data_4LZN
# 
_entry.id   4LZN 
# 
_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   4LZN         
RCSB  RCSB081281   
WWPDB D_1000081281 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4LYG . unspecified 
PDB 4LZO . unspecified 
PDB 4M0P . unspecified 
PDB 4M0U . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4LZN 
_pdbx_database_status.recvd_initial_deposition_date   2013-07-31 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.methods_development_category    ? 
_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.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           4LZN 
_cell.length_a           170.776 
_cell.length_b           170.776 
_cell.length_c           61.698 
_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                         4LZN 
_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' 35949.391 2  2.7.6.1 D65N ? ? 
2 non-polymer syn 'SULFATE ION'                          96.063    6  ?       ?    ? ? 
3 water       nat water                                  18.015    69 ?       ?    ? ? 
# 
_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       
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINNNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINNNLMELLIMINACKIA
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  ASN 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                       ? 
_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 4LZN B 1 ? 318 ? P60891 1 ? 318 ? 1 318 
2 1 4LZN 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 4LZN ASN B 65  ? UNP P60891 ASP 65 'ENGINEERED MUTATION' 65  1  
1 4LZN LEU B 319 ? UNP P60891 ?   ?  'EXPRESSION TAG'      319 2  
1 4LZN GLU B 320 ? UNP P60891 ?   ?  'EXPRESSION TAG'      320 3  
1 4LZN HIS B 321 ? UNP P60891 ?   ?  'EXPRESSION TAG'      321 4  
1 4LZN HIS B 322 ? UNP P60891 ?   ?  'EXPRESSION TAG'      322 5  
1 4LZN HIS B 323 ? UNP P60891 ?   ?  'EXPRESSION TAG'      323 6  
1 4LZN HIS B 324 ? UNP P60891 ?   ?  'EXPRESSION TAG'      324 7  
1 4LZN HIS B 325 ? UNP P60891 ?   ?  'EXPRESSION TAG'      325 8  
1 4LZN HIS B 326 ? UNP P60891 ?   ?  'EXPRESSION TAG'      326 9  
2 4LZN ASN A 65  ? UNP P60891 ASP 65 'ENGINEERED MUTATION' 65  10 
2 4LZN LEU A 319 ? UNP P60891 ?   ?  'EXPRESSION TAG'      319 11 
2 4LZN GLU A 320 ? UNP P60891 ?   ?  'EXPRESSION TAG'      320 12 
2 4LZN HIS A 321 ? UNP P60891 ?   ?  'EXPRESSION TAG'      321 13 
2 4LZN HIS A 322 ? UNP P60891 ?   ?  'EXPRESSION TAG'      322 14 
2 4LZN HIS A 323 ? UNP P60891 ?   ?  'EXPRESSION TAG'      323 15 
2 4LZN HIS A 324 ? UNP P60891 ?   ?  'EXPRESSION TAG'      324 16 
2 4LZN HIS A 325 ? UNP P60891 ?   ?  'EXPRESSION TAG'      325 17 
2 4LZN HIS A 326 ? UNP P60891 ?   ?  'EXPRESSION TAG'      326 18 
# 
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          4LZN 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.41 
_exptl_crystal.density_percent_sol   48.92 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.temp            295 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              4.1 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    'pH 4.1, VAPOR DIFFUSION, temperature 295K' 
# 
_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                   'ADSC QUANTUM 315r' 
_diffrn_detector.pdbx_collection_date   ? 
_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.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4LZN 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             49.3 
_reflns.d_resolution_high            2.14 
_reflns.number_obs                   35171 
_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         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4LZN 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     33412 
_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                             49.30 
_refine.ls_d_res_high                            2.14 
_refine.ls_percent_reflns_obs                    95.35 
_refine.ls_R_factor_obs                          0.22621 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.22420 
_refine.ls_R_factor_R_free                       0.26319 
_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                  1759 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.941 
_refine.correlation_coeff_Fo_to_Fc_free          0.893 
_refine.B_iso_mean                               55.204 
_refine.aniso_B[1][1]                            1.40 
_refine.aniso_B[2][2]                            1.40 
_refine.aniso_B[3][3]                            -2.10 
_refine.aniso_B[1][2]                            0.70 
_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                      4F8E 
_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                       0.287 
_refine.pdbx_overall_ESU_R_Free                  0.220 
_refine.overall_SU_ML                            0.155 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             5.857 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.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_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4673 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             69 
_refine_hist.number_atoms_total               4772 
_refine_hist.d_res_high                       2.14 
_refine_hist.d_res_low                        49.30 
# 
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_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.007  0.022  ? 4770 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.066  1.959  ? 6453 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       5.341  5.000  ? 608  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       37.521 24.523 ? 199  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.542 15.000 ? 855  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       18.630 15.000 ? 30   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.073  0.200  ? 763  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.004  0.021  ? 3478 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  2.343  1.500  ? 3039 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 3.659  2.000  ? 4916 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.115  3.000  ? 1731 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 3.460  4.500  ? 1537 'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    '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                       2.142 
_refine_ls_shell.d_res_low                        2.197 
_refine_ls_shell.number_reflns_R_work             1748 
_refine_ls_shell.R_factor_R_work                  0.270 
_refine_ls_shell.percent_reflns_obs               68.22 
_refine_ls_shell.R_factor_R_free                  0.295 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             87 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  4LZN 
_struct.title                     'Crystal structure of human PRS1 D65N mutant' 
_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        4LZN 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            'PRS1, PRPP synthesis enzyme, ATP R5P, 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 ? 7 ? 
C ? 5 ? 
D ? 2 ? 
E ? 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 
B 2 3 ? parallel      
B 3 4 ? parallel      
B 4 5 ? parallel      
B 5 6 ? parallel      
B 6 7 ? parallel      
C 1 2 ? parallel      
C 2 3 ? parallel      
C 3 4 ? parallel      
C 4 5 ? parallel      
D 1 2 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? parallel      
E 3 4 ? parallel      
E 4 5 ? parallel      
E 5 6 ? parallel      
E 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 MET A 205 ? VAL A 208 ? MET B 205 VAL B 208 
B 2 ASP A 188 ? LYS A 194 ? ASP B 188 LYS B 194 
B 3 THR A 166 ? SER A 169 ? THR B 166 SER B 169 
B 4 ALA A 216 ? ALA A 223 ? ALA B 216 ALA B 223 
B 5 VAL A 244 ? GLY A 251 ? VAL B 244 GLY B 251 
B 6 ALA A 268 ? THR A 272 ? ALA B 268 THR B 272 
B 7 ILE A 287 ? ILE A 290 ? ILE B 287 ILE B 290 
C 1 ILE B 4   ? SER B 8   ? ILE A 4   SER A 8   
C 2 ASP B 52  ? VAL B 56  ? ASP A 52  VAL A 56  
C 3 ARG B 84  ? ILE B 89  ? ARG A 84  ILE A 89  
C 4 HIS B 123 ? MET B 127 ? HIS A 123 MET A 127 
C 5 VAL B 142 ? LEU B 145 ? VAL A 142 LEU A 145 
D 1 LYS B 33  ? LYS B 34  ? LYS A 33  LYS A 34  
D 2 THR B 40  ? CYS B 41  ? THR A 40  CYS A 41  
E 1 MET B 205 ? VAL B 208 ? MET A 205 VAL A 208 
E 2 ASP B 188 ? LYS B 194 ? ASP A 188 LYS A 194 
E 3 THR B 166 ? SER B 169 ? THR A 166 SER A 169 
E 4 ALA B 216 ? ALA B 223 ? ALA A 216 ALA A 223 
E 5 VAL B 244 ? GLY B 251 ? VAL A 244 GLY A 251 
E 6 ALA B 268 ? THR B 272 ? ALA A 268 THR A 272 
E 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 ILE A 55  ? N ILE B 55  O VAL A 88  ? O VAL B 88  
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 O VAL A 208 ? O VAL B 208 N LEU A 191 ? N LEU B 191 
B 2 3 O ILE A 192 ? O ILE B 192 N SER A 169 ? N SER B 169 
B 3 4 N VAL A 168 ? N VAL B 168 O ILE A 217 ? O ILE B 217 
B 4 5 N LEU A 218 ? N LEU B 218 O TYR A 245 ? O TYR B 245 
B 5 6 N LEU A 248 ? N LEU B 248 O VAL A 270 ? O VAL B 270 
B 6 7 N VAL A 271 ? N VAL B 271 O ILE A 290 ? O ILE B 290 
C 1 2 N PHE B 7   ? N PHE A 7   O VAL B 56  ? O VAL A 56  
C 2 3 N ILE B 55  ? N ILE A 55  O VAL B 88  ? O VAL A 88  
C 3 4 N ILE B 89  ? N ILE A 89  O ILE B 125 ? O ILE A 125 
C 4 5 N THR B 126 ? N THR A 126 O LEU B 145 ? O LEU A 145 
D 1 2 N LYS B 33  ? N LYS A 33  O CYS B 41  ? O CYS A 41  
E 1 2 O VAL B 206 ? O VAL A 206 N HIS B 193 ? N HIS A 193 
E 2 3 O ILE B 192 ? O ILE A 192 N SER B 169 ? N SER A 169 
E 3 4 N VAL B 168 ? N VAL A 168 O ILE B 217 ? O ILE A 217 
E 4 5 N LEU B 218 ? N LEU A 218 O ILE B 247 ? O ILE A 247 
E 5 6 N ALA B 246 ? N ALA A 246 O VAL B 270 ? O VAL A 270 
E 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 ? ? ? ? 7  'BINDING SITE FOR RESIDUE SO4 B 401'  
AC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE SO4 B 402'  
AC3 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE SO4 B 403'  
AC4 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 A 1001' 
AC5 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE SO4 A 1002' 
AC6 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 A 1003' 
# 
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 7  ARG B 104 ? ARG A 104  . ? 3_555 ? 
2  AC1 7  SER A 47  ? SER B 47   . ? 3_555 ? 
3  AC1 7  ARG A 49  ? ARG B 49   . ? 3_555 ? 
4  AC1 7  SER A 308 ? SER B 308  . ? 1_555 ? 
5  AC1 7  VAL A 309 ? VAL B 309  . ? 1_555 ? 
6  AC1 7  SER A 310 ? SER B 310  . ? 1_555 ? 
7  AC1 7  HOH I .   ? HOH B 507  . ? 3_555 ? 
8  AC2 5  ASP A 224 ? ASP B 224  . ? 1_555 ? 
9  AC2 5  THR A 225 ? THR B 225  . ? 1_555 ? 
10 AC2 5  CYS A 226 ? CYS B 226  . ? 1_555 ? 
11 AC2 5  GLY A 227 ? GLY B 227  . ? 1_555 ? 
12 AC2 5  THR A 228 ? THR B 228  . ? 1_555 ? 
13 AC3 10 LYS B 99  ? LYS A 99   . ? 3_555 ? 
14 AC3 10 LYS B 100 ? LYS A 100  . ? 3_555 ? 
15 AC3 10 ASP B 101 ? ASP A 101  . ? 3_555 ? 
16 AC3 10 LYS B 102 ? LYS A 102  . ? 3_555 ? 
17 AC3 10 SER A 132 ? SER B 132  . ? 1_555 ? 
18 AC3 10 GLN A 135 ? GLN B 135  . ? 1_555 ? 
19 AC3 10 ASN A 144 ? ASN B 144  . ? 1_555 ? 
20 AC3 10 TYR A 146 ? TYR B 146  . ? 1_555 ? 
21 AC3 10 HOH I .   ? HOH B 503  . ? 1_555 ? 
22 AC3 10 HOH I .   ? HOH B 523  . ? 1_555 ? 
23 AC4 8  SER B 47  ? SER A 47   . ? 2_555 ? 
24 AC4 8  ARG B 49  ? ARG A 49   . ? 2_555 ? 
25 AC4 8  SER B 308 ? SER A 308  . ? 1_555 ? 
26 AC4 8  VAL B 309 ? VAL A 309  . ? 1_555 ? 
27 AC4 8  SER B 310 ? SER A 310  . ? 1_555 ? 
28 AC4 8  HOH J .   ? HOH A 1107 . ? 1_555 ? 
29 AC4 8  HOH J .   ? HOH A 1121 . ? 1_555 ? 
30 AC4 8  ARG A 104 ? ARG B 104  . ? 2_555 ? 
31 AC5 6  ALA B 223 ? ALA A 223  . ? 1_555 ? 
32 AC5 6  ASP B 224 ? ASP A 224  . ? 1_555 ? 
33 AC5 6  THR B 225 ? THR A 225  . ? 1_555 ? 
34 AC5 6  CYS B 226 ? CYS A 226  . ? 1_555 ? 
35 AC5 6  GLY B 227 ? GLY A 227  . ? 1_555 ? 
36 AC5 6  THR B 228 ? THR A 228  . ? 1_555 ? 
37 AC6 8  SER B 132 ? SER A 132  . ? 1_555 ? 
38 AC6 8  GLN B 135 ? GLN A 135  . ? 1_555 ? 
39 AC6 8  ASN B 144 ? ASN A 144  . ? 1_555 ? 
40 AC6 8  TYR B 146 ? TYR A 146  . ? 1_555 ? 
41 AC6 8  HOH J .   ? HOH A 1117 . ? 1_555 ? 
42 AC6 8  LYS A 100 ? LYS B 100  . ? 2_555 ? 
43 AC6 8  ASP A 101 ? ASP B 101  . ? 2_555 ? 
44 AC6 8  LYS A 102 ? LYS B 102  . ? 2_555 ? 
# 
_database_PDB_matrix.entry_id          4LZN 
_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                    4LZN 
_atom_sites.fract_transf_matrix[1][1]   0.005856 
_atom_sites.fract_transf_matrix[1][2]   0.003381 
_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]   0.006761 
_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]   0.016208 
_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   ? 5.654   -10.463 -28.097 0.71   38.75  ? 3    ASN B N   1 
ATOM   2    C CA  . ASN A 1 3   ? 5.059   -9.790  -26.912 0.71   38.51  ? 3    ASN B CA  1 
ATOM   3    C C   . ASN A 1 3   ? 4.665   -10.842 -25.881 0.71   37.99  ? 3    ASN B C   1 
ATOM   4    O O   . ASN A 1 3   ? 4.828   -10.626 -24.697 0.71   37.85  ? 3    ASN B O   1 
ATOM   5    C CB  . ASN A 1 3   ? 3.855   -8.917  -27.310 0.71   38.91  ? 3    ASN B CB  1 
ATOM   6    C CG  . ASN A 1 3   ? 3.802   -7.583  -26.551 0.71   41.49  ? 3    ASN B CG  1 
ATOM   7    O OD1 . ASN A 1 3   ? 3.675   -6.513  -27.155 0.71   44.16  ? 3    ASN B OD1 1 
ATOM   8    N ND2 . ASN A 1 3   ? 3.890   -7.645  -25.226 0.71   44.68  ? 3    ASN B ND2 1 
ATOM   9    N N   . ILE A 1 4   ? 4.171   -11.982 -26.350 1.00   37.11  ? 4    ILE B N   1 
ATOM   10   C CA  . ILE A 1 4   ? 3.754   -13.096 -25.497 1.00   37.24  ? 4    ILE B CA  1 
ATOM   11   C C   . ILE A 1 4   ? 4.975   -13.963 -25.159 1.00   35.36  ? 4    ILE B C   1 
ATOM   12   O O   . ILE A 1 4   ? 5.730   -14.342 -26.051 1.00   36.55  ? 4    ILE B O   1 
ATOM   13   C CB  . ILE A 1 4   ? 2.633   -13.932 -26.208 1.00   37.77  ? 4    ILE B CB  1 
ATOM   14   C CG1 . ILE A 1 4   ? 1.762   -14.727 -25.221 1.00   39.42  ? 4    ILE B CG1 1 
ATOM   15   C CG2 . ILE A 1 4   ? 3.203   -14.806 -27.344 1.00   41.53  ? 4    ILE B CG2 1 
ATOM   16   C CD1 . ILE A 1 4   ? 2.452   -15.884 -24.507 1.00   39.40  ? 4    ILE B CD1 1 
ATOM   17   N N   . LYS A 1 5   ? 5.187   -14.248 -23.877 0.52   31.45  ? 5    LYS B N   1 
ATOM   18   C CA  . LYS A 1 5   ? 6.286   -15.116 -23.465 0.52   29.58  ? 5    LYS B CA  1 
ATOM   19   C C   . LYS A 1 5   ? 5.872   -16.101 -22.369 0.52   30.19  ? 5    LYS B C   1 
ATOM   20   O O   . LYS A 1 5   ? 5.340   -15.705 -21.325 0.52   26.32  ? 5    LYS B O   1 
ATOM   21   C CB  . LYS A 1 5   ? 7.470   -14.276 -22.998 0.52   29.01  ? 5    LYS B CB  1 
ATOM   22   C CG  . LYS A 1 5   ? 8.779   -15.043 -22.926 0.52   30.23  ? 5    LYS B CG  1 
ATOM   23   C CD  . LYS A 1 5   ? 9.765   -14.545 -23.980 0.52   34.10  ? 5    LYS B CD  1 
ATOM   24   C CE  . LYS A 1 5   ? 9.722   -15.378 -25.255 0.52   35.24  ? 5    LYS B CE  1 
ATOM   25   N NZ  . LYS A 1 5   ? 10.394  -16.715 -25.092 0.52   37.66  ? 5    LYS B NZ  1 
ATOM   26   N N   . ILE A 1 6   ? 6.134   -17.386 -22.594 1.00   32.90  ? 6    ILE B N   1 
ATOM   27   C CA  . ILE A 1 6   ? 5.702   -18.420 -21.647 1.00   35.45  ? 6    ILE B CA  1 
ATOM   28   C C   . ILE A 1 6   ? 6.880   -19.120 -20.990 1.00   36.60  ? 6    ILE B C   1 
ATOM   29   O O   . ILE A 1 6   ? 7.802   -19.567 -21.680 1.00   37.02  ? 6    ILE B O   1 
ATOM   30   C CB  . ILE A 1 6   ? 4.823   -19.492 -22.317 1.00   35.77  ? 6    ILE B CB  1 
ATOM   31   C CG1 . ILE A 1 6   ? 3.604   -18.853 -22.968 1.00   38.41  ? 6    ILE B CG1 1 
ATOM   32   C CG2 . ILE A 1 6   ? 4.365   -20.537 -21.286 1.00   36.40  ? 6    ILE B CG2 1 
ATOM   33   C CD1 . ILE A 1 6   ? 2.886   -19.770 -23.893 1.00   41.60  ? 6    ILE B CD1 1 
ATOM   34   N N   . PHE A 1 7   ? 6.842   -19.219 -19.660 1.00   37.25  ? 7    PHE B N   1 
ATOM   35   C CA  . PHE A 1 7   ? 7.904   -19.906 -18.906 1.00   39.47  ? 7    PHE B CA  1 
ATOM   36   C C   . PHE A 1 7   ? 7.312   -21.027 -18.072 1.00   41.80  ? 7    PHE B C   1 
ATOM   37   O O   . PHE A 1 7   ? 6.159   -20.955 -17.629 1.00   40.80  ? 7    PHE B O   1 
ATOM   38   C CB  . PHE A 1 7   ? 8.648   -18.950 -17.962 1.00   39.16  ? 7    PHE B CB  1 
ATOM   39   C CG  . PHE A 1 7   ? 9.525   -17.947 -18.655 1.00   38.29  ? 7    PHE B CG  1 
ATOM   40   C CD1 . PHE A 1 7   ? 9.029   -16.703 -19.016 1.00   39.59  ? 7    PHE B CD1 1 
ATOM   41   C CD2 . PHE A 1 7   ? 10.850  -18.242 -18.936 1.00   37.16  ? 7    PHE B CD2 1 
ATOM   42   C CE1 . PHE A 1 7   ? 9.843   -15.767 -19.645 1.00   39.83  ? 7    PHE B CE1 1 
ATOM   43   C CE2 . PHE A 1 7   ? 11.669  -17.317 -19.554 1.00   38.37  ? 7    PHE B CE2 1 
ATOM   44   C CZ  . PHE A 1 7   ? 11.167  -16.078 -19.916 1.00   39.37  ? 7    PHE B CZ  1 
ATOM   45   N N   . SER A 1 8   ? 8.112   -22.056 -17.842 1.00   45.79  ? 8    SER B N   1 
ATOM   46   C CA  . SER A 1 8   ? 7.702   -23.158 -16.991 1.00   51.94  ? 8    SER B CA  1 
ATOM   47   C C   . SER A 1 8   ? 8.476   -23.095 -15.685 1.00   56.59  ? 8    SER B C   1 
ATOM   48   O O   . SER A 1 8   ? 9.642   -22.689 -15.667 1.00   56.17  ? 8    SER B O   1 
ATOM   49   C CB  . SER A 1 8   ? 8.000   -24.487 -17.675 1.00   51.49  ? 8    SER B CB  1 
ATOM   50   O OG  . SER A 1 8   ? 7.493   -25.567 -16.909 1.00   52.49  ? 8    SER B OG  1 
ATOM   51   N N   . GLY A 1 9   ? 7.780   -23.471 -14.619 1.00   75.38  ? 9    GLY B N   1 
ATOM   52   C CA  . GLY A 1 9   ? 8.327   -23.674 -13.294 1.00   73.58  ? 9    GLY B CA  1 
ATOM   53   C C   . GLY A 1 9   ? 9.221   -24.858 -13.616 1.00   78.22  ? 9    GLY B C   1 
ATOM   54   O O   . GLY A 1 9   ? 9.162   -25.467 -14.665 1.00   87.22  ? 9    GLY B O   1 
ATOM   55   N N   . SER A 1 10  ? 9.857   -25.311 -12.567 0.79   77.30  ? 10   SER B N   1 
ATOM   56   C CA  . SER A 1 10  ? 10.723  -26.453 -12.614 0.79   79.84  ? 10   SER B CA  1 
ATOM   57   C C   . SER A 1 10  ? 10.038  -27.718 -13.070 0.79   81.03  ? 10   SER B C   1 
ATOM   58   O O   . SER A 1 10  ? 9.099   -28.216 -12.445 0.79   81.51  ? 10   SER B O   1 
ATOM   59   C CB  . SER A 1 10  ? 11.297  -26.699 -11.231 0.79   79.98  ? 10   SER B CB  1 
ATOM   60   O OG  . SER A 1 10  ? 10.504  -27.655 -10.548 0.79   80.26  ? 10   SER B OG  1 
ATOM   61   N N   . SER A 1 11  ? 10.755  -28.316 -14.080 0.33   82.07  ? 11   SER B N   1 
ATOM   62   C CA  . SER A 1 11  ? 10.708  -29.744 -14.254 0.33   83.02  ? 11   SER B CA  1 
ATOM   63   C C   . SER A 1 11  ? 9.522   -30.483 -14.803 0.33   83.73  ? 11   SER B C   1 
ATOM   64   O O   . SER A 1 11  ? 9.676   -31.269 -15.713 0.33   83.80  ? 11   SER B O   1 
ATOM   65   C CB  . SER A 1 11  ? 10.947  -30.429 -12.911 0.33   82.89  ? 11   SER B CB  1 
ATOM   66   N N   . HIS A 1 12  ? 8.351   -30.288 -14.225 1.00   94.29  ? 12   HIS B N   1 
ATOM   67   C CA  . HIS A 1 12  ? 7.226   -31.038 -14.694 1.00   89.79  ? 12   HIS B CA  1 
ATOM   68   C C   . HIS A 1 12  ? 6.920   -29.926 -15.654 1.00   88.50  ? 12   HIS B C   1 
ATOM   69   O O   . HIS A 1 12  ? 6.357   -28.884 -15.291 1.00   87.06  ? 12   HIS B O   1 
ATOM   70   C CB  . HIS A 1 12  ? 6.192   -31.315 -13.617 1.00   20.00  ? 12   HIS B CB  1 
ATOM   71   N N   . GLN A 1 13  ? 7.308   -30.149 -16.898 1.00   76.66  ? 13   GLN B N   1 
ATOM   72   C CA  . GLN A 1 13  ? 7.278   -29.152 -17.929 1.00   70.72  ? 13   GLN B CA  1 
ATOM   73   C C   . GLN A 1 13  ? 6.285   -29.626 -18.977 1.00   64.90  ? 13   GLN B C   1 
ATOM   74   O O   . GLN A 1 13  ? 6.060   -28.956 -19.942 1.00   64.59  ? 13   GLN B O   1 
ATOM   75   C CB  . GLN A 1 13  ? 8.615   -28.837 -18.584 1.00   71.84  ? 13   GLN B CB  1 
ATOM   76   C CG  . GLN A 1 13  ? 9.530   -27.925 -17.784 1.00   73.86  ? 13   GLN B CG  1 
ATOM   77   C CD  . GLN A 1 13  ? 10.655  -27.359 -18.630 1.00   79.11  ? 13   GLN B CD  1 
ATOM   78   O OE1 . GLN A 1 13  ? 10.922  -26.171 -18.617 1.00   77.69  ? 13   GLN B OE1 1 
ATOM   79   N NE2 . GLN A 1 13  ? 11.312  -28.216 -19.375 1.00   79.66  ? 13   GLN B NE2 1 
ATOM   80   N N   . ASP A 1 14  ? 5.667   -30.768 -18.769 0.58   56.83  ? 14   ASP B N   1 
ATOM   81   C CA  . ASP A 1 14  ? 4.753   -31.284 -19.760 0.58   50.41  ? 14   ASP B CA  1 
ATOM   82   C C   . ASP A 1 14  ? 3.652   -30.322 -20.068 0.58   46.82  ? 14   ASP B C   1 
ATOM   83   O O   . ASP A 1 14  ? 3.548   -29.884 -21.166 0.58   44.20  ? 14   ASP B O   1 
ATOM   84   C CB  . ASP A 1 14  ? 4.169   -32.635 -19.365 0.58   50.10  ? 14   ASP B CB  1 
ATOM   85   C CG  . ASP A 1 14  ? 3.647   -33.419 -20.564 0.58   50.57  ? 14   ASP B CG  1 
ATOM   86   O OD1 . ASP A 1 14  ? 4.443   -34.049 -21.274 0.58   51.36  ? 14   ASP B OD1 1 
ATOM   87   O OD2 . ASP A 1 14  ? 2.433   -33.412 -20.807 0.58   50.81  ? 14   ASP B OD2 1 
ATOM   88   N N   . LEU A 1 15  ? 2.829   -30.006 -19.094 1.00   44.12  ? 15   LEU B N   1 
ATOM   89   C CA  . LEU A 1 15  ? 1.725   -29.068 -19.295 1.00   42.43  ? 15   LEU B CA  1 
ATOM   90   C C   . LEU A 1 15  ? 2.230   -27.794 -19.936 1.00   41.22  ? 15   LEU B C   1 
ATOM   91   O O   . LEU A 1 15  ? 1.631   -27.295 -20.889 1.00   41.07  ? 15   LEU B O   1 
ATOM   92   C CB  . LEU A 1 15  ? 1.078   -28.691 -17.960 1.00   42.01  ? 15   LEU B CB  1 
ATOM   93   C CG  . LEU A 1 15  ? -0.448  -28.642 -17.819 1.00   42.62  ? 15   LEU B CG  1 
ATOM   94   C CD1 . LEU A 1 15  ? -0.822  -27.725 -16.659 1.00   42.02  ? 15   LEU B CD1 1 
ATOM   95   C CD2 . LEU A 1 15  ? -1.205  -28.234 -19.090 1.00   38.56  ? 15   LEU B CD2 1 
ATOM   96   N N   . SER A 1 16  ? 3.326   -27.269 -19.390 1.00   39.60  ? 16   SER B N   1 
ATOM   97   C CA  . SER A 1 16  ? 3.917   -26.030 -19.872 1.00   40.91  ? 16   SER B CA  1 
ATOM   98   C C   . SER A 1 16  ? 4.224   -26.139 -21.357 1.00   41.48  ? 16   SER B C   1 
ATOM   99   O O   . SER A 1 16  ? 3.971   -25.199 -22.112 1.00   40.35  ? 16   SER B O   1 
ATOM   100  C CB  . SER A 1 16  ? 5.197   -25.721 -19.112 1.00   40.27  ? 16   SER B CB  1 
ATOM   101  O OG  . SER A 1 16  ? 4.905   -25.301 -17.796 1.00   44.30  ? 16   SER B OG  1 
ATOM   102  N N   . GLN A 1 17  ? 4.762   -27.293 -21.758 1.00   42.97  ? 17   GLN B N   1 
ATOM   103  C CA  . GLN A 1 17  ? 5.123   -27.549 -23.151 1.00   44.37  ? 17   GLN B CA  1 
ATOM   104  C C   . GLN A 1 17  ? 3.894   -27.694 -24.031 1.00   44.08  ? 17   GLN B C   1 
ATOM   105  O O   . GLN A 1 17  ? 3.868   -27.147 -25.125 1.00   44.69  ? 17   GLN B O   1 
ATOM   106  C CB  . GLN A 1 17  ? 6.052   -28.767 -23.273 1.00   44.98  ? 17   GLN B CB  1 
ATOM   107  C CG  . GLN A 1 17  ? 6.627   -29.007 -24.674 1.00   47.81  ? 17   GLN B CG  1 
ATOM   108  C CD  . GLN A 1 17  ? 7.497   -27.861 -25.179 1.00   51.15  ? 17   GLN B CD  1 
ATOM   109  O OE1 . GLN A 1 17  ? 8.503   -27.504 -24.561 1.00   52.65  ? 17   GLN B OE1 1 
ATOM   110  N NE2 . GLN A 1 17  ? 7.120   -27.293 -26.321 1.00   52.34  ? 17   GLN B NE2 1 
ATOM   111  N N   . LYS A 1 18  ? 2.878   -28.416 -23.560 1.00   43.87  ? 18   LYS B N   1 
ATOM   112  C CA  . LYS A 1 18  ? 1.621   -28.529 -24.309 1.00   43.19  ? 18   LYS B CA  1 
ATOM   113  C C   . LYS A 1 18  ? 0.971   -27.172 -24.574 1.00   41.67  ? 18   LYS B C   1 
ATOM   114  O O   . LYS A 1 18  ? 0.427   -26.945 -25.656 1.00   41.38  ? 18   LYS B O   1 
ATOM   115  C CB  . LYS A 1 18  ? 0.621   -29.432 -23.587 1.00   44.24  ? 18   LYS B CB  1 
ATOM   116  C CG  . LYS A 1 18  ? 0.879   -30.917 -23.728 1.00   46.78  ? 18   LYS B CG  1 
ATOM   117  C CD  . LYS A 1 18  ? -0.259  -31.705 -23.102 1.00   51.71  ? 18   LYS B CD  1 
ATOM   118  C CE  . LYS A 1 18  ? -0.115  -33.196 -23.358 1.00   53.92  ? 18   LYS B CE  1 
ATOM   119  N NZ  . LYS A 1 18  ? -1.340  -33.935 -22.951 1.00   58.10  ? 18   LYS B NZ  1 
ATOM   120  N N   . ILE A 1 19  ? 1.017   -26.281 -23.585 1.00   39.37  ? 19   ILE B N   1 
ATOM   121  C CA  . ILE A 1 19  ? 0.422   -24.951 -23.734 1.00   37.15  ? 19   ILE B CA  1 
ATOM   122  C C   . ILE A 1 19  ? 1.225   -24.141 -24.749 1.00   36.33  ? 19   ILE B C   1 
ATOM   123  O O   . ILE A 1 19  ? 0.650   -23.523 -25.643 1.00   34.84  ? 19   ILE B O   1 
ATOM   124  C CB  . ILE A 1 19  ? 0.338   -24.182 -22.386 1.00   36.72  ? 19   ILE B CB  1 
ATOM   125  C CG1 . ILE A 1 19  ? -0.619  -24.897 -21.422 1.00   35.68  ? 19   ILE B CG1 1 
ATOM   126  C CG2 . ILE A 1 19  ? -0.144  -22.754 -22.626 1.00   35.41  ? 19   ILE B CG2 1 
ATOM   127  C CD1 . ILE A 1 19  ? -0.418  -24.555 -19.929 1.00   31.70  ? 19   ILE B CD1 1 
ATOM   128  N N   . ALA A 1 20  ? 2.548   -24.155 -24.607 1.00   35.74  ? 20   ALA B N   1 
ATOM   129  C CA  . ALA A 1 20  ? 3.415   -23.415 -25.515 1.00   36.40  ? 20   ALA B CA  1 
ATOM   130  C C   . ALA A 1 20  ? 3.246   -23.918 -26.957 1.00   36.70  ? 20   ALA B C   1 
ATOM   131  O O   . ALA A 1 20  ? 3.062   -23.107 -27.875 1.00   37.70  ? 20   ALA B O   1 
ATOM   132  C CB  . ALA A 1 20  ? 4.868   -23.486 -25.063 1.00   35.76  ? 20   ALA B CB  1 
ATOM   133  N N   . ASP A 1 21  ? 3.264   -25.240 -27.141 0.56   36.31  ? 21   ASP B N   1 
ATOM   134  C CA  . ASP A 1 21  ? 2.987   -25.855 -28.446 0.56   36.88  ? 21   ASP B CA  1 
ATOM   135  C C   . ASP A 1 21  ? 1.716   -25.299 -29.076 0.56   38.17  ? 21   ASP B C   1 
ATOM   136  O O   . ASP A 1 21  ? 1.723   -24.894 -30.241 0.56   37.21  ? 21   ASP B O   1 
ATOM   137  C CB  . ASP A 1 21  ? 2.837   -27.381 -28.325 0.56   36.32  ? 21   ASP B CB  1 
ATOM   138  C CG  . ASP A 1 21  ? 4.152   -28.093 -28.083 0.56   36.60  ? 21   ASP B CG  1 
ATOM   139  O OD1 . ASP A 1 21  ? 5.223   -27.476 -28.245 0.56   36.45  ? 21   ASP B OD1 1 
ATOM   140  O OD2 . ASP A 1 21  ? 4.113   -29.290 -27.721 0.56   38.69  ? 21   ASP B OD2 1 
ATOM   141  N N   . ARG A 1 22  ? 0.632   -25.272 -28.302 1.00   40.51  ? 22   ARG B N   1 
ATOM   142  C CA  . ARG A 1 22  ? -0.667  -24.833 -28.823 1.00   42.39  ? 22   ARG B CA  1 
ATOM   143  C C   . ARG A 1 22  ? -0.712  -23.339 -29.174 1.00   42.27  ? 22   ARG B C   1 
ATOM   144  O O   . ARG A 1 22  ? -1.567  -22.899 -29.941 1.00   42.70  ? 22   ARG B O   1 
ATOM   145  C CB  . ARG A 1 22  ? -1.805  -25.242 -27.875 1.00   42.82  ? 22   ARG B CB  1 
ATOM   146  C CG  . ARG A 1 22  ? -1.836  -26.749 -27.611 1.00   46.26  ? 22   ARG B CG  1 
ATOM   147  C CD  . ARG A 1 22  ? -2.933  -27.165 -26.650 1.00   50.48  ? 22   ARG B CD  1 
ATOM   148  N NE  . ARG A 1 22  ? -4.146  -27.525 -27.372 1.00   55.41  ? 22   ARG B NE  1 
ATOM   149  C CZ  . ARG A 1 22  ? -4.585  -28.770 -27.554 1.00   56.79  ? 22   ARG B CZ  1 
ATOM   150  N NH1 . ARG A 1 22  ? -3.925  -29.809 -27.049 1.00   57.31  ? 22   ARG B NH1 1 
ATOM   151  N NH2 . ARG A 1 22  ? -5.702  -28.972 -28.238 1.00   56.79  ? 22   ARG B NH2 1 
ATOM   152  N N   . LEU A 1 23  ? 0.223   -22.568 -28.632 1.00   42.03  ? 23   LEU B N   1 
ATOM   153  C CA  . LEU A 1 23  ? 0.305   -21.139 -28.938 1.00   41.42  ? 23   LEU B CA  1 
ATOM   154  C C   . LEU A 1 23  ? 1.304   -20.846 -30.053 1.00   40.86  ? 23   LEU B C   1 
ATOM   155  O O   . LEU A 1 23  ? 1.377   -19.720 -30.545 1.00   41.16  ? 23   LEU B O   1 
ATOM   156  C CB  . LEU A 1 23  ? 0.667   -20.341 -27.683 1.00   41.32  ? 23   LEU B CB  1 
ATOM   157  C CG  . LEU A 1 23  ? -0.368  -20.382 -26.548 1.00   41.03  ? 23   LEU B CG  1 
ATOM   158  C CD1 . LEU A 1 23  ? 0.203   -19.786 -25.291 1.00   41.89  ? 23   LEU B CD1 1 
ATOM   159  C CD2 . LEU A 1 23  ? -1.635  -19.657 -26.939 1.00   40.68  ? 23   LEU B CD2 1 
ATOM   160  N N   . GLY A 1 24  ? 2.078   -21.862 -30.432 1.00   40.00  ? 24   GLY B N   1 
ATOM   161  C CA  . GLY A 1 24  ? 3.071   -21.727 -31.500 1.00   39.08  ? 24   GLY B CA  1 
ATOM   162  C C   . GLY A 1 24  ? 4.393   -21.229 -30.970 1.00   38.29  ? 24   GLY B C   1 
ATOM   163  O O   . GLY A 1 24  ? 5.191   -20.638 -31.710 1.00   38.93  ? 24   GLY B O   1 
ATOM   164  N N   . LEU A 1 25  ? 4.635   -21.469 -29.682 1.00   36.71  ? 25   LEU B N   1 
ATOM   165  C CA  . LEU A 1 25  ? 5.799   -20.886 -29.015 1.00   35.58  ? 25   LEU B CA  1 
ATOM   166  C C   . LEU A 1 25  ? 6.741   -21.932 -28.442 1.00   34.92  ? 25   LEU B C   1 
ATOM   167  O O   . LEU A 1 25  ? 6.322   -23.043 -28.142 1.00   34.72  ? 25   LEU B O   1 
ATOM   168  C CB  . LEU A 1 25  ? 5.337   -19.960 -27.883 1.00   35.81  ? 25   LEU B CB  1 
ATOM   169  C CG  . LEU A 1 25  ? 4.354   -18.859 -28.285 1.00   36.69  ? 25   LEU B CG  1 
ATOM   170  C CD1 . LEU A 1 25  ? 3.892   -18.080 -27.057 1.00   37.95  ? 25   LEU B CD1 1 
ATOM   171  C CD2 . LEU A 1 25  ? 4.968   -17.912 -29.332 1.00   36.57  ? 25   LEU B CD2 1 
ATOM   172  N N   . GLU A 1 26  ? 8.007   -21.564 -28.295 0.79   34.64  ? 26   GLU B N   1 
ATOM   173  C CA  . GLU A 1 26  ? 8.925   -22.289 -27.442 0.79   36.11  ? 26   GLU B CA  1 
ATOM   174  C C   . GLU A 1 26  ? 8.872   -21.704 -26.039 0.79   36.57  ? 26   GLU B C   1 
ATOM   175  O O   . GLU A 1 26  ? 8.714   -20.492 -25.869 0.79   35.83  ? 26   GLU B O   1 
ATOM   176  C CB  . GLU A 1 26  ? 10.356  -22.167 -27.952 0.79   36.29  ? 26   GLU B CB  1 
ATOM   177  C CG  . GLU A 1 26  ? 10.706  -23.061 -29.124 0.79   39.75  ? 26   GLU B CG  1 
ATOM   178  C CD  . GLU A 1 26  ? 12.154  -22.882 -29.563 0.79   43.89  ? 26   GLU B CD  1 
ATOM   179  O OE1 . GLU A 1 26  ? 12.837  -21.964 -29.050 0.79   45.83  ? 26   GLU B OE1 1 
ATOM   180  O OE2 . GLU A 1 26  ? 12.614  -23.667 -30.419 0.79   46.66  ? 26   GLU B OE2 1 
ATOM   181  N N   . LEU A 1 27  ? 9.023   -22.566 -25.037 1.00   37.50  ? 27   LEU B N   1 
ATOM   182  C CA  . LEU A 1 27  ? 9.187   -22.107 -23.652 1.00   39.24  ? 27   LEU B CA  1 
ATOM   183  C C   . LEU A 1 27  ? 10.420  -21.228 -23.530 1.00   40.15  ? 27   LEU B C   1 
ATOM   184  O O   . LEU A 1 27  ? 11.437  -21.508 -24.152 1.00   40.61  ? 27   LEU B O   1 
ATOM   185  C CB  . LEU A 1 27  ? 9.305   -23.296 -22.696 1.00   39.00  ? 27   LEU B CB  1 
ATOM   186  C CG  . LEU A 1 27  ? 8.006   -24.081 -22.483 1.00   39.51  ? 27   LEU B CG  1 
ATOM   187  C CD1 . LEU A 1 27  ? 8.284   -25.403 -21.757 1.00   38.44  ? 27   LEU B CD1 1 
ATOM   188  C CD2 . LEU A 1 27  ? 6.981   -23.233 -21.728 1.00   37.46  ? 27   LEU B CD2 1 
ATOM   189  N N   . GLY A 1 28  ? 10.328  -20.168 -22.730 1.00   41.85  ? 28   GLY B N   1 
ATOM   190  C CA  . GLY A 1 28  ? 11.463  -19.270 -22.502 1.00   43.34  ? 28   GLY B CA  1 
ATOM   191  C C   . GLY A 1 28  ? 12.569  -19.955 -21.722 1.00   45.00  ? 28   GLY B C   1 
ATOM   192  O O   . GLY A 1 28  ? 12.318  -20.907 -20.979 1.00   44.10  ? 28   GLY B O   1 
ATOM   193  N N   . LYS A 1 29  ? 13.793  -19.469 -21.891 1.00   46.94  ? 29   LYS B N   1 
ATOM   194  C CA  . LYS A 1 29  ? 14.966  -20.063 -21.256 1.00   50.34  ? 29   LYS B CA  1 
ATOM   195  C C   . LYS A 1 29  ? 14.999  -19.728 -19.764 1.00   52.25  ? 29   LYS B C   1 
ATOM   196  O O   . LYS A 1 29  ? 14.825  -18.566 -19.382 1.00   51.34  ? 29   LYS B O   1 
ATOM   197  C CB  . LYS A 1 29  ? 16.251  -19.562 -21.928 1.00   50.31  ? 29   LYS B CB  1 
ATOM   198  C CG  . LYS A 1 29  ? 16.175  -19.509 -23.452 1.00   53.47  ? 29   LYS B CG  1 
ATOM   199  C CD  . LYS A 1 29  ? 17.350  -18.735 -24.047 1.00   57.61  ? 29   LYS B CD  1 
ATOM   200  C CE  . LYS A 1 29  ? 17.215  -18.565 -25.558 1.00   59.56  ? 29   LYS B CE  1 
ATOM   201  N NZ  . LYS A 1 29  ? 17.410  -19.846 -26.311 1.00   61.06  ? 29   LYS B NZ  1 
ATOM   202  N N   . VAL A 1 30  ? 15.196  -20.749 -18.930 1.00   55.63  ? 30   VAL B N   1 
ATOM   203  C CA  . VAL A 1 30  ? 15.367  -20.546 -17.488 1.00   59.93  ? 30   VAL B CA  1 
ATOM   204  C C   . VAL A 1 30  ? 16.553  -21.342 -16.954 1.00   63.05  ? 30   VAL B C   1 
ATOM   205  O O   . VAL A 1 30  ? 16.709  -22.520 -17.273 1.00   63.44  ? 30   VAL B O   1 
ATOM   206  C CB  . VAL A 1 30  ? 14.122  -20.966 -16.660 1.00   59.60  ? 30   VAL B CB  1 
ATOM   207  C CG1 . VAL A 1 30  ? 14.179  -20.337 -15.268 1.00   59.80  ? 30   VAL B CG1 1 
ATOM   208  C CG2 . VAL A 1 30  ? 12.829  -20.576 -17.347 1.00   59.71  ? 30   VAL B CG2 1 
ATOM   209  N N   . VAL A 1 31  ? 17.380  -20.691 -16.141 1.00   67.34  ? 31   VAL B N   1 
ATOM   210  C CA  . VAL A 1 31  ? 18.419  -21.374 -15.368 1.00   71.48  ? 31   VAL B CA  1 
ATOM   211  C C   . VAL A 1 31  ? 17.851  -21.643 -13.972 1.00   73.77  ? 31   VAL B C   1 
ATOM   212  O O   . VAL A 1 31  ? 17.931  -20.783 -13.093 1.00   74.27  ? 31   VAL B O   1 
ATOM   213  C CB  . VAL A 1 31  ? 19.705  -20.510 -15.260 1.00   71.56  ? 31   VAL B CB  1 
ATOM   214  C CG1 . VAL A 1 31  ? 20.821  -21.276 -14.551 1.00   72.01  ? 31   VAL B CG1 1 
ATOM   215  C CG2 . VAL A 1 31  ? 20.170  -20.052 -16.639 1.00   72.13  ? 31   VAL B CG2 1 
ATOM   216  N N   . THR A 1 32  ? 17.270  -22.826 -13.772 0.35   76.35  ? 32   THR B N   1 
ATOM   217  C CA  . THR A 1 32  ? 16.464  -23.088 -12.572 0.35   78.65  ? 32   THR B CA  1 
ATOM   218  C C   . THR A 1 32  ? 16.860  -24.327 -11.772 0.35   80.18  ? 32   THR B C   1 
ATOM   219  O O   . THR A 1 32  ? 16.317  -25.411 -11.989 0.35   80.38  ? 32   THR B O   1 
ATOM   220  C CB  . THR A 1 32  ? 14.963  -23.186 -12.923 0.35   78.61  ? 32   THR B CB  1 
ATOM   221  O OG1 . THR A 1 32  ? 14.219  -23.560 -11.758 0.35   78.66  ? 32   THR B OG1 1 
ATOM   222  C CG2 . THR A 1 32  ? 14.738  -24.220 -14.016 0.35   78.84  ? 32   THR B CG2 1 
ATOM   223  N N   . LYS A 1 33  ? 17.788  -24.161 -10.833 0.31   82.15  ? 33   LYS B N   1 
ATOM   224  C CA  . LYS A 1 33  ? 18.214  -25.274 -9.984  0.31   84.31  ? 33   LYS B CA  1 
ATOM   225  C C   . LYS A 1 33  ? 17.826  -25.057 -8.516  0.31   86.57  ? 33   LYS B C   1 
ATOM   226  O O   . LYS A 1 33  ? 17.152  -24.082 -8.182  0.31   86.55  ? 33   LYS B O   1 
ATOM   227  C CB  . LYS A 1 33  ? 19.724  -25.516 -10.136 0.31   83.80  ? 33   LYS B CB  1 
ATOM   228  C CG  . LYS A 1 33  ? 20.604  -24.400 -9.599  0.31   83.37  ? 33   LYS B CG  1 
ATOM   229  C CD  . LYS A 1 33  ? 21.753  -24.085 -10.554 0.31   82.62  ? 33   LYS B CD  1 
ATOM   230  C CE  . LYS A 1 33  ? 22.652  -22.988 -10.000 0.31   82.26  ? 33   LYS B CE  1 
ATOM   231  N NZ  . LYS A 1 33  ? 23.547  -22.420 -11.045 0.31   82.03  ? 33   LYS B NZ  1 
ATOM   232  N N   . LYS A 1 34  ? 18.218  -25.996 -7.658  1.00   105.27 ? 34   LYS B N   1 
ATOM   233  C CA  . LYS A 1 34  ? 18.106  -25.831 -6.213  1.00   102.45 ? 34   LYS B CA  1 
ATOM   234  C C   . LYS A 1 34  ? 19.480  -26.010 -5.587  1.00   106.25 ? 34   LYS B C   1 
ATOM   235  O O   . LYS A 1 34  ? 20.078  -27.087 -5.684  1.00   106.08 ? 34   LYS B O   1 
ATOM   236  C CB  . LYS A 1 34  ? 17.115  -26.825 -5.605  1.00   96.87  ? 34   LYS B CB  1 
ATOM   237  C CG  . LYS A 1 34  ? 15.695  -26.292 -5.462  1.00   102.29 ? 34   LYS B CG  1 
ATOM   238  C CD  . LYS A 1 34  ? 15.150  -26.504 -4.043  1.00   98.10  ? 34   LYS B CD  1 
ATOM   239  C CE  . LYS A 1 34  ? 15.223  -27.970 -3.593  1.00   99.76  ? 34   LYS B CE  1 
ATOM   240  N NZ  . LYS A 1 34  ? 14.865  -28.116 -2.150  1.00   101.33 ? 34   LYS B NZ  1 
ATOM   241  N N   . PHE A 1 35  ? 19.979  -24.951 -4.953  0.62   89.18  ? 35   PHE B N   1 
ATOM   242  C CA  . PHE A 1 35  ? 21.324  -24.948 -4.371  0.62   86.06  ? 35   PHE B CA  1 
ATOM   243  C C   . PHE A 1 35  ? 21.502  -25.997 -3.278  0.62   83.95  ? 35   PHE B C   1 
ATOM   244  O O   . PHE A 1 35  ? 20.534  -26.562 -2.759  0.62   83.81  ? 35   PHE B O   1 
ATOM   245  C CB  . PHE A 1 35  ? 21.662  -23.584 -3.774  0.62   86.06  ? 35   PHE B CB  1 
ATOM   246  C CG  . PHE A 1 35  ? 21.562  -22.446 -4.739  0.62   85.65  ? 35   PHE B CG  1 
ATOM   247  C CD1 . PHE A 1 35  ? 20.476  -21.579 -4.689  0.62   85.32  ? 35   PHE B CD1 1 
ATOM   248  C CD2 . PHE A 1 35  ? 22.560  -22.220 -5.683  0.62   85.48  ? 35   PHE B CD2 1 
ATOM   249  C CE1 . PHE A 1 35  ? 20.380  -20.509 -5.563  0.62   85.01  ? 35   PHE B CE1 1 
ATOM   250  C CE2 . PHE A 1 35  ? 22.470  -21.153 -6.571  0.62   85.40  ? 35   PHE B CE2 1 
ATOM   251  C CZ  . PHE A 1 35  ? 21.378  -20.294 -6.509  0.62   85.26  ? 35   PHE B CZ  1 
ATOM   252  N N   . SER A 1 36  ? 22.757  -26.227 -2.917  0.34   81.28  ? 36   SER B N   1 
ATOM   253  C CA  . SER A 1 36  ? 23.096  -27.264 -1.956  0.34   78.77  ? 36   SER B CA  1 
ATOM   254  C C   . SER A 1 36  ? 22.251  -27.231 -0.676  0.34   77.11  ? 36   SER B C   1 
ATOM   255  O O   . SER A 1 36  ? 21.952  -28.280 -0.102  0.34   76.87  ? 36   SER B O   1 
ATOM   256  C CB  . SER A 1 36  ? 24.582  -27.193 -1.617  0.34   78.77  ? 36   SER B CB  1 
ATOM   257  O OG  . SER A 1 36  ? 25.033  -28.426 -1.066  0.34   78.61  ? 36   SER B OG  1 
ATOM   258  N N   . ASN A 1 37  ? 21.863  -26.037 -0.232  0.36   75.04  ? 37   ASN B N   1 
ATOM   259  C CA  . ASN A 1 37  ? 21.117  -25.910 1.022   0.36   72.68  ? 37   ASN B CA  1 
ATOM   260  C C   . ASN A 1 37  ? 19.602  -25.849 0.839   0.36   70.23  ? 37   ASN B C   1 
ATOM   261  O O   . ASN A 1 37  ? 18.874  -25.433 1.742   0.36   70.20  ? 37   ASN B O   1 
ATOM   262  C CB  . ASN A 1 37  ? 21.599  -24.699 1.820   0.36   73.22  ? 37   ASN B CB  1 
ATOM   263  C CG  . ASN A 1 37  ? 21.076  -23.392 1.271   0.36   73.46  ? 37   ASN B CG  1 
ATOM   264  O OD1 . ASN A 1 37  ? 21.164  -23.128 0.072   0.36   73.77  ? 37   ASN B OD1 1 
ATOM   265  N ND2 . ASN A 1 37  ? 20.530  -22.559 2.151   0.36   73.53  ? 37   ASN B ND2 1 
ATOM   266  N N   . GLN A 1 38  ? 19.137  -26.266 -0.335  0.33   66.50  ? 38   GLN B N   1 
ATOM   267  C CA  . GLN A 1 38  ? 17.705  -26.379 -0.616  0.33   62.85  ? 38   GLN B CA  1 
ATOM   268  C C   . GLN A 1 38  ? 17.058  -25.073 -1.088  0.33   60.96  ? 38   GLN B C   1 
ATOM   269  O O   . GLN A 1 38  ? 15.813  -25.003 -1.255  0.33   60.41  ? 38   GLN B O   1 
ATOM   270  C CB  . GLN A 1 38  ? 16.946  -26.915 0.602   0.33   62.69  ? 38   GLN B CB  1 
ATOM   271  C CG  . GLN A 1 38  ? 17.633  -28.068 1.314   0.33   62.23  ? 38   GLN B CG  1 
ATOM   272  C CD  . GLN A 1 38  ? 18.419  -28.951 0.367   0.33   62.02  ? 38   GLN B CD  1 
ATOM   273  O OE1 . GLN A 1 38  ? 19.648  -28.880 0.319   0.33   62.16  ? 38   GLN B OE1 1 
ATOM   274  N NE2 . GLN A 1 38  ? 17.718  -29.780 -0.400  0.33   61.73  ? 38   GLN B NE2 1 
ATOM   275  N N   . GLU A 1 39  ? 17.891  -24.046 -1.310  0.53   59.24  ? 39   GLU B N   1 
ATOM   276  C CA  . GLU A 1 39  ? 17.360  -22.774 -1.799  0.53   58.26  ? 39   GLU B CA  1 
ATOM   277  C C   . GLU A 1 39  ? 17.102  -22.868 -3.290  0.53   58.74  ? 39   GLU B C   1 
ATOM   278  O O   . GLU A 1 39  ? 17.897  -23.460 -4.023  0.53   58.48  ? 39   GLU B O   1 
ATOM   279  C CB  . GLU A 1 39  ? 18.327  -21.619 -1.517  0.53   57.55  ? 39   GLU B CB  1 
ATOM   280  C CG  . GLU A 1 39  ? 18.700  -21.455 -0.050  0.53   56.06  ? 39   GLU B CG  1 
ATOM   281  C CD  . GLU A 1 39  ? 19.252  -20.077 0.287   0.53   54.71  ? 39   GLU B CD  1 
ATOM   282  O OE1 . GLU A 1 39  ? 19.607  -19.312 -0.643  0.53   54.17  ? 39   GLU B OE1 1 
ATOM   283  O OE2 . GLU A 1 39  ? 19.333  -19.758 1.495   0.53   53.52  ? 39   GLU B OE2 1 
ATOM   284  N N   . THR A 1 40  ? 15.992  -22.285 -3.735  1.00   59.71  ? 40   THR B N   1 
ATOM   285  C CA  . THR A 1 40  ? 15.679  -22.220 -5.159  1.00   60.93  ? 40   THR B CA  1 
ATOM   286  C C   . THR A 1 40  ? 16.621  -21.268 -5.895  1.00   62.75  ? 40   THR B C   1 
ATOM   287  O O   . THR A 1 40  ? 16.862  -20.141 -5.447  1.00   62.06  ? 40   THR B O   1 
ATOM   288  C CB  . THR A 1 40  ? 14.223  -21.756 -5.407  1.00   60.65  ? 40   THR B CB  1 
ATOM   289  O OG1 . THR A 1 40  ? 13.319  -22.596 -4.682  1.00   58.08  ? 40   THR B OG1 1 
ATOM   290  C CG2 . THR A 1 40  ? 13.877  -21.812 -6.901  1.00   60.26  ? 40   THR B CG2 1 
ATOM   291  N N   . CYS A 1 41  ? 17.143  -21.736 -7.025  1.00   65.32  ? 41   CYS B N   1 
ATOM   292  C CA  . CYS A 1 41  ? 17.889  -20.894 -7.956  1.00   67.60  ? 41   CYS B CA  1 
ATOM   293  C C   . CYS A 1 41  ? 17.084  -20.622 -9.216  1.00   67.26  ? 41   CYS B C   1 
ATOM   294  O O   . CYS A 1 41  ? 16.496  -21.534 -9.802  1.00   67.71  ? 41   CYS B O   1 
ATOM   295  C CB  . CYS A 1 41  ? 19.201  -21.561 -8.360  1.00   73.36  ? 41   CYS B CB  1 
ATOM   296  S SG  . CYS A 1 41  ? 19.879  -20.943 -9.942  1.00   91.42  ? 41   CYS B SG  1 
ATOM   297  N N   . VAL A 1 42  ? 17.077  -19.359 -9.628  1.00   65.94  ? 42   VAL B N   1 
ATOM   298  C CA  . VAL A 1 42  ? 16.496  -18.959 -10.902 1.00   63.84  ? 42   VAL B CA  1 
ATOM   299  C C   . VAL A 1 42  ? 17.317  -17.855 -11.544 1.00   62.02  ? 42   VAL B C   1 
ATOM   300  O O   . VAL A 1 42  ? 17.991  -17.078 -10.861 1.00   62.13  ? 42   VAL B O   1 
ATOM   301  C CB  . VAL A 1 42  ? 14.998  -18.561 -10.767 1.00   64.11  ? 42   VAL B CB  1 
ATOM   302  C CG1 . VAL A 1 42  ? 14.627  -17.397 -11.683 1.00   63.30  ? 42   VAL B CG1 1 
ATOM   303  C CG2 . VAL A 1 42  ? 14.112  -19.760 -11.051 1.00   64.09  ? 42   VAL B CG2 1 
ATOM   304  N N   . GLU A 1 43  ? 17.268  -17.821 -12.870 0.47   59.11  ? 43   GLU B N   1 
ATOM   305  C CA  . GLU A 1 43  ? 17.862  -16.764 -13.657 0.47   56.53  ? 43   GLU B CA  1 
ATOM   306  C C   . GLU A 1 43  ? 17.187  -16.833 -15.014 0.47   55.13  ? 43   GLU B C   1 
ATOM   307  O O   . GLU A 1 43  ? 17.403  -17.780 -15.770 0.47   54.22  ? 43   GLU B O   1 
ATOM   308  C CB  . GLU A 1 43  ? 19.366  -16.990 -13.792 0.47   56.41  ? 43   GLU B CB  1 
ATOM   309  C CG  . GLU A 1 43  ? 20.090  -15.944 -14.611 0.47   56.61  ? 43   GLU B CG  1 
ATOM   310  C CD  . GLU A 1 43  ? 21.521  -16.347 -14.907 0.47   57.57  ? 43   GLU B CD  1 
ATOM   311  O OE1 . GLU A 1 43  ? 22.031  -15.983 -15.993 0.47   57.80  ? 43   GLU B OE1 1 
ATOM   312  O OE2 . GLU A 1 43  ? 22.133  -17.038 -14.061 0.47   57.92  ? 43   GLU B OE2 1 
ATOM   313  N N   . ILE A 1 44  ? 16.339  -15.848 -15.298 1.00   54.31  ? 44   ILE B N   1 
ATOM   314  C CA  . ILE A 1 44  ? 15.654  -15.764 -16.587 1.00   53.53  ? 44   ILE B CA  1 
ATOM   315  C C   . ILE A 1 44  ? 16.700  -15.608 -17.693 1.00   52.97  ? 44   ILE B C   1 
ATOM   316  O O   . ILE A 1 44  ? 17.380  -14.584 -17.778 1.00   53.19  ? 44   ILE B O   1 
ATOM   317  C CB  . ILE A 1 44  ? 14.638  -14.584 -16.628 1.00   53.47  ? 44   ILE B CB  1 
ATOM   318  C CG1 . ILE A 1 44  ? 13.689  -14.619 -15.416 1.00   53.43  ? 44   ILE B CG1 1 
ATOM   319  C CG2 . ILE A 1 44  ? 13.850  -14.576 -17.945 1.00   52.80  ? 44   ILE B CG2 1 
ATOM   320  C CD1 . ILE A 1 44  ? 12.795  -15.864 -15.309 1.00   53.90  ? 44   ILE B CD1 1 
ATOM   321  N N   . GLY A 1 45  ? 16.820  -16.633 -18.534 1.00   51.84  ? 45   GLY B N   1 
ATOM   322  C CA  . GLY A 1 45  ? 17.888  -16.698 -19.529 1.00   50.57  ? 45   GLY B CA  1 
ATOM   323  C C   . GLY A 1 45  ? 17.713  -15.847 -20.774 1.00   49.79  ? 45   GLY B C   1 
ATOM   324  O O   . GLY A 1 45  ? 18.478  -15.982 -21.725 1.00   50.21  ? 45   GLY B O   1 
ATOM   325  N N   . GLU A 1 46  ? 16.706  -14.983 -20.778 1.00   48.73  ? 46   GLU B N   1 
ATOM   326  C CA  . GLU A 1 46  ? 16.472  -14.081 -21.899 1.00   47.34  ? 46   GLU B CA  1 
ATOM   327  C C   . GLU A 1 46  ? 15.782  -12.816 -21.411 1.00   45.65  ? 46   GLU B C   1 
ATOM   328  O O   . GLU A 1 46  ? 15.129  -12.836 -20.370 1.00   44.63  ? 46   GLU B O   1 
ATOM   329  C CB  . GLU A 1 46  ? 15.639  -14.773 -22.986 1.00   47.96  ? 46   GLU B CB  1 
ATOM   330  C CG  . GLU A 1 46  ? 14.371  -15.466 -22.492 1.00   49.71  ? 46   GLU B CG  1 
ATOM   331  C CD  . GLU A 1 46  ? 13.645  -16.209 -23.607 1.00   52.59  ? 46   GLU B CD  1 
ATOM   332  O OE1 . GLU A 1 46  ? 12.783  -15.587 -24.262 1.00   54.84  ? 46   GLU B OE1 1 
ATOM   333  O OE2 . GLU A 1 46  ? 13.936  -17.404 -23.839 1.00   52.97  ? 46   GLU B OE2 1 
ATOM   334  N N   . SER A 1 47  ? 15.934  -11.720 -22.150 1.00   43.57  ? 47   SER B N   1 
ATOM   335  C CA  . SER A 1 47  ? 15.254  -10.475 -21.810 1.00   41.56  ? 47   SER B CA  1 
ATOM   336  C C   . SER A 1 47  ? 13.748  -10.697 -21.819 1.00   40.36  ? 47   SER B C   1 
ATOM   337  O O   . SER A 1 47  ? 13.227  -11.368 -22.703 1.00   38.90  ? 47   SER B O   1 
ATOM   338  C CB  . SER A 1 47  ? 15.612  -9.374  -22.803 1.00   41.43  ? 47   SER B CB  1 
ATOM   339  O OG  . SER A 1 47  ? 14.847  -8.207  -22.550 1.00   40.96  ? 47   SER B OG  1 
ATOM   340  N N   . VAL A 1 48  ? 13.049  -10.158 -20.824 1.00   38.53  ? 48   VAL B N   1 
ATOM   341  C CA  . VAL A 1 48  ? 11.587  -10.188 -20.854 1.00   36.67  ? 48   VAL B CA  1 
ATOM   342  C C   . VAL A 1 48  ? 11.062  -8.765  -20.943 1.00   36.51  ? 48   VAL B C   1 
ATOM   343  O O   . VAL A 1 48  ? 9.855   -8.523  -20.812 1.00   35.77  ? 48   VAL B O   1 
ATOM   344  C CB  . VAL A 1 48  ? 10.991  -10.914 -19.628 1.00   37.18  ? 48   VAL B CB  1 
ATOM   345  C CG1 . VAL A 1 48  ? 11.264  -12.414 -19.720 1.00   36.41  ? 48   VAL B CG1 1 
ATOM   346  C CG2 . VAL A 1 48  ? 11.540  -10.320 -18.315 1.00   35.33  ? 48   VAL B CG2 1 
ATOM   347  N N   . ARG A 1 49  ? 11.974  -7.827  -21.187 1.00   35.58  ? 49   ARG B N   1 
ATOM   348  C CA  . ARG A 1 49  ? 11.654  -6.399  -21.139 1.00   36.01  ? 49   ARG B CA  1 
ATOM   349  C C   . ARG A 1 49  ? 10.494  -6.060  -22.069 1.00   35.73  ? 49   ARG B C   1 
ATOM   350  O O   . ARG A 1 49  ? 10.541  -6.364  -23.245 1.00   35.55  ? 49   ARG B O   1 
ATOM   351  C CB  . ARG A 1 49  ? 12.895  -5.552  -21.464 1.00   36.40  ? 49   ARG B CB  1 
ATOM   352  C CG  . ARG A 1 49  ? 12.713  -4.049  -21.235 1.00   37.30  ? 49   ARG B CG  1 
ATOM   353  C CD  . ARG A 1 49  ? 14.019  -3.252  -21.412 1.00   38.83  ? 49   ARG B CD  1 
ATOM   354  N NE  . ARG A 1 49  ? 15.102  -3.680  -20.516 1.00   38.78  ? 49   ARG B NE  1 
ATOM   355  C CZ  . ARG A 1 49  ? 15.378  -3.137  -19.330 1.00   40.53  ? 49   ARG B CZ  1 
ATOM   356  N NH1 . ARG A 1 49  ? 14.661  -2.124  -18.866 1.00   41.32  ? 49   ARG B NH1 1 
ATOM   357  N NH2 . ARG A 1 49  ? 16.387  -3.600  -18.602 1.00   41.84  ? 49   ARG B NH2 1 
ATOM   358  N N   . GLY A 1 50  ? 9.441   -5.459  -21.523 1.00   35.41  ? 50   GLY B N   1 
ATOM   359  C CA  . GLY A 1 50  ? 8.273   -5.071  -22.305 1.00   33.95  ? 50   GLY B CA  1 
ATOM   360  C C   . GLY A 1 50  ? 7.416   -6.220  -22.822 1.00   33.41  ? 50   GLY B C   1 
ATOM   361  O O   . GLY A 1 50  ? 6.601   -6.023  -23.724 1.00   35.02  ? 50   GLY B O   1 
ATOM   362  N N   . GLU A 1 51  ? 7.582   -7.412  -22.254 0.52   30.53  ? 51   GLU B N   1 
ATOM   363  C CA  . GLU A 1 51  ? 6.878   -8.599  -22.742 0.52   28.42  ? 51   GLU B CA  1 
ATOM   364  C C   . GLU A 1 51  ? 5.682   -8.997  -21.871 0.52   28.29  ? 51   GLU B C   1 
ATOM   365  O O   . GLU A 1 51  ? 5.652   -8.697  -20.683 0.52   25.43  ? 51   GLU B O   1 
ATOM   366  C CB  . GLU A 1 51  ? 7.856   -9.752  -22.856 0.52   28.57  ? 51   GLU B CB  1 
ATOM   367  C CG  . GLU A 1 51  ? 9.092   -9.407  -23.674 0.52   29.57  ? 51   GLU B CG  1 
ATOM   368  C CD  . GLU A 1 51  ? 8.927   -9.728  -25.123 0.52   32.61  ? 51   GLU B CD  1 
ATOM   369  O OE1 . GLU A 1 51  ? 8.299   -8.919  -25.855 0.52   31.27  ? 51   GLU B OE1 1 
ATOM   370  O OE2 . GLU A 1 51  ? 9.433   -10.799 -25.527 0.52   35.70  ? 51   GLU B OE2 1 
ATOM   371  N N   . ASP A 1 52  ? 4.699   -9.657  -22.480 1.00   29.72  ? 52   ASP B N   1 
ATOM   372  C CA  . ASP A 1 52  ? 3.533   -10.189 -21.783 1.00   32.11  ? 52   ASP B CA  1 
ATOM   373  C C   . ASP A 1 52  ? 3.885   -11.605 -21.304 1.00   32.54  ? 52   ASP B C   1 
ATOM   374  O O   . ASP A 1 52  ? 3.785   -12.576 -22.057 1.00   33.14  ? 52   ASP B O   1 
ATOM   375  C CB  . ASP A 1 52  ? 2.303   -10.191 -22.714 1.00   31.74  ? 52   ASP B CB  1 
ATOM   376  C CG  . ASP A 1 52  ? 0.997   -10.398 -21.971 1.00   35.21  ? 52   ASP B CG  1 
ATOM   377  O OD1 . ASP A 1 52  ? 0.977   -10.209 -20.732 1.00   37.49  ? 52   ASP B OD1 1 
ATOM   378  O OD2 . ASP A 1 52  ? -0.025  -10.743 -22.618 1.00   36.32  ? 52   ASP B OD2 1 
ATOM   379  N N   . VAL A 1 53  ? 4.313   -11.701 -20.045 1.00   32.52  ? 53   VAL B N   1 
ATOM   380  C CA  . VAL A 1 53  ? 4.901   -12.930 -19.495 1.00   31.95  ? 53   VAL B CA  1 
ATOM   381  C C   . VAL A 1 53  ? 3.880   -13.813 -18.762 1.00   31.77  ? 53   VAL B C   1 
ATOM   382  O O   . VAL A 1 53  ? 3.129   -13.329 -17.914 1.00   32.97  ? 53   VAL B O   1 
ATOM   383  C CB  . VAL A 1 53  ? 6.093   -12.600 -18.541 1.00   32.04  ? 53   VAL B CB  1 
ATOM   384  C CG1 . VAL A 1 53  ? 6.630   -13.871 -17.857 1.00   31.70  ? 53   VAL B CG1 1 
ATOM   385  C CG2 . VAL A 1 53  ? 7.224   -11.878 -19.298 1.00   32.52  ? 53   VAL B CG2 1 
ATOM   386  N N   . TYR A 1 54  ? 3.870   -15.105 -19.086 1.00   30.11  ? 54   TYR B N   1 
ATOM   387  C CA  . TYR A 1 54  ? 3.027   -16.078 -18.401 1.00   29.80  ? 54   TYR B CA  1 
ATOM   388  C C   . TYR A 1 54  ? 3.930   -17.122 -17.794 1.00   30.31  ? 54   TYR B C   1 
ATOM   389  O O   . TYR A 1 54  ? 4.749   -17.704 -18.499 1.00   30.28  ? 54   TYR B O   1 
ATOM   390  C CB  . TYR A 1 54  ? 2.032   -16.713 -19.385 1.00   29.28  ? 54   TYR B CB  1 
ATOM   391  C CG  . TYR A 1 54  ? 1.103   -15.671 -19.946 1.00   30.16  ? 54   TYR B CG  1 
ATOM   392  C CD1 . TYR A 1 54  ? 1.541   -14.779 -20.925 1.00   31.90  ? 54   TYR B CD1 1 
ATOM   393  C CD2 . TYR A 1 54  ? -0.202  -15.537 -19.467 1.00   28.03  ? 54   TYR B CD2 1 
ATOM   394  C CE1 . TYR A 1 54  ? 0.704   -13.787 -21.421 1.00   30.70  ? 54   TYR B CE1 1 
ATOM   395  C CE2 . TYR A 1 54  ? -1.044  -14.546 -19.959 1.00   29.17  ? 54   TYR B CE2 1 
ATOM   396  C CZ  . TYR A 1 54  ? -0.586  -13.682 -20.943 1.00   31.28  ? 54   TYR B CZ  1 
ATOM   397  O OH  . TYR A 1 54  ? -1.407  -12.698 -21.443 1.00   32.16  ? 54   TYR B OH  1 
ATOM   398  N N   . ILE A 1 55  ? 3.803   -17.345 -16.485 1.00   30.47  ? 55   ILE B N   1 
ATOM   399  C CA  . ILE A 1 55  ? 4.614   -18.366 -15.813 1.00   30.06  ? 55   ILE B CA  1 
ATOM   400  C C   . ILE A 1 55  ? 3.707   -19.486 -15.364 1.00   30.51  ? 55   ILE B C   1 
ATOM   401  O O   . ILE A 1 55  ? 2.776   -19.258 -14.593 1.00   30.25  ? 55   ILE B O   1 
ATOM   402  C CB  . ILE A 1 55  ? 5.385   -17.817 -14.594 1.00   30.64  ? 55   ILE B CB  1 
ATOM   403  C CG1 . ILE A 1 55  ? 6.329   -16.690 -15.021 1.00   29.93  ? 55   ILE B CG1 1 
ATOM   404  C CG2 . ILE A 1 55  ? 6.175   -18.954 -13.896 1.00   29.44  ? 55   ILE B CG2 1 
ATOM   405  C CD1 . ILE A 1 55  ? 6.714   -15.763 -13.878 1.00   32.93  ? 55   ILE B CD1 1 
ATOM   406  N N   . VAL A 1 56  ? 3.986   -20.694 -15.850 1.00   31.20  ? 56   VAL B N   1 
ATOM   407  C CA  . VAL A 1 56  ? 3.123   -21.846 -15.593 1.00   32.66  ? 56   VAL B CA  1 
ATOM   408  C C   . VAL A 1 56  ? 3.637   -22.677 -14.415 1.00   34.05  ? 56   VAL B C   1 
ATOM   409  O O   . VAL A 1 56  ? 4.766   -23.154 -14.435 1.00   35.27  ? 56   VAL B O   1 
ATOM   410  C CB  . VAL A 1 56  ? 2.979   -22.750 -16.846 1.00   32.39  ? 56   VAL B CB  1 
ATOM   411  C CG1 . VAL A 1 56  ? 2.026   -23.906 -16.561 1.00   32.78  ? 56   VAL B CG1 1 
ATOM   412  C CG2 . VAL A 1 56  ? 2.476   -21.940 -18.026 1.00   32.53  ? 56   VAL B CG2 1 
ATOM   413  N N   . GLN A 1 57  ? 2.867   -22.872 -13.370 0.32   34.00  ? 57   GLN B N   1 
ATOM   414  C CA  . GLN A 1 57  ? 3.343   -23.600 -12.182 0.32   38.46  ? 57   GLN B CA  1 
ATOM   415  C C   . GLN A 1 57  ? 3.716   -25.093 -12.384 0.32   43.62  ? 57   GLN B C   1 
ATOM   416  O O   . GLN A 1 57  ? 3.037   -25.805 -13.090 0.32   42.07  ? 57   GLN B O   1 
ATOM   417  C CB  . GLN A 1 57  ? 2.363   -23.395 -11.035 0.32   36.60  ? 57   GLN B CB  1 
ATOM   418  C CG  . GLN A 1 57  ? 1.598   -24.636 -10.597 0.32   35.67  ? 57   GLN B CG  1 
ATOM   419  C CD  . GLN A 1 57  ? 1.706   -24.912 -9.089  0.32   33.83  ? 57   GLN B CD  1 
ATOM   420  O OE1 . GLN A 1 57  ? 1.549   -26.042 -8.638  0.32   33.52  ? 57   GLN B OE1 1 
ATOM   421  N NE2 . GLN A 1 57  ? 1.990   -23.877 -8.320  0.32   32.43  ? 57   GLN B NE2 1 
ATOM   422  N N   . SER A 1 58  ? 4.925   -25.396 -11.902 1.00   69.02  ? 58   SER B N   1 
ATOM   423  C CA  . SER A 1 58  ? 5.627   -26.642 -12.147 1.00   78.21  ? 58   SER B CA  1 
ATOM   424  C C   . SER A 1 58  ? 5.091   -27.690 -11.260 1.00   81.25  ? 58   SER B C   1 
ATOM   425  O O   . SER A 1 58  ? 4.669   -27.410 -10.165 1.00   83.19  ? 58   SER B O   1 
ATOM   426  C CB  . SER A 1 58  ? 7.105   -26.548 -11.764 1.00   81.07  ? 58   SER B CB  1 
ATOM   427  O OG  . SER A 1 58  ? 7.717   -27.823 -11.764 1.00   83.28  ? 58   SER B OG  1 
ATOM   428  N N   . GLY A 1 59  ? 5.083   -28.916 -11.715 0.0000 67.29  ? 59   GLY B N   1 
ATOM   429  C CA  . GLY A 1 59  ? 4.357   -29.881 -10.942 0.0000 69.33  ? 59   GLY B CA  1 
ATOM   430  C C   . GLY A 1 59  ? 4.878   -30.925 -10.000 0.0000 70.69  ? 59   GLY B C   1 
ATOM   431  O O   . GLY A 1 59  ? 4.291   -32.002 -9.909  0.0000 70.77  ? 59   GLY B O   1 
ATOM   432  N N   . CYS A 1 60  ? 5.988   -30.668 -9.314  0.010  72.13  ? 60   CYS B N   1 
ATOM   433  C CA  . CYS A 1 60  ? 6.796   -31.857 -9.059  0.010  73.74  ? 60   CYS B CA  1 
ATOM   434  C C   . CYS A 1 60  ? 6.020   -32.267 -7.763  0.010  74.79  ? 60   CYS B C   1 
ATOM   435  O O   . CYS A 1 60  ? 6.392   -33.233 -7.100  0.010  75.25  ? 60   CYS B O   1 
ATOM   436  C CB  . CYS A 1 60  ? 8.293   -31.754 -8.937  0.010  73.45  ? 60   CYS B CB  1 
ATOM   437  S SG  . CYS A 1 60  ? 8.789   -30.146 -8.354  0.010  73.75  ? 60   CYS B SG  1 
ATOM   438  N N   . GLY A 1 61  ? 4.956   -31.567 -7.394  0.010  106.97 ? 61   GLY B N   1 
ATOM   439  C CA  . GLY A 1 61  ? 4.251   -31.945 -6.172  0.010  102.07 ? 61   GLY B CA  1 
ATOM   440  C C   . GLY A 1 61  ? 4.827   -31.552 -4.807  0.010  98.29  ? 61   GLY B C   1 
ATOM   441  O O   . GLY A 1 61  ? 4.104   -31.555 -3.820  0.010  99.50  ? 61   GLY B O   1 
ATOM   442  N N   . GLU A 1 62  ? 6.091   -31.176 -4.726  0.40   66.44  ? 62   GLU B N   1 
ATOM   443  C CA  . GLU A 1 62  ? 6.562   -30.560 -3.501  0.40   60.40  ? 62   GLU B CA  1 
ATOM   444  C C   . GLU A 1 62  ? 6.137   -29.117 -3.494  0.40   56.67  ? 62   GLU B C   1 
ATOM   445  O O   . GLU A 1 62  ? 6.811   -28.290 -4.031  0.40   54.84  ? 62   GLU B O   1 
ATOM   446  C CB  . GLU A 1 62  ? 8.066   -30.630 -3.392  0.40   60.40  ? 62   GLU B CB  1 
ATOM   447  C CG  . GLU A 1 62  ? 8.543   -30.931 -1.985  0.40   59.31  ? 62   GLU B CG  1 
ATOM   448  C CD  . GLU A 1 62  ? 8.719   -29.699 -1.111  0.40   58.31  ? 62   GLU B CD  1 
ATOM   449  O OE1 . GLU A 1 62  ? 8.195   -28.619 -1.451  0.40   56.05  ? 62   GLU B OE1 1 
ATOM   450  O OE2 . GLU A 1 62  ? 9.389   -29.828 -0.069  0.40   57.97  ? 62   GLU B OE2 1 
ATOM   451  N N   . ILE A 1 63  ? 5.007   -28.845 -2.877  1.00   53.19  ? 63   ILE B N   1 
ATOM   452  C CA  . ILE A 1 63  ? 4.368   -27.550 -2.906  1.00   50.28  ? 63   ILE B CA  1 
ATOM   453  C C   . ILE A 1 63  ? 5.179   -26.326 -2.521  1.00   47.95  ? 63   ILE B C   1 
ATOM   454  O O   . ILE A 1 63  ? 5.100   -25.316 -3.174  1.00   47.21  ? 63   ILE B O   1 
ATOM   455  C CB  . ILE A 1 63  ? 3.167   -27.558 -2.001  1.00   50.74  ? 63   ILE B CB  1 
ATOM   456  C CG1 . ILE A 1 63  ? 2.378   -28.803 -2.234  1.00   51.33  ? 63   ILE B CG1 1 
ATOM   457  C CG2 . ILE A 1 63  ? 2.282   -26.379 -2.277  1.00   51.50  ? 63   ILE B CG2 1 
ATOM   458  C CD1 . ILE A 1 63  ? 1.306   -28.971 -1.200  1.00   53.06  ? 63   ILE B CD1 1 
ATOM   459  N N   . ASN A 1 64  ? 5.925   -26.383 -1.444  1.00   44.40  ? 64   ASN B N   1 
ATOM   460  C CA  . ASN A 1 64  ? 6.569   -25.175 -1.020  1.00   42.12  ? 64   ASN B CA  1 
ATOM   461  C C   . ASN A 1 64  ? 7.690   -24.806 -1.936  1.00   41.03  ? 64   ASN B C   1 
ATOM   462  O O   . ASN A 1 64  ? 7.968   -23.659 -2.121  1.00   40.11  ? 64   ASN B O   1 
ATOM   463  C CB  . ASN A 1 64  ? 7.015   -25.251 0.425   1.00   41.64  ? 64   ASN B CB  1 
ATOM   464  C CG  . ASN A 1 64  ? 5.858   -25.331 1.390   1.00   41.21  ? 64   ASN B CG  1 
ATOM   465  O OD1 . ASN A 1 64  ? 5.972   -25.939 2.411   1.00   42.74  ? 64   ASN B OD1 1 
ATOM   466  N ND2 . ASN A 1 64  ? 4.764   -24.723 1.066   1.00   37.79  ? 64   ASN B ND2 1 
ATOM   467  N N   . ASN A 1 65  ? 8.320   -25.800 -2.519  1.00   40.19  ? 65   ASN B N   1 
ATOM   468  C CA  . ASN A 1 65  ? 9.329   -25.536 -3.511  1.00   40.60  ? 65   ASN B CA  1 
ATOM   469  C C   . ASN A 1 65  ? 8.752   -24.990 -4.807  1.00   39.39  ? 65   ASN B C   1 
ATOM   470  O O   . ASN A 1 65  ? 9.267   -24.055 -5.348  1.00   38.20  ? 65   ASN B O   1 
ATOM   471  C CB  . ASN A 1 65  ? 10.176  -26.767 -3.789  1.00   41.43  ? 65   ASN B CB  1 
ATOM   472  C CG  . ASN A 1 65  ? 11.047  -27.158 -2.623  1.00   43.43  ? 65   ASN B CG  1 
ATOM   473  O OD1 . ASN A 1 65  ? 11.531  -26.342 -1.892  1.00   43.56  ? 65   ASN B OD1 1 
ATOM   474  N ND2 . ASN A 1 65  ? 11.247  -28.432 -2.469  1.00   45.47  ? 65   ASN B ND2 1 
ATOM   475  N N   . ASN A 1 66  ? 7.685   -25.594 -5.294  1.00   38.74  ? 66   ASN B N   1 
ATOM   476  C CA  . ASN A 1 66  ? 7.003   -25.102 -6.486  1.00   38.42  ? 66   ASN B CA  1 
ATOM   477  C C   . ASN A 1 66  ? 6.509   -23.685 -6.274  1.00   36.77  ? 66   ASN B C   1 
ATOM   478  O O   . ASN A 1 66  ? 6.668   -22.815 -7.135  1.00   35.72  ? 66   ASN B O   1 
ATOM   479  C CB  . ASN A 1 66  ? 5.830   -26.013 -6.833  1.00   39.50  ? 66   ASN B CB  1 
ATOM   480  C CG  . ASN A 1 66  ? 6.284   -27.371 -7.331  1.00   42.47  ? 66   ASN B CG  1 
ATOM   481  O OD1 . ASN A 1 66  ? 7.374   -27.513 -7.890  1.00   45.52  ? 66   ASN B OD1 1 
ATOM   482  N ND2 . ASN A 1 66  ? 5.453   -28.374 -7.123  1.00   44.82  ? 66   ASN B ND2 1 
ATOM   483  N N   . LEU A 1 67  ? 5.932   -23.446 -5.106  1.00   35.26  ? 67   LEU B N   1 
ATOM   484  C CA  . LEU A 1 67  ? 5.411   -22.131 -4.803  1.00   33.52  ? 67   LEU B CA  1 
ATOM   485  C C   . LEU A 1 67  ? 6.523   -21.081 -4.743  1.00   31.63  ? 67   LEU B C   1 
ATOM   486  O O   . LEU A 1 67  ? 6.376   -20.014 -5.325  1.00   30.36  ? 67   LEU B O   1 
ATOM   487  C CB  . LEU A 1 67  ? 4.607   -22.134 -3.511  1.00   34.10  ? 67   LEU B CB  1 
ATOM   488  C CG  . LEU A 1 67  ? 4.094   -20.746 -3.104  1.00   35.32  ? 67   LEU B CG  1 
ATOM   489  C CD1 . LEU A 1 67  ? 3.154   -20.132 -4.169  1.00   33.45  ? 67   LEU B CD1 1 
ATOM   490  C CD2 . LEU A 1 67  ? 3.416   -20.813 -1.750  1.00   37.47  ? 67   LEU B CD2 1 
ATOM   491  N N   . MET A 1 68  ? 7.624   -21.383 -4.059  0.60   29.05  ? 68   MET B N   1 
ATOM   492  C CA  . MET A 1 68  ? 8.706   -20.414 -3.933  0.60   28.82  ? 68   MET B CA  1 
ATOM   493  C C   . MET A 1 68  ? 9.360   -20.146 -5.281  0.60   28.86  ? 68   MET B C   1 
ATOM   494  O O   . MET A 1 68  ? 9.700   -19.006 -5.604  0.60   25.81  ? 68   MET B O   1 
ATOM   495  C CB  . MET A 1 68  ? 9.748   -20.872 -2.903  0.60   28.97  ? 68   MET B CB  1 
ATOM   496  C CG  . MET A 1 68  ? 9.288   -20.739 -1.448  0.60   29.86  ? 68   MET B CG  1 
ATOM   497  S SD  . MET A 1 68  ? 8.826   -19.062 -0.976  0.60   32.95  ? 68   MET B SD  1 
ATOM   498  C CE  . MET A 1 68  ? 10.201  -18.147 -1.714  0.60   27.44  ? 68   MET B CE  1 
ATOM   499  N N   . GLU A 1 69  ? 9.510   -21.203 -6.070  1.00   31.27  ? 69   GLU B N   1 
ATOM   500  C CA  . GLU A 1 69  ? 10.044  -21.099 -7.425  1.00   33.58  ? 69   GLU B CA  1 
ATOM   501  C C   . GLU A 1 69  ? 9.203   -20.147 -8.281  1.00   32.19  ? 69   GLU B C   1 
ATOM   502  O O   . GLU A 1 69  ? 9.739   -19.260 -8.937  1.00   32.72  ? 69   GLU B O   1 
ATOM   503  C CB  . GLU A 1 69  ? 10.120  -22.491 -8.067  1.00   34.78  ? 69   GLU B CB  1 
ATOM   504  C CG  . GLU A 1 69  ? 10.963  -22.571 -9.338  1.00   40.75  ? 69   GLU B CG  1 
ATOM   505  C CD  . GLU A 1 69  ? 11.128  -24.007 -9.836  1.00   52.02  ? 69   GLU B CD  1 
ATOM   506  O OE1 . GLU A 1 69  ? 10.111  -24.730 -9.937  1.00   49.94  ? 69   GLU B OE1 1 
ATOM   507  O OE2 . GLU A 1 69  ? 12.275  -24.413 -10.123 1.00   56.56  ? 69   GLU B OE2 1 
ATOM   508  N N   . LEU A 1 70  ? 7.890   -20.332 -8.258  1.00   30.62  ? 70   LEU B N   1 
ATOM   509  C CA  . LEU A 1 70  ? 6.974   -19.429 -8.935  1.00   29.65  ? 70   LEU B CA  1 
ATOM   510  C C   . LEU A 1 70  ? 7.127   -17.975 -8.476  1.00   29.62  ? 70   LEU B C   1 
ATOM   511  O O   . LEU A 1 70  ? 7.195   -17.063 -9.301  1.00   29.96  ? 70   LEU B O   1 
ATOM   512  C CB  . LEU A 1 70  ? 5.532   -19.884 -8.705  1.00   28.67  ? 70   LEU B CB  1 
ATOM   513  C CG  . LEU A 1 70  ? 4.424   -18.984 -9.246  1.00   28.37  ? 70   LEU B CG  1 
ATOM   514  C CD1 . LEU A 1 70  ? 4.462   -18.898 -10.785 1.00   26.73  ? 70   LEU B CD1 1 
ATOM   515  C CD2 . LEU A 1 70  ? 3.094   -19.539 -8.785  1.00   29.20  ? 70   LEU B CD2 1 
ATOM   516  N N   . LEU A 1 71  ? 7.169   -17.751 -7.161  1.00   29.07  ? 71   LEU B N   1 
ATOM   517  C CA  . LEU A 1 71  ? 7.277   -16.388 -6.646  1.00   27.70  ? 71   LEU B CA  1 
ATOM   518  C C   . LEU A 1 71  ? 8.580   -15.731 -7.079  1.00   28.62  ? 71   LEU B C   1 
ATOM   519  O O   . LEU A 1 71  ? 8.608   -14.550 -7.463  1.00   28.09  ? 71   LEU B O   1 
ATOM   520  C CB  . LEU A 1 71  ? 7.172   -16.382 -5.126  1.00   26.56  ? 71   LEU B CB  1 
ATOM   521  C CG  . LEU A 1 71  ? 5.815   -16.826 -4.591  1.00   28.51  ? 71   LEU B CG  1 
ATOM   522  C CD1 . LEU A 1 71  ? 5.877   -16.996 -3.073  1.00   31.67  ? 71   LEU B CD1 1 
ATOM   523  C CD2 . LEU A 1 71  ? 4.731   -15.855 -4.969  1.00   28.73  ? 71   LEU B CD2 1 
ATOM   524  N N   . ILE A 1 72  ? 9.655   -16.513 -7.054  1.00   30.20  ? 72   ILE B N   1 
ATOM   525  C CA  . ILE A 1 72  ? 10.962  -16.001 -7.441  1.00   31.89  ? 72   ILE B CA  1 
ATOM   526  C C   . ILE A 1 72  ? 10.990  -15.594 -8.927  1.00   31.72  ? 72   ILE B C   1 
ATOM   527  O O   . ILE A 1 72  ? 11.577  -14.565 -9.283  1.00   31.31  ? 72   ILE B O   1 
ATOM   528  C CB  . ILE A 1 72  ? 12.083  -17.003 -7.086  1.00   32.61  ? 72   ILE B CB  1 
ATOM   529  C CG1 . ILE A 1 72  ? 12.327  -16.992 -5.572  1.00   34.36  ? 72   ILE B CG1 1 
ATOM   530  C CG2 . ILE A 1 72  ? 13.368  -16.673 -7.833  1.00   33.11  ? 72   ILE B CG2 1 
ATOM   531  C CD1 . ILE A 1 72  ? 13.106  -18.196 -5.042  1.00   36.04  ? 72   ILE B CD1 1 
ATOM   532  N N   . MET A 1 73  ? 10.330  -16.380 -9.777  0.89   31.15  ? 73   MET B N   1 
ATOM   533  C CA  . MET A 1 73  ? 10.264  -16.074 -11.212 0.89   31.59  ? 73   MET B CA  1 
ATOM   534  C C   . MET A 1 73  ? 9.374   -14.878 -11.506 0.89   31.14  ? 73   MET B C   1 
ATOM   535  O O   . MET A 1 73  ? 9.706   -14.036 -12.348 0.89   30.10  ? 73   MET B O   1 
ATOM   536  C CB  . MET A 1 73  ? 9.771   -17.279 -12.006 0.89   32.29  ? 73   MET B CB  1 
ATOM   537  C CG  . MET A 1 73  ? 10.707  -18.464 -11.970 0.89   34.36  ? 73   MET B CG  1 
ATOM   538  S SD  . MET A 1 73  ? 10.006  -19.870 -12.845 0.89   42.85  ? 73   MET B SD  1 
ATOM   539  C CE  . MET A 1 73  ? 10.156  -19.284 -14.530 0.89   38.32  ? 73   MET B CE  1 
ATOM   540  N N   . ILE A 1 74  ? 8.227   -14.804 -10.835 1.00   31.74  ? 74   ILE B N   1 
ATOM   541  C CA  . ILE A 1 74  ? 7.409   -13.605 -10.902 1.00   31.90  ? 74   ILE B CA  1 
ATOM   542  C C   . ILE A 1 74  ? 8.288   -12.403 -10.555 1.00   32.63  ? 74   ILE B C   1 
ATOM   543  O O   . ILE A 1 74  ? 8.371   -11.447 -11.321 1.00   32.09  ? 74   ILE B O   1 
ATOM   544  C CB  . ILE A 1 74  ? 6.172   -13.692 -9.965  1.00   31.85  ? 74   ILE B CB  1 
ATOM   545  C CG1 . ILE A 1 74  ? 5.191   -14.752 -10.491 1.00   31.95  ? 74   ILE B CG1 1 
ATOM   546  C CG2 . ILE A 1 74  ? 5.488   -12.334 -9.860  1.00   31.09  ? 74   ILE B CG2 1 
ATOM   547  C CD1 . ILE A 1 74  ? 4.085   -15.165 -9.519  1.00   31.20  ? 74   ILE B CD1 1 
ATOM   548  N N   . ASN A 1 75  ? 8.985   -12.486 -9.423  1.00   33.13  ? 75   ASN B N   1 
ATOM   549  C CA  . ASN A 1 75  ? 9.827   -11.396 -8.950  1.00   34.09  ? 75   ASN B CA  1 
ATOM   550  C C   . ASN A 1 75  ? 10.870  -11.002 -9.987  1.00   33.96  ? 75   ASN B C   1 
ATOM   551  O O   . ASN A 1 75  ? 11.058  -9.820  -10.284 1.00   32.72  ? 75   ASN B O   1 
ATOM   552  C CB  . ASN A 1 75  ? 10.536  -11.782 -7.650  1.00   34.84  ? 75   ASN B CB  1 
ATOM   553  C CG  . ASN A 1 75  ? 11.487  -10.710 -7.182  1.00   37.31  ? 75   ASN B CG  1 
ATOM   554  O OD1 . ASN A 1 75  ? 11.065  -9.596  -6.884  1.00   38.56  ? 75   ASN B OD1 1 
ATOM   555  N ND2 . ASN A 1 75  ? 12.779  -11.018 -7.162  1.00   39.30  ? 75   ASN B ND2 1 
ATOM   556  N N   . ALA A 1 76  ? 11.536  -12.023 -10.525 1.00   34.23  ? 76   ALA B N   1 
ATOM   557  C CA  . ALA A 1 76  ? 12.593  -11.860 -11.515 1.00   33.89  ? 76   ALA B CA  1 
ATOM   558  C C   . ALA A 1 76  ? 12.072  -11.129 -12.755 1.00   33.26  ? 76   ALA B C   1 
ATOM   559  O O   . ALA A 1 76  ? 12.706  -10.203 -13.249 1.00   33.25  ? 76   ALA B O   1 
ATOM   560  C CB  . ALA A 1 76  ? 13.175  -13.221 -11.889 1.00   33.75  ? 76   ALA B CB  1 
ATOM   561  N N   . CYS A 1 77  ? 10.900  -11.512 -13.237 1.00   33.36  ? 77   CYS B N   1 
ATOM   562  C CA  . CYS A 1 77  ? 10.364  -10.892 -14.442 1.00   34.25  ? 77   CYS B CA  1 
ATOM   563  C C   . CYS A 1 77  ? 9.941   -9.444  -14.209 1.00   34.65  ? 77   CYS B C   1 
ATOM   564  O O   . CYS A 1 77  ? 10.172  -8.580  -15.051 1.00   34.47  ? 77   CYS B O   1 
ATOM   565  C CB  . CYS A 1 77  ? 9.216   -11.726 -15.008 1.00   34.49  ? 77   CYS B CB  1 
ATOM   566  S SG  . CYS A 1 77  ? 9.805   -13.329 -15.587 1.00   35.87  ? 77   CYS B SG  1 
ATOM   567  N N   . LYS A 1 78  ? 9.330   -9.172  -13.063 1.00   34.74  ? 78   LYS B N   1 
ATOM   568  C CA  . LYS A 1 78  ? 8.883   -7.824  -12.760 1.00   35.51  ? 78   LYS B CA  1 
ATOM   569  C C   . LYS A 1 78  ? 10.042  -6.827  -12.677 1.00   35.71  ? 78   LYS B C   1 
ATOM   570  O O   . LYS A 1 78  ? 9.946   -5.727  -13.219 1.00   35.62  ? 78   LYS B O   1 
ATOM   571  C CB  . LYS A 1 78  ? 8.044   -7.804  -11.480 1.00   36.22  ? 78   LYS B CB  1 
ATOM   572  C CG  . LYS A 1 78  ? 6.527   -7.822  -11.721 1.00   39.15  ? 78   LYS B CG  1 
ATOM   573  C CD  . LYS A 1 78  ? 5.924   -6.434  -11.498 1.00   43.28  ? 78   LYS B CD  1 
ATOM   574  C CE  . LYS A 1 78  ? 4.461   -6.370  -11.914 1.00   44.38  ? 78   LYS B CE  1 
ATOM   575  N NZ  . LYS A 1 78  ? 4.315   -6.354  -13.398 1.00   47.54  ? 78   LYS B NZ  1 
ATOM   576  N N   . ILE A 1 79  ? 11.135  -7.200  -12.020 1.00   36.03  ? 79   ILE B N   1 
ATOM   577  C CA  . ILE A 1 79  ? 12.242  -6.250  -11.866 1.00   36.97  ? 79   ILE B CA  1 
ATOM   578  C C   . ILE A 1 79  ? 13.101  -6.224  -13.129 1.00   37.25  ? 79   ILE B C   1 
ATOM   579  O O   . ILE A 1 79  ? 13.936  -5.330  -13.301 1.00   37.75  ? 79   ILE B O   1 
ATOM   580  C CB  . ILE A 1 79  ? 13.128  -6.509  -10.604 1.00   37.27  ? 79   ILE B CB  1 
ATOM   581  C CG1 . ILE A 1 79  ? 13.918  -7.816  -10.747 1.00   39.16  ? 79   ILE B CG1 1 
ATOM   582  C CG2 . ILE A 1 79  ? 12.297  -6.443  -9.303  1.00   36.78  ? 79   ILE B CG2 1 
ATOM   583  C CD1 . ILE A 1 79  ? 14.813  -8.151  -9.562  1.00   41.68  ? 79   ILE B CD1 1 
ATOM   584  N N   . ALA A 1 80  ? 12.900  -7.208  -14.007 1.00   36.89  ? 80   ALA B N   1 
ATOM   585  C CA  . ALA A 1 80  ? 13.489  -7.157  -15.348 1.00   36.33  ? 80   ALA B CA  1 
ATOM   586  C C   . ALA A 1 80  ? 12.566  -6.433  -16.336 1.00   36.10  ? 80   ALA B C   1 
ATOM   587  O O   . ALA A 1 80  ? 12.722  -6.565  -17.552 1.00   36.36  ? 80   ALA B O   1 
ATOM   588  C CB  . ALA A 1 80  ? 13.853  -8.563  -15.848 1.00   35.53  ? 80   ALA B CB  1 
ATOM   589  N N   . SER A 1 81  ? 11.605  -5.678  -15.806 1.00   35.16  ? 81   SER B N   1 
ATOM   590  C CA  . SER A 1 81  ? 10.725  -4.799  -16.600 1.00   35.30  ? 81   SER B CA  1 
ATOM   591  C C   . SER A 1 81  ? 9.800   -5.496  -17.608 1.00   35.27  ? 81   SER B C   1 
ATOM   592  O O   . SER A 1 81  ? 9.461   -4.913  -18.642 1.00   34.83  ? 81   SER B O   1 
ATOM   593  C CB  . SER A 1 81  ? 11.521  -3.691  -17.323 1.00   35.53  ? 81   SER B CB  1 
ATOM   594  O OG  . SER A 1 81  ? 12.246  -2.878  -16.416 1.00   36.91  ? 81   SER B OG  1 
ATOM   595  N N   . ALA A 1 82  ? 9.377   -6.722  -17.320 1.00   35.11  ? 82   ALA B N   1 
ATOM   596  C CA  . ALA A 1 82  ? 8.271   -7.295  -18.075 1.00   35.34  ? 82   ALA B CA  1 
ATOM   597  C C   . ALA A 1 82  ? 7.119   -6.283  -18.142 1.00   36.60  ? 82   ALA B C   1 
ATOM   598  O O   . ALA A 1 82  ? 6.888   -5.533  -17.193 1.00   37.47  ? 82   ALA B O   1 
ATOM   599  C CB  . ALA A 1 82  ? 7.795   -8.597  -17.431 1.00   34.33  ? 82   ALA B CB  1 
ATOM   600  N N   . SER A 1 83  ? 6.397   -6.251  -19.258 1.00   38.06  ? 83   SER B N   1 
ATOM   601  C CA  . SER A 1 83  ? 5.227   -5.382  -19.358 1.00   39.42  ? 83   SER B CA  1 
ATOM   602  C C   . SER A 1 83  ? 4.090   -5.837  -18.434 1.00   39.31  ? 83   SER B C   1 
ATOM   603  O O   . SER A 1 83  ? 3.398   -5.007  -17.841 1.00   39.77  ? 83   SER B O   1 
ATOM   604  C CB  . SER A 1 83  ? 4.751   -5.285  -20.812 1.00   39.98  ? 83   SER B CB  1 
ATOM   605  O OG  . SER A 1 83  ? 3.443   -4.769  -20.899 1.00   42.57  ? 83   SER B OG  1 
ATOM   606  N N   . ARG A 1 84  ? 3.898   -7.152  -18.333 1.00   38.27  ? 84   ARG B N   1 
ATOM   607  C CA  . ARG A 1 84  ? 2.888   -7.743  -17.457 1.00   37.21  ? 84   ARG B CA  1 
ATOM   608  C C   . ARG A 1 84  ? 3.322   -9.155  -17.094 1.00   36.14  ? 84   ARG B C   1 
ATOM   609  O O   . ARG A 1 84  ? 3.996   -9.830  -17.879 1.00   35.22  ? 84   ARG B O   1 
ATOM   610  C CB  . ARG A 1 84  ? 1.495   -7.754  -18.121 1.00   37.69  ? 84   ARG B CB  1 
ATOM   611  C CG  . ARG A 1 84  ? 0.362   -8.307  -17.237 1.00   39.98  ? 84   ARG B CG  1 
ATOM   612  C CD  . ARG A 1 84  ? -1.047  -8.144  -17.866 1.00   43.53  ? 84   ARG B CD  1 
ATOM   613  N NE  . ARG A 1 84  ? -1.120  -8.705  -19.219 1.00   46.66  ? 84   ARG B NE  1 
ATOM   614  C CZ  . ARG A 1 84  ? -2.207  -8.730  -19.987 1.00   47.94  ? 84   ARG B CZ  1 
ATOM   615  N NH1 . ARG A 1 84  ? -3.366  -8.228  -19.565 1.00   49.01  ? 84   ARG B NH1 1 
ATOM   616  N NH2 . ARG A 1 84  ? -2.128  -9.265  -21.195 1.00   46.04  ? 84   ARG B NH2 1 
ATOM   617  N N   . VAL A 1 85  ? 2.964   -9.588  -15.889 1.00   34.57  ? 85   VAL B N   1 
ATOM   618  C CA  . VAL A 1 85  ? 3.305   -10.922 -15.427 1.00   33.56  ? 85   VAL B CA  1 
ATOM   619  C C   . VAL A 1 85  ? 2.050   -11.625 -14.939 1.00   32.72  ? 85   VAL B C   1 
ATOM   620  O O   . VAL A 1 85  ? 1.390   -11.159 -14.024 1.00   32.44  ? 85   VAL B O   1 
ATOM   621  C CB  . VAL A 1 85  ? 4.379   -10.904 -14.304 1.00   34.10  ? 85   VAL B CB  1 
ATOM   622  C CG1 . VAL A 1 85  ? 4.695   -12.332 -13.845 1.00   33.81  ? 85   VAL B CG1 1 
ATOM   623  C CG2 . VAL A 1 85  ? 5.657   -10.227 -14.782 1.00   32.66  ? 85   VAL B CG2 1 
ATOM   624  N N   . THR A 1 86  ? 1.727   -12.748 -15.564 1.00   31.06  ? 86   THR B N   1 
ATOM   625  C CA  . THR A 1 86  ? 0.559   -13.527 -15.189 1.00   30.31  ? 86   THR B CA  1 
ATOM   626  C C   . THR A 1 86  ? 1.015   -14.848 -14.602 1.00   29.92  ? 86   THR B C   1 
ATOM   627  O O   . THR A 1 86  ? 1.879   -15.520 -15.176 1.00   29.77  ? 86   THR B O   1 
ATOM   628  C CB  . THR A 1 86  ? -0.365  -13.762 -16.407 1.00   30.55  ? 86   THR B CB  1 
ATOM   629  O OG1 . THR A 1 86  ? -0.900  -12.511 -16.839 1.00   31.50  ? 86   THR B OG1 1 
ATOM   630  C CG2 . THR A 1 86  ? -1.512  -14.682 -16.066 1.00   27.52  ? 86   THR B CG2 1 
ATOM   631  N N   . ALA A 1 87  ? 0.471   -15.201 -13.436 1.00   29.08  ? 87   ALA B N   1 
ATOM   632  C CA  . ALA A 1 87  ? 0.738   -16.511 -12.859 1.00   28.26  ? 87   ALA B CA  1 
ATOM   633  C C   . ALA A 1 87  ? -0.331  -17.488 -13.329 1.00   28.58  ? 87   ALA B C   1 
ATOM   634  O O   . ALA A 1 87  ? -1.522  -17.260 -13.132 1.00   28.45  ? 87   ALA B O   1 
ATOM   635  C CB  . ALA A 1 87  ? 0.773   -16.445 -11.327 1.00   27.94  ? 87   ALA B CB  1 
ATOM   636  N N   . VAL A 1 88  ? 0.103   -18.569 -13.969 1.00   28.73  ? 88   VAL B N   1 
ATOM   637  C CA  . VAL A 1 88  ? -0.817  -19.592 -14.455 1.00   28.37  ? 88   VAL B CA  1 
ATOM   638  C C   . VAL A 1 88  ? -0.716  -20.770 -13.509 1.00   29.33  ? 88   VAL B C   1 
ATOM   639  O O   . VAL A 1 88  ? 0.276   -21.493 -13.493 1.00   28.42  ? 88   VAL B O   1 
ATOM   640  C CB  . VAL A 1 88  ? -0.478  -20.062 -15.892 1.00   28.75  ? 88   VAL B CB  1 
ATOM   641  C CG1 . VAL A 1 88  ? -1.534  -21.043 -16.387 1.00   27.17  ? 88   VAL B CG1 1 
ATOM   642  C CG2 . VAL A 1 88  ? -0.388  -18.868 -16.852 1.00   28.22  ? 88   VAL B CG2 1 
ATOM   643  N N   . ILE A 1 89  ? -1.747  -20.958 -12.710 1.00   29.74  ? 89   ILE B N   1 
ATOM   644  C CA  . ILE A 1 89  ? -1.647  -21.861 -11.583 1.00   31.92  ? 89   ILE B CA  1 
ATOM   645  C C   . ILE A 1 89  ? -2.823  -22.803 -11.667 1.00   33.41  ? 89   ILE B C   1 
ATOM   646  O O   . ILE A 1 89  ? -3.854  -22.556 -11.045 1.00   33.93  ? 89   ILE B O   1 
ATOM   647  C CB  . ILE A 1 89  ? -1.699  -21.104 -10.234 1.00   32.40  ? 89   ILE B CB  1 
ATOM   648  C CG1 . ILE A 1 89  ? -0.609  -20.034 -10.161 1.00   30.72  ? 89   ILE B CG1 1 
ATOM   649  C CG2 . ILE A 1 89  ? -1.550  -22.083 -9.066  1.00   32.70  ? 89   ILE B CG2 1 
ATOM   650  C CD1 . ILE A 1 89  ? -0.660  -19.223 -8.863  1.00   32.82  ? 89   ILE B CD1 1 
ATOM   651  N N   . PRO A 1 90  ? -2.679  -23.880 -12.455 1.00   35.35  ? 90   PRO B N   1 
ATOM   652  C CA  . PRO A 1 90  ? -3.803  -24.761 -12.741 1.00   36.92  ? 90   PRO B CA  1 
ATOM   653  C C   . PRO A 1 90  ? -4.474  -25.229 -11.454 1.00   37.80  ? 90   PRO B C   1 
ATOM   654  O O   . PRO A 1 90  ? -5.693  -25.096 -11.305 1.00   38.23  ? 90   PRO B O   1 
ATOM   655  C CB  . PRO A 1 90  ? -3.147  -25.921 -13.494 1.00   37.29  ? 90   PRO B CB  1 
ATOM   656  C CG  . PRO A 1 90  ? -1.988  -25.303 -14.167 1.00   36.99  ? 90   PRO B CG  1 
ATOM   657  C CD  . PRO A 1 90  ? -1.462  -24.297 -13.173 1.00   35.23  ? 90   PRO B CD  1 
ATOM   658  N N   . CYS A 1 91  ? -3.675  -25.718 -10.513 1.00   38.17  ? 91   CYS B N   1 
ATOM   659  C CA  . CYS A 1 91  ? -4.201  -26.126 -9.210  1.00   39.38  ? 91   CYS B CA  1 
ATOM   660  C C   . CYS A 1 91  ? -3.668  -25.221 -8.103  1.00   38.35  ? 91   CYS B C   1 
ATOM   661  O O   . CYS A 1 91  ? -2.479  -25.242 -7.806  1.00   37.92  ? 91   CYS B O   1 
ATOM   662  C CB  . CYS A 1 91  ? -3.838  -27.584 -8.927  1.00   39.78  ? 91   CYS B CB  1 
ATOM   663  S SG  . CYS A 1 91  ? -4.460  -28.177 -7.342  1.00   45.74  ? 91   CYS B SG  1 
ATOM   664  N N   . PHE A 1 92  ? -4.547  -24.433 -7.491  1.00   38.53  ? 92   PHE B N   1 
ATOM   665  C CA  . PHE A 1 92  ? -4.106  -23.364 -6.595  1.00   38.79  ? 92   PHE B CA  1 
ATOM   666  C C   . PHE A 1 92  ? -3.717  -23.883 -5.200  1.00   40.05  ? 92   PHE B C   1 
ATOM   667  O O   . PHE A 1 92  ? -4.535  -24.473 -4.503  1.00   40.13  ? 92   PHE B O   1 
ATOM   668  C CB  . PHE A 1 92  ? -5.171  -22.265 -6.508  1.00   38.50  ? 92   PHE B CB  1 
ATOM   669  C CG  . PHE A 1 92  ? -4.709  -21.006 -5.805  1.00   36.94  ? 92   PHE B CG  1 
ATOM   670  C CD1 . PHE A 1 92  ? -4.208  -19.925 -6.529  1.00   36.36  ? 92   PHE B CD1 1 
ATOM   671  C CD2 . PHE A 1 92  ? -4.794  -20.902 -4.419  1.00   35.39  ? 92   PHE B CD2 1 
ATOM   672  C CE1 . PHE A 1 92  ? -3.790  -18.768 -5.878  1.00   37.36  ? 92   PHE B CE1 1 
ATOM   673  C CE2 . PHE A 1 92  ? -4.385  -19.742 -3.752  1.00   33.45  ? 92   PHE B CE2 1 
ATOM   674  C CZ  . PHE A 1 92  ? -3.887  -18.673 -4.483  1.00   35.31  ? 92   PHE B CZ  1 
ATOM   675  N N   . PRO A 1 93  ? -2.459  -23.655 -4.797  1.00   41.12  ? 93   PRO B N   1 
ATOM   676  C CA  . PRO A 1 93  ? -1.890  -24.192 -3.547  1.00   42.17  ? 93   PRO B CA  1 
ATOM   677  C C   . PRO A 1 93  ? -2.581  -23.677 -2.284  1.00   42.58  ? 93   PRO B C   1 
ATOM   678  O O   . PRO A 1 93  ? -2.977  -22.509 -2.232  1.00   42.80  ? 93   PRO B O   1 
ATOM   679  C CB  . PRO A 1 93  ? -0.433  -23.709 -3.579  1.00   42.36  ? 93   PRO B CB  1 
ATOM   680  C CG  . PRO A 1 93  ? -0.389  -22.605 -4.569  1.00   42.33  ? 93   PRO B CG  1 
ATOM   681  C CD  . PRO A 1 93  ? -1.479  -22.861 -5.561  1.00   41.59  ? 93   PRO B CD  1 
ATOM   682  N N   . TYR A 1 94  ? -2.733  -24.552 -1.289  1.00   42.95  ? 94   TYR B N   1 
ATOM   683  C CA  . TYR A 1 94  ? -3.331  -24.195 0.002   1.00   43.38  ? 94   TYR B CA  1 
ATOM   684  C C   . TYR A 1 94  ? -4.782  -23.754 -0.138  1.00   44.36  ? 94   TYR B C   1 
ATOM   685  O O   . TYR A 1 94  ? -5.354  -23.159 0.782   1.00   43.38  ? 94   TYR B O   1 
ATOM   686  C CB  . TYR A 1 94  ? -2.487  -23.129 0.728   1.00   43.01  ? 94   TYR B CB  1 
ATOM   687  C CG  . TYR A 1 94  ? -1.147  -23.664 1.186   1.00   43.42  ? 94   TYR B CG  1 
ATOM   688  C CD1 . TYR A 1 94  ? -0.014  -23.521 0.392   1.00   43.56  ? 94   TYR B CD1 1 
ATOM   689  C CD2 . TYR A 1 94  ? -1.021  -24.343 2.403   1.00   42.64  ? 94   TYR B CD2 1 
ATOM   690  C CE1 . TYR A 1 94  ? 1.213   -24.013 0.798   1.00   43.16  ? 94   TYR B CE1 1 
ATOM   691  C CE2 . TYR A 1 94  ? 0.211   -24.852 2.817   1.00   41.99  ? 94   TYR B CE2 1 
ATOM   692  C CZ  . TYR A 1 94  ? 1.320   -24.682 2.005   1.00   43.12  ? 94   TYR B CZ  1 
ATOM   693  O OH  . TYR A 1 94  ? 2.550   -25.174 2.380   1.00   41.67  ? 94   TYR B OH  1 
ATOM   694  N N   . ALA A 1 95  ? -5.377  -24.069 -1.289  1.00   45.75  ? 95   ALA B N   1 
ATOM   695  C CA  . ALA A 1 95  ? -6.775  -23.739 -1.555  1.00   47.35  ? 95   ALA B CA  1 
ATOM   696  C C   . ALA A 1 95  ? -7.728  -24.322 -0.515  1.00   48.51  ? 95   ALA B C   1 
ATOM   697  O O   . ALA A 1 95  ? -8.752  -23.711 -0.211  1.00   49.27  ? 95   ALA B O   1 
ATOM   698  C CB  . ALA A 1 95  ? -7.181  -24.184 -2.948  1.00   46.63  ? 95   ALA B CB  1 
ATOM   699  N N   . ARG A 1 96  ? -7.402  -25.491 0.031   1.00   49.55  ? 96   ARG B N   1 
ATOM   700  C CA  . ARG A 1 96  ? -8.218  -26.063 1.101   1.00   50.12  ? 96   ARG B CA  1 
ATOM   701  C C   . ARG A 1 96  ? -8.023  -25.353 2.443   1.00   48.50  ? 96   ARG B C   1 
ATOM   702  O O   . ARG A 1 96  ? -8.693  -25.685 3.423   1.00   49.19  ? 96   ARG B O   1 
ATOM   703  C CB  . ARG A 1 96  ? -7.978  -27.563 1.244   1.00   51.16  ? 96   ARG B CB  1 
ATOM   704  C CG  . ARG A 1 96  ? -8.581  -28.394 0.115   1.00   54.94  ? 96   ARG B CG  1 
ATOM   705  C CD  . ARG A 1 96  ? -7.987  -29.787 0.105   1.00   60.63  ? 96   ARG B CD  1 
ATOM   706  N NE  . ARG A 1 96  ? -6.525  -29.731 0.074   1.00   64.64  ? 96   ARG B NE  1 
ATOM   707  C CZ  . ARG A 1 96  ? -5.724  -30.718 0.460   1.00   66.90  ? 96   ARG B CZ  1 
ATOM   708  N NH1 . ARG A 1 96  ? -6.229  -31.863 0.914   1.00   67.57  ? 96   ARG B NH1 1 
ATOM   709  N NH2 . ARG A 1 96  ? -4.411  -30.555 0.398   1.00   68.07  ? 96   ARG B NH2 1 
ATOM   710  N N   . GLN A 1 97  ? -7.117  -24.374 2.477   0.55   45.27  ? 97   GLN B N   1 
ATOM   711  C CA  . GLN A 1 97  ? -6.901  -23.547 3.666   0.55   41.47  ? 97   GLN B CA  1 
ATOM   712  C C   . GLN A 1 97  ? -7.339  -22.105 3.383   0.55   37.73  ? 97   GLN B C   1 
ATOM   713  O O   . GLN A 1 97  ? -6.522  -21.196 3.279   0.55   37.81  ? 97   GLN B O   1 
ATOM   714  C CB  . GLN A 1 97  ? -5.439  -23.624 4.134   0.55   42.16  ? 97   GLN B CB  1 
ATOM   715  C CG  . GLN A 1 97  ? -4.902  -25.056 4.276   0.55   43.97  ? 97   GLN B CG  1 
ATOM   716  C CD  . GLN A 1 97  ? -3.589  -25.151 5.043   0.55   46.06  ? 97   GLN B CD  1 
ATOM   717  O OE1 . GLN A 1 97  ? -3.133  -24.186 5.660   0.55   47.44  ? 97   GLN B OE1 1 
ATOM   718  N NE2 . GLN A 1 97  ? -2.978  -26.330 5.010   0.55   46.22  ? 97   GLN B NE2 1 
ATOM   719  N N   . ASP A 1 98  ? -8.650  -21.913 3.271   0.15   32.60  ? 98   ASP B N   1 
ATOM   720  C CA  . ASP A 1 98  ? -9.216  -20.644 2.841   0.15   28.70  ? 98   ASP B CA  1 
ATOM   721  C C   . ASP A 1 98  ? -10.244 -20.101 3.834   0.15   29.42  ? 98   ASP B C   1 
ATOM   722  O O   . ASP A 1 98  ? -10.938 -19.124 3.549   0.15   27.26  ? 98   ASP B O   1 
ATOM   723  C CB  . ASP A 1 98  ? -9.856  -20.804 1.460   0.15   26.82  ? 98   ASP B CB  1 
ATOM   724  C CG  . ASP A 1 98  ? -11.078 -21.691 1.492   0.15   23.29  ? 98   ASP B CG  1 
ATOM   725  O OD1 . ASP A 1 98  ? -11.201 -22.492 2.438   0.15   19.42  ? 98   ASP B OD1 1 
ATOM   726  O OD2 . ASP A 1 98  ? -11.916 -21.587 0.576   0.15   19.45  ? 98   ASP B OD2 1 
ATOM   727  N N   . LYS A 1 99  ? -10.342 -20.748 4.993   0.22   32.79  ? 99   LYS B N   1 
ATOM   728  C CA  . LYS A 1 99  ? -11.135 -20.234 6.110   0.22   38.36  ? 99   LYS B CA  1 
ATOM   729  C C   . LYS A 1 99  ? -10.598 -20.751 7.450   0.22   44.29  ? 99   LYS B C   1 
ATOM   730  O O   . LYS A 1 99  ? -9.705  -21.601 7.476   0.22   42.89  ? 99   LYS B O   1 
ATOM   731  C CB  . LYS A 1 99  ? -12.621 -20.559 5.936   0.22   37.09  ? 99   LYS B CB  1 
ATOM   732  C CG  . LYS A 1 99  ? -12.935 -22.032 5.719   0.22   36.52  ? 99   LYS B CG  1 
ATOM   733  C CD  . LYS A 1 99  ? -14.369 -22.199 5.247   0.22   36.06  ? 99   LYS B CD  1 
ATOM   734  C CE  . LYS A 1 99  ? -14.659 -23.621 4.805   0.22   35.78  ? 99   LYS B CE  1 
ATOM   735  N NZ  . LYS A 1 99  ? -16.026 -23.731 4.226   0.22   35.99  ? 99   LYS B NZ  1 
ATOM   736  N N   . LYS A 1 100 ? -11.134 -20.226 8.550   1.00   66.09  ? 100  LYS B N   1 
ATOM   737  C CA  . LYS A 1 100 ? -10.649 -20.564 9.892   1.00   73.48  ? 100  LYS B CA  1 
ATOM   738  C C   . LYS A 1 100 ? -11.288 -21.820 10.487  1.00   75.06  ? 100  LYS B C   1 
ATOM   739  O O   . LYS A 1 100 ? -10.683 -22.469 11.344  1.00   76.35  ? 100  LYS B O   1 
ATOM   740  C CB  . LYS A 1 100 ? -10.846 -19.390 10.860  1.00   72.62  ? 100  LYS B CB  1 
ATOM   741  C CG  . LYS A 1 100 ? -9.919  -18.201 10.655  1.00   67.28  ? 100  LYS B CG  1 
ATOM   742  C CD  . LYS A 1 100 ? -9.974  -17.288 11.874  1.00   68.12  ? 100  LYS B CD  1 
ATOM   743  C CE  . LYS A 1 100 ? -9.365  -15.913 11.575  1.00   69.17  ? 100  LYS B CE  1 
ATOM   744  N NZ  . LYS A 1 100 ? -9.647  -14.940 12.692  1.00   69.72  ? 100  LYS B NZ  1 
ATOM   745  N N   . ASP A 1 101 ? -12.504 -22.149 10.044  0.36   72.31  ? 101  ASP B N   1 
ATOM   746  C CA  . ASP A 1 101 ? -13.228 -23.344 10.506  0.36   76.20  ? 101  ASP B CA  1 
ATOM   747  C C   . ASP A 1 101 ? -13.316 -23.444 12.026  0.36   78.90  ? 101  ASP B C   1 
ATOM   748  O O   . ASP A 1 101 ? -13.047 -24.509 12.587  0.36   79.15  ? 101  ASP B O   1 
ATOM   749  C CB  . ASP A 1 101 ? -12.575 -24.621 9.965   0.36   75.96  ? 101  ASP B CB  1 
ATOM   750  C CG  . ASP A 1 101 ? -12.484 -24.635 8.457   0.36   76.37  ? 101  ASP B CG  1 
ATOM   751  O OD1 . ASP A 1 101 ? -13.492 -24.303 7.796   0.36   76.57  ? 101  ASP B OD1 1 
ATOM   752  O OD2 . ASP A 1 101 ? -11.406 -24.986 7.933   0.36   76.58  ? 101  ASP B OD2 1 
ATOM   753  N N   . LYS A 1 102 ? -13.686 -22.343 12.680  1.00   94.02  ? 102  LYS B N   1 
ATOM   754  C CA  . LYS A 1 102 ? -13.751 -22.271 14.146  1.00   99.97  ? 102  LYS B CA  1 
ATOM   755  C C   . LYS A 1 102 ? -12.428 -22.642 14.823  1.00   100.52 ? 102  LYS B C   1 
ATOM   756  O O   . LYS A 1 102 ? -12.422 -23.302 15.866  1.00   101.58 ? 102  LYS B O   1 
ATOM   757  C CB  . LYS A 1 102 ? -14.869 -23.165 14.703  1.00   96.73  ? 102  LYS B CB  1 
ATOM   758  C CG  . LYS A 1 102 ? -16.282 -22.764 14.317  1.00   102.64 ? 102  LYS B CG  1 
ATOM   759  C CD  . LYS A 1 102 ? -17.299 -23.249 15.350  1.00   111.20 ? 102  LYS B CD  1 
ATOM   760  C CE  . LYS A 1 102 ? -17.391 -24.773 15.407  1.00   127.03 ? 102  LYS B CE  1 
ATOM   761  N NZ  . LYS A 1 102 ? -18.277 -25.232 16.511  1.00   126.87 ? 102  LYS B NZ  1 
ATOM   762  N N   . SER A 1 103 ? -11.312 -22.225 14.231  0.59   79.24  ? 103  SER B N   1 
ATOM   763  C CA  . SER A 1 103 ? -9.999  -22.532 14.791  0.59   75.34  ? 103  SER B CA  1 
ATOM   764  C C   . SER A 1 103 ? -9.017  -21.369 14.681  0.59   73.11  ? 103  SER B C   1 
ATOM   765  O O   . SER A 1 103 ? -9.264  -20.396 13.966  0.59   72.73  ? 103  SER B O   1 
ATOM   766  C CB  . SER A 1 103 ? -9.416  -23.789 14.134  0.59   75.19  ? 103  SER B CB  1 
ATOM   767  O OG  . SER A 1 103 ? -8.239  -24.211 14.804  0.59   74.97  ? 103  SER B OG  1 
ATOM   768  N N   . ARG A 1 104 ? -7.900  -21.488 15.396  1.00   70.89  ? 104  ARG B N   1 
ATOM   769  C CA  . ARG A 1 104 ? -6.850  -20.475 15.405  1.00   68.60  ? 104  ARG B CA  1 
ATOM   770  C C   . ARG A 1 104 ? -5.894  -20.712 14.237  1.00   66.24  ? 104  ARG B C   1 
ATOM   771  O O   . ARG A 1 104 ? -4.670  -20.698 14.400  1.00   66.35  ? 104  ARG B O   1 
ATOM   772  C CB  . ARG A 1 104 ? -6.106  -20.532 16.738  1.00   69.05  ? 104  ARG B CB  1 
ATOM   773  C CG  . ARG A 1 104 ? -5.723  -19.178 17.321  1.00   69.62  ? 104  ARG B CG  1 
ATOM   774  C CD  . ARG A 1 104 ? -6.196  -19.068 18.771  1.00   70.05  ? 104  ARG B CD  1 
ATOM   775  N NE  . ARG A 1 104 ? -6.303  -20.386 19.394  1.00   71.06  ? 104  ARG B NE  1 
ATOM   776  C CZ  . ARG A 1 104 ? -7.004  -20.663 20.489  1.00   71.21  ? 104  ARG B CZ  1 
ATOM   777  N NH1 . ARG A 1 104 ? -7.678  -19.715 21.124  1.00   70.77  ? 104  ARG B NH1 1 
ATOM   778  N NH2 . ARG A 1 104 ? -7.023  -21.905 20.952  1.00   71.84  ? 104  ARG B NH2 1 
ATOM   779  N N   . ALA A 1 105 ? -6.471  -20.910 13.055  1.00   62.43  ? 105  ALA B N   1 
ATOM   780  C CA  . ALA A 1 105 ? -5.729  -21.340 11.877  1.00   58.30  ? 105  ALA B CA  1 
ATOM   781  C C   . ALA A 1 105 ? -5.407  -20.189 10.920  1.00   54.89  ? 105  ALA B C   1 
ATOM   782  O O   . ALA A 1 105 ? -6.115  -19.170 10.896  1.00   53.79  ? 105  ALA B O   1 
ATOM   783  C CB  . ALA A 1 105 ? -6.514  -22.430 11.141  1.00   58.77  ? 105  ALA B CB  1 
ATOM   784  N N   . PRO A 1 106 ? -4.346  -20.357 10.114  0.65   51.45  ? 106  PRO B N   1 
ATOM   785  C CA  . PRO A 1 106 ? -4.123  -19.387 9.060   0.65   49.09  ? 106  PRO B CA  1 
ATOM   786  C C   . PRO A 1 106 ? -5.184  -19.571 7.976   0.65   46.86  ? 106  PRO B C   1 
ATOM   787  O O   . PRO A 1 106 ? -5.724  -20.661 7.813   0.65   45.73  ? 106  PRO B O   1 
ATOM   788  C CB  . PRO A 1 106 ? -2.758  -19.797 8.515   0.65   48.99  ? 106  PRO B CB  1 
ATOM   789  C CG  . PRO A 1 106 ? -2.747  -21.282 8.686   0.65   49.90  ? 106  PRO B CG  1 
ATOM   790  C CD  . PRO A 1 106 ? -3.430  -21.512 10.003  0.65   51.38  ? 106  PRO B CD  1 
ATOM   791  N N   . ILE A 1 107 ? -5.511  -18.501 7.271   1.00   45.67  ? 107  ILE B N   1 
ATOM   792  C CA  . ILE A 1 107 ? -6.195  -18.644 5.996   1.00   44.14  ? 107  ILE B CA  1 
ATOM   793  C C   . ILE A 1 107 ? -5.060  -18.608 4.983   1.00   42.59  ? 107  ILE B C   1 
ATOM   794  O O   . ILE A 1 107 ? -4.713  -17.548 4.452   1.00   41.49  ? 107  ILE B O   1 
ATOM   795  C CB  . ILE A 1 107 ? -7.205  -17.518 5.761   1.00   44.82  ? 107  ILE B CB  1 
ATOM   796  C CG1 . ILE A 1 107 ? -8.171  -17.440 6.954   1.00   45.56  ? 107  ILE B CG1 1 
ATOM   797  C CG2 . ILE A 1 107 ? -7.927  -17.718 4.419   1.00   43.71  ? 107  ILE B CG2 1 
ATOM   798  C CD1 . ILE A 1 107 ? -9.255  -16.372 6.833   1.00   47.30  ? 107  ILE B CD1 1 
ATOM   799  N N   . SER A 1 108 ? -4.460  -19.778 4.768   1.00   41.09  ? 108  SER B N   1 
ATOM   800  C CA  . SER A 1 108 ? -3.216  -19.900 4.024   1.00   40.20  ? 108  SER B CA  1 
ATOM   801  C C   . SER A 1 108 ? -3.374  -19.514 2.563   1.00   39.02  ? 108  SER B C   1 
ATOM   802  O O   . SER A 1 108 ? -2.431  -19.021 1.948   1.00   39.41  ? 108  SER B O   1 
ATOM   803  C CB  . SER A 1 108 ? -2.675  -21.325 4.125   1.00   40.39  ? 108  SER B CB  1 
ATOM   804  O OG  . SER A 1 108 ? -2.239  -21.605 5.441   1.00   42.03  ? 108  SER B OG  1 
ATOM   805  N N   . ALA A 1 109 ? -4.562  -19.742 2.012   1.00   37.18  ? 109  ALA B N   1 
ATOM   806  C CA  . ALA A 1 109 ? -4.842  -19.362 0.633   1.00   36.10  ? 109  ALA B CA  1 
ATOM   807  C C   . ALA A 1 109 ? -4.813  -17.846 0.491   1.00   35.24  ? 109  ALA B C   1 
ATOM   808  O O   . ALA A 1 109 ? -4.372  -17.331 -0.534  1.00   34.63  ? 109  ALA B O   1 
ATOM   809  C CB  . ALA A 1 109 ? -6.164  -19.919 0.176   1.00   35.86  ? 109  ALA B CB  1 
ATOM   810  N N   . LYS A 1 110 ? -5.268  -17.132 1.519   1.00   34.50  ? 110  LYS B N   1 
ATOM   811  C CA  . LYS A 1 110 ? -5.141  -15.681 1.520   1.00   33.96  ? 110  LYS B CA  1 
ATOM   812  C C   . LYS A 1 110 ? -3.677  -15.280 1.650   1.00   33.46  ? 110  LYS B C   1 
ATOM   813  O O   . LYS A 1 110 ? -3.227  -14.352 0.979   1.00   32.65  ? 110  LYS B O   1 
ATOM   814  C CB  . LYS A 1 110 ? -5.997  -15.032 2.619   1.00   34.63  ? 110  LYS B CB  1 
ATOM   815  C CG  . LYS A 1 110 ? -5.847  -13.514 2.725   1.00   34.73  ? 110  LYS B CG  1 
ATOM   816  C CD  . LYS A 1 110 ? -6.177  -12.814 1.398   1.00   36.83  ? 110  LYS B CD  1 
ATOM   817  C CE  . LYS A 1 110 ? -5.867  -11.315 1.445   1.00   37.44  ? 110  LYS B CE  1 
ATOM   818  N NZ  . LYS A 1 110 ? -6.661  -10.643 2.509   1.00   39.51  ? 110  LYS B NZ  1 
ATOM   819  N N   . LEU A 1 111 ? -2.926  -15.985 2.495   1.00   32.74  ? 111  LEU B N   1 
ATOM   820  C CA  . LEU A 1 111 ? -1.495  -15.727 2.584   1.00   32.67  ? 111  LEU B CA  1 
ATOM   821  C C   . LEU A 1 111 ? -0.836  -15.934 1.203   1.00   31.73  ? 111  LEU B C   1 
ATOM   822  O O   . LEU A 1 111 ? -0.072  -15.092 0.738   1.00   30.54  ? 111  LEU B O   1 
ATOM   823  C CB  . LEU A 1 111 ? -0.847  -16.609 3.658   1.00   33.33  ? 111  LEU B CB  1 
ATOM   824  C CG  . LEU A 1 111 ? 0.684   -16.600 3.769   1.00   35.40  ? 111  LEU B CG  1 
ATOM   825  C CD1 . LEU A 1 111 ? 1.221   -15.183 4.033   1.00   36.34  ? 111  LEU B CD1 1 
ATOM   826  C CD2 . LEU A 1 111 ? 1.166   -17.580 4.842   1.00   36.68  ? 111  LEU B CD2 1 
ATOM   827  N N   . VAL A 1 112 ? -1.156  -17.044 0.546   1.00   30.96  ? 112  VAL B N   1 
ATOM   828  C CA  . VAL A 1 112 ? -0.591  -17.341 -0.771  1.00   30.85  ? 112  VAL B CA  1 
ATOM   829  C C   . VAL A 1 112 ? -0.934  -16.227 -1.768  1.00   30.28  ? 112  VAL B C   1 
ATOM   830  O O   . VAL A 1 112 ? -0.067  -15.767 -2.509  1.00   29.75  ? 112  VAL B O   1 
ATOM   831  C CB  . VAL A 1 112 ? -1.033  -18.726 -1.289  1.00   30.74  ? 112  VAL B CB  1 
ATOM   832  C CG1 . VAL A 1 112 ? -0.751  -18.859 -2.777  1.00   30.90  ? 112  VAL B CG1 1 
ATOM   833  C CG2 . VAL A 1 112 ? -0.331  -19.829 -0.514  1.00   30.33  ? 112  VAL B CG2 1 
ATOM   834  N N   . ALA A 1 113 ? -2.180  -15.760 -1.746  1.00   30.22  ? 113  ALA B N   1 
ATOM   835  C CA  . ALA A 1 113 ? -2.586  -14.653 -2.609  1.00   30.40  ? 113  ALA B CA  1 
ATOM   836  C C   . ALA A 1 113 ? -1.749  -13.406 -2.341  1.00   30.73  ? 113  ALA B C   1 
ATOM   837  O O   . ALA A 1 113 ? -1.319  -12.722 -3.279  1.00   31.11  ? 113  ALA B O   1 
ATOM   838  C CB  . ALA A 1 113 ? -4.078  -14.356 -2.449  1.00   30.03  ? 113  ALA B CB  1 
ATOM   839  N N   . ASN A 1 114 ? -1.507  -13.111 -1.061  1.00   29.84  ? 114  ASN B N   1 
ATOM   840  C CA  . ASN A 1 114 ? -0.708  -11.945 -0.700  1.00   29.48  ? 114  ASN B CA  1 
ATOM   841  C C   . ASN A 1 114 ? 0.711   -12.095 -1.180  1.00   28.04  ? 114  ASN B C   1 
ATOM   842  O O   . ASN A 1 114 ? 1.307   -11.146 -1.672  1.00   29.60  ? 114  ASN B O   1 
ATOM   843  C CB  . ASN A 1 114 ? -0.736  -11.701 0.816   1.00   29.88  ? 114  ASN B CB  1 
ATOM   844  C CG  . ASN A 1 114 ? -2.024  -11.065 1.279   1.00   31.88  ? 114  ASN B CG  1 
ATOM   845  O OD1 . ASN A 1 114 ? -2.761  -10.476 0.492   1.00   35.59  ? 114  ASN B OD1 1 
ATOM   846  N ND2 . ASN A 1 114 ? -2.290  -11.154 2.572   1.00   34.00  ? 114  ASN B ND2 1 
ATOM   847  N N   . MET A 1 115 ? 1.249   -13.302 -1.057  0.86   26.23  ? 115  MET B N   1 
ATOM   848  C CA  . MET A 1 115 ? 2.596   -13.580 -1.527  0.86   26.56  ? 115  MET B CA  1 
ATOM   849  C C   . MET A 1 115 ? 2.688   -13.375 -3.045  0.86   26.83  ? 115  MET B C   1 
ATOM   850  O O   . MET A 1 115 ? 3.570   -12.670 -3.522  0.86   25.44  ? 115  MET B O   1 
ATOM   851  C CB  . MET A 1 115 ? 3.020   -14.996 -1.111  0.86   25.50  ? 115  MET B CB  1 
ATOM   852  C CG  . MET A 1 115 ? 3.243   -15.158 0.408   0.86   28.21  ? 115  MET B CG  1 
ATOM   853  S SD  . MET A 1 115 ? 3.616   -16.873 0.794   0.86   37.40  ? 115  MET B SD  1 
ATOM   854  C CE  . MET A 1 115 ? 2.031   -17.563 1.105   0.86   36.65  ? 115  MET B CE  1 
ATOM   855  N N   . LEU A 1 116 ? 1.757   -13.962 -3.793  1.00   28.54  ? 116  LEU B N   1 
ATOM   856  C CA  . LEU A 1 116 ? 1.721   -13.785 -5.253  1.00   29.39  ? 116  LEU B CA  1 
ATOM   857  C C   . LEU A 1 116 ? 1.601   -12.304 -5.604  1.00   30.57  ? 116  LEU B C   1 
ATOM   858  O O   . LEU A 1 116 ? 2.275   -11.819 -6.513  1.00   30.31  ? 116  LEU B O   1 
ATOM   859  C CB  . LEU A 1 116 ? 0.575   -14.595 -5.878  1.00   29.03  ? 116  LEU B CB  1 
ATOM   860  C CG  . LEU A 1 116 ? 0.686   -16.128 -5.873  1.00   30.23  ? 116  LEU B CG  1 
ATOM   861  C CD1 . LEU A 1 116 ? -0.688  -16.784 -6.009  1.00   29.22  ? 116  LEU B CD1 1 
ATOM   862  C CD2 . LEU A 1 116 ? 1.622   -16.607 -6.974  1.00   29.97  ? 116  LEU B CD2 1 
ATOM   863  N N   . SER A 1 117 ? 0.768   -11.578 -4.862  1.00   31.96  ? 117  SER B N   1 
ATOM   864  C CA  . SER A 1 117 ? 0.611   -10.150 -5.082  1.00   33.32  ? 117  SER B CA  1 
ATOM   865  C C   . SER A 1 117 ? 1.897   -9.340  -4.834  1.00   33.70  ? 117  SER B C   1 
ATOM   866  O O   . SER A 1 117 ? 2.334   -8.586  -5.713  1.00   33.98  ? 117  SER B O   1 
ATOM   867  C CB  . SER A 1 117 ? -0.568  -9.601  -4.272  1.00   34.15  ? 117  SER B CB  1 
ATOM   868  O OG  . SER A 1 117 ? -1.789  -10.234 -4.655  1.00   37.15  ? 117  SER B OG  1 
ATOM   869  N N   . VAL A 1 118 ? 2.517   -9.497  -3.663  1.00   33.78  ? 118  VAL B N   1 
ATOM   870  C CA  . VAL A 1 118 ? 3.739   -8.737  -3.375  1.00   33.94  ? 118  VAL B CA  1 
ATOM   871  C C   . VAL A 1 118 ? 4.900   -9.145  -4.274  1.00   33.60  ? 118  VAL B C   1 
ATOM   872  O O   . VAL A 1 118 ? 5.738   -8.315  -4.599  1.00   34.22  ? 118  VAL B O   1 
ATOM   873  C CB  . VAL A 1 118 ? 4.182   -8.760  -1.876  1.00   34.17  ? 118  VAL B CB  1 
ATOM   874  C CG1 . VAL A 1 118 ? 3.146   -8.095  -1.010  1.00   35.88  ? 118  VAL B CG1 1 
ATOM   875  C CG2 . VAL A 1 118 ? 4.517   -10.195 -1.375  1.00   34.23  ? 118  VAL B CG2 1 
ATOM   876  N N   . ALA A 1 119 ? 4.945   -10.410 -4.689  1.00   32.31  ? 119  ALA B N   1 
ATOM   877  C CA  . ALA A 1 119 ? 5.974   -10.833 -5.640  1.00   32.10  ? 119  ALA B CA  1 
ATOM   878  C C   . ALA A 1 119 ? 5.798   -10.043 -6.936  1.00   32.17  ? 119  ALA B C   1 
ATOM   879  O O   . ALA A 1 119 ? 6.750   -9.852  -7.676  1.00   31.30  ? 119  ALA B O   1 
ATOM   880  C CB  . ALA A 1 119 ? 5.915   -12.340 -5.904  1.00   31.41  ? 119  ALA B CB  1 
ATOM   881  N N   . GLY A 1 120 ? 4.584   -9.558  -7.194  1.00   32.36  ? 120  GLY B N   1 
ATOM   882  C CA  . GLY A 1 120 ? 4.344   -8.760  -8.389  1.00   32.47  ? 120  GLY B CA  1 
ATOM   883  C C   . GLY A 1 120 ? 3.479   -9.359  -9.499  1.00   32.38  ? 120  GLY B C   1 
ATOM   884  O O   . GLY A 1 120 ? 3.543   -8.903  -10.630 1.00   32.10  ? 120  GLY B O   1 
ATOM   885  N N   . ALA A 1 121 ? 2.654   -10.361 -9.204  1.00   31.45  ? 121  ALA B N   1 
ATOM   886  C CA  . ALA A 1 121 ? 1.713   -10.863 -10.222 1.00   30.82  ? 121  ALA B CA  1 
ATOM   887  C C   . ALA A 1 121 ? 0.702   -9.774  -10.580 1.00   30.63  ? 121  ALA B C   1 
ATOM   888  O O   . ALA A 1 121 ? 0.182   -9.118  -9.692  1.00   29.49  ? 121  ALA B O   1 
ATOM   889  C CB  . ALA A 1 121 ? 0.999   -12.080 -9.721  1.00   31.07  ? 121  ALA B CB  1 
ATOM   890  N N   . ASP A 1 122 ? 0.425   -9.580  -11.871 1.00   29.76  ? 122  ASP B N   1 
ATOM   891  C CA  . ASP A 1 122 ? -0.597  -8.621  -12.297 1.00   29.18  ? 122  ASP B CA  1 
ATOM   892  C C   . ASP A 1 122 ? -1.914  -9.316  -12.586 1.00   29.05  ? 122  ASP B C   1 
ATOM   893  O O   . ASP A 1 122 ? -2.966  -8.677  -12.671 1.00   28.63  ? 122  ASP B O   1 
ATOM   894  C CB  . ASP A 1 122 ? -0.142  -7.854  -13.546 1.00   29.94  ? 122  ASP B CB  1 
ATOM   895  C CG  . ASP A 1 122 ? 1.170   -7.122  -13.337 1.00   32.80  ? 122  ASP B CG  1 
ATOM   896  O OD1 . ASP A 1 122 ? 1.253   -6.272  -12.412 1.00   34.18  ? 122  ASP B OD1 1 
ATOM   897  O OD2 . ASP A 1 122 ? 2.128   -7.404  -14.096 1.00   33.46  ? 122  ASP B OD2 1 
ATOM   898  N N   . HIS A 1 123 ? -1.856  -10.632 -12.726 1.00   28.97  ? 123  HIS B N   1 
ATOM   899  C CA  . HIS A 1 123 ? -2.993  -11.396 -13.235 1.00   30.03  ? 123  HIS B CA  1 
ATOM   900  C C   . HIS A 1 123 ? -2.804  -12.845 -12.830 1.00   29.22  ? 123  HIS B C   1 
ATOM   901  O O   . HIS A 1 123 ? -1.686  -13.336 -12.812 1.00   29.13  ? 123  HIS B O   1 
ATOM   902  C CB  . HIS A 1 123 ? -3.043  -11.262 -14.774 1.00   30.76  ? 123  HIS B CB  1 
ATOM   903  C CG  . HIS A 1 123 ? -4.208  -11.944 -15.427 1.00   35.10  ? 123  HIS B CG  1 
ATOM   904  N ND1 . HIS A 1 123 ? -5.498  -11.837 -14.956 1.00   39.32  ? 123  HIS B ND1 1 
ATOM   905  C CD2 . HIS A 1 123 ? -4.280  -12.717 -16.537 1.00   39.09  ? 123  HIS B CD2 1 
ATOM   906  C CE1 . HIS A 1 123 ? -6.313  -12.522 -15.736 1.00   38.52  ? 123  HIS B CE1 1 
ATOM   907  N NE2 . HIS A 1 123 ? -5.600  -13.063 -16.708 1.00   41.44  ? 123  HIS B NE2 1 
ATOM   908  N N   . ILE A 1 124 ? -3.898  -13.524 -12.507 1.00   28.33  ? 124  ILE B N   1 
ATOM   909  C CA  . ILE A 1 124 ? -3.851  -14.942 -12.190 1.00   28.28  ? 124  ILE B CA  1 
ATOM   910  C C   . ILE A 1 124 ? -4.754  -15.717 -13.139 1.00   28.62  ? 124  ILE B C   1 
ATOM   911  O O   . ILE A 1 124 ? -5.875  -15.313 -13.412 1.00   28.78  ? 124  ILE B O   1 
ATOM   912  C CB  . ILE A 1 124 ? -4.343  -15.259 -10.735 1.00   28.67  ? 124  ILE B CB  1 
ATOM   913  C CG1 . ILE A 1 124 ? -3.637  -14.395 -9.673  1.00   28.09  ? 124  ILE B CG1 1 
ATOM   914  C CG2 . ILE A 1 124 ? -4.192  -16.773 -10.439 1.00   28.06  ? 124  ILE B CG2 1 
ATOM   915  C CD1 . ILE A 1 124 ? -2.119  -14.564 -9.604  1.00   29.25  ? 124  ILE B CD1 1 
ATOM   916  N N   . ILE A 1 125 ? -4.279  -16.860 -13.612 1.00   28.04  ? 125  ILE B N   1 
ATOM   917  C CA  . ILE A 1 125 ? -5.151  -17.747 -14.360 1.00   28.86  ? 125  ILE B CA  1 
ATOM   918  C C   . ILE A 1 125 ? -5.118  -19.064 -13.619 1.00   29.30  ? 125  ILE B C   1 
ATOM   919  O O   . ILE A 1 125 ? -4.050  -19.611 -13.372 1.00   29.19  ? 125  ILE B O   1 
ATOM   920  C CB  . ILE A 1 125 ? -4.691  -17.902 -15.836 1.00   29.60  ? 125  ILE B CB  1 
ATOM   921  C CG1 . ILE A 1 125 ? -4.893  -16.591 -16.597 1.00   30.63  ? 125  ILE B CG1 1 
ATOM   922  C CG2 . ILE A 1 125 ? -5.470  -19.024 -16.554 1.00   29.26  ? 125  ILE B CG2 1 
ATOM   923  C CD1 . ILE A 1 125 ? -4.212  -16.581 -17.962 1.00   32.03  ? 125  ILE B CD1 1 
ATOM   924  N N   . THR A 1 126 ? -6.282  -19.553 -13.218 1.00   30.20  ? 126  THR B N   1 
ATOM   925  C CA  . THR A 1 126 ? -6.343  -20.796 -12.462 1.00   31.88  ? 126  THR B CA  1 
ATOM   926  C C   . THR A 1 126 ? -7.508  -21.653 -12.953 1.00   33.70  ? 126  THR B C   1 
ATOM   927  O O   . THR A 1 126 ? -8.312  -21.199 -13.780 1.00   33.90  ? 126  THR B O   1 
ATOM   928  C CB  . THR A 1 126 ? -6.441  -20.522 -10.922 1.00   32.15  ? 126  THR B CB  1 
ATOM   929  O OG1 . THR A 1 126 ? -6.244  -21.747 -10.203 1.00   35.73  ? 126  THR B OG1 1 
ATOM   930  C CG2 . THR A 1 126 ? -7.781  -19.937 -10.552 1.00   31.52  ? 126  THR B CG2 1 
ATOM   931  N N   . MET A 1 127 ? -7.595  -22.885 -12.460 1.00   35.21  ? 127  MET B N   1 
ATOM   932  C CA  . MET A 1 127 ? -8.706  -23.772 -12.814 1.00   37.62  ? 127  MET B CA  1 
ATOM   933  C C   . MET A 1 127 ? -9.401  -24.374 -11.593 1.00   38.49  ? 127  MET B C   1 
ATOM   934  O O   . MET A 1 127 ? -8.752  -24.964 -10.742 1.00   38.12  ? 127  MET B O   1 
ATOM   935  C CB  . MET A 1 127 ? -8.248  -24.887 -13.769 1.00   38.36  ? 127  MET B CB  1 
ATOM   936  C CG  . MET A 1 127 ? -9.380  -25.838 -14.171 1.00   41.04  ? 127  MET B CG  1 
ATOM   937  S SD  . MET A 1 127 ? -9.045  -26.913 -15.580 1.00   48.18  ? 127  MET B SD  1 
ATOM   938  C CE  . MET A 1 127 ? -9.156  -25.765 -16.941 1.00   42.93  ? 127  MET B CE  1 
ATOM   939  N N   . ASP A 1 128 ? -10.724 -24.219 -11.536 1.00   40.10  ? 128  ASP B N   1 
ATOM   940  C CA  . ASP A 1 128 ? -11.564 -24.745 -10.459 1.00   42.35  ? 128  ASP B CA  1 
ATOM   941  C C   . ASP A 1 128 ? -11.019 -24.508 -9.058  1.00   42.71  ? 128  ASP B C   1 
ATOM   942  O O   . ASP A 1 128 ? -10.615 -25.459 -8.381  1.00   43.22  ? 128  ASP B O   1 
ATOM   943  C CB  . ASP A 1 128 ? -11.831 -26.245 -10.653 1.00   43.13  ? 128  ASP B CB  1 
ATOM   944  C CG  . ASP A 1 128 ? -12.725 -26.529 -11.838 1.00   45.25  ? 128  ASP B CG  1 
ATOM   945  O OD1 . ASP A 1 128 ? -13.829 -25.961 -11.909 1.00   46.62  ? 128  ASP B OD1 1 
ATOM   946  O OD2 . ASP A 1 128 ? -12.323 -27.333 -12.696 1.00   49.34  ? 128  ASP B OD2 1 
ATOM   947  N N   . LEU A 1 129 ? -11.018 -23.250 -8.619  1.00   42.56  ? 129  LEU B N   1 
ATOM   948  C CA  . LEU A 1 129 ? -10.644 -22.934 -7.240  1.00   42.66  ? 129  LEU B CA  1 
ATOM   949  C C   . LEU A 1 129 ? -11.539 -23.723 -6.305  1.00   43.73  ? 129  LEU B C   1 
ATOM   950  O O   . LEU A 1 129 ? -12.744 -23.864 -6.565  1.00   43.57  ? 129  LEU B O   1 
ATOM   951  C CB  . LEU A 1 129 ? -10.797 -21.441 -6.959  1.00   41.63  ? 129  LEU B CB  1 
ATOM   952  C CG  . LEU A 1 129 ? -9.707  -20.533 -7.525  1.00   41.12  ? 129  LEU B CG  1 
ATOM   953  C CD1 . LEU A 1 129 ? -10.180 -19.084 -7.521  1.00   41.47  ? 129  LEU B CD1 1 
ATOM   954  C CD2 . LEU A 1 129 ? -8.406  -20.676 -6.743  1.00   38.13  ? 129  LEU B CD2 1 
ATOM   955  N N   . HIS A 1 130 ? -10.954 -24.239 -5.225  1.00   45.34  ? 130  HIS B N   1 
ATOM   956  C CA  . HIS A 1 130 ? -11.691 -25.062 -4.263  1.00   46.95  ? 130  HIS B CA  1 
ATOM   957  C C   . HIS A 1 130 ? -12.906 -24.312 -3.738  1.00   47.38  ? 130  HIS B C   1 
ATOM   958  O O   . HIS A 1 130 ? -13.955 -24.909 -3.472  1.00   47.26  ? 130  HIS B O   1 
ATOM   959  C CB  . HIS A 1 130 ? -10.791 -25.471 -3.096  1.00   47.60  ? 130  HIS B CB  1 
ATOM   960  C CG  . HIS A 1 130 ? -11.525 -26.154 -1.984  1.00   49.62  ? 130  HIS B CG  1 
ATOM   961  N ND1 . HIS A 1 130 ? -12.080 -27.408 -2.124  1.00   51.11  ? 130  HIS B ND1 1 
ATOM   962  C CD2 . HIS A 1 130 ? -11.804 -25.756 -0.719  1.00   50.83  ? 130  HIS B CD2 1 
ATOM   963  C CE1 . HIS A 1 130 ? -12.671 -27.753 -0.993  1.00   51.62  ? 130  HIS B CE1 1 
ATOM   964  N NE2 . HIS A 1 130 ? -12.519 -26.768 -0.125  1.00   51.05  ? 130  HIS B NE2 1 
ATOM   965  N N   . ALA A 1 131 ? -12.741 -23.000 -3.582  1.00   47.76  ? 131  ALA B N   1 
ATOM   966  C CA  . ALA A 1 131 ? -13.839 -22.114 -3.222  1.00   48.45  ? 131  ALA B CA  1 
ATOM   967  C C   . ALA A 1 131 ? -13.699 -20.852 -4.040  1.00   49.01  ? 131  ALA B C   1 
ATOM   968  O O   . ALA A 1 131 ? -12.666 -20.179 -3.980  1.00   49.27  ? 131  ALA B O   1 
ATOM   969  C CB  . ALA A 1 131 ? -13.815 -21.794 -1.733  1.00   47.88  ? 131  ALA B CB  1 
ATOM   970  N N   . SER A 1 132 ? -14.735 -20.541 -4.810  1.00   49.85  ? 132  SER B N   1 
ATOM   971  C CA  . SER A 1 132 ? -14.758 -19.354 -5.665  1.00   50.29  ? 132  SER B CA  1 
ATOM   972  C C   . SER A 1 132 ? -14.381 -18.064 -4.937  1.00   49.39  ? 132  SER B C   1 
ATOM   973  O O   . SER A 1 132 ? -13.849 -17.143 -5.559  1.00   49.46  ? 132  SER B O   1 
ATOM   974  C CB  . SER A 1 132 ? -16.140 -19.188 -6.295  1.00   50.74  ? 132  SER B CB  1 
ATOM   975  O OG  . SER A 1 132 ? -16.501 -20.343 -7.033  1.00   57.72  ? 132  SER B OG  1 
ATOM   976  N N   . GLN A 1 133 ? -14.649 -18.005 -3.631  1.00   47.49  ? 133  GLN B N   1 
ATOM   977  C CA  . GLN A 1 133 ? -14.359 -16.806 -2.846  1.00   46.46  ? 133  GLN B CA  1 
ATOM   978  C C   . GLN A 1 133 ? -12.875 -16.496 -2.890  1.00   45.08  ? 133  GLN B C   1 
ATOM   979  O O   . GLN A 1 133 ? -12.464 -15.368 -2.629  1.00   44.72  ? 133  GLN B O   1 
ATOM   980  C CB  . GLN A 1 133 ? -14.806 -16.958 -1.393  1.00   46.75  ? 133  GLN B CB  1 
ATOM   981  C CG  . GLN A 1 133 ? -16.309 -16.984 -1.188  1.00   48.49  ? 133  GLN B CG  1 
ATOM   982  C CD  . GLN A 1 133 ? -16.929 -18.352 -1.445  1.00   50.77  ? 133  GLN B CD  1 
ATOM   983  O OE1 . GLN A 1 133 ? -16.233 -19.328 -1.727  1.00   51.31  ? 133  GLN B OE1 1 
ATOM   984  N NE2 . GLN A 1 133 ? -18.251 -18.422 -1.349  1.00   52.14  ? 133  GLN B NE2 1 
ATOM   985  N N   . ILE A 1 134 ? -12.067 -17.492 -3.230  1.00   43.22  ? 134  ILE B N   1 
ATOM   986  C CA  . ILE A 1 134 ? -10.637 -17.262 -3.326  1.00   42.35  ? 134  ILE B CA  1 
ATOM   987  C C   . ILE A 1 134 ? -10.290 -16.138 -4.327  1.00   41.69  ? 134  ILE B C   1 
ATOM   988  O O   . ILE A 1 134 ? -9.340  -15.400 -4.101  1.00   41.52  ? 134  ILE B O   1 
ATOM   989  C CB  . ILE A 1 134 ? -9.836  -18.569 -3.560  1.00   42.61  ? 134  ILE B CB  1 
ATOM   990  C CG1 . ILE A 1 134 ? -9.985  -19.488 -2.336  1.00   42.37  ? 134  ILE B CG1 1 
ATOM   991  C CG2 . ILE A 1 134 ? -8.357  -18.259 -3.821  1.00   42.14  ? 134  ILE B CG2 1 
ATOM   992  C CD1 . ILE A 1 134 ? -9.396  -20.873 -2.493  1.00   41.64  ? 134  ILE B CD1 1 
ATOM   993  N N   . GLN A 1 135 ? -11.070 -15.974 -5.396  1.00   40.38  ? 135  GLN B N   1 
ATOM   994  C CA  . GLN A 1 135 ? -10.927 -14.781 -6.237  1.00   39.56  ? 135  GLN B CA  1 
ATOM   995  C C   . GLN A 1 135 ? -10.982 -13.511 -5.394  1.00   38.53  ? 135  GLN B C   1 
ATOM   996  O O   . GLN A 1 135 ? -10.282 -12.548 -5.682  1.00   37.66  ? 135  GLN B O   1 
ATOM   997  C CB  . GLN A 1 135 ? -12.011 -14.714 -7.301  1.00   40.27  ? 135  GLN B CB  1 
ATOM   998  C CG  . GLN A 1 135 ? -11.814 -15.666 -8.465  1.00   43.22  ? 135  GLN B CG  1 
ATOM   999  C CD  . GLN A 1 135 ? -12.634 -15.258 -9.685  1.00   47.24  ? 135  GLN B CD  1 
ATOM   1000 O OE1 . GLN A 1 135 ? -12.917 -14.083 -9.888  1.00   50.80  ? 135  GLN B OE1 1 
ATOM   1001 N NE2 . GLN A 1 135 ? -13.005 -16.226 -10.500 1.00   48.44  ? 135  GLN B NE2 1 
ATOM   1002 N N   . GLY A 1 136 ? -11.825 -13.514 -4.360  1.00   37.21  ? 136  GLY B N   1 
ATOM   1003 C CA  . GLY A 1 136 ? -11.887 -12.406 -3.405  1.00   36.69  ? 136  GLY B CA  1 
ATOM   1004 C C   . GLY A 1 136 ? -10.631 -12.187 -2.563  1.00   35.92  ? 136  GLY B C   1 
ATOM   1005 O O   . GLY A 1 136 ? -10.523 -11.171 -1.885  1.00   36.35  ? 136  GLY B O   1 
ATOM   1006 N N   . PHE A 1 137 ? -9.678  -13.120 -2.608  1.00   34.81  ? 137  PHE B N   1 
ATOM   1007 C CA  . PHE A 1 137 ? -8.412  -12.977 -1.867  1.00   33.61  ? 137  PHE B CA  1 
ATOM   1008 C C   . PHE A 1 137 ? -7.381  -12.075 -2.531  1.00   32.29  ? 137  PHE B C   1 
ATOM   1009 O O   . PHE A 1 137 ? -6.385  -11.719 -1.905  1.00   31.64  ? 137  PHE B O   1 
ATOM   1010 C CB  . PHE A 1 137 ? -7.779  -14.349 -1.556  1.00   34.31  ? 137  PHE B CB  1 
ATOM   1011 C CG  . PHE A 1 137 ? -8.589  -15.193 -0.598  1.00   35.52  ? 137  PHE B CG  1 
ATOM   1012 C CD1 . PHE A 1 137 ? -8.212  -16.490 -0.302  1.00   37.22  ? 137  PHE B CD1 1 
ATOM   1013 C CD2 . PHE A 1 137 ? -9.740  -14.688 -0.010  1.00   36.73  ? 137  PHE B CD2 1 
ATOM   1014 C CE1 . PHE A 1 137 ? -8.960  -17.259 0.568   1.00   37.40  ? 137  PHE B CE1 1 
ATOM   1015 C CE2 . PHE A 1 137 ? -10.499 -15.456 0.843   1.00   37.16  ? 137  PHE B CE2 1 
ATOM   1016 C CZ  . PHE A 1 137 ? -10.110 -16.736 1.139   1.00   36.48  ? 137  PHE B CZ  1 
ATOM   1017 N N   . PHE A 1 138 ? -7.630  -11.704 -3.787  1.00   30.01  ? 138  PHE B N   1 
ATOM   1018 C CA  . PHE A 1 138 ? -6.700  -10.888 -4.582  1.00   29.02  ? 138  PHE B CA  1 
ATOM   1019 C C   . PHE A 1 138 ? -7.354  -9.553  -4.837  1.00   27.97  ? 138  PHE B C   1 
ATOM   1020 O O   . PHE A 1 138 ? -8.584  -9.449  -4.761  1.00   29.10  ? 138  PHE B O   1 
ATOM   1021 C CB  . PHE A 1 138 ? -6.447  -11.543 -5.953  1.00   28.69  ? 138  PHE B CB  1 
ATOM   1022 C CG  . PHE A 1 138 ? -5.731  -12.861 -5.884  1.00   28.55  ? 138  PHE B CG  1 
ATOM   1023 C CD1 . PHE A 1 138 ? -6.435  -14.048 -5.698  1.00   27.71  ? 138  PHE B CD1 1 
ATOM   1024 C CD2 . PHE A 1 138 ? -4.349  -12.915 -6.023  1.00   27.34  ? 138  PHE B CD2 1 
ATOM   1025 C CE1 . PHE A 1 138 ? -5.765  -15.267 -5.641  1.00   28.13  ? 138  PHE B CE1 1 
ATOM   1026 C CE2 . PHE A 1 138 ? -3.672  -14.136 -5.975  1.00   26.81  ? 138  PHE B CE2 1 
ATOM   1027 C CZ  . PHE A 1 138 ? -4.385  -15.308 -5.785  1.00   25.87  ? 138  PHE B CZ  1 
ATOM   1028 N N   . ASP A 1 139 ? -6.566  -8.534  -5.164  0.52   24.31  ? 139  ASP B N   1 
ATOM   1029 C CA  . ASP A 1 139 ? -7.162  -7.312  -5.708  0.52   24.31  ? 139  ASP B CA  1 
ATOM   1030 C C   . ASP A 1 139 ? -6.932  -7.198  -7.225  0.52   24.73  ? 139  ASP B C   1 
ATOM   1031 O O   . ASP A 1 139 ? -7.622  -6.457  -7.913  0.52   23.85  ? 139  ASP B O   1 
ATOM   1032 C CB  . ASP A 1 139 ? -6.701  -6.067  -4.938  0.52   23.82  ? 139  ASP B CB  1 
ATOM   1033 C CG  . ASP A 1 139 ? -7.344  -5.968  -3.543  0.52   25.18  ? 139  ASP B CG  1 
ATOM   1034 O OD1 . ASP A 1 139 ? -8.592  -6.045  -3.429  0.52   23.89  ? 139  ASP B OD1 1 
ATOM   1035 O OD2 . ASP A 1 139 ? -6.598  -5.808  -2.557  0.52   27.34  ? 139  ASP B OD2 1 
ATOM   1036 N N   . ILE A 1 140 ? -5.983  -7.973  -7.733  1.00   26.27  ? 140  ILE B N   1 
ATOM   1037 C CA  . ILE A 1 140 ? -5.739  -8.100  -9.173  1.00   28.57  ? 140  ILE B CA  1 
ATOM   1038 C C   . ILE A 1 140 ? -6.748  -9.068  -9.781  1.00   29.87  ? 140  ILE B C   1 
ATOM   1039 O O   . ILE A 1 140 ? -7.314  -9.907  -9.065  1.00   29.88  ? 140  ILE B O   1 
ATOM   1040 C CB  . ILE A 1 140 ? -4.318  -8.634  -9.447  1.00   28.49  ? 140  ILE B CB  1 
ATOM   1041 C CG1 . ILE A 1 140 ? -4.123  -9.987  -8.755  1.00   29.64  ? 140  ILE B CG1 1 
ATOM   1042 C CG2 . ILE A 1 140 ? -3.256  -7.607  -9.000  1.00   27.71  ? 140  ILE B CG2 1 
ATOM   1043 C CD1 . ILE A 1 140 ? -2.776  -10.629 -9.003  1.00   27.77  ? 140  ILE B CD1 1 
ATOM   1044 N N   . PRO A 1 141 ? -6.979  -8.969  -11.108 1.00   30.48  ? 141  PRO B N   1 
ATOM   1045 C CA  . PRO A 1 141 ? -7.958  -9.872  -11.706 1.00   30.30  ? 141  PRO B CA  1 
ATOM   1046 C C   . PRO A 1 141 ? -7.509  -11.328 -11.721 1.00   30.76  ? 141  PRO B C   1 
ATOM   1047 O O   . PRO A 1 141 ? -6.321  -11.645 -11.879 1.00   30.24  ? 141  PRO B O   1 
ATOM   1048 C CB  . PRO A 1 141 ? -8.138  -9.329  -13.133 1.00   31.40  ? 141  PRO B CB  1 
ATOM   1049 C CG  . PRO A 1 141 ? -6.965  -8.449  -13.390 1.00   30.81  ? 141  PRO B CG  1 
ATOM   1050 C CD  . PRO A 1 141 ? -6.480  -7.956  -12.061 1.00   30.50  ? 141  PRO B CD  1 
ATOM   1051 N N   . VAL A 1 142 ? -8.475  -12.208 -11.518 1.00   30.06  ? 142  VAL B N   1 
ATOM   1052 C CA  . VAL A 1 142 ? -8.232  -13.640 -11.537 1.00   31.07  ? 142  VAL B CA  1 
ATOM   1053 C C   . VAL A 1 142 ? -9.199  -14.231 -12.557 1.00   32.18  ? 142  VAL B C   1 
ATOM   1054 O O   . VAL A 1 142 ? -10.382 -13.906 -12.545 1.00   32.78  ? 142  VAL B O   1 
ATOM   1055 C CB  . VAL A 1 142 ? -8.513  -14.259 -10.136 1.00   31.05  ? 142  VAL B CB  1 
ATOM   1056 C CG1 . VAL A 1 142 ? -8.381  -15.778 -10.159 1.00   30.99  ? 142  VAL B CG1 1 
ATOM   1057 C CG2 . VAL A 1 142 ? -7.604  -13.639 -9.066  1.00   28.84  ? 142  VAL B CG2 1 
ATOM   1058 N N   . ASP A 1 143 ? -8.692  -15.059 -13.465 1.00   32.59  ? 143  ASP B N   1 
ATOM   1059 C CA  . ASP A 1 143 ? -9.574  -15.870 -14.310 1.00   33.02  ? 143  ASP B CA  1 
ATOM   1060 C C   . ASP A 1 143 ? -9.557  -17.312 -13.826 1.00   33.33  ? 143  ASP B C   1 
ATOM   1061 O O   . ASP A 1 143 ? -8.537  -18.000 -13.894 1.00   33.49  ? 143  ASP B O   1 
ATOM   1062 C CB  . ASP A 1 143 ? -9.190  -15.740 -15.787 1.00   33.89  ? 143  ASP B CB  1 
ATOM   1063 C CG  . ASP A 1 143 ? -9.397  -14.325 -16.307 1.00   35.54  ? 143  ASP B CG  1 
ATOM   1064 O OD1 . ASP A 1 143 ? -10.488 -13.767 -16.078 1.00   38.02  ? 143  ASP B OD1 1 
ATOM   1065 O OD2 . ASP A 1 143 ? -8.473  -13.763 -16.929 1.00   37.87  ? 143  ASP B OD2 1 
ATOM   1066 N N   . ASN A 1 144 ? -10.698 -17.736 -13.296 1.00   32.50  ? 144  ASN B N   1 
ATOM   1067 C CA  . ASN A 1 144 ? -10.882 -19.067 -12.744 1.00   34.65  ? 144  ASN B CA  1 
ATOM   1068 C C   . ASN A 1 144 ? -11.642 -19.913 -13.762 1.00   35.35  ? 144  ASN B C   1 
ATOM   1069 O O   . ASN A 1 144 ? -12.872 -19.855 -13.838 1.00   36.70  ? 144  ASN B O   1 
ATOM   1070 C CB  . ASN A 1 144 ? -11.648 -18.983 -11.414 1.00   34.39  ? 144  ASN B CB  1 
ATOM   1071 C CG  . ASN A 1 144 ? -11.902 -20.349 -10.784 1.00   36.13  ? 144  ASN B CG  1 
ATOM   1072 O OD1 . ASN A 1 144 ? -11.042 -21.238 -10.797 1.00   35.61  ? 144  ASN B OD1 1 
ATOM   1073 N ND2 . ASN A 1 144 ? -13.083 -20.513 -10.213 1.00   37.88  ? 144  ASN B ND2 1 
ATOM   1074 N N   . LEU A 1 145 ? -10.895 -20.680 -14.551 1.00   35.88  ? 145  LEU B N   1 
ATOM   1075 C CA  . LEU A 1 145 ? -11.462 -21.507 -15.621 1.00   35.94  ? 145  LEU B CA  1 
ATOM   1076 C C   . LEU A 1 145 ? -12.154 -22.726 -15.026 1.00   36.51  ? 145  LEU B C   1 
ATOM   1077 O O   . LEU A 1 145 ? -11.853 -23.127 -13.907 1.00   37.03  ? 145  LEU B O   1 
ATOM   1078 C CB  . LEU A 1 145 ? -10.347 -21.941 -16.567 1.00   36.04  ? 145  LEU B CB  1 
ATOM   1079 C CG  . LEU A 1 145 ? -9.460  -20.798 -17.048 1.00   36.10  ? 145  LEU B CG  1 
ATOM   1080 C CD1 . LEU A 1 145 ? -8.185  -21.339 -17.617 1.00   36.40  ? 145  LEU B CD1 1 
ATOM   1081 C CD2 . LEU A 1 145 ? -10.198 -19.945 -18.071 1.00   39.06  ? 145  LEU B CD2 1 
ATOM   1082 N N   . TYR A 1 146 ? -13.092 -23.307 -15.761 0.68   36.64  ? 146  TYR B N   1 
ATOM   1083 C CA  . TYR A 1 146 ? -13.834 -24.452 -15.255 0.68   36.76  ? 146  TYR B CA  1 
ATOM   1084 C C   . TYR A 1 146 ? -13.522 -25.700 -16.038 0.68   37.07  ? 146  TYR B C   1 
ATOM   1085 O O   . TYR A 1 146 ? -13.336 -25.641 -17.245 0.68   34.65  ? 146  TYR B O   1 
ATOM   1086 C CB  . TYR A 1 146 ? -15.320 -24.181 -15.335 0.68   37.22  ? 146  TYR B CB  1 
ATOM   1087 C CG  . TYR A 1 146 ? -15.770 -23.095 -14.410 0.68   39.91  ? 146  TYR B CG  1 
ATOM   1088 C CD1 . TYR A 1 146 ? -16.088 -21.831 -14.896 0.68   42.70  ? 146  TYR B CD1 1 
ATOM   1089 C CD2 . TYR A 1 146 ? -15.876 -23.328 -13.040 0.68   42.72  ? 146  TYR B CD2 1 
ATOM   1090 C CE1 . TYR A 1 146 ? -16.506 -20.824 -14.037 0.68   44.63  ? 146  TYR B CE1 1 
ATOM   1091 C CE2 . TYR A 1 146 ? -16.288 -22.336 -12.178 0.68   44.38  ? 146  TYR B CE2 1 
ATOM   1092 C CZ  . TYR A 1 146 ? -16.604 -21.090 -12.681 0.68   45.27  ? 146  TYR B CZ  1 
ATOM   1093 O OH  . TYR A 1 146 ? -17.023 -20.111 -11.821 0.68   47.51  ? 146  TYR B OH  1 
ATOM   1094 N N   . ALA A 1 147 ? -13.462 -26.833 -15.347 1.00   38.80  ? 147  ALA B N   1 
ATOM   1095 C CA  . ALA A 1 147 ? -13.323 -28.115 -16.024 1.00   40.49  ? 147  ALA B CA  1 
ATOM   1096 C C   . ALA A 1 147 ? -14.686 -28.691 -16.433 1.00   40.86  ? 147  ALA B C   1 
ATOM   1097 O O   . ALA A 1 147 ? -14.740 -29.601 -17.249 1.00   41.71  ? 147  ALA B O   1 
ATOM   1098 C CB  . ALA A 1 147 ? -12.552 -29.100 -15.161 1.00   40.68  ? 147  ALA B CB  1 
ATOM   1099 N N   . GLU A 1 148 ? -15.767 -28.131 -15.886 1.00   42.18  ? 148  GLU B N   1 
ATOM   1100 C CA  . GLU A 1 148 ? -17.137 -28.601 -16.135 1.00   44.76  ? 148  GLU B CA  1 
ATOM   1101 C C   . GLU A 1 148 ? -17.442 -28.907 -17.617 1.00   45.49  ? 148  GLU B C   1 
ATOM   1102 O O   . GLU A 1 148 ? -17.859 -30.021 -17.930 1.00   45.75  ? 148  GLU B O   1 
ATOM   1103 C CB  . GLU A 1 148 ? -18.170 -27.641 -15.524 1.00   45.10  ? 148  GLU B CB  1 
ATOM   1104 C CG  . GLU A 1 148 ? -19.636 -28.001 -15.813 1.00   48.33  ? 148  GLU B CG  1 
ATOM   1105 C CD  . GLU A 1 148 ? -20.615 -27.424 -14.792 1.00   52.55  ? 148  GLU B CD  1 
ATOM   1106 O OE1 . GLU A 1 148 ? -20.176 -26.911 -13.737 1.00   55.08  ? 148  GLU B OE1 1 
ATOM   1107 O OE2 . GLU A 1 148 ? -21.838 -27.498 -15.034 1.00   54.17  ? 148  GLU B OE2 1 
ATOM   1108 N N   . PRO A 1 149 ? -17.207 -27.942 -18.532 1.00   46.48  ? 149  PRO B N   1 
ATOM   1109 C CA  . PRO A 1 149 ? -17.541 -28.266 -19.925 1.00   46.79  ? 149  PRO B CA  1 
ATOM   1110 C C   . PRO A 1 149 ? -16.799 -29.505 -20.426 1.00   46.67  ? 149  PRO B C   1 
ATOM   1111 O O   . PRO A 1 149 ? -17.398 -30.335 -21.118 1.00   46.77  ? 149  PRO B O   1 
ATOM   1112 C CB  . PRO A 1 149 ? -17.104 -27.016 -20.702 1.00   47.17  ? 149  PRO B CB  1 
ATOM   1113 C CG  . PRO A 1 149 ? -17.075 -25.925 -19.685 1.00   47.30  ? 149  PRO B CG  1 
ATOM   1114 C CD  . PRO A 1 149 ? -16.639 -26.584 -18.411 1.00   46.62  ? 149  PRO B CD  1 
ATOM   1115 N N   . ALA A 1 150 ? -15.524 -29.640 -20.059 1.00   45.59  ? 150  ALA B N   1 
ATOM   1116 C CA  . ALA A 1 150 ? -14.727 -30.803 -20.453 1.00   45.02  ? 150  ALA B CA  1 
ATOM   1117 C C   . ALA A 1 150 ? -15.217 -32.073 -19.751 1.00   44.51  ? 150  ALA B C   1 
ATOM   1118 O O   . ALA A 1 150 ? -15.151 -33.171 -20.309 1.00   44.67  ? 150  ALA B O   1 
ATOM   1119 C CB  . ALA A 1 150 ? -13.252 -30.571 -20.166 1.00   44.60  ? 150  ALA B CB  1 
ATOM   1120 N N   . VAL A 1 151 ? -15.713 -31.907 -18.529 1.00   43.21  ? 151  VAL B N   1 
ATOM   1121 C CA  . VAL A 1 151 ? -16.263 -33.018 -17.758 1.00   42.68  ? 151  VAL B CA  1 
ATOM   1122 C C   . VAL A 1 151 ? -17.593 -33.494 -18.371 1.00   43.55  ? 151  VAL B C   1 
ATOM   1123 O O   . VAL A 1 151 ? -17.741 -34.678 -18.693 1.00   43.35  ? 151  VAL B O   1 
ATOM   1124 C CB  . VAL A 1 151 ? -16.410 -32.636 -16.268 1.00   41.90  ? 151  VAL B CB  1 
ATOM   1125 C CG1 . VAL A 1 151 ? -17.273 -33.641 -15.518 1.00   40.64  ? 151  VAL B CG1 1 
ATOM   1126 C CG2 . VAL A 1 151 ? -15.018 -32.515 -15.614 1.00   40.68  ? 151  VAL B CG2 1 
ATOM   1127 N N   . LEU A 1 152 ? -18.536 -32.569 -18.550 1.00   44.24  ? 152  LEU B N   1 
ATOM   1128 C CA  . LEU A 1 152 ? -19.809 -32.873 -19.206 1.00   45.51  ? 152  LEU B CA  1 
ATOM   1129 C C   . LEU A 1 152 ? -19.596 -33.622 -20.526 1.00   46.34  ? 152  LEU B C   1 
ATOM   1130 O O   . LEU A 1 152 ? -20.282 -34.609 -20.808 1.00   46.56  ? 152  LEU B O   1 
ATOM   1131 C CB  . LEU A 1 152 ? -20.613 -31.594 -19.439 1.00   45.15  ? 152  LEU B CB  1 
ATOM   1132 C CG  . LEU A 1 152 ? -21.169 -30.897 -18.195 1.00   45.84  ? 152  LEU B CG  1 
ATOM   1133 C CD1 . LEU A 1 152 ? -21.645 -29.484 -18.511 1.00   45.64  ? 152  LEU B CD1 1 
ATOM   1134 C CD2 . LEU A 1 152 ? -22.284 -31.701 -17.590 1.00   46.27  ? 152  LEU B CD2 1 
ATOM   1135 N N   . LYS A 1 153 ? -18.630 -33.162 -21.316 1.00   47.53  ? 153  LYS B N   1 
ATOM   1136 C CA  . LYS A 1 153 ? -18.292 -33.803 -22.583 1.00   48.35  ? 153  LYS B CA  1 
ATOM   1137 C C   . LYS A 1 153 ? -17.783 -35.223 -22.379 1.00   48.24  ? 153  LYS B C   1 
ATOM   1138 O O   . LYS A 1 153 ? -18.170 -36.133 -23.119 1.00   48.61  ? 153  LYS B O   1 
ATOM   1139 C CB  . LYS A 1 153 ? -17.248 -32.984 -23.343 1.00   48.91  ? 153  LYS B CB  1 
ATOM   1140 C CG  . LYS A 1 153 ? -16.649 -33.688 -24.555 1.00   51.19  ? 153  LYS B CG  1 
ATOM   1141 C CD  . LYS A 1 153 ? -15.751 -32.747 -25.348 1.00   54.91  ? 153  LYS B CD  1 
ATOM   1142 C CE  . LYS A 1 153 ? -15.150 -33.438 -26.558 1.00   57.06  ? 153  LYS B CE  1 
ATOM   1143 N NZ  . LYS A 1 153 ? -14.051 -34.380 -26.184 1.00   59.72  ? 153  LYS B NZ  1 
ATOM   1144 N N   . TRP A 1 154 ? -16.911 -35.412 -21.390 1.00   47.62  ? 154  TRP B N   1 
ATOM   1145 C CA  . TRP A 1 154 ? -16.381 -36.742 -21.111 1.00   46.88  ? 154  TRP B CA  1 
ATOM   1146 C C   . TRP A 1 154 ? -17.514 -37.690 -20.722 1.00   46.19  ? 154  TRP B C   1 
ATOM   1147 O O   . TRP A 1 154 ? -17.559 -38.836 -21.167 1.00   46.02  ? 154  TRP B O   1 
ATOM   1148 C CB  . TRP A 1 154 ? -15.309 -36.720 -20.017 1.00   46.78  ? 154  TRP B CB  1 
ATOM   1149 C CG  . TRP A 1 154 ? -14.640 -38.061 -19.852 1.00   47.32  ? 154  TRP B CG  1 
ATOM   1150 C CD1 . TRP A 1 154 ? -13.473 -38.469 -20.435 1.00   47.96  ? 154  TRP B CD1 1 
ATOM   1151 C CD2 . TRP A 1 154 ? -15.112 -39.174 -19.075 1.00   47.39  ? 154  TRP B CD2 1 
ATOM   1152 N NE1 . TRP A 1 154 ? -13.181 -39.763 -20.061 1.00   48.16  ? 154  TRP B NE1 1 
ATOM   1153 C CE2 . TRP A 1 154 ? -14.170 -40.219 -19.228 1.00   47.85  ? 154  TRP B CE2 1 
ATOM   1154 C CE3 . TRP A 1 154 ? -16.231 -39.387 -18.256 1.00   46.61  ? 154  TRP B CE3 1 
ATOM   1155 C CZ2 . TRP A 1 154 ? -14.320 -41.463 -18.604 1.00   47.08  ? 154  TRP B CZ2 1 
ATOM   1156 C CZ3 . TRP A 1 154 ? -16.375 -40.624 -17.630 1.00   46.92  ? 154  TRP B CZ3 1 
ATOM   1157 C CH2 . TRP A 1 154 ? -15.423 -41.646 -17.811 1.00   46.22  ? 154  TRP B CH2 1 
ATOM   1158 N N   . ILE A 1 155 ? -18.422 -37.208 -19.884 1.00   45.65  ? 155  ILE B N   1 
ATOM   1159 C CA  . ILE A 1 155 ? -19.541 -38.024 -19.427 1.00   45.58  ? 155  ILE B CA  1 
ATOM   1160 C C   . ILE A 1 155 ? -20.402 -38.463 -20.617 1.00   46.42  ? 155  ILE B C   1 
ATOM   1161 O O   . ILE A 1 155 ? -20.634 -39.666 -20.809 1.00   46.14  ? 155  ILE B O   1 
ATOM   1162 C CB  . ILE A 1 155 ? -20.386 -37.276 -18.385 1.00   44.70  ? 155  ILE B CB  1 
ATOM   1163 C CG1 . ILE A 1 155 ? -19.620 -37.190 -17.059 1.00   44.02  ? 155  ILE B CG1 1 
ATOM   1164 C CG2 . ILE A 1 155 ? -21.738 -37.959 -18.174 1.00   44.42  ? 155  ILE B CG2 1 
ATOM   1165 C CD1 . ILE A 1 155 ? -20.164 -36.156 -16.067 1.00   42.08  ? 155  ILE B CD1 1 
ATOM   1166 N N   . ARG A 1 156 ? -20.839 -37.489 -21.416 1.00   47.00  ? 156  ARG B N   1 
ATOM   1167 C CA  . ARG A 1 156 ? -21.708 -37.751 -22.559 1.00   47.68  ? 156  ARG B CA  1 
ATOM   1168 C C   . ARG A 1 156 ? -21.088 -38.744 -23.543 1.00   47.09  ? 156  ARG B C   1 
ATOM   1169 O O   . ARG A 1 156 ? -21.802 -39.561 -24.120 1.00   47.83  ? 156  ARG B O   1 
ATOM   1170 C CB  . ARG A 1 156 ? -22.094 -36.454 -23.277 1.00   48.00  ? 156  ARG B CB  1 
ATOM   1171 C CG  . ARG A 1 156 ? -23.116 -35.605 -22.547 1.00   49.32  ? 156  ARG B CG  1 
ATOM   1172 C CD  . ARG A 1 156 ? -23.566 -34.438 -23.419 1.00   51.91  ? 156  ARG B CD  1 
ATOM   1173 N NE  . ARG A 1 156 ? -24.463 -33.524 -22.713 1.00   54.62  ? 156  ARG B NE  1 
ATOM   1174 C CZ  . ARG A 1 156 ? -24.141 -32.287 -22.341 1.00   55.86  ? 156  ARG B CZ  1 
ATOM   1175 N NH1 . ARG A 1 156 ? -22.934 -31.793 -22.605 1.00   55.75  ? 156  ARG B NH1 1 
ATOM   1176 N NH2 . ARG A 1 156 ? -25.034 -31.535 -21.710 1.00   56.17  ? 156  ARG B NH2 1 
ATOM   1177 N N   . GLU A 1 157 ? -19.768 -38.695 -23.712 0.52   45.74  ? 157  GLU B N   1 
ATOM   1178 C CA  . GLU A 1 157 ? -19.106 -39.561 -24.691 0.52   44.91  ? 157  GLU B CA  1 
ATOM   1179 C C   . GLU A 1 157 ? -18.602 -40.907 -24.140 0.52   44.90  ? 157  GLU B C   1 
ATOM   1180 O O   . GLU A 1 157 ? -18.223 -41.784 -24.915 0.52   44.14  ? 157  GLU B O   1 
ATOM   1181 C CB  . GLU A 1 157 ? -18.001 -38.800 -25.448 0.52   44.56  ? 157  GLU B CB  1 
ATOM   1182 C CG  . GLU A 1 157 ? -16.611 -38.904 -24.839 0.52   45.27  ? 157  GLU B CG  1 
ATOM   1183 C CD  . GLU A 1 157 ? -15.586 -37.957 -25.457 0.52   46.15  ? 157  GLU B CD  1 
ATOM   1184 O OE1 . GLU A 1 157 ? -14.429 -37.964 -24.976 0.52   46.06  ? 157  GLU B OE1 1 
ATOM   1185 O OE2 . GLU A 1 157 ? -15.923 -37.211 -26.407 0.52   46.20  ? 157  GLU B OE2 1 
ATOM   1186 N N   . ASN A 1 158 ? -18.622 -41.087 -22.820 1.00   46.09  ? 158  ASN B N   1 
ATOM   1187 C CA  . ASN A 1 158 ? -18.076 -42.309 -22.208 1.00   47.41  ? 158  ASN B CA  1 
ATOM   1188 C C   . ASN A 1 158 ? -19.044 -43.126 -21.362 1.00   47.61  ? 158  ASN B C   1 
ATOM   1189 O O   . ASN A 1 158 ? -18.776 -44.284 -21.059 1.00   47.67  ? 158  ASN B O   1 
ATOM   1190 C CB  . ASN A 1 158 ? -16.847 -41.999 -21.349 1.00   47.96  ? 158  ASN B CB  1 
ATOM   1191 C CG  . ASN A 1 158 ? -15.652 -41.588 -22.166 1.00   50.04  ? 158  ASN B CG  1 
ATOM   1192 O OD1 . ASN A 1 158 ? -14.800 -42.409 -22.487 1.00   52.74  ? 158  ASN B OD1 1 
ATOM   1193 N ND2 . ASN A 1 158 ? -15.573 -40.305 -22.496 1.00   51.70  ? 158  ASN B ND2 1 
ATOM   1194 N N   . ILE A 1 159 ? -20.144 -42.518 -20.946 1.00   48.32  ? 159  ILE B N   1 
ATOM   1195 C CA  . ILE A 1 159 ? -21.111 -43.224 -20.119 1.00   49.27  ? 159  ILE B CA  1 
ATOM   1196 C C   . ILE A 1 159 ? -22.421 -43.328 -20.882 1.00   50.04  ? 159  ILE B C   1 
ATOM   1197 O O   . ILE A 1 159 ? -23.136 -42.336 -21.040 1.00   49.97  ? 159  ILE B O   1 
ATOM   1198 C CB  . ILE A 1 159 ? -21.284 -42.554 -18.726 1.00   49.14  ? 159  ILE B CB  1 
ATOM   1199 C CG1 . ILE A 1 159 ? -19.951 -42.598 -17.970 1.00   49.42  ? 159  ILE B CG1 1 
ATOM   1200 C CG2 . ILE A 1 159 ? -22.364 -43.271 -17.909 1.00   48.45  ? 159  ILE B CG2 1 
ATOM   1201 C CD1 . ILE A 1 159 ? -19.844 -41.601 -16.834 1.00   50.05  ? 159  ILE B CD1 1 
ATOM   1202 N N   . SER A 1 160 ? -22.706 -44.537 -21.368 1.00   51.23  ? 160  SER B N   1 
ATOM   1203 C CA  . SER A 1 160 ? -23.882 -44.809 -22.194 1.00   52.08  ? 160  SER B CA  1 
ATOM   1204 C C   . SER A 1 160 ? -25.154 -44.347 -21.499 1.00   51.89  ? 160  SER B C   1 
ATOM   1205 O O   . SER A 1 160 ? -26.027 -43.746 -22.121 1.00   51.97  ? 160  SER B O   1 
ATOM   1206 C CB  . SER A 1 160 ? -23.983 -46.305 -22.512 1.00   52.46  ? 160  SER B CB  1 
ATOM   1207 O OG  . SER A 1 160 ? -22.763 -46.822 -23.018 1.00   53.55  ? 160  SER B OG  1 
ATOM   1208 N N   . GLU A 1 161 ? -25.225 -44.596 -20.196 1.00   51.69  ? 161  GLU B N   1 
ATOM   1209 C CA  . GLU A 1 161 ? -26.414 -44.306 -19.403 1.00   51.26  ? 161  GLU B CA  1 
ATOM   1210 C C   . GLU A 1 161 ? -26.421 -42.903 -18.808 1.00   50.23  ? 161  GLU B C   1 
ATOM   1211 O O   . GLU A 1 161 ? -27.118 -42.674 -17.819 1.00   49.63  ? 161  GLU B O   1 
ATOM   1212 C CB  . GLU A 1 161 ? -26.563 -45.326 -18.262 1.00   51.83  ? 161  GLU B CB  1 
ATOM   1213 C CG  . GLU A 1 161 ? -26.414 -46.791 -18.664 1.00   53.87  ? 161  GLU B CG  1 
ATOM   1214 C CD  . GLU A 1 161 ? -24.972 -47.290 -18.611 1.00   56.44  ? 161  GLU B CD  1 
ATOM   1215 O OE1 . GLU A 1 161 ? -24.031 -46.495 -18.842 1.00   57.10  ? 161  GLU B OE1 1 
ATOM   1216 O OE2 . GLU A 1 161 ? -24.780 -48.495 -18.340 1.00   57.94  ? 161  GLU B OE2 1 
ATOM   1217 N N   . TRP A 1 162 ? -25.666 -41.966 -19.390 1.00   49.11  ? 162  TRP B N   1 
ATOM   1218 C CA  . TRP A 1 162 ? -25.532 -40.640 -18.764 1.00   48.70  ? 162  TRP B CA  1 
ATOM   1219 C C   . TRP A 1 162 ? -26.876 -39.944 -18.567 1.00   49.45  ? 162  TRP B C   1 
ATOM   1220 O O   . TRP A 1 162 ? -27.060 -39.188 -17.609 1.00   48.93  ? 162  TRP B O   1 
ATOM   1221 C CB  . TRP A 1 162 ? -24.529 -39.735 -19.495 1.00   48.30  ? 162  TRP B CB  1 
ATOM   1222 C CG  . TRP A 1 162 ? -24.930 -39.246 -20.867 1.00   46.63  ? 162  TRP B CG  1 
ATOM   1223 C CD1 . TRP A 1 162 ? -24.531 -39.765 -22.063 1.00   46.30  ? 162  TRP B CD1 1 
ATOM   1224 C CD2 . TRP A 1 162 ? -25.774 -38.128 -21.180 1.00   47.05  ? 162  TRP B CD2 1 
ATOM   1225 N NE1 . TRP A 1 162 ? -25.079 -39.055 -23.100 1.00   46.28  ? 162  TRP B NE1 1 
ATOM   1226 C CE2 . TRP A 1 162 ? -25.851 -38.047 -22.590 1.00   47.01  ? 162  TRP B CE2 1 
ATOM   1227 C CE3 . TRP A 1 162 ? -26.484 -37.195 -20.409 1.00   46.46  ? 162  TRP B CE3 1 
ATOM   1228 C CZ2 . TRP A 1 162 ? -26.599 -37.065 -23.247 1.00   46.81  ? 162  TRP B CZ2 1 
ATOM   1229 C CZ3 . TRP A 1 162 ? -27.229 -36.220 -21.062 1.00   46.49  ? 162  TRP B CZ3 1 
ATOM   1230 C CH2 . TRP A 1 162 ? -27.281 -36.164 -22.470 1.00   46.89  ? 162  TRP B CH2 1 
ATOM   1231 N N   . ARG A 1 163 ? -27.823 -40.227 -19.459 1.00   50.60  ? 163  ARG B N   1 
ATOM   1232 C CA  . ARG A 1 163 ? -29.156 -39.626 -19.377 1.00   51.55  ? 163  ARG B CA  1 
ATOM   1233 C C   . ARG A 1 163 ? -29.984 -40.147 -18.208 1.00   51.71  ? 163  ARG B C   1 
ATOM   1234 O O   . ARG A 1 163 ? -31.049 -39.605 -17.912 1.00   52.14  ? 163  ARG B O   1 
ATOM   1235 C CB  . ARG A 1 163 ? -29.916 -39.824 -20.682 1.00   51.64  ? 163  ARG B CB  1 
ATOM   1236 C CG  . ARG A 1 163 ? -29.302 -39.095 -21.850 1.00   52.63  ? 163  ARG B CG  1 
ATOM   1237 C CD  . ARG A 1 163 ? -30.148 -39.300 -23.082 1.00   53.52  ? 163  ARG B CD  1 
ATOM   1238 N NE  . ARG A 1 163 ? -29.491 -38.828 -24.295 1.00   53.92  ? 163  ARG B NE  1 
ATOM   1239 C CZ  . ARG A 1 163 ? -28.501 -39.465 -24.916 1.00   54.03  ? 163  ARG B CZ  1 
ATOM   1240 N NH1 . ARG A 1 163 ? -28.022 -40.607 -24.433 1.00   52.23  ? 163  ARG B NH1 1 
ATOM   1241 N NH2 . ARG A 1 163 ? -27.986 -38.953 -26.025 1.00   54.27  ? 163  ARG B NH2 1 
ATOM   1242 N N   . ASN A 1 164 ? -29.495 -41.189 -17.546 1.00   51.70  ? 164  ASN B N   1 
ATOM   1243 C CA  . ASN A 1 164 ? -30.181 -41.745 -16.385 1.00   51.98  ? 164  ASN B CA  1 
ATOM   1244 C C   . ASN A 1 164 ? -29.279 -41.909 -15.171 1.00   51.10  ? 164  ASN B C   1 
ATOM   1245 O O   . ASN A 1 164 ? -29.620 -42.625 -14.228 1.00   51.38  ? 164  ASN B O   1 
ATOM   1246 C CB  . ASN A 1 164 ? -30.840 -43.080 -16.745 1.00   52.56  ? 164  ASN B CB  1 
ATOM   1247 C CG  . ASN A 1 164 ? -32.132 -42.896 -17.502 1.00   54.00  ? 164  ASN B CG  1 
ATOM   1248 O OD1 . ASN A 1 164 ? -33.215 -42.936 -16.918 1.00   56.18  ? 164  ASN B OD1 1 
ATOM   1249 N ND2 . ASN A 1 164 ? -32.027 -42.662 -18.808 1.00   54.03  ? 164  ASN B ND2 1 
ATOM   1250 N N   . CYS A 1 165 ? -28.133 -41.236 -15.190 1.00   49.48  ? 165  CYS B N   1 
ATOM   1251 C CA  . CYS A 1 165 ? -27.152 -41.388 -14.124 1.00   48.15  ? 165  CYS B CA  1 
ATOM   1252 C C   . CYS A 1 165 ? -27.488 -40.468 -12.950 1.00   47.61  ? 165  CYS B C   1 
ATOM   1253 O O   . CYS A 1 165 ? -28.438 -39.685 -13.018 1.00   47.26  ? 165  CYS B O   1 
ATOM   1254 C CB  . CYS A 1 165 ? -25.750 -41.089 -14.654 1.00   47.76  ? 165  CYS B CB  1 
ATOM   1255 S SG  . CYS A 1 165 ? -25.472 -39.323 -14.947 1.00   47.28  ? 165  CYS B SG  1 
ATOM   1256 N N   . THR A 1 166 ? -26.717 -40.579 -11.871 1.00   47.21  ? 166  THR B N   1 
ATOM   1257 C CA  . THR A 1 166 ? -26.812 -39.649 -10.745 1.00   46.76  ? 166  THR B CA  1 
ATOM   1258 C C   . THR A 1 166 ? -25.446 -39.038 -10.482 1.00   45.69  ? 166  THR B C   1 
ATOM   1259 O O   . THR A 1 166 ? -24.442 -39.749 -10.362 1.00   45.54  ? 166  THR B O   1 
ATOM   1260 C CB  . THR A 1 166 ? -27.294 -40.332 -9.447  1.00   47.24  ? 166  THR B CB  1 
ATOM   1261 O OG1 . THR A 1 166 ? -28.553 -40.968 -9.673  1.00   48.16  ? 166  THR B OG1 1 
ATOM   1262 C CG2 . THR A 1 166 ? -27.458 -39.313 -8.321  1.00   47.71  ? 166  THR B CG2 1 
ATOM   1263 N N   . ILE A 1 167 ? -25.411 -37.715 -10.405 1.00   44.16  ? 167  ILE B N   1 
ATOM   1264 C CA  . ILE A 1 167 ? -24.188 -37.018 -10.029 1.00   42.21  ? 167  ILE B CA  1 
ATOM   1265 C C   . ILE A 1 167 ? -24.158 -36.914 -8.508  1.00   41.82  ? 167  ILE B C   1 
ATOM   1266 O O   . ILE A 1 167 ? -25.129 -36.485 -7.880  1.00   41.51  ? 167  ILE B O   1 
ATOM   1267 C CB  . ILE A 1 167 ? -24.079 -35.623 -10.700 1.00   42.39  ? 167  ILE B CB  1 
ATOM   1268 C CG1 . ILE A 1 167 ? -24.399 -35.706 -12.208 1.00   40.32  ? 167  ILE B CG1 1 
ATOM   1269 C CG2 . ILE A 1 167 ? -22.690 -35.010 -10.448 1.00   41.04  ? 167  ILE B CG2 1 
ATOM   1270 C CD1 . ILE A 1 167 ? -23.495 -36.658 -13.020 1.00   39.65  ? 167  ILE B CD1 1 
ATOM   1271 N N   . VAL A 1 168 ? -23.047 -37.340 -7.920  1.00   40.71  ? 168  VAL B N   1 
ATOM   1272 C CA  . VAL A 1 168 ? -22.950 -37.464 -6.469  1.00   40.51  ? 168  VAL B CA  1 
ATOM   1273 C C   . VAL A 1 168 ? -21.784 -36.660 -5.913  1.00   40.48  ? 168  VAL B C   1 
ATOM   1274 O O   . VAL A 1 168 ? -20.649 -36.780 -6.382  1.00   40.22  ? 168  VAL B O   1 
ATOM   1275 C CB  . VAL A 1 168 ? -22.760 -38.937 -6.022  1.00   39.82  ? 168  VAL B CB  1 
ATOM   1276 C CG1 . VAL A 1 168 ? -23.025 -39.076 -4.527  1.00   40.29  ? 168  VAL B CG1 1 
ATOM   1277 C CG2 . VAL A 1 168 ? -23.678 -39.870 -6.797  1.00   40.89  ? 168  VAL B CG2 1 
ATOM   1278 N N   . SER A 1 169 ? -22.073 -35.854 -4.901  1.00   40.93  ? 169  SER B N   1 
ATOM   1279 C CA  . SER A 1 169 ? -21.029 -35.155 -4.160  1.00   42.30  ? 169  SER B CA  1 
ATOM   1280 C C   . SER A 1 169 ? -20.569 -36.036 -3.012  1.00   43.21  ? 169  SER B C   1 
ATOM   1281 O O   . SER A 1 169 ? -21.400 -36.564 -2.270  1.00   43.01  ? 169  SER B O   1 
ATOM   1282 C CB  . SER A 1 169 ? -21.542 -33.818 -3.611  1.00   42.21  ? 169  SER B CB  1 
ATOM   1283 O OG  . SER A 1 169 ? -20.512 -33.134 -2.913  1.00   42.27  ? 169  SER B OG  1 
ATOM   1284 N N   . PRO A 1 170 ? -19.245 -36.204 -2.867  1.00   45.05  ? 170  PRO B N   1 
ATOM   1285 C CA  . PRO A 1 170 ? -18.659 -36.980 -1.772  1.00   46.26  ? 170  PRO B CA  1 
ATOM   1286 C C   . PRO A 1 170 ? -18.748 -36.274 -0.420  1.00   47.35  ? 170  PRO B C   1 
ATOM   1287 O O   . PRO A 1 170 ? -18.487 -36.893 0.605   1.00   47.98  ? 170  PRO B O   1 
ATOM   1288 C CB  . PRO A 1 170 ? -17.195 -37.141 -2.192  1.00   46.34  ? 170  PRO B CB  1 
ATOM   1289 C CG  . PRO A 1 170 ? -16.934 -36.017 -3.113  1.00   46.41  ? 170  PRO B CG  1 
ATOM   1290 C CD  . PRO A 1 170 ? -18.226 -35.743 -3.828  1.00   45.37  ? 170  PRO B CD  1 
ATOM   1291 N N   . ASP A 1 171 ? -19.105 -34.993 -0.414  1.00   48.09  ? 171  ASP B N   1 
ATOM   1292 C CA  . ASP A 1 171 ? -19.291 -34.272 0.846   1.00   49.04  ? 171  ASP B CA  1 
ATOM   1293 C C   . ASP A 1 171 ? -20.339 -33.179 0.742   1.00   49.30  ? 171  ASP B C   1 
ATOM   1294 O O   . ASP A 1 171 ? -20.815 -32.867 -0.348  1.00   48.82  ? 171  ASP B O   1 
ATOM   1295 C CB  . ASP A 1 171 ? -17.962 -33.710 1.373   1.00   49.56  ? 171  ASP B CB  1 
ATOM   1296 C CG  . ASP A 1 171 ? -17.223 -32.860 0.348   1.00   51.69  ? 171  ASP B CG  1 
ATOM   1297 O OD1 . ASP A 1 171 ? -17.874 -32.201 -0.493  1.00   54.60  ? 171  ASP B OD1 1 
ATOM   1298 O OD2 . ASP A 1 171 ? -15.974 -32.847 0.392   1.00   54.83  ? 171  ASP B OD2 1 
ATOM   1299 N N   . ALA A 1 172 ? -20.685 -32.599 1.888   1.00   50.64  ? 172  ALA B N   1 
ATOM   1300 C CA  . ALA A 1 172 ? -21.685 -31.536 1.962   1.00   51.79  ? 172  ALA B CA  1 
ATOM   1301 C C   . ALA A 1 172 ? -21.239 -30.297 1.198   1.00   52.37  ? 172  ALA B C   1 
ATOM   1302 O O   . ALA A 1 172 ? -22.057 -29.610 0.589   1.00   52.56  ? 172  ALA B O   1 
ATOM   1303 C CB  . ALA A 1 172 ? -21.983 -31.187 3.415   1.00   52.08  ? 172  ALA B CB  1 
ATOM   1304 N N   . GLY A 1 173 ? -19.935 -30.038 1.211   1.00   52.95  ? 173  GLY B N   1 
ATOM   1305 C CA  . GLY A 1 173 ? -19.366 -28.865 0.555   1.00   52.92  ? 173  GLY B CA  1 
ATOM   1306 C C   . GLY A 1 173 ? -19.398 -28.861 -0.966  1.00   52.45  ? 173  GLY B C   1 
ATOM   1307 O O   . GLY A 1 173 ? -19.114 -27.836 -1.585  1.00   52.95  ? 173  GLY B O   1 
ATOM   1308 N N   . GLY A 1 174 ? -19.737 -29.992 -1.578  1.00   51.41  ? 174  GLY B N   1 
ATOM   1309 C CA  . GLY A 1 174 ? -19.749 -30.089 -3.043  1.00   49.44  ? 174  GLY B CA  1 
ATOM   1310 C C   . GLY A 1 174 ? -21.135 -30.042 -3.651  1.00   48.12  ? 174  GLY B C   1 
ATOM   1311 O O   . GLY A 1 174 ? -21.305 -30.279 -4.847  1.00   48.25  ? 174  GLY B O   1 
ATOM   1312 N N   . ALA A 1 175 ? -22.124 -29.721 -2.827  1.00   47.08  ? 175  ALA B N   1 
ATOM   1313 C CA  . ALA A 1 175 ? -23.518 -29.716 -3.248  1.00   45.72  ? 175  ALA B CA  1 
ATOM   1314 C C   . ALA A 1 175 ? -23.755 -28.879 -4.503  1.00   44.57  ? 175  ALA B C   1 
ATOM   1315 O O   . ALA A 1 175 ? -24.337 -29.369 -5.471  1.00   45.15  ? 175  ALA B O   1 
ATOM   1316 C CB  . ALA A 1 175 ? -24.401 -29.235 -2.120  1.00   45.97  ? 175  ALA B CB  1 
ATOM   1317 N N   . LYS A 1 176 ? -23.301 -27.625 -4.481  0.40   41.76  ? 176  LYS B N   1 
ATOM   1318 C CA  . LYS A 1 176 ? -23.551 -26.698 -5.585  0.40   39.99  ? 176  LYS B CA  1 
ATOM   1319 C C   . LYS A 1 176 ? -22.927 -27.188 -6.884  0.40   39.30  ? 176  LYS B C   1 
ATOM   1320 O O   . LYS A 1 176 ? -23.555 -27.136 -7.936  0.40   37.50  ? 176  LYS B O   1 
ATOM   1321 C CB  . LYS A 1 176 ? -23.077 -25.285 -5.229  0.40   39.77  ? 176  LYS B CB  1 
ATOM   1322 C CG  . LYS A 1 176 ? -24.125 -24.483 -4.469  0.40   40.64  ? 176  LYS B CG  1 
ATOM   1323 C CD  . LYS A 1 176 ? -23.664 -23.058 -4.188  0.40   42.60  ? 176  LYS B CD  1 
ATOM   1324 C CE  . LYS A 1 176 ? -24.812 -22.053 -4.335  0.40   43.25  ? 176  LYS B CE  1 
ATOM   1325 N NZ  . LYS A 1 176 ? -26.052 -22.434 -3.598  0.40   43.87  ? 176  LYS B NZ  1 
ATOM   1326 N N   . ARG A 1 177 ? -21.704 -27.695 -6.788  0.70   40.91  ? 177  ARG B N   1 
ATOM   1327 C CA  . ARG A 1 177 ? -20.979 -28.240 -7.929  0.70   43.16  ? 177  ARG B CA  1 
ATOM   1328 C C   . ARG A 1 177 ? -21.698 -29.409 -8.605  0.70   44.38  ? 177  ARG B C   1 
ATOM   1329 O O   . ARG A 1 177 ? -21.761 -29.461 -9.834  0.70   44.60  ? 177  ARG B O   1 
ATOM   1330 C CB  . ARG A 1 177 ? -19.575 -28.652 -7.488  0.70   43.35  ? 177  ARG B CB  1 
ATOM   1331 C CG  . ARG A 1 177 ? -18.733 -29.361 -8.528  0.70   44.68  ? 177  ARG B CG  1 
ATOM   1332 C CD  . ARG A 1 177 ? -17.409 -29.807 -7.906  0.70   46.51  ? 177  ARG B CD  1 
ATOM   1333 N NE  . ARG A 1 177 ? -16.744 -28.703 -7.208  0.70   47.69  ? 177  ARG B NE  1 
ATOM   1334 C CZ  . ARG A 1 177 ? -16.045 -27.746 -7.815  0.70   48.34  ? 177  ARG B CZ  1 
ATOM   1335 N NH1 . ARG A 1 177 ? -15.906 -27.758 -9.133  0.70   47.19  ? 177  ARG B NH1 1 
ATOM   1336 N NH2 . ARG A 1 177 ? -15.474 -26.779 -7.105  0.70   49.18  ? 177  ARG B NH2 1 
ATOM   1337 N N   . VAL A 1 178 ? -22.237 -30.346 -7.822  1.00   45.88  ? 178  VAL B N   1 
ATOM   1338 C CA  . VAL A 1 178 ? -22.945 -31.481 -8.432  1.00   46.86  ? 178  VAL B CA  1 
ATOM   1339 C C   . VAL A 1 178 ? -24.343 -31.129 -8.934  1.00   47.59  ? 178  VAL B C   1 
ATOM   1340 O O   . VAL A 1 178 ? -24.728 -31.585 -10.005 1.00   46.42  ? 178  VAL B O   1 
ATOM   1341 C CB  . VAL A 1 178 ? -22.977 -32.769 -7.555  1.00   47.16  ? 178  VAL B CB  1 
ATOM   1342 C CG1 . VAL A 1 178 ? -21.572 -33.158 -7.134  1.00   46.16  ? 178  VAL B CG1 1 
ATOM   1343 C CG2 . VAL A 1 178 ? -23.912 -32.629 -6.355  1.00   47.10  ? 178  VAL B CG2 1 
ATOM   1344 N N   . THR A 1 179 ? -25.103 -30.326 -8.189  1.00   49.06  ? 179  THR B N   1 
ATOM   1345 C CA  . THR A 1 179 ? -26.412 -29.900 -8.697  1.00   50.74  ? 179  THR B CA  1 
ATOM   1346 C C   . THR A 1 179 ? -26.237 -29.145 -10.019 1.00   51.37  ? 179  THR B C   1 
ATOM   1347 O O   . THR A 1 179 ? -27.040 -29.299 -10.940 1.00   51.57  ? 179  THR B O   1 
ATOM   1348 C CB  . THR A 1 179 ? -27.234 -29.057 -7.684  1.00   51.02  ? 179  THR B CB  1 
ATOM   1349 O OG1 . THR A 1 179 ? -26.492 -27.894 -7.295  1.00   52.05  ? 179  THR B OG1 1 
ATOM   1350 C CG2 . THR A 1 179 ? -27.587 -29.877 -6.447  1.00   50.84  ? 179  THR B CG2 1 
ATOM   1351 N N   . SER A 1 180 ? -25.165 -28.363 -10.121 1.00   51.96  ? 180  SER B N   1 
ATOM   1352 C CA  . SER A 1 180 ? -24.864 -27.642 -11.354 1.00   52.36  ? 180  SER B CA  1 
ATOM   1353 C C   . SER A 1 180 ? -24.677 -28.605 -12.526 1.00   52.00  ? 180  SER B C   1 
ATOM   1354 O O   . SER A 1 180 ? -25.201 -28.366 -13.615 1.00   51.91  ? 180  SER B O   1 
ATOM   1355 C CB  . SER A 1 180 ? -23.621 -26.759 -11.189 1.00   52.60  ? 180  SER B CB  1 
ATOM   1356 O OG  . SER A 1 180 ? -23.253 -26.166 -12.423 1.00   53.66  ? 180  SER B OG  1 
ATOM   1357 N N   . ILE A 1 181 ? -23.932 -29.686 -12.302 1.00   51.47  ? 181  ILE B N   1 
ATOM   1358 C CA  . ILE A 1 181 ? -23.717 -30.694 -13.347 1.00   51.01  ? 181  ILE B CA  1 
ATOM   1359 C C   . ILE A 1 181 ? -25.006 -31.469 -13.624 1.00   50.75  ? 181  ILE B C   1 
ATOM   1360 O O   . ILE A 1 181 ? -25.390 -31.648 -14.783 1.00   50.38  ? 181  ILE B O   1 
ATOM   1361 C CB  . ILE A 1 181 ? -22.545 -31.658 -13.024 1.00   51.02  ? 181  ILE B CB  1 
ATOM   1362 C CG1 . ILE A 1 181 ? -21.245 -30.868 -12.814 1.00   51.41  ? 181  ILE B CG1 1 
ATOM   1363 C CG2 . ILE A 1 181 ? -22.375 -32.693 -14.138 1.00   50.11  ? 181  ILE B CG2 1 
ATOM   1364 C CD1 . ILE A 1 181 ? -19.965 -31.711 -12.833 1.00   51.20  ? 181  ILE B CD1 1 
ATOM   1365 N N   . ALA A 1 182 ? -25.679 -31.907 -12.563 1.00   50.52  ? 182  ALA B N   1 
ATOM   1366 C CA  . ALA A 1 182 ? -26.937 -32.637 -12.709 1.00   50.85  ? 182  ALA B CA  1 
ATOM   1367 C C   . ALA A 1 182 ? -27.973 -31.841 -13.505 1.00   51.28  ? 182  ALA B C   1 
ATOM   1368 O O   . ALA A 1 182 ? -28.656 -32.401 -14.360 1.00   51.30  ? 182  ALA B O   1 
ATOM   1369 C CB  . ALA A 1 182 ? -27.498 -33.042 -11.350 1.00   50.41  ? 182  ALA B CB  1 
ATOM   1370 N N   . ASP A 1 183 ? -28.082 -30.544 -13.230 0.86   51.71  ? 183  ASP B N   1 
ATOM   1371 C CA  . ASP A 1 183 ? -29.049 -29.706 -13.937 0.86   52.71  ? 183  ASP B CA  1 
ATOM   1372 C C   . ASP A 1 183 ? -28.725 -29.608 -15.420 0.86   53.20  ? 183  ASP B C   1 
ATOM   1373 O O   . ASP A 1 183 ? -29.611 -29.782 -16.257 0.86   52.90  ? 183  ASP B O   1 
ATOM   1374 C CB  . ASP A 1 183 ? -29.151 -28.317 -13.309 0.86   52.46  ? 183  ASP B CB  1 
ATOM   1375 C CG  . ASP A 1 183 ? -29.860 -28.334 -11.967 0.86   53.58  ? 183  ASP B CG  1 
ATOM   1376 O OD1 . ASP A 1 183 ? -30.460 -29.370 -11.598 0.86   54.67  ? 183  ASP B OD1 1 
ATOM   1377 O OD2 . ASP A 1 183 ? -29.817 -27.297 -11.272 0.86   55.24  ? 183  ASP B OD2 1 
ATOM   1378 N N   . ARG A 1 184 ? -27.460 -29.354 -15.747 1.00   54.66  ? 184  ARG B N   1 
ATOM   1379 C CA  . ARG A 1 184 ? -27.050 -29.285 -17.149 1.00   56.15  ? 184  ARG B CA  1 
ATOM   1380 C C   . ARG A 1 184 ? -27.364 -30.570 -17.900 1.00   56.02  ? 184  ARG B C   1 
ATOM   1381 O O   . ARG A 1 184 ? -27.961 -30.527 -18.973 1.00   56.26  ? 184  ARG B O   1 
ATOM   1382 C CB  . ARG A 1 184 ? -25.575 -28.911 -17.287 1.00   56.72  ? 184  ARG B CB  1 
ATOM   1383 C CG  . ARG A 1 184 ? -25.341 -27.429 -17.058 1.00   59.64  ? 184  ARG B CG  1 
ATOM   1384 C CD  . ARG A 1 184 ? -24.064 -26.948 -17.743 1.00   63.99  ? 184  ARG B CD  1 
ATOM   1385 N NE  . ARG A 1 184 ? -23.704 -25.589 -17.333 1.00   67.49  ? 184  ARG B NE  1 
ATOM   1386 C CZ  . ARG A 1 184 ? -23.523 -25.197 -16.070 1.00   69.44  ? 184  ARG B CZ  1 
ATOM   1387 N NH1 . ARG A 1 184 ? -23.690 -26.046 -15.059 1.00   70.07  ? 184  ARG B NH1 1 
ATOM   1388 N NH2 . ARG A 1 184 ? -23.189 -23.942 -15.808 1.00   70.04  ? 184  ARG B NH2 1 
ATOM   1389 N N   . LEU A 1 185 ? -26.984 -31.710 -17.324 1.00   55.57  ? 185  LEU B N   1 
ATOM   1390 C CA  . LEU A 1 185 ? -27.276 -33.006 -17.929 1.00   55.07  ? 185  LEU B CA  1 
ATOM   1391 C C   . LEU A 1 185 ? -28.760 -33.363 -17.831 1.00   55.00  ? 185  LEU B C   1 
ATOM   1392 O O   . LEU A 1 185 ? -29.224 -34.261 -18.531 1.00   54.89  ? 185  LEU B O   1 
ATOM   1393 C CB  . LEU A 1 185 ? -26.427 -34.116 -17.297 1.00   54.62  ? 185  LEU B CB  1 
ATOM   1394 C CG  . LEU A 1 185 ? -24.917 -34.130 -17.557 1.00   54.06  ? 185  LEU B CG  1 
ATOM   1395 C CD1 . LEU A 1 185 ? -24.212 -35.143 -16.660 1.00   52.61  ? 185  LEU B CD1 1 
ATOM   1396 C CD2 . LEU A 1 185 ? -24.604 -34.412 -19.019 1.00   53.69  ? 185  LEU B CD2 1 
ATOM   1397 N N   . ASN A 1 186 ? -29.492 -32.648 -16.977 1.00   54.93  ? 186  ASN B N   1 
ATOM   1398 C CA  . ASN A 1 186 ? -30.901 -32.945 -16.690 1.00   54.81  ? 186  ASN B CA  1 
ATOM   1399 C C   . ASN A 1 186 ? -31.076 -34.339 -16.081 1.00   54.25  ? 186  ASN B C   1 
ATOM   1400 O O   . ASN A 1 186 ? -31.923 -35.126 -16.511 1.00   54.29  ? 186  ASN B O   1 
ATOM   1401 C CB  . ASN A 1 186 ? -31.783 -32.764 -17.939 1.00   55.12  ? 186  ASN B CB  1 
ATOM   1402 C CG  . ASN A 1 186 ? -33.269 -32.851 -17.627 1.00   56.09  ? 186  ASN B CG  1 
ATOM   1403 O OD1 . ASN A 1 186 ? -34.017 -33.554 -18.309 1.00   57.89  ? 186  ASN B OD1 1 
ATOM   1404 N ND2 . ASN A 1 186 ? -33.705 -32.143 -16.586 1.00   55.54  ? 186  ASN B ND2 1 
ATOM   1405 N N   . VAL A 1 187 ? -30.256 -34.632 -15.076 1.00   53.33  ? 187  VAL B N   1 
ATOM   1406 C CA  . VAL A 1 187 ? -30.312 -35.905 -14.362 1.00   52.13  ? 187  VAL B CA  1 
ATOM   1407 C C   . VAL A 1 187 ? -30.426 -35.637 -12.866 1.00   52.15  ? 187  VAL B C   1 
ATOM   1408 O O   . VAL A 1 187 ? -30.554 -34.486 -12.444 1.00   52.37  ? 187  VAL B O   1 
ATOM   1409 C CB  . VAL A 1 187 ? -29.067 -36.779 -14.654 1.00   52.10  ? 187  VAL B CB  1 
ATOM   1410 C CG1 . VAL A 1 187 ? -28.926 -37.018 -16.150 1.00   51.19  ? 187  VAL B CG1 1 
ATOM   1411 C CG2 . VAL A 1 187 ? -27.793 -36.135 -14.082 1.00   49.75  ? 187  VAL B CG2 1 
ATOM   1412 N N   . ASP A 1 188 ? -30.368 -36.698 -12.068 1.00   51.70  ? 188  ASP B N   1 
ATOM   1413 C CA  . ASP A 1 188 ? -30.455 -36.576 -10.619 1.00   51.11  ? 188  ASP B CA  1 
ATOM   1414 C C   . ASP A 1 188 ? -29.103 -36.250 -9.988  1.00   50.09  ? 188  ASP B C   1 
ATOM   1415 O O   . ASP A 1 188 ? -28.050 -36.386 -10.615 1.00   49.85  ? 188  ASP B O   1 
ATOM   1416 C CB  . ASP A 1 188 ? -31.013 -37.867 -10.015 1.00   51.80  ? 188  ASP B CB  1 
ATOM   1417 C CG  . ASP A 1 188 ? -32.437 -38.162 -10.465 1.00   53.96  ? 188  ASP B CG  1 
ATOM   1418 O OD1 . ASP A 1 188 ? -33.114 -37.259 -11.001 1.00   56.41  ? 188  ASP B OD1 1 
ATOM   1419 O OD2 . ASP A 1 188 ? -32.887 -39.309 -10.276 1.00   56.56  ? 188  ASP B OD2 1 
ATOM   1420 N N   . PHE A 1 189 ? -29.151 -35.803 -8.741  1.00   48.96  ? 189  PHE B N   1 
ATOM   1421 C CA  . PHE A 1 189 ? -27.952 -35.605 -7.958  1.00   48.10  ? 189  PHE B CA  1 
ATOM   1422 C C   . PHE A 1 189 ? -28.208 -36.250 -6.615  1.00   47.25  ? 189  PHE B C   1 
ATOM   1423 O O   . PHE A 1 189 ? -29.360 -36.418 -6.207  1.00   46.60  ? 189  PHE B O   1 
ATOM   1424 C CB  . PHE A 1 189 ? -27.641 -34.115 -7.785  1.00   48.29  ? 189  PHE B CB  1 
ATOM   1425 C CG  . PHE A 1 189 ? -28.475 -33.444 -6.733  1.00   49.34  ? 189  PHE B CG  1 
ATOM   1426 C CD1 . PHE A 1 189 ? -28.059 -33.432 -5.403  1.00   50.66  ? 189  PHE B CD1 1 
ATOM   1427 C CD2 . PHE A 1 189 ? -29.681 -32.843 -7.064  1.00   51.03  ? 189  PHE B CD2 1 
ATOM   1428 C CE1 . PHE A 1 189 ? -28.827 -32.828 -4.421  1.00   52.11  ? 189  PHE B CE1 1 
ATOM   1429 C CE2 . PHE A 1 189 ? -30.460 -32.229 -6.089  1.00   52.42  ? 189  PHE B CE2 1 
ATOM   1430 C CZ  . PHE A 1 189 ? -30.033 -32.222 -4.765  1.00   52.67  ? 189  PHE B CZ  1 
ATOM   1431 N N   . ALA A 1 190 ? -27.135 -36.622 -5.935  1.00   46.44  ? 190  ALA B N   1 
ATOM   1432 C CA  . ALA A 1 190 ? -27.241 -37.135 -4.580  1.00   46.60  ? 190  ALA B CA  1 
ATOM   1433 C C   . ALA A 1 190 ? -26.068 -36.600 -3.786  1.00   46.65  ? 190  ALA B C   1 
ATOM   1434 O O   . ALA A 1 190 ? -25.165 -35.973 -4.342  1.00   46.73  ? 190  ALA B O   1 
ATOM   1435 C CB  . ALA A 1 190 ? -27.256 -38.663 -4.575  1.00   46.13  ? 190  ALA B CB  1 
ATOM   1436 N N   . LEU A 1 191 ? -26.073 -36.849 -2.486  1.00   47.29  ? 191  LEU B N   1 
ATOM   1437 C CA  . LEU A 1 191 ? -25.079 -36.240 -1.618  1.00   47.73  ? 191  LEU B CA  1 
ATOM   1438 C C   . LEU A 1 191 ? -24.692 -37.161 -0.477  1.00   47.11  ? 191  LEU B C   1 
ATOM   1439 O O   . LEU A 1 191 ? -25.550 -37.700 0.219   1.00   47.00  ? 191  LEU B O   1 
ATOM   1440 C CB  . LEU A 1 191 ? -25.619 -34.914 -1.079  1.00   48.46  ? 191  LEU B CB  1 
ATOM   1441 C CG  . LEU A 1 191 ? -24.643 -33.956 -0.402  1.00   50.53  ? 191  LEU B CG  1 
ATOM   1442 C CD1 . LEU A 1 191 ? -24.904 -32.543 -0.897  1.00   52.25  ? 191  LEU B CD1 1 
ATOM   1443 C CD2 . LEU A 1 191 ? -24.744 -34.040 1.122   1.00   51.42  ? 191  LEU B CD2 1 
ATOM   1444 N N   . ILE A 1 192 ? -23.389 -37.331 -0.298  1.00   45.87  ? 192  ILE B N   1 
ATOM   1445 C CA  . ILE A 1 192 ? -22.862 -38.087 0.816   1.00   46.76  ? 192  ILE B CA  1 
ATOM   1446 C C   . ILE A 1 192 ? -22.379 -37.124 1.881   1.00   47.53  ? 192  ILE B C   1 
ATOM   1447 O O   . ILE A 1 192 ? -21.762 -36.110 1.573   1.00   47.52  ? 192  ILE B O   1 
ATOM   1448 C CB  . ILE A 1 192 ? -21.714 -39.005 0.368   1.00   46.36  ? 192  ILE B CB  1 
ATOM   1449 C CG1 . ILE A 1 192 ? -22.284 -40.172 -0.449  1.00   46.71  ? 192  ILE B CG1 1 
ATOM   1450 C CG2 . ILE A 1 192 ? -20.916 -39.521 1.578   1.00   46.48  ? 192  ILE B CG2 1 
ATOM   1451 C CD1 . ILE A 1 192 ? -21.264 -40.966 -1.194  1.00   46.38  ? 192  ILE B CD1 1 
ATOM   1452 N N   . HIS A 1 193 ? -22.669 -37.444 3.133   1.00   49.00  ? 193  HIS B N   1 
ATOM   1453 C CA  . HIS A 1 193 ? -22.185 -36.650 4.242   1.00   50.65  ? 193  HIS B CA  1 
ATOM   1454 C C   . HIS A 1 193 ? -21.537 -37.570 5.262   1.00   51.59  ? 193  HIS B C   1 
ATOM   1455 O O   . HIS A 1 193 ? -22.170 -38.507 5.755   1.00   51.77  ? 193  HIS B O   1 
ATOM   1456 C CB  . HIS A 1 193 ? -23.336 -35.845 4.853   1.00   50.94  ? 193  HIS B CB  1 
ATOM   1457 C CG  . HIS A 1 193 ? -23.031 -35.288 6.206   1.00   52.04  ? 193  HIS B CG  1 
ATOM   1458 N ND1 . HIS A 1 193 ? -21.902 -34.544 6.466   1.00   53.59  ? 193  HIS B ND1 1 
ATOM   1459 C CD2 . HIS A 1 193 ? -23.709 -35.366 7.375   1.00   53.38  ? 193  HIS B CD2 1 
ATOM   1460 C CE1 . HIS A 1 193 ? -21.893 -34.193 7.740   1.00   54.38  ? 193  HIS B CE1 1 
ATOM   1461 N NE2 . HIS A 1 193 ? -22.979 -34.679 8.314   1.00   54.05  ? 193  HIS B NE2 1 
ATOM   1462 N N   . LYS A 1 194 ? -20.267 -37.316 5.556   0.60   52.57  ? 194  LYS B N   1 
ATOM   1463 C CA  . LYS A 1 194 ? -19.548 -38.094 6.552   0.60   55.05  ? 194  LYS B CA  1 
ATOM   1464 C C   . LYS A 1 194 ? -19.760 -37.500 7.943   0.60   58.10  ? 194  LYS B C   1 
ATOM   1465 O O   . LYS A 1 194 ? -19.440 -36.332 8.187   0.60   57.15  ? 194  LYS B O   1 
ATOM   1466 C CB  . LYS A 1 194 ? -18.055 -38.169 6.215   0.60   54.37  ? 194  LYS B CB  1 
ATOM   1467 C CG  . LYS A 1 194 ? -17.256 -39.072 7.144   0.60   54.79  ? 194  LYS B CG  1 
ATOM   1468 C CD  . LYS A 1 194 ? -16.001 -39.593 6.467   0.60   55.49  ? 194  LYS B CD  1 
ATOM   1469 C CE  . LYS A 1 194 ? -15.491 -40.847 7.168   0.60   56.50  ? 194  LYS B CE  1 
ATOM   1470 N NZ  . LYS A 1 194 ? -14.496 -41.608 6.345   0.60   56.63  ? 194  LYS B NZ  1 
ATOM   1471 N N   . GLU A 1 195 ? -20.311 -38.311 8.841   1.00   69.09  ? 195  GLU B N   1 
ATOM   1472 C CA  . GLU A 1 195 ? -20.514 -37.920 10.233  1.00   77.36  ? 195  GLU B CA  1 
ATOM   1473 C C   . GLU A 1 195 ? -19.263 -38.196 11.065  1.00   78.33  ? 195  GLU B C   1 
ATOM   1474 O O   . GLU A 1 195 ? -18.313 -37.409 11.063  1.00   78.63  ? 195  GLU B O   1 
ATOM   1475 C CB  . GLU A 1 195 ? -21.707 -38.667 10.827  1.00   71.95  ? 195  GLU B CB  1 
ATOM   1476 C CG  . GLU A 1 195 ? -23.056 -38.242 10.264  1.00   75.10  ? 195  GLU B CG  1 
ATOM   1477 C CD  . GLU A 1 195 ? -24.067 -39.373 10.265  1.00   86.15  ? 195  GLU B CD  1 
ATOM   1478 O OE1 . GLU A 1 195 ? -23.667 -40.537 10.035  1.00   91.97  ? 195  GLU B OE1 1 
ATOM   1479 O OE2 . GLU A 1 195 ? -25.266 -39.100 10.486  1.00   88.79  ? 195  GLU B OE2 1 
ATOM   1480 N N   . ASP A 1 203 ? -18.165 -42.210 12.508  0.42   68.84  ? 203  ASP B N   1 
ATOM   1481 C CA  . ASP A 1 203 ? -17.210 -42.483 11.442  0.42   68.37  ? 203  ASP B CA  1 
ATOM   1482 C C   . ASP A 1 203 ? -17.946 -43.050 10.232  0.42   66.70  ? 203  ASP B C   1 
ATOM   1483 O O   . ASP A 1 203 ? -17.422 -43.905 9.518   0.42   66.86  ? 203  ASP B O   1 
ATOM   1484 C CB  . ASP A 1 203 ? -16.157 -43.486 11.922  0.42   69.23  ? 203  ASP B CB  1 
ATOM   1485 C CG  . ASP A 1 203 ? -14.750 -43.098 11.509  0.42   70.32  ? 203  ASP B CG  1 
ATOM   1486 O OD1 . ASP A 1 203 ? -14.273 -43.594 10.465  0.42   71.06  ? 203  ASP B OD1 1 
ATOM   1487 O OD2 . ASP A 1 203 ? -14.124 -42.289 12.228  0.42   71.18  ? 203  ASP B OD2 1 
ATOM   1488 N N   . ARG A 1 204 ? -19.162 -42.559 10.005  0.36   63.75  ? 204  ARG B N   1 
ATOM   1489 C CA  . ARG A 1 204 ? -20.048 -43.131 8.993   0.36   60.72  ? 204  ARG B CA  1 
ATOM   1490 C C   . ARG A 1 204 ? -20.475 -42.132 7.921   0.36   59.10  ? 204  ARG B C   1 
ATOM   1491 O O   . ARG A 1 204 ? -20.415 -40.920 8.125   0.36   58.56  ? 204  ARG B O   1 
ATOM   1492 C CB  . ARG A 1 204 ? -21.298 -43.721 9.655   0.36   60.49  ? 204  ARG B CB  1 
ATOM   1493 C CG  . ARG A 1 204 ? -21.084 -45.063 10.333  0.36   60.29  ? 204  ARG B CG  1 
ATOM   1494 C CD  . ARG A 1 204 ? -20.618 -46.119 9.339   0.36   59.83  ? 204  ARG B CD  1 
ATOM   1495 N NE  . ARG A 1 204 ? -21.597 -46.391 8.285   0.36   60.04  ? 204  ARG B NE  1 
ATOM   1496 C CZ  . ARG A 1 204 ? -22.908 -46.179 8.386   0.36   60.10  ? 204  ARG B CZ  1 
ATOM   1497 N NH1 . ARG A 1 204 ? -23.426 -45.687 9.506   0.36   60.17  ? 204  ARG B NH1 1 
ATOM   1498 N NH2 . ARG A 1 204 ? -23.704 -46.464 7.361   0.36   60.17  ? 204  ARG B NH2 1 
ATOM   1499 N N   . MET A 1 205 ? -20.915 -42.665 6.784   1.00   57.52  ? 205  MET B N   1 
ATOM   1500 C CA  . MET A 1 205 ? -21.434 -41.863 5.687   1.00   56.56  ? 205  MET B CA  1 
ATOM   1501 C C   . MET A 1 205 ? -22.938 -42.016 5.564   1.00   55.82  ? 205  MET B C   1 
ATOM   1502 O O   . MET A 1 205 ? -23.477 -43.119 5.694   1.00   56.01  ? 205  MET B O   1 
ATOM   1503 C CB  . MET A 1 205 ? -20.775 -42.270 4.368   1.00   56.47  ? 205  MET B CB  1 
ATOM   1504 C CG  . MET A 1 205 ? -19.350 -41.793 4.234   1.00   55.99  ? 205  MET B CG  1 
ATOM   1505 S SD  . MET A 1 205 ? -18.594 -42.320 2.695   1.00   54.81  ? 205  MET B SD  1 
ATOM   1506 C CE  . MET A 1 205 ? -17.197 -41.201 2.630   1.00   55.96  ? 205  MET B CE  1 
ATOM   1507 N N   . VAL A 1 206 ? -23.615 -40.904 5.322   1.00   54.78  ? 206  VAL B N   1 
ATOM   1508 C CA  . VAL A 1 206 ? -25.030 -40.948 4.993   1.00   54.13  ? 206  VAL B CA  1 
ATOM   1509 C C   . VAL A 1 206 ? -25.233 -40.424 3.583   1.00   53.71  ? 206  VAL B C   1 
ATOM   1510 O O   . VAL A 1 206 ? -24.595 -39.452 3.168   1.00   53.69  ? 206  VAL B O   1 
ATOM   1511 C CB  . VAL A 1 206 ? -25.911 -40.179 6.004   1.00   54.12  ? 206  VAL B CB  1 
ATOM   1512 C CG1 . VAL A 1 206 ? -25.790 -40.798 7.395   1.00   54.73  ? 206  VAL B CG1 1 
ATOM   1513 C CG2 . VAL A 1 206 ? -25.543 -38.717 6.046   1.00   54.14  ? 206  VAL B CG2 1 
ATOM   1514 N N   . LEU A 1 207 ? -26.104 -41.094 2.843   1.00   53.16  ? 207  LEU B N   1 
ATOM   1515 C CA  . LEU A 1 207 ? -26.400 -40.705 1.484   1.00   52.84  ? 207  LEU B CA  1 
ATOM   1516 C C   . LEU A 1 207 ? -27.826 -40.201 1.421   1.00   52.86  ? 207  LEU B C   1 
ATOM   1517 O O   . LEU A 1 207 ? -28.731 -40.812 2.002   1.00   52.94  ? 207  LEU B O   1 
ATOM   1518 C CB  . LEU A 1 207 ? -26.223 -41.895 0.544   1.00   52.83  ? 207  LEU B CB  1 
ATOM   1519 C CG  . LEU A 1 207 ? -26.643 -41.718 -0.919  1.00   52.56  ? 207  LEU B CG  1 
ATOM   1520 C CD1 . LEU A 1 207 ? -25.708 -40.783 -1.677  1.00   50.44  ? 207  LEU B CD1 1 
ATOM   1521 C CD2 . LEU A 1 207 ? -26.716 -43.070 -1.609  1.00   53.28  ? 207  LEU B CD2 1 
ATOM   1522 N N   . VAL A 1 208 ? -28.016 -39.080 0.732   1.00   52.41  ? 208  VAL B N   1 
ATOM   1523 C CA  . VAL A 1 208 ? -29.351 -38.575 0.424   1.00   52.16  ? 208  VAL B CA  1 
ATOM   1524 C C   . VAL A 1 208 ? -29.480 -38.359 -1.085  1.00   51.89  ? 208  VAL B C   1 
ATOM   1525 O O   . VAL A 1 208 ? -28.546 -37.889 -1.736  1.00   52.30  ? 208  VAL B O   1 
ATOM   1526 C CB  . VAL A 1 208 ? -29.697 -37.288 1.224   1.00   52.28  ? 208  VAL B CB  1 
ATOM   1527 C CG1 . VAL A 1 208 ? -29.728 -37.585 2.724   1.00   52.55  ? 208  VAL B CG1 1 
ATOM   1528 C CG2 . VAL A 1 208 ? -28.712 -36.155 0.924   1.00   51.97  ? 208  VAL B CG2 1 
ATOM   1529 N N   . GLY A 1 209 ? -30.638 -38.710 -1.633  1.00   51.46  ? 209  GLY B N   1 
ATOM   1530 C CA  . GLY A 1 209 ? -30.858 -38.675 -3.078  1.00   51.27  ? 209  GLY B CA  1 
ATOM   1531 C C   . GLY A 1 209 ? -30.891 -40.096 -3.610  1.00   51.21  ? 209  GLY B C   1 
ATOM   1532 O O   . GLY A 1 209 ? -30.372 -41.016 -2.972  1.00   51.18  ? 209  GLY B O   1 
ATOM   1533 N N   . ASP A 1 210 ? -31.495 -40.283 -4.779  0.55   50.94  ? 210  ASP B N   1 
ATOM   1534 C CA  . ASP A 1 210 ? -31.656 -41.626 -5.326  0.55   50.55  ? 210  ASP B CA  1 
ATOM   1535 C C   . ASP A 1 210 ? -30.537 -42.005 -6.285  0.55   49.82  ? 210  ASP B C   1 
ATOM   1536 O O   . ASP A 1 210 ? -30.196 -41.248 -7.194  0.55   49.17  ? 210  ASP B O   1 
ATOM   1537 C CB  . ASP A 1 210 ? -33.012 -41.784 -6.015  0.55   50.99  ? 210  ASP B CB  1 
ATOM   1538 C CG  . ASP A 1 210 ? -33.331 -43.233 -6.338  0.55   52.05  ? 210  ASP B CG  1 
ATOM   1539 O OD1 . ASP A 1 210 ? -33.408 -43.567 -7.539  0.55   52.99  ? 210  ASP B OD1 1 
ATOM   1540 O OD2 . ASP A 1 210 ? -33.486 -44.041 -5.393  0.55   53.45  ? 210  ASP B OD2 1 
ATOM   1541 N N   . VAL A 1 211 ? -29.974 -43.186 -6.068  1.00   49.38  ? 211  VAL B N   1 
ATOM   1542 C CA  . VAL A 1 211 ? -28.922 -43.718 -6.931  1.00   49.63  ? 211  VAL B CA  1 
ATOM   1543 C C   . VAL A 1 211 ? -29.258 -45.138 -7.384  1.00   50.06  ? 211  VAL B C   1 
ATOM   1544 O O   . VAL A 1 211 ? -28.509 -45.749 -8.159  1.00   48.81  ? 211  VAL B O   1 
ATOM   1545 C CB  . VAL A 1 211 ? -27.547 -43.726 -6.223  1.00   49.52  ? 211  VAL B CB  1 
ATOM   1546 C CG1 . VAL A 1 211 ? -27.110 -42.298 -5.853  1.00   49.24  ? 211  VAL B CG1 1 
ATOM   1547 C CG2 . VAL A 1 211 ? -27.577 -44.620 -4.992  1.00   48.76  ? 211  VAL B CG2 1 
ATOM   1548 N N   . LYS A 1 212 ? -30.381 -45.658 -6.894  0.76   51.34  ? 212  LYS B N   1 
ATOM   1549 C CA  . LYS A 1 212 ? -30.718 -47.063 -7.111  0.76   53.21  ? 212  LYS B CA  1 
ATOM   1550 C C   . LYS A 1 212 ? -30.905 -47.389 -8.585  0.76   54.03  ? 212  LYS B C   1 
ATOM   1551 O O   . LYS A 1 212 ? -31.672 -46.726 -9.288  0.76   53.71  ? 212  LYS B O   1 
ATOM   1552 C CB  . LYS A 1 212 ? -31.949 -47.487 -6.303  0.76   53.34  ? 212  LYS B CB  1 
ATOM   1553 C CG  . LYS A 1 212 ? -32.381 -48.925 -6.597  0.76   55.11  ? 212  LYS B CG  1 
ATOM   1554 C CD  . LYS A 1 212 ? -33.295 -49.496 -5.529  0.76   58.01  ? 212  LYS B CD  1 
ATOM   1555 C CE  . LYS A 1 212 ? -33.446 -51.007 -5.695  0.76   59.60  ? 212  LYS B CE  1 
ATOM   1556 N NZ  . LYS A 1 212 ? -32.136 -51.737 -5.646  0.76   60.59  ? 212  LYS B NZ  1 
ATOM   1557 N N   . ASP A 1 213 ? -30.174 -48.410 -9.029  0.97   55.86  ? 213  ASP B N   1 
ATOM   1558 C CA  . ASP A 1 213 ? -30.218 -48.915 -10.401 0.97   57.41  ? 213  ASP B CA  1 
ATOM   1559 C C   . ASP A 1 213 ? -29.811 -47.882 -11.447 0.97   56.96  ? 213  ASP B C   1 
ATOM   1560 O O   . ASP A 1 213 ? -30.201 -47.968 -12.616 0.97   57.36  ? 213  ASP B O   1 
ATOM   1561 C CB  . ASP A 1 213 ? -31.588 -49.528 -10.718 0.97   58.22  ? 213  ASP B CB  1 
ATOM   1562 C CG  . ASP A 1 213 ? -31.838 -50.817 -9.956  0.97   61.97  ? 213  ASP B CG  1 
ATOM   1563 O OD1 . ASP A 1 213 ? -32.984 -51.024 -9.507  0.97   62.66  ? 213  ASP B OD1 1 
ATOM   1564 O OD2 . ASP A 1 213 ? -30.891 -51.622 -9.799  0.97   62.44  ? 213  ASP B OD2 1 
ATOM   1565 N N   . ARG A 1 214 ? -29.011 -46.916 -11.011 0.87   55.63  ? 214  ARG B N   1 
ATOM   1566 C CA  . ARG A 1 214 ? -28.454 -45.906 -11.895 0.87   53.83  ? 214  ARG B CA  1 
ATOM   1567 C C   . ARG A 1 214 ? -26.940 -45.938 -11.814 0.87   51.68  ? 214  ARG B C   1 
ATOM   1568 O O   . ARG A 1 214 ? -26.365 -46.413 -10.833 0.87   51.09  ? 214  ARG B O   1 
ATOM   1569 C CB  . ARG A 1 214 ? -28.950 -44.520 -11.489 0.87   54.30  ? 214  ARG B CB  1 
ATOM   1570 C CG  . ARG A 1 214 ? -30.453 -44.386 -11.491 0.87   56.42  ? 214  ARG B CG  1 
ATOM   1571 C CD  . ARG A 1 214 ? -30.898 -43.089 -10.857 0.87   59.14  ? 214  ARG B CD  1 
ATOM   1572 N NE  . ARG A 1 214 ? -32.047 -42.564 -11.580 0.87   62.63  ? 214  ARG B NE  1 
ATOM   1573 C CZ  . ARG A 1 214 ? -31.997 -41.552 -12.441 0.87   63.90  ? 214  ARG B CZ  1 
ATOM   1574 N NH1 . ARG A 1 214 ? -30.856 -40.911 -12.670 0.87   64.70  ? 214  ARG B NH1 1 
ATOM   1575 N NH2 . ARG A 1 214 ? -33.103 -41.161 -13.058 0.87   64.62  ? 214  ARG B NH2 1 
ATOM   1576 N N   . VAL A 1 215 ? -26.294 -45.434 -12.854 1.00   49.19  ? 215  VAL B N   1 
ATOM   1577 C CA  . VAL A 1 215 ? -24.863 -45.186 -12.803 1.00   47.02  ? 215  VAL B CA  1 
ATOM   1578 C C   . VAL A 1 215 ? -24.639 -43.974 -11.887 1.00   46.13  ? 215  VAL B C   1 
ATOM   1579 O O   . VAL A 1 215 ? -25.339 -42.969 -12.001 1.00   46.07  ? 215  VAL B O   1 
ATOM   1580 C CB  . VAL A 1 215 ? -24.316 -44.936 -14.214 1.00   46.80  ? 215  VAL B CB  1 
ATOM   1581 C CG1 . VAL A 1 215 ? -22.850 -44.533 -14.181 1.00   46.36  ? 215  VAL B CG1 1 
ATOM   1582 C CG2 . VAL A 1 215 ? -24.520 -46.185 -15.075 1.00   45.89  ? 215  VAL B CG2 1 
ATOM   1583 N N   . ALA A 1 216 ? -23.701 -44.093 -10.953 1.00   44.54  ? 216  ALA B N   1 
ATOM   1584 C CA  . ALA A 1 216 ? -23.364 -42.987 -10.059 1.00   43.82  ? 216  ALA B CA  1 
ATOM   1585 C C   . ALA A 1 216 ? -22.006 -42.410 -10.424 1.00   43.49  ? 216  ALA B C   1 
ATOM   1586 O O   . ALA A 1 216 ? -21.032 -43.147 -10.598 1.00   43.14  ? 216  ALA B O   1 
ATOM   1587 C CB  . ALA A 1 216 ? -23.388 -43.432 -8.595  1.00   43.27  ? 216  ALA B CB  1 
ATOM   1588 N N   . ILE A 1 217 ? -21.961 -41.086 -10.548 1.00   42.87  ? 217  ILE B N   1 
ATOM   1589 C CA  . ILE A 1 217 ? -20.735 -40.375 -10.874 1.00   42.35  ? 217  ILE B CA  1 
ATOM   1590 C C   . ILE A 1 217 ? -20.384 -39.450 -9.721  1.00   41.85  ? 217  ILE B C   1 
ATOM   1591 O O   . ILE A 1 217 ? -21.073 -38.446 -9.485  1.00   41.57  ? 217  ILE B O   1 
ATOM   1592 C CB  . ILE A 1 217 ? -20.875 -39.544 -12.174 1.00   42.41  ? 217  ILE B CB  1 
ATOM   1593 C CG1 . ILE A 1 217 ? -21.605 -40.361 -13.254 1.00   42.71  ? 217  ILE B CG1 1 
ATOM   1594 C CG2 . ILE A 1 217 ? -19.497 -39.049 -12.643 1.00   42.00  ? 217  ILE B CG2 1 
ATOM   1595 C CD1 . ILE A 1 217 ? -21.701 -39.678 -14.602 1.00   43.80  ? 217  ILE B CD1 1 
ATOM   1596 N N   . LEU A 1 218 ? -19.326 -39.802 -8.998  1.00   40.64  ? 218  LEU B N   1 
ATOM   1597 C CA  . LEU A 1 218 ? -18.807 -38.951 -7.940  1.00   41.29  ? 218  LEU B CA  1 
ATOM   1598 C C   . LEU A 1 218 ? -18.003 -37.842 -8.592  1.00   42.22  ? 218  LEU B C   1 
ATOM   1599 O O   . LEU A 1 218 ? -17.065 -38.103 -9.346  1.00   41.77  ? 218  LEU B O   1 
ATOM   1600 C CB  . LEU A 1 218 ? -17.911 -39.729 -6.977  1.00   40.59  ? 218  LEU B CB  1 
ATOM   1601 C CG  . LEU A 1 218 ? -18.567 -40.568 -5.884  1.00   41.16  ? 218  LEU B CG  1 
ATOM   1602 C CD1 . LEU A 1 218 ? -17.644 -41.724 -5.470  1.00   41.65  ? 218  LEU B CD1 1 
ATOM   1603 C CD2 . LEU A 1 218 ? -18.964 -39.709 -4.685  1.00   40.13  ? 218  LEU B CD2 1 
ATOM   1604 N N   . VAL A 1 219 ? -18.393 -36.605 -8.322  1.00   43.32  ? 219  VAL B N   1 
ATOM   1605 C CA  . VAL A 1 219 ? -17.710 -35.464 -8.910  1.00   45.38  ? 219  VAL B CA  1 
ATOM   1606 C C   . VAL A 1 219 ? -17.175 -34.606 -7.787  1.00   46.54  ? 219  VAL B C   1 
ATOM   1607 O O   . VAL A 1 219 ? -17.928 -34.194 -6.907  1.00   47.19  ? 219  VAL B O   1 
ATOM   1608 C CB  . VAL A 1 219 ? -18.648 -34.631 -9.804  1.00   45.18  ? 219  VAL B CB  1 
ATOM   1609 C CG1 . VAL A 1 219 ? -17.900 -33.428 -10.382 1.00   46.24  ? 219  VAL B CG1 1 
ATOM   1610 C CG2 . VAL A 1 219 ? -19.213 -35.490 -10.926 1.00   44.90  ? 219  VAL B CG2 1 
ATOM   1611 N N   . ASP A 1 220 ? -15.872 -34.371 -7.796  1.00   48.15  ? 220  ASP B N   1 
ATOM   1612 C CA  . ASP A 1 220 ? -15.270 -33.477 -6.823  1.00   49.43  ? 220  ASP B CA  1 
ATOM   1613 C C   . ASP A 1 220 ? -14.258 -32.557 -7.500  1.00   48.96  ? 220  ASP B C   1 
ATOM   1614 O O   . ASP A 1 220 ? -13.867 -32.790 -8.649  1.00   48.67  ? 220  ASP B O   1 
ATOM   1615 C CB  . ASP A 1 220 ? -14.624 -34.274 -5.689  1.00   50.40  ? 220  ASP B CB  1 
ATOM   1616 C CG  . ASP A 1 220 ? -14.778 -33.598 -4.335  1.00   53.27  ? 220  ASP B CG  1 
ATOM   1617 O OD1 . ASP A 1 220 ? -15.802 -32.911 -4.110  1.00   56.27  ? 220  ASP B OD1 1 
ATOM   1618 O OD2 . ASP A 1 220 ? -13.878 -33.767 -3.485  1.00   55.83  ? 220  ASP B OD2 1 
ATOM   1619 N N   . ASP A 1 221 ? -13.850 -31.508 -6.791  0.77   48.01  ? 221  ASP B N   1 
ATOM   1620 C CA  . ASP A 1 221 ? -12.858 -30.573 -7.315  0.77   47.86  ? 221  ASP B CA  1 
ATOM   1621 C C   . ASP A 1 221 ? -11.465 -31.197 -7.295  0.77   48.65  ? 221  ASP B C   1 
ATOM   1622 O O   . ASP A 1 221 ? -10.657 -30.965 -8.190  0.77   47.87  ? 221  ASP B O   1 
ATOM   1623 C CB  . ASP A 1 221 ? -12.871 -29.262 -6.515  0.77   47.04  ? 221  ASP B CB  1 
ATOM   1624 C CG  . ASP A 1 221 ? -12.517 -29.464 -5.049  0.77   47.46  ? 221  ASP B CG  1 
ATOM   1625 O OD1 . ASP A 1 221 ? -13.002 -30.438 -4.426  0.77   48.75  ? 221  ASP B OD1 1 
ATOM   1626 O OD2 . ASP A 1 221 ? -11.749 -28.643 -4.514  0.77   48.57  ? 221  ASP B OD2 1 
ATOM   1627 N N   . MET A 1 222 ? -11.194 -31.997 -6.269  1.00   51.44  ? 222  MET B N   1 
ATOM   1628 C CA  . MET A 1 222 ? -9.879  -32.604 -6.092  1.00   54.40  ? 222  MET B CA  1 
ATOM   1629 C C   . MET A 1 222 ? -9.934  -33.863 -5.233  1.00   56.01  ? 222  MET B C   1 
ATOM   1630 O O   . MET A 1 222 ? -10.759 -33.973 -4.319  1.00   56.34  ? 222  MET B O   1 
ATOM   1631 C CB  . MET A 1 222 ? -8.895  -31.601 -5.480  1.00   54.80  ? 222  MET B CB  1 
ATOM   1632 C CG  . MET A 1 222 ? -9.148  -31.267 -4.011  1.00   57.29  ? 222  MET B CG  1 
ATOM   1633 S SD  . MET A 1 222 ? -7.775  -30.359 -3.274  1.00   62.53  ? 222  MET B SD  1 
ATOM   1634 C CE  . MET A 1 222 ? -8.030  -28.715 -3.963  1.00   60.83  ? 222  MET B CE  1 
ATOM   1635 N N   . ALA A 1 223 ? -9.053  -34.812 -5.540  1.00   57.81  ? 223  ALA B N   1 
ATOM   1636 C CA  . ALA A 1 223 ? -8.871  -35.997 -4.706  1.00   59.43  ? 223  ALA B CA  1 
ATOM   1637 C C   . ALA A 1 223 ? -7.420  -36.092 -4.285  1.00   60.55  ? 223  ALA B C   1 
ATOM   1638 O O   . ALA A 1 223 ? -6.515  -35.950 -5.115  1.00   60.38  ? 223  ALA B O   1 
ATOM   1639 C CB  . ALA A 1 223 ? -9.290  -37.253 -5.443  1.00   59.40  ? 223  ALA B CB  1 
ATOM   1640 N N   . ASP A 1 224 ? -7.206  -36.335 -2.991  1.00   62.42  ? 224  ASP B N   1 
ATOM   1641 C CA  . ASP A 1 224 ? -5.852  -36.359 -2.431  1.00   64.30  ? 224  ASP B CA  1 
ATOM   1642 C C   . ASP A 1 224 ? -5.365  -37.742 -1.989  1.00   65.07  ? 224  ASP B C   1 
ATOM   1643 O O   . ASP A 1 224 ? -4.484  -38.321 -2.626  1.00   65.64  ? 224  ASP B O   1 
ATOM   1644 C CB  . ASP A 1 224 ? -5.715  -35.366 -1.269  1.00   64.54  ? 224  ASP B CB  1 
ATOM   1645 C CG  . ASP A 1 224 ? -4.262  -35.132 -0.893  1.00   65.46  ? 224  ASP B CG  1 
ATOM   1646 O OD1 . ASP A 1 224 ? -3.361  -35.736 -1.518  1.00   66.03  ? 224  ASP B OD1 1 
ATOM   1647 O OD2 . ASP A 1 224 ? -4.017  -34.330 0.031   1.00   66.93  ? 224  ASP B OD2 1 
ATOM   1648 N N   . THR A 1 225 ? -5.909  -38.239 -0.876  1.00   65.77  ? 225  THR B N   1 
ATOM   1649 C CA  . THR A 1 225 ? -5.531  -39.560 -0.367  1.00   66.56  ? 225  THR B CA  1 
ATOM   1650 C C   . THR A 1 225 ? -6.584  -40.559 -0.811  1.00   66.80  ? 225  THR B C   1 
ATOM   1651 O O   . THR A 1 225 ? -6.377  -41.771 -0.736  1.00   67.12  ? 225  THR B O   1 
ATOM   1652 C CB  . THR A 1 225 ? -5.417  -39.581 1.173   1.00   66.55  ? 225  THR B CB  1 
ATOM   1653 O OG1 . THR A 1 225 ? -6.692  -39.289 1.760   1.00   66.80  ? 225  THR B OG1 1 
ATOM   1654 C CG2 . THR A 1 225 ? -4.384  -38.572 1.658   1.00   66.57  ? 225  THR B CG2 1 
ATOM   1655 N N   . CYS A 1 226 ? -7.716  -40.021 -1.266  1.00   66.82  ? 226  CYS B N   1 
ATOM   1656 C CA  . CYS A 1 226 ? -8.819  -40.794 -1.840  1.00   66.72  ? 226  CYS B CA  1 
ATOM   1657 C C   . CYS A 1 226 ? -9.582  -41.629 -0.822  1.00   66.60  ? 226  CYS B C   1 
ATOM   1658 O O   . CYS A 1 226 ? -10.470 -42.393 -1.198  1.00   66.61  ? 226  CYS B O   1 
ATOM   1659 C CB  . CYS A 1 226 ? -8.345  -41.671 -3.009  1.00   66.82  ? 226  CYS B CB  1 
ATOM   1660 S SG  . CYS A 1 226 ? -7.755  -40.733 -4.425  1.00   66.68  ? 226  CYS B SG  1 
ATOM   1661 N N   . GLY A 1 227 ? -9.243  -41.479 0.456   1.00   66.45  ? 227  GLY B N   1 
ATOM   1662 C CA  . GLY A 1 227 ? -9.976  -42.142 1.528   1.00   66.04  ? 227  GLY B CA  1 
ATOM   1663 C C   . GLY A 1 227 ? -11.471 -41.935 1.370   1.00   65.69  ? 227  GLY B C   1 
ATOM   1664 O O   . GLY A 1 227 ? -12.252 -42.885 1.467   1.00   65.61  ? 227  GLY B O   1 
ATOM   1665 N N   . THR A 1 228 ? -11.863 -40.695 1.086   1.00   64.90  ? 228  THR B N   1 
ATOM   1666 C CA  . THR A 1 228 ? -13.273 -40.333 0.977   1.00   63.78  ? 228  THR B CA  1 
ATOM   1667 C C   . THR A 1 228 ? -13.966 -40.944 -0.248  1.00   62.12  ? 228  THR B C   1 
ATOM   1668 O O   . THR A 1 228 ? -14.978 -41.635 -0.097  1.00   61.83  ? 228  THR B O   1 
ATOM   1669 C CB  . THR A 1 228 ? -13.481 -38.795 1.024   1.00   64.27  ? 228  THR B CB  1 
ATOM   1670 O OG1 . THR A 1 228 ? -12.895 -38.267 2.222   1.00   64.78  ? 228  THR B OG1 1 
ATOM   1671 C CG2 . THR A 1 228 ? -14.969 -38.440 1.000   1.00   64.33  ? 228  THR B CG2 1 
ATOM   1672 N N   . ILE A 1 229 ? -13.432 -40.703 -1.446  1.00   59.62  ? 229  ILE B N   1 
ATOM   1673 C CA  . ILE A 1 229 ? -14.077 -41.216 -2.663  1.00   58.00  ? 229  ILE B CA  1 
ATOM   1674 C C   . ILE A 1 229 ? -14.193 -42.742 -2.676  1.00   56.53  ? 229  ILE B C   1 
ATOM   1675 O O   . ILE A 1 229 ? -15.171 -43.281 -3.195  1.00   56.16  ? 229  ILE B O   1 
ATOM   1676 C CB  . ILE A 1 229 ? -13.428 -40.715 -3.988  1.00   58.01  ? 229  ILE B CB  1 
ATOM   1677 C CG1 . ILE A 1 229 ? -11.906 -40.893 -3.971  1.00   57.90  ? 229  ILE B CG1 1 
ATOM   1678 C CG2 . ILE A 1 229 ? -13.831 -39.266 -4.264  1.00   58.54  ? 229  ILE B CG2 1 
ATOM   1679 C CD1 . ILE A 1 229 ? -11.287 -40.994 -5.361  1.00   57.68  ? 229  ILE B CD1 1 
ATOM   1680 N N   . CYS A 1 230 ? -13.209 -43.425 -2.096  1.00   54.65  ? 230  CYS B N   1 
ATOM   1681 C CA  . CYS A 1 230 ? -13.248 -44.885 -2.007  1.00   52.86  ? 230  CYS B CA  1 
ATOM   1682 C C   . CYS A 1 230 ? -14.405 -45.384 -1.146  1.00   50.14  ? 230  CYS B C   1 
ATOM   1683 O O   . CYS A 1 230 ? -15.165 -46.248 -1.588  1.00   49.87  ? 230  CYS B O   1 
ATOM   1684 C CB  . CYS A 1 230 ? -11.914 -45.443 -1.522  1.00   53.40  ? 230  CYS B CB  1 
ATOM   1685 S SG  . CYS A 1 230 ? -10.623 -45.264 -2.756  1.00   56.47  ? 230  CYS B SG  1 
ATOM   1686 N N   . HIS A 1 231 ? -14.544 -44.828 0.059   0.64   46.41  ? 231  HIS B N   1 
ATOM   1687 C CA  . HIS A 1 231 ? -15.687 -45.115 0.932   0.64   43.45  ? 231  HIS B CA  1 
ATOM   1688 C C   . HIS A 1 231 ? -17.010 -44.719 0.300   0.64   41.85  ? 231  HIS B C   1 
ATOM   1689 O O   . HIS A 1 231 ? -18.034 -45.367 0.528   0.64   39.83  ? 231  HIS B O   1 
ATOM   1690 C CB  . HIS A 1 231 ? -15.546 -44.377 2.261   0.64   43.34  ? 231  HIS B CB  1 
ATOM   1691 C CG  . HIS A 1 231 ? -14.489 -44.943 3.152   0.64   45.12  ? 231  HIS B CG  1 
ATOM   1692 N ND1 . HIS A 1 231 ? -13.156 -44.958 2.803   0.64   46.26  ? 231  HIS B ND1 1 
ATOM   1693 C CD2 . HIS A 1 231 ? -14.564 -45.515 4.376   0.64   46.32  ? 231  HIS B CD2 1 
ATOM   1694 C CE1 . HIS A 1 231 ? -12.456 -45.516 3.772   0.64   46.98  ? 231  HIS B CE1 1 
ATOM   1695 N NE2 . HIS A 1 231 ? -13.286 -45.864 4.738   0.64   47.25  ? 231  HIS B NE2 1 
ATOM   1696 N N   . ALA A 1 232 ? -16.992 -43.640 -0.478  1.00   41.56  ? 232  ALA B N   1 
ATOM   1697 C CA  . ALA A 1 232 ? -18.197 -43.160 -1.130  1.00   41.23  ? 232  ALA B CA  1 
ATOM   1698 C C   . ALA A 1 232 ? -18.672 -44.160 -2.184  1.00   40.90  ? 232  ALA B C   1 
ATOM   1699 O O   . ALA A 1 232 ? -19.868 -44.395 -2.317  1.00   40.61  ? 232  ALA B O   1 
ATOM   1700 C CB  . ALA A 1 232 ? -17.960 -41.782 -1.744  1.00   41.47  ? 232  ALA B CB  1 
ATOM   1701 N N   . ALA A 1 233 ? -17.730 -44.755 -2.913  1.00   40.90  ? 233  ALA B N   1 
ATOM   1702 C CA  . ALA A 1 233 ? -18.050 -45.768 -3.928  1.00   42.38  ? 233  ALA B CA  1 
ATOM   1703 C C   . ALA A 1 233 ? -18.760 -46.993 -3.329  1.00   43.11  ? 233  ALA B C   1 
ATOM   1704 O O   . ALA A 1 233 ? -19.837 -47.401 -3.807  1.00   42.88  ? 233  ALA B O   1 
ATOM   1705 C CB  . ALA A 1 233 ? -16.789 -46.183 -4.672  1.00   42.23  ? 233  ALA B CB  1 
ATOM   1706 N N   . ASP A 1 234 ? -18.151 -47.561 -2.284  1.00   43.84  ? 234  ASP B N   1 
ATOM   1707 C CA  . ASP A 1 234 ? -18.761 -48.645 -1.497  1.00   44.83  ? 234  ASP B CA  1 
ATOM   1708 C C   . ASP A 1 234 ? -20.173 -48.285 -1.076  1.00   44.59  ? 234  ASP B C   1 
ATOM   1709 O O   . ASP A 1 234 ? -21.114 -49.048 -1.300  1.00   44.43  ? 234  ASP B O   1 
ATOM   1710 C CB  . ASP A 1 234 ? -17.939 -48.927 -0.234  1.00   45.50  ? 234  ASP B CB  1 
ATOM   1711 C CG  . ASP A 1 234 ? -16.549 -49.463 -0.535  1.00   47.67  ? 234  ASP B CG  1 
ATOM   1712 O OD1 . ASP A 1 234 ? -16.327 -49.996 -1.643  1.00   50.50  ? 234  ASP B OD1 1 
ATOM   1713 O OD2 . ASP A 1 234 ? -15.674 -49.350 0.349   1.00   51.16  ? 234  ASP B OD2 1 
ATOM   1714 N N   . LYS A 1 235 ? -20.308 -47.114 -0.456  1.00   44.59  ? 235  LYS B N   1 
ATOM   1715 C CA  . LYS A 1 235 ? -21.600 -46.616 -0.018  1.00   44.45  ? 235  LYS B CA  1 
ATOM   1716 C C   . LYS A 1 235 ? -22.578 -46.568 -1.186  1.00   44.44  ? 235  LYS B C   1 
ATOM   1717 O O   . LYS A 1 235 ? -23.726 -46.985 -1.059  1.00   45.01  ? 235  LYS B O   1 
ATOM   1718 C CB  . LYS A 1 235 ? -21.447 -45.229 0.621   1.00   44.99  ? 235  LYS B CB  1 
ATOM   1719 C CG  . LYS A 1 235 ? -22.731 -44.632 1.173   1.00   46.59  ? 235  LYS B CG  1 
ATOM   1720 C CD  . LYS A 1 235 ? -23.164 -45.340 2.445   1.00   50.19  ? 235  LYS B CD  1 
ATOM   1721 C CE  . LYS A 1 235 ? -24.593 -44.994 2.800   1.00   52.48  ? 235  LYS B CE  1 
ATOM   1722 N NZ  . LYS A 1 235 ? -24.902 -45.330 4.217   1.00   54.11  ? 235  LYS B NZ  1 
ATOM   1723 N N   . LEU A 1 236 ? -22.112 -46.080 -2.330  1.00   43.54  ? 236  LEU B N   1 
ATOM   1724 C CA  . LEU A 1 236 ? -22.978 -45.938 -3.492  1.00   43.35  ? 236  LEU B CA  1 
ATOM   1725 C C   . LEU A 1 236 ? -23.418 -47.295 -4.041  1.00   43.41  ? 236  LEU B C   1 
ATOM   1726 O O   . LEU A 1 236 ? -24.599 -47.479 -4.340  1.00   43.11  ? 236  LEU B O   1 
ATOM   1727 C CB  . LEU A 1 236 ? -22.303 -45.088 -4.573  1.00   43.36  ? 236  LEU B CB  1 
ATOM   1728 C CG  . LEU A 1 236 ? -22.232 -43.583 -4.272  1.00   43.07  ? 236  LEU B CG  1 
ATOM   1729 C CD1 . LEU A 1 236 ? -21.292 -42.880 -5.241  1.00   41.76  ? 236  LEU B CD1 1 
ATOM   1730 C CD2 . LEU A 1 236 ? -23.619 -42.937 -4.293  1.00   43.49  ? 236  LEU B CD2 1 
ATOM   1731 N N   . LEU A 1 237 ? -22.481 -48.238 -4.162  1.00   43.24  ? 237  LEU B N   1 
ATOM   1732 C CA  . LEU A 1 237 ? -22.842 -49.613 -4.533  1.00   43.63  ? 237  LEU B CA  1 
ATOM   1733 C C   . LEU A 1 237 ? -23.831 -50.259 -3.546  1.00   43.75  ? 237  LEU B C   1 
ATOM   1734 O O   . LEU A 1 237 ? -24.787 -50.909 -3.976  1.00   43.51  ? 237  LEU B O   1 
ATOM   1735 C CB  . LEU A 1 237 ? -21.602 -50.489 -4.754  1.00   43.78  ? 237  LEU B CB  1 
ATOM   1736 C CG  . LEU A 1 237 ? -20.732 -50.218 -5.996  1.00   44.30  ? 237  LEU B CG  1 
ATOM   1737 C CD1 . LEU A 1 237 ? -19.602 -51.209 -6.069  1.00   45.38  ? 237  LEU B CD1 1 
ATOM   1738 C CD2 . LEU A 1 237 ? -21.500 -50.223 -7.325  1.00   42.93  ? 237  LEU B CD2 1 
ATOM   1739 N N   . SER A 1 238 ? -23.630 -50.046 -2.242  1.00   43.55  ? 238  SER B N   1 
ATOM   1740 C CA  . SER A 1 238 ? -24.556 -50.559 -1.213  1.00   44.32  ? 238  SER B CA  1 
ATOM   1741 C C   . SER A 1 238 ? -25.964 -50.002 -1.339  1.00   44.92  ? 238  SER B C   1 
ATOM   1742 O O   . SER A 1 238 ? -26.926 -50.636 -0.905  1.00   44.92  ? 238  SER B O   1 
ATOM   1743 C CB  . SER A 1 238 ? -24.041 -50.251 0.191   1.00   43.68  ? 238  SER B CB  1 
ATOM   1744 O OG  . SER A 1 238 ? -22.859 -50.977 0.451   1.00   45.55  ? 238  SER B OG  1 
ATOM   1745 N N   . ALA A 1 239 ? -26.078 -48.806 -1.909  1.00   45.99  ? 239  ALA B N   1 
ATOM   1746 C CA  . ALA A 1 239 ? -27.376 -48.157 -2.066  1.00   46.92  ? 239  ALA B CA  1 
ATOM   1747 C C   . ALA A 1 239 ? -28.018 -48.522 -3.405  1.00   47.44  ? 239  ALA B C   1 
ATOM   1748 O O   . ALA A 1 239 ? -29.107 -48.050 -3.734  1.00   47.57  ? 239  ALA B O   1 
ATOM   1749 C CB  . ALA A 1 239 ? -27.237 -46.653 -1.925  1.00   46.96  ? 239  ALA B CB  1 
ATOM   1750 N N   . GLY A 1 240 ? -27.332 -49.361 -4.174  1.00   48.02  ? 240  GLY B N   1 
ATOM   1751 C CA  . GLY A 1 240 ? -27.912 -49.929 -5.378  1.00   48.82  ? 240  GLY B CA  1 
ATOM   1752 C C   . GLY A 1 240 ? -27.437 -49.327 -6.684  1.00   49.36  ? 240  GLY B C   1 
ATOM   1753 O O   . GLY A 1 240 ? -28.047 -49.574 -7.730  1.00   49.85  ? 240  GLY B O   1 
ATOM   1754 N N   . ALA A 1 241 ? -26.360 -48.542 -6.643  1.00   49.03  ? 241  ALA B N   1 
ATOM   1755 C CA  . ALA A 1 241 ? -25.806 -47.996 -7.880  1.00   48.92  ? 241  ALA B CA  1 
ATOM   1756 C C   . ALA A 1 241 ? -25.277 -49.139 -8.736  1.00   49.21  ? 241  ALA B C   1 
ATOM   1757 O O   . ALA A 1 241 ? -24.660 -50.077 -8.229  1.00   49.52  ? 241  ALA B O   1 
ATOM   1758 C CB  . ALA A 1 241 ? -24.707 -46.966 -7.607  1.00   47.35  ? 241  ALA B CB  1 
ATOM   1759 N N   . THR A 1 242 ? -25.541 -49.047 -10.033 1.00   49.65  ? 242  THR B N   1 
ATOM   1760 C CA  . THR A 1 242 ? -25.116 -50.047 -11.007 1.00   50.83  ? 242  THR B CA  1 
ATOM   1761 C C   . THR A 1 242 ? -23.595 -50.109 -11.070 1.00   50.64  ? 242  THR B C   1 
ATOM   1762 O O   . THR A 1 242 ? -22.998 -51.178 -10.974 1.00   50.76  ? 242  THR B O   1 
ATOM   1763 C CB  . THR A 1 242 ? -25.682 -49.707 -12.396 1.00   50.98  ? 242  THR B CB  1 
ATOM   1764 O OG1 . THR A 1 242 ? -27.111 -49.641 -12.310 1.00   52.66  ? 242  THR B OG1 1 
ATOM   1765 C CG2 . THR A 1 242 ? -25.291 -50.767 -13.426 1.00   52.13  ? 242  THR B CG2 1 
ATOM   1766 N N   . ARG A 1 243 ? -22.981 -48.949 -11.252 1.00   50.43  ? 243  ARG B N   1 
ATOM   1767 C CA  . ARG A 1 243 ? -21.543 -48.811 -11.115 1.00   50.09  ? 243  ARG B CA  1 
ATOM   1768 C C   . ARG A 1 243 ? -21.209 -47.366 -10.786 1.00   48.53  ? 243  ARG B C   1 
ATOM   1769 O O   . ARG A 1 243 ? -22.084 -46.496 -10.785 1.00   48.35  ? 243  ARG B O   1 
ATOM   1770 C CB  . ARG A 1 243 ? -20.792 -49.315 -12.353 1.00   50.79  ? 243  ARG B CB  1 
ATOM   1771 C CG  . ARG A 1 243 ? -21.276 -48.732 -13.649 1.00   53.75  ? 243  ARG B CG  1 
ATOM   1772 C CD  . ARG A 1 243 ? -21.260 -49.769 -14.760 1.00   58.26  ? 243  ARG B CD  1 
ATOM   1773 N NE  . ARG A 1 243 ? -21.869 -49.199 -15.955 1.00   62.53  ? 243  ARG B NE  1 
ATOM   1774 C CZ  . ARG A 1 243 ? -21.222 -48.403 -16.799 1.00   64.76  ? 243  ARG B CZ  1 
ATOM   1775 N NH1 . ARG A 1 243 ? -19.947 -48.120 -16.585 1.00   66.13  ? 243  ARG B NH1 1 
ATOM   1776 N NH2 . ARG A 1 243 ? -21.838 -47.900 -17.861 1.00   65.62  ? 243  ARG B NH2 1 
ATOM   1777 N N   . VAL A 1 244 ? -19.939 -47.127 -10.501 1.00   46.19  ? 244  VAL B N   1 
ATOM   1778 C CA  . VAL A 1 244 ? -19.513 -45.889 -9.874  1.00   45.86  ? 244  VAL B CA  1 
ATOM   1779 C C   . VAL A 1 244 ? -18.339 -45.285 -10.618 1.00   45.94  ? 244  VAL B C   1 
ATOM   1780 O O   . VAL A 1 244 ? -17.352 -45.967 -10.898 1.00   45.98  ? 244  VAL B O   1 
ATOM   1781 C CB  . VAL A 1 244 ? -19.145 -46.113 -8.381  1.00   45.40  ? 244  VAL B CB  1 
ATOM   1782 C CG1 . VAL A 1 244 ? -18.669 -44.818 -7.736  1.00   44.89  ? 244  VAL B CG1 1 
ATOM   1783 C CG2 . VAL A 1 244 ? -20.344 -46.645 -7.616  1.00   45.10  ? 244  VAL B CG2 1 
ATOM   1784 N N   . TYR A 1 245 ? -18.465 -44.005 -10.949 1.00   46.10  ? 245  TYR B N   1 
ATOM   1785 C CA  . TYR A 1 245 ? -17.352 -43.248 -11.507 1.00   46.44  ? 245  TYR B CA  1 
ATOM   1786 C C   . TYR A 1 245 ? -16.936 -42.153 -10.533 1.00   45.84  ? 245  TYR B C   1 
ATOM   1787 O O   . TYR A 1 245 ? -17.753 -41.675 -9.744  1.00   44.54  ? 245  TYR B O   1 
ATOM   1788 C CB  . TYR A 1 245 ? -17.740 -42.644 -12.859 1.00   46.64  ? 245  TYR B CB  1 
ATOM   1789 C CG  . TYR A 1 245 ? -17.930 -43.672 -13.956 1.00   49.13  ? 245  TYR B CG  1 
ATOM   1790 C CD1 . TYR A 1 245 ? -19.153 -44.325 -14.126 1.00   50.51  ? 245  TYR B CD1 1 
ATOM   1791 C CD2 . TYR A 1 245 ? -16.889 -43.988 -14.825 1.00   50.42  ? 245  TYR B CD2 1 
ATOM   1792 C CE1 . TYR A 1 245 ? -19.331 -45.261 -15.130 1.00   52.02  ? 245  TYR B CE1 1 
ATOM   1793 C CE2 . TYR A 1 245 ? -17.055 -44.919 -15.832 1.00   52.02  ? 245  TYR B CE2 1 
ATOM   1794 C CZ  . TYR A 1 245 ? -18.277 -45.552 -15.980 1.00   53.32  ? 245  TYR B CZ  1 
ATOM   1795 O OH  . TYR A 1 245 ? -18.440 -46.478 -16.985 1.00   54.11  ? 245  TYR B OH  1 
ATOM   1796 N N   . ALA A 1 246 ? -15.656 -41.788 -10.580 1.00   45.83  ? 246  ALA B N   1 
ATOM   1797 C CA  . ALA A 1 246 ? -15.148 -40.622 -9.865  1.00   46.34  ? 246  ALA B CA  1 
ATOM   1798 C C   . ALA A 1 246 ? -14.478 -39.699 -10.872 1.00   46.73  ? 246  ALA B C   1 
ATOM   1799 O O   . ALA A 1 246 ? -13.605 -40.129 -11.633 1.00   46.62  ? 246  ALA B O   1 
ATOM   1800 C CB  . ALA A 1 246 ? -14.160 -41.035 -8.775  1.00   46.26  ? 246  ALA B CB  1 
ATOM   1801 N N   . ILE A 1 247 ? -14.909 -38.440 -10.895 1.00   47.34  ? 247  ILE B N   1 
ATOM   1802 C CA  . ILE A 1 247 ? -14.324 -37.444 -11.789 1.00   48.25  ? 247  ILE B CA  1 
ATOM   1803 C C   . ILE A 1 247 ? -13.835 -36.260 -10.964 1.00   49.08  ? 247  ILE B C   1 
ATOM   1804 O O   . ILE A 1 247 ? -14.634 -35.542 -10.360 1.00   49.21  ? 247  ILE B O   1 
ATOM   1805 C CB  . ILE A 1 247 ? -15.319 -36.977 -12.901 1.00   47.93  ? 247  ILE B CB  1 
ATOM   1806 C CG1 . ILE A 1 247 ? -15.841 -38.178 -13.701 1.00   47.81  ? 247  ILE B CG1 1 
ATOM   1807 C CG2 . ILE A 1 247 ? -14.643 -35.964 -13.843 1.00   47.82  ? 247  ILE B CG2 1 
ATOM   1808 C CD1 . ILE A 1 247 ? -16.833 -37.823 -14.794 1.00   47.72  ? 247  ILE B CD1 1 
ATOM   1809 N N   . LEU A 1 248 ? -12.519 -36.092 -10.917 1.00   50.10  ? 248  LEU B N   1 
ATOM   1810 C CA  . LEU A 1 248 ? -11.899 -34.996 -10.188 1.00   50.98  ? 248  LEU B CA  1 
ATOM   1811 C C   . LEU A 1 248 ? -11.290 -34.033 -11.186 1.00   50.62  ? 248  LEU B C   1 
ATOM   1812 O O   . LEU A 1 248 ? -10.842 -34.454 -12.252 1.00   51.11  ? 248  LEU B O   1 
ATOM   1813 C CB  . LEU A 1 248 ? -10.806 -35.518 -9.250  1.00   51.48  ? 248  LEU B CB  1 
ATOM   1814 C CG  . LEU A 1 248 ? -11.193 -36.529 -8.158  1.00   53.21  ? 248  LEU B CG  1 
ATOM   1815 C CD1 . LEU A 1 248 ? -12.606 -36.286 -7.615  1.00   54.22  ? 248  LEU B CD1 1 
ATOM   1816 C CD2 . LEU A 1 248 ? -11.045 -37.975 -8.636  1.00   53.80  ? 248  LEU B CD2 1 
ATOM   1817 N N   . THR A 1 249 ? -11.270 -32.742 -10.875 1.00   49.33  ? 249  THR B N   1 
ATOM   1818 C CA  . THR A 1 249 ? -10.471 -31.862 -11.727 1.00   48.55  ? 249  THR B CA  1 
ATOM   1819 C C   . THR A 1 249 ? -8.971  -31.981 -11.393 1.00   47.94  ? 249  THR B C   1 
ATOM   1820 O O   . THR A 1 249 ? -8.157  -32.188 -12.291 1.00   47.23  ? 249  THR B O   1 
ATOM   1821 C CB  . THR A 1 249 ? -11.035 -30.412 -11.887 1.00   48.41  ? 249  THR B CB  1 
ATOM   1822 O OG1 . THR A 1 249 ? -9.956  -29.465 -12.000 1.00   49.58  ? 249  THR B OG1 1 
ATOM   1823 C CG2 . THR A 1 249 ? -11.950 -30.035 -10.754 1.00   49.26  ? 249  THR B CG2 1 
ATOM   1824 N N   . HIS A 1 250 ? -8.627  -31.919 -10.107 1.00   47.72  ? 250  HIS B N   1 
ATOM   1825 C CA  . HIS A 1 250 ? -7.230  -31.993 -9.670  1.00   48.33  ? 250  HIS B CA  1 
ATOM   1826 C C   . HIS A 1 250 ? -6.904  -33.334 -9.015  1.00   48.99  ? 250  HIS B C   1 
ATOM   1827 O O   . HIS A 1 250 ? -7.386  -33.630 -7.917  1.00   49.01  ? 250  HIS B O   1 
ATOM   1828 C CB  . HIS A 1 250 ? -6.900  -30.846 -8.703  1.00   48.12  ? 250  HIS B CB  1 
ATOM   1829 C CG  . HIS A 1 250 ? -7.265  -29.489 -9.226  1.00   47.53  ? 250  HIS B CG  1 
ATOM   1830 N ND1 . HIS A 1 250 ? -6.633  -28.916 -10.308 1.00   45.87  ? 250  HIS B ND1 1 
ATOM   1831 C CD2 . HIS A 1 250 ? -8.201  -28.595 -8.820  1.00   46.31  ? 250  HIS B CD2 1 
ATOM   1832 C CE1 . HIS A 1 250 ? -7.161  -27.728 -10.547 1.00   43.81  ? 250  HIS B CE1 1 
ATOM   1833 N NE2 . HIS A 1 250 ? -8.114  -27.509 -9.659  1.00   45.43  ? 250  HIS B NE2 1 
ATOM   1834 N N   . GLY A 1 251 ? -6.082  -34.136 -9.687  1.00   49.27  ? 251  GLY B N   1 
ATOM   1835 C CA  . GLY A 1 251 ? -5.693  -35.442 -9.163  1.00   50.61  ? 251  GLY B CA  1 
ATOM   1836 C C   . GLY A 1 251 ? -4.390  -35.409 -8.386  1.00   51.38  ? 251  GLY B C   1 
ATOM   1837 O O   . GLY A 1 251 ? -3.332  -35.727 -8.929  1.00   51.18  ? 251  GLY B O   1 
ATOM   1838 N N   . ILE A 1 252 ? -4.465  -35.023 -7.113  1.00   52.56  ? 252  ILE B N   1 
ATOM   1839 C CA  . ILE A 1 252 ? -3.270  -34.975 -6.252  1.00   53.88  ? 252  ILE B CA  1 
ATOM   1840 C C   . ILE A 1 252 ? -2.722  -36.385 -5.986  1.00   54.26  ? 252  ILE B C   1 
ATOM   1841 O O   . ILE A 1 252 ? -1.537  -36.644 -6.195  1.00   53.83  ? 252  ILE B O   1 
ATOM   1842 C CB  . ILE A 1 252 ? -3.526  -34.227 -4.916  1.00   54.12  ? 252  ILE B CB  1 
ATOM   1843 C CG1 . ILE A 1 252 ? -4.184  -32.863 -5.174  1.00   54.83  ? 252  ILE B CG1 1 
ATOM   1844 C CG2 . ILE A 1 252 ? -2.211  -34.037 -4.156  1.00   54.34  ? 252  ILE B CG2 1 
ATOM   1845 C CD1 . ILE A 1 252 ? -4.623  -32.122 -3.915  1.00   55.84  ? 252  ILE B CD1 1 
ATOM   1846 N N   . PHE A 1 253 ? -3.585  -37.293 -5.536  1.00   55.22  ? 253  PHE B N   1 
ATOM   1847 C CA  . PHE A 1 253 ? -3.194  -38.691 -5.377  1.00   56.25  ? 253  PHE B CA  1 
ATOM   1848 C C   . PHE A 1 253 ? -1.874  -38.831 -4.606  1.00   57.55  ? 253  PHE B C   1 
ATOM   1849 O O   . PHE A 1 253 ? -0.922  -39.433 -5.106  1.00   57.90  ? 253  PHE B O   1 
ATOM   1850 C CB  . PHE A 1 253 ? -3.062  -39.380 -6.754  1.00   55.82  ? 253  PHE B CB  1 
ATOM   1851 C CG  . PHE A 1 253 ? -4.324  -39.365 -7.585  1.00   54.04  ? 253  PHE B CG  1 
ATOM   1852 C CD1 . PHE A 1 253 ? -4.258  -39.180 -8.964  1.00   53.11  ? 253  PHE B CD1 1 
ATOM   1853 C CD2 . PHE A 1 253 ? -5.569  -39.559 -7.000  1.00   52.31  ? 253  PHE B CD2 1 
ATOM   1854 C CE1 . PHE A 1 253 ? -5.417  -39.182 -9.740  1.00   51.83  ? 253  PHE B CE1 1 
ATOM   1855 C CE2 . PHE A 1 253 ? -6.730  -39.555 -7.767  1.00   50.93  ? 253  PHE B CE2 1 
ATOM   1856 C CZ  . PHE A 1 253 ? -6.654  -39.370 -9.135  1.00   50.68  ? 253  PHE B CZ  1 
ATOM   1857 N N   . SER A 1 254 ? -1.795  -38.256 -3.408  1.00   58.89  ? 254  SER B N   1 
ATOM   1858 C CA  . SER A 1 254 ? -0.588  -38.426 -2.592  1.00   60.28  ? 254  SER B CA  1 
ATOM   1859 C C   . SER A 1 254 ? -0.728  -39.627 -1.655  1.00   61.04  ? 254  SER B C   1 
ATOM   1860 O O   . SER A 1 254 ? -1.827  -40.172 -1.494  1.00   61.13  ? 254  SER B O   1 
ATOM   1861 C CB  . SER A 1 254 ? -0.250  -37.155 -1.809  1.00   60.21  ? 254  SER B CB  1 
ATOM   1862 O OG  . SER A 1 254 ? -1.231  -36.869 -0.830  1.00   60.31  ? 254  SER B OG  1 
ATOM   1863 N N   . GLY A 1 255 ? 0.388   -40.038 -1.054  1.00   61.78  ? 255  GLY B N   1 
ATOM   1864 C CA  . GLY A 1 255 ? 0.400   -41.137 -0.087  1.00   62.77  ? 255  GLY B CA  1 
ATOM   1865 C C   . GLY A 1 255 ? -0.172  -42.433 -0.635  1.00   63.58  ? 255  GLY B C   1 
ATOM   1866 O O   . GLY A 1 255 ? 0.292   -42.925 -1.660  1.00   63.54  ? 255  GLY B O   1 
ATOM   1867 N N   . PRO A 1 256 ? -1.200  -42.985 0.037   1.00   64.34  ? 256  PRO B N   1 
ATOM   1868 C CA  . PRO A 1 256 ? -1.735  -44.302 -0.311  1.00   64.80  ? 256  PRO B CA  1 
ATOM   1869 C C   . PRO A 1 256 ? -2.839  -44.280 -1.374  1.00   64.82  ? 256  PRO B C   1 
ATOM   1870 O O   . PRO A 1 256 ? -3.520  -45.293 -1.558  1.00   65.11  ? 256  PRO B O   1 
ATOM   1871 C CB  . PRO A 1 256 ? -2.318  -44.782 1.020   1.00   64.97  ? 256  PRO B CB  1 
ATOM   1872 C CG  . PRO A 1 256 ? -2.809  -43.523 1.674   1.00   64.86  ? 256  PRO B CG  1 
ATOM   1873 C CD  . PRO A 1 256 ? -1.892  -42.405 1.205   1.00   64.45  ? 256  PRO B CD  1 
ATOM   1874 N N   . ALA A 1 257 ? -3.011  -43.152 -2.064  1.00   64.19  ? 257  ALA B N   1 
ATOM   1875 C CA  . ALA A 1 257 ? -4.150  -42.979 -2.971  1.00   63.36  ? 257  ALA B CA  1 
ATOM   1876 C C   . ALA A 1 257 ? -4.192  -44.017 -4.093  1.00   62.88  ? 257  ALA B C   1 
ATOM   1877 O O   . ALA A 1 257 ? -5.230  -44.652 -4.306  1.00   62.60  ? 257  ALA B O   1 
ATOM   1878 C CB  . ALA A 1 257 ? -4.195  -41.558 -3.536  1.00   63.16  ? 257  ALA B CB  1 
ATOM   1879 N N   . ILE A 1 258 ? -3.070  -44.193 -4.792  1.00   62.25  ? 258  ILE B N   1 
ATOM   1880 C CA  . ILE A 1 258 ? -3.004  -45.128 -5.919  1.00   62.85  ? 258  ILE B CA  1 
ATOM   1881 C C   . ILE A 1 258 ? -3.350  -46.550 -5.480  1.00   63.80  ? 258  ILE B C   1 
ATOM   1882 O O   . ILE A 1 258 ? -3.939  -47.314 -6.244  1.00   63.46  ? 258  ILE B O   1 
ATOM   1883 C CB  . ILE A 1 258 ? -1.629  -45.072 -6.647  1.00   62.60  ? 258  ILE B CB  1 
ATOM   1884 C CG1 . ILE A 1 258 ? -1.416  -43.691 -7.283  1.00   62.32  ? 258  ILE B CG1 1 
ATOM   1885 C CG2 . ILE A 1 258 ? -1.500  -46.177 -7.721  1.00   62.34  ? 258  ILE B CG2 1 
ATOM   1886 C CD1 . ILE A 1 258 ? -2.578  -43.193 -8.146  1.00   61.25  ? 258  ILE B CD1 1 
ATOM   1887 N N   . SER A 1 259 ? -2.998  -46.884 -4.242  1.00   65.43  ? 259  SER B N   1 
ATOM   1888 C CA  . SER A 1 259 ? -3.326  -48.183 -3.666  1.00   67.05  ? 259  SER B CA  1 
ATOM   1889 C C   . SER A 1 259 ? -4.804  -48.290 -3.295  1.00   67.41  ? 259  SER B C   1 
ATOM   1890 O O   . SER A 1 259 ? -5.414  -49.345 -3.482  1.00   67.59  ? 259  SER B O   1 
ATOM   1891 C CB  . SER A 1 259 ? -2.445  -48.470 -2.449  1.00   67.32  ? 259  SER B CB  1 
ATOM   1892 O OG  . SER A 1 259 ? -1.069  -48.478 -2.813  1.00   68.30  ? 259  SER B OG  1 
ATOM   1893 N N   . ARG A 1 260 ? -5.370  -47.205 -2.765  1.00   67.59  ? 260  ARG B N   1 
ATOM   1894 C CA  . ARG A 1 260 ? -6.809  -47.141 -2.499  1.00   67.73  ? 260  ARG B CA  1 
ATOM   1895 C C   . ARG A 1 260 ? -7.638  -47.250 -3.779  1.00   67.56  ? 260  ARG B C   1 
ATOM   1896 O O   . ARG A 1 260 ? -8.726  -47.827 -3.766  1.00   67.37  ? 260  ARG B O   1 
ATOM   1897 C CB  . ARG A 1 260 ? -7.183  -45.864 -1.741  1.00   68.01  ? 260  ARG B CB  1 
ATOM   1898 C CG  . ARG A 1 260 ? -7.553  -46.088 -0.280  1.00   68.87  ? 260  ARG B CG  1 
ATOM   1899 C CD  . ARG A 1 260 ? -6.401  -45.762 0.652   1.00   70.09  ? 260  ARG B CD  1 
ATOM   1900 N NE  . ARG A 1 260 ? -6.330  -44.331 0.945   1.00   71.34  ? 260  ARG B NE  1 
ATOM   1901 C CZ  . ARG A 1 260 ? -6.535  -43.787 2.145   1.00   71.98  ? 260  ARG B CZ  1 
ATOM   1902 N NH1 . ARG A 1 260 ? -6.818  -44.546 3.197   1.00   72.43  ? 260  ARG B NH1 1 
ATOM   1903 N NH2 . ARG A 1 260 ? -6.450  -42.472 2.295   1.00   71.93  ? 260  ARG B NH2 1 
ATOM   1904 N N   . ILE A 1 261 ? -7.113  -46.706 -4.876  1.00   67.55  ? 261  ILE B N   1 
ATOM   1905 C CA  . ILE A 1 261 ? -7.814  -46.706 -6.163  1.00   67.79  ? 261  ILE B CA  1 
ATOM   1906 C C   . ILE A 1 261 ? -7.772  -48.079 -6.841  1.00   68.32  ? 261  ILE B C   1 
ATOM   1907 O O   . ILE A 1 261 ? -8.799  -48.570 -7.324  1.00   67.91  ? 261  ILE B O   1 
ATOM   1908 C CB  . ILE A 1 261 ? -7.270  -45.620 -7.118  1.00   67.57  ? 261  ILE B CB  1 
ATOM   1909 C CG1 . ILE A 1 261 ? -7.492  -44.228 -6.519  1.00   67.43  ? 261  ILE B CG1 1 
ATOM   1910 C CG2 . ILE A 1 261 ? -7.957  -45.708 -8.480  1.00   67.45  ? 261  ILE B CG2 1 
ATOM   1911 C CD1 . ILE A 1 261 ? -6.607  -43.153 -7.111  1.00   67.26  ? 261  ILE B CD1 1 
ATOM   1912 N N   . ASN A 1 262 ? -6.587  -48.687 -6.871  1.00   69.03  ? 262  ASN B N   1 
ATOM   1913 C CA  . ASN A 1 262 ? -6.421  -50.047 -7.384  1.00   69.99  ? 262  ASN B CA  1 
ATOM   1914 C C   . ASN A 1 262 ? -7.361  -51.050 -6.710  1.00   70.39  ? 262  ASN B C   1 
ATOM   1915 O O   . ASN A 1 262 ? -7.761  -52.039 -7.324  1.00   70.50  ? 262  ASN B O   1 
ATOM   1916 C CB  . ASN A 1 262 ? -4.967  -50.509 -7.227  1.00   69.99  ? 262  ASN B CB  1 
ATOM   1917 C CG  . ASN A 1 262 ? -4.005  -49.761 -8.144  1.00   70.65  ? 262  ASN B CG  1 
ATOM   1918 O OD1 . ASN A 1 262 ? -4.385  -49.280 -9.215  1.00   71.40  ? 262  ASN B OD1 1 
ATOM   1919 N ND2 . ASN A 1 262 ? -2.745  -49.676 -7.730  1.00   70.85  ? 262  ASN B ND2 1 
ATOM   1920 N N   . ASN A 1 263 ? -7.724  -50.778 -5.458  1.00   71.03  ? 263  ASN B N   1 
ATOM   1921 C CA  . ASN A 1 263 ? -8.575  -51.679 -4.680  1.00   71.69  ? 263  ASN B CA  1 
ATOM   1922 C C   . ASN A 1 263 ? -10.050 -51.281 -4.615  1.00   71.54  ? 263  ASN B C   1 
ATOM   1923 O O   . ASN A 1 263 ? -10.896 -52.090 -4.217  1.00   71.78  ? 263  ASN B O   1 
ATOM   1924 C CB  . ASN A 1 263 ? -8.024  -51.837 -3.258  1.00   71.98  ? 263  ASN B CB  1 
ATOM   1925 C CG  . ASN A 1 263 ? -6.654  -52.500 -3.228  1.00   72.86  ? 263  ASN B CG  1 
ATOM   1926 O OD1 . ASN A 1 263 ? -5.788  -52.118 -2.440  1.00   73.18  ? 263  ASN B OD1 1 
ATOM   1927 N ND2 . ASN A 1 263 ? -6.452  -53.499 -4.085  1.00   73.20  ? 263  ASN B ND2 1 
ATOM   1928 N N   . ALA A 1 264 ? -10.353 -50.043 -5.000  1.00   70.79  ? 264  ALA B N   1 
ATOM   1929 C CA  . ALA A 1 264 ? -11.711 -49.520 -4.887  1.00   69.78  ? 264  ALA B CA  1 
ATOM   1930 C C   . ALA A 1 264 ? -12.612 -50.006 -6.014  1.00   68.91  ? 264  ALA B C   1 
ATOM   1931 O O   . ALA A 1 264 ? -12.139 -50.447 -7.065  1.00   68.92  ? 264  ALA B O   1 
ATOM   1932 C CB  . ALA A 1 264 ? -11.694 -48.004 -4.835  1.00   69.90  ? 264  ALA B CB  1 
ATOM   1933 N N   . CYS A 1 265 ? -13.915 -49.905 -5.789  1.00   67.62  ? 265  CYS B N   1 
ATOM   1934 C CA  . CYS A 1 265 ? -14.897 -50.404 -6.737  1.00   66.47  ? 265  CYS B CA  1 
ATOM   1935 C C   . CYS A 1 265 ? -15.261 -49.414 -7.856  1.00   64.99  ? 265  CYS B C   1 
ATOM   1936 O O   . CYS A 1 265 ? -16.356 -49.495 -8.417  1.00   65.15  ? 265  CYS B O   1 
ATOM   1937 C CB  . CYS A 1 265 ? -16.150 -50.850 -5.981  1.00   66.76  ? 265  CYS B CB  1 
ATOM   1938 S SG  . CYS A 1 265 ? -16.909 -49.552 -4.956  1.00   68.48  ? 265  CYS B SG  1 
ATOM   1939 N N   . PHE A 1 266 ? -14.355 -48.490 -8.185  1.00   62.74  ? 266  PHE B N   1 
ATOM   1940 C CA  . PHE A 1 266 ? -14.588 -47.564 -9.299  1.00   60.73  ? 266  PHE B CA  1 
ATOM   1941 C C   . PHE A 1 266 ? -14.512 -48.282 -10.633 1.00   60.21  ? 266  PHE B C   1 
ATOM   1942 O O   . PHE A 1 266 ? -13.674 -49.157 -10.828 1.00   60.30  ? 266  PHE B O   1 
ATOM   1943 C CB  . PHE A 1 266 ? -13.567 -46.418 -9.323  1.00   60.01  ? 266  PHE B CB  1 
ATOM   1944 C CG  . PHE A 1 266 ? -13.570 -45.570 -8.094  1.00   57.74  ? 266  PHE B CG  1 
ATOM   1945 C CD1 . PHE A 1 266 ? -12.451 -45.521 -7.280  1.00   56.00  ? 266  PHE B CD1 1 
ATOM   1946 C CD2 . PHE A 1 266 ? -14.687 -44.818 -7.750  1.00   55.87  ? 266  PHE B CD2 1 
ATOM   1947 C CE1 . PHE A 1 266 ? -12.439 -44.735 -6.142  1.00   55.24  ? 266  PHE B CE1 1 
ATOM   1948 C CE2 . PHE A 1 266 ? -14.685 -44.026 -6.610  1.00   55.67  ? 266  PHE B CE2 1 
ATOM   1949 C CZ  . PHE A 1 266 ? -13.558 -43.989 -5.806  1.00   55.39  ? 266  PHE B CZ  1 
ATOM   1950 N N   . GLU A 1 267 ? -15.386 -47.898 -11.555 1.00   59.44  ? 267  GLU B N   1 
ATOM   1951 C CA  . GLU A 1 267 ? -15.257 -48.319 -12.937 1.00   58.82  ? 267  GLU B CA  1 
ATOM   1952 C C   . GLU A 1 267 ? -14.085 -47.566 -13.570 1.00   57.33  ? 267  GLU B C   1 
ATOM   1953 O O   . GLU A 1 267 ? -13.364 -48.112 -14.406 1.00   57.61  ? 267  GLU B O   1 
ATOM   1954 C CB  . GLU A 1 267 ? -16.552 -48.023 -13.695 1.00   59.44  ? 267  GLU B CB  1 
ATOM   1955 C CG  . GLU A 1 267 ? -16.577 -48.519 -15.139 1.00   61.96  ? 267  GLU B CG  1 
ATOM   1956 C CD  . GLU A 1 267 ? -17.047 -49.959 -15.274 1.00   64.73  ? 267  GLU B CD  1 
ATOM   1957 O OE1 . GLU A 1 267 ? -17.084 -50.691 -14.260 1.00   65.49  ? 267  GLU B OE1 1 
ATOM   1958 O OE2 . GLU A 1 267 ? -17.388 -50.360 -16.407 1.00   66.39  ? 267  GLU B OE2 1 
ATOM   1959 N N   . ALA A 1 268 ? -13.906 -46.312 -13.149 1.00   54.97  ? 268  ALA B N   1 
ATOM   1960 C CA  . ALA A 1 268 ? -12.902 -45.405 -13.711 1.00   52.76  ? 268  ALA B CA  1 
ATOM   1961 C C   . ALA A 1 268 ? -12.730 -44.183 -12.815 1.00   51.42  ? 268  ALA B C   1 
ATOM   1962 O O   . ALA A 1 268 ? -13.678 -43.745 -12.159 1.00   50.79  ? 268  ALA B O   1 
ATOM   1963 C CB  . ALA A 1 268 ? -13.304 -44.962 -15.116 1.00   52.51  ? 268  ALA B CB  1 
ATOM   1964 N N   . VAL A 1 269 ? -11.514 -43.648 -12.785 1.00   50.06  ? 269  VAL B N   1 
ATOM   1965 C CA  . VAL A 1 269 ? -11.225 -42.415 -12.064 1.00   49.13  ? 269  VAL B CA  1 
ATOM   1966 C C   . VAL A 1 269 ? -10.646 -41.406 -13.052 1.00   48.03  ? 269  VAL B C   1 
ATOM   1967 O O   . VAL A 1 269 ? -9.539  -41.580 -13.560 1.00   47.91  ? 269  VAL B O   1 
ATOM   1968 C CB  . VAL A 1 269 ? -10.266 -42.651 -10.868 1.00   49.28  ? 269  VAL B CB  1 
ATOM   1969 C CG1 . VAL A 1 269 ? -10.036 -41.360 -10.090 1.00   49.16  ? 269  VAL B CG1 1 
ATOM   1970 C CG2 . VAL A 1 269 ? -10.830 -43.722 -9.941  1.00   49.43  ? 269  VAL B CG2 1 
ATOM   1971 N N   . VAL A 1 270 ? -11.414 -40.356 -13.321 1.00   46.79  ? 270  VAL B N   1 
ATOM   1972 C CA  . VAL A 1 270 ? -11.070 -39.380 -14.353 1.00   45.47  ? 270  VAL B CA  1 
ATOM   1973 C C   . VAL A 1 270 ? -10.560 -38.095 -13.709 1.00   44.63  ? 270  VAL B C   1 
ATOM   1974 O O   . VAL A 1 270 ? -11.219 -37.526 -12.830 1.00   44.12  ? 270  VAL B O   1 
ATOM   1975 C CB  . VAL A 1 270 ? -12.300 -39.056 -15.230 1.00   45.70  ? 270  VAL B CB  1 
ATOM   1976 C CG1 . VAL A 1 270 ? -11.920 -38.170 -16.411 1.00   44.92  ? 270  VAL B CG1 1 
ATOM   1977 C CG2 . VAL A 1 270 ? -12.965 -40.346 -15.706 1.00   45.97  ? 270  VAL B CG2 1 
ATOM   1978 N N   . VAL A 1 271 ? -9.390  -37.643 -14.149 1.00   43.33  ? 271  VAL B N   1 
ATOM   1979 C CA  . VAL A 1 271 ? -8.790  -36.414 -13.633 1.00   42.85  ? 271  VAL B CA  1 
ATOM   1980 C C   . VAL A 1 271 ? -8.276  -35.559 -14.786 1.00   42.18  ? 271  VAL B C   1 
ATOM   1981 O O   . VAL A 1 271 ? -8.048  -36.076 -15.881 1.00   42.60  ? 271  VAL B O   1 
ATOM   1982 C CB  . VAL A 1 271 ? -7.623  -36.713 -12.661 1.00   43.08  ? 271  VAL B CB  1 
ATOM   1983 C CG1 . VAL A 1 271 ? -8.147  -37.318 -11.376 1.00   43.38  ? 271  VAL B CG1 1 
ATOM   1984 C CG2 . VAL A 1 271 ? -6.588  -37.629 -13.313 1.00   43.07  ? 271  VAL B CG2 1 
ATOM   1985 N N   . THR A 1 272 ? -8.091  -34.259 -14.566 1.00   40.33  ? 272  THR B N   1 
ATOM   1986 C CA  . THR A 1 272 ? -7.438  -33.459 -15.599 1.00   39.74  ? 272  THR B CA  1 
ATOM   1987 C C   . THR A 1 272 ? -5.929  -33.593 -15.454 1.00   39.61  ? 272  THR B C   1 
ATOM   1988 O O   . THR A 1 272 ? -5.452  -34.215 -14.513 1.00   38.63  ? 272  THR B O   1 
ATOM   1989 C CB  . THR A 1 272 ? -7.850  -31.973 -15.588 1.00   38.95  ? 272  THR B CB  1 
ATOM   1990 O OG1 . THR A 1 272 ? -7.235  -31.316 -14.480 1.00   38.99  ? 272  THR B OG1 1 
ATOM   1991 C CG2 . THR A 1 272 ? -9.358  -31.815 -15.506 1.00   37.92  ? 272  THR B CG2 1 
ATOM   1992 N N   . ASN A 1 273 ? -5.180  -33.031 -16.392 1.00   40.51  ? 273  ASN B N   1 
ATOM   1993 C CA  . ASN A 1 273 ? -3.728  -32.960 -16.248 1.00   41.62  ? 273  ASN B CA  1 
ATOM   1994 C C   . ASN A 1 273 ? -3.238  -31.642 -15.631 1.00   42.45  ? 273  ASN B C   1 
ATOM   1995 O O   . ASN A 1 273 ? -2.104  -31.229 -15.897 1.00   41.97  ? 273  ASN B O   1 
ATOM   1996 C CB  . ASN A 1 273 ? -3.022  -33.220 -17.590 1.00   41.29  ? 273  ASN B CB  1 
ATOM   1997 C CG  . ASN A 1 273 ? -3.424  -32.226 -18.678 1.00   42.72  ? 273  ASN B CG  1 
ATOM   1998 O OD1 . ASN A 1 273 ? -4.462  -31.562 -18.592 1.00   42.96  ? 273  ASN B OD1 1 
ATOM   1999 N ND2 . ASN A 1 273 ? -2.607  -32.141 -19.723 1.00   43.67  ? 273  ASN B ND2 1 
ATOM   2000 N N   . THR A 1 274 ? -4.074  -30.988 -14.814 1.00   43.36  ? 274  THR B N   1 
ATOM   2001 C CA  . THR A 1 274 ? -3.617  -29.806 -14.055 1.00   44.98  ? 274  THR B CA  1 
ATOM   2002 C C   . THR A 1 274 ? -2.455  -30.224 -13.170 1.00   46.44  ? 274  THR B C   1 
ATOM   2003 O O   . THR A 1 274 ? -1.544  -29.440 -12.903 1.00   45.93  ? 274  THR B O   1 
ATOM   2004 C CB  . THR A 1 274 ? -4.699  -29.193 -13.131 1.00   44.80  ? 274  THR B CB  1 
ATOM   2005 O OG1 . THR A 1 274 ? -5.179  -30.188 -12.215 1.00   44.15  ? 274  THR B OG1 1 
ATOM   2006 C CG2 . THR A 1 274 ? -5.858  -28.604 -13.925 1.00   44.74  ? 274  THR B CG2 1 
ATOM   2007 N N   . ILE A 1 275 ? -2.523  -31.465 -12.698 1.00   48.52  ? 275  ILE B N   1 
ATOM   2008 C CA  . ILE A 1 275 ? -1.431  -32.096 -11.986 1.00   50.51  ? 275  ILE B CA  1 
ATOM   2009 C C   . ILE A 1 275 ? -0.943  -33.244 -12.862 1.00   51.48  ? 275  ILE B C   1 
ATOM   2010 O O   . ILE A 1 275 ? -1.760  -33.963 -13.436 1.00   51.57  ? 275  ILE B O   1 
ATOM   2011 C CB  . ILE A 1 275 ? -1.884  -32.597 -10.591 1.00   50.70  ? 275  ILE B CB  1 
ATOM   2012 C CG1 . ILE A 1 275 ? -2.314  -31.403 -9.729  1.00   51.23  ? 275  ILE B CG1 1 
ATOM   2013 C CG2 . ILE A 1 275 ? -0.785  -33.401 -9.902  1.00   50.88  ? 275  ILE B CG2 1 
ATOM   2014 C CD1 . ILE A 1 275 ? -2.918  -31.761 -8.396  1.00   51.37  ? 275  ILE B CD1 1 
ATOM   2015 N N   . PRO A 1 276 ? 0.388   -33.398 -12.998 1.00   52.42  ? 276  PRO B N   1 
ATOM   2016 C CA  . PRO A 1 276 ? 0.974   -34.459 -13.830 1.00   53.77  ? 276  PRO B CA  1 
ATOM   2017 C C   . PRO A 1 276 ? 0.552   -35.852 -13.360 1.00   54.99  ? 276  PRO B C   1 
ATOM   2018 O O   . PRO A 1 276 ? 0.613   -36.151 -12.166 1.00   55.14  ? 276  PRO B O   1 
ATOM   2019 C CB  . PRO A 1 276 ? 2.488   -34.253 -13.661 1.00   53.49  ? 276  PRO B CB  1 
ATOM   2020 C CG  . PRO A 1 276 ? 2.638   -33.392 -12.455 1.00   53.00  ? 276  PRO B CG  1 
ATOM   2021 C CD  . PRO A 1 276 ? 1.428   -32.524 -12.430 1.00   52.72  ? 276  PRO B CD  1 
ATOM   2022 N N   . GLN A 1 277 ? 0.108   -36.681 -14.301 1.00   56.72  ? 277  GLN B N   1 
ATOM   2023 C CA  . GLN A 1 277 ? -0.500  -37.976 -13.980 1.00   58.18  ? 277  GLN B CA  1 
ATOM   2024 C C   . GLN A 1 277 ? 0.220   -39.166 -14.606 1.00   59.19  ? 277  GLN B C   1 
ATOM   2025 O O   . GLN A 1 277 ? -0.123  -40.319 -14.333 1.00   59.43  ? 277  GLN B O   1 
ATOM   2026 C CB  . GLN A 1 277 ? -1.965  -38.000 -14.433 1.00   57.95  ? 277  GLN B CB  1 
ATOM   2027 C CG  . GLN A 1 277 ? -2.823  -36.835 -13.939 1.00   58.19  ? 277  GLN B CG  1 
ATOM   2028 C CD  . GLN A 1 277 ? -2.973  -36.787 -12.420 1.00   57.51  ? 277  GLN B CD  1 
ATOM   2029 O OE1 . GLN A 1 277 ? -3.296  -35.744 -11.858 1.00   56.60  ? 277  GLN B OE1 1 
ATOM   2030 N NE2 . GLN A 1 277 ? -2.751  -37.918 -11.758 1.00   56.78  ? 277  GLN B NE2 1 
ATOM   2031 N N   . GLU A 1 278 ? 1.209   -38.880 -15.446 0.35   60.47  ? 278  GLU B N   1 
ATOM   2032 C CA  . GLU A 1 278 ? 1.845   -39.902 -16.279 0.35   62.20  ? 278  GLU B CA  1 
ATOM   2033 C C   . GLU A 1 278 ? 2.439   -41.057 -15.464 0.35   64.92  ? 278  GLU B C   1 
ATOM   2034 O O   . GLU A 1 278 ? 2.149   -42.229 -15.731 0.35   64.66  ? 278  GLU B O   1 
ATOM   2035 C CB  . GLU A 1 278 ? 2.891   -39.258 -17.198 0.35   61.32  ? 278  GLU B CB  1 
ATOM   2036 C CG  . GLU A 1 278 ? 2.330   -38.132 -18.075 0.35   59.50  ? 278  GLU B CG  1 
ATOM   2037 C CD  . GLU A 1 278 ? 1.916   -36.896 -17.278 0.35   57.21  ? 278  GLU B CD  1 
ATOM   2038 O OE1 . GLU A 1 278 ? 2.808   -36.214 -16.729 0.35   55.83  ? 278  GLU B OE1 1 
ATOM   2039 O OE2 . GLU A 1 278 ? 0.701   -36.597 -17.213 0.35   56.01  ? 278  GLU B OE2 1 
ATOM   2040 N N   . ASP A 1 279 ? 3.249   -40.717 -14.464 0.91   69.25  ? 279  ASP B N   1 
ATOM   2041 C CA  . ASP A 1 279 ? 3.847   -41.705 -13.563 0.91   74.33  ? 279  ASP B CA  1 
ATOM   2042 C C   . ASP A 1 279 ? 2.796   -42.466 -12.741 0.91   74.44  ? 279  ASP B C   1 
ATOM   2043 O O   . ASP A 1 279 ? 2.922   -43.676 -12.530 0.91   74.89  ? 279  ASP B O   1 
ATOM   2044 C CB  . ASP A 1 279 ? 4.866   -41.028 -12.638 0.91   75.32  ? 279  ASP B CB  1 
ATOM   2045 C CG  . ASP A 1 279 ? 5.617   -42.017 -11.760 0.91   81.77  ? 279  ASP B CG  1 
ATOM   2046 O OD1 . ASP A 1 279 ? 5.639   -41.812 -10.528 0.91   77.11  ? 279  ASP B OD1 1 
ATOM   2047 O OD2 . ASP A 1 279 ? 6.183   -42.997 -12.295 0.91   83.03  ? 279  ASP B OD2 1 
ATOM   2048 N N   . LYS A 1 280 ? 1.770   -41.748 -12.284 1.00   75.22  ? 280  LYS B N   1 
ATOM   2049 C CA  . LYS A 1 280 ? 0.662   -42.337 -11.524 1.00   75.72  ? 280  LYS B CA  1 
ATOM   2050 C C   . LYS A 1 280 ? -0.119  -43.372 -12.332 1.00   76.60  ? 280  LYS B C   1 
ATOM   2051 O O   . LYS A 1 280 ? -0.588  -44.373 -11.782 1.00   76.58  ? 280  LYS B O   1 
ATOM   2052 C CB  . LYS A 1 280 ? -0.300  -41.246 -11.038 1.00   75.38  ? 280  LYS B CB  1 
ATOM   2053 C CG  . LYS A 1 280 ? 0.279   -40.299 -9.992  1.00   74.85  ? 280  LYS B CG  1 
ATOM   2054 C CD  . LYS A 1 280 ? 0.478   -40.999 -8.657  1.00   74.93  ? 280  LYS B CD  1 
ATOM   2055 C CE  . LYS A 1 280 ? 1.123   -40.084 -7.626  1.00   75.32  ? 280  LYS B CE  1 
ATOM   2056 N NZ  . LYS A 1 280 ? 0.286   -38.882 -7.329  1.00   75.46  ? 280  LYS B NZ  1 
ATOM   2057 N N   . MET A 1 281 ? -0.258  -43.118 -13.631 1.00   77.73  ? 281  MET B N   1 
ATOM   2058 C CA  . MET A 1 281 ? -1.024  -43.994 -14.514 1.00   78.85  ? 281  MET B CA  1 
ATOM   2059 C C   . MET A 1 281 ? -0.348  -45.345 -14.723 1.00   79.59  ? 281  MET B C   1 
ATOM   2060 O O   . MET A 1 281 ? -1.027  -46.363 -14.879 1.00   79.75  ? 281  MET B O   1 
ATOM   2061 C CB  . MET A 1 281 ? -1.283  -43.312 -15.859 1.00   78.76  ? 281  MET B CB  1 
ATOM   2062 C CG  . MET A 1 281 ? -2.371  -42.251 -15.810 1.00   78.48  ? 281  MET B CG  1 
ATOM   2063 S SD  . MET A 1 281 ? -2.321  -41.143 -17.227 1.00   77.93  ? 281  MET B SD  1 
ATOM   2064 C CE  . MET A 1 281 ? -3.031  -42.177 -18.509 1.00   78.30  ? 281  MET B CE  1 
ATOM   2065 N N   . LYS A 1 282 ? 0.983   -45.350 -14.719 0.67   80.39  ? 282  LYS B N   1 
ATOM   2066 C CA  . LYS A 1 282 ? 1.748   -46.587 -14.858 0.67   81.38  ? 282  LYS B CA  1 
ATOM   2067 C C   . LYS A 1 282 ? 1.412   -47.582 -13.745 0.67   82.13  ? 282  LYS B C   1 
ATOM   2068 O O   . LYS A 1 282 ? 1.390   -48.791 -13.976 0.67   82.16  ? 282  LYS B O   1 
ATOM   2069 C CB  . LYS A 1 282 ? 3.252   -46.298 -14.893 0.67   81.23  ? 282  LYS B CB  1 
ATOM   2070 C CG  . LYS A 1 282 ? 3.704   -45.543 -16.136 0.67   81.52  ? 282  LYS B CG  1 
ATOM   2071 C CD  . LYS A 1 282 ? 5.186   -45.215 -16.091 0.67   81.90  ? 282  LYS B CD  1 
ATOM   2072 C CE  . LYS A 1 282 ? 5.579   -44.324 -17.260 0.67   82.23  ? 282  LYS B CE  1 
ATOM   2073 N NZ  . LYS A 1 282 ? 7.050   -44.114 -17.333 0.67   82.38  ? 282  LYS B NZ  1 
ATOM   2074 N N   . HIS A 1 283 ? 1.134   -47.063 -12.550 1.00   83.15  ? 283  HIS B N   1 
ATOM   2075 C CA  . HIS A 1 283 ? 0.767   -47.897 -11.405 1.00   83.81  ? 283  HIS B CA  1 
ATOM   2076 C C   . HIS A 1 283 ? -0.747  -48.020 -11.188 1.00   82.26  ? 283  HIS B C   1 
ATOM   2077 O O   . HIS A 1 283 ? -1.184  -48.692 -10.249 1.00   82.41  ? 283  HIS B O   1 
ATOM   2078 C CB  . HIS A 1 283 ? 1.426   -47.374 -10.122 1.00   85.49  ? 283  HIS B CB  1 
ATOM   2079 C CG  . HIS A 1 283 ? 2.921   -47.344 -10.173 1.00   90.87  ? 283  HIS B CG  1 
ATOM   2080 N ND1 . HIS A 1 283 ? 3.681   -48.461 -10.449 1.00   94.48  ? 283  HIS B ND1 1 
ATOM   2081 C CD2 . HIS A 1 283 ? 3.799   -46.335 -9.964  1.00   93.27  ? 283  HIS B CD2 1 
ATOM   2082 C CE1 . HIS A 1 283 ? 4.961   -48.138 -10.420 1.00   97.09  ? 283  HIS B CE1 1 
ATOM   2083 N NE2 . HIS A 1 283 ? 5.060   -46.854 -10.127 1.00   99.54  ? 283  HIS B NE2 1 
ATOM   2084 N N   . CYS A 1 284 ? -1.543  -47.383 -12.048 1.00   79.62  ? 284  CYS B N   1 
ATOM   2085 C CA  . CYS A 1 284 ? -2.993  -47.350 -11.853 1.00   76.93  ? 284  CYS B CA  1 
ATOM   2086 C C   . CYS A 1 284 ? -3.772  -47.276 -13.169 1.00   75.77  ? 284  CYS B C   1 
ATOM   2087 O O   . CYS A 1 284 ? -3.842  -46.226 -13.813 1.00   75.52  ? 284  CYS B O   1 
ATOM   2088 C CB  . CYS A 1 284 ? -3.377  -46.195 -10.920 1.00   76.69  ? 284  CYS B CB  1 
ATOM   2089 S SG  . CYS A 1 284 ? -5.068  -46.264 -10.311 1.00   74.71  ? 284  CYS B SG  1 
ATOM   2090 N N   . SER A 1 285 ? -4.367  -48.403 -13.548 1.00   74.30  ? 285  SER B N   1 
ATOM   2091 C CA  . SER A 1 285 ? -5.044  -48.547 -14.839 1.00   72.71  ? 285  SER B CA  1 
ATOM   2092 C C   . SER A 1 285 ? -6.450  -47.941 -14.883 1.00   71.20  ? 285  SER B C   1 
ATOM   2093 O O   . SER A 1 285 ? -7.014  -47.753 -15.966 1.00   70.89  ? 285  SER B O   1 
ATOM   2094 C CB  . SER A 1 285 ? -5.085  -50.022 -15.252 1.00   73.04  ? 285  SER B CB  1 
ATOM   2095 O OG  . SER A 1 285 ? -5.435  -50.856 -14.148 1.00   72.96  ? 285  SER B OG  1 
ATOM   2096 N N   . LYS A 1 286 ? -7.007  -47.644 -13.709 1.00   69.03  ? 286  LYS B N   1 
ATOM   2097 C CA  . LYS A 1 286 ? -8.315  -46.993 -13.610 1.00   66.86  ? 286  LYS B CA  1 
ATOM   2098 C C   . LYS A 1 286 ? -8.276  -45.514 -13.998 1.00   64.92  ? 286  LYS B C   1 
ATOM   2099 O O   . LYS A 1 286 ? -9.303  -44.927 -14.349 1.00   64.68  ? 286  LYS B O   1 
ATOM   2100 C CB  . LYS A 1 286 ? -8.879  -47.129 -12.199 1.00   66.99  ? 286  LYS B CB  1 
ATOM   2101 C CG  . LYS A 1 286 ? -9.278  -48.538 -11.837 1.00   67.88  ? 286  LYS B CG  1 
ATOM   2102 C CD  . LYS A 1 286 ? -10.531 -48.526 -10.983 1.00   68.98  ? 286  LYS B CD  1 
ATOM   2103 C CE  . LYS A 1 286 ? -10.799 -49.900 -10.403 1.00   69.24  ? 286  LYS B CE  1 
ATOM   2104 N NZ  . LYS A 1 286 ? -9.954  -50.152 -9.212  1.00   69.52  ? 286  LYS B NZ  1 
ATOM   2105 N N   . ILE A 1 287 ? -7.089  -44.920 -13.933 1.00   62.47  ? 287  ILE B N   1 
ATOM   2106 C CA  . ILE A 1 287 ? -6.936  -43.490 -14.158 1.00   60.20  ? 287  ILE B CA  1 
ATOM   2107 C C   . ILE A 1 287 ? -6.984  -43.119 -15.639 1.00   58.26  ? 287  ILE B C   1 
ATOM   2108 O O   . ILE A 1 287 ? -6.204  -43.618 -16.451 1.00   58.03  ? 287  ILE B O   1 
ATOM   2109 C CB  . ILE A 1 287 ? -5.646  -42.930 -13.503 1.00   60.38  ? 287  ILE B CB  1 
ATOM   2110 C CG1 . ILE A 1 287 ? -5.679  -43.158 -11.987 1.00   60.52  ? 287  ILE B CG1 1 
ATOM   2111 C CG2 . ILE A 1 287 ? -5.485  -41.442 -13.819 1.00   60.14  ? 287  ILE B CG2 1 
ATOM   2112 C CD1 . ILE A 1 287 ? -4.451  -42.638 -11.248 1.00   60.65  ? 287  ILE B CD1 1 
ATOM   2113 N N   . GLN A 1 288 ? -7.925  -42.248 -15.978 1.00   55.75  ? 288  GLN B N   1 
ATOM   2114 C CA  . GLN A 1 288 ? -7.942  -41.623 -17.286 1.00   53.95  ? 288  GLN B CA  1 
ATOM   2115 C C   . GLN A 1 288 ? -7.740  -40.122 -17.120 1.00   52.88  ? 288  GLN B C   1 
ATOM   2116 O O   . GLN A 1 288 ? -8.059  -39.552 -16.067 1.00   52.12  ? 288  GLN B O   1 
ATOM   2117 C CB  . GLN A 1 288 ? -9.239  -41.954 -18.027 1.00   54.16  ? 288  GLN B CB  1 
ATOM   2118 C CG  . GLN A 1 288 ? -9.439  -43.465 -18.232 1.00   54.78  ? 288  GLN B CG  1 
ATOM   2119 C CD  . GLN A 1 288 ? -10.711 -43.801 -18.979 1.00   56.41  ? 288  GLN B CD  1 
ATOM   2120 O OE1 . GLN A 1 288 ? -11.457 -44.700 -18.587 1.00   56.39  ? 288  GLN B OE1 1 
ATOM   2121 N NE2 . GLN A 1 288 ? -10.969 -43.080 -20.066 1.00   57.43  ? 288  GLN B NE2 1 
ATOM   2122 N N   . VAL A 1 289 ? -7.192  -39.492 -18.155 1.00   51.88  ? 289  VAL B N   1 
ATOM   2123 C CA  . VAL A 1 289 ? -6.772  -38.098 -18.073 1.00   51.10  ? 289  VAL B CA  1 
ATOM   2124 C C   . VAL A 1 289 ? -7.420  -37.237 -19.137 1.00   50.38  ? 289  VAL B C   1 
ATOM   2125 O O   . VAL A 1 289 ? -7.282  -37.508 -20.333 1.00   50.89  ? 289  VAL B O   1 
ATOM   2126 C CB  . VAL A 1 289 ? -5.233  -37.965 -18.189 1.00   51.19  ? 289  VAL B CB  1 
ATOM   2127 C CG1 . VAL A 1 289 ? -4.821  -36.512 -18.370 1.00   51.03  ? 289  VAL B CG1 1 
ATOM   2128 C CG2 . VAL A 1 289 ? -4.561  -38.542 -16.957 1.00   51.56  ? 289  VAL B CG2 1 
ATOM   2129 N N   . ILE A 1 290 ? -8.127  -36.199 -18.699 1.00   49.01  ? 290  ILE B N   1 
ATOM   2130 C CA  . ILE A 1 290 ? -8.579  -35.161 -19.614 1.00   47.58  ? 290  ILE B CA  1 
ATOM   2131 C C   . ILE A 1 290 ? -7.485  -34.103 -19.753 1.00   47.26  ? 290  ILE B C   1 
ATOM   2132 O O   . ILE A 1 290 ? -7.002  -33.555 -18.761 1.00   46.32  ? 290  ILE B O   1 
ATOM   2133 C CB  . ILE A 1 290 ? -9.888  -34.502 -19.143 1.00   47.70  ? 290  ILE B CB  1 
ATOM   2134 C CG1 . ILE A 1 290 ? -10.982 -35.555 -18.973 1.00   47.01  ? 290  ILE B CG1 1 
ATOM   2135 C CG2 . ILE A 1 290 ? -10.332 -33.410 -20.138 1.00   47.44  ? 290  ILE B CG2 1 
ATOM   2136 C CD1 . ILE A 1 290 ? -12.289 -35.014 -18.394 1.00   46.17  ? 290  ILE B CD1 1 
ATOM   2137 N N   . ASP A 1 291 ? -7.090  -33.833 -20.993 1.00   46.91  ? 291  ASP B N   1 
ATOM   2138 C CA  . ASP A 1 291 ? -6.078  -32.822 -21.288 1.00   46.53  ? 291  ASP B CA  1 
ATOM   2139 C C   . ASP A 1 291 ? -6.709  -31.435 -21.228 1.00   45.66  ? 291  ASP B C   1 
ATOM   2140 O O   . ASP A 1 291 ? -7.644  -31.156 -21.968 1.00   45.16  ? 291  ASP B O   1 
ATOM   2141 C CB  . ASP A 1 291 ? -5.489  -33.077 -22.680 1.00   46.97  ? 291  ASP B CB  1 
ATOM   2142 C CG  . ASP A 1 291 ? -4.553  -31.971 -23.138 1.00   48.06  ? 291  ASP B CG  1 
ATOM   2143 O OD1 . ASP A 1 291 ? -3.986  -31.260 -22.282 1.00   47.80  ? 291  ASP B OD1 1 
ATOM   2144 O OD2 . ASP A 1 291 ? -4.381  -31.815 -24.365 1.00   50.14  ? 291  ASP B OD2 1 
ATOM   2145 N N   . ILE A 1 292 ? -6.212  -30.567 -20.351 1.00   44.58  ? 292  ILE B N   1 
ATOM   2146 C CA  . ILE A 1 292 ? -6.790  -29.221 -20.256 1.00   43.56  ? 292  ILE B CA  1 
ATOM   2147 C C   . ILE A 1 292 ? -5.896  -28.117 -20.836 1.00   42.69  ? 292  ILE B C   1 
ATOM   2148 O O   . ILE A 1 292 ? -6.184  -26.922 -20.671 1.00   42.47  ? 292  ILE B O   1 
ATOM   2149 C CB  . ILE A 1 292 ? -7.276  -28.873 -18.808 1.00   43.80  ? 292  ILE B CB  1 
ATOM   2150 C CG1 . ILE A 1 292 ? -6.219  -29.206 -17.752 1.00   42.50  ? 292  ILE B CG1 1 
ATOM   2151 C CG2 . ILE A 1 292 ? -8.570  -29.612 -18.495 1.00   43.77  ? 292  ILE B CG2 1 
ATOM   2152 C CD1 . ILE A 1 292 ? -5.042  -28.272 -17.710 1.00   39.64  ? 292  ILE B CD1 1 
ATOM   2153 N N   . SER A 1 293 ? -4.827  -28.522 -21.520 1.00   41.43  ? 293  SER B N   1 
ATOM   2154 C CA  . SER A 1 293 ? -3.872  -27.575 -22.098 1.00   40.86  ? 293  SER B CA  1 
ATOM   2155 C C   . SER A 1 293 ? -4.506  -26.629 -23.113 1.00   40.56  ? 293  SER B C   1 
ATOM   2156 O O   . SER A 1 293 ? -4.068  -25.487 -23.241 1.00   40.13  ? 293  SER B O   1 
ATOM   2157 C CB  . SER A 1 293 ? -2.691  -28.304 -22.728 1.00   41.12  ? 293  SER B CB  1 
ATOM   2158 O OG  . SER A 1 293 ? -3.129  -29.170 -23.763 1.00   41.63  ? 293  SER B OG  1 
ATOM   2159 N N   . MET A 1 294 ? -5.541  -27.084 -23.811 0.90   40.53  ? 294  MET B N   1 
ATOM   2160 C CA  . MET A 1 294 ? -6.170  -26.237 -24.827 0.90   41.57  ? 294  MET B CA  1 
ATOM   2161 C C   . MET A 1 294 ? -6.931  -25.093 -24.171 0.90   40.46  ? 294  MET B C   1 
ATOM   2162 O O   . MET A 1 294 ? -6.944  -23.970 -24.683 0.90   39.98  ? 294  MET B O   1 
ATOM   2163 C CB  . MET A 1 294 ? -7.079  -27.045 -25.768 0.90   42.38  ? 294  MET B CB  1 
ATOM   2164 C CG  . MET A 1 294 ? -8.362  -27.605 -25.144 0.90   46.40  ? 294  MET B CG  1 
ATOM   2165 S SD  . MET A 1 294 ? -8.091  -28.691 -23.726 0.90   54.53  ? 294  MET B SD  1 
ATOM   2166 C CE  . MET A 1 294 ? -6.935  -29.867 -24.443 0.90   52.81  ? 294  MET B CE  1 
ATOM   2167 N N   . ILE A 1 295 ? -7.544  -25.394 -23.026 1.00   39.63  ? 295  ILE B N   1 
ATOM   2168 C CA  . ILE A 1 295 ? -8.296  -24.414 -22.238 1.00   38.78  ? 295  ILE B CA  1 
ATOM   2169 C C   . ILE A 1 295 ? -7.344  -23.375 -21.656 1.00   37.29  ? 295  ILE B C   1 
ATOM   2170 O O   . ILE A 1 295 ? -7.624  -22.181 -21.699 1.00   37.68  ? 295  ILE B O   1 
ATOM   2171 C CB  . ILE A 1 295 ? -9.102  -25.101 -21.107 1.00   39.51  ? 295  ILE B CB  1 
ATOM   2172 C CG1 . ILE A 1 295 ? -10.073 -26.128 -21.700 1.00   40.84  ? 295  ILE B CG1 1 
ATOM   2173 C CG2 . ILE A 1 295 ? -9.861  -24.076 -20.259 1.00   38.39  ? 295  ILE B CG2 1 
ATOM   2174 C CD1 . ILE A 1 295 ? -10.844 -26.938 -20.665 1.00   42.98  ? 295  ILE B CD1 1 
ATOM   2175 N N   . LEU A 1 296 ? -6.217  -23.835 -21.123 1.00   35.51  ? 296  LEU B N   1 
ATOM   2176 C CA  . LEU A 1 296 ? -5.213  -22.932 -20.587 1.00   34.57  ? 296  LEU B CA  1 
ATOM   2177 C C   . LEU A 1 296 ? -4.607  -22.077 -21.703 1.00   34.34  ? 296  LEU B C   1 
ATOM   2178 O O   . LEU A 1 296 ? -4.543  -20.853 -21.569 1.00   33.07  ? 296  LEU B O   1 
ATOM   2179 C CB  . LEU A 1 296 ? -4.149  -23.699 -19.791 1.00   33.14  ? 296  LEU B CB  1 
ATOM   2180 C CG  . LEU A 1 296 ? -4.664  -24.263 -18.449 1.00   33.44  ? 296  LEU B CG  1 
ATOM   2181 C CD1 . LEU A 1 296 ? -3.597  -25.100 -17.771 1.00   32.48  ? 296  LEU B CD1 1 
ATOM   2182 C CD2 . LEU A 1 296 ? -5.127  -23.160 -17.508 1.00   33.06  ? 296  LEU B CD2 1 
ATOM   2183 N N   . ALA A 1 297 ? -4.231  -22.728 -22.814 1.00   34.11  ? 297  ALA B N   1 
ATOM   2184 C CA  . ALA A 1 297 ? -3.650  -22.069 -23.989 1.00   33.96  ? 297  ALA B CA  1 
ATOM   2185 C C   . ALA A 1 297 ? -4.565  -20.975 -24.512 1.00   33.24  ? 297  ALA B C   1 
ATOM   2186 O O   . ALA A 1 297 ? -4.119  -19.874 -24.829 1.00   34.02  ? 297  ALA B O   1 
ATOM   2187 C CB  . ALA A 1 297 ? -3.360  -23.104 -25.102 1.00   33.80  ? 297  ALA B CB  1 
ATOM   2188 N N   . GLU A 1 298 ? -5.849  -21.294 -24.578 0.71   32.04  ? 298  GLU B N   1 
ATOM   2189 C CA  . GLU A 1 298 ? -6.875  -20.375 -25.036 0.71   32.94  ? 298  GLU B CA  1 
ATOM   2190 C C   . GLU A 1 298 ? -7.113  -19.217 -24.070 0.71   32.90  ? 298  GLU B C   1 
ATOM   2191 O O   . GLU A 1 298 ? -7.362  -18.094 -24.505 0.71   32.13  ? 298  GLU B O   1 
ATOM   2192 C CB  . GLU A 1 298 ? -8.169  -21.155 -25.271 0.71   33.28  ? 298  GLU B CB  1 
ATOM   2193 C CG  . GLU A 1 298 ? -9.271  -20.398 -25.981 0.71   37.22  ? 298  GLU B CG  1 
ATOM   2194 C CD  . GLU A 1 298 ? -8.924  -19.996 -27.411 0.71   40.86  ? 298  GLU B CD  1 
ATOM   2195 O OE1 . GLU A 1 298 ? -7.848  -20.378 -27.932 0.71   42.34  ? 298  GLU B OE1 1 
ATOM   2196 O OE2 . GLU A 1 298 ? -9.747  -19.284 -28.018 0.71   42.71  ? 298  GLU B OE2 1 
ATOM   2197 N N   . ALA A 1 299 ? -7.043  -19.487 -22.766 1.00   33.36  ? 299  ALA B N   1 
ATOM   2198 C CA  . ALA A 1 299 ? -7.171  -18.435 -21.756 1.00   33.42  ? 299  ALA B CA  1 
ATOM   2199 C C   . ALA A 1 299 ? -6.000  -17.453 -21.843 1.00   33.25  ? 299  ALA B C   1 
ATOM   2200 O O   . ALA A 1 299 ? -6.186  -16.240 -21.697 1.00   33.34  ? 299  ALA B O   1 
ATOM   2201 C CB  . ALA A 1 299 ? -7.277  -19.030 -20.342 1.00   33.34  ? 299  ALA B CB  1 
ATOM   2202 N N   . ILE A 1 300 ? -4.808  -17.978 -22.102 1.00   33.17  ? 300  ILE B N   1 
ATOM   2203 C CA  . ILE A 1 300 ? -3.613  -17.151 -22.267 1.00   34.08  ? 300  ILE B CA  1 
ATOM   2204 C C   . ILE A 1 300 ? -3.707  -16.291 -23.535 1.00   35.70  ? 300  ILE B C   1 
ATOM   2205 O O   . ILE A 1 300 ? -3.519  -15.063 -23.493 1.00   34.88  ? 300  ILE B O   1 
ATOM   2206 C CB  . ILE A 1 300 ? -2.332  -18.016 -22.298 1.00   33.90  ? 300  ILE B CB  1 
ATOM   2207 C CG1 . ILE A 1 300 ? -2.064  -18.630 -20.911 1.00   34.58  ? 300  ILE B CG1 1 
ATOM   2208 C CG2 . ILE A 1 300 ? -1.134  -17.200 -22.773 1.00   31.73  ? 300  ILE B CG2 1 
ATOM   2209 C CD1 . ILE A 1 300 ? -1.000  -19.715 -20.901 1.00   31.74  ? 300  ILE B CD1 1 
ATOM   2210 N N   . ARG A 1 301 ? -4.012  -16.941 -24.654 1.00   37.97  ? 301  ARG B N   1 
ATOM   2211 C CA  . ARG A 1 301 ? -4.184  -16.255 -25.932 1.00   40.30  ? 301  ARG B CA  1 
ATOM   2212 C C   . ARG A 1 301 ? -5.202  -15.122 -25.836 1.00   41.26  ? 301  ARG B C   1 
ATOM   2213 O O   . ARG A 1 301 ? -4.931  -14.006 -26.289 1.00   41.28  ? 301  ARG B O   1 
ATOM   2214 C CB  . ARG A 1 301 ? -4.601  -17.249 -27.020 1.00   41.23  ? 301  ARG B CB  1 
ATOM   2215 C CG  . ARG A 1 301 ? -4.779  -16.618 -28.393 1.00   44.73  ? 301  ARG B CG  1 
ATOM   2216 C CD  . ARG A 1 301 ? -5.408  -17.590 -29.383 1.00   51.07  ? 301  ARG B CD  1 
ATOM   2217 N NE  . ARG A 1 301 ? -6.354  -16.885 -30.250 1.00   56.28  ? 301  ARG B NE  1 
ATOM   2218 C CZ  . ARG A 1 301 ? -7.667  -16.844 -30.051 1.00   58.77  ? 301  ARG B CZ  1 
ATOM   2219 N NH1 . ARG A 1 301 ? -8.209  -17.482 -29.024 1.00   60.66  ? 301  ARG B NH1 1 
ATOM   2220 N NH2 . ARG A 1 301 ? -8.447  -16.173 -30.887 1.00   60.72  ? 301  ARG B NH2 1 
ATOM   2221 N N   . ARG A 1 302 ? -6.361  -15.402 -25.241 0.89   42.69  ? 302  ARG B N   1 
ATOM   2222 C CA  . ARG A 1 302 ? -7.410  -14.387 -25.083 0.89   44.19  ? 302  ARG B CA  1 
ATOM   2223 C C   . ARG A 1 302 ? -6.958  -13.254 -24.179 0.89   43.92  ? 302  ARG B C   1 
ATOM   2224 O O   . ARG A 1 302 ? -7.132  -12.081 -24.520 0.89   44.59  ? 302  ARG B O   1 
ATOM   2225 C CB  . ARG A 1 302 ? -8.693  -14.981 -24.509 0.89   44.92  ? 302  ARG B CB  1 
ATOM   2226 C CG  . ARG A 1 302 ? -9.164  -16.237 -25.174 0.89   48.47  ? 302  ARG B CG  1 
ATOM   2227 C CD  . ARG A 1 302 ? -10.274 -15.990 -26.153 0.89   54.17  ? 302  ARG B CD  1 
ATOM   2228 N NE  . ARG A 1 302 ? -10.809 -17.259 -26.633 0.89   57.43  ? 302  ARG B NE  1 
ATOM   2229 C CZ  . ARG A 1 302 ? -12.093 -17.486 -26.894 0.89   59.18  ? 302  ARG B CZ  1 
ATOM   2230 N NH1 . ARG A 1 302 ? -13.003 -16.530 -26.718 0.89   59.23  ? 302  ARG B NH1 1 
ATOM   2231 N NH2 . ARG A 1 302 ? -12.467 -18.681 -27.331 0.89   60.10  ? 302  ARG B NH2 1 
ATOM   2232 N N   . THR A 1 303 ? -6.384  -13.617 -23.027 1.00   42.90  ? 303  THR B N   1 
ATOM   2233 C CA  . THR A 1 303 ? -5.860  -12.649 -22.068 1.00   42.34  ? 303  THR B CA  1 
ATOM   2234 C C   . THR A 1 303 ? -4.901  -11.709 -22.775 1.00   42.37  ? 303  THR B C   1 
ATOM   2235 O O   . THR A 1 303 ? -4.949  -10.494 -22.582 1.00   42.27  ? 303  THR B O   1 
ATOM   2236 C CB  . THR A 1 303 ? -5.092  -13.338 -20.901 1.00   42.30  ? 303  THR B CB  1 
ATOM   2237 O OG1 . THR A 1 303 ? -5.997  -14.115 -20.111 1.00   44.63  ? 303  THR B OG1 1 
ATOM   2238 C CG2 . THR A 1 303 ? -4.426  -12.324 -20.010 1.00   41.65  ? 303  THR B CG2 1 
ATOM   2239 N N   . HIS A 1 304 ? -4.017  -12.275 -23.589 1.00   41.87  ? 304  HIS B N   1 
ATOM   2240 C CA  . HIS A 1 304 ? -3.049  -11.452 -24.303 1.00   42.74  ? 304  HIS B CA  1 
ATOM   2241 C C   . HIS A 1 304 ? -3.708  -10.552 -25.365 1.00   44.00  ? 304  HIS B C   1 
ATOM   2242 O O   . HIS A 1 304 ? -3.267  -9.427  -25.564 1.00   43.95  ? 304  HIS B O   1 
ATOM   2243 C CB  . HIS A 1 304 ? -1.971  -12.318 -24.932 1.00   41.13  ? 304  HIS B CB  1 
ATOM   2244 C CG  . HIS A 1 304 ? -1.028  -11.560 -25.806 1.00   41.44  ? 304  HIS B CG  1 
ATOM   2245 N ND1 . HIS A 1 304 ? 0.014   -10.808 -25.302 1.00   38.08  ? 304  HIS B ND1 1 
ATOM   2246 C CD2 . HIS A 1 304 ? -0.971  -11.432 -27.153 1.00   40.34  ? 304  HIS B CD2 1 
ATOM   2247 C CE1 . HIS A 1 304 ? 0.673   -10.252 -26.304 1.00   40.58  ? 304  HIS B CE1 1 
ATOM   2248 N NE2 . HIS A 1 304 ? 0.096   -10.615 -27.437 1.00   40.01  ? 304  HIS B NE2 1 
ATOM   2249 N N   . ASN A 1 305 ? -4.753  -11.051 -26.028 1.00   46.11  ? 305  ASN B N   1 
ATOM   2250 C CA  . ASN A 1 305 ? -5.432  -10.316 -27.112 1.00   48.12  ? 305  ASN B CA  1 
ATOM   2251 C C   . ASN A 1 305 ? -6.486  -9.348  -26.625 1.00   49.49  ? 305  ASN B C   1 
ATOM   2252 O O   . ASN A 1 305 ? -6.985  -8.525  -27.398 1.00   49.98  ? 305  ASN B O   1 
ATOM   2253 C CB  . ASN A 1 305 ? -6.139  -11.281 -28.068 1.00   48.26  ? 305  ASN B CB  1 
ATOM   2254 C CG  . ASN A 1 305 ? -5.186  -12.139 -28.847 1.00   49.39  ? 305  ASN B CG  1 
ATOM   2255 O OD1 . ASN A 1 305 ? -4.017  -11.809 -28.991 1.00   50.18  ? 305  ASN B OD1 1 
ATOM   2256 N ND2 . ASN A 1 305 ? -5.684  -13.257 -29.361 1.00   52.00  ? 305  ASN B ND2 1 
ATOM   2257 N N   . GLY A 1 306 ? -6.856  -9.471  -25.356 1.00   50.59  ? 306  GLY B N   1 
ATOM   2258 C CA  . GLY A 1 306 ? -7.999  -8.733  -24.825 1.00   52.27  ? 306  GLY B CA  1 
ATOM   2259 C C   . GLY A 1 306 ? -9.328  -9.305  -25.299 1.00   53.55  ? 306  GLY B C   1 
ATOM   2260 O O   . GLY A 1 306 ? -10.312 -8.577  -25.407 1.00   53.21  ? 306  GLY B O   1 
ATOM   2261 N N   . GLU A 1 307 ? -9.363  -10.608 -25.573 1.00   55.62  ? 307  GLU B N   1 
ATOM   2262 C CA  . GLU A 1 307 ? -10.588 -11.270 -26.024 1.00   57.92  ? 307  GLU B CA  1 
ATOM   2263 C C   . GLU A 1 307 ? -11.305 -11.962 -24.875 1.00   58.91  ? 307  GLU B C   1 
ATOM   2264 O O   . GLU A 1 307 ? -10.672 -12.345 -23.882 1.00   58.71  ? 307  GLU B O   1 
ATOM   2265 C CB  . GLU A 1 307 ? -10.280 -12.281 -27.129 1.00   58.22  ? 307  GLU B CB  1 
ATOM   2266 C CG  . GLU A 1 307 ? -9.936  -11.641 -28.463 1.00   60.67  ? 307  GLU B CG  1 
ATOM   2267 C CD  . GLU A 1 307 ? -9.245  -12.590 -29.428 1.00   64.12  ? 307  GLU B CD  1 
ATOM   2268 O OE1 . GLU A 1 307 ? -8.581  -12.085 -30.362 1.00   66.09  ? 307  GLU B OE1 1 
ATOM   2269 O OE2 . GLU A 1 307 ? -9.356  -13.828 -29.265 1.00   65.50  ? 307  GLU B OE2 1 
ATOM   2270 N N   . SER A 1 308 ? -12.619 -12.134 -25.030 1.00   60.13  ? 308  SER B N   1 
ATOM   2271 C CA  . SER A 1 308 ? -13.460 -12.752 -24.010 1.00   61.14  ? 308  SER B CA  1 
ATOM   2272 C C   . SER A 1 308 ? -12.956 -14.131 -23.603 1.00   61.68  ? 308  SER B C   1 
ATOM   2273 O O   . SER A 1 308 ? -12.690 -14.990 -24.447 1.00   62.03  ? 308  SER B O   1 
ATOM   2274 C CB  . SER A 1 308 ? -14.913 -12.842 -24.479 1.00   61.31  ? 308  SER B CB  1 
ATOM   2275 O OG  . SER A 1 308 ? -15.713 -13.497 -23.507 1.00   61.84  ? 308  SER B OG  1 
ATOM   2276 N N   . VAL A 1 309 ? -12.825 -14.321 -22.295 1.00   61.89  ? 309  VAL B N   1 
ATOM   2277 C CA  . VAL A 1 309 ? -12.363 -15.578 -21.725 1.00   62.28  ? 309  VAL B CA  1 
ATOM   2278 C C   . VAL A 1 309 ? -13.563 -16.410 -21.247 1.00   63.29  ? 309  VAL B C   1 
ATOM   2279 O O   . VAL A 1 309 ? -13.444 -17.623 -21.056 1.00   63.21  ? 309  VAL B O   1 
ATOM   2280 C CB  . VAL A 1 309 ? -11.354 -15.311 -20.568 1.00   62.22  ? 309  VAL B CB  1 
ATOM   2281 C CG1 . VAL A 1 309 ? -11.121 -16.555 -19.714 1.00   61.91  ? 309  VAL B CG1 1 
ATOM   2282 C CG2 . VAL A 1 309 ? -10.022 -14.802 -21.120 1.00   60.79  ? 309  VAL B CG2 1 
ATOM   2283 N N   . SER A 1 310 ? -14.719 -15.754 -21.091 1.00   64.18  ? 310  SER B N   1 
ATOM   2284 C CA  . SER A 1 310 ? -15.928 -16.366 -20.509 1.00   65.04  ? 310  SER B CA  1 
ATOM   2285 C C   . SER A 1 310 ? -16.532 -17.451 -21.380 1.00   64.84  ? 310  SER B C   1 
ATOM   2286 O O   . SER A 1 310 ? -17.258 -18.323 -20.905 1.00   65.10  ? 310  SER B O   1 
ATOM   2287 C CB  . SER A 1 310 ? -17.026 -15.307 -20.318 1.00   65.35  ? 310  SER B CB  1 
ATOM   2288 O OG  . SER A 1 310 ? -16.506 -14.124 -19.742 1.00   66.30  ? 310  SER B OG  1 
ATOM   2289 N N   . TYR A 1 311 ? -16.263 -17.344 -22.664 0.64   64.43  ? 311  TYR B N   1 
ATOM   2290 C CA  . TYR A 1 311 ? -16.642 -18.335 -23.651 0.64   64.28  ? 311  TYR B CA  1 
ATOM   2291 C C   . TYR A 1 311 ? -16.299 -19.794 -23.219 0.64   64.47  ? 311  TYR B C   1 
ATOM   2292 O O   . TYR A 1 311 ? -17.090 -20.708 -23.427 0.64   64.06  ? 311  TYR B O   1 
ATOM   2293 C CB  . TYR A 1 311 ? -15.895 -17.841 -24.910 0.64   64.29  ? 311  TYR B CB  1 
ATOM   2294 C CG  . TYR A 1 311 ? -15.919 -18.695 -26.123 0.64   65.46  ? 311  TYR B CG  1 
ATOM   2295 C CD1 . TYR A 1 311 ? -16.488 -18.219 -27.304 0.64   66.68  ? 311  TYR B CD1 1 
ATOM   2296 C CD2 . TYR A 1 311 ? -15.314 -19.945 -26.128 0.64   66.29  ? 311  TYR B CD2 1 
ATOM   2297 C CE1 . TYR A 1 311 ? -16.487 -18.982 -28.450 0.64   67.63  ? 311  TYR B CE1 1 
ATOM   2298 C CE2 . TYR A 1 311 ? -15.306 -20.717 -27.267 0.64   67.46  ? 311  TYR B CE2 1 
ATOM   2299 C CZ  . TYR A 1 311 ? -15.895 -20.229 -28.427 0.64   67.95  ? 311  TYR B CZ  1 
ATOM   2300 O OH  . TYR A 1 311 ? -15.900 -20.992 -29.571 0.64   68.61  ? 311  TYR B OH  1 
ATOM   2301 N N   . LEU A 1 312 ? -15.159 -19.976 -22.564 1.00   65.43  ? 312  LEU B N   1 
ATOM   2302 C CA  . LEU A 1 312 ? -14.660 -21.282 -22.114 1.00   66.74  ? 312  LEU B CA  1 
ATOM   2303 C C   . LEU A 1 312 ? -15.339 -21.898 -20.893 1.00   68.11  ? 312  LEU B C   1 
ATOM   2304 O O   . LEU A 1 312 ? -15.137 -23.077 -20.576 1.00   67.95  ? 312  LEU B O   1 
ATOM   2305 C CB  . LEU A 1 312 ? -13.168 -20.997 -21.669 1.00   66.22  ? 312  LEU B CB  1 
ATOM   2306 C CG  . LEU A 1 312 ? -12.208 -20.796 -22.878 1.00   65.39  ? 312  LEU B CG  1 
ATOM   2307 C CD1 . LEU A 1 312 ? -10.925 -20.199 -22.349 1.00   62.93  ? 312  LEU B CD1 1 
ATOM   2308 C CD2 . LEU A 1 312 ? -11.915 -22.142 -23.535 1.00   64.84  ? 312  LEU B CD2 1 
ATOM   2309 N N   . PHE A 1 313 ? -16.107 -21.071 -20.190 1.00   70.07  ? 313  PHE B N   1 
ATOM   2310 C CA  . PHE A 1 313 ? -16.813 -21.474 -18.978 1.00   71.99  ? 313  PHE B CA  1 
ATOM   2311 C C   . PHE A 1 313 ? -17.916 -22.480 -19.287 1.00   73.05  ? 313  PHE B C   1 
ATOM   2312 O O   . PHE A 1 313 ? -18.427 -23.152 -18.388 1.00   73.31  ? 313  PHE B O   1 
ATOM   2313 C CB  . PHE A 1 313 ? -17.416 -20.239 -18.302 1.00   72.03  ? 313  PHE B CB  1 
ATOM   2314 C CG  . PHE A 1 313 ? -16.399 -19.314 -17.684 1.00   72.41  ? 313  PHE B CG  1 
ATOM   2315 C CD1 . PHE A 1 313 ? -15.031 -19.512 -17.863 1.00   72.83  ? 313  PHE B CD1 1 
ATOM   2316 C CD2 . PHE A 1 313 ? -16.817 -18.219 -16.940 1.00   72.46  ? 313  PHE B CD2 1 
ATOM   2317 C CE1 . PHE A 1 313 ? -14.101 -18.653 -17.294 1.00   72.78  ? 313  PHE B CE1 1 
ATOM   2318 C CE2 . PHE A 1 313 ? -15.892 -17.351 -16.368 1.00   72.48  ? 313  PHE B CE2 1 
ATOM   2319 C CZ  . PHE A 1 313 ? -14.530 -17.570 -16.547 1.00   72.71  ? 313  PHE B CZ  1 
ATOM   2320 N N   . SER A 1 314 ? -18.276 -22.581 -20.563 0.68   74.17  ? 314  SER B N   1 
ATOM   2321 C CA  . SER A 1 314 ? -19.354 -23.457 -20.992 0.68   75.10  ? 314  SER B CA  1 
ATOM   2322 C C   . SER A 1 314 ? -19.038 -24.107 -22.326 0.68   75.44  ? 314  SER B C   1 
ATOM   2323 O O   . SER A 1 314 ? -19.869 -24.819 -22.894 0.68   75.56  ? 314  SER B O   1 
ATOM   2324 C CB  . SER A 1 314 ? -20.651 -22.661 -21.111 0.68   75.27  ? 314  SER B CB  1 
ATOM   2325 O OG  . SER A 1 314 ? -20.516 -21.614 -22.060 0.68   75.75  ? 314  SER B OG  1 
ATOM   2326 N N   . HIS A 1 315 ? -17.833 -23.863 -22.820 0.59   75.86  ? 315  HIS B N   1 
ATOM   2327 C CA  . HIS A 1 315 ? -17.480 -24.261 -24.162 0.59   77.18  ? 315  HIS B CA  1 
ATOM   2328 C C   . HIS A 1 315 ? -16.059 -24.774 -24.151 0.59   79.10  ? 315  HIS B C   1 
ATOM   2329 O O   . HIS A 1 315 ? -15.130 -24.058 -23.775 0.59   78.79  ? 315  HIS B O   1 
ATOM   2330 C CB  . HIS A 1 315 ? -17.631 -23.060 -25.102 0.59   76.39  ? 315  HIS B CB  1 
ATOM   2331 C CG  . HIS A 1 315 ? -17.653 -23.411 -26.556 0.59   76.18  ? 315  HIS B CG  1 
ATOM   2332 N ND1 . HIS A 1 315 ? -17.794 -24.702 -27.019 0.59   76.01  ? 315  HIS B ND1 1 
ATOM   2333 C CD2 . HIS A 1 315 ? -17.599 -22.623 -27.655 0.59   75.85  ? 315  HIS B CD2 1 
ATOM   2334 C CE1 . HIS A 1 315 ? -17.792 -24.696 -28.341 0.59   75.71  ? 315  HIS B CE1 1 
ATOM   2335 N NE2 . HIS A 1 315 ? -17.673 -23.446 -28.752 0.59   75.63  ? 315  HIS B NE2 1 
ATOM   2336 N N   . VAL A 1 316 ? -15.905 -26.034 -24.541 1.00   103.25 ? 316  VAL B N   1 
ATOM   2337 C CA  . VAL A 1 316 ? -14.596 -26.652 -24.664 1.00   100.31 ? 316  VAL B CA  1 
ATOM   2338 C C   . VAL A 1 316 ? -13.999 -26.186 -25.988 1.00   102.03 ? 316  VAL B C   1 
ATOM   2339 O O   . VAL A 1 316 ? -14.614 -26.388 -27.039 1.00   106.78 ? 316  VAL B O   1 
ATOM   2340 C CB  . VAL A 1 316 ? -14.689 -28.197 -24.662 1.00   103.73 ? 316  VAL B CB  1 
ATOM   2341 C CG1 . VAL A 1 316 ? -13.423 -28.805 -24.074 1.00   105.69 ? 316  VAL B CG1 1 
ATOM   2342 C CG2 . VAL A 1 316 ? -15.918 -28.676 -23.886 1.00   95.50  ? 316  VAL B CG2 1 
ATOM   2343 N N   . PRO A 1 317 ? -12.810 -25.553 -25.949 0.54   79.92  ? 317  PRO B N   1 
ATOM   2344 C CA  . PRO A 1 317 ? -12.227 -25.019 -27.184 0.54   77.84  ? 317  PRO B CA  1 
ATOM   2345 C C   . PRO A 1 317 ? -11.822 -26.124 -28.160 0.54   76.94  ? 317  PRO B C   1 
ATOM   2346 O O   . PRO A 1 317 ? -12.641 -26.556 -28.977 0.54   76.31  ? 317  PRO B O   1 
ATOM   2347 C CB  . PRO A 1 317 ? -10.993 -24.259 -26.695 0.54   77.19  ? 317  PRO B CB  1 
ATOM   2348 C CG  . PRO A 1 317 ? -10.628 -24.915 -25.419 0.54   77.59  ? 317  PRO B CG  1 
ATOM   2349 C CD  . PRO A 1 317 ? -11.903 -25.401 -24.796 0.54   79.20  ? 317  PRO B CD  1 
ATOM   2350 N N   . ASN B 1 3   ? 2.414   -12.356 28.724  1.00   53.01  ? 3    ASN A N   1 
ATOM   2351 C CA  . ASN B 1 3   ? 2.498   -11.270 27.699  1.00   52.61  ? 3    ASN A CA  1 
ATOM   2352 C C   . ASN B 1 3   ? 3.500   -11.613 26.601  1.00   51.30  ? 3    ASN A C   1 
ATOM   2353 O O   . ASN B 1 3   ? 3.189   -11.489 25.424  1.00   51.48  ? 3    ASN A O   1 
ATOM   2354 C CB  . ASN B 1 3   ? 2.832   -9.928  28.351  1.00   53.33  ? 3    ASN A CB  1 
ATOM   2355 C CG  . ASN B 1 3   ? 2.798   -8.777  27.371  1.00   55.07  ? 3    ASN A CG  1 
ATOM   2356 O OD1 . ASN B 1 3   ? 1.734   -8.339  26.923  1.00   57.47  ? 3    ASN A OD1 1 
ATOM   2357 N ND2 . ASN B 1 3   ? 3.968   -8.265  27.045  1.00   57.02  ? 3    ASN A ND2 1 
ATOM   2358 N N   . ILE B 1 4   ? 4.695   -12.043 26.988  1.00   48.99  ? 4    ILE A N   1 
ATOM   2359 C CA  . ILE B 1 4   ? 5.648   -12.624 26.041  1.00   47.37  ? 4    ILE A CA  1 
ATOM   2360 C C   . ILE B 1 4   ? 5.326   -14.098 25.755  1.00   45.86  ? 4    ILE A C   1 
ATOM   2361 O O   . ILE B 1 4   ? 5.217   -14.908 26.681  1.00   45.64  ? 4    ILE A O   1 
ATOM   2362 C CB  . ILE B 1 4   ? 7.099   -12.485 26.548  1.00   47.52  ? 4    ILE A CB  1 
ATOM   2363 C CG1 . ILE B 1 4   ? 8.089   -13.114 25.567  1.00   48.22  ? 4    ILE A CG1 1 
ATOM   2364 C CG2 . ILE B 1 4   ? 7.253   -13.092 27.950  1.00   48.70  ? 4    ILE A CG2 1 
ATOM   2365 C CD1 . ILE B 1 4   ? 9.532   -12.734 25.852  1.00   50.81  ? 4    ILE A CD1 1 
ATOM   2366 N N   . LYS B 1 5   ? 5.179   -14.434 24.472  1.00   43.52  ? 5    LYS A N   1 
ATOM   2367 C CA  . LYS B 1 5   ? 4.979   -15.817 24.035  1.00   41.60  ? 5    LYS A CA  1 
ATOM   2368 C C   . LYS B 1 5   ? 6.022   -16.212 22.993  1.00   41.10  ? 5    LYS A C   1 
ATOM   2369 O O   . LYS B 1 5   ? 6.218   -15.497 22.003  1.00   41.15  ? 5    LYS A O   1 
ATOM   2370 C CB  . LYS B 1 5   ? 3.569   -16.011 23.476  1.00   41.68  ? 5    LYS A CB  1 
ATOM   2371 C CG  . LYS B 1 5   ? 2.604   -16.662 24.451  1.00   44.98  ? 5    LYS A CG  1 
ATOM   2372 C CD  . LYS B 1 5   ? 2.955   -18.137 24.645  1.00   49.34  ? 5    LYS A CD  1 
ATOM   2373 C CE  . LYS B 1 5   ? 2.526   -18.633 26.009  1.00   51.56  ? 5    LYS A CE  1 
ATOM   2374 N NZ  . LYS B 1 5   ? 3.001   -20.030 26.253  1.00   54.41  ? 5    LYS A NZ  1 
ATOM   2375 N N   . ILE B 1 6   ? 6.702   -17.333 23.220  1.00   39.49  ? 6    ILE A N   1 
ATOM   2376 C CA  . ILE B 1 6   ? 7.706   -17.821 22.276  1.00   38.50  ? 6    ILE A CA  1 
ATOM   2377 C C   . ILE B 1 6   ? 7.255   -19.133 21.647  1.00   37.91  ? 6    ILE A C   1 
ATOM   2378 O O   . ILE B 1 6   ? 6.919   -20.085 22.354  1.00   36.37  ? 6    ILE A O   1 
ATOM   2379 C CB  . ILE B 1 6   ? 9.098   -18.034 22.921  1.00   39.06  ? 6    ILE A CB  1 
ATOM   2380 C CG1 . ILE B 1 6   ? 9.651   -16.722 23.481  1.00   40.60  ? 6    ILE A CG1 1 
ATOM   2381 C CG2 . ILE B 1 6   ? 10.089  -18.593 21.888  1.00   37.59  ? 6    ILE A CG2 1 
ATOM   2382 C CD1 . ILE B 1 6   ? 10.993  -16.877 24.151  1.00   43.38  ? 6    ILE A CD1 1 
ATOM   2383 N N   . PHE B 1 7   ? 7.258   -19.160 20.314  1.00   36.94  ? 7    PHE A N   1 
ATOM   2384 C CA  . PHE B 1 7   ? 6.912   -20.336 19.522  1.00   38.28  ? 7    PHE A CA  1 
ATOM   2385 C C   . PHE B 1 7   ? 8.106   -20.737 18.662  1.00   40.73  ? 7    PHE A C   1 
ATOM   2386 O O   . PHE B 1 7   ? 8.928   -19.896 18.272  1.00   39.07  ? 7    PHE A O   1 
ATOM   2387 C CB  . PHE B 1 7   ? 5.727   -20.051 18.591  1.00   37.93  ? 7    PHE A CB  1 
ATOM   2388 C CG  . PHE B 1 7   ? 4.407   -19.875 19.289  1.00   37.68  ? 7    PHE A CG  1 
ATOM   2389 C CD1 . PHE B 1 7   ? 3.984   -18.610 19.684  1.00   37.97  ? 7    PHE A CD1 1 
ATOM   2390 C CD2 . PHE B 1 7   ? 3.559   -20.961 19.507  1.00   36.37  ? 7    PHE A CD2 1 
ATOM   2391 C CE1 . PHE B 1 7   ? 2.760   -18.439 20.317  1.00   39.06  ? 7    PHE A CE1 1 
ATOM   2392 C CE2 . PHE B 1 7   ? 2.329   -20.794 20.133  1.00   36.59  ? 7    PHE A CE2 1 
ATOM   2393 C CZ  . PHE B 1 7   ? 1.928   -19.535 20.538  1.00   38.09  ? 7    PHE A CZ  1 
ATOM   2394 N N   . SER B 1 8   ? 8.188   -22.025 18.350  1.00   45.13  ? 8    SER A N   1 
ATOM   2395 C CA  . SER B 1 8   ? 9.278   -22.559 17.550  1.00   51.82  ? 8    SER A CA  1 
ATOM   2396 C C   . SER B 1 8   ? 8.786   -23.068 16.205  1.00   57.53  ? 8    SER A C   1 
ATOM   2397 O O   . SER B 1 8   ? 7.659   -23.547 16.096  1.00   57.24  ? 8    SER A O   1 
ATOM   2398 C CB  . SER B 1 8   ? 9.939   -23.715 18.291  1.00   51.39  ? 8    SER A CB  1 
ATOM   2399 O OG  . SER B 1 8   ? 10.900  -24.355 17.467  1.00   51.82  ? 8    SER A OG  1 
ATOM   2400 N N   . GLY B 1 9   ? 9.645   -22.979 15.189  1.00   65.52  ? 9    GLY A N   1 
ATOM   2401 C CA  . GLY B 1 9   ? 9.415   -23.659 13.908  1.00   76.05  ? 9    GLY A CA  1 
ATOM   2402 C C   . GLY B 1 9   ? 9.470   -25.186 14.020  1.00   83.73  ? 9    GLY A C   1 
ATOM   2403 O O   . GLY B 1 9   ? 9.896   -25.735 15.038  1.00   83.93  ? 9    GLY A O   1 
ATOM   2404 N N   . SER B 1 10  ? 9.122   -25.858 12.959  1.00   111.23 ? 10   SER A N   1 
ATOM   2405 C CA  . SER B 1 10  ? 8.925   -27.276 13.047  1.00   114.73 ? 10   SER A CA  1 
ATOM   2406 C C   . SER B 1 10  ? 10.152  -28.049 13.391  1.00   117.37 ? 10   SER A C   1 
ATOM   2407 O O   . SER B 1 10  ? 11.208  -27.854 12.805  1.00   121.99 ? 10   SER A O   1 
ATOM   2408 C CB  . SER B 1 10  ? 8.510   -27.839 11.697  1.00   115.09 ? 10   SER A CB  1 
ATOM   2409 O OG  . SER B 1 10  ? 9.635   -28.311 10.989  1.00   119.19 ? 10   SER A OG  1 
ATOM   2410 N N   . SER B 1 11  ? 9.976   -28.943 14.347  1.00   102.64 ? 11   SER A N   1 
ATOM   2411 C CA  . SER B 1 11  ? 10.895  -30.021 14.582  1.00   104.82 ? 11   SER A CA  1 
ATOM   2412 C C   . SER B 1 11  ? 12.146  -29.521 15.242  1.00   100.95 ? 11   SER A C   1 
ATOM   2413 O O   . SER B 1 11  ? 12.537  -30.052 16.273  1.00   101.73 ? 11   SER A O   1 
ATOM   2414 C CB  . SER B 1 11  ? 11.307  -30.718 13.283  1.00   112.45 ? 11   SER A CB  1 
ATOM   2415 N N   . HIS B 1 12  ? 12.770  -28.508 14.646  0.010  96.53  ? 12   HIS A N   1 
ATOM   2416 C CA  . HIS B 1 12  ? 13.992  -27.917 15.180  0.010  91.88  ? 12   HIS A CA  1 
ATOM   2417 C C   . HIS B 1 12  ? 13.626  -27.036 16.329  0.010  87.86  ? 12   HIS A C   1 
ATOM   2418 O O   . HIS B 1 12  ? 13.285  -25.872 16.158  0.010  87.63  ? 12   HIS A O   1 
ATOM   2419 C CB  . HIS B 1 12  ? 14.751  -27.160 14.097  0.010  92.43  ? 12   HIS A CB  1 
ATOM   2420 C CG  . HIS B 1 12  ? 15.511  -25.951 14.600  0.010  92.25  ? 12   HIS A CG  1 
ATOM   2421 N ND1 . HIS B 1 12  ? 14.960  -24.744 14.686  0.010  92.31  ? 12   HIS A ND1 1 
ATOM   2422 C CD2 . HIS B 1 12  ? 16.829  -25.806 15.003  0.010  92.30  ? 12   HIS A CD2 1 
ATOM   2423 C CE1 . HIS B 1 12  ? 15.868  -23.867 15.141  0.010  92.27  ? 12   HIS A CE1 1 
ATOM   2424 N NE2 . HIS B 1 12  ? 17.012  -24.520 15.328  0.010  92.31  ? 12   HIS A NE2 1 
ATOM   2425 N N   . GLN B 1 13  ? 13.748  -27.563 17.512  1.00   82.07  ? 13   GLN A N   1 
ATOM   2426 C CA  . GLN B 1 13  ? 13.322  -26.917 18.748  1.00   76.39  ? 13   GLN A CA  1 
ATOM   2427 C C   . GLN B 1 13  ? 14.485  -26.604 19.669  1.00   72.16  ? 13   GLN A C   1 
ATOM   2428 O O   . GLN B 1 13  ? 14.339  -25.818 20.600  1.00   71.40  ? 13   GLN A O   1 
ATOM   2429 C CB  . GLN B 1 13  ? 12.327  -27.835 19.471  1.00   76.75  ? 13   GLN A CB  1 
ATOM   2430 C CG  . GLN B 1 13  ? 10.852  -27.566 19.166  1.00   77.23  ? 13   GLN A CG  1 
ATOM   2431 C CD  . GLN B 1 13  ? 9.914   -28.052 20.272  1.00   78.07  ? 13   GLN A CD  1 
ATOM   2432 O OE1 . GLN B 1 13  ? 8.694   -27.907 20.173  1.00   78.38  ? 13   GLN A OE1 1 
ATOM   2433 N NE2 . GLN B 1 13  ? 10.482  -28.623 21.332  1.00   78.31  ? 13   GLN A NE2 1 
ATOM   2434 N N   . ASP B 1 14  ? 15.641  -27.205 19.401  1.00   67.32  ? 14   ASP A N   1 
ATOM   2435 C CA  . ASP B 1 14  ? 16.776  -27.091 20.313  1.00   63.26  ? 14   ASP A CA  1 
ATOM   2436 C C   . ASP B 1 14  ? 17.162  -25.646 20.604  1.00   59.34  ? 14   ASP A C   1 
ATOM   2437 O O   . ASP B 1 14  ? 17.292  -25.273 21.769  1.00   59.13  ? 14   ASP A O   1 
ATOM   2438 C CB  . ASP B 1 14  ? 17.982  -27.898 19.827  1.00   63.97  ? 14   ASP A CB  1 
ATOM   2439 C CG  . ASP B 1 14  ? 19.015  -28.123 20.923  1.00   65.86  ? 14   ASP A CG  1 
ATOM   2440 O OD1 . ASP B 1 14  ? 20.209  -28.295 20.589  1.00   71.79  ? 14   ASP A OD1 1 
ATOM   2441 O OD2 . ASP B 1 14  ? 18.641  -28.130 22.118  1.00   67.63  ? 14   ASP A OD2 1 
ATOM   2442 N N   . LEU B 1 15  ? 17.329  -24.835 19.558  1.00   54.46  ? 15   LEU A N   1 
ATOM   2443 C CA  . LEU B 1 15  ? 17.612  -23.411 19.747  1.00   50.11  ? 15   LEU A CA  1 
ATOM   2444 C C   . LEU B 1 15  ? 16.446  -22.733 20.456  1.00   48.20  ? 15   LEU A C   1 
ATOM   2445 O O   . LEU B 1 15  ? 16.644  -22.034 21.449  1.00   47.61  ? 15   LEU A O   1 
ATOM   2446 C CB  . LEU B 1 15  ? 17.880  -22.707 18.414  1.00   49.28  ? 15   LEU A CB  1 
ATOM   2447 C CG  . LEU B 1 15  ? 18.952  -21.613 18.353  1.00   47.95  ? 15   LEU A CG  1 
ATOM   2448 C CD1 . LEU B 1 15  ? 18.705  -20.700 17.143  1.00   46.44  ? 15   LEU A CD1 1 
ATOM   2449 C CD2 . LEU B 1 15  ? 19.061  -20.775 19.627  1.00   43.95  ? 15   LEU A CD2 1 
ATOM   2450 N N   . SER B 1 16  ? 15.236  -22.962 19.953  1.00   46.49  ? 16   SER A N   1 
ATOM   2451 C CA  . SER B 1 16  ? 14.031  -22.342 20.493  1.00   46.38  ? 16   SER A CA  1 
ATOM   2452 C C   . SER B 1 16  ? 13.791  -22.694 21.956  1.00   46.32  ? 16   SER A C   1 
ATOM   2453 O O   . SER B 1 16  ? 13.205  -21.904 22.701  1.00   45.48  ? 16   SER A O   1 
ATOM   2454 C CB  . SER B 1 16  ? 12.817  -22.775 19.685  1.00   45.76  ? 16   SER A CB  1 
ATOM   2455 O OG  . SER B 1 16  ? 12.852  -22.191 18.404  1.00   47.89  ? 16   SER A OG  1 
ATOM   2456 N N   . GLN B 1 17  ? 14.241  -23.883 22.345  1.00   46.63  ? 17   GLN A N   1 
ATOM   2457 C CA  . GLN B 1 17  ? 14.084  -24.380 23.706  1.00   47.82  ? 17   GLN A CA  1 
ATOM   2458 C C   . GLN B 1 17  ? 15.123  -23.723 24.594  1.00   47.80  ? 17   GLN A C   1 
ATOM   2459 O O   . GLN B 1 17  ? 14.831  -23.343 25.725  1.00   47.93  ? 17   GLN A O   1 
ATOM   2460 C CB  . GLN B 1 17  ? 14.238  -25.908 23.739  1.00   48.35  ? 17   GLN A CB  1 
ATOM   2461 C CG  . GLN B 1 17  ? 13.974  -26.554 25.095  1.00   50.89  ? 17   GLN A CG  1 
ATOM   2462 C CD  . GLN B 1 17  ? 12.579  -26.264 25.623  1.00   53.83  ? 17   GLN A CD  1 
ATOM   2463 O OE1 . GLN B 1 17  ? 11.579  -26.688 25.038  1.00   55.46  ? 17   GLN A OE1 1 
ATOM   2464 N NE2 . GLN B 1 17  ? 12.507  -25.540 26.740  1.00   54.13  ? 17   GLN A NE2 1 
ATOM   2465 N N   . LYS B 1 18  ? 16.339  -23.587 24.077  1.00   47.72  ? 18   LYS A N   1 
ATOM   2466 C CA  . LYS B 1 18  ? 17.382  -22.908 24.815  1.00   47.50  ? 18   LYS A CA  1 
ATOM   2467 C C   . LYS B 1 18  ? 16.928  -21.488 25.108  1.00   46.26  ? 18   LYS A C   1 
ATOM   2468 O O   . LYS B 1 18  ? 17.016  -21.027 26.252  1.00   46.55  ? 18   LYS A O   1 
ATOM   2469 C CB  . LYS B 1 18  ? 18.703  -22.921 24.047  1.00   48.22  ? 18   LYS A CB  1 
ATOM   2470 C CG  . LYS B 1 18  ? 19.456  -24.233 24.147  1.00   50.52  ? 18   LYS A CG  1 
ATOM   2471 C CD  . LYS B 1 18  ? 20.800  -24.158 23.438  1.00   54.39  ? 18   LYS A CD  1 
ATOM   2472 C CE  . LYS B 1 18  ? 21.649  -25.393 23.701  1.00   56.18  ? 18   LYS A CE  1 
ATOM   2473 N NZ  . LYS B 1 18  ? 21.065  -26.641 23.117  1.00   58.52  ? 18   LYS A NZ  1 
ATOM   2474 N N   . ILE B 1 19  ? 16.405  -20.813 24.084  1.00   44.14  ? 19   ILE A N   1 
ATOM   2475 C CA  . ILE B 1 19  ? 15.896  -19.451 24.240  1.00   41.70  ? 19   ILE A CA  1 
ATOM   2476 C C   . ILE B 1 19  ? 14.776  -19.381 25.268  1.00   41.61  ? 19   ILE A C   1 
ATOM   2477 O O   . ILE B 1 19  ? 14.812  -18.540 26.160  1.00   39.96  ? 19   ILE A O   1 
ATOM   2478 C CB  . ILE B 1 19  ? 15.404  -18.858 22.899  1.00   41.26  ? 19   ILE A CB  1 
ATOM   2479 C CG1 . ILE B 1 19  ? 16.588  -18.666 21.947  1.00   39.52  ? 19   ILE A CG1 1 
ATOM   2480 C CG2 . ILE B 1 19  ? 14.695  -17.525 23.132  1.00   41.33  ? 19   ILE A CG2 1 
ATOM   2481 C CD1 . ILE B 1 19  ? 16.203  -18.561 20.463  1.00   38.26  ? 19   ILE A CD1 1 
ATOM   2482 N N   . ALA B 1 20  ? 13.780  -20.257 25.156  1.00   42.35  ? 20   ALA A N   1 
ATOM   2483 C CA  . ALA B 1 20  ? 12.669  -20.200 26.096  1.00   43.95  ? 20   ALA A CA  1 
ATOM   2484 C C   . ALA B 1 20  ? 13.139  -20.451 27.537  1.00   45.48  ? 20   ALA A C   1 
ATOM   2485 O O   . ALA B 1 20  ? 12.588  -19.869 28.471  1.00   45.66  ? 20   ALA A O   1 
ATOM   2486 C CB  . ALA B 1 20  ? 11.563  -21.162 25.705  1.00   43.10  ? 20   ALA A CB  1 
ATOM   2487 N N   . ASP B 1 21  ? 14.158  -21.293 27.705  1.00   47.51  ? 21   ASP A N   1 
ATOM   2488 C CA  . ASP B 1 21  ? 14.688  -21.603 29.035  1.00   49.14  ? 21   ASP A CA  1 
ATOM   2489 C C   . ASP B 1 21  ? 15.260  -20.363 29.700  1.00   48.73  ? 21   ASP A C   1 
ATOM   2490 O O   . ASP B 1 21  ? 14.855  -20.006 30.813  1.00   49.25  ? 21   ASP A O   1 
ATOM   2491 C CB  . ASP B 1 21  ? 15.747  -22.707 28.961  1.00   50.11  ? 21   ASP A CB  1 
ATOM   2492 C CG  . ASP B 1 21  ? 15.157  -24.063 28.612  1.00   52.55  ? 21   ASP A CG  1 
ATOM   2493 O OD1 . ASP B 1 21  ? 13.920  -24.224 28.710  1.00   55.09  ? 21   ASP A OD1 1 
ATOM   2494 O OD2 . ASP B 1 21  ? 15.929  -24.972 28.231  1.00   55.30  ? 21   ASP A OD2 1 
ATOM   2495 N N   . ARG B 1 22  ? 16.169  -19.696 28.992  0.89   47.25  ? 22   ARG A N   1 
ATOM   2496 C CA  . ARG B 1 22  ? 16.828  -18.483 29.481  0.89   46.82  ? 22   ARG A CA  1 
ATOM   2497 C C   . ARG B 1 22  ? 15.850  -17.371 29.843  0.89   46.34  ? 22   ARG A C   1 
ATOM   2498 O O   . ARG B 1 22  ? 16.197  -16.446 30.580  0.89   46.92  ? 22   ARG A O   1 
ATOM   2499 C CB  . ARG B 1 22  ? 17.843  -17.970 28.456  0.89   46.00  ? 22   ARG A CB  1 
ATOM   2500 C CG  . ARG B 1 22  ? 18.944  -18.959 28.128  0.89   47.25  ? 22   ARG A CG  1 
ATOM   2501 C CD  . ARG B 1 22  ? 20.027  -18.289 27.312  0.89   49.62  ? 22   ARG A CD  1 
ATOM   2502 N NE  . ARG B 1 22  ? 21.102  -19.206 26.929  0.89   50.72  ? 22   ARG A NE  1 
ATOM   2503 C CZ  . ARG B 1 22  ? 22.214  -19.414 27.637  0.89   52.87  ? 22   ARG A CZ  1 
ATOM   2504 N NH1 . ARG B 1 22  ? 22.415  -18.786 28.794  0.89   52.57  ? 22   ARG A NH1 1 
ATOM   2505 N NH2 . ARG B 1 22  ? 23.133  -20.266 27.191  0.89   52.94  ? 22   ARG A NH2 1 
ATOM   2506 N N   . LEU B 1 23  ? 14.632  -17.455 29.323  1.00   45.98  ? 23   LEU A N   1 
ATOM   2507 C CA  . LEU B 1 23  ? 13.622  -16.447 29.615  1.00   45.47  ? 23   LEU A CA  1 
ATOM   2508 C C   . LEU B 1 23  ? 12.622  -16.927 30.665  1.00   44.30  ? 23   LEU A C   1 
ATOM   2509 O O   . LEU B 1 23  ? 11.748  -16.168 31.077  1.00   44.61  ? 23   LEU A O   1 
ATOM   2510 C CB  . LEU B 1 23  ? 12.900  -16.010 28.333  1.00   45.75  ? 23   LEU A CB  1 
ATOM   2511 C CG  . LEU B 1 23  ? 13.743  -15.299 27.263  1.00   47.10  ? 23   LEU A CG  1 
ATOM   2512 C CD1 . LEU B 1 23  ? 13.004  -15.245 25.957  1.00   47.80  ? 23   LEU A CD1 1 
ATOM   2513 C CD2 . LEU B 1 23  ? 14.133  -13.893 27.696  1.00   47.79  ? 23   LEU A CD2 1 
ATOM   2514 N N   . GLY B 1 24  ? 12.748  -18.183 31.087  1.00   42.82  ? 24   GLY A N   1 
ATOM   2515 C CA  . GLY B 1 24  ? 11.868  -18.745 32.117  1.00   41.10  ? 24   GLY A CA  1 
ATOM   2516 C C   . GLY B 1 24  ? 10.488  -19.072 31.588  1.00   40.17  ? 24   GLY A C   1 
ATOM   2517 O O   . GLY B 1 24  ? 9.496   -19.036 32.327  1.00   40.03  ? 24   GLY A O   1 
ATOM   2518 N N   . LEU B 1 25  ? 10.422  -19.405 30.300  1.00   38.60  ? 25   LEU A N   1 
ATOM   2519 C CA  . LEU B 1 25  ? 9.145   -19.645 29.640  1.00   36.43  ? 25   LEU A CA  1 
ATOM   2520 C C   . LEU B 1 25  ? 9.095   -21.041 29.063  1.00   34.41  ? 25   LEU A C   1 
ATOM   2521 O O   . LEU B 1 25  ? 10.133  -21.627 28.769  1.00   34.31  ? 25   LEU A O   1 
ATOM   2522 C CB  . LEU B 1 25  ? 8.945   -18.645 28.493  1.00   36.91  ? 25   LEU A CB  1 
ATOM   2523 C CG  . LEU B 1 25  ? 9.060   -17.158 28.802  1.00   38.66  ? 25   LEU A CG  1 
ATOM   2524 C CD1 . LEU B 1 25  ? 8.881   -16.361 27.512  1.00   40.03  ? 25   LEU A CD1 1 
ATOM   2525 C CD2 . LEU B 1 25  ? 8.038   -16.730 29.873  1.00   40.17  ? 25   LEU A CD2 1 
ATOM   2526 N N   . GLU B 1 26  ? 7.887   -21.570 28.902  0.50   32.17  ? 26   GLU A N   1 
ATOM   2527 C CA  . GLU B 1 26  ? 7.697   -22.756 28.094  0.50   31.44  ? 26   GLU A CA  1 
ATOM   2528 C C   . GLU B 1 26  ? 7.361   -22.305 26.669  0.50   31.88  ? 26   GLU A C   1 
ATOM   2529 O O   . GLU B 1 26  ? 6.730   -21.254 26.475  0.50   27.82  ? 26   GLU A O   1 
ATOM   2530 C CB  . GLU B 1 26  ? 6.586   -23.639 28.657  0.50   31.36  ? 26   GLU A CB  1 
ATOM   2531 C CG  . GLU B 1 26  ? 6.892   -24.244 30.034  0.50   33.18  ? 26   GLU A CG  1 
ATOM   2532 C CD  . GLU B 1 26  ? 5.753   -25.110 30.565  0.50   36.06  ? 26   GLU A CD  1 
ATOM   2533 O OE1 . GLU B 1 26  ? 4.797   -25.394 29.803  0.50   36.73  ? 26   GLU A OE1 1 
ATOM   2534 O OE2 . GLU B 1 26  ? 5.817   -25.504 31.751  0.50   38.63  ? 26   GLU A OE2 1 
ATOM   2535 N N   . LEU B 1 27  ? 7.801   -23.086 25.682  1.00   34.34  ? 27   LEU A N   1 
ATOM   2536 C CA  . LEU B 1 27  ? 7.438   -22.833 24.282  1.00   37.27  ? 27   LEU A CA  1 
ATOM   2537 C C   . LEU B 1 27  ? 5.932   -22.966 24.091  1.00   38.14  ? 27   LEU A C   1 
ATOM   2538 O O   . LEU B 1 27  ? 5.310   -23.870 24.641  1.00   38.57  ? 27   LEU A O   1 
ATOM   2539 C CB  . LEU B 1 27  ? 8.164   -23.794 23.335  1.00   37.59  ? 27   LEU A CB  1 
ATOM   2540 C CG  . LEU B 1 27  ? 9.667   -23.598 23.088  1.00   39.97  ? 27   LEU A CG  1 
ATOM   2541 C CD1 . LEU B 1 27  ? 10.230  -24.770 22.295  1.00   41.46  ? 27   LEU A CD1 1 
ATOM   2542 C CD2 . LEU B 1 27  ? 9.964   -22.287 22.370  1.00   41.59  ? 27   LEU A CD2 1 
ATOM   2543 N N   . GLY B 1 28  ? 5.348   -22.060 23.314  1.00   38.99  ? 28   GLY A N   1 
ATOM   2544 C CA  . GLY B 1 28  ? 3.912   -22.099 23.036  1.00   39.87  ? 28   GLY A CA  1 
ATOM   2545 C C   . GLY B 1 28  ? 3.496   -23.374 22.322  1.00   40.55  ? 28   GLY A C   1 
ATOM   2546 O O   . GLY B 1 28  ? 4.294   -23.978 21.604  1.00   41.31  ? 28   GLY A O   1 
ATOM   2547 N N   . LYS B 1 29  ? 2.245   -23.779 22.527  0.53   40.63  ? 29   LYS A N   1 
ATOM   2548 C CA  . LYS B 1 29  ? 1.697   -24.972 21.900  0.53   43.03  ? 29   LYS A CA  1 
ATOM   2549 C C   . LYS B 1 29  ? 1.374   -24.695 20.436  0.53   45.70  ? 29   LYS A C   1 
ATOM   2550 O O   . LYS B 1 29  ? 0.663   -23.739 20.116  0.53   44.07  ? 29   LYS A O   1 
ATOM   2551 C CB  . LYS B 1 29  ? 0.429   -25.430 22.633  0.53   42.62  ? 29   LYS A CB  1 
ATOM   2552 C CG  . LYS B 1 29  ? 0.594   -25.589 24.149  0.53   43.58  ? 29   LYS A CG  1 
ATOM   2553 C CD  . LYS B 1 29  ? -0.601  -26.293 24.798  0.53   45.09  ? 29   LYS A CD  1 
ATOM   2554 C CE  . LYS B 1 29  ? -1.765  -25.339 25.091  0.53   46.19  ? 29   LYS A CE  1 
ATOM   2555 N NZ  . LYS B 1 29  ? -1.462  -24.361 26.178  0.53   46.96  ? 29   LYS A NZ  1 
ATOM   2556 N N   . VAL B 1 30  ? 1.915   -25.524 19.551  1.00   50.81  ? 30   VAL A N   1 
ATOM   2557 C CA  . VAL B 1 30  ? 1.550   -25.473 18.134  1.00   57.23  ? 30   VAL A CA  1 
ATOM   2558 C C   . VAL B 1 30  ? 1.536   -26.869 17.518  1.00   62.16  ? 30   VAL A C   1 
ATOM   2559 O O   . VAL B 1 30  ? 2.451   -27.664 17.739  1.00   62.51  ? 30   VAL A O   1 
ATOM   2560 C CB  . VAL B 1 30  ? 2.447   -24.502 17.308  1.00   56.87  ? 30   VAL A CB  1 
ATOM   2561 C CG1 . VAL B 1 30  ? 3.925   -24.764 17.527  1.00   56.20  ? 30   VAL A CG1 1 
ATOM   2562 C CG2 . VAL B 1 30  ? 2.088   -24.548 15.827  1.00   57.59  ? 30   VAL A CG2 1 
ATOM   2563 N N   . VAL B 1 31  ? 0.479   -27.156 16.764  1.00   68.81  ? 31   VAL A N   1 
ATOM   2564 C CA  . VAL B 1 31  ? 0.357   -28.408 16.021  1.00   75.41  ? 31   VAL A CA  1 
ATOM   2565 C C   . VAL B 1 31  ? 0.901   -28.209 14.605  1.00   79.26  ? 31   VAL A C   1 
ATOM   2566 O O   . VAL B 1 31  ? 0.154   -27.818 13.701  1.00   79.93  ? 31   VAL A O   1 
ATOM   2567 C CB  . VAL B 1 31  ? -1.121  -28.868 15.924  1.00   75.31  ? 31   VAL A CB  1 
ATOM   2568 C CG1 . VAL B 1 31  ? -1.207  -30.308 15.429  1.00   76.19  ? 31   VAL A CG1 1 
ATOM   2569 C CG2 . VAL B 1 31  ? -1.830  -28.725 17.265  1.00   76.13  ? 31   VAL A CG2 1 
ATOM   2570 N N   . THR B 1 32  ? 2.199   -28.455 14.418  1.00   100.67 ? 32   THR A N   1 
ATOM   2571 C CA  . THR B 1 32  ? 2.821   -28.325 13.096  1.00   99.99  ? 32   THR A CA  1 
ATOM   2572 C C   . THR B 1 32  ? 3.065   -29.682 12.452  1.00   104.99 ? 32   THR A C   1 
ATOM   2573 O O   . THR B 1 32  ? 3.546   -30.611 13.108  1.00   107.41 ? 32   THR A O   1 
ATOM   2574 C CB  . THR B 1 32  ? 4.157   -27.544 13.134  1.00   103.23 ? 32   THR A CB  1 
ATOM   2575 O OG1 . THR B 1 32  ? 5.001   -28.070 14.167  1.00   106.45 ? 32   THR A OG1 1 
ATOM   2576 C CG2 . THR B 1 32  ? 3.915   -26.068 13.387  1.00   100.93 ? 32   THR A CG2 1 
ATOM   2577 N N   . LYS B 1 33  ? 2.730   -29.788 11.168  0.36   71.67  ? 33   LYS A N   1 
ATOM   2578 C CA  . LYS B 1 33  ? 2.929   -31.025 10.416  0.36   78.93  ? 33   LYS A CA  1 
ATOM   2579 C C   . LYS B 1 33  ? 2.995   -30.794 8.907   0.36   72.37  ? 33   LYS A C   1 
ATOM   2580 O O   . LYS B 1 33  ? 2.875   -29.662 8.429   0.36   65.49  ? 33   LYS A O   1 
ATOM   2581 C CB  . LYS B 1 33  ? 1.832   -32.047 10.746  0.36   79.26  ? 33   LYS A CB  1 
ATOM   2582 C CG  . LYS B 1 33  ? 0.440   -31.455 10.914  0.36   74.30  ? 33   LYS A CG  1 
ATOM   2583 C CD  . LYS B 1 33  ? -0.623  -32.492 10.572  0.36   68.89  ? 33   LYS A CD  1 
ATOM   2584 C CE  . LYS B 1 33  ? -1.910  -32.239 11.337  0.36   65.62  ? 33   LYS A CE  1 
ATOM   2585 N NZ  . LYS B 1 33  ? -1.748  -32.564 12.783  0.36   62.44  ? 33   LYS A NZ  1 
ATOM   2586 N N   . LYS B 1 34  ? 3.214   -31.882 8.173   1.00   97.02  ? 34   LYS A N   1 
ATOM   2587 C CA  . LYS B 1 34  ? 3.150   -31.866 6.721   1.00   95.55  ? 34   LYS A CA  1 
ATOM   2588 C C   . LYS B 1 34  ? 2.170   -32.930 6.258   1.00   96.38  ? 34   LYS A C   1 
ATOM   2589 O O   . LYS B 1 34  ? 2.344   -34.119 6.551   1.00   96.97  ? 34   LYS A O   1 
ATOM   2590 C CB  . LYS B 1 34  ? 4.528   -32.113 6.100   1.00   98.45  ? 34   LYS A CB  1 
ATOM   2591 C CG  . LYS B 1 34  ? 5.458   -30.904 6.116   1.00   103.32 ? 34   LYS A CG  1 
ATOM   2592 C CD  . LYS B 1 34  ? 6.120   -30.682 4.753   1.00   98.56  ? 34   LYS A CD  1 
ATOM   2593 C CE  . LYS B 1 34  ? 7.003   -31.854 4.331   1.00   108.85 ? 34   LYS A CE  1 
ATOM   2594 N NZ  . LYS B 1 34  ? 7.381   -31.774 2.891   1.00   107.02 ? 34   LYS A NZ  1 
ATOM   2595 N N   . PHE B 1 35  ? 1.131   -32.494 5.549   1.00   99.14  ? 35   PHE A N   1 
ATOM   2596 C CA  . PHE B 1 35  ? 0.160   -33.413 4.970   1.00   98.75  ? 35   PHE A CA  1 
ATOM   2597 C C   . PHE B 1 35  ? 0.840   -34.350 3.985   1.00   101.35 ? 35   PHE A C   1 
ATOM   2598 O O   . PHE B 1 35  ? 1.917   -34.046 3.463   1.00   102.13 ? 35   PHE A O   1 
ATOM   2599 C CB  . PHE B 1 35  ? -0.950  -32.652 4.246   1.00   96.30  ? 35   PHE A CB  1 
ATOM   2600 C CG  . PHE B 1 35  ? -1.755  -31.748 5.129   1.00   96.71  ? 35   PHE A CG  1 
ATOM   2601 C CD1 . PHE B 1 35  ? -1.764  -30.377 4.904   1.00   98.76  ? 35   PHE A CD1 1 
ATOM   2602 C CD2 . PHE B 1 35  ? -2.519  -32.264 6.173   1.00   98.78  ? 35   PHE A CD2 1 
ATOM   2603 C CE1 . PHE B 1 35  ? -2.517  -29.531 5.702   1.00   99.91  ? 35   PHE A CE1 1 
ATOM   2604 C CE2 . PHE B 1 35  ? -3.270  -31.426 6.984   1.00   99.93  ? 35   PHE A CE2 1 
ATOM   2605 C CZ  . PHE B 1 35  ? -3.275  -30.056 6.744   1.00   100.39 ? 35   PHE A CZ  1 
ATOM   2606 N N   . SER B 1 36  ? 0.199   -35.488 3.736   0.32   84.13  ? 36   SER A N   1 
ATOM   2607 C CA  . SER B 1 36  ? 0.668   -36.449 2.745   0.32   78.80  ? 36   SER A CA  1 
ATOM   2608 C C   . SER B 1 36  ? 1.087   -35.765 1.440   0.32   76.49  ? 36   SER A C   1 
ATOM   2609 O O   . SER B 1 36  ? 2.069   -36.165 0.810   0.32   75.84  ? 36   SER A O   1 
ATOM   2610 C CB  . SER B 1 36  ? -0.421  -37.485 2.467   0.32   78.36  ? 36   SER A CB  1 
ATOM   2611 O OG  . SER B 1 36  ? 0.049   -38.482 1.583   0.32   77.03  ? 36   SER A OG  1 
ATOM   2612 N N   . ASN B 1 37  ? 0.350   -34.727 1.050   0.72   74.60  ? 37   ASN A N   1 
ATOM   2613 C CA  . ASN B 1 37  ? 0.610   -34.035 -0.210  0.72   73.55  ? 37   ASN A CA  1 
ATOM   2614 C C   . ASN B 1 37  ? 1.512   -32.805 -0.111  0.72   73.38  ? 37   ASN A C   1 
ATOM   2615 O O   . ASN B 1 37  ? 1.448   -31.914 -0.962  0.72   73.16  ? 37   ASN A O   1 
ATOM   2616 C CB  . ASN B 1 37  ? -0.701  -33.712 -0.933  0.72   73.20  ? 37   ASN A CB  1 
ATOM   2617 C CG  . ASN B 1 37  ? -1.493  -32.607 -0.269  0.72   72.94  ? 37   ASN A CG  1 
ATOM   2618 O OD1 . ASN B 1 37  ? -1.203  -32.183 0.856   0.72   72.94  ? 37   ASN A OD1 1 
ATOM   2619 N ND2 . ASN B 1 37  ? -2.512  -32.129 -0.970  0.72   72.86  ? 37   ASN A ND2 1 
ATOM   2620 N N   . GLN B 1 38  ? 2.340   -32.763 0.932   1.00   73.60  ? 38   GLN A N   1 
ATOM   2621 C CA  . GLN B 1 38  ? 3.450   -31.799 1.047   1.00   73.79  ? 38   GLN A CA  1 
ATOM   2622 C C   . GLN B 1 38  ? 3.092   -30.395 1.564   1.00   72.49  ? 38   GLN A C   1 
ATOM   2623 O O   . GLN B 1 38  ? 3.991   -29.589 1.817   1.00   72.72  ? 38   GLN A O   1 
ATOM   2624 C CB  . GLN B 1 38  ? 4.245   -31.693 -0.273  1.00   74.43  ? 38   GLN A CB  1 
ATOM   2625 C CG  . GLN B 1 38  ? 4.580   -33.027 -0.952  1.00   76.75  ? 38   GLN A CG  1 
ATOM   2626 C CD  . GLN B 1 38  ? 5.733   -33.769 -0.301  1.00   79.15  ? 38   GLN A CD  1 
ATOM   2627 O OE1 . GLN B 1 38  ? 5.829   -33.857 0.926   1.00   80.42  ? 38   GLN A OE1 1 
ATOM   2628 N NE2 . GLN B 1 38  ? 6.614   -34.319 -1.128  1.00   79.61  ? 38   GLN A NE2 1 
ATOM   2629 N N   . GLU B 1 39  ? 1.803   -30.101 1.725   1.00   70.24  ? 39   GLU A N   1 
ATOM   2630 C CA  . GLU B 1 39  ? 1.377   -28.789 2.225   1.00   67.70  ? 39   GLU A CA  1 
ATOM   2631 C C   . GLU B 1 39  ? 1.707   -28.624 3.706   1.00   65.39  ? 39   GLU A C   1 
ATOM   2632 O O   . GLU B 1 39  ? 1.546   -29.562 4.491   1.00   65.23  ? 39   GLU A O   1 
ATOM   2633 C CB  . GLU B 1 39  ? -0.122  -28.571 1.991   1.00   68.06  ? 39   GLU A CB  1 
ATOM   2634 C CG  . GLU B 1 39  ? -0.554  -28.733 0.534   1.00   69.15  ? 39   GLU A CG  1 
ATOM   2635 C CD  . GLU B 1 39  ? -1.868  -28.036 0.211   1.00   70.42  ? 39   GLU A CD  1 
ATOM   2636 O OE1 . GLU B 1 39  ? -2.617  -27.684 1.151   1.00   71.05  ? 39   GLU A OE1 1 
ATOM   2637 O OE2 . GLU B 1 39  ? -2.152  -27.840 -0.993  1.00   70.63  ? 39   GLU A OE2 1 
ATOM   2638 N N   . THR B 1 40  ? 2.179   -27.435 4.079   1.00   62.28  ? 40   THR A N   1 
ATOM   2639 C CA  . THR B 1 40  ? 2.494   -27.135 5.479   1.00   58.99  ? 40   THR A CA  1 
ATOM   2640 C C   . THR B 1 40  ? 1.209   -26.965 6.294   1.00   58.04  ? 40   THR A C   1 
ATOM   2641 O O   . THR B 1 40  ? 0.370   -26.116 5.980   1.00   57.28  ? 40   THR A O   1 
ATOM   2642 C CB  . THR B 1 40  ? 3.353   -25.861 5.620   1.00   58.85  ? 40   THR A CB  1 
ATOM   2643 O OG1 . THR B 1 40  ? 4.500   -25.951 4.767   1.00   56.16  ? 40   THR A OG1 1 
ATOM   2644 C CG2 . THR B 1 40  ? 3.809   -25.674 7.068   1.00   57.83  ? 40   THR A CG2 1 
ATOM   2645 N N   . CYS B 1 41  ? 1.059   -27.785 7.332   0.47   56.89  ? 41   CYS A N   1 
ATOM   2646 C CA  . CYS B 1 41  ? -0.070  -27.668 8.249   0.47   56.91  ? 41   CYS A CA  1 
ATOM   2647 C C   . CYS B 1 41  ? 0.371   -27.126 9.598   0.47   57.90  ? 41   CYS A C   1 
ATOM   2648 O O   . CYS B 1 41  ? 1.260   -27.694 10.235  0.47   57.28  ? 41   CYS A O   1 
ATOM   2649 C CB  . CYS B 1 41  ? -0.736  -29.022 8.466   0.47   56.53  ? 41   CYS A CB  1 
ATOM   2650 S SG  . CYS B 1 41  ? -2.097  -28.964 9.662   0.47   55.58  ? 41   CYS A SG  1 
ATOM   2651 N N   . VAL B 1 42  ? -0.268  -26.039 10.027  1.00   59.93  ? 42   VAL A N   1 
ATOM   2652 C CA  . VAL B 1 42  ? 0.031   -25.387 11.304  1.00   61.78  ? 42   VAL A CA  1 
ATOM   2653 C C   . VAL B 1 42  ? -1.248  -25.072 12.070  1.00   63.14  ? 42   VAL A C   1 
ATOM   2654 O O   . VAL B 1 42  ? -2.269  -24.704 11.479  1.00   63.38  ? 42   VAL A O   1 
ATOM   2655 C CB  . VAL B 1 42  ? 0.823   -24.070 11.098  1.00   62.36  ? 42   VAL A CB  1 
ATOM   2656 C CG1 . VAL B 1 42  ? 0.702   -23.132 12.315  1.00   62.86  ? 42   VAL A CG1 1 
ATOM   2657 C CG2 . VAL B 1 42  ? 2.285   -24.361 10.778  1.00   63.03  ? 42   VAL A CG2 1 
ATOM   2658 N N   . GLU B 1 43  ? -1.181  -25.214 13.390  0.57   60.24  ? 43   GLU A N   1 
ATOM   2659 C CA  . GLU B 1 43  ? -2.274  -24.817 14.254  0.57   58.79  ? 43   GLU A CA  1 
ATOM   2660 C C   . GLU B 1 43  ? -1.701  -24.284 15.555  0.57   57.52  ? 43   GLU A C   1 
ATOM   2661 O O   . GLU B 1 43  ? -1.138  -25.046 16.336  0.57   57.03  ? 43   GLU A O   1 
ATOM   2662 C CB  . GLU B 1 43  ? -3.191  -26.010 14.529  0.57   59.01  ? 43   GLU A CB  1 
ATOM   2663 C CG  . GLU B 1 43  ? -4.636  -25.644 14.829  0.57   60.05  ? 43   GLU A CG  1 
ATOM   2664 C CD  . GLU B 1 43  ? -5.483  -25.555 13.574  0.57   61.74  ? 43   GLU A CD  1 
ATOM   2665 O OE1 . GLU B 1 43  ? -6.534  -26.230 13.517  0.57   62.29  ? 43   GLU A OE1 1 
ATOM   2666 O OE2 . GLU B 1 43  ? -5.094  -24.825 12.637  0.57   62.60  ? 43   GLU A OE2 1 
ATOM   2667 N N   . ILE B 1 44  ? -1.823  -22.976 15.773  1.00   56.68  ? 44   ILE A N   1 
ATOM   2668 C CA  . ILE B 1 44  ? -1.435  -22.365 17.042  1.00   55.72  ? 44   ILE A CA  1 
ATOM   2669 C C   . ILE B 1 44  ? -2.355  -22.926 18.132  1.00   55.13  ? 44   ILE A C   1 
ATOM   2670 O O   . ILE B 1 44  ? -3.560  -22.671 18.125  1.00   55.21  ? 44   ILE A O   1 
ATOM   2671 C CB  . ILE B 1 44  ? -1.524  -20.812 17.003  1.00   55.90  ? 44   ILE A CB  1 
ATOM   2672 C CG1 . ILE B 1 44  ? -0.686  -20.223 15.850  1.00   55.50  ? 44   ILE A CG1 1 
ATOM   2673 C CG2 . ILE B 1 44  ? -1.099  -20.206 18.340  1.00   55.05  ? 44   ILE A CG2 1 
ATOM   2674 C CD1 . ILE B 1 44  ? 0.843   -20.366 15.998  1.00   55.84  ? 44   ILE A CD1 1 
ATOM   2675 N N   . GLY B 1 45  ? -1.786  -23.691 19.061  1.00   53.80  ? 45   GLY A N   1 
ATOM   2676 C CA  . GLY B 1 45  ? -2.590  -24.397 20.054  1.00   52.01  ? 45   GLY A CA  1 
ATOM   2677 C C   . GLY B 1 45  ? -2.975  -23.626 21.306  1.00   50.63  ? 45   GLY A C   1 
ATOM   2678 O O   . GLY B 1 45  ? -3.310  -24.237 22.318  1.00   51.16  ? 45   GLY A O   1 
ATOM   2679 N N   . GLU B 1 46  ? -2.926  -22.298 21.249  0.81   48.51  ? 46   GLU A N   1 
ATOM   2680 C CA  . GLU B 1 46  ? -3.340  -21.458 22.375  0.81   46.36  ? 46   GLU A CA  1 
ATOM   2681 C C   . GLU B 1 46  ? -3.610  -20.025 21.923  0.81   45.43  ? 46   GLU A C   1 
ATOM   2682 O O   . GLU B 1 46  ? -3.108  -19.588 20.888  0.81   44.37  ? 46   GLU A O   1 
ATOM   2683 C CB  . GLU B 1 46  ? -2.286  -21.473 23.490  0.81   46.35  ? 46   GLU A CB  1 
ATOM   2684 C CG  . GLU B 1 46  ? -0.918  -20.950 23.079  0.81   45.72  ? 46   GLU A CG  1 
ATOM   2685 C CD  . GLU B 1 46  ? 0.117   -21.097 24.175  0.81   46.48  ? 46   GLU A CD  1 
ATOM   2686 O OE1 . GLU B 1 46  ? 0.355   -20.109 24.896  0.81   48.47  ? 46   GLU A OE1 1 
ATOM   2687 O OE2 . GLU B 1 46  ? 0.692   -22.198 24.319  0.81   46.38  ? 46   GLU A OE2 1 
ATOM   2688 N N   . SER B 1 47  ? -4.397  -19.300 22.710  1.00   44.31  ? 47   SER A N   1 
ATOM   2689 C CA  . SER B 1 47  ? -4.725  -17.917 22.403  1.00   43.80  ? 47   SER A CA  1 
ATOM   2690 C C   . SER B 1 47  ? -3.472  -17.060 22.466  1.00   42.56  ? 47   SER A C   1 
ATOM   2691 O O   . SER B 1 47  ? -2.684  -17.184 23.399  1.00   42.32  ? 47   SER A O   1 
ATOM   2692 C CB  . SER B 1 47  ? -5.765  -17.387 23.389  1.00   44.00  ? 47   SER A CB  1 
ATOM   2693 O OG  . SER B 1 47  ? -6.004  -16.008 23.168  1.00   45.10  ? 47   SER A OG  1 
ATOM   2694 N N   . VAL B 1 48  ? -3.276  -16.203 21.470  1.00   40.33  ? 48   VAL A N   1 
ATOM   2695 C CA  . VAL B 1 48  ? -2.147  -15.277 21.519  1.00   39.14  ? 48   VAL A CA  1 
ATOM   2696 C C   . VAL B 1 48  ? -2.653  -13.853 21.536  1.00   39.23  ? 48   VAL A C   1 
ATOM   2697 O O   . VAL B 1 48  ? -1.900  -12.911 21.304  1.00   38.68  ? 48   VAL A O   1 
ATOM   2698 C CB  . VAL B 1 48  ? -1.164  -15.501 20.355  1.00   39.08  ? 48   VAL A CB  1 
ATOM   2699 C CG1 . VAL B 1 48  ? -0.483  -16.841 20.507  1.00   38.57  ? 48   VAL A CG1 1 
ATOM   2700 C CG2 . VAL B 1 48  ? -1.885  -15.403 19.003  1.00   39.34  ? 48   VAL A CG2 1 
ATOM   2701 N N   . ARG B 1 49  ? -3.944  -13.711 21.826  1.00   39.84  ? 49   ARG A N   1 
ATOM   2702 C CA  . ARG B 1 49  ? -4.613  -12.421 21.785  1.00   40.90  ? 49   ARG A CA  1 
ATOM   2703 C C   . ARG B 1 49  ? -3.936  -11.438 22.718  1.00   40.91  ? 49   ARG A C   1 
ATOM   2704 O O   . ARG B 1 49  ? -3.777  -11.717 23.894  1.00   40.63  ? 49   ARG A O   1 
ATOM   2705 C CB  . ARG B 1 49  ? -6.081  -12.586 22.171  1.00   41.40  ? 49   ARG A CB  1 
ATOM   2706 C CG  . ARG B 1 49  ? -6.940  -11.372 21.862  1.00   42.04  ? 49   ARG A CG  1 
ATOM   2707 C CD  . ARG B 1 49  ? -8.421  -11.673 22.082  1.00   43.59  ? 49   ARG A CD  1 
ATOM   2708 N NE  . ARG B 1 49  ? -8.945  -12.649 21.125  1.00   43.54  ? 49   ARG A NE  1 
ATOM   2709 C CZ  . ARG B 1 49  ? -9.531  -12.339 19.969  1.00   44.01  ? 49   ARG A CZ  1 
ATOM   2710 N NH1 . ARG B 1 49  ? -9.678  -11.073 19.600  1.00   44.21  ? 49   ARG A NH1 1 
ATOM   2711 N NH2 . ARG B 1 49  ? -9.972  -13.297 19.173  1.00   43.91  ? 49   ARG A NH2 1 
ATOM   2712 N N   . GLY B 1 50  ? -3.512  -10.299 22.184  1.00   41.44  ? 50   GLY A N   1 
ATOM   2713 C CA  . GLY B 1 50  ? -2.885  -9.263  22.993  1.00   41.41  ? 50   GLY A CA  1 
ATOM   2714 C C   . GLY B 1 50  ? -1.492  -9.599  23.493  1.00   41.78  ? 50   GLY A C   1 
ATOM   2715 O O   . GLY B 1 50  ? -0.936  -8.870  24.313  1.00   42.23  ? 50   GLY A O   1 
ATOM   2716 N N   . GLU B 1 51  ? -0.909  -10.685 22.995  1.00   41.28  ? 51   GLU A N   1 
ATOM   2717 C CA  . GLU B 1 51  ? 0.441   -11.065 23.420  1.00   40.82  ? 51   GLU A CA  1 
ATOM   2718 C C   . GLU B 1 51  ? 1.557   -10.554 22.508  1.00   39.49  ? 51   GLU A C   1 
ATOM   2719 O O   . GLU B 1 51  ? 1.320   -10.209 21.346  1.00   39.14  ? 51   GLU A O   1 
ATOM   2720 C CB  . GLU B 1 51  ? 0.533   -12.573 23.581  1.00   41.62  ? 51   GLU A CB  1 
ATOM   2721 C CG  . GLU B 1 51  ? -0.477  -13.099 24.596  1.00   46.23  ? 51   GLU A CG  1 
ATOM   2722 C CD  . GLU B 1 51  ? -0.196  -14.520 25.002  1.00   51.69  ? 51   GLU A CD  1 
ATOM   2723 O OE1 . GLU B 1 51  ? -0.207  -15.397 24.112  1.00   54.71  ? 51   GLU A OE1 1 
ATOM   2724 O OE2 . GLU B 1 51  ? 0.029   -14.763 26.208  1.00   54.76  ? 51   GLU A OE2 1 
ATOM   2725 N N   . ASP B 1 52  ? 2.763   -10.489 23.067  1.00   37.52  ? 52   ASP A N   1 
ATOM   2726 C CA  . ASP B 1 52  ? 3.965   -10.123 22.344  1.00   37.39  ? 52   ASP A CA  1 
ATOM   2727 C C   . ASP B 1 52  ? 4.616   -11.423 21.877  1.00   36.54  ? 52   ASP A C   1 
ATOM   2728 O O   . ASP B 1 52  ? 5.248   -12.127 22.659  1.00   36.35  ? 52   ASP A O   1 
ATOM   2729 C CB  . ASP B 1 52  ? 4.915   -9.312  23.246  1.00   37.45  ? 52   ASP A CB  1 
ATOM   2730 C CG  . ASP B 1 52  ? 6.047   -8.663  22.471  1.00   39.62  ? 52   ASP A CG  1 
ATOM   2731 O OD1 . ASP B 1 52  ? 5.935   -8.577  21.226  1.00   41.96  ? 52   ASP A OD1 1 
ATOM   2732 O OD2 . ASP B 1 52  ? 7.049   -8.224  23.092  1.00   39.93  ? 52   ASP A OD2 1 
ATOM   2733 N N   . VAL B 1 53  ? 4.437   -11.748 20.600  1.00   35.70  ? 53   VAL A N   1 
ATOM   2734 C CA  . VAL B 1 53  ? 4.811   -13.068 20.077  1.00   34.94  ? 53   VAL A CA  1 
ATOM   2735 C C   . VAL B 1 53  ? 6.133   -13.083 19.319  1.00   34.50  ? 53   VAL A C   1 
ATOM   2736 O O   . VAL B 1 53  ? 6.374   -12.222 18.470  1.00   35.00  ? 53   VAL A O   1 
ATOM   2737 C CB  . VAL B 1 53  ? 3.697   -13.635 19.163  1.00   35.43  ? 53   VAL A CB  1 
ATOM   2738 C CG1 . VAL B 1 53  ? 4.081   -15.005 18.614  1.00   35.35  ? 53   VAL A CG1 1 
ATOM   2739 C CG2 . VAL B 1 53  ? 2.372   -13.720 19.920  1.00   34.43  ? 53   VAL A CG2 1 
ATOM   2740 N N   . TYR B 1 54  ? 6.963   -14.088 19.618  1.00   33.05  ? 54   TYR A N   1 
ATOM   2741 C CA  . TYR B 1 54  ? 8.239   -14.313 18.952  1.00   32.17  ? 54   TYR A CA  1 
ATOM   2742 C C   . TYR B 1 54  ? 8.250   -15.703 18.346  1.00   33.02  ? 54   TYR A C   1 
ATOM   2743 O O   . TYR B 1 54  ? 8.099   -16.706 19.059  1.00   32.71  ? 54   TYR A O   1 
ATOM   2744 C CB  . TYR B 1 54  ? 9.420   -14.136 19.930  1.00   32.23  ? 54   TYR A CB  1 
ATOM   2745 C CG  . TYR B 1 54  ? 9.477   -12.734 20.502  1.00   32.87  ? 54   TYR A CG  1 
ATOM   2746 C CD1 . TYR B 1 54  ? 8.597   -12.345 21.511  1.00   34.87  ? 54   TYR A CD1 1 
ATOM   2747 C CD2 . TYR B 1 54  ? 10.378  -11.788 20.013  1.00   32.41  ? 54   TYR A CD2 1 
ATOM   2748 C CE1 . TYR B 1 54  ? 8.609   -11.054 22.023  1.00   34.88  ? 54   TYR A CE1 1 
ATOM   2749 C CE2 . TYR B 1 54  ? 10.401  -10.484 20.526  1.00   34.09  ? 54   TYR A CE2 1 
ATOM   2750 C CZ  . TYR B 1 54  ? 9.508   -10.133 21.533  1.00   34.28  ? 54   TYR A CZ  1 
ATOM   2751 O OH  . TYR B 1 54  ? 9.506   -8.862  22.058  1.00   34.55  ? 54   TYR A OH  1 
ATOM   2752 N N   . ILE B 1 55  ? 8.409   -15.768 17.027  1.00   32.96  ? 55   ILE A N   1 
ATOM   2753 C CA  . ILE B 1 55  ? 8.467   -17.055 16.352  1.00   33.31  ? 55   ILE A CA  1 
ATOM   2754 C C   . ILE B 1 55  ? 9.894   -17.296 15.928  1.00   33.89  ? 55   ILE A C   1 
ATOM   2755 O O   . ILE B 1 55  ? 10.454  -16.522 15.158  1.00   33.78  ? 55   ILE A O   1 
ATOM   2756 C CB  . ILE B 1 55  ? 7.529   -17.113 15.142  1.00   33.25  ? 55   ILE A CB  1 
ATOM   2757 C CG1 . ILE B 1 55  ? 6.101   -16.827 15.610  1.00   32.60  ? 55   ILE A CG1 1 
ATOM   2758 C CG2 . ILE B 1 55  ? 7.630   -18.497 14.464  1.00   32.91  ? 55   ILE A CG2 1 
ATOM   2759 C CD1 . ILE B 1 55  ? 5.164   -16.419 14.518  1.00   32.66  ? 55   ILE A CD1 1 
ATOM   2760 N N   . VAL B 1 56  ? 10.485  -18.361 16.453  1.00   34.27  ? 56   VAL A N   1 
ATOM   2761 C CA  . VAL B 1 56  ? 11.879  -18.648 16.207  1.00   37.09  ? 56   VAL A CA  1 
ATOM   2762 C C   . VAL B 1 56  ? 11.964  -19.670 15.089  1.00   41.60  ? 56   VAL A C   1 
ATOM   2763 O O   . VAL B 1 56  ? 11.407  -20.764 15.201  1.00   41.51  ? 56   VAL A O   1 
ATOM   2764 C CB  . VAL B 1 56  ? 12.587  -19.180 17.469  1.00   36.34  ? 56   VAL A CB  1 
ATOM   2765 C CG1 . VAL B 1 56  ? 14.044  -19.564 17.154  1.00   34.51  ? 56   VAL A CG1 1 
ATOM   2766 C CG2 . VAL B 1 56  ? 12.538  -18.143 18.576  1.00   34.71  ? 56   VAL A CG2 1 
ATOM   2767 N N   . GLN B 1 57  ? 12.684  -19.306 14.031  1.00   46.97  ? 57   GLN A N   1 
ATOM   2768 C CA  . GLN B 1 57  ? 12.741  -20.083 12.787  1.00   52.85  ? 57   GLN A CA  1 
ATOM   2769 C C   . GLN B 1 57  ? 13.379  -21.479 12.922  1.00   55.53  ? 57   GLN A C   1 
ATOM   2770 O O   . GLN B 1 57  ? 14.442  -21.638 13.539  1.00   56.37  ? 57   GLN A O   1 
ATOM   2771 C CB  . GLN B 1 57  ? 13.424  -19.244 11.692  1.00   53.14  ? 57   GLN A CB  1 
ATOM   2772 C CG  . GLN B 1 57  ? 14.556  -19.924 10.925  1.00   56.85  ? 57   GLN A CG  1 
ATOM   2773 C CD  . GLN B 1 57  ? 15.845  -20.065 11.740  1.00   60.65  ? 57   GLN A CD  1 
ATOM   2774 O OE1 . GLN B 1 57  ? 16.908  -20.348 11.185  1.00   62.43  ? 57   GLN A OE1 1 
ATOM   2775 N NE2 . GLN B 1 57  ? 15.753  -19.875 13.057  1.00   61.95  ? 57   GLN A NE2 1 
ATOM   2776 N N   . SER B 1 58  ? 12.722  -22.478 12.324  0.48   58.50  ? 58   SER A N   1 
ATOM   2777 C CA  . SER B 1 58  ? 13.156  -23.878 12.393  0.48   61.04  ? 58   SER A CA  1 
ATOM   2778 C C   . SER B 1 58  ? 14.319  -24.184 11.469  0.48   62.65  ? 58   SER A C   1 
ATOM   2779 O O   . SER B 1 58  ? 14.696  -23.364 10.631  0.48   62.97  ? 58   SER A O   1 
ATOM   2780 C CB  . SER B 1 58  ? 12.004  -24.811 12.001  0.48   60.99  ? 58   SER A CB  1 
ATOM   2781 O OG  . SER B 1 58  ? 12.332  -26.160 12.333  0.48   61.09  ? 58   SER A OG  1 
ATOM   2782 N N   . GLY B 1 59  ? 14.863  -25.391 11.604  0.40   64.47  ? 59   GLY A N   1 
ATOM   2783 C CA  . GLY B 1 59  ? 16.000  -25.801 10.788  0.40   66.34  ? 59   GLY A CA  1 
ATOM   2784 C C   . GLY B 1 59  ? 15.921  -27.207 10.223  0.40   67.19  ? 59   GLY A C   1 
ATOM   2785 O O   . GLY B 1 59  ? 16.901  -27.951 10.263  0.40   67.56  ? 59   GLY A O   1 
ATOM   2786 N N   . CYS B 1 60  ? 14.763  -27.578 9.687   0.37   67.24  ? 60   CYS A N   1 
ATOM   2787 C CA  . CYS B 1 60  ? 14.618  -28.883 9.050   0.37   66.54  ? 60   CYS A CA  1 
ATOM   2788 C C   . CYS B 1 60  ? 15.501  -29.007 7.809   0.37   64.53  ? 60   CYS A C   1 
ATOM   2789 O O   . CYS B 1 60  ? 15.496  -30.036 7.131   0.37   64.84  ? 60   CYS A O   1 
ATOM   2790 C CB  . CYS B 1 60  ? 13.148  -29.167 8.714   0.37   67.12  ? 60   CYS A CB  1 
ATOM   2791 S SG  . CYS B 1 60  ? 12.160  -29.655 10.149  0.37   81.89  ? 60   CYS A SG  1 
ATOM   2792 N N   . GLY B 1 61  ? 16.265  -27.956 7.523   0.35   61.24  ? 61   GLY A N   1 
ATOM   2793 C CA  . GLY B 1 61  ? 17.201  -27.983 6.404   0.35   56.14  ? 61   GLY A CA  1 
ATOM   2794 C C   . GLY B 1 61  ? 16.491  -27.993 5.064   0.35   52.16  ? 61   GLY A C   1 
ATOM   2795 O O   . GLY B 1 61  ? 17.106  -28.235 4.017   0.35   52.35  ? 61   GLY A O   1 
ATOM   2796 N N   . GLU B 1 62  ? 15.182  -27.751 5.109   0.18   47.66  ? 62   GLU A N   1 
ATOM   2797 C CA  . GLU B 1 62  ? 14.416  -27.566 3.880   0.18   43.65  ? 62   GLU A CA  1 
ATOM   2798 C C   . GLU B 1 62  ? 13.976  -26.121 3.972   0.18   43.30  ? 62   GLU A C   1 
ATOM   2799 O O   . GLU B 1 62  ? 12.996  -25.801 4.640   0.18   41.07  ? 62   GLU A O   1 
ATOM   2800 C CB  . GLU B 1 62  ? 13.211  -28.507 3.841   0.18   42.55  ? 62   GLU A CB  1 
ATOM   2801 C CG  . GLU B 1 62  ? 12.960  -29.144 2.473   0.18   38.84  ? 62   GLU A CG  1 
ATOM   2802 C CD  . GLU B 1 62  ? 12.352  -28.183 1.459   0.18   34.37  ? 62   GLU A CD  1 
ATOM   2803 O OE1 . GLU B 1 62  ? 12.148  -27.000 1.802   0.18   31.09  ? 62   GLU A OE1 1 
ATOM   2804 O OE2 . GLU B 1 62  ? 12.072  -28.624 0.319   0.18   32.84  ? 62   GLU A OE2 1 
ATOM   2805 N N   . ILE B 1 63  ? 14.740  -25.247 3.330   1.00   45.08  ? 63   ILE A N   1 
ATOM   2806 C CA  . ILE B 1 63  ? 14.534  -23.806 3.442   1.00   46.95  ? 63   ILE A CA  1 
ATOM   2807 C C   . ILE B 1 63  ? 13.131  -23.325 3.034   1.00   46.34  ? 63   ILE A C   1 
ATOM   2808 O O   . ILE B 1 63  ? 12.547  -22.480 3.713   1.00   46.88  ? 63   ILE A O   1 
ATOM   2809 C CB  . ILE B 1 63  ? 15.608  -23.018 2.677   1.00   47.80  ? 63   ILE A CB  1 
ATOM   2810 C CG1 . ILE B 1 63  ? 15.432  -21.522 2.922   1.00   49.36  ? 63   ILE A CG1 1 
ATOM   2811 C CG2 . ILE B 1 63  ? 15.550  -23.324 1.200   1.00   49.92  ? 63   ILE A CG2 1 
ATOM   2812 C CD1 . ILE B 1 63  ? 16.515  -20.684 2.341   1.00   51.75  ? 63   ILE A CD1 1 
ATOM   2813 N N   . ASN B 1 64  ? 12.592  -23.859 1.943   1.00   44.48  ? 64   ASN A N   1 
ATOM   2814 C CA  . ASN B 1 64  ? 11.268  -23.450 1.498   1.00   43.11  ? 64   ASN A CA  1 
ATOM   2815 C C   . ASN B 1 64  ? 10.145  -23.891 2.429   1.00   42.61  ? 64   ASN A C   1 
ATOM   2816 O O   . ASN B 1 64  ? 9.200   -23.129 2.652   1.00   42.13  ? 64   ASN A O   1 
ATOM   2817 C CB  . ASN B 1 64  ? 10.997  -23.895 0.063   1.00   43.00  ? 64   ASN A CB  1 
ATOM   2818 C CG  . ASN B 1 64  ? 11.870  -23.167 -0.942  1.00   43.32  ? 64   ASN A CG  1 
ATOM   2819 O OD1 . ASN B 1 64  ? 12.283  -22.021 -0.712  1.00   42.01  ? 64   ASN A OD1 1 
ATOM   2820 N ND2 . ASN B 1 64  ? 12.163  -23.830 -2.067  1.00   41.80  ? 64   ASN A ND2 1 
ATOM   2821 N N   . ASN B 1 65  ? 10.241  -25.110 2.962   1.00   41.36  ? 65   ASN A N   1 
ATOM   2822 C CA  . ASN B 1 65  ? 9.284   -25.574 3.967   1.00   42.10  ? 65   ASN A CA  1 
ATOM   2823 C C   . ASN B 1 65  ? 9.426   -24.771 5.254   1.00   41.41  ? 65   ASN A C   1 
ATOM   2824 O O   . ASN B 1 65  ? 8.432   -24.462 5.898   1.00   40.97  ? 65   ASN A O   1 
ATOM   2825 C CB  . ASN B 1 65  ? 9.466   -27.062 4.285   1.00   42.88  ? 65   ASN A CB  1 
ATOM   2826 C CG  . ASN B 1 65  ? 9.134   -27.970 3.108   1.00   45.11  ? 65   ASN A CG  1 
ATOM   2827 O OD1 . ASN B 1 65  ? 9.858   -28.927 2.841   1.00   48.63  ? 65   ASN A OD1 1 
ATOM   2828 N ND2 . ASN B 1 65  ? 8.032   -27.695 2.419   1.00   44.38  ? 65   ASN A ND2 1 
ATOM   2829 N N   . ASN B 1 66  ? 10.662  -24.444 5.623   1.00   40.80  ? 66   ASN A N   1 
ATOM   2830 C CA  . ASN B 1 66  ? 10.891  -23.643 6.817   1.00   40.75  ? 66   ASN A CA  1 
ATOM   2831 C C   . ASN B 1 66  ? 10.376  -22.223 6.666   1.00   38.94  ? 66   ASN A C   1 
ATOM   2832 O O   . ASN B 1 66  ? 9.786   -21.677 7.599   1.00   38.47  ? 66   ASN A O   1 
ATOM   2833 C CB  . ASN B 1 66  ? 12.360  -23.684 7.232   1.00   41.84  ? 66   ASN A CB  1 
ATOM   2834 C CG  . ASN B 1 66  ? 12.747  -25.032 7.823   1.00   44.61  ? 66   ASN A CG  1 
ATOM   2835 O OD1 . ASN B 1 66  ? 11.899  -25.762 8.344   1.00   48.16  ? 66   ASN A OD1 1 
ATOM   2836 N ND2 . ASN B 1 66  ? 14.026  -25.373 7.735   1.00   47.31  ? 66   ASN A ND2 1 
ATOM   2837 N N   . LEU B 1 67  ? 10.542  -21.652 5.475   1.00   37.06  ? 67   LEU A N   1 
ATOM   2838 C CA  . LEU B 1 67  ? 10.052  -20.307 5.215   1.00   34.53  ? 67   LEU A CA  1 
ATOM   2839 C C   . LEU B 1 67  ? 8.526   -20.275 5.202   1.00   33.51  ? 67   LEU A C   1 
ATOM   2840 O O   . LEU B 1 67  ? 7.931   -19.437 5.874   1.00   32.42  ? 67   LEU A O   1 
ATOM   2841 C CB  . LEU B 1 67  ? 10.647  -19.726 3.924   1.00   34.82  ? 67   LEU A CB  1 
ATOM   2842 C CG  . LEU B 1 67  ? 10.182  -18.328 3.504   1.00   31.83  ? 67   LEU A CG  1 
ATOM   2843 C CD1 . LEU B 1 67  ? 10.397  -17.287 4.623   1.00   31.62  ? 67   LEU A CD1 1 
ATOM   2844 C CD2 . LEU B 1 67  ? 10.905  -17.903 2.243   1.00   34.40  ? 67   LEU A CD2 1 
ATOM   2845 N N   . MET B 1 68  ? 7.890   -21.200 4.484   0.77   32.84  ? 68   MET A N   1 
ATOM   2846 C CA  . MET B 1 68  ? 6.423   -21.246 4.463   0.77   32.70  ? 68   MET A CA  1 
ATOM   2847 C C   . MET B 1 68  ? 5.824   -21.472 5.845   0.77   32.78  ? 68   MET A C   1 
ATOM   2848 O O   . MET B 1 68  ? 4.824   -20.850 6.208   0.77   31.00  ? 68   MET A O   1 
ATOM   2849 C CB  . MET B 1 68  ? 5.904   -22.304 3.482   0.77   32.97  ? 68   MET A CB  1 
ATOM   2850 C CG  . MET B 1 68  ? 5.960   -21.859 2.027   0.77   35.28  ? 68   MET A CG  1 
ATOM   2851 S SD  . MET B 1 68  ? 5.136   -20.278 1.766   0.77   43.18  ? 68   MET A SD  1 
ATOM   2852 C CE  . MET B 1 68  ? 3.528   -20.623 2.466   0.77   28.53  ? 68   MET A CE  1 
ATOM   2853 N N   . GLU B 1 69  ? 6.429   -22.365 6.616   1.00   34.85  ? 69   GLU A N   1 
ATOM   2854 C CA  . GLU B 1 69  ? 5.978   -22.589 7.983   1.00   36.43  ? 69   GLU A CA  1 
ATOM   2855 C C   . GLU B 1 69  ? 6.084   -21.322 8.835   1.00   35.37  ? 69   GLU A C   1 
ATOM   2856 O O   . GLU B 1 69  ? 5.142   -20.978 9.553   1.00   35.64  ? 69   GLU A O   1 
ATOM   2857 C CB  . GLU B 1 69  ? 6.741   -23.738 8.632   1.00   37.87  ? 69   GLU A CB  1 
ATOM   2858 C CG  . GLU B 1 69  ? 6.133   -24.174 9.952   1.00   43.31  ? 69   GLU A CG  1 
ATOM   2859 C CD  . GLU B 1 69  ? 7.002   -25.146 10.704  1.00   54.02  ? 69   GLU A CD  1 
ATOM   2860 O OE1 . GLU B 1 69  ? 8.243   -25.087 10.557  1.00   51.72  ? 69   GLU A OE1 1 
ATOM   2861 O OE2 . GLU B 1 69  ? 6.437   -25.967 11.451  1.00   61.12  ? 69   GLU A OE2 1 
ATOM   2862 N N   . LEU B 1 70  ? 7.215   -20.624 8.746   1.00   33.94  ? 70   LEU A N   1 
ATOM   2863 C CA  . LEU B 1 70  ? 7.358   -19.342 9.424   1.00   33.24  ? 70   LEU A CA  1 
ATOM   2864 C C   . LEU B 1 70  ? 6.263   -18.348 8.993   1.00   33.20  ? 70   LEU A C   1 
ATOM   2865 O O   . LEU B 1 70  ? 5.618   -17.719 9.837   1.00   32.87  ? 70   LEU A O   1 
ATOM   2866 C CB  . LEU B 1 70  ? 8.754   -18.759 9.174   1.00   33.57  ? 70   LEU A CB  1 
ATOM   2867 C CG  . LEU B 1 70  ? 9.060   -17.352 9.695   1.00   34.53  ? 70   LEU A CG  1 
ATOM   2868 C CD1 . LEU B 1 70  ? 8.903   -17.256 11.227  1.00   34.53  ? 70   LEU A CD1 1 
ATOM   2869 C CD2 . LEU B 1 70  ? 10.456  -16.934 9.268   1.00   35.24  ? 70   LEU A CD2 1 
ATOM   2870 N N   . LEU B 1 71  ? 6.034   -18.233 7.684   1.00   32.09  ? 71   LEU A N   1 
ATOM   2871 C CA  . LEU B 1 71  ? 5.049   -17.290 7.162   1.00   31.67  ? 71   LEU A CA  1 
ATOM   2872 C C   . LEU B 1 71  ? 3.640   -17.614 7.635   1.00   31.69  ? 71   LEU A C   1 
ATOM   2873 O O   . LEU B 1 71  ? 2.860   -16.719 8.001   1.00   31.19  ? 71   LEU A O   1 
ATOM   2874 C CB  . LEU B 1 71  ? 5.086   -17.284 5.630   1.00   30.56  ? 71   LEU A CB  1 
ATOM   2875 C CG  . LEU B 1 71  ? 6.384   -16.740 5.032   1.00   30.54  ? 71   LEU A CG  1 
ATOM   2876 C CD1 . LEU B 1 71  ? 6.366   -16.879 3.516   1.00   31.36  ? 71   LEU A CD1 1 
ATOM   2877 C CD2 . LEU B 1 71  ? 6.546   -15.283 5.427   1.00   28.81  ? 71   LEU A CD2 1 
ATOM   2878 N N   . ILE B 1 72  ? 3.309   -18.898 7.617   1.00   32.29  ? 72   ILE A N   1 
ATOM   2879 C CA  . ILE B 1 72  ? 1.988   -19.340 8.051   1.00   33.69  ? 72   ILE A CA  1 
ATOM   2880 C C   . ILE B 1 72  ? 1.782   -19.015 9.538   1.00   33.62  ? 72   ILE A C   1 
ATOM   2881 O O   . ILE B 1 72  ? 0.713   -18.547 9.947   1.00   34.78  ? 72   ILE A O   1 
ATOM   2882 C CB  . ILE B 1 72  ? 1.775   -20.846 7.749   1.00   34.56  ? 72   ILE A CB  1 
ATOM   2883 C CG1 . ILE B 1 72  ? 1.504   -21.050 6.251   1.00   35.72  ? 72   ILE A CG1 1 
ATOM   2884 C CG2 . ILE B 1 72  ? 0.615   -21.414 8.559   1.00   35.30  ? 72   ILE A CG2 1 
ATOM   2885 C CD1 . ILE B 1 72  ? 1.771   -22.462 5.762   1.00   37.82  ? 72   ILE A CD1 1 
ATOM   2886 N N   . MET B 1 73  ? 2.814   -19.231 10.342  1.00   33.24  ? 73   MET A N   1 
ATOM   2887 C CA  . MET B 1 73  ? 2.711   -18.941 11.769  1.00   33.40  ? 73   MET A CA  1 
ATOM   2888 C C   . MET B 1 73  ? 2.593   -17.457 12.076  1.00   32.94  ? 73   MET A C   1 
ATOM   2889 O O   . MET B 1 73  ? 1.852   -17.062 12.980  1.00   33.19  ? 73   MET A O   1 
ATOM   2890 C CB  . MET B 1 73  ? 3.894   -19.540 12.512  1.00   34.01  ? 73   MET A CB  1 
ATOM   2891 C CG  . MET B 1 73  ? 3.804   -21.045 12.625  1.00   38.23  ? 73   MET A CG  1 
ATOM   2892 S SD  . MET B 1 73  ? 5.254   -21.746 13.421  1.00   47.21  ? 73   MET A SD  1 
ATOM   2893 C CE  . MET B 1 73  ? 4.979   -21.207 15.108  1.00   45.32  ? 73   MET A CE  1 
ATOM   2894 N N   . ILE B 1 74  ? 3.335   -16.630 11.345  1.00   31.69  ? 74   ILE A N   1 
ATOM   2895 C CA  . ILE B 1 74  ? 3.238   -15.200 11.529  1.00   31.24  ? 74   ILE A CA  1 
ATOM   2896 C C   . ILE B 1 74  ? 1.807   -14.767 11.246  1.00   32.26  ? 74   ILE A C   1 
ATOM   2897 O O   . ILE B 1 74  ? 1.205   -14.020 12.013  1.00   32.18  ? 74   ILE A O   1 
ATOM   2898 C CB  . ILE B 1 74  ? 4.230   -14.444 10.614  1.00   30.67  ? 74   ILE A CB  1 
ATOM   2899 C CG1 . ILE B 1 74  ? 5.652   -14.597 11.163  1.00   30.76  ? 74   ILE A CG1 1 
ATOM   2900 C CG2 . ILE B 1 74  ? 3.839   -12.967 10.501  1.00   29.57  ? 74   ILE A CG2 1 
ATOM   2901 C CD1 . ILE B 1 74  ? 6.743   -14.311 10.165  1.00   30.59  ? 74   ILE A CD1 1 
ATOM   2902 N N   . ASN B 1 75  ? 1.258   -15.268 10.147  1.00   33.23  ? 75   ASN A N   1 
ATOM   2903 C CA  . ASN B 1 75  ? -0.070  -14.881 9.715   1.00   34.29  ? 75   ASN A CA  1 
ATOM   2904 C C   . ASN B 1 75  ? -1.173  -15.334 10.675  1.00   34.83  ? 75   ASN A C   1 
ATOM   2905 O O   . ASN B 1 75  ? -2.107  -14.569 10.967  1.00   34.44  ? 75   ASN A O   1 
ATOM   2906 C CB  . ASN B 1 75  ? -0.320  -15.409 8.305   1.00   34.41  ? 75   ASN A CB  1 
ATOM   2907 C CG  . ASN B 1 75  ? -1.644  -14.962 7.745   1.00   36.55  ? 75   ASN A CG  1 
ATOM   2908 O OD1 . ASN B 1 75  ? -2.508  -15.783 7.466   1.00   40.75  ? 75   ASN A OD1 1 
ATOM   2909 N ND2 . ASN B 1 75  ? -1.817  -13.660 7.586   1.00   37.26  ? 75   ASN A ND2 1 
ATOM   2910 N N   . ALA B 1 76  ? -1.060  -16.579 11.146  1.00   34.96  ? 76   ALA A N   1 
ATOM   2911 C CA  . ALA B 1 76  ? -1.993  -17.141 12.126  1.00   35.87  ? 76   ALA A CA  1 
ATOM   2912 C C   . ALA B 1 76  ? -2.028  -16.292 13.395  1.00   36.20  ? 76   ALA A C   1 
ATOM   2913 O O   . ALA B 1 76  ? -3.103  -16.001 13.903  1.00   36.03  ? 76   ALA A O   1 
ATOM   2914 C CB  . ALA B 1 76  ? -1.618  -18.582 12.465  1.00   35.49  ? 76   ALA A CB  1 
ATOM   2915 N N   . CYS B 1 77  ? -0.855  -15.900 13.896  1.00   37.31  ? 77   CYS A N   1 
ATOM   2916 C CA  . CYS B 1 77  ? -0.777  -15.044 15.082  1.00   39.10  ? 77   CYS A CA  1 
ATOM   2917 C C   . CYS B 1 77  ? -1.388  -13.668 14.835  1.00   40.24  ? 77   CYS A C   1 
ATOM   2918 O O   . CYS B 1 77  ? -2.070  -13.118 15.705  1.00   40.44  ? 77   CYS A O   1 
ATOM   2919 C CB  . CYS B 1 77  ? 0.666   -14.911 15.567  1.00   38.78  ? 77   CYS A CB  1 
ATOM   2920 S SG  . CYS B 1 77  ? 1.355   -16.473 16.187  1.00   38.85  ? 77   CYS A SG  1 
ATOM   2921 N N   . LYS B 1 78  ? -1.161  -13.129 13.640  1.00   41.42  ? 78   LYS A N   1 
ATOM   2922 C CA  . LYS B 1 78  ? -1.663  -11.810 13.288  1.00   42.17  ? 78   LYS A CA  1 
ATOM   2923 C C   . LYS B 1 78  ? -3.185  -11.790 13.265  1.00   41.79  ? 78   LYS A C   1 
ATOM   2924 O O   . LYS B 1 78  ? -3.809  -10.916 13.871  1.00   42.16  ? 78   LYS A O   1 
ATOM   2925 C CB  . LYS B 1 78  ? -1.106  -11.362 11.931  1.00   42.99  ? 78   LYS A CB  1 
ATOM   2926 C CG  . LYS B 1 78  ? -0.906  -9.862  11.827  1.00   45.74  ? 78   LYS A CG  1 
ATOM   2927 C CD  . LYS B 1 78  ? 0.108   -9.398  12.871  1.00   49.36  ? 78   LYS A CD  1 
ATOM   2928 C CE  . LYS B 1 78  ? 0.130   -7.891  13.021  1.00   51.25  ? 78   LYS A CE  1 
ATOM   2929 N NZ  . LYS B 1 78  ? 0.854   -7.224  11.907  1.00   52.78  ? 78   LYS A NZ  1 
ATOM   2930 N N   . ILE B 1 79  ? -3.786  -12.760 12.581  1.00   40.34  ? 79   ILE A N   1 
ATOM   2931 C CA  . ILE B 1 79  ? -5.245  -12.797 12.495  1.00   40.91  ? 79   ILE A CA  1 
ATOM   2932 C C   . ILE B 1 79  ? -5.906  -13.280 13.796  1.00   40.46  ? 79   ILE A C   1 
ATOM   2933 O O   . ILE B 1 79  ? -7.117  -13.127 13.969  1.00   40.58  ? 79   ILE A O   1 
ATOM   2934 C CB  . ILE B 1 79  ? -5.768  -13.592 11.260  1.00   41.20  ? 79   ILE A CB  1 
ATOM   2935 C CG1 . ILE B 1 79  ? -5.423  -15.078 11.370  1.00   42.84  ? 79   ILE A CG1 1 
ATOM   2936 C CG2 . ILE B 1 79  ? -5.207  -12.999 9.962   1.00   42.17  ? 79   ILE A CG2 1 
ATOM   2937 C CD1 . ILE B 1 79  ? -5.946  -15.921 10.212  1.00   46.62  ? 79   ILE A CD1 1 
ATOM   2938 N N   . ALA B 1 80  ? -5.109  -13.849 14.702  1.00   39.70  ? 80   ALA A N   1 
ATOM   2939 C CA  . ALA B 1 80  ? -5.584  -14.168 16.054  1.00   39.31  ? 80   ALA A CA  1 
ATOM   2940 C C   . ALA B 1 80  ? -5.272  -13.029 17.031  1.00   39.24  ? 80   ALA A C   1 
ATOM   2941 O O   . ALA B 1 80  ? -5.202  -13.237 18.254  1.00   39.11  ? 80   ALA A O   1 
ATOM   2942 C CB  . ALA B 1 80  ? -4.993  -15.493 16.540  1.00   38.45  ? 80   ALA A CB  1 
ATOM   2943 N N   . SER B 1 81  ? -5.071  -11.830 16.489  1.00   39.12  ? 81   SER A N   1 
ATOM   2944 C CA  . SER B 1 81  ? -4.980  -10.604 17.292  1.00   39.85  ? 81   SER A CA  1 
ATOM   2945 C C   . SER B 1 81  ? -3.840  -10.545 18.305  1.00   40.26  ? 81   SER A C   1 
ATOM   2946 O O   . SER B 1 81  ? -3.953  -9.855  19.326  1.00   40.87  ? 81   SER A O   1 
ATOM   2947 C CB  . SER B 1 81  ? -6.310  -10.301 18.005  1.00   40.08  ? 81   SER A CB  1 
ATOM   2948 O OG  . SER B 1 81  ? -7.394  -10.203 17.092  1.00   40.43  ? 81   SER A OG  1 
ATOM   2949 N N   . ALA B 1 82  ? -2.739  -11.241 18.033  1.00   40.98  ? 82   ALA A N   1 
ATOM   2950 C CA  . ALA B 1 82  ? -1.506  -10.964 18.763  1.00   41.41  ? 82   ALA A CA  1 
ATOM   2951 C C   . ALA B 1 82  ? -1.264  -9.459  18.751  1.00   41.93  ? 82   ALA A C   1 
ATOM   2952 O O   . ALA B 1 82  ? -1.609  -8.776  17.781  1.00   41.82  ? 82   ALA A O   1 
ATOM   2953 C CB  . ALA B 1 82  ? -0.329  -11.685 18.141  1.00   40.91  ? 82   ALA A CB  1 
ATOM   2954 N N   . SER B 1 83  ? -0.689  -8.941  19.830  1.00   42.43  ? 83   SER A N   1 
ATOM   2955 C CA  . SER B 1 83  ? -0.372  -7.525  19.902  1.00   42.90  ? 83   SER A CA  1 
ATOM   2956 C C   . SER B 1 83  ? 0.827   -7.162  19.027  1.00   42.27  ? 83   SER A C   1 
ATOM   2957 O O   . SER B 1 83  ? 0.881   -6.061  18.478  1.00   42.60  ? 83   SER A O   1 
ATOM   2958 C CB  . SER B 1 83  ? -0.122  -7.099  21.349  1.00   43.52  ? 83   SER A CB  1 
ATOM   2959 O OG  . SER B 1 83  ? 0.551   -5.854  21.401  1.00   45.36  ? 83   SER A OG  1 
ATOM   2960 N N   . ARG B 1 84  ? 1.792   -8.075  18.918  1.00   40.84  ? 84   ARG A N   1 
ATOM   2961 C CA  . ARG B 1 84  ? 2.982   -7.850  18.097  1.00   39.28  ? 84   ARG A CA  1 
ATOM   2962 C C   . ARG B 1 84  ? 3.610   -9.178  17.699  1.00   37.66  ? 84   ARG A C   1 
ATOM   2963 O O   . ARG B 1 84  ? 3.676   -10.109 18.509  1.00   36.00  ? 84   ARG A O   1 
ATOM   2964 C CB  . ARG B 1 84  ? 4.006   -6.967  18.833  1.00   40.03  ? 84   ARG A CB  1 
ATOM   2965 C CG  . ARG B 1 84  ? 5.267   -6.665  18.022  1.00   42.49  ? 84   ARG A CG  1 
ATOM   2966 C CD  . ARG B 1 84  ? 6.124   -5.552  18.631  1.00   46.03  ? 84   ARG A CD  1 
ATOM   2967 N NE  . ARG B 1 84  ? 6.758   -5.956  19.886  1.00   50.95  ? 84   ARG A NE  1 
ATOM   2968 C CZ  . ARG B 1 84  ? 7.394   -5.123  20.705  1.00   52.58  ? 84   ARG A CZ  1 
ATOM   2969 N NH1 . ARG B 1 84  ? 7.485   -3.828  20.411  1.00   54.13  ? 84   ARG A NH1 1 
ATOM   2970 N NH2 . ARG B 1 84  ? 7.939   -5.582  21.821  1.00   52.11  ? 84   ARG A NH2 1 
ATOM   2971 N N   . VAL B 1 85  ? 4.052   -9.276  16.445  1.00   35.62  ? 85   VAL A N   1 
ATOM   2972 C CA  . VAL B 1 85  ? 4.727   -10.489 15.985  1.00   34.27  ? 85   VAL A CA  1 
ATOM   2973 C C   . VAL B 1 85  ? 6.141   -10.205 15.486  1.00   33.33  ? 85   VAL A C   1 
ATOM   2974 O O   . VAL B 1 85  ? 6.340   -9.426  14.561  1.00   33.88  ? 85   VAL A O   1 
ATOM   2975 C CB  . VAL B 1 85  ? 3.930   -11.234 14.885  1.00   34.61  ? 85   VAL A CB  1 
ATOM   2976 C CG1 . VAL B 1 85  ? 4.595   -12.567 14.566  1.00   34.04  ? 85   VAL A CG1 1 
ATOM   2977 C CG2 . VAL B 1 85  ? 2.478   -11.441 15.300  1.00   34.36  ? 85   VAL A CG2 1 
ATOM   2978 N N   . THR B 1 86  ? 7.111   -10.859 16.107  1.00   31.14  ? 86   THR A N   1 
ATOM   2979 C CA  . THR B 1 86  ? 8.510   -10.759 15.719  1.00   30.91  ? 86   THR A CA  1 
ATOM   2980 C C   . THR B 1 86  ? 8.933   -12.086 15.139  1.00   30.63  ? 86   THR A C   1 
ATOM   2981 O O   . THR B 1 86  ? 8.649   -13.140 15.722  1.00   29.57  ? 86   THR A O   1 
ATOM   2982 C CB  . THR B 1 86  ? 9.398   -10.439 16.938  1.00   31.47  ? 86   THR A CB  1 
ATOM   2983 O OG1 . THR B 1 86  ? 9.057   -9.142  17.423  1.00   33.07  ? 86   THR A OG1 1 
ATOM   2984 C CG2 . THR B 1 86  ? 10.900  -10.474 16.593  1.00   28.78  ? 86   THR A CG2 1 
ATOM   2985 N N   . ALA B 1 87  ? 9.584   -12.039 13.979  1.00   29.81  ? 87   ALA A N   1 
ATOM   2986 C CA  . ALA B 1 87  ? 10.205  -13.227 13.424  1.00   30.20  ? 87   ALA A CA  1 
ATOM   2987 C C   . ALA B 1 87  ? 11.641  -13.217 13.890  1.00   30.17  ? 87   ALA A C   1 
ATOM   2988 O O   . ALA B 1 87  ? 12.361  -12.245 13.682  1.00   29.95  ? 87   ALA A O   1 
ATOM   2989 C CB  . ALA B 1 87  ? 10.120  -13.234 11.884  1.00   29.61  ? 87   ALA A CB  1 
ATOM   2990 N N   . VAL B 1 88  ? 12.048  -14.291 14.557  1.00   29.96  ? 88   VAL A N   1 
ATOM   2991 C CA  . VAL B 1 88  ? 13.414  -14.414 15.034  1.00   29.54  ? 88   VAL A CA  1 
ATOM   2992 C C   . VAL B 1 88  ? 14.064  -15.395 14.079  1.00   30.88  ? 88   VAL A C   1 
ATOM   2993 O O   . VAL B 1 88  ? 13.699  -16.563 14.034  1.00   30.21  ? 88   VAL A O   1 
ATOM   2994 C CB  . VAL B 1 88  ? 13.486  -14.920 16.510  1.00   29.05  ? 88   VAL A CB  1 
ATOM   2995 C CG1 . VAL B 1 88  ? 14.900  -15.304 16.882  1.00   28.60  ? 88   VAL A CG1 1 
ATOM   2996 C CG2 . VAL B 1 88  ? 12.946  -13.852 17.483  1.00   28.96  ? 88   VAL A CG2 1 
ATOM   2997 N N   . ILE B 1 89  ? 15.011  -14.901 13.295  1.00   31.67  ? 89   ILE A N   1 
ATOM   2998 C CA  . ILE B 1 89  ? 15.548  -15.669 12.173  1.00   34.64  ? 89   ILE A CA  1 
ATOM   2999 C C   . ILE B 1 89  ? 17.076  -15.612 12.183  1.00   36.60  ? 89   ILE A C   1 
ATOM   3000 O O   . ILE B 1 89  ? 17.670  -14.802 11.484  1.00   36.26  ? 89   ILE A O   1 
ATOM   3001 C CB  . ILE B 1 89  ? 15.015  -15.121 10.817  1.00   35.12  ? 89   ILE A CB  1 
ATOM   3002 C CG1 . ILE B 1 89  ? 13.488  -15.040 10.795  1.00   35.43  ? 89   ILE A CG1 1 
ATOM   3003 C CG2 . ILE B 1 89  ? 15.471  -15.999 9.646   1.00   35.07  ? 89   ILE A CG2 1 
ATOM   3004 C CD1 . ILE B 1 89  ? 12.986  -14.112 9.655   1.00   38.43  ? 89   ILE A CD1 1 
ATOM   3005 N N   . PRO B 1 90  ? 17.723  -16.478 12.977  1.00   39.76  ? 90   PRO A N   1 
ATOM   3006 C CA  . PRO B 1 90  ? 19.180  -16.423 13.125  1.00   41.29  ? 90   PRO A CA  1 
ATOM   3007 C C   . PRO B 1 90  ? 19.911  -16.417 11.782  1.00   42.24  ? 90   PRO A C   1 
ATOM   3008 O O   . PRO B 1 90  ? 20.843  -15.631 11.596  1.00   43.16  ? 90   PRO A O   1 
ATOM   3009 C CB  . PRO B 1 90  ? 19.503  -17.697 13.905  1.00   41.62  ? 90   PRO A CB  1 
ATOM   3010 C CG  . PRO B 1 90  ? 18.259  -18.037 14.615  1.00   41.59  ? 90   PRO A CG  1 
ATOM   3011 C CD  . PRO B 1 90  ? 17.134  -17.591 13.739  1.00   40.28  ? 90   PRO A CD  1 
ATOM   3012 N N   . CYS B 1 91  ? 19.481  -17.265 10.852  1.00   42.70  ? 91   CYS A N   1 
ATOM   3013 C CA  . CYS B 1 91  ? 20.087  -17.311 9.518   1.00   43.56  ? 91   CYS A CA  1 
ATOM   3014 C C   . CYS B 1 91  ? 19.040  -16.950 8.460   1.00   42.74  ? 91   CYS A C   1 
ATOM   3015 O O   . CYS B 1 91  ? 18.085  -17.694 8.241   1.00   41.98  ? 91   CYS A O   1 
ATOM   3016 C CB  . CYS B 1 91  ? 20.717  -18.689 9.253   1.00   43.94  ? 91   CYS A CB  1 
ATOM   3017 S SG  . CYS B 1 91  ? 21.552  -18.851 7.638   1.00   49.61  ? 91   CYS A SG  1 
ATOM   3018 N N   . PHE B 1 92  ? 19.220  -15.799 7.819   1.00   42.00  ? 92   PHE A N   1 
ATOM   3019 C CA  . PHE B 1 92  ? 18.171  -15.227 6.976   1.00   42.85  ? 92   PHE A CA  1 
ATOM   3020 C C   . PHE B 1 92  ? 18.177  -15.887 5.595   1.00   44.33  ? 92   PHE A C   1 
ATOM   3021 O O   . PHE B 1 92  ? 19.182  -15.814 4.880   1.00   44.00  ? 92   PHE A O   1 
ATOM   3022 C CB  . PHE B 1 92  ? 18.344  -13.708 6.873   1.00   42.07  ? 92   PHE A CB  1 
ATOM   3023 C CG  . PHE B 1 92  ? 17.175  -12.989 6.233   1.00   40.20  ? 92   PHE A CG  1 
ATOM   3024 C CD1 . PHE B 1 92  ? 16.210  -12.366 7.018   1.00   39.59  ? 92   PHE A CD1 1 
ATOM   3025 C CD2 . PHE B 1 92  ? 17.056  -12.917 4.847   1.00   39.34  ? 92   PHE A CD2 1 
ATOM   3026 C CE1 . PHE B 1 92  ? 15.143  -11.696 6.432   1.00   39.65  ? 92   PHE A CE1 1 
ATOM   3027 C CE2 . PHE B 1 92  ? 15.987  -12.247 4.251   1.00   36.80  ? 92   PHE A CE2 1 
ATOM   3028 C CZ  . PHE B 1 92  ? 15.040  -11.632 5.042   1.00   37.67  ? 92   PHE A CZ  1 
ATOM   3029 N N   . PRO B 1 93  ? 17.055  -16.539 5.225   1.00   45.72  ? 93   PRO A N   1 
ATOM   3030 C CA  . PRO B 1 93  ? 16.945  -17.311 3.987   1.00   46.47  ? 93   PRO A CA  1 
ATOM   3031 C C   . PRO B 1 93  ? 17.108  -16.434 2.763   1.00   46.58  ? 93   PRO A C   1 
ATOM   3032 O O   . PRO B 1 93  ? 16.665  -15.277 2.771   1.00   46.88  ? 93   PRO A O   1 
ATOM   3033 C CB  . PRO B 1 93  ? 15.515  -17.857 4.038   1.00   46.74  ? 93   PRO A CB  1 
ATOM   3034 C CG  . PRO B 1 93  ? 14.782  -16.940 4.927   1.00   46.70  ? 93   PRO A CG  1 
ATOM   3035 C CD  . PRO B 1 93  ? 15.773  -16.497 5.953   1.00   46.07  ? 93   PRO A CD  1 
ATOM   3036 N N   . TYR B 1 94  ? 17.743  -16.988 1.729   1.00   46.22  ? 94   TYR A N   1 
ATOM   3037 C CA  . TYR B 1 94  ? 18.024  -16.272 0.484   1.00   45.49  ? 94   TYR A CA  1 
ATOM   3038 C C   . TYR B 1 94  ? 18.849  -15.006 0.689   1.00   44.95  ? 94   TYR A C   1 
ATOM   3039 O O   . TYR B 1 94  ? 18.879  -14.146 -0.187  1.00   44.87  ? 94   TYR A O   1 
ATOM   3040 C CB  . TYR B 1 94  ? 16.722  -15.963 -0.278  1.00   45.73  ? 94   TYR A CB  1 
ATOM   3041 C CG  . TYR B 1 94  ? 16.025  -17.211 -0.758  1.00   46.11  ? 94   TYR A CG  1 
ATOM   3042 C CD1 . TYR B 1 94  ? 15.154  -17.905 0.075   1.00   47.36  ? 94   TYR A CD1 1 
ATOM   3043 C CD2 . TYR B 1 94  ? 16.260  -17.719 -2.035  1.00   47.08  ? 94   TYR A CD2 1 
ATOM   3044 C CE1 . TYR B 1 94  ? 14.519  -19.056 -0.351  1.00   46.79  ? 94   TYR A CE1 1 
ATOM   3045 C CE2 . TYR B 1 94  ? 15.632  -18.874 -2.471  1.00   46.69  ? 94   TYR A CE2 1 
ATOM   3046 C CZ  . TYR B 1 94  ? 14.761  -19.536 -1.620  1.00   47.08  ? 94   TYR A CZ  1 
ATOM   3047 O OH  . TYR B 1 94  ? 14.126  -20.684 -2.023  1.00   45.97  ? 94   TYR A OH  1 
ATOM   3048 N N   . ALA B 1 95  ? 19.526  -14.888 1.830   1.00   43.86  ? 95   ALA A N   1 
ATOM   3049 C CA  . ALA B 1 95  ? 20.356  -13.698 2.079   1.00   43.23  ? 95   ALA A CA  1 
ATOM   3050 C C   . ALA B 1 95  ? 21.402  -13.477 0.985   1.00   42.23  ? 95   ALA A C   1 
ATOM   3051 O O   . ALA B 1 95  ? 21.685  -12.333 0.621   1.00   43.13  ? 95   ALA A O   1 
ATOM   3052 C CB  . ALA B 1 95  ? 21.023  -13.755 3.444   1.00   43.31  ? 95   ALA A CB  1 
ATOM   3053 N N   . ARG B 1 96  ? 21.962  -14.563 0.455   0.33   39.77  ? 96   ARG A N   1 
ATOM   3054 C CA  . ARG B 1 96  ? 22.945  -14.461 -0.620  0.33   38.55  ? 96   ARG A CA  1 
ATOM   3055 C C   . ARG B 1 96  ? 22.345  -13.984 -1.942  0.33   38.92  ? 96   ARG A C   1 
ATOM   3056 O O   . ARG B 1 96  ? 23.082  -13.628 -2.857  0.33   35.63  ? 96   ARG A O   1 
ATOM   3057 C CB  . ARG B 1 96  ? 23.662  -15.792 -0.823  0.33   38.35  ? 96   ARG A CB  1 
ATOM   3058 C CG  . ARG B 1 96  ? 24.611  -16.129 0.301   0.33   38.88  ? 96   ARG A CG  1 
ATOM   3059 C CD  . ARG B 1 96  ? 24.338  -17.519 0.793   0.33   40.82  ? 96   ARG A CD  1 
ATOM   3060 N NE  . ARG B 1 96  ? 24.971  -18.534 -0.034  0.33   42.79  ? 96   ARG A NE  1 
ATOM   3061 C CZ  . ARG B 1 96  ? 24.527  -19.781 -0.141  0.33   43.45  ? 96   ARG A CZ  1 
ATOM   3062 N NH1 . ARG B 1 96  ? 23.436  -20.153 0.516   0.33   43.08  ? 96   ARG A NH1 1 
ATOM   3063 N NH2 . ARG B 1 96  ? 25.166  -20.649 -0.914  0.33   43.85  ? 96   ARG A NH2 1 
ATOM   3064 N N   . GLN B 1 97  ? 21.019  -13.994 -2.045  0.62   41.95  ? 97   GLN A N   1 
ATOM   3065 C CA  . GLN B 1 97  ? 20.341  -13.512 -3.246  0.62   45.75  ? 97   GLN A CA  1 
ATOM   3066 C C   . GLN B 1 97  ? 19.770  -12.113 -2.996  0.62   47.94  ? 97   GLN A C   1 
ATOM   3067 O O   . GLN B 1 97  ? 18.553  -11.918 -2.962  0.62   47.98  ? 97   GLN A O   1 
ATOM   3068 C CB  . GLN B 1 97  ? 19.251  -14.498 -3.694  0.62   45.79  ? 97   GLN A CB  1 
ATOM   3069 C CG  . GLN B 1 97  ? 19.790  -15.803 -4.293  0.62   46.99  ? 97   GLN A CG  1 
ATOM   3070 C CD  . GLN B 1 97  ? 18.695  -16.786 -4.684  0.62   48.57  ? 97   GLN A CD  1 
ATOM   3071 O OE1 . GLN B 1 97  ? 17.799  -16.467 -5.472  0.62   48.88  ? 97   GLN A OE1 1 
ATOM   3072 N NE2 . GLN B 1 97  ? 18.770  -17.996 -4.139  0.62   48.81  ? 97   GLN A NE2 1 
ATOM   3073 N N   . ASP B 1 98  ? 20.675  -11.150 -2.838  1.00   51.00  ? 98   ASP A N   1 
ATOM   3074 C CA  . ASP B 1 98  ? 20.332  -9.798  -2.401  1.00   53.68  ? 98   ASP A CA  1 
ATOM   3075 C C   . ASP B 1 98  ? 20.690  -8.712  -3.425  1.00   54.61  ? 98   ASP A C   1 
ATOM   3076 O O   . ASP B 1 98  ? 20.570  -7.515  -3.140  1.00   55.05  ? 98   ASP A O   1 
ATOM   3077 C CB  . ASP B 1 98  ? 20.996  -9.501  -1.050  1.00   54.13  ? 98   ASP A CB  1 
ATOM   3078 C CG  . ASP B 1 98  ? 22.513  -9.403  -1.144  1.00   56.19  ? 98   ASP A CG  1 
ATOM   3079 O OD1 . ASP B 1 98  ? 23.124  -10.054 -2.022  1.00   58.21  ? 98   ASP A OD1 1 
ATOM   3080 O OD2 . ASP B 1 98  ? 23.103  -8.678  -0.321  1.00   58.43  ? 98   ASP A OD2 1 
ATOM   3081 N N   . LYS B 1 99  ? 21.123  -9.142  -4.609  1.00   55.24  ? 99   LYS A N   1 
ATOM   3082 C CA  . LYS B 1 99  ? 21.423  -8.244  -5.730  1.00   55.46  ? 99   LYS A CA  1 
ATOM   3083 C C   . LYS B 1 99  ? 21.384  -9.028  -7.048  1.00   54.59  ? 99   LYS A C   1 
ATOM   3084 O O   . LYS B 1 99  ? 21.478  -10.256 -7.043  1.00   54.56  ? 99   LYS A O   1 
ATOM   3085 C CB  . LYS B 1 99  ? 22.793  -7.585  -5.544  1.00   55.74  ? 99   LYS A CB  1 
ATOM   3086 C CG  . LYS B 1 99  ? 23.945  -8.579  -5.489  1.00   58.20  ? 99   LYS A CG  1 
ATOM   3087 C CD  . LYS B 1 99  ? 25.264  -7.904  -5.168  1.00   61.47  ? 99   LYS A CD  1 
ATOM   3088 C CE  . LYS B 1 99  ? 26.438  -8.787  -5.572  1.00   63.45  ? 99   LYS A CE  1 
ATOM   3089 N NZ  . LYS B 1 99  ? 26.399  -10.138 -4.933  1.00   64.48  ? 99   LYS A NZ  1 
ATOM   3090 N N   . LYS B 1 100 ? 21.246  -8.319  -8.167  0.71   53.46  ? 100  LYS A N   1 
ATOM   3091 C CA  . LYS B 1 100 ? 21.193  -8.963  -9.490  0.71   52.16  ? 100  LYS A CA  1 
ATOM   3092 C C   . LYS B 1 100 ? 22.569  -9.404  -9.980  0.71   51.35  ? 100  LYS A C   1 
ATOM   3093 O O   . LYS B 1 100 ? 22.685  -10.389 -10.709 0.71   51.45  ? 100  LYS A O   1 
ATOM   3094 C CB  . LYS B 1 100 ? 20.572  -8.037  -10.536 0.71   52.05  ? 100  LYS A CB  1 
ATOM   3095 C CG  . LYS B 1 100 ? 19.099  -7.731  -10.353 0.71   51.32  ? 100  LYS A CG  1 
ATOM   3096 C CD  . LYS B 1 100 ? 18.625  -6.896  -11.522 0.71   49.55  ? 100  LYS A CD  1 
ATOM   3097 C CE  . LYS B 1 100 ? 17.326  -6.183  -11.211 0.71   49.32  ? 100  LYS A CE  1 
ATOM   3098 N NZ  . LYS B 1 100 ? 17.093  -5.007  -12.116 0.71   47.64  ? 100  LYS A NZ  1 
ATOM   3099 N N   . ASP B 1 101 ? 23.602  -8.658  -9.601  0.22   50.12  ? 101  ASP A N   1 
ATOM   3100 C CA  . ASP B 1 101 ? 24.976  -9.009  -9.955  0.22   49.54  ? 101  ASP A CA  1 
ATOM   3101 C C   . ASP B 1 101 ? 25.163  -9.145  -11.467 0.22   50.04  ? 101  ASP A C   1 
ATOM   3102 O O   . ASP B 1 101 ? 25.723  -10.134 -11.937 0.22   49.46  ? 101  ASP A O   1 
ATOM   3103 C CB  . ASP B 1 101 ? 25.381  -10.315 -9.260  0.22   49.00  ? 101  ASP A CB  1 
ATOM   3104 C CG  . ASP B 1 101 ? 26.875  -10.580 -9.325  0.22   48.57  ? 101  ASP A CG  1 
ATOM   3105 O OD1 . ASP B 1 101 ? 27.657  -9.712  -8.880  0.22   47.99  ? 101  ASP A OD1 1 
ATOM   3106 O OD2 . ASP B 1 101 ? 27.269  -11.665 -9.805  0.22   48.34  ? 101  ASP A OD2 1 
ATOM   3107 N N   . LYS B 1 102 ? 24.691  -8.155  -12.224 0.48   51.71  ? 102  LYS A N   1 
ATOM   3108 C CA  . LYS B 1 102 ? 24.842  -8.164  -13.683 0.48   54.00  ? 102  LYS A CA  1 
ATOM   3109 C C   . LYS B 1 102 ? 23.943  -9.155  -14.418 0.48   55.84  ? 102  LYS A C   1 
ATOM   3110 O O   . LYS B 1 102 ? 23.984  -9.237  -15.653 0.48   55.94  ? 102  LYS A O   1 
ATOM   3111 C CB  . LYS B 1 102 ? 26.288  -8.477  -14.071 0.48   53.81  ? 102  LYS A CB  1 
ATOM   3112 C CG  . LYS B 1 102 ? 27.097  -7.297  -14.561 0.48   54.18  ? 102  LYS A CG  1 
ATOM   3113 C CD  . LYS B 1 102 ? 28.244  -7.778  -15.440 0.48   54.82  ? 102  LYS A CD  1 
ATOM   3114 C CE  . LYS B 1 102 ? 29.052  -6.617  -15.993 0.48   55.07  ? 102  LYS A CE  1 
ATOM   3115 N NZ  . LYS B 1 102 ? 29.929  -7.038  -17.127 0.48   55.34  ? 102  LYS A NZ  1 
ATOM   3116 N N   . SER B 1 103 ? 23.149  -9.914  -13.666 1.00   58.28  ? 103  SER A N   1 
ATOM   3117 C CA  . SER B 1 103 ? 22.314  -10.954 -14.261 1.00   60.33  ? 103  SER A CA  1 
ATOM   3118 C C   . SER B 1 103 ? 20.851  -10.530 -14.288 1.00   60.64  ? 103  SER A C   1 
ATOM   3119 O O   . SER B 1 103 ? 20.490  -9.462  -13.780 1.00   61.17  ? 103  SER A O   1 
ATOM   3120 C CB  . SER B 1 103 ? 22.476  -12.276 -13.499 1.00   60.70  ? 103  SER A CB  1 
ATOM   3121 O OG  . SER B 1 103 ? 23.799  -12.773 -13.607 1.00   61.73  ? 103  SER A OG  1 
ATOM   3122 N N   . ARG B 1 104 ? 20.017  -11.368 -14.898 1.00   60.27  ? 104  ARG A N   1 
ATOM   3123 C CA  . ARG B 1 104 ? 18.571  -11.179 -14.885 1.00   59.36  ? 104  ARG A CA  1 
ATOM   3124 C C   . ARG B 1 104 ? 17.978  -12.026 -13.765 1.00   58.18  ? 104  ARG A C   1 
ATOM   3125 O O   . ARG B 1 104 ? 17.065  -12.826 -13.984 1.00   58.39  ? 104  ARG A O   1 
ATOM   3126 C CB  . ARG B 1 104 ? 17.960  -11.559 -16.240 1.00   59.70  ? 104  ARG A CB  1 
ATOM   3127 C CG  . ARG B 1 104 ? 17.967  -10.439 -17.271 1.00   60.66  ? 104  ARG A CG  1 
ATOM   3128 C CD  . ARG B 1 104 ? 17.289  -10.860 -18.578 1.00   61.42  ? 104  ARG A CD  1 
ATOM   3129 N NE  . ARG B 1 104 ? 18.150  -11.709 -19.402 1.00   62.09  ? 104  ARG A NE  1 
ATOM   3130 C CZ  . ARG B 1 104 ? 18.836  -11.286 -20.461 1.00   63.27  ? 104  ARG A CZ  1 
ATOM   3131 N NH1 . ARG B 1 104 ? 18.764  -10.018 -20.844 1.00   62.72  ? 104  ARG A NH1 1 
ATOM   3132 N NH2 . ARG B 1 104 ? 19.591  -12.138 -21.146 1.00   64.25  ? 104  ARG A NH2 1 
ATOM   3133 N N   . ALA B 1 105 ? 18.505  -11.831 -12.560 1.00   56.05  ? 105  ALA A N   1 
ATOM   3134 C CA  . ALA B 1 105 ? 18.193  -12.686 -11.422 1.00   54.07  ? 105  ALA A CA  1 
ATOM   3135 C C   . ALA B 1 105 ? 17.169  -12.045 -10.484 1.00   52.33  ? 105  ALA A C   1 
ATOM   3136 O O   . ALA B 1 105 ? 16.963  -10.827 -10.519 1.00   51.69  ? 105  ALA A O   1 
ATOM   3137 C CB  . ALA B 1 105 ? 19.477  -13.026 -10.665 1.00   54.34  ? 105  ALA A CB  1 
ATOM   3138 N N   . PRO B 1 106 ? 16.515  -12.863 -9.644  1.00   50.89  ? 106  PRO A N   1 
ATOM   3139 C CA  . PRO B 1 106 ? 15.636  -12.263 -8.653  1.00   50.10  ? 106  PRO A CA  1 
ATOM   3140 C C   . PRO B 1 106 ? 16.472  -11.670 -7.520  1.00   49.14  ? 106  PRO A C   1 
ATOM   3141 O O   . PRO B 1 106 ? 17.582  -12.146 -7.266  1.00   48.64  ? 106  PRO A O   1 
ATOM   3142 C CB  . PRO B 1 106 ? 14.855  -13.463 -8.128  1.00   50.14  ? 106  PRO A CB  1 
ATOM   3143 C CG  . PRO B 1 106 ? 15.848  -14.597 -8.221  1.00   50.56  ? 106  PRO A CG  1 
ATOM   3144 C CD  . PRO B 1 106 ? 16.596  -14.333 -9.497  1.00   50.92  ? 106  PRO A CD  1 
ATOM   3145 N N   . ILE B 1 107 ? 15.964  -10.636 -6.859  1.00   48.39  ? 107  ILE A N   1 
ATOM   3146 C CA  . ILE B 1 107 ? 16.524  -10.250 -5.562  1.00   47.40  ? 107  ILE A CA  1 
ATOM   3147 C C   . ILE B 1 107 ? 15.657  -10.970 -4.523  1.00   45.99  ? 107  ILE A C   1 
ATOM   3148 O O   . ILE B 1 107 ? 14.718  -10.392 -3.969  1.00   45.69  ? 107  ILE A O   1 
ATOM   3149 C CB  . ILE B 1 107 ? 16.526  -8.725  -5.353  1.00   47.93  ? 107  ILE A CB  1 
ATOM   3150 C CG1 . ILE B 1 107 ? 17.047  -8.019  -6.613  1.00   48.45  ? 107  ILE A CG1 1 
ATOM   3151 C CG2 . ILE B 1 107 ? 17.355  -8.351  -4.109  1.00   48.10  ? 107  ILE A CG2 1 
ATOM   3152 C CD1 . ILE B 1 107 ? 16.864  -6.516  -6.622  1.00   49.58  ? 107  ILE A CD1 1 
ATOM   3153 N N   . SER B 1 108 ? 15.959  -12.250 -4.309  1.00   44.13  ? 108  SER A N   1 
ATOM   3154 C CA  . SER B 1 108 ? 15.106  -13.140 -3.524  1.00   42.61  ? 108  SER A CA  1 
ATOM   3155 C C   . SER B 1 108 ? 15.003  -12.692 -2.073  1.00   41.27  ? 108  SER A C   1 
ATOM   3156 O O   . SER B 1 108 ? 13.936  -12.786 -1.468  1.00   40.91  ? 108  SER A O   1 
ATOM   3157 C CB  . SER B 1 108 ? 15.622  -14.577 -3.587  1.00   43.05  ? 108  SER A CB  1 
ATOM   3158 O OG  . SER B 1 108 ? 15.489  -15.111 -4.886  1.00   43.65  ? 108  SER A OG  1 
ATOM   3159 N N   . ALA B 1 109 ? 16.113  -12.191 -1.535  1.00   39.48  ? 109  ALA A N   1 
ATOM   3160 C CA  . ALA B 1 109 ? 16.153  -11.665 -0.170  1.00   37.78  ? 109  ALA A CA  1 
ATOM   3161 C C   . ALA B 1 109 ? 15.157  -10.524 0.012   1.00   36.66  ? 109  ALA A C   1 
ATOM   3162 O O   . ALA B 1 109 ? 14.561  -10.390 1.084   1.00   36.06  ? 109  ALA A O   1 
ATOM   3163 C CB  . ALA B 1 109 ? 17.560  -11.200 0.185   1.00   38.03  ? 109  ALA A CB  1 
ATOM   3164 N N   . LYS B 1 110 ? 14.975  -9.708  -1.029  1.00   34.93  ? 110  LYS A N   1 
ATOM   3165 C CA  . LYS B 1 110 ? 13.956  -8.662  -1.004  1.00   34.18  ? 110  LYS A CA  1 
ATOM   3166 C C   . LYS B 1 110 ? 12.576  -9.280  -1.099  1.00   33.67  ? 110  LYS A C   1 
ATOM   3167 O O   . LYS B 1 110 ? 11.647  -8.837  -0.434  1.00   33.72  ? 110  LYS A O   1 
ATOM   3168 C CB  . LYS B 1 110 ? 14.154  -7.633  -2.129  1.00   34.23  ? 110  LYS A CB  1 
ATOM   3169 C CG  . LYS B 1 110 ? 13.044  -6.560  -2.182  1.00   33.49  ? 110  LYS A CG  1 
ATOM   3170 C CD  . LYS B 1 110 ? 12.940  -5.825  -0.832  1.00   35.38  ? 110  LYS A CD  1 
ATOM   3171 C CE  . LYS B 1 110 ? 11.802  -4.822  -0.791  1.00   35.32  ? 110  LYS A CE  1 
ATOM   3172 N NZ  . LYS B 1 110 ? 11.924  -3.864  -1.911  1.00   39.17  ? 110  LYS A NZ  1 
ATOM   3173 N N   . LEU B 1 111 ? 12.446  -10.312 -1.928  1.00   33.63  ? 111  LEU A N   1 
ATOM   3174 C CA  . LEU B 1 111 ? 11.203  -11.060 -1.999  1.00   33.51  ? 111  LEU A CA  1 
ATOM   3175 C C   . LEU B 1 111 ? 10.848  -11.596 -0.596  1.00   32.05  ? 111  LEU A C   1 
ATOM   3176 O O   . LEU B 1 111 ? 9.742   -11.374 -0.099  1.00   32.60  ? 111  LEU A O   1 
ATOM   3177 C CB  . LEU B 1 111 ? 11.363  -12.214 -2.985  1.00   34.12  ? 111  LEU A CB  1 
ATOM   3178 C CG  . LEU B 1 111 ? 10.168  -12.869 -3.682  1.00   36.77  ? 111  LEU A CG  1 
ATOM   3179 C CD1 . LEU B 1 111 ? 10.405  -14.366 -3.743  1.00   37.59  ? 111  LEU A CD1 1 
ATOM   3180 C CD2 . LEU B 1 111 ? 8.829   -12.574 -3.040  1.00   37.81  ? 111  LEU A CD2 1 
ATOM   3181 N N   . VAL B 1 112 ? 11.786  -12.295 0.034   1.00   30.03  ? 112  VAL A N   1 
ATOM   3182 C CA  . VAL B 1 112 ? 11.571  -12.839 1.383   1.00   30.30  ? 112  VAL A CA  1 
ATOM   3183 C C   . VAL B 1 112 ? 11.189  -11.739 2.382   1.00   29.95  ? 112  VAL A C   1 
ATOM   3184 O O   . VAL B 1 112 ? 10.250  -11.898 3.155   1.00   30.46  ? 112  VAL A O   1 
ATOM   3185 C CB  . VAL B 1 112 ? 12.789  -13.636 1.894   1.00   30.30  ? 112  VAL A CB  1 
ATOM   3186 C CG1 . VAL B 1 112 ? 12.542  -14.120 3.337   1.00   30.44  ? 112  VAL A CG1 1 
ATOM   3187 C CG2 . VAL B 1 112 ? 13.051  -14.842 0.989   1.00   30.17  ? 112  VAL A CG2 1 
ATOM   3188 N N   . ALA B 1 113 ? 11.867  -10.601 2.329   1.00   30.36  ? 113  ALA A N   1 
ATOM   3189 C CA  . ALA B 1 113 ? 11.509  -9.480  3.205   1.00   30.51  ? 113  ALA A CA  1 
ATOM   3190 C C   . ALA B 1 113 ? 10.048  -9.064  2.998   1.00   30.64  ? 113  ALA A C   1 
ATOM   3191 O O   . ALA B 1 113 ? 9.302   -8.856  3.971   1.00   30.79  ? 113  ALA A O   1 
ATOM   3192 C CB  . ALA B 1 113 ? 12.446  -8.305  2.976   1.00   29.71  ? 113  ALA A CB  1 
ATOM   3193 N N   . ASN B 1 114 ? 9.646   -8.946  1.728   1.00   29.93  ? 114  ASN A N   1 
ATOM   3194 C CA  . ASN B 1 114 ? 8.271   -8.593  1.377   1.00   30.27  ? 114  ASN A CA  1 
ATOM   3195 C C   . ASN B 1 114 ? 7.269   -9.637  1.844   1.00   29.56  ? 114  ASN A C   1 
ATOM   3196 O O   . ASN B 1 114 ? 6.186   -9.296  2.305   1.00   30.91  ? 114  ASN A O   1 
ATOM   3197 C CB  . ASN B 1 114 ? 8.126   -8.372  -0.138  1.00   30.90  ? 114  ASN A CB  1 
ATOM   3198 C CG  . ASN B 1 114 ? 8.675   -7.024  -0.594  1.00   33.38  ? 114  ASN A CG  1 
ATOM   3199 O OD1 . ASN B 1 114 ? 8.882   -6.112  0.211   1.00   37.68  ? 114  ASN A OD1 1 
ATOM   3200 N ND2 . ASN B 1 114 ? 8.879   -6.882  -1.900  1.00   32.22  ? 114  ASN A ND2 1 
ATOM   3201 N N   . MET B 1 115 ? 7.626   -10.910 1.726   1.00   29.31  ? 115  MET A N   1 
ATOM   3202 C CA  . MET B 1 115 ? 6.731   -11.974 2.166   1.00   29.47  ? 115  MET A CA  1 
ATOM   3203 C C   . MET B 1 115 ? 6.485   -11.929 3.675   1.00   29.23  ? 115  MET A C   1 
ATOM   3204 O O   . MET B 1 115 ? 5.338   -11.988 4.126   1.00   28.81  ? 115  MET A O   1 
ATOM   3205 C CB  . MET B 1 115 ? 7.266   -13.339 1.737   1.00   29.17  ? 115  MET A CB  1 
ATOM   3206 C CG  . MET B 1 115 ? 7.172   -13.534 0.214   1.00   34.45  ? 115  MET A CG  1 
ATOM   3207 S SD  . MET B 1 115 ? 7.704   -15.167 -0.258  1.00   45.48  ? 115  MET A SD  1 
ATOM   3208 C CE  . MET B 1 115 ? 9.452   -15.074 -0.003  1.00   42.23  ? 115  MET A CE  1 
ATOM   3209 N N   . LEU B 1 116 ? 7.568   -11.809 4.442   1.00   29.86  ? 116  LEU A N   1 
ATOM   3210 C CA  . LEU B 1 116 ? 7.485   -11.666 5.903   1.00   30.55  ? 116  LEU A CA  1 
ATOM   3211 C C   . LEU B 1 116 ? 6.655   -10.464 6.290   1.00   31.93  ? 116  LEU A C   1 
ATOM   3212 O O   . LEU B 1 116 ? 5.839   -10.537 7.208   1.00   32.43  ? 116  LEU A O   1 
ATOM   3213 C CB  . LEU B 1 116 ? 8.879   -11.559 6.515   1.00   29.57  ? 116  LEU A CB  1 
ATOM   3214 C CG  . LEU B 1 116 ? 9.738   -12.818 6.431   1.00   29.36  ? 116  LEU A CG  1 
ATOM   3215 C CD1 . LEU B 1 116 ? 11.228  -12.505 6.599   1.00   28.16  ? 116  LEU A CD1 1 
ATOM   3216 C CD2 . LEU B 1 116 ? 9.284   -13.842 7.462   1.00   29.07  ? 116  LEU A CD2 1 
ATOM   3217 N N   . SER B 1 117 ? 6.850   -9.362  5.569   1.00   33.65  ? 117  SER A N   1 
ATOM   3218 C CA  . SER B 1 117 ? 6.104   -8.139  5.804   1.00   35.73  ? 117  SER A CA  1 
ATOM   3219 C C   . SER B 1 117 ? 4.615   -8.319  5.526   1.00   35.93  ? 117  SER A C   1 
ATOM   3220 O O   . SER B 1 117 ? 3.774   -8.003  6.377   1.00   36.52  ? 117  SER A O   1 
ATOM   3221 C CB  . SER B 1 117 ? 6.674   -6.989  4.967   1.00   36.55  ? 117  SER A CB  1 
ATOM   3222 O OG  . SER B 1 117 ? 8.029   -6.730  5.327   1.00   39.72  ? 117  SER A OG  1 
ATOM   3223 N N   . VAL B 1 118 ? 4.280   -8.837  4.347   1.00   35.58  ? 118  VAL A N   1 
ATOM   3224 C CA  . VAL B 1 118 ? 2.879   -9.071  4.032   1.00   35.68  ? 118  VAL A CA  1 
ATOM   3225 C C   . VAL B 1 118 ? 2.280   -10.162 4.928   1.00   35.36  ? 118  VAL A C   1 
ATOM   3226 O O   . VAL B 1 118 ? 1.109   -10.094 5.250   1.00   35.06  ? 118  VAL A O   1 
ATOM   3227 C CB  . VAL B 1 118 ? 2.635   -9.376  2.531   1.00   35.92  ? 118  VAL A CB  1 
ATOM   3228 C CG1 . VAL B 1 118 ? 2.872   -10.863 2.210   1.00   35.30  ? 118  VAL A CG1 1 
ATOM   3229 C CG2 . VAL B 1 118 ? 1.236   -8.969  2.147   1.00   37.75  ? 118  VAL A CG2 1 
ATOM   3230 N N   . ALA B 1 119 ? 3.073   -11.150 5.350   1.00   34.44  ? 119  ALA A N   1 
ATOM   3231 C CA  . ALA B 1 119 ? 2.542   -12.151 6.279   1.00   34.67  ? 119  ALA A CA  1 
ATOM   3232 C C   . ALA B 1 119 ? 2.139   -11.472 7.580   1.00   34.61  ? 119  ALA A C   1 
ATOM   3233 O O   . ALA B 1 119 ? 1.288   -11.974 8.304   1.00   35.23  ? 119  ALA A O   1 
ATOM   3234 C CB  . ALA B 1 119 ? 3.537   -13.268 6.548   1.00   33.77  ? 119  ALA A CB  1 
ATOM   3235 N N   . GLY B 1 120 ? 2.752   -10.325 7.863   1.00   34.36  ? 120  GLY A N   1 
ATOM   3236 C CA  . GLY B 1 120 ? 2.386   -9.526  9.027   1.00   33.00  ? 120  GLY A CA  1 
ATOM   3237 C C   . GLY B 1 120 ? 3.435   -9.383  10.125  1.00   32.68  ? 120  GLY A C   1 
ATOM   3238 O O   . GLY B 1 120 ? 3.085   -9.046  11.247  1.00   33.37  ? 120  GLY A O   1 
ATOM   3239 N N   . ALA B 1 121 ? 4.714   -9.623  9.830   1.00   30.97  ? 121  ALA A N   1 
ATOM   3240 C CA  . ALA B 1 121 ? 5.767   -9.432  10.841  1.00   28.72  ? 121  ALA A CA  1 
ATOM   3241 C C   . ALA B 1 121 ? 5.887   -7.956  11.203  1.00   27.42  ? 121  ALA A C   1 
ATOM   3242 O O   . ALA B 1 121 ? 5.845   -7.100  10.322  1.00   28.78  ? 121  ALA A O   1 
ATOM   3243 C CB  . ALA B 1 121 ? 7.094   -9.958  10.347  1.00   28.07  ? 121  ALA A CB  1 
ATOM   3244 N N   . ASP B 1 122 ? 6.032   -7.655  12.494  0.63   21.69  ? 122  ASP A N   1 
ATOM   3245 C CA  . ASP B 1 122 ? 6.152   -6.270  12.944  0.63   21.92  ? 122  ASP A CA  1 
ATOM   3246 C C   . ASP B 1 122 ? 7.589   -5.946  13.196  0.63   22.33  ? 122  ASP A C   1 
ATOM   3247 O O   . ASP B 1 122 ? 7.966   -4.784  13.331  0.63   20.22  ? 122  ASP A O   1 
ATOM   3248 C CB  . ASP B 1 122 ? 5.384   -6.050  14.245  0.63   22.09  ? 122  ASP A CB  1 
ATOM   3249 C CG  . ASP B 1 122 ? 3.894   -6.193  14.074  0.63   23.04  ? 122  ASP A CG  1 
ATOM   3250 O OD1 . ASP B 1 122 ? 3.286   -7.009  14.803  0.63   23.15  ? 122  ASP A OD1 1 
ATOM   3251 O OD2 . ASP B 1 122 ? 3.327   -5.490  13.212  0.63   22.86  ? 122  ASP A OD2 1 
ATOM   3252 N N   . HIS B 1 123 ? 8.410   -6.979  13.272  1.00   26.40  ? 123  HIS A N   1 
ATOM   3253 C CA  . HIS B 1 123 ? 9.756   -6.799  13.776  1.00   29.45  ? 123  HIS A CA  1 
ATOM   3254 C C   . HIS B 1 123 ? 10.552  -8.040  13.419  1.00   29.54  ? 123  HIS A C   1 
ATOM   3255 O O   . HIS B 1 123 ? 10.023  -9.149  13.428  1.00   30.38  ? 123  HIS A O   1 
ATOM   3256 C CB  . HIS B 1 123 ? 9.702   -6.557  15.307  1.00   31.48  ? 123  HIS A CB  1 
ATOM   3257 C CG  . HIS B 1 123 ? 11.031  -6.268  15.932  1.00   36.03  ? 123  HIS A CG  1 
ATOM   3258 N ND1 . HIS B 1 123 ? 11.594  -7.081  16.891  1.00   42.33  ? 123  HIS A ND1 1 
ATOM   3259 C CD2 . HIS B 1 123 ? 11.917  -5.265  15.723  1.00   40.99  ? 123  HIS A CD2 1 
ATOM   3260 C CE1 . HIS B 1 123 ? 12.768  -6.591  17.249  1.00   42.83  ? 123  HIS A CE1 1 
ATOM   3261 N NE2 . HIS B 1 123 ? 12.989  -5.490  16.554  1.00   43.08  ? 123  HIS A NE2 1 
ATOM   3262 N N   . ILE B 1 124 ? 11.811  -7.837  13.066  1.00   29.27  ? 124  ILE A N   1 
ATOM   3263 C CA  . ILE B 1 124 ? 12.721  -8.930  12.747  1.00   29.92  ? 124  ILE A CA  1 
ATOM   3264 C C   . ILE B 1 124 ? 13.920  -8.918  13.698  1.00   30.86  ? 124  ILE A C   1 
ATOM   3265 O O   . ILE B 1 124 ? 14.475  -7.864  14.000  1.00   31.29  ? 124  ILE A O   1 
ATOM   3266 C CB  . ILE B 1 124 ? 13.271  -8.834  11.271  1.00   30.07  ? 124  ILE A CB  1 
ATOM   3267 C CG1 . ILE B 1 124 ? 12.146  -8.654  10.241  1.00   28.23  ? 124  ILE A CG1 1 
ATOM   3268 C CG2 . ILE B 1 124 ? 14.172  -10.049 10.924  1.00   30.22  ? 124  ILE A CG2 1 
ATOM   3269 C CD1 . ILE B 1 124 ? 11.183  -9.854  10.094  1.00   26.54  ? 124  ILE A CD1 1 
ATOM   3270 N N   . ILE B 1 125 ? 14.323  -10.100 14.148  1.00   31.80  ? 125  ILE A N   1 
ATOM   3271 C CA  . ILE B 1 125 ? 15.597  -10.269 14.843  1.00   32.80  ? 125  ILE A CA  1 
ATOM   3272 C C   . ILE B 1 125 ? 16.395  -11.316 14.096  1.00   33.22  ? 125  ILE A C   1 
ATOM   3273 O O   . ILE B 1 125 ? 15.914  -12.418 13.849  1.00   32.93  ? 125  ILE A O   1 
ATOM   3274 C CB  . ILE B 1 125 ? 15.404  -10.707 16.333  1.00   33.84  ? 125  ILE A CB  1 
ATOM   3275 C CG1 . ILE B 1 125 ? 14.676  -9.605  17.121  1.00   34.07  ? 125  ILE A CG1 1 
ATOM   3276 C CG2 . ILE B 1 125 ? 16.762  -11.022 16.987  1.00   33.12  ? 125  ILE A CG2 1 
ATOM   3277 C CD1 . ILE B 1 125 ? 14.157  -10.049 18.494  1.00   34.36  ? 125  ILE A CD1 1 
ATOM   3278 N N   . THR B 1 126 ? 17.623  -10.974 13.735  1.00   33.74  ? 126  THR A N   1 
ATOM   3279 C CA  . THR B 1 126 ? 18.423  -11.860 12.920  1.00   36.42  ? 126  THR A CA  1 
ATOM   3280 C C   . THR B 1 126 ? 19.878  -11.770 13.358  1.00   38.08  ? 126  THR A C   1 
ATOM   3281 O O   . THR B 1 126 ? 20.221  -10.918 14.178  1.00   39.03  ? 126  THR A O   1 
ATOM   3282 C CB  . THR B 1 126 ? 18.242  -11.544 11.402  1.00   36.27  ? 126  THR A CB  1 
ATOM   3283 O OG1 . THR B 1 126 ? 18.757  -12.628 10.624  1.00   38.26  ? 126  THR A OG1 1 
ATOM   3284 C CG2 . THR B 1 126 ? 18.945  -10.244 11.021  1.00   36.38  ? 126  THR A CG2 1 
ATOM   3285 N N   . MET B 1 127 ? 20.719  -12.660 12.839  1.00   40.36  ? 127  MET A N   1 
ATOM   3286 C CA  . MET B 1 127 ? 22.143  -12.657 13.172  1.00   42.46  ? 127  MET A CA  1 
ATOM   3287 C C   . MET B 1 127 ? 23.050  -12.681 11.947  1.00   42.37  ? 127  MET A C   1 
ATOM   3288 O O   . MET B 1 127 ? 22.898  -13.534 11.078  1.00   43.26  ? 127  MET A O   1 
ATOM   3289 C CB  . MET B 1 127 ? 22.493  -13.837 14.088  1.00   43.07  ? 127  MET A CB  1 
ATOM   3290 C CG  . MET B 1 127 ? 23.987  -13.927 14.414  1.00   46.95  ? 127  MET A CG  1 
ATOM   3291 S SD  . MET B 1 127 ? 24.405  -14.769 15.957  1.00   54.57  ? 127  MET A SD  1 
ATOM   3292 C CE  . MET B 1 127 ? 23.372  -13.878 17.121  1.00   52.12  ? 127  MET A CE  1 
ATOM   3293 N N   . ASP B 1 128 ? 24.009  -11.758 11.916  0.68   42.76  ? 128  ASP A N   1 
ATOM   3294 C CA  . ASP B 1 128 ? 24.993  -11.638 10.835  0.68   44.20  ? 128  ASP A CA  1 
ATOM   3295 C C   . ASP B 1 128 ? 24.412  -11.763 9.423   0.68   44.93  ? 128  ASP A C   1 
ATOM   3296 O O   . ASP B 1 128 ? 24.709  -12.720 8.704   0.68   44.79  ? 128  ASP A O   1 
ATOM   3297 C CB  . ASP B 1 128 ? 26.149  -12.627 11.032  0.68   44.54  ? 128  ASP A CB  1 
ATOM   3298 C CG  . ASP B 1 128 ? 27.040  -12.259 12.204  0.68   45.78  ? 128  ASP A CG  1 
ATOM   3299 O OD1 . ASP B 1 128 ? 27.493  -13.180 12.913  0.68   47.96  ? 128  ASP A OD1 1 
ATOM   3300 O OD2 . ASP B 1 128 ? 27.280  -11.054 12.423  0.68   46.10  ? 128  ASP A OD2 1 
ATOM   3301 N N   . LEU B 1 129 ? 23.576  -10.806 9.034   1.00   45.99  ? 129  LEU A N   1 
ATOM   3302 C CA  . LEU B 1 129 ? 23.038  -10.778 7.673   1.00   47.72  ? 129  LEU A CA  1 
ATOM   3303 C C   . LEU B 1 129 ? 24.161  -10.806 6.642   1.00   48.91  ? 129  LEU A C   1 
ATOM   3304 O O   . LEU B 1 129 ? 25.163  -10.101 6.810   1.00   48.99  ? 129  LEU A O   1 
ATOM   3305 C CB  . LEU B 1 129 ? 22.211  -9.514  7.468   1.00   47.59  ? 129  LEU A CB  1 
ATOM   3306 C CG  . LEU B 1 129 ? 20.864  -9.452  8.167   1.00   47.96  ? 129  LEU A CG  1 
ATOM   3307 C CD1 . LEU B 1 129 ? 20.227  -8.091  7.945   1.00   48.85  ? 129  LEU A CD1 1 
ATOM   3308 C CD2 . LEU B 1 129 ? 19.956  -10.568 7.675   1.00   46.85  ? 129  LEU A CD2 1 
ATOM   3309 N N   . HIS B 1 130 ? 23.997  -11.607 5.583   1.00   50.43  ? 130  HIS A N   1 
ATOM   3310 C CA  . HIS B 1 130 ? 25.030  -11.736 4.537   1.00   51.71  ? 130  HIS A CA  1 
ATOM   3311 C C   . HIS B 1 130 ? 25.501  -10.377 4.047   1.00   51.51  ? 130  HIS A C   1 
ATOM   3312 O O   . HIS B 1 130 ? 26.676  -10.194 3.741   1.00   51.79  ? 130  HIS A O   1 
ATOM   3313 C CB  . HIS B 1 130 ? 24.539  -12.562 3.345   1.00   52.50  ? 130  HIS A CB  1 
ATOM   3314 C CG  . HIS B 1 130 ? 25.570  -12.742 2.271   1.00   55.03  ? 130  HIS A CG  1 
ATOM   3315 N ND1 . HIS B 1 130 ? 26.643  -13.598 2.406   1.00   57.35  ? 130  HIS A ND1 1 
ATOM   3316 C CD2 . HIS B 1 130 ? 25.693  -12.178 1.045   1.00   57.04  ? 130  HIS A CD2 1 
ATOM   3317 C CE1 . HIS B 1 130 ? 27.381  -13.554 1.312   1.00   57.83  ? 130  HIS A CE1 1 
ATOM   3318 N NE2 . HIS B 1 130 ? 26.827  -12.700 0.470   1.00   58.23  ? 130  HIS A NE2 1 
ATOM   3319 N N   . ALA B 1 131 ? 24.566  -9.434  3.969   1.00   50.95  ? 131  ALA A N   1 
ATOM   3320 C CA  . ALA B 1 131 ? 24.880  -8.041  3.675   1.00   50.91  ? 131  ALA A CA  1 
ATOM   3321 C C   . ALA B 1 131 ? 23.992  -7.151  4.520   1.00   51.14  ? 131  ALA A C   1 
ATOM   3322 O O   . ALA B 1 131 ? 22.779  -7.361  4.589   1.00   50.74  ? 131  ALA A O   1 
ATOM   3323 C CB  . ALA B 1 131 ? 24.685  -7.742  2.199   1.00   50.70  ? 131  ALA A CB  1 
ATOM   3324 N N   . SER B 1 132 ? 24.597  -6.159  5.161   1.00   51.83  ? 132  SER A N   1 
ATOM   3325 C CA  . SER B 1 132 ? 23.876  -5.281  6.078   1.00   52.11  ? 132  SER A CA  1 
ATOM   3326 C C   . SER B 1 132 ? 22.754  -4.480  5.405   1.00   50.97  ? 132  SER A C   1 
ATOM   3327 O O   . SER B 1 132 ? 21.799  -4.068  6.069   1.00   51.24  ? 132  SER A O   1 
ATOM   3328 C CB  . SER B 1 132 ? 24.849  -4.339  6.780   1.00   52.59  ? 132  SER A CB  1 
ATOM   3329 O OG  . SER B 1 132 ? 24.143  -3.382  7.545   1.00   56.90  ? 132  SER A OG  1 
ATOM   3330 N N   . GLN B 1 133 ? 22.876  -4.265  4.096   0.75   48.65  ? 133  GLN A N   1 
ATOM   3331 C CA  . GLN B 1 133 ? 21.860  -3.543  3.330   0.75   46.85  ? 133  GLN A CA  1 
ATOM   3332 C C   . GLN B 1 133 ? 20.505  -4.255  3.371   0.75   45.97  ? 133  GLN A C   1 
ATOM   3333 O O   . GLN B 1 133 ? 19.464  -3.636  3.165   0.75   45.17  ? 133  GLN A O   1 
ATOM   3334 C CB  . GLN B 1 133 ? 22.312  -3.345  1.879   0.75   46.64  ? 133  GLN A CB  1 
ATOM   3335 C CG  . GLN B 1 133 ? 23.447  -2.340  1.703   0.75   46.59  ? 133  GLN A CG  1 
ATOM   3336 C CD  . GLN B 1 133 ? 24.829  -2.944  1.905   0.75   47.86  ? 133  GLN A CD  1 
ATOM   3337 O OE1 . GLN B 1 133 ? 24.976  -4.137  2.191   0.75   48.18  ? 133  GLN A OE1 1 
ATOM   3338 N NE2 . GLN B 1 133 ? 25.854  -2.116  1.751   0.75   49.06  ? 133  GLN A NE2 1 
ATOM   3339 N N   . ILE B 1 134 ? 20.526  -5.557  3.646   1.00   45.32  ? 134  ILE A N   1 
ATOM   3340 C CA  . ILE B 1 134 ? 19.301  -6.335  3.808   1.00   45.29  ? 134  ILE A CA  1 
ATOM   3341 C C   . ILE B 1 134 ? 18.309  -5.716  4.819   1.00   44.75  ? 134  ILE A C   1 
ATOM   3342 O O   . ILE B 1 134 ? 17.096  -5.817  4.628   1.00   45.30  ? 134  ILE A O   1 
ATOM   3343 C CB  . ILE B 1 134 ? 19.611  -7.844  4.095   1.00   45.44  ? 134  ILE A CB  1 
ATOM   3344 C CG1 . ILE B 1 134 ? 20.319  -8.467  2.878   1.00   45.65  ? 134  ILE A CG1 1 
ATOM   3345 C CG2 . ILE B 1 134 ? 18.343  -8.623  4.426   1.00   44.70  ? 134  ILE A CG2 1 
ATOM   3346 C CD1 . ILE B 1 134 ? 20.688  -9.936  3.012   1.00   44.82  ? 134  ILE A CD1 1 
ATOM   3347 N N   . GLN B 1 135 ? 18.809  -5.062  5.869   1.00   43.02  ? 135  GLN A N   1 
ATOM   3348 C CA  . GLN B 1 135 ? 17.939  -4.264  6.753   1.00   41.57  ? 135  GLN A CA  1 
ATOM   3349 C C   . GLN B 1 135 ? 17.144  -3.229  5.945   1.00   40.43  ? 135  GLN A C   1 
ATOM   3350 O O   . GLN B 1 135 ? 15.991  -2.912  6.266   1.00   39.58  ? 135  GLN A O   1 
ATOM   3351 C CB  . GLN B 1 135 ? 18.752  -3.571  7.858   1.00   42.21  ? 135  GLN A CB  1 
ATOM   3352 C CG  . GLN B 1 135 ? 19.523  -4.551  8.768   1.00   45.32  ? 135  GLN A CG  1 
ATOM   3353 C CD  . GLN B 1 135 ? 20.188  -3.890  9.982   1.00   50.59  ? 135  GLN A CD  1 
ATOM   3354 O OE1 . GLN B 1 135 ? 19.598  -3.052  10.661  1.00   52.57  ? 135  GLN A OE1 1 
ATOM   3355 N NE2 . GLN B 1 135 ? 21.423  -4.283  10.258  1.00   53.12  ? 135  GLN A NE2 1 
ATOM   3356 N N   . GLY B 1 136 ? 17.762  -2.713  4.885   1.00   38.47  ? 136  GLY A N   1 
ATOM   3357 C CA  . GLY B 1 136 ? 17.072  -1.813  3.964   1.00   37.73  ? 136  GLY A CA  1 
ATOM   3358 C C   . GLY B 1 136 ? 15.925  -2.440  3.182   1.00   36.40  ? 136  GLY A C   1 
ATOM   3359 O O   . GLY B 1 136 ? 15.129  -1.719  2.595   1.00   36.37  ? 136  GLY A O   1 
ATOM   3360 N N   . PHE B 1 137 ? 15.837  -3.771  3.175   1.00   34.64  ? 137  PHE A N   1 
ATOM   3361 C CA  . PHE B 1 137 ? 14.763  -4.475  2.461   1.00   34.59  ? 137  PHE A CA  1 
ATOM   3362 C C   . PHE B 1 137 ? 13.415  -4.431  3.168   1.00   34.11  ? 137  PHE A C   1 
ATOM   3363 O O   . PHE B 1 137 ? 12.389  -4.770  2.572   1.00   34.02  ? 137  PHE A O   1 
ATOM   3364 C CB  . PHE B 1 137 ? 15.147  -5.930  2.179   1.00   34.46  ? 137  PHE A CB  1 
ATOM   3365 C CG  . PHE B 1 137 ? 16.288  -6.080  1.203   1.00   37.10  ? 137  PHE A CG  1 
ATOM   3366 C CD1 . PHE B 1 137 ? 16.850  -7.319  0.958   1.00   38.81  ? 137  PHE A CD1 1 
ATOM   3367 C CD2 . PHE B 1 137 ? 16.814  -4.974  0.547   1.00   38.06  ? 137  PHE A CD2 1 
ATOM   3368 C CE1 . PHE B 1 137 ? 17.899  -7.456  0.072   1.00   40.36  ? 137  PHE A CE1 1 
ATOM   3369 C CE2 . PHE B 1 137 ? 17.877  -5.104  -0.331  1.00   38.82  ? 137  PHE A CE2 1 
ATOM   3370 C CZ  . PHE B 1 137 ? 18.412  -6.346  -0.575  1.00   40.72  ? 137  PHE A CZ  1 
ATOM   3371 N N   . PHE B 1 138 ? 13.422  -4.011  4.429   1.00   32.96  ? 138  PHE A N   1 
ATOM   3372 C CA  . PHE B 1 138 ? 12.214  -3.964  5.247   1.00   33.51  ? 138  PHE A CA  1 
ATOM   3373 C C   . PHE B 1 138 ? 11.851  -2.521  5.481   1.00   34.23  ? 138  PHE A C   1 
ATOM   3374 O O   . PHE B 1 138 ? 12.715  -1.650  5.359   1.00   35.36  ? 138  PHE A O   1 
ATOM   3375 C CB  . PHE B 1 138 ? 12.485  -4.607  6.607   1.00   32.27  ? 138  PHE A CB  1 
ATOM   3376 C CG  . PHE B 1 138 ? 12.687  -6.084  6.550   1.00   30.83  ? 138  PHE A CG  1 
ATOM   3377 C CD1 . PHE B 1 138 ? 13.953  -6.617  6.361   1.00   30.37  ? 138  PHE A CD1 1 
ATOM   3378 C CD2 . PHE B 1 138 ? 11.608  -6.944  6.673   1.00   30.43  ? 138  PHE A CD2 1 
ATOM   3379 C CE1 . PHE B 1 138 ? 14.142  -7.981  6.318   1.00   30.10  ? 138  PHE A CE1 1 
ATOM   3380 C CE2 . PHE B 1 138 ? 11.789  -8.320  6.631   1.00   28.49  ? 138  PHE A CE2 1 
ATOM   3381 C CZ  . PHE B 1 138 ? 13.063  -8.837  6.459   1.00   27.91  ? 138  PHE A CZ  1 
ATOM   3382 N N   . ASP B 1 139 ? 10.583  -2.267  5.803   1.00   34.86  ? 139  ASP A N   1 
ATOM   3383 C CA  . ASP B 1 139 ? 10.154  -0.966  6.336   1.00   35.73  ? 139  ASP A CA  1 
ATOM   3384 C C   . ASP B 1 139 ? 9.829   -1.108  7.827   1.00   35.08  ? 139  ASP A C   1 
ATOM   3385 O O   . ASP B 1 139 ? 9.500   -0.140  8.504   1.00   36.68  ? 139  ASP A O   1 
ATOM   3386 C CB  . ASP B 1 139 ? 8.930   -0.434  5.586   1.00   36.31  ? 139  ASP A CB  1 
ATOM   3387 C CG  . ASP B 1 139 ? 9.245   -0.042  4.135   1.00   39.94  ? 139  ASP A CG  1 
ATOM   3388 O OD1 . ASP B 1 139 ? 10.244  0.670   3.880   1.00   42.27  ? 139  ASP A OD1 1 
ATOM   3389 O OD2 . ASP B 1 139 ? 8.472   -0.433  3.243   1.00   43.26  ? 139  ASP A OD2 1 
ATOM   3390 N N   . ILE B 1 140 ? 9.916   -2.332  8.323   1.00   32.84  ? 140  ILE A N   1 
ATOM   3391 C CA  . ILE B 1 140 ? 9.732   -2.603  9.736   1.00   31.46  ? 140  ILE A CA  1 
ATOM   3392 C C   . ILE B 1 140 ? 11.115  -2.662  10.355  1.00   31.89  ? 140  ILE A C   1 
ATOM   3393 O O   . ILE B 1 140 ? 12.102  -2.879  9.632   1.00   31.12  ? 140  ILE A O   1 
ATOM   3394 C CB  . ILE B 1 140 ? 8.964   -3.921  9.960   1.00   30.38  ? 140  ILE A CB  1 
ATOM   3395 C CG1 . ILE B 1 140 ? 9.735   -5.106  9.378   1.00   30.34  ? 140  ILE A CG1 1 
ATOM   3396 C CG2 . ILE B 1 140 ? 7.524   -3.823  9.391   1.00   29.92  ? 140  ILE A CG2 1 
ATOM   3397 C CD1 . ILE B 1 140 ? 9.113   -6.444  9.692   1.00   29.84  ? 140  ILE A CD1 1 
ATOM   3398 N N   . PRO B 1 141 ? 11.211  -2.462  11.686  1.00   32.29  ? 141  PRO A N   1 
ATOM   3399 C CA  . PRO B 1 141 ? 12.518  -2.495  12.354  1.00   31.99  ? 141  PRO A CA  1 
ATOM   3400 C C   . PRO B 1 141 ? 13.172  -3.880  12.313  1.00   31.50  ? 141  PRO A C   1 
ATOM   3401 O O   . PRO B 1 141 ? 12.504  -4.900  12.498  1.00   30.48  ? 141  PRO A O   1 
ATOM   3402 C CB  . PRO B 1 141 ? 12.191  -2.122  13.810  1.00   32.59  ? 141  PRO A CB  1 
ATOM   3403 C CG  . PRO B 1 141 ? 10.849  -1.509  13.788  1.00   33.18  ? 141  PRO A CG  1 
ATOM   3404 C CD  . PRO B 1 141 ? 10.125  -2.030  12.587  1.00   32.41  ? 141  PRO A CD  1 
ATOM   3405 N N   . VAL B 1 142 ? 14.477  -3.898  12.081  1.00   31.39  ? 142  VAL A N   1 
ATOM   3406 C CA  . VAL B 1 142 ? 15.259  -5.122  12.112  1.00   32.52  ? 142  VAL A CA  1 
ATOM   3407 C C   . VAL B 1 142 ? 16.400  -4.930  13.116  1.00   34.67  ? 142  VAL A C   1 
ATOM   3408 O O   . VAL B 1 142 ? 17.156  -3.964  13.021  1.00   35.47  ? 142  VAL A O   1 
ATOM   3409 C CB  . VAL B 1 142 ? 15.868  -5.439  10.727  1.00   32.41  ? 142  VAL A CB  1 
ATOM   3410 C CG1 . VAL B 1 142 ? 16.584  -6.798  10.745  1.00   31.60  ? 142  VAL A CG1 1 
ATOM   3411 C CG2 . VAL B 1 142 ? 14.798  -5.416  9.638   1.00   30.97  ? 142  VAL A CG2 1 
ATOM   3412 N N   . ASP B 1 143 ? 16.509  -5.839  14.080  0.94   36.22  ? 143  ASP A N   1 
ATOM   3413 C CA  . ASP B 1 143 ? 17.697  -5.904  14.943  0.94   37.68  ? 143  ASP A CA  1 
ATOM   3414 C C   . ASP B 1 143 ? 18.633  -6.991  14.436  0.94   38.00  ? 143  ASP A C   1 
ATOM   3415 O O   . ASP B 1 143 ? 18.315  -8.178  14.501  0.94   38.11  ? 143  ASP A O   1 
ATOM   3416 C CB  . ASP B 1 143 ? 17.299  -6.164  16.400  0.94   38.46  ? 143  ASP A CB  1 
ATOM   3417 C CG  . ASP B 1 143 ? 16.410  -5.073  16.958  0.94   41.21  ? 143  ASP A CG  1 
ATOM   3418 O OD1 . ASP B 1 143 ? 16.650  -3.885  16.657  0.94   44.03  ? 143  ASP A OD1 1 
ATOM   3419 O OD2 . ASP B 1 143 ? 15.459  -5.399  17.692  0.94   45.83  ? 143  ASP A OD2 1 
ATOM   3420 N N   . ASN B 1 144 ? 19.776  -6.569  13.909  1.00   39.04  ? 144  ASN A N   1 
ATOM   3421 C CA  . ASN B 1 144 ? 20.766  -7.461  13.310  1.00   41.41  ? 144  ASN A CA  1 
ATOM   3422 C C   . ASN B 1 144 ? 21.919  -7.702  14.289  1.00   43.54  ? 144  ASN A C   1 
ATOM   3423 O O   . ASN B 1 144 ? 22.844  -6.895  14.391  1.00   44.32  ? 144  ASN A O   1 
ATOM   3424 C CB  . ASN B 1 144 ? 21.273  -6.862  11.988  1.00   40.92  ? 144  ASN A CB  1 
ATOM   3425 C CG  . ASN B 1 144 ? 22.284  -7.759  11.257  1.00   42.33  ? 144  ASN A CG  1 
ATOM   3426 O OD1 . ASN B 1 144 ? 22.291  -8.988  11.396  1.00   42.23  ? 144  ASN A OD1 1 
ATOM   3427 N ND2 . ASN B 1 144 ? 23.135  -7.130  10.456  1.00   43.91  ? 144  ASN A ND2 1 
ATOM   3428 N N   . LEU B 1 145 ? 21.842  -8.807  15.022  1.00   45.38  ? 145  LEU A N   1 
ATOM   3429 C CA  . LEU B 1 145 ? 22.854  -9.156  16.020  1.00   47.14  ? 145  LEU A CA  1 
ATOM   3430 C C   . LEU B 1 145 ? 24.159  -9.599  15.360  1.00   48.98  ? 145  LEU A C   1 
ATOM   3431 O O   . LEU B 1 145 ? 24.157  -10.022 14.204  1.00   49.32  ? 145  LEU A O   1 
ATOM   3432 C CB  . LEU B 1 145 ? 22.318  -10.253 16.937  1.00   46.06  ? 145  LEU A CB  1 
ATOM   3433 C CG  . LEU B 1 145 ? 20.922  -9.934  17.484  1.00   45.51  ? 145  LEU A CG  1 
ATOM   3434 C CD1 . LEU B 1 145 ? 20.268  -11.164 18.036  1.00   43.66  ? 145  LEU A CD1 1 
ATOM   3435 C CD2 . LEU B 1 145 ? 20.972  -8.830  18.536  1.00   45.51  ? 145  LEU A CD2 1 
ATOM   3436 N N   . TYR B 1 146 ? 25.266  -9.495  16.089  1.00   51.22  ? 146  TYR A N   1 
ATOM   3437 C CA  . TYR B 1 146 ? 26.573  -9.872  15.553  1.00   53.25  ? 146  TYR A CA  1 
ATOM   3438 C C   . TYR B 1 146 ? 27.188  -10.990 16.379  1.00   53.50  ? 146  TYR A C   1 
ATOM   3439 O O   . TYR B 1 146 ? 27.113  -10.975 17.606  1.00   53.61  ? 146  TYR A O   1 
ATOM   3440 C CB  . TYR B 1 146 ? 27.497  -8.650  15.495  1.00   54.23  ? 146  TYR A CB  1 
ATOM   3441 C CG  . TYR B 1 146 ? 26.828  -7.458  14.850  1.00   57.64  ? 146  TYR A CG  1 
ATOM   3442 C CD1 . TYR B 1 146 ? 26.143  -6.519  15.619  1.00   60.35  ? 146  TYR A CD1 1 
ATOM   3443 C CD2 . TYR B 1 146 ? 26.845  -7.289  13.462  1.00   60.71  ? 146  TYR A CD2 1 
ATOM   3444 C CE1 . TYR B 1 146 ? 25.507  -5.435  15.027  1.00   62.32  ? 146  TYR A CE1 1 
ATOM   3445 C CE2 . TYR B 1 146 ? 26.209  -6.200  12.858  1.00   61.86  ? 146  TYR A CE2 1 
ATOM   3446 C CZ  . TYR B 1 146 ? 25.541  -5.282  13.649  1.00   63.17  ? 146  TYR A CZ  1 
ATOM   3447 O OH  . TYR B 1 146 ? 24.906  -4.202  13.074  1.00   64.51  ? 146  TYR A OH  1 
ATOM   3448 N N   . ALA B 1 147 ? 27.770  -11.976 15.703  1.00   53.75  ? 147  ALA A N   1 
ATOM   3449 C CA  . ALA B 1 147 ? 28.480  -13.038 16.399  1.00   53.86  ? 147  ALA A CA  1 
ATOM   3450 C C   . ALA B 1 147 ? 29.927  -12.632 16.670  1.00   53.72  ? 147  ALA A C   1 
ATOM   3451 O O   . ALA B 1 147 ? 30.611  -13.278 17.458  1.00   53.76  ? 147  ALA A O   1 
ATOM   3452 C CB  . ALA B 1 147 ? 28.416  -14.345 15.617  1.00   53.94  ? 147  ALA A CB  1 
ATOM   3453 N N   . GLU B 1 148 ? 30.366  -11.548 16.025  1.00   53.62  ? 148  GLU A N   1 
ATOM   3454 C CA  . GLU B 1 148 ? 31.727  -11.025 16.151  1.00   54.38  ? 148  GLU A CA  1 
ATOM   3455 C C   . GLU B 1 148 ? 32.299  -11.111 17.574  1.00   54.89  ? 148  GLU A C   1 
ATOM   3456 O O   . GLU B 1 148 ? 33.367  -11.699 17.755  1.00   54.80  ? 148  GLU A O   1 
ATOM   3457 C CB  . GLU B 1 148 ? 31.842  -9.594  15.604  1.00   54.64  ? 148  GLU A CB  1 
ATOM   3458 C CG  . GLU B 1 148 ? 33.246  -8.988  15.769  1.00   57.39  ? 148  GLU A CG  1 
ATOM   3459 C CD  . GLU B 1 148 ? 33.450  -7.680  15.012  1.00   60.73  ? 148  GLU A CD  1 
ATOM   3460 O OE1 . GLU B 1 148 ? 32.883  -7.511  13.909  1.00   62.33  ? 148  GLU A OE1 1 
ATOM   3461 O OE2 . GLU B 1 148 ? 34.202  -6.820  15.515  1.00   62.69  ? 148  GLU A OE2 1 
ATOM   3462 N N   . PRO B 1 149 ? 31.594  -10.546 18.582  1.00   55.53  ? 149  PRO A N   1 
ATOM   3463 C CA  . PRO B 1 149 ? 32.179  -10.603 19.924  1.00   56.57  ? 149  PRO A CA  1 
ATOM   3464 C C   . PRO B 1 149 ? 32.385  -12.031 20.421  1.00   57.47  ? 149  PRO A C   1 
ATOM   3465 O O   . PRO B 1 149 ? 33.412  -12.317 21.035  1.00   57.94  ? 149  PRO A O   1 
ATOM   3466 C CB  . PRO B 1 149 ? 31.158  -9.856  20.791  1.00   56.23  ? 149  PRO A CB  1 
ATOM   3467 C CG  . PRO B 1 149 ? 30.411  -8.987  19.827  1.00   56.27  ? 149  PRO A CG  1 
ATOM   3468 C CD  . PRO B 1 149 ? 30.313  -9.815  18.587  1.00   55.61  ? 149  PRO A CD  1 
ATOM   3469 N N   . ALA B 1 150 ? 31.439  -12.921 20.130  1.00   58.48  ? 150  ALA A N   1 
ATOM   3470 C CA  . ALA B 1 150 ? 31.549  -14.325 20.527  1.00   59.29  ? 150  ALA A CA  1 
ATOM   3471 C C   . ALA B 1 150 ? 32.718  -15.033 19.833  1.00   59.84  ? 150  ALA A C   1 
ATOM   3472 O O   . ALA B 1 150 ? 33.311  -15.963 20.387  1.00   59.97  ? 150  ALA A O   1 
ATOM   3473 C CB  . ALA B 1 150 ? 30.248  -15.054 20.245  1.00   59.34  ? 150  ALA A CB  1 
ATOM   3474 N N   . VAL B 1 151 ? 33.036  -14.587 18.619  1.00   60.14  ? 151  VAL A N   1 
ATOM   3475 C CA  . VAL B 1 151 ? 34.099  -15.185 17.811  1.00   60.15  ? 151  VAL A CA  1 
ATOM   3476 C C   . VAL B 1 151 ? 35.480  -14.731 18.295  1.00   60.17  ? 151  VAL A C   1 
ATOM   3477 O O   . VAL B 1 151 ? 36.422  -15.530 18.360  1.00   60.32  ? 151  VAL A O   1 
ATOM   3478 C CB  . VAL B 1 151 ? 33.929  -14.827 16.311  1.00   60.14  ? 151  VAL A CB  1 
ATOM   3479 C CG1 . VAL B 1 151 ? 35.123  -15.304 15.490  1.00   60.17  ? 151  VAL A CG1 1 
ATOM   3480 C CG2 . VAL B 1 151 ? 32.628  -15.414 15.759  1.00   59.73  ? 151  VAL A CG2 1 
ATOM   3481 N N   . LEU B 1 152 ? 35.588  -13.443 18.612  1.00   59.77  ? 152  LEU A N   1 
ATOM   3482 C CA  . LEU B 1 152 ? 36.826  -12.862 19.123  1.00   59.65  ? 152  LEU A CA  1 
ATOM   3483 C C   . LEU B 1 152 ? 37.214  -13.572 20.404  1.00   59.39  ? 152  LEU A C   1 
ATOM   3484 O O   . LEU B 1 152 ? 38.358  -14.014 20.562  1.00   59.48  ? 152  LEU A O   1 
ATOM   3485 C CB  . LEU B 1 152 ? 36.643  -11.367 19.386  1.00   59.46  ? 152  LEU A CB  1 
ATOM   3486 C CG  . LEU B 1 152 ? 37.139  -10.348 18.353  1.00   60.09  ? 152  LEU A CG  1 
ATOM   3487 C CD1 . LEU B 1 152 ? 36.941  -10.811 16.911  1.00   60.36  ? 152  LEU A CD1 1 
ATOM   3488 C CD2 . LEU B 1 152 ? 36.453  -9.007  18.581  1.00   60.01  ? 152  LEU A CD2 1 
ATOM   3489 N N   . LYS B 1 153 ? 36.235  -13.690 21.300  0.69   58.91  ? 153  LYS A N   1 
ATOM   3490 C CA  . LYS B 1 153 ? 36.398  -14.393 22.565  0.69   59.06  ? 153  LYS A CA  1 
ATOM   3491 C C   . LYS B 1 153 ? 36.960  -15.785 22.335  0.69   59.87  ? 153  LYS A C   1 
ATOM   3492 O O   . LYS B 1 153 ? 37.934  -16.171 22.978  0.69   59.69  ? 153  LYS A O   1 
ATOM   3493 C CB  . LYS B 1 153 ? 35.064  -14.473 23.313  0.69   58.72  ? 153  LYS A CB  1 
ATOM   3494 C CG  . LYS B 1 153 ? 35.156  -15.125 24.686  0.69   58.46  ? 153  LYS A CG  1 
ATOM   3495 C CD  . LYS B 1 153 ? 34.023  -14.666 25.590  0.69   59.01  ? 153  LYS A CD  1 
ATOM   3496 C CE  . LYS B 1 153 ? 34.277  -15.034 27.050  0.69   59.23  ? 153  LYS A CE  1 
ATOM   3497 N NZ  . LYS B 1 153 ? 34.313  -16.510 27.282  0.69   60.04  ? 153  LYS A NZ  1 
ATOM   3498 N N   . TRP B 1 154 ? 36.356  -16.521 21.404  1.00   61.70  ? 154  TRP A N   1 
ATOM   3499 C CA  . TRP B 1 154 ? 36.775  -17.888 21.113  1.00   63.94  ? 154  TRP A CA  1 
ATOM   3500 C C   . TRP B 1 154 ? 38.207  -17.953 20.576  1.00   65.06  ? 154  TRP A C   1 
ATOM   3501 O O   . TRP B 1 154 ? 38.991  -18.798 21.010  1.00   65.16  ? 154  TRP A O   1 
ATOM   3502 C CB  . TRP B 1 154 ? 35.808  -18.566 20.135  1.00   64.05  ? 154  TRP A CB  1 
ATOM   3503 C CG  . TRP B 1 154 ? 36.092  -20.026 19.964  1.00   65.40  ? 154  TRP A CG  1 
ATOM   3504 C CD1 . TRP B 1 154 ? 35.454  -21.061 20.581  1.00   66.21  ? 154  TRP A CD1 1 
ATOM   3505 C CD2 . TRP B 1 154 ? 37.106  -20.615 19.136  1.00   66.48  ? 154  TRP A CD2 1 
ATOM   3506 N NE1 . TRP B 1 154 ? 35.999  -22.259 20.184  1.00   67.06  ? 154  TRP A NE1 1 
ATOM   3507 C CE2 . TRP B 1 154 ? 37.015  -22.014 19.298  1.00   67.00  ? 154  TRP A CE2 1 
ATOM   3508 C CE3 . TRP B 1 154 ? 38.079  -20.096 18.269  1.00   66.80  ? 154  TRP A CE3 1 
ATOM   3509 C CZ2 . TRP B 1 154 ? 37.865  -22.905 18.629  1.00   67.22  ? 154  TRP A CZ2 1 
ATOM   3510 C CZ3 . TRP B 1 154 ? 38.922  -20.980 17.604  1.00   66.92  ? 154  TRP A CZ3 1 
ATOM   3511 C CH2 . TRP B 1 154 ? 38.808  -22.369 17.788  1.00   66.97  ? 154  TRP A CH2 1 
ATOM   3512 N N   . ILE B 1 155 ? 38.533  -17.075 19.627  1.00   66.54  ? 155  ILE A N   1 
ATOM   3513 C CA  . ILE B 1 155 ? 39.883  -17.020 19.053  1.00   67.92  ? 155  ILE A CA  1 
ATOM   3514 C C   . ILE B 1 155 ? 40.934  -16.790 20.141  1.00   69.44  ? 155  ILE A C   1 
ATOM   3515 O O   . ILE B 1 155 ? 41.886  -17.562 20.266  1.00   69.32  ? 155  ILE A O   1 
ATOM   3516 C CB  . ILE B 1 155 ? 40.016  -15.932 17.956  1.00   67.67  ? 155  ILE A CB  1 
ATOM   3517 C CG1 . ILE B 1 155 ? 39.176  -16.296 16.728  1.00   67.00  ? 155  ILE A CG1 1 
ATOM   3518 C CG2 . ILE B 1 155 ? 41.488  -15.732 17.561  1.00   67.23  ? 155  ILE A CG2 1 
ATOM   3519 C CD1 . ILE B 1 155 ? 39.205  -15.249 15.616  1.00   65.84  ? 155  ILE A CD1 1 
ATOM   3520 N N   . ARG B 1 156 ? 40.748  -15.733 20.927  1.00   71.53  ? 156  ARG A N   1 
ATOM   3521 C CA  . ARG B 1 156 ? 41.674  -15.407 22.003  1.00   73.69  ? 156  ARG A CA  1 
ATOM   3522 C C   . ARG B 1 156 ? 41.847  -16.582 22.965  1.00   74.49  ? 156  ARG A C   1 
ATOM   3523 O O   . ARG B 1 156 ? 42.955  -16.855 23.430  1.00   74.76  ? 156  ARG A O   1 
ATOM   3524 C CB  . ARG B 1 156 ? 41.187  -14.183 22.780  1.00   73.96  ? 156  ARG A CB  1 
ATOM   3525 C CG  . ARG B 1 156 ? 41.228  -12.873 22.019  1.00   75.46  ? 156  ARG A CG  1 
ATOM   3526 C CD  . ARG B 1 156 ? 40.690  -11.760 22.900  1.00   78.16  ? 156  ARG A CD  1 
ATOM   3527 N NE  . ARG B 1 156 ? 40.843  -10.438 22.296  1.00   80.36  ? 156  ARG A NE  1 
ATOM   3528 C CZ  . ARG B 1 156 ? 39.837  -9.678  21.866  1.00   81.37  ? 156  ARG A CZ  1 
ATOM   3529 N NH1 . ARG B 1 156 ? 38.581  -10.097 21.972  1.00   81.45  ? 156  ARG A NH1 1 
ATOM   3530 N NH2 . ARG B 1 156 ? 40.088  -8.489  21.334  1.00   81.95  ? 156  ARG A NH2 1 
ATOM   3531 N N   . GLU B 1 157 ? 40.747  -17.280 23.242  1.00   75.25  ? 157  GLU A N   1 
ATOM   3532 C CA  . GLU B 1 157 ? 40.724  -18.321 24.267  1.00   75.92  ? 157  GLU A CA  1 
ATOM   3533 C C   . GLU B 1 157 ? 41.063  -19.725 23.763  1.00   76.13  ? 157  GLU A C   1 
ATOM   3534 O O   . GLU B 1 157 ? 41.097  -20.670 24.553  1.00   76.24  ? 157  GLU A O   1 
ATOM   3535 C CB  . GLU B 1 157 ? 39.371  -18.324 24.995  1.00   75.93  ? 157  GLU A CB  1 
ATOM   3536 C CG  . GLU B 1 157 ? 39.118  -17.072 25.849  1.00   76.83  ? 157  GLU A CG  1 
ATOM   3537 C CD  . GLU B 1 157 ? 37.729  -17.041 26.488  1.00   77.78  ? 157  GLU A CD  1 
ATOM   3538 O OE1 . GLU B 1 157 ? 37.431  -16.060 27.207  1.00   77.52  ? 157  GLU A OE1 1 
ATOM   3539 O OE2 . GLU B 1 157 ? 36.936  -17.987 26.276  1.00   77.90  ? 157  GLU A OE2 1 
ATOM   3540 N N   . ASN B 1 158 ? 41.317  -19.872 22.465  1.00   76.54  ? 158  ASN A N   1 
ATOM   3541 C CA  . ASN B 1 158 ? 41.582  -21.203 21.905  1.00   77.03  ? 158  ASN A CA  1 
ATOM   3542 C C   . ASN B 1 158 ? 42.765  -21.282 20.949  1.00   77.21  ? 158  ASN A C   1 
ATOM   3543 O O   . ASN B 1 158 ? 43.184  -22.376 20.563  1.00   77.27  ? 158  ASN A O   1 
ATOM   3544 C CB  . ASN B 1 158 ? 40.325  -21.777 21.242  1.00   77.18  ? 158  ASN A CB  1 
ATOM   3545 C CG  . ASN B 1 158 ? 39.244  -22.126 22.246  1.00   77.50  ? 158  ASN A CG  1 
ATOM   3546 O OD1 . ASN B 1 158 ? 38.576  -21.248 22.791  1.00   78.04  ? 158  ASN A OD1 1 
ATOM   3547 N ND2 . ASN B 1 158 ? 39.058  -23.418 22.487  1.00   77.94  ? 158  ASN A ND2 1 
ATOM   3548 N N   . ILE B 1 159 ? 43.292  -20.124 20.566  1.00   77.39  ? 159  ILE A N   1 
ATOM   3549 C CA  . ILE B 1 159 ? 44.469  -20.065 19.712  1.00   77.67  ? 159  ILE A CA  1 
ATOM   3550 C C   . ILE B 1 159 ? 45.602  -19.396 20.481  1.00   77.76  ? 159  ILE A C   1 
ATOM   3551 O O   . ILE B 1 159 ? 45.549  -18.198 20.759  1.00   77.65  ? 159  ILE A O   1 
ATOM   3552 C CB  . ILE B 1 159 ? 44.179  -19.315 18.388  1.00   77.76  ? 159  ILE A CB  1 
ATOM   3553 C CG1 . ILE B 1 159 ? 42.961  -19.945 17.691  1.00   78.03  ? 159  ILE A CG1 1 
ATOM   3554 C CG2 . ILE B 1 159 ? 45.428  -19.294 17.501  1.00   77.54  ? 159  ILE A CG2 1 
ATOM   3555 C CD1 . ILE B 1 159 ? 42.767  -19.558 16.235  1.00   78.52  ? 159  ILE A CD1 1 
ATOM   3556 N N   . SER B 1 160 ? 46.617  -20.181 20.834  1.00   77.78  ? 160  SER A N   1 
ATOM   3557 C CA  . SER B 1 160 ? 47.740  -19.670 21.622  1.00   77.88  ? 160  SER A CA  1 
ATOM   3558 C C   . SER B 1 160 ? 48.521  -18.580 20.881  1.00   78.01  ? 160  SER A C   1 
ATOM   3559 O O   . SER B 1 160 ? 48.986  -17.613 21.493  1.00   77.63  ? 160  SER A O   1 
ATOM   3560 C CB  . SER B 1 160 ? 48.667  -20.811 22.056  1.00   77.80  ? 160  SER A CB  1 
ATOM   3561 O OG  . SER B 1 160 ? 49.135  -21.562 20.946  1.00   78.01  ? 160  SER A OG  1 
ATOM   3562 N N   . GLU B 1 161 ? 48.627  -18.730 19.563  1.00   78.34  ? 161  GLU A N   1 
ATOM   3563 C CA  . GLU B 1 161 ? 49.403  -17.816 18.726  1.00   78.48  ? 161  GLU A CA  1 
ATOM   3564 C C   . GLU B 1 161 ? 48.551  -16.684 18.162  1.00   77.39  ? 161  GLU A C   1 
ATOM   3565 O O   . GLU B 1 161 ? 49.005  -15.940 17.287  1.00   77.64  ? 161  GLU A O   1 
ATOM   3566 C CB  . GLU B 1 161 ? 50.063  -18.576 17.567  1.00   79.03  ? 161  GLU A CB  1 
ATOM   3567 C CG  . GLU B 1 161 ? 50.676  -19.922 17.939  1.00   80.58  ? 161  GLU A CG  1 
ATOM   3568 C CD  . GLU B 1 161 ? 49.671  -21.066 17.904  1.00   82.30  ? 161  GLU A CD  1 
ATOM   3569 O OE1 . GLU B 1 161 ? 48.479  -20.842 18.216  1.00   82.84  ? 161  GLU A OE1 1 
ATOM   3570 O OE2 . GLU B 1 161 ? 50.074  -22.200 17.564  1.00   82.72  ? 161  GLU A OE2 1 
ATOM   3571 N N   . TRP B 1 162 ? 47.326  -16.545 18.666  1.00   75.38  ? 162  TRP A N   1 
ATOM   3572 C CA  . TRP B 1 162 ? 46.376  -15.578 18.115  1.00   73.21  ? 162  TRP A CA  1 
ATOM   3573 C C   . TRP B 1 162 ? 46.929  -14.154 18.032  1.00   72.37  ? 162  TRP A C   1 
ATOM   3574 O O   . TRP B 1 162 ? 46.490  -13.363 17.193  1.00   72.12  ? 162  TRP A O   1 
ATOM   3575 C CB  . TRP B 1 162 ? 45.060  -15.596 18.894  1.00   72.75  ? 162  TRP A CB  1 
ATOM   3576 C CG  . TRP B 1 162 ? 45.123  -14.933 20.234  1.00   71.39  ? 162  TRP A CG  1 
ATOM   3577 C CD1 . TRP B 1 162 ? 45.326  -15.537 21.440  1.00   70.41  ? 162  TRP A CD1 1 
ATOM   3578 C CD2 . TRP B 1 162 ? 44.963  -13.536 20.507  1.00   70.43  ? 162  TRP A CD2 1 
ATOM   3579 N NE1 . TRP B 1 162 ? 45.306  -14.605 22.448  1.00   70.05  ? 162  TRP A NE1 1 
ATOM   3580 C CE2 . TRP B 1 162 ? 45.085  -13.368 21.904  1.00   70.46  ? 162  TRP A CE2 1 
ATOM   3581 C CE3 . TRP B 1 162 ? 44.726  -12.409 19.708  1.00   70.45  ? 162  TRP A CE3 1 
ATOM   3582 C CZ2 . TRP B 1 162 ? 44.984  -12.116 22.520  1.00   71.00  ? 162  TRP A CZ2 1 
ATOM   3583 C CZ3 . TRP B 1 162 ? 44.628  -11.163 20.319  1.00   70.58  ? 162  TRP A CZ3 1 
ATOM   3584 C CH2 . TRP B 1 162 ? 44.756  -11.028 21.713  1.00   71.15  ? 162  TRP A CH2 1 
ATOM   3585 N N   . ARG B 1 163 ? 47.887  -13.832 18.902  1.00   71.37  ? 163  ARG A N   1 
ATOM   3586 C CA  . ARG B 1 163 ? 48.471  -12.492 18.944  1.00   70.75  ? 163  ARG A CA  1 
ATOM   3587 C C   . ARG B 1 163 ? 49.305  -12.172 17.700  1.00   70.53  ? 163  ARG A C   1 
ATOM   3588 O O   . ARG B 1 163 ? 49.536  -11.002 17.389  1.00   70.30  ? 163  ARG A O   1 
ATOM   3589 C CB  . ARG B 1 163 ? 49.283  -12.277 20.229  1.00   70.73  ? 163  ARG A CB  1 
ATOM   3590 C CG  . ARG B 1 163 ? 48.430  -12.233 21.495  1.00   70.73  ? 163  ARG A CG  1 
ATOM   3591 C CD  . ARG B 1 163 ? 49.228  -11.775 22.706  1.00   71.12  ? 163  ARG A CD  1 
ATOM   3592 N NE  . ARG B 1 163 ? 48.411  -11.738 23.920  1.00   71.16  ? 163  ARG A NE  1 
ATOM   3593 C CZ  . ARG B 1 163 ? 47.725  -10.677 24.347  1.00   70.88  ? 163  ARG A CZ  1 
ATOM   3594 N NH1 . ARG B 1 163 ? 47.743  -9.539  23.664  1.00   69.53  ? 163  ARG A NH1 1 
ATOM   3595 N NH2 . ARG B 1 163 ? 47.016  -10.756 25.466  1.00   71.34  ? 163  ARG A NH2 1 
ATOM   3596 N N   . ASN B 1 164 ? 49.734  -13.208 16.984  0.87   70.66  ? 164  ASN A N   1 
ATOM   3597 C CA  . ASN B 1 164 ? 50.451  -13.020 15.725  0.87   70.86  ? 164  ASN A CA  1 
ATOM   3598 C C   . ASN B 1 164 ? 49.852  -13.824 14.566  0.87   70.34  ? 164  ASN A C   1 
ATOM   3599 O O   . ASN B 1 164 ? 50.564  -14.228 13.645  0.87   70.35  ? 164  ASN A O   1 
ATOM   3600 C CB  . ASN B 1 164 ? 51.946  -13.331 15.904  0.87   71.32  ? 164  ASN A CB  1 
ATOM   3601 C CG  . ASN B 1 164 ? 52.670  -12.272 16.721  0.87   72.10  ? 164  ASN A CG  1 
ATOM   3602 O OD1 . ASN B 1 164 ? 52.962  -12.476 17.899  0.87   73.08  ? 164  ASN A OD1 1 
ATOM   3603 N ND2 . ASN B 1 164 ? 52.955  -11.130 16.100  0.87   73.02  ? 164  ASN A ND2 1 
ATOM   3604 N N   . CYS B 1 165 ? 48.541  -14.045 14.616  1.00   69.51  ? 165  CYS A N   1 
ATOM   3605 C CA  . CYS B 1 165 ? 47.843  -14.814 13.589  1.00   68.62  ? 165  CYS A CA  1 
ATOM   3606 C C   . CYS B 1 165 ? 47.371  -13.919 12.442  1.00   68.11  ? 165  CYS A C   1 
ATOM   3607 O O   . CYS B 1 165 ? 47.499  -12.693 12.505  1.00   67.73  ? 165  CYS A O   1 
ATOM   3608 C CB  . CYS B 1 165 ? 46.639  -15.526 14.200  1.00   68.62  ? 165  CYS A CB  1 
ATOM   3609 S SG  . CYS B 1 165 ? 45.244  -14.420 14.505  1.00   68.41  ? 165  CYS A SG  1 
ATOM   3610 N N   . THR B 1 166 ? 46.813  -14.547 11.407  1.00   67.44  ? 166  THR A N   1 
ATOM   3611 C CA  . THR B 1 166 ? 46.246  -13.833 10.264  1.00   66.64  ? 166  THR A CA  1 
ATOM   3612 C C   . THR B 1 166 ? 44.812  -14.269 9.983   1.00   65.08  ? 166  THR A C   1 
ATOM   3613 O O   . THR B 1 166 ? 44.538  -15.458 9.776   1.00   65.07  ? 166  THR A O   1 
ATOM   3614 C CB  . THR B 1 166 ? 47.079  -14.042 8.980   1.00   67.05  ? 166  THR A CB  1 
ATOM   3615 O OG1 . THR B 1 166 ? 48.446  -13.695 9.230   1.00   67.62  ? 166  THR A OG1 1 
ATOM   3616 C CG2 . THR B 1 166 ? 46.540  -13.173 7.838   1.00   67.28  ? 166  THR A CG2 1 
ATOM   3617 N N   . ILE B 1 167 ? 43.906  -13.294 9.967   1.00   62.59  ? 167  ILE A N   1 
ATOM   3618 C CA  . ILE B 1 167 ? 42.508  -13.532 9.613   1.00   60.10  ? 167  ILE A CA  1 
ATOM   3619 C C   . ILE B 1 167 ? 42.369  -13.461 8.098   1.00   58.56  ? 167  ILE A C   1 
ATOM   3620 O O   . ILE B 1 167 ? 42.703  -12.451 7.487   1.00   58.31  ? 167  ILE A O   1 
ATOM   3621 C CB  . ILE B 1 167 ? 41.564  -12.490 10.260  1.00   60.15  ? 167  ILE A CB  1 
ATOM   3622 C CG1 . ILE B 1 167 ? 41.924  -12.243 11.737  1.00   60.26  ? 167  ILE A CG1 1 
ATOM   3623 C CG2 . ILE B 1 167 ? 40.100  -12.898 10.086  1.00   59.78  ? 167  ILE A CG2 1 
ATOM   3624 C CD1 . ILE B 1 167 ? 41.859  -13.476 12.640  1.00   60.44  ? 167  ILE A CD1 1 
ATOM   3625 N N   . VAL B 1 168 ? 41.872  -14.535 7.497   1.00   57.00  ? 168  VAL A N   1 
ATOM   3626 C CA  . VAL B 1 168 ? 41.855  -14.672 6.044   1.00   55.91  ? 168  VAL A CA  1 
ATOM   3627 C C   . VAL B 1 168 ? 40.432  -14.753 5.507   1.00   55.66  ? 168  VAL A C   1 
ATOM   3628 O O   . VAL B 1 168 ? 39.614  -15.505 6.031   1.00   54.81  ? 168  VAL A O   1 
ATOM   3629 C CB  . VAL B 1 168 ? 42.627  -15.943 5.588   1.00   55.81  ? 168  VAL A CB  1 
ATOM   3630 C CG1 . VAL B 1 168 ? 42.712  -16.016 4.071   1.00   55.22  ? 168  VAL A CG1 1 
ATOM   3631 C CG2 . VAL B 1 168 ? 44.023  -15.982 6.197   1.00   55.59  ? 168  VAL A CG2 1 
ATOM   3632 N N   . SER B 1 169 ? 40.146  -13.977 4.464   1.00   56.12  ? 169  SER A N   1 
ATOM   3633 C CA  . SER B 1 169 ? 38.865  -14.062 3.769   1.00   56.89  ? 169  SER A CA  1 
ATOM   3634 C C   . SER B 1 169 ? 38.962  -14.965 2.548   1.00   57.43  ? 169  SER A C   1 
ATOM   3635 O O   . SER B 1 169 ? 39.844  -14.773 1.709   1.00   57.58  ? 169  SER A O   1 
ATOM   3636 C CB  . SER B 1 169 ? 38.363  -12.679 3.339   1.00   56.98  ? 169  SER A CB  1 
ATOM   3637 O OG  . SER B 1 169 ? 37.193  -12.802 2.543   1.00   56.41  ? 169  SER A OG  1 
ATOM   3638 N N   . PRO B 1 170 ? 38.041  -15.942 2.445   1.00   57.82  ? 170  PRO A N   1 
ATOM   3639 C CA  . PRO B 1 170 ? 37.918  -16.931 1.370   1.00   58.29  ? 170  PRO A CA  1 
ATOM   3640 C C   . PRO B 1 170 ? 37.710  -16.317 -0.009  1.00   58.67  ? 170  PRO A C   1 
ATOM   3641 O O   . PRO B 1 170 ? 38.060  -16.937 -1.014  1.00   58.60  ? 170  PRO A O   1 
ATOM   3642 C CB  . PRO B 1 170 ? 36.658  -17.712 1.754   1.00   58.28  ? 170  PRO A CB  1 
ATOM   3643 C CG  . PRO B 1 170 ? 36.516  -17.525 3.206   1.00   58.41  ? 170  PRO A CG  1 
ATOM   3644 C CD  . PRO B 1 170 ? 37.030  -16.155 3.496   1.00   58.03  ? 170  PRO A CD  1 
ATOM   3645 N N   . ASP B 1 171 ? 37.126  -15.122 -0.050  1.00   59.32  ? 171  ASP A N   1 
ATOM   3646 C CA  . ASP B 1 171 ? 36.831  -14.439 -1.304  1.00   60.21  ? 171  ASP A CA  1 
ATOM   3647 C C   . ASP B 1 171 ? 37.011  -12.926 -1.164  1.00   60.85  ? 171  ASP A C   1 
ATOM   3648 O O   . ASP B 1 171 ? 37.284  -12.423 -0.069  1.00   60.75  ? 171  ASP A O   1 
ATOM   3649 C CB  . ASP B 1 171 ? 35.415  -14.780 -1.786  1.00   60.03  ? 171  ASP A CB  1 
ATOM   3650 C CG  . ASP B 1 171 ? 34.338  -14.399 -0.777  1.00   61.02  ? 171  ASP A CG  1 
ATOM   3651 O OD1 . ASP B 1 171 ? 33.280  -15.061 -0.768  1.00   62.86  ? 171  ASP A OD1 1 
ATOM   3652 O OD2 . ASP B 1 171 ? 34.532  -13.447 0.008   1.00   61.01  ? 171  ASP A OD2 1 
ATOM   3653 N N   . ALA B 1 172 ? 36.854  -12.217 -2.278  1.00   62.02  ? 172  ALA A N   1 
ATOM   3654 C CA  . ALA B 1 172 ? 37.001  -10.764 -2.323  1.00   63.17  ? 172  ALA A CA  1 
ATOM   3655 C C   . ALA B 1 172 ? 35.915  -10.044 -1.525  1.00   63.76  ? 172  ALA A C   1 
ATOM   3656 O O   . ALA B 1 172 ? 36.176  -9.025  -0.884  1.00   63.88  ? 172  ALA A O   1 
ATOM   3657 C CB  . ALA B 1 172 ? 37.004  -10.283 -3.766  1.00   63.14  ? 172  ALA A CB  1 
ATOM   3658 N N   . GLY B 1 173 ? 34.703  -10.588 -1.562  1.00   64.29  ? 173  GLY A N   1 
ATOM   3659 C CA  . GLY B 1 173 ? 33.554  -9.965  -0.911  1.00   64.31  ? 173  GLY A CA  1 
ATOM   3660 C C   . GLY B 1 173 ? 33.644  -9.907  0.601   1.00   63.77  ? 173  GLY A C   1 
ATOM   3661 O O   . GLY B 1 173 ? 33.038  -9.036  1.230   1.00   64.23  ? 173  GLY A O   1 
ATOM   3662 N N   . GLY B 1 174 ? 34.409  -10.828 1.183   1.00   62.44  ? 174  GLY A N   1 
ATOM   3663 C CA  . GLY B 1 174 ? 34.507  -10.936 2.638   1.00   60.06  ? 174  GLY A CA  1 
ATOM   3664 C C   . GLY B 1 174 ? 35.519  -10.010 3.285   1.00   58.29  ? 174  GLY A C   1 
ATOM   3665 O O   . GLY B 1 174 ? 35.750  -10.096 4.491   1.00   58.28  ? 174  GLY A O   1 
ATOM   3666 N N   . ALA B 1 175 ? 36.119  -9.127  2.486   1.00   56.72  ? 175  ALA A N   1 
ATOM   3667 C CA  . ALA B 1 175 ? 37.167  -8.213  2.956   1.00   55.81  ? 175  ALA A CA  1 
ATOM   3668 C C   . ALA B 1 175 ? 36.788  -7.416  4.206   1.00   56.04  ? 175  ALA A C   1 
ATOM   3669 O O   . ALA B 1 175 ? 37.519  -7.431  5.197   1.00   55.96  ? 175  ALA A O   1 
ATOM   3670 C CB  . ALA B 1 175 ? 37.585  -7.272  1.836   1.00   55.62  ? 175  ALA A CB  1 
ATOM   3671 N N   . LYS B 1 176 ? 35.651  -6.726  4.160   1.00   56.91  ? 176  LYS A N   1 
ATOM   3672 C CA  . LYS B 1 176 ? 35.236  -5.846  5.257   1.00   57.75  ? 176  LYS A CA  1 
ATOM   3673 C C   . LYS B 1 176 ? 35.114  -6.597  6.581   1.00   57.53  ? 176  LYS A C   1 
ATOM   3674 O O   . LYS B 1 176 ? 35.499  -6.084  7.637   1.00   57.49  ? 176  LYS A O   1 
ATOM   3675 C CB  . LYS B 1 176 ? 33.918  -5.157  4.911   1.00   58.26  ? 176  LYS A CB  1 
ATOM   3676 C CG  . LYS B 1 176 ? 33.814  -3.741  5.438   1.00   60.47  ? 176  LYS A CG  1 
ATOM   3677 C CD  . LYS B 1 176 ? 32.902  -2.905  4.553   1.00   64.34  ? 176  LYS A CD  1 
ATOM   3678 C CE  . LYS B 1 176 ? 33.096  -1.413  4.801   1.00   67.65  ? 176  LYS A CE  1 
ATOM   3679 N NZ  . LYS B 1 176 ? 34.450  -0.937  4.365   1.00   68.13  ? 176  LYS A NZ  1 
ATOM   3680 N N   . ARG B 1 177 ? 34.596  -7.820  6.501   0.83   57.13  ? 177  ARG A N   1 
ATOM   3681 C CA  . ARG B 1 177 ? 34.371  -8.664  7.662   0.83   56.78  ? 177  ARG A CA  1 
ATOM   3682 C C   . ARG B 1 177 ? 35.677  -9.039  8.363   0.83   56.20  ? 177  ARG A C   1 
ATOM   3683 O O   . ARG B 1 177 ? 35.776  -8.943  9.591   0.83   56.12  ? 177  ARG A O   1 
ATOM   3684 C CB  . ARG B 1 177 ? 33.620  -9.924  7.237   0.83   57.16  ? 177  ARG A CB  1 
ATOM   3685 C CG  . ARG B 1 177 ? 32.995  -10.716 8.372   0.83   58.41  ? 177  ARG A CG  1 
ATOM   3686 C CD  . ARG B 1 177 ? 32.258  -11.951 7.851   0.83   60.78  ? 177  ARG A CD  1 
ATOM   3687 N NE  . ARG B 1 177 ? 31.141  -11.609 6.967   0.83   62.58  ? 177  ARG A NE  1 
ATOM   3688 C CZ  . ARG B 1 177 ? 31.111  -11.828 5.653   0.83   63.86  ? 177  ARG A CZ  1 
ATOM   3689 N NH1 . ARG B 1 177 ? 32.139  -12.403 5.037   0.83   64.39  ? 177  ARG A NH1 1 
ATOM   3690 N NH2 . ARG B 1 177 ? 30.041  -11.476 4.948   0.83   64.10  ? 177  ARG A NH2 1 
ATOM   3691 N N   . VAL B 1 178 ? 36.675  -9.463  7.589   1.00   55.17  ? 178  VAL A N   1 
ATOM   3692 C CA  . VAL B 1 178 ? 37.949  -9.884  8.176   1.00   54.46  ? 178  VAL A CA  1 
ATOM   3693 C C   . VAL B 1 178 ? 38.803  -8.729  8.688   1.00   53.79  ? 178  VAL A C   1 
ATOM   3694 O O   . VAL B 1 178 ? 39.413  -8.848  9.755   1.00   53.24  ? 178  VAL A O   1 
ATOM   3695 C CB  . VAL B 1 178 ? 38.795  -10.807 7.241   1.00   54.62  ? 178  VAL A CB  1 
ATOM   3696 C CG1 . VAL B 1 178 ? 38.020  -12.072 6.886   1.00   54.28  ? 178  VAL A CG1 1 
ATOM   3697 C CG2 . VAL B 1 178 ? 39.259  -10.073 5.990   1.00   54.79  ? 178  VAL A CG2 1 
ATOM   3698 N N   . THR B 1 179 ? 38.851  -7.621  7.943   1.00   53.00  ? 179  THR A N   1 
ATOM   3699 C CA  . THR B 1 179 ? 39.652  -6.481  8.379   1.00   52.44  ? 179  THR A CA  1 
ATOM   3700 C C   . THR B 1 179 ? 39.092  -5.913  9.676   1.00   53.16  ? 179  THR A C   1 
ATOM   3701 O O   . THR B 1 179 ? 39.826  -5.341  10.474  1.00   53.30  ? 179  THR A O   1 
ATOM   3702 C CB  . THR B 1 179 ? 39.787  -5.366  7.314   1.00   51.89  ? 179  THR A CB  1 
ATOM   3703 O OG1 . THR B 1 179 ? 38.512  -4.776  7.042   1.00   51.68  ? 179  THR A OG1 1 
ATOM   3704 C CG2 . THR B 1 179 ? 40.383  -5.906  6.038   1.00   51.56  ? 179  THR A CG2 1 
ATOM   3705 N N   . SER B 1 180 ? 37.791  -6.088  9.883   1.00   54.12  ? 180  SER A N   1 
ATOM   3706 C CA  . SER B 1 180 ? 37.160  -5.700  11.136  1.00   55.84  ? 180  SER A CA  1 
ATOM   3707 C C   . SER B 1 180 ? 37.652  -6.587  12.277  1.00   57.18  ? 180  SER A C   1 
ATOM   3708 O O   . SER B 1 180 ? 37.989  -6.093  13.345  1.00   56.38  ? 180  SER A O   1 
ATOM   3709 C CB  . SER B 1 180 ? 35.640  -5.785  11.028  1.00   55.41  ? 180  SER A CB  1 
ATOM   3710 O OG  . SER B 1 180 ? 35.050  -5.702  12.314  1.00   57.12  ? 180  SER A OG  1 
ATOM   3711 N N   . ILE B 1 181 ? 37.693  -7.895  12.041  1.00   59.54  ? 181  ILE A N   1 
ATOM   3712 C CA  . ILE B 1 181 ? 38.134  -8.843  13.061  1.00   61.69  ? 181  ILE A CA  1 
ATOM   3713 C C   . ILE B 1 181 ? 39.634  -8.711  13.333  1.00   62.10  ? 181  ILE A C   1 
ATOM   3714 O O   . ILE B 1 181 ? 40.055  -8.617  14.489  1.00   62.49  ? 181  ILE A O   1 
ATOM   3715 C CB  . ILE B 1 181 ? 37.742  -10.294 12.689  1.00   62.14  ? 181  ILE A CB  1 
ATOM   3716 C CG1 . ILE B 1 181 ? 36.233  -10.481 12.882  1.00   62.74  ? 181  ILE A CG1 1 
ATOM   3717 C CG2 . ILE B 1 181 ? 38.523  -11.317 13.526  1.00   62.41  ? 181  ILE A CG2 1 
ATOM   3718 C CD1 . ILE B 1 181 ? 35.691  -11.790 12.349  1.00   63.14  ? 181  ILE A CD1 1 
ATOM   3719 N N   . ALA B 1 182 ? 40.424  -8.691  12.262  1.00   62.01  ? 182  ALA A N   1 
ATOM   3720 C CA  . ALA B 1 182 ? 41.865  -8.480  12.351  1.00   61.74  ? 182  ALA A CA  1 
ATOM   3721 C C   . ALA B 1 182 ? 42.193  -7.177  13.077  1.00   61.65  ? 182  ALA A C   1 
ATOM   3722 O O   . ALA B 1 182 ? 43.112  -7.136  13.900  1.00   61.58  ? 182  ALA A O   1 
ATOM   3723 C CB  . ALA B 1 182 ? 42.494  -8.491  10.964  1.00   61.74  ? 182  ALA A CB  1 
ATOM   3724 N N   . ASP B 1 183 ? 41.441  -6.119  12.774  1.00   61.11  ? 183  ASP A N   1 
ATOM   3725 C CA  . ASP B 1 183 ? 41.623  -4.846  13.463  1.00   61.59  ? 183  ASP A CA  1 
ATOM   3726 C C   . ASP B 1 183 ? 41.350  -4.955  14.961  1.00   62.40  ? 183  ASP A C   1 
ATOM   3727 O O   . ASP B 1 183 ? 42.144  -4.472  15.773  1.00   62.33  ? 183  ASP A O   1 
ATOM   3728 C CB  . ASP B 1 183 ? 40.772  -3.737  12.838  1.00   61.24  ? 183  ASP A CB  1 
ATOM   3729 C CG  . ASP B 1 183 ? 41.431  -3.108  11.620  1.00   61.31  ? 183  ASP A CG  1 
ATOM   3730 O OD1 . ASP B 1 183 ? 42.474  -3.625  11.164  1.00   61.11  ? 183  ASP A OD1 1 
ATOM   3731 O OD2 . ASP B 1 183 ? 40.902  -2.094  11.112  1.00   61.23  ? 183  ASP A OD2 1 
ATOM   3732 N N   . ARG B 1 184 ? 40.243  -5.600  15.325  0.80   63.69  ? 184  ARG A N   1 
ATOM   3733 C CA  . ARG B 1 184 ? 39.886  -5.775  16.736  0.80   65.10  ? 184  ARG A CA  1 
ATOM   3734 C C   . ARG B 1 184 ? 40.951  -6.560  17.500  0.80   65.65  ? 184  ARG A C   1 
ATOM   3735 O O   . ARG B 1 184 ? 41.238  -6.260  18.658  0.80   65.65  ? 184  ARG A O   1 
ATOM   3736 C CB  . ARG B 1 184 ? 38.515  -6.442  16.875  0.80   65.32  ? 184  ARG A CB  1 
ATOM   3737 C CG  . ARG B 1 184 ? 37.323  -5.475  16.884  0.80   66.98  ? 184  ARG A CG  1 
ATOM   3738 C CD  . ARG B 1 184 ? 37.392  -4.475  15.733  0.80   69.86  ? 184  ARG A CD  1 
ATOM   3739 N NE  . ARG B 1 184 ? 36.092  -3.913  15.369  0.80   71.64  ? 184  ARG A NE  1 
ATOM   3740 C CZ  . ARG B 1 184 ? 35.913  -2.978  14.438  0.80   72.24  ? 184  ARG A CZ  1 
ATOM   3741 N NH1 . ARG B 1 184 ? 36.950  -2.487  13.769  0.80   71.85  ? 184  ARG A NH1 1 
ATOM   3742 N NH2 . ARG B 1 184 ? 34.693  -2.525  14.179  0.80   72.49  ? 184  ARG A NH2 1 
ATOM   3743 N N   . LEU B 1 185 ? 41.537  -7.551  16.832  1.00   66.57  ? 185  LEU A N   1 
ATOM   3744 C CA  . LEU B 1 185 ? 42.581  -8.392  17.409  1.00   67.43  ? 185  LEU A CA  1 
ATOM   3745 C C   . LEU B 1 185 ? 43.971  -7.767  17.305  1.00   68.23  ? 185  LEU A C   1 
ATOM   3746 O O   . LEU B 1 185 ? 44.914  -8.232  17.951  1.00   68.40  ? 185  LEU A O   1 
ATOM   3747 C CB  . LEU B 1 185 ? 42.599  -9.754  16.711  1.00   67.30  ? 185  LEU A CB  1 
ATOM   3748 C CG  . LEU B 1 185 ? 41.451  -10.729 16.973  1.00   66.99  ? 185  LEU A CG  1 
ATOM   3749 C CD1 . LEU B 1 185 ? 41.592  -11.955 16.089  1.00   66.16  ? 185  LEU A CD1 1 
ATOM   3750 C CD2 . LEU B 1 185 ? 41.385  -11.137 18.446  1.00   67.09  ? 185  LEU A CD2 1 
ATOM   3751 N N   . ASN B 1 186 ? 44.082  -6.723  16.485  1.00   68.94  ? 186  ASN A N   1 
ATOM   3752 C CA  . ASN B 1 186 ? 45.356  -6.091  16.131  1.00   69.33  ? 186  ASN A CA  1 
ATOM   3753 C C   . ASN B 1 186 ? 46.345  -7.060  15.476  1.00   68.46  ? 186  ASN A C   1 
ATOM   3754 O O   . ASN B 1 186 ? 47.523  -7.104  15.841  1.00   68.49  ? 186  ASN A O   1 
ATOM   3755 C CB  . ASN B 1 186 ? 45.986  -5.394  17.341  1.00   69.95  ? 186  ASN A CB  1 
ATOM   3756 C CG  . ASN B 1 186 ? 46.240  -3.927  17.088  1.00   72.35  ? 186  ASN A CG  1 
ATOM   3757 O OD1 . ASN B 1 186 ? 47.325  -3.535  16.658  1.00   75.96  ? 186  ASN A OD1 1 
ATOM   3758 N ND2 . ASN B 1 186 ? 45.226  -3.104  17.331  1.00   72.79  ? 186  ASN A ND2 1 
ATOM   3759 N N   . VAL B 1 187 ? 45.851  -7.831  14.510  1.00   67.03  ? 187  VAL A N   1 
ATOM   3760 C CA  . VAL B 1 187 ? 46.677  -8.785  13.766  1.00   65.51  ? 187  VAL A CA  1 
ATOM   3761 C C   . VAL B 1 187 ? 46.562  -8.557  12.251  1.00   64.83  ? 187  VAL A C   1 
ATOM   3762 O O   . VAL B 1 187 ? 45.875  -7.631  11.812  1.00   64.49  ? 187  VAL A O   1 
ATOM   3763 C CB  . VAL B 1 187 ? 46.332  -10.253 14.130  1.00   65.49  ? 187  VAL A CB  1 
ATOM   3764 C CG1 . VAL B 1 187 ? 46.399  -10.461 15.643  1.00   65.29  ? 187  VAL A CG1 1 
ATOM   3765 C CG2 . VAL B 1 187 ? 44.956  -10.652 13.589  1.00   65.27  ? 187  VAL A CG2 1 
ATOM   3766 N N   . ASP B 1 188 ? 47.232  -9.400  11.466  0.92   64.05  ? 188  ASP A N   1 
ATOM   3767 C CA  . ASP B 1 188 ? 47.235  -9.283  10.009  0.92   63.43  ? 188  ASP A CA  1 
ATOM   3768 C C   . ASP B 1 188 ? 45.958  -9.833  9.383   0.92   62.13  ? 188  ASP A C   1 
ATOM   3769 O O   . ASP B 1 188 ? 45.309  -10.713 9.948   0.92   62.40  ? 188  ASP A O   1 
ATOM   3770 C CB  . ASP B 1 188 ? 48.436  -10.031 9.419   0.92   64.00  ? 188  ASP A CB  1 
ATOM   3771 C CG  . ASP B 1 188 ? 49.767  -9.365  9.737   0.92   65.17  ? 188  ASP A CG  1 
ATOM   3772 O OD1 . ASP B 1 188 ? 49.787  -8.179  10.133  0.92   66.27  ? 188  ASP A OD1 1 
ATOM   3773 O OD2 . ASP B 1 188 ? 50.807  -10.037 9.580   0.92   66.60  ? 188  ASP A OD2 1 
ATOM   3774 N N   . PHE B 1 189 ? 45.602  -9.306  8.215   1.00   60.01  ? 189  PHE A N   1 
ATOM   3775 C CA  . PHE B 1 189 ? 44.527  -9.887  7.415   1.00   57.96  ? 189  PHE A CA  1 
ATOM   3776 C C   . PHE B 1 189 ? 45.065  -10.246 6.040   1.00   57.21  ? 189  PHE A C   1 
ATOM   3777 O O   . PHE B 1 189 ? 46.044  -9.660  5.578   1.00   57.00  ? 189  PHE A O   1 
ATOM   3778 C CB  . PHE B 1 189 ? 43.329  -8.931  7.292   1.00   57.16  ? 189  PHE A CB  1 
ATOM   3779 C CG  . PHE B 1 189 ? 43.563  -7.782  6.358   1.00   55.84  ? 189  PHE A CG  1 
ATOM   3780 C CD1 . PHE B 1 189 ? 43.209  -7.874  5.012   1.00   54.48  ? 189  PHE A CD1 1 
ATOM   3781 C CD2 . PHE B 1 189 ? 44.146  -6.608  6.819   1.00   54.53  ? 189  PHE A CD2 1 
ATOM   3782 C CE1 . PHE B 1 189 ? 43.434  -6.812  4.141   1.00   54.22  ? 189  PHE A CE1 1 
ATOM   3783 C CE2 . PHE B 1 189 ? 44.374  -5.544  5.957   1.00   53.78  ? 189  PHE A CE2 1 
ATOM   3784 C CZ  . PHE B 1 189 ? 44.018  -5.645  4.614   1.00   53.86  ? 189  PHE A CZ  1 
ATOM   3785 N N   . ALA B 1 190 ? 44.419  -11.205 5.391   1.00   56.77  ? 190  ALA A N   1 
ATOM   3786 C CA  . ALA B 1 190 ? 44.747  -11.555 4.019   1.00   56.84  ? 190  ALA A CA  1 
ATOM   3787 C C   . ALA B 1 190 ? 43.486  -11.979 3.298   1.00   57.18  ? 190  ALA A C   1 
ATOM   3788 O O   . ALA B 1 190 ? 42.485  -12.318 3.929   1.00   57.32  ? 190  ALA A O   1 
ATOM   3789 C CB  . ALA B 1 190 ? 45.795  -12.658 3.976   1.00   56.61  ? 190  ALA A CB  1 
ATOM   3790 N N   . LEU B 1 191 ? 43.528  -11.948 1.974   1.00   57.88  ? 191  LEU A N   1 
ATOM   3791 C CA  . LEU B 1 191 ? 42.345  -12.235 1.194   1.00   58.58  ? 191  LEU A CA  1 
ATOM   3792 C C   . LEU B 1 191 ? 42.643  -13.215 0.080   1.00   58.94  ? 191  LEU A C   1 
ATOM   3793 O O   . LEU B 1 191 ? 43.711  -13.171 -0.528  1.00   58.98  ? 191  LEU A O   1 
ATOM   3794 C CB  . LEU B 1 191 ? 41.760  -10.939 0.632   1.00   58.79  ? 191  LEU A CB  1 
ATOM   3795 C CG  . LEU B 1 191 ? 40.486  -11.087 -0.200  1.00   59.46  ? 191  LEU A CG  1 
ATOM   3796 C CD1 . LEU B 1 191 ? 39.429  -10.097 0.269   1.00   60.36  ? 191  LEU A CD1 1 
ATOM   3797 C CD2 . LEU B 1 191 ? 40.782  -10.955 -1.695  1.00   59.51  ? 191  LEU A CD2 1 
ATOM   3798 N N   . ILE B 1 192 ? 41.686  -14.097 -0.183  1.00   59.39  ? 192  ILE A N   1 
ATOM   3799 C CA  . ILE B 1 192 ? 41.796  -15.031 -1.289  1.00   60.12  ? 192  ILE A CA  1 
ATOM   3800 C C   . ILE B 1 192 ? 40.826  -14.644 -2.393  1.00   60.40  ? 192  ILE A C   1 
ATOM   3801 O O   . ILE B 1 192 ? 39.715  -14.201 -2.128  1.00   60.53  ? 192  ILE A O   1 
ATOM   3802 C CB  . ILE B 1 192 ? 41.565  -16.490 -0.830  1.00   60.28  ? 192  ILE A CB  1 
ATOM   3803 C CG1 . ILE B 1 192 ? 42.698  -16.920 0.106   1.00   60.87  ? 192  ILE A CG1 1 
ATOM   3804 C CG2 . ILE B 1 192 ? 41.482  -17.446 -2.028  1.00   60.44  ? 192  ILE A CG2 1 
ATOM   3805 C CD1 . ILE B 1 192 ? 42.464  -18.235 0.808   1.00   61.93  ? 192  ILE A CD1 1 
ATOM   3806 N N   . HIS B 1 193 ? 41.266  -14.799 -3.634  1.00   60.90  ? 193  HIS A N   1 
ATOM   3807 C CA  . HIS B 1 193 ? 40.404  -14.588 -4.780  1.00   61.52  ? 193  HIS A CA  1 
ATOM   3808 C C   . HIS B 1 193 ? 40.539  -15.748 -5.759  1.00   62.62  ? 193  HIS A C   1 
ATOM   3809 O O   . HIS B 1 193 ? 41.653  -16.200 -6.046  1.00   62.61  ? 193  HIS A O   1 
ATOM   3810 C CB  . HIS B 1 193 ? 40.746  -13.264 -5.460  1.00   61.16  ? 193  HIS A CB  1 
ATOM   3811 C CG  . HIS B 1 193 ? 39.974  -13.017 -6.715  1.00   60.01  ? 193  HIS A CG  1 
ATOM   3812 N ND1 . HIS B 1 193 ? 38.596  -13.025 -6.753  1.00   58.96  ? 193  HIS A ND1 1 
ATOM   3813 C CD2 . HIS B 1 193 ? 40.384  -12.753 -7.978  1.00   59.40  ? 193  HIS A CD2 1 
ATOM   3814 C CE1 . HIS B 1 193 ? 38.190  -12.780 -7.986  1.00   58.61  ? 193  HIS A CE1 1 
ATOM   3815 N NE2 . HIS B 1 193 ? 39.255  -12.612 -8.749  1.00   59.00  ? 193  HIS A NE2 1 
ATOM   3816 N N   . LYS B 1 194 ? 39.407  -16.239 -6.259  0.57   64.20  ? 194  LYS A N   1 
ATOM   3817 C CA  . LYS B 1 194 ? 39.435  -17.273 -7.284  0.57   66.66  ? 194  LYS A CA  1 
ATOM   3818 C C   . LYS B 1 194 ? 39.421  -16.641 -8.671  0.57   69.68  ? 194  LYS A C   1 
ATOM   3819 O O   . LYS B 1 194 ? 38.435  -16.014 -9.075  0.57   69.00  ? 194  LYS A O   1 
ATOM   3820 C CB  . LYS B 1 194 ? 38.293  -18.280 -7.116  0.57   66.00  ? 194  LYS A CB  1 
ATOM   3821 C CG  . LYS B 1 194 ? 38.475  -19.535 -7.966  0.57   65.67  ? 194  LYS A CG  1 
ATOM   3822 C CD  . LYS B 1 194 ? 37.612  -20.696 -7.492  0.57   65.37  ? 194  LYS A CD  1 
ATOM   3823 C CE  . LYS B 1 194 ? 38.115  -22.022 -8.072  0.57   65.26  ? 194  LYS A CE  1 
ATOM   3824 N NZ  . LYS B 1 194 ? 37.144  -23.144 -7.905  0.57   65.12  ? 194  LYS A NZ  1 
ATOM   3825 N N   . GLU B 1 195 ? 40.532  -16.818 -9.383  1.00   90.81  ? 195  GLU A N   1 
ATOM   3826 C CA  . GLU B 1 195 ? 40.732  -16.254 -10.715 1.00   86.28  ? 195  GLU A CA  1 
ATOM   3827 C C   . GLU B 1 195 ? 39.738  -16.828 -11.722 1.00   85.33  ? 195  GLU A C   1 
ATOM   3828 O O   . GLU B 1 195 ? 39.758  -18.021 -12.024 1.00   86.60  ? 195  GLU A O   1 
ATOM   3829 C CB  . GLU B 1 195 ? 42.163  -16.519 -11.186 1.00   86.45  ? 195  GLU A CB  1 
ATOM   3830 C CG  . GLU B 1 195 ? 42.854  -15.325 -11.823 1.00   89.52  ? 195  GLU A CG  1 
ATOM   3831 C CD  . GLU B 1 195 ? 43.599  -14.464 -10.813 1.00   91.74  ? 195  GLU A CD  1 
ATOM   3832 O OE1 . GLU B 1 195 ? 43.015  -14.114 -9.761  1.00   95.18  ? 195  GLU A OE1 1 
ATOM   3833 O OE2 . GLU B 1 195 ? 44.774  -14.129 -11.077 1.00   92.64  ? 195  GLU A OE2 1 
ATOM   3834 N N   . ASP B 1 203 ? 39.719  -23.270 -11.666 0.47   73.38  ? 203  ASP A N   1 
ATOM   3835 C CA  . ASP B 1 203 ? 40.348  -21.959 -11.547 0.47   73.43  ? 203  ASP A CA  1 
ATOM   3836 C C   . ASP B 1 203 ? 41.531  -21.997 -10.587 0.47   73.66  ? 203  ASP A C   1 
ATOM   3837 O O   . ASP B 1 203 ? 41.735  -22.985 -9.876  0.47   73.64  ? 203  ASP A O   1 
ATOM   3838 C CB  . ASP B 1 203 ? 39.335  -20.921 -11.064 0.47   73.36  ? 203  ASP A CB  1 
ATOM   3839 C CG  . ASP B 1 203 ? 38.159  -20.770 -11.999 0.47   73.12  ? 203  ASP A CG  1 
ATOM   3840 O OD1 . ASP B 1 203 ? 38.373  -20.739 -13.230 0.47   72.86  ? 203  ASP A OD1 1 
ATOM   3841 O OD2 . ASP B 1 203 ? 37.017  -20.674 -11.502 0.47   73.18  ? 203  ASP A OD2 1 
ATOM   3842 N N   . ARG B 1 204 ? 42.303  -20.912 -10.571 0.54   73.94  ? 204  ARG A N   1 
ATOM   3843 C CA  . ARG B 1 204 ? 43.445  -20.792 -9.673  0.54   74.02  ? 204  ARG A CA  1 
ATOM   3844 C C   . ARG B 1 204 ? 43.131  -19.787 -8.566  0.54   73.13  ? 204  ARG A C   1 
ATOM   3845 O O   . ARG B 1 204 ? 42.506  -18.749 -8.811  0.54   73.15  ? 204  ARG A O   1 
ATOM   3846 C CB  . ARG B 1 204 ? 44.709  -20.391 -10.449 0.54   74.57  ? 204  ARG A CB  1 
ATOM   3847 C CG  . ARG B 1 204 ? 45.278  -19.016 -10.103 0.54   75.92  ? 204  ARG A CG  1 
ATOM   3848 C CD  . ARG B 1 204 ? 46.372  -18.599 -11.064 0.54   78.18  ? 204  ARG A CD  1 
ATOM   3849 N NE  . ARG B 1 204 ? 47.153  -17.483 -10.532 0.54   79.68  ? 204  ARG A NE  1 
ATOM   3850 C CZ  . ARG B 1 204 ? 47.932  -16.688 -11.262 0.54   80.34  ? 204  ARG A CZ  1 
ATOM   3851 N NH1 . ARG B 1 204 ? 48.040  -16.863 -12.573 0.54   80.55  ? 204  ARG A NH1 1 
ATOM   3852 N NH2 . ARG B 1 204 ? 48.601  -15.704 -10.677 0.54   80.50  ? 204  ARG A NH2 1 
ATOM   3853 N N   . MET B 1 205 ? 43.556  -20.109 -7.348  0.80   71.70  ? 205  MET A N   1 
ATOM   3854 C CA  . MET B 1 205 ? 43.357  -19.218 -6.213  0.80   70.43  ? 205  MET A CA  1 
ATOM   3855 C C   . MET B 1 205 ? 44.558  -18.309 -5.994  0.80   69.26  ? 205  MET A C   1 
ATOM   3856 O O   . MET B 1 205 ? 45.700  -18.770 -5.948  0.80   69.29  ? 205  MET A O   1 
ATOM   3857 C CB  . MET B 1 205 ? 43.060  -20.015 -4.944  0.80   70.61  ? 205  MET A CB  1 
ATOM   3858 C CG  . MET B 1 205 ? 41.630  -20.498 -4.844  0.80   71.59  ? 205  MET A CG  1 
ATOM   3859 S SD  . MET B 1 205 ? 41.270  -21.170 -3.214  0.80   73.94  ? 205  MET A SD  1 
ATOM   3860 C CE  . MET B 1 205 ? 39.495  -20.893 -3.127  0.80   74.14  ? 205  MET A CE  1 
ATOM   3861 N N   . VAL B 1 206 ? 44.289  -17.013 -5.871  1.00   67.70  ? 206  VAL A N   1 
ATOM   3862 C CA  . VAL B 1 206 ? 45.324  -16.040 -5.555  1.00   66.18  ? 206  VAL A CA  1 
ATOM   3863 C C   . VAL B 1 206 ? 45.195  -15.611 -4.097  1.00   65.32  ? 206  VAL A C   1 
ATOM   3864 O O   . VAL B 1 206 ? 44.089  -15.516 -3.562  1.00   64.44  ? 206  VAL A O   1 
ATOM   3865 C CB  . VAL B 1 206 ? 45.267  -14.812 -6.502  1.00   66.22  ? 206  VAL A CB  1 
ATOM   3866 C CG1 . VAL B 1 206 ? 46.226  -13.718 -6.053  1.00   66.03  ? 206  VAL A CG1 1 
ATOM   3867 C CG2 . VAL B 1 206 ? 45.600  -15.229 -7.923  1.00   66.28  ? 206  VAL A CG2 1 
ATOM   3868 N N   . LEU B 1 207 ? 46.337  -15.370 -3.461  1.00   64.78  ? 207  LEU A N   1 
ATOM   3869 C CA  . LEU B 1 207 ? 46.373  -14.899 -2.089  1.00   64.51  ? 207  LEU A CA  1 
ATOM   3870 C C   . LEU B 1 207 ? 47.161  -13.599 -1.990  1.00   64.23  ? 207  LEU A C   1 
ATOM   3871 O O   . LEU B 1 207 ? 48.300  -13.510 -2.464  1.00   64.07  ? 207  LEU A O   1 
ATOM   3872 C CB  . LEU B 1 207 ? 46.994  -15.965 -1.183  1.00   64.72  ? 207  LEU A CB  1 
ATOM   3873 C CG  . LEU B 1 207 ? 46.926  -15.770 0.336   1.00   65.16  ? 207  LEU A CG  1 
ATOM   3874 C CD1 . LEU B 1 207 ? 47.057  -17.104 1.023   1.00   66.31  ? 207  LEU A CD1 1 
ATOM   3875 C CD2 . LEU B 1 207 ? 47.991  -14.807 0.846   1.00   65.83  ? 207  LEU A CD2 1 
ATOM   3876 N N   . VAL B 1 208 ? 46.545  -12.596 -1.368  1.00   63.80  ? 208  VAL A N   1 
ATOM   3877 C CA  . VAL B 1 208 ? 47.217  -11.336 -1.078  1.00   63.49  ? 208  VAL A CA  1 
ATOM   3878 C C   . VAL B 1 208 ? 47.256  -11.130 0.432   1.00   64.25  ? 208  VAL A C   1 
ATOM   3879 O O   . VAL B 1 208 ? 46.274  -11.396 1.127   1.00   64.00  ? 208  VAL A O   1 
ATOM   3880 C CB  . VAL B 1 208 ? 46.551  -10.128 -1.791  1.00   63.08  ? 208  VAL A CB  1 
ATOM   3881 C CG1 . VAL B 1 208 ? 46.349  -10.426 -3.274  1.00   62.36  ? 208  VAL A CG1 1 
ATOM   3882 C CG2 . VAL B 1 208 ? 45.221  -9.755  -1.139  1.00   62.78  ? 208  VAL A CG2 1 
ATOM   3883 N N   . GLY B 1 209 ? 48.393  -10.659 0.930   1.00   65.35  ? 209  GLY A N   1 
ATOM   3884 C CA  . GLY B 1 209 ? 48.615  -10.556 2.367   1.00   68.02  ? 209  GLY A CA  1 
ATOM   3885 C C   . GLY B 1 209 ? 49.537  -11.655 2.859   1.00   70.04  ? 209  GLY A C   1 
ATOM   3886 O O   . GLY B 1 209 ? 49.910  -12.554 2.100   1.00   70.13  ? 209  GLY A O   1 
ATOM   3887 N N   . ASP B 1 210 ? 49.893  -11.595 4.138   1.00   72.26  ? 210  ASP A N   1 
ATOM   3888 C CA  . ASP B 1 210 ? 50.932  -12.466 4.677   1.00   74.31  ? 210  ASP A CA  1 
ATOM   3889 C C   . ASP B 1 210 ? 50.397  -13.537 5.622   1.00   74.44  ? 210  ASP A C   1 
ATOM   3890 O O   . ASP B 1 210 ? 49.668  -13.237 6.566   1.00   74.81  ? 210  ASP A O   1 
ATOM   3891 C CB  . ASP B 1 210 ? 52.006  -11.631 5.379   1.00   74.98  ? 210  ASP A CB  1 
ATOM   3892 C CG  . ASP B 1 210 ? 53.342  -12.348 5.460   1.00   78.52  ? 210  ASP A CG  1 
ATOM   3893 O OD1 . ASP B 1 210 ? 53.728  -13.021 4.476   1.00   77.71  ? 210  ASP A OD1 1 
ATOM   3894 O OD2 . ASP B 1 210 ? 54.013  -12.232 6.508   1.00   81.89  ? 210  ASP A OD2 1 
ATOM   3895 N N   . VAL B 1 211 ? 50.776  -14.785 5.363   1.00   74.08  ? 211  VAL A N   1 
ATOM   3896 C CA  . VAL B 1 211 ? 50.339  -15.916 6.185   1.00   73.50  ? 211  VAL A CA  1 
ATOM   3897 C C   . VAL B 1 211 ? 51.498  -16.818 6.624   1.00   73.05  ? 211  VAL A C   1 
ATOM   3898 O O   . VAL B 1 211 ? 51.299  -17.757 7.399   1.00   73.12  ? 211  VAL A O   1 
ATOM   3899 C CB  . VAL B 1 211 ? 49.276  -16.780 5.458   1.00   73.52  ? 211  VAL A CB  1 
ATOM   3900 C CG1 . VAL B 1 211 ? 48.113  -15.915 4.966   1.00   73.52  ? 211  VAL A CG1 1 
ATOM   3901 C CG2 . VAL B 1 211 ? 49.903  -17.549 4.305   1.00   73.40  ? 211  VAL A CG2 1 
ATOM   3902 N N   . LYS B 1 212 ? 52.698  -16.522 6.125   0.64   72.42  ? 212  LYS A N   1 
ATOM   3903 C CA  . LYS B 1 212 ? 53.878  -17.361 6.336   0.64   72.17  ? 212  LYS A CA  1 
ATOM   3904 C C   . LYS B 1 212 ? 54.260  -17.475 7.809   0.64   73.14  ? 212  LYS A C   1 
ATOM   3905 O O   . LYS B 1 212 ? 54.435  -16.461 8.495   0.64   72.61  ? 212  LYS A O   1 
ATOM   3906 C CB  . LYS B 1 212 ? 55.064  -16.824 5.522   0.64   71.73  ? 212  LYS A CB  1 
ATOM   3907 C CG  . LYS B 1 212 ? 56.238  -17.794 5.373   0.64   70.78  ? 212  LYS A CG  1 
ATOM   3908 C CD  . LYS B 1 212 ? 55.939  -18.891 4.354   0.64   70.02  ? 212  LYS A CD  1 
ATOM   3909 C CE  . LYS B 1 212 ? 57.097  -19.875 4.218   0.64   69.61  ? 212  LYS A CE  1 
ATOM   3910 N NZ  . LYS B 1 212 ? 56.801  -20.943 3.218   0.64   69.40  ? 212  LYS A NZ  1 
ATOM   3911 N N   . ASP B 1 213 ? 54.383  -18.718 8.276   1.00   75.11  ? 213  ASP A N   1 
ATOM   3912 C CA  . ASP B 1 213 ? 54.792  -19.031 9.650   1.00   77.01  ? 213  ASP A CA  1 
ATOM   3913 C C   . ASP B 1 213 ? 53.866  -18.428 10.703  1.00   77.12  ? 213  ASP A C   1 
ATOM   3914 O O   . ASP B 1 213 ? 54.322  -17.991 11.764  1.00   77.49  ? 213  ASP A O   1 
ATOM   3915 C CB  . ASP B 1 213 ? 56.239  -18.581 9.920   1.00   77.64  ? 213  ASP A CB  1 
ATOM   3916 C CG  . ASP B 1 213 ? 57.235  -19.153 8.927   1.00   78.78  ? 213  ASP A CG  1 
ATOM   3917 O OD1 . ASP B 1 213 ? 58.304  -18.531 8.754   1.00   79.97  ? 213  ASP A OD1 1 
ATOM   3918 O OD2 . ASP B 1 213 ? 56.962  -20.213 8.320   1.00   79.23  ? 213  ASP A OD2 1 
ATOM   3919 N N   . ARG B 1 214 ? 52.572  -18.397 10.412  0.73   76.54  ? 214  ARG A N   1 
ATOM   3920 C CA  . ARG B 1 214 ? 51.603  -17.864 11.366  0.73   75.70  ? 214  ARG A CA  1 
ATOM   3921 C C   . ARG B 1 214 ? 50.259  -18.572 11.259  0.73   75.52  ? 214  ARG A C   1 
ATOM   3922 O O   . ARG B 1 214 ? 49.870  -19.022 10.178  0.73   75.25  ? 214  ARG A O   1 
ATOM   3923 C CB  . ARG B 1 214 ? 51.460  -16.338 11.222  0.73   75.43  ? 214  ARG A CB  1 
ATOM   3924 C CG  . ARG B 1 214 ? 51.314  -15.835 9.792   0.73   74.56  ? 214  ARG A CG  1 
ATOM   3925 C CD  . ARG B 1 214 ? 51.734  -14.373 9.626   0.73   72.45  ? 214  ARG A CD  1 
ATOM   3926 N NE  . ARG B 1 214 ? 50.921  -13.469 10.436  0.73   70.32  ? 214  ARG A NE  1 
ATOM   3927 C CZ  . ARG B 1 214 ? 51.395  -12.665 11.384  0.73   69.62  ? 214  ARG A CZ  1 
ATOM   3928 N NH1 . ARG B 1 214 ? 52.696  -12.628 11.652  0.73   69.34  ? 214  ARG A NH1 1 
ATOM   3929 N NH2 . ARG B 1 214 ? 50.562  -11.888 12.066  0.73   68.56  ? 214  ARG A NH2 1 
ATOM   3930 N N   . VAL B 1 215 ? 49.577  -18.701 12.394  1.00   75.57  ? 215  VAL A N   1 
ATOM   3931 C CA  . VAL B 1 215 ? 48.254  -19.316 12.432  1.00   75.38  ? 215  VAL A CA  1 
ATOM   3932 C C   . VAL B 1 215 ? 47.310  -18.541 11.517  1.00   73.82  ? 215  VAL A C   1 
ATOM   3933 O O   . VAL B 1 215 ? 47.235  -17.316 11.585  1.00   73.94  ? 215  VAL A O   1 
ATOM   3934 C CB  . VAL B 1 215 ? 47.687  -19.375 13.873  1.00   75.97  ? 215  VAL A CB  1 
ATOM   3935 C CG1 . VAL B 1 215 ? 46.233  -19.839 13.872  1.00   76.26  ? 215  VAL A CG1 1 
ATOM   3936 C CG2 . VAL B 1 215 ? 48.523  -20.309 14.724  1.00   76.49  ? 215  VAL A CG2 1 
ATOM   3937 N N   . ALA B 1 216 ? 46.614  -19.262 10.646  1.00   71.02  ? 216  ALA A N   1 
ATOM   3938 C CA  . ALA B 1 216 ? 45.680  -18.641 9.714   1.00   68.77  ? 216  ALA A CA  1 
ATOM   3939 C C   . ALA B 1 216 ? 44.236  -19.013 10.035  1.00   67.25  ? 216  ALA A C   1 
ATOM   3940 O O   . ALA B 1 216 ? 43.892  -20.193 10.104  1.00   67.03  ? 216  ALA A O   1 
ATOM   3941 C CB  . ALA B 1 216 ? 46.029  -19.013 8.280   1.00   68.44  ? 216  ALA A CB  1 
ATOM   3942 N N   . ILE B 1 217 ? 43.400  -17.999 10.234  1.00   65.95  ? 217  ILE A N   1 
ATOM   3943 C CA  . ILE B 1 217 ? 41.992  -18.214 10.555  1.00   64.87  ? 217  ILE A CA  1 
ATOM   3944 C C   . ILE B 1 217 ? 41.097  -17.743 9.415   1.00   64.27  ? 217  ILE A C   1 
ATOM   3945 O O   . ILE B 1 217 ? 40.968  -16.541 9.173   1.00   64.09  ? 217  ILE A O   1 
ATOM   3946 C CB  . ILE B 1 217 ? 41.579  -17.499 11.864  1.00   64.91  ? 217  ILE A CB  1 
ATOM   3947 C CG1 . ILE B 1 217 ? 42.631  -17.717 12.959  1.00   64.28  ? 217  ILE A CG1 1 
ATOM   3948 C CG2 . ILE B 1 217 ? 40.193  -17.960 12.305  1.00   64.49  ? 217  ILE A CG2 1 
ATOM   3949 C CD1 . ILE B 1 217 ? 42.522  -16.752 14.122  1.00   63.62  ? 217  ILE A CD1 1 
ATOM   3950 N N   . LEU B 1 218 ? 40.495  -18.697 8.711   1.00   63.60  ? 218  LEU A N   1 
ATOM   3951 C CA  . LEU B 1 218 ? 39.511  -18.389 7.681   1.00   63.38  ? 218  LEU A CA  1 
ATOM   3952 C C   . LEU B 1 218 ? 38.203  -17.989 8.329   1.00   63.85  ? 218  LEU A C   1 
ATOM   3953 O O   . LEU B 1 218 ? 37.596  -18.772 9.063   1.00   63.76  ? 218  LEU A O   1 
ATOM   3954 C CB  . LEU B 1 218 ? 39.276  -19.584 6.762   1.00   63.04  ? 218  LEU A CB  1 
ATOM   3955 C CG  . LEU B 1 218 ? 40.168  -19.712 5.532   1.00   62.97  ? 218  LEU A CG  1 
ATOM   3956 C CD1 . LEU B 1 218 ? 40.168  -21.150 5.040   1.00   62.73  ? 218  LEU A CD1 1 
ATOM   3957 C CD2 . LEU B 1 218 ? 39.719  -18.757 4.434   1.00   62.72  ? 218  LEU A CD2 1 
ATOM   3958 N N   . VAL B 1 219 ? 37.776  -16.760 8.066   1.00   64.50  ? 219  VAL A N   1 
ATOM   3959 C CA  . VAL B 1 219 ? 36.527  -16.265 8.622   1.00   65.41  ? 219  VAL A CA  1 
ATOM   3960 C C   . VAL B 1 219 ? 35.542  -15.951 7.504   1.00   65.92  ? 219  VAL A C   1 
ATOM   3961 O O   . VAL B 1 219 ? 35.866  -15.229 6.560   1.00   66.01  ? 219  VAL A O   1 
ATOM   3962 C CB  . VAL B 1 219 ? 36.741  -15.029 9.529   1.00   65.36  ? 219  VAL A CB  1 
ATOM   3963 C CG1 . VAL B 1 219 ? 35.408  -14.516 10.061  1.00   65.49  ? 219  VAL A CG1 1 
ATOM   3964 C CG2 . VAL B 1 219 ? 37.658  -15.382 10.691  1.00   65.42  ? 219  VAL A CG2 1 
ATOM   3965 N N   . ASP B 1 220 ? 34.346  -16.517 7.614   1.00   66.43  ? 220  ASP A N   1 
ATOM   3966 C CA  . ASP B 1 220 ? 33.284  -16.270 6.652   1.00   67.19  ? 220  ASP A CA  1 
ATOM   3967 C C   . ASP B 1 220 ? 31.926  -16.254 7.351   1.00   67.70  ? 220  ASP A C   1 
ATOM   3968 O O   . ASP B 1 220 ? 31.763  -16.854 8.413   1.00   67.57  ? 220  ASP A O   1 
ATOM   3969 C CB  . ASP B 1 220 ? 33.313  -17.328 5.550   1.00   67.09  ? 220  ASP A CB  1 
ATOM   3970 C CG  . ASP B 1 220 ? 32.622  -16.871 4.284   1.00   68.17  ? 220  ASP A CG  1 
ATOM   3971 O OD1 . ASP B 1 220 ? 32.492  -15.643 4.079   1.00   68.19  ? 220  ASP A OD1 1 
ATOM   3972 O OD2 . ASP B 1 220 ? 32.216  -17.742 3.485   1.00   69.67  ? 220  ASP A OD2 1 
ATOM   3973 N N   . ASP B 1 221 ? 30.954  -15.561 6.765   1.00   68.68  ? 221  ASP A N   1 
ATOM   3974 C CA  . ASP B 1 221 ? 29.630  -15.463 7.379   1.00   69.95  ? 221  ASP A CA  1 
ATOM   3975 C C   . ASP B 1 221 ? 28.892  -16.798 7.334   1.00   71.18  ? 221  ASP A C   1 
ATOM   3976 O O   . ASP B 1 221 ? 28.130  -17.122 8.249   1.00   71.17  ? 221  ASP A O   1 
ATOM   3977 C CB  . ASP B 1 221 ? 28.796  -14.353 6.731   1.00   69.75  ? 221  ASP A CB  1 
ATOM   3978 C CG  . ASP B 1 221 ? 28.426  -14.656 5.285   1.00   69.75  ? 221  ASP A CG  1 
ATOM   3979 O OD1 . ASP B 1 221 ? 27.224  -14.560 4.961   1.00   70.20  ? 221  ASP A OD1 1 
ATOM   3980 O OD2 . ASP B 1 221 ? 29.324  -14.993 4.479   1.00   69.57  ? 221  ASP A OD2 1 
ATOM   3981 N N   . MET B 1 222 ? 29.133  -17.564 6.270   1.00   73.09  ? 222  MET A N   1 
ATOM   3982 C CA  . MET B 1 222 ? 28.519  -18.877 6.091   1.00   75.02  ? 222  MET A CA  1 
ATOM   3983 C C   . MET B 1 222 ? 29.310  -19.771 5.145   1.00   75.78  ? 222  MET A C   1 
ATOM   3984 O O   . MET B 1 222 ? 30.025  -19.287 4.269   1.00   75.96  ? 222  MET A O   1 
ATOM   3985 C CB  . MET B 1 222 ? 27.074  -18.748 5.598   1.00   75.38  ? 222  MET A CB  1 
ATOM   3986 C CG  . MET B 1 222 ? 26.913  -18.121 4.217   1.00   76.57  ? 222  MET A CG  1 
ATOM   3987 S SD  . MET B 1 222 ? 25.182  -18.158 3.707   1.00   79.69  ? 222  MET A SD  1 
ATOM   3988 C CE  . MET B 1 222 ? 24.489  -16.790 4.644   1.00   78.62  ? 222  MET A CE  1 
ATOM   3989 N N   . ALA B 1 223 ? 29.169  -21.079 5.339   1.00   76.71  ? 223  ALA A N   1 
ATOM   3990 C CA  . ALA B 1 223 ? 29.775  -22.076 4.462   1.00   77.91  ? 223  ALA A CA  1 
ATOM   3991 C C   . ALA B 1 223 ? 28.755  -23.161 4.175   1.00   79.16  ? 223  ALA A C   1 
ATOM   3992 O O   . ALA B 1 223 ? 28.150  -23.723 5.095   1.00   79.09  ? 223  ALA A O   1 
ATOM   3993 C CB  . ALA B 1 223 ? 31.011  -22.670 5.090   1.00   77.51  ? 223  ALA A CB  1 
ATOM   3994 N N   . ASP B 1 224 ? 28.565  -23.442 2.891   1.00   81.10  ? 224  ASP A N   1 
ATOM   3995 C CA  . ASP B 1 224 ? 27.550  -24.389 2.457   1.00   82.92  ? 224  ASP A CA  1 
ATOM   3996 C C   . ASP B 1 224 ? 28.143  -25.747 2.109   1.00   83.85  ? 224  ASP A C   1 
ATOM   3997 O O   . ASP B 1 224 ? 28.033  -26.695 2.882   1.00   84.19  ? 224  ASP A O   1 
ATOM   3998 C CB  . ASP B 1 224 ? 26.782  -23.834 1.256   1.00   83.04  ? 224  ASP A CB  1 
ATOM   3999 C CG  . ASP B 1 224 ? 25.486  -24.578 1.004   1.00   83.28  ? 224  ASP A CG  1 
ATOM   4000 O OD1 . ASP B 1 224 ? 25.247  -25.621 1.649   1.00   83.10  ? 224  ASP A OD1 1 
ATOM   4001 O OD2 . ASP B 1 224 ? 24.697  -24.108 0.158   1.00   83.52  ? 224  ASP A OD2 1 
ATOM   4002 N N   . THR B 1 225 ? 28.747  -25.831 0.928   1.00   84.60  ? 225  THR A N   1 
ATOM   4003 C CA  . THR B 1 225 ? 29.366  -27.066 0.462   1.00   85.32  ? 225  THR A CA  1 
ATOM   4004 C C   . THR B 1 225 ? 30.813  -27.064 0.906   1.00   85.75  ? 225  THR A C   1 
ATOM   4005 O O   . THR B 1 225 ? 31.491  -28.094 0.871   1.00   85.84  ? 225  THR A O   1 
ATOM   4006 C CB  . THR B 1 225 ? 29.335  -27.180 -1.070  1.00   85.25  ? 225  THR A CB  1 
ATOM   4007 O OG1 . THR B 1 225 ? 30.158  -26.155 -1.641  1.00   85.38  ? 225  THR A OG1 1 
ATOM   4008 C CG2 . THR B 1 225 ? 27.922  -27.032 -1.597  1.00   85.34  ? 225  THR A CG2 1 
ATOM   4009 N N   . CYS B 1 226 ? 31.283  -25.880 1.293   1.00   86.24  ? 226  CYS A N   1 
ATOM   4010 C CA  . CYS B 1 226 ? 32.626  -25.698 1.821   1.00   86.67  ? 226  CYS A CA  1 
ATOM   4011 C C   . CYS B 1 226 ? 33.714  -25.903 0.769   1.00   87.30  ? 226  CYS A C   1 
ATOM   4012 O O   . CYS B 1 226 ? 34.891  -25.998 1.105   1.00   87.25  ? 226  CYS A O   1 
ATOM   4013 C CB  . CYS B 1 226 ? 32.849  -26.607 3.036   1.00   86.57  ? 226  CYS A CB  1 
ATOM   4014 S SG  . CYS B 1 226 ? 31.707  -26.267 4.383   1.00   85.27  ? 226  CYS A SG  1 
ATOM   4015 N N   . GLY B 1 227 ? 33.318  -25.954 -0.500  1.00   87.84  ? 227  GLY A N   1 
ATOM   4016 C CA  . GLY B 1 227 ? 34.272  -26.080 -1.601  1.00   90.69  ? 227  GLY A CA  1 
ATOM   4017 C C   . GLY B 1 227 ? 35.288  -24.956 -1.593  1.00   90.71  ? 227  GLY A C   1 
ATOM   4018 O O   . GLY B 1 227 ? 36.495  -25.192 -1.720  1.00   90.76  ? 227  GLY A O   1 
ATOM   4019 N N   . THR B 1 228 ? 34.789  -23.734 -1.430  1.00   86.33  ? 228  THR A N   1 
ATOM   4020 C CA  . THR B 1 228 ? 35.627  -22.542 -1.373  1.00   84.94  ? 228  THR A CA  1 
ATOM   4021 C C   . THR B 1 228 ? 36.474  -22.521 -0.104  1.00   85.26  ? 228  THR A C   1 
ATOM   4022 O O   . THR B 1 228 ? 37.674  -22.259 -0.170  1.00   84.62  ? 228  THR A O   1 
ATOM   4023 C CB  . THR B 1 228 ? 34.781  -21.252 -1.485  1.00   84.55  ? 228  THR A CB  1 
ATOM   4024 O OG1 . THR B 1 228 ? 34.120  -21.231 -2.756  1.00   84.07  ? 228  THR A OG1 1 
ATOM   4025 C CG2 . THR B 1 228 ? 35.653  -20.000 -1.355  1.00   83.61  ? 228  THR A CG2 1 
ATOM   4026 N N   . ILE B 1 229 ? 35.854  -22.813 1.040   1.00   86.51  ? 229  ILE A N   1 
ATOM   4027 C CA  . ILE B 1 229 ? 36.570  -22.821 2.317   1.00   87.97  ? 229  ILE A CA  1 
ATOM   4028 C C   . ILE B 1 229 ? 37.672  -23.888 2.355   1.00   88.70  ? 229  ILE A C   1 
ATOM   4029 O O   . ILE B 1 229 ? 38.709  -23.692 2.993   1.00   88.79  ? 229  ILE A O   1 
ATOM   4030 C CB  . ILE B 1 229 ? 35.610  -22.965 3.539   1.00   88.08  ? 229  ILE A CB  1 
ATOM   4031 C CG1 . ILE B 1 229 ? 36.238  -22.370 4.803   1.00   88.23  ? 229  ILE A CG1 1 
ATOM   4032 C CG2 . ILE B 1 229 ? 35.240  -24.410 3.803   1.00   88.05  ? 229  ILE A CG2 1 
ATOM   4033 C CD1 . ILE B 1 229 ? 35.903  -20.894 5.022   1.00   88.09  ? 229  ILE A CD1 1 
ATOM   4034 N N   . CYS B 1 230 ? 37.446  -25.000 1.653   1.00   89.44  ? 230  CYS A N   1 
ATOM   4035 C CA  . CYS B 1 230 ? 38.380  -26.127 1.648   1.00   90.32  ? 230  CYS A CA  1 
ATOM   4036 C C   . CYS B 1 230 ? 39.552  -25.932 0.693   1.00   91.24  ? 230  CYS A C   1 
ATOM   4037 O O   . CYS B 1 230 ? 40.680  -26.321 1.008   1.00   90.94  ? 230  CYS A O   1 
ATOM   4038 C CB  . CYS B 1 230 ? 37.656  -27.441 1.348   1.00   90.08  ? 230  CYS A CB  1 
ATOM   4039 S SG  . CYS B 1 230 ? 36.603  -28.013 2.706   1.00   90.49  ? 230  CYS A SG  1 
ATOM   4040 N N   . HIS B 1 231 ? 39.289  -25.343 -0.470  1.00   92.95  ? 231  HIS A N   1 
ATOM   4041 C CA  . HIS B 1 231 ? 40.368  -24.951 -1.370  1.00   94.57  ? 231  HIS A CA  1 
ATOM   4042 C C   . HIS B 1 231 ? 41.211  -23.865 -0.723  1.00   93.73  ? 231  HIS A C   1 
ATOM   4043 O O   . HIS B 1 231 ? 42.442  -23.898 -0.796  1.00   93.95  ? 231  HIS A O   1 
ATOM   4044 C CB  . HIS B 1 231 ? 39.828  -24.448 -2.707  1.00   95.74  ? 231  HIS A CB  1 
ATOM   4045 C CG  . HIS B 1 231 ? 39.322  -25.530 -3.604  1.00   99.69  ? 231  HIS A CG  1 
ATOM   4046 N ND1 . HIS B 1 231 ? 39.505  -26.869 -3.334  1.00   105.84 ? 231  HIS A ND1 1 
ATOM   4047 C CD2 . HIS B 1 231 ? 38.664  -25.470 -4.786  1.00   105.54 ? 231  HIS A CD2 1 
ATOM   4048 C CE1 . HIS B 1 231 ? 38.963  -27.589 -4.301  1.00   109.50 ? 231  HIS A CE1 1 
ATOM   4049 N NE2 . HIS B 1 231 ? 38.449  -26.764 -5.195  1.00   110.23 ? 231  HIS A NE2 1 
ATOM   4050 N N   . ALA B 1 232 ? 40.532  -22.907 -0.091  1.00   92.09  ? 232  ALA A N   1 
ATOM   4051 C CA  . ALA B 1 232 ? 41.184  -21.809 0.610   1.00   90.43  ? 232  ALA A CA  1 
ATOM   4052 C C   . ALA B 1 232 ? 42.227  -22.325 1.594   1.00   89.63  ? 232  ALA A C   1 
ATOM   4053 O O   . ALA B 1 232 ? 43.345  -21.808 1.646   1.00   89.34  ? 232  ALA A O   1 
ATOM   4054 C CB  . ALA B 1 232 ? 40.153  -20.953 1.325   1.00   90.26  ? 232  ALA A CB  1 
ATOM   4055 N N   . ALA B 1 233 ? 41.856  -23.352 2.356   1.00   89.15  ? 233  ALA A N   1 
ATOM   4056 C CA  . ALA B 1 233 ? 42.744  -23.963 3.343   1.00   88.84  ? 233  ALA A CA  1 
ATOM   4057 C C   . ALA B 1 233 ? 43.984  -24.582 2.701   1.00   88.50  ? 233  ALA A C   1 
ATOM   4058 O O   . ALA B 1 233 ? 45.073  -24.531 3.279   1.00   88.52  ? 233  ALA A O   1 
ATOM   4059 C CB  . ALA B 1 233 ? 41.995  -25.003 4.158   1.00   88.92  ? 233  ALA A CB  1 
ATOM   4060 N N   . ASP B 1 234 ? 43.810  -25.169 1.515   1.00   87.82  ? 234  ASP A N   1 
ATOM   4061 C CA  . ASP B 1 234 ? 44.927  -25.726 0.754   1.00   87.04  ? 234  ASP A CA  1 
ATOM   4062 C C   . ASP B 1 234 ? 45.928  -24.634 0.431   1.00   85.74  ? 234  ASP A C   1 
ATOM   4063 O O   . ASP B 1 234 ? 47.111  -24.748 0.765   1.00   85.74  ? 234  ASP A O   1 
ATOM   4064 C CB  . ASP B 1 234 ? 44.443  -26.377 -0.546  1.00   87.48  ? 234  ASP A CB  1 
ATOM   4065 C CG  . ASP B 1 234 ? 43.636  -27.640 -0.309  1.00   88.35  ? 234  ASP A CG  1 
ATOM   4066 O OD1 . ASP B 1 234 ? 43.813  -28.286 0.746   1.00   89.12  ? 234  ASP A OD1 1 
ATOM   4067 O OD2 . ASP B 1 234 ? 42.825  -27.996 -1.191  1.00   89.00  ? 234  ASP A OD2 1 
ATOM   4068 N N   . LYS B 1 235 ? 45.435  -23.577 -0.213  1.00   83.96  ? 235  LYS A N   1 
ATOM   4069 C CA  . LYS B 1 235 ? 46.255  -22.439 -0.599  1.00   82.17  ? 235  LYS A CA  1 
ATOM   4070 C C   . LYS B 1 235 ? 47.011  -21.882 0.604   1.00   80.99  ? 235  LYS A C   1 
ATOM   4071 O O   . LYS B 1 235 ? 48.210  -21.605 0.514   1.00   80.83  ? 235  LYS A O   1 
ATOM   4072 C CB  . LYS B 1 235 ? 45.384  -21.349 -1.232  1.00   82.26  ? 235  LYS A CB  1 
ATOM   4073 C CG  . LYS B 1 235 ? 45.948  -20.761 -2.524  1.00   82.21  ? 235  LYS A CG  1 
ATOM   4074 C CD  . LYS B 1 235 ? 47.146  -19.854 -2.273  1.00   82.26  ? 235  LYS A CD  1 
ATOM   4075 C CE  . LYS B 1 235 ? 47.797  -19.436 -3.586  1.00   82.29  ? 235  LYS A CE  1 
ATOM   4076 N NZ  . LYS B 1 235 ? 48.858  -18.412 -3.376  1.00   82.21  ? 235  LYS A NZ  1 
ATOM   4077 N N   . LEU B 1 236 ? 46.309  -21.736 1.727   1.00   79.55  ? 236  LEU A N   1 
ATOM   4078 C CA  . LEU B 1 236 ? 46.907  -21.195 2.943   1.00   78.38  ? 236  LEU A CA  1 
ATOM   4079 C C   . LEU B 1 236 ? 48.055  -22.054 3.471   1.00   78.25  ? 236  LEU A C   1 
ATOM   4080 O O   . LEU B 1 236 ? 49.085  -21.520 3.885   1.00   77.83  ? 236  LEU A O   1 
ATOM   4081 C CB  . LEU B 1 236 ? 45.849  -20.966 4.025   1.00   78.08  ? 236  LEU A CB  1 
ATOM   4082 C CG  . LEU B 1 236 ? 44.961  -19.726 3.866   1.00   77.46  ? 236  LEU A CG  1 
ATOM   4083 C CD1 . LEU B 1 236 ? 43.872  -19.729 4.914   1.00   76.57  ? 236  LEU A CD1 1 
ATOM   4084 C CD2 . LEU B 1 236 ? 45.774  -18.446 3.967   1.00   76.81  ? 236  LEU A CD2 1 
ATOM   4085 N N   . LEU B 1 237 ? 47.883  -23.374 3.441   1.00   78.58  ? 237  LEU A N   1 
ATOM   4086 C CA  . LEU B 1 237 ? 48.973  -24.285 3.787   1.00   79.23  ? 237  LEU A CA  1 
ATOM   4087 C C   . LEU B 1 237 ? 50.178  -24.068 2.883   1.00   79.69  ? 237  LEU A C   1 
ATOM   4088 O O   . LEU B 1 237 ? 51.295  -23.856 3.369   1.00   79.81  ? 237  LEU A O   1 
ATOM   4089 C CB  . LEU B 1 237 ? 48.527  -25.744 3.719   1.00   79.12  ? 237  LEU A CB  1 
ATOM   4090 C CG  . LEU B 1 237 ? 47.882  -26.362 4.961   1.00   79.24  ? 237  LEU A CG  1 
ATOM   4091 C CD1 . LEU B 1 237 ? 47.995  -27.876 4.859   1.00   79.60  ? 237  LEU A CD1 1 
ATOM   4092 C CD2 . LEU B 1 237 ? 48.525  -25.878 6.261   1.00   78.69  ? 237  LEU A CD2 1 
ATOM   4093 N N   . SER B 1 238 ? 49.933  -24.107 1.571   1.00   80.26  ? 238  SER A N   1 
ATOM   4094 C CA  . SER B 1 238 ? 50.956  -23.860 0.554   1.00   80.73  ? 238  SER A CA  1 
ATOM   4095 C C   . SER B 1 238 ? 51.724  -22.562 0.794   1.00   80.94  ? 238  SER A C   1 
ATOM   4096 O O   . SER B 1 238 ? 52.908  -22.465 0.464   1.00   81.11  ? 238  SER A O   1 
ATOM   4097 C CB  . SER B 1 238 ? 50.318  -23.811 -0.835  1.00   80.74  ? 238  SER A CB  1 
ATOM   4098 O OG  . SER B 1 238 ? 49.317  -24.804 -0.978  1.00   81.06  ? 238  SER A OG  1 
ATOM   4099 N N   . ALA B 1 239 ? 51.043  -21.572 1.367   1.00   81.11  ? 239  ALA A N   1 
ATOM   4100 C CA  . ALA B 1 239 ? 51.633  -20.258 1.600   1.00   81.33  ? 239  ALA A CA  1 
ATOM   4101 C C   . ALA B 1 239 ? 52.343  -20.165 2.954   1.00   81.73  ? 239  ALA A C   1 
ATOM   4102 O O   . ALA B 1 239 ? 52.798  -19.090 3.356   1.00   81.71  ? 239  ALA A O   1 
ATOM   4103 C CB  . ALA B 1 239 ? 50.576  -19.173 1.453   1.00   81.17  ? 239  ALA A CB  1 
ATOM   4104 N N   . GLY B 1 240 ? 52.432  -21.300 3.646   1.00   82.41  ? 240  GLY A N   1 
ATOM   4105 C CA  . GLY B 1 240 ? 53.237  -21.416 4.857   1.00   83.46  ? 240  GLY A CA  1 
ATOM   4106 C C   . GLY B 1 240 ? 52.504  -21.133 6.152   1.00   84.53  ? 240  GLY A C   1 
ATOM   4107 O O   . GLY B 1 240 ? 53.135  -20.812 7.164   1.00   84.23  ? 240  GLY A O   1 
ATOM   4108 N N   . ALA B 1 241 ? 51.176  -21.241 6.122   1.00   85.83  ? 241  ALA A N   1 
ATOM   4109 C CA  . ALA B 1 241 ? 50.373  -21.086 7.329   1.00   87.24  ? 241  ALA A CA  1 
ATOM   4110 C C   . ALA B 1 241 ? 50.767  -22.175 8.316   1.00   88.02  ? 241  ALA A C   1 
ATOM   4111 O O   . ALA B 1 241 ? 50.860  -23.348 7.944   1.00   88.20  ? 241  ALA A O   1 
ATOM   4112 C CB  . ALA B 1 241 ? 48.890  -21.173 7.004   1.00   87.27  ? 241  ALA A CB  1 
ATOM   4113 N N   . THR B 1 242 ? 51.024  -21.778 9.561   1.00   88.61  ? 242  THR A N   1 
ATOM   4114 C CA  . THR B 1 242 ? 51.358  -22.727 10.619  1.00   88.91  ? 242  THR A CA  1 
ATOM   4115 C C   . THR B 1 242 ? 50.234  -23.750 10.750  1.00   88.16  ? 242  THR A C   1 
ATOM   4116 O O   . THR B 1 242 ? 50.442  -24.950 10.553  1.00   88.41  ? 242  THR A O   1 
ATOM   4117 C CB  . THR B 1 242 ? 51.594  -22.014 11.971  1.00   89.16  ? 242  THR A CB  1 
ATOM   4118 O OG1 . THR B 1 242 ? 52.718  -21.131 11.855  1.00   89.59  ? 242  THR A OG1 1 
ATOM   4119 C CG2 . THR B 1 242 ? 51.870  -23.027 13.083  1.00   89.48  ? 242  THR A CG2 1 
ATOM   4120 N N   . ARG B 1 243 ? 49.044  -23.252 11.072  1.00   86.56  ? 243  ARG A N   1 
ATOM   4121 C CA  . ARG B 1 243 ? 47.837  -24.059 11.177  1.00   84.34  ? 243  ARG A CA  1 
ATOM   4122 C C   . ARG B 1 243 ? 46.683  -23.215 10.653  1.00   81.43  ? 243  ARG A C   1 
ATOM   4123 O O   . ARG B 1 243 ? 46.719  -21.985 10.739  1.00   81.39  ? 243  ARG A O   1 
ATOM   4124 C CB  . ARG B 1 243 ? 47.586  -24.471 12.633  1.00   85.11  ? 243  ARG A CB  1 
ATOM   4125 C CG  . ARG B 1 243 ? 48.726  -25.277 13.263  1.00   86.75  ? 243  ARG A CG  1 
ATOM   4126 C CD  . ARG B 1 243 ? 48.579  -25.476 14.767  1.00   88.89  ? 243  ARG A CD  1 
ATOM   4127 N NE  . ARG B 1 243 ? 48.498  -24.218 15.510  1.00   90.07  ? 243  ARG A NE  1 
ATOM   4128 C CZ  . ARG B 1 243 ? 47.504  -23.905 16.337  1.00   90.57  ? 243  ARG A CZ  1 
ATOM   4129 N NH1 . ARG B 1 243 ? 46.514  -24.763 16.537  1.00   90.88  ? 243  ARG A NH1 1 
ATOM   4130 N NH2 . ARG B 1 243 ? 47.496  -22.745 16.973  1.00   90.19  ? 243  ARG A NH2 1 
ATOM   4131 N N   . VAL B 1 244 ? 45.664  -23.872 10.110  1.00   77.13  ? 244  VAL A N   1 
ATOM   4132 C CA  . VAL B 1 244 ? 44.521  -23.165 9.541   1.00   73.17  ? 244  VAL A CA  1 
ATOM   4133 C C   . VAL B 1 244 ? 43.229  -23.457 10.311  1.00   70.54  ? 244  VAL A C   1 
ATOM   4134 O O   . VAL B 1 244 ? 42.901  -24.617 10.569  1.00   70.00  ? 244  VAL A O   1 
ATOM   4135 C CB  . VAL B 1 244 ? 44.354  -23.477 8.023   1.00   73.23  ? 244  VAL A CB  1 
ATOM   4136 C CG1 . VAL B 1 244 ? 44.124  -24.966 7.782   1.00   73.27  ? 244  VAL A CG1 1 
ATOM   4137 C CG2 . VAL B 1 244 ? 43.233  -22.647 7.410   1.00   73.18  ? 244  VAL A CG2 1 
ATOM   4138 N N   . TYR B 1 245 ? 42.513  -22.403 10.692  0.66   67.40  ? 245  TYR A N   1 
ATOM   4139 C CA  . TYR B 1 245 ? 41.183  -22.562 11.272  0.66   65.07  ? 245  TYR A CA  1 
ATOM   4140 C C   . TYR B 1 245 ? 40.144  -21.963 10.334  0.66   64.14  ? 245  TYR A C   1 
ATOM   4141 O O   . TYR B 1 245 ? 40.456  -21.083 9.531   0.66   63.24  ? 245  TYR A O   1 
ATOM   4142 C CB  . TYR B 1 245 ? 41.085  -21.873 12.635  0.66   64.81  ? 245  TYR A CB  1 
ATOM   4143 C CG  . TYR B 1 245 ? 41.909  -22.488 13.746  0.66   64.72  ? 245  TYR A CG  1 
ATOM   4144 C CD1 . TYR B 1 245 ? 43.294  -22.317 13.795  0.66   64.66  ? 245  TYR A CD1 1 
ATOM   4145 C CD2 . TYR B 1 245 ? 41.297  -23.206 14.771  0.66   64.79  ? 245  TYR A CD2 1 
ATOM   4146 C CE1 . TYR B 1 245 ? 44.051  -22.866 14.822  0.66   65.07  ? 245  TYR A CE1 1 
ATOM   4147 C CE2 . TYR B 1 245 ? 42.041  -23.756 15.804  0.66   65.02  ? 245  TYR A CE2 1 
ATOM   4148 C CZ  . TYR B 1 245 ? 43.416  -23.582 15.825  0.66   65.39  ? 245  TYR A CZ  1 
ATOM   4149 O OH  . TYR B 1 245 ? 44.150  -24.129 16.851  0.66   65.63  ? 245  TYR A OH  1 
ATOM   4150 N N   . ALA B 1 246 ? 38.910  -22.445 10.440  1.00   63.83  ? 246  ALA A N   1 
ATOM   4151 C CA  . ALA B 1 246 ? 37.787  -21.851 9.722   1.00   63.93  ? 246  ALA A CA  1 
ATOM   4152 C C   . ALA B 1 246 ? 36.701  -21.442 10.711  1.00   64.18  ? 246  ALA A C   1 
ATOM   4153 O O   . ALA B 1 246 ? 36.220  -22.269 11.488  1.00   64.07  ? 246  ALA A O   1 
ATOM   4154 C CB  . ALA B 1 246 ? 37.237  -22.818 8.689   1.00   63.72  ? 246  ALA A CB  1 
ATOM   4155 N N   . ILE B 1 247 ? 36.334  -20.163 10.701  1.00   64.70  ? 247  ILE A N   1 
ATOM   4156 C CA  . ILE B 1 247 ? 35.240  -19.679 11.542  1.00   65.57  ? 247  ILE A CA  1 
ATOM   4157 C C   . ILE B 1 247 ? 34.093  -19.137 10.697  1.00   67.08  ? 247  ILE A C   1 
ATOM   4158 O O   . ILE B 1 247 ? 34.267  -18.213 9.896   1.00   66.86  ? 247  ILE A O   1 
ATOM   4159 C CB  . ILE B 1 247 ? 35.698  -18.621 12.567  1.00   65.18  ? 247  ILE A CB  1 
ATOM   4160 C CG1 . ILE B 1 247 ? 36.834  -19.182 13.427  1.00   64.56  ? 247  ILE A CG1 1 
ATOM   4161 C CG2 . ILE B 1 247 ? 34.520  -18.193 13.441  1.00   64.82  ? 247  ILE A CG2 1 
ATOM   4162 C CD1 . ILE B 1 247 ? 37.268  -18.284 14.555  1.00   64.72  ? 247  ILE A CD1 1 
ATOM   4163 N N   . LEU B 1 248 ? 32.925  -19.740 10.879  1.00   69.23  ? 248  LEU A N   1 
ATOM   4164 C CA  . LEU B 1 248 ? 31.728  -19.374 10.141  1.00   71.09  ? 248  LEU A CA  1 
ATOM   4165 C C   . LEU B 1 248 ? 30.604  -19.206 11.140  1.00   72.25  ? 248  LEU A C   1 
ATOM   4166 O O   . LEU B 1 248 ? 30.421  -20.052 12.014  1.00   71.46  ? 248  LEU A O   1 
ATOM   4167 C CB  . LEU B 1 248 ? 31.368  -20.475 9.145   1.00   71.71  ? 248  LEU A CB  1 
ATOM   4168 C CG  . LEU B 1 248 ? 32.559  -21.162 8.473   1.00   72.97  ? 248  LEU A CG  1 
ATOM   4169 C CD1 . LEU B 1 248 ? 32.315  -22.650 8.312   1.00   73.72  ? 248  LEU A CD1 1 
ATOM   4170 C CD2 . LEU B 1 248 ? 32.902  -20.495 7.154   1.00   73.80  ? 248  LEU A CD2 1 
ATOM   4171 N N   . THR B 1 249 ? 29.857  -18.115 11.035  1.00   70.12  ? 249  THR A N   1 
ATOM   4172 C CA  . THR B 1 249 ? 28.731  -17.923 11.942  1.00   68.97  ? 249  THR A CA  1 
ATOM   4173 C C   . THR B 1 249 ? 27.549  -18.820 11.563  1.00   68.14  ? 249  THR A C   1 
ATOM   4174 O O   . THR B 1 249 ? 26.887  -19.387 12.437  1.00   67.88  ? 249  THR A O   1 
ATOM   4175 C CB  . THR B 1 249 ? 28.326  -16.434 12.090  1.00   68.91  ? 249  THR A CB  1 
ATOM   4176 O OG1 . THR B 1 249 ? 26.928  -16.278 11.809  1.00   69.19  ? 249  THR A OG1 1 
ATOM   4177 C CG2 . THR B 1 249 ? 29.131  -15.547 11.145  1.00   69.00  ? 249  THR A CG2 1 
ATOM   4178 N N   . HIS B 1 250 ? 27.311  -18.969 10.262  1.00   67.30  ? 250  HIS A N   1 
ATOM   4179 C CA  . HIS B 1 250 ? 26.275  -19.877 9.775   1.00   66.76  ? 250  HIS A CA  1 
ATOM   4180 C C   . HIS B 1 250 ? 26.908  -21.110 9.151   1.00   67.43  ? 250  HIS A C   1 
ATOM   4181 O O   . HIS B 1 250 ? 27.533  -21.033 8.094   1.00   67.34  ? 250  HIS A O   1 
ATOM   4182 C CB  . HIS B 1 250 ? 25.340  -19.181 8.775   1.00   65.99  ? 250  HIS A CB  1 
ATOM   4183 C CG  . HIS B 1 250 ? 24.777  -17.887 9.277   1.00   63.90  ? 250  HIS A CG  1 
ATOM   4184 N ND1 . HIS B 1 250 ? 23.985  -17.811 10.403  1.00   61.61  ? 250  HIS A ND1 1 
ATOM   4185 C CD2 . HIS B 1 250 ? 24.895  -16.620 8.813   1.00   61.70  ? 250  HIS A CD2 1 
ATOM   4186 C CE1 . HIS B 1 250 ? 23.644  -16.552 10.614  1.00   60.45  ? 250  HIS A CE1 1 
ATOM   4187 N NE2 . HIS B 1 250 ? 24.183  -15.809 9.663   1.00   61.43  ? 250  HIS A NE2 1 
ATOM   4188 N N   . GLY B 1 251 ? 26.752  -22.246 9.824   1.00   68.46  ? 251  GLY A N   1 
ATOM   4189 C CA  . GLY B 1 251 ? 27.281  -23.513 9.331   1.00   69.88  ? 251  GLY A CA  1 
ATOM   4190 C C   . GLY B 1 251 ? 26.093  -24.183 8.676   1.00   71.01  ? 251  GLY A C   1 
ATOM   4191 O O   . GLY B 1 251 ? 25.258  -24.791 9.354   1.00   70.86  ? 251  GLY A O   1 
ATOM   4192 N N   . ILE B 1 252 ? 26.013  -24.073 7.353   1.00   72.26  ? 252  ILE A N   1 
ATOM   4193 C CA  . ILE B 1 252 ? 25.015  -24.804 6.576   1.00   73.76  ? 252  ILE A CA  1 
ATOM   4194 C C   . ILE B 1 252 ? 25.485  -26.235 6.280   1.00   75.00  ? 252  ILE A C   1 
ATOM   4195 O O   . ILE B 1 252 ? 24.731  -27.192 6.485   1.00   75.08  ? 252  ILE A O   1 
ATOM   4196 C CB  . ILE B 1 252 ? 24.624  -24.055 5.285   1.00   73.69  ? 252  ILE A CB  1 
ATOM   4197 C CG1 . ILE B 1 252 ? 24.309  -22.585 5.599   1.00   73.98  ? 252  ILE A CG1 1 
ATOM   4198 C CG2 . ILE B 1 252 ? 23.438  -24.739 4.624   1.00   73.36  ? 252  ILE A CG2 1 
ATOM   4199 C CD1 . ILE B 1 252 ? 24.030  -21.708 4.381   1.00   74.56  ? 252  ILE A CD1 1 
ATOM   4200 N N   . PHE B 1 253 ? 26.722  -26.369 5.806   1.00   76.69  ? 253  PHE A N   1 
ATOM   4201 C CA  . PHE B 1 253 ? 27.372  -27.673 5.652   1.00   78.47  ? 253  PHE A CA  1 
ATOM   4202 C C   . PHE B 1 253 ? 26.523  -28.729 4.935   1.00   79.88  ? 253  PHE A C   1 
ATOM   4203 O O   . PHE B 1 253 ? 26.327  -29.826 5.458   1.00   80.03  ? 253  PHE A O   1 
ATOM   4204 C CB  . PHE B 1 253 ? 27.802  -28.235 7.017   1.00   78.33  ? 253  PHE A CB  1 
ATOM   4205 C CG  . PHE B 1 253 ? 28.762  -27.368 7.769   1.00   77.98  ? 253  PHE A CG  1 
ATOM   4206 C CD1 . PHE B 1 253 ? 28.646  -27.227 9.145   1.00   77.91  ? 253  PHE A CD1 1 
ATOM   4207 C CD2 . PHE B 1 253 ? 29.790  -26.706 7.112   1.00   77.85  ? 253  PHE A CD2 1 
ATOM   4208 C CE1 . PHE B 1 253 ? 29.539  -26.435 9.854   1.00   77.97  ? 253  PHE A CE1 1 
ATOM   4209 C CE2 . PHE B 1 253 ? 30.684  -25.908 7.809   1.00   77.78  ? 253  PHE A CE2 1 
ATOM   4210 C CZ  . PHE B 1 253 ? 30.562  -25.773 9.181   1.00   77.50  ? 253  PHE A CZ  1 
ATOM   4211 N N   . SER B 1 254 ? 26.024  -28.414 3.747   1.00   81.65  ? 254  SER A N   1 
ATOM   4212 C CA  . SER B 1 254 ? 25.250  -29.399 2.997   1.00   83.56  ? 254  SER A CA  1 
ATOM   4213 C C   . SER B 1 254 ? 26.072  -30.032 1.875   1.00   85.16  ? 254  SER A C   1 
ATOM   4214 O O   . SER B 1 254 ? 27.089  -29.480 1.447   1.00   85.25  ? 254  SER A O   1 
ATOM   4215 C CB  . SER B 1 254 ? 23.959  -28.787 2.452   1.00   83.34  ? 254  SER A CB  1 
ATOM   4216 O OG  . SER B 1 254 ? 24.230  -27.888 1.397   1.00   82.91  ? 254  SER A OG  1 
ATOM   4217 N N   . GLY B 1 255 ? 25.616  -31.192 1.407   1.00   87.05  ? 255  GLY A N   1 
ATOM   4218 C CA  . GLY B 1 255 ? 26.293  -31.930 0.345   1.00   89.21  ? 255  GLY A CA  1 
ATOM   4219 C C   . GLY B 1 255 ? 27.586  -32.565 0.824   1.00   90.58  ? 255  GLY A C   1 
ATOM   4220 O O   . GLY B 1 255 ? 27.605  -33.222 1.868   1.00   90.76  ? 255  GLY A O   1 
ATOM   4221 N N   . PRO B 1 256 ? 28.681  -32.365 0.063   1.00   91.39  ? 256  PRO A N   1 
ATOM   4222 C CA  . PRO B 1 256 ? 30.004  -32.914 0.368   1.00   91.59  ? 256  PRO A CA  1 
ATOM   4223 C C   . PRO B 1 256 ? 30.717  -32.158 1.482   1.00   91.30  ? 256  PRO A C   1 
ATOM   4224 O O   . PRO B 1 256 ? 31.836  -32.520 1.856   1.00   91.40  ? 256  PRO A O   1 
ATOM   4225 C CB  . PRO B 1 256 ? 30.760  -32.722 -0.948  1.00   91.84  ? 256  PRO A CB  1 
ATOM   4226 C CG  . PRO B 1 256 ? 30.147  -31.504 -1.543  1.00   91.83  ? 256  PRO A CG  1 
ATOM   4227 C CD  . PRO B 1 256 ? 28.698  -31.537 -1.158  1.00   91.53  ? 256  PRO A CD  1 
ATOM   4228 N N   . ALA B 1 257 ? 30.064  -31.121 2.001   1.00   90.62  ? 257  ALA A N   1 
ATOM   4229 C CA  . ALA B 1 257 ? 30.663  -30.217 2.973   1.00   90.48  ? 257  ALA A CA  1 
ATOM   4230 C C   . ALA B 1 257 ? 31.398  -30.946 4.082   1.00   91.28  ? 257  ALA A C   1 
ATOM   4231 O O   . ALA B 1 257 ? 32.601  -30.750 4.259   1.00   91.01  ? 257  ALA A O   1 
ATOM   4232 C CB  . ALA B 1 257 ? 29.614  -29.293 3.555   1.00   89.76  ? 257  ALA A CB  1 
ATOM   4233 N N   . ILE B 1 258 ? 30.674  -31.802 4.801   1.00   93.42  ? 258  ILE A N   1 
ATOM   4234 C CA  . ILE B 1 258 ? 31.196  -32.474 5.994   1.00   95.85  ? 258  ILE A CA  1 
ATOM   4235 C C   . ILE B 1 258 ? 32.400  -33.382 5.718   1.00   97.54  ? 258  ILE A C   1 
ATOM   4236 O O   . ILE B 1 258 ? 33.321  -33.461 6.538   1.00   97.74  ? 258  ILE A O   1 
ATOM   4237 C CB  . ILE B 1 258 ? 30.075  -33.239 6.755   1.00   95.76  ? 258  ILE A CB  1 
ATOM   4238 C CG1 . ILE B 1 258 ? 29.080  -32.254 7.388   1.00   95.67  ? 258  ILE A CG1 1 
ATOM   4239 C CG2 . ILE B 1 258 ? 30.647  -34.185 7.813   1.00   95.99  ? 258  ILE A CG2 1 
ATOM   4240 C CD1 . ILE B 1 258 ? 29.701  -31.248 8.370   1.00   95.25  ? 258  ILE A CD1 1 
ATOM   4241 N N   . SER B 1 259 ? 32.396  -34.053 4.566   1.00   99.50  ? 259  SER A N   1 
ATOM   4242 C CA  . SER B 1 259 ? 33.501  -34.937 4.196   1.00   101.19 ? 259  SER A CA  1 
ATOM   4243 C C   . SER B 1 259 ? 34.743  -34.145 3.795   1.00   101.94 ? 259  SER A C   1 
ATOM   4244 O O   . SER B 1 259 ? 35.851  -34.464 4.234   1.00   102.13 ? 259  SER A O   1 
ATOM   4245 C CB  . SER B 1 259 ? 33.088  -35.909 3.084   1.00   101.30 ? 259  SER A CB  1 
ATOM   4246 O OG  . SER B 1 259 ? 32.903  -35.243 1.842   1.00   101.48 ? 259  SER A OG  1 
ATOM   4247 N N   . ARG B 1 260 ? 34.547  -33.116 2.970   1.00   102.49 ? 260  ARG A N   1 
ATOM   4248 C CA  . ARG B 1 260 ? 35.627  -32.222 2.550   1.00   102.61 ? 260  ARG A CA  1 
ATOM   4249 C C   . ARG B 1 260 ? 36.348  -31.626 3.759   1.00   102.11 ? 260  ARG A C   1 
ATOM   4250 O O   . ARG B 1 260 ? 37.561  -31.418 3.724   1.00   102.14 ? 260  ARG A O   1 
ATOM   4251 C CB  . ARG B 1 260 ? 35.080  -31.094 1.672   1.00   102.93 ? 260  ARG A CB  1 
ATOM   4252 C CG  . ARG B 1 260 ? 34.590  -31.528 0.298   1.00   103.52 ? 260  ARG A CG  1 
ATOM   4253 C CD  . ARG B 1 260 ? 33.904  -30.364 -0.408  1.00   104.52 ? 260  ARG A CD  1 
ATOM   4254 N NE  . ARG B 1 260 ? 33.550  -30.687 -1.788  1.00   105.32 ? 260  ARG A NE  1 
ATOM   4255 C CZ  . ARG B 1 260 ? 32.885  -29.878 -2.612  1.00   105.76 ? 260  ARG A CZ  1 
ATOM   4256 N NH1 . ARG B 1 260 ? 32.475  -28.683 -2.204  1.00   105.98 ? 260  ARG A NH1 1 
ATOM   4257 N NH2 . ARG B 1 260 ? 32.614  -30.273 -3.849  1.00   105.72 ? 260  ARG A NH2 1 
ATOM   4258 N N   . ILE B 1 261 ? 35.587  -31.368 4.821   1.00   101.29 ? 261  ILE A N   1 
ATOM   4259 C CA  . ILE B 1 261 ? 36.113  -30.784 6.053   1.00   100.76 ? 261  ILE A CA  1 
ATOM   4260 C C   . ILE B 1 261 ? 37.118  -31.703 6.752   1.00   101.80 ? 261  ILE A C   1 
ATOM   4261 O O   . ILE B 1 261 ? 38.214  -31.263 7.110   1.00   101.70 ? 261  ILE A O   1 
ATOM   4262 C CB  . ILE B 1 261 ? 34.976  -30.370 7.018   1.00   100.11 ? 261  ILE A CB  1 
ATOM   4263 C CG1 . ILE B 1 261 ? 34.190  -29.193 6.425   1.00   99.38  ? 261  ILE A CG1 1 
ATOM   4264 C CG2 . ILE B 1 261 ? 35.546  -29.969 8.367   1.00   99.66  ? 261  ILE A CG2 1 
ATOM   4265 C CD1 . ILE B 1 261 ? 32.923  -28.815 7.196   1.00   98.70  ? 261  ILE A CD1 1 
ATOM   4266 N N   . ASN B 1 262 ? 36.743  -32.968 6.940   1.00   108.62 ? 262  ASN A N   1 
ATOM   4267 C CA  . ASN B 1 262 ? 37.661  -33.977 7.469   1.00   107.91 ? 262  ASN A CA  1 
ATOM   4268 C C   . ASN B 1 262 ? 38.857  -34.153 6.541   1.00   107.73 ? 262  ASN A C   1 
ATOM   4269 O O   . ASN B 1 262 ? 40.006  -34.198 6.989   1.00   105.13 ? 262  ASN A O   1 
ATOM   4270 C CB  . ASN B 1 262 ? 36.949  -35.320 7.652   1.00   105.51 ? 262  ASN A CB  1 
ATOM   4271 C CG  . ASN B 1 262 ? 35.765  -35.234 8.595   1.00   107.81 ? 262  ASN A CG  1 
ATOM   4272 O OD1 . ASN B 1 262 ? 35.891  -34.791 9.738   1.00   107.28 ? 262  ASN A OD1 1 
ATOM   4273 N ND2 . ASN B 1 262 ? 34.605  -35.669 8.121   1.00   108.24 ? 262  ASN A ND2 1 
ATOM   4274 N N   . ASN B 1 263 ? 38.564  -34.238 5.242   1.00   101.95 ? 263  ASN A N   1 
ATOM   4275 C CA  . ASN B 1 263 ? 39.577  -34.336 4.189   1.00   99.85  ? 263  ASN A CA  1 
ATOM   4276 C C   . ASN B 1 263 ? 40.465  -33.098 4.046   1.00   98.74  ? 263  ASN A C   1 
ATOM   4277 O O   . ASN B 1 263 ? 41.415  -33.093 3.255   1.00   98.40  ? 263  ASN A O   1 
ATOM   4278 C CB  . ASN B 1 263 ? 38.912  -34.647 2.846   1.00   99.69  ? 263  ASN A CB  1 
ATOM   4279 C CG  . ASN B 1 263 ? 38.963  -36.120 2.497   1.00   99.40  ? 263  ASN A CG  1 
ATOM   4280 O OD1 . ASN B 1 263 ? 39.946  -36.807 2.779   1.00   99.35  ? 263  ASN A OD1 1 
ATOM   4281 N ND2 . ASN B 1 263 ? 37.904  -36.614 1.864   1.00   99.17  ? 263  ASN A ND2 1 
ATOM   4282 N N   . ALA B 1 264 ? 40.142  -32.054 4.805   1.00   97.62  ? 264  ALA A N   1 
ATOM   4283 C CA  . ALA B 1 264 ? 40.941  -30.836 4.830   1.00   96.63  ? 264  ALA A CA  1 
ATOM   4284 C C   . ALA B 1 264 ? 41.744  -30.739 6.122   1.00   95.76  ? 264  ALA A C   1 
ATOM   4285 O O   . ALA B 1 264 ? 41.532  -31.509 7.064   1.00   95.68  ? 264  ALA A O   1 
ATOM   4286 C CB  . ALA B 1 264 ? 40.057  -29.607 4.643   1.00   96.74  ? 264  ALA A CB  1 
ATOM   4287 N N   . CYS B 1 265 ? 42.656  -29.776 6.156   1.00   94.38  ? 265  CYS A N   1 
ATOM   4288 C CA  . CYS B 1 265 ? 43.643  -29.659 7.219   1.00   92.56  ? 265  CYS A CA  1 
ATOM   4289 C C   . CYS B 1 265 ? 43.197  -28.770 8.378   1.00   90.32  ? 265  CYS A C   1 
ATOM   4290 O O   . CYS B 1 265 ? 44.023  -28.378 9.211   1.00   90.01  ? 265  CYS A O   1 
ATOM   4291 C CB  . CYS B 1 265 ? 44.940  -29.118 6.625   1.00   93.22  ? 265  CYS A CB  1 
ATOM   4292 S SG  . CYS B 1 265 ? 44.653  -27.748 5.482   1.00   98.24  ? 265  CYS A SG  1 
ATOM   4293 N N   . PHE B 1 266 ? 41.905  -28.455 8.441   1.00   85.94  ? 266  PHE A N   1 
ATOM   4294 C CA  . PHE B 1 266 ? 41.403  -27.568 9.487   1.00   82.15  ? 266  PHE A CA  1 
ATOM   4295 C C   . PHE B 1 266 ? 41.730  -28.110 10.872  1.00   81.00  ? 266  PHE A C   1 
ATOM   4296 O O   . PHE B 1 266 ? 41.221  -29.160 11.272  1.00   80.48  ? 266  PHE A O   1 
ATOM   4297 C CB  . PHE B 1 266 ? 39.891  -27.347 9.364   1.00   81.26  ? 266  PHE A CB  1 
ATOM   4298 C CG  . PHE B 1 266 ? 39.473  -26.663 8.093   1.00   78.56  ? 266  PHE A CG  1 
ATOM   4299 C CD1 . PHE B 1 266 ? 38.686  -27.330 7.163   1.00   76.36  ? 266  PHE A CD1 1 
ATOM   4300 C CD2 . PHE B 1 266 ? 39.861  -25.350 7.827   1.00   76.51  ? 266  PHE A CD2 1 
ATOM   4301 C CE1 . PHE B 1 266 ? 38.292  -26.703 5.981   1.00   75.80  ? 266  PHE A CE1 1 
ATOM   4302 C CE2 . PHE B 1 266 ? 39.472  -24.716 6.648   1.00   75.53  ? 266  PHE A CE2 1 
ATOM   4303 C CZ  . PHE B 1 266 ? 38.687  -25.396 5.724   1.00   75.14  ? 266  PHE A CZ  1 
ATOM   4304 N N   . GLU B 1 267 ? 42.593  -27.403 11.594  1.00   80.14  ? 267  GLU A N   1 
ATOM   4305 C CA  . GLU B 1 267 ? 42.778  -27.686 13.005  1.00   79.66  ? 267  GLU A CA  1 
ATOM   4306 C C   . GLU B 1 267 ? 41.394  -27.767 13.647  1.00   79.03  ? 267  GLU A C   1 
ATOM   4307 O O   . GLU B 1 267 ? 41.133  -28.632 14.488  1.00   79.20  ? 267  GLU A O   1 
ATOM   4308 C CB  . GLU B 1 267 ? 43.631  -26.603 13.670  1.00   79.82  ? 267  GLU A CB  1 
ATOM   4309 C CG  . GLU B 1 267 ? 43.746  -26.728 15.190  1.00   80.41  ? 267  GLU A CG  1 
ATOM   4310 C CD  . GLU B 1 267 ? 44.419  -28.007 15.661  1.00   81.20  ? 267  GLU A CD  1 
ATOM   4311 O OE1 . GLU B 1 267 ? 45.114  -28.667 14.855  1.00   81.37  ? 267  GLU A OE1 1 
ATOM   4312 O OE2 . GLU B 1 267 ? 44.253  -28.354 16.852  1.00   81.55  ? 267  GLU A OE2 1 
ATOM   4313 N N   . ALA B 1 268 ? 40.507  -26.871 13.211  1.00   77.75  ? 268  ALA A N   1 
ATOM   4314 C CA  . ALA B 1 268 ? 39.120  -26.847 13.654  1.00   75.88  ? 268  ALA A CA  1 
ATOM   4315 C C   . ALA B 1 268 ? 38.238  -26.030 12.710  1.00   74.07  ? 268  ALA A C   1 
ATOM   4316 O O   . ALA B 1 268 ? 38.723  -25.212 11.923  1.00   74.02  ? 268  ALA A O   1 
ATOM   4317 C CB  . ALA B 1 268 ? 39.020  -26.302 15.079  1.00   76.24  ? 268  ALA A CB  1 
ATOM   4318 N N   . VAL B 1 269 ? 36.935  -26.278 12.798  1.00   71.12  ? 269  VAL A N   1 
ATOM   4319 C CA  . VAL B 1 269 ? 35.929  -25.487 12.106  1.00   68.14  ? 269  VAL A CA  1 
ATOM   4320 C C   . VAL B 1 269 ? 34.904  -25.051 13.145  1.00   66.35  ? 269  VAL A C   1 
ATOM   4321 O O   . VAL B 1 269 ? 34.219  -25.886 13.736  1.00   66.18  ? 269  VAL A O   1 
ATOM   4322 C CB  . VAL B 1 269 ? 35.240  -26.288 10.977  1.00   68.14  ? 269  VAL A CB  1 
ATOM   4323 C CG1 . VAL B 1 269 ? 34.273  -25.398 10.196  1.00   67.76  ? 269  VAL A CG1 1 
ATOM   4324 C CG2 . VAL B 1 269 ? 36.274  -26.883 10.039  1.00   67.53  ? 269  VAL A CG2 1 
ATOM   4325 N N   . VAL B 1 270 ? 34.810  -23.748 13.382  1.00   64.17  ? 270  VAL A N   1 
ATOM   4326 C CA  . VAL B 1 270 ? 33.904  -23.230 14.404  1.00   62.19  ? 270  VAL A CA  1 
ATOM   4327 C C   . VAL B 1 270 ? 32.661  -22.617 13.771  1.00   60.73  ? 270  VAL A C   1 
ATOM   4328 O O   . VAL B 1 270 ? 32.755  -21.866 12.800  1.00   60.66  ? 270  VAL A O   1 
ATOM   4329 C CB  . VAL B 1 270 ? 34.589  -22.180 15.309  1.00   62.25  ? 270  VAL A CB  1 
ATOM   4330 C CG1 . VAL B 1 270 ? 33.743  -21.892 16.544  1.00   62.11  ? 270  VAL A CG1 1 
ATOM   4331 C CG2 . VAL B 1 270 ? 35.966  -22.654 15.723  1.00   62.38  ? 270  VAL A CG2 1 
ATOM   4332 N N   . VAL B 1 271 ? 31.501  -22.948 14.329  1.00   58.84  ? 271  VAL A N   1 
ATOM   4333 C CA  . VAL B 1 271 ? 30.240  -22.350 13.910  1.00   56.95  ? 271  VAL A CA  1 
ATOM   4334 C C   . VAL B 1 271 ? 29.389  -21.981 15.116  1.00   56.34  ? 271  VAL A C   1 
ATOM   4335 O O   . VAL B 1 271 ? 29.694  -22.371 16.246  1.00   55.69  ? 271  VAL A O   1 
ATOM   4336 C CB  . VAL B 1 271 ? 29.450  -23.268 12.955  1.00   56.86  ? 271  VAL A CB  1 
ATOM   4337 C CG1 . VAL B 1 271 ? 30.146  -23.356 11.611  1.00   56.59  ? 271  VAL A CG1 1 
ATOM   4338 C CG2 . VAL B 1 271 ? 29.261  -24.657 13.562  1.00   57.05  ? 271  VAL A CG2 1 
ATOM   4339 N N   . THR B 1 272 ? 28.338  -21.205 14.876  1.00   55.78  ? 272  THR A N   1 
ATOM   4340 C CA  . THR B 1 272 ? 27.347  -20.932 15.904  1.00   55.56  ? 272  THR A CA  1 
ATOM   4341 C C   . THR B 1 272 ? 26.225  -21.939 15.716  1.00   55.88  ? 272  THR A C   1 
ATOM   4342 O O   . THR B 1 272 ? 26.150  -22.592 14.676  1.00   55.71  ? 272  THR A O   1 
ATOM   4343 C CB  . THR B 1 272 ? 26.754  -19.520 15.778  1.00   55.33  ? 272  THR A CB  1 
ATOM   4344 O OG1 . THR B 1 272 ? 25.863  -19.480 14.658  1.00   54.53  ? 272  THR A OG1 1 
ATOM   4345 C CG2 . THR B 1 272 ? 27.852  -18.468 15.605  1.00   55.08  ? 272  THR A CG2 1 
ATOM   4346 N N   . ASN B 1 273 ? 25.346  -22.057 16.704  1.00   56.59  ? 273  ASN A N   1 
ATOM   4347 C CA  . ASN B 1 273 ? 24.168  -22.909 16.558  1.00   57.59  ? 273  ASN A CA  1 
ATOM   4348 C C   . ASN B 1 273 ? 22.927  -22.186 15.995  1.00   58.28  ? 273  ASN A C   1 
ATOM   4349 O O   . ASN B 1 273 ? 21.797  -22.480 16.395  1.00   58.05  ? 273  ASN A O   1 
ATOM   4350 C CB  . ASN B 1 273 ? 23.849  -23.637 17.873  1.00   57.54  ? 273  ASN A CB  1 
ATOM   4351 C CG  . ASN B 1 273 ? 23.522  -22.684 19.015  1.00   57.44  ? 273  ASN A CG  1 
ATOM   4352 O OD1 . ASN B 1 273 ? 22.841  -23.060 19.972  1.00   58.14  ? 273  ASN A OD1 1 
ATOM   4353 N ND2 . ASN B 1 273 ? 24.002  -21.452 18.923  1.00   56.57  ? 273  ASN A ND2 1 
ATOM   4354 N N   . THR B 1 274 ? 23.136  -21.248 15.068  1.00   59.48  ? 274  THR A N   1 
ATOM   4355 C CA  . THR B 1 274 ? 22.014  -20.648 14.329  1.00   60.94  ? 274  THR A CA  1 
ATOM   4356 C C   . THR B 1 274 ? 21.346  -21.701 13.439  1.00   62.05  ? 274  THR A C   1 
ATOM   4357 O O   . THR B 1 274 ? 20.149  -21.622 13.150  1.00   62.16  ? 274  THR A O   1 
ATOM   4358 C CB  . THR B 1 274 ? 22.426  -19.415 13.464  1.00   60.87  ? 274  THR A CB  1 
ATOM   4359 O OG1 . THR B 1 274 ? 23.320  -19.812 12.415  1.00   60.71  ? 274  THR A OG1 1 
ATOM   4360 C CG2 . THR B 1 274 ? 23.068  -18.321 14.314  1.00   60.85  ? 274  THR A CG2 1 
ATOM   4361 N N   . ILE B 1 275 ? 22.147  -22.676 13.011  1.00   63.63  ? 275  ILE A N   1 
ATOM   4362 C CA  . ILE B 1 275 ? 21.683  -23.856 12.284  1.00   65.65  ? 275  ILE A CA  1 
ATOM   4363 C C   . ILE B 1 275 ? 22.048  -25.062 13.149  1.00   67.74  ? 275  ILE A C   1 
ATOM   4364 O O   . ILE B 1 275 ? 23.122  -25.067 13.753  1.00   67.53  ? 275  ILE A O   1 
ATOM   4365 C CB  . ILE B 1 275 ? 22.348  -23.945 10.873  1.00   65.33  ? 275  ILE A CB  1 
ATOM   4366 C CG1 . ILE B 1 275 ? 21.855  -22.783 9.992   1.00   65.58  ? 275  ILE A CG1 1 
ATOM   4367 C CG2 . ILE B 1 275 ? 22.075  -25.302 10.193  1.00   65.31  ? 275  ILE A CG2 1 
ATOM   4368 C CD1 . ILE B 1 275 ? 22.350  -22.817 8.551   1.00   65.98  ? 275  ILE A CD1 1 
ATOM   4369 N N   . PRO B 1 276 ? 21.156  -26.073 13.235  1.00   70.64  ? 276  PRO A N   1 
ATOM   4370 C CA  . PRO B 1 276 ? 21.422  -27.242 14.084  1.00   72.61  ? 276  PRO A CA  1 
ATOM   4371 C C   . PRO B 1 276 ? 22.672  -28.000 13.632  1.00   74.03  ? 276  PRO A C   1 
ATOM   4372 O O   . PRO B 1 276 ? 22.802  -28.337 12.452  1.00   74.40  ? 276  PRO A O   1 
ATOM   4373 C CB  . PRO B 1 276 ? 20.174  -28.115 13.899  1.00   72.81  ? 276  PRO A CB  1 
ATOM   4374 C CG  . PRO B 1 276 ? 19.154  -27.237 13.289  1.00   72.09  ? 276  PRO A CG  1 
ATOM   4375 C CD  . PRO B 1 276 ? 19.878  -26.202 12.513  1.00   71.00  ? 276  PRO A CD  1 
ATOM   4376 N N   . GLN B 1 277 ? 23.581  -28.257 14.570  0.66   75.12  ? 277  GLN A N   1 
ATOM   4377 C CA  . GLN B 1 277 ? 24.893  -28.823 14.241  0.66   76.25  ? 277  GLN A CA  1 
ATOM   4378 C C   . GLN B 1 277 ? 25.157  -30.183 14.885  0.66   78.39  ? 277  GLN A C   1 
ATOM   4379 O O   . GLN B 1 277 ? 26.163  -30.828 14.582  0.66   78.41  ? 277  GLN A O   1 
ATOM   4380 C CB  . GLN B 1 277 ? 26.014  -27.854 14.646  0.66   75.42  ? 277  GLN A CB  1 
ATOM   4381 C CG  . GLN B 1 277 ? 25.870  -26.420 14.134  0.66   72.85  ? 277  GLN A CG  1 
ATOM   4382 C CD  . GLN B 1 277 ? 25.961  -26.300 12.620  0.66   69.68  ? 277  GLN A CD  1 
ATOM   4383 O OE1 . GLN B 1 277 ? 25.447  -25.350 12.037  0.66   67.97  ? 277  GLN A OE1 1 
ATOM   4384 N NE2 . GLN B 1 277 ? 26.621  -27.258 11.980  0.66   69.42  ? 277  GLN A NE2 1 
ATOM   4385 N N   . GLU B 1 278 ? 24.250  -30.613 15.761  0.47   81.49  ? 278  GLU A N   1 
ATOM   4386 C CA  . GLU B 1 278 ? 24.450  -31.810 16.582  0.47   84.82  ? 278  GLU A CA  1 
ATOM   4387 C C   . GLU B 1 278 ? 24.629  -33.097 15.771  0.47   87.77  ? 278  GLU A C   1 
ATOM   4388 O O   . GLU B 1 278 ? 25.420  -33.966 16.148  0.47   88.04  ? 278  GLU A O   1 
ATOM   4389 C CB  . GLU B 1 278 ? 23.314  -31.959 17.599  0.47   84.37  ? 278  GLU A CB  1 
ATOM   4390 C CG  . GLU B 1 278 ? 23.130  -30.742 18.507  0.47   83.63  ? 278  GLU A CG  1 
ATOM   4391 C CD  . GLU B 1 278 ? 22.487  -29.562 17.793  0.47   82.60  ? 278  GLU A CD  1 
ATOM   4392 O OE1 . GLU B 1 278 ? 23.126  -28.490 17.712  0.47   82.34  ? 278  GLU A OE1 1 
ATOM   4393 O OE2 . GLU B 1 278 ? 21.342  -29.707 17.310  0.47   82.14  ? 278  GLU A OE2 1 
ATOM   4394 N N   . ASP B 1 279 ? 23.898  -33.206 14.663  1.00   91.46  ? 279  ASP A N   1 
ATOM   4395 C CA  . ASP B 1 279 ? 24.002  -34.350 13.755  1.00   94.68  ? 279  ASP A CA  1 
ATOM   4396 C C   . ASP B 1 279 ? 25.394  -34.429 13.123  1.00   96.05  ? 279  ASP A C   1 
ATOM   4397 O O   . ASP B 1 279 ? 26.053  -35.472 13.179  1.00   95.99  ? 279  ASP A O   1 
ATOM   4398 C CB  . ASP B 1 279 ? 22.922  -34.259 12.665  1.00   95.33  ? 279  ASP A CB  1 
ATOM   4399 C CG  . ASP B 1 279 ? 22.860  -35.501 11.772  1.00   98.00  ? 279  ASP A CG  1 
ATOM   4400 O OD1 . ASP B 1 279 ? 23.914  -36.053 11.385  1.00   97.40  ? 279  ASP A OD1 1 
ATOM   4401 O OD2 . ASP B 1 279 ? 21.733  -35.918 11.434  1.00   100.24 ? 279  ASP A OD2 1 
ATOM   4402 N N   . LYS B 1 280 ? 25.830  -33.318 12.533  0.97   96.15  ? 280  LYS A N   1 
ATOM   4403 C CA  . LYS B 1 280 ? 27.096  -33.247 11.803  0.97   96.64  ? 280  LYS A CA  1 
ATOM   4404 C C   . LYS B 1 280 ? 28.327  -33.355 12.699  0.97   98.29  ? 280  LYS A C   1 
ATOM   4405 O O   . LYS B 1 280 ? 29.364  -33.854 12.265  0.97   98.10  ? 280  LYS A O   1 
ATOM   4406 C CB  . LYS B 1 280 ? 27.160  -31.959 10.983  0.97   95.88  ? 280  LYS A CB  1 
ATOM   4407 C CG  . LYS B 1 280 ? 26.080  -31.862 9.926   0.97   94.12  ? 280  LYS A CG  1 
ATOM   4408 C CD  . LYS B 1 280 ? 26.128  -30.538 9.201   0.97   91.33  ? 280  LYS A CD  1 
ATOM   4409 C CE  . LYS B 1 280 ? 24.985  -30.422 8.199   0.97   90.12  ? 280  LYS A CE  1 
ATOM   4410 N NZ  . LYS B 1 280 ? 25.069  -31.447 7.113   0.97   88.74  ? 280  LYS A NZ  1 
ATOM   4411 N N   . MET B 1 281 ? 28.210  -32.878 13.937  1.00   101.05 ? 281  MET A N   1 
ATOM   4412 C CA  . MET B 1 281 ? 29.309  -32.943 14.903  1.00   103.89 ? 281  MET A CA  1 
ATOM   4413 C C   . MET B 1 281 ? 29.746  -34.381 15.179  1.00   105.82 ? 281  MET A C   1 
ATOM   4414 O O   . MET B 1 281 ? 30.917  -34.639 15.471  1.00   106.16 ? 281  MET A O   1 
ATOM   4415 C CB  . MET B 1 281 ? 28.923  -32.261 16.214  1.00   103.83 ? 281  MET A CB  1 
ATOM   4416 C CG  . MET B 1 281 ? 28.901  -30.748 16.146  1.00   103.66 ? 281  MET A CG  1 
ATOM   4417 S SD  . MET B 1 281 ? 28.880  -29.996 17.782  1.00   103.51 ? 281  MET A SD  1 
ATOM   4418 C CE  . MET B 1 281 ? 27.229  -30.393 18.358  1.00   103.43 ? 281  MET A CE  1 
ATOM   4419 N N   . LYS B 1 282 ? 28.795  -35.307 15.089  0.65   107.81 ? 282  LYS A N   1 
ATOM   4420 C CA  . LYS B 1 282 ? 29.076  -36.734 15.218  0.65   109.44 ? 282  LYS A CA  1 
ATOM   4421 C C   . LYS B 1 282 ? 29.890  -37.239 14.029  0.65   109.76 ? 282  LYS A C   1 
ATOM   4422 O O   . LYS B 1 282 ? 30.648  -38.203 14.152  0.65   109.90 ? 282  LYS A O   1 
ATOM   4423 C CB  . LYS B 1 282 ? 27.772  -37.527 15.335  0.65   109.81 ? 282  LYS A CB  1 
ATOM   4424 C CG  . LYS B 1 282 ? 26.960  -37.217 16.586  0.65   111.25 ? 282  LYS A CG  1 
ATOM   4425 C CD  . LYS B 1 282 ? 25.534  -37.731 16.465  0.65   113.40 ? 282  LYS A CD  1 
ATOM   4426 C CE  . LYS B 1 282 ? 24.699  -37.323 17.669  0.65   118.37 ? 282  LYS A CE  1 
ATOM   4427 N NZ  . LYS B 1 282 ? 23.263  -37.718 17.514  0.65   122.77 ? 282  LYS A NZ  1 
ATOM   4428 N N   . HIS B 1 283 ? 29.730  -36.576 12.886  0.87   109.94 ? 283  HIS A N   1 
ATOM   4429 C CA  . HIS B 1 283 ? 30.398  -36.976 11.650  0.87   109.86 ? 283  HIS A CA  1 
ATOM   4430 C C   . HIS B 1 283 ? 31.621  -36.109 11.340  0.87   109.04 ? 283  HIS A C   1 
ATOM   4431 O O   . HIS B 1 283 ? 32.290  -36.309 10.322  0.87   109.11 ? 283  HIS A O   1 
ATOM   4432 C CB  . HIS B 1 283 ? 29.409  -36.924 10.484  0.87   110.28 ? 283  HIS A CB  1 
ATOM   4433 C CG  . HIS B 1 283 ? 29.335  -38.198 9.704   0.87   111.46 ? 283  HIS A CG  1 
ATOM   4434 N ND1 . HIS B 1 283 ? 30.273  -38.549 8.757   0.87   112.36 ? 283  HIS A ND1 1 
ATOM   4435 C CD2 . HIS B 1 283 ? 28.435  -39.209 9.736   0.87   112.35 ? 283  HIS A CD2 1 
ATOM   4436 C CE1 . HIS B 1 283 ? 29.952  -39.721 8.238   0.87   112.80 ? 283  HIS A CE1 1 
ATOM   4437 N NE2 . HIS B 1 283 ? 28.841  -40.143 8.815   0.87   112.78 ? 283  HIS A NE2 1 
ATOM   4438 N N   . CYS B 1 284 ? 31.906  -35.153 12.223  0.90   107.67 ? 284  CYS A N   1 
ATOM   4439 C CA  . CYS B 1 284 ? 33.032  -34.239 12.049  0.90   106.03 ? 284  CYS A CA  1 
ATOM   4440 C C   . CYS B 1 284 ? 33.594  -33.804 13.402  0.90   104.47 ? 284  CYS A C   1 
ATOM   4441 O O   . CYS B 1 284 ? 32.950  -33.058 14.148  0.90   104.33 ? 284  CYS A O   1 
ATOM   4442 C CB  . CYS B 1 284 ? 32.611  -33.026 11.218  0.90   106.29 ? 284  CYS A CB  1 
ATOM   4443 S SG  . CYS B 1 284 ? 33.983  -32.060 10.576  0.90   106.46 ? 284  CYS A SG  1 
ATOM   4444 N N   . SER B 1 285 ? 34.802  -34.275 13.703  1.00   102.30 ? 285  SER A N   1 
ATOM   4445 C CA  . SER B 1 285 ? 35.424  -34.081 15.015  1.00   100.12 ? 285  SER A CA  1 
ATOM   4446 C C   . SER B 1 285 ? 35.912  -32.656 15.264  1.00   98.58  ? 285  SER A C   1 
ATOM   4447 O O   . SER B 1 285 ? 35.924  -32.192 16.408  1.00   98.35  ? 285  SER A O   1 
ATOM   4448 C CB  . SER B 1 285 ? 36.584  -35.066 15.198  1.00   100.22 ? 285  SER A CB  1 
ATOM   4449 O OG  . SER B 1 285 ? 37.323  -34.781 16.374  1.00   100.14 ? 285  SER A OG  1 
ATOM   4450 N N   . LYS B 1 286 ? 36.310  -31.970 14.195  1.00   96.56  ? 286  LYS A N   1 
ATOM   4451 C CA  . LYS B 1 286 ? 36.911  -30.640 14.308  1.00   94.35  ? 286  LYS A CA  1 
ATOM   4452 C C   . LYS B 1 286 ? 35.903  -29.504 14.540  1.00   92.15  ? 286  LYS A C   1 
ATOM   4453 O O   . LYS B 1 286 ? 36.297  -28.388 14.890  1.00   91.96  ? 286  LYS A O   1 
ATOM   4454 C CB  . LYS B 1 286 ? 37.812  -30.347 13.101  1.00   94.79  ? 286  LYS A CB  1 
ATOM   4455 C CG  . LYS B 1 286 ? 37.235  -30.764 11.751  1.00   95.18  ? 286  LYS A CG  1 
ATOM   4456 C CD  . LYS B 1 286 ? 38.239  -30.550 10.619  1.00   96.02  ? 286  LYS A CD  1 
ATOM   4457 C CE  . LYS B 1 286 ? 39.107  -31.782 10.356  1.00   96.29  ? 286  LYS A CE  1 
ATOM   4458 N NZ  . LYS B 1 286 ? 40.150  -31.997 11.397  1.00   96.49  ? 286  LYS A NZ  1 
ATOM   4459 N N   . ILE B 1 287 ? 34.613  -29.796 14.363  1.00   89.10  ? 287  ILE A N   1 
ATOM   4460 C CA  . ILE B 1 287 ? 33.549  -28.799 14.548  1.00   86.26  ? 287  ILE A CA  1 
ATOM   4461 C C   . ILE B 1 287 ? 33.307  -28.453 16.019  1.00   84.74  ? 287  ILE A C   1 
ATOM   4462 O O   . ILE B 1 287 ? 33.118  -29.338 16.856  1.00   84.38  ? 287  ILE A O   1 
ATOM   4463 C CB  . ILE B 1 287 ? 32.209  -29.237 13.891  1.00   86.19  ? 287  ILE A CB  1 
ATOM   4464 C CG1 . ILE B 1 287 ? 32.355  -29.322 12.366  1.00   86.06  ? 287  ILE A CG1 1 
ATOM   4465 C CG2 . ILE B 1 287 ? 31.077  -28.272 14.265  1.00   85.80  ? 287  ILE A CG2 1 
ATOM   4466 C CD1 . ILE B 1 287 ? 31.079  -29.723 11.629  1.00   86.10  ? 287  ILE A CD1 1 
ATOM   4467 N N   . GLN B 1 288 ? 33.320  -27.159 16.321  1.00   83.20  ? 288  GLN A N   1 
ATOM   4468 C CA  . GLN B 1 288 ? 32.955  -26.671 17.645  1.00   81.84  ? 288  GLN A CA  1 
ATOM   4469 C C   . GLN B 1 288 ? 31.879  -25.602 17.503  1.00   79.81  ? 288  GLN A C   1 
ATOM   4470 O O   . GLN B 1 288 ? 31.955  -24.754 16.612  1.00   79.71  ? 288  GLN A O   1 
ATOM   4471 C CB  . GLN B 1 288 ? 34.174  -26.102 18.372  1.00   82.45  ? 288  GLN A CB  1 
ATOM   4472 C CG  . GLN B 1 288 ? 35.322  -27.092 18.546  1.00   84.13  ? 288  GLN A CG  1 
ATOM   4473 C CD  . GLN B 1 288 ? 36.392  -26.589 19.496  1.00   85.97  ? 288  GLN A CD  1 
ATOM   4474 O OE1 . GLN B 1 288 ? 36.096  -25.945 20.505  1.00   86.50  ? 288  GLN A OE1 1 
ATOM   4475 N NE2 . GLN B 1 288 ? 37.648  -26.888 19.182  1.00   86.49  ? 288  GLN A NE2 1 
ATOM   4476 N N   . VAL B 1 289 ? 30.874  -25.648 18.373  1.00   76.85  ? 289  VAL A N   1 
ATOM   4477 C CA  . VAL B 1 289 ? 29.777  -24.686 18.288  1.00   73.94  ? 289  VAL A CA  1 
ATOM   4478 C C   . VAL B 1 289 ? 29.827  -23.624 19.381  1.00   71.90  ? 289  VAL A C   1 
ATOM   4479 O O   . VAL B 1 289 ? 30.057  -23.923 20.560  1.00   71.78  ? 289  VAL A O   1 
ATOM   4480 C CB  . VAL B 1 289 ? 28.370  -25.359 18.245  1.00   73.99  ? 289  VAL A CB  1 
ATOM   4481 C CG1 . VAL B 1 289 ? 28.366  -26.553 17.281  1.00   73.70  ? 289  VAL A CG1 1 
ATOM   4482 C CG2 . VAL B 1 289 ? 27.907  -25.786 19.644  1.00   74.10  ? 289  VAL A CG2 1 
ATOM   4483 N N   . ILE B 1 290 ? 29.627  -22.379 18.964  1.00   69.21  ? 290  ILE A N   1 
ATOM   4484 C CA  . ILE B 1 290 ? 29.387  -21.288 19.890  1.00   66.75  ? 290  ILE A CA  1 
ATOM   4485 C C   . ILE B 1 290 ? 27.875  -21.128 20.032  1.00   65.11  ? 290  ILE A C   1 
ATOM   4486 O O   . ILE B 1 290 ? 27.170  -20.876 19.053  1.00   64.92  ? 290  ILE A O   1 
ATOM   4487 C CB  . ILE B 1 290 ? 30.031  -19.974 19.403  1.00   66.76  ? 290  ILE A CB  1 
ATOM   4488 C CG1 . ILE B 1 290 ? 31.556  -20.136 19.313  1.00   66.67  ? 290  ILE A CG1 1 
ATOM   4489 C CG2 . ILE B 1 290 ? 29.649  -18.814 20.327  1.00   66.76  ? 290  ILE A CG2 1 
ATOM   4490 C CD1 . ILE B 1 290 ? 32.285  -18.978 18.626  1.00   65.82  ? 290  ILE A CD1 1 
ATOM   4491 N N   . ASP B 1 291 ? 27.391  -21.302 21.257  1.00   62.78  ? 291  ASP A N   1 
ATOM   4492 C CA  . ASP B 1 291 ? 25.978  -21.148 21.580  1.00   60.58  ? 291  ASP A CA  1 
ATOM   4493 C C   . ASP B 1 291 ? 25.590  -19.675 21.490  1.00   58.49  ? 291  ASP A C   1 
ATOM   4494 O O   . ASP B 1 291 ? 26.221  -18.828 22.123  1.00   58.18  ? 291  ASP A O   1 
ATOM   4495 C CB  . ASP B 1 291 ? 25.724  -21.685 22.992  1.00   60.84  ? 291  ASP A CB  1 
ATOM   4496 C CG  . ASP B 1 291 ? 24.269  -21.580 23.420  1.00   61.68  ? 291  ASP A CG  1 
ATOM   4497 O OD1 . ASP B 1 291 ? 23.393  -21.268 22.583  1.00   61.93  ? 291  ASP A OD1 1 
ATOM   4498 O OD2 . ASP B 1 291 ? 24.001  -21.825 24.616  1.00   62.63  ? 291  ASP A OD2 1 
ATOM   4499 N N   . ILE B 1 292 ? 24.564  -19.365 20.701  1.00   55.61  ? 292  ILE A N   1 
ATOM   4500 C CA  . ILE B 1 292 ? 24.148  -17.969 20.559  1.00   53.45  ? 292  ILE A CA  1 
ATOM   4501 C C   . ILE B 1 292 ? 22.767  -17.712 21.143  1.00   51.83  ? 292  ILE A C   1 
ATOM   4502 O O   . ILE B 1 292 ? 22.211  -16.618 20.988  1.00   51.22  ? 292  ILE A O   1 
ATOM   4503 C CB  . ILE B 1 292 ? 24.294  -17.421 19.091  1.00   53.57  ? 292  ILE A CB  1 
ATOM   4504 C CG1 . ILE B 1 292 ? 23.708  -18.374 18.046  1.00   52.90  ? 292  ILE A CG1 1 
ATOM   4505 C CG2 . ILE B 1 292 ? 25.759  -17.179 18.767  1.00   53.87  ? 292  ILE A CG2 1 
ATOM   4506 C CD1 . ILE B 1 292 ? 22.206  -18.424 17.997  1.00   51.28  ? 292  ILE A CD1 1 
ATOM   4507 N N   . SER B 1 293 ? 22.237  -18.717 21.837  1.00   50.09  ? 293  SER A N   1 
ATOM   4508 C CA  . SER B 1 293 ? 20.920  -18.625 22.462  1.00   48.60  ? 293  SER A CA  1 
ATOM   4509 C C   . SER B 1 293 ? 20.792  -17.524 23.522  1.00   47.69  ? 293  SER A C   1 
ATOM   4510 O O   . SER B 1 293 ? 19.692  -17.010 23.743  1.00   47.96  ? 293  SER A O   1 
ATOM   4511 C CB  . SER B 1 293 ? 20.501  -19.974 23.044  1.00   48.77  ? 293  SER A CB  1 
ATOM   4512 O OG  . SER B 1 293 ? 21.359  -20.360 24.103  1.00   48.60  ? 293  SER A OG  1 
ATOM   4513 N N   . MET B 1 294 ? 21.893  -17.148 24.169  0.65   46.41  ? 294  MET A N   1 
ATOM   4514 C CA  . MET B 1 294 ? 21.817  -16.076 25.167  0.65   46.24  ? 294  MET A CA  1 
ATOM   4515 C C   . MET B 1 294 ? 21.679  -14.711 24.510  0.65   45.38  ? 294  MET A C   1 
ATOM   4516 O O   . MET B 1 294 ? 20.906  -13.867 24.966  0.65   44.61  ? 294  MET A O   1 
ATOM   4517 C CB  . MET B 1 294 ? 23.006  -16.096 26.134  0.65   46.63  ? 294  MET A CB  1 
ATOM   4518 C CG  . MET B 1 294 ? 22.997  -14.945 27.155  0.65   48.97  ? 294  MET A CG  1 
ATOM   4519 S SD  . MET B 1 294 ? 21.466  -14.782 28.112  0.65   55.39  ? 294  MET A SD  1 
ATOM   4520 C CE  . MET B 1 294 ? 21.825  -15.842 29.514  0.65   54.78  ? 294  MET A CE  1 
ATOM   4521 N N   . ILE B 1 295 ? 22.437  -14.508 23.439  1.00   45.31  ? 295  ILE A N   1 
ATOM   4522 C CA  . ILE B 1 295 ? 22.327  -13.307 22.618  1.00   45.37  ? 295  ILE A CA  1 
ATOM   4523 C C   . ILE B 1 295 ? 20.889  -13.123 22.126  1.00   43.82  ? 295  ILE A C   1 
ATOM   4524 O O   . ILE B 1 295 ? 20.340  -12.023 22.194  1.00   43.72  ? 295  ILE A O   1 
ATOM   4525 C CB  . ILE B 1 295 ? 23.312  -13.346 21.424  1.00   45.83  ? 295  ILE A CB  1 
ATOM   4526 C CG1 . ILE B 1 295 ? 24.710  -13.745 21.913  1.00   47.29  ? 295  ILE A CG1 1 
ATOM   4527 C CG2 . ILE B 1 295 ? 23.370  -11.994 20.732  1.00   46.73  ? 295  ILE A CG2 1 
ATOM   4528 C CD1 . ILE B 1 295 ? 25.744  -13.932 20.812  1.00   49.34  ? 295  ILE A CD1 1 
ATOM   4529 N N   . LEU B 1 296 ? 20.268  -14.206 21.670  1.00   42.25  ? 296  LEU A N   1 
ATOM   4530 C CA  . LEU B 1 296 ? 18.913  -14.117 21.114  1.00   41.24  ? 296  LEU A CA  1 
ATOM   4531 C C   . LEU B 1 296 ? 17.875  -13.873 22.187  1.00   41.14  ? 296  LEU A C   1 
ATOM   4532 O O   . LEU B 1 296 ? 16.992  -13.034 22.015  1.00   41.18  ? 296  LEU A O   1 
ATOM   4533 C CB  . LEU B 1 296 ? 18.564  -15.367 20.304  1.00   40.01  ? 296  LEU A CB  1 
ATOM   4534 C CG  . LEU B 1 296 ? 19.355  -15.524 18.995  1.00   40.55  ? 296  LEU A CG  1 
ATOM   4535 C CD1 . LEU B 1 296 ? 19.085  -16.891 18.404  1.00   38.93  ? 296  LEU A CD1 1 
ATOM   4536 C CD2 . LEU B 1 296 ? 19.012  -14.424 17.977  1.00   39.70  ? 296  LEU A CD2 1 
ATOM   4537 N N   . ALA B 1 297 ? 17.995  -14.601 23.298  1.00   41.16  ? 297  ALA A N   1 
ATOM   4538 C CA  . ALA B 1 297 ? 17.103  -14.438 24.439  1.00   41.38  ? 297  ALA A CA  1 
ATOM   4539 C C   . ALA B 1 297 ? 17.171  -13.007 24.946  1.00   42.38  ? 297  ALA A C   1 
ATOM   4540 O O   . ALA B 1 297 ? 16.139  -12.370 25.211  1.00   42.43  ? 297  ALA A O   1 
ATOM   4541 C CB  . ALA B 1 297 ? 17.491  -15.412 25.549  1.00   41.14  ? 297  ALA A CB  1 
ATOM   4542 N N   . GLU B 1 298 ? 18.392  -12.500 25.063  1.00   43.36  ? 298  GLU A N   1 
ATOM   4543 C CA  . GLU B 1 298 ? 18.593  -11.148 25.540  1.00   45.03  ? 298  GLU A CA  1 
ATOM   4544 C C   . GLU B 1 298 ? 17.954  -10.152 24.586  1.00   44.45  ? 298  GLU A C   1 
ATOM   4545 O O   . GLU B 1 298 ? 17.264  -9.233  25.031  1.00   45.01  ? 298  GLU A O   1 
ATOM   4546 C CB  . GLU B 1 298 ? 20.082  -10.858 25.746  1.00   45.75  ? 298  GLU A CB  1 
ATOM   4547 C CG  . GLU B 1 298 ? 20.382  -9.629  26.600  1.00   49.98  ? 298  GLU A CG  1 
ATOM   4548 C CD  . GLU B 1 298 ? 19.897  -9.745  28.049  1.00   54.18  ? 298  GLU A CD  1 
ATOM   4549 O OE1 . GLU B 1 298 ? 19.479  -10.843 28.482  1.00   56.04  ? 298  GLU A OE1 1 
ATOM   4550 O OE2 . GLU B 1 298 ? 19.932  -8.720  28.764  1.00   56.42  ? 298  GLU A OE2 1 
ATOM   4551 N N   . ALA B 1 299 ? 18.156  -10.344 23.281  1.00   43.65  ? 299  ALA A N   1 
ATOM   4552 C CA  . ALA B 1 299 ? 17.537  -9.473  22.276  1.00   42.36  ? 299  ALA A CA  1 
ATOM   4553 C C   . ALA B 1 299 ? 16.007  -9.502  22.353  1.00   41.85  ? 299  ALA A C   1 
ATOM   4554 O O   . ALA B 1 299 ? 15.359  -8.465  22.200  1.00   41.77  ? 299  ALA A O   1 
ATOM   4555 C CB  . ALA B 1 299 ? 18.020  -9.828  20.876  1.00   42.63  ? 299  ALA A CB  1 
ATOM   4556 N N   . ILE B 1 300 ? 15.436  -10.677 22.615  1.00   40.92  ? 300  ILE A N   1 
ATOM   4557 C CA  . ILE B 1 300 ? 13.988  -10.803 22.787  1.00   40.90  ? 300  ILE A CA  1 
ATOM   4558 C C   . ILE B 1 300 ? 13.528  -10.096 24.058  1.00   41.62  ? 300  ILE A C   1 
ATOM   4559 O O   . ILE B 1 300 ? 12.603  -9.268  24.022  1.00   41.26  ? 300  ILE A O   1 
ATOM   4560 C CB  . ILE B 1 300 ? 13.545  -12.281 22.822  1.00   41.13  ? 300  ILE A CB  1 
ATOM   4561 C CG1 . ILE B 1 300 ? 13.788  -12.933 21.456  1.00   40.78  ? 300  ILE A CG1 1 
ATOM   4562 C CG2 . ILE B 1 300 ? 12.075  -12.402 23.229  1.00   39.70  ? 300  ILE A CG2 1 
ATOM   4563 C CD1 . ILE B 1 300 ? 13.464  -14.413 21.412  1.00   39.28  ? 300  ILE A CD1 1 
ATOM   4564 N N   . ARG B 1 301 ? 14.175  -10.422 25.177  0.99   42.09  ? 301  ARG A N   1 
ATOM   4565 C CA  . ARG B 1 301 ? 13.832  -9.809  26.448  0.99   42.68  ? 301  ARG A CA  1 
ATOM   4566 C C   . ARG B 1 301 ? 13.944  -8.306  26.324  0.99   42.29  ? 301  ARG A C   1 
ATOM   4567 O O   . ARG B 1 301 ? 13.030  -7.577  26.709  0.99   42.33  ? 301  ARG A O   1 
ATOM   4568 C CB  . ARG B 1 301 ? 14.739  -10.309 27.576  0.99   43.57  ? 301  ARG A CB  1 
ATOM   4569 C CG  . ARG B 1 301 ? 14.073  -10.209 28.948  0.99   46.91  ? 301  ARG A CG  1 
ATOM   4570 C CD  . ARG B 1 301 ? 15.027  -10.503 30.090  0.99   51.68  ? 301  ARG A CD  1 
ATOM   4571 N NE  . ARG B 1 301 ? 15.586  -9.266  30.619  0.99   56.26  ? 301  ARG A NE  1 
ATOM   4572 C CZ  . ARG B 1 301 ? 16.756  -8.763  30.248  0.99   58.47  ? 301  ARG A CZ  1 
ATOM   4573 N NH1 . ARG B 1 301 ? 17.491  -9.408  29.355  0.99   59.90  ? 301  ARG A NH1 1 
ATOM   4574 N NH2 . ARG B 1 301 ? 17.194  -7.625  30.770  0.99   59.54  ? 301  ARG A NH2 1 
ATOM   4575 N N   . ARG B 1 302 ? 15.051  -7.838  25.755  0.72   42.25  ? 302  ARG A N   1 
ATOM   4576 C CA  . ARG B 1 302 ? 15.268  -6.399  25.625  0.72   43.35  ? 302  ARG A CA  1 
ATOM   4577 C C   . ARG B 1 302 ? 14.309  -5.742  24.640  0.72   43.83  ? 302  ARG A C   1 
ATOM   4578 O O   . ARG B 1 302 ? 13.792  -4.658  24.918  0.72   44.16  ? 302  ARG A O   1 
ATOM   4579 C CB  . ARG B 1 302 ? 16.729  -6.082  25.324  0.72   43.50  ? 302  ARG A CB  1 
ATOM   4580 C CG  . ARG B 1 302 ? 17.618  -6.369  26.532  0.72   46.22  ? 302  ARG A CG  1 
ATOM   4581 C CD  . ARG B 1 302 ? 19.097  -6.384  26.205  0.72   50.27  ? 302  ARG A CD  1 
ATOM   4582 N NE  . ARG B 1 302 ? 19.882  -6.368  27.437  0.72   53.39  ? 302  ARG A NE  1 
ATOM   4583 C CZ  . ARG B 1 302 ? 20.589  -5.329  27.875  0.72   55.05  ? 302  ARG A CZ  1 
ATOM   4584 N NH1 . ARG B 1 302 ? 20.647  -4.202  27.174  0.72   54.96  ? 302  ARG A NH1 1 
ATOM   4585 N NH2 . ARG B 1 302 ? 21.257  -5.425  29.018  0.72   55.70  ? 302  ARG A NH2 1 
ATOM   4586 N N   . THR B 1 303 ? 14.049  -6.410  23.512  1.00   44.77  ? 303  THR A N   1 
ATOM   4587 C CA  . THR B 1 303 ? 13.023  -5.970  22.561  1.00   45.51  ? 303  THR A CA  1 
ATOM   4588 C C   . THR B 1 303 ? 11.683  -5.844  23.262  1.00   46.05  ? 303  THR A C   1 
ATOM   4589 O O   . THR B 1 303 ? 10.913  -4.914  23.005  1.00   46.49  ? 303  THR A O   1 
ATOM   4590 C CB  . THR B 1 303 ? 12.828  -6.992  21.407  1.00   45.36  ? 303  THR A CB  1 
ATOM   4591 O OG1 . THR B 1 303 ? 13.969  -6.980  20.549  1.00   47.40  ? 303  THR A OG1 1 
ATOM   4592 C CG2 . THR B 1 303 ? 11.596  -6.657  20.579  1.00   45.41  ? 303  THR A CG2 1 
ATOM   4593 N N   . HIS B 1 304 ? 11.393  -6.814  24.126  1.00   46.42  ? 304  HIS A N   1 
ATOM   4594 C CA  . HIS B 1 304 ? 10.124  -6.843  24.827  1.00   47.06  ? 304  HIS A CA  1 
ATOM   4595 C C   . HIS B 1 304 ? 9.986   -5.724  25.858  1.00   48.20  ? 304  HIS A C   1 
ATOM   4596 O O   . HIS B 1 304 ? 8.888   -5.182  26.038  1.00   47.79  ? 304  HIS A O   1 
ATOM   4597 C CB  . HIS B 1 304 ? 9.910   -8.184  25.523  1.00   46.85  ? 304  HIS A CB  1 
ATOM   4598 C CG  . HIS B 1 304 ? 8.643   -8.236  26.308  1.00   46.69  ? 304  HIS A CG  1 
ATOM   4599 N ND1 . HIS B 1 304 ? 7.406   -8.226  25.703  1.00   45.43  ? 304  HIS A ND1 1 
ATOM   4600 C CD2 . HIS B 1 304 ? 8.413   -8.250  27.642  1.00   47.44  ? 304  HIS A CD2 1 
ATOM   4601 C CE1 . HIS B 1 304 ? 6.466   -8.260  26.629  1.00   46.06  ? 304  HIS A CE1 1 
ATOM   4602 N NE2 . HIS B 1 304 ? 7.049   -8.274  27.815  1.00   47.38  ? 304  HIS A NE2 1 
ATOM   4603 N N   . ASN B 1 305 ? 11.092  -5.390  26.525  1.00   49.35  ? 305  ASN A N   1 
ATOM   4604 C CA  . ASN B 1 305 ? 11.073  -4.437  27.645  1.00   51.72  ? 305  ASN A CA  1 
ATOM   4605 C C   . ASN B 1 305 ? 11.348  -3.001  27.230  1.00   53.44  ? 305  ASN A C   1 
ATOM   4606 O O   . ASN B 1 305 ? 11.461  -2.116  28.081  1.00   54.09  ? 305  ASN A O   1 
ATOM   4607 C CB  . ASN B 1 305 ? 12.089  -4.847  28.721  1.00   50.77  ? 305  ASN A CB  1 
ATOM   4608 C CG  . ASN B 1 305 ? 11.742  -6.169  29.383  1.00   52.89  ? 305  ASN A CG  1 
ATOM   4609 O OD1 . ASN B 1 305 ? 10.573  -6.480  29.605  1.00   55.21  ? 305  ASN A OD1 1 
ATOM   4610 N ND2 . ASN B 1 305 ? 12.764  -6.951  29.711  1.00   54.95  ? 305  ASN A ND2 1 
ATOM   4611 N N   . GLY B 1 306 ? 11.464  -2.765  25.927  1.00   55.42  ? 306  GLY A N   1 
ATOM   4612 C CA  . GLY B 1 306 ? 11.886  -1.455  25.432  1.00   57.51  ? 306  GLY A CA  1 
ATOM   4613 C C   . GLY B 1 306 ? 13.298  -1.118  25.880  1.00   59.45  ? 306  GLY A C   1 
ATOM   4614 O O   . GLY B 1 306 ? 13.649  0.054   26.028  1.00   58.97  ? 306  GLY A O   1 
ATOM   4615 N N   . GLU B 1 307 ? 14.111  -2.149  26.098  1.00   62.19  ? 307  GLU A N   1 
ATOM   4616 C CA  . GLU B 1 307 ? 15.496  -1.971  26.532  1.00   65.39  ? 307  GLU A CA  1 
ATOM   4617 C C   . GLU B 1 307 ? 16.447  -2.005  25.335  1.00   66.87  ? 307  GLU A C   1 
ATOM   4618 O O   . GLU B 1 307 ? 16.117  -2.565  24.289  1.00   66.83  ? 307  GLU A O   1 
ATOM   4619 C CB  . GLU B 1 307 ? 15.871  -3.045  27.565  1.00   65.59  ? 307  GLU A CB  1 
ATOM   4620 C CG  . GLU B 1 307 ? 17.349  -3.076  27.976  1.00   68.46  ? 307  GLU A CG  1 
ATOM   4621 C CD  . GLU B 1 307 ? 17.682  -2.147  29.133  1.00   71.53  ? 307  GLU A CD  1 
ATOM   4622 O OE1 . GLU B 1 307 ? 16.906  -1.205  29.404  1.00   72.94  ? 307  GLU A OE1 1 
ATOM   4623 O OE2 . GLU B 1 307 ? 18.731  -2.361  29.777  1.00   75.24  ? 307  GLU A OE2 1 
ATOM   4624 N N   . SER B 1 308 ? 17.627  -1.410  25.505  1.00   68.88  ? 308  SER A N   1 
ATOM   4625 C CA  . SER B 1 308 ? 18.622  -1.311  24.441  1.00   70.54  ? 308  SER A CA  1 
ATOM   4626 C C   . SER B 1 308 ? 19.126  -2.680  23.974  1.00   70.91  ? 308  SER A C   1 
ATOM   4627 O O   . SER B 1 308 ? 19.516  -3.522  24.784  1.00   71.22  ? 308  SER A O   1 
ATOM   4628 C CB  . SER B 1 308 ? 19.795  -0.438  24.896  1.00   70.82  ? 308  SER A CB  1 
ATOM   4629 O OG  . SER B 1 308 ? 20.809  -0.379  23.906  1.00   71.48  ? 308  SER A OG  1 
ATOM   4630 N N   . VAL B 1 309 ? 19.105  -2.886  22.660  1.00   70.74  ? 309  VAL A N   1 
ATOM   4631 C CA  . VAL B 1 309 ? 19.624  -4.106  22.042  1.00   70.35  ? 309  VAL A CA  1 
ATOM   4632 C C   . VAL B 1 309 ? 21.053  -3.896  21.518  1.00   70.52  ? 309  VAL A C   1 
ATOM   4633 O O   . VAL B 1 309 ? 21.867  -4.826  21.533  1.00   70.40  ? 309  VAL A O   1 
ATOM   4634 C CB  . VAL B 1 309 ? 18.686  -4.600  20.908  1.00   70.35  ? 309  VAL A CB  1 
ATOM   4635 C CG1 . VAL B 1 309 ? 19.307  -5.743  20.117  1.00   69.93  ? 309  VAL A CG1 1 
ATOM   4636 C CG2 . VAL B 1 309 ? 17.337  -5.023  21.480  1.00   69.68  ? 309  VAL A CG2 1 
ATOM   4637 N N   . SER B 1 310 ? 21.355  -2.672  21.079  0.43   70.73  ? 310  SER A N   1 
ATOM   4638 C CA  . SER B 1 310 ? 22.668  -2.346  20.512  0.43   72.15  ? 310  SER A CA  1 
ATOM   4639 C C   . SER B 1 310 ? 23.806  -2.768  21.435  0.43   74.67  ? 310  SER A C   1 
ATOM   4640 O O   . SER B 1 310 ? 24.921  -3.030  20.981  0.43   74.22  ? 310  SER A O   1 
ATOM   4641 C CB  . SER B 1 310 ? 22.777  -0.850  20.212  0.43   71.33  ? 310  SER A CB  1 
ATOM   4642 O OG  . SER B 1 310 ? 22.950  -0.100  21.406  0.43   70.62  ? 310  SER A OG  1 
ATOM   4643 N N   . TYR B 1 311 ? 23.508  -2.834  22.731  0.75   84.32  ? 311  TYR A N   1 
ATOM   4644 C CA  . TYR B 1 311 ? 24.464  -3.277  23.738  0.75   85.13  ? 311  TYR A CA  1 
ATOM   4645 C C   . TYR B 1 311 ? 25.139  -4.613  23.387  0.75   85.19  ? 311  TYR A C   1 
ATOM   4646 O O   . TYR B 1 311 ? 26.327  -4.807  23.656  0.75   84.39  ? 311  TYR A O   1 
ATOM   4647 C CB  . TYR B 1 311 ? 23.786  -3.350  25.112  0.75   84.47  ? 311  TYR A CB  1 
ATOM   4648 C CG  . TYR B 1 311 ? 24.665  -3.927  26.195  0.75   88.32  ? 311  TYR A CG  1 
ATOM   4649 C CD1 . TYR B 1 311 ? 25.994  -3.516  26.332  0.75   91.32  ? 311  TYR A CD1 1 
ATOM   4650 C CD2 . TYR B 1 311 ? 24.172  -4.877  27.088  0.75   91.22  ? 311  TYR A CD2 1 
ATOM   4651 C CE1 . TYR B 1 311 ? 26.811  -4.045  27.313  0.75   94.12  ? 311  TYR A CE1 1 
ATOM   4652 C CE2 . TYR B 1 311 ? 24.983  -5.409  28.084  0.75   93.31  ? 311  TYR A CE2 1 
ATOM   4653 C CZ  . TYR B 1 311 ? 26.301  -4.987  28.188  0.75   96.52  ? 311  TYR A CZ  1 
ATOM   4654 O OH  . TYR B 1 311 ? 27.114  -5.504  29.168  0.75   101.63 ? 311  TYR A OH  1 
ATOM   4655 N N   . LEU B 1 312 ? 24.381  -5.516  22.772  1.00   84.23  ? 312  LEU A N   1 
ATOM   4656 C CA  . LEU B 1 312 ? 24.892  -6.828  22.380  1.00   84.11  ? 312  LEU A CA  1 
ATOM   4657 C C   . LEU B 1 312 ? 25.812  -6.770  21.159  1.00   84.89  ? 312  LEU A C   1 
ATOM   4658 O O   . LEU B 1 312 ? 26.548  -7.725  20.891  1.00   84.92  ? 312  LEU A O   1 
ATOM   4659 C CB  . LEU B 1 312 ? 23.730  -7.788  22.108  1.00   83.52  ? 312  LEU A CB  1 
ATOM   4660 C CG  . LEU B 1 312 ? 22.747  -8.041  23.257  1.00   82.31  ? 312  LEU A CG  1 
ATOM   4661 C CD1 . LEU B 1 312 ? 21.395  -8.515  22.728  1.00   79.84  ? 312  LEU A CD1 1 
ATOM   4662 C CD2 . LEU B 1 312 ? 23.323  -9.038  24.263  1.00   81.39  ? 312  LEU A CD2 1 
ATOM   4663 N N   . PHE B 1 313 ? 25.765  -5.659  20.424  0.87   85.98  ? 313  PHE A N   1 
ATOM   4664 C CA  . PHE B 1 313 ? 26.563  -5.506  19.205  0.87   86.90  ? 313  PHE A CA  1 
ATOM   4665 C C   . PHE B 1 313 ? 28.059  -5.535  19.508  0.87   87.17  ? 313  PHE A C   1 
ATOM   4666 O O   . PHE B 1 313 ? 28.840  -6.128  18.757  0.87   87.37  ? 313  PHE A O   1 
ATOM   4667 C CB  . PHE B 1 313 ? 26.206  -4.212  18.457  0.87   87.12  ? 313  PHE A CB  1 
ATOM   4668 C CG  . PHE B 1 313 ? 24.800  -4.180  17.904  0.87   87.46  ? 313  PHE A CG  1 
ATOM   4669 C CD1 . PHE B 1 313 ? 24.311  -3.024  17.303  0.87   87.66  ? 313  PHE A CD1 1 
ATOM   4670 C CD2 . PHE B 1 313 ? 23.963  -5.295  17.987  0.87   87.45  ? 313  PHE A CD2 1 
ATOM   4671 C CE1 . PHE B 1 313 ? 23.020  -2.981  16.784  0.87   87.73  ? 313  PHE A CE1 1 
ATOM   4672 C CE2 . PHE B 1 313 ? 22.674  -5.261  17.473  0.87   87.44  ? 313  PHE A CE2 1 
ATOM   4673 C CZ  . PHE B 1 313 ? 22.200  -4.102  16.872  0.87   87.76  ? 313  PHE A CZ  1 
HETATM 4674 S S   . SO4 C 2 .   ? -14.483 -11.660 -20.493 1.00   48.54  ? 401  SO4 B S   1 
HETATM 4675 O O1  . SO4 C 2 .   ? -13.557 -10.781 -21.194 1.00   49.99  ? 401  SO4 B O1  1 
HETATM 4676 O O2  . SO4 C 2 .   ? -15.608 -12.005 -21.355 1.00   50.69  ? 401  SO4 B O2  1 
HETATM 4677 O O3  . SO4 C 2 .   ? -13.759 -12.868 -20.128 1.00   49.73  ? 401  SO4 B O3  1 
HETATM 4678 O O4  . SO4 C 2 .   ? -15.022 -11.012 -19.301 1.00   49.03  ? 401  SO4 B O4  1 
HETATM 4679 S S   . SO4 D 2 .   ? -9.327  -37.065 0.275   1.00   80.09  ? 402  SO4 B S   1 
HETATM 4680 O O1  . SO4 D 2 .   ? -8.025  -36.576 0.722   1.00   79.32  ? 402  SO4 B O1  1 
HETATM 4681 O O2  . SO4 D 2 .   ? -9.321  -37.231 -1.176  1.00   78.47  ? 402  SO4 B O2  1 
HETATM 4682 O O3  . SO4 D 2 .   ? -9.600  -38.358 0.905   1.00   79.79  ? 402  SO4 B O3  1 
HETATM 4683 O O4  . SO4 D 2 .   ? -10.356 -36.102 0.659   1.00   80.15  ? 402  SO4 B O4  1 
HETATM 4684 S S   . SO4 E 2 .   ? -16.405 -17.970 -9.733  0.58   66.09  ? 403  SO4 B S   1 
HETATM 4685 O O1  . SO4 E 2 .   ? -15.013 -17.548 -9.625  0.58   65.57  ? 403  SO4 B O1  1 
HETATM 4686 O O2  . SO4 E 2 .   ? -16.969 -17.540 -11.010 0.58   66.14  ? 403  SO4 B O2  1 
HETATM 4687 O O3  . SO4 E 2 .   ? -16.465 -19.425 -9.611  0.58   65.53  ? 403  SO4 B O3  1 
HETATM 4688 O O4  . SO4 E 2 .   ? -17.191 -17.363 -8.662  0.58   66.00  ? 403  SO4 B O4  1 
HETATM 4689 S S   . SO4 F 2 .   ? 18.680  0.428   21.060  1.00   54.25  ? 1001 SO4 A S   1 
HETATM 4690 O O1  . SO4 F 2 .   ? 18.647  1.322   19.915  1.00   53.58  ? 1001 SO4 A O1  1 
HETATM 4691 O O2  . SO4 F 2 .   ? 19.180  -0.873  20.625  1.00   54.28  ? 1001 SO4 A O2  1 
HETATM 4692 O O3  . SO4 F 2 .   ? 19.565  1.014   22.060  1.00   54.94  ? 1001 SO4 A O3  1 
HETATM 4693 O O4  . SO4 F 2 .   ? 17.346  0.268   21.633  1.00   53.09  ? 1001 SO4 A O4  1 
HETATM 4694 S S   . SO4 G 2 .   ? 30.308  -22.672 -0.398  0.69   101.40 ? 1002 SO4 A S   1 
HETATM 4695 O O1  . SO4 G 2 .   ? 30.067  -21.233 -0.341  0.69   101.33 ? 1002 SO4 A O1  1 
HETATM 4696 O O2  . SO4 G 2 .   ? 31.527  -22.930 -1.161  0.69   101.42 ? 1002 SO4 A O2  1 
HETATM 4697 O O3  . SO4 G 2 .   ? 30.467  -23.187 0.959   0.69   101.30 ? 1002 SO4 A O3  1 
HETATM 4698 O O4  . SO4 G 2 .   ? 29.180  -23.335 -1.048  0.69   101.13 ? 1002 SO4 A O4  1 
HETATM 4699 S S   . SO4 H 2 .   ? 24.381  -2.946  10.487  0.45   64.96  ? 1003 SO4 A S   1 
HETATM 4700 O O1  . SO4 H 2 .   ? 24.214  -1.933  9.449   0.45   64.84  ? 1003 SO4 A O1  1 
HETATM 4701 O O2  . SO4 H 2 .   ? 25.808  -3.097  10.774  0.45   65.40  ? 1003 SO4 A O2  1 
HETATM 4702 O O3  . SO4 H 2 .   ? 23.679  -2.513  11.696  0.45   65.11  ? 1003 SO4 A O3  1 
HETATM 4703 O O4  . SO4 H 2 .   ? 23.854  -4.233  10.045  0.45   63.85  ? 1003 SO4 A O4  1 
HETATM 4704 O O   . HOH I 3 .   ? 1.068   -11.549 -18.265 1.00   32.79  ? 501  HOH B O   1 
HETATM 4705 O O   . HOH I 3 .   ? -4.831  -33.255 -12.104 1.00   44.06  ? 502  HOH B O   1 
HETATM 4706 O O   . HOH I 3 .   ? -15.072 -15.681 -7.639  1.00   54.47  ? 503  HOH B O   1 
HETATM 4707 O O   . HOH I 3 .   ? -27.843 -42.074 -21.972 1.00   51.21  ? 504  HOH B O   1 
HETATM 4708 O O   . HOH I 3 .   ? -9.859  -10.597 -8.150  1.00   35.56  ? 505  HOH B O   1 
HETATM 4709 O O   . HOH I 3 .   ? -3.901  -10.407 -1.994  1.00   40.74  ? 506  HOH B O   1 
HETATM 4710 O O   . HOH I 3 .   ? 14.348  -8.317  -19.274 1.00   38.90  ? 507  HOH B O   1 
HETATM 4711 O O   . HOH I 3 .   ? -7.307  -23.894 -8.651  1.00   39.53  ? 508  HOH B O   1 
HETATM 4712 O O   . HOH I 3 .   ? 14.688  -3.576  -15.682 1.00   46.40  ? 509  HOH B O   1 
HETATM 4713 O O   . HOH I 3 .   ? -15.874 -27.002 -13.047 1.00   49.43  ? 510  HOH B O   1 
HETATM 4714 O O   . HOH I 3 .   ? 7.801   -4.272  -14.073 1.00   43.03  ? 511  HOH B O   1 
HETATM 4715 O O   . HOH I 3 .   ? 8.958   -8.362  -7.175  1.00   47.98  ? 512  HOH B O   1 
HETATM 4716 O O   . HOH I 3 .   ? -0.814  -12.260 4.504   1.00   40.44  ? 513  HOH B O   1 
HETATM 4717 O O   . HOH I 3 .   ? 6.797   -23.597 -10.048 1.00   48.58  ? 514  HOH B O   1 
HETATM 4718 O O   . HOH I 3 .   ? 0.569   -7.504  -7.716  1.00   42.55  ? 515  HOH B O   1 
HETATM 4719 O O   . HOH I 3 .   ? -3.852  -8.521  -5.174  1.00   37.15  ? 516  HOH B O   1 
HETATM 4720 O O   . HOH I 3 .   ? 0.468   -31.628 -15.773 1.00   55.02  ? 517  HOH B O   1 
HETATM 4721 O O   . HOH I 3 .   ? -27.449 -43.640 4.076   1.00   51.08  ? 518  HOH B O   1 
HETATM 4722 O O   . HOH I 3 .   ? 7.842   -18.153 -24.874 1.00   37.98  ? 519  HOH B O   1 
HETATM 4723 O O   . HOH I 3 .   ? 10.540  -22.265 -19.166 1.00   43.88  ? 520  HOH B O   1 
HETATM 4724 O O   . HOH I 3 .   ? -0.994  -36.924 -9.367  1.00   54.00  ? 521  HOH B O   1 
HETATM 4725 O O   . HOH I 3 .   ? -13.204 -15.918 -13.192 1.00   45.57  ? 522  HOH B O   1 
HETATM 4726 O O   . HOH I 3 .   ? -15.432 -18.018 -12.733 1.00   62.78  ? 523  HOH B O   1 
HETATM 4727 O O   . HOH I 3 .   ? 9.107   -25.442 -25.754 1.00   54.24  ? 524  HOH B O   1 
HETATM 4728 O O   . HOH I 3 .   ? 0.699   -16.832 -29.839 1.00   54.23  ? 525  HOH B O   1 
HETATM 4729 O O   . HOH I 3 .   ? -13.573 -23.730 -18.918 1.00   53.88  ? 526  HOH B O   1 
HETATM 4730 O O   . HOH I 3 .   ? -8.619  -35.046 -23.311 1.00   57.39  ? 527  HOH B O   1 
HETATM 4731 O O   . HOH I 3 .   ? -11.210 -9.190  -5.876  1.00   43.35  ? 528  HOH B O   1 
HETATM 4732 O O   . HOH I 3 .   ? -13.679 -25.011 -21.840 1.00   58.19  ? 529  HOH B O   1 
HETATM 4733 O O   . HOH I 3 .   ? -3.336  -5.965  -12.723 1.00   39.26  ? 530  HOH B O   1 
HETATM 4734 O O   . HOH I 3 .   ? 8.455   -17.165 -27.405 1.00   38.31  ? 531  HOH B O   1 
HETATM 4735 O O   . HOH I 3 .   ? -14.392 -22.998 -8.438  1.00   45.45  ? 532  HOH B O   1 
HETATM 4736 O O   . HOH I 3 .   ? 0.287   -32.975 -19.531 1.00   52.69  ? 533  HOH B O   1 
HETATM 4737 O O   . HOH I 3 .   ? -19.874 -20.711 0.082   1.00   63.78  ? 534  HOH B O   1 
HETATM 4738 O O   . HOH I 3 .   ? 5.448   -14.454 -30.436 1.00   55.30  ? 535  HOH B O   1 
HETATM 4739 O O   . HOH I 3 .   ? 7.008   -14.562 -28.518 1.00   47.57  ? 536  HOH B O   1 
HETATM 4740 O O   . HOH J 3 .   ? 6.651   -9.497  18.849  1.00   38.41  ? 1101 HOH A O   1 
HETATM 4741 O O   . HOH J 3 .   ? -5.014  -27.338 -0.257  1.00   47.77  ? 1102 HOH A O   1 
HETATM 4742 O O   . HOH J 3 .   ? 6.544   -2.453  13.141  1.00   45.01  ? 1103 HOH A O   1 
HETATM 4743 O O   . HOH J 3 .   ? 14.395  -1.695  8.719   1.00   39.05  ? 1104 HOH A O   1 
HETATM 4744 O O   . HOH J 3 .   ? 9.841   -5.347  2.746   1.00   38.55  ? 1105 HOH A O   1 
HETATM 4745 O O   . HOH J 3 .   ? 4.134   -6.248  8.449   1.00   38.01  ? 1106 HOH A O   1 
HETATM 4746 O O   . HOH J 3 .   ? 16.421  3.031   19.739  1.00   37.88  ? 1107 HOH A O   1 
HETATM 4747 O O   . HOH J 3 .   ? 36.259  -13.953 -5.087  1.00   57.97  ? 1108 HOH A O   1 
HETATM 4748 O O   . HOH J 3 .   ? 3.815   -3.088  11.904  1.00   49.81  ? 1109 HOH A O   1 
HETATM 4749 O O   . HOH J 3 .   ? 15.597  -3.921  -10.163 1.00   43.93  ? 1110 HOH A O   1 
HETATM 4750 O O   . HOH J 3 .   ? 21.196  -14.087 8.833   1.00   50.24  ? 1111 HOH A O   1 
HETATM 4751 O O   . HOH J 3 .   ? 8.631   -8.821  -3.807  1.00   40.57  ? 1112 HOH A O   1 
HETATM 4752 O O   . HOH J 3 .   ? 8.680   -4.157  5.758   1.00   39.88  ? 1113 HOH A O   1 
HETATM 4753 O O   . HOH J 3 .   ? 7.148   0.028   11.653  1.00   58.55  ? 1114 HOH A O   1 
HETATM 4754 O O   . HOH J 3 .   ? 9.334   -25.584 26.578  1.00   49.91  ? 1115 HOH A O   1 
HETATM 4755 O O   . HOH J 3 .   ? 5.989   -18.851 25.502  1.00   42.07  ? 1116 HOH A O   1 
HETATM 4756 O O   . HOH J 3 .   ? 21.904  -2.318  8.189   1.00   58.64  ? 1117 HOH A O   1 
HETATM 4757 O O   . HOH J 3 .   ? 10.344  -1.382  -1.134  1.00   46.88  ? 1118 HOH A O   1 
HETATM 4758 O O   . HOH J 3 .   ? 22.570  -13.927 6.307   1.00   56.55  ? 1119 HOH A O   1 
HETATM 4759 O O   . HOH J 3 .   ? 18.509  -4.482  -14.457 1.00   52.49  ? 1120 HOH A O   1 
HETATM 4760 O O   . HOH J 3 .   ? 18.089  0.332   17.118  1.00   50.74  ? 1121 HOH A O   1 
HETATM 4761 O O   . HOH J 3 .   ? 6.722   -23.835 19.879  1.00   44.08  ? 1122 HOH A O   1 
HETATM 4762 O O   . HOH J 3 .   ? -5.495  -17.615 13.596  1.00   45.90  ? 1123 HOH A O   1 
HETATM 4763 O O   . HOH J 3 .   ? 25.833  -8.457  8.569   1.00   51.28  ? 1124 HOH A O   1 
HETATM 4764 O O   . HOH J 3 .   ? 32.739  -8.305  4.104   1.00   54.07  ? 1125 HOH A O   1 
HETATM 4765 O O   . HOH J 3 .   ? 49.970  -12.278 -4.232  1.00   57.01  ? 1126 HOH A O   1 
HETATM 4766 O O   . HOH J 3 .   ? -8.998  -12.115 16.533  1.00   50.72  ? 1127 HOH A O   1 
HETATM 4767 O O   . HOH J 3 .   ? 4.877   -18.563 28.008  1.00   41.37  ? 1128 HOH A O   1 
HETATM 4768 O O   . HOH J 3 .   ? 10.422  -22.481 10.731  1.00   64.26  ? 1129 HOH A O   1 
HETATM 4769 O O   . HOH J 3 .   ? 16.093  -1.694  10.215  1.00   55.50  ? 1130 HOH A O   1 
HETATM 4770 O O   . HOH J 3 .   ? 2.518   -22.764 26.605  1.00   54.46  ? 1131 HOH A O   1 
HETATM 4771 O O   . HOH J 3 .   ? 14.637  0.014   6.750   1.00   43.56  ? 1132 HOH A O   1 
HETATM 4772 O O   . HOH J 3 .   ? 28.688  -11.149 8.407   1.00   64.98  ? 1133 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  ASN 65  65  65  ASN ASN 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  ASN 65  65  65  ASN ASN 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   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3 
_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)' 28930 ? 
1 MORE         -429  ? 
1 'SSA (A^2)'  59030 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000  0.0000000000 0.0000000000 0.0000000000  1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -y,x-y,z  -0.5000000000 -0.8660254038 0.0000000000 0.0000000000 0.8660254038  -0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_555 -x+y,-x,z -0.5000000000 0.8660254038  0.0000000000 0.0000000000 -0.8660254038 -0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 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 2015-02-04 
2 'Structure model' 1 1 2015-03-25 
# 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O B SER 10 ? ? OG B SER 58 ? ? 1.59 
2 1 O A SER 10 ? ? OG A SER 58 ? ? 2.09 
# 
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 N B GLY 9  ? ? CA B GLY 9  ? ? C  B GLY 9  ? ? 97.92  113.10 -15.18 2.50 N 
2 1 N B HIS 12 ? ? CA B HIS 12 ? ? C  B HIS 12 ? ? 88.95  111.00 -22.05 2.70 N 
3 1 N B GLY 59 ? ? CA B GLY 59 ? ? C  B GLY 59 ? ? 129.15 113.10 16.05  2.50 N 
4 1 N B CYS 60 ? ? CA B CYS 60 ? ? CB B CYS 60 ? ? 120.58 110.80 9.78   1.50 N 
5 1 N B CYS 60 ? ? CA B CYS 60 ? ? C  B CYS 60 ? ? 94.79  111.00 -16.21 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 11  ? ? 72.95   -53.93 
2  1 GLN B 38  ? ? 85.13   6.39   
3  1 GLU B 43  ? ? -160.74 108.65 
4  1 GLN B 97  ? ? -112.95 70.78  
5  1 ARG B 104 ? ? -85.94  48.15  
6  1 ASP B 224 ? ? -110.95 -72.87 
7  1 SER A 11  ? ? 74.45   -52.93 
8  1 GLN A 38  ? ? 82.41   -7.42  
9  1 CYS A 60  ? ? -64.57  1.44   
10 1 TYR A 94  ? ? 57.91   18.57  
11 1 GLN A 97  ? ? -102.54 67.92  
12 1 LYS A 102 ? ? 73.33   -1.32  
13 1 ARG A 104 ? ? -96.13  53.91  
14 1 ASP A 224 ? ? -101.40 -77.84 
15 1 ASN A 273 ? ? -90.65  36.16  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    59 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   CYS 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    60 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -147.46 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B SER 11 ? OG  ? A SER 11 OG  
2 1 Y 1 B HIS 12 ? CG  ? A HIS 12 CG  
3 1 Y 1 B HIS 12 ? ND1 ? A HIS 12 ND1 
4 1 Y 1 B HIS 12 ? CD2 ? A HIS 12 CD2 
5 1 Y 1 B HIS 12 ? CE1 ? A HIS 12 CE1 
6 1 Y 1 B HIS 12 ? NE2 ? A HIS 12 NE2 
7 1 Y 1 A SER 11 ? OG  ? B SER 11 OG  
# 
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 0 B GLY 59  ? A GLY 59  
4  1 Y 1 B ARG 196 ? A ARG 196 
5  1 Y 1 B LYS 197 ? A LYS 197 
6  1 Y 1 B LYS 198 ? A LYS 198 
7  1 Y 1 B ALA 199 ? A ALA 199 
8  1 Y 1 B ASN 200 ? A ASN 200 
9  1 Y 1 B GLU 201 ? A GLU 201 
10 1 Y 1 B VAL 202 ? A VAL 202 
11 1 Y 1 B LEU 318 ? A LEU 318 
12 1 Y 1 B LEU 319 ? A LEU 319 
13 1 Y 1 B GLU 320 ? A GLU 320 
14 1 Y 1 B HIS 321 ? A HIS 321 
15 1 Y 1 B HIS 322 ? A HIS 322 
16 1 Y 1 B HIS 323 ? A HIS 323 
17 1 Y 1 B HIS 324 ? A HIS 324 
18 1 Y 1 B HIS 325 ? A HIS 325 
19 1 Y 1 B HIS 326 ? A HIS 326 
20 1 Y 1 A MET 1   ? B MET 1   
21 1 Y 1 A PRO 2   ? B PRO 2   
22 1 Y 1 A ARG 196 ? B ARG 196 
23 1 Y 1 A LYS 197 ? B LYS 197 
24 1 Y 1 A LYS 198 ? B LYS 198 
25 1 Y 1 A ALA 199 ? B ALA 199 
26 1 Y 1 A ASN 200 ? B ASN 200 
27 1 Y 1 A GLU 201 ? B GLU 201 
28 1 Y 1 A VAL 202 ? B VAL 202 
29 1 Y 1 A SER 314 ? B SER 314 
30 1 Y 1 A HIS 315 ? B HIS 315 
31 1 Y 1 A VAL 316 ? B VAL 316 
32 1 Y 1 A PRO 317 ? B PRO 317 
33 1 Y 1 A LEU 318 ? B LEU 318 
34 1 Y 1 A LEU 319 ? B LEU 319 
35 1 Y 1 A GLU 320 ? B GLU 320 
36 1 Y 1 A HIS 321 ? B HIS 321 
37 1 Y 1 A HIS 322 ? B HIS 322 
38 1 Y 1 A HIS 323 ? B HIS 323 
39 1 Y 1 A HIS 324 ? B HIS 324 
40 1 Y 1 A HIS 325 ? B HIS 325 
41 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  401  1002 SO4 SO4 B . 
D 2 SO4 1  402  1003 SO4 SO4 B . 
E 2 SO4 1  403  1005 SO4 SO4 B . 
F 2 SO4 1  1001 1001 SO4 SO4 A . 
G 2 SO4 1  1002 1004 SO4 SO4 A . 
H 2 SO4 1  1003 1006 SO4 SO4 A . 
I 3 HOH 1  501  2    HOH HOH B . 
I 3 HOH 2  502  3    HOH HOH B . 
I 3 HOH 3  503  5    HOH HOH B . 
I 3 HOH 4  504  7    HOH HOH B . 
I 3 HOH 5  505  8    HOH HOH B . 
I 3 HOH 6  506  9    HOH HOH B . 
I 3 HOH 7  507  11   HOH HOH B . 
I 3 HOH 8  508  14   HOH HOH B . 
I 3 HOH 9  509  15   HOH HOH B . 
I 3 HOH 10 510  16   HOH HOH B . 
I 3 HOH 11 511  22   HOH HOH B . 
I 3 HOH 12 512  23   HOH HOH B . 
I 3 HOH 13 513  24   HOH HOH B . 
I 3 HOH 14 514  25   HOH HOH B . 
I 3 HOH 15 515  26   HOH HOH B . 
I 3 HOH 16 516  27   HOH HOH B . 
I 3 HOH 17 517  29   HOH HOH B . 
I 3 HOH 18 518  30   HOH HOH B . 
I 3 HOH 19 519  31   HOH HOH B . 
I 3 HOH 20 520  33   HOH HOH B . 
I 3 HOH 21 521  35   HOH HOH B . 
I 3 HOH 22 522  36   HOH HOH B . 
I 3 HOH 23 523  38   HOH HOH B . 
I 3 HOH 24 524  42   HOH HOH B . 
I 3 HOH 25 525  43   HOH HOH B . 
I 3 HOH 26 526  44   HOH HOH B . 
I 3 HOH 27 527  51   HOH HOH B . 
I 3 HOH 28 528  52   HOH HOH B . 
I 3 HOH 29 529  53   HOH HOH B . 
I 3 HOH 30 530  54   HOH HOH B . 
I 3 HOH 31 531  57   HOH HOH B . 
I 3 HOH 32 532  59   HOH HOH B . 
I 3 HOH 33 533  60   HOH HOH B . 
I 3 HOH 34 534  61   HOH HOH B . 
I 3 HOH 35 535  66   HOH HOH B . 
I 3 HOH 36 536  68   HOH HOH B . 
J 3 HOH 1  1101 1    HOH HOH A . 
J 3 HOH 2  1102 4    HOH HOH A . 
J 3 HOH 3  1103 6    HOH HOH A . 
J 3 HOH 4  1104 10   HOH HOH A . 
J 3 HOH 5  1105 12   HOH HOH A . 
J 3 HOH 6  1106 13   HOH HOH A . 
J 3 HOH 7  1107 17   HOH HOH A . 
J 3 HOH 8  1108 18   HOH HOH A . 
J 3 HOH 9  1109 19   HOH HOH A . 
J 3 HOH 10 1110 20   HOH HOH A . 
J 3 HOH 11 1111 21   HOH HOH A . 
J 3 HOH 12 1112 28   HOH HOH A . 
J 3 HOH 13 1113 34   HOH HOH A . 
J 3 HOH 14 1114 37   HOH HOH A . 
J 3 HOH 15 1115 39   HOH HOH A . 
J 3 HOH 16 1116 40   HOH HOH A . 
J 3 HOH 17 1117 41   HOH HOH A . 
J 3 HOH 18 1118 45   HOH HOH A . 
J 3 HOH 19 1119 46   HOH HOH A . 
J 3 HOH 20 1120 47   HOH HOH A . 
J 3 HOH 21 1121 48   HOH HOH A . 
J 3 HOH 22 1122 49   HOH HOH A . 
J 3 HOH 23 1123 50   HOH HOH A . 
J 3 HOH 24 1124 55   HOH HOH A . 
J 3 HOH 25 1125 56   HOH HOH A . 
J 3 HOH 26 1126 58   HOH HOH A . 
J 3 HOH 27 1127 62   HOH HOH A . 
J 3 HOH 28 1128 63   HOH HOH A . 
J 3 HOH 29 1129 64   HOH HOH A . 
J 3 HOH 30 1130 65   HOH HOH A . 
J 3 HOH 31 1131 67   HOH HOH A . 
J 3 HOH 32 1132 69   HOH HOH A . 
J 3 HOH 33 1133 70   HOH HOH A . 
# 
