I 3 .   ? -17.254 5.456   23.052  1.00  37.93 ? 3154 HOH B O   1 
HETATM 4802 O O   . HOH I 3 .   ? -16.881 -23.341 -4.856  1.00  40.63 ? 3155 HOH B O   1 
HETATM 4803 O O   . HOH I 3 .   ? -5.898  -11.371 29.267  1.00  49.84 ? 3157 HOH B O   1 
HETATM 4804 O O   . HOH I 3 .   ? -13.530 -23.041 16.017  1.00  36.13 ? 3160 HOH B O   1 
HETATM 4805 O O   . HOH I 3 .   ? -25.256 -8.504  12.582  1.00  38.16 ? 3161 HOH B O   1 
HETATM 4806 O O   . HOH I 3 .   ? -34.911 -36.319 0.852   1.00  43.82 ? 3163 HOH B O   1 
HETATM 4807 O O   . HOH I 3 .   ? -21.429 -40.892 23.840  1.00  41.18 ? 3164 HOH B O   1 
HETATM 4808 O O   . HOH I 3 .   ? -41.385 -25.721 13.774  1.00  47.30 ? 3169 HOH B O   1 
HETATM 4809 O O   . HOH I 3 .   ? -23.187 -24.349 21.345  1.00  38.05 ? 3170 HOH B O   1 
HETATM 4810 O O   . HOH I 3 .   ? -22.143 -33.161 25.241  1.00  46.61 ? 3172 HOH B O   1 
HETATM 4811 O O   . HOH I 3 .   ? -5.739  -4.806  21.649  1.00  43.86 ? 3174 HOH B O   1 
HETATM 4812 O O   . HOH I 3 .   ? -10.289 -15.297 -16.937 1.00  41.34 ? 3175 HOH B O   1 
HETATM 4813 O O   . HOH I 3 .   ? -8.486  -4.110  27.360  1.00  38.36 ? 3176 HOH B O   1 
HETATM 4814 O O   . HOH I 3 .   ? -5.908  4.640   9.823   1.00  44.78 ? 3179 HOH B O   1 
HETATM 4815 O O   . HOH I 3 .   ? -39.486 -31.803 -2.737  1.00  53.90 ? 3180 HOH B O   1 
HETATM 4816 O O   . HOH I 3 .   ? -10.431 -4.877  15.959  1.00  30.00 ? 3181 HOH B O   1 
HETATM 4817 O O   . HOH J 3 .   ? -21.253 -17.970 -1.845  1.00  39.00 ? 3008 HOH A O   1 
HETATM 4818 O O   . HOH J 3 .   ? -7.491  0.410   -10.754 1.00  23.72 ? 3011 HOH A O   1 
HETATM 4819 O O   . HOH J 3 .   ? -23.967 -6.146  -22.470 1.00  27.15 ? 3013 HOH A O   1 
HETATM 4820 O O   . HOH J 3 .   ? -11.283 11.644  7.735   1.00  28.92 ? 3014 HOH A O   1 
HETATM 4821 O O   . HOH J 3 .   ? -7.752  5.271   -8.360  1.00  22.52 ? 3016 HOH A O   1 
HETATM 4822 O O   . HOH J 3 .   ? -6.647  8.278   -1.232  1.00  28.62 ? 3017 HOH A O   1 
HETATM 4823 O O   . HOH J 3 .   ? -19.232 -4.242  -27.973 1.00  27.61 ? 3019 HOH A O   1 
HETATM 4824 O O   . HOH J 3 .   ? -8.773  11.775  -11.070 1.00  28.38 ? 3020 HOH A O   1 
HETATM 4825 O O   . HOH J 3 .   ? -9.685  5.657   -5.083  1.00  24.69 ? 3022 HOH A O   1 
HETATM 4826 O O   . HOH J 3 .   ? -22.545 11.406  -11.536 1.00  29.97 ? 3023 HOH A O   1 
HETATM 4827 O O   . HOH J 3 .   ? -19.914 17.977  -11.197 1.00  31.96 ? 3026 HOH A O   1 
HETATM 4828 O O   . HOH J 3 .   ? -8.561  15.796  -19.464 1.00  34.83 ? 3027 HOH A O   1 
HETATM 4829 O O   . HOH J 3 .   ? -23.366 12.618  -8.820  1.00  33.53 ? 3029 HOH A O   1 
HETATM 4830 O O   . HOH J 3 .   ? -12.451 -13.536 -16.089 1.00  34.70 ? 3033 HOH A O   1 
HETATM 4831 O O   . HOH J 3 .   ? -10.759 -12.617 -22.238 1.00  29.25 ? 3036 HOH A O   1 
HETATM 4832 O O   . HOH J 3 .   ? -25.628 3.738   -11.252 1.00  48.33 ? 3037 HOH A O   1 
HETATM 4833 O O   . HOH J 3 .   ? -6.192  -13.840 -18.857 1.00  37.19 ? 3040 HOH A O   1 
HETATM 4834 O O   . HOH J 3 .   ? -31.921 10.344  -14.699 1.00  39.58 ? 3042 HOH A O   1 
HETATM 4835 O O   . HOH J 3 .   ? -31.422 -5.871  -7.983  1.00  41.37 ? 3050 HOH A O   1 
HETATM 4836 O O   . HOH J 3 .   ? -26.710 -4.627  -28.929 1.00  33.05 ? 3051 HOH A O   1 
HETATM 4837 O O   . HOH J 3 .   ? -11.767 3.177   1.440   1.00  27.53 ? 3053 HOH A O   1 
HETATM 4838 O O   . HOH J 3 .   ? -7.371  12.594  -9.097  1.00  31.32 ? 3054 HOH A O   1 
HETATM 4839 O O   . HOH J 3 .   ? -12.571 17.925  -10.443 1.00  43.01 ? 3056 HOH A O   1 
HETATM 4840 O O   . HOH J 3 .   ? -13.343 15.851  -16.106 1.00  35.58 ? 3062 HOH A O   1 
HETATM 4841 O O   . HOH J 3 .   ? -35.662 36.826  1.926   1.00  50.91 ? 3063 HOH A O   1 
HETATM 4842 O O   . HOH J 3 .   ? -15.676 -4.453  -31.613 1.00  38.17 ? 3065 HOH A O   1 
HETATM 4843 O O   . HOH J 3 .   ? -12.857 13.555  12.149  1.00  40.52 ? 3070 HOH A O   1 
HETATM 4844 O O   . HOH J 3 .   ? -28.561 23.620  -7.849  1.00  40.53 ? 3071 HOH A O   1 
HETATM 4845 O O   . HOH J 3 .   ? -25.246 14.571  -8.816  1.00  40.87 ? 3073 HOH A O   1 
HETATM 4846 O O   . HOH J 3 .   ? -6.298  -4.505  -6.926  1.00  36.74 ? 3074 HOH A O   1 
HETATM 4847 O O   . HOH J 3 .   ? -30.979 33.781  -29.349 1.00  54.66 ? 3077 HOH A O   1 
HETATM 4848 O O   . HOH J 3 .   ? -26.874 -0.530  -17.725 1.00  42.27 ? 3078 HOH A O   1 
HETATM 4849 O O   . HOH J 3 .   ? -21.157 11.075  4.570   1.00  40.80 ? 3080 HOH A O   1 
HETATM 4850 O O   . HOH J 3 .   ? -35.725 -6.186  -17.969 1.00  54.60 ? 3082 HOH A O   1 
HETATM 4851 O O   . HOH J 3 .   ? -43.798 12.247  -19.229 1.00  50.55 ? 3083 HOH A O   1 
HETATM 4852 O O   . HOH J 3 .   ? -38.671 34.790  1.657   1.00  49.20 ? 3085 HOH A O   1 
HETATM 4853 O O   . HOH J 3 .   ? -32.729 5.458   -22.527 1.00  46.63 ? 3087 HOH A O   1 
HETATM 4854 O O   . HOH J 3 .   ? -23.647 24.357  -6.579  1.00  39.74 ? 3088 HOH A O   1 
HETATM 4855 O O   . HOH J 3 .   ? -4.174  -4.534  -27.443 1.00  43.22 ? 3091 HOH A O   1 
HETATM 4856 O O   . HOH J 3 .   ? -4.694  14.209  -27.775 1.00  41.71 ? 3098 HOH A O   1 
HETATM 4857 O O   . HOH J 3 .   ? -26.674 -7.745  -8.396  1.00  31.40 ? 3100 HOH A O   1 
HETATM 4858 O O   . HOH J 3 .   ? -7.961  8.143   -23.687 1.00  37.25 ? 3103 HOH A O   1 
HETATM 4859 O O   . HOH J 3 .   ? -5.327  4.439   -15.644 1.00  33.79 ? 3104 HOH A O   1 
HETATM 4860 O O   . HOH J 3 .   ? -35.349 25.268  12.192  1.00  49.90 ? 3109 HOH A O   1 
HETATM 4861 O O   . HOH J 3 .   ? -33.998 36.559  4.044   1.00  50.76 ? 3111 HOH A O   1 
HETATM 4862 O O   . HOH J 3 .   ? -45.891 26.510  -13.065 1.00  52.21 ? 3114 HOH A O   1 
HETATM 4863 O O   . HOH J 3 .   ? -23.001 13.618  7.847   1.00  43.35 ? 3118 HOH A O   1 
HETATM 4864 O O   . HOH J 3 .   ? -20.794 -8.836  -29.076 1.00  42.45 ? 3119 HOH A O   1 
HETATM 4865 O O   . HOH J 3 .   ? -4.639  2.001   -14.329 1.00  39.78 ? 3121 HOH A O   1 
HETATM 4866 O O   . HOH J 3 .   ? -35.463 12.176  -25.158 1.00  51.07 ? 3122 HOH A O   1 
HETATM 4867 O O   . HOH J 3 .   ? -34.392 38.536  -0.958  1.00  46.69 ? 3125 HOH A O   1 
HETATM 4868 O O   . HOH J 3 .   ? -7.968  -8.464  -9.118  1.00  40.61 ? 3129 HOH A O   1 
HETATM 4869 O O   . HOH J 3 .   ? -42.542 18.306  -0.768  1.00  56.09 ? 3130 HOH A O   1 
HETATM 4870 O O   . HOH J 3 .   ? -37.016 35.646  -26.178 1.00  50.86 ? 3134 HOH A O   1 
HETATM 4871 O O   . HOH J 3 .   ? -9.630  13.170  -13.004 1.00  38.97 ? 3136 HOH A O   1 
HETATM 4872 O O   . HOH J 3 .   ? -42.904 6.334   -21.005 1.00  55.64 ? 3138 HOH A O   1 
HETATM 4873 O O   . HOH J 3 .   ? -43.458 24.861  -20.786 1.00  48.77 ? 3142 HOH A O   1 
HETATM 4874 O O   . HOH J 3 .   ? -5.966  -0.273  -12.761 1.00  42.77 ? 3143 HOH A O   1 
HETATM 4875 O O   . HOH J 3 .   ? -41.015 20.863  7.739   1.00  47.70 ? 3147 HOH A O   1 
HETATM 4876 O O   . HOH J 3 .   ? -20.807 -11.768 -31.220 1.00  40.67 ? 3148 HOH A O   1 
HETATM 4877 O O   . HOH J 3 .   ? -5.892  -7.110  -17.048 1.00  35.45 ? 3152 HOH A O   1 
HETATM 4878 O O   . HOH J 3 .   ? -45.044 8.017   -21.192 1.00  58.21 ? 3156 HOH A O   1 
HETATM 4879 O O   . HOH J 3 .   ? -23.618 16.827  -0.213  1.00  42.80 ? 3158 HOH A O   1 
HETATM 4880 O O   . HOH J 3 .   ? -33.009 0.611   -19.751 1.00  45.54 ? 3162 HOH A O   1 
HETATM 4881 O O   . HOH J 3 .   ? -10.781 -3.962  -33.291 1.00  48.17 ? 3165 HOH A O   1 
HETATM 4882 O O   . HOH J 3 .   ? -6.648  -2.164  -27.926 1.00  55.24 ? 3166 HOH A O   1 
HETATM 4883 O O   . HOH J 3 .   ? -29.773 37.648  -9.527  1.00  50.05 ? 3167 HOH A O   1 
HETATM 4884 O O   . HOH J 3 .   ? -30.530 24.589  2.723   1.00  47.43 ? 3168 HOH A O   1 
HETATM 4885 O O   . HOH J 3 .   ? -26.494 4.252   -9.053  1.00  50.09 ? 3171 HOH A O   1 
HETATM 4886 O O   . HOH J 3 .   ? -8.920  -1.152  -33.556 1.00  53.08 ? 3177 HOH A O   1 
HETATM 4887 O O   . HOH J 3 .   ? -47.249 37.493  -9.750  1.00  57.32 ? 3178 HOH A O   1 
HETATM 4888 O O   . HOH J 3 .   ? -11.430 1.079   -21.220 1.00  30.00 ? 3182 HOH A O   1 
# 
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   1   ?   ?   ?   B . n 
A 1 2   PRO 2   2   ?   ?   ?   B . n 
A 1 3   ASN 3   3   3   ASN ASN B . n 
A 1 4   ILE 4   4   4   ILE ILE B . n 
A 1 5   LYS 5   5   5   LYS LYS B . n 
A 1 6   ILE 6   6   6   ILE ILE B . n 
A 1 7   PHE 7   7   7   PHE PHE B . n 
A 1 8   SER 8   8   8   SER SER B . n 
A 1 9   GLY 9   9   9   GLY GLY B . n 
A 1 10  SER 10  10  10  SER SER B . n 
A 1 11  SER 11  11  11  SER SER B . n 
A 1 12  HIS 12  12  12  HIS HIS B . n 
A 1 13  GLN 13  13  13  GLN GLN B . n 
A 1 14  ASP 14  14  14  ASP ASP B . n 
A 1 15  LEU 15  15  15  LEU LEU B . n 
A 1 16  SER 16  16  16  SER SER B . n 
A 1 17  GLN 17  17  17  GLN GLN B . n 
A 1 18  LYS 18  18  18  LYS LYS B . n 
A 1 19  ILE 19  19  19  ILE ILE B . n 
A 1 20  ALA 20  20  20  ALA ALA B . n 
A 1 21  ASP 21  21  21  ASP ASP B . n 
A 1 22  ARG 22  22  22  ARG ARG B . n 
A 1 23  LEU 23  23  23  LEU LEU B . n 
A 1 24  GLY 24  24  24  GLY GLY B . n 
A 1 25  LEU 25  25  25  LEU LEU B . n 
A 1 26  GLU 26  26  26  GLU GLU B . n 
A 1 27  LEU 27  27  27  LEU LEU B . n 
A 1 28  GLY 28  28  28  GLY GLY B . n 
A 1 29  LYS 29  29  29  LYS LYS B . n 
A 1 30  VAL 30  30  30  VAL VAL B . n 
A 1 31  VAL 31  31  31  VAL VAL B . n 
A 1 32  THR 32  32  32  THR THR B . n 
A 1 33  LYS 33  33  33  LYS LYS B . n 
A 1 34  LYS 34  34  34  LYS LYS B . n 
A 1 35  PHE 35  35  35  PHE PHE B . n 
A 1 36  SER 36  36  36  SER SER B . n 
A 1 37  ASN 37  37  37  ASN ASN B . n 
A 1 38  GLN 38  38  38  GLN GLN B . n 
A 1 39  GLU 39  39  39  GLU GLU B . n 
A 1 40  THR 40  40  40  THR THR B . n 
A 1 41  CYS 41  41  41  CYS CYS B . n 
A 1 42  VAL 42  42  42  VAL VAL B . n 
A 1 43  GLU 43  43  43  GLU GLU B . n 
A 1 44  ILE 44  44  44  ILE ILE B . n 
A 1 45  GLY 45  45  45  GLY GLY B . n 
A 1 46  GLU 46  46  46  GLU GLU B . n 
A 1 47  SER 47  47  47  SER SER B . n 
A 1 48  VAL 48  48  48  VAL VAL B . n 
A 1 49  ARG 49  49  49  ARG ARG B . n 
A 1 50  GLY 50  50  50  GLY GLY B . n 
A 1 51  GLU 51  51  51  GLU GLU B . n 
A 1 52  ASP 52  52  52  ASP ASP B . n 
A 1 53  VAL 53  53  53  VAL VAL B . n 
A 1 54  TYR 54  54  54  TYR TYR B . n 
A 1 55  ILE 55  55  55  ILE ILE B . n 
A 1 56  VAL 56  56  56  VAL VAL B . n 
A 1 57  GLN 57  57  57  GLN GLN B . n 
A 1 58  SER 58  58  58  SER SER B . n 
A 1 59  GLY 59  59  59  GLY GLY B . n 
A 1 60  CYS 60  60  60  CYS CYS B . n 
A 1 61  GLY 61  61  61  GLY GLY B . n 
A 1 62  GLU 62  62  62  GLU GLU B . n 
A 1 63  ILE 63  63  63  ILE ILE B . n 
A 1 64  ASN 64  64  64  ASN ASN B . n 
A 1 65  ASP 65  65  65  ASP ASP B . n 
A 1 66  ASN 66  66  66  ASN ASN B . n 
A 1 67  LEU 67  67  67  LEU LEU B . n 
A 1 68  MET 68  68  68  MET MET B . n 
A 1 69  GLU 69  69  69  GLU GLU B . n 
A 1 70  LEU 70  70  70  LEU LEU B . n 
A 1 71  LEU 71  71  71  LEU LEU B . n 
A 1 72  ILE 72  72  72  ILE ILE B . n 
A 1 73  MET 73  73  73  MET MET B . n 
A 1 74  ILE 74  74  74  ILE ILE B . n 
A 1 75  ASN 75  75  75  ASN ASN B . n 
A 1 76  ALA 76  76  76  ALA ALA B . n 
A 1 77  CYS 77  77  77  CYS CYS B . n 
A 1 78  LYS 78  78  78  LYS LYS B . n 
A 1 79  ILE 79  79  79  ILE ILE B . n 
A 1 80  ALA 80  80  80  ALA ALA B . n 
A 1 81  SER 81  81  81  SER SER B . n 
A 1 82  ALA 82  82  82  ALA ALA B . n 
A 1 83  SER 83  83  83  SER SER B . n 
A 1 84  ARG 84  84  84  ARG ARG B . n 
A 1 85  VAL 85  85  85  VAL VAL B . n 
A 1 86  THR 86  86  86  THR THR B . n 
A 1 87  ALA 87  87  87  ALA ALA B . n 
A 1 88  VAL 88  88  88  VAL VAL B . n 
A 1 89  ILE 89  89  89  ILE ILE B . n 
A 1 90  PRO 90  90  90  PRO PRO B . n 
A 1 91  CYS 91  91  91  CYS CYS B . n 
A 1 92  PHE 92  92  92  PHE PHE B . n 
A 1 93  PRO 93  93  93  PRO PRO B . n 
A 1 94  TYR 94  94  94  TYR TYR B . n 
A 1 95  ALA 95  95  95  ALA ALA B . n 
A 1 96  ARG 96  96  96  ARG ARG B . n 
A 1 97  GLN 97  97  97  GLN GLN B . n 
A 1 98  ASP 98  98  98  ASP ASP B . n 
A 1 99  LYS 99  99  99  LYS LYS B . n 
A 1 100 LYS 100 100 100 LYS LYS B . n 
A 1 101 ASP 101 101 101 ASP ASP B . n 
A 1 102 LYS 102 102 102 LYS LYS B . n 
A 1 103 SER 103 103 103 SER SER B . n 
A 1 104 ARG 104 104 104 ARG ARG B . n 
A 1 105 ALA 105 105 105 ALA ALA B . n 
A 1 106 PRO 106 106 106 PRO PRO B . n 
A 1 107 ILE 107 107 107 ILE ILE B . n 
A 1 108 SER 108 108 108 SER SER B . n 
A 1 109 ALA 109 109 109 ALA ALA B . n 
A 1 110 LYS 110 110 110 LYS LYS B . n 
A 1 111 LEU 111 111 111 LEU LEU B . n 
A 1 112 VAL 112 112 112 VAL VAL B . n 
A 1 113 ALA 113 113 113 ALA ALA B . n 
A 1 114 ASN 114 114 114 ASN ASN B . n 
A 1 115 MET 115 115 115 MET MET B . n 
A 1 116 LEU 116 116 116 LEU LEU B . n 
A 1 117 SER 117 117 117 SER SER B . n 
A 1 118 VAL 118 118 118 VAL VAL B . n 
A 1 119 ALA 119 119 119 ALA ALA B . n 
A 1 120 GLY 120 120 120 GLY GLY B . n 
A 1 121 ALA 121 121 121 ALA ALA B . n 
A 1 122 ASP 122 122 122 ASP ASP B . n 
A 1 123 HIS 123 123 123 HIS HIS B . n 
A 1 124 ILE 124 124 124 ILE ILE B . n 
A 1 125 ILE 125 125 125 ILE ILE B . n 
A 1 126 THR 126 126 126 THR THR B . n 
A 1 127 MET 127 127 127 MET MET B . n 
A 1 128 ASP 128 128 128 ASP ASP B . n 
A 1 129 LEU 129 129 129 LEU LEU B . n 
A 1 130 HIS 130 130 130 HIS HIS B . n 
A 1 131 ALA 131 131 131 ALA ALA B . n 
A 1 132 SER 132 132 132 SER SER B . n 
A 1 133 GLN 133 133 133 GLN GLN B . n 
A 1 134 ILE 134 134 134 ILE ILE B . n 
A 1 135 GLN 135 135 135 GLN GLN B . n 
A 1 136 GLY 136 136 136 GLY GLY B . n 
A 1 137 PHE 137 137 137 PHE PHE B . n 
A 1 138 PHE 138 138 138 PHE PHE B . n 
A 1 139 ASP 139 139 139 ASP ASP B . n 
A 1 140 ILE 140 140 140 ILE ILE B . n 
A 1 141 PRO 141 141 141 PRO PRO B . n 
A 1 142 VAL 142 142 142 VAL VAL B . n 
A 1 143 ASP 143 143 143 ASP ASP B . n 
A 1 144 ASN 144 144 144 ASN ASN B . n 
A 1 145 LEU 145 145 145 LEU LEU B . n 
A 1 146 TYR 146 146 146 TYR TYR B . n 
A 1 147 ALA 147 147 147 ALA ALA B . n 
A 1 148 GLU 148 148 148 GLU GLU B . n 
A 1 149 PRO 149 149 149 PRO PRO B . n 
A 1 150 ALA 150 150 150 ALA ALA B . n 
A 1 151 VAL 151 151 151 VAL VAL B . n 
A 1 152 LEU 152 152 152 LEU LEU B . n 
A 1 153 LYS 153 153 153 LYS LYS B . n 
A 1 154 TRP 154 154 154 TRP TRP B . n 
A 1 155 ILE 155 155 155 ILE ILE B . n 
A 1 156 ARG 156 156 156 ARG ARG B . n 
A 1 157 GLU 157 157 157 GLU GLU B . n 
A 1 158 ASN 158 158 158 ASN ASN B . n 
A 1 159 ILE 159 159 159 ILE ILE B . n 
A 1 160 SER 160 160 160 SER SER B . n 
A 1 161 GLU 161 161 161 GLU GLU B . n 
A 1 162 TRP 162 162 162 TRP TRP B . n 
A 1 163 ARG 163 163 163 ARG ARG B . n 
A 1 164 ASN 164 164 164 ASN ASN B . n 
A 1 165 CYS 165 165 165 CYS CYS B . n 
A 1 166 THR 166 166 166 THR THR B . n 
A 1 167 ILE 167 167 167 ILE ILE B . n 
A 1 168 VAL 168 168 168 VAL VAL B . n 
A 1 169 SER 169 169 169 SER SER B . n 
A 1 170 PRO 170 170 170 PRO PRO B . n 
A 1 171 ASP 171 171 171 ASP ASP B . n 
A 1 172 ALA 172 172 172 ALA ALA B . n 
A 1 173 GLY 173 173 173 GLY GLY B . n 
A 1 174 GLY 174 174 174 GLY GLY B . n 
A 1 175 ALA 175 175 175 ALA ALA B . n 
A 1 176 LYS 176 176 176 LYS LYS B . n 
A 1 177 ARG 177 177 177 ARG ARG B . n 
A 1 178 VAL 178 178 178 VAL VAL B . n 
A 1 179 THR 179 179 179 THR THR B . n 
A 1 180 SER 180 180 180 SER SER B . n 
A 1 181 ILE 181 181 181 ILE ILE B . n 
A 1 182 ALA 182 182 182 ALA ALA B . n 
A 1 183 ASP 183 183 183 ASP ASP B . n 
A 1 184 ARG 184 184 184 ARG ARG B . n 
A 1 185 LEU 185 185 185 LEU LEU B . n 
A 1 186 ASN 186 186 186 ASN ASN B . n 
A 1 187 VAL 187 187 187 VAL VAL B . n 
A 1 188 ASP 188 188 188 ASP ASP B . n 
A 1 189 PHE 189 189 189 PHE PHE B . n 
A 1 190 ALA 190 190 190 ALA ALA B . n 
A 1 191 LEU 191 191 191 LEU LEU B . n 
A 1 192 ILE 192 192 192 ILE ILE B . n 
A 1 193 HIS 193 193 193 HIS HIS B . n 
A 1 194 LYS 194 194 194 LYS LYS B . n 
A 1 195 GLU 195 195 195 GLU GLU B . n 
A 1 196 ARG 196 196 ?   ?   ?   B . n 
A 1 197 LYS 197 197 ?   ?   ?   B . n 
A 1 198 LYS 198 198 ?   ?   ?   B . n 
A 1 199 ALA 199 199 ?   ?   ?   B . n 
A 1 200 ASN 200 200 ?   ?   ?   B . n 
A 1 201 GLU 201 201 ?   ?   ?   B . n 
A 1 202 VAL 202 202 ?   ?   ?   B . n 
A 1 203 ASP 203 203 203 ASP ASP B . n 
A 1 204 ARG 204 204 204 ARG ARG B . n 
A 1 205 MET 205 205 205 MET MET B . n 
A 1 206 VAL 206 206 206 VAL VAL B . n 
A 1 207 LEU 207 207 207 LEU LEU B . n 
A 1 208 VAL 208 208 208 VAL VAL B . n 
A 1 209 GLY 209 209 209 GLY GLY B . n 
A 1 210 ASP 210 210 210 ASP ASP B . n 
A 1 211 VAL 211 211 211 VAL VAL B . n 
A 1 212 LYS 212 212 212 LYS LYS B . n 
A 1 213 ASP 213 213 213 ASP ASP B . n 
A 1 214 ARG 214 214 214 ARG ARG B . n 
A 1 215 VAL 215 215 215 VAL VAL B . n 
A 1 216 ALA 216 216 216 ALA ALA B . n 
A 1 217 ILE 217 217 217 ILE ILE B . n 
A 1 218 LEU 218 218 218 LEU LEU B . n 
A 1 219 VAL 219 219 219 VAL VAL B . n 
A 1 220 ASP 220 220 220 ASP ASP B . n 
A 1 221 ASP 221 221 221 ASP ASP B . n 
A 1 222 MET 222 222 222 MET MET B . n 
A 1 223 ALA 223 223 223 ALA ALA B . n 
A 1 224 ASP 224 224 224 ASP ASP B . n 
A 1 225 THR 225 225 225 THR THR B . n 
A 1 226 CYS 226 226 226 CYS CYS B . n 
A 1 227 GLY 227 227 227 GLY GLY B . n 
A 1 228 THR 228 228 228 THR THR B . n 
A 1 229 ILE 229 229 229 ILE ILE B . n 
A 1 230 CYS 230 230 230 CYS CYS B . n 
A 1 231 HIS 231 231 231 HIS HIS B . n 
A 1 232 ALA 232 232 232 ALA ALA B . n 
A 1 233 ALA 233 233 233 ALA ALA B . n 
A 1 234 ASP 234 234 234 ASP ASP B . n 
A 1 235 LYS 235 235 235 LYS LYS B . n 
A 1 236 LEU 236 236 236 LEU LEU B . n 
A 1 237 LEU 237 237 237 LEU LEU B . n 
A 1 238 SER 238 238 238 SER SER B . n 
A 1 239 ALA 239 239 239 ALA ALA B . n 
A 1 240 GLY 240 240 240 GLY GLY B . n 
A 1 241 ALA 241 241 241 ALA ALA B . n 
A 1 242 THR 242 242 242 THR THR B . n 
A 1 243 ARG 243 243 243 ARG ARG B . n 
A 1 244 VAL 244 244 244 VAL VAL B . n 
A 1 245 TYR 245 245 245 TYR TYR B . n 
A 1 246 ALA 246 246 246 ALA ALA B . n 
A 1 247 ILE 247 247 247 ILE ILE B . n 
A 1 248 LEU 248 248 248 LEU LEU B . n 
A 1 249 THR 249 249 249 THR THR B . n 
A 1 250 HIS 250 250 250 HIS HIS B . n 
A 1 251 GLY 251 251 251 GLY GLY B . n 
A 1 252 ILE 252 252 252 ILE ILE B . n 
A 1 253 PHE 253 253 253 PHE PHE B . n 
A 1 254 SER 254 254 254 SER SER B . n 
A 1 255 GLY 255 255 255 GLY GLY B . n 
A 1 256 PRO 256 256 256 PRO PRO B . n 
A 1 257 ALA 257 257 257 ALA ALA B . n 
A 1 258 ILE 258 258 258 ILE ILE B . n 
A 1 259 SER 259 259 259 SER SER B . n 
A 1 260 ARG 260 260 260 ARG ARG B . n 
A 1 261 ILE 261 261 261 ILE ILE B . n 
A 1 262 ASN 262 262 262 ASN ASN B . n 
A 1 263 ASN 263 263 263 ASN ASN B . n 
A 1 264 ALA 264 264 264 ALA ALA B . n 
A 1 265 CYS 265 265 265 CYS CYS B . n 
A 1 266 PHE 266 266 266 PHE PHE B . n 
A 1 267 GLU 267 267 267 GLU GLU B . n 
A 1 268 ALA 268 268 268 ALA ALA B . n 
A 1 269 VAL 269 269 269 VAL VAL B . n 
A 1 270 VAL 270 270 270 VAL VAL B . n 
A 1 271 VAL 271 271 271 VAL VAL B . n 
A 1 272 THR 272 272 272 THR THR B . n 
A 1 273 ASN 273 273 273 ASN ASN B . n 
A 1 274 THR 274 274 274 THR THR B . n 
A 1 275 ILE 275 275 275 ILE ILE B . n 
A 1 276 PRO 276 276 276 PRO PRO B . n 
A 1 277 GLN 277 277 277 GLN GLN B . n 
A 1 278 GLU 278 278 278 GLU GLU B . n 
A 1 279 ASP 279 279 279 ASP ASP B . n 
A 1 280 LYS 280 280 280 LYS LYS B . n 
A 1 281 MET 281 281 281 MET MET B . n 
A 1 282 LYS 282 282 282 LYS LYS B . n 
A 1 283 HIS 283 283 283 HIS HIS B . n 
A 1 284 CYS 284 284 284 CYS CYS B . n 
A 1 285 SER 285 285 285 SER SER B . n 
A 1 286 LYS 286 286 286 LYS LYS B . n 
A 1 287 ILE 287 287 287 ILE ILE B . n 
A 1 288 GLN 288 288 288 GLN GLN B . n 
A 1 289 VAL 289 289 289 VAL VAL B . n 
A 1 290 ILE 290 290 290 ILE ILE B . n 
A 1 291 ASP 291 291 291 ASP ASP B . n 
A 1 292 ILE 292 292 292 ILE ILE B . n 
A 1 293 SER 293 293 293 SER SER B . n 
A 1 294 MET 294 294 294 MET MET B . n 
A 1 295 ILE 295 295 295 ILE ILE B . n 
A 1 296 LEU 296 296 296 LEU LEU B . n 
A 1 297 ALA 297 297 297 ALA ALA B . n 
A 1 298 GLU 298 298 298 GLU GLU B . n 
A 1 299 ALA 299 299 299 ALA ALA B . n 
A 1 300 ILE 300 300 300 ILE ILE B . n 
A 1 301 ARG 301 301 301 ARG ARG B . n 
A 1 302 ARG 302 302 302 ARG ARG B . n 
A 1 303 THR 303 303 303 THR THR B . n 
A 1 304 HIS 304 304 304 HIS HIS B . n 
A 1 305 ASN 305 305 305 ASN ASN B . n 
A 1 306 GLY 306 306 306 GLY GLY B . n 
A 1 307 GLU 307 307 307 GLU GLU B . n 
A 1 308 SER 308 308 308 SER SER B . n 
A 1 309 VAL 309 309 309 VAL VAL B . n 
A 1 310 SER 310 310 310 SER SER B . n 
A 1 311 TYR 311 311 311 TYR TYR B . n 
A 1 312 LEU 312 312 312 LEU LEU B . n 
A 1 313 PHE 313 313 313 PHE PHE B . n 
A 1 314 SER 314 314 314 SER SER B . n 
A 1 315 HIS 315 315 315 HIS HIS B . n 
A 1 316 VAL 316 316 316 VAL VAL B . n 
A 1 317 PRO 317 317 317 PRO PRO B . n 
A 1 318 LEU 318 318 ?   ?   ?   B . n 
A 1 319 LEU 319 319 ?   ?   ?   B . n 
A 1 320 GLU 320 320 ?   ?   ?   B . n 
A 1 321 HIS 321 321 ?   ?   ?   B . n 
A 1 322 HIS 322 322 ?   ?   ?   B . n 
A 1 323 HIS 323 323 ?   ?   ?   B . n 
A 1 324 HIS 324 324 ?   ?   ?   B . n 
A 1 325 HIS 325 325 ?   ?   ?   B . n 
A 1 326 HIS 326 326 ?   ?   ?   B . n 
B 1 1   MET 1   1   ?   ?   ?   A . n 
B 1 2   PRO 2   2   ?   ?   ?   A . n 
B 1 3   ASN 3   3   3   ASN ASN A . n 
B 1 4   ILE 4   4   4   ILE ILE A . n 
B 1 5   LYS 5   5   5   LYS LYS A . n 
B 1 6   ILE 6   6   6   ILE ILE A . n 
B 1 7   PHE 7   7   7   PHE PHE A . n 
B 1 8   SER 8   8   8   SER SER A . n 
B 1 9   GLY 9   9   9   GLY GLY A . n 
B 1 10  SER 10  10  10  SER SER A . n 
B 1 11  SER 11  11  11  SER SER A . n 
B 1 12  HIS 12  12  12  HIS HIS A . n 
B 1 13  GLN 13  13  13  GLN GLN A . n 
B 1 14  ASP 14  14  14  ASP ASP A . n 
B 1 15  LEU 15  15  15  LEU LEU A . n 
B 1 16  SER 16  16  16  SER SER A . n 
B 1 17  GLN 17  17  17  GLN GLN A . n 
B 1 18  LYS 18  18  18  LYS LYS A . n 
B 1 19  ILE 19  19  19  ILE ILE A . n 
B 1 20  ALA 20  20  20  ALA ALA A . n 
B 1 21  ASP 21  21  21  ASP ASP A . n 
B 1 22  ARG 22  22  22  ARG ARG A . n 
B 1 23  LEU 23  23  23  LEU LEU A . n 
B 1 24  GLY 24  24  24  GLY GLY A . n 
B 1 25  LEU 25  25  25  LEU LEU A . n 
B 1 26  GLU 26  26  26  GLU GLU A . n 
B 1 27  LEU 27  27  27  LEU LEU A . n 
B 1 28  GLY 28  28  28  GLY GLY A . n 
B 1 29  LYS 29  29  29  LYS LYS A . n 
B 1 30  VAL 30  30  30  VAL VAL A . n 
B 1 31  VAL 31  31  31  VAL VAL A . n 
B 1 32  THR 32  32  32  THR THR A . n 
B 1 33  LYS 33  33  33  LYS LYS A . n 
B 1 34  LYS 34  34  34  LYS LYS A . n 
B 1 35  PHE 35  35  35  PHE PHE A . n 
B 1 36  SER 36  36  36  SER SER A . n 
B 1 37  ASN 37  37  37  ASN ASN A . n 
B 1 38  GLN 38  38  38  GLN GLN A . n 
B 1 39  GLU 39  39  39  GLU GLU A . n 
B 1 40  THR 40  40  40  THR THR A . n 
B 1 41  CYS 41  41  41  CYS CYS A . n 
B 1 42  VAL 42  42  42  VAL VAL A . n 
B 1 43  GLU 43  43  43  GLU GLU A . n 
B 1 44  ILE 44  44  44  ILE ILE A . n 
B 1 45  GLY 45  45  45  GLY GLY A . n 
B 1 46  GLU 46  46  46  GLU GLU A . n 
B 1 47  SER 47  47  47  SER SER A . n 
B 1 48  VAL 48  48  48  VAL VAL A . n 
B 1 49  ARG 49  49  49  ARG ARG A . n 
B 1 50  GLY 50  50  50  GLY GLY A . n 
B 1 51  GLU 51  51  51  GLU GLU A . n 
B 1 52  ASP 52  52  52  ASP ASP A . n 
B 1 53  VAL 53  53  53  VAL VAL A . n 
B 1 54  TYR 54  54  54  TYR TYR A . n 
B 1 55  ILE 55  55  55  ILE ILE A . n 
B 1 56  VAL 56  56  56  VAL VAL A . n 
B 1 57  GLN 57  57  57  GLN GLN A . n 
B 1 58  SER 58  58  58  SER SER A . n 
B 1 59  GLY 59  59  59  GLY GLY A . n 
B 1 60  CYS 60  60  60  CYS CYS A . n 
B 1 61  GLY 61  61  61  GLY GLY A . n 
B 1 62  GLU 62  62  62  GLU GLU A . n 
B 1 63  ILE 63  63  63  ILE ILE A . n 
B 1 64  ASN 64  64  64  ASN ASN A . n 
B 1 65  ASP 65  65  65  ASP ASP A . n 
B 1 66  ASN 66  66  66  ASN ASN A . n 
B 1 67  LEU 67  67  67  LEU LEU A . n 
B 1 68  MET 68  68  68  MET MET A . n 
B 1 69  GLU 69  69  69  GLU GLU A . n 
B 1 70  LEU 70  70  70  LEU LEU A . n 
B 1 71  LEU 71  71  71  LEU LEU A . n 
B 1 72  ILE 72  72  72  ILE ILE A . n 
B 1 73  MET 73  73  73  MET MET A . n 
B 1 74  ILE 74  74  74  ILE ILE A . n 
B 1 75  ASN 75  75  75  ASN ASN A . n 
B 1 76  ALA 76  76  76  ALA ALA A . n 
B 1 77  CYS 77  77  77  CYS CYS A . n 
B 1 78  LYS 78  78  78  LYS LYS A . n 
B 1 79  ILE 79  79  79  ILE ILE A . n 
B 1 80  ALA 80  80  80  ALA ALA A . n 
B 1 81  SER 81  81  81  SER SER A . n 
B 1 82  ALA 82  82  82  ALA ALA A . n 
B 1 83  SER 83  83  83  SER SER A . n 
B 1 84  ARG 84  84  84  ARG ARG A . n 
B 1 85  VAL 85  85  85  VAL VAL A . n 
B 1 86  THR 86  86  86  THR THR A . n 
B 1 87  ALA 87  87  87  ALA ALA A . n 
B 1 88  VAL 88  88  88  VAL VAL A . n 
B 1 89  ILE 89  89  89  ILE ILE A . n 
B 1 90  PRO 90  90  90  PRO PRO A . n 
B 1 91  CYS 91  91  91  CYS CYS A . n 
B 1 92  PHE 92  92  92  PHE PHE A . n 
B 1 93  PRO 93  93  93  PRO PRO A . n 
B 1 94  TYR 94  94  94  TYR TYR A . n 
B 1 95  ALA 95  95  95  ALA ALA A . n 
B 1 96  ARG 96  96  96  ARG ARG A . n 
B 1 97  GLN 97  97  97  GLN GLN A . n 
B 1 98  ASP 98  98  98  ASP ASP A . n 
B 1 99  LYS 99  99  99  LYS LYS A . n 
B 1 100 LYS 100 100 100 LYS LYS A . n 
B 1 101 ASP 101 101 101 ASP ASP A . n 
B 1 102 LYS 102 102 102 LYS LYS A . n 
B 1 103 SER 103 103 103 SER SER A . n 
B 1 104 ARG 104 104 104 ARG ARG A . n 
B 1 105 ALA 105 105 105 ALA ALA A . n 
B 1 106 PRO 106 106 106 PRO PRO A . n 
B 1 107 ILE 107 107 107 ILE ILE A . n 
B 1 108 SER 108 108 108 SER SER A . n 
B 1 109 ALA 109 109 109 ALA ALA A . n 
B 1 110 LYS 110 110 110 LYS LYS A . n 
B 1 111 LEU 111 111 111 LEU LEU A . n 
B 1 112 VAL 112 112 112 VAL VAL A . n 
B 1 113 ALA 113 113 113 ALA ALA A . n 
B 1 114 ASN 114 114 114 ASN ASN A . n 
B 1 115 MET 115 115 115 MET MET A . n 
B 1 116 LEU 116 116 116 LEU LEU A . n 
B 1 117 SER 117 117 117 SER SER A . n 
B 1 118 VAL 118 118 118 VAL VAL A . n 
B 1 119 ALA 119 119 119 ALA ALA A . n 
B 1 120 GLY 120 120 120 GLY GLY A . n 
B 1 121 ALA 121 121 121 ALA ALA A . n 
B 1 122 ASP 122 122 122 ASP ASP A . n 
B 1 123 HIS 123 123 123 HIS HIS A . n 
B 1 124 ILE 124 124 124 ILE ILE A . n 
B 1 125 ILE 125 125 125 ILE ILE A . n 
B 1 126 THR 126 126 126 THR THR A . n 
B 1 127 MET 127 127 127 MET MET A . n 
B 1 128 ASP 128 128 128 ASP ASP A . n 
B 1 129 LEU 129 129 129 LEU LEU A . n 
B 1 130 HIS 130 130 130 HIS HIS A . n 
B 1 131 ALA 131 131 131 ALA ALA A . n 
B 1 132 SER 132 132 132 SER SER A . n 
B 1 133 GLN 133 133 133 GLN GLN A . n 
B 1 134 ILE 134 134 134 ILE ILE A . n 
B 1 135 GLN 135 135 135 GLN GLN A . n 
B 1 136 GLY 136 136 136 GLY GLY A . n 
B 1 137 PHE 137 137 137 PHE PHE A . n 
B 1 138 PHE 138 138 138 PHE PHE A . n 
B 1 139 ASP 139 139 139 ASP ASP A . n 
B 1 140 ILE 140 140 140 ILE ILE A . n 
B 1 141 PRO 141 141 141 PRO PRO A . n 
B 1 142 VAL 142 142 142 VAL VAL A . n 
B 1 143 ASP 143 143 143 ASP ASP A . n 
B 1 144 ASN 144 144 144 ASN ASN A . n 
B 1 145 LEU 145 145 145 LEU LEU A . n 
B 1 146 TYR 146 146 146 TYR TYR A . n 
B 1 147 ALA 147 147 147 ALA ALA A . n 
B 1 148 GLU 148 148 148 GLU GLU A . n 
B 1 149 PRO 149 149 149 PRO PRO A . n 
B 1 150 ALA 150 150 150 ALA ALA A . n 
B 1 151 VAL 151 151 151 VAL VAL A . n 
B 1 152 LEU 152 152 152 LEU LEU A . n 
B 1 153 LYS 153 153 153 LYS LYS A . n 
B 1 154 TRP 154 154 154 TRP TRP A . n 
B 1 155 ILE 155 155 155 ILE ILE A . n 
B 1 156 ARG 156 156 156 ARG ARG A . n 
B 1 157 GLU 157 157 157 GLU GLU A . n 
B 1 158 ASN 158 158 158 ASN ASN A . n 
B 1 159 ILE 159 159 159 ILE ILE A . n 
B 1 160 SER 160 160 160 SER SER A . n 
B 1 161 GLU 161 161 161 GLU GLU A . n 
B 1 162 TRP 162 162 162 TRP TRP A . n 
B 1 163 ARG 163 163 163 ARG ARG A . n 
B 1 164 ASN 164 164 164 ASN ASN A . n 
B 1 165 CYS 165 165 165 CYS CYS A . n 
B 1 166 THR 166 166 166 THR THR A . n 
B 1 167 ILE 167 167 167 ILE ILE A . n 
B 1 168 VAL 168 168 168 VAL VAL A . n 
B 1 169 SER 169 169 169 SER SER A . n 
B 1 170 PRO 170 170 170 PRO PRO A . n 
B 1 171 ASP 171 171 171 ASP ASP A . n 
B 1 172 ALA 172 172 172 ALA ALA A . n 
B 1 173 GLY 173 173 173 GLY GLY A . n 
B 1 174 GLY 174 174 174 GLY GLY A . n 
B 1 175 ALA 175 175 175 ALA ALA A . n 
B 1 176 LYS 176 176 176 LYS LYS A . n 
B 1 177 ARG 177 177 177 ARG ARG A . n 
B 1 178 VAL 178 178 178 VAL VAL A . n 
B 1 179 THR 179 179 179 THR THR A . n 
B 1 180 SER 180 180 180 SER SER A . n 
B 1 181 ILE 181 181 181 ILE ILE A . n 
B 1 182 ALA 182 182 182 ALA ALA A . n 
B 1 183 ASP 183 183 183 ASP ASP A . n 
B 1 184 ARG 184 184 184 ARG ARG A . n 
B 1 185 LEU 185 185 185 LEU LEU A . n 
B 1 186 ASN 186 186 186 ASN ASN A . n 
B 1 187 VAL 187 187 187 VAL VAL A . n 
B 1 188 ASP 188 188 188 ASP ASP A . n 
B 1 189 PHE 189 189 189 PHE PHE A . n 
B 1 190 ALA 190 190 190 ALA ALA A . n 
B 1 191 LEU 191 191 191 LEU LEU A . n 
B 1 192 ILE 192 192 192 ILE ILE A . n 
B 1 193 HIS 193 193 193 HIS HIS A . n 
B 1 194 LYS 194 194 194 LYS LYS A . n 
B 1 195 GLU 195 195 195 GLU GLU A . n 
B 1 196 ARG 196 196 ?   ?   ?   A . n 
B 1 197 LYS 197 197 ?   ?   ?   A . n 
B 1 198 LYS 198 198 ?   ?   ?   A . n 
B 1 199 ALA 199 199 ?   ?   ?   A . n 
B 1 200 ASN 200 200 ?   ?   ?   A . n 
B 1 201 GLU 201 201 ?   ?   ?   A . n 
B 1 202 VAL 202 202 ?   ?   ?   A . n 
B 1 203 ASP 203 203 203 ASP ASP A . n 
B 1 204 ARG 204 204 204 ARG ARG A . n 
B 1 205 MET 205 205 205 MET MET A . n 
B 1 206 VAL 206 206 206 VAL VAL A . n 
B 1 207 LEU 207 207 207 LEU LEU A . n 
B 1 208 VAL 208 208 208 VAL VAL A . n 
B 1 209 GLY 209 209 209 GLY GLY A . n 
B 1 210 ASP 210 210 210 ASP ASP A . n 
B 1 211 VAL 211 211 211 VAL VAL A . n 
B 1 212 LYS 212 212 212 LYS LYS A . n 
B 1 213 ASP 213 213 213 ASP ASP A . n 
B 1 214 ARG 214 214 214 ARG ARG A . n 
B 1 215 VAL 215 215 215 VAL VAL A . n 
B 1 216 ALA 216 216 216 ALA ALA A . n 
B 1 217 ILE 217 217 217 ILE ILE A . n 
B 1 218 LEU 218 218 218 LEU LEU A . n 
B 1 219 VAL 219 219 219 VAL VAL A . n 
B 1 220 ASP 220 220 220 ASP ASP A . n 
B 1 221 ASP 221 221 221 ASP ASP A . n 
B 1 222 MET 222 222 222 MET MET A . n 
B 1 223 ALA 223 223 223 ALA ALA A . n 
B 1 224 ASP 224 224 224 ASP ASP A . n 
B 1 225 THR 225 225 225 THR THR A . n 
B 1 226 CYS 226 226 226 CYS CYS A . n 
B 1 227 GLY 227 227 227 GLY GLY A . n 
B 1 228 THR 228 228 228 THR THR A . n 
B 1 229 ILE 229 229 229 ILE ILE A . n 
B 1 230 CYS 230 230 230 CYS CYS A . n 
B 1 231 HIS 231 231 231 HIS HIS A . n 
B 1 232 ALA 232 232 232 ALA ALA A . n 
B 1 233 ALA 233 233 233 ALA ALA A . n 
B 1 234 ASP 234 234 234 ASP ASP A . n 
B 1 235 LYS 235 235 235 LYS LYS A . n 
B 1 236 LEU 236 236 236 LEU LEU A . n 
B 1 237 LEU 237 237 237 LEU LEU A . n 
B 1 238 SER 238 238 238 SER SER A . n 
B 1 239 ALA 239 239 239 ALA ALA A . n 
B 1 240 GLY 240 240 240 GLY GLY A . n 
B 1 241 ALA 241 241 241 ALA ALA A . n 
B 1 242 THR 242 242 242 THR THR A . n 
B 1 243 ARG 243 243 243 ARG ARG A . n 
B 1 244 VAL 244 244 244 VAL VAL A . n 
B 1 245 TYR 245 245 245 TYR TYR A . n 
B 1 246 ALA 246 246 246 ALA ALA A . n 
B 1 247 ILE 247 247 247 ILE ILE A . n 
B 1 248 LEU 248 248 248 LEU LEU A . n 
B 1 249 THR 249 249 249 THR THR A . n 
B 1 250 HIS 250 250 250 HIS HIS A . n 
B 1 251 GLY 251 251 251 GLY GLY A . n 
B 1 252 ILE 252 252 252 ILE ILE A . n 
B 1 253 PHE 253 253 253 PHE PHE A . n 
B 1 254 SER 254 254 254 SER SER A . n 
B 1 255 GLY 255 255 255 GLY GLY A . n 
B 1 256 PRO 256 256 256 PRO PRO A . n 
B 1 257 ALA 257 257 257 ALA ALA A . n 
B 1 258 ILE 258 258 258 ILE ILE A . n 
B 1 259 SER 259 259 259 SER SER A . n 
B 1 260 ARG 260 260 260 ARG ARG A . n 
B 1 261 ILE 261 261 261 ILE ILE A . n 
B 1 262 ASN 262 262 262 ASN ASN A . n 
B 1 263 ASN 263 263 263 ASN ASN A . n 
B 1 264 ALA 264 264 264 ALA ALA A . n 
B 1 265 CYS 265 265 265 CYS CYS A . n 
B 1 266 PHE 266 266 266 PHE PHE A . n 
B 1 267 GLU 267 267 267 GLU GLU A . n 
B 1 268 ALA 268 268 268 ALA ALA A . n 
B 1 269 VAL 269 269 269 VAL VAL A . n 
B 1 270 VAL 270 270 270 VAL VAL A . n 
B 1 271 VAL 271 271 271 VAL VAL A . n 
B 1 272 THR 272 272 272 THR THR A . n 
B 1 273 ASN 273 273 273 ASN ASN A . n 
B 1 274 THR 274 274 274 THR THR A . n 
B 1 275 ILE 275 275 275 ILE ILE A . n 
B 1 276 PRO 276 276 276 PRO PRO A . n 
B 1 277 GLN 277 277 277 GLN GLN A . n 
B 1 278 GLU 278 278 278 GLU GLU A . n 
B 1 279 ASP 279 279 279 ASP ASP A . n 
B 1 280 LYS 280 280 280 LYS LYS A . n 
B 1 281 MET 281 281 281 MET MET A . n 
B 1 282 LYS 282 282 282 LYS LYS A . n 
B 1 283 HIS 283 283 283 HIS HIS A . n 
B 1 284 CYS 284 284 284 CYS CYS A . n 
B 1 285 SER 285 285 285 SER SER A . n 
B 1 286 LYS 286 286 286 LYS LYS A . n 
B 1 287 ILE 287 287 287 ILE ILE A . n 
B 1 288 GLN 288 288 288 GLN GLN A . n 
B 1 289 VAL 289 289 289 VAL VAL A . n 
B 1 290 ILE 290 290 290 ILE ILE A . n 
B 1 291 ASP 291 291 291 ASP ASP A . n 
B 1 292 ILE 292 292 292 ILE ILE A . n 
B 1 293 SER 293 293 293 SER SER A . n 
B 1 294 MET 294 294 294 MET MET A . n 
B 1 295 ILE 295 295 295 ILE ILE A . n 
B 1 296 LEU 296 296 296 LEU LEU A . n 
B 1 297 ALA 297 297 297 ALA ALA A . n 
B 1 298 GLU 298 298 298 GLU GLU A . n 
B 1 299 ALA 299 299 299 ALA ALA A . n 
B 1 300 ILE 300 300 300 ILE ILE A . n 
B 1 301 ARG 301 301 301 ARG ARG A . n 
B 1 302 ARG 302 302 302 ARG ARG A . n 
B 1 303 THR 303 303 303 THR THR A . n 
B 1 304 HIS 304 304 304 HIS HIS A . n 
B 1 305 ASN 305 305 305 ASN ASN A . n 
B 1 306 GLY 306 306 306 GLY GLY A . n 
B 1 307 GLU 307 307 307 GLU GLU A . n 
B 1 308 SER 308 308 308 SER SER A . n 
B 1 309 VAL 309 309 309 VAL VAL A . n 
B 1 310 SER 310 310 310 SER SER A . n 
B 1 311 TYR 311 311 311 TYR TYR A . n 
B 1 312 LEU 312 312 312 LEU LEU A . n 
B 1 313 PHE 313 313 313 PHE PHE A . n 
B 1 314 SER 314 314 ?   ?   ?   A . n 
B 1 315 HIS 315 315 ?   ?   ?   A . n 
B 1 316 VAL 316 316 ?   ?   ?   A . n 
B 1 317 PRO 317 317 ?   ?   ?   A . n 
B 1 318 LEU 318 318 ?   ?   ?   A . n 
B 1 319 LEU 319 319 ?   ?   ?   A . n 
B 1 320 GLU 320 320 ?   ?   ?   A . n 
B 1 321 HIS 321 321 ?   ?   ?   A . n 
B 1 322 HIS 322 322 ?   ?   ?   A . n 
B 1 323 HIS 323 323 ?   ?   ?   A . n 
B 1 324 HIS 324 324 ?   ?   ?   A . n 
B 1 325 HIS 325 325 ?   ?   ?   A . n 
B 1 326 HIS 326 326 ?   ?   ?   A . n 
# 
_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 
# 
_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,H,I,J 
# 
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)' 3870  ? 
1 MORE         -19   ? 
1 'SSA (A^2)'  24450 ? 
# 
_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_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2012-05-23 
2 'Structure model' 1 1 2015-04-22 
# 
_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_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HKL-2000 'data collection' .        ? 1 
MOLREP   phasing           .        ? 2 
REFMAC   refinement        5.5.0109 ? 3 
HKL-2000 'data reduction'  .        ? 4 
HKL-2000 'data scaling'    .        ? 5 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A SER 10 ? ? CA A SER 10 ? ? C A SER 10 ? ? 94.66  110.10 -15.44 1.90 N 
2 1 N  A SER 10 ? ? CA A SER 10 ? ? C A SER 10 ? ? 135.38 111.00 24.38  2.70 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 SER B 10  ? ? 55.47   -136.92 
2  1 PHE B 35  ? ? -66.61  -178.25 
3  1 GLN B 38  ? ? 81.67   -12.13  
4  1 GLN B 97  ? ? -104.83 67.46   
5  1 ASP B 224 ? ? -105.19 -65.69  
6  1 ASN B 273 ? ? -95.85  32.49   
7  1 SER A 11  ? ? -136.31 -39.87  
8  1 GLN A 38  ? ? 81.39   -13.20  
9  1 CYS A 60  ? ? -75.62  24.59   
10 1 ILE A 107 ? ? -100.63 77.78   
11 1 ASN A 263 ? ? -59.22  -0.15   
12 1 ASN A 273 ? ? -92.75  38.35   
# 
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 B MET 1   ? A MET 1   
2  1 Y 1 B PRO 2   ? A PRO 2   
3  1 Y 1 B ARG 196 ? A ARG 196 
4  1 Y 1 B LYS 197 ? A LYS 197 
5  1 Y 1 B LYS 198 ? A LYS 198 
6  1 Y 1 B ALA 199 ? A ALA 199 
7  1 Y 1 B ASN 200 ? A ASN 200 
8  1 Y 1 B GLU 201 ? A GLU 201 
9  1 Y 1 B VAL 202 ? A VAL 202 
10 1 Y 1 B LEU 318 ? A LEU 318 
11 1 Y 1 B LEU 319 ? A LEU 319 
12 1 Y 1 B GLU 320 ? A GLU 320 
13 1 Y 1 B HIS 321 ? A HIS 321 
14 1 Y 1 B HIS 322 ? A HIS 322 
15 1 Y 1 B HIS 323 ? A HIS 323 
16 1 Y 1 B HIS 324 ? A HIS 324 
17 1 Y 1 B HIS 325 ? A HIS 325 
18 1 Y 1 B HIS 326 ? A HIS 326 
19 1 Y 1 A MET 1   ? B MET 1   
20 1 Y 1 A PRO 2   ? B PRO 2   
21 1 Y 1 A ARG 196 ? B ARG 196 
22 1 Y 1 A LYS 197 ? B LYS 197 
23 1 Y 1 A LYS 198 ? B LYS 198 
24 1 Y 1 A ALA 199 ? B ALA 199 
25 1 Y 1 A ASN 200 ? B ASN 200 
26 1 Y 1 A GLU 201 ? B GLU 201 
27 1 Y 1 A VAL 202 ? B VAL 202 
28 1 Y 1 A SER 314 ? B SER 314 
29 1 Y 1 A HIS 315 ? B HIS 315 
30 1 Y 1 A VAL 316 ? B VAL 316 
31 1 Y 1 A PRO 317 ? B PRO 317 
32 1 Y 1 A LEU 318 ? B LEU 318 
33 1 Y 1 A LEU 319 ? B LEU 319 
34 1 Y 1 A GLU 320 ? B GLU 320 
35 1 Y 1 A HIS 321 ? B HIS 321 
36 1 Y 1 A HIS 322 ? B HIS 322 
37 1 Y 1 A HIS 323 ? B HIS 323 
38 1 Y 1 A HIS 324 ? B HIS 324 
39 1 Y 1 A HIS 325 ? B HIS 325 
40 1 Y 1 A HIS 326 ? B HIS 326 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 water         HOH 
# 
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 SO4 1   1002 1002 SO4 SO4 B . 
D 2 SO4 1   1003 1003 SO4 SO4 B . 
E 2 SO4 1   1005 1005 SO4 SO4 B . 
F 2 SO4 1   1001 1001 SO4 SO4 A . 
G 2 SO4 1   1004 1004 SO4 SO4 A . 
H 2 SO4 1   1006 1006 SO4 SO4 A . 
I 3 HOH 1   3001 3001 HOH HOH B . 
I 3 HOH 2   3002 3002 HOH HOH B . 
I 3 HOH 3   3003 3003 HOH HOH B . 
I 3 HOH 4   3004 3004 HOH HOH B . 
I 3 HOH 5   3005 3005 HOH HOH B . 
I 3 HOH 6   3006 3006 HOH HOH B . 
I 3 HOH 7   3007 3007 HOH HOH B . 
I 3 HOH 8   3009 3009 HOH HOH B . 
I 3 HOH 9   3010 3010 HOH HOH B . 
I 3 HOH 10  3012 3012 HOH HOH B . 
I 3 HOH 11  3015 3015 HOH HOH B . 
I 3 HOH 12  3018 3018 HOH HOH B . 
I 3 HOH 13  3021 3021 HOH HOH B . 
I 3 HOH 14  3024 3024 HOH HOH B . 
I 3 HOH 15  3025 3025 HOH HOH B . 
I 3 HOH 16  3028 3028 HOH HOH B . 
I 3 HOH 17  3030 3030 HOH HOH B . 
I 3 HOH 18  3031 3031 HOH HOH B . 
I 3 HOH 19  3032 3032 HOH HOH B . 
I 3 HOH 20  3034 3034 HOH HOH B . 
I 3 HOH 21  3035 3035 HOH HOH B . 
I 3 HOH 22  3038 3038 HOH HOH B . 
I 3 HOH 23  3039 3039 HOH HOH B . 
I 3 HOH 24  3041 3041 HOH HOH B . 
I 3 HOH 25  3043 3043 HOH HOH B . 
I 3 HOH 26  3044 3044 HOH HOH B . 
I 3 HOH 27  3045 3045 HOH HOH B . 
I 3 HOH 28  3046 3046 HOH HOH B . 
I 3 HOH 29  3047 3047 HOH HOH B . 
I 3 HOH 30  3048 3048 HOH HOH B . 
I 3 HOH 31  3049 3049 HOH HOH B . 
I 3 HOH 32  3052 3052 HOH HOH B . 
I 3 HOH 33  3055 3055 HOH HOH B . 
I 3 HOH 34  3057 3057 HOH HOH B . 
I 3 HOH 35  3058 3058 HOH HOH B . 
I 3 HOH 36  3059 3059 HOH HOH B . 
I 3 HOH 37  3060 3060 HOH HOH B . 
I 3 HOH 38  3061 3061 HOH HOH B . 
I 3 HOH 39  3064 3064 HOH HOH B . 
I 3 HOH 40  3066 3066 HOH HOH B . 
I 3 HOH 41  3067 3067 HOH HOH B . 
I 3 HOH 42  3068 3068 HOH HOH B . 
I 3 HOH 43  3069 3069 HOH HOH B . 
I 3 HOH 44  3072 3072 HOH HOH B . 
I 3 HOH 45  3075 3075 HOH HOH B . 
I 3 HOH 46  3076 3076 HOH HOH B . 
I 3 HOH 47  3079 3079 HOH HOH B . 
I 3 HOH 48  3081 3081 HOH HOH B . 
I 3 HOH 49  3084 3084 HOH HOH B . 
I 3 HOH 50  3086 3086 HOH HOH B . 
I 3 HOH 51  3089 3089 HOH HOH B . 
I 3 HOH 52  3090 3090 HOH HOH B . 
I 3 HOH 53  3092 3092 HOH HOH B . 
I 3 HOH 54  3093 3093 HOH HOH B . 
I 3 HOH 55  3094 3094 HOH HOH B . 
I 3 HOH 56  3095 3095 HOH HOH B . 
I 3 HOH 57  3096 3096 HOH HOH B . 
I 3 HOH 58  3097 3097 HOH HOH B . 
I 3 HOH 59  3099 3099 HOH HOH B . 
I 3 HOH 60  3101 3101 HOH HOH B . 
I 3 HOH 61  3102 3102 HOH HOH B . 
I 3 HOH 62  3105 3105 HOH HOH B . 
I 3 HOH 63  3106 3106 HOH HOH B . 
I 3 HOH 64  3107 3107 HOH HOH B . 
I 3 HOH 65  3108 3108 HOH HOH B . 
I 3 HOH 66  3110 3110 HOH HOH B . 
I 3 HOH 67  3112 3112 HOH HOH B . 
I 3 HOH 68  3113 3113 HOH HOH B . 
I 3 HOH 69  3115 3115 HOH HOH B . 
I 3 HOH 70  3116 3116 HOH HOH B . 
I 3 HOH 71  3117 3117 HOH HOH B . 
I 3 HOH 72  3120 3120 HOH HOH B . 
I 3 HOH 73  3123 3123 HOH HOH B . 
I 3 HOH 74  3124 3124 HOH HOH B . 
I 3 HOH 75  3126 3126 HOH HOH B . 
I 3 HOH 76  3127 3127 HOH HOH B . 
I 3 HOH 77  3128 3128 HOH HOH B . 
I 3 HOH 78  3131 3131 HOH HOH B . 
I 3 HOH 79  3132 3132 HOH HOH B . 
I 3 HOH 80  3133 3133 HOH HOH B . 
I 3 HOH 81  3137 3137 HOH HOH B . 
I 3 HOH 82  3139 3139 HOH HOH B . 
I 3 HOH 83  3140 3140 HOH HOH B . 
I 3 HOH 84  3141 3141 HOH HOH B . 
I 3 HOH 85  3144 3144 HOH HOH B . 
I 3 HOH 86  3145 3145 HOH HOH B . 
I 3 HOH 87  3146 3146 HOH HOH B . 
I 3 HOH 88  3149 3149 HOH HOH B . 
I 3 HOH 89  3151 3151 HOH HOH B . 
I 3 HOH 90  3153 3153 HOH HOH B . 
I 3 HOH 91  3154 3154 HOH HOH B . 
I 3 HOH 92  3155 3155 HOH HOH B . 
I 3 HOH 93  3157 3157 HOH HOH B . 
I 3 HOH 94  3160 3160 HOH HOH B . 
I 3 HOH 95  3161 3161 HOH HOH B . 
I 3 HOH 96  3163 3163 HOH HOH B . 
I 3 HOH 97  3164 3164 HOH HOH B . 
I 3 HOH 98  3169 3169 HOH HOH B . 
I 3 HOH 99  3170 3170 HOH HOH B . 
I 3 HOH 100 3172 3172 HOH HOH B . 
I 3 HOH 101 3174 3174 HOH HOH B . 
I 3 HOH 102 3175 3175 HOH HOH B . 
I 3 HOH 103 3176 3176 HOH HOH B . 
I 3 HOH 104 3179 3179 HOH HOH B . 
I 3 HOH 105 3180 3180 HOH HOH B . 
I 3 HOH 106 3181 3181 HOH HOH B . 
J 3 HOH 1   3008 3008 HOH HOH A . 
J 3 HOH 2   3011 3011 HOH HOH A . 
J 3 HOH 3   3013 3013 HOH HOH A . 
J 3 HOH 4   3014 3014 HOH HOH A . 
J 3 HOH 5   3016 3016 HOH HOH A . 
J 3 HOH 6   3017 3017 HOH HOH A . 
J 3 HOH 7   3019 3019 HOH HOH A . 
J 3 HOH 8   3020 3020 HOH HOH A . 
J 3 HOH 9   3022 3022 HOH HOH A . 
J 3 HOH 10  3023 3023 HOH HOH A . 
J 3 HOH 11  3026 3026 HOH HOH A . 
J 3 HOH 12  3027 3027 HOH HOH A . 
J 3 HOH 13  3029 3029 HOH HOH A . 
J 3 HOH 14  3033 3033 HOH HOH A . 
J 3 HOH 15  3036 3036 HOH HOH A . 
J 3 HOH 16  3037 3037 HOH HOH A . 
J 3 HOH 17  3040 3040 HOH HOH A . 
J 3 HOH 18  3042 3042 HOH HOH A . 
J 3 HOH 19  3050 3050 HOH HOH A . 
J 3 HOH 20  3051 3051 HOH HOH A . 
J 3 HOH 21  3053 3053 HOH HOH A . 
J 3 HOH 22  3054 3054 HOH HOH A . 
J 3 HOH 23  3056 3056 HOH HOH A . 
J 3 HOH 24  3062 3062 HOH HOH A . 
J 3 HOH 25  3063 3063 HOH HOH A . 
J 3 HOH 26  3065 3065 HOH HOH A . 
J 3 HOH 27  3070 3070 HOH HOH A . 
J 3 HOH 28  3071 3071 HOH HOH A . 
J 3 HOH 29  3073 3073 HOH HOH A . 
J 3 HOH 30  3074 3074 HOH HOH A . 
J 3 HOH 31  3077 3077 HOH HOH A . 
J 3 HOH 32  3078 3078 HOH HOH A . 
J 3 HOH 33  3080 3080 HOH HOH A . 
J 3 HOH 34  3082 3082 HOH HOH A . 
J 3 HOH 35  3083 3083 HOH HOH A . 
J 3 HOH 36  3085 3085 HOH HOH A . 
J 3 HOH 37  3087 3087 HOH HOH A . 
J 3 HOH 38  3088 3088 HOH HOH A . 
J 3 HOH 39  3091 3091 HOH HOH A . 
J 3 HOH 40  3098 3098 HOH HOH A . 
J 3 HOH 41  3100 3100 HOH HOH A . 
J 3 HOH 42  3103 3103 HOH HOH A . 
J 3 HOH 43  3104 3104 HOH HOH A . 
J 3 HOH 44  3109 3109 HOH HOH A . 
J 3 HOH 45  3111 3111 HOH HOH A . 
J 3 HOH 46  3114 3114 HOH HOH A . 
J 3 HOH 47  3118 3118 HOH HOH A . 
J 3 HOH 48  3119 3119 HOH HOH A . 
J 3 HOH 49  3121 3121 HOH HOH A . 
J 3 HOH 50  3122 3122 HOH HOH A . 
J 3 HOH 51  3125 3125 HOH HOH A . 
J 3 HOH 52  3129 3129 HOH HOH A . 
J 3 HOH 53  3130 3130 HOH HOH A . 
J 3 HOH 54  3134 3134 HOH HOH A . 
J 3 HOH 55  3136 3136 HOH HOH A . 
J 3 HOH 56  3138 3138 HOH HOH A . 
J 3 HOH 57  3142 3142 HOH HOH A . 
J 3 HOH 58  3143 3143 HOH HOH A . 
J 3 HOH 59  3147 3147 HOH HOH A . 
J 3 HOH 60  3148 3148 HOH HOH A . 
J 3 HOH 61  3152 3152 HOH HOH A . 
J 3 HOH 62  3156 3156 HOH HOH A . 
J 3 HOH 63  3158 3158 HOH HOH A . 
J 3 HOH 64  3162 3162 HOH HOH A . 
J 3 HOH 65  3165 3165 HOH HOH A . 
J 3 HOH 66  3166 3166 HOH HOH A . 
J 3 HOH 67  3167 3167 HOH HOH A . 
J 3 HOH 68  3168 3168 HOH HOH A . 
J 3 HOH 69  3171 3171 HOH HOH A . 
J 3 HOH 70  3177 3177 HOH HOH A . 
J 3 HOH 71  3178 3178 HOH HOH A . 
J 3 HOH 72  3182 3182 HOH HOH A . 
# 
